data_4KP8
# 
_entry.id   4KP8 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.397 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   4KP8         pdb_00004kp8 10.2210/pdb4kp8/pdb 
RCSB  RCSB079621   ?            ?                   
WWPDB D_1000079621 ?            ?                   
# 
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 2017-10-04 
3 'Structure model' 1 2 2023-11-08 
4 'Structure model' 1 3 2024-10-30 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'        
2 3 'Structure model' 'Data collection'        
3 3 'Structure model' 'Database references'    
4 3 'Structure model' 'Derived calculations'   
5 3 'Structure model' 'Refinement description' 
6 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_detector               
2  3 'Structure model' chem_comp_atom                
3  3 'Structure model' chem_comp_bond                
4  3 'Structure model' database_2                    
5  3 'Structure model' diffrn_source                 
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_detector.detector'                   
2  3 'Structure model' '_database_2.pdbx_DOI'                        
3  3 'Structure model' '_database_2.pdbx_database_accession'         
4  3 'Structure model' '_diffrn_source.pdbx_synchrotron_site'        
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.status_code                     REL 
_pdbx_database_status.entry_id                        4KP8 
_pdbx_database_status.recvd_initial_deposition_date   2013-05-13 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.methods_development_category    ? 
_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 4KP5 . 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 '3-[(pyrimidin-2-ylsulfanyl)acetyl]benzenesulfonamide' 309.364   3   ?       ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                   78.133    1   ?       ? ? ? 
5 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                106.120   2   ?       ? ? ? 
6 non-polymer syn 1,2-ETHANEDIOL                                         62.068    1   ?       ? ? ? 
7 water       nat water                                                  18.015    997 ?       ? ? ? 
# 
_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 '3-[(pyrimidin-2-ylsulfanyl)acetyl]benzenesulfonamide' E1G 
4 'DIMETHYL SULFOXIDE'                                   DMS 
5 'DI(HYDROXYETHYL)ETHER'                                PEG 
6 1,2-ETHANEDIOL                                         EDO 
7 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 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                   ?                 'C2 H6 O S'        78.133  
E1G non-polymer         . '3-[(pyrimidin-2-ylsulfanyl)acetyl]benzenesulfonamide' ?                 'C12 H11 N3 O3 S2' 309.364 
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 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'                                ?                 'C4 H10 O3'        106.120 
PHE 'L-peptide linking' y PHENYLALANINE                                          ?                 'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                                                ?                 'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                                                 ?                 'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE                                              ?                 'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                             ?                 'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE                                               ?                 'C9 H11 N O3'      181.189 
VAL 'L-peptide linking' y VALINE                                                 ?                 'C5 H11 N O2'      117.146 
ZN  non-polymer         . 'ZINC ION'                                             ?                 'Zn 2'             65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   TRP 4   4   4   TRP TRP A . n 
A 1 5   THR 5   5   5   THR THR A . n 
A 1 6   TYR 6   6   6   TYR TYR A . n 
A 1 7   PHE 7   7   7   PHE PHE A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  GLU 12  12  12  GLU GLU A . n 
A 1 13  ASN 13  13  13  ASN ASN A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  TRP 15  15  15  TRP TRP A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  LYS 17  17  17  LYS LYS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  TYR 19  19  19  TYR TYR A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  GLY 24  24  24  GLY GLY A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  GLN 27  27  27  GLN GLN A . n 
A 1 28  SER 28  28  28  SER SER A . n 
A 1 29  PRO 29  29  29  PRO PRO A . n 
A 1 30  ILE 30  30  30  ILE ILE A . n 
A 1 31  ASP 31  31  31  ASP ASP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  HIS 33  33  33  HIS HIS A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ASP 35  35  35  ASP ASP A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  GLN 38  38  38  GLN GLN A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  SER 42  42  42  SER SER A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  GLN 49  49  49  GLN GLN A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASN 52  52  52  ASN ASN A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  SER 54  54  54  SER SER A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  ASN 56  56  56  ASN ASN A . n 
A 1 57  LYS 57  57  57  LYS LYS A . n 
A 1 58  GLN 58  58  58  GLN GLN A . n 
A 1 59  PHE 59  59  59  PHE PHE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  THR 62  62  62  THR THR A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  ASN 64  64  64  ASN ASN A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  HIS 66  66  66  HIS HIS A . n 
A 1 67  SER 67  67  67  SER SER A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  ASN 71  71  71  ASN ASN A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  PRO 73  73  73  PRO PRO A . n 
A 1 74  SER 74  74  74  SER SER A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  MET 76  76  76  MET MET A . n 
A 1 77  HIS 77  77  77  HIS HIS A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLN 79  79  79  GLN GLN A . n 
A 1 80  GLY 80  80  80  GLY GLY A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  GLN 82  82  82  GLN GLN A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  TYR 85  85  85  TYR TYR A . n 
A 1 86  SER 86  86  86  SER SER A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  GLN 89  89  89  GLN GLN A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  HIS 93  93  93  HIS HIS A . n 
A 1 94  TRP 94  94  94  TRP TRP A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  ASN 96  96  96  ASN ASN A . n 
A 1 97  PRO 97  97  97  PRO PRO A . n 
A 1 98  ASN 98  98  98  ASN ASN A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 PRO 100 100 100 PRO PRO A . n 
A 1 101 HIS 101 101 101 HIS HIS A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 HIS 105 105 105 HIS HIS A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 HIS 111 111 111 HIS HIS A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 HIS 117 117 117 HIS HIS A . n 
A 1 118 ILE 118 118 118 ILE ILE A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 TYR 121 121 121 TYR TYR A . n 
A 1 122 ASN 122 122 122 ASN ASN A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 PRO 127 127 127 PRO PRO A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 SER 130 130 130 SER SER A . n 
A 1 131 THR 131 131 131 THR THR A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 SER 133 133 133 SER SER A . n 
A 1 134 ASN 134 134 134 ASN ASN A . n 
A 1 135 LYS 135 135 135 LYS LYS A . n 
A 1 136 SER 136 136 136 SER SER A . n 
A 1 137 GLU 137 137 137 GLU GLU A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 ILE 146 146 146 ILE ILE A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 MET 148 148 148 MET MET A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 SER 150 150 150 SER SER A . n 
A 1 151 PHE 151 151 151 PHE PHE A . n 
A 1 152 ASN 152 152 152 ASN ASN A . n 
A 1 153 PRO 153 153 153 PRO PRO A . n 
A 1 154 SER 154 154 154 SER SER A . n 
A 1 155 TYR 155 155 155 TYR TYR A . n 
A 1 156 ASP 156 156 156 ASP ASP A . n 
A 1 157 LYS 157 157 157 LYS LYS A . n 
A 1 158 ILE 158 158 158 ILE ILE A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 HIS 161 161 161 HIS HIS A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 GLN 163 163 163 GLN GLN A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 LYS 166 166 166 LYS LYS A . n 
A 1 167 TYR 167 167 167 TYR TYR A . n 
A 1 168 LYS 168 168 168 LYS LYS A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 GLN 170 170 170 GLN GLN A . n 
A 1 171 GLU 171 171 171 GLU GLU A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 PHE 173 173 173 PHE PHE A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 PRO 175 175 175 PRO PRO A . n 
A 1 176 GLY 176 176 176 GLY GLY A . n 
A 1 177 PHE 177 177 177 PHE PHE A . n 
A 1 178 ASN 178 178 178 ASN ASN A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 GLU 180 180 180 GLU GLU A . n 
A 1 181 GLU 181 181 181 GLU GLU A . n 
A 1 182 LEU 182 182 182 LEU LEU A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 GLU 185 185 185 GLU GLU A . n 
A 1 186 ARG 186 186 186 ARG ARG A . n 
A 1 187 THR 187 187 187 THR THR A . n 
A 1 188 ALA 188 188 188 ALA ALA A . n 
A 1 189 GLU 189 189 189 GLU GLU A . n 
A 1 190 TYR 190 190 190 TYR TYR A . n 
A 1 191 TYR 191 191 191 TYR TYR A . n 
A 1 192 ARG 192 192 192 ARG ARG A . n 
A 1 193 TYR 193 193 193 TYR TYR A . n 
A 1 194 ARG 194 194 194 ARG ARG A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 CYS 202 202 202 CYS CYS A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 PRO 204 204 204 PRO PRO A . n 
A 1 205 THR 205 205 205 THR THR A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 TRP 208 208 208 TRP TRP A . n 
A 1 209 THR 209 209 209 THR THR A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 PHE 211 211 211 PHE PHE A . n 
A 1 212 ARG 212 212 212 ARG ARG A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 VAL 215 215 215 VAL VAL A . n 
A 1 216 GLN 216 216 216 GLN GLN A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 SER 218 218 218 SER SER A . n 
A 1 219 GLN 219 219 219 GLN GLN A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 GLN 221 221 221 GLN GLN A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 LEU 225 225 225 LEU LEU A . n 
A 1 226 GLU 226 226 226 GLU GLU A . n 
A 1 227 THR 227 227 227 THR THR A . n 
A 1 228 ALA 228 228 228 ALA ALA A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 TYR 230 230 230 TYR TYR A . n 
A 1 231 CYS 231 231 231 CYS CYS A . n 
A 1 232 THR 232 232 232 THR THR A . n 
A 1 233 HIS 233 233 233 HIS HIS A . n 
A 1 234 MET 234 234 234 MET MET A . n 
A 1 235 ASP 235 235 235 ASP ASP A . n 
A 1 236 ASP 236 236 236 ASP ASP A . n 
A 1 237 PRO 237 237 237 PRO PRO A . n 
A 1 238 SER 238 238 238 SER SER A . n 
A 1 239 PRO 239 239 239 PRO PRO A . n 
A 1 240 ARG 240 240 240 ARG ARG A . n 
A 1 241 GLU 241 241 241 GLU GLU A . n 
A 1 242 MET 242 242 242 MET MET A . n 
A 1 243 ILE 243 243 243 ILE ILE A . n 
A 1 244 ASN 244 244 244 ASN ASN A . n 
A 1 245 ASN 245 245 245 ASN ASN A . n 
A 1 246 PHE 246 246 246 PHE PHE A . n 
A 1 247 ARG 247 247 247 ARG ARG A . n 
A 1 248 GLN 248 248 248 GLN GLN A . n 
A 1 249 VAL 249 249 249 VAL VAL A . n 
A 1 250 GLN 250 250 250 GLN GLN A . n 
A 1 251 LYS 251 251 251 LYS LYS A . n 
A 1 252 PHE 252 252 252 PHE PHE A . n 
A 1 253 ASP 253 253 253 ASP ASP A . n 
A 1 254 GLU 254 254 254 GLU GLU A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 LEU 256 256 256 LEU LEU A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 TYR 258 258 258 TYR TYR A . n 
A 1 259 THR 259 259 259 THR THR A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 SER 262 262 262 SER SER A . n 
A 1 263 GLN 263 263 263 GLN GLN A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   LYS 3   3   ?   ?   ?   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 ?   ?   ?   B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   SER 2   2   ?   ?   ?   C . n 
C 1 3   LYS 3   3   3   LYS LYS C . n 
C 1 4   TRP 4   4   4   TRP TRP C . n 
C 1 5   THR 5   5   5   THR THR C . n 
C 1 6   TYR 6   6   6   TYR TYR C . n 
C 1 7   PHE 7   7   7   PHE PHE C . n 
C 1 8   GLY 8   8   8   GLY GLY C . n 
C 1 9   PRO 9   9   9   PRO PRO C . n 
C 1 10  ASP 10  10  10  ASP ASP C . n 
C 1 11  GLY 11  11  11  GLY GLY C . n 
C 1 12  GLU 12  12  12  GLU GLU C . n 
C 1 13  ASN 13  13  13  ASN ASN C . n 
C 1 14  SER 14  14  14  SER SER C . n 
C 1 15  TRP 15  15  15  TRP TRP C . n 
C 1 16  SER 16  16  16  SER SER C . n 
C 1 17  LYS 17  17  17  LYS LYS C . n 
C 1 18  LYS 18  18  18  LYS LYS C . n 
C 1 19  TYR 19  19  19  TYR TYR C . n 
C 1 20  PRO 20  20  20  PRO PRO C . n 
C 1 21  SER 21  21  21  SER SER C . n 
C 1 22  CYS 22  22  22  CYS CYS C . n 
C 1 23  GLY 23  23  23  GLY GLY C . n 
C 1 24  GLY 24  24  24  GLY GLY C . n 
C 1 25  LEU 25  25  25  LEU LEU C . n 
C 1 26  LEU 26  26  26  LEU LEU C . n 
C 1 27  GLN 27  27  27  GLN GLN C . n 
C 1 28  SER 28  28  28  SER SER C . n 
C 1 29  PRO 29  29  29  PRO PRO C . n 
C 1 30  ILE 30  30  30  ILE ILE C . n 
C 1 31  ASP 31  31  31  ASP ASP C . n 
C 1 32  LEU 32  32  32  LEU LEU C . n 
C 1 33  HIS 33  33  33  HIS HIS C . n 
C 1 34  SER 34  34  34  SER SER C . n 
C 1 35  ASP 35  35  35  ASP ASP C . n 
C 1 36  ILE 36  36  36  ILE ILE C . n 
C 1 37  LEU 37  37  37  LEU LEU C . n 
C 1 38  GLN 38  38  38  GLN GLN C . n 
C 1 39  TYR 39  39  39  TYR TYR C . n 
C 1 40  ASP 40  40  40  ASP ASP C . n 
C 1 41  ALA 41  41  41  ALA ALA C . n 
C 1 42  SER 42  42  42  SER SER C . n 
C 1 43  LEU 43  43  43  LEU LEU C . n 
C 1 44  THR 44  44  44  THR THR C . n 
C 1 45  PRO 45  45  45  PRO PRO C . n 
C 1 46  LEU 46  46  46  LEU LEU C . n 
C 1 47  GLU 47  47  47  GLU GLU C . n 
C 1 48  PHE 48  48  48  PHE PHE C . n 
C 1 49  GLN 49  49  49  GLN GLN C . n 
C 1 50  GLY 50  50  50  GLY GLY C . n 
C 1 51  TYR 51  51  51  TYR TYR C . n 
C 1 52  ASN 52  52  52  ASN ASN C . n 
C 1 53  LEU 53  53  53  LEU LEU C . n 
C 1 54  SER 54  54  54  SER SER C . n 
C 1 55  ALA 55  55  55  ALA ALA C . n 
C 1 56  ASN 56  56  56  ASN ASN C . n 
C 1 57  LYS 57  57  57  LYS LYS C . n 
C 1 58  GLN 58  58  58  GLN GLN C . n 
C 1 59  PHE 59  59  59  PHE PHE C . n 
C 1 60  LEU 60  60  60  LEU LEU C . n 
C 1 61  LEU 61  61  61  LEU LEU C . n 
C 1 62  THR 62  62  62  THR THR C . n 
C 1 63  ASN 63  63  63  ASN ASN C . n 
C 1 64  ASN 64  64  64  ASN ASN C . n 
C 1 65  GLY 65  65  65  GLY GLY C . n 
C 1 66  HIS 66  66  66  HIS HIS C . n 
C 1 67  SER 67  67  67  SER SER C . n 
C 1 68  VAL 68  68  68  VAL VAL C . n 
C 1 69  LYS 69  69  69  LYS LYS C . n 
C 1 70  LEU 70  70  70  LEU LEU C . n 
C 1 71  ASN 71  71  71  ASN ASN C . n 
C 1 72  LEU 72  72  72  LEU LEU C . n 
C 1 73  PRO 73  73  73  PRO PRO C . n 
C 1 74  SER 74  74  74  SER SER C . n 
C 1 75  ASP 75  75  75  ASP ASP C . n 
C 1 76  MET 76  76  76  MET MET C . n 
C 1 77  HIS 77  77  77  HIS HIS C . n 
C 1 78  ILE 78  78  78  ILE ILE C . n 
C 1 79  GLN 79  79  79  GLN GLN C . n 
C 1 80  GLY 80  80  80  GLY GLY C . n 
C 1 81  LEU 81  81  81  LEU LEU C . n 
C 1 82  GLN 82  82  82  GLN GLN C . n 
C 1 83  SER 83  83  83  SER SER C . n 
C 1 84  ARG 84  84  84  ARG ARG C . n 
C 1 85  TYR 85  85  85  TYR TYR C . n 
C 1 86  SER 86  86  86  SER SER C . n 
C 1 87  ALA 87  87  87  ALA ALA C . n 
C 1 88  THR 88  88  88  THR THR C . n 
C 1 89  GLN 89  89  89  GLN GLN C . n 
C 1 90  LEU 90  90  90  LEU LEU C . n 
C 1 91  HIS 91  91  91  HIS HIS C . n 
C 1 92  LEU 92  92  92  LEU LEU C . n 
C 1 93  HIS 93  93  93  HIS HIS C . n 
C 1 94  TRP 94  94  94  TRP TRP C . n 
C 1 95  GLY 95  95  95  GLY GLY C . n 
C 1 96  ASN 96  96  96  ASN ASN C . n 
C 1 97  PRO 97  97  97  PRO PRO C . n 
C 1 98  ASN 98  98  98  ASN ASN C . n 
C 1 99  ASP 99  99  99  ASP ASP C . n 
C 1 100 PRO 100 100 100 PRO PRO C . n 
C 1 101 HIS 101 101 101 HIS HIS C . n 
C 1 102 GLY 102 102 102 GLY GLY C . n 
C 1 103 SER 103 103 103 SER SER C . n 
C 1 104 GLU 104 104 104 GLU GLU C . n 
C 1 105 HIS 105 105 105 HIS HIS C . n 
C 1 106 THR 106 106 106 THR THR C . n 
C 1 107 VAL 107 107 107 VAL VAL C . n 
C 1 108 SER 108 108 108 SER SER C . n 
C 1 109 GLY 109 109 109 GLY GLY C . n 
C 1 110 GLN 110 110 110 GLN GLN C . n 
C 1 111 HIS 111 111 111 HIS HIS C . n 
C 1 112 PHE 112 112 112 PHE PHE C . n 
C 1 113 ALA 113 113 113 ALA ALA C . n 
C 1 114 ALA 114 114 114 ALA ALA C . n 
C 1 115 GLU 115 115 115 GLU GLU C . n 
C 1 116 LEU 116 116 116 LEU LEU C . n 
C 1 117 HIS 117 117 117 HIS HIS C . n 
C 1 118 ILE 118 118 118 ILE ILE C . n 
C 1 119 VAL 119 119 119 VAL VAL C . n 
C 1 120 HIS 120 120 120 HIS HIS C . n 
C 1 121 TYR 121 121 121 TYR TYR C . n 
C 1 122 ASN 122 122 122 ASN ASN C . n 
C 1 123 SER 123 123 123 SER SER C . n 
C 1 124 ASP 124 124 124 ASP ASP C . n 
C 1 125 LEU 125 125 125 LEU LEU C . n 
C 1 126 TYR 126 126 126 TYR TYR C . n 
C 1 127 PRO 127 127 127 PRO PRO C . n 
C 1 128 ASP 128 128 128 ASP ASP C . n 
C 1 129 ALA 129 129 129 ALA ALA C . n 
C 1 130 SER 130 130 130 SER SER C . n 
C 1 131 THR 131 131 131 THR THR C . n 
C 1 132 ALA 132 132 132 ALA ALA C . n 
C 1 133 SER 133 133 133 SER SER C . n 
C 1 134 ASN 134 134 134 ASN ASN C . n 
C 1 135 LYS 135 135 135 LYS LYS C . n 
C 1 136 SER 136 136 136 SER SER C . n 
C 1 137 GLU 137 137 137 GLU GLU C . n 
C 1 138 GLY 138 138 138 GLY GLY C . n 
C 1 139 LEU 139 139 139 LEU LEU C . n 
C 1 140 ALA 140 140 140 ALA ALA C . n 
C 1 141 VAL 141 141 141 VAL VAL C . n 
C 1 142 LEU 142 142 142 LEU LEU C . n 
C 1 143 ALA 143 143 143 ALA ALA C . n 
C 1 144 VAL 144 144 144 VAL VAL C . n 
C 1 145 LEU 145 145 145 LEU LEU C . n 
C 1 146 ILE 146 146 146 ILE ILE C . n 
C 1 147 GLU 147 147 147 GLU GLU C . n 
C 1 148 MET 148 148 148 MET MET C . n 
C 1 149 GLY 149 149 149 GLY GLY C . n 
C 1 150 SER 150 150 150 SER SER C . n 
C 1 151 PHE 151 151 151 PHE PHE C . n 
C 1 152 ASN 152 152 152 ASN ASN C . n 
C 1 153 PRO 153 153 153 PRO PRO C . n 
C 1 154 SER 154 154 154 SER SER C . n 
C 1 155 TYR 155 155 155 TYR TYR C . n 
C 1 156 ASP 156 156 156 ASP ASP C . n 
C 1 157 LYS 157 157 157 LYS LYS C . n 
C 1 158 ILE 158 158 158 ILE ILE C . n 
C 1 159 PHE 159 159 159 PHE PHE C . n 
C 1 160 SER 160 160 160 SER SER C . n 
C 1 161 HIS 161 161 161 HIS HIS C . n 
C 1 162 LEU 162 162 162 LEU LEU C . n 
C 1 163 GLN 163 163 163 GLN GLN C . n 
C 1 164 HIS 164 164 164 HIS HIS C . n 
C 1 165 VAL 165 165 165 VAL VAL C . n 
C 1 166 LYS 166 166 166 LYS LYS C . n 
C 1 167 TYR 167 167 167 TYR TYR C . n 
C 1 168 LYS 168 168 168 LYS LYS C . n 
C 1 169 GLY 169 169 169 GLY GLY C . n 
C 1 170 GLN 170 170 170 GLN GLN C . n 
C 1 171 GLU 171 171 171 GLU GLU C . n 
C 1 172 ALA 172 172 172 ALA ALA C . n 
C 1 173 PHE 173 173 173 PHE PHE C . n 
C 1 174 VAL 174 174 174 VAL VAL C . n 
C 1 175 PRO 175 175 175 PRO PRO C . n 
C 1 176 GLY 176 176 176 GLY GLY C . n 
C 1 177 PHE 177 177 177 PHE PHE C . n 
C 1 178 ASN 178 178 178 ASN ASN C . n 
C 1 179 ILE 179 179 179 ILE ILE C . n 
C 1 180 GLU 180 180 180 GLU GLU C . n 
C 1 181 GLU 181 181 181 GLU GLU C . n 
C 1 182 LEU 182 182 182 LEU LEU C . n 
C 1 183 LEU 183 183 183 LEU LEU C . n 
C 1 184 PRO 184 184 184 PRO PRO C . n 
C 1 185 GLU 185 185 185 GLU GLU C . n 
C 1 186 ARG 186 186 186 ARG ARG C . n 
C 1 187 THR 187 187 187 THR THR C . n 
C 1 188 ALA 188 188 188 ALA ALA C . n 
C 1 189 GLU 189 189 189 GLU GLU C . n 
C 1 190 TYR 190 190 190 TYR TYR C . n 
C 1 191 TYR 191 191 191 TYR TYR C . n 
C 1 192 ARG 192 192 192 ARG ARG C . n 
C 1 193 TYR 193 193 193 TYR TYR C . n 
C 1 194 ARG 194 194 194 ARG ARG C . n 
C 1 195 GLY 195 195 195 GLY GLY C . n 
C 1 196 SER 196 196 196 SER SER C . n 
C 1 197 LEU 197 197 197 LEU LEU C . n 
C 1 198 THR 198 198 198 THR THR C . n 
C 1 199 THR 199 199 199 THR THR C . n 
C 1 200 PRO 200 200 200 PRO PRO C . n 
C 1 201 PRO 201 201 201 PRO PRO C . n 
C 1 202 CYS 202 202 202 CYS CYS C . n 
C 1 203 ASN 203 203 203 ASN ASN C . n 
C 1 204 PRO 204 204 204 PRO PRO C . n 
C 1 205 THR 205 205 205 THR THR C . n 
C 1 206 VAL 206 206 206 VAL VAL C . n 
C 1 207 LEU 207 207 207 LEU LEU C . n 
C 1 208 TRP 208 208 208 TRP TRP C . n 
C 1 209 THR 209 209 209 THR THR C . n 
C 1 210 VAL 210 210 210 VAL VAL C . n 
C 1 211 PHE 211 211 211 PHE PHE C . n 
C 1 212 ARG 212 212 212 ARG ARG C . n 
C 1 213 ASN 213 213 213 ASN ASN C . n 
C 1 214 PRO 214 214 214 PRO PRO C . n 
C 1 215 VAL 215 215 215 VAL VAL C . n 
C 1 216 GLN 216 216 216 GLN GLN C . n 
C 1 217 ILE 217 217 217 ILE ILE C . n 
C 1 218 SER 218 218 218 SER SER C . n 
C 1 219 GLN 219 219 219 GLN GLN C . n 
C 1 220 GLU 220 220 220 GLU GLU C . n 
C 1 221 GLN 221 221 221 GLN GLN C . n 
C 1 222 LEU 222 222 222 LEU LEU C . n 
C 1 223 LEU 223 223 223 LEU LEU C . n 
C 1 224 ALA 224 224 224 ALA ALA C . n 
C 1 225 LEU 225 225 225 LEU LEU C . n 
C 1 226 GLU 226 226 226 GLU GLU C . n 
C 1 227 THR 227 227 227 THR THR C . n 
C 1 228 ALA 228 228 228 ALA ALA C . n 
C 1 229 LEU 229 229 229 LEU LEU C . n 
C 1 230 TYR 230 230 230 TYR TYR C . n 
C 1 231 CYS 231 231 231 CYS CYS C . n 
C 1 232 THR 232 232 232 THR THR C . n 
C 1 233 HIS 233 233 233 HIS HIS C . n 
C 1 234 MET 234 234 234 MET MET C . n 
C 1 235 ASP 235 235 235 ASP ASP C . n 
C 1 236 ASP 236 236 236 ASP ASP C . n 
C 1 237 PRO 237 237 237 PRO PRO C . n 
C 1 238 SER 238 238 238 SER SER C . n 
C 1 239 PRO 239 239 239 PRO PRO C . n 
C 1 240 ARG 240 240 240 ARG ARG C . n 
C 1 241 GLU 241 241 241 GLU GLU C . n 
C 1 242 MET 242 242 242 MET MET C . n 
C 1 243 ILE 243 243 243 ILE ILE C . n 
C 1 244 ASN 244 244 244 ASN ASN C . n 
C 1 245 ASN 245 245 245 ASN ASN C . n 
C 1 246 PHE 246 246 246 PHE PHE C . n 
C 1 247 ARG 247 247 247 ARG ARG C . n 
C 1 248 GLN 248 248 248 GLN GLN C . n 
C 1 249 VAL 249 249 249 VAL VAL C . n 
C 1 250 GLN 250 250 250 GLN GLN C . n 
C 1 251 LYS 251 251 251 LYS LYS C . n 
C 1 252 PHE 252 252 252 PHE PHE C . n 
C 1 253 ASP 253 253 253 ASP ASP C . n 
C 1 254 GLU 254 254 254 GLU GLU C . n 
C 1 255 ARG 255 255 255 ARG ARG C . n 
C 1 256 LEU 256 256 256 LEU LEU C . n 
C 1 257 VAL 257 257 257 VAL VAL C . n 
C 1 258 TYR 258 258 258 TYR TYR C . n 
C 1 259 THR 259 259 259 THR THR C . n 
C 1 260 SER 260 260 260 SER SER C . n 
C 1 261 PHE 261 261 261 PHE PHE C . n 
C 1 262 SER 262 262 262 SER SER C . n 
C 1 263 GLN 263 263 263 GLN GLN C . n 
D 1 1   MET 1   1   ?   ?   ?   D . n 
D 1 2   SER 2   2   ?   ?   ?   D . n 
D 1 3   LYS 3   3   ?   ?   ?   D . n 
D 1 4   TRP 4   4   4   TRP TRP D . n 
D 1 5   THR 5   5   5   THR THR D . n 
D 1 6   TYR 6   6   6   TYR TYR D . n 
D 1 7   PHE 7   7   7   PHE PHE D . n 
D 1 8   GLY 8   8   8   GLY GLY D . n 
D 1 9   PRO 9   9   9   PRO PRO D . n 
D 1 10  ASP 10  10  10  ASP ASP D . n 
D 1 11  GLY 11  11  11  GLY GLY D . n 
D 1 12  GLU 12  12  12  GLU GLU D . n 
D 1 13  ASN 13  13  13  ASN ASN D . n 
D 1 14  SER 14  14  14  SER SER D . n 
D 1 15  TRP 15  15  15  TRP TRP D . n 
D 1 16  SER 16  16  16  SER SER D . n 
D 1 17  LYS 17  17  17  LYS LYS D . n 
D 1 18  LYS 18  18  18  LYS LYS D . n 
D 1 19  TYR 19  19  19  TYR TYR D . n 
D 1 20  PRO 20  20  20  PRO PRO D . n 
D 1 21  SER 21  21  21  SER SER D . n 
D 1 22  CYS 22  22  22  CYS CYS D . n 
D 1 23  GLY 23  23  23  GLY GLY D . n 
D 1 24  GLY 24  24  24  GLY GLY D . n 
D 1 25  LEU 25  25  25  LEU LEU D . n 
D 1 26  LEU 26  26  26  LEU LEU D . n 
D 1 27  GLN 27  27  27  GLN GLN D . n 
D 1 28  SER 28  28  28  SER SER D . n 
D 1 29  PRO 29  29  29  PRO PRO D . n 
D 1 30  ILE 30  30  30  ILE ILE D . n 
D 1 31  ASP 31  31  31  ASP ASP D . n 
D 1 32  LEU 32  32  32  LEU LEU D . n 
D 1 33  HIS 33  33  33  HIS HIS D . n 
D 1 34  SER 34  34  34  SER SER D . n 
D 1 35  ASP 35  35  35  ASP ASP D . n 
D 1 36  ILE 36  36  36  ILE ILE D . n 
D 1 37  LEU 37  37  37  LEU LEU D . n 
D 1 38  GLN 38  38  38  GLN GLN D . n 
D 1 39  TYR 39  39  39  TYR TYR D . n 
D 1 40  ASP 40  40  40  ASP ASP D . n 
D 1 41  ALA 41  41  41  ALA ALA D . n 
D 1 42  SER 42  42  42  SER SER D . n 
D 1 43  LEU 43  43  43  LEU LEU D . n 
D 1 44  THR 44  44  44  THR THR D . n 
D 1 45  PRO 45  45  45  PRO PRO D . n 
D 1 46  LEU 46  46  46  LEU LEU D . n 
D 1 47  GLU 47  47  47  GLU GLU D . n 
D 1 48  PHE 48  48  48  PHE PHE D . n 
D 1 49  GLN 49  49  49  GLN GLN D . n 
D 1 50  GLY 50  50  50  GLY GLY D . n 
D 1 51  TYR 51  51  51  TYR TYR D . n 
D 1 52  ASN 52  52  52  ASN ASN D . n 
D 1 53  LEU 53  53  53  LEU LEU D . n 
D 1 54  SER 54  54  54  SER SER D . n 
D 1 55  ALA 55  55  55  ALA ALA D . n 
D 1 56  ASN 56  56  56  ASN ASN D . n 
D 1 57  LYS 57  57  57  LYS LYS D . n 
D 1 58  GLN 58  58  58  GLN GLN D . n 
D 1 59  PHE 59  59  59  PHE PHE D . n 
D 1 60  LEU 60  60  60  LEU LEU D . n 
D 1 61  LEU 61  61  61  LEU LEU D . n 
D 1 62  THR 62  62  62  THR THR D . n 
D 1 63  ASN 63  63  63  ASN ASN D . n 
D 1 64  ASN 64  64  64  ASN ASN D . n 
D 1 65  GLY 65  65  65  GLY GLY D . n 
D 1 66  HIS 66  66  66  HIS HIS D . n 
D 1 67  SER 67  67  67  SER SER D . n 
D 1 68  VAL 68  68  68  VAL VAL D . n 
D 1 69  LYS 69  69  69  LYS LYS D . n 
D 1 70  LEU 70  70  70  LEU LEU D . n 
D 1 71  ASN 71  71  71  ASN ASN D . n 
D 1 72  LEU 72  72  72  LEU LEU D . n 
D 1 73  PRO 73  73  73  PRO PRO D . n 
D 1 74  SER 74  74  74  SER SER D . n 
D 1 75  ASP 75  75  75  ASP ASP D . n 
D 1 76  MET 76  76  76  MET MET D . n 
D 1 77  HIS 77  77  77  HIS HIS D . n 
D 1 78  ILE 78  78  78  ILE ILE D . n 
D 1 79  GLN 79  79  79  GLN GLN D . n 
D 1 80  GLY 80  80  80  GLY GLY D . n 
D 1 81  LEU 81  81  81  LEU LEU D . n 
D 1 82  GLN 82  82  82  GLN GLN D . n 
D 1 83  SER 83  83  83  SER SER D . n 
D 1 84  ARG 84  84  84  ARG ARG D . n 
D 1 85  TYR 85  85  85  TYR TYR D . n 
D 1 86  SER 86  86  86  SER SER D . n 
D 1 87  ALA 87  87  87  ALA ALA D . n 
D 1 88  THR 88  88  88  THR THR D . n 
D 1 89  GLN 89  89  89  GLN GLN D . n 
D 1 90  LEU 90  90  90  LEU LEU D . n 
D 1 91  HIS 91  91  91  HIS HIS D . n 
D 1 92  LEU 92  92  92  LEU LEU D . n 
D 1 93  HIS 93  93  93  HIS HIS D . n 
D 1 94  TRP 94  94  94  TRP TRP D . n 
D 1 95  GLY 95  95  95  GLY GLY D . n 
D 1 96  ASN 96  96  96  ASN ASN D . n 
D 1 97  PRO 97  97  97  PRO PRO D . n 
D 1 98  ASN 98  98  98  ASN ASN D . n 
D 1 99  ASP 99  99  99  ASP ASP D . n 
D 1 100 PRO 100 100 100 PRO PRO D . n 
D 1 101 HIS 101 101 101 HIS HIS D . n 
D 1 102 GLY 102 102 102 GLY GLY D . n 
D 1 103 SER 103 103 103 SER SER D . n 
D 1 104 GLU 104 104 104 GLU GLU D . n 
D 1 105 HIS 105 105 105 HIS HIS D . n 
D 1 106 THR 106 106 106 THR THR D . n 
D 1 107 VAL 107 107 107 VAL VAL D . n 
D 1 108 SER 108 108 108 SER SER D . n 
D 1 109 GLY 109 109 109 GLY GLY D . n 
D 1 110 GLN 110 110 110 GLN GLN D . n 
D 1 111 HIS 111 111 111 HIS HIS D . n 
D 1 112 PHE 112 112 112 PHE PHE D . n 
D 1 113 ALA 113 113 113 ALA ALA D . n 
D 1 114 ALA 114 114 114 ALA ALA D . n 
D 1 115 GLU 115 115 115 GLU GLU D . n 
D 1 116 LEU 116 116 116 LEU LEU D . n 
D 1 117 HIS 117 117 117 HIS HIS D . n 
D 1 118 ILE 118 118 118 ILE ILE D . n 
D 1 119 VAL 119 119 119 VAL VAL D . n 
D 1 120 HIS 120 120 120 HIS HIS D . n 
D 1 121 TYR 121 121 121 TYR TYR D . n 
D 1 122 ASN 122 122 122 ASN ASN D . n 
D 1 123 SER 123 123 123 SER SER D . n 
D 1 124 ASP 124 124 124 ASP ASP D . n 
D 1 125 LEU 125 125 125 LEU LEU D . n 
D 1 126 TYR 126 126 126 TYR TYR D . n 
D 1 127 PRO 127 127 127 PRO PRO D . n 
D 1 128 ASP 128 128 128 ASP ASP D . n 
D 1 129 ALA 129 129 129 ALA ALA D . n 
D 1 130 SER 130 130 130 SER SER D . n 
D 1 131 THR 131 131 131 THR THR D . n 
D 1 132 ALA 132 132 132 ALA ALA D . n 
D 1 133 SER 133 133 133 SER SER D . n 
D 1 134 ASN 134 134 134 ASN ASN D . n 
D 1 135 LYS 135 135 135 LYS LYS D . n 
D 1 136 SER 136 136 136 SER SER D . n 
D 1 137 GLU 137 137 137 GLU GLU D . n 
D 1 138 GLY 138 138 138 GLY GLY D . n 
D 1 139 LEU 139 139 139 LEU LEU D . n 
D 1 140 ALA 140 140 140 ALA ALA D . n 
D 1 141 VAL 141 141 141 VAL VAL D . n 
D 1 142 LEU 142 142 142 LEU LEU D . n 
D 1 143 ALA 143 143 143 ALA ALA D . n 
D 1 144 VAL 144 144 144 VAL VAL D . n 
D 1 145 LEU 145 145 145 LEU LEU D . n 
D 1 146 ILE 146 146 146 ILE ILE D . n 
D 1 147 GLU 147 147 147 GLU GLU D . n 
D 1 148 MET 148 148 148 MET MET D . n 
D 1 149 GLY 149 149 149 GLY GLY D . n 
D 1 150 SER 150 150 150 SER SER D . n 
D 1 151 PHE 151 151 151 PHE PHE D . n 
D 1 152 ASN 152 152 152 ASN ASN D . n 
D 1 153 PRO 153 153 153 PRO PRO D . n 
D 1 154 SER 154 154 154 SER SER D . n 
D 1 155 TYR 155 155 155 TYR TYR D . n 
D 1 156 ASP 156 156 156 ASP ASP D . n 
D 1 157 LYS 157 157 157 LYS LYS D . n 
D 1 158 ILE 158 158 158 ILE ILE D . n 
D 1 159 PHE 159 159 159 PHE PHE D . n 
D 1 160 SER 160 160 160 SER SER D . n 
D 1 161 HIS 161 161 161 HIS HIS D . n 
D 1 162 LEU 162 162 162 LEU LEU D . n 
D 1 163 GLN 163 163 163 GLN GLN D . n 
D 1 164 HIS 164 164 164 HIS HIS D . n 
D 1 165 VAL 165 165 165 VAL VAL D . n 
D 1 166 LYS 166 166 166 LYS LYS D . n 
D 1 167 TYR 167 167 167 TYR TYR D . n 
D 1 168 LYS 168 168 168 LYS LYS D . n 
D 1 169 GLY 169 169 169 GLY GLY D . n 
D 1 170 GLN 170 170 170 GLN GLN D . n 
D 1 171 GLU 171 171 171 GLU GLU D . n 
D 1 172 ALA 172 172 172 ALA ALA D . n 
D 1 173 PHE 173 173 173 PHE PHE D . n 
D 1 174 VAL 174 174 174 VAL VAL D . n 
D 1 175 PRO 175 175 175 PRO PRO D . n 
D 1 176 GLY 176 176 176 GLY GLY D . n 
D 1 177 PHE 177 177 177 PHE PHE D . n 
D 1 178 ASN 178 178 178 ASN ASN D . n 
D 1 179 ILE 179 179 179 ILE ILE D . n 
D 1 180 GLU 180 180 180 GLU GLU D . n 
D 1 181 GLU 181 181 181 GLU GLU D . n 
D 1 182 LEU 182 182 182 LEU LEU D . n 
D 1 183 LEU 183 183 183 LEU LEU D . n 
D 1 184 PRO 184 184 184 PRO PRO D . n 
D 1 185 GLU 185 185 185 GLU GLU D . n 
D 1 186 ARG 186 186 186 ARG ARG D . n 
D 1 187 THR 187 187 187 THR THR D . n 
D 1 188 ALA 188 188 188 ALA ALA D . n 
D 1 189 GLU 189 189 189 GLU GLU D . n 
D 1 190 TYR 190 190 190 TYR TYR D . n 
D 1 191 TYR 191 191 191 TYR TYR D . n 
D 1 192 ARG 192 192 192 ARG ARG D . n 
D 1 193 TYR 193 193 193 TYR TYR D . n 
D 1 194 ARG 194 194 194 ARG ARG D . n 
D 1 195 GLY 195 195 195 GLY GLY D . n 
D 1 196 SER 196 196 196 SER SER D . n 
D 1 197 LEU 197 197 197 LEU LEU D . n 
D 1 198 THR 198 198 198 THR THR D . n 
D 1 199 THR 199 199 199 THR THR D . n 
D 1 200 PRO 200 200 200 PRO PRO D . n 
D 1 201 PRO 201 201 201 PRO PRO D . n 
D 1 202 CYS 202 202 202 CYS CYS D . n 
D 1 203 ASN 203 203 203 ASN ASN D . n 
D 1 204 PRO 204 204 204 PRO PRO D . n 
D 1 205 THR 205 205 205 THR THR D . n 
D 1 206 VAL 206 206 206 VAL VAL D . n 
D 1 207 LEU 207 207 207 LEU LEU D . n 
D 1 208 TRP 208 208 208 TRP TRP D . n 
D 1 209 THR 209 209 209 THR THR D . n 
D 1 210 VAL 210 210 210 VAL VAL D . n 
D 1 211 PHE 211 211 211 PHE PHE D . n 
D 1 212 ARG 212 212 212 ARG ARG D . n 
D 1 213 ASN 213 213 213 ASN ASN D . n 
D 1 214 PRO 214 214 214 PRO PRO D . n 
D 1 215 VAL 215 215 215 VAL VAL D . n 
D 1 216 GLN 216 216 216 GLN GLN D . n 
D 1 217 ILE 217 217 217 ILE ILE D . n 
D 1 218 SER 218 218 218 SER SER D . n 
D 1 219 GLN 219 219 219 GLN GLN D . n 
D 1 220 GLU 220 220 220 GLU GLU D . n 
D 1 221 GLN 221 221 221 GLN GLN D . n 
D 1 222 LEU 222 222 222 LEU LEU D . n 
D 1 223 LEU 223 223 223 LEU LEU D . n 
D 1 224 ALA 224 224 224 ALA ALA D . n 
D 1 225 LEU 225 225 225 LEU LEU D . n 
D 1 226 GLU 226 226 226 GLU GLU D . n 
D 1 227 THR 227 227 227 THR THR D . n 
D 1 228 ALA 228 228 228 ALA ALA D . n 
D 1 229 LEU 229 229 229 LEU LEU D . n 
D 1 230 TYR 230 230 230 TYR TYR D . n 
D 1 231 CYS 231 231 231 CYS CYS D . n 
D 1 232 THR 232 232 232 THR THR D . n 
D 1 233 HIS 233 233 233 HIS HIS D . n 
D 1 234 MET 234 234 234 MET MET D . n 
D 1 235 ASP 235 235 235 ASP ASP D . n 
D 1 236 ASP 236 236 236 ASP ASP D . n 
D 1 237 PRO 237 237 237 PRO PRO D . n 
D 1 238 SER 238 238 238 SER SER D . n 
D 1 239 PRO 239 239 239 PRO PRO D . n 
D 1 240 ARG 240 240 240 ARG ARG D . n 
D 1 241 GLU 241 241 241 GLU GLU D . n 
D 1 242 MET 242 242 242 MET MET D . n 
D 1 243 ILE 243 243 243 ILE ILE D . n 
D 1 244 ASN 244 244 244 ASN ASN D . n 
D 1 245 ASN 245 245 245 ASN ASN D . n 
D 1 246 PHE 246 246 246 PHE PHE D . n 
D 1 247 ARG 247 247 247 ARG ARG D . n 
D 1 248 GLN 248 248 248 GLN GLN D . n 
D 1 249 VAL 249 249 249 VAL VAL D . n 
D 1 250 GLN 250 250 250 GLN GLN D . n 
D 1 251 LYS 251 251 251 LYS LYS D . n 
D 1 252 PHE 252 252 252 PHE PHE D . n 
D 1 253 ASP 253 253 253 ASP ASP D . n 
D 1 254 GLU 254 254 254 GLU GLU D . n 
D 1 255 ARG 255 255 255 ARG ARG D . n 
D 1 256 LEU 256 256 256 LEU LEU D . n 
D 1 257 VAL 257 257 257 VAL VAL D . n 
D 1 258 TYR 258 258 258 TYR TYR D . n 
D 1 259 THR 259 259 259 THR THR D . n 
D 1 260 SER 260 260 260 SER SER D . n 
D 1 261 PHE 261 261 261 PHE PHE D . n 
D 1 262 SER 262 262 262 SER SER D . n 
D 1 263 GLN 263 263 263 GLN GLN D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 2 ZN  1   301 1   ZN  ZN  A . 
F 3 E1G 1   302 3   E1G E19 A . 
G 4 DMS 1   303 1   DMS DMS A . 
H 2 ZN  1   301 2   ZN  ZN  B . 
I 3 E1G 1   302 1   E1G E19 B . 
J 5 PEG 1   303 1   PEG PEE B . 
K 6 EDO 1   304 1   EDO EGL B . 
L 2 ZN  1   301 3   ZN  ZN  C . 
M 2 ZN  1   301 4   ZN  ZN  D . 
N 3 E1G 1   302 2   E1G E19 D . 
O 5 PEG 1   303 2   PEG PEE D . 
P 7 HOH 1   401 9   HOH HOH A . 
P 7 HOH 2   402 10  HOH HOH A . 
P 7 HOH 3   403 11  HOH HOH A . 
P 7 HOH 4   404 15  HOH HOH A . 
P 7 HOH 5   405 16  HOH HOH A . 
P 7 HOH 6   406 26  HOH HOH A . 
P 7 HOH 7   407 28  HOH HOH A . 
P 7 HOH 8   408 31  HOH HOH A . 
P 7 HOH 9   409 33  HOH HOH A . 
P 7 HOH 10  410 38  HOH HOH A . 
P 7 HOH 11  411 39  HOH HOH A . 
P 7 HOH 12  412 40  HOH HOH A . 
P 7 HOH 13  413 44  HOH HOH A . 
P 7 HOH 14  414 45  HOH HOH A . 
P 7 HOH 15  415 46  HOH HOH A . 
P 7 HOH 16  416 48  HOH HOH A . 
P 7 HOH 17  417 50  HOH HOH A . 
P 7 HOH 18  418 53  HOH HOH A . 
P 7 HOH 19  419 55  HOH HOH A . 
P 7 HOH 20  420 57  HOH HOH A . 
P 7 HOH 21  421 61  HOH HOH A . 
P 7 HOH 22  422 62  HOH HOH A . 
P 7 HOH 23  423 65  HOH HOH A . 
P 7 HOH 24  424 68  HOH HOH A . 
P 7 HOH 25  425 72  HOH HOH A . 
P 7 HOH 26  426 87  HOH HOH A . 
P 7 HOH 27  427 91  HOH HOH A . 
P 7 HOH 28  428 92  HOH HOH A . 
P 7 HOH 29  429 98  HOH HOH A . 
P 7 HOH 30  430 108 HOH HOH A . 
P 7 HOH 31  431 109 HOH HOH A . 
P 7 HOH 32  432 110 HOH HOH A . 
P 7 HOH 33  433 113 HOH HOH A . 
P 7 HOH 34  434 117 HOH HOH A . 
P 7 HOH 35  435 127 HOH HOH A . 
P 7 HOH 36  436 128 HOH HOH A . 
P 7 HOH 37  437 129 HOH HOH A . 
P 7 HOH 38  438 131 HOH HOH A . 
P 7 HOH 39  439 140 HOH HOH A . 
P 7 HOH 40  440 147 HOH HOH A . 
P 7 HOH 41  441 149 HOH HOH A . 
P 7 HOH 42  442 152 HOH HOH A . 
P 7 HOH 43  443 153 HOH HOH A . 
P 7 HOH 44  444 154 HOH HOH A . 
P 7 HOH 45  445 155 HOH HOH A . 
P 7 HOH 46  446 156 HOH HOH A . 
P 7 HOH 47  447 157 HOH HOH A . 
P 7 HOH 48  448 163 HOH HOH A . 
P 7 HOH 49  449 164 HOH HOH A . 
P 7 HOH 50  450 172 HOH HOH A . 
P 7 HOH 51  451 175 HOH HOH A . 
P 7 HOH 52  452 186 HOH HOH A . 
P 7 HOH 53  453 188 HOH HOH A . 
P 7 HOH 54  454 190 HOH HOH A . 
P 7 HOH 55  455 196 HOH HOH A . 
P 7 HOH 56  456 199 HOH HOH A . 
P 7 HOH 57  457 203 HOH HOH A . 
P 7 HOH 58  458 206 HOH HOH A . 
P 7 HOH 59  459 212 HOH HOH A . 
P 7 HOH 60  460 214 HOH HOH A . 
P 7 HOH 61  461 215 HOH HOH A . 
P 7 HOH 62  462 217 HOH HOH A . 
P 7 HOH 63  463 238 HOH HOH A . 
P 7 HOH 64  464 243 HOH HOH A . 
P 7 HOH 65  465 246 HOH HOH A . 
P 7 HOH 66  466 249 HOH HOH A . 
P 7 HOH 67  467 250 HOH HOH A . 
P 7 HOH 68  468 251 HOH HOH A . 
P 7 HOH 69  469 262 HOH HOH A . 
P 7 HOH 70  470 263 HOH HOH A . 
P 7 HOH 71  471 264 HOH HOH A . 
P 7 HOH 72  472 269 HOH HOH A . 
P 7 HOH 73  473 273 HOH HOH A . 
P 7 HOH 74  474 277 HOH HOH A . 
P 7 HOH 75  475 279 HOH HOH A . 
P 7 HOH 76  476 280 HOH HOH A . 
P 7 HOH 77  477 283 HOH HOH A . 
P 7 HOH 78  478 285 HOH HOH A . 
P 7 HOH 79  479 287 HOH HOH A . 
P 7 HOH 80  480 292 HOH HOH A . 
P 7 HOH 81  481 293 HOH HOH A . 
P 7 HOH 82  482 297 HOH HOH A . 
P 7 HOH 83  483 306 HOH HOH A . 
P 7 HOH 84  484 308 HOH HOH A . 
P 7 HOH 85  485 310 HOH HOH A . 
P 7 HOH 86  486 313 HOH HOH A . 
P 7 HOH 87  487 318 HOH HOH A . 
P 7 HOH 88  488 329 HOH HOH A . 
P 7 HOH 89  489 331 HOH HOH A . 
P 7 HOH 90  490 332 HOH HOH A . 
P 7 HOH 91  491 334 HOH HOH A . 
P 7 HOH 92  492 338 HOH HOH A . 
P 7 HOH 93  493 339 HOH HOH A . 
P 7 HOH 94  494 340 HOH HOH A . 
P 7 HOH 95  495 341 HOH HOH A . 
P 7 HOH 96  496 342 HOH HOH A . 
P 7 HOH 97  497 349 HOH HOH A . 
P 7 HOH 98  498 353 HOH HOH A . 
P 7 HOH 99  499 360 HOH HOH A . 
P 7 HOH 100 500 364 HOH HOH A . 
P 7 HOH 101 501 372 HOH HOH A . 
P 7 HOH 102 502 375 HOH HOH A . 
P 7 HOH 103 503 376 HOH HOH A . 
P 7 HOH 104 504 384 HOH HOH A . 
P 7 HOH 105 505 395 HOH HOH A . 
P 7 HOH 106 506 397 HOH HOH A . 
P 7 HOH 107 507 407 HOH HOH A . 
P 7 HOH 108 508 409 HOH HOH A . 
P 7 HOH 109 509 410 HOH HOH A . 
P 7 HOH 110 510 412 HOH HOH A . 
P 7 HOH 111 511 415 HOH HOH A . 
P 7 HOH 112 512 418 HOH HOH A . 
P 7 HOH 113 513 419 HOH HOH A . 
P 7 HOH 114 514 422 HOH HOH A . 
P 7 HOH 115 515 426 HOH HOH A . 
P 7 HOH 116 516 442 HOH HOH A . 
P 7 HOH 117 517 449 HOH HOH A . 
P 7 HOH 118 518 454 HOH HOH A . 
P 7 HOH 119 519 457 HOH HOH A . 
P 7 HOH 120 520 465 HOH HOH A . 
P 7 HOH 121 521 468 HOH HOH A . 
P 7 HOH 122 522 476 HOH HOH A . 
P 7 HOH 123 523 478 HOH HOH A . 
P 7 HOH 124 524 485 HOH HOH A . 
P 7 HOH 125 525 487 HOH HOH A . 
P 7 HOH 126 526 488 HOH HOH A . 
P 7 HOH 127 527 490 HOH HOH A . 
P 7 HOH 128 528 498 HOH HOH A . 
P 7 HOH 129 529 505 HOH HOH A . 
P 7 HOH 130 530 506 HOH HOH A . 
P 7 HOH 131 531 507 HOH HOH A . 
P 7 HOH 132 532 509 HOH HOH A . 
P 7 HOH 133 533 510 HOH HOH A . 
P 7 HOH 134 534 511 HOH HOH A . 
P 7 HOH 135 535 512 HOH HOH A . 
P 7 HOH 136 536 513 HOH HOH A . 
P 7 HOH 137 537 514 HOH HOH A . 
P 7 HOH 138 538 515 HOH HOH A . 
P 7 HOH 139 539 516 HOH HOH A . 
P 7 HOH 140 540 517 HOH HOH A . 
P 7 HOH 141 541 518 HOH HOH A . 
P 7 HOH 142 542 519 HOH HOH A . 
P 7 HOH 143 543 520 HOH HOH A . 
P 7 HOH 144 544 521 HOH HOH A . 
P 7 HOH 145 545 522 HOH HOH A . 
P 7 HOH 146 546 523 HOH HOH A . 
P 7 HOH 147 547 524 HOH HOH A . 
P 7 HOH 148 548 525 HOH HOH A . 
P 7 HOH 149 549 526 HOH HOH A . 
P 7 HOH 150 550 527 HOH HOH A . 
P 7 HOH 151 551 528 HOH HOH A . 
P 7 HOH 152 552 529 HOH HOH A . 
P 7 HOH 153 553 530 HOH HOH A . 
P 7 HOH 154 554 531 HOH HOH A . 
P 7 HOH 155 555 532 HOH HOH A . 
P 7 HOH 156 556 533 HOH HOH A . 
P 7 HOH 157 557 536 HOH HOH A . 
P 7 HOH 158 558 538 HOH HOH A . 
P 7 HOH 159 559 546 HOH HOH A . 
P 7 HOH 160 560 594 HOH HOH A . 
P 7 HOH 161 561 595 HOH HOH A . 
P 7 HOH 162 562 596 HOH HOH A . 
P 7 HOH 163 563 599 HOH HOH A . 
P 7 HOH 164 564 601 HOH HOH A . 
P 7 HOH 165 565 602 HOH HOH A . 
P 7 HOH 166 566 607 HOH HOH A . 
P 7 HOH 167 567 608 HOH HOH A . 
P 7 HOH 168 568 611 HOH HOH A . 
P 7 HOH 169 569 612 HOH HOH A . 
P 7 HOH 170 570 636 HOH HOH A . 
P 7 HOH 171 571 638 HOH HOH A . 
P 7 HOH 172 572 640 HOH HOH A . 
P 7 HOH 173 573 641 HOH HOH A . 
P 7 HOH 174 574 642 HOH HOH A . 
P 7 HOH 175 575 643 HOH HOH A . 
P 7 HOH 176 576 644 HOH HOH A . 
P 7 HOH 177 577 645 HOH HOH A . 
P 7 HOH 178 578 646 HOH HOH A . 
P 7 HOH 179 579 647 HOH HOH A . 
P 7 HOH 180 580 649 HOH HOH A . 
P 7 HOH 181 581 650 HOH HOH A . 
P 7 HOH 182 582 651 HOH HOH A . 
P 7 HOH 183 583 652 HOH HOH A . 
P 7 HOH 184 584 653 HOH HOH A . 
P 7 HOH 185 585 654 HOH HOH A . 
P 7 HOH 186 586 655 HOH HOH A . 
P 7 HOH 187 587 656 HOH HOH A . 
P 7 HOH 188 588 657 HOH HOH A . 
P 7 HOH 189 589 658 HOH HOH A . 
P 7 HOH 190 590 712 HOH HOH A . 
P 7 HOH 191 591 713 HOH HOH A . 
P 7 HOH 192 592 715 HOH HOH A . 
P 7 HOH 193 593 721 HOH HOH A . 
P 7 HOH 194 594 742 HOH HOH A . 
P 7 HOH 195 595 749 HOH HOH A . 
P 7 HOH 196 596 756 HOH HOH A . 
P 7 HOH 197 597 761 HOH HOH A . 
P 7 HOH 198 598 767 HOH HOH A . 
P 7 HOH 199 599 768 HOH HOH A . 
P 7 HOH 200 600 777 HOH HOH A . 
P 7 HOH 201 601 786 HOH HOH A . 
P 7 HOH 202 602 788 HOH HOH A . 
P 7 HOH 203 603 794 HOH HOH A . 
P 7 HOH 204 604 796 HOH HOH A . 
P 7 HOH 205 605 797 HOH HOH A . 
P 7 HOH 206 606 798 HOH HOH A . 
P 7 HOH 207 607 800 HOH HOH A . 
P 7 HOH 208 608 802 HOH HOH A . 
P 7 HOH 209 609 803 HOH HOH A . 
P 7 HOH 210 610 804 HOH HOH A . 
P 7 HOH 211 611 805 HOH HOH A . 
P 7 HOH 212 612 806 HOH HOH A . 
P 7 HOH 213 613 807 HOH HOH A . 
P 7 HOH 214 614 808 HOH HOH A . 
P 7 HOH 215 615 809 HOH HOH A . 
P 7 HOH 216 616 810 HOH HOH A . 
P 7 HOH 217 617 811 HOH HOH A . 
P 7 HOH 218 618 812 HOH HOH A . 
P 7 HOH 219 619 813 HOH HOH A . 
P 7 HOH 220 620 815 HOH HOH A . 
P 7 HOH 221 621 816 HOH HOH A . 
P 7 HOH 222 622 817 HOH HOH A . 
P 7 HOH 223 623 818 HOH HOH A . 
P 7 HOH 224 624 819 HOH HOH A . 
P 7 HOH 225 625 820 HOH HOH A . 
P 7 HOH 226 626 821 HOH HOH A . 
P 7 HOH 227 627 822 HOH HOH A . 
P 7 HOH 228 628 898 HOH HOH A . 
P 7 HOH 229 629 899 HOH HOH A . 
P 7 HOH 230 630 902 HOH HOH A . 
P 7 HOH 231 631 908 HOH HOH A . 
P 7 HOH 232 632 911 HOH HOH A . 
P 7 HOH 233 633 912 HOH HOH A . 
P 7 HOH 234 634 913 HOH HOH A . 
P 7 HOH 235 635 914 HOH HOH A . 
P 7 HOH 236 636 915 HOH HOH A . 
P 7 HOH 237 637 916 HOH HOH A . 
P 7 HOH 238 638 917 HOH HOH A . 
P 7 HOH 239 639 918 HOH HOH A . 
P 7 HOH 240 640 919 HOH HOH A . 
P 7 HOH 241 641 920 HOH HOH A . 
P 7 HOH 242 642 921 HOH HOH A . 
P 7 HOH 243 643 922 HOH HOH A . 
P 7 HOH 244 644 923 HOH HOH A . 
P 7 HOH 245 645 924 HOH HOH A . 
P 7 HOH 246 646 925 HOH HOH A . 
P 7 HOH 247 647 926 HOH HOH A . 
P 7 HOH 248 648 927 HOH HOH A . 
P 7 HOH 249 649 928 HOH HOH A . 
P 7 HOH 250 650 929 HOH HOH A . 
P 7 HOH 251 651 936 HOH HOH A . 
P 7 HOH 252 652 964 HOH HOH A . 
P 7 HOH 253 653 965 HOH HOH A . 
P 7 HOH 254 654 966 HOH HOH A . 
P 7 HOH 255 655 967 HOH HOH A . 
P 7 HOH 256 656 968 HOH HOH A . 
P 7 HOH 257 657 969 HOH HOH A . 
P 7 HOH 258 658 992 HOH HOH A . 
Q 7 HOH 1   401 1   HOH HOH B . 
Q 7 HOH 2   402 14  HOH HOH B . 
Q 7 HOH 3   403 17  HOH HOH B . 
Q 7 HOH 4   404 21  HOH HOH B . 
Q 7 HOH 5   405 23  HOH HOH B . 
Q 7 HOH 6   406 24  HOH HOH B . 
Q 7 HOH 7   407 25  HOH HOH B . 
Q 7 HOH 8   408 29  HOH HOH B . 
Q 7 HOH 9   409 30  HOH HOH B . 
Q 7 HOH 10  410 34  HOH HOH B . 
Q 7 HOH 11  411 42  HOH HOH B . 
Q 7 HOH 12  412 43  HOH HOH B . 
Q 7 HOH 13  413 47  HOH HOH B . 
Q 7 HOH 14  414 54  HOH HOH B . 
Q 7 HOH 15  415 58  HOH HOH B . 
Q 7 HOH 16  416 60  HOH HOH B . 
Q 7 HOH 17  417 63  HOH HOH B . 
Q 7 HOH 18  418 64  HOH HOH B . 
Q 7 HOH 19  419 67  HOH HOH B . 
Q 7 HOH 20  420 70  HOH HOH B . 
Q 7 HOH 21  421 73  HOH HOH B . 
Q 7 HOH 22  422 74  HOH HOH B . 
Q 7 HOH 23  423 78  HOH HOH B . 
Q 7 HOH 24  424 80  HOH HOH B . 
Q 7 HOH 25  425 84  HOH HOH B . 
Q 7 HOH 26  426 86  HOH HOH B . 
Q 7 HOH 27  427 90  HOH HOH B . 
Q 7 HOH 28  428 94  HOH HOH B . 
Q 7 HOH 29  429 100 HOH HOH B . 
Q 7 HOH 30  430 103 HOH HOH B . 
Q 7 HOH 31  431 106 HOH HOH B . 
Q 7 HOH 32  432 115 HOH HOH B . 
Q 7 HOH 33  433 118 HOH HOH B . 
Q 7 HOH 34  434 119 HOH HOH B . 
Q 7 HOH 35  435 122 HOH HOH B . 
Q 7 HOH 36  436 123 HOH HOH B . 
Q 7 HOH 37  437 124 HOH HOH B . 
Q 7 HOH 38  438 132 HOH HOH B . 
Q 7 HOH 39  439 134 HOH HOH B . 
Q 7 HOH 40  440 136 HOH HOH B . 
Q 7 HOH 41  441 139 HOH HOH B . 
Q 7 HOH 42  442 145 HOH HOH B . 
Q 7 HOH 43  443 148 HOH HOH B . 
Q 7 HOH 44  444 151 HOH HOH B . 
Q 7 HOH 45  445 165 HOH HOH B . 
Q 7 HOH 46  446 166 HOH HOH B . 
Q 7 HOH 47  447 167 HOH HOH B . 
Q 7 HOH 48  448 174 HOH HOH B . 
Q 7 HOH 49  449 176 HOH HOH B . 
Q 7 HOH 50  450 177 HOH HOH B . 
Q 7 HOH 51  451 179 HOH HOH B . 
Q 7 HOH 52  452 181 HOH HOH B . 
Q 7 HOH 53  453 182 HOH HOH B . 
Q 7 HOH 54  454 183 HOH HOH B . 
Q 7 HOH 55  455 185 HOH HOH B . 
Q 7 HOH 56  456 191 HOH HOH B . 
Q 7 HOH 57  457 192 HOH HOH B . 
Q 7 HOH 58  458 197 HOH HOH B . 
Q 7 HOH 59  459 201 HOH HOH B . 
Q 7 HOH 60  460 204 HOH HOH B . 
Q 7 HOH 61  461 216 HOH HOH B . 
Q 7 HOH 62  462 218 HOH HOH B . 
Q 7 HOH 63  463 221 HOH HOH B . 
Q 7 HOH 64  464 227 HOH HOH B . 
Q 7 HOH 65  465 230 HOH HOH B . 
Q 7 HOH 66  466 233 HOH HOH B . 
Q 7 HOH 67  467 236 HOH HOH B . 
Q 7 HOH 68  468 237 HOH HOH B . 
Q 7 HOH 69  469 240 HOH HOH B . 
Q 7 HOH 70  470 248 HOH HOH B . 
Q 7 HOH 71  471 253 HOH HOH B . 
Q 7 HOH 72  472 254 HOH HOH B . 
Q 7 HOH 73  473 257 HOH HOH B . 
Q 7 HOH 74  474 265 HOH HOH B . 
Q 7 HOH 75  475 276 HOH HOH B . 
Q 7 HOH 76  476 278 HOH HOH B . 
Q 7 HOH 77  477 286 HOH HOH B . 
Q 7 HOH 78  478 289 HOH HOH B . 
Q 7 HOH 79  479 290 HOH HOH B . 
Q 7 HOH 80  480 294 HOH HOH B . 
Q 7 HOH 81  481 298 HOH HOH B . 
Q 7 HOH 82  482 299 HOH HOH B . 
Q 7 HOH 83  483 300 HOH HOH B . 
Q 7 HOH 84  484 302 HOH HOH B . 
Q 7 HOH 85  485 305 HOH HOH B . 
Q 7 HOH 86  486 309 HOH HOH B . 
Q 7 HOH 87  487 314 HOH HOH B . 
Q 7 HOH 88  488 322 HOH HOH B . 
Q 7 HOH 89  489 326 HOH HOH B . 
Q 7 HOH 90  490 327 HOH HOH B . 
Q 7 HOH 91  491 328 HOH HOH B . 
Q 7 HOH 92  492 336 HOH HOH B . 
Q 7 HOH 93  493 343 HOH HOH B . 
Q 7 HOH 94  494 346 HOH HOH B . 
Q 7 HOH 95  495 347 HOH HOH B . 
Q 7 HOH 96  496 363 HOH HOH B . 
Q 7 HOH 97  497 369 HOH HOH B . 
Q 7 HOH 98  498 374 HOH HOH B . 
Q 7 HOH 99  499 377 HOH HOH B . 
Q 7 HOH 100 500 388 HOH HOH B . 
Q 7 HOH 101 501 390 HOH HOH B . 
Q 7 HOH 102 502 398 HOH HOH B . 
Q 7 HOH 103 503 400 HOH HOH B . 
Q 7 HOH 104 504 402 HOH HOH B . 
Q 7 HOH 105 505 413 HOH HOH B . 
Q 7 HOH 106 506 414 HOH HOH B . 
Q 7 HOH 107 507 432 HOH HOH B . 
Q 7 HOH 108 508 438 HOH HOH B . 
Q 7 HOH 109 509 441 HOH HOH B . 
Q 7 HOH 110 510 446 HOH HOH B . 
Q 7 HOH 111 511 447 HOH HOH B . 
Q 7 HOH 112 512 448 HOH HOH B . 
Q 7 HOH 113 513 450 HOH HOH B . 
Q 7 HOH 114 514 459 HOH HOH B . 
Q 7 HOH 115 515 461 HOH HOH B . 
Q 7 HOH 116 516 462 HOH HOH B . 
Q 7 HOH 117 517 463 HOH HOH B . 
Q 7 HOH 118 518 467 HOH HOH B . 
Q 7 HOH 119 519 480 HOH HOH B . 
Q 7 HOH 120 520 481 HOH HOH B . 
Q 7 HOH 121 521 482 HOH HOH B . 
Q 7 HOH 122 522 483 HOH HOH B . 
Q 7 HOH 123 523 486 HOH HOH B . 
Q 7 HOH 124 524 489 HOH HOH B . 
Q 7 HOH 125 525 493 HOH HOH B . 
Q 7 HOH 126 526 503 HOH HOH B . 
Q 7 HOH 127 527 504 HOH HOH B . 
Q 7 HOH 128 528 508 HOH HOH B . 
Q 7 HOH 129 529 534 HOH HOH B . 
Q 7 HOH 130 530 535 HOH HOH B . 
Q 7 HOH 131 531 537 HOH HOH B . 
Q 7 HOH 132 532 539 HOH HOH B . 
Q 7 HOH 133 533 540 HOH HOH B . 
Q 7 HOH 134 534 541 HOH HOH B . 
Q 7 HOH 135 535 542 HOH HOH B . 
Q 7 HOH 136 536 543 HOH HOH B . 
Q 7 HOH 137 537 544 HOH HOH B . 
Q 7 HOH 138 538 545 HOH HOH B . 
Q 7 HOH 139 539 547 HOH HOH B . 
Q 7 HOH 140 540 548 HOH HOH B . 
Q 7 HOH 141 541 549 HOH HOH B . 
Q 7 HOH 142 542 550 HOH HOH B . 
Q 7 HOH 143 543 551 HOH HOH B . 
Q 7 HOH 144 544 552 HOH HOH B . 
Q 7 HOH 145 545 584 HOH HOH B . 
Q 7 HOH 146 546 585 HOH HOH B . 
Q 7 HOH 147 547 597 HOH HOH B . 
Q 7 HOH 148 548 598 HOH HOH B . 
Q 7 HOH 149 549 628 HOH HOH B . 
Q 7 HOH 150 550 629 HOH HOH B . 
Q 7 HOH 151 551 630 HOH HOH B . 
Q 7 HOH 152 552 631 HOH HOH B . 
Q 7 HOH 153 553 639 HOH HOH B . 
Q 7 HOH 154 554 648 HOH HOH B . 
Q 7 HOH 155 555 660 HOH HOH B . 
Q 7 HOH 156 556 661 HOH HOH B . 
Q 7 HOH 157 557 662 HOH HOH B . 
Q 7 HOH 158 558 663 HOH HOH B . 
Q 7 HOH 159 559 664 HOH HOH B . 
Q 7 HOH 160 560 665 HOH HOH B . 
Q 7 HOH 161 561 666 HOH HOH B . 
Q 7 HOH 162 562 667 HOH HOH B . 
Q 7 HOH 163 563 668 HOH HOH B . 
Q 7 HOH 164 564 669 HOH HOH B . 
Q 7 HOH 165 565 670 HOH HOH B . 
Q 7 HOH 166 566 702 HOH HOH B . 
Q 7 HOH 167 567 704 HOH HOH B . 
Q 7 HOH 168 568 706 HOH HOH B . 
Q 7 HOH 169 569 709 HOH HOH B . 
Q 7 HOH 170 570 716 HOH HOH B . 
Q 7 HOH 171 571 717 HOH HOH B . 
Q 7 HOH 172 572 718 HOH HOH B . 
Q 7 HOH 173 573 719 HOH HOH B . 
Q 7 HOH 174 574 720 HOH HOH B . 
Q 7 HOH 175 575 723 HOH HOH B . 
Q 7 HOH 176 576 724 HOH HOH B . 
Q 7 HOH 177 577 726 HOH HOH B . 
Q 7 HOH 178 578 729 HOH HOH B . 
Q 7 HOH 179 579 732 HOH HOH B . 
Q 7 HOH 180 580 737 HOH HOH B . 
Q 7 HOH 181 581 739 HOH HOH B . 
Q 7 HOH 182 582 741 HOH HOH B . 
Q 7 HOH 183 583 745 HOH HOH B . 
Q 7 HOH 184 584 747 HOH HOH B . 
Q 7 HOH 185 585 751 HOH HOH B . 
Q 7 HOH 186 586 754 HOH HOH B . 
Q 7 HOH 187 587 755 HOH HOH B . 
Q 7 HOH 188 588 757 HOH HOH B . 
Q 7 HOH 189 589 763 HOH HOH B . 
Q 7 HOH 190 590 764 HOH HOH B . 
Q 7 HOH 191 591 765 HOH HOH B . 
Q 7 HOH 192 592 774 HOH HOH B . 
Q 7 HOH 193 593 776 HOH HOH B . 
Q 7 HOH 194 594 781 HOH HOH B . 
Q 7 HOH 195 595 782 HOH HOH B . 
Q 7 HOH 196 596 791 HOH HOH B . 
Q 7 HOH 197 597 792 HOH HOH B . 
Q 7 HOH 198 598 799 HOH HOH B . 
Q 7 HOH 199 599 801 HOH HOH B . 
Q 7 HOH 200 600 814 HOH HOH B . 
Q 7 HOH 201 601 823 HOH HOH B . 
Q 7 HOH 202 602 824 HOH HOH B . 
Q 7 HOH 203 603 825 HOH HOH B . 
Q 7 HOH 204 604 826 HOH HOH B . 
Q 7 HOH 205 605 827 HOH HOH B . 
Q 7 HOH 206 606 829 HOH HOH B . 
Q 7 HOH 207 607 830 HOH HOH B . 
Q 7 HOH 208 608 831 HOH HOH B . 
Q 7 HOH 209 609 832 HOH HOH B . 
Q 7 HOH 210 610 833 HOH HOH B . 
Q 7 HOH 211 611 834 HOH HOH B . 
Q 7 HOH 212 612 835 HOH HOH B . 
Q 7 HOH 213 613 836 HOH HOH B . 
Q 7 HOH 214 614 837 HOH HOH B . 
Q 7 HOH 215 615 838 HOH HOH B . 
Q 7 HOH 216 616 839 HOH HOH B . 
Q 7 HOH 217 617 840 HOH HOH B . 
Q 7 HOH 218 618 841 HOH HOH B . 
Q 7 HOH 219 619 845 HOH HOH B . 
Q 7 HOH 220 620 846 HOH HOH B . 
Q 7 HOH 221 621 847 HOH HOH B . 
Q 7 HOH 222 622 848 HOH HOH B . 
Q 7 HOH 223 623 849 HOH HOH B . 
Q 7 HOH 224 624 850 HOH HOH B . 
Q 7 HOH 225 625 851 HOH HOH B . 
Q 7 HOH 226 626 852 HOH HOH B . 
Q 7 HOH 227 627 853 HOH HOH B . 
Q 7 HOH 228 628 854 HOH HOH B . 
Q 7 HOH 229 629 855 HOH HOH B . 
Q 7 HOH 230 630 856 HOH HOH B . 
Q 7 HOH 231 631 857 HOH HOH B . 
Q 7 HOH 232 632 860 HOH HOH B . 
Q 7 HOH 233 633 904 HOH HOH B . 
Q 7 HOH 234 634 907 HOH HOH B . 
Q 7 HOH 235 635 930 HOH HOH B . 
Q 7 HOH 236 636 931 HOH HOH B . 
Q 7 HOH 237 637 932 HOH HOH B . 
Q 7 HOH 238 638 933 HOH HOH B . 
Q 7 HOH 239 639 934 HOH HOH B . 
Q 7 HOH 240 640 935 HOH HOH B . 
Q 7 HOH 241 641 937 HOH HOH B . 
Q 7 HOH 242 642 940 HOH HOH B . 
Q 7 HOH 243 643 941 HOH HOH B . 
Q 7 HOH 244 644 942 HOH HOH B . 
Q 7 HOH 245 645 943 HOH HOH B . 
Q 7 HOH 246 646 944 HOH HOH B . 
Q 7 HOH 247 647 945 HOH HOH B . 
Q 7 HOH 248 648 946 HOH HOH B . 
Q 7 HOH 249 649 947 HOH HOH B . 
Q 7 HOH 250 650 970 HOH HOH B . 
Q 7 HOH 251 651 971 HOH HOH B . 
Q 7 HOH 252 652 972 HOH HOH B . 
Q 7 HOH 253 653 990 HOH HOH B . 
Q 7 HOH 254 654 994 HOH HOH B . 
Q 7 HOH 255 655 995 HOH HOH B . 
R 7 HOH 1   401 184 HOH HOH C . 
R 7 HOH 2   402 380 HOH HOH C . 
R 7 HOH 3   403 382 HOH HOH C . 
R 7 HOH 4   404 466 HOH HOH C . 
R 7 HOH 5   405 2   HOH HOH C . 
R 7 HOH 6   406 4   HOH HOH C . 
R 7 HOH 7   407 6   HOH HOH C . 
R 7 HOH 8   408 8   HOH HOH C . 
R 7 HOH 9   409 13  HOH HOH C . 
R 7 HOH 10  410 18  HOH HOH C . 
R 7 HOH 11  411 32  HOH HOH C . 
R 7 HOH 12  412 35  HOH HOH C . 
R 7 HOH 13  413 41  HOH HOH C . 
R 7 HOH 14  414 49  HOH HOH C . 
R 7 HOH 15  415 51  HOH HOH C . 
R 7 HOH 16  416 52  HOH HOH C . 
R 7 HOH 17  417 56  HOH HOH C . 
R 7 HOH 18  418 59  HOH HOH C . 
R 7 HOH 19  419 71  HOH HOH C . 
R 7 HOH 20  420 76  HOH HOH C . 
R 7 HOH 21  421 79  HOH HOH C . 
R 7 HOH 22  422 85  HOH HOH C . 
R 7 HOH 23  423 88  HOH HOH C . 
R 7 HOH 24  424 89  HOH HOH C . 
R 7 HOH 25  425 95  HOH HOH C . 
R 7 HOH 26  426 101 HOH HOH C . 
R 7 HOH 27  427 102 HOH HOH C . 
R 7 HOH 28  428 112 HOH HOH C . 
R 7 HOH 29  429 114 HOH HOH C . 
R 7 HOH 30  430 135 HOH HOH C . 
R 7 HOH 31  431 138 HOH HOH C . 
R 7 HOH 32  432 142 HOH HOH C . 
R 7 HOH 33  433 144 HOH HOH C . 
R 7 HOH 34  434 146 HOH HOH C . 
R 7 HOH 35  435 158 HOH HOH C . 
R 7 HOH 36  436 168 HOH HOH C . 
R 7 HOH 37  437 170 HOH HOH C . 
R 7 HOH 38  438 173 HOH HOH C . 
R 7 HOH 39  439 178 HOH HOH C . 
R 7 HOH 40  440 180 HOH HOH C . 
R 7 HOH 41  441 187 HOH HOH C . 
R 7 HOH 42  442 193 HOH HOH C . 
R 7 HOH 43  443 195 HOH HOH C . 
R 7 HOH 44  444 202 HOH HOH C . 
R 7 HOH 45  445 205 HOH HOH C . 
R 7 HOH 46  446 211 HOH HOH C . 
R 7 HOH 47  447 213 HOH HOH C . 
R 7 HOH 48  448 220 HOH HOH C . 
R 7 HOH 49  449 223 HOH HOH C . 
R 7 HOH 50  450 224 HOH HOH C . 
R 7 HOH 51  451 225 HOH HOH C . 
R 7 HOH 52  452 226 HOH HOH C . 
R 7 HOH 53  453 229 HOH HOH C . 
R 7 HOH 54  454 239 HOH HOH C . 
R 7 HOH 55  455 241 HOH HOH C . 
R 7 HOH 56  456 247 HOH HOH C . 
R 7 HOH 57  457 258 HOH HOH C . 
R 7 HOH 58  458 268 HOH HOH C . 
R 7 HOH 59  459 270 HOH HOH C . 
R 7 HOH 60  460 271 HOH HOH C . 
R 7 HOH 61  461 274 HOH HOH C . 
R 7 HOH 62  462 288 HOH HOH C . 
R 7 HOH 63  463 301 HOH HOH C . 
R 7 HOH 64  464 304 HOH HOH C . 
R 7 HOH 65  465 311 HOH HOH C . 
R 7 HOH 66  466 317 HOH HOH C . 
R 7 HOH 67  467 323 HOH HOH C . 
R 7 HOH 68  468 324 HOH HOH C . 
R 7 HOH 69  469 330 HOH HOH C . 
R 7 HOH 70  470 337 HOH HOH C . 
R 7 HOH 71  471 345 HOH HOH C . 
R 7 HOH 72  472 348 HOH HOH C . 
R 7 HOH 73  473 351 HOH HOH C . 
R 7 HOH 74  474 352 HOH HOH C . 
R 7 HOH 75  475 354 HOH HOH C . 
R 7 HOH 76  476 355 HOH HOH C . 
R 7 HOH 77  477 357 HOH HOH C . 
R 7 HOH 78  478 359 HOH HOH C . 
R 7 HOH 79  479 361 HOH HOH C . 
R 7 HOH 80  480 366 HOH HOH C . 
R 7 HOH 81  481 367 HOH HOH C . 
R 7 HOH 82  482 370 HOH HOH C . 
R 7 HOH 83  483 373 HOH HOH C . 
R 7 HOH 84  484 378 HOH HOH C . 
R 7 HOH 85  485 381 HOH HOH C . 
R 7 HOH 86  486 389 HOH HOH C . 
R 7 HOH 87  487 392 HOH HOH C . 
R 7 HOH 88  488 393 HOH HOH C . 
R 7 HOH 89  489 403 HOH HOH C . 
R 7 HOH 90  490 406 HOH HOH C . 
R 7 HOH 91  491 416 HOH HOH C . 
R 7 HOH 92  492 420 HOH HOH C . 
R 7 HOH 93  493 423 HOH HOH C . 
R 7 HOH 94  494 427 HOH HOH C . 
R 7 HOH 95  495 428 HOH HOH C . 
R 7 HOH 96  496 431 HOH HOH C . 
R 7 HOH 97  497 433 HOH HOH C . 
R 7 HOH 98  498 434 HOH HOH C . 
R 7 HOH 99  499 437 HOH HOH C . 
R 7 HOH 100 500 440 HOH HOH C . 
R 7 HOH 101 501 443 HOH HOH C . 
R 7 HOH 102 502 451 HOH HOH C . 
R 7 HOH 103 503 453 HOH HOH C . 
R 7 HOH 104 504 456 HOH HOH C . 
R 7 HOH 105 505 458 HOH HOH C . 
R 7 HOH 106 506 464 HOH HOH C . 
R 7 HOH 107 507 471 HOH HOH C . 
R 7 HOH 108 508 472 HOH HOH C . 
R 7 HOH 109 509 491 HOH HOH C . 
R 7 HOH 110 510 492 HOH HOH C . 
R 7 HOH 111 511 499 HOH HOH C . 
R 7 HOH 112 512 500 HOH HOH C . 
R 7 HOH 113 513 501 HOH HOH C . 
R 7 HOH 114 514 502 HOH HOH C . 
R 7 HOH 115 515 553 HOH HOH C . 
R 7 HOH 116 516 554 HOH HOH C . 
R 7 HOH 117 517 555 HOH HOH C . 
R 7 HOH 118 518 556 HOH HOH C . 
R 7 HOH 119 519 557 HOH HOH C . 
R 7 HOH 120 520 558 HOH HOH C . 
R 7 HOH 121 521 561 HOH HOH C . 
R 7 HOH 122 522 562 HOH HOH C . 
R 7 HOH 123 523 563 HOH HOH C . 
R 7 HOH 124 524 564 HOH HOH C . 
R 7 HOH 125 525 571 HOH HOH C . 
R 7 HOH 126 526 586 HOH HOH C . 
R 7 HOH 127 527 587 HOH HOH C . 
R 7 HOH 128 528 588 HOH HOH C . 
R 7 HOH 129 529 589 HOH HOH C . 
R 7 HOH 130 530 590 HOH HOH C . 
R 7 HOH 131 531 591 HOH HOH C . 
R 7 HOH 132 532 614 HOH HOH C . 
R 7 HOH 133 533 615 HOH HOH C . 
R 7 HOH 134 534 616 HOH HOH C . 
R 7 HOH 135 535 617 HOH HOH C . 
R 7 HOH 136 536 618 HOH HOH C . 
R 7 HOH 137 537 619 HOH HOH C . 
R 7 HOH 138 538 620 HOH HOH C . 
R 7 HOH 139 539 621 HOH HOH C . 
R 7 HOH 140 540 627 HOH HOH C . 
R 7 HOH 141 541 632 HOH HOH C . 
R 7 HOH 142 542 633 HOH HOH C . 
R 7 HOH 143 543 637 HOH HOH C . 
R 7 HOH 144 544 659 HOH HOH C . 
R 7 HOH 145 545 671 HOH HOH C . 
R 7 HOH 146 546 672 HOH HOH C . 
R 7 HOH 147 547 673 HOH HOH C . 
R 7 HOH 148 548 674 HOH HOH C . 
R 7 HOH 149 549 675 HOH HOH C . 
R 7 HOH 150 550 676 HOH HOH C . 
R 7 HOH 151 551 677 HOH HOH C . 
R 7 HOH 152 552 678 HOH HOH C . 
R 7 HOH 153 553 679 HOH HOH C . 
R 7 HOH 154 554 680 HOH HOH C . 
R 7 HOH 155 555 681 HOH HOH C . 
R 7 HOH 156 556 683 HOH HOH C . 
R 7 HOH 157 557 705 HOH HOH C . 
R 7 HOH 158 558 708 HOH HOH C . 
R 7 HOH 159 559 711 HOH HOH C . 
R 7 HOH 160 560 727 HOH HOH C . 
R 7 HOH 161 561 728 HOH HOH C . 
R 7 HOH 162 562 738 HOH HOH C . 
R 7 HOH 163 563 740 HOH HOH C . 
R 7 HOH 164 564 743 HOH HOH C . 
R 7 HOH 165 565 746 HOH HOH C . 
R 7 HOH 166 566 752 HOH HOH C . 
R 7 HOH 167 567 753 HOH HOH C . 
R 7 HOH 168 568 760 HOH HOH C . 
R 7 HOH 169 569 769 HOH HOH C . 
R 7 HOH 170 570 772 HOH HOH C . 
R 7 HOH 171 571 773 HOH HOH C . 
R 7 HOH 172 572 778 HOH HOH C . 
R 7 HOH 173 573 780 HOH HOH C . 
R 7 HOH 174 574 783 HOH HOH C . 
R 7 HOH 175 575 784 HOH HOH C . 
R 7 HOH 176 576 785 HOH HOH C . 
R 7 HOH 177 577 787 HOH HOH C . 
R 7 HOH 178 578 790 HOH HOH C . 
R 7 HOH 179 579 793 HOH HOH C . 
R 7 HOH 180 580 795 HOH HOH C . 
R 7 HOH 181 581 828 HOH HOH C . 
R 7 HOH 182 582 858 HOH HOH C . 
R 7 HOH 183 583 861 HOH HOH C . 
R 7 HOH 184 584 862 HOH HOH C . 
R 7 HOH 185 585 863 HOH HOH C . 
R 7 HOH 186 586 864 HOH HOH C . 
R 7 HOH 187 587 865 HOH HOH C . 
R 7 HOH 188 588 866 HOH HOH C . 
R 7 HOH 189 589 867 HOH HOH C . 
R 7 HOH 190 590 868 HOH HOH C . 
R 7 HOH 191 591 869 HOH HOH C . 
R 7 HOH 192 592 870 HOH HOH C . 
R 7 HOH 193 593 871 HOH HOH C . 
R 7 HOH 194 594 872 HOH HOH C . 
R 7 HOH 195 595 873 HOH HOH C . 
R 7 HOH 196 596 874 HOH HOH C . 
R 7 HOH 197 597 875 HOH HOH C . 
R 7 HOH 198 598 876 HOH HOH C . 
R 7 HOH 199 599 877 HOH HOH C . 
R 7 HOH 200 600 903 HOH HOH C . 
R 7 HOH 201 601 910 HOH HOH C . 
R 7 HOH 202 602 948 HOH HOH C . 
R 7 HOH 203 603 949 HOH HOH C . 
R 7 HOH 204 604 950 HOH HOH C . 
R 7 HOH 205 605 951 HOH HOH C . 
R 7 HOH 206 606 952 HOH HOH C . 
R 7 HOH 207 607 953 HOH HOH C . 
R 7 HOH 208 608 955 HOH HOH C . 
R 7 HOH 209 609 961 HOH HOH C . 
R 7 HOH 210 610 962 HOH HOH C . 
R 7 HOH 211 611 963 HOH HOH C . 
R 7 HOH 212 612 973 HOH HOH C . 
R 7 HOH 213 613 974 HOH HOH C . 
R 7 HOH 214 614 975 HOH HOH C . 
R 7 HOH 215 615 976 HOH HOH C . 
R 7 HOH 216 616 977 HOH HOH C . 
R 7 HOH 217 617 991 HOH HOH C . 
R 7 HOH 218 618 993 HOH HOH C . 
R 7 HOH 219 619 996 HOH HOH C . 
R 7 HOH 220 620 997 HOH HOH C . 
S 7 HOH 1   401 3   HOH HOH D . 
S 7 HOH 2   402 5   HOH HOH D . 
S 7 HOH 3   403 7   HOH HOH D . 
S 7 HOH 4   404 12  HOH HOH D . 
S 7 HOH 5   405 19  HOH HOH D . 
S 7 HOH 6   406 20  HOH HOH D . 
S 7 HOH 7   407 22  HOH HOH D . 
S 7 HOH 8   408 27  HOH HOH D . 
S 7 HOH 9   409 36  HOH HOH D . 
S 7 HOH 10  410 37  HOH HOH D . 
S 7 HOH 11  411 66  HOH HOH D . 
S 7 HOH 12  412 69  HOH HOH D . 
S 7 HOH 13  413 75  HOH HOH D . 
S 7 HOH 14  414 77  HOH HOH D . 
S 7 HOH 15  415 81  HOH HOH D . 
S 7 HOH 16  416 82  HOH HOH D . 
S 7 HOH 17  417 83  HOH HOH D . 
S 7 HOH 18  418 93  HOH HOH D . 
S 7 HOH 19  419 96  HOH HOH D . 
S 7 HOH 20  420 97  HOH HOH D . 
S 7 HOH 21  421 99  HOH HOH D . 
S 7 HOH 22  422 104 HOH HOH D . 
S 7 HOH 23  423 105 HOH HOH D . 
S 7 HOH 24  424 107 HOH HOH D . 
S 7 HOH 25  425 111 HOH HOH D . 
S 7 HOH 26  426 116 HOH HOH D . 
S 7 HOH 27  427 120 HOH HOH D . 
S 7 HOH 28  428 121 HOH HOH D . 
S 7 HOH 29  429 125 HOH HOH D . 
S 7 HOH 30  430 126 HOH HOH D . 
S 7 HOH 31  431 130 HOH HOH D . 
S 7 HOH 32  432 133 HOH HOH D . 
S 7 HOH 33  433 137 HOH HOH D . 
S 7 HOH 34  434 141 HOH HOH D . 
S 7 HOH 35  435 143 HOH HOH D . 
S 7 HOH 36  436 150 HOH HOH D . 
S 7 HOH 37  437 159 HOH HOH D . 
S 7 HOH 38  438 160 HOH HOH D . 
S 7 HOH 39  439 161 HOH HOH D . 
S 7 HOH 40  440 162 HOH HOH D . 
S 7 HOH 41  441 169 HOH HOH D . 
S 7 HOH 42  442 171 HOH HOH D . 
S 7 HOH 43  443 189 HOH HOH D . 
S 7 HOH 44  444 194 HOH HOH D . 
S 7 HOH 45  445 198 HOH HOH D . 
S 7 HOH 46  446 200 HOH HOH D . 
S 7 HOH 47  447 207 HOH HOH D . 
S 7 HOH 48  448 208 HOH HOH D . 
S 7 HOH 49  449 209 HOH HOH D . 
S 7 HOH 50  450 210 HOH HOH D . 
S 7 HOH 51  451 219 HOH HOH D . 
S 7 HOH 52  452 222 HOH HOH D . 
S 7 HOH 53  453 228 HOH HOH D . 
S 7 HOH 54  454 231 HOH HOH D . 
S 7 HOH 55  455 232 HOH HOH D . 
S 7 HOH 56  456 234 HOH HOH D . 
S 7 HOH 57  457 235 HOH HOH D . 
S 7 HOH 58  458 242 HOH HOH D . 
S 7 HOH 59  459 244 HOH HOH D . 
S 7 HOH 60  460 245 HOH HOH D . 
S 7 HOH 61  461 252 HOH HOH D . 
S 7 HOH 62  462 255 HOH HOH D . 
S 7 HOH 63  463 256 HOH HOH D . 
S 7 HOH 64  464 259 HOH HOH D . 
S 7 HOH 65  465 260 HOH HOH D . 
S 7 HOH 66  466 261 HOH HOH D . 
S 7 HOH 67  467 266 HOH HOH D . 
S 7 HOH 68  468 267 HOH HOH D . 
S 7 HOH 69  469 272 HOH HOH D . 
S 7 HOH 70  470 275 HOH HOH D . 
S 7 HOH 71  471 281 HOH HOH D . 
S 7 HOH 72  472 282 HOH HOH D . 
S 7 HOH 73  473 284 HOH HOH D . 
S 7 HOH 74  474 291 HOH HOH D . 
S 7 HOH 75  475 295 HOH HOH D . 
S 7 HOH 76  476 296 HOH HOH D . 
S 7 HOH 77  477 303 HOH HOH D . 
S 7 HOH 78  478 307 HOH HOH D . 
S 7 HOH 79  479 312 HOH HOH D . 
S 7 HOH 80  480 315 HOH HOH D . 
S 7 HOH 81  481 316 HOH HOH D . 
S 7 HOH 82  482 319 HOH HOH D . 
S 7 HOH 83  483 320 HOH HOH D . 
S 7 HOH 84  484 321 HOH HOH D . 
S 7 HOH 85  485 325 HOH HOH D . 
S 7 HOH 86  486 333 HOH HOH D . 
S 7 HOH 87  487 335 HOH HOH D . 
S 7 HOH 88  488 344 HOH HOH D . 
S 7 HOH 89  489 350 HOH HOH D . 
S 7 HOH 90  490 356 HOH HOH D . 
S 7 HOH 91  491 358 HOH HOH D . 
S 7 HOH 92  492 362 HOH HOH D . 
S 7 HOH 93  493 365 HOH HOH D . 
S 7 HOH 94  494 368 HOH HOH D . 
S 7 HOH 95  495 371 HOH HOH D . 
S 7 HOH 96  496 379 HOH HOH D . 
S 7 HOH 97  497 383 HOH HOH D . 
S 7 HOH 98  498 385 HOH HOH D . 
S 7 HOH 99  499 386 HOH HOH D . 
S 7 HOH 100 500 387 HOH HOH D . 
S 7 HOH 101 501 391 HOH HOH D . 
S 7 HOH 102 502 394 HOH HOH D . 
S 7 HOH 103 503 396 HOH HOH D . 
S 7 HOH 104 504 399 HOH HOH D . 
S 7 HOH 105 505 401 HOH HOH D . 
S 7 HOH 106 506 404 HOH HOH D . 
S 7 HOH 107 507 405 HOH HOH D . 
S 7 HOH 108 508 408 HOH HOH D . 
S 7 HOH 109 509 411 HOH HOH D . 
S 7 HOH 110 510 417 HOH HOH D . 
S 7 HOH 111 511 421 HOH HOH D . 
S 7 HOH 112 512 424 HOH HOH D . 
S 7 HOH 113 513 425 HOH HOH D . 
S 7 HOH 114 514 429 HOH HOH D . 
S 7 HOH 115 515 430 HOH HOH D . 
S 7 HOH 116 516 435 HOH HOH D . 
S 7 HOH 117 517 436 HOH HOH D . 
S 7 HOH 118 518 439 HOH HOH D . 
S 7 HOH 119 519 444 HOH HOH D . 
S 7 HOH 120 520 445 HOH HOH D . 
S 7 HOH 121 521 452 HOH HOH D . 
S 7 HOH 122 522 455 HOH HOH D . 
S 7 HOH 123 523 460 HOH HOH D . 
S 7 HOH 124 524 469 HOH HOH D . 
S 7 HOH 125 525 470 HOH HOH D . 
S 7 HOH 126 526 473 HOH HOH D . 
S 7 HOH 127 527 474 HOH HOH D . 
S 7 HOH 128 528 475 HOH HOH D . 
S 7 HOH 129 529 477 HOH HOH D . 
S 7 HOH 130 530 479 HOH HOH D . 
S 7 HOH 131 531 484 HOH HOH D . 
S 7 HOH 132 532 494 HOH HOH D . 
S 7 HOH 133 533 495 HOH HOH D . 
S 7 HOH 134 534 496 HOH HOH D . 
S 7 HOH 135 535 497 HOH HOH D . 
S 7 HOH 136 536 559 HOH HOH D . 
S 7 HOH 137 537 560 HOH HOH D . 
S 7 HOH 138 538 565 HOH HOH D . 
S 7 HOH 139 539 566 HOH HOH D . 
S 7 HOH 140 540 567 HOH HOH D . 
S 7 HOH 141 541 568 HOH HOH D . 
S 7 HOH 142 542 569 HOH HOH D . 
S 7 HOH 143 543 570 HOH HOH D . 
S 7 HOH 144 544 572 HOH HOH D . 
S 7 HOH 145 545 573 HOH HOH D . 
S 7 HOH 146 546 574 HOH HOH D . 
S 7 HOH 147 547 575 HOH HOH D . 
S 7 HOH 148 548 576 HOH HOH D . 
S 7 HOH 149 549 577 HOH HOH D . 
S 7 HOH 150 550 578 HOH HOH D . 
S 7 HOH 151 551 579 HOH HOH D . 
S 7 HOH 152 552 580 HOH HOH D . 
S 7 HOH 153 553 581 HOH HOH D . 
S 7 HOH 154 554 582 HOH HOH D . 
S 7 HOH 155 555 583 HOH HOH D . 
S 7 HOH 156 556 592 HOH HOH D . 
S 7 HOH 157 557 593 HOH HOH D . 
S 7 HOH 158 558 600 HOH HOH D . 
S 7 HOH 159 559 603 HOH HOH D . 
S 7 HOH 160 560 604 HOH HOH D . 
S 7 HOH 161 561 605 HOH HOH D . 
S 7 HOH 162 562 606 HOH HOH D . 
S 7 HOH 163 563 609 HOH HOH D . 
S 7 HOH 164 564 610 HOH HOH D . 
S 7 HOH 165 565 613 HOH HOH D . 
S 7 HOH 166 566 622 HOH HOH D . 
S 7 HOH 167 567 623 HOH HOH D . 
S 7 HOH 168 568 624 HOH HOH D . 
S 7 HOH 169 569 625 HOH HOH D . 
S 7 HOH 170 570 626 HOH HOH D . 
S 7 HOH 171 571 634 HOH HOH D . 
S 7 HOH 172 572 635 HOH HOH D . 
S 7 HOH 173 573 682 HOH HOH D . 
S 7 HOH 174 574 684 HOH HOH D . 
S 7 HOH 175 575 685 HOH HOH D . 
S 7 HOH 176 576 686 HOH HOH D . 
S 7 HOH 177 577 687 HOH HOH D . 
S 7 HOH 178 578 688 HOH HOH D . 
S 7 HOH 179 579 689 HOH HOH D . 
S 7 HOH 180 580 690 HOH HOH D . 
S 7 HOH 181 581 691 HOH HOH D . 
S 7 HOH 182 582 692 HOH HOH D . 
S 7 HOH 183 583 693 HOH HOH D . 
S 7 HOH 184 584 694 HOH HOH D . 
S 7 HOH 185 585 695 HOH HOH D . 
S 7 HOH 186 586 696 HOH HOH D . 
S 7 HOH 187 587 697 HOH HOH D . 
S 7 HOH 188 588 698 HOH HOH D . 
S 7 HOH 189 589 699 HOH HOH D . 
S 7 HOH 190 590 700 HOH HOH D . 
S 7 HOH 191 591 701 HOH HOH D . 
S 7 HOH 192 592 703 HOH HOH D . 
S 7 HOH 193 593 707 HOH HOH D . 
S 7 HOH 194 594 710 HOH HOH D . 
S 7 HOH 195 595 714 HOH HOH D . 
S 7 HOH 196 596 722 HOH HOH D . 
S 7 HOH 197 597 725 HOH HOH D . 
S 7 HOH 198 598 730 HOH HOH D . 
S 7 HOH 199 599 731 HOH HOH D . 
S 7 HOH 200 600 733 HOH HOH D . 
S 7 HOH 201 601 734 HOH HOH D . 
S 7 HOH 202 602 735 HOH HOH D . 
S 7 HOH 203 603 736 HOH HOH D . 
S 7 HOH 204 604 744 HOH HOH D . 
S 7 HOH 205 605 748 HOH HOH D . 
S 7 HOH 206 606 750 HOH HOH D . 
S 7 HOH 207 607 758 HOH HOH D . 
S 7 HOH 208 608 759 HOH HOH D . 
S 7 HOH 209 609 762 HOH HOH D . 
S 7 HOH 210 610 766 HOH HOH D . 
S 7 HOH 211 611 770 HOH HOH D . 
S 7 HOH 212 612 771 HOH HOH D . 
S 7 HOH 213 613 775 HOH HOH D . 
S 7 HOH 214 614 779 HOH HOH D . 
S 7 HOH 215 615 789 HOH HOH D . 
S 7 HOH 216 616 842 HOH HOH D . 
S 7 HOH 217 617 843 HOH HOH D . 
S 7 HOH 218 618 844 HOH HOH D . 
S 7 HOH 219 619 859 HOH HOH D . 
S 7 HOH 220 620 878 HOH HOH D . 
S 7 HOH 221 621 879 HOH HOH D . 
S 7 HOH 222 622 880 HOH HOH D . 
S 7 HOH 223 623 881 HOH HOH D . 
S 7 HOH 224 624 882 HOH HOH D . 
S 7 HOH 225 625 883 HOH HOH D . 
S 7 HOH 226 626 884 HOH HOH D . 
S 7 HOH 227 627 885 HOH HOH D . 
S 7 HOH 228 628 886 HOH HOH D . 
S 7 HOH 229 629 887 HOH HOH D . 
S 7 HOH 230 630 888 HOH HOH D . 
S 7 HOH 231 631 889 HOH HOH D . 
S 7 HOH 232 632 890 HOH HOH D . 
S 7 HOH 233 633 891 HOH HOH D . 
S 7 HOH 234 634 892 HOH HOH D . 
S 7 HOH 235 635 893 HOH HOH D . 
S 7 HOH 236 636 894 HOH HOH D . 
S 7 HOH 237 637 895 HOH HOH D . 
S 7 HOH 238 638 896 HOH HOH D . 
S 7 HOH 239 639 897 HOH HOH D . 
S 7 HOH 240 640 900 HOH HOH D . 
S 7 HOH 241 641 901 HOH HOH D . 
S 7 HOH 242 642 905 HOH HOH D . 
S 7 HOH 243 643 906 HOH HOH D . 
S 7 HOH 244 644 909 HOH HOH D . 
S 7 HOH 245 645 938 HOH HOH D . 
S 7 HOH 246 646 939 HOH HOH D . 
S 7 HOH 247 647 954 HOH HOH D . 
S 7 HOH 248 648 956 HOH HOH D . 
S 7 HOH 249 649 957 HOH HOH D . 
S 7 HOH 250 650 958 HOH HOH D . 
S 7 HOH 251 651 959 HOH HOH D . 
S 7 HOH 252 652 960 HOH HOH D . 
S 7 HOH 253 653 978 HOH HOH D . 
S 7 HOH 254 654 979 HOH HOH D . 
S 7 HOH 255 655 980 HOH HOH D . 
S 7 HOH 256 656 981 HOH HOH D . 
S 7 HOH 257 657 982 HOH HOH D . 
S 7 HOH 258 658 983 HOH HOH D . 
S 7 HOH 259 659 984 HOH HOH D . 
S 7 HOH 260 660 985 HOH HOH D . 
S 7 HOH 261 661 986 HOH HOH D . 
S 7 HOH 262 662 987 HOH HOH D . 
S 7 HOH 263 663 988 HOH HOH D . 
S 7 HOH 264 664 989 HOH HOH D . 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
_software.date 
_software.type 
_software.location 
_software.language 
DNA    'data collection' .        ? 1 ? ? ? ? 
MOLREP phasing           .        ? 2 ? ? ? ? 
REFMAC refinement        5.6.0117 ? 3 ? ? ? ? 
MOSFLM 'data reduction'  .        ? 4 ? ? ? ? 
SCALA  'data scaling'    .        ? 5 ? ? ? ? 
# 
_cell.entry_id           4KP8 
_cell.length_a           46.817 
_cell.length_b           67.258 
_cell.length_c           81.190 
_cell.angle_alpha        81.88 
_cell.angle_beta         83.99 
_cell.angle_gamma        86.51 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         4KP8 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
# 
_exptl.entry_id          4KP8 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.10 
_exptl_crystal.density_percent_sol   41.46 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              5.0 
_exptl_crystal_grow.pdbx_details    '0.1M ammonium citrate pH 5.0, 24% PEG 4000, VAPOR DIFFUSION, SITTING DROP, temperature 291K' 
_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               'IMAGE PLATE' 
_diffrn_detector.type                   'MAR555 FLAT PANEL' 
_diffrn_detector.pdbx_collection_date   2011-11-16 
_diffrn_detector.details                'Detector swing-out angle up to 30 degrees' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'Si (111), horizontally focussing' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.815 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'EMBL/DESY, HAMBURG BEAMLINE X11' 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
_diffrn_source.pdbx_synchrotron_beamline   X11 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.815 
# 
_reflns.entry_id                     4KP8 
_reflns.observed_criterion_sigma_I   0 
_reflns.observed_criterion_sigma_F   0 
_reflns.d_resolution_low             39.998 
_reflns.d_resolution_high            1.800 
_reflns.number_obs                   88867 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         96.880 
_reflns.pdbx_Rmerge_I_obs            0.181 
_reflns.pdbx_Rsym_value              0.181 
_reflns.pdbx_netI_over_sigmaI        3.800 
_reflns.B_iso_Wilson_estimate        19.045 
_reflns.pdbx_redundancy              3.900 
_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 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.number_unique_all 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
1.80 1.90  97.6 0.440 0.440 1.90 3.6 ? 10842 ? ? ? ? ? ? ? ? ? ? ? ? ? 1  1 
1.90 2.01  97.8 0.311 0.311 2.7  3.9 ? 12228 ? ? ? ? ? ? ? ? ? ? ? ? ? 2  1 
2.01 2.15  98.1 0.253 0.253 3.4  3.9 ? 11494 ? ? ? ? ? ? ? ? ? ? ? ? ? 3  1 
2.15 2.32  98.4 0.226 0.226 3.8  3.9 ? 10733 ? ? ? ? ? ? ? ? ? ? ? ? ? 4  1 
2.32 2.55  98.6 0.205 0.205 4.2  3.9 ? 9855  ? ? ? ? ? ? ? ? ? ? ? ? ? 5  1 
2.55 2.85  98.8 0.177 0.177 4.6  3.9 ? 8948  ? ? ? ? ? ? ? ? ? ? ? ? ? 6  1 
2.85 3.29  99.1 0.160 0.160 5.0  3.9 ? 7963  ? ? ? ? ? ? ? ? ? ? ? ? ? 7  1 
3.29 4.02  99.3 0.151 0.151 5.4  3.9 ? 6702  ? ? ? ? ? ? ? ? ? ? ? ? ? 8  1 
4.02 5.69  99.7 0.152 0.152 5.4  3.9 ? 5206  ? ? ? ? ? ? ? ? ? ? ? ? ? 9  1 
5.69 40.00 99.0 0.169 0.169 5.4  3.8 ? 2746  ? ? ? ? ? ? ? ? ? ? ? ? ? 10 1 
# 
_refine.entry_id                                 4KP8 
_refine.ls_number_reflns_obs                     80039 
_refine.ls_number_reflns_all                     80039 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             39.998 
_refine.ls_d_res_high                            1.80 
_refine.ls_percent_reflns_obs                    98.38 
_refine.ls_R_factor_obs                          0.20357 
_refine.ls_R_factor_all                          0.20357 
_refine.ls_R_factor_R_work                       0.19840 
_refine.ls_R_factor_R_free                       0.25053 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 9.9 
_refine.ls_number_reflns_R_free                  8778 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.939 
_refine.correlation_coeff_Fo_to_Fc_free          0.906 
_refine.B_iso_mean                               16.723 
_refine.aniso_B[1][1]                            -0.79 
_refine.aniso_B[2][2]                            -0.18 
_refine.aniso_B[3][3]                            0.52 
_refine.aniso_B[1][2]                            0.41 
_refine.aniso_B[1][3]                            0.41 
_refine.aniso_B[2][3]                            1.12 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.40 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_refine.pdbx_starting_model                      1JD0 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.179 
_refine.pdbx_overall_ESU_R_Free                  0.163 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.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        8363 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         86 
_refine_hist.number_atoms_solvent             997 
_refine_hist.number_atoms_total               9446 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        39.998 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d       0.019  0.020  ? 8886  ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg    1.832  1.951  ? 12128 ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg 7.208  5.000  ? 1077  ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg 36.594 24.452 ? 447   ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg 14.451 15.000 ? 1386  ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg 20.063 15.000 ? 38    ? 'X-RAY DIFFRACTION' 
r_chiral_restr         0.138  0.200  ? 1268  ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined   0.011  0.021  ? 7051  ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.800 
_refine_ls_shell.d_res_low                        1.847 
_refine_ls_shell.number_reflns_R_work             5829 
_refine_ls_shell.R_factor_R_work                  0.416 
_refine_ls_shell.percent_reflns_obs               96.88 
_refine_ls_shell.R_factor_R_free                  0.471 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             622 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
# 
_database_PDB_matrix.entry_id          4KP8 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_struct.entry_id                  4KP8 
_struct.title                     
;Crystal structure of catalytic domain of human carbonic anhydrase isozyme XII with 3-[(Pyrimidin-2-ylsulfanyl)acetyl]benzenesulfonamide
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4KP8 
_struct_keywords.pdbx_keywords   'LYASE/LYASE INHIBITOR' 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, LYASE-LYASE INHIBITOR complex' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 2 ? 
I N N 3 ? 
J N N 5 ? 
K N N 6 ? 
L N N 2 ? 
M N N 2 ? 
N N N 3 ? 
O N N 5 ? 
P N N 7 ? 
Q N N 7 ? 
R N N 7 ? 
S N N 7 ? 
# 
_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 4KP8 A 2 ? 263 ? O43570 30 ? 291 ? 2 263 
2 1 4KP8 B 2 ? 263 ? O43570 30 ? 291 ? 2 263 
3 1 4KP8 C 2 ? 263 ? O43570 30 ? 291 ? 2 263 
4 1 4KP8 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 4KP8 MET A 1 ? UNP O43570 ? ? 'expression tag' 1 1 
2 4KP8 MET B 1 ? UNP O43570 ? ? 'expression tag' 1 2 
3 4KP8 MET C 1 ? UNP O43570 ? ? 'expression tag' 1 3 
4 4KP8 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,P,Q 
2 1 C,D,L,M,N,O,R,S       
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  GLY A 11  ? ASN A 13  ? GLY A 11  ASN A 13  5 ? 3  
HELX_P HELX_P2  2  SER A 14  ? TYR A 19  ? SER A 14  TYR A 19  1 ? 6  
HELX_P HELX_P3  3  PRO A 20  ? GLY A 24  ? PRO A 20  GLY A 24  5 ? 5  
HELX_P HELX_P4  4  HIS A 33  ? ASP A 35  ? HIS A 33  ASP A 35  5 ? 3  
HELX_P HELX_P5  5  ASP A 128 ? SER A 133 ? ASP A 128 SER A 133 1 ? 6  
HELX_P HELX_P6  6  ASN A 152 ? SER A 160 ? ASN A 152 SER A 160 1 ? 9  
HELX_P HELX_P7  7  HIS A 161 ? VAL A 165 ? HIS A 161 VAL A 165 5 ? 5  
HELX_P HELX_P8  8  ASN A 178 ? LEU A 183 ? ASN A 178 LEU A 183 5 ? 6  
HELX_P HELX_P9  9  SER A 218 ? ALA A 228 ? SER A 218 ALA A 228 1 ? 11 
HELX_P HELX_P10 10 GLY B 11  ? ASN B 13  ? GLY B 11  ASN B 13  5 ? 3  
HELX_P HELX_P11 11 SER B 14  ? TYR B 19  ? SER B 14  TYR B 19  1 ? 6  
HELX_P HELX_P12 12 PRO B 20  ? GLY B 24  ? PRO B 20  GLY B 24  5 ? 5  
HELX_P HELX_P13 13 HIS B 33  ? ASP B 35  ? HIS B 33  ASP B 35  5 ? 3  
HELX_P HELX_P14 14 ASP B 128 ? SER B 133 ? ASP B 128 SER B 133 1 ? 6  
HELX_P HELX_P15 15 ASN B 152 ? SER B 160 ? ASN B 152 SER B 160 1 ? 9  
HELX_P HELX_P16 16 HIS B 161 ? VAL B 165 ? HIS B 161 VAL B 165 5 ? 5  
HELX_P HELX_P17 17 ASN B 178 ? LEU B 183 ? ASN B 178 LEU B 183 5 ? 6  
HELX_P HELX_P18 18 SER B 218 ? LEU B 229 ? SER B 218 LEU B 229 1 ? 12 
HELX_P HELX_P19 19 GLY C 11  ? ASN C 13  ? GLY C 11  ASN C 13  5 ? 3  
HELX_P HELX_P20 20 SER C 14  ? TYR C 19  ? SER C 14  TYR C 19  1 ? 6  
HELX_P HELX_P21 21 PRO C 20  ? GLY C 24  ? PRO C 20  GLY C 24  5 ? 5  
HELX_P HELX_P22 22 HIS C 33  ? ASP C 35  ? HIS C 33  ASP C 35  5 ? 3  
HELX_P HELX_P23 23 ASP C 128 ? SER C 133 ? ASP C 128 SER C 133 1 ? 6  
HELX_P HELX_P24 24 ASN C 152 ? SER C 160 ? ASN C 152 SER C 160 1 ? 9  
HELX_P HELX_P25 25 HIS C 161 ? VAL C 165 ? HIS C 161 VAL C 165 5 ? 5  
HELX_P HELX_P26 26 ASN C 178 ? LEU C 183 ? ASN C 178 LEU C 183 5 ? 6  
HELX_P HELX_P27 27 SER C 218 ? ALA C 228 ? SER C 218 ALA C 228 1 ? 11 
HELX_P HELX_P28 28 PHE D 7   ? LYS D 18  ? PHE D 7   LYS D 18  5 ? 12 
HELX_P HELX_P29 29 TYR D 19  ? GLY D 24  ? TYR D 19  GLY D 24  5 ? 6  
HELX_P HELX_P30 30 HIS D 33  ? ASP D 35  ? HIS D 33  ASP D 35  5 ? 3  
HELX_P HELX_P31 31 ASP D 128 ? SER D 133 ? ASP D 128 SER D 133 1 ? 6  
HELX_P HELX_P32 32 ASN D 152 ? SER D 160 ? ASN D 152 SER D 160 1 ? 9  
HELX_P HELX_P33 33 HIS D 161 ? VAL D 165 ? HIS D 161 VAL D 165 5 ? 5  
HELX_P HELX_P34 34 ASN D 178 ? LEU D 183 ? ASN D 178 LEU D 183 5 ? 6  
HELX_P HELX_P35 35 SER D 218 ? ALA D 228 ? SER D 218 ALA D 228 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 22  SG  ? ? ? 1_555 A CYS 202 SG  ? ? A CYS 22  A CYS 202 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
disulf2  disulf ? ? B CYS 22  SG  ? ? ? 1_555 B CYS 202 SG  ? ? B CYS 22  B CYS 202 1_555 ? ? ? ? ? ? ? 2.002 ? ? 
disulf3  disulf ? ? C CYS 22  SG  ? ? ? 1_555 C CYS 202 SG  ? ? C CYS 22  C CYS 202 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
disulf4  disulf ? ? D CYS 22  SG  ? ? ? 1_555 D CYS 202 SG  ? ? D CYS 22  D CYS 202 1_555 ? ? ? ? ? ? ? 1.982 ? ? 
metalc1  metalc ? ? A HIS 91  NE2 ? ? ? 1_555 E ZN  .   ZN  ? ? A HIS 91  A ZN  301 1_555 ? ? ? ? ? ? ? 2.117 ? ? 
metalc2  metalc ? ? A HIS 93  NE2 ? ? ? 1_555 E ZN  .   ZN  ? ? A HIS 93  A ZN  301 1_555 ? ? ? ? ? ? ? 2.117 ? ? 
metalc3  metalc ? ? A HIS 117 ND1 ? ? ? 1_555 E ZN  .   ZN  ? ? A HIS 117 A ZN  301 1_555 ? ? ? ? ? ? ? 2.118 ? ? 
metalc4  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 F E1G .   N20 ? ? A ZN  301 A E1G 302 1_555 ? ? ? ? ? ? ? 1.827 ? ? 
metalc5  metalc ? ? B HIS 91  NE2 ? ? ? 1_555 H ZN  .   ZN  ? ? B HIS 91  B ZN  301 1_555 ? ? ? ? ? ? ? 2.009 ? ? 
metalc6  metalc ? ? B HIS 93  NE2 ? ? ? 1_555 H ZN  .   ZN  ? ? B HIS 93  B ZN  301 1_555 ? ? ? ? ? ? ? 2.099 ? ? 
metalc7  metalc ? ? B HIS 117 ND1 ? ? ? 1_555 H ZN  .   ZN  ? ? B HIS 117 B ZN  301 1_555 ? ? ? ? ? ? ? 1.998 ? ? 
metalc8  metalc ? ? H ZN  .   ZN  ? ? ? 1_555 I E1G .   N20 ? ? B ZN  301 B E1G 302 1_555 ? ? ? ? ? ? ? 1.793 ? ? 
metalc9  metalc ? ? C HIS 91  NE2 ? ? ? 1_555 L ZN  .   ZN  ? ? C HIS 91  C ZN  301 1_555 ? ? ? ? ? ? ? 1.927 ? ? 
metalc10 metalc ? ? C HIS 93  NE2 ? ? ? 1_555 L ZN  .   ZN  ? ? C HIS 93  C ZN  301 1_555 ? ? ? ? ? ? ? 2.026 ? ? 
metalc11 metalc ? ? C HIS 117 ND1 ? ? ? 1_555 L ZN  .   ZN  ? ? C HIS 117 C ZN  301 1_555 ? ? ? ? ? ? ? 1.955 ? ? 
metalc12 metalc ? ? D HIS 91  NE2 ? ? ? 1_555 M ZN  .   ZN  ? ? D HIS 91  D ZN  301 1_555 ? ? ? ? ? ? ? 2.058 ? ? 
metalc13 metalc ? ? D HIS 93  NE2 ? ? ? 1_555 M ZN  .   ZN  ? ? D HIS 93  D ZN  301 1_555 ? ? ? ? ? ? ? 2.138 ? ? 
metalc14 metalc ? ? D HIS 117 ND1 ? ? ? 1_555 M ZN  .   ZN  ? ? D HIS 117 D ZN  301 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
metalc15 metalc ? ? M ZN  .   ZN  ? ? ? 1_555 N E1G .   N20 ? ? D ZN  301 D E1G 302 1_555 ? ? ? ? ? ? ? 1.808 ? ? 
metalc16 metalc ? ? M ZN  .   ZN  ? ? ? 1_555 N E1G .   S17 ? ? D ZN  301 D E1G 302 1_555 ? ? ? ? ? ? ? 2.987 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 93  ? A HIS 93  ? 1_555 103.8 ? 
2  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 117 ? A HIS 117 ? 1_555 114.9 ? 
3  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 117 ? A HIS 117 ? 1_555 99.6  ? 
4  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N20 ? F E1G .   ? A E1G 302 ? 1_555 105.7 ? 
5  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N20 ? F E1G .   ? A E1G 302 ? 1_555 111.2 ? 
6  ND1 ? A HIS 117 ? A HIS 117 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N20 ? F E1G .   ? A E1G 302 ? 1_555 120.4 ? 
7  NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? H ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 104.2 ? 
8  NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? H ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 112.4 ? 
9  NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? H ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 100.3 ? 
10 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? H ZN . ? B ZN 301 ? 1_555 N20 ? I E1G .   ? B E1G 302 ? 1_555 111.2 ? 
11 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? H ZN . ? B ZN 301 ? 1_555 N20 ? I E1G .   ? B E1G 302 ? 1_555 111.7 ? 
12 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 ZN ? H ZN . ? B ZN 301 ? 1_555 N20 ? I E1G .   ? B E1G 302 ? 1_555 116.0 ? 
13 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? L ZN . ? C ZN 301 ? 1_555 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 106.8 ? 
14 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? L 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 ? L ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 103.0 ? 
16 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? M ZN . ? D ZN 301 ? 1_555 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 100.3 ? 
17 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? M ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 110.1 ? 
18 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? M ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 99.1  ? 
19 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? M ZN . ? D ZN 301 ? 1_555 N20 ? N E1G .   ? D E1G 302 ? 1_555 112.9 ? 
20 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? M ZN . ? D ZN 301 ? 1_555 N20 ? N E1G .   ? D E1G 302 ? 1_555 112.9 ? 
21 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 ZN ? M ZN . ? D ZN 301 ? 1_555 N20 ? N E1G .   ? D E1G 302 ? 1_555 119.2 ? 
22 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? M ZN . ? D ZN 301 ? 1_555 S17 ? N E1G .   ? D E1G 302 ? 1_555 96.6  ? 
23 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? M ZN . ? D ZN 301 ? 1_555 S17 ? N E1G .   ? D E1G 302 ? 1_555 143.9 ? 
24 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 ZN ? M ZN . ? D ZN 301 ? 1_555 S17 ? N E1G .   ? D E1G 302 ? 1_555 104.7 ? 
25 N20 ? N E1G .   ? D E1G 302 ? 1_555 ZN ? M ZN . ? D ZN 301 ? 1_555 S17 ? N E1G .   ? D E1G 302 ? 1_555 31.2  ? 
# 
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 1.52 
2 PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 9.19 
3 SER 28  B . ? SER 28  B PRO 29  B ? PRO 29  B 1 0.41 
4 PRO 200 B . ? PRO 200 B PRO 201 B ? PRO 201 B 1 5.13 
5 SER 28  C . ? SER 28  C PRO 29  C ? PRO 29  C 1 0.51 
6 PRO 200 C . ? PRO 200 C PRO 201 C ? PRO 201 C 1 9.93 
7 SER 28  D . ? SER 28  D PRO 29  D ? PRO 29  D 1 2.29 
8 PRO 200 D . ? PRO 200 D PRO 201 D ? PRO 201 D 1 3.74 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 10 ? 
C ? 6  ? 
D ? 2  ? 
E ? 10 ? 
F ? 6  ? 
G ? 2  ? 
H ? 10 ? 
I ? 6  ? 
J ? 2  ? 
K ? 10 ? 
L ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2  ? parallel      
B 1 2  ? parallel      
B 2 3  ? anti-parallel 
B 3 4  ? anti-parallel 
B 4 5  ? parallel      
B 5 6  ? anti-parallel 
B 6 7  ? anti-parallel 
B 7 8  ? anti-parallel 
B 8 9  ? anti-parallel 
B 9 10 ? anti-parallel 
C 1 2  ? anti-parallel 
C 2 3  ? anti-parallel 
C 3 4  ? anti-parallel 
C 4 5  ? anti-parallel 
C 5 6  ? parallel      
D 1 2  ? parallel      
E 1 2  ? parallel      
E 2 3  ? anti-parallel 
E 3 4  ? anti-parallel 
E 4 5  ? parallel      
E 5 6  ? anti-parallel 
E 6 7  ? anti-parallel 
E 7 8  ? anti-parallel 
E 8 9  ? anti-parallel 
E 9 10 ? anti-parallel 
F 1 2  ? anti-parallel 
F 2 3  ? anti-parallel 
F 3 4  ? anti-parallel 
F 4 5  ? anti-parallel 
F 5 6  ? parallel      
G 1 2  ? parallel      
H 1 2  ? parallel      
H 2 3  ? anti-parallel 
H 3 4  ? anti-parallel 
H 4 5  ? parallel      
H 5 6  ? anti-parallel 
H 6 7  ? anti-parallel 
H 7 8  ? anti-parallel 
H 8 9  ? anti-parallel 
H 9 10 ? anti-parallel 
I 1 2  ? anti-parallel 
I 2 3  ? anti-parallel 
I 3 4  ? anti-parallel 
I 4 5  ? anti-parallel 
I 5 6  ? parallel      
J 1 2  ? parallel      
K 1 2  ? parallel      
K 2 3  ? anti-parallel 
K 3 4  ? anti-parallel 
K 4 5  ? parallel      
K 5 6  ? anti-parallel 
K 6 7  ? anti-parallel 
K 7 8  ? anti-parallel 
K 8 9  ? anti-parallel 
K 9 10 ? anti-parallel 
L 1 2  ? anti-parallel 
L 2 3  ? anti-parallel 
L 3 4  ? anti-parallel 
L 4 5  ? anti-parallel 
L 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1  ASP A 31  ? LEU A 32  ? ASP A 31  LEU A 32  
A 2  THR A 106 ? VAL A 107 ? THR A 106 VAL A 107 
B 1  LEU A 37  ? TYR A 39  ? LEU A 37  TYR A 39  
B 2  VAL A 257 ? THR A 259 ? VAL A 257 THR A 259 
B 3  TYR A 190 ? GLY A 195 ? TYR A 190 GLY A 195 
B 4  VAL A 206 ? PHE A 211 ? VAL A 206 PHE A 211 
B 5  LEU A 139 ? MET A 148 ? LEU A 139 MET A 148 
B 6  ALA A 114 ? ASN A 122 ? ALA A 114 ASN A 122 
B 7  TYR A 85  ? TRP A 94  ? TYR A 85  TRP A 94  
B 8  VAL A 68  ? ASN A 71  ? VAL A 68  ASN A 71  
B 9  GLN A 58  ? ASN A 63  ? GLN A 58  ASN A 63  
B 10 GLU A 171 ? PRO A 175 ? GLU A 171 PRO A 175 
C 1  GLU A 47  ? GLN A 49  ? GLU A 47  GLN A 49  
C 2  HIS A 77  ? GLN A 79  ? HIS A 77  GLN A 79  
C 3  TYR A 85  ? TRP A 94  ? TYR A 85  TRP A 94  
C 4  ALA A 114 ? ASN A 122 ? ALA A 114 ASN A 122 
C 5  LEU A 139 ? MET A 148 ? LEU A 139 MET A 148 
C 6  VAL A 215 ? ILE A 217 ? VAL A 215 ILE A 217 
D 1  ASP B 31  ? LEU B 32  ? ASP B 31  LEU B 32  
D 2  THR B 106 ? VAL B 107 ? THR B 106 VAL B 107 
E 1  LEU B 37  ? TYR B 39  ? LEU B 37  TYR B 39  
E 2  VAL B 257 ? THR B 259 ? VAL B 257 THR B 259 
E 3  TYR B 190 ? GLY B 195 ? TYR B 190 GLY B 195 
E 4  VAL B 206 ? PHE B 211 ? VAL B 206 PHE B 211 
E 5  LEU B 139 ? MET B 148 ? LEU B 139 MET B 148 
E 6  ALA B 114 ? ASN B 122 ? ALA B 114 ASN B 122 
E 7  TYR B 85  ? TRP B 94  ? TYR B 85  TRP B 94  
E 8  VAL B 68  ? ASN B 71  ? VAL B 68  ASN B 71  
E 9  GLN B 58  ? ASN B 63  ? GLN B 58  ASN B 63  
E 10 GLU B 171 ? PRO B 175 ? GLU B 171 PRO B 175 
F 1  GLU B 47  ? GLN B 49  ? GLU B 47  GLN B 49  
F 2  HIS B 77  ? GLN B 79  ? HIS B 77  GLN B 79  
F 3  TYR B 85  ? TRP B 94  ? TYR B 85  TRP B 94  
F 4  ALA B 114 ? ASN B 122 ? ALA B 114 ASN B 122 
F 5  LEU B 139 ? MET B 148 ? LEU B 139 MET B 148 
F 6  VAL B 215 ? ILE B 217 ? VAL B 215 ILE B 217 
G 1  ASP C 31  ? LEU C 32  ? ASP C 31  LEU C 32  
G 2  THR C 106 ? VAL C 107 ? THR C 106 VAL C 107 
H 1  LEU C 37  ? TYR C 39  ? LEU C 37  TYR C 39  
H 2  VAL C 257 ? THR C 259 ? VAL C 257 THR C 259 
H 3  TYR C 190 ? GLY C 195 ? TYR C 190 GLY C 195 
H 4  VAL C 206 ? PHE C 211 ? VAL C 206 PHE C 211 
H 5  LEU C 139 ? MET C 148 ? LEU C 139 MET C 148 
H 6  ALA C 114 ? ASN C 122 ? ALA C 114 ASN C 122 
H 7  TYR C 85  ? TRP C 94  ? TYR C 85  TRP C 94  
H 8  VAL C 68  ? ASN C 71  ? VAL C 68  ASN C 71  
H 9  GLN C 58  ? ASN C 63  ? GLN C 58  ASN C 63  
H 10 GLU C 171 ? PRO C 175 ? GLU C 171 PRO C 175 
I 1  GLU C 47  ? GLN C 49  ? GLU C 47  GLN C 49  
I 2  HIS C 77  ? GLN C 79  ? HIS C 77  GLN C 79  
I 3  TYR C 85  ? TRP C 94  ? TYR C 85  TRP C 94  
I 4  ALA C 114 ? ASN C 122 ? ALA C 114 ASN C 122 
I 5  LEU C 139 ? MET C 148 ? LEU C 139 MET C 148 
I 6  VAL C 215 ? ILE C 217 ? VAL C 215 ILE C 217 
J 1  ASP D 31  ? LEU D 32  ? ASP D 31  LEU D 32  
J 2  THR D 106 ? VAL D 107 ? THR D 106 VAL D 107 
K 1  LEU D 37  ? TYR D 39  ? LEU D 37  TYR D 39  
K 2  VAL D 257 ? THR D 259 ? VAL D 257 THR D 259 
K 3  TYR D 190 ? GLY D 195 ? TYR D 190 GLY D 195 
K 4  VAL D 206 ? PHE D 211 ? VAL D 206 PHE D 211 
K 5  LEU D 139 ? MET D 148 ? LEU D 139 MET D 148 
K 6  ALA D 114 ? ASN D 122 ? ALA D 114 ASN D 122 
K 7  TYR D 85  ? TRP D 94  ? TYR D 85  TRP D 94  
K 8  VAL D 68  ? ASN D 71  ? VAL D 68  ASN D 71  
K 9  GLN D 58  ? ASN D 63  ? GLN D 58  ASN D 63  
K 10 GLU D 171 ? PRO D 175 ? GLU D 171 PRO D 175 
L 1  GLU D 47  ? GLN D 49  ? GLU D 47  GLN D 49  
L 2  HIS D 77  ? GLN D 79  ? HIS D 77  GLN D 79  
L 3  TYR D 85  ? TRP D 94  ? TYR D 85  TRP D 94  
L 4  ALA D 114 ? ASN D 122 ? ALA D 114 ASN D 122 
L 5  LEU D 139 ? MET D 148 ? LEU D 139 MET D 148 
L 6  VAL D 215 ? ILE D 217 ? VAL D 215 ILE D 217 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2  N LEU A 32  ? N LEU A 32  O THR A 106 ? O THR A 106 
B 1 2  N GLN A 38  ? N GLN A 38  O VAL A 257 ? O VAL A 257 
B 2 3  O TYR A 258 ? O TYR A 258 N ARG A 192 ? N ARG A 192 
B 3 4  N GLY A 195 ? N GLY A 195 O VAL A 206 ? O VAL A 206 
B 4 5  O THR A 209 ? O THR A 209 N ALA A 143 ? N ALA A 143 
B 5 6  O ILE A 146 ? O ILE A 146 N ALA A 114 ? N ALA A 114 
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 LYS A 69  ? O LYS A 69  N THR A 62  ? N THR A 62  
B 9 10 N LEU A 61  ? N LEU A 61  O ALA A 172 ? O ALA A 172 
C 1 2  N GLU A 47  ? N GLU A 47  O GLN A 79  ? O GLN A 79  
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 ALA A 114 ? N ALA A 114 O ILE A 146 ? O ILE A 146 
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 GLY B 195 ? N GLY B 195 O VAL B 206 ? O VAL B 206 
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 LYS B 69  ? O LYS B 69  N THR B 62  ? N THR B 62  
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 THR C 259 ? O THR C 259 
H 2 3  O TYR C 258 ? O TYR C 258 N ARG C 192 ? N ARG C 192 
H 3 4  N GLY C 195 ? N GLY C 195 O VAL C 206 ? O VAL C 206 
H 4 5  O THR C 209 ? O THR C 209 N ALA C 143 ? N ALA C 143 
H 5 6  O 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 TYR D 121 ? O TYR D 121 N SER D 86  ? N SER D 86  
K 7 8  O LEU D 90  ? O LEU D 90  N LEU D 70  ? N LEU D 70  
K 8 9  O LYS D 69  ? O LYS D 69  N THR D 62  ? N THR D 62  
K 9 10 N LEU D 61  ? N LEU D 61  O ALA D 172 ? O ALA D 172 
L 1 2  N GLN D 49  ? N GLN D 49  O HIS D 77  ? O HIS D 77  
L 2 3  N ILE D 78  ? N ILE D 78  O TYR D 85  ? O TYR D 85  
L 3 4  N SER D 86  ? N SER D 86  O TYR D 121 ? O TYR D 121 
L 4 5  N LEU D 116 ? N LEU D 116 O VAL D 144 ? O VAL D 144 
L 5 6  N GLU D 147 ? N GLU D 147 O VAL D 215 ? O VAL D 215 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN A 301'  
AC2 Software A E1G 302 ? 11 'BINDING SITE FOR RESIDUE E1G A 302' 
AC3 Software A DMS 303 ? 3  'BINDING SITE FOR RESIDUE DMS A 303' 
AC4 Software B ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN B 301'  
AC5 Software B E1G 302 ? 13 'BINDING SITE FOR RESIDUE E1G B 302' 
AC6 Software B PEG 303 ? 7  'BINDING SITE FOR RESIDUE PEG B 303' 
AC7 Software B EDO 304 ? 3  'BINDING SITE FOR RESIDUE EDO B 304' 
AC8 Software C ZN  301 ? 3  'BINDING SITE FOR RESIDUE ZN C 301'  
AC9 Software D ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN D 301'  
BC1 Software D E1G 302 ? 13 'BINDING SITE FOR RESIDUE E1G D 302' 
BC2 Software D PEG 303 ? 10 'BINDING SITE FOR RESIDUE PEG D 303' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 91  ? HIS A 91  . ? 1_555 ? 
2  AC1 4  HIS A 93  ? HIS A 93  . ? 1_555 ? 
3  AC1 4  HIS A 117 ? HIS A 117 . ? 1_555 ? 
4  AC1 4  E1G F .   ? E1G A 302 . ? 1_555 ? 
5  AC2 11 GLN A 89  ? GLN A 89  . ? 1_555 ? 
6  AC2 11 HIS A 91  ? HIS A 91  . ? 1_555 ? 
7  AC2 11 HIS A 93  ? HIS A 93  . ? 1_555 ? 
8  AC2 11 HIS A 117 ? HIS A 117 . ? 1_555 ? 
9  AC2 11 VAL A 119 ? VAL A 119 . ? 1_555 ? 
10 AC2 11 SER A 133 ? SER A 133 . ? 1_555 ? 
11 AC2 11 LEU A 197 ? LEU A 197 . ? 1_555 ? 
12 AC2 11 THR A 198 ? THR A 198 . ? 1_555 ? 
13 AC2 11 THR A 199 ? THR A 199 . ? 1_555 ? 
14 AC2 11 PRO A 201 ? PRO A 201 . ? 1_555 ? 
15 AC2 11 ZN  E .   ? ZN  A 301 . ? 1_555 ? 
16 AC3 3  PHE A 151 ? PHE A 151 . ? 1_555 ? 
17 AC3 3  HOH P .   ? HOH A 584 . ? 1_555 ? 
18 AC3 3  LYS C 18  ? LYS C 18  . ? 1_554 ? 
19 AC4 4  HIS B 91  ? HIS B 91  . ? 1_555 ? 
20 AC4 4  HIS B 93  ? HIS B 93  . ? 1_555 ? 
21 AC4 4  HIS B 117 ? HIS B 117 . ? 1_555 ? 
22 AC4 4  E1G I .   ? E1G B 302 . ? 1_555 ? 
23 AC5 13 GLN B 89  ? GLN B 89  . ? 1_555 ? 
24 AC5 13 HIS B 91  ? HIS B 91  . ? 1_555 ? 
25 AC5 13 HIS B 93  ? HIS B 93  . ? 1_555 ? 
26 AC5 13 HIS B 117 ? HIS B 117 . ? 1_555 ? 
27 AC5 13 VAL B 119 ? VAL B 119 . ? 1_555 ? 
28 AC5 13 SER B 133 ? SER B 133 . ? 1_555 ? 
29 AC5 13 LEU B 197 ? LEU B 197 . ? 1_555 ? 
30 AC5 13 THR B 198 ? THR B 198 . ? 1_555 ? 
31 AC5 13 THR B 199 ? THR B 199 . ? 1_555 ? 
32 AC5 13 PRO B 201 ? PRO B 201 . ? 1_555 ? 
33 AC5 13 TRP B 208 ? TRP B 208 . ? 1_555 ? 
34 AC5 13 ZN  H .   ? ZN  B 301 . ? 1_555 ? 
35 AC5 13 HOH Q .   ? HOH B 580 . ? 1_555 ? 
36 AC6 7  TRP B 4   ? TRP B 4   . ? 1_555 ? 
37 AC6 7  ASN B 64  ? ASN B 64  . ? 1_555 ? 
38 AC6 7  HIS B 66  ? HIS B 66  . ? 1_555 ? 
39 AC6 7  GLN B 89  ? GLN B 89  . ? 1_555 ? 
40 AC6 7  HIS B 91  ? HIS B 91  . ? 1_555 ? 
41 AC6 7  THR B 199 ? THR B 199 . ? 1_555 ? 
42 AC6 7  HOH Q .   ? HOH B 566 . ? 1_555 ? 
43 AC7 3  ASP B 156 ? ASP B 156 . ? 1_555 ? 
44 AC7 3  SER B 160 ? SER B 160 . ? 1_555 ? 
45 AC7 3  HOH Q .   ? HOH B 513 . ? 1_555 ? 
46 AC8 3  HIS C 91  ? HIS C 91  . ? 1_555 ? 
47 AC8 3  HIS C 93  ? HIS C 93  . ? 1_555 ? 
48 AC8 3  HIS C 117 ? HIS C 117 . ? 1_555 ? 
49 AC9 4  HIS D 91  ? HIS D 91  . ? 1_555 ? 
50 AC9 4  HIS D 93  ? HIS D 93  . ? 1_555 ? 
51 AC9 4  HIS D 117 ? HIS D 117 . ? 1_555 ? 
52 AC9 4  E1G N .   ? E1G D 302 . ? 1_555 ? 
53 BC1 13 GLN D 89  ? GLN D 89  . ? 1_555 ? 
54 BC1 13 HIS D 91  ? HIS D 91  . ? 1_555 ? 
55 BC1 13 HIS D 93  ? HIS D 93  . ? 1_555 ? 
56 BC1 13 HIS D 117 ? HIS D 117 . ? 1_555 ? 
57 BC1 13 VAL D 119 ? VAL D 119 . ? 1_555 ? 
58 BC1 13 SER D 133 ? SER D 133 . ? 1_555 ? 
59 BC1 13 LEU D 197 ? LEU D 197 . ? 1_555 ? 
60 BC1 13 THR D 198 ? THR D 198 . ? 1_555 ? 
61 BC1 13 THR D 199 ? THR D 199 . ? 1_555 ? 
62 BC1 13 PRO D 201 ? PRO D 201 . ? 1_555 ? 
63 BC1 13 ZN  M .   ? ZN  D 301 . ? 1_555 ? 
64 BC1 13 PEG O .   ? PEG D 303 . ? 1_555 ? 
65 BC1 13 HOH S .   ? HOH D 535 . ? 1_555 ? 
66 BC2 10 TRP D 4   ? TRP D 4   . ? 1_555 ? 
67 BC2 10 ASN D 64  ? ASN D 64  . ? 1_555 ? 
68 BC2 10 HIS D 66  ? HIS D 66  . ? 1_555 ? 
69 BC2 10 SER D 67  ? SER D 67  . ? 1_555 ? 
70 BC2 10 GLN D 89  ? GLN D 89  . ? 1_555 ? 
71 BC2 10 HIS D 91  ? HIS D 91  . ? 1_555 ? 
72 BC2 10 THR D 199 ? THR D 199 . ? 1_555 ? 
73 BC2 10 E1G N .   ? E1G D 302 . ? 1_555 ? 
74 BC2 10 HOH S .   ? HOH D 422 . ? 1_555 ? 
75 BC2 10 HOH S .   ? HOH D 533 . ? 1_555 ? 
# 
_pdbx_entry_details.entry_id                   4KP8 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 245 ? ? -91.95  50.87  
2 1 ASP B 99  ? ? -153.54 76.89  
3 1 ASN B 245 ? ? -85.92  48.77  
4 1 SER C 238 ? ? -110.97 77.41  
5 1 ASN C 245 ? ? -89.39  48.80  
6 1 PHE C 252 ? ? -152.40 88.42  
7 1 GLU C 254 ? ? 73.07   -46.58 
8 1 GLU C 254 ? ? 73.07   -45.82 
9 1 GLU D 254 ? ? 49.55   25.94  
# 
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 B LYS 3   ? B LYS 3   
6  1 Y 1 B GLN 263 ? B GLN 263 
7  1 Y 1 C MET 1   ? C MET 1   
8  1 Y 1 C SER 2   ? C SER 2   
9  1 Y 1 D MET 1   ? D MET 1   
10 1 Y 1 D SER 2   ? D SER 2   
11 1 Y 1 D LYS 3   ? D LYS 3   
# 
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  
DMS S    S  N N 88  
DMS O    O  N N 89  
DMS C1   C  N N 90  
DMS C2   C  N N 91  
DMS H11  H  N N 92  
DMS H12  H  N N 93  
DMS H13  H  N N 94  
DMS H21  H  N N 95  
DMS H22  H  N N 96  
DMS H23  H  N N 97  
E1G O19  O  N N 98  
E1G S17  S  N N 99  
E1G O18  O  N N 100 
E1G N20  N  N N 101 
E1G C4   C  Y N 102 
E1G C5   C  Y N 103 
E1G C6   C  Y N 104 
E1G C1   C  Y N 105 
E1G C3   C  Y N 106 
E1G C2   C  Y N 107 
E1G C7   C  N N 108 
E1G O13  O  N N 109 
E1G C8   C  N N 110 
E1G S9   S  N N 111 
E1G C10  C  Y N 112 
E1G N12  N  Y N 113 
E1G C15  C  Y N 114 
E1G C16  C  Y N 115 
E1G C14  C  Y N 116 
E1G N11  N  Y N 117 
E1G H1   H  N N 118 
E1G H2   H  N N 119 
E1G H3   H  N N 120 
E1G H4   H  N N 121 
E1G H5   H  N N 122 
E1G H6   H  N N 123 
E1G H7   H  N N 124 
E1G H8   H  N N 125 
E1G H9   H  N N 126 
E1G H10  H  N N 127 
E1G H11  H  N N 128 
EDO C1   C  N N 129 
EDO O1   O  N N 130 
EDO C2   C  N N 131 
EDO O2   O  N N 132 
EDO H11  H  N N 133 
EDO H12  H  N N 134 
EDO HO1  H  N N 135 
EDO H21  H  N N 136 
EDO H22  H  N N 137 
EDO HO2  H  N N 138 
GLN N    N  N N 139 
GLN CA   C  N S 140 
GLN C    C  N N 141 
GLN O    O  N N 142 
GLN CB   C  N N 143 
GLN CG   C  N N 144 
GLN CD   C  N N 145 
GLN OE1  O  N N 146 
GLN NE2  N  N N 147 
GLN OXT  O  N N 148 
GLN H    H  N N 149 
GLN H2   H  N N 150 
GLN HA   H  N N 151 
GLN HB2  H  N N 152 
GLN HB3  H  N N 153 
GLN HG2  H  N N 154 
GLN HG3  H  N N 155 
GLN HE21 H  N N 156 
GLN HE22 H  N N 157 
GLN HXT  H  N N 158 
GLU N    N  N N 159 
GLU CA   C  N S 160 
GLU C    C  N N 161 
GLU O    O  N N 162 
GLU CB   C  N N 163 
GLU CG   C  N N 164 
GLU CD   C  N N 165 
GLU OE1  O  N N 166 
GLU OE2  O  N N 167 
GLU OXT  O  N N 168 
GLU H    H  N N 169 
GLU H2   H  N N 170 
GLU HA   H  N N 171 
GLU HB2  H  N N 172 
GLU HB3  H  N N 173 
GLU HG2  H  N N 174 
GLU HG3  H  N N 175 
GLU HE2  H  N N 176 
GLU HXT  H  N N 177 
GLY N    N  N N 178 
GLY CA   C  N N 179 
GLY C    C  N N 180 
GLY O    O  N N 181 
GLY OXT  O  N N 182 
GLY H    H  N N 183 
GLY H2   H  N N 184 
GLY HA2  H  N N 185 
GLY HA3  H  N N 186 
GLY HXT  H  N N 187 
HIS N    N  N N 188 
HIS CA   C  N S 189 
HIS C    C  N N 190 
HIS O    O  N N 191 
HIS CB   C  N N 192 
HIS CG   C  Y N 193 
HIS ND1  N  Y N 194 
HIS CD2  C  Y N 195 
HIS CE1  C  Y N 196 
HIS NE2  N  Y N 197 
HIS OXT  O  N N 198 
HIS H    H  N N 199 
HIS H2   H  N N 200 
HIS HA   H  N N 201 
HIS HB2  H  N N 202 
HIS HB3  H  N N 203 
HIS HD1  H  N N 204 
HIS HD2  H  N N 205 
HIS HE1  H  N N 206 
HIS HE2  H  N N 207 
HIS HXT  H  N N 208 
HOH O    O  N N 209 
HOH H1   H  N N 210 
HOH H2   H  N N 211 
ILE N    N  N N 212 
ILE CA   C  N S 213 
ILE C    C  N N 214 
ILE O    O  N N 215 
ILE CB   C  N S 216 
ILE CG1  C  N N 217 
ILE CG2  C  N N 218 
ILE CD1  C  N N 219 
ILE OXT  O  N N 220 
ILE H    H  N N 221 
ILE H2   H  N N 222 
ILE HA   H  N N 223 
ILE HB   H  N N 224 
ILE HG12 H  N N 225 
ILE HG13 H  N N 226 
ILE HG21 H  N N 227 
ILE HG22 H  N N 228 
ILE HG23 H  N N 229 
ILE HD11 H  N N 230 
ILE HD12 H  N N 231 
ILE HD13 H  N N 232 
ILE HXT  H  N N 233 
LEU N    N  N N 234 
LEU CA   C  N S 235 
LEU C    C  N N 236 
LEU O    O  N N 237 
LEU CB   C  N N 238 
LEU CG   C  N N 239 
LEU CD1  C  N N 240 
LEU CD2  C  N N 241 
LEU OXT  O  N N 242 
LEU H    H  N N 243 
LEU H2   H  N N 244 
LEU HA   H  N N 245 
LEU HB2  H  N N 246 
LEU HB3  H  N N 247 
LEU HG   H  N N 248 
LEU HD11 H  N N 249 
LEU HD12 H  N N 250 
LEU HD13 H  N N 251 
LEU HD21 H  N N 252 
LEU HD22 H  N N 253 
LEU HD23 H  N N 254 
LEU HXT  H  N N 255 
LYS N    N  N N 256 
LYS CA   C  N S 257 
LYS C    C  N N 258 
LYS O    O  N N 259 
LYS CB   C  N N 260 
LYS CG   C  N N 261 
LYS CD   C  N N 262 
LYS CE   C  N N 263 
LYS NZ   N  N N 264 
LYS OXT  O  N N 265 
LYS H    H  N N 266 
LYS H2   H  N N 267 
LYS HA   H  N N 268 
LYS HB2  H  N N 269 
LYS HB3  H  N N 270 
LYS HG2  H  N N 271 
LYS HG3  H  N N 272 
LYS HD2  H  N N 273 
LYS HD3  H  N N 274 
LYS HE2  H  N N 275 
LYS HE3  H  N N 276 
LYS HZ1  H  N N 277 
LYS HZ2  H  N N 278 
LYS HZ3  H  N N 279 
LYS HXT  H  N N 280 
MET N    N  N N 281 
MET CA   C  N S 282 
MET C    C  N N 283 
MET O    O  N N 284 
MET CB   C  N N 285 
MET CG   C  N N 286 
MET SD   S  N N 287 
MET CE   C  N N 288 
MET OXT  O  N N 289 
MET H    H  N N 290 
MET H2   H  N N 291 
MET HA   H  N N 292 
MET HB2  H  N N 293 
MET HB3  H  N N 294 
MET HG2  H  N N 295 
MET HG3  H  N N 296 
MET HE1  H  N N 297 
MET HE2  H  N N 298 
MET HE3  H  N N 299 
MET HXT  H  N N 300 
PEG C1   C  N N 301 
PEG O1   O  N N 302 
PEG C2   C  N N 303 
PEG O2   O  N N 304 
PEG C3   C  N N 305 
PEG C4   C  N N 306 
PEG O4   O  N N 307 
PEG H11  H  N N 308 
PEG H12  H  N N 309 
PEG HO1  H  N N 310 
PEG H21  H  N N 311 
PEG H22  H  N N 312 
PEG H31  H  N N 313 
PEG H32  H  N N 314 
PEG H41  H  N N 315 
PEG H42  H  N N 316 
PEG HO4  H  N N 317 
PHE N    N  N N 318 
PHE CA   C  N S 319 
PHE C    C  N N 320 
PHE O    O  N N 321 
PHE CB   C  N N 322 
PHE CG   C  Y N 323 
PHE CD1  C  Y N 324 
PHE CD2  C  Y N 325 
PHE CE1  C  Y N 326 
PHE CE2  C  Y N 327 
PHE CZ   C  Y N 328 
PHE OXT  O  N N 329 
PHE H    H  N N 330 
PHE H2   H  N N 331 
PHE HA   H  N N 332 
PHE HB2  H  N N 333 
PHE HB3  H  N N 334 
PHE HD1  H  N N 335 
PHE HD2  H  N N 336 
PHE HE1  H  N N 337 
PHE HE2  H  N N 338 
PHE HZ   H  N N 339 
PHE HXT  H  N N 340 
PRO N    N  N N 341 
PRO CA   C  N S 342 
PRO C    C  N N 343 
PRO O    O  N N 344 
PRO CB   C  N N 345 
PRO CG   C  N N 346 
PRO CD   C  N N 347 
PRO OXT  O  N N 348 
PRO H    H  N N 349 
PRO HA   H  N N 350 
PRO HB2  H  N N 351 
PRO HB3  H  N N 352 
PRO HG2  H  N N 353 
PRO HG3  H  N N 354 
PRO HD2  H  N N 355 
PRO HD3  H  N N 356 
PRO HXT  H  N N 357 
SER N    N  N N 358 
SER CA   C  N S 359 
SER C    C  N N 360 
SER O    O  N N 361 
SER CB   C  N N 362 
SER OG   O  N N 363 
SER OXT  O  N N 364 
SER H    H  N N 365 
SER H2   H  N N 366 
SER HA   H  N N 367 
SER HB2  H  N N 368 
SER HB3  H  N N 369 
SER HG   H  N N 370 
SER HXT  H  N N 371 
THR N    N  N N 372 
THR CA   C  N S 373 
THR C    C  N N 374 
THR O    O  N N 375 
THR CB   C  N R 376 
THR OG1  O  N N 377 
THR CG2  C  N N 378 
THR OXT  O  N N 379 
THR H    H  N N 380 
THR H2   H  N N 381 
THR HA   H  N N 382 
THR HB   H  N N 383 
THR HG1  H  N N 384 
THR HG21 H  N N 385 
THR HG22 H  N N 386 
THR HG23 H  N N 387 
THR HXT  H  N N 388 
TRP N    N  N N 389 
TRP CA   C  N S 390 
TRP C    C  N N 391 
TRP O    O  N N 392 
TRP CB   C  N N 393 
TRP CG   C  Y N 394 
TRP CD1  C  Y N 395 
TRP CD2  C  Y N 396 
TRP NE1  N  Y N 397 
TRP CE2  C  Y N 398 
TRP CE3  C  Y N 399 
TRP CZ2  C  Y N 400 
TRP CZ3  C  Y N 401 
TRP CH2  C  Y N 402 
TRP OXT  O  N N 403 
TRP H    H  N N 404 
TRP H2   H  N N 405 
TRP HA   H  N N 406 
TRP HB2  H  N N 407 
TRP HB3  H  N N 408 
TRP HD1  H  N N 409 
TRP HE1  H  N N 410 
TRP HE3  H  N N 411 
TRP HZ2  H  N N 412 
TRP HZ3  H  N N 413 
TRP HH2  H  N N 414 
TRP HXT  H  N N 415 
TYR N    N  N N 416 
TYR CA   C  N S 417 
TYR C    C  N N 418 
TYR O    O  N N 419 
TYR CB   C  N N 420 
TYR CG   C  Y N 421 
TYR CD1  C  Y N 422 
TYR CD2  C  Y N 423 
TYR CE1  C  Y N 424 
TYR CE2  C  Y N 425 
TYR CZ   C  Y N 426 
TYR OH   O  N N 427 
TYR OXT  O  N N 428 
TYR H    H  N N 429 
TYR H2   H  N N 430 
TYR HA   H  N N 431 
TYR HB2  H  N N 432 
TYR HB3  H  N N 433 
TYR HD1  H  N N 434 
TYR HD2  H  N N 435 
TYR HE1  H  N N 436 
TYR HE2  H  N N 437 
TYR HH   H  N N 438 
TYR HXT  H  N N 439 
VAL N    N  N N 440 
VAL CA   C  N S 441 
VAL C    C  N N 442 
VAL O    O  N N 443 
VAL CB   C  N N 444 
VAL CG1  C  N N 445 
VAL CG2  C  N N 446 
VAL OXT  O  N N 447 
VAL H    H  N N 448 
VAL H2   H  N N 449 
VAL HA   H  N N 450 
VAL HB   H  N N 451 
VAL HG11 H  N N 452 
VAL HG12 H  N N 453 
VAL HG13 H  N N 454 
VAL HG21 H  N N 455 
VAL HG22 H  N N 456 
VAL HG23 H  N N 457 
VAL HXT  H  N N 458 
ZN  ZN   ZN N N 459 
# 
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  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
E1G N20 S17  sing N N 92  
E1G O19 S17  doub N N 93  
E1G S17 O18  doub N N 94  
E1G S17 C4   sing N N 95  
E1G C4  C5   doub Y N 96  
E1G C4  C3   sing Y N 97  
E1G C5  C6   sing Y N 98  
E1G C3  C2   doub Y N 99  
E1G C6  C1   doub Y N 100 
E1G C2  C1   sing Y N 101 
E1G C2  C7   sing N N 102 
E1G O13 C7   doub N N 103 
E1G C7  C8   sing N N 104 
E1G C8  S9   sing N N 105 
E1G S9  C10  sing N N 106 
E1G C10 N11  doub Y N 107 
E1G C10 N12  sing Y N 108 
E1G N11 C14  sing Y N 109 
E1G N12 C15  doub Y N 110 
E1G C14 C16  doub Y N 111 
E1G C15 C16  sing Y N 112 
E1G N20 H1   sing N N 113 
E1G N20 H2   sing N N 114 
E1G C5  H3   sing N N 115 
E1G C6  H4   sing N N 116 
E1G C1  H5   sing N N 117 
E1G C3  H6   sing N N 118 
E1G C8  H7   sing N N 119 
E1G C8  H8   sing N N 120 
E1G C15 H9   sing N N 121 
E1G C16 H10  sing N N 122 
E1G C14 H11  sing N N 123 
EDO C1  O1   sing N N 124 
EDO C1  C2   sing N N 125 
EDO C1  H11  sing N N 126 
EDO C1  H12  sing N N 127 
EDO O1  HO1  sing N N 128 
EDO C2  O2   sing N N 129 
EDO C2  H21  sing N N 130 
EDO C2  H22  sing N N 131 
EDO O2  HO2  sing N N 132 
GLN N   CA   sing N N 133 
GLN N   H    sing N N 134 
GLN N   H2   sing N N 135 
GLN CA  C    sing N N 136 
GLN CA  CB   sing N N 137 
GLN CA  HA   sing N N 138 
GLN C   O    doub N N 139 
GLN C   OXT  sing N N 140 
GLN CB  CG   sing N N 141 
GLN CB  HB2  sing N N 142 
GLN CB  HB3  sing N N 143 
GLN CG  CD   sing N N 144 
GLN CG  HG2  sing N N 145 
GLN CG  HG3  sing N N 146 
GLN CD  OE1  doub N N 147 
GLN CD  NE2  sing N N 148 
GLN NE2 HE21 sing N N 149 
GLN NE2 HE22 sing N N 150 
GLN OXT HXT  sing N N 151 
GLU N   CA   sing N N 152 
GLU N   H    sing N N 153 
GLU N   H2   sing N N 154 
GLU CA  C    sing N N 155 
GLU CA  CB   sing N N 156 
GLU CA  HA   sing N N 157 
GLU C   O    doub N N 158 
GLU C   OXT  sing N N 159 
GLU CB  CG   sing N N 160 
GLU CB  HB2  sing N N 161 
GLU CB  HB3  sing N N 162 
GLU CG  CD   sing N N 163 
GLU CG  HG2  sing N N 164 
GLU CG  HG3  sing N N 165 
GLU CD  OE1  doub N N 166 
GLU CD  OE2  sing N N 167 
GLU OE2 HE2  sing N N 168 
GLU OXT HXT  sing N N 169 
GLY N   CA   sing N N 170 
GLY N   H    sing N N 171 
GLY N   H2   sing N N 172 
GLY CA  C    sing N N 173 
GLY CA  HA2  sing N N 174 
GLY CA  HA3  sing N N 175 
GLY C   O    doub N N 176 
GLY C   OXT  sing N N 177 
GLY OXT HXT  sing N N 178 
HIS N   CA   sing N N 179 
HIS N   H    sing N N 180 
HIS N   H2   sing N N 181 
HIS CA  C    sing N N 182 
HIS CA  CB   sing N N 183 
HIS CA  HA   sing N N 184 
HIS C   O    doub N N 185 
HIS C   OXT  sing N N 186 
HIS CB  CG   sing N N 187 
HIS CB  HB2  sing N N 188 
HIS CB  HB3  sing N N 189 
HIS CG  ND1  sing Y N 190 
HIS CG  CD2  doub Y N 191 
HIS ND1 CE1  doub Y N 192 
HIS ND1 HD1  sing N N 193 
HIS CD2 NE2  sing Y N 194 
HIS CD2 HD2  sing N N 195 
HIS CE1 NE2  sing Y N 196 
HIS CE1 HE1  sing N N 197 
HIS NE2 HE2  sing N N 198 
HIS OXT HXT  sing N N 199 
HOH O   H1   sing N N 200 
HOH O   H2   sing N N 201 
ILE N   CA   sing N N 202 
ILE N   H    sing N N 203 
ILE N   H2   sing N N 204 
ILE CA  C    sing N N 205 
ILE CA  CB   sing N N 206 
ILE CA  HA   sing N N 207 
ILE C   O    doub N N 208 
ILE C   OXT  sing N N 209 
ILE CB  CG1  sing N N 210 
ILE CB  CG2  sing N N 211 
ILE CB  HB   sing N N 212 
ILE CG1 CD1  sing N N 213 
ILE CG1 HG12 sing N N 214 
ILE CG1 HG13 sing N N 215 
ILE CG2 HG21 sing N N 216 
ILE CG2 HG22 sing N N 217 
ILE CG2 HG23 sing N N 218 
ILE CD1 HD11 sing N N 219 
ILE CD1 HD12 sing N N 220 
ILE CD1 HD13 sing N N 221 
ILE OXT HXT  sing N N 222 
LEU N   CA   sing N N 223 
LEU N   H    sing N N 224 
LEU N   H2   sing N N 225 
LEU CA  C    sing N N 226 
LEU CA  CB   sing N N 227 
LEU CA  HA   sing N N 228 
LEU C   O    doub N N 229 
LEU C   OXT  sing N N 230 
LEU CB  CG   sing N N 231 
LEU CB  HB2  sing N N 232 
LEU CB  HB3  sing N N 233 
LEU CG  CD1  sing N N 234 
LEU CG  CD2  sing N N 235 
LEU CG  HG   sing N N 236 
LEU CD1 HD11 sing N N 237 
LEU CD1 HD12 sing N N 238 
LEU CD1 HD13 sing N N 239 
LEU CD2 HD21 sing N N 240 
LEU CD2 HD22 sing N N 241 
LEU CD2 HD23 sing N N 242 
LEU OXT HXT  sing N N 243 
LYS N   CA   sing N N 244 
LYS N   H    sing N N 245 
LYS N   H2   sing N N 246 
LYS CA  C    sing N N 247 
LYS CA  CB   sing N N 248 
LYS CA  HA   sing N N 249 
LYS C   O    doub N N 250 
LYS C   OXT  sing N N 251 
LYS CB  CG   sing N N 252 
LYS CB  HB2  sing N N 253 
LYS CB  HB3  sing N N 254 
LYS CG  CD   sing N N 255 
LYS CG  HG2  sing N N 256 
LYS CG  HG3  sing N N 257 
LYS CD  CE   sing N N 258 
LYS CD  HD2  sing N N 259 
LYS CD  HD3  sing N N 260 
LYS CE  NZ   sing N N 261 
LYS CE  HE2  sing N N 262 
LYS CE  HE3  sing N N 263 
LYS NZ  HZ1  sing N N 264 
LYS NZ  HZ2  sing N N 265 
LYS NZ  HZ3  sing N N 266 
LYS OXT HXT  sing N N 267 
MET N   CA   sing N N 268 
MET N   H    sing N N 269 
MET N   H2   sing N N 270 
MET CA  C    sing N N 271 
MET CA  CB   sing N N 272 
MET CA  HA   sing N N 273 
MET C   O    doub N N 274 
MET C   OXT  sing N N 275 
MET CB  CG   sing N N 276 
MET CB  HB2  sing N N 277 
MET CB  HB3  sing N N 278 
MET CG  SD   sing N N 279 
MET CG  HG2  sing N N 280 
MET CG  HG3  sing N N 281 
MET SD  CE   sing N N 282 
MET CE  HE1  sing N N 283 
MET CE  HE2  sing N N 284 
MET CE  HE3  sing N N 285 
MET OXT HXT  sing N N 286 
PEG C1  O1   sing N N 287 
PEG C1  C2   sing N N 288 
PEG C1  H11  sing N N 289 
PEG C1  H12  sing N N 290 
PEG O1  HO1  sing N N 291 
PEG C2  O2   sing N N 292 
PEG C2  H21  sing N N 293 
PEG C2  H22  sing N N 294 
PEG O2  C3   sing N N 295 
PEG C3  C4   sing N N 296 
PEG C3  H31  sing N N 297 
PEG C3  H32  sing N N 298 
PEG C4  O4   sing N N 299 
PEG C4  H41  sing N N 300 
PEG C4  H42  sing N N 301 
PEG O4  HO4  sing N N 302 
PHE N   CA   sing N N 303 
PHE N   H    sing N N 304 
PHE N   H2   sing N N 305 
PHE CA  C    sing N N 306 
PHE CA  CB   sing N N 307 
PHE CA  HA   sing N N 308 
PHE C   O    doub N N 309 
PHE C   OXT  sing N N 310 
PHE CB  CG   sing N N 311 
PHE CB  HB2  sing N N 312 
PHE CB  HB3  sing N N 313 
PHE CG  CD1  doub Y N 314 
PHE CG  CD2  sing Y N 315 
PHE CD1 CE1  sing Y N 316 
PHE CD1 HD1  sing N N 317 
PHE CD2 CE2  doub Y N 318 
PHE CD2 HD2  sing N N 319 
PHE CE1 CZ   doub Y N 320 
PHE CE1 HE1  sing N N 321 
PHE CE2 CZ   sing Y N 322 
PHE CE2 HE2  sing N N 323 
PHE CZ  HZ   sing N N 324 
PHE OXT HXT  sing N N 325 
PRO N   CA   sing N N 326 
PRO N   CD   sing N N 327 
PRO N   H    sing N N 328 
PRO CA  C    sing N N 329 
PRO CA  CB   sing N N 330 
PRO CA  HA   sing N N 331 
PRO C   O    doub N N 332 
PRO C   OXT  sing N N 333 
PRO CB  CG   sing N N 334 
PRO CB  HB2  sing N N 335 
PRO CB  HB3  sing N N 336 
PRO CG  CD   sing N N 337 
PRO CG  HG2  sing N N 338 
PRO CG  HG3  sing N N 339 
PRO CD  HD2  sing N N 340 
PRO CD  HD3  sing N N 341 
PRO OXT HXT  sing N N 342 
SER N   CA   sing N N 343 
SER N   H    sing N N 344 
SER N   H2   sing N N 345 
SER CA  C    sing N N 346 
SER CA  CB   sing N N 347 
SER CA  HA   sing N N 348 
SER C   O    doub N N 349 
SER C   OXT  sing N N 350 
SER CB  OG   sing N N 351 
SER CB  HB2  sing N N 352 
SER CB  HB3  sing N N 353 
SER OG  HG   sing N N 354 
SER OXT HXT  sing N N 355 
THR N   CA   sing N N 356 
THR N   H    sing N N 357 
THR N   H2   sing N N 358 
THR CA  C    sing N N 359 
THR CA  CB   sing N N 360 
THR CA  HA   sing N N 361 
THR C   O    doub N N 362 
THR C   OXT  sing N N 363 
THR CB  OG1  sing N N 364 
THR CB  CG2  sing N N 365 
THR CB  HB   sing N N 366 
THR OG1 HG1  sing N N 367 
THR CG2 HG21 sing N N 368 
THR CG2 HG22 sing N N 369 
THR CG2 HG23 sing N N 370 
THR OXT HXT  sing N N 371 
TRP N   CA   sing N N 372 
TRP N   H    sing N N 373 
TRP N   H2   sing N N 374 
TRP CA  C    sing N N 375 
TRP CA  CB   sing N N 376 
TRP CA  HA   sing N N 377 
TRP C   O    doub N N 378 
TRP C   OXT  sing N N 379 
TRP CB  CG   sing N N 380 
TRP CB  HB2  sing N N 381 
TRP CB  HB3  sing N N 382 
TRP CG  CD1  doub Y N 383 
TRP CG  CD2  sing Y N 384 
TRP CD1 NE1  sing Y N 385 
TRP CD1 HD1  sing N N 386 
TRP CD2 CE2  doub Y N 387 
TRP CD2 CE3  sing Y N 388 
TRP NE1 CE2  sing Y N 389 
TRP NE1 HE1  sing N N 390 
TRP CE2 CZ2  sing Y N 391 
TRP CE3 CZ3  doub Y N 392 
TRP CE3 HE3  sing N N 393 
TRP CZ2 CH2  doub Y N 394 
TRP CZ2 HZ2  sing N N 395 
TRP CZ3 CH2  sing Y N 396 
TRP CZ3 HZ3  sing N N 397 
TRP CH2 HH2  sing N N 398 
TRP OXT HXT  sing N N 399 
TYR N   CA   sing N N 400 
TYR N   H    sing N N 401 
TYR N   H2   sing N N 402 
TYR CA  C    sing N N 403 
TYR CA  CB   sing N N 404 
TYR CA  HA   sing N N 405 
TYR C   O    doub N N 406 
TYR C   OXT  sing N N 407 
TYR CB  CG   sing N N 408 
TYR CB  HB2  sing N N 409 
TYR CB  HB3  sing N N 410 
TYR CG  CD1  doub Y N 411 
TYR CG  CD2  sing Y N 412 
TYR CD1 CE1  sing Y N 413 
TYR CD1 HD1  sing N N 414 
TYR CD2 CE2  doub Y N 415 
TYR CD2 HD2  sing N N 416 
TYR CE1 CZ   doub Y N 417 
TYR CE1 HE1  sing N N 418 
TYR CE2 CZ   sing Y N 419 
TYR CE2 HE2  sing N N 420 
TYR CZ  OH   sing N N 421 
TYR OH  HH   sing N N 422 
TYR OXT HXT  sing N N 423 
VAL N   CA   sing N N 424 
VAL N   H    sing N N 425 
VAL N   H2   sing N N 426 
VAL CA  C    sing N N 427 
VAL CA  CB   sing N N 428 
VAL CA  HA   sing N N 429 
VAL C   O    doub N N 430 
VAL C   OXT  sing N N 431 
VAL CB  CG1  sing N N 432 
VAL CB  CG2  sing N N 433 
VAL CB  HB   sing N N 434 
VAL CG1 HG11 sing N N 435 
VAL CG1 HG12 sing N N 436 
VAL CG1 HG13 sing N N 437 
VAL CG2 HG21 sing N N 438 
VAL CG2 HG22 sing N N 439 
VAL CG2 HG23 sing N N 440 
VAL OXT HXT  sing N N 441 
# 
_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                    4KP8 
_atom_sites.fract_transf_matrix[1][1]   0.021360 
_atom_sites.fract_transf_matrix[1][2]   -0.001304 
_atom_sites.fract_transf_matrix[1][3]   -0.002090 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014896 
_atom_sites.fract_transf_matrix[2][3]   -0.002043 
_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]   0.012501 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . LYS A 1 3   ? 1.599   21.249  9.496   1.00 25.80 ? 3   LYS A N   1 
ATOM   2    C  CA  . LYS A 1 3   ? 2.302   20.889  8.234   1.00 26.87 ? 3   LYS A CA  1 
ATOM   3    C  C   . LYS A 1 3   ? 2.187   19.383  8.042   1.00 24.30 ? 3   LYS A C   1 
ATOM   4    O  O   . LYS A 1 3   ? 1.803   18.653  8.978   1.00 23.67 ? 3   LYS A O   1 
ATOM   5    C  CB  . LYS A 1 3   ? 3.780   21.233  8.319   1.00 29.63 ? 3   LYS A CB  1 
ATOM   6    C  CG  . LYS A 1 3   ? 4.418   20.697  9.586   1.00 32.17 ? 3   LYS A CG  1 
ATOM   7    C  CD  . LYS A 1 3   ? 5.756   21.375  9.904   1.00 35.12 ? 3   LYS A CD  1 
ATOM   8    C  CE  . LYS A 1 3   ? 5.795   21.813  11.377  1.00 35.71 ? 3   LYS A CE  1 
ATOM   9    N  NZ  . LYS A 1 3   ? 4.641   21.256  12.160  1.00 37.00 ? 3   LYS A NZ  1 
ATOM   10   N  N   . TRP A 1 4   ? 2.535   18.930  6.841   1.00 19.19 ? 4   TRP A N   1 
ATOM   11   C  CA  . TRP A 1 4   ? 2.488   17.522  6.577   1.00 17.08 ? 4   TRP A CA  1 
ATOM   12   C  C   . TRP A 1 4   ? 3.624   17.208  5.594   1.00 14.60 ? 4   TRP A C   1 
ATOM   13   O  O   . TRP A 1 4   ? 4.066   18.076  4.842   1.00 15.75 ? 4   TRP A O   1 
ATOM   14   C  CB  . TRP A 1 4   ? 1.112   17.177  6.046   1.00 15.21 ? 4   TRP A CB  1 
ATOM   15   C  CG  . TRP A 1 4   ? 0.693   17.860  4.751   1.00 15.46 ? 4   TRP A CG  1 
ATOM   16   C  CD1 . TRP A 1 4   ? -0.021  19.018  4.635   1.00 13.92 ? 4   TRP A CD1 1 
ATOM   17   C  CD2 . TRP A 1 4   ? 0.927   17.403  3.405   1.00 14.03 ? 4   TRP A CD2 1 
ATOM   18   N  NE1 . TRP A 1 4   ? -0.232  19.320  3.311   1.00 13.87 ? 4   TRP A NE1 1 
ATOM   19   C  CE2 . TRP A 1 4   ? 0.339   18.347  2.536   1.00 13.14 ? 4   TRP A CE2 1 
ATOM   20   C  CE3 . TRP A 1 4   ? 1.583   16.297  2.852   1.00 13.97 ? 4   TRP A CE3 1 
ATOM   21   C  CZ2 . TRP A 1 4   ? 0.387   18.219  1.148   1.00 14.90 ? 4   TRP A CZ2 1 
ATOM   22   C  CZ3 . TRP A 1 4   ? 1.629   16.173  1.467   1.00 14.16 ? 4   TRP A CZ3 1 
ATOM   23   C  CH2 . TRP A 1 4   ? 1.033   17.130  0.635   1.00 15.06 ? 4   TRP A CH2 1 
ATOM   24   N  N   . THR A 1 5   ? 4.080   15.973  5.601   1.00 13.40 ? 5   THR A N   1 
ATOM   25   C  CA  . THR A 1 5   ? 5.131   15.485  4.721   1.00 14.94 ? 5   THR A CA  1 
ATOM   26   C  C   . THR A 1 5   ? 4.769   14.079  4.231   1.00 13.94 ? 5   THR A C   1 
ATOM   27   O  O   . THR A 1 5   ? 3.660   13.560  4.519   1.00 13.08 ? 5   THR A O   1 
ATOM   28   C  CB  . THR A 1 5   ? 6.483   15.404  5.463   1.00 15.72 ? 5   THR A CB  1 
ATOM   29   O  OG1 . THR A 1 5   ? 6.391   14.459  6.519   1.00 18.17 ? 5   THR A OG1 1 
ATOM   30   C  CG2 . THR A 1 5   ? 6.832   16.737  6.079   1.00 15.31 ? 5   THR A CG2 1 
ATOM   31   N  N   . TYR A 1 6   ? 5.702   13.463  3.498   1.00 12.83 ? 6   TYR A N   1 
ATOM   32   C  CA  . TYR A 1 6   ? 5.623   12.032  3.172   1.00 12.59 ? 6   TYR A CA  1 
ATOM   33   C  C   . TYR A 1 6   ? 6.625   11.169  3.949   1.00 14.19 ? 6   TYR A C   1 
ATOM   34   O  O   . TYR A 1 6   ? 6.790   9.984   3.663   1.00 13.50 ? 6   TYR A O   1 
ATOM   35   C  CB  . TYR A 1 6   ? 5.841   11.856  1.676   1.00 11.47 ? 6   TYR A CB  1 
ATOM   36   C  CG  . TYR A 1 6   ? 4.750   12.439  0.769   1.00 11.00 ? 6   TYR A CG  1 
ATOM   37   C  CD1 . TYR A 1 6   ? 4.826   13.745  0.293   1.00 10.37 ? 6   TYR A CD1 1 
ATOM   38   C  CD2 . TYR A 1 6   ? 3.675   11.649  0.342   1.00 10.38 ? 6   TYR A CD2 1 
ATOM   39   C  CE1 . TYR A 1 6   ? 3.867   14.271  -0.574  1.00 10.12 ? 6   TYR A CE1 1 
ATOM   40   C  CE2 . TYR A 1 6   ? 2.719   12.140  -0.527  1.00 9.25  ? 6   TYR A CE2 1 
ATOM   41   C  CZ  . TYR A 1 6   ? 2.795   13.461  -0.939  1.00 10.05 ? 6   TYR A CZ  1 
ATOM   42   O  OH  . TYR A 1 6   ? 1.849   13.942  -1.793  1.00 9.28  ? 6   TYR A OH  1 
ATOM   43   N  N   . PHE A 1 7   ? 7.273   11.710  4.970   1.00 14.53 ? 7   PHE A N   1 
ATOM   44   C  CA  . PHE A 1 7   ? 8.351   10.948  5.609   1.00 17.23 ? 7   PHE A CA  1 
ATOM   45   C  C   . PHE A 1 7   ? 8.500   11.408  7.034   1.00 17.11 ? 7   PHE A C   1 
ATOM   46   O  O   . PHE A 1 7   ? 8.707   12.608  7.264   1.00 17.90 ? 7   PHE A O   1 
ATOM   47   C  CB  . PHE A 1 7   ? 9.701   11.187  4.856   1.00 19.70 ? 7   PHE A CB  1 
ATOM   48   C  CG  . PHE A 1 7   ? 10.927  10.461  5.456   1.00 25.95 ? 7   PHE A CG  1 
ATOM   49   C  CD1 . PHE A 1 7   ? 11.013  9.052   5.467   1.00 28.33 ? 7   PHE A CD1 1 
ATOM   50   C  CD2 . PHE A 1 7   ? 12.011  11.192  5.981   1.00 27.70 ? 7   PHE A CD2 1 
ATOM   51   C  CE1 . PHE A 1 7   ? 12.147  8.401   5.996   1.00 28.58 ? 7   PHE A CE1 1 
ATOM   52   C  CE2 . PHE A 1 7   ? 13.147  10.542  6.497   1.00 31.67 ? 7   PHE A CE2 1 
ATOM   53   C  CZ  . PHE A 1 7   ? 13.207  9.148   6.515   1.00 28.75 ? 7   PHE A CZ  1 
ATOM   54   N  N   . GLY A 1 8   ? 8.507   10.474  7.985   1.00 17.65 ? 8   GLY A N   1 
ATOM   55   C  CA  . GLY A 1 8   ? 8.738   10.839  9.424   1.00 16.75 ? 8   GLY A CA  1 
ATOM   56   C  C   . GLY A 1 8   ? 7.453   11.163  10.195  1.00 16.36 ? 8   GLY A C   1 
ATOM   57   O  O   . GLY A 1 8   ? 6.399   10.772  9.771   1.00 18.36 ? 8   GLY A O   1 
ATOM   58   N  N   . PRO A 1 9   ? 7.535   11.866  11.360  1.00 16.36 ? 9   PRO A N   1 
ATOM   59   C  CA  . PRO A 1 9   ? 6.385   12.055  12.264  1.00 17.31 ? 9   PRO A CA  1 
ATOM   60   C  C   . PRO A 1 9   ? 5.199   12.678  11.581  1.00 16.67 ? 9   PRO A C   1 
ATOM   61   O  O   . PRO A 1 9   ? 4.076   12.432  11.971  1.00 18.42 ? 9   PRO A O   1 
ATOM   62   C  CB  . PRO A 1 9   ? 6.916   13.010  13.390  1.00 17.39 ? 9   PRO A CB  1 
ATOM   63   C  CG  . PRO A 1 9   ? 8.352   13.214  13.124  1.00 17.90 ? 9   PRO A CG  1 
ATOM   64   C  CD  . PRO A 1 9   ? 8.775   12.542  11.846  1.00 17.39 ? 9   PRO A CD  1 
ATOM   65   N  N   . ASP A 1 10  ? 5.429   13.452  10.521  1.00 16.97 ? 10  ASP A N   1 
ATOM   66   C  CA  . ASP A 1 10  ? 4.301   14.118  9.836   1.00 15.74 ? 10  ASP A CA  1 
ATOM   67   C  C   . ASP A 1 10  ? 3.822   13.470  8.542   1.00 13.65 ? 10  ASP A C   1 
ATOM   68   O  O   . ASP A 1 10  ? 3.032   14.083  7.828   1.00 12.89 ? 10  ASP A O   1 
ATOM   69   C  CB  . ASP A 1 10  ? 4.596   15.610  9.615   1.00 17.34 ? 10  ASP A CB  1 
ATOM   70   C  CG  . ASP A 1 10  ? 4.765   16.372  10.925  1.00 22.55 ? 10  ASP A CG  1 
ATOM   71   O  OD1 . ASP A 1 10  ? 3.968   16.139  11.857  1.00 22.20 ? 10  ASP A OD1 1 
ATOM   72   O  OD2 . ASP A 1 10  ? 5.720   17.180  11.022  1.00 26.76 ? 10  ASP A OD2 1 
ATOM   73   N  N   . GLY A 1 11  ? 4.347   12.279  8.234   1.00 13.41 ? 11  GLY A N   1 
ATOM   74   C  CA  . GLY A 1 11  ? 3.987   11.510  7.010   1.00 12.64 ? 11  GLY A CA  1 
ATOM   75   C  C   . GLY A 1 11  ? 2.601   10.883  7.080   1.00 11.36 ? 11  GLY A C   1 
ATOM   76   O  O   . GLY A 1 11  ? 1.826   11.064  8.061   1.00 12.07 ? 11  GLY A O   1 
ATOM   77   N  N   . GLU A 1 12  ? 2.325   10.047  6.091   1.00 10.54 ? 12  GLU A N   1 
ATOM   78   C  CA  . GLU A 1 12  ? 0.957   9.710   5.789   1.00 10.59 ? 12  GLU A CA  1 
ATOM   79   C  C   . GLU A 1 12  ? 0.168   8.970   6.875   1.00 10.67 ? 12  GLU A C   1 
ATOM   80   O  O   . GLU A 1 12  ? -1.050  9.140   6.941   1.00 12.55 ? 12  GLU A O   1 
ATOM   81   C  CB  . GLU A 1 12  ? 0.877   9.003   4.416   1.00 8.97  ? 12  GLU A CB  1 
ATOM   82   C  CG  . GLU A 1 12  ? 1.364   7.565   4.503   1.00 8.67  ? 12  GLU A CG  1 
ATOM   83   C  CD  . GLU A 1 12  ? 1.645   7.076   3.109   1.00 9.06  ? 12  GLU A CD  1 
ATOM   84   O  OE1 . GLU A 1 12  ? 0.711   6.633   2.389   1.00 8.63  ? 12  GLU A OE1 1 
ATOM   85   O  OE2 . GLU A 1 12  ? 2.781   7.171   2.732   1.00 9.13  ? 12  GLU A OE2 1 
ATOM   86   N  N   . ASN A 1 13  ? 0.818   8.207   7.756   1.00 10.51 ? 13  ASN A N   1 
ATOM   87   C  CA  . ASN A 1 13  ? 0.049   7.544   8.839   1.00 9.37  ? 13  ASN A CA  1 
ATOM   88   C  C   . ASN A 1 13  ? -0.506  8.479   9.917   1.00 8.18  ? 13  ASN A C   1 
ATOM   89   O  O   . ASN A 1 13  ? -1.405  8.106   10.671  1.00 7.52  ? 13  ASN A O   1 
ATOM   90   C  CB  . ASN A 1 13  ? 0.805   6.367   9.480   1.00 9.06  ? 13  ASN A CB  1 
ATOM   91   C  CG  . ASN A 1 13  ? 1.007   5.206   8.515   1.00 8.95  ? 13  ASN A CG  1 
ATOM   92   O  OD1 . ASN A 1 13  ? 0.487   5.190   7.348   1.00 8.02  ? 13  ASN A OD1 1 
ATOM   93   N  ND2 . ASN A 1 13  ? 1.689   4.203   8.993   1.00 8.50  ? 13  ASN A ND2 1 
ATOM   94   N  N   . SER A 1 14  ? 0.038   9.685   9.959   1.00 8.61  ? 14  SER A N   1 
ATOM   95   C  CA  . SER A 1 14  ? -0.323  10.753  10.902  1.00 9.22  ? 14  SER A CA  1 
ATOM   96   C  C   . SER A 1 14  ? -1.099  11.912  10.257  1.00 10.24 ? 14  SER A C   1 
ATOM   97   O  O   . SER A 1 14  ? -1.595  12.806  10.971  1.00 9.78  ? 14  SER A O   1 
ATOM   98   C  CB  . SER A 1 14  ? 0.992   11.327  11.522  1.00 10.00 ? 14  SER A CB  1 
ATOM   99   O  OG  . SER A 1 14  ? 1.621   10.317  12.334  1.00 11.85 ? 14  SER A OG  1 
ATOM   100  N  N   . TRP A 1 15  ? -1.382  11.861  8.942   1.00 9.47  ? 15  TRP A N   1 
ATOM   101  C  CA  . TRP A 1 15  ? -2.250  12.905  8.315   1.00 10.87 ? 15  TRP A CA  1 
ATOM   102  C  C   . TRP A 1 15  ? -3.614  13.079  9.020   1.00 11.91 ? 15  TRP A C   1 
ATOM   103  O  O   . TRP A 1 15  ? -4.084  14.219  9.233   1.00 12.35 ? 15  TRP A O   1 
ATOM   104  C  CB  . TRP A 1 15  ? -2.474  12.633  6.814   1.00 10.36 ? 15  TRP A CB  1 
ATOM   105  C  CG  . TRP A 1 15  ? -1.219  12.764  5.941   1.00 9.50  ? 15  TRP A CG  1 
ATOM   106  C  CD1 . TRP A 1 15  ? 0.063   13.214  6.298   1.00 9.49  ? 15  TRP A CD1 1 
ATOM   107  C  CD2 . TRP A 1 15  ? -1.159  12.486  4.508   1.00 9.53  ? 15  TRP A CD2 1 
ATOM   108  N  NE1 . TRP A 1 15  ? 0.916   13.222  5.174   1.00 9.42  ? 15  TRP A NE1 1 
ATOM   109  C  CE2 . TRP A 1 15  ? 0.217   12.804  4.063   1.00 9.56  ? 15  TRP A CE2 1 
ATOM   110  C  CE3 . TRP A 1 15  ? -2.093  11.994  3.567   1.00 8.21  ? 15  TRP A CE3 1 
ATOM   111  C  CZ2 . TRP A 1 15  ? 0.624   12.634  2.743   1.00 9.91  ? 15  TRP A CZ2 1 
ATOM   112  C  CZ3 . TRP A 1 15  ? -1.659  11.857  2.212   1.00 9.96  ? 15  TRP A CZ3 1 
ATOM   113  C  CH2 . TRP A 1 15  ? -0.330  12.139  1.820   1.00 9.47  ? 15  TRP A CH2 1 
ATOM   114  N  N   . SER A 1 16  ? -4.215  11.957  9.409   1.00 11.96 ? 16  SER A N   1 
ATOM   115  C  CA  . SER A 1 16  ? -5.525  11.929  10.062  1.00 13.59 ? 16  SER A CA  1 
ATOM   116  C  C   . SER A 1 16  ? -5.620  12.764  11.314  1.00 14.12 ? 16  SER A C   1 
ATOM   117  O  O   . SER A 1 16  ? -6.727  13.185  11.656  1.00 12.89 ? 16  SER A O   1 
ATOM   118  C  CB  . SER A 1 16  ? -5.982  10.481  10.365  1.00 13.99 ? 16  SER A CB  1 
ATOM   119  O  OG  . SER A 1 16  ? -5.120  9.844   11.296  1.00 15.48 ? 16  SER A OG  1 
ATOM   120  N  N   . LYS A 1 17  ? -4.486  12.948  12.026  1.00 14.21 ? 17  LYS A N   1 
ATOM   121  C  CA  . LYS A 1 17  ? -4.459  13.791  13.206  1.00 16.09 ? 17  LYS A CA  1 
ATOM   122  C  C   . LYS A 1 17  ? -4.773  15.272  12.922  1.00 16.03 ? 17  LYS A C   1 
ATOM   123  O  O   . LYS A 1 17  ? -5.532  15.918  13.666  1.00 17.52 ? 17  LYS A O   1 
ATOM   124  C  CB  . LYS A 1 17  ? -3.125  13.673  13.990  1.00 17.78 ? 17  LYS A CB  1 
ATOM   125  C  CG  . LYS A 1 17  ? -2.866  12.333  14.643  1.00 19.93 ? 17  LYS A CG  1 
ATOM   126  C  CD  . LYS A 1 17  ? -1.369  12.069  14.484  1.00 22.21 ? 17  LYS A CD  1 
ATOM   127  C  CE  . LYS A 1 17  ? -0.784  11.208  15.551  1.00 21.95 ? 17  LYS A CE  1 
ATOM   128  N  NZ  . LYS A 1 17  ? 0.697   11.157  15.322  1.00 24.90 ? 17  LYS A NZ  1 
ATOM   129  N  N   . LYS A 1 18  ? -4.209  15.843  11.893  1.00 15.20 ? 18  LYS A N   1 
ATOM   130  C  CA  . LYS A 1 18  ? -4.536  17.254  11.582  1.00 16.02 ? 18  LYS A CA  1 
ATOM   131  C  C   . LYS A 1 18  ? -5.601  17.401  10.527  1.00 14.87 ? 18  LYS A C   1 
ATOM   132  O  O   . LYS A 1 18  ? -6.185  18.467  10.386  1.00 15.32 ? 18  LYS A O   1 
ATOM   133  C  CB  . LYS A 1 18  ? -3.321  18.137  11.235  1.00 20.06 ? 18  LYS A CB  1 
ATOM   134  C  CG  . LYS A 1 18  ? -2.348  18.485  12.370  1.00 24.03 ? 18  LYS A CG  1 
ATOM   135  C  CD  . LYS A 1 18  ? -2.897  19.556  13.327  1.00 27.56 ? 18  LYS A CD  1 
ATOM   136  C  CE  . LYS A 1 18  ? -1.854  20.015  14.347  1.00 29.83 ? 18  LYS A CE  1 
ATOM   137  N  NZ  . LYS A 1 18  ? -2.060  21.469  14.665  1.00 32.46 ? 18  LYS A NZ  1 
ATOM   138  N  N   . TYR A 1 19  ? -5.908  16.329  9.804   1.00 12.22 ? 19  TYR A N   1 
ATOM   139  C  CA  . TYR A 1 19  ? -6.774  16.448  8.615   1.00 12.28 ? 19  TYR A CA  1 
ATOM   140  C  C   . TYR A 1 19  ? -7.700  15.247  8.678   1.00 12.31 ? 19  TYR A C   1 
ATOM   141  O  O   . TYR A 1 19  ? -7.351  14.174  8.189   1.00 13.31 ? 19  TYR A O   1 
ATOM   142  C  CB  . TYR A 1 19  ? -5.955  16.433  7.309   1.00 13.03 ? 19  TYR A CB  1 
ATOM   143  C  CG  . TYR A 1 19  ? -4.943  17.557  7.162   1.00 12.95 ? 19  TYR A CG  1 
ATOM   144  C  CD1 . TYR A 1 19  ? -3.631  17.401  7.588   1.00 15.48 ? 19  TYR A CD1 1 
ATOM   145  C  CD2 . TYR A 1 19  ? -5.326  18.777  6.668   1.00 14.67 ? 19  TYR A CD2 1 
ATOM   146  C  CE1 . TYR A 1 19  ? -2.704  18.464  7.477   1.00 16.18 ? 19  TYR A CE1 1 
ATOM   147  C  CE2 . TYR A 1 19  ? -4.430  19.844  6.569   1.00 15.61 ? 19  TYR A CE2 1 
ATOM   148  C  CZ  . TYR A 1 19  ? -3.130  19.681  6.956   1.00 15.47 ? 19  TYR A CZ  1 
ATOM   149  O  OH  . TYR A 1 19  ? -2.265  20.775  6.811   1.00 17.99 ? 19  TYR A OH  1 
ATOM   150  N  N   . PRO A 1 20  ? -8.851  15.408  9.319   1.00 12.39 ? 20  PRO A N   1 
ATOM   151  C  CA  . PRO A 1 20  ? -9.592  14.233  9.706   1.00 12.31 ? 20  PRO A CA  1 
ATOM   152  C  C   . PRO A 1 20  ? -10.174 13.463  8.516   1.00 11.63 ? 20  PRO A C   1 
ATOM   153  O  O   . PRO A 1 20  ? -10.389 12.250  8.646   1.00 11.09 ? 20  PRO A O   1 
ATOM   154  C  CB  . PRO A 1 20  ? -10.688 14.773  10.634  1.00 14.34 ? 20  PRO A CB  1 
ATOM   155  C  CG  . PRO A 1 20  ? -10.335 16.182  10.980  1.00 14.53 ? 20  PRO A CG  1 
ATOM   156  C  CD  . PRO A 1 20  ? -9.289  16.647  10.010  1.00 14.19 ? 20  PRO A CD  1 
ATOM   157  N  N   . SER A 1 21  ? -10.368 14.119  7.360   1.00 11.37 ? 21  SER A N   1 
ATOM   158  C  CA  . SER A 1 21  ? -10.864 13.357  6.176   1.00 10.59 ? 21  SER A CA  1 
ATOM   159  C  C   . SER A 1 21  ? -9.826  12.311  5.677   1.00 11.49 ? 21  SER A C   1 
ATOM   160  O  O   . SER A 1 21  ? -10.186 11.366  4.962   1.00 11.43 ? 21  SER A O   1 
ATOM   161  C  CB  . SER A 1 21  ? -11.326 14.284  5.043   1.00 11.12 ? 21  SER A CB  1 
ATOM   162  O  OG  . SER A 1 21  ? -12.400 15.152  5.460   1.00 10.89 ? 21  SER A OG  1 
ATOM   163  N  N   . CYS A 1 22  ? -8.549  12.457  6.059   1.00 11.17 ? 22  CYS A N   1 
ATOM   164  C  CA  . CYS A 1 22  ? -7.535  11.487  5.623   1.00 10.35 ? 22  CYS A CA  1 
ATOM   165  C  C   . CYS A 1 22  ? -7.773  10.106  6.235   1.00 11.55 ? 22  CYS A C   1 
ATOM   166  O  O   . CYS A 1 22  ? -7.217  9.090   5.749   1.00 10.95 ? 22  CYS A O   1 
ATOM   167  C  CB  . CYS A 1 22  ? -6.106  12.016  5.894   1.00 10.72 ? 22  CYS A CB  1 
ATOM   168  S  SG  . CYS A 1 22  ? -5.720  13.537  4.978   1.00 12.14 ? 22  CYS A SG  1 
ATOM   169  N  N   . GLY A 1 23  ? -8.550  10.089  7.347   1.00 11.45 ? 23  GLY A N   1 
ATOM   170  C  CA  . GLY A 1 23  ? -8.949  8.832   8.041   1.00 11.83 ? 23  GLY A CA  1 
ATOM   171  C  C   . GLY A 1 23  ? -10.368 8.394   7.662   1.00 12.54 ? 23  GLY A C   1 
ATOM   172  O  O   . GLY A 1 23  ? -10.925 7.416   8.223   1.00 12.99 ? 23  GLY A O   1 
ATOM   173  N  N   . GLY A 1 24  ? -10.976 9.079   6.721   1.00 12.78 ? 24  GLY A N   1 
ATOM   174  C  CA  . GLY A 1 24  ? -12.411 8.833   6.472   1.00 13.18 ? 24  GLY A CA  1 
ATOM   175  C  C   . GLY A 1 24  ? -12.652 7.993   5.253   1.00 13.12 ? 24  GLY A C   1 
ATOM   176  O  O   . GLY A 1 24  ? -11.815 7.262   4.825   1.00 14.39 ? 24  GLY A O   1 
ATOM   177  N  N   . LEU A 1 25  ? -13.849 8.052   4.716   1.00 15.38 ? 25  LEU A N   1 
ATOM   178  C  CA  . LEU A 1 25  ? -14.209 7.174   3.638   1.00 16.37 ? 25  LEU A CA  1 
ATOM   179  C  C   . LEU A 1 25  ? -13.717 7.666   2.274   1.00 16.84 ? 25  LEU A C   1 
ATOM   180  O  O   . LEU A 1 25  ? -13.174 8.803   2.124   1.00 14.68 ? 25  LEU A O   1 
ATOM   181  C  CB  . LEU A 1 25  ? -15.740 7.058   3.585   1.00 17.72 ? 25  LEU A CB  1 
ATOM   182  C  CG  . LEU A 1 25  ? -16.503 6.554   4.809   1.00 20.28 ? 25  LEU A CG  1 
ATOM   183  C  CD1 . LEU A 1 25  ? -17.997 6.725   4.465   1.00 22.68 ? 25  LEU A CD1 1 
ATOM   184  C  CD2 . LEU A 1 25  ? -16.121 5.108   5.144   1.00 20.96 ? 25  LEU A CD2 1 
ATOM   185  N  N   . LEU A 1 26  ? -13.896 6.792   1.286   1.00 15.56 ? 26  LEU A N   1 
ATOM   186  C  CA  . LEU A 1 26  ? -13.606 7.099   -0.169  1.00 15.67 ? 26  LEU A CA  1 
ATOM   187  C  C   . LEU A 1 26  ? -12.145 7.566   -0.503  1.00 13.68 ? 26  LEU A C   1 
ATOM   188  O  O   . LEU A 1 26  ? -11.940 8.432   -1.367  1.00 11.11 ? 26  LEU A O   1 
ATOM   189  C  CB  . LEU A 1 26  ? -14.591 8.132   -0.701  1.00 16.12 ? 26  LEU A CB  1 
ATOM   190  C  CG  . LEU A 1 26  ? -16.091 7.803   -0.796  1.00 17.93 ? 26  LEU A CG  1 
ATOM   191  C  CD1 . LEU A 1 26  ? -16.865 8.962   -1.416  1.00 17.70 ? 26  LEU A CD1 1 
ATOM   192  C  CD2 . LEU A 1 26  ? -16.306 6.483   -1.470  1.00 16.67 ? 26  LEU A CD2 1 
ATOM   193  N  N   . GLN A 1 27  ? -11.132 7.012   0.177   1.00 12.55 ? 27  GLN A N   1 
ATOM   194  C  CA  . GLN A 1 27  ? -9.801  7.595   0.021   1.00 10.93 ? 27  GLN A CA  1 
ATOM   195  C  C   . GLN A 1 27  ? -9.113  7.056   -1.196  1.00 10.48 ? 27  GLN A C   1 
ATOM   196  O  O   . GLN A 1 27  ? -9.316  5.890   -1.563  1.00 10.76 ? 27  GLN A O   1 
ATOM   197  C  CB  . GLN A 1 27  ? -8.932  7.334   1.239   1.00 10.88 ? 27  GLN A CB  1 
ATOM   198  C  CG  . GLN A 1 27  ? -9.482  8.036   2.425   1.00 10.58 ? 27  GLN A CG  1 
ATOM   199  C  CD  . GLN A 1 27  ? -9.351  9.548   2.321   1.00 10.42 ? 27  GLN A CD  1 
ATOM   200  O  OE1 . GLN A 1 27  ? -10.344 10.269  2.108   1.00 10.95 ? 27  GLN A OE1 1 
ATOM   201  N  NE2 . GLN A 1 27  ? -8.156  10.033  2.524   1.00 8.87  ? 27  GLN A NE2 1 
ATOM   202  N  N   . SER A 1 28  ? -8.307  7.903   -1.812  1.00 9.67  ? 28  SER A N   1 
ATOM   203  C  CA  . SER A 1 28  ? -7.410  7.518   -2.951  1.00 8.86  ? 28  SER A CA  1 
ATOM   204  C  C   . SER A 1 28  ? -5.918  7.724   -2.555  1.00 8.85  ? 28  SER A C   1 
ATOM   205  O  O   . SER A 1 28  ? -5.654  8.472   -1.598  1.00 9.46  ? 28  SER A O   1 
ATOM   206  C  CB  . SER A 1 28  ? -7.735  8.410   -4.158  1.00 9.91  ? 28  SER A CB  1 
ATOM   207  O  OG  . SER A 1 28  ? -9.090  8.336   -4.613  1.00 10.81 ? 28  SER A OG  1 
ATOM   208  N  N   . PRO A 1 29  ? -4.944  7.116   -3.320  1.00 8.64  ? 29  PRO A N   1 
ATOM   209  C  CA  . PRO A 1 29  ? -5.096  6.282   -4.533  1.00 8.56  ? 29  PRO A CA  1 
ATOM   210  C  C   . PRO A 1 29  ? -5.388  4.829   -4.198  1.00 9.27  ? 29  PRO A C   1 
ATOM   211  O  O   . PRO A 1 29  ? -5.520  4.503   -3.020  1.00 9.31  ? 29  PRO A O   1 
ATOM   212  C  CB  . PRO A 1 29  ? -3.681  6.335   -5.178  1.00 8.11  ? 29  PRO A CB  1 
ATOM   213  C  CG  . PRO A 1 29  ? -2.757  6.381   -3.955  1.00 7.62  ? 29  PRO A CG  1 
ATOM   214  C  CD  . PRO A 1 29  ? -3.529  7.164   -2.903  1.00 8.10  ? 29  PRO A CD  1 
ATOM   215  N  N   . ILE A 1 30  ? -5.592  4.001   -5.234  1.00 9.24  ? 30  ILE A N   1 
ATOM   216  C  CA  . ILE A 1 30  ? -5.961  2.577   -5.065  1.00 9.46  ? 30  ILE A CA  1 
ATOM   217  C  C   . ILE A 1 30  ? -5.172  1.715   -6.060  1.00 9.37  ? 30  ILE A C   1 
ATOM   218  O  O   . ILE A 1 30  ? -4.644  2.219   -7.098  1.00 9.12  ? 30  ILE A O   1 
ATOM   219  C  CB  . ILE A 1 30  ? -7.513  2.297   -5.256  1.00 9.09  ? 30  ILE A CB  1 
ATOM   220  C  CG1 . ILE A 1 30  ? -8.047  2.823   -6.594  1.00 9.22  ? 30  ILE A CG1 1 
ATOM   221  C  CG2 . ILE A 1 30  ? -8.359  2.803   -4.144  1.00 9.83  ? 30  ILE A CG2 1 
ATOM   222  C  CD1 . ILE A 1 30  ? -9.548  2.560   -6.846  1.00 10.19 ? 30  ILE A CD1 1 
ATOM   223  N  N   . ASP A 1 31  ? -5.212  0.389   -5.806  1.00 10.29 ? 31  ASP A N   1 
ATOM   224  C  CA  . ASP A 1 31  ? -4.653  -0.537  -6.751  1.00 10.64 ? 31  ASP A CA  1 
ATOM   225  C  C   . ASP A 1 31  ? -5.766  -1.022  -7.688  1.00 11.02 ? 31  ASP A C   1 
ATOM   226  O  O   . ASP A 1 31  ? -6.828  -1.472  -7.215  1.00 11.28 ? 31  ASP A O   1 
ATOM   227  C  CB  . ASP A 1 31  ? -4.014  -1.735  -6.023  1.00 11.61 ? 31  ASP A CB  1 
ATOM   228  C  CG  . ASP A 1 31  ? -3.519  -2.775  -7.017  1.00 11.81 ? 31  ASP A CG  1 
ATOM   229  O  OD1 . ASP A 1 31  ? -2.732  -2.413  -7.894  1.00 12.39 ? 31  ASP A OD1 1 
ATOM   230  O  OD2 . ASP A 1 31  ? -3.959  -3.925  -6.956  1.00 14.07 ? 31  ASP A OD2 1 
ATOM   231  N  N   . LEU A 1 32  ? -5.525  -0.883  -9.001  1.00 10.26 ? 32  LEU A N   1 
ATOM   232  C  CA  . LEU A 1 32  ? -6.556  -1.129  -10.016 1.00 11.01 ? 32  LEU A CA  1 
ATOM   233  C  C   . LEU A 1 32  ? -6.313  -2.576  -10.474 1.00 11.27 ? 32  LEU A C   1 
ATOM   234  O  O   . LEU A 1 32  ? -5.302  -2.873  -11.167 1.00 11.25 ? 32  LEU A O   1 
ATOM   235  C  CB  . LEU A 1 32  ? -6.433  -0.112  -11.185 1.00 10.72 ? 32  LEU A CB  1 
ATOM   236  C  CG  . LEU A 1 32  ? -6.558  1.375   -10.812 1.00 11.42 ? 32  LEU A CG  1 
ATOM   237  C  CD1 . LEU A 1 32  ? -5.908  2.281   -11.875 1.00 11.50 ? 32  LEU A CD1 1 
ATOM   238  C  CD2 . LEU A 1 32  ? -8.015  1.816   -10.516 1.00 12.01 ? 32  LEU A CD2 1 
ATOM   239  N  N   . HIS A 1 33  ? -7.183  -3.497  -10.059 1.00 13.68 ? 33  HIS A N   1 
ATOM   240  C  CA  . HIS A 1 33  ? -6.909  -4.931  -10.263 1.00 14.90 ? 33  HIS A CA  1 
ATOM   241  C  C   . HIS A 1 33  ? -8.216  -5.644  -10.533 1.00 15.66 ? 33  HIS A C   1 
ATOM   242  O  O   . HIS A 1 33  ? -9.285  -5.183  -10.139 1.00 13.99 ? 33  HIS A O   1 
ATOM   243  C  CB  . HIS A 1 33  ? -6.145  -5.537  -9.079  1.00 16.34 ? 33  HIS A CB  1 
ATOM   244  C  CG  . HIS A 1 33  ? -6.907  -5.558  -7.765  1.00 18.11 ? 33  HIS A CG  1 
ATOM   245  N  ND1 . HIS A 1 33  ? -7.008  -4.469  -6.945  1.00 18.31 ? 33  HIS A ND1 1 
ATOM   246  C  CD2 . HIS A 1 33  ? -7.599  -6.596  -7.124  1.00 19.03 ? 33  HIS A CD2 1 
ATOM   247  C  CE1 . HIS A 1 33  ? -7.724  -4.799  -5.844  1.00 19.84 ? 33  HIS A CE1 1 
ATOM   248  N  NE2 . HIS A 1 33  ? -8.100  -6.098  -5.968  1.00 19.19 ? 33  HIS A NE2 1 
ATOM   249  N  N   . SER A 1 34  ? -8.144  -6.780  -11.204 1.00 17.21 ? 34  SER A N   1 
ATOM   250  C  CA  . SER A 1 34  ? -9.338  -7.372  -11.842 1.00 18.56 ? 34  SER A CA  1 
ATOM   251  C  C   . SER A 1 34  ? -10.569 -7.585  -10.934 1.00 18.40 ? 34  SER A C   1 
ATOM   252  O  O   . SER A 1 34  ? -11.725 -7.385  -11.375 1.00 18.22 ? 34  SER A O   1 
ATOM   253  C  CB  . SER A 1 34  ? -8.931  -8.679  -12.517 1.00 20.16 ? 34  SER A CB  1 
ATOM   254  O  OG  . SER A 1 34  ? -8.523  -9.575  -11.519 1.00 24.87 ? 34  SER A OG  1 
ATOM   255  N  N   . ASP A 1 35  ? -10.332 -7.984  -9.671  1.00 16.87 ? 35  ASP A N   1 
ATOM   256  C  CA  . ASP A 1 35  ? -11.412 -8.305  -8.741  1.00 17.94 ? 35  ASP A CA  1 
ATOM   257  C  C   . ASP A 1 35  ? -12.333 -7.126  -8.514  1.00 17.35 ? 35  ASP A C   1 
ATOM   258  O  O   . ASP A 1 35  ? -13.496 -7.327  -8.172  1.00 18.53 ? 35  ASP A O   1 
ATOM   259  C  CB  . ASP A 1 35  ? -10.908 -8.815  -7.360  1.00 20.86 ? 35  ASP A CB  1 
ATOM   260  C  CG  . ASP A 1 35  ? -9.858  -9.889  -7.473  1.00 24.24 ? 35  ASP A CG  1 
ATOM   261  O  OD1 . ASP A 1 35  ? -8.731  -9.537  -7.936  1.00 24.82 ? 35  ASP A OD1 1 
ATOM   262  O  OD2 . ASP A 1 35  ? -10.178 -11.067 -7.111  1.00 22.97 ? 35  ASP A OD2 1 
ATOM   263  N  N   . ILE A 1 36  ? -11.823 -5.902  -8.656  1.00 15.96 ? 36  ILE A N   1 
ATOM   264  C  CA  . ILE A 1 36  ? -12.641 -4.726  -8.406  1.00 16.60 ? 36  ILE A CA  1 
ATOM   265  C  C   . ILE A 1 36  ? -12.976 -3.855  -9.652  1.00 17.21 ? 36  ILE A C   1 
ATOM   266  O  O   . ILE A 1 36  ? -13.609 -2.782  -9.511  1.00 20.42 ? 36  ILE A O   1 
ATOM   267  C  CB  . ILE A 1 36  ? -12.179 -3.897  -7.182  1.00 16.64 ? 36  ILE A CB  1 
ATOM   268  C  CG1 . ILE A 1 36  ? -10.747 -3.358  -7.265  1.00 17.80 ? 36  ILE A CG1 1 
ATOM   269  C  CG2 . ILE A 1 36  ? -12.230 -4.779  -5.909  1.00 18.51 ? 36  ILE A CG2 1 
ATOM   270  C  CD1 . ILE A 1 36  ? -10.323 -2.487  -8.393  1.00 16.18 ? 36  ILE A CD1 1 
ATOM   271  N  N   . LEU A 1 37  ? -12.684 -4.377  -10.851 1.00 16.74 ? 37  LEU A N   1 
ATOM   272  C  CA  . LEU A 1 37  ? -12.981 -3.694  -12.140 1.00 16.09 ? 37  LEU A CA  1 
ATOM   273  C  C   . LEU A 1 37  ? -14.237 -4.236  -12.798 1.00 16.92 ? 37  LEU A C   1 
ATOM   274  O  O   . LEU A 1 37  ? -14.418 -5.461  -12.832 1.00 17.55 ? 37  LEU A O   1 
ATOM   275  C  CB  . LEU A 1 37  ? -11.843 -3.909  -13.144 1.00 15.11 ? 37  LEU A CB  1 
ATOM   276  C  CG  . LEU A 1 37  ? -10.475 -3.435  -12.637 1.00 14.49 ? 37  LEU A CG  1 
ATOM   277  C  CD1 . LEU A 1 37  ? -9.311  -3.863  -13.492 1.00 15.82 ? 37  LEU A CD1 1 
ATOM   278  C  CD2 . LEU A 1 37  ? -10.524 -1.937  -12.526 1.00 12.69 ? 37  LEU A CD2 1 
ATOM   279  N  N   . GLN A 1 38  ? -15.063 -3.341  -13.352 1.00 15.31 ? 38  GLN A N   1 
ATOM   280  C  CA  . GLN A 1 38  ? -16.219 -3.756  -14.194 1.00 15.84 ? 38  GLN A CA  1 
ATOM   281  C  C   . GLN A 1 38  ? -16.410 -2.824  -15.369 1.00 16.59 ? 38  GLN A C   1 
ATOM   282  O  O   . GLN A 1 38  ? -16.437 -1.578  -15.210 1.00 16.69 ? 38  GLN A O   1 
ATOM   283  C  CB  . GLN A 1 38  ? -17.494 -3.773  -13.370 1.00 16.96 ? 38  GLN A CB  1 
ATOM   284  C  CG  . GLN A 1 38  ? -18.745 -4.287  -14.118 1.00 20.91 ? 38  GLN A CG  1 
ATOM   285  C  CD  . GLN A 1 38  ? -19.940 -4.514  -13.213 1.00 22.23 ? 38  GLN A CD  1 
ATOM   286  O  OE1 . GLN A 1 38  ? -20.135 -5.624  -12.692 1.00 25.37 ? 38  GLN A OE1 1 
ATOM   287  N  NE2 . GLN A 1 38  ? -20.773 -3.472  -13.040 1.00 22.60 ? 38  GLN A NE2 1 
ATOM   288  N  N   . TYR A 1 39  ? -16.587 -3.418  -16.554 1.00 15.51 ? 39  TYR A N   1 
ATOM   289  C  CA  . TYR A 1 39  ? -16.814 -2.625  -17.773 1.00 13.71 ? 39  TYR A CA  1 
ATOM   290  C  C   . TYR A 1 39  ? -18.139 -1.894  -17.721 1.00 13.45 ? 39  TYR A C   1 
ATOM   291  O  O   . TYR A 1 39  ? -19.209 -2.486  -17.389 1.00 12.84 ? 39  TYR A O   1 
ATOM   292  C  CB  . TYR A 1 39  ? -16.715 -3.533  -19.003 1.00 12.95 ? 39  TYR A CB  1 
ATOM   293  C  CG  . TYR A 1 39  ? -17.111 -2.908  -20.343 1.00 12.20 ? 39  TYR A CG  1 
ATOM   294  C  CD1 . TYR A 1 39  ? -16.448 -1.797  -20.874 1.00 11.83 ? 39  TYR A CD1 1 
ATOM   295  C  CD2 . TYR A 1 39  ? -18.114 -3.489  -21.120 1.00 11.64 ? 39  TYR A CD2 1 
ATOM   296  C  CE1 . TYR A 1 39  ? -16.821 -1.233  -22.116 1.00 11.94 ? 39  TYR A CE1 1 
ATOM   297  C  CE2 . TYR A 1 39  ? -18.499 -2.923  -22.339 1.00 11.71 ? 39  TYR A CE2 1 
ATOM   298  C  CZ  . TYR A 1 39  ? -17.870 -1.815  -22.858 1.00 11.90 ? 39  TYR A CZ  1 
ATOM   299  O  OH  . TYR A 1 39  ? -18.291 -1.339  -24.145 1.00 12.17 ? 39  TYR A OH  1 
ATOM   300  N  N   . ASP A 1 40  ? -18.074 -0.600  -18.062 1.00 13.67 ? 40  ASP A N   1 
ATOM   301  C  CA  . ASP A 1 40  ? -19.300 0.234   -18.161 1.00 14.10 ? 40  ASP A CA  1 
ATOM   302  C  C   . ASP A 1 40  ? -19.383 0.868   -19.529 1.00 13.70 ? 40  ASP A C   1 
ATOM   303  O  O   . ASP A 1 40  ? -18.693 1.827   -19.778 1.00 12.72 ? 40  ASP A O   1 
ATOM   304  C  CB  . ASP A 1 40  ? -19.336 1.297   -17.072 1.00 15.50 ? 40  ASP A CB  1 
ATOM   305  C  CG  . ASP A 1 40  ? -20.590 2.177   -17.121 1.00 18.55 ? 40  ASP A CG  1 
ATOM   306  O  OD1 . ASP A 1 40  ? -20.658 3.078   -16.255 1.00 19.04 ? 40  ASP A OD1 1 
ATOM   307  O  OD2 . ASP A 1 40  ? -21.508 1.977   -17.990 1.00 15.40 ? 40  ASP A OD2 1 
ATOM   308  N  N   . ALA A 1 41  ? -20.208 0.304   -20.410 1.00 12.92 ? 41  ALA A N   1 
ATOM   309  C  CA  . ALA A 1 41  ? -20.297 0.758   -21.806 1.00 13.94 ? 41  ALA A CA  1 
ATOM   310  C  C   . ALA A 1 41  ? -20.864 2.179   -21.960 1.00 13.63 ? 41  ALA A C   1 
ATOM   311  O  O   . ALA A 1 41  ? -20.743 2.778   -23.035 1.00 15.15 ? 41  ALA A O   1 
ATOM   312  C  CB  . ALA A 1 41  ? -21.159 -0.219  -22.626 1.00 13.22 ? 41  ALA A CB  1 
ATOM   313  N  N   . SER A 1 42  ? -21.497 2.715   -20.930 1.00 13.40 ? 42  SER A N   1 
ATOM   314  C  CA  . SER A 1 42  ? -22.018 4.070   -21.024 1.00 15.53 ? 42  SER A CA  1 
ATOM   315  C  C   . SER A 1 42  ? -20.885 5.136   -20.881 1.00 15.35 ? 42  SER A C   1 
ATOM   316  O  O   . SER A 1 42  ? -21.110 6.341   -21.160 1.00 15.33 ? 42  SER A O   1 
ATOM   317  C  CB  . SER A 1 42  ? -23.150 4.260   -19.986 1.00 17.68 ? 42  SER A CB  1 
ATOM   318  O  OG  . SER A 1 42  ? -22.574 4.643   -18.746 1.00 19.33 ? 42  SER A OG  1 
ATOM   319  N  N   . LEU A 1 43  ? -19.678 4.699   -20.501 1.00 13.68 ? 43  LEU A N   1 
ATOM   320  C  CA  . LEU A 1 43  ? -18.524 5.640   -20.320 1.00 13.56 ? 43  LEU A CA  1 
ATOM   321  C  C   . LEU A 1 43  ? -17.945 6.124   -21.687 1.00 15.44 ? 43  LEU A C   1 
ATOM   322  O  O   . LEU A 1 43  ? -17.295 5.368   -22.444 1.00 15.62 ? 43  LEU A O   1 
ATOM   323  C  CB  . LEU A 1 43  ? -17.454 5.011   -19.401 1.00 12.81 ? 43  LEU A CB  1 
ATOM   324  C  CG  . LEU A 1 43  ? -17.765 4.770   -17.884 1.00 12.24 ? 43  LEU A CG  1 
ATOM   325  C  CD1 . LEU A 1 43  ? -16.669 3.938   -17.158 1.00 13.07 ? 43  LEU A CD1 1 
ATOM   326  C  CD2 . LEU A 1 43  ? -18.022 6.084   -17.130 1.00 13.43 ? 43  LEU A CD2 1 
ATOM   327  N  N   . THR A 1 44  ? -18.177 7.395   -21.981 1.00 17.00 ? 44  THR A N   1 
ATOM   328  C  CA  . THR A 1 44  ? -17.950 7.965   -23.307 1.00 17.52 ? 44  THR A CA  1 
ATOM   329  C  C   . THR A 1 44  ? -16.647 8.740   -23.248 1.00 17.09 ? 44  THR A C   1 
ATOM   330  O  O   . THR A 1 44  ? -16.164 9.049   -22.143 1.00 16.59 ? 44  THR A O   1 
ATOM   331  C  CB  . THR A 1 44  ? -19.102 8.916   -23.740 1.00 18.82 ? 44  THR A CB  1 
ATOM   332  O  OG1 . THR A 1 44  ? -19.301 9.901   -22.704 1.00 19.02 ? 44  THR A OG1 1 
ATOM   333  C  CG2 . THR A 1 44  ? -20.428 8.205   -23.957 1.00 18.99 ? 44  THR A CG2 1 
ATOM   334  N  N   . PRO A 1 45  ? -16.069 9.076   -24.434 1.00 16.91 ? 45  PRO A N   1 
ATOM   335  C  CA  . PRO A 1 45  ? -14.838 9.848   -24.408 1.00 17.46 ? 45  PRO A CA  1 
ATOM   336  C  C   . PRO A 1 45  ? -15.032 11.229  -23.785 1.00 17.29 ? 45  PRO A C   1 
ATOM   337  O  O   . PRO A 1 45  ? -16.039 11.911  -24.074 1.00 17.25 ? 45  PRO A O   1 
ATOM   338  C  CB  . PRO A 1 45  ? -14.441 9.928   -25.908 1.00 18.38 ? 45  PRO A CB  1 
ATOM   339  C  CG  . PRO A 1 45  ? -15.118 8.747   -26.523 1.00 19.66 ? 45  PRO A CG  1 
ATOM   340  C  CD  . PRO A 1 45  ? -16.444 8.717   -25.818 1.00 16.21 ? 45  PRO A CD  1 
ATOM   341  N  N   . LEU A 1 46  ? -14.097 11.655  -22.934 1.00 17.43 ? 46  LEU A N   1 
ATOM   342  C  CA  . LEU A 1 46  ? -14.076 13.051  -22.532 1.00 16.89 ? 46  LEU A CA  1 
ATOM   343  C  C   . LEU A 1 46  ? -13.684 13.944  -23.718 1.00 17.23 ? 46  LEU A C   1 
ATOM   344  O  O   . LEU A 1 46  ? -12.926 13.527  -24.618 1.00 16.48 ? 46  LEU A O   1 
ATOM   345  C  CB  . LEU A 1 46  ? -13.130 13.257  -21.295 1.00 17.21 ? 46  LEU A CB  1 
ATOM   346  C  CG  . LEU A 1 46  ? -13.579 12.574  -19.973 1.00 17.00 ? 46  LEU A CG  1 
ATOM   347  C  CD1 . LEU A 1 46  ? -12.534 12.838  -18.854 1.00 17.76 ? 46  LEU A CD1 1 
ATOM   348  C  CD2 . LEU A 1 46  ? -14.923 13.160  -19.573 1.00 17.45 ? 46  LEU A CD2 1 
ATOM   349  N  N   . GLU A 1 47  ? -14.179 15.176  -23.734 1.00 17.02 ? 47  GLU A N   1 
ATOM   350  C  CA  . GLU A 1 47  ? -13.683 16.145  -24.714 1.00 19.35 ? 47  GLU A CA  1 
ATOM   351  C  C   . GLU A 1 47  ? -12.906 17.210  -23.958 1.00 19.41 ? 47  GLU A C   1 
ATOM   352  O  O   . GLU A 1 47  ? -13.400 17.756  -22.929 1.00 20.23 ? 47  GLU A O   1 
ATOM   353  C  CB  . GLU A 1 47  ? -14.831 16.724  -25.548 1.00 24.62 ? 47  GLU A CB  1 
ATOM   354  C  CG  . GLU A 1 47  ? -15.689 15.622  -26.162 1.00 27.17 ? 47  GLU A CG  1 
ATOM   355  C  CD  . GLU A 1 47  ? -16.703 16.111  -27.176 1.00 34.25 ? 47  GLU A CD  1 
ATOM   356  O  OE1 . GLU A 1 47  ? -16.645 15.655  -28.354 1.00 35.57 ? 47  GLU A OE1 1 
ATOM   357  O  OE2 . GLU A 1 47  ? -17.568 16.939  -26.790 1.00 36.50 ? 47  GLU A OE2 1 
ATOM   358  N  N   . PHE A 1 48  ? -11.694 17.456  -24.449 1.00 17.77 ? 48  PHE A N   1 
ATOM   359  C  CA  . PHE A 1 48  ? -10.727 18.383  -23.870 1.00 19.79 ? 48  PHE A CA  1 
ATOM   360  C  C   . PHE A 1 48  ? -10.731 19.734  -24.621 1.00 19.59 ? 48  PHE A C   1 
ATOM   361  O  O   . PHE A 1 48  ? -10.286 19.816  -25.770 1.00 22.19 ? 48  PHE A O   1 
ATOM   362  C  CB  . PHE A 1 48  ? -9.334  17.734  -23.889 1.00 19.44 ? 48  PHE A CB  1 
ATOM   363  C  CG  . PHE A 1 48  ? -9.326  16.310  -23.395 1.00 21.84 ? 48  PHE A CG  1 
ATOM   364  C  CD1 . PHE A 1 48  ? -9.218  15.261  -24.295 1.00 23.41 ? 48  PHE A CD1 1 
ATOM   365  C  CD2 . PHE A 1 48  ? -9.438  16.021  -22.029 1.00 20.78 ? 48  PHE A CD2 1 
ATOM   366  C  CE1 . PHE A 1 48  ? -9.215  13.927  -23.861 1.00 22.01 ? 48  PHE A CE1 1 
ATOM   367  C  CE2 . PHE A 1 48  ? -9.413  14.709  -21.581 1.00 22.28 ? 48  PHE A CE2 1 
ATOM   368  C  CZ  . PHE A 1 48  ? -9.310  13.661  -22.498 1.00 22.16 ? 48  PHE A CZ  1 
ATOM   369  N  N   . GLN A 1 49  ? -11.248 20.788  -23.983 1.00 19.02 ? 49  GLN A N   1 
ATOM   370  C  CA  . GLN A 1 49  ? -11.510 22.028  -24.672 1.00 17.10 ? 49  GLN A CA  1 
ATOM   371  C  C   . GLN A 1 49  ? -10.623 23.115  -24.074 1.00 15.04 ? 49  GLN A C   1 
ATOM   372  O  O   . GLN A 1 49  ? -10.414 23.143  -22.865 1.00 12.76 ? 49  GLN A O   1 
ATOM   373  C  CB  . GLN A 1 49  ? -12.984 22.386  -24.544 1.00 21.56 ? 49  GLN A CB  1 
ATOM   374  C  CG  . GLN A 1 49  ? -13.894 21.332  -25.187 1.00 25.10 ? 49  GLN A CG  1 
ATOM   375  C  CD  . GLN A 1 49  ? -15.358 21.753  -25.254 1.00 31.30 ? 49  GLN A CD  1 
ATOM   376  O  OE1 . GLN A 1 49  ? -15.869 22.423  -24.345 1.00 28.40 ? 49  GLN A OE1 1 
ATOM   377  N  NE2 . GLN A 1 49  ? -16.045 21.345  -26.331 1.00 37.10 ? 49  GLN A NE2 1 
ATOM   378  N  N   . GLY A 1 50  ? -10.093 23.985  -24.923 1.00 13.18 ? 50  GLY A N   1 
ATOM   379  C  CA  . GLY A 1 50  ? -9.121  24.999  -24.425 1.00 13.06 ? 50  GLY A CA  1 
ATOM   380  C  C   . GLY A 1 50  ? -7.806  24.466  -23.865 1.00 13.30 ? 50  GLY A C   1 
ATOM   381  O  O   . GLY A 1 50  ? -7.113  25.206  -23.173 1.00 11.71 ? 50  GLY A O   1 
ATOM   382  N  N   . TYR A 1 51  ? -7.477  23.193  -24.132 1.00 12.92 ? 51  TYR A N   1 
ATOM   383  C  CA  . TYR A 1 51  ? -6.169  22.561  -23.708 1.00 13.40 ? 51  TYR A CA  1 
ATOM   384  C  C   . TYR A 1 51  ? -4.968  23.098  -24.502 1.00 15.41 ? 51  TYR A C   1 
ATOM   385  O  O   . TYR A 1 51  ? -3.837  23.054  -24.013 1.00 14.99 ? 51  TYR A O   1 
ATOM   386  C  CB  . TYR A 1 51  ? -6.217  21.000  -23.831 1.00 12.77 ? 51  TYR A CB  1 
ATOM   387  C  CG  . TYR A 1 51  ? -6.791  20.286  -22.585 1.00 11.88 ? 51  TYR A CG  1 
ATOM   388  C  CD1 . TYR A 1 51  ? -7.941  20.794  -21.921 1.00 12.06 ? 51  TYR A CD1 1 
ATOM   389  C  CD2 . TYR A 1 51  ? -6.133  19.160  -22.013 1.00 12.27 ? 51  TYR A CD2 1 
ATOM   390  C  CE1 . TYR A 1 51  ? -8.450  20.165  -20.760 1.00 11.57 ? 51  TYR A CE1 1 
ATOM   391  C  CE2 . TYR A 1 51  ? -6.637  18.540  -20.871 1.00 11.34 ? 51  TYR A CE2 1 
ATOM   392  C  CZ  . TYR A 1 51  ? -7.770  19.071  -20.226 1.00 11.85 ? 51  TYR A CZ  1 
ATOM   393  O  OH  . TYR A 1 51  ? -8.229  18.407  -19.100 1.00 12.34 ? 51  TYR A OH  1 
ATOM   394  N  N   . ASN A 1 52  ? -5.221  23.597  -25.715 1.00 16.81 ? 52  ASN A N   1 
ATOM   395  C  CA  . ASN A 1 52  ? -4.184  24.190  -26.561 1.00 17.59 ? 52  ASN A CA  1 
ATOM   396  C  C   . ASN A 1 52  ? -3.863  25.608  -26.110 1.00 18.24 ? 52  ASN A C   1 
ATOM   397  O  O   . ASN A 1 52  ? -4.320  26.589  -26.704 1.00 18.84 ? 52  ASN A O   1 
ATOM   398  C  CB  . ASN A 1 52  ? -4.581  24.113  -28.037 1.00 22.03 ? 52  ASN A CB  1 
ATOM   399  C  CG  . ASN A 1 52  ? -3.378  24.236  -28.957 1.00 24.87 ? 52  ASN A CG  1 
ATOM   400  O  OD1 . ASN A 1 52  ? -2.224  24.221  -28.493 1.00 22.37 ? 52  ASN A OD1 1 
ATOM   401  N  ND2 . ASN A 1 52  ? -3.633  24.368  -30.257 1.00 26.69 ? 52  ASN A ND2 1 
ATOM   402  N  N   . LEU A 1 53  ? -3.102  25.697  -25.021 1.00 15.69 ? 53  LEU A N   1 
ATOM   403  C  CA  . LEU A 1 53  ? -2.853  26.967  -24.365 1.00 15.17 ? 53  LEU A CA  1 
ATOM   404  C  C   . LEU A 1 53  ? -2.118  27.952  -25.290 1.00 14.16 ? 53  LEU A C   1 
ATOM   405  O  O   . LEU A 1 53  ? -1.247  27.565  -26.046 1.00 13.73 ? 53  LEU A O   1 
ATOM   406  C  CB  . LEU A 1 53  ? -2.063  26.767  -23.066 1.00 15.73 ? 53  LEU A CB  1 
ATOM   407  C  CG  . LEU A 1 53  ? -2.715  25.944  -21.934 1.00 15.31 ? 53  LEU A CG  1 
ATOM   408  C  CD1 . LEU A 1 53  ? -1.774  25.836  -20.742 1.00 15.52 ? 53  LEU A CD1 1 
ATOM   409  C  CD2 . LEU A 1 53  ? -4.069  26.516  -21.494 1.00 15.65 ? 53  LEU A CD2 1 
ATOM   410  N  N   . SER A 1 54  ? -2.519  29.214  -25.235 1.00 13.25 ? 54  SER A N   1 
ATOM   411  C  CA  . SER A 1 54  ? -1.858  30.272  -25.997 1.00 13.77 ? 54  SER A CA  1 
ATOM   412  C  C   . SER A 1 54  ? -0.342  30.310  -25.783 1.00 13.16 ? 54  SER A C   1 
ATOM   413  O  O   . SER A 1 54  ? 0.105   30.596  -24.652 1.00 12.03 ? 54  SER A O   1 
ATOM   414  C  CB  . SER A 1 54  ? -2.402  31.607  -25.537 1.00 13.39 ? 54  SER A CB  1 
ATOM   415  O  OG  . SER A 1 54  ? -1.959  32.573  -26.484 1.00 14.97 ? 54  SER A OG  1 
ATOM   416  N  N   . ALA A 1 55  ? 0.448   30.064  -26.850 1.00 13.54 ? 55  ALA A N   1 
ATOM   417  C  CA  . ALA A 1 55  ? 1.910   30.261  -26.747 1.00 14.04 ? 55  ALA A CA  1 
ATOM   418  C  C   . ALA A 1 55  ? 2.301   31.738  -26.464 1.00 13.58 ? 55  ALA A C   1 
ATOM   419  O  O   . ALA A 1 55  ? 3.424   32.023  -25.960 1.00 13.70 ? 55  ALA A O   1 
ATOM   420  C  CB  . ALA A 1 55  ? 2.630   29.750  -27.981 1.00 15.54 ? 55  ALA A CB  1 
ATOM   421  N  N   . ASN A 1 56  ? 1.363   32.685  -26.703 1.00 15.14 ? 56  ASN A N   1 
ATOM   422  C  CA  . ASN A 1 56  ? 1.613   34.121  -26.360 1.00 14.56 ? 56  ASN A CA  1 
ATOM   423  C  C   . ASN A 1 56  ? 1.288   34.564  -24.914 1.00 15.65 ? 56  ASN A C   1 
ATOM   424  O  O   . ASN A 1 56  ? 1.433   35.774  -24.549 1.00 15.95 ? 56  ASN A O   1 
ATOM   425  C  CB  . ASN A 1 56  ? 0.905   35.039  -27.379 1.00 15.74 ? 56  ASN A CB  1 
ATOM   426  C  CG  . ASN A 1 56  ? 1.462   34.884  -28.782 1.00 17.78 ? 56  ASN A CG  1 
ATOM   427  O  OD1 . ASN A 1 56  ? 2.638   34.532  -28.967 1.00 18.11 ? 56  ASN A OD1 1 
ATOM   428  N  ND2 . ASN A 1 56  ? 0.614   35.023  -29.760 1.00 20.09 ? 56  ASN A ND2 1 
ATOM   429  N  N   . LYS A 1 57  ? 0.835   33.578  -24.124 1.00 15.32 ? 57  LYS A N   1 
ATOM   430  C  CA  . LYS A 1 57  ? 0.471   33.675  -22.697 1.00 15.78 ? 57  LYS A CA  1 
ATOM   431  C  C   . LYS A 1 57  ? 1.488   32.874  -21.884 1.00 14.79 ? 57  LYS A C   1 
ATOM   432  O  O   . LYS A 1 57  ? 2.023   31.885  -22.406 1.00 17.24 ? 57  LYS A O   1 
ATOM   433  C  CB  . LYS A 1 57  ? -0.963  33.104  -22.474 1.00 16.06 ? 57  LYS A CB  1 
ATOM   434  C  CG  . LYS A 1 57  ? -1.563  33.345  -21.048 1.00 17.01 ? 57  LYS A CG  1 
ATOM   435  C  CD  . LYS A 1 57  ? -3.112  33.311  -21.024 1.00 16.19 ? 57  LYS A CD  1 
ATOM   436  C  CE  . LYS A 1 57  ? -3.685  33.020  -19.631 1.00 17.84 ? 57  LYS A CE  1 
ATOM   437  N  NZ  . LYS A 1 57  ? -5.145  32.753  -19.771 1.00 17.86 ? 57  LYS A NZ  1 
ATOM   438  N  N   . GLN A 1 58  ? 1.763   33.293  -20.656 1.00 13.38 ? 58  GLN A N   1 
ATOM   439  C  CA  . GLN A 1 58  ? 2.561   32.513  -19.718 1.00 13.02 ? 58  GLN A CA  1 
ATOM   440  C  C   . GLN A 1 58  ? 1.774   32.008  -18.484 1.00 12.56 ? 58  GLN A C   1 
ATOM   441  O  O   . GLN A 1 58  ? 0.863   32.692  -17.967 1.00 12.36 ? 58  GLN A O   1 
ATOM   442  C  CB  . GLN A 1 58  ? 3.747   33.368  -19.217 1.00 14.34 ? 58  GLN A CB  1 
ATOM   443  C  CG  . GLN A 1 58  ? 4.678   33.877  -20.297 1.00 16.90 ? 58  GLN A CG  1 
ATOM   444  C  CD  . GLN A 1 58  ? 5.596   34.981  -19.765 1.00 17.96 ? 58  GLN A CD  1 
ATOM   445  O  OE1 . GLN A 1 58  ? 5.146   36.079  -19.415 1.00 24.10 ? 58  GLN A OE1 1 
ATOM   446  N  NE2 . GLN A 1 58  ? 6.864   34.694  -19.709 1.00 17.07 ? 58  GLN A NE2 1 
ATOM   447  N  N   . PHE A 1 59  ? 2.192   30.838  -17.982 1.00 12.57 ? 59  PHE A N   1 
ATOM   448  C  CA  . PHE A 1 59  ? 1.549   30.135  -16.911 1.00 12.47 ? 59  PHE A CA  1 
ATOM   449  C  C   . PHE A 1 59  ? 2.537   29.889  -15.772 1.00 12.32 ? 59  PHE A C   1 
ATOM   450  O  O   . PHE A 1 59  ? 3.617   29.442  -16.007 1.00 13.88 ? 59  PHE A O   1 
ATOM   451  C  CB  . PHE A 1 59  ? 0.942   28.821  -17.453 1.00 12.50 ? 59  PHE A CB  1 
ATOM   452  C  CG  . PHE A 1 59  ? -0.079  29.066  -18.541 1.00 12.59 ? 59  PHE A CG  1 
ATOM   453  C  CD1 . PHE A 1 59  ? 0.304   29.208  -19.885 1.00 12.90 ? 59  PHE A CD1 1 
ATOM   454  C  CD2 . PHE A 1 59  ? -1.406  29.367  -18.185 1.00 14.28 ? 59  PHE A CD2 1 
ATOM   455  C  CE1 . PHE A 1 59  ? -0.654  29.527  -20.891 1.00 12.87 ? 59  PHE A CE1 1 
ATOM   456  C  CE2 . PHE A 1 59  ? -2.336  29.684  -19.177 1.00 13.85 ? 59  PHE A CE2 1 
ATOM   457  C  CZ  . PHE A 1 59  ? -1.965  29.756  -20.523 1.00 12.95 ? 59  PHE A CZ  1 
ATOM   458  N  N   . LEU A 1 60  ? 2.116   30.143  -14.558 1.00 12.22 ? 60  LEU A N   1 
ATOM   459  C  CA  . LEU A 1 60  ? 2.973   30.087  -13.376 1.00 13.05 ? 60  LEU A CA  1 
ATOM   460  C  C   . LEU A 1 60  ? 3.253   28.640  -12.904 1.00 12.89 ? 60  LEU A C   1 
ATOM   461  O  O   . LEU A 1 60  ? 2.338   27.869  -12.596 1.00 13.22 ? 60  LEU A O   1 
ATOM   462  C  CB  . LEU A 1 60  ? 2.325   30.897  -12.252 1.00 14.30 ? 60  LEU A CB  1 
ATOM   463  C  CG  . LEU A 1 60  ? 3.208   31.254  -11.054 1.00 14.25 ? 60  LEU A CG  1 
ATOM   464  C  CD1 . LEU A 1 60  ? 4.212   32.329  -11.448 1.00 16.46 ? 60  LEU A CD1 1 
ATOM   465  C  CD2 . LEU A 1 60  ? 2.283   31.828  -9.967  1.00 16.50 ? 60  LEU A CD2 1 
ATOM   466  N  N   . LEU A 1 61  ? 4.532   28.311  -12.856 1.00 14.97 ? 61  LEU A N   1 
ATOM   467  C  CA  . LEU A 1 61  ? 5.012   27.062  -12.263 1.00 13.02 ? 61  LEU A CA  1 
ATOM   468  C  C   . LEU A 1 61  ? 5.613   27.311  -10.877 1.00 13.90 ? 61  LEU A C   1 
ATOM   469  O  O   . LEU A 1 61  ? 6.386   28.251  -10.704 1.00 16.49 ? 61  LEU A O   1 
ATOM   470  C  CB  . LEU A 1 61  ? 6.062   26.480  -13.245 1.00 13.14 ? 61  LEU A CB  1 
ATOM   471  C  CG  . LEU A 1 61  ? 6.674   25.154  -12.825 1.00 12.48 ? 61  LEU A CG  1 
ATOM   472  C  CD1 . LEU A 1 61  ? 5.776   24.006  -13.274 1.00 12.07 ? 61  LEU A CD1 1 
ATOM   473  C  CD2 . LEU A 1 61  ? 8.045   25.084  -13.495 1.00 12.86 ? 61  LEU A CD2 1 
ATOM   474  N  N   . THR A 1 62  ? 5.259   26.486  -9.878  1.00 13.73 ? 62  THR A N   1 
ATOM   475  C  CA  . THR A 1 62  ? 5.518   26.775  -8.458  1.00 14.32 ? 62  THR A CA  1 
ATOM   476  C  C   . THR A 1 62  ? 5.951   25.507  -7.712  1.00 13.66 ? 62  THR A C   1 
ATOM   477  O  O   . THR A 1 62  ? 5.306   24.449  -7.860  1.00 14.27 ? 62  THR A O   1 
ATOM   478  C  CB  . THR A 1 62  ? 4.238   27.317  -7.748  1.00 16.51 ? 62  THR A CB  1 
ATOM   479  O  OG1 . THR A 1 62  ? 3.793   28.515  -8.420  1.00 16.39 ? 62  THR A OG1 1 
ATOM   480  C  CG2 . THR A 1 62  ? 4.508   27.637  -6.244  1.00 16.62 ? 62  THR A CG2 1 
ATOM   481  N  N   . ASN A 1 63  ? 7.057   25.617  -6.953  1.00 14.14 ? 63  ASN A N   1 
ATOM   482  C  CA  . ASN A 1 63  ? 7.448   24.607  -5.970  1.00 14.55 ? 63  ASN A CA  1 
ATOM   483  C  C   . ASN A 1 63  ? 6.671   24.994  -4.691  1.00 14.89 ? 63  ASN A C   1 
ATOM   484  O  O   . ASN A 1 63  ? 6.958   25.994  -4.075  1.00 15.78 ? 63  ASN A O   1 
ATOM   485  C  CB  . ASN A 1 63  ? 8.981   24.624  -5.734  1.00 14.62 ? 63  ASN A CB  1 
ATOM   486  C  CG  . ASN A 1 63  ? 9.450   23.604  -4.667  1.00 13.41 ? 63  ASN A CG  1 
ATOM   487  O  OD1 . ASN A 1 63  ? 8.716   23.294  -3.717  1.00 12.77 ? 63  ASN A OD1 1 
ATOM   488  N  ND2 . ASN A 1 63  ? 10.664  23.076  -4.825  1.00 13.37 ? 63  ASN A ND2 1 
ATOM   489  N  N   . ASN A 1 64  ? 5.660   24.210  -4.312  1.00 13.59 ? 64  ASN A N   1 
ATOM   490  C  CA  . ASN A 1 64  ? 4.829   24.573  -3.161  1.00 14.36 ? 64  ASN A CA  1 
ATOM   491  C  C   . ASN A 1 64  ? 5.270   23.795  -1.908  1.00 13.85 ? 64  ASN A C   1 
ATOM   492  O  O   . ASN A 1 64  ? 4.503   23.726  -0.928  1.00 14.24 ? 64  ASN A O   1 
ATOM   493  C  CB  . ASN A 1 64  ? 3.319   24.342  -3.453  1.00 14.59 ? 64  ASN A CB  1 
ATOM   494  C  CG  . ASN A 1 64  ? 2.950   22.829  -3.592  1.00 15.62 ? 64  ASN A CG  1 
ATOM   495  O  OD1 . ASN A 1 64  ? 3.778   21.947  -3.379  1.00 15.15 ? 64  ASN A OD1 1 
ATOM   496  N  ND2 . ASN A 1 64  ? 1.683   22.538  -4.045  1.00 18.25 ? 64  ASN A ND2 1 
ATOM   497  N  N   . GLY A 1 65  ? 6.412   23.114  -2.007  1.00 12.69 ? 65  GLY A N   1 
ATOM   498  C  CA  . GLY A 1 65  ? 6.981   22.363  -0.863  1.00 13.82 ? 65  GLY A CA  1 
ATOM   499  C  C   . GLY A 1 65  ? 6.530   20.907  -0.791  1.00 12.44 ? 65  GLY A C   1 
ATOM   500  O  O   . GLY A 1 65  ? 7.077   20.142  -0.032  1.00 13.65 ? 65  GLY A O   1 
ATOM   501  N  N   . HIS A 1 66  ? 5.524   20.541  -1.602  1.00 13.50 ? 66  HIS A N   1 
ATOM   502  C  CA  . HIS A 1 66  ? 5.037   19.175  -1.680  1.00 13.13 ? 66  HIS A CA  1 
ATOM   503  C  C   . HIS A 1 66  ? 5.089   18.564  -3.083  1.00 12.41 ? 66  HIS A C   1 
ATOM   504  O  O   . HIS A 1 66  ? 5.095   17.315  -3.227  1.00 13.98 ? 66  HIS A O   1 
ATOM   505  C  CB  . HIS A 1 66  ? 3.613   19.104  -1.221  1.00 13.68 ? 66  HIS A CB  1 
ATOM   506  C  CG  . HIS A 1 66  ? 3.350   19.675  0.170   1.00 14.66 ? 66  HIS A CG  1 
ATOM   507  N  ND1 . HIS A 1 66  ? 3.678   19.009  1.346   1.00 15.61 ? 66  HIS A ND1 1 
ATOM   508  C  CD2 . HIS A 1 66  ? 2.640   20.812  0.556   1.00 14.91 ? 66  HIS A CD2 1 
ATOM   509  C  CE1 . HIS A 1 66  ? 3.218   19.716  2.398   1.00 14.46 ? 66  HIS A CE1 1 
ATOM   510  N  NE2 . HIS A 1 66  ? 2.629   20.840  1.925   1.00 15.07 ? 66  HIS A NE2 1 
ATOM   511  N  N   . SER A 1 67  ? 5.061   19.406  -4.106  1.00 11.08 ? 67  SER A N   1 
ATOM   512  C  CA  . SER A 1 67  ? 5.119   18.996  -5.545  1.00 11.49 ? 67  SER A CA  1 
ATOM   513  C  C   . SER A 1 67  ? 5.544   20.214  -6.404  1.00 13.06 ? 67  SER A C   1 
ATOM   514  O  O   . SER A 1 67  ? 5.848   21.292  -5.852  1.00 15.75 ? 67  SER A O   1 
ATOM   515  C  CB  . SER A 1 67  ? 3.764   18.394  -5.982  1.00 12.03 ? 67  SER A CB  1 
ATOM   516  O  OG  . SER A 1 67  ? 3.756   18.078  -7.381  1.00 11.23 ? 67  SER A OG  1 
ATOM   517  N  N   . VAL A 1 68  ? 5.630   20.054  -7.717  1.00 12.17 ? 68  VAL A N   1 
ATOM   518  C  CA  . VAL A 1 68  ? 5.844   21.183  -8.642  1.00 14.01 ? 68  VAL A CA  1 
ATOM   519  C  C   . VAL A 1 68  ? 4.525   21.347  -9.375  1.00 14.24 ? 68  VAL A C   1 
ATOM   520  O  O   . VAL A 1 68  ? 3.987   20.359  -9.866  1.00 12.12 ? 68  VAL A O   1 
ATOM   521  C  CB  . VAL A 1 68  ? 7.070   21.001  -9.601  1.00 13.95 ? 68  VAL A CB  1 
ATOM   522  C  CG1 . VAL A 1 68  ? 7.001   19.694  -10.413 1.00 12.99 ? 68  VAL A CG1 1 
ATOM   523  C  CG2 . VAL A 1 68  ? 7.274   22.211  -10.519 1.00 14.55 ? 68  VAL A CG2 1 
ATOM   524  N  N   . LYS A 1 69  ? 3.965   22.567  -9.322  1.00 13.94 ? 69  LYS A N   1 
ATOM   525  C  CA  . LYS A 1 69  ? 2.576   22.790  -9.777  1.00 14.03 ? 69  LYS A CA  1 
ATOM   526  C  C   . LYS A 1 69  ? 2.488   23.839  -10.899 1.00 12.99 ? 69  LYS A C   1 
ATOM   527  O  O   . LYS A 1 69  ? 3.080   24.870  -10.791 1.00 13.65 ? 69  LYS A O   1 
ATOM   528  C  CB  . LYS A 1 69  ? 1.715   23.218  -8.578  1.00 14.75 ? 69  LYS A CB  1 
ATOM   529  C  CG  . LYS A 1 69  ? 0.714   24.323  -8.784  1.00 18.69 ? 69  LYS A CG  1 
ATOM   530  C  CD  . LYS A 1 69  ? -0.092  24.596  -7.498  1.00 19.68 ? 69  LYS A CD  1 
ATOM   531  C  CE  . LYS A 1 69  ? -0.080  26.112  -7.191  1.00 20.41 ? 69  LYS A CE  1 
ATOM   532  N  NZ  . LYS A 1 69  ? -0.921  26.432  -5.963  1.00 20.59 ? 69  LYS A NZ  1 
ATOM   533  N  N   . LEU A 1 70  ? 1.737   23.563  -11.953 1.00 12.37 ? 70  LEU A N   1 
ATOM   534  C  CA  . LEU A 1 70  ? 1.564   24.576  -12.993 1.00 12.58 ? 70  LEU A CA  1 
ATOM   535  C  C   . LEU A 1 70  ? 0.129   25.105  -12.963 1.00 12.51 ? 70  LEU A C   1 
ATOM   536  O  O   . LEU A 1 70  ? -0.807  24.317  -13.112 1.00 11.30 ? 70  LEU A O   1 
ATOM   537  C  CB  . LEU A 1 70  ? 1.862   23.980  -14.373 1.00 11.52 ? 70  LEU A CB  1 
ATOM   538  C  CG  . LEU A 1 70  ? 1.568   24.858  -15.633 1.00 11.13 ? 70  LEU A CG  1 
ATOM   539  C  CD1 . LEU A 1 70  ? 2.636   25.971  -15.715 1.00 10.86 ? 70  LEU A CD1 1 
ATOM   540  C  CD2 . LEU A 1 70  ? 1.638   23.999  -16.862 1.00 10.83 ? 70  LEU A CD2 1 
ATOM   541  N  N   . ASN A 1 71  ? -0.058  26.419  -12.784 1.00 13.24 ? 71  ASN A N   1 
ATOM   542  C  CA  . ASN A 1 71  ? -1.423  26.960  -12.761 1.00 13.23 ? 71  ASN A CA  1 
ATOM   543  C  C   . ASN A 1 71  ? -2.047  26.849  -14.170 1.00 13.53 ? 71  ASN A C   1 
ATOM   544  O  O   . ASN A 1 71  ? -1.346  27.039  -15.154 1.00 13.16 ? 71  ASN A O   1 
ATOM   545  C  CB  . ASN A 1 71  ? -1.426  28.435  -12.355 1.00 17.13 ? 71  ASN A CB  1 
ATOM   546  C  CG  . ASN A 1 71  ? -1.311  28.645  -10.860 1.00 21.04 ? 71  ASN A CG  1 
ATOM   547  O  OD1 . ASN A 1 71  ? -1.214  27.684  -10.095 1.00 22.91 ? 71  ASN A OD1 1 
ATOM   548  N  ND2 . ASN A 1 71  ? -1.232  29.934  -10.437 1.00 25.70 ? 71  ASN A ND2 1 
ATOM   549  N  N   . LEU A 1 72  ? -3.350  26.581  -14.271 1.00 12.07 ? 72  LEU A N   1 
ATOM   550  C  CA  . LEU A 1 72  ? -4.031  26.416  -15.568 1.00 11.29 ? 72  LEU A CA  1 
ATOM   551  C  C   . LEU A 1 72  ? -5.233  27.376  -15.582 1.00 12.08 ? 72  LEU A C   1 
ATOM   552  O  O   . LEU A 1 72  ? -5.731  27.730  -14.505 1.00 11.65 ? 72  LEU A O   1 
ATOM   553  C  CB  . LEU A 1 72  ? -4.484  24.941  -15.632 1.00 10.96 ? 72  LEU A CB  1 
ATOM   554  C  CG  . LEU A 1 72  ? -3.363  23.892  -15.763 1.00 9.61  ? 72  LEU A CG  1 
ATOM   555  C  CD1 . LEU A 1 72  ? -3.991  22.466  -15.697 1.00 10.86 ? 72  LEU A CD1 1 
ATOM   556  C  CD2 . LEU A 1 72  ? -2.591  24.131  -17.096 1.00 9.13  ? 72  LEU A CD2 1 
ATOM   557  N  N   . PRO A 1 73  ? -5.691  27.809  -16.786 1.00 13.48 ? 73  PRO A N   1 
ATOM   558  C  CA  . PRO A 1 73  ? -6.762  28.808  -16.887 1.00 13.65 ? 73  PRO A CA  1 
ATOM   559  C  C   . PRO A 1 73  ? -8.127  28.233  -16.824 1.00 15.39 ? 73  PRO A C   1 
ATOM   560  O  O   . PRO A 1 73  ? -8.327  27.082  -17.198 1.00 13.90 ? 73  PRO A O   1 
ATOM   561  C  CB  . PRO A 1 73  ? -6.554  29.414  -18.290 1.00 13.42 ? 73  PRO A CB  1 
ATOM   562  C  CG  . PRO A 1 73  ? -5.922  28.299  -19.077 1.00 12.49 ? 73  PRO A CG  1 
ATOM   563  C  CD  . PRO A 1 73  ? -5.125  27.472  -18.120 1.00 11.86 ? 73  PRO A CD  1 
ATOM   564  N  N   . SER A 1 74  ? -9.074  29.035  -16.351 1.00 17.57 ? 74  SER A N   1 
ATOM   565  C  CA  . SER A 1 74  ? -10.447 28.542  -16.233 1.00 16.88 ? 74  SER A CA  1 
ATOM   566  C  C   . SER A 1 74  ? -11.142 28.290  -17.579 1.00 17.03 ? 74  SER A C   1 
ATOM   567  O  O   . SER A 1 74  ? -12.199 27.685  -17.577 1.00 15.95 ? 74  SER A O   1 
ATOM   568  C  CB  . SER A 1 74  ? -11.295 29.519  -15.384 1.00 19.31 ? 74  SER A CB  1 
ATOM   569  O  OG  . SER A 1 74  ? -11.343 30.825  -15.982 1.00 21.37 ? 74  SER A OG  1 
ATOM   570  N  N   . ASP A 1 75  ? -10.600 28.775  -18.704 1.00 15.13 ? 75  ASP A N   1 
ATOM   571  C  CA  . ASP A 1 75  ? -11.228 28.439  -20.015 1.00 15.14 ? 75  ASP A CA  1 
ATOM   572  C  C   . ASP A 1 75  ? -10.867 27.050  -20.527 1.00 14.10 ? 75  ASP A C   1 
ATOM   573  O  O   . ASP A 1 75  ? -11.388 26.615  -21.508 1.00 13.33 ? 75  ASP A O   1 
ATOM   574  C  CB  . ASP A 1 75  ? -10.932 29.490  -21.114 1.00 14.16 ? 75  ASP A CB  1 
ATOM   575  C  CG  . ASP A 1 75  ? -9.462  29.529  -21.516 1.00 15.40 ? 75  ASP A CG  1 
ATOM   576  O  OD1 . ASP A 1 75  ? -8.611  29.975  -20.695 1.00 16.46 ? 75  ASP A OD1 1 
ATOM   577  O  OD2 . ASP A 1 75  ? -9.162  29.134  -22.654 1.00 15.66 ? 75  ASP A OD2 1 
ATOM   578  N  N   . MET A 1 76  ? -9.909  26.398  -19.894 1.00 13.38 ? 76  MET A N   1 
ATOM   579  C  CA  . MET A 1 76  ? -9.607  25.011  -20.162 1.00 14.21 ? 76  MET A CA  1 
ATOM   580  C  C   . MET A 1 76  ? -10.660 24.160  -19.411 1.00 14.89 ? 76  MET A C   1 
ATOM   581  O  O   . MET A 1 76  ? -10.964 24.431  -18.269 1.00 16.55 ? 76  MET A O   1 
ATOM   582  C  CB  . MET A 1 76  ? -8.166  24.783  -19.672 1.00 14.23 ? 76  MET A CB  1 
ATOM   583  C  CG  . MET A 1 76  ? -7.582  23.393  -19.913 1.00 15.61 ? 76  MET A CG  1 
ATOM   584  S  SD  . MET A 1 76  ? -5.843  23.446  -19.303 1.00 14.26 ? 76  MET A SD  1 
ATOM   585  C  CE  . MET A 1 76  ? -5.690  21.680  -19.170 1.00 14.35 ? 76  MET A CE  1 
ATOM   586  N  N   . HIS A 1 77  ? -11.278 23.177  -20.050 1.00 15.70 ? 77  HIS A N   1 
ATOM   587  C  CA  . HIS A 1 77  ? -12.252 22.362  -19.315 1.00 17.81 ? 77  HIS A CA  1 
ATOM   588  C  C   . HIS A 1 77  ? -12.489 21.008  -19.908 1.00 17.43 ? 77  HIS A C   1 
ATOM   589  O  O   . HIS A 1 77  ? -12.144 20.796  -21.064 1.00 16.57 ? 77  HIS A O   1 
ATOM   590  C  CB  . HIS A 1 77  ? -13.592 23.093  -19.172 1.00 19.31 ? 77  HIS A CB  1 
ATOM   591  C  CG  . HIS A 1 77  ? -14.185 23.571  -20.464 1.00 21.15 ? 77  HIS A CG  1 
ATOM   592  N  ND1 . HIS A 1 77  ? -14.151 24.884  -20.832 1.00 22.98 ? 77  HIS A ND1 1 
ATOM   593  C  CD2 . HIS A 1 77  ? -14.876 22.901  -21.459 1.00 23.98 ? 77  HIS A CD2 1 
ATOM   594  C  CE1 . HIS A 1 77  ? -14.743 25.034  -22.019 1.00 23.51 ? 77  HIS A CE1 1 
ATOM   595  N  NE2 . HIS A 1 77  ? -15.194 23.817  -22.415 1.00 25.72 ? 77  HIS A NE2 1 
ATOM   596  N  N   . ILE A 1 78  ? -13.107 20.125  -19.128 1.00 15.62 ? 78  ILE A N   1 
ATOM   597  C  CA  . ILE A 1 78  ? -13.607 18.839  -19.616 1.00 17.18 ? 78  ILE A CA  1 
ATOM   598  C  C   . ILE A 1 78  ? -15.087 18.900  -19.874 1.00 17.16 ? 78  ILE A C   1 
ATOM   599  O  O   . ILE A 1 78  ? -15.847 19.386  -19.027 1.00 19.01 ? 78  ILE A O   1 
ATOM   600  C  CB  . ILE A 1 78  ? -13.552 17.793  -18.503 1.00 17.90 ? 78  ILE A CB  1 
ATOM   601  C  CG1 . ILE A 1 78  ? -12.115 17.513  -18.055 1.00 19.59 ? 78  ILE A CG1 1 
ATOM   602  C  CG2 . ILE A 1 78  ? -14.298 16.536  -18.946 1.00 19.35 ? 78  ILE A CG2 1 
ATOM   603  C  CD1 . ILE A 1 78  ? -12.070 16.874  -16.679 1.00 21.15 ? 78  ILE A CD1 1 
ATOM   604  N  N   . GLN A 1 79  ? -15.512 18.413  -21.022 1.00 17.62 ? 79  GLN A N   1 
ATOM   605  C  CA  . GLN A 1 79  ? -16.898 18.192  -21.210 1.00 19.84 ? 79  GLN A CA  1 
ATOM   606  C  C   . GLN A 1 79  ? -17.177 16.714  -21.381 1.00 19.17 ? 79  GLN A C   1 
ATOM   607  O  O   . GLN A 1 79  ? -16.306 15.908  -21.858 1.00 17.69 ? 79  GLN A O   1 
ATOM   608  C  CB  . GLN A 1 79  ? -17.465 19.062  -22.342 1.00 25.40 ? 79  GLN A CB  1 
ATOM   609  C  CG  . GLN A 1 79  ? -18.078 18.334  -23.528 1.00 30.67 ? 79  GLN A CG  1 
ATOM   610  C  CD  . GLN A 1 79  ? -18.843 19.263  -24.445 1.00 38.31 ? 79  GLN A CD  1 
ATOM   611  O  OE1 . GLN A 1 79  ? -19.128 18.923  -25.598 1.00 45.50 ? 79  GLN A OE1 1 
ATOM   612  N  NE2 . GLN A 1 79  ? -19.211 20.438  -23.928 1.00 41.41 ? 79  GLN A NE2 1 
ATOM   613  N  N   . GLY A 1 80  ? -18.391 16.354  -20.978 1.00 19.93 ? 80  GLY A N   1 
ATOM   614  C  CA  . GLY A 1 80  ? -18.876 14.966  -21.042 1.00 21.04 ? 80  GLY A CA  1 
ATOM   615  C  C   . GLY A 1 80  ? -19.393 14.418  -19.711 1.00 20.53 ? 80  GLY A C   1 
ATOM   616  O  O   . GLY A 1 80  ? -20.044 13.378  -19.700 1.00 21.36 ? 80  GLY A O   1 
ATOM   617  N  N   . LEU A 1 81  ? -19.087 15.079  -18.598 1.00 18.80 ? 81  LEU A N   1 
ATOM   618  C  CA  . LEU A 1 81  ? -19.647 14.718  -17.289 1.00 18.48 ? 81  LEU A CA  1 
ATOM   619  C  C   . LEU A 1 81  ? -20.959 15.488  -17.059 1.00 19.16 ? 81  LEU A C   1 
ATOM   620  O  O   . LEU A 1 81  ? -21.292 16.311  -17.920 1.00 21.42 ? 81  LEU A O   1 
ATOM   621  C  CB  . LEU A 1 81  ? -18.624 14.984  -16.178 1.00 16.65 ? 81  LEU A CB  1 
ATOM   622  C  CG  . LEU A 1 81  ? -17.265 14.270  -16.281 1.00 15.64 ? 81  LEU A CG  1 
ATOM   623  C  CD1 . LEU A 1 81  ? -16.193 14.774  -15.296 1.00 15.20 ? 81  LEU A CD1 1 
ATOM   624  C  CD2 . LEU A 1 81  ? -17.461 12.786  -16.056 1.00 15.94 ? 81  LEU A CD2 1 
ATOM   625  N  N   . GLN A 1 82  ? -21.687 15.253  -15.941 1.00 19.86 ? 82  GLN A N   1 
ATOM   626  C  CA  . GLN A 1 82  ? -23.034 15.884  -15.743 1.00 19.93 ? 82  GLN A CA  1 
ATOM   627  C  C   . GLN A 1 82  ? -22.934 17.412  -15.787 1.00 20.31 ? 82  GLN A C   1 
ATOM   628  O  O   . GLN A 1 82  ? -23.833 18.093  -16.308 1.00 18.79 ? 82  GLN A O   1 
ATOM   629  C  CB  . GLN A 1 82  ? -23.769 15.433  -14.451 1.00 22.45 ? 82  GLN A CB  1 
ATOM   630  C  CG  . GLN A 1 82  ? -25.218 16.018  -14.385 1.00 26.29 ? 82  GLN A CG  1 
ATOM   631  C  CD  . GLN A 1 82  ? -25.960 15.929  -13.029 1.00 29.15 ? 82  GLN A CD  1 
ATOM   632  O  OE1 . GLN A 1 82  ? -25.687 16.696  -12.097 1.00 33.59 ? 82  GLN A OE1 1 
ATOM   633  N  NE2 . GLN A 1 82  ? -26.934 15.018  -12.939 1.00 27.25 ? 82  GLN A NE2 1 
ATOM   634  N  N   . SER A 1 83  ? -21.856 17.932  -15.173 1.00 17.55 ? 83  SER A N   1 
ATOM   635  C  CA  . SER A 1 83  ? -21.510 19.358  -15.208 1.00 18.35 ? 83  SER A CA  1 
ATOM   636  C  C   . SER A 1 83  ? -20.194 19.525  -15.963 1.00 19.56 ? 83  SER A C   1 
ATOM   637  O  O   . SER A 1 83  ? -19.396 18.588  -16.065 1.00 18.80 ? 83  SER A O   1 
ATOM   638  C  CB  . SER A 1 83  ? -21.212 19.883  -13.807 1.00 17.36 ? 83  SER A CB  1 
ATOM   639  O  OG  . SER A 1 83  ? -22.279 19.826  -12.815 1.00 17.50 ? 83  SER A OG  1 
ATOM   640  N  N   . ARG A 1 84  ? -19.939 20.761  -16.402 1.00 18.38 ? 84  ARG A N   1 
ATOM   641  C  CA  . ARG A 1 84  ? -18.635 21.185  -16.894 1.00 16.55 ? 84  ARG A CA  1 
ATOM   642  C  C   . ARG A 1 84  ? -17.660 21.328  -15.746 1.00 13.93 ? 84  ARG A C   1 
ATOM   643  O  O   . ARG A 1 84  ? -18.000 21.832  -14.678 1.00 13.35 ? 84  ARG A O   1 
ATOM   644  C  CB  . ARG A 1 84  ? -18.734 22.574  -17.531 1.00 16.67 ? 84  ARG A CB  1 
ATOM   645  C  CG  . ARG A 1 84  ? -17.408 23.034  -18.121 1.00 17.66 ? 84  ARG A CG  1 
ATOM   646  C  CD  . ARG A 1 84  ? -17.536 24.424  -18.740 1.00 17.03 ? 84  ARG A CD  1 
ATOM   647  N  NE  . ARG A 1 84  ? -17.959 24.356  -20.142 1.00 16.10 ? 84  ARG A NE  1 
ATOM   648  C  CZ  . ARG A 1 84  ? -18.008 25.410  -20.969 1.00 17.75 ? 84  ARG A CZ  1 
ATOM   649  N  NH1 . ARG A 1 84  ? -18.436 25.259  -22.223 1.00 16.80 ? 84  ARG A NH1 1 
ATOM   650  N  NH2 . ARG A 1 84  ? -17.653 26.615  -20.518 1.00 18.13 ? 84  ARG A NH2 1 
ATOM   651  N  N   . TYR A 1 85  ? -16.431 20.860  -15.961 1.00 13.37 ? 85  TYR A N   1 
ATOM   652  C  CA  . TYR A 1 85  ? -15.376 21.022  -14.942 1.00 13.66 ? 85  TYR A CA  1 
ATOM   653  C  C   . TYR A 1 85  ? -14.264 21.843  -15.546 1.00 13.81 ? 85  TYR A C   1 
ATOM   654  O  O   . TYR A 1 85  ? -13.737 21.468  -16.605 1.00 16.69 ? 85  TYR A O   1 
ATOM   655  C  CB  . TYR A 1 85  ? -14.814 19.648  -14.546 1.00 14.17 ? 85  TYR A CB  1 
ATOM   656  C  CG  . TYR A 1 85  ? -15.732 18.894  -13.596 1.00 14.55 ? 85  TYR A CG  1 
ATOM   657  C  CD1 . TYR A 1 85  ? -16.813 18.177  -14.105 1.00 15.25 ? 85  TYR A CD1 1 
ATOM   658  C  CD2 . TYR A 1 85  ? -15.530 18.923  -12.214 1.00 13.19 ? 85  TYR A CD2 1 
ATOM   659  C  CE1 . TYR A 1 85  ? -17.682 17.530  -13.267 1.00 16.59 ? 85  TYR A CE1 1 
ATOM   660  C  CE2 . TYR A 1 85  ? -16.388 18.259  -11.343 1.00 14.66 ? 85  TYR A CE2 1 
ATOM   661  C  CZ  . TYR A 1 85  ? -17.472 17.550  -11.873 1.00 16.12 ? 85  TYR A CZ  1 
ATOM   662  O  OH  . TYR A 1 85  ? -18.358 16.834  -11.046 1.00 14.73 ? 85  TYR A OH  1 
ATOM   663  N  N   . SER A 1 86  ? -13.860 22.900  -14.866 1.00 13.71 ? 86  SER A N   1 
ATOM   664  C  CA  . SER A 1 86  ? -12.809 23.794  -15.372 1.00 13.49 ? 86  SER A CA  1 
ATOM   665  C  C   . SER A 1 86  ? -11.464 23.545  -14.698 1.00 13.20 ? 86  SER A C   1 
ATOM   666  O  O   . SER A 1 86  ? -11.416 23.338  -13.472 1.00 13.62 ? 86  SER A O   1 
ATOM   667  C  CB  . SER A 1 86  ? -13.221 25.255  -15.227 1.00 13.57 ? 86  SER A CB  1 
ATOM   668  O  OG  . SER A 1 86  ? -14.426 25.565  -15.977 1.00 13.44 ? 86  SER A OG  1 
ATOM   669  N  N   . ALA A 1 87  ? -10.387 23.620  -15.504 1.00 13.20 ? 87  ALA A N   1 
ATOM   670  C  CA  . ALA A 1 87  ? -9.000  23.332  -15.015 1.00 13.59 ? 87  ALA A CA  1 
ATOM   671  C  C   . ALA A 1 87  ? -8.587  24.301  -13.960 1.00 14.20 ? 87  ALA A C   1 
ATOM   672  O  O   . ALA A 1 87  ? -9.007  25.491  -13.996 1.00 16.01 ? 87  ALA A O   1 
ATOM   673  C  CB  . ALA A 1 87  ? -7.979  23.294  -16.177 1.00 12.89 ? 87  ALA A CB  1 
ATOM   674  N  N   . THR A 1 88  ? -7.800  23.828  -12.990 1.00 11.93 ? 88  THR A N   1 
ATOM   675  C  CA  . THR A 1 88  ? -7.202  24.732  -12.024 1.00 11.36 ? 88  THR A CA  1 
ATOM   676  C  C   . THR A 1 88  ? -5.673  24.663  -11.928 1.00 11.30 ? 88  THR A C   1 
ATOM   677  O  O   . THR A 1 88  ? -4.966  25.730  -11.749 1.00 9.78  ? 88  THR A O   1 
ATOM   678  C  CB  . THR A 1 88  ? -7.870  24.612  -10.615 1.00 12.28 ? 88  THR A CB  1 
ATOM   679  O  OG1 . THR A 1 88  ? -7.317  25.629  -9.774  1.00 14.69 ? 88  THR A OG1 1 
ATOM   680  C  CG2 . THR A 1 88  ? -7.618  23.233  -9.956  1.00 10.72 ? 88  THR A CG2 1 
ATOM   681  N  N   . GLN A 1 89  ? -5.128  23.444  -12.031 1.00 10.36 ? 89  GLN A N   1 
ATOM   682  C  CA  . GLN A 1 89  ? -3.668  23.302  -11.962 1.00 11.26 ? 89  GLN A CA  1 
ATOM   683  C  C   . GLN A 1 89  ? -3.297  21.881  -12.361 1.00 11.79 ? 89  GLN A C   1 
ATOM   684  O  O   . GLN A 1 89  ? -4.185  21.006  -12.427 1.00 11.89 ? 89  GLN A O   1 
ATOM   685  C  CB  . GLN A 1 89  ? -3.160  23.615  -10.513 1.00 13.32 ? 89  GLN A CB  1 
ATOM   686  C  CG  . GLN A 1 89  ? -3.863  22.868  -9.360  1.00 16.75 ? 89  GLN A CG  1 
ATOM   687  C  CD  . GLN A 1 89  ? -3.033  21.750  -8.734  1.00 19.09 ? 89  GLN A CD  1 
ATOM   688  O  OE1 . GLN A 1 89  ? -2.358  20.961  -9.410  1.00 17.30 ? 89  GLN A OE1 1 
ATOM   689  N  NE2 . GLN A 1 89  ? -3.099  21.662  -7.409  1.00 24.99 ? 89  GLN A NE2 1 
ATOM   690  N  N   . LEU A 1 90  ? -2.017  21.639  -12.636 1.00 10.56 ? 90  LEU A N   1 
ATOM   691  C  CA  . LEU A 1 90  ? -1.527  20.234  -12.774 1.00 10.57 ? 90  LEU A CA  1 
ATOM   692  C  C   . LEU A 1 90  ? -0.263  20.128  -11.918 1.00 10.73 ? 90  LEU A C   1 
ATOM   693  O  O   . LEU A 1 90  ? 0.329   21.153  -11.542 1.00 11.14 ? 90  LEU A O   1 
ATOM   694  C  CB  . LEU A 1 90  ? -1.292  19.866  -14.247 1.00 9.53  ? 90  LEU A CB  1 
ATOM   695  C  CG  . LEU A 1 90  ? -0.343  20.634  -15.182 1.00 10.95 ? 90  LEU A CG  1 
ATOM   696  C  CD1 . LEU A 1 90  ? 1.131   20.436  -14.717 1.00 10.55 ? 90  LEU A CD1 1 
ATOM   697  C  CD2 . LEU A 1 90  ? -0.465  20.192  -16.624 1.00 10.38 ? 90  LEU A CD2 1 
ATOM   698  N  N   . HIS A 1 91  ? 0.140   18.901  -11.593 1.00 10.71 ? 91  HIS A N   1 
ATOM   699  C  CA  . HIS A 1 91  ? 1.320   18.669  -10.767 1.00 11.17 ? 91  HIS A CA  1 
ATOM   700  C  C   . HIS A 1 91  ? 1.643   17.175  -10.876 1.00 10.73 ? 91  HIS A C   1 
ATOM   701  O  O   . HIS A 1 91  ? 0.875   16.385  -11.497 1.00 9.86  ? 91  HIS A O   1 
ATOM   702  C  CB  . HIS A 1 91  ? 1.042   19.074  -9.298  1.00 10.92 ? 91  HIS A CB  1 
ATOM   703  C  CG  . HIS A 1 91  ? -0.072  18.247  -8.667  1.00 11.13 ? 91  HIS A CG  1 
ATOM   704  N  ND1 . HIS A 1 91  ? -1.375  18.668  -8.601  1.00 10.76 ? 91  HIS A ND1 1 
ATOM   705  C  CD2 . HIS A 1 91  ? -0.061  16.935  -8.177  1.00 10.61 ? 91  HIS A CD2 1 
ATOM   706  C  CE1 . HIS A 1 91  ? -2.118  17.695  -8.061  1.00 11.23 ? 91  HIS A CE1 1 
ATOM   707  N  NE2 . HIS A 1 91  ? -1.296  16.648  -7.766  1.00 9.76  ? 91  HIS A NE2 1 
ATOM   708  N  N   . LEU A 1 92  ? 2.752   16.774  -10.254 1.00 10.11 ? 92  LEU A N   1 
ATOM   709  C  CA  . LEU A 1 92  ? 3.249   15.387  -10.330 1.00 10.18 ? 92  LEU A CA  1 
ATOM   710  C  C   . LEU A 1 92  ? 3.605   14.738  -8.962  1.00 9.22  ? 92  LEU A C   1 
ATOM   711  O  O   . LEU A 1 92  ? 3.712   15.426  -7.969  1.00 9.53  ? 92  LEU A O   1 
ATOM   712  C  CB  . LEU A 1 92  ? 4.425   15.276  -11.326 1.00 11.26 ? 92  LEU A CB  1 
ATOM   713  C  CG  . LEU A 1 92  ? 4.181   15.733  -12.784 1.00 10.65 ? 92  LEU A CG  1 
ATOM   714  C  CD1 . LEU A 1 92  ? 4.802   17.130  -12.978 1.00 12.00 ? 92  LEU A CD1 1 
ATOM   715  C  CD2 . LEU A 1 92  ? 4.915   14.799  -13.693 1.00 13.97 ? 92  LEU A CD2 1 
ATOM   716  N  N   . HIS A 1 93  ? 3.837   13.441  -8.994  1.00 9.02  ? 93  HIS A N   1 
ATOM   717  C  CA  . HIS A 1 93  ? 4.182   12.568  -7.847  1.00 9.10  ? 93  HIS A CA  1 
ATOM   718  C  C   . HIS A 1 93  ? 5.228   11.607  -8.354  1.00 8.70  ? 93  HIS A C   1 
ATOM   719  O  O   . HIS A 1 93  ? 5.095   11.097  -9.448  1.00 8.32  ? 93  HIS A O   1 
ATOM   720  C  CB  . HIS A 1 93  ? 2.976   11.744  -7.374  1.00 9.25  ? 93  HIS A CB  1 
ATOM   721  C  CG  . HIS A 1 93  ? 1.856   12.589  -6.878  1.00 8.66  ? 93  HIS A CG  1 
ATOM   722  N  ND1 . HIS A 1 93  ? 1.783   13.069  -5.600  1.00 8.89  ? 93  HIS A ND1 1 
ATOM   723  C  CD2 . HIS A 1 93  ? 0.755   13.076  -7.552  1.00 8.57  ? 93  HIS A CD2 1 
ATOM   724  C  CE1 . HIS A 1 93  ? 0.629   13.770  -5.471  1.00 8.72  ? 93  HIS A CE1 1 
ATOM   725  N  NE2 . HIS A 1 93  ? 0.023   13.787  -6.685  1.00 8.84  ? 93  HIS A NE2 1 
ATOM   726  N  N   . TRP A 1 94  ? 6.321   11.426  -7.608  1.00 8.77  ? 94  TRP A N   1 
ATOM   727  C  CA  . TRP A 1 94  ? 7.390   10.516  -8.033  1.00 8.70  ? 94  TRP A CA  1 
ATOM   728  C  C   . TRP A 1 94  ? 8.099   9.840   -6.874  1.00 9.53  ? 94  TRP A C   1 
ATOM   729  O  O   . TRP A 1 94  ? 7.793   10.121  -5.704  1.00 9.41  ? 94  TRP A O   1 
ATOM   730  C  CB  . TRP A 1 94  ? 8.360   11.321  -8.901  1.00 8.76  ? 94  TRP A CB  1 
ATOM   731  C  CG  . TRP A 1 94  ? 8.933   12.516  -8.153  1.00 8.35  ? 94  TRP A CG  1 
ATOM   732  C  CD1 . TRP A 1 94  ? 10.077  12.572  -7.301  1.00 9.04  ? 94  TRP A CD1 1 
ATOM   733  C  CD2 . TRP A 1 94  ? 8.417   13.891  -8.182  1.00 8.49  ? 94  TRP A CD2 1 
ATOM   734  N  NE1 . TRP A 1 94  ? 10.250  13.864  -6.829  1.00 8.57  ? 94  TRP A NE1 1 
ATOM   735  C  CE2 . TRP A 1 94  ? 9.285   14.684  -7.298  1.00 8.29  ? 94  TRP A CE2 1 
ATOM   736  C  CE3 . TRP A 1 94  ? 7.325   14.509  -8.763  1.00 8.09  ? 94  TRP A CE3 1 
ATOM   737  C  CZ2 . TRP A 1 94  ? 9.093   16.056  -7.125  1.00 8.19  ? 94  TRP A CZ2 1 
ATOM   738  C  CZ3 . TRP A 1 94  ? 7.144   15.885  -8.540  1.00 7.63  ? 94  TRP A CZ3 1 
ATOM   739  C  CH2 . TRP A 1 94  ? 8.011   16.627  -7.735  1.00 7.92  ? 94  TRP A CH2 1 
ATOM   740  N  N   . GLY A 1 95  ? 9.041   8.940   -7.187  1.00 9.65  ? 95  GLY A N   1 
ATOM   741  C  CA  . GLY A 1 95  ? 9.796   8.166   -6.225  1.00 9.99  ? 95  GLY A CA  1 
ATOM   742  C  C   . GLY A 1 95  ? 11.190  8.745   -5.987  1.00 9.94  ? 95  GLY A C   1 
ATOM   743  O  O   . GLY A 1 95  ? 11.307  9.904   -5.612  1.00 8.87  ? 95  GLY A O   1 
ATOM   744  N  N   . ASN A 1 96  ? 12.238  7.946   -6.196  1.00 9.71  ? 96  ASN A N   1 
ATOM   745  C  CA  . ASN A 1 96  ? 13.611  8.435   -5.944  1.00 11.39 ? 96  ASN A CA  1 
ATOM   746  C  C   . ASN A 1 96  ? 14.562  7.590   -6.760  1.00 12.21 ? 96  ASN A C   1 
ATOM   747  O  O   . ASN A 1 96  ? 14.172  6.503   -7.216  1.00 13.17 ? 96  ASN A O   1 
ATOM   748  C  CB  . ASN A 1 96  ? 13.935  8.306   -4.435  1.00 11.87 ? 96  ASN A CB  1 
ATOM   749  C  CG  . ASN A 1 96  ? 14.216  6.864   -4.008  1.00 12.00 ? 96  ASN A CG  1 
ATOM   750  O  OD1 . ASN A 1 96  ? 15.383  6.373   -4.084  1.00 14.44 ? 96  ASN A OD1 1 
ATOM   751  N  ND2 . ASN A 1 96  ? 13.184  6.190   -3.497  1.00 10.99 ? 96  ASN A ND2 1 
ATOM   752  N  N   . PRO A 1 97  ? 15.806  8.033   -6.932  1.00 13.89 ? 97  PRO A N   1 
ATOM   753  C  CA  . PRO A 1 97  ? 16.677  7.261   -7.862  1.00 13.99 ? 97  PRO A CA  1 
ATOM   754  C  C   . PRO A 1 97  ? 17.011  5.794   -7.479  1.00 15.17 ? 97  PRO A C   1 
ATOM   755  O  O   . PRO A 1 97  ? 17.309  5.002   -8.346  1.00 15.38 ? 97  PRO A O   1 
ATOM   756  C  CB  . PRO A 1 97  ? 17.945  8.145   -7.957  1.00 15.37 ? 97  PRO A CB  1 
ATOM   757  C  CG  . PRO A 1 97  ? 17.431  9.524   -7.630  1.00 14.71 ? 97  PRO A CG  1 
ATOM   758  C  CD  . PRO A 1 97  ? 16.460  9.280   -6.497  1.00 13.00 ? 97  PRO A CD  1 
ATOM   759  N  N   . ASN A 1 98  ? 17.031  5.458   -6.203  1.00 16.46 ? 98  ASN A N   1 
ATOM   760  C  CA  . ASN A 1 98  ? 17.263  4.082   -5.759  1.00 16.78 ? 98  ASN A CA  1 
ATOM   761  C  C   . ASN A 1 98  ? 16.019  3.197   -5.880  1.00 17.37 ? 98  ASN A C   1 
ATOM   762  O  O   . ASN A 1 98  ? 16.141  1.953   -5.885  1.00 17.92 ? 98  ASN A O   1 
ATOM   763  C  CB  . ASN A 1 98  ? 17.791  4.087   -4.324  1.00 20.76 ? 98  ASN A CB  1 
ATOM   764  C  CG  . ASN A 1 98  ? 19.049  4.949   -4.173  1.00 26.08 ? 98  ASN A CG  1 
ATOM   765  O  OD1 . ASN A 1 98  ? 20.043  4.733   -4.864  1.00 29.41 ? 98  ASN A OD1 1 
ATOM   766  N  ND2 . ASN A 1 98  ? 19.000  5.942   -3.291  1.00 31.39 ? 98  ASN A ND2 1 
ATOM   767  N  N   . ASP A 1 99  ? 14.834  3.805   -6.001  1.00 14.56 ? 99  ASP A N   1 
ATOM   768  C  CA  . ASP A 1 99  ? 13.601  3.024   -6.215  1.00 14.41 ? 99  ASP A CA  1 
ATOM   769  C  C   . ASP A 1 99  ? 12.626  3.852   -7.064  1.00 13.17 ? 99  ASP A C   1 
ATOM   770  O  O   . ASP A 1 99  ? 11.709  4.510   -6.519  1.00 13.70 ? 99  ASP A O   1 
ATOM   771  C  CB  . ASP A 1 99  ? 13.034  2.622   -4.842  1.00 15.41 ? 99  ASP A CB  1 
ATOM   772  C  CG  . ASP A 1 99  ? 12.000  1.528   -4.930  1.00 16.74 ? 99  ASP A CG  1 
ATOM   773  O  OD1 . ASP A 1 99  ? 11.485  1.257   -6.049  1.00 18.22 ? 99  ASP A OD1 1 
ATOM   774  O  OD2 . ASP A 1 99  ? 11.713  0.923   -3.856  1.00 18.80 ? 99  ASP A OD2 1 
ATOM   775  N  N   . PRO A 1 100 ? 12.846  3.857   -8.402  1.00 12.61 ? 100 PRO A N   1 
ATOM   776  C  CA  . PRO A 1 100 ? 12.185  4.839   -9.250  1.00 12.70 ? 100 PRO A CA  1 
ATOM   777  C  C   . PRO A 1 100 ? 10.758  4.476   -9.672  1.00 14.13 ? 100 PRO A C   1 
ATOM   778  O  O   . PRO A 1 100 ? 10.459  4.431   -10.884 1.00 15.32 ? 100 PRO A O   1 
ATOM   779  C  CB  . PRO A 1 100 ? 13.118  4.949   -10.451 1.00 12.59 ? 100 PRO A CB  1 
ATOM   780  C  CG  . PRO A 1 100 ? 13.648  3.547   -10.644 1.00 12.55 ? 100 PRO A CG  1 
ATOM   781  C  CD  . PRO A 1 100 ? 13.822  3.039   -9.176  1.00 11.65 ? 100 PRO A CD  1 
ATOM   782  N  N   . HIS A 1 101 ? 9.917   4.263   -8.647  1.00 16.04 ? 101 HIS A N   1 
ATOM   783  C  CA  . HIS A 1 101 ? 8.561   3.725   -8.777  1.00 14.38 ? 101 HIS A CA  1 
ATOM   784  C  C   . HIS A 1 101 ? 7.604   4.475   -7.878  1.00 14.98 ? 101 HIS A C   1 
ATOM   785  O  O   . HIS A 1 101 ? 7.160   3.925   -6.848  1.00 17.14 ? 101 HIS A O   1 
ATOM   786  C  CB  . HIS A 1 101 ? 8.584   2.262   -8.368  1.00 16.13 ? 101 HIS A CB  1 
ATOM   787  C  CG  . HIS A 1 101 ? 9.534   1.457   -9.181  1.00 17.61 ? 101 HIS A CG  1 
ATOM   788  N  ND1 . HIS A 1 101 ? 10.668  0.941   -8.663  1.00 18.11 ? 101 HIS A ND1 1 
ATOM   789  C  CD2 . HIS A 1 101 ? 9.526   1.142   -10.526 1.00 19.11 ? 101 HIS A CD2 1 
ATOM   790  C  CE1 . HIS A 1 101 ? 11.344  0.304   -9.629  1.00 17.94 ? 101 HIS A CE1 1 
ATOM   791  N  NE2 . HIS A 1 101 ? 10.661  0.448   -10.782 1.00 20.28 ? 101 HIS A NE2 1 
ATOM   792  N  N   . GLY A 1 102 ? 7.295   5.714   -8.245  1.00 11.46 ? 102 GLY A N   1 
ATOM   793  C  CA  . GLY A 1 102 ? 6.476   6.629   -7.445  1.00 11.56 ? 102 GLY A CA  1 
ATOM   794  C  C   . GLY A 1 102 ? 5.142   7.128   -8.009  1.00 11.09 ? 102 GLY A C   1 
ATOM   795  O  O   . GLY A 1 102 ? 4.675   8.202   -7.584  1.00 11.91 ? 102 GLY A O   1 
ATOM   796  N  N   . SER A 1 103 ? 4.455   6.321   -8.839  1.00 10.19 ? 103 SER A N   1 
ATOM   797  C  CA  . SER A 1 103 ? 3.053   6.623   -9.133  1.00 9.15  ? 103 SER A CA  1 
ATOM   798  C  C   . SER A 1 103 ? 2.176   6.503   -7.871  1.00 8.92  ? 103 SER A C   1 
ATOM   799  O  O   . SER A 1 103 ? 2.590   5.957   -6.832  1.00 9.20  ? 103 SER A O   1 
ATOM   800  C  CB  . SER A 1 103 ? 2.482   5.779   -10.300 1.00 8.70  ? 103 SER A CB  1 
ATOM   801  O  OG  . SER A 1 103 ? 2.471   4.383   -9.929  1.00 8.89  ? 103 SER A OG  1 
ATOM   802  N  N   . GLU A 1 104 ? 0.975   7.056   -7.938  1.00 8.36  ? 104 GLU A N   1 
ATOM   803  C  CA  . GLU A 1 104 ? 0.038   6.952   -6.820  1.00 8.45  ? 104 GLU A CA  1 
ATOM   804  C  C   . GLU A 1 104 ? -0.863  5.711   -7.036  1.00 7.97  ? 104 GLU A C   1 
ATOM   805  O  O   . GLU A 1 104 ? -0.938  4.798   -6.190  1.00 8.24  ? 104 GLU A O   1 
ATOM   806  C  CB  . GLU A 1 104 ? -0.802  8.213   -6.781  1.00 8.33  ? 104 GLU A CB  1 
ATOM   807  C  CG  . GLU A 1 104 ? 0.129   9.414   -6.462  1.00 9.30  ? 104 GLU A CG  1 
ATOM   808  C  CD  . GLU A 1 104 ? -0.494  10.270  -5.388  1.00 10.24 ? 104 GLU A CD  1 
ATOM   809  O  OE1 . GLU A 1 104 ? -1.435  10.942  -5.742  1.00 10.24 ? 104 GLU A OE1 1 
ATOM   810  O  OE2 . GLU A 1 104 ? 0.001   10.358  -4.252  1.00 10.62 ? 104 GLU A OE2 1 
ATOM   811  N  N   . HIS A 1 105 ? -1.535  5.691   -8.189  1.00 7.64  ? 105 HIS A N   1 
ATOM   812  C  CA  . HIS A 1 105 ? -2.315  4.519   -8.542  1.00 7.85  ? 105 HIS A CA  1 
ATOM   813  C  C   . HIS A 1 105 ? -1.342  3.419   -9.034  1.00 8.63  ? 105 HIS A C   1 
ATOM   814  O  O   . HIS A 1 105 ? -0.276  3.734   -9.591  1.00 8.75  ? 105 HIS A O   1 
ATOM   815  C  CB  . HIS A 1 105 ? -3.303  4.894   -9.636  1.00 7.98  ? 105 HIS A CB  1 
ATOM   816  C  CG  . HIS A 1 105 ? -4.417  5.770   -9.178  1.00 7.74  ? 105 HIS A CG  1 
ATOM   817  N  ND1 . HIS A 1 105 ? -4.357  7.116   -9.247  1.00 8.13  ? 105 HIS A ND1 1 
ATOM   818  C  CD2 . HIS A 1 105 ? -5.639  5.454   -8.567  1.00 7.86  ? 105 HIS A CD2 1 
ATOM   819  C  CE1 . HIS A 1 105 ? -5.481  7.630   -8.688  1.00 7.56  ? 105 HIS A CE1 1 
ATOM   820  N  NE2 . HIS A 1 105 ? -6.266  6.603   -8.304  1.00 7.50  ? 105 HIS A NE2 1 
ATOM   821  N  N   . THR A 1 106 ? -1.729  2.146   -8.861  1.00 9.28  ? 106 THR A N   1 
ATOM   822  C  CA  . THR A 1 106 ? -0.939  1.021   -9.311  1.00 9.91  ? 106 THR A CA  1 
ATOM   823  C  C   . THR A 1 106 ? -1.918  0.155   -10.132 1.00 10.33 ? 106 THR A C   1 
ATOM   824  O  O   . THR A 1 106 ? -3.124  0.336   -10.023 1.00 10.20 ? 106 THR A O   1 
ATOM   825  C  CB  . THR A 1 106 ? -0.379  0.194   -8.128  1.00 10.69 ? 106 THR A CB  1 
ATOM   826  O  OG1 . THR A 1 106 ? -1.440  -0.306  -7.285  1.00 11.19 ? 106 THR A OG1 1 
ATOM   827  C  CG2 . THR A 1 106 ? 0.564   1.036   -7.244  1.00 10.21 ? 106 THR A CG2 1 
ATOM   828  N  N   . VAL A 1 107 ? -1.400  -0.693  -10.993 1.00 10.99 ? 107 VAL A N   1 
ATOM   829  C  CA  . VAL A 1 107 ? -2.286  -1.526  -11.845 1.00 12.16 ? 107 VAL A CA  1 
ATOM   830  C  C   . VAL A 1 107 ? -1.782  -2.945  -11.662 1.00 12.64 ? 107 VAL A C   1 
ATOM   831  O  O   . VAL A 1 107 ? -0.580  -3.218  -11.883 1.00 15.57 ? 107 VAL A O   1 
ATOM   832  C  CB  . VAL A 1 107 ? -2.140  -1.144  -13.344 1.00 12.71 ? 107 VAL A CB  1 
ATOM   833  C  CG1 . VAL A 1 107 ? -2.821  -2.207  -14.263 1.00 13.25 ? 107 VAL A CG1 1 
ATOM   834  C  CG2 . VAL A 1 107 ? -2.618  0.262   -13.620 1.00 14.47 ? 107 VAL A CG2 1 
ATOM   835  N  N   . SER A 1 108 ? -2.667  -3.826  -11.211 1.00 13.45 ? 108 SER A N   1 
ATOM   836  C  CA  . SER A 1 108 ? -2.319  -5.220  -10.881 1.00 14.35 ? 108 SER A CA  1 
ATOM   837  C  C   . SER A 1 108 ? -1.065  -5.240  -10.008 1.00 13.56 ? 108 SER A C   1 
ATOM   838  O  O   . SER A 1 108 ? -0.153  -6.024  -10.252 1.00 12.28 ? 108 SER A O   1 
ATOM   839  C  CB  . SER A 1 108 ? -2.079  -5.922  -12.205 1.00 14.42 ? 108 SER A CB  1 
ATOM   840  O  OG  . SER A 1 108 ? -3.331  -5.905  -12.901 1.00 16.78 ? 108 SER A OG  1 
ATOM   841  N  N   . GLY A 1 109 ? -1.032  -4.305  -9.073  1.00 14.92 ? 109 GLY A N   1 
ATOM   842  C  CA  . GLY A 1 109 ? 0.071   -4.234  -8.098  1.00 16.47 ? 109 GLY A CA  1 
ATOM   843  C  C   . GLY A 1 109 ? 1.351   -3.547  -8.566  1.00 18.70 ? 109 GLY A C   1 
ATOM   844  O  O   . GLY A 1 109 ? 2.271   -3.327  -7.707  1.00 19.24 ? 109 GLY A O   1 
ATOM   845  N  N   A GLN A 1 110 ? 1.412   -3.228  -9.880  0.50 17.89 ? 110 GLN A N   1 
ATOM   846  N  N   B GLN A 1 110 ? 1.444   -3.224  -9.852  0.50 18.98 ? 110 GLN A N   1 
ATOM   847  C  CA  A GLN A 1 110 ? 2.511   -2.451  -10.566 0.50 16.80 ? 110 GLN A CA  1 
ATOM   848  C  CA  B GLN A 1 110 ? 2.636   -2.547  -10.362 0.50 18.58 ? 110 GLN A CA  1 
ATOM   849  C  C   A GLN A 1 110 ? 2.539   -0.953  -10.256 0.50 16.12 ? 110 GLN A C   1 
ATOM   850  C  C   B GLN A 1 110 ? 2.571   -1.029  -10.227 0.50 17.13 ? 110 GLN A C   1 
ATOM   851  O  O   A GLN A 1 110 ? 1.633   -0.234  -10.659 0.50 15.43 ? 110 GLN A O   1 
ATOM   852  O  O   B GLN A 1 110 ? 1.643   -0.393  -10.705 0.50 16.37 ? 110 GLN A O   1 
ATOM   853  C  CB  A GLN A 1 110 ? 2.494   -2.605  -12.129 0.50 16.53 ? 110 GLN A CB  1 
ATOM   854  C  CB  B GLN A 1 110 ? 2.906   -2.889  -11.824 0.50 19.83 ? 110 GLN A CB  1 
ATOM   855  C  CG  A GLN A 1 110 ? 3.136   -1.414  -12.887 0.50 16.35 ? 110 GLN A CG  1 
ATOM   856  C  CG  B GLN A 1 110 ? 2.068   -4.004  -12.431 0.50 21.51 ? 110 GLN A CG  1 
ATOM   857  C  CD  A GLN A 1 110 ? 3.604   -1.635  -14.353 0.50 16.56 ? 110 GLN A CD  1 
ATOM   858  C  CD  B GLN A 1 110 ? 1.787   -3.744  -13.910 0.50 21.29 ? 110 GLN A CD  1 
ATOM   859  O  OE1 A GLN A 1 110 ? 4.658   -1.128  -14.754 0.50 16.29 ? 110 GLN A OE1 1 
ATOM   860  O  OE1 B GLN A 1 110 ? 0.624   -3.805  -14.382 0.50 19.33 ? 110 GLN A OE1 1 
ATOM   861  N  NE2 A GLN A 1 110 ? 2.804   -2.311  -15.161 0.50 14.73 ? 110 GLN A NE2 1 
ATOM   862  N  NE2 B GLN A 1 110 ? 2.859   -3.460  -14.662 0.50 21.76 ? 110 GLN A NE2 1 
ATOM   863  N  N   . HIS A 1 111 ? 3.604   -0.467  -9.613  1.00 15.34 ? 111 HIS A N   1 
ATOM   864  C  CA  . HIS A 1 111 ? 3.826   0.982   -9.535  1.00 16.32 ? 111 HIS A CA  1 
ATOM   865  C  C   . HIS A 1 111 ? 4.515   1.495   -10.752 1.00 16.72 ? 111 HIS A C   1 
ATOM   866  O  O   . HIS A 1 111 ? 5.548   0.951   -11.122 1.00 19.02 ? 111 HIS A O   1 
ATOM   867  C  CB  . HIS A 1 111 ? 4.821   1.240   -8.474  1.00 18.72 ? 111 HIS A CB  1 
ATOM   868  C  CG  . HIS A 1 111 ? 4.261   1.796   -7.257  1.00 20.94 ? 111 HIS A CG  1 
ATOM   869  N  ND1 . HIS A 1 111 ? 3.974   1.012   -6.178  1.00 24.99 ? 111 HIS A ND1 1 
ATOM   870  C  CD2 . HIS A 1 111 ? 3.953   3.110   -6.908  1.00 18.86 ? 111 HIS A CD2 1 
ATOM   871  C  CE1 . HIS A 1 111 ? 3.516   1.803   -5.177  1.00 24.28 ? 111 HIS A CE1 1 
ATOM   872  N  NE2 . HIS A 1 111 ? 3.515   3.093   -5.638  1.00 25.32 ? 111 HIS A NE2 1 
ATOM   873  N  N   . PHE A 1 112 ? 4.006   2.556   -11.379 1.00 13.36 ? 112 PHE A N   1 
ATOM   874  C  CA  . PHE A 1 112 ? 4.761   3.173   -12.488 1.00 12.22 ? 112 PHE A CA  1 
ATOM   875  C  C   . PHE A 1 112 ? 5.752   4.170   -11.876 1.00 10.55 ? 112 PHE A C   1 
ATOM   876  O  O   . PHE A 1 112 ? 5.809   4.324   -10.625 1.00 11.43 ? 112 PHE A O   1 
ATOM   877  C  CB  . PHE A 1 112 ? 3.819   3.819   -13.475 1.00 13.61 ? 112 PHE A CB  1 
ATOM   878  C  CG  . PHE A 1 112 ? 2.943   2.808   -14.172 1.00 16.09 ? 112 PHE A CG  1 
ATOM   879  C  CD1 . PHE A 1 112 ? 1.827   2.250   -13.545 1.00 16.17 ? 112 PHE A CD1 1 
ATOM   880  C  CD2 . PHE A 1 112 ? 3.290   2.382   -15.423 1.00 17.65 ? 112 PHE A CD2 1 
ATOM   881  C  CE1 . PHE A 1 112 ? 1.035   1.296   -14.207 1.00 18.47 ? 112 PHE A CE1 1 
ATOM   882  C  CE2 . PHE A 1 112 ? 2.522   1.416   -16.082 1.00 19.84 ? 112 PHE A CE2 1 
ATOM   883  C  CZ  . PHE A 1 112 ? 1.416   0.856   -15.457 1.00 18.30 ? 112 PHE A CZ  1 
ATOM   884  N  N   . ALA A 1 113 ? 6.581   4.744   -12.744 1.00 9.51  ? 113 ALA A N   1 
ATOM   885  C  CA  . ALA A 1 113 ? 7.683   5.638   -12.350 1.00 9.20  ? 113 ALA A CA  1 
ATOM   886  C  C   . ALA A 1 113 ? 7.162   6.919   -11.678 1.00 8.83  ? 113 ALA A C   1 
ATOM   887  O  O   . ALA A 1 113 ? 7.767   7.375   -10.707 1.00 7.95  ? 113 ALA A O   1 
ATOM   888  C  CB  . ALA A 1 113 ? 8.567   5.993   -13.551 1.00 8.92  ? 113 ALA A CB  1 
ATOM   889  N  N   . ALA A 1 114 ? 6.055   7.462   -12.201 1.00 8.80  ? 114 ALA A N   1 
ATOM   890  C  CA  . ALA A 1 114 ? 5.508   8.746   -11.788 1.00 9.05  ? 114 ALA A CA  1 
ATOM   891  C  C   . ALA A 1 114 ? 4.046   8.860   -12.274 1.00 9.26  ? 114 ALA A C   1 
ATOM   892  O  O   . ALA A 1 114 ? 3.501   7.936   -12.832 1.00 9.87  ? 114 ALA A O   1 
ATOM   893  C  CB  . ALA A 1 114 ? 6.357   9.925   -12.354 1.00 8.38  ? 114 ALA A CB  1 
ATOM   894  N  N   . GLU A 1 115 ? 3.407   9.971   -11.935 1.00 10.72 ? 115 GLU A N   1 
ATOM   895  C  CA  . GLU A 1 115 ? 1.950   10.184  -12.217 1.00 9.64  ? 115 GLU A CA  1 
ATOM   896  C  C   . GLU A 1 115 ? 1.703   11.684  -12.313 1.00 10.02 ? 115 GLU A C   1 
ATOM   897  O  O   . GLU A 1 115 ? 2.133   12.459  -11.446 1.00 10.95 ? 115 GLU A O   1 
ATOM   898  C  CB  . GLU A 1 115 ? 1.073   9.609   -11.085 1.00 10.44 ? 115 GLU A CB  1 
ATOM   899  C  CG  . GLU A 1 115 ? -0.422  9.495   -11.463 1.00 9.77  ? 115 GLU A CG  1 
ATOM   900  C  CD  . GLU A 1 115 ? -1.234  8.521   -10.581 1.00 9.54  ? 115 GLU A CD  1 
ATOM   901  O  OE1 . GLU A 1 115 ? -2.392  8.835   -10.235 1.00 9.88  ? 115 GLU A OE1 1 
ATOM   902  O  OE2 . GLU A 1 115 ? -0.700  7.458   -10.229 1.00 8.35  ? 115 GLU A OE2 1 
ATOM   903  N  N   . LEU A 1 116 ? 0.982   12.073  -13.347 1.00 8.66  ? 116 LEU A N   1 
ATOM   904  C  CA  . LEU A 1 116 ? 0.598   13.478  -13.568 1.00 8.97  ? 116 LEU A CA  1 
ATOM   905  C  C   . LEU A 1 116 ? -0.869  13.574  -13.167 1.00 8.94  ? 116 LEU A C   1 
ATOM   906  O  O   . LEU A 1 116 ? -1.694  12.693  -13.554 1.00 9.32  ? 116 LEU A O   1 
ATOM   907  C  CB  . LEU A 1 116 ? 0.718   13.781  -15.106 1.00 8.14  ? 116 LEU A CB  1 
ATOM   908  C  CG  . LEU A 1 116 ? 0.138   15.181  -15.560 1.00 7.70  ? 116 LEU A CG  1 
ATOM   909  C  CD1 . LEU A 1 116 ? 1.051   16.282  -15.045 1.00 8.88  ? 116 LEU A CD1 1 
ATOM   910  C  CD2 . LEU A 1 116 ? -0.019  15.389  -17.068 1.00 7.93  ? 116 LEU A CD2 1 
ATOM   911  N  N   . HIS A 1 117 ? -1.217  14.637  -12.457 1.00 8.93  ? 117 HIS A N   1 
ATOM   912  C  CA  . HIS A 1 117 ? -2.635  14.949  -12.195 1.00 9.11  ? 117 HIS A CA  1 
ATOM   913  C  C   . HIS A 1 117 ? -3.051  16.303  -12.732 1.00 9.12  ? 117 HIS A C   1 
ATOM   914  O  O   . HIS A 1 117 ? -2.356  17.305  -12.521 1.00 8.83  ? 117 HIS A O   1 
ATOM   915  C  CB  . HIS A 1 117 ? -2.956  14.927  -10.705 1.00 9.03  ? 117 HIS A CB  1 
ATOM   916  C  CG  . HIS A 1 117 ? -2.797  13.565  -10.078 1.00 8.91  ? 117 HIS A CG  1 
ATOM   917  N  ND1 . HIS A 1 117 ? -2.396  13.412  -8.798  1.00 9.68  ? 117 HIS A ND1 1 
ATOM   918  C  CD2 . HIS A 1 117 ? -3.112  12.283  -10.563 1.00 8.41  ? 117 HIS A CD2 1 
ATOM   919  C  CE1 . HIS A 1 117 ? -2.339  12.075  -8.521  1.00 8.82  ? 117 HIS A CE1 1 
ATOM   920  N  NE2 . HIS A 1 117 ? -2.825  11.406  -9.605  1.00 7.91  ? 117 HIS A NE2 1 
ATOM   921  N  N   . ILE A 1 118 ? -4.149  16.317  -13.473 1.00 8.88  ? 118 ILE A N   1 
ATOM   922  C  CA  . ILE A 1 118 ? -4.712  17.560  -14.036 1.00 9.37  ? 118 ILE A CA  1 
ATOM   923  C  C   . ILE A 1 118 ? -6.050  17.791  -13.309 1.00 9.85  ? 118 ILE A C   1 
ATOM   924  O  O   . ILE A 1 118 ? -6.988  16.970  -13.425 1.00 11.11 ? 118 ILE A O   1 
ATOM   925  C  CB  . ILE A 1 118 ? -4.924  17.495  -15.566 1.00 9.36  ? 118 ILE A CB  1 
ATOM   926  C  CG1 . ILE A 1 118 ? -3.617  17.124  -16.297 1.00 9.08  ? 118 ILE A CG1 1 
ATOM   927  C  CG2 . ILE A 1 118 ? -5.324  18.892  -16.096 1.00 9.25  ? 118 ILE A CG2 1 
ATOM   928  C  CD1 . ILE A 1 118 ? -3.913  16.962  -17.778 1.00 9.66  ? 118 ILE A CD1 1 
ATOM   929  N  N   . VAL A 1 119 ? -6.073  18.819  -12.486 1.00 10.13 ? 119 VAL A N   1 
ATOM   930  C  CA  . VAL A 1 119 ? -7.129  19.006  -11.484 1.00 10.81 ? 119 VAL A CA  1 
ATOM   931  C  C   . VAL A 1 119 ? -8.141  20.020  -12.029 1.00 10.97 ? 119 VAL A C   1 
ATOM   932  O  O   . VAL A 1 119 ? -7.735  21.082  -12.508 1.00 10.28 ? 119 VAL A O   1 
ATOM   933  C  CB  . VAL A 1 119 ? -6.544  19.508  -10.130 1.00 10.75 ? 119 VAL A CB  1 
ATOM   934  C  CG1 . VAL A 1 119 ? -7.660  19.747  -9.091  1.00 10.85 ? 119 VAL A CG1 1 
ATOM   935  C  CG2 . VAL A 1 119 ? -5.517  18.503  -9.577  1.00 11.70 ? 119 VAL A CG2 1 
ATOM   936  N  N   . HIS A 1 120 ? -9.425  19.628  -12.012 1.00 11.43 ? 120 HIS A N   1 
ATOM   937  C  CA  . HIS A 1 120 ? -10.574 20.461  -12.443 1.00 11.77 ? 120 HIS A CA  1 
ATOM   938  C  C   . HIS A 1 120 ? -11.617 20.576  -11.335 1.00 11.95 ? 120 HIS A C   1 
ATOM   939  O  O   . HIS A 1 120 ? -11.704 19.715  -10.430 1.00 11.01 ? 120 HIS A O   1 
ATOM   940  C  CB  . HIS A 1 120 ? -11.244 19.920  -13.750 1.00 11.16 ? 120 HIS A CB  1 
ATOM   941  C  CG  . HIS A 1 120 ? -10.276 19.600  -14.894 1.00 11.28 ? 120 HIS A CG  1 
ATOM   942  N  ND1 . HIS A 1 120 ? -9.416  18.540  -14.858 1.00 11.72 ? 120 HIS A ND1 1 
ATOM   943  C  CD2 . HIS A 1 120 ? -10.105 20.189  -16.125 1.00 11.80 ? 120 HIS A CD2 1 
ATOM   944  C  CE1 . HIS A 1 120 ? -8.705  18.490  -15.998 1.00 11.91 ? 120 HIS A CE1 1 
ATOM   945  N  NE2 . HIS A 1 120 ? -9.120  19.502  -16.782 1.00 12.99 ? 120 HIS A NE2 1 
ATOM   946  N  N   . TYR A 1 121 ? -12.392 21.674  -11.352 1.00 12.33 ? 121 TYR A N   1 
ATOM   947  C  CA  . TYR A 1 121 ? -13.489 21.866  -10.404 1.00 15.55 ? 121 TYR A CA  1 
ATOM   948  C  C   . TYR A 1 121 ? -14.814 22.047  -11.169 1.00 15.45 ? 121 TYR A C   1 
ATOM   949  O  O   . TYR A 1 121 ? -14.827 22.433  -12.356 1.00 13.51 ? 121 TYR A O   1 
ATOM   950  C  CB  . TYR A 1 121 ? -13.234 23.048  -9.469  1.00 16.94 ? 121 TYR A CB  1 
ATOM   951  C  CG  . TYR A 1 121 ? -13.299 24.446  -10.141 1.00 20.69 ? 121 TYR A CG  1 
ATOM   952  C  CD1 . TYR A 1 121 ? -14.423 25.297  -9.970  1.00 22.13 ? 121 TYR A CD1 1 
ATOM   953  C  CD2 . TYR A 1 121 ? -12.244 24.917  -10.898 1.00 20.74 ? 121 TYR A CD2 1 
ATOM   954  C  CE1 . TYR A 1 121 ? -14.452 26.549  -10.578 1.00 24.89 ? 121 TYR A CE1 1 
ATOM   955  C  CE2 . TYR A 1 121 ? -12.271 26.197  -11.503 1.00 23.37 ? 121 TYR A CE2 1 
ATOM   956  C  CZ  . TYR A 1 121 ? -13.357 26.995  -11.355 1.00 24.90 ? 121 TYR A CZ  1 
ATOM   957  O  OH  . TYR A 1 121 ? -13.330 28.250  -11.996 1.00 27.46 ? 121 TYR A OH  1 
ATOM   958  N  N   . ASN A 1 122 ? -15.903 21.717  -10.500 1.00 15.83 ? 122 ASN A N   1 
ATOM   959  C  CA  . ASN A 1 122 ? -17.236 21.856  -11.083 1.00 17.37 ? 122 ASN A CA  1 
ATOM   960  C  C   . ASN A 1 122 ? -17.675 23.339  -11.095 1.00 16.42 ? 122 ASN A C   1 
ATOM   961  O  O   . ASN A 1 122 ? -18.164 23.888  -10.115 1.00 16.40 ? 122 ASN A O   1 
ATOM   962  C  CB  . ASN A 1 122 ? -18.238 20.994  -10.306 1.00 18.60 ? 122 ASN A CB  1 
ATOM   963  C  CG  . ASN A 1 122 ? -19.623 21.006  -10.925 1.00 19.91 ? 122 ASN A CG  1 
ATOM   964  O  OD1 . ASN A 1 122 ? -19.994 21.939  -11.664 1.00 19.88 ? 122 ASN A OD1 1 
ATOM   965  N  ND2 . ASN A 1 122 ? -20.406 19.961  -10.634 1.00 20.00 ? 122 ASN A ND2 1 
ATOM   966  N  N   . SER A 1 123 ? -17.498 23.970  -12.235 1.00 16.23 ? 123 SER A N   1 
ATOM   967  C  CA  . SER A 1 123 ? -17.661 25.428  -12.326 1.00 16.03 ? 123 SER A CA  1 
ATOM   968  C  C   . SER A 1 123 ? -19.095 25.816  -12.689 1.00 16.81 ? 123 SER A C   1 
ATOM   969  O  O   . SER A 1 123 ? -19.455 27.017  -12.614 1.00 16.84 ? 123 SER A O   1 
ATOM   970  C  CB  . SER A 1 123 ? -16.692 25.982  -13.372 1.00 15.49 ? 123 SER A CB  1 
ATOM   971  O  OG  . SER A 1 123 ? -16.859 25.323  -14.625 1.00 12.84 ? 123 SER A OG  1 
ATOM   972  N  N   . ASP A 1 124 ? -19.889 24.830  -13.117 1.00 16.31 ? 124 ASP A N   1 
ATOM   973  C  CA  . ASP A 1 124 ? -21.338 25.049  -13.258 1.00 18.72 ? 124 ASP A CA  1 
ATOM   974  C  C   . ASP A 1 124 ? -21.974 25.261  -11.854 1.00 21.01 ? 124 ASP A C   1 
ATOM   975  O  O   . ASP A 1 124 ? -22.887 26.078  -11.691 1.00 22.29 ? 124 ASP A O   1 
ATOM   976  C  CB  . ASP A 1 124 ? -22.069 23.898  -13.964 1.00 17.60 ? 124 ASP A CB  1 
ATOM   977  C  CG  . ASP A 1 124 ? -21.790 23.809  -15.443 1.00 17.20 ? 124 ASP A CG  1 
ATOM   978  O  OD1 . ASP A 1 124 ? -21.317 24.799  -16.057 1.00 17.83 ? 124 ASP A OD1 1 
ATOM   979  O  OD2 . ASP A 1 124 ? -22.096 22.723  -16.040 1.00 18.48 ? 124 ASP A OD2 1 
ATOM   980  N  N   . LEU A 1 125 ? -21.495 24.530  -10.843 1.00 20.81 ? 125 LEU A N   1 
ATOM   981  C  CA  . LEU A 1 125 ? -22.130 24.532  -9.524  1.00 22.35 ? 125 LEU A CA  1 
ATOM   982  C  C   . LEU A 1 125 ? -21.414 25.455  -8.553  1.00 24.04 ? 125 LEU A C   1 
ATOM   983  O  O   . LEU A 1 125 ? -22.042 26.050  -7.685  1.00 23.58 ? 125 LEU A O   1 
ATOM   984  C  CB  . LEU A 1 125 ? -22.219 23.101  -8.970  1.00 23.74 ? 125 LEU A CB  1 
ATOM   985  C  CG  . LEU A 1 125 ? -23.295 22.088  -9.468  1.00 26.63 ? 125 LEU A CG  1 
ATOM   986  C  CD1 . LEU A 1 125 ? -24.535 22.038  -8.599  1.00 27.09 ? 125 LEU A CD1 1 
ATOM   987  C  CD2 . LEU A 1 125 ? -23.733 22.266  -10.913 1.00 25.75 ? 125 LEU A CD2 1 
ATOM   988  N  N   . TYR A 1 126 ? -20.113 25.650  -8.717  1.00 24.28 ? 126 TYR A N   1 
ATOM   989  C  CA  . TYR A 1 126 ? -19.387 26.443  -7.720  1.00 23.65 ? 126 TYR A CA  1 
ATOM   990  C  C   . TYR A 1 126 ? -18.566 27.593  -8.295  1.00 24.61 ? 126 TYR A C   1 
ATOM   991  O  O   . TYR A 1 126 ? -18.164 27.540  -9.457  1.00 23.41 ? 126 TYR A O   1 
ATOM   992  C  CB  . TYR A 1 126 ? -18.552 25.512  -6.839  1.00 23.71 ? 126 TYR A CB  1 
ATOM   993  C  CG  . TYR A 1 126 ? -19.371 24.338  -6.356  1.00 24.29 ? 126 TYR A CG  1 
ATOM   994  C  CD1 . TYR A 1 126 ? -19.231 23.083  -6.948  1.00 23.15 ? 126 TYR A CD1 1 
ATOM   995  C  CD2 . TYR A 1 126 ? -20.310 24.495  -5.323  1.00 24.07 ? 126 TYR A CD2 1 
ATOM   996  C  CE1 . TYR A 1 126 ? -19.988 22.006  -6.524  1.00 24.50 ? 126 TYR A CE1 1 
ATOM   997  C  CE2 . TYR A 1 126 ? -21.073 23.426  -4.885  1.00 24.58 ? 126 TYR A CE2 1 
ATOM   998  C  CZ  . TYR A 1 126 ? -20.908 22.193  -5.485  1.00 25.99 ? 126 TYR A CZ  1 
ATOM   999  O  OH  . TYR A 1 126 ? -21.675 21.152  -5.077  1.00 24.72 ? 126 TYR A OH  1 
ATOM   1000 N  N   . PRO A 1 127 ? -18.324 28.644  -7.482  1.00 26.56 ? 127 PRO A N   1 
ATOM   1001 C  CA  . PRO A 1 127 ? -17.539 29.844  -7.871  1.00 28.20 ? 127 PRO A CA  1 
ATOM   1002 C  C   . PRO A 1 127 ? -16.085 29.588  -8.332  1.00 29.19 ? 127 PRO A C   1 
ATOM   1003 O  O   . PRO A 1 127 ? -15.655 30.118  -9.365  1.00 32.15 ? 127 PRO A O   1 
ATOM   1004 C  CB  . PRO A 1 127 ? -17.504 30.659  -6.568  1.00 27.98 ? 127 PRO A CB  1 
ATOM   1005 C  CG  . PRO A 1 127 ? -18.730 30.282  -5.863  1.00 26.20 ? 127 PRO A CG  1 
ATOM   1006 C  CD  . PRO A 1 127 ? -18.946 28.817  -6.163  1.00 26.50 ? 127 PRO A CD  1 
ATOM   1007 N  N   . ASP A 1 128 ? -15.324 28.814  -7.556  1.00 27.92 ? 128 ASP A N   1 
ATOM   1008 C  CA  . ASP A 1 128 ? -13.891 28.611  -7.813  1.00 28.84 ? 128 ASP A CA  1 
ATOM   1009 C  C   . ASP A 1 128 ? -13.487 27.236  -7.204  1.00 28.05 ? 128 ASP A C   1 
ATOM   1010 O  O   . ASP A 1 128 ? -14.339 26.604  -6.582  1.00 25.19 ? 128 ASP A O   1 
ATOM   1011 C  CB  . ASP A 1 128 ? -13.107 29.792  -7.203  1.00 29.06 ? 128 ASP A CB  1 
ATOM   1012 C  CG  . ASP A 1 128 ? -13.673 30.219  -5.876  1.00 33.44 ? 128 ASP A CG  1 
ATOM   1013 O  OD1 . ASP A 1 128 ? -13.894 29.330  -5.050  1.00 33.67 ? 128 ASP A OD1 1 
ATOM   1014 O  OD2 . ASP A 1 128 ? -13.911 31.422  -5.634  1.00 36.93 ? 128 ASP A OD2 1 
ATOM   1015 N  N   . ALA A 1 129 ? -12.221 26.797  -7.366  1.00 27.94 ? 129 ALA A N   1 
ATOM   1016 C  CA  . ALA A 1 129 ? -11.755 25.484  -6.867  1.00 27.05 ? 129 ALA A CA  1 
ATOM   1017 C  C   . ALA A 1 129 ? -11.817 25.359  -5.338  1.00 28.37 ? 129 ALA A C   1 
ATOM   1018 O  O   . ALA A 1 129 ? -12.292 24.346  -4.808  1.00 28.99 ? 129 ALA A O   1 
ATOM   1019 C  CB  . ALA A 1 129 ? -10.349 25.159  -7.390  1.00 25.45 ? 129 ALA A CB  1 
ATOM   1020 N  N   . SER A 1 130 ? -11.387 26.398  -4.623  1.00 30.38 ? 130 SER A N   1 
ATOM   1021 C  CA  . SER A 1 130 ? -11.333 26.285  -3.160  1.00 34.20 ? 130 SER A CA  1 
ATOM   1022 C  C   . SER A 1 130 ? -12.706 26.157  -2.518  1.00 33.85 ? 130 SER A C   1 
ATOM   1023 O  O   . SER A 1 130 ? -12.841 25.454  -1.528  1.00 32.68 ? 130 SER A O   1 
ATOM   1024 C  CB  . SER A 1 130 ? -10.453 27.361  -2.492  1.00 35.67 ? 130 SER A CB  1 
ATOM   1025 O  OG  . SER A 1 130 ? -11.023 28.649  -2.554  1.00 36.47 ? 130 SER A OG  1 
ATOM   1026 N  N   . THR A 1 131 ? -13.744 26.782  -3.079  1.00 33.37 ? 131 THR A N   1 
ATOM   1027 C  CA  . THR A 1 131 ? -15.099 26.436  -2.600  1.00 28.64 ? 131 THR A CA  1 
ATOM   1028 C  C   . THR A 1 131 ? -15.675 25.121  -3.182  1.00 27.38 ? 131 THR A C   1 
ATOM   1029 O  O   . THR A 1 131 ? -16.453 24.418  -2.513  1.00 24.69 ? 131 THR A O   1 
ATOM   1030 C  CB  . THR A 1 131 ? -16.105 27.645  -2.486  1.00 30.89 ? 131 THR A CB  1 
ATOM   1031 O  OG1 . THR A 1 131 ? -17.367 27.326  -3.083  1.00 31.69 ? 131 THR A OG1 1 
ATOM   1032 C  CG2 . THR A 1 131 ? -15.555 28.961  -3.076  1.00 28.63 ? 131 THR A CG2 1 
ATOM   1033 N  N   . ALA A 1 132 ? -15.295 24.744  -4.403  1.00 25.24 ? 132 ALA A N   1 
ATOM   1034 C  CA  . ALA A 1 132 ? -15.682 23.384  -4.895  1.00 26.28 ? 132 ALA A CA  1 
ATOM   1035 C  C   . ALA A 1 132 ? -15.041 22.244  -4.056  1.00 23.15 ? 132 ALA A C   1 
ATOM   1036 O  O   . ALA A 1 132 ? -15.616 21.185  -3.923  1.00 21.77 ? 132 ALA A O   1 
ATOM   1037 C  CB  . ALA A 1 132 ? -15.312 23.196  -6.356  1.00 24.21 ? 132 ALA A CB  1 
ATOM   1038 N  N   . SER A 1 133 ? -13.856 22.497  -3.498  1.00 25.46 ? 133 SER A N   1 
ATOM   1039 C  CA  . SER A 1 133 ? -13.021 21.458  -2.884  1.00 28.22 ? 133 SER A CA  1 
ATOM   1040 C  C   . SER A 1 133 ? -13.711 20.548  -1.848  1.00 26.52 ? 133 SER A C   1 
ATOM   1041 O  O   . SER A 1 133 ? -13.564 19.317  -1.864  1.00 26.41 ? 133 SER A O   1 
ATOM   1042 C  CB  . SER A 1 133 ? -11.808 22.128  -2.255  1.00 27.70 ? 133 SER A CB  1 
ATOM   1043 O  OG  . SER A 1 133 ? -10.730 21.236  -2.324  1.00 35.55 ? 133 SER A OG  1 
ATOM   1044 N  N   . ASN A 1 134 ? -14.451 21.148  -0.928  1.00 28.16 ? 134 ASN A N   1 
ATOM   1045 C  CA  . ASN A 1 134 ? -15.026 20.346  0.154   1.00 32.53 ? 134 ASN A CA  1 
ATOM   1046 C  C   . ASN A 1 134 ? -16.526 20.141  0.009   1.00 29.91 ? 134 ASN A C   1 
ATOM   1047 O  O   . ASN A 1 134 ? -17.205 20.015  0.992   1.00 36.31 ? 134 ASN A O   1 
ATOM   1048 C  CB  . ASN A 1 134 ? -14.608 20.866  1.564   1.00 30.68 ? 134 ASN A CB  1 
ATOM   1049 C  CG  . ASN A 1 134 ? -14.976 22.327  1.808   1.00 37.79 ? 134 ASN A CG  1 
ATOM   1050 O  OD1 . ASN A 1 134 ? -15.778 22.912  1.082   1.00 38.18 ? 134 ASN A OD1 1 
ATOM   1051 N  ND2 . ASN A 1 134 ? -14.387 22.924  2.860   1.00 36.78 ? 134 ASN A ND2 1 
ATOM   1052 N  N   . LYS A 1 135 ? -17.001 20.093  -1.239  1.00 30.38 ? 135 LYS A N   1 
ATOM   1053 C  CA  . LYS A 1 135 ? -18.421 20.008  -1.624  1.00 31.49 ? 135 LYS A CA  1 
ATOM   1054 C  C   . LYS A 1 135 ? -18.618 18.824  -2.559  1.00 31.07 ? 135 LYS A C   1 
ATOM   1055 O  O   . LYS A 1 135 ? -17.706 18.450  -3.310  1.00 32.03 ? 135 LYS A O   1 
ATOM   1056 C  CB  . LYS A 1 135 ? -18.900 21.313  -2.324  1.00 32.41 ? 135 LYS A CB  1 
ATOM   1057 C  CG  . LYS A 1 135 ? -18.551 22.625  -1.621  1.00 35.81 ? 135 LYS A CG  1 
ATOM   1058 C  CD  . LYS A 1 135 ? -19.725 23.236  -0.843  1.00 38.39 ? 135 LYS A CD  1 
ATOM   1059 C  CE  . LYS A 1 135 ? -19.498 24.717  -0.498  1.00 38.55 ? 135 LYS A CE  1 
ATOM   1060 N  NZ  . LYS A 1 135 ? -18.143 25.101  0.012   1.00 35.09 ? 135 LYS A NZ  1 
ATOM   1061 N  N   . SER A 1 136 ? -19.806 18.228  -2.527  1.00 34.24 ? 136 SER A N   1 
ATOM   1062 C  CA  . SER A 1 136 ? -20.107 17.030  -3.305  1.00 35.01 ? 136 SER A CA  1 
ATOM   1063 C  C   . SER A 1 136 ? -20.009 17.178  -4.854  1.00 35.70 ? 136 SER A C   1 
ATOM   1064 O  O   . SER A 1 136 ? -20.523 18.165  -5.414  1.00 40.71 ? 136 SER A O   1 
ATOM   1065 C  CB  . SER A 1 136 ? -21.542 16.566  -3.000  1.00 39.07 ? 136 SER A CB  1 
ATOM   1066 O  OG  . SER A 1 136 ? -22.513 17.304  -3.728  1.00 39.60 ? 136 SER A OG  1 
ATOM   1067 N  N   . GLU A 1 137 ? -19.377 16.196  -5.505  1.00 31.07 ? 137 GLU A N   1 
ATOM   1068 C  CA  . GLU A 1 137 ? -18.952 16.240  -6.945  1.00 33.67 ? 137 GLU A CA  1 
ATOM   1069 C  C   . GLU A 1 137 ? -18.313 17.626  -7.314  1.00 27.34 ? 137 GLU A C   1 
ATOM   1070 O  O   . GLU A 1 137 ? -18.539 18.198  -8.405  1.00 26.01 ? 137 GLU A O   1 
ATOM   1071 C  CB  . GLU A 1 137 ? -20.083 15.867  -7.926  1.00 41.38 ? 137 GLU A CB  1 
ATOM   1072 C  CG  . GLU A 1 137 ? -19.746 14.744  -8.916  1.00 44.27 ? 137 GLU A CG  1 
ATOM   1073 C  CD  . GLU A 1 137 ? -20.183 13.339  -8.488  1.00 50.61 ? 137 GLU A CD  1 
ATOM   1074 O  OE1 . GLU A 1 137 ? -20.898 12.654  -9.267  1.00 51.50 ? 137 GLU A OE1 1 
ATOM   1075 O  OE2 . GLU A 1 137 ? -19.788 12.892  -7.396  1.00 51.80 ? 137 GLU A OE2 1 
ATOM   1076 N  N   . GLY A 1 138 ? -17.489 18.132  -6.403  1.00 20.34 ? 138 GLY A N   1 
ATOM   1077 C  CA  . GLY A 1 138 ? -16.785 19.380  -6.589  1.00 18.86 ? 138 GLY A CA  1 
ATOM   1078 C  C   . GLY A 1 138 ? -15.567 19.274  -7.506  1.00 16.69 ? 138 GLY A C   1 
ATOM   1079 O  O   . GLY A 1 138 ? -15.214 20.270  -8.176  1.00 15.63 ? 138 GLY A O   1 
ATOM   1080 N  N   . LEU A 1 139 ? -14.913 18.098  -7.516  1.00 13.44 ? 139 LEU A N   1 
ATOM   1081 C  CA  . LEU A 1 139 ? -13.637 17.977  -8.224  1.00 12.76 ? 139 LEU A CA  1 
ATOM   1082 C  C   . LEU A 1 139 ? -13.616 16.835  -9.193  1.00 12.82 ? 139 LEU A C   1 
ATOM   1083 O  O   . LEU A 1 139 ? -14.202 15.752  -8.942  1.00 12.28 ? 139 LEU A O   1 
ATOM   1084 C  CB  . LEU A 1 139 ? -12.453 17.933  -7.210  1.00 11.85 ? 139 LEU A CB  1 
ATOM   1085 C  CG  . LEU A 1 139 ? -12.242 19.019  -6.147  1.00 12.25 ? 139 LEU A CG  1 
ATOM   1086 C  CD1 . LEU A 1 139 ? -11.066 18.674  -5.263  1.00 12.39 ? 139 LEU A CD1 1 
ATOM   1087 C  CD2 . LEU A 1 139 ? -11.988 20.381  -6.808  1.00 12.36 ? 139 LEU A CD2 1 
ATOM   1088 N  N   . ALA A 1 140 ? -12.948 17.037  -10.331 1.00 12.77 ? 140 ALA A N   1 
ATOM   1089 C  CA  . ALA A 1 140 ? -12.549 15.929  -11.200 1.00 11.79 ? 140 ALA A CA  1 
ATOM   1090 C  C   . ALA A 1 140 ? -11.082 15.968  -11.551 1.00 11.99 ? 140 ALA A C   1 
ATOM   1091 O  O   . ALA A 1 140 ? -10.577 17.013  -11.962 1.00 11.59 ? 140 ALA A O   1 
ATOM   1092 C  CB  . ALA A 1 140 ? -13.387 15.872  -12.487 1.00 10.92 ? 140 ALA A CB  1 
ATOM   1093 N  N   . VAL A 1 141 ? -10.409 14.813  -11.460 1.00 11.12 ? 141 VAL A N   1 
ATOM   1094 C  CA  . VAL A 1 141 ? -8.959  14.770  -11.740 1.00 11.51 ? 141 VAL A CA  1 
ATOM   1095 C  C   . VAL A 1 141 ? -8.662  13.700  -12.786 1.00 11.44 ? 141 VAL A C   1 
ATOM   1096 O  O   . VAL A 1 141 ? -9.167  12.554  -12.675 1.00 11.94 ? 141 VAL A O   1 
ATOM   1097 C  CB  . VAL A 1 141 ? -8.100  14.527  -10.443 1.00 11.35 ? 141 VAL A CB  1 
ATOM   1098 C  CG1 . VAL A 1 141 ? -6.622  14.533  -10.790 1.00 10.99 ? 141 VAL A CG1 1 
ATOM   1099 C  CG2 . VAL A 1 141 ? -8.428  15.493  -9.327  1.00 11.52 ? 141 VAL A CG2 1 
ATOM   1100 N  N   . LEU A 1 142 ? -7.923  14.101  -13.827 1.00 10.91 ? 142 LEU A N   1 
ATOM   1101 C  CA  . LEU A 1 142 ? -7.324  13.224  -14.801 1.00 10.80 ? 142 LEU A CA  1 
ATOM   1102 C  C   . LEU A 1 142 ? -5.971  12.739  -14.352 1.00 10.63 ? 142 LEU A C   1 
ATOM   1103 O  O   . LEU A 1 142 ? -5.100  13.550  -14.017 1.00 10.75 ? 142 LEU A O   1 
ATOM   1104 C  CB  . LEU A 1 142 ? -7.143  13.967  -16.114 1.00 12.92 ? 142 LEU A CB  1 
ATOM   1105 C  CG  . LEU A 1 142 ? -8.419  14.628  -16.654 1.00 11.94 ? 142 LEU A CG  1 
ATOM   1106 C  CD1 . LEU A 1 142 ? -8.113  15.190  -18.035 1.00 15.05 ? 142 LEU A CD1 1 
ATOM   1107 C  CD2 . LEU A 1 142 ? -9.565  13.660  -16.743 1.00 12.59 ? 142 LEU A CD2 1 
ATOM   1108 N  N   . ALA A 1 143 ? -5.753  11.421  -14.382 1.00 9.52  ? 143 ALA A N   1 
ATOM   1109 C  CA  . ALA A 1 143 ? -4.429  10.871  -13.972 1.00 10.13 ? 143 ALA A CA  1 
ATOM   1110 C  C   . ALA A 1 143 ? -3.740  10.228  -15.173 1.00 9.14  ? 143 ALA A C   1 
ATOM   1111 O  O   . ALA A 1 143 ? -4.382  9.423   -15.883 1.00 9.32  ? 143 ALA A O   1 
ATOM   1112 C  CB  . ALA A 1 143 ? -4.585  9.835   -12.857 1.00 9.66  ? 143 ALA A CB  1 
ATOM   1113 N  N   A VAL A 1 144 ? -2.484  10.621  -15.400 0.50 9.29  ? 144 VAL A N   1 
ATOM   1114 N  N   B VAL A 1 144 ? -2.462  10.561  -15.372 0.50 8.93  ? 144 VAL A N   1 
ATOM   1115 C  CA  A VAL A 1 144 ? -1.599  9.968   -16.365 0.50 9.13  ? 144 VAL A CA  1 
ATOM   1116 C  CA  B VAL A 1 144 ? -1.619  10.008  -16.443 0.50 8.56  ? 144 VAL A CA  1 
ATOM   1117 C  C   A VAL A 1 144 ? -0.513  9.200   -15.648 0.50 9.90  ? 144 VAL A C   1 
ATOM   1118 C  C   B VAL A 1 144 ? -0.439  9.253   -15.839 0.50 9.49  ? 144 VAL A C   1 
ATOM   1119 O  O   A VAL A 1 144 ? 0.266   9.743   -14.858 0.50 9.29  ? 144 VAL A O   1 
ATOM   1120 O  O   B VAL A 1 144 ? 0.483   9.876   -15.295 0.50 8.64  ? 144 VAL A O   1 
ATOM   1121 C  CB  A VAL A 1 144 ? -0.956  10.904  -17.428 0.50 9.62  ? 144 VAL A CB  1 
ATOM   1122 C  CB  B VAL A 1 144 ? -1.073  11.099  -17.421 0.50 8.57  ? 144 VAL A CB  1 
ATOM   1123 C  CG1 A VAL A 1 144 ? 0.127   11.791  -16.835 0.50 9.26  ? 144 VAL A CG1 1 
ATOM   1124 C  CG1 B VAL A 1 144 ? -0.117  10.441  -18.438 0.50 8.00  ? 144 VAL A CG1 1 
ATOM   1125 C  CG2 A VAL A 1 144 ? -0.287  10.059  -18.500 0.50 8.79  ? 144 VAL A CG2 1 
ATOM   1126 C  CG2 B VAL A 1 144 ? -2.206  11.863  -18.103 0.50 7.56  ? 144 VAL A CG2 1 
ATOM   1127 N  N   . LEU A 1 145 ? -0.461  7.918   -15.955 1.00 9.35  ? 145 LEU A N   1 
ATOM   1128 C  CA  . LEU A 1 145 ? 0.637   7.096   -15.433 1.00 10.47 ? 145 LEU A CA  1 
ATOM   1129 C  C   . LEU A 1 145 ? 1.891   7.269   -16.293 1.00 10.66 ? 145 LEU A C   1 
ATOM   1130 O  O   . LEU A 1 145 ? 1.814   7.204   -17.537 1.00 10.49 ? 145 LEU A O   1 
ATOM   1131 C  CB  . LEU A 1 145 ? 0.210   5.598   -15.382 1.00 10.91 ? 145 LEU A CB  1 
ATOM   1132 C  CG  . LEU A 1 145 ? -1.005  5.334   -14.498 1.00 10.92 ? 145 LEU A CG  1 
ATOM   1133 C  CD1 . LEU A 1 145 ? -1.657  4.028   -14.988 1.00 10.54 ? 145 LEU A CD1 1 
ATOM   1134 C  CD2 . LEU A 1 145 ? -0.640  5.279   -13.009 1.00 10.74 ? 145 LEU A CD2 1 
ATOM   1135 N  N   . ILE A 1 146 ? 3.062   7.458   -15.638 1.00 10.72 ? 146 ILE A N   1 
ATOM   1136 C  CA  . ILE A 1 146 ? 4.318   7.722   -16.380 1.00 10.91 ? 146 ILE A CA  1 
ATOM   1137 C  C   . ILE A 1 146 ? 5.312   6.583   -16.261 1.00 11.70 ? 146 ILE A C   1 
ATOM   1138 O  O   . ILE A 1 146 ? 5.617   6.169   -15.174 1.00 11.68 ? 146 ILE A O   1 
ATOM   1139 C  CB  . ILE A 1 146 ? 4.977   9.037   -15.908 1.00 10.36 ? 146 ILE A CB  1 
ATOM   1140 C  CG1 . ILE A 1 146 ? 3.918   10.167  -16.072 1.00 10.33 ? 146 ILE A CG1 1 
ATOM   1141 C  CG2 . ILE A 1 146 ? 6.223   9.347   -16.725 1.00 9.75  ? 146 ILE A CG2 1 
ATOM   1142 C  CD1 . ILE A 1 146 ? 4.339   11.557  -15.538 1.00 9.03  ? 146 ILE A CD1 1 
ATOM   1143 N  N   . GLU A 1 147 ? 5.908   6.168   -17.347 1.00 12.30 ? 147 GLU A N   1 
ATOM   1144 C  CA  . GLU A 1 147 ? 6.985   5.135   -17.203 1.00 14.40 ? 147 GLU A CA  1 
ATOM   1145 C  C   . GLU A 1 147 ? 8.307   5.576   -17.851 1.00 15.31 ? 147 GLU A C   1 
ATOM   1146 O  O   . GLU A 1 147 ? 8.310   6.485   -18.715 1.00 13.50 ? 147 GLU A O   1 
ATOM   1147 C  CB  . GLU A 1 147 ? 6.513   3.793   -17.736 1.00 17.74 ? 147 GLU A CB  1 
ATOM   1148 C  CG  . GLU A 1 147 ? 6.314   3.772   -19.234 1.00 19.94 ? 147 GLU A CG  1 
ATOM   1149 C  CD  . GLU A 1 147 ? 5.723   2.473   -19.735 1.00 23.97 ? 147 GLU A CD  1 
ATOM   1150 O  OE1 . GLU A 1 147 ? 5.276   1.651   -18.908 1.00 23.30 ? 147 GLU A OE1 1 
ATOM   1151 O  OE2 . GLU A 1 147 ? 5.698   2.292   -20.979 1.00 23.85 ? 147 GLU A OE2 1 
ATOM   1152 N  N   . MET A 1 148 ? 9.426   4.980   -17.426 1.00 14.09 ? 148 MET A N   1 
ATOM   1153 C  CA  . MET A 1 148 ? 10.699  5.375   -17.950 1.00 14.32 ? 148 MET A CA  1 
ATOM   1154 C  C   . MET A 1 148 ? 10.919  4.746   -19.334 1.00 13.70 ? 148 MET A C   1 
ATOM   1155 O  O   . MET A 1 148 ? 10.698  3.532   -19.514 1.00 13.89 ? 148 MET A O   1 
ATOM   1156 C  CB  . MET A 1 148 ? 11.831  5.001   -17.003 1.00 16.33 ? 148 MET A CB  1 
ATOM   1157 C  CG  . MET A 1 148 ? 13.174  5.581   -17.405 1.00 16.79 ? 148 MET A CG  1 
ATOM   1158 S  SD  . MET A 1 148 ? 14.075  4.666   -18.663 1.00 21.73 ? 148 MET A SD  1 
ATOM   1159 C  CE  . MET A 1 148 ? 15.018  3.592   -17.582 1.00 23.30 ? 148 MET A CE  1 
ATOM   1160 N  N   . GLY A 1 149 ? 11.368  5.556   -20.276 1.00 11.89 ? 149 GLY A N   1 
ATOM   1161 C  CA  . GLY A 1 149 ? 11.622  5.104   -21.686 1.00 11.87 ? 149 GLY A CA  1 
ATOM   1162 C  C   . GLY A 1 149 ? 12.101  6.204   -22.623 1.00 10.51 ? 149 GLY A C   1 
ATOM   1163 O  O   . GLY A 1 149 ? 13.175  6.711   -22.465 1.00 10.82 ? 149 GLY A O   1 
ATOM   1164 N  N   . SER A 1 150 ? 11.297  6.551   -23.639 1.00 9.70  ? 150 SER A N   1 
ATOM   1165 C  CA  . SER A 1 150 ? 11.649  7.562   -24.623 1.00 10.42 ? 150 SER A CA  1 
ATOM   1166 C  C   . SER A 1 150 ? 11.510  8.960   -24.042 1.00 9.99  ? 150 SER A C   1 
ATOM   1167 O  O   . SER A 1 150 ? 10.524  9.266   -23.309 1.00 10.83 ? 150 SER A O   1 
ATOM   1168 C  CB  . SER A 1 150 ? 10.640  7.531   -25.782 1.00 9.40  ? 150 SER A CB  1 
ATOM   1169 O  OG  . SER A 1 150 ? 10.678  6.326   -26.455 1.00 10.13 ? 150 SER A OG  1 
ATOM   1170 N  N   . PHE A 1 151 ? 12.428  9.848   -24.402 1.00 11.38 ? 151 PHE A N   1 
ATOM   1171 C  CA  . PHE A 1 151 ? 12.269  11.306  -24.143 1.00 11.09 ? 151 PHE A CA  1 
ATOM   1172 C  C   . PHE A 1 151 ? 10.922  11.829  -24.663 1.00 12.31 ? 151 PHE A C   1 
ATOM   1173 O  O   . PHE A 1 151 ? 10.418  11.416  -25.763 1.00 11.74 ? 151 PHE A O   1 
ATOM   1174 C  CB  . PHE A 1 151 ? 13.398  12.047  -24.852 1.00 11.70 ? 151 PHE A CB  1 
ATOM   1175 C  CG  . PHE A 1 151 ? 13.390  13.548  -24.647 1.00 12.77 ? 151 PHE A CG  1 
ATOM   1176 C  CD1 . PHE A 1 151 ? 13.915  14.120  -23.477 1.00 12.81 ? 151 PHE A CD1 1 
ATOM   1177 C  CD2 . PHE A 1 151 ? 12.948  14.375  -25.657 1.00 13.51 ? 151 PHE A CD2 1 
ATOM   1178 C  CE1 . PHE A 1 151 ? 13.947  15.529  -23.310 1.00 14.29 ? 151 PHE A CE1 1 
ATOM   1179 C  CE2 . PHE A 1 151 ? 12.959  15.753  -25.501 1.00 13.61 ? 151 PHE A CE2 1 
ATOM   1180 C  CZ  . PHE A 1 151 ? 13.460  16.322  -24.333 1.00 13.94 ? 151 PHE A CZ  1 
ATOM   1181 N  N   . ASN A 1 152 ? 10.356  12.793  -23.929 1.00 12.29 ? 152 ASN A N   1 
ATOM   1182 C  CA  . ASN A 1 152 ? 9.008   13.267  -24.217 1.00 12.81 ? 152 ASN A CA  1 
ATOM   1183 C  C   . ASN A 1 152 ? 9.129   14.791  -24.342 1.00 12.69 ? 152 ASN A C   1 
ATOM   1184 O  O   . ASN A 1 152 ? 9.326   15.477  -23.341 1.00 12.92 ? 152 ASN A O   1 
ATOM   1185 C  CB  . ASN A 1 152 ? 7.992   12.880  -23.104 1.00 12.45 ? 152 ASN A CB  1 
ATOM   1186 C  CG  . ASN A 1 152 ? 6.537   13.172  -23.518 1.00 10.95 ? 152 ASN A CG  1 
ATOM   1187 O  OD1 . ASN A 1 152 ? 6.193   14.340  -23.850 1.00 10.65 ? 152 ASN A OD1 1 
ATOM   1188 N  ND2 . ASN A 1 152 ? 5.672   12.159  -23.459 1.00 9.88  ? 152 ASN A ND2 1 
ATOM   1189 N  N   . PRO A 1 153 ? 9.087   15.297  -25.577 1.00 13.57 ? 153 PRO A N   1 
ATOM   1190 C  CA  . PRO A 1 153 ? 9.181   16.766  -25.781 1.00 13.22 ? 153 PRO A CA  1 
ATOM   1191 C  C   . PRO A 1 153 ? 8.161   17.612  -25.029 1.00 13.98 ? 153 PRO A C   1 
ATOM   1192 O  O   . PRO A 1 153 ? 8.530   18.674  -24.486 1.00 13.42 ? 153 PRO A O   1 
ATOM   1193 C  CB  . PRO A 1 153 ? 9.023   16.902  -27.309 1.00 14.87 ? 153 PRO A CB  1 
ATOM   1194 C  CG  . PRO A 1 153 ? 9.677   15.660  -27.842 1.00 15.85 ? 153 PRO A CG  1 
ATOM   1195 C  CD  . PRO A 1 153 ? 9.328   14.554  -26.843 1.00 13.17 ? 153 PRO A CD  1 
ATOM   1196 N  N   . SER A 1 154 ? 6.894   17.169  -25.004 1.00 13.74 ? 154 SER A N   1 
ATOM   1197 C  CA  . SER A 1 154 ? 5.815   17.884  -24.332 1.00 12.84 ? 154 SER A CA  1 
ATOM   1198 C  C   . SER A 1 154 ? 6.023   17.954  -22.804 1.00 13.00 ? 154 SER A C   1 
ATOM   1199 O  O   . SER A 1 154 ? 5.921   19.035  -22.260 1.00 11.93 ? 154 SER A O   1 
ATOM   1200 C  CB  . SER A 1 154 ? 4.446   17.310  -24.708 1.00 14.45 ? 154 SER A CB  1 
ATOM   1201 O  OG  . SER A 1 154 ? 4.303   17.390  -26.139 1.00 16.06 ? 154 SER A OG  1 
ATOM   1202 N  N   . TYR A 1 155 ? 6.354   16.838  -22.124 1.00 11.91 ? 155 TYR A N   1 
ATOM   1203 C  CA  . TYR A 1 155 ? 6.696   16.907  -20.662 1.00 11.72 ? 155 TYR A CA  1 
ATOM   1204 C  C   . TYR A 1 155 ? 7.907   17.818  -20.403 1.00 11.75 ? 155 TYR A C   1 
ATOM   1205 O  O   . TYR A 1 155 ? 8.025   18.399  -19.331 1.00 12.08 ? 155 TYR A O   1 
ATOM   1206 C  CB  . TYR A 1 155 ? 6.925   15.514  -20.031 1.00 11.23 ? 155 TYR A CB  1 
ATOM   1207 C  CG  . TYR A 1 155 ? 5.602   14.835  -19.699 1.00 9.88  ? 155 TYR A CG  1 
ATOM   1208 C  CD1 . TYR A 1 155 ? 4.820   14.258  -20.720 1.00 10.21 ? 155 TYR A CD1 1 
ATOM   1209 C  CD2 . TYR A 1 155 ? 5.110   14.839  -18.387 1.00 10.37 ? 155 TYR A CD2 1 
ATOM   1210 C  CE1 . TYR A 1 155 ? 3.609   13.670  -20.412 1.00 9.85  ? 155 TYR A CE1 1 
ATOM   1211 C  CE2 . TYR A 1 155 ? 3.893   14.264  -18.058 1.00 9.76  ? 155 TYR A CE2 1 
ATOM   1212 C  CZ  . TYR A 1 155 ? 3.137   13.700  -19.091 1.00 9.96  ? 155 TYR A CZ  1 
ATOM   1213 O  OH  . TYR A 1 155 ? 1.912   13.155  -18.818 1.00 9.56  ? 155 TYR A OH  1 
ATOM   1214 N  N   . ASP A 1 156 ? 8.824   17.897  -21.373 1.00 11.69 ? 156 ASP A N   1 
ATOM   1215 C  CA  . ASP A 1 156 ? 10.021  18.714  -21.197 1.00 12.25 ? 156 ASP A CA  1 
ATOM   1216 C  C   . ASP A 1 156 ? 9.708   20.234  -21.194 1.00 11.77 ? 156 ASP A C   1 
ATOM   1217 O  O   . ASP A 1 156 ? 10.478  21.025  -20.610 1.00 11.75 ? 156 ASP A O   1 
ATOM   1218 C  CB  . ASP A 1 156 ? 11.166  18.305  -22.161 1.00 14.29 ? 156 ASP A CB  1 
ATOM   1219 C  CG  . ASP A 1 156 ? 12.532  18.259  -21.412 1.00 17.07 ? 156 ASP A CG  1 
ATOM   1220 O  OD1 . ASP A 1 156 ? 13.464  19.033  -21.828 1.00 15.27 ? 156 ASP A OD1 1 
ATOM   1221 O  OD2 . ASP A 1 156 ? 12.590  17.539  -20.361 1.00 14.95 ? 156 ASP A OD2 1 
ATOM   1222 N  N   . LYS A 1 157 ? 8.567   20.608  -21.781 1.00 12.10 ? 157 LYS A N   1 
ATOM   1223 C  CA  . LYS A 1 157 ? 8.013   21.967  -21.630 1.00 13.55 ? 157 LYS A CA  1 
ATOM   1224 C  C   . LYS A 1 157 ? 7.864   22.348  -20.164 1.00 12.40 ? 157 LYS A C   1 
ATOM   1225 O  O   . LYS A 1 157 ? 8.023   23.508  -19.833 1.00 14.51 ? 157 LYS A O   1 
ATOM   1226 C  CB  . LYS A 1 157 ? 6.703   22.147  -22.431 1.00 14.77 ? 157 LYS A CB  1 
ATOM   1227 C  CG  . LYS A 1 157 ? 7.012   21.868  -23.919 1.00 20.00 ? 157 LYS A CG  1 
ATOM   1228 C  CD  . LYS A 1 157 ? 5.919   22.335  -24.850 1.00 22.79 ? 157 LYS A CD  1 
ATOM   1229 C  CE  . LYS A 1 157 ? 6.510   22.658  -26.227 1.00 25.91 ? 157 LYS A CE  1 
ATOM   1230 N  NZ  . LYS A 1 157 ? 5.499   22.138  -27.205 1.00 28.23 ? 157 LYS A NZ  1 
ATOM   1231 N  N   . ILE A 1 158 ? 7.506   21.394  -19.307 1.00 12.32 ? 158 ILE A N   1 
ATOM   1232 C  CA  . ILE A 1 158 ? 7.569   21.595  -17.851 1.00 11.90 ? 158 ILE A CA  1 
ATOM   1233 C  C   . ILE A 1 158 ? 8.964   21.327  -17.240 1.00 11.96 ? 158 ILE A C   1 
ATOM   1234 O  O   . ILE A 1 158 ? 9.492   22.176  -16.570 1.00 11.49 ? 158 ILE A O   1 
ATOM   1235 C  CB  . ILE A 1 158 ? 6.536   20.707  -17.105 1.00 13.09 ? 158 ILE A CB  1 
ATOM   1236 C  CG1 . ILE A 1 158 ? 5.104   21.157  -17.420 1.00 14.28 ? 158 ILE A CG1 1 
ATOM   1237 C  CG2 . ILE A 1 158 ? 6.688   20.821  -15.596 1.00 13.20 ? 158 ILE A CG2 1 
ATOM   1238 C  CD1 . ILE A 1 158 ? 4.113   20.043  -17.215 1.00 16.39 ? 158 ILE A CD1 1 
ATOM   1239 N  N   . PHE A 1 159 ? 9.544   20.129  -17.495 1.00 11.47 ? 159 PHE A N   1 
ATOM   1240 C  CA  . PHE A 1 159 ? 10.792  19.701  -16.842 1.00 13.32 ? 159 PHE A CA  1 
ATOM   1241 C  C   . PHE A 1 159 ? 12.037  20.623  -17.043 1.00 13.54 ? 159 PHE A C   1 
ATOM   1242 O  O   . PHE A 1 159 ? 12.915  20.684  -16.177 1.00 12.68 ? 159 PHE A O   1 
ATOM   1243 C  CB  . PHE A 1 159 ? 11.156  18.280  -17.258 1.00 12.70 ? 159 PHE A CB  1 
ATOM   1244 C  CG  . PHE A 1 159 ? 10.102  17.246  -16.921 1.00 12.56 ? 159 PHE A CG  1 
ATOM   1245 C  CD1 . PHE A 1 159 ? 9.198   17.446  -15.880 1.00 12.17 ? 159 PHE A CD1 1 
ATOM   1246 C  CD2 . PHE A 1 159 ? 10.073  16.023  -17.595 1.00 12.62 ? 159 PHE A CD2 1 
ATOM   1247 C  CE1 . PHE A 1 159 ? 8.250   16.455  -15.556 1.00 12.83 ? 159 PHE A CE1 1 
ATOM   1248 C  CE2 . PHE A 1 159 ? 9.129   15.021  -17.247 1.00 13.08 ? 159 PHE A CE2 1 
ATOM   1249 C  CZ  . PHE A 1 159 ? 8.192   15.265  -16.230 1.00 10.80 ? 159 PHE A CZ  1 
ATOM   1250 N  N   . SER A 1 160 ? 12.126  21.310  -18.182 1.00 14.29 ? 160 SER A N   1 
ATOM   1251 C  CA  . SER A 1 160 ? 13.242  22.216  -18.466 1.00 15.63 ? 160 SER A CA  1 
ATOM   1252 C  C   . SER A 1 160 ? 13.312  23.375  -17.503 1.00 16.30 ? 160 SER A C   1 
ATOM   1253 O  O   . SER A 1 160 ? 14.416  23.958  -17.317 1.00 17.56 ? 160 SER A O   1 
ATOM   1254 C  CB  . SER A 1 160 ? 13.175  22.722  -19.916 1.00 16.18 ? 160 SER A CB  1 
ATOM   1255 O  OG  . SER A 1 160 ? 12.045  23.566  -20.042 1.00 16.80 ? 160 SER A OG  1 
ATOM   1256 N  N   . HIS A 1 161 ? 12.185  23.700  -16.837 1.00 15.05 ? 161 HIS A N   1 
ATOM   1257 C  CA  . HIS A 1 161 ? 12.194  24.642  -15.702 1.00 15.95 ? 161 HIS A CA  1 
ATOM   1258 C  C   . HIS A 1 161 ? 12.615  24.181  -14.315 1.00 14.80 ? 161 HIS A C   1 
ATOM   1259 O  O   . HIS A 1 161 ? 12.766  25.011  -13.410 1.00 15.28 ? 161 HIS A O   1 
ATOM   1260 C  CB  . HIS A 1 161 ? 10.845  25.336  -15.635 1.00 15.46 ? 161 HIS A CB  1 
ATOM   1261 C  CG  . HIS A 1 161 ? 10.494  26.048  -16.942 1.00 15.28 ? 161 HIS A CG  1 
ATOM   1262 N  ND1 . HIS A 1 161 ? 10.921  27.323  -17.224 1.00 16.20 ? 161 HIS A ND1 1 
ATOM   1263 C  CD2 . HIS A 1 161 ? 9.810   25.610  -18.078 1.00 15.42 ? 161 HIS A CD2 1 
ATOM   1264 C  CE1 . HIS A 1 161 ? 10.498  27.671  -18.448 1.00 15.54 ? 161 HIS A CE1 1 
ATOM   1265 N  NE2 . HIS A 1 161 ? 9.811   26.632  -18.969 1.00 15.13 ? 161 HIS A NE2 1 
ATOM   1266 N  N   . LEU A 1 162 ? 12.800  22.868  -14.116 1.00 13.95 ? 162 LEU A N   1 
ATOM   1267 C  CA  . LEU A 1 162 ? 12.944  22.370  -12.783 1.00 14.70 ? 162 LEU A CA  1 
ATOM   1268 C  C   . LEU A 1 162 ? 14.133  22.943  -12.027 1.00 16.11 ? 162 LEU A C   1 
ATOM   1269 O  O   . LEU A 1 162 ? 13.949  23.267  -10.868 1.00 15.31 ? 162 LEU A O   1 
ATOM   1270 C  CB  . LEU A 1 162 ? 13.003  20.821  -12.713 1.00 16.71 ? 162 LEU A CB  1 
ATOM   1271 C  CG  . LEU A 1 162 ? 11.692  20.182  -13.148 1.00 14.87 ? 162 LEU A CG  1 
ATOM   1272 C  CD1 . LEU A 1 162 ? 11.922  18.708  -13.442 1.00 19.35 ? 162 LEU A CD1 1 
ATOM   1273 C  CD2 . LEU A 1 162 ? 10.624  20.299  -12.055 1.00 17.15 ? 162 LEU A CD2 1 
ATOM   1274 N  N   . GLN A 1 163 ? 15.309  23.080  -12.681 1.00 16.15 ? 163 GLN A N   1 
ATOM   1275 C  CA  . GLN A 1 163 ? 16.494  23.626  -11.992 1.00 17.70 ? 163 GLN A CA  1 
ATOM   1276 C  C   . GLN A 1 163 ? 16.368  25.105  -11.638 1.00 17.00 ? 163 GLN A C   1 
ATOM   1277 O  O   . GLN A 1 163 ? 17.280  25.680  -10.998 1.00 15.29 ? 163 GLN A O   1 
ATOM   1278 C  CB  . GLN A 1 163 ? 17.813  23.376  -12.783 1.00 20.30 ? 163 GLN A CB  1 
ATOM   1279 C  CG  . GLN A 1 163 ? 18.144  21.914  -13.090 1.00 24.17 ? 163 GLN A CG  1 
ATOM   1280 C  CD  . GLN A 1 163 ? 18.450  21.042  -11.865 1.00 25.48 ? 163 GLN A CD  1 
ATOM   1281 O  OE1 . GLN A 1 163 ? 18.679  21.544  -10.759 1.00 26.01 ? 163 GLN A OE1 1 
ATOM   1282 N  NE2 . GLN A 1 163 ? 18.514  19.719  -12.082 1.00 25.42 ? 163 GLN A NE2 1 
ATOM   1283 N  N   . HIS A 1 164 ? 15.244  25.721  -12.006 1.00 16.12 ? 164 HIS A N   1 
ATOM   1284 C  CA  . HIS A 1 164 ? 14.971  27.147  -11.674 1.00 17.43 ? 164 HIS A CA  1 
ATOM   1285 C  C   . HIS A 1 164 ? 13.831  27.311  -10.687 1.00 17.76 ? 164 HIS A C   1 
ATOM   1286 O  O   . HIS A 1 164 ? 13.494  28.434  -10.258 1.00 16.99 ? 164 HIS A O   1 
ATOM   1287 C  CB  . HIS A 1 164 ? 14.829  28.030  -12.960 1.00 17.71 ? 164 HIS A CB  1 
ATOM   1288 C  CG  . HIS A 1 164 ? 15.933  27.775  -13.973 1.00 19.81 ? 164 HIS A CG  1 
ATOM   1289 N  ND1 . HIS A 1 164 ? 17.245  27.953  -13.673 1.00 18.77 ? 164 HIS A ND1 1 
ATOM   1290 C  CD2 . HIS A 1 164 ? 15.900  27.270  -15.279 1.00 19.60 ? 164 HIS A CD2 1 
ATOM   1291 C  CE1 . HIS A 1 164 ? 18.008  27.583  -14.708 1.00 19.39 ? 164 HIS A CE1 1 
ATOM   1292 N  NE2 . HIS A 1 164 ? 17.198  27.134  -15.686 1.00 22.12 ? 164 HIS A NE2 1 
ATOM   1293 N  N   . VAL A 1 165 ? 13.251  26.185  -10.259 1.00 16.44 ? 165 VAL A N   1 
ATOM   1294 C  CA  . VAL A 1 165 ? 12.322  26.188  -9.119  1.00 17.54 ? 165 VAL A CA  1 
ATOM   1295 C  C   . VAL A 1 165 ? 12.731  25.163  -8.030  1.00 16.61 ? 165 VAL A C   1 
ATOM   1296 O  O   . VAL A 1 165 ? 11.895  24.470  -7.485  1.00 16.82 ? 165 VAL A O   1 
ATOM   1297 C  CB  . VAL A 1 165 ? 10.845  25.958  -9.586  1.00 18.15 ? 165 VAL A CB  1 
ATOM   1298 C  CG1 . VAL A 1 165 ? 10.338  27.167  -10.355 1.00 18.46 ? 165 VAL A CG1 1 
ATOM   1299 C  CG2 . VAL A 1 165 ? 10.730  24.707  -10.448 1.00 18.29 ? 165 VAL A CG2 1 
ATOM   1300 N  N   . LYS A 1 166 ? 14.001  25.147  -7.631  1.00 15.96 ? 166 LYS A N   1 
ATOM   1301 C  CA  . LYS A 1 166 ? 14.541  24.064  -6.775  1.00 15.84 ? 166 LYS A CA  1 
ATOM   1302 C  C   . LYS A 1 166 ? 14.036  24.049  -5.324  1.00 15.12 ? 166 LYS A C   1 
ATOM   1303 O  O   . LYS A 1 166 ? 13.983  22.988  -4.680  1.00 14.69 ? 166 LYS A O   1 
ATOM   1304 C  CB  . LYS A 1 166 ? 16.095  24.068  -6.768  1.00 16.06 ? 166 LYS A CB  1 
ATOM   1305 C  CG  . LYS A 1 166 ? 16.710  23.752  -8.109  1.00 18.14 ? 166 LYS A CG  1 
ATOM   1306 C  CD  . LYS A 1 166 ? 18.246  23.858  -8.099  1.00 17.86 ? 166 LYS A CD  1 
ATOM   1307 C  CE  . LYS A 1 166 ? 18.849  22.750  -7.241  1.00 20.62 ? 166 LYS A CE  1 
ATOM   1308 N  NZ  . LYS A 1 166 ? 18.689  21.406  -7.914  1.00 18.20 ? 166 LYS A NZ  1 
ATOM   1309 N  N   . TYR A 1 167 ? 13.621  25.213  -4.821  1.00 16.18 ? 167 TYR A N   1 
ATOM   1310 C  CA  . TYR A 1 167 ? 13.258  25.382  -3.404  1.00 17.35 ? 167 TYR A CA  1 
ATOM   1311 C  C   . TYR A 1 167 ? 11.848  25.902  -3.248  1.00 16.37 ? 167 TYR A C   1 
ATOM   1312 O  O   . TYR A 1 167 ? 11.306  26.576  -4.141  1.00 15.44 ? 167 TYR A O   1 
ATOM   1313 C  CB  . TYR A 1 167 ? 14.242  26.371  -2.730  1.00 19.12 ? 167 TYR A CB  1 
ATOM   1314 C  CG  . TYR A 1 167 ? 15.657  25.839  -2.769  1.00 22.11 ? 167 TYR A CG  1 
ATOM   1315 C  CD1 . TYR A 1 167 ? 16.556  26.240  -3.788  1.00 24.07 ? 167 TYR A CD1 1 
ATOM   1316 C  CD2 . TYR A 1 167 ? 16.092  24.899  -1.846  1.00 22.06 ? 167 TYR A CD2 1 
ATOM   1317 C  CE1 . TYR A 1 167 ? 17.844  25.755  -3.853  1.00 24.69 ? 167 TYR A CE1 1 
ATOM   1318 C  CE2 . TYR A 1 167 ? 17.376  24.370  -1.929  1.00 26.91 ? 167 TYR A CE2 1 
ATOM   1319 C  CZ  . TYR A 1 167 ? 18.257  24.820  -2.904  1.00 27.98 ? 167 TYR A CZ  1 
ATOM   1320 O  OH  . TYR A 1 167 ? 19.545  24.311  -2.961  1.00 30.12 ? 167 TYR A OH  1 
ATOM   1321 N  N   . LYS A 1 168 ? 11.253  25.570  -2.118  1.00 17.24 ? 168 LYS A N   1 
ATOM   1322 C  CA  . LYS A 1 168 ? 9.905   26.020  -1.763  1.00 17.35 ? 168 LYS A CA  1 
ATOM   1323 C  C   . LYS A 1 168 ? 9.672   27.506  -1.948  1.00 17.86 ? 168 LYS A C   1 
ATOM   1324 O  O   . LYS A 1 168 ? 10.457  28.351  -1.478  1.00 19.25 ? 168 LYS A O   1 
ATOM   1325 C  CB  . LYS A 1 168 ? 9.560   25.642  -0.302  1.00 16.82 ? 168 LYS A CB  1 
ATOM   1326 C  CG  . LYS A 1 168 ? 8.135   26.003  0.125   1.00 16.30 ? 168 LYS A CG  1 
ATOM   1327 C  CD  . LYS A 1 168 ? 7.838   25.547  1.572   1.00 18.34 ? 168 LYS A CD  1 
ATOM   1328 C  CE  . LYS A 1 168 ? 6.454   26.031  1.958   1.00 22.99 ? 168 LYS A CE  1 
ATOM   1329 N  NZ  . LYS A 1 168 ? 5.864   25.486  3.218   1.00 24.02 ? 168 LYS A NZ  1 
ATOM   1330 N  N   . GLY A 1 169 ? 8.567   27.815  -2.606  1.00 16.64 ? 169 GLY A N   1 
ATOM   1331 C  CA  . GLY A 1 169 ? 8.158   29.229  -2.819  1.00 17.75 ? 169 GLY A CA  1 
ATOM   1332 C  C   . GLY A 1 169 ? 8.614   29.821  -4.139  1.00 17.24 ? 169 GLY A C   1 
ATOM   1333 O  O   . GLY A 1 169 ? 8.123   30.883  -4.536  1.00 16.74 ? 169 GLY A O   1 
ATOM   1334 N  N   . GLN A 1 170 ? 9.586   29.177  -4.825  1.00 16.67 ? 170 GLN A N   1 
ATOM   1335 C  CA  . GLN A 1 170 ? 10.099  29.704  -6.101  1.00 15.56 ? 170 GLN A CA  1 
ATOM   1336 C  C   . GLN A 1 170 ? 9.151   29.465  -7.267  1.00 17.08 ? 170 GLN A C   1 
ATOM   1337 O  O   . GLN A 1 170 ? 8.440   28.491  -7.257  1.00 15.53 ? 170 GLN A O   1 
ATOM   1338 C  CB  . GLN A 1 170 ? 11.461  29.111  -6.411  1.00 17.43 ? 170 GLN A CB  1 
ATOM   1339 C  CG  . GLN A 1 170 ? 12.471  29.353  -5.270  1.00 17.29 ? 170 GLN A CG  1 
ATOM   1340 C  CD  . GLN A 1 170 ? 13.894  29.004  -5.668  1.00 17.94 ? 170 GLN A CD  1 
ATOM   1341 O  OE1 . GLN A 1 170 ? 14.168  27.933  -6.218  1.00 16.01 ? 170 GLN A OE1 1 
ATOM   1342 N  NE2 . GLN A 1 170 ? 14.831  29.911  -5.344  1.00 19.43 ? 170 GLN A NE2 1 
ATOM   1343 N  N   . GLU A 1 171 ? 9.201   30.336  -8.277  1.00 18.06 ? 171 GLU A N   1 
ATOM   1344 C  CA  . GLU A 1 171 ? 8.247   30.357  -9.392  1.00 17.87 ? 171 GLU A CA  1 
ATOM   1345 C  C   . GLU A 1 171 ? 9.025   30.554  -10.636 1.00 17.74 ? 171 GLU A C   1 
ATOM   1346 O  O   . GLU A 1 171 ? 10.101  31.219  -10.626 1.00 19.75 ? 171 GLU A O   1 
ATOM   1347 C  CB  . GLU A 1 171 ? 7.345   31.617  -9.326  1.00 19.85 ? 171 GLU A CB  1 
ATOM   1348 C  CG  . GLU A 1 171 ? 6.267   31.646  -8.288  1.00 25.72 ? 171 GLU A CG  1 
ATOM   1349 C  CD  . GLU A 1 171 ? 5.733   33.074  -8.061  1.00 26.62 ? 171 GLU A CD  1 
ATOM   1350 O  OE1 . GLU A 1 171 ? 4.926   33.216  -7.143  1.00 30.02 ? 171 GLU A OE1 1 
ATOM   1351 O  OE2 . GLU A 1 171 ? 6.108   34.033  -8.800  1.00 29.43 ? 171 GLU A OE2 1 
ATOM   1352 N  N   . ALA A 1 172 ? 8.479   30.000  -11.713 1.00 18.40 ? 172 ALA A N   1 
ATOM   1353 C  CA  . ALA A 1 172 ? 8.912   30.275  -13.083 1.00 17.00 ? 172 ALA A CA  1 
ATOM   1354 C  C   . ALA A 1 172 ? 7.675   30.487  -13.955 1.00 17.86 ? 172 ALA A C   1 
ATOM   1355 O  O   . ALA A 1 172 ? 6.584   30.114  -13.584 1.00 18.18 ? 172 ALA A O   1 
ATOM   1356 C  CB  . ALA A 1 172 ? 9.705   29.083  -13.662 1.00 15.96 ? 172 ALA A CB  1 
ATOM   1357 N  N   . PHE A 1 173 ? 7.890   31.020  -15.158 1.00 20.37 ? 173 PHE A N   1 
ATOM   1358 C  CA  . PHE A 1 173 ? 6.819   31.280  -16.141 1.00 19.22 ? 173 PHE A CA  1 
ATOM   1359 C  C   . PHE A 1 173 ? 7.039   30.313  -17.265 1.00 19.81 ? 173 PHE A C   1 
ATOM   1360 O  O   . PHE A 1 173 ? 8.175   30.173  -17.725 1.00 18.42 ? 173 PHE A O   1 
ATOM   1361 C  CB  . PHE A 1 173 ? 6.821   32.793  -16.554 1.00 19.86 ? 173 PHE A CB  1 
ATOM   1362 C  CG  . PHE A 1 173 ? 6.336   33.676  -15.444 1.00 20.60 ? 173 PHE A CG  1 
ATOM   1363 C  CD1 . PHE A 1 173 ? 7.246   34.201  -14.519 1.00 22.82 ? 173 PHE A CD1 1 
ATOM   1364 C  CD2 . PHE A 1 173 ? 4.959   33.846  -15.220 1.00 21.95 ? 173 PHE A CD2 1 
ATOM   1365 C  CE1 . PHE A 1 173 ? 6.804   34.966  -13.428 1.00 23.63 ? 173 PHE A CE1 1 
ATOM   1366 C  CE2 . PHE A 1 173 ? 4.504   34.603  -14.133 1.00 22.00 ? 173 PHE A CE2 1 
ATOM   1367 C  CZ  . PHE A 1 173 ? 5.428   35.144  -13.234 1.00 24.16 ? 173 PHE A CZ  1 
ATOM   1368 N  N   . VAL A 1 174 ? 5.963   29.594  -17.649 1.00 16.53 ? 174 VAL A N   1 
ATOM   1369 C  CA  . VAL A 1 174 ? 5.944   28.644  -18.724 1.00 14.59 ? 174 VAL A CA  1 
ATOM   1370 C  C   . VAL A 1 174 ? 5.024   29.126  -19.822 1.00 14.06 ? 174 VAL A C   1 
ATOM   1371 O  O   . VAL A 1 174 ? 3.848   29.324  -19.560 1.00 13.93 ? 174 VAL A O   1 
ATOM   1372 C  CB  . VAL A 1 174 ? 5.418   27.284  -18.216 1.00 14.12 ? 174 VAL A CB  1 
ATOM   1373 C  CG1 . VAL A 1 174 ? 5.382   26.254  -19.335 1.00 14.18 ? 174 VAL A CG1 1 
ATOM   1374 C  CG2 . VAL A 1 174 ? 6.251   26.810  -17.038 1.00 13.34 ? 174 VAL A CG2 1 
ATOM   1375 N  N   . PRO A 1 175 ? 5.559   29.367  -21.059 1.00 14.11 ? 175 PRO A N   1 
ATOM   1376 C  CA  . PRO A 1 175 ? 4.708   29.713  -22.191 1.00 14.66 ? 175 PRO A CA  1 
ATOM   1377 C  C   . PRO A 1 175 ? 3.706   28.606  -22.425 1.00 15.32 ? 175 PRO A C   1 
ATOM   1378 O  O   . PRO A 1 175 ? 4.026   27.416  -22.230 1.00 15.45 ? 175 PRO A O   1 
ATOM   1379 C  CB  . PRO A 1 175 ? 5.683   29.744  -23.387 1.00 15.19 ? 175 PRO A CB  1 
ATOM   1380 C  CG  . PRO A 1 175 ? 6.996   30.146  -22.746 1.00 16.31 ? 175 PRO A CG  1 
ATOM   1381 C  CD  . PRO A 1 175 ? 6.981   29.384  -21.422 1.00 14.80 ? 175 PRO A CD  1 
ATOM   1382 N  N   . GLY A 1 176 ? 2.525   28.978  -22.913 1.00 15.08 ? 176 GLY A N   1 
ATOM   1383 C  CA  . GLY A 1 176 ? 1.491   27.973  -23.210 1.00 14.02 ? 176 GLY A CA  1 
ATOM   1384 C  C   . GLY A 1 176 ? 1.923   27.017  -24.281 1.00 14.53 ? 176 GLY A C   1 
ATOM   1385 O  O   . GLY A 1 176 ? 2.650   27.414  -25.223 1.00 13.50 ? 176 GLY A O   1 
ATOM   1386 N  N   . PHE A 1 177 ? 1.494   25.745  -24.121 1.00 14.49 ? 177 PHE A N   1 
ATOM   1387 C  CA  . PHE A 1 177 ? 1.697   24.685  -25.070 1.00 15.25 ? 177 PHE A CA  1 
ATOM   1388 C  C   . PHE A 1 177 ? 0.471   23.783  -24.970 1.00 15.65 ? 177 PHE A C   1 
ATOM   1389 O  O   . PHE A 1 177 ? -0.368  23.988  -24.048 1.00 15.98 ? 177 PHE A O   1 
ATOM   1390 C  CB  . PHE A 1 177 ? 2.985   23.913  -24.738 1.00 15.95 ? 177 PHE A CB  1 
ATOM   1391 C  CG  . PHE A 1 177 ? 2.958   23.143  -23.410 1.00 16.38 ? 177 PHE A CG  1 
ATOM   1392 C  CD1 . PHE A 1 177 ? 2.628   21.778  -23.401 1.00 15.45 ? 177 PHE A CD1 1 
ATOM   1393 C  CD2 . PHE A 1 177 ? 3.323   23.753  -22.201 1.00 15.69 ? 177 PHE A CD2 1 
ATOM   1394 C  CE1 . PHE A 1 177 ? 2.599   21.062  -22.212 1.00 15.61 ? 177 PHE A CE1 1 
ATOM   1395 C  CE2 . PHE A 1 177 ? 3.292   23.025  -20.995 1.00 16.87 ? 177 PHE A CE2 1 
ATOM   1396 C  CZ  . PHE A 1 177 ? 2.944   21.669  -21.025 1.00 15.54 ? 177 PHE A CZ  1 
ATOM   1397 N  N   . ASN A 1 178 ? 0.369   22.809  -25.866 1.00 15.52 ? 178 ASN A N   1 
ATOM   1398 C  CA  . ASN A 1 178 ? -0.779  21.917  -25.915 1.00 16.34 ? 178 ASN A CA  1 
ATOM   1399 C  C   . ASN A 1 178 ? -0.774  20.857  -24.766 1.00 14.69 ? 178 ASN A C   1 
ATOM   1400 O  O   . ASN A 1 178 ? -0.075  19.859  -24.803 1.00 16.85 ? 178 ASN A O   1 
ATOM   1401 C  CB  . ASN A 1 178 ? -0.959  21.305  -27.329 1.00 18.08 ? 178 ASN A CB  1 
ATOM   1402 C  CG  . ASN A 1 178 ? -2.321  20.650  -27.519 1.00 17.33 ? 178 ASN A CG  1 
ATOM   1403 O  OD1 . ASN A 1 178 ? -3.132  20.608  -26.605 1.00 17.56 ? 178 ASN A OD1 1 
ATOM   1404 N  ND2 . ASN A 1 178 ? -2.567  20.102  -28.721 1.00 18.66 ? 178 ASN A ND2 1 
ATOM   1405 N  N   . ILE A 1 179 ? -1.584  21.075  -23.738 1.00 13.36 ? 179 ILE A N   1 
ATOM   1406 C  CA  . ILE A 1 179 ? -1.655  20.149  -22.568 1.00 13.47 ? 179 ILE A CA  1 
ATOM   1407 C  C   . ILE A 1 179 ? -2.193  18.768  -22.995 1.00 13.55 ? 179 ILE A C   1 
ATOM   1408 O  O   . ILE A 1 179 ? -1.910  17.757  -22.374 1.00 13.17 ? 179 ILE A O   1 
ATOM   1409 C  CB  . ILE A 1 179 ? -2.528  20.766  -21.386 1.00 12.43 ? 179 ILE A CB  1 
ATOM   1410 C  CG1 . ILE A 1 179 ? -2.024  22.181  -21.012 1.00 12.22 ? 179 ILE A CG1 1 
ATOM   1411 C  CG2 . ILE A 1 179 ? -2.688  19.778  -20.173 1.00 12.82 ? 179 ILE A CG2 1 
ATOM   1412 C  CD1 . ILE A 1 179 ? -0.698  22.267  -20.260 1.00 12.11 ? 179 ILE A CD1 1 
ATOM   1413 N  N   . GLU A 1 180 ? -2.954  18.719  -24.078 1.00 15.05 ? 180 GLU A N   1 
ATOM   1414 C  CA  . GLU A 1 180 ? -3.405  17.436  -24.606 1.00 17.98 ? 180 GLU A CA  1 
ATOM   1415 C  C   . GLU A 1 180 ? -2.209  16.538  -25.010 1.00 16.05 ? 180 GLU A C   1 
ATOM   1416 O  O   . GLU A 1 180 ? -2.321  15.294  -25.116 1.00 15.54 ? 180 GLU A O   1 
ATOM   1417 C  CB  . GLU A 1 180 ? -4.358  17.642  -25.812 1.00 19.99 ? 180 GLU A CB  1 
ATOM   1418 C  CG  . GLU A 1 180 ? -4.951  16.331  -26.279 1.00 23.55 ? 180 GLU A CG  1 
ATOM   1419 C  CD  . GLU A 1 180 ? -6.295  16.455  -26.980 1.00 30.70 ? 180 GLU A CD  1 
ATOM   1420 O  OE1 . GLU A 1 180 ? -6.717  17.579  -27.311 1.00 34.77 ? 180 GLU A OE1 1 
ATOM   1421 O  OE2 . GLU A 1 180 ? -6.925  15.394  -27.225 1.00 38.02 ? 180 GLU A OE2 1 
ATOM   1422 N  N   . GLU A 1 181 ? -1.063  17.165  -25.206 1.00 16.43 ? 181 GLU A N   1 
ATOM   1423 C  CA  . GLU A 1 181 ? 0.147   16.402  -25.596 1.00 16.82 ? 181 GLU A CA  1 
ATOM   1424 C  C   . GLU A 1 181 ? 0.787   15.731  -24.395 1.00 14.79 ? 181 GLU A C   1 
ATOM   1425 O  O   . GLU A 1 181 ? 1.670   14.935  -24.596 1.00 15.74 ? 181 GLU A O   1 
ATOM   1426 C  CB  . GLU A 1 181 ? 1.149   17.244  -26.374 1.00 19.16 ? 181 GLU A CB  1 
ATOM   1427 C  CG  . GLU A 1 181 ? 0.521   17.642  -27.684 1.00 26.63 ? 181 GLU A CG  1 
ATOM   1428 C  CD  . GLU A 1 181 ? 1.482   18.245  -28.649 1.00 33.06 ? 181 GLU A CD  1 
ATOM   1429 O  OE1 . GLU A 1 181 ? 1.765   19.476  -28.537 1.00 34.30 ? 181 GLU A OE1 1 
ATOM   1430 O  OE2 . GLU A 1 181 ? 1.896   17.476  -29.555 1.00 41.31 ? 181 GLU A OE2 1 
ATOM   1431 N  N   . LEU A 1 182 ? 0.293   16.007  -23.178 1.00 13.74 ? 182 LEU A N   1 
ATOM   1432 C  CA  . LEU A 1 182 ? 0.698   15.201  -21.974 1.00 12.10 ? 182 LEU A CA  1 
ATOM   1433 C  C   . LEU A 1 182 ? -0.130  13.910  -21.771 1.00 12.19 ? 182 LEU A C   1 
ATOM   1434 O  O   . LEU A 1 182 ? 0.191   13.115  -20.878 1.00 13.29 ? 182 LEU A O   1 
ATOM   1435 C  CB  . LEU A 1 182 ? 0.672   16.022  -20.698 1.00 11.40 ? 182 LEU A CB  1 
ATOM   1436 C  CG  . LEU A 1 182 ? 1.400   17.375  -20.855 1.00 10.38 ? 182 LEU A CG  1 
ATOM   1437 C  CD1 . LEU A 1 182 ? 1.134   18.085  -19.546 1.00 9.75  ? 182 LEU A CD1 1 
ATOM   1438 C  CD2 . LEU A 1 182 ? 2.884   17.155  -21.080 1.00 10.31 ? 182 LEU A CD2 1 
ATOM   1439 N  N   . LEU A 1 183 ? -1.219  13.774  -22.546 1.00 11.30 ? 183 LEU A N   1 
ATOM   1440 C  CA  . LEU A 1 183 ? -2.133  12.642  -22.456 1.00 11.88 ? 183 LEU A CA  1 
ATOM   1441 C  C   . LEU A 1 183 ? -1.595  11.500  -23.290 1.00 12.49 ? 183 LEU A C   1 
ATOM   1442 O  O   . LEU A 1 183 ? -0.908  11.719  -24.340 1.00 12.41 ? 183 LEU A O   1 
ATOM   1443 C  CB  . LEU A 1 183 ? -3.523  13.017  -22.955 1.00 12.41 ? 183 LEU A CB  1 
ATOM   1444 C  CG  . LEU A 1 183 ? -4.134  14.219  -22.173 1.00 13.11 ? 183 LEU A CG  1 
ATOM   1445 C  CD1 . LEU A 1 183 ? -5.586  14.501  -22.591 1.00 14.56 ? 183 LEU A CD1 1 
ATOM   1446 C  CD2 . LEU A 1 183 ? -3.965  14.096  -20.617 1.00 12.75 ? 183 LEU A CD2 1 
ATOM   1447 N  N   . PRO A 1 184 ? -1.925  10.283  -22.865 1.00 12.76 ? 184 PRO A N   1 
ATOM   1448 C  CA  . PRO A 1 184 ? -1.421  9.065   -23.511 1.00 13.61 ? 184 PRO A CA  1 
ATOM   1449 C  C   . PRO A 1 184 ? -2.264  8.685   -24.741 1.00 15.21 ? 184 PRO A C   1 
ATOM   1450 O  O   . PRO A 1 184 ? -3.240  9.397   -25.060 1.00 12.80 ? 184 PRO A O   1 
ATOM   1451 C  CB  . PRO A 1 184 ? -1.584  8.031   -22.401 1.00 14.05 ? 184 PRO A CB  1 
ATOM   1452 C  CG  . PRO A 1 184 ? -2.798  8.501   -21.650 1.00 13.42 ? 184 PRO A CG  1 
ATOM   1453 C  CD  . PRO A 1 184 ? -2.651  10.002  -21.612 1.00 13.77 ? 184 PRO A CD  1 
ATOM   1454 N  N   . GLU A 1 185 ? -1.875  7.610   -25.438 1.00 15.72 ? 185 GLU A N   1 
ATOM   1455 C  CA  . GLU A 1 185 ? -2.725  7.140   -26.570 1.00 18.89 ? 185 GLU A CA  1 
ATOM   1456 C  C   . GLU A 1 185 ? -4.066  6.613   -26.096 1.00 17.90 ? 185 GLU A C   1 
ATOM   1457 O  O   . GLU A 1 185 ? -4.201  6.085   -24.974 1.00 17.46 ? 185 GLU A O   1 
ATOM   1458 C  CB  . GLU A 1 185 ? -2.043  6.005   -27.296 1.00 20.24 ? 185 GLU A CB  1 
ATOM   1459 C  CG  . GLU A 1 185 ? -0.646  6.334   -27.727 1.00 24.16 ? 185 GLU A CG  1 
ATOM   1460 C  CD  . GLU A 1 185 ? 0.004   5.245   -28.536 1.00 31.26 ? 185 GLU A CD  1 
ATOM   1461 O  OE1 . GLU A 1 185 ? -0.592  4.137   -28.702 1.00 36.45 ? 185 GLU A OE1 1 
ATOM   1462 O  OE2 . GLU A 1 185 ? 1.131   5.520   -29.007 1.00 35.75 ? 185 GLU A OE2 1 
ATOM   1463 N  N   A ARG A 1 186 ? -5.056  6.715   -26.974 0.50 18.17 ? 186 ARG A N   1 
ATOM   1464 N  N   B ARG A 1 186 ? -5.061  6.681   -26.974 0.50 18.55 ? 186 ARG A N   1 
ATOM   1465 C  CA  A ARG A 1 186 ? -6.382  6.179   -26.695 0.50 17.93 ? 186 ARG A CA  1 
ATOM   1466 C  CA  B ARG A 1 186 ? -6.399  6.176   -26.656 0.50 18.59 ? 186 ARG A CA  1 
ATOM   1467 C  C   A ARG A 1 186 ? -6.984  6.668   -25.348 0.50 17.44 ? 186 ARG A C   1 
ATOM   1468 C  C   B ARG A 1 186 ? -6.974  6.676   -25.319 0.50 17.71 ? 186 ARG A C   1 
ATOM   1469 O  O   A ARG A 1 186 ? -7.317  5.861   -24.476 0.50 17.19 ? 186 ARG A O   1 
ATOM   1470 O  O   B ARG A 1 186 ? -7.288  5.886   -24.426 0.50 17.45 ? 186 ARG A O   1 
ATOM   1471 C  CB  A ARG A 1 186 ? -6.368  4.633   -26.816 0.50 18.38 ? 186 ARG A CB  1 
ATOM   1472 C  CB  B ARG A 1 186 ? -6.442  4.639   -26.712 0.50 19.67 ? 186 ARG A CB  1 
ATOM   1473 C  CG  A ARG A 1 186 ? -5.764  4.133   -28.140 0.50 19.11 ? 186 ARG A CG  1 
ATOM   1474 C  CG  B ARG A 1 186 ? -6.188  4.073   -28.100 0.50 21.74 ? 186 ARG A CG  1 
ATOM   1475 C  CD  A ARG A 1 186 ? -5.693  2.602   -28.247 0.50 18.72 ? 186 ARG A CD  1 
ATOM   1476 C  CD  B ARG A 1 186 ? -6.301  2.556   -28.085 0.50 21.77 ? 186 ARG A CD  1 
ATOM   1477 N  NE  A ARG A 1 186 ? -4.409  2.072   -27.791 0.50 20.34 ? 186 ARG A NE  1 
ATOM   1478 N  NE  B ARG A 1 186 ? -6.743  2.058   -29.382 0.50 23.75 ? 186 ARG A NE  1 
ATOM   1479 C  CZ  A ARG A 1 186 ? -3.266  2.176   -28.467 0.50 19.46 ? 186 ARG A CZ  1 
ATOM   1480 C  CZ  B ARG A 1 186 ? -5.927  1.839   -30.403 0.50 25.13 ? 186 ARG A CZ  1 
ATOM   1481 N  NH1 A ARG A 1 186 ? -2.138  1.697   -27.950 0.50 21.09 ? 186 ARG A NH1 1 
ATOM   1482 N  NH1 B ARG A 1 186 ? -6.405  1.401   -31.559 0.50 25.63 ? 186 ARG A NH1 1 
ATOM   1483 N  NH2 A ARG A 1 186 ? -3.246  2.788   -29.640 0.50 19.37 ? 186 ARG A NH2 1 
ATOM   1484 N  NH2 B ARG A 1 186 ? -4.626  2.061   -30.266 0.50 27.04 ? 186 ARG A NH2 1 
ATOM   1485 N  N   . THR A 1 187 ? -7.143  7.988   -25.212 1.00 17.25 ? 187 THR A N   1 
ATOM   1486 C  CA  . THR A 1 187 ? -7.788  8.609   -24.032 1.00 16.42 ? 187 THR A CA  1 
ATOM   1487 C  C   . THR A 1 187 ? -9.253  8.217   -23.797 1.00 15.51 ? 187 THR A C   1 
ATOM   1488 O  O   . THR A 1 187 ? -9.809  8.481   -22.719 1.00 15.99 ? 187 THR A O   1 
ATOM   1489 C  CB  . THR A 1 187 ? -7.720  10.150  -24.069 1.00 16.20 ? 187 THR A CB  1 
ATOM   1490 O  OG1 . THR A 1 187 ? -8.148  10.645  -25.359 1.00 16.16 ? 187 THR A OG1 1 
ATOM   1491 C  CG2 . THR A 1 187 ? -6.282  10.592  -23.808 1.00 15.99 ? 187 THR A CG2 1 
ATOM   1492 N  N   . ALA A 1 188 ? -9.862  7.602   -24.808 1.00 14.50 ? 188 ALA A N   1 
ATOM   1493 C  CA  . ALA A 1 188 ? -11.201 6.991   -24.675 1.00 14.17 ? 188 ALA A CA  1 
ATOM   1494 C  C   . ALA A 1 188 ? -11.201 5.801   -23.693 1.00 13.26 ? 188 ALA A C   1 
ATOM   1495 O  O   . ALA A 1 188 ? -12.233 5.503   -23.125 1.00 13.10 ? 188 ALA A O   1 
ATOM   1496 C  CB  . ALA A 1 188 ? -11.752 6.524   -26.033 1.00 13.69 ? 188 ALA A CB  1 
ATOM   1497 N  N   . GLU A 1 189 ? -10.067 5.113   -23.552 1.00 12.69 ? 189 GLU A N   1 
ATOM   1498 C  CA  . GLU A 1 189 ? -9.887  4.026   -22.582 1.00 12.87 ? 189 GLU A CA  1 
ATOM   1499 C  C   . GLU A 1 189 ? -9.387  4.482   -21.233 1.00 12.46 ? 189 GLU A C   1 
ATOM   1500 O  O   . GLU A 1 189 ? -8.252  4.931   -21.145 1.00 12.47 ? 189 GLU A O   1 
ATOM   1501 C  CB  . GLU A 1 189 ? -8.934  3.028   -23.197 1.00 12.98 ? 189 GLU A CB  1 
ATOM   1502 C  CG  . GLU A 1 189 ? -9.423  2.563   -24.551 1.00 14.97 ? 189 GLU A CG  1 
ATOM   1503 C  CD  . GLU A 1 189 ? -8.495  1.567   -25.197 1.00 15.29 ? 189 GLU A CD  1 
ATOM   1504 O  OE1 . GLU A 1 189 ? -7.559  1.135   -24.544 1.00 16.69 ? 189 GLU A OE1 1 
ATOM   1505 O  OE2 . GLU A 1 189 ? -8.734  1.206   -26.353 1.00 16.57 ? 189 GLU A OE2 1 
ATOM   1506 N  N   . TYR A 1 190 ? -10.231 4.350   -20.188 1.00 12.96 ? 190 TYR A N   1 
ATOM   1507 C  CA  . TYR A 1 190 ? -9.890  4.816   -18.832 1.00 11.55 ? 190 TYR A CA  1 
ATOM   1508 C  C   . TYR A 1 190 ? -10.587 4.047   -17.716 1.00 11.17 ? 190 TYR A C   1 
ATOM   1509 O  O   . TYR A 1 190 ? -11.628 3.339   -17.946 1.00 10.85 ? 190 TYR A O   1 
ATOM   1510 C  CB  . TYR A 1 190 ? -10.230 6.313   -18.639 1.00 12.62 ? 190 TYR A CB  1 
ATOM   1511 C  CG  . TYR A 1 190 ? -11.673 6.709   -18.930 1.00 12.75 ? 190 TYR A CG  1 
ATOM   1512 C  CD1 . TYR A 1 190 ? -12.680 6.590   -17.969 1.00 11.70 ? 190 TYR A CD1 1 
ATOM   1513 C  CD2 . TYR A 1 190 ? -12.015 7.279   -20.198 1.00 13.32 ? 190 TYR A CD2 1 
ATOM   1514 C  CE1 . TYR A 1 190 ? -14.017 6.987   -18.247 1.00 12.64 ? 190 TYR A CE1 1 
ATOM   1515 C  CE2 . TYR A 1 190 ? -13.323 7.644   -20.483 1.00 13.66 ? 190 TYR A CE2 1 
ATOM   1516 C  CZ  . TYR A 1 190 ? -14.314 7.519   -19.506 1.00 12.93 ? 190 TYR A CZ  1 
ATOM   1517 O  OH  . TYR A 1 190 ? -15.588 7.914   -19.874 1.00 12.87 ? 190 TYR A OH  1 
ATOM   1518 N  N   . TYR A 1 191 ? -10.037 4.186   -16.502 1.00 10.21 ? 191 TYR A N   1 
ATOM   1519 C  CA  . TYR A 1 191 ? -10.682 3.756   -15.279 1.00 10.08 ? 191 TYR A CA  1 
ATOM   1520 C  C   . TYR A 1 191 ? -11.376 4.943   -14.651 1.00 10.13 ? 191 TYR A C   1 
ATOM   1521 O  O   . TYR A 1 191 ? -10.794 6.035   -14.588 1.00 10.56 ? 191 TYR A O   1 
ATOM   1522 C  CB  . TYR A 1 191 ? -9.627  3.305   -14.219 1.00 8.66  ? 191 TYR A CB  1 
ATOM   1523 C  CG  . TYR A 1 191 ? -8.639  2.281   -14.680 1.00 9.42  ? 191 TYR A CG  1 
ATOM   1524 C  CD1 . TYR A 1 191 ? -7.419  2.661   -15.246 1.00 9.31  ? 191 TYR A CD1 1 
ATOM   1525 C  CD2 . TYR A 1 191 ? -8.912  0.925   -14.548 1.00 9.24  ? 191 TYR A CD2 1 
ATOM   1526 C  CE1 . TYR A 1 191 ? -6.460  1.710   -15.663 1.00 10.52 ? 191 TYR A CE1 1 
ATOM   1527 C  CE2 . TYR A 1 191 ? -7.971  -0.016  -14.925 1.00 10.52 ? 191 TYR A CE2 1 
ATOM   1528 C  CZ  . TYR A 1 191 ? -6.776  0.374   -15.517 1.00 9.95  ? 191 TYR A CZ  1 
ATOM   1529 O  OH  . TYR A 1 191 ? -5.910  -0.595  -15.931 1.00 13.31 ? 191 TYR A OH  1 
ATOM   1530 N  N   . ARG A 1 192 ? -12.549 4.690   -14.085 1.00 10.75 ? 192 ARG A N   1 
ATOM   1531 C  CA  . ARG A 1 192 ? -13.396 5.713   -13.435 1.00 10.76 ? 192 ARG A CA  1 
ATOM   1532 C  C   . ARG A 1 192 ? -13.900 5.285   -12.040 1.00 11.08 ? 192 ARG A C   1 
ATOM   1533 O  O   . ARG A 1 192 ? -14.466 4.189   -11.866 1.00 11.68 ? 192 ARG A O   1 
ATOM   1534 C  CB  . ARG A 1 192 ? -14.593 6.041   -14.384 1.00 11.13 ? 192 ARG A CB  1 
ATOM   1535 C  CG  . ARG A 1 192 ? -15.699 6.909   -13.732 1.00 12.32 ? 192 ARG A CG  1 
ATOM   1536 C  CD  . ARG A 1 192 ? -15.272 8.382   -13.448 1.00 12.28 ? 192 ARG A CD  1 
ATOM   1537 N  NE  . ARG A 1 192 ? -14.659 9.078   -14.613 1.00 12.56 ? 192 ARG A NE  1 
ATOM   1538 C  CZ  . ARG A 1 192 ? -15.312 9.424   -15.751 1.00 13.14 ? 192 ARG A CZ  1 
ATOM   1539 N  NH1 . ARG A 1 192 ? -14.674 10.013  -16.754 1.00 12.50 ? 192 ARG A NH1 1 
ATOM   1540 N  NH2 . ARG A 1 192 ? -16.613 9.235   -15.880 1.00 11.92 ? 192 ARG A NH2 1 
ATOM   1541 N  N   . TYR A 1 193 ? -13.705 6.142   -11.030 1.00 10.15 ? 193 TYR A N   1 
ATOM   1542 C  CA  . TYR A 1 193 ? -14.260 5.888   -9.710  1.00 10.52 ? 193 TYR A CA  1 
ATOM   1543 C  C   . TYR A 1 193 ? -14.376 7.150   -8.878  1.00 10.81 ? 193 TYR A C   1 
ATOM   1544 O  O   . TYR A 1 193 ? -13.752 8.196   -9.221  1.00 11.65 ? 193 TYR A O   1 
ATOM   1545 C  CB  . TYR A 1 193 ? -13.440 4.762   -8.970  1.00 9.60  ? 193 TYR A CB  1 
ATOM   1546 C  CG  . TYR A 1 193 ? -12.103 5.248   -8.377  1.00 9.17  ? 193 TYR A CG  1 
ATOM   1547 C  CD1 . TYR A 1 193 ? -12.003 5.577   -7.036  1.00 9.47  ? 193 TYR A CD1 1 
ATOM   1548 C  CD2 . TYR A 1 193 ? -10.991 5.413   -9.193  1.00 8.70  ? 193 TYR A CD2 1 
ATOM   1549 C  CE1 . TYR A 1 193 ? -10.793 6.008   -6.504  1.00 9.12  ? 193 TYR A CE1 1 
ATOM   1550 C  CE2 . TYR A 1 193 ? -9.774  5.876   -8.677  1.00 8.77  ? 193 TYR A CE2 1 
ATOM   1551 C  CZ  . TYR A 1 193 ? -9.706  6.167   -7.347  1.00 8.92  ? 193 TYR A CZ  1 
ATOM   1552 O  OH  . TYR A 1 193 ? -8.534  6.655   -6.820  1.00 9.55  ? 193 TYR A OH  1 
ATOM   1553 N  N   . ARG A 1 194 ? -15.179 7.058   -7.808  1.00 11.29 ? 194 ARG A N   1 
ATOM   1554 C  CA  . ARG A 1 194 ? -15.301 8.088   -6.862  1.00 12.75 ? 194 ARG A CA  1 
ATOM   1555 C  C   . ARG A 1 194 ? -14.257 7.969   -5.735  1.00 11.71 ? 194 ARG A C   1 
ATOM   1556 O  O   . ARG A 1 194 ? -14.191 6.952   -5.040  1.00 11.08 ? 194 ARG A O   1 
ATOM   1557 C  CB  . ARG A 1 194 ? -16.719 8.088   -6.265  1.00 16.17 ? 194 ARG A CB  1 
ATOM   1558 C  CG  . ARG A 1 194 ? -17.745 8.692   -7.193  1.00 21.15 ? 194 ARG A CG  1 
ATOM   1559 C  CD  . ARG A 1 194 ? -17.587 10.219  -7.159  1.00 26.59 ? 194 ARG A CD  1 
ATOM   1560 N  NE  . ARG A 1 194 ? -18.121 10.873  -5.946  1.00 37.73 ? 194 ARG A NE  1 
ATOM   1561 C  CZ  . ARG A 1 194 ? -17.858 12.144  -5.592  1.00 36.25 ? 194 ARG A CZ  1 
ATOM   1562 N  NH1 . ARG A 1 194 ? -17.069 12.899  -6.346  1.00 31.39 ? 194 ARG A NH1 1 
ATOM   1563 N  NH2 . ARG A 1 194 ? -18.390 12.659  -4.483  1.00 38.50 ? 194 ARG A NH2 1 
ATOM   1564 N  N   . GLY A 1 195 ? -13.473 9.016   -5.541  1.00 11.13 ? 195 GLY A N   1 
ATOM   1565 C  CA  . GLY A 1 195 ? -12.459 8.992   -4.454  1.00 10.31 ? 195 GLY A CA  1 
ATOM   1566 C  C   . GLY A 1 195 ? -12.168 10.346  -3.870  1.00 10.15 ? 195 GLY A C   1 
ATOM   1567 O  O   . GLY A 1 195 ? -13.086 11.164  -3.704  1.00 10.20 ? 195 GLY A O   1 
ATOM   1568 N  N   . SER A 1 196 ? -10.898 10.560  -3.495  1.00 10.89 ? 196 SER A N   1 
ATOM   1569 C  CA  . SER A 1 196 ? -10.520 11.711  -2.734  1.00 10.71 ? 196 SER A CA  1 
ATOM   1570 C  C   . SER A 1 196 ? -9.285  12.364  -3.301  1.00 10.69 ? 196 SER A C   1 
ATOM   1571 O  O   . SER A 1 196 ? -8.582  11.783  -4.132  1.00 9.75  ? 196 SER A O   1 
ATOM   1572 C  CB  . SER A 1 196 ? -10.186 11.301  -1.284  1.00 10.86 ? 196 SER A CB  1 
ATOM   1573 O  OG  . SER A 1 196 ? -8.966  10.545  -1.210  1.00 13.36 ? 196 SER A OG  1 
ATOM   1574 N  N   . LEU A 1 197 ? -9.024  13.592  -2.854  1.00 10.96 ? 197 LEU A N   1 
ATOM   1575 C  CA  . LEU A 1 197 ? -7.682  14.142  -3.004  1.00 11.21 ? 197 LEU A CA  1 
ATOM   1576 C  C   . LEU A 1 197 ? -6.695  13.207  -2.280  1.00 10.85 ? 197 LEU A C   1 
ATOM   1577 O  O   . LEU A 1 197 ? -7.013  12.730  -1.180  1.00 12.06 ? 197 LEU A O   1 
ATOM   1578 C  CB  . LEU A 1 197 ? -7.557  15.467  -2.336  1.00 12.04 ? 197 LEU A CB  1 
ATOM   1579 C  CG  . LEU A 1 197 ? -8.376  16.602  -2.907  1.00 14.38 ? 197 LEU A CG  1 
ATOM   1580 C  CD1 . LEU A 1 197 ? -8.093  17.795  -2.032  1.00 16.09 ? 197 LEU A CD1 1 
ATOM   1581 C  CD2 . LEU A 1 197 ? -7.956  16.866  -4.319  1.00 15.32 ? 197 LEU A CD2 1 
ATOM   1582 N  N   . THR A 1 198 ? -5.525  12.980  -2.886  1.00 10.11 ? 198 THR A N   1 
ATOM   1583 C  CA  . THR A 1 198 ? -4.487  12.039  -2.321  1.00 9.57  ? 198 THR A CA  1 
ATOM   1584 C  C   . THR A 1 198 ? -3.524  12.746  -1.398  1.00 9.57  ? 198 THR A C   1 
ATOM   1585 O  O   . THR A 1 198 ? -2.599  12.116  -0.891  1.00 9.87  ? 198 THR A O   1 
ATOM   1586 C  CB  . THR A 1 198 ? -3.599  11.414  -3.438  1.00 9.64  ? 198 THR A CB  1 
ATOM   1587 O  OG1 . THR A 1 198 ? -2.893  12.429  -4.157  1.00 9.53  ? 198 THR A OG1 1 
ATOM   1588 C  CG2 . THR A 1 198 ? -4.460  10.606  -4.417  1.00 9.02  ? 198 THR A CG2 1 
ATOM   1589 N  N   A THR A 1 199 ? -3.790  14.032  -1.165  0.50 9.51  ? 199 THR A N   1 
ATOM   1590 N  N   B THR A 1 199 ? -3.708  14.066  -1.227  0.50 9.12  ? 199 THR A N   1 
ATOM   1591 C  CA  A THR A 1 199 ? -2.975  14.888  -0.328  0.50 10.56 ? 199 THR A CA  1 
ATOM   1592 C  CA  B THR A 1 199 ? -2.933  14.851  -0.246  0.50 9.82  ? 199 THR A CA  1 
ATOM   1593 C  C   A THR A 1 199 ? -3.901  15.499  0.760   0.50 10.43 ? 199 THR A C   1 
ATOM   1594 C  C   B THR A 1 199 ? -3.878  15.506  0.761   0.50 10.00 ? 199 THR A C   1 
ATOM   1595 O  O   A THR A 1 199 ? -5.102  15.659  0.529   0.50 9.67  ? 199 THR A O   1 
ATOM   1596 O  O   B THR A 1 199 ? -5.053  15.744  0.462   0.50 9.33  ? 199 THR A O   1 
ATOM   1597 C  CB  A THR A 1 199 ? -2.384  15.988  -1.240  0.50 11.39 ? 199 THR A CB  1 
ATOM   1598 C  CB  B THR A 1 199 ? -2.107  15.980  -0.911  0.50 9.66  ? 199 THR A CB  1 
ATOM   1599 O  OG1 A THR A 1 199 ? -1.329  15.461  -2.090  0.50 11.14 ? 199 THR A OG1 1 
ATOM   1600 O  OG1 B THR A 1 199 ? -2.992  16.857  -1.645  0.50 9.25  ? 199 THR A OG1 1 
ATOM   1601 C  CG2 A THR A 1 199 ? -1.916  17.131  -0.467  0.50 10.50 ? 199 THR A CG2 1 
ATOM   1602 C  CG2 B THR A 1 199 ? -1.089  15.396  -1.931  0.50 9.73  ? 199 THR A CG2 1 
ATOM   1603 N  N   . PRO A 1 200 ? -3.379  15.819  1.958   1.00 9.52  ? 200 PRO A N   1 
ATOM   1604 C  CA  . PRO A 1 200 ? -4.263  16.540  2.908   1.00 9.91  ? 200 PRO A CA  1 
ATOM   1605 C  C   . PRO A 1 200 ? -4.824  17.831  2.209   1.00 10.94 ? 200 PRO A C   1 
ATOM   1606 O  O   . PRO A 1 200 ? -4.089  18.471  1.447   1.00 11.60 ? 200 PRO A O   1 
ATOM   1607 C  CB  . PRO A 1 200 ? -3.297  16.896  4.083   1.00 9.83  ? 200 PRO A CB  1 
ATOM   1608 C  CG  . PRO A 1 200 ? -2.292  15.795  4.025   1.00 9.46  ? 200 PRO A CG  1 
ATOM   1609 C  CD  . PRO A 1 200 ? -2.087  15.472  2.553   1.00 10.33 ? 200 PRO A CD  1 
ATOM   1610 N  N   . PRO A 1 201 ? -6.115  18.219  2.451   1.00 10.69 ? 201 PRO A N   1 
ATOM   1611 C  CA  . PRO A 1 201 ? -7.052  17.673  3.462   1.00 11.10 ? 201 PRO A CA  1 
ATOM   1612 C  C   . PRO A 1 201 ? -7.784  16.392  3.072   1.00 11.53 ? 201 PRO A C   1 
ATOM   1613 O  O   . PRO A 1 201 ? -8.698  16.046  3.754   1.00 11.82 ? 201 PRO A O   1 
ATOM   1614 C  CB  . PRO A 1 201 ? -8.107  18.773  3.622   1.00 11.57 ? 201 PRO A CB  1 
ATOM   1615 C  CG  . PRO A 1 201 ? -7.444  19.988  3.086   1.00 12.49 ? 201 PRO A CG  1 
ATOM   1616 C  CD  . PRO A 1 201 ? -6.654  19.462  1.883   1.00 12.21 ? 201 PRO A CD  1 
ATOM   1617 N  N   . CYS A 1 202 ? -7.321  15.683  2.043   1.00 11.39 ? 202 CYS A N   1 
ATOM   1618 C  CA  . CYS A 1 202 ? -7.940  14.408  1.603   1.00 12.30 ? 202 CYS A CA  1 
ATOM   1619 C  C   . CYS A 1 202 ? -9.464  14.428  1.333   1.00 12.35 ? 202 CYS A C   1 
ATOM   1620 O  O   . CYS A 1 202 ? -10.154 13.420  1.560   1.00 12.78 ? 202 CYS A O   1 
ATOM   1621 C  CB  . CYS A 1 202 ? -7.589  13.262  2.578   1.00 13.17 ? 202 CYS A CB  1 
ATOM   1622 S  SG  . CYS A 1 202 ? -5.821  13.080  2.993   1.00 12.40 ? 202 CYS A SG  1 
ATOM   1623 N  N   . ASN A 1 203 ? -9.987  15.524  0.823   1.00 12.70 ? 203 ASN A N   1 
ATOM   1624 C  CA  . ASN A 1 203 ? -11.470 15.658  0.673   1.00 13.02 ? 203 ASN A CA  1 
ATOM   1625 C  C   . ASN A 1 203 ? -12.054 14.541  -0.218  1.00 12.51 ? 203 ASN A C   1 
ATOM   1626 O  O   . ASN A 1 203 ? -11.504 14.280  -1.329  1.00 11.11 ? 203 ASN A O   1 
ATOM   1627 C  CB  . ASN A 1 203 ? -11.866 16.963  0.046   1.00 15.21 ? 203 ASN A CB  1 
ATOM   1628 C  CG  . ASN A 1 203 ? -11.410 18.169  0.815   1.00 18.48 ? 203 ASN A CG  1 
ATOM   1629 O  OD1 . ASN A 1 203 ? -10.922 18.090  1.924   1.00 23.88 ? 203 ASN A OD1 1 
ATOM   1630 N  ND2 . ASN A 1 203 ? -11.593 19.309  0.221   1.00 23.02 ? 203 ASN A ND2 1 
ATOM   1631 N  N   . PRO A 1 204 ? -13.140 13.890  0.241   1.00 12.83 ? 204 PRO A N   1 
ATOM   1632 C  CA  . PRO A 1 204 ? -13.640 12.741  -0.481  1.00 12.66 ? 204 PRO A CA  1 
ATOM   1633 C  C   . PRO A 1 204 ? -14.559 13.206  -1.613  1.00 13.56 ? 204 PRO A C   1 
ATOM   1634 O  O   . PRO A 1 204 ? -15.674 12.676  -1.799  1.00 14.21 ? 204 PRO A O   1 
ATOM   1635 C  CB  . PRO A 1 204 ? -14.332 11.899  0.611   1.00 12.88 ? 204 PRO A CB  1 
ATOM   1636 C  CG  . PRO A 1 204 ? -14.881 12.978  1.530   1.00 13.18 ? 204 PRO A CG  1 
ATOM   1637 C  CD  . PRO A 1 204 ? -13.750 14.012  1.590   1.00 12.78 ? 204 PRO A CD  1 
ATOM   1638 N  N   . THR A 1 205 ? -14.038 14.139  -2.412  1.00 13.30 ? 205 THR A N   1 
ATOM   1639 C  CA  . THR A 1 205 ? -14.891 14.884  -3.343  1.00 14.14 ? 205 THR A CA  1 
ATOM   1640 C  C   . THR A 1 205 ? -14.472 14.758  -4.817  1.00 13.11 ? 205 THR A C   1 
ATOM   1641 O  O   . THR A 1 205 ? -14.905 15.556  -5.657  1.00 14.33 ? 205 THR A O   1 
ATOM   1642 C  CB  . THR A 1 205 ? -14.921 16.367  -2.957  1.00 14.37 ? 205 THR A CB  1 
ATOM   1643 O  OG1 . THR A 1 205 ? -13.589 16.821  -2.893  1.00 14.13 ? 205 THR A OG1 1 
ATOM   1644 C  CG2 . THR A 1 205 ? -15.608 16.622  -1.602  1.00 14.26 ? 205 THR A CG2 1 
ATOM   1645 N  N   . VAL A 1 206 ? -13.675 13.755  -5.156  1.00 11.84 ? 206 VAL A N   1 
ATOM   1646 C  CA  . VAL A 1 206 ? -13.039 13.682  -6.495  1.00 11.03 ? 206 VAL A CA  1 
ATOM   1647 C  C   . VAL A 1 206 ? -13.663 12.609  -7.343  1.00 11.89 ? 206 VAL A C   1 
ATOM   1648 O  O   . VAL A 1 206 ? -13.686 11.426  -6.978  1.00 11.17 ? 206 VAL A O   1 
ATOM   1649 C  CB  . VAL A 1 206 ? -11.512 13.333  -6.385  1.00 10.81 ? 206 VAL A CB  1 
ATOM   1650 C  CG1 . VAL A 1 206 ? -10.829 13.322  -7.757  1.00 10.12 ? 206 VAL A CG1 1 
ATOM   1651 C  CG2 . VAL A 1 206 ? -10.798 14.381  -5.533  1.00 11.14 ? 206 VAL A CG2 1 
ATOM   1652 N  N   . LEU A 1 207 ? -14.066 13.001  -8.537  1.00 10.83 ? 207 LEU A N   1 
ATOM   1653 C  CA  . LEU A 1 207 ? -14.327 12.013  -9.538  1.00 11.44 ? 207 LEU A CA  1 
ATOM   1654 C  C   . LEU A 1 207 ? -13.030 11.715  -10.269 1.00 10.97 ? 207 LEU A C   1 
ATOM   1655 O  O   . LEU A 1 207 ? -12.515 12.585  -10.971 1.00 11.46 ? 207 LEU A O   1 
ATOM   1656 C  CB  . LEU A 1 207 ? -15.437 12.489  -10.523 1.00 13.07 ? 207 LEU A CB  1 
ATOM   1657 C  CG  . LEU A 1 207 ? -15.970 11.343  -11.421 1.00 14.63 ? 207 LEU A CG  1 
ATOM   1658 C  CD1 . LEU A 1 207 ? -16.732 10.195  -10.708 1.00 16.93 ? 207 LEU A CD1 1 
ATOM   1659 C  CD2 . LEU A 1 207 ? -16.818 11.902  -12.575 1.00 17.57 ? 207 LEU A CD2 1 
ATOM   1660 N  N   . TRP A 1 208 ? -12.519 10.483  -10.151 1.00 9.88  ? 208 TRP A N   1 
ATOM   1661 C  CA  . TRP A 1 208 ? -11.237 10.105  -10.817 1.00 9.97  ? 208 TRP A CA  1 
ATOM   1662 C  C   . TRP A 1 208 ? -11.365 9.584   -12.211 1.00 10.64 ? 208 TRP A C   1 
ATOM   1663 O  O   . TRP A 1 208 ? -12.230 8.759   -12.450 1.00 10.56 ? 208 TRP A O   1 
ATOM   1664 C  CB  . TRP A 1 208 ? -10.441 9.066   -10.004 1.00 9.65  ? 208 TRP A CB  1 
ATOM   1665 C  CG  . TRP A 1 208 ? -9.733  9.670   -8.835  1.00 9.21  ? 208 TRP A CG  1 
ATOM   1666 C  CD1 . TRP A 1 208 ? -10.164 9.728   -7.507  1.00 9.34  ? 208 TRP A CD1 1 
ATOM   1667 C  CD2 . TRP A 1 208 ? -8.459  10.401  -8.856  1.00 9.19  ? 208 TRP A CD2 1 
ATOM   1668 N  NE1 . TRP A 1 208 ? -9.205  10.400  -6.731  1.00 10.42 ? 208 TRP A NE1 1 
ATOM   1669 C  CE2 . TRP A 1 208 ? -8.186  10.811  -7.468  1.00 8.88  ? 208 TRP A CE2 1 
ATOM   1670 C  CE3 . TRP A 1 208 ? -7.522  10.712  -9.850  1.00 8.61  ? 208 TRP A CE3 1 
ATOM   1671 C  CZ2 . TRP A 1 208 ? -7.059  11.584  -7.119  1.00 9.16  ? 208 TRP A CZ2 1 
ATOM   1672 C  CZ3 . TRP A 1 208 ? -6.352  11.453  -9.478  1.00 8.53  ? 208 TRP A CZ3 1 
ATOM   1673 C  CH2 . TRP A 1 208 ? -6.129  11.867  -8.151  1.00 8.66  ? 208 TRP A CH2 1 
ATOM   1674 N  N   . THR A 1 209 ? -10.489 10.013  -13.123 1.00 10.67 ? 209 THR A N   1 
ATOM   1675 C  CA  . THR A 1 209 ? -10.305 9.354   -14.434 1.00 11.71 ? 209 THR A CA  1 
ATOM   1676 C  C   . THR A 1 209 ? -8.825  9.030   -14.614 1.00 11.16 ? 209 THR A C   1 
ATOM   1677 O  O   . THR A 1 209 ? -7.995  9.931   -14.798 1.00 10.71 ? 209 THR A O   1 
ATOM   1678 C  CB  . THR A 1 209 ? -10.786 10.285  -15.620 1.00 11.60 ? 209 THR A CB  1 
ATOM   1679 O  OG1 . THR A 1 209 ? -12.146 10.656  -15.387 1.00 12.45 ? 209 THR A OG1 1 
ATOM   1680 C  CG2 . THR A 1 209 ? -10.619 9.628   -16.977 1.00 11.92 ? 209 THR A CG2 1 
ATOM   1681 N  N   . VAL A 1 210 ? -8.496  7.734   -14.591 1.00 9.85  ? 210 VAL A N   1 
ATOM   1682 C  CA  . VAL A 1 210 ? -7.096  7.335   -14.735 1.00 10.05 ? 210 VAL A CA  1 
ATOM   1683 C  C   . VAL A 1 210 ? -6.966  6.726   -16.112 1.00 10.11 ? 210 VAL A C   1 
ATOM   1684 O  O   . VAL A 1 210 ? -7.631  5.669   -16.426 1.00 9.80  ? 210 VAL A O   1 
ATOM   1685 C  CB  . VAL A 1 210 ? -6.725  6.245   -13.703 1.00 9.67  ? 210 VAL A CB  1 
ATOM   1686 C  CG1 . VAL A 1 210 ? -5.308  5.709   -13.941 1.00 10.22 ? 210 VAL A CG1 1 
ATOM   1687 C  CG2 . VAL A 1 210 ? -6.963  6.729   -12.275 1.00 9.80  ? 210 VAL A CG2 1 
ATOM   1688 N  N   . PHE A 1 211 ? -6.141  7.346   -16.952 1.00 10.77 ? 211 PHE A N   1 
ATOM   1689 C  CA  . PHE A 1 211 ? -5.989  6.776   -18.324 1.00 12.39 ? 211 PHE A CA  1 
ATOM   1690 C  C   . PHE A 1 211 ? -5.393  5.363   -18.383 1.00 12.17 ? 211 PHE A C   1 
ATOM   1691 O  O   . PHE A 1 211 ? -4.486  5.042   -17.607 1.00 12.07 ? 211 PHE A O   1 
ATOM   1692 C  CB  . PHE A 1 211 ? -5.344  7.757   -19.298 1.00 12.18 ? 211 PHE A CB  1 
ATOM   1693 C  CG  . PHE A 1 211 ? -6.145  9.020   -19.437 1.00 11.35 ? 211 PHE A CG  1 
ATOM   1694 C  CD1 . PHE A 1 211 ? -5.644  10.235  -18.979 1.00 11.36 ? 211 PHE A CD1 1 
ATOM   1695 C  CD2 . PHE A 1 211 ? -7.382  8.996   -20.055 1.00 11.57 ? 211 PHE A CD2 1 
ATOM   1696 C  CE1 . PHE A 1 211 ? -6.365  11.420  -19.100 1.00 11.66 ? 211 PHE A CE1 1 
ATOM   1697 C  CE2 . PHE A 1 211 ? -8.103  10.176  -20.202 1.00 12.21 ? 211 PHE A CE2 1 
ATOM   1698 C  CZ  . PHE A 1 211 ? -7.584  11.386  -19.713 1.00 12.68 ? 211 PHE A CZ  1 
ATOM   1699 N  N   . ARG A 1 212 ? -5.980  4.499   -19.219 1.00 12.41 ? 212 ARG A N   1 
ATOM   1700 C  CA  . ARG A 1 212 ? -5.457  3.127   -19.317 1.00 13.37 ? 212 ARG A CA  1 
ATOM   1701 C  C   . ARG A 1 212 ? -3.941  2.996   -19.661 1.00 13.47 ? 212 ARG A C   1 
ATOM   1702 O  O   . ARG A 1 212 ? -3.241  2.202   -19.040 1.00 14.49 ? 212 ARG A O   1 
ATOM   1703 C  CB  . ARG A 1 212 ? -6.292  2.272   -20.280 1.00 14.17 ? 212 ARG A CB  1 
ATOM   1704 C  CG  . ARG A 1 212 ? -5.777  0.850   -20.393 1.00 14.38 ? 212 ARG A CG  1 
ATOM   1705 C  CD  . ARG A 1 212 ? -6.576  0.100   -21.477 1.00 16.75 ? 212 ARG A CD  1 
ATOM   1706 N  NE  . ARG A 1 212 ? -6.398  -1.349  -21.407 1.00 18.39 ? 212 ARG A NE  1 
ATOM   1707 C  CZ  . ARG A 1 212 ? -6.982  -2.223  -22.245 1.00 20.31 ? 212 ARG A CZ  1 
ATOM   1708 N  NH1 . ARG A 1 212 ? -7.771  -1.801  -23.241 1.00 20.27 ? 212 ARG A NH1 1 
ATOM   1709 N  NH2 . ARG A 1 212 ? -6.793  -3.548  -22.090 1.00 20.71 ? 212 ARG A NH2 1 
ATOM   1710 N  N   . ASN A 1 213 ? -3.454  3.781   -20.626 1.00 14.02 ? 213 ASN A N   1 
ATOM   1711 C  CA  . ASN A 1 213 ? -2.125  3.641   -21.201 1.00 13.07 ? 213 ASN A CA  1 
ATOM   1712 C  C   . ASN A 1 213 ? -1.182  4.644   -20.546 1.00 12.07 ? 213 ASN A C   1 
ATOM   1713 O  O   . ASN A 1 213 ? -1.595  5.816   -20.316 1.00 12.03 ? 213 ASN A O   1 
ATOM   1714 C  CB  . ASN A 1 213 ? -2.243  3.831   -22.716 1.00 15.56 ? 213 ASN A CB  1 
ATOM   1715 C  CG  . ASN A 1 213 ? -2.997  2.682   -23.361 1.00 18.42 ? 213 ASN A CG  1 
ATOM   1716 O  OD1 . ASN A 1 213 ? -2.873  1.539   -22.924 1.00 21.26 ? 213 ASN A OD1 1 
ATOM   1717 N  ND2 . ASN A 1 213 ? -3.824  2.979   -24.317 1.00 19.01 ? 213 ASN A ND2 1 
ATOM   1718 N  N   . PRO A 1 214 ? 0.032   4.203   -20.172 1.00 11.04 ? 214 PRO A N   1 
ATOM   1719 C  CA  . PRO A 1 214 ? 1.038   5.175   -19.659 1.00 11.71 ? 214 PRO A CA  1 
ATOM   1720 C  C   . PRO A 1 214 ? 1.665   6.026   -20.785 1.00 11.55 ? 214 PRO A C   1 
ATOM   1721 O  O   . PRO A 1 214 ? 1.562   5.668   -21.970 1.00 11.75 ? 214 PRO A O   1 
ATOM   1722 C  CB  . PRO A 1 214 ? 2.091   4.296   -19.023 1.00 11.84 ? 214 PRO A CB  1 
ATOM   1723 C  CG  . PRO A 1 214 ? 2.018   2.998   -19.776 1.00 12.75 ? 214 PRO A CG  1 
ATOM   1724 C  CD  . PRO A 1 214 ? 0.604   2.848   -20.329 1.00 12.89 ? 214 PRO A CD  1 
ATOM   1725 N  N   . VAL A 1 215 ? 2.325   7.131   -20.428 1.00 10.88 ? 215 VAL A N   1 
ATOM   1726 C  CA  . VAL A 1 215 ? 3.223   7.820   -21.391 1.00 11.90 ? 215 VAL A CA  1 
ATOM   1727 C  C   . VAL A 1 215 ? 4.664   7.458   -20.949 1.00 11.17 ? 215 VAL A C   1 
ATOM   1728 O  O   . VAL A 1 215 ? 4.834   6.952   -19.781 1.00 9.46  ? 215 VAL A O   1 
ATOM   1729 C  CB  . VAL A 1 215 ? 3.026   9.358   -21.357 1.00 11.67 ? 215 VAL A CB  1 
ATOM   1730 C  CG1 . VAL A 1 215 ? 1.616   9.721   -21.735 1.00 12.36 ? 215 VAL A CG1 1 
ATOM   1731 C  CG2 . VAL A 1 215 ? 3.346   9.934   -19.956 1.00 11.86 ? 215 VAL A CG2 1 
ATOM   1732 N  N   . GLN A 1 216 ? 5.663   7.701   -21.826 1.00 11.03 ? 216 GLN A N   1 
ATOM   1733 C  CA  . GLN A 1 216 ? 7.051   7.582   -21.421 1.00 10.52 ? 216 GLN A CA  1 
ATOM   1734 C  C   . GLN A 1 216 ? 7.757   8.943   -21.331 1.00 9.97  ? 216 GLN A C   1 
ATOM   1735 O  O   . GLN A 1 216 ? 7.475   9.877   -22.109 1.00 9.16  ? 216 GLN A O   1 
ATOM   1736 C  CB  . GLN A 1 216 ? 7.843   6.647   -22.371 1.00 12.12 ? 216 GLN A CB  1 
ATOM   1737 C  CG  . GLN A 1 216 ? 7.378   5.167   -22.297 1.00 13.28 ? 216 GLN A CG  1 
ATOM   1738 C  CD  . GLN A 1 216 ? 7.985   4.324   -23.384 1.00 14.28 ? 216 GLN A CD  1 
ATOM   1739 O  OE1 . GLN A 1 216 ? 8.993   4.713   -23.977 1.00 15.33 ? 216 GLN A OE1 1 
ATOM   1740 N  NE2 . GLN A 1 216 ? 7.338   3.178   -23.700 1.00 16.28 ? 216 GLN A NE2 1 
ATOM   1741 N  N   . ILE A 1 217 ? 8.698   9.005   -20.405 1.00 9.69  ? 217 ILE A N   1 
ATOM   1742 C  CA  . ILE A 1 217 ? 9.686   10.086  -20.308 1.00 10.36 ? 217 ILE A CA  1 
ATOM   1743 C  C   . ILE A 1 217 ? 11.074  9.413   -20.258 1.00 10.87 ? 217 ILE A C   1 
ATOM   1744 O  O   . ILE A 1 217 ? 11.125  8.237   -19.962 1.00 10.09 ? 217 ILE A O   1 
ATOM   1745 C  CB  . ILE A 1 217 ? 9.469   11.008  -19.099 1.00 10.23 ? 217 ILE A CB  1 
ATOM   1746 C  CG1 . ILE A 1 217 ? 9.628   10.269  -17.748 1.00 9.80  ? 217 ILE A CG1 1 
ATOM   1747 C  CG2 . ILE A 1 217 ? 8.181   11.799  -19.264 1.00 10.43 ? 217 ILE A CG2 1 
ATOM   1748 C  CD1 . ILE A 1 217 ? 9.626   11.199  -16.524 1.00 9.60  ? 217 ILE A CD1 1 
ATOM   1749 N  N   . SER A 1 218 ? 12.168  10.136  -20.579 1.00 11.87 ? 218 SER A N   1 
ATOM   1750 C  CA  . SER A 1 218 ? 13.502  9.550   -20.598 1.00 11.66 ? 218 SER A CA  1 
ATOM   1751 C  C   . SER A 1 218 ? 14.065  9.362   -19.187 1.00 12.05 ? 218 SER A C   1 
ATOM   1752 O  O   . SER A 1 218 ? 13.570  9.953   -18.210 1.00 10.74 ? 218 SER A O   1 
ATOM   1753 C  CB  . SER A 1 218 ? 14.469  10.384  -21.454 1.00 12.83 ? 218 SER A CB  1 
ATOM   1754 O  OG  . SER A 1 218 ? 14.877  11.593  -20.801 1.00 11.93 ? 218 SER A OG  1 
ATOM   1755 N  N   . GLN A 1 219 ? 15.089  8.518   -19.099 1.00 12.62 ? 219 GLN A N   1 
ATOM   1756 C  CA  . GLN A 1 219 ? 15.801  8.249   -17.827 1.00 14.31 ? 219 GLN A CA  1 
ATOM   1757 C  C   . GLN A 1 219 ? 16.329  9.565   -17.341 1.00 13.15 ? 219 GLN A C   1 
ATOM   1758 O  O   . GLN A 1 219 ? 16.312  9.780   -16.147 1.00 14.50 ? 219 GLN A O   1 
ATOM   1759 C  CB  . GLN A 1 219 ? 16.956  7.241   -17.993 1.00 18.08 ? 219 GLN A CB  1 
ATOM   1760 C  CG  . GLN A 1 219 ? 17.357  6.356   -16.783 1.00 23.62 ? 219 GLN A CG  1 
ATOM   1761 C  CD  . GLN A 1 219 ? 17.337  6.981   -15.392 1.00 31.13 ? 219 GLN A CD  1 
ATOM   1762 O  OE1 . GLN A 1 219 ? 18.410  7.240   -14.808 1.00 41.59 ? 219 GLN A OE1 1 
ATOM   1763 N  NE2 . GLN A 1 219 ? 16.142  7.162   -14.812 1.00 29.19 ? 219 GLN A NE2 1 
ATOM   1764 N  N   . GLU A 1 220 ? 16.751  10.452  -18.252 1.00 12.06 ? 220 GLU A N   1 
ATOM   1765 C  CA  . GLU A 1 220 ? 17.369  11.720  -17.856 1.00 12.35 ? 220 GLU A CA  1 
ATOM   1766 C  C   . GLU A 1 220 ? 16.283  12.643  -17.268 1.00 10.79 ? 220 GLU A C   1 
ATOM   1767 O  O   . GLU A 1 220 ? 16.469  13.275  -16.242 1.00 10.04 ? 220 GLU A O   1 
ATOM   1768 C  CB  . GLU A 1 220 ? 18.079  12.381  -19.043 1.00 15.69 ? 220 GLU A CB  1 
ATOM   1769 C  CG  . GLU A 1 220 ? 19.406  11.647  -19.359 1.00 21.24 ? 220 GLU A CG  1 
ATOM   1770 C  CD  . GLU A 1 220 ? 19.280  10.605  -20.464 1.00 27.82 ? 220 GLU A CD  1 
ATOM   1771 O  OE1 . GLU A 1 220 ? 18.142  10.331  -20.921 1.00 30.35 ? 220 GLU A OE1 1 
ATOM   1772 O  OE2 . GLU A 1 220 ? 20.334  10.058  -20.915 1.00 33.54 ? 220 GLU A OE2 1 
ATOM   1773 N  N   . GLN A 1 221 ? 15.138  12.688  -17.939 1.00 9.42  ? 221 GLN A N   1 
ATOM   1774 C  CA  . GLN A 1 221 ? 13.964  13.512  -17.465 1.00 8.92  ? 221 GLN A CA  1 
ATOM   1775 C  C   . GLN A 1 221 ? 13.481  13.002  -16.102 1.00 9.88  ? 221 GLN A C   1 
ATOM   1776 O  O   . GLN A 1 221 ? 13.166  13.836  -15.242 1.00 9.23  ? 221 GLN A O   1 
ATOM   1777 C  CB  . GLN A 1 221 ? 12.782  13.416  -18.458 1.00 8.89  ? 221 GLN A CB  1 
ATOM   1778 C  CG  . GLN A 1 221 ? 12.962  14.252  -19.775 1.00 10.30 ? 221 GLN A CG  1 
ATOM   1779 C  CD  . GLN A 1 221 ? 11.797  14.103  -20.751 1.00 10.54 ? 221 GLN A CD  1 
ATOM   1780 O  OE1 . GLN A 1 221 ? 11.452  12.984  -21.159 1.00 10.43 ? 221 GLN A OE1 1 
ATOM   1781 N  NE2 . GLN A 1 221 ? 11.213  15.220  -21.161 1.00 11.64 ? 221 GLN A NE2 1 
ATOM   1782 N  N   . LEU A 1 222 ? 13.308  11.673  -15.948 1.00 9.04  ? 222 LEU A N   1 
ATOM   1783 C  CA  . LEU A 1 222 ? 12.870  11.140  -14.688 1.00 10.47 ? 222 LEU A CA  1 
ATOM   1784 C  C   . LEU A 1 222 ? 13.885  11.478  -13.569 1.00 10.38 ? 222 LEU A C   1 
ATOM   1785 O  O   . LEU A 1 222 ? 13.511  11.853  -12.457 1.00 11.36 ? 222 LEU A O   1 
ATOM   1786 C  CB  . LEU A 1 222 ? 12.624  9.608   -14.800 1.00 10.96 ? 222 LEU A CB  1 
ATOM   1787 C  CG  . LEU A 1 222 ? 12.339  8.901   -13.469 1.00 11.58 ? 222 LEU A CG  1 
ATOM   1788 C  CD1 . LEU A 1 222 ? 11.131  9.501   -12.730 1.00 12.48 ? 222 LEU A CD1 1 
ATOM   1789 C  CD2 . LEU A 1 222 ? 12.203  7.405   -13.692 1.00 12.89 ? 222 LEU A CD2 1 
ATOM   1790 N  N   . LEU A 1 223 ? 15.177  11.381  -13.883 1.00 10.90 ? 223 LEU A N   1 
ATOM   1791 C  CA  . LEU A 1 223 ? 16.173  11.702  -12.841 1.00 12.48 ? 223 LEU A CA  1 
ATOM   1792 C  C   . LEU A 1 223 ? 16.150  13.189  -12.441 1.00 12.02 ? 223 LEU A C   1 
ATOM   1793 O  O   . LEU A 1 223 ? 16.328  13.527  -11.250 1.00 11.58 ? 223 LEU A O   1 
ATOM   1794 C  CB  . LEU A 1 223 ? 17.569  11.209  -13.268 1.00 14.86 ? 223 LEU A CB  1 
ATOM   1795 C  CG  . LEU A 1 223 ? 18.654  11.371  -12.205 1.00 17.05 ? 223 LEU A CG  1 
ATOM   1796 C  CD1 . LEU A 1 223 ? 18.580  10.248  -11.139 1.00 18.12 ? 223 LEU A CD1 1 
ATOM   1797 C  CD2 . LEU A 1 223 ? 19.965  11.381  -13.004 1.00 19.81 ? 223 LEU A CD2 1 
ATOM   1798 N  N   . ALA A 1 224 ? 15.907  14.072  -13.427 1.00 11.93 ? 224 ALA A N   1 
ATOM   1799 C  CA  . ALA A 1 224 ? 15.845  15.513  -13.176 1.00 11.96 ? 224 ALA A CA  1 
ATOM   1800 C  C   . ALA A 1 224 ? 14.646  15.752  -12.236 1.00 12.48 ? 224 ALA A C   1 
ATOM   1801 O  O   . ALA A 1 224 ? 14.739  16.496  -11.269 1.00 12.11 ? 224 ALA A O   1 
ATOM   1802 C  CB  . ALA A 1 224 ? 15.665  16.319  -14.478 1.00 11.59 ? 224 ALA A CB  1 
ATOM   1803 N  N   . LEU A 1 225 ? 13.525  15.065  -12.506 1.00 11.18 ? 225 LEU A N   1 
ATOM   1804 C  CA  . LEU A 1 225 ? 12.330  15.234  -11.672 1.00 11.47 ? 225 LEU A CA  1 
ATOM   1805 C  C   . LEU A 1 225 ? 12.589  14.787  -10.233 1.00 12.58 ? 225 LEU A C   1 
ATOM   1806 O  O   . LEU A 1 225 ? 12.134  15.447  -9.312  1.00 13.19 ? 225 LEU A O   1 
ATOM   1807 C  CB  . LEU A 1 225 ? 11.143  14.430  -12.254 1.00 11.34 ? 225 LEU A CB  1 
ATOM   1808 C  CG  . LEU A 1 225 ? 9.805   14.610  -11.536 1.00 11.68 ? 225 LEU A CG  1 
ATOM   1809 C  CD1 . LEU A 1 225 ? 9.367   16.096  -11.479 1.00 11.36 ? 225 LEU A CD1 1 
ATOM   1810 C  CD2 . LEU A 1 225 ? 8.744   13.724  -12.251 1.00 11.28 ? 225 LEU A CD2 1 
ATOM   1811 N  N   . GLU A 1 226 ? 13.356  13.684  -10.067 1.00 12.96 ? 226 GLU A N   1 
ATOM   1812 C  CA  . GLU A 1 226 ? 13.606  13.060  -8.771  1.00 13.15 ? 226 GLU A CA  1 
ATOM   1813 C  C   . GLU A 1 226 ? 14.695  13.808  -7.979  1.00 14.95 ? 226 GLU A C   1 
ATOM   1814 O  O   . GLU A 1 226 ? 14.761  13.644  -6.771  1.00 17.65 ? 226 GLU A O   1 
ATOM   1815 C  CB  . GLU A 1 226 ? 14.031  11.587  -8.945  1.00 12.81 ? 226 GLU A CB  1 
ATOM   1816 C  CG  . GLU A 1 226 ? 12.948  10.596  -9.368  1.00 12.72 ? 226 GLU A CG  1 
ATOM   1817 C  CD  . GLU A 1 226 ? 13.544  9.307   -9.968  1.00 13.65 ? 226 GLU A CD  1 
ATOM   1818 O  OE1 . GLU A 1 226 ? 14.745  9.319   -10.321 1.00 14.07 ? 226 GLU A OE1 1 
ATOM   1819 O  OE2 . GLU A 1 226 ? 12.851  8.277   -10.125 1.00 11.86 ? 226 GLU A OE2 1 
ATOM   1820 N  N   . THR A 1 227 ? 15.544  14.595  -8.650  1.00 14.14 ? 227 THR A N   1 
ATOM   1821 C  CA  . THR A 1 227 ? 16.771  15.173  -7.999  1.00 14.51 ? 227 THR A CA  1 
ATOM   1822 C  C   . THR A 1 227 ? 16.871  16.686  -7.958  1.00 14.68 ? 227 THR A C   1 
ATOM   1823 O  O   . THR A 1 227 ? 17.740  17.245  -7.235  1.00 15.79 ? 227 THR A O   1 
ATOM   1824 C  CB  . THR A 1 227 ? 18.091  14.604  -8.640  1.00 13.77 ? 227 THR A CB  1 
ATOM   1825 O  OG1 . THR A 1 227 ? 18.173  14.966  -10.043 1.00 13.36 ? 227 THR A OG1 1 
ATOM   1826 C  CG2 . THR A 1 227 ? 18.138  13.094  -8.488  1.00 14.25 ? 227 THR A CG2 1 
ATOM   1827 N  N   . ALA A 1 228 ? 16.063  17.376  -8.759  1.00 13.79 ? 228 ALA A N   1 
ATOM   1828 C  CA  . ALA A 1 228 ? 16.140  18.857  -8.849  1.00 13.57 ? 228 ALA A CA  1 
ATOM   1829 C  C   . ALA A 1 228 ? 15.627  19.585  -7.623  1.00 14.08 ? 228 ALA A C   1 
ATOM   1830 O  O   . ALA A 1 228 ? 16.046  20.709  -7.353  1.00 15.09 ? 228 ALA A O   1 
ATOM   1831 C  CB  . ALA A 1 228 ? 15.333  19.332  -10.051 1.00 13.93 ? 228 ALA A CB  1 
ATOM   1832 N  N   . LEU A 1 229 ? 14.611  19.012  -6.980  1.00 12.44 ? 229 LEU A N   1 
ATOM   1833 C  CA  . LEU A 1 229 ? 13.728  19.792  -6.090  1.00 12.72 ? 229 LEU A CA  1 
ATOM   1834 C  C   . LEU A 1 229 ? 13.849  19.433  -4.591  1.00 12.52 ? 229 LEU A C   1 
ATOM   1835 O  O   . LEU A 1 229 ? 14.098  18.279  -4.216  1.00 12.42 ? 229 LEU A O   1 
ATOM   1836 C  CB  . LEU A 1 229 ? 12.264  19.672  -6.580  1.00 12.62 ? 229 LEU A CB  1 
ATOM   1837 C  CG  . LEU A 1 229 ? 12.052  19.951  -8.099  1.00 13.23 ? 229 LEU A CG  1 
ATOM   1838 C  CD1 . LEU A 1 229 ? 10.582  19.648  -8.464  1.00 15.10 ? 229 LEU A CD1 1 
ATOM   1839 C  CD2 . LEU A 1 229 ? 12.387  21.423  -8.367  1.00 13.06 ? 229 LEU A CD2 1 
ATOM   1840 N  N   . TYR A 1 230 ? 13.594  20.436  -3.758  1.00 13.94 ? 230 TYR A N   1 
ATOM   1841 C  CA  . TYR A 1 230 ? 13.624  20.361  -2.277  1.00 13.84 ? 230 TYR A CA  1 
ATOM   1842 C  C   . TYR A 1 230 ? 12.289  20.820  -1.742  1.00 12.99 ? 230 TYR A C   1 
ATOM   1843 O  O   . TYR A 1 230 ? 11.718  21.707  -2.308  1.00 13.40 ? 230 TYR A O   1 
ATOM   1844 C  CB  . TYR A 1 230 ? 14.780  21.264  -1.708  1.00 15.25 ? 230 TYR A CB  1 
ATOM   1845 C  CG  . TYR A 1 230 ? 16.132  20.684  -2.171  1.00 19.53 ? 230 TYR A CG  1 
ATOM   1846 C  CD1 . TYR A 1 230 ? 16.643  20.985  -3.439  1.00 19.91 ? 230 TYR A CD1 1 
ATOM   1847 C  CD2 . TYR A 1 230 ? 16.834  19.752  -1.373  1.00 21.06 ? 230 TYR A CD2 1 
ATOM   1848 C  CE1 . TYR A 1 230 ? 17.824  20.415  -3.924  1.00 24.12 ? 230 TYR A CE1 1 
ATOM   1849 C  CE2 . TYR A 1 230 ? 18.036  19.181  -1.842  1.00 22.63 ? 230 TYR A CE2 1 
ATOM   1850 C  CZ  . TYR A 1 230 ? 18.519  19.526  -3.109  1.00 24.64 ? 230 TYR A CZ  1 
ATOM   1851 O  OH  . TYR A 1 230 ? 19.688  19.008  -3.593  1.00 23.21 ? 230 TYR A OH  1 
ATOM   1852 N  N   . CYS A 1 231 ? 11.829  20.217  -0.644  1.00 13.36 ? 231 CYS A N   1 
ATOM   1853 C  CA  . CYS A 1 231 ? 10.629  20.649  0.142   1.00 14.90 ? 231 CYS A CA  1 
ATOM   1854 C  C   . CYS A 1 231 ? 10.864  21.945  0.936   1.00 16.68 ? 231 CYS A C   1 
ATOM   1855 O  O   . CYS A 1 231 ? 9.933   22.674  1.325   1.00 15.80 ? 231 CYS A O   1 
ATOM   1856 C  CB  . CYS A 1 231 ? 10.239  19.568  1.136   1.00 16.03 ? 231 CYS A CB  1 
ATOM   1857 S  SG  . CYS A 1 231 ? 9.803   17.943  0.387   1.00 17.93 ? 231 CYS A SG  1 
ATOM   1858 N  N   . THR A 1 232 ? 12.125  22.277  1.128   1.00 19.52 ? 232 THR A N   1 
ATOM   1859 C  CA  . THR A 1 232 ? 12.440  23.406  2.007   1.00 17.94 ? 232 THR A CA  1 
ATOM   1860 C  C   . THR A 1 232 ? 12.894  24.689  1.291   1.00 19.69 ? 232 THR A C   1 
ATOM   1861 O  O   . THR A 1 232 ? 13.278  24.649  0.125   1.00 17.20 ? 232 THR A O   1 
ATOM   1862 C  CB  . THR A 1 232 ? 13.519  22.952  2.960   1.00 19.35 ? 232 THR A CB  1 
ATOM   1863 O  OG1 . THR A 1 232 ? 14.463  22.206  2.203   1.00 18.82 ? 232 THR A OG1 1 
ATOM   1864 C  CG2 . THR A 1 232 ? 12.906  22.030  4.030   1.00 20.21 ? 232 THR A CG2 1 
ATOM   1865 N  N   . HIS A 1 233 ? 12.811  25.830  1.994   1.00 23.20 ? 233 HIS A N   1 
ATOM   1866 C  CA  . HIS A 1 233 ? 13.267  27.134  1.439   1.00 25.24 ? 233 HIS A CA  1 
ATOM   1867 C  C   . HIS A 1 233 ? 14.758  27.106  1.142   1.00 24.77 ? 233 HIS A C   1 
ATOM   1868 O  O   . HIS A 1 233 ? 15.487  26.242  1.660   1.00 24.01 ? 233 HIS A O   1 
ATOM   1869 C  CB  . HIS A 1 233 ? 12.872  28.315  2.348   1.00 27.91 ? 233 HIS A CB  1 
ATOM   1870 C  CG  . HIS A 1 233 ? 11.375  28.571  2.428   1.00 30.55 ? 233 HIS A CG  1 
ATOM   1871 N  ND1 . HIS A 1 233 ? 10.652  29.065  1.392   1.00 33.40 ? 233 HIS A ND1 1 
ATOM   1872 C  CD2 . HIS A 1 233 ? 10.484  28.430  3.491   1.00 32.44 ? 233 HIS A CD2 1 
ATOM   1873 C  CE1 . HIS A 1 233 ? 9.360   29.207  1.773   1.00 34.71 ? 233 HIS A CE1 1 
ATOM   1874 N  NE2 . HIS A 1 233 ? 9.262   28.817  3.056   1.00 34.02 ? 233 HIS A NE2 1 
ATOM   1875 N  N   A MET A 1 234 ? 15.198  28.041  0.291   0.50 25.80 ? 234 MET A N   1 
ATOM   1876 N  N   B MET A 1 234 ? 15.222  28.011  0.278   0.50 24.90 ? 234 MET A N   1 
ATOM   1877 C  CA  A MET A 1 234 ? 16.585  28.190  -0.165  0.50 26.88 ? 234 MET A CA  1 
ATOM   1878 C  CA  B MET A 1 234 ? 16.627  28.038  -0.096  0.50 25.51 ? 234 MET A CA  1 
ATOM   1879 C  C   A MET A 1 234 ? 17.548  28.488  0.991   0.50 27.72 ? 234 MET A C   1 
ATOM   1880 C  C   B MET A 1 234 ? 17.499  28.296  1.127   0.50 26.84 ? 234 MET A C   1 
ATOM   1881 O  O   A MET A 1 234 ? 18.707  28.071  0.965   0.50 27.54 ? 234 MET A O   1 
ATOM   1882 O  O   B MET A 1 234 ? 18.539  27.665  1.286   0.50 26.15 ? 234 MET A O   1 
ATOM   1883 C  CB  A MET A 1 234 ? 16.658  29.282  -1.257  0.50 27.15 ? 234 MET A CB  1 
ATOM   1884 C  CB  B MET A 1 234 ? 16.920  29.066  -1.194  0.50 24.33 ? 234 MET A CB  1 
ATOM   1885 C  CG  A MET A 1 234 ? 18.021  29.904  -1.552  0.50 29.12 ? 234 MET A CG  1 
ATOM   1886 C  CG  B MET A 1 234 ? 18.375  29.065  -1.649  0.50 25.47 ? 234 MET A CG  1 
ATOM   1887 S  SD  A MET A 1 234 ? 17.946  31.045  -2.965  0.50 31.58 ? 234 MET A SD  1 
ATOM   1888 S  SD  B MET A 1 234 ? 18.600  29.886  -3.230  0.50 24.41 ? 234 MET A SD  1 
ATOM   1889 C  CE  A MET A 1 234 ? 18.020  29.927  -4.365  0.50 27.77 ? 234 MET A CE  1 
ATOM   1890 C  CE  B MET A 1 234 ? 17.940  31.503  -2.808  0.50 26.82 ? 234 MET A CE  1 
ATOM   1891 N  N   . ASP A 1 235 ? 17.041  29.187  2.000   1.00 29.45 ? 235 ASP A N   1 
ATOM   1892 C  CA  . ASP A 1 235 ? 17.826  29.570  3.212   1.00 38.03 ? 235 ASP A CA  1 
ATOM   1893 C  C   . ASP A 1 235 ? 18.092  28.431  4.233   1.00 39.01 ? 235 ASP A C   1 
ATOM   1894 O  O   . ASP A 1 235 ? 19.020  28.531  5.056   1.00 39.39 ? 235 ASP A O   1 
ATOM   1895 C  CB  . ASP A 1 235 ? 17.184  30.792  3.925   1.00 44.68 ? 235 ASP A CB  1 
ATOM   1896 C  CG  . ASP A 1 235 ? 17.576  32.132  3.295   1.00 52.86 ? 235 ASP A CG  1 
ATOM   1897 O  OD1 . ASP A 1 235 ? 18.058  32.145  2.127   1.00 55.92 ? 235 ASP A OD1 1 
ATOM   1898 O  OD2 . ASP A 1 235 ? 17.397  33.176  3.975   1.00 56.00 ? 235 ASP A OD2 1 
ATOM   1899 N  N   . ASP A 1 236 ? 17.307  27.350  4.146   1.00 37.39 ? 236 ASP A N   1 
ATOM   1900 C  CA  . ASP A 1 236 ? 17.313  26.261  5.127   1.00 38.55 ? 236 ASP A CA  1 
ATOM   1901 C  C   . ASP A 1 236 ? 18.669  25.568  5.328   1.00 39.28 ? 236 ASP A C   1 
ATOM   1902 O  O   . ASP A 1 236 ? 19.221  24.955  4.388   1.00 40.41 ? 236 ASP A O   1 
ATOM   1903 C  CB  . ASP A 1 236 ? 16.227  25.219  4.780   1.00 39.05 ? 236 ASP A CB  1 
ATOM   1904 C  CG  . ASP A 1 236 ? 15.660  24.542  6.016   1.00 41.13 ? 236 ASP A CG  1 
ATOM   1905 O  OD1 . ASP A 1 236 ? 16.448  24.010  6.837   1.00 39.94 ? 236 ASP A OD1 1 
ATOM   1906 O  OD2 . ASP A 1 236 ? 14.421  24.544  6.167   1.00 40.56 ? 236 ASP A OD2 1 
ATOM   1907 N  N   . PRO A 1 237 ? 19.207  25.654  6.568   1.00 42.75 ? 237 PRO A N   1 
ATOM   1908 C  CA  . PRO A 1 237 ? 20.480  25.007  6.891   1.00 38.33 ? 237 PRO A CA  1 
ATOM   1909 C  C   . PRO A 1 237 ? 20.390  23.481  6.754   1.00 34.94 ? 237 PRO A C   1 
ATOM   1910 O  O   . PRO A 1 237 ? 21.431  22.825  6.580   1.00 35.33 ? 237 PRO A O   1 
ATOM   1911 C  CB  . PRO A 1 237 ? 20.709  25.399  8.359   1.00 40.75 ? 237 PRO A CB  1 
ATOM   1912 C  CG  . PRO A 1 237 ? 19.328  25.582  8.914   1.00 42.94 ? 237 PRO A CG  1 
ATOM   1913 C  CD  . PRO A 1 237 ? 18.562  26.221  7.775   1.00 41.52 ? 237 PRO A CD  1 
ATOM   1914 N  N   A SER A 1 238 ? 19.173  22.937  6.801   0.50 31.56 ? 238 SER A N   1 
ATOM   1915 N  N   B SER A 1 238 ? 19.167  22.944  6.842   0.50 31.76 ? 238 SER A N   1 
ATOM   1916 C  CA  A SER A 1 238 ? 18.951  21.492  6.708   0.50 28.87 ? 238 SER A CA  1 
ATOM   1917 C  CA  B SER A 1 238 ? 18.891  21.506  6.721   0.50 29.08 ? 238 SER A CA  1 
ATOM   1918 C  C   A SER A 1 238 ? 17.921  21.161  5.634   0.50 27.97 ? 238 SER A C   1 
ATOM   1919 C  C   B SER A 1 238 ? 17.882  21.241  5.612   0.50 28.16 ? 238 SER A C   1 
ATOM   1920 O  O   A SER A 1 238 ? 16.727  20.990  5.933   0.50 26.94 ? 238 SER A O   1 
ATOM   1921 O  O   B SER A 1 238 ? 16.665  21.188  5.867   0.50 26.86 ? 238 SER A O   1 
ATOM   1922 C  CB  A SER A 1 238 ? 18.519  20.939  8.071   0.50 28.46 ? 238 SER A CB  1 
ATOM   1923 C  CB  B SER A 1 238 ? 18.351  20.936  8.043   0.50 28.59 ? 238 SER A CB  1 
ATOM   1924 O  OG  A SER A 1 238 ? 19.349  21.477  9.092   0.50 26.01 ? 238 SER A OG  1 
ATOM   1925 O  OG  B SER A 1 238 ? 17.157  21.591  8.438   0.50 26.80 ? 238 SER A OG  1 
ATOM   1926 N  N   . PRO A 1 239 ? 18.371  21.090  4.369   1.00 27.93 ? 239 PRO A N   1 
ATOM   1927 C  CA  . PRO A 1 239 ? 17.426  20.828  3.291   1.00 24.98 ? 239 PRO A CA  1 
ATOM   1928 C  C   . PRO A 1 239 ? 16.808  19.422  3.346   1.00 24.38 ? 239 PRO A C   1 
ATOM   1929 O  O   . PRO A 1 239 ? 17.434  18.474  3.865   1.00 23.48 ? 239 PRO A O   1 
ATOM   1930 C  CB  . PRO A 1 239 ? 18.283  20.981  2.025   1.00 29.29 ? 239 PRO A CB  1 
ATOM   1931 C  CG  . PRO A 1 239 ? 19.529  21.716  2.456   1.00 32.90 ? 239 PRO A CG  1 
ATOM   1932 C  CD  . PRO A 1 239 ? 19.748  21.264  3.872   1.00 28.79 ? 239 PRO A CD  1 
ATOM   1933 N  N   A ARG A 1 240 ? 15.575  19.290  2.844   0.50 20.80 ? 240 ARG A N   1 
ATOM   1934 N  N   B ARG A 1 240 ? 15.597  19.283  2.815   0.50 21.74 ? 240 ARG A N   1 
ATOM   1935 C  CA  A ARG A 1 240 ? 14.915  17.991  2.702   0.50 19.09 ? 240 ARG A CA  1 
ATOM   1936 C  CA  B ARG A 1 240 ? 14.986  17.975  2.696   0.50 20.47 ? 240 ARG A CA  1 
ATOM   1937 C  C   A ARG A 1 240 ? 14.609  17.819  1.201   0.50 18.40 ? 240 ARG A C   1 
ATOM   1938 C  C   B ARG A 1 240 ? 14.604  17.808  1.215   0.50 19.25 ? 240 ARG A C   1 
ATOM   1939 O  O   A ARG A 1 240 ? 13.995  18.698  0.591   0.50 15.66 ? 240 ARG A O   1 
ATOM   1940 O  O   B ARG A 1 240 ? 13.952  18.680  0.632   0.50 16.31 ? 240 ARG A O   1 
ATOM   1941 C  CB  A ARG A 1 240 ? 13.606  17.936  3.500   0.50 19.57 ? 240 ARG A CB  1 
ATOM   1942 C  CB  B ARG A 1 240 ? 13.765  17.858  3.603   0.50 22.41 ? 240 ARG A CB  1 
ATOM   1943 C  CG  A ARG A 1 240 ? 13.720  17.670  5.005   0.50 19.84 ? 240 ARG A CG  1 
ATOM   1944 C  CG  B ARG A 1 240 ? 13.866  18.543  4.973   0.50 24.29 ? 240 ARG A CG  1 
ATOM   1945 C  CD  A ARG A 1 240 ? 12.334  17.545  5.648   0.50 19.11 ? 240 ARG A CD  1 
ATOM   1946 C  CD  B ARG A 1 240 ? 12.457  18.704  5.535   0.50 24.45 ? 240 ARG A CD  1 
ATOM   1947 N  NE  A ARG A 1 240 ? 11.618  18.825  5.729   0.50 17.41 ? 240 ARG A NE  1 
ATOM   1948 N  NE  B ARG A 1 240 ? 12.250  19.836  6.444   0.50 26.83 ? 240 ARG A NE  1 
ATOM   1949 C  CZ  A ARG A 1 240 ? 10.528  19.135  5.032   0.50 17.48 ? 240 ARG A CZ  1 
ATOM   1950 C  CZ  B ARG A 1 240 ? 13.157  20.339  7.274   0.50 24.81 ? 240 ARG A CZ  1 
ATOM   1951 N  NH1 A ARG A 1 240 ? 9.974   18.246  4.206   0.50 15.08 ? 240 ARG A NH1 1 
ATOM   1952 N  NH1 B ARG A 1 240 ? 14.379  19.811  7.355   0.50 26.35 ? 240 ARG A NH1 1 
ATOM   1953 N  NH2 A ARG A 1 240 ? 9.979   20.339  5.175   0.50 16.47 ? 240 ARG A NH2 1 
ATOM   1954 N  NH2 B ARG A 1 240 ? 12.818  21.360  8.042   0.50 26.47 ? 240 ARG A NH2 1 
ATOM   1955 N  N   . GLU A 1 241 ? 15.032  16.700  0.616   1.00 18.39 ? 241 GLU A N   1 
ATOM   1956 C  CA  . GLU A 1 241 ? 14.818  16.433  -0.834  1.00 19.03 ? 241 GLU A CA  1 
ATOM   1957 C  C   . GLU A 1 241 ? 13.339  16.135  -1.098  1.00 16.93 ? 241 GLU A C   1 
ATOM   1958 O  O   . GLU A 1 241 ? 12.687  15.523  -0.264  1.00 16.93 ? 241 GLU A O   1 
ATOM   1959 C  CB  . GLU A 1 241 ? 15.675  15.227  -1.312  1.00 21.08 ? 241 GLU A CB  1 
ATOM   1960 C  CG  . GLU A 1 241 ? 17.172  15.396  -1.095  1.00 24.63 ? 241 GLU A CG  1 
ATOM   1961 C  CD  . GLU A 1 241 ? 18.017  14.269  -1.689  1.00 29.61 ? 241 GLU A CD  1 
ATOM   1962 O  OE1 . GLU A 1 241 ? 17.449  13.252  -2.147  1.00 31.60 ? 241 GLU A OE1 1 
ATOM   1963 O  OE2 . GLU A 1 241 ? 19.268  14.395  -1.681  1.00 35.39 ? 241 GLU A OE2 1 
ATOM   1964 N  N   . MET A 1 242 ? 12.805  16.614  -2.222  1.00 13.68 ? 242 MET A N   1 
ATOM   1965 C  CA  . MET A 1 242 ? 11.450  16.309  -2.583  1.00 12.19 ? 242 MET A CA  1 
ATOM   1966 C  C   . MET A 1 242 ? 11.489  15.018  -3.397  1.00 11.36 ? 242 MET A C   1 
ATOM   1967 O  O   . MET A 1 242 ? 11.663  15.039  -4.614  1.00 11.05 ? 242 MET A O   1 
ATOM   1968 C  CB  . MET A 1 242 ? 10.746  17.463  -3.316  1.00 12.58 ? 242 MET A CB  1 
ATOM   1969 C  CG  . MET A 1 242 ? 9.268   17.176  -3.703  1.00 12.47 ? 242 MET A CG  1 
ATOM   1970 S  SD  . MET A 1 242 ? 8.562   18.580  -4.635  1.00 13.25 ? 242 MET A SD  1 
ATOM   1971 C  CE  . MET A 1 242 ? 8.730   19.974  -3.518  1.00 12.06 ? 242 MET A CE  1 
ATOM   1972 N  N   . ILE A 1 243 ? 11.320  13.904  -2.672  1.00 11.20 ? 243 ILE A N   1 
ATOM   1973 C  CA  . ILE A 1 243 ? 11.330  12.549  -3.233  1.00 11.69 ? 243 ILE A CA  1 
ATOM   1974 C  C   . ILE A 1 243 ? 10.217  11.750  -2.568  1.00 11.46 ? 243 ILE A C   1 
ATOM   1975 O  O   . ILE A 1 243 ? 9.727   12.137  -1.472  1.00 11.15 ? 243 ILE A O   1 
ATOM   1976 C  CB  . ILE A 1 243 ? 12.671  11.787  -2.988  1.00 12.51 ? 243 ILE A CB  1 
ATOM   1977 C  CG1 . ILE A 1 243 ? 13.036  11.842  -1.482  1.00 13.36 ? 243 ILE A CG1 1 
ATOM   1978 C  CG2 . ILE A 1 243 ? 13.766  12.345  -3.915  1.00 11.98 ? 243 ILE A CG2 1 
ATOM   1979 C  CD1 . ILE A 1 243 ? 14.465  11.344  -1.148  1.00 13.83 ? 243 ILE A CD1 1 
ATOM   1980 N  N   . ASN A 1 244 ? 9.809   10.650  -3.211  1.00 11.40 ? 244 ASN A N   1 
ATOM   1981 C  CA  . ASN A 1 244 ? 8.796   9.774   -2.589  1.00 11.09 ? 244 ASN A CA  1 
ATOM   1982 C  C   . ASN A 1 244 ? 7.526   10.559  -2.183  1.00 10.46 ? 244 ASN A C   1 
ATOM   1983 O  O   . ASN A 1 244 ? 6.921   10.300  -1.109  1.00 8.99  ? 244 ASN A O   1 
ATOM   1984 C  CB  . ASN A 1 244 ? 9.417   8.998   -1.398  1.00 11.37 ? 244 ASN A CB  1 
ATOM   1985 C  CG  . ASN A 1 244 ? 10.706  8.255   -1.843  1.00 12.77 ? 244 ASN A CG  1 
ATOM   1986 O  OD1 . ASN A 1 244 ? 10.771  7.770   -2.962  1.00 12.11 ? 244 ASN A OD1 1 
ATOM   1987 N  ND2 . ASN A 1 244 ? 11.760  8.246   -0.997  1.00 12.20 ? 244 ASN A ND2 1 
ATOM   1988 N  N   . ASN A 1 245 ? 7.123   11.514  -3.046  1.00 9.65  ? 245 ASN A N   1 
ATOM   1989 C  CA  . ASN A 1 245 ? 5.900   12.360  -2.713  1.00 9.10  ? 245 ASN A CA  1 
ATOM   1990 C  C   . ASN A 1 245 ? 4.591   11.765  -3.285  1.00 9.29  ? 245 ASN A C   1 
ATOM   1991 O  O   . ASN A 1 245 ? 3.852   12.422  -3.997  1.00 9.28  ? 245 ASN A O   1 
ATOM   1992 C  CB  . ASN A 1 245 ? 6.137   13.823  -3.217  1.00 9.31  ? 245 ASN A CB  1 
ATOM   1993 C  CG  . ASN A 1 245 ? 6.272   13.929  -4.740  1.00 9.44  ? 245 ASN A CG  1 
ATOM   1994 O  OD1 . ASN A 1 245 ? 6.675   12.962  -5.440  1.00 9.25  ? 245 ASN A OD1 1 
ATOM   1995 N  ND2 . ASN A 1 245 ? 6.051   15.138  -5.263  1.00 8.99  ? 245 ASN A ND2 1 
ATOM   1996 N  N   . PHE A 1 246 ? 4.362   10.470  -3.012  1.00 8.58  ? 246 PHE A N   1 
ATOM   1997 C  CA  . PHE A 1 246 ? 3.175   9.740   -3.412  1.00 9.43  ? 246 PHE A CA  1 
ATOM   1998 C  C   . PHE A 1 246 ? 2.588   9.043   -2.141  1.00 9.70  ? 246 PHE A C   1 
ATOM   1999 O  O   . PHE A 1 246 ? 3.357   8.653   -1.184  1.00 9.77  ? 246 PHE A O   1 
ATOM   2000 C  CB  . PHE A 1 246 ? 3.505   8.679   -4.480  1.00 9.38  ? 246 PHE A CB  1 
ATOM   2001 C  CG  . PHE A 1 246 ? 4.460   7.599   -3.990  1.00 9.04  ? 246 PHE A CG  1 
ATOM   2002 C  CD1 . PHE A 1 246 ? 3.980   6.341   -3.532  1.00 8.73  ? 246 PHE A CD1 1 
ATOM   2003 C  CD2 . PHE A 1 246 ? 5.833   7.844   -3.947  1.00 8.88  ? 246 PHE A CD2 1 
ATOM   2004 C  CE1 . PHE A 1 246 ? 4.864   5.350   -3.052  1.00 9.34  ? 246 PHE A CE1 1 
ATOM   2005 C  CE2 . PHE A 1 246 ? 6.740   6.844   -3.480  1.00 9.35  ? 246 PHE A CE2 1 
ATOM   2006 C  CZ  . PHE A 1 246 ? 6.249   5.602   -3.007  1.00 9.51  ? 246 PHE A CZ  1 
ATOM   2007 N  N   . ARG A 1 247 ? 1.248   8.890   -2.124  1.00 8.74  ? 247 ARG A N   1 
ATOM   2008 C  CA  . ARG A 1 247 ? 0.566   8.225   -1.029  1.00 8.10  ? 247 ARG A CA  1 
ATOM   2009 C  C   . ARG A 1 247 ? 0.528   6.681   -1.290  1.00 8.22  ? 247 ARG A C   1 
ATOM   2010 O  O   . ARG A 1 247 ? 0.388   6.243   -2.489  1.00 8.80  ? 247 ARG A O   1 
ATOM   2011 C  CB  . ARG A 1 247 ? -0.847  8.798   -0.903  1.00 8.00  ? 247 ARG A CB  1 
ATOM   2012 C  CG  . ARG A 1 247 ? -1.546  8.354   0.390   1.00 7.67  ? 247 ARG A CG  1 
ATOM   2013 C  CD  . ARG A 1 247 ? -2.997  8.918   0.444   1.00 7.34  ? 247 ARG A CD  1 
ATOM   2014 N  NE  . ARG A 1 247 ? -3.508  8.927   1.822   1.00 7.77  ? 247 ARG A NE  1 
ATOM   2015 C  CZ  . ARG A 1 247 ? -4.756  9.229   2.135   1.00 7.91  ? 247 ARG A CZ  1 
ATOM   2016 N  NH1 . ARG A 1 247 ? -5.665  9.441   1.157   1.00 7.69  ? 247 ARG A NH1 1 
ATOM   2017 N  NH2 . ARG A 1 247 ? -5.144  9.231   3.388   1.00 8.18  ? 247 ARG A NH2 1 
ATOM   2018 N  N   . GLN A 1 248 ? 0.695   5.854   -0.236  1.00 7.94  ? 248 GLN A N   1 
ATOM   2019 C  CA  . GLN A 1 248 ? 0.458   4.380   -0.411  1.00 8.47  ? 248 GLN A CA  1 
ATOM   2020 C  C   . GLN A 1 248 ? -0.994  4.147   -0.932  1.00 8.68  ? 248 GLN A C   1 
ATOM   2021 O  O   . GLN A 1 248 ? -1.907  4.961   -0.619  1.00 9.13  ? 248 GLN A O   1 
ATOM   2022 C  CB  . GLN A 1 248 ? 0.672   3.647   0.927   1.00 8.31  ? 248 GLN A CB  1 
ATOM   2023 C  CG  . GLN A 1 248 ? 2.096   3.747   1.502   1.00 8.03  ? 248 GLN A CG  1 
ATOM   2024 C  CD  . GLN A 1 248 ? 3.054   3.090   0.551   1.00 8.07  ? 248 GLN A CD  1 
ATOM   2025 O  OE1 . GLN A 1 248 ? 3.704   3.761   -0.271  1.00 7.02  ? 248 GLN A OE1 1 
ATOM   2026 N  NE2 . GLN A 1 248 ? 3.142   1.740   0.655   1.00 8.25  ? 248 GLN A NE2 1 
ATOM   2027 N  N   . VAL A 1 249 ? -1.239  3.096   -1.730  1.00 9.31  ? 249 VAL A N   1 
ATOM   2028 C  CA  . VAL A 1 249 ? -2.650  2.694   -2.003  1.00 9.68  ? 249 VAL A CA  1 
ATOM   2029 C  C   . VAL A 1 249 ? -3.541  2.457   -0.751  1.00 9.53  ? 249 VAL A C   1 
ATOM   2030 O  O   . VAL A 1 249 ? -3.050  2.076   0.286   1.00 10.11 ? 249 VAL A O   1 
ATOM   2031 C  CB  . VAL A 1 249 ? -2.718  1.480   -2.949  1.00 9.42  ? 249 VAL A CB  1 
ATOM   2032 C  CG1 . VAL A 1 249 ? -2.062  1.883   -4.248  1.00 8.96  ? 249 VAL A CG1 1 
ATOM   2033 C  CG2 . VAL A 1 249 ? -1.985  0.239   -2.374  1.00 9.40  ? 249 VAL A CG2 1 
ATOM   2034 N  N   . GLN A 1 250 ? -4.857  2.658   -0.883  1.00 8.86  ? 250 GLN A N   1 
ATOM   2035 C  CA  . GLN A 1 250 ? -5.798  2.687   0.251   1.00 8.76  ? 250 GLN A CA  1 
ATOM   2036 C  C   . GLN A 1 250 ? -6.629  1.376   0.136   1.00 9.99  ? 250 GLN A C   1 
ATOM   2037 O  O   . GLN A 1 250 ? -6.746  0.830   -0.980  1.00 9.10  ? 250 GLN A O   1 
ATOM   2038 C  CB  . GLN A 1 250 ? -6.703  3.938   0.082   1.00 8.49  ? 250 GLN A CB  1 
ATOM   2039 C  CG  . GLN A 1 250 ? -5.901  5.229   0.054   1.00 9.57  ? 250 GLN A CG  1 
ATOM   2040 C  CD  . GLN A 1 250 ? -5.296  5.470   1.423   1.00 10.13 ? 250 GLN A CD  1 
ATOM   2041 O  OE1 . GLN A 1 250 ? -6.045  5.545   2.416   1.00 10.42 ? 250 GLN A OE1 1 
ATOM   2042 N  NE2 . GLN A 1 250 ? -3.951  5.529   1.506   1.00 9.98  ? 250 GLN A NE2 1 
ATOM   2043 N  N   . LYS A 1 251 ? -7.200  0.894   1.250   1.00 10.60 ? 251 LYS A N   1 
ATOM   2044 C  CA  . LYS A 1 251 ? -8.206  -0.199  1.148   1.00 10.99 ? 251 LYS A CA  1 
ATOM   2045 C  C   . LYS A 1 251 ? -9.324  0.240   0.180   1.00 11.72 ? 251 LYS A C   1 
ATOM   2046 O  O   . LYS A 1 251 ? -9.780  1.398   0.225   1.00 11.32 ? 251 LYS A O   1 
ATOM   2047 C  CB  . LYS A 1 251 ? -8.820  -0.479  2.553   1.00 11.61 ? 251 LYS A CB  1 
ATOM   2048 C  CG  . LYS A 1 251 ? -7.930  -1.199  3.573   1.00 12.40 ? 251 LYS A CG  1 
ATOM   2049 C  CD  . LYS A 1 251 ? -7.792  -2.702  3.358   1.00 12.04 ? 251 LYS A CD  1 
ATOM   2050 C  CE  . LYS A 1 251 ? -7.073  -3.450  4.486   1.00 10.30 ? 251 LYS A CE  1 
ATOM   2051 N  NZ  . LYS A 1 251 ? -5.687  -2.850  4.718   1.00 10.88 ? 251 LYS A NZ  1 
ATOM   2052 N  N   . PHE A 1 252 ? -9.892  -0.715  -0.563  1.00 12.80 ? 252 PHE A N   1 
ATOM   2053 C  CA  . PHE A 1 252 ? -11.010 -0.426  -1.505  1.00 15.27 ? 252 PHE A CA  1 
ATOM   2054 C  C   . PHE A 1 252 ? -11.794 -1.729  -1.511  1.00 19.22 ? 252 PHE A C   1 
ATOM   2055 O  O   . PHE A 1 252 ? -11.465 -2.677  -2.233  1.00 19.31 ? 252 PHE A O   1 
ATOM   2056 C  CB  . PHE A 1 252 ? -10.455 -0.104  -2.891  1.00 15.83 ? 252 PHE A CB  1 
ATOM   2057 C  CG  . PHE A 1 252 ? -11.476 0.370   -3.890  1.00 16.50 ? 252 PHE A CG  1 
ATOM   2058 C  CD1 . PHE A 1 252 ? -11.796 1.693   -3.985  1.00 16.88 ? 252 PHE A CD1 1 
ATOM   2059 C  CD2 . PHE A 1 252 ? -12.097 -0.538  -4.721  1.00 17.39 ? 252 PHE A CD2 1 
ATOM   2060 C  CE1 . PHE A 1 252 ? -12.723 2.146   -4.922  1.00 18.87 ? 252 PHE A CE1 1 
ATOM   2061 C  CE2 . PHE A 1 252 ? -13.037 -0.111  -5.634  1.00 17.69 ? 252 PHE A CE2 1 
ATOM   2062 C  CZ  . PHE A 1 252 ? -13.318 1.234   -5.768  1.00 16.53 ? 252 PHE A CZ  1 
ATOM   2063 N  N   . ASP A 1 253 ? -12.781 -1.761  -0.627  1.00 23.46 ? 253 ASP A N   1 
ATOM   2064 C  CA  . ASP A 1 253 ? -13.549 -2.977  -0.295  1.00 30.94 ? 253 ASP A CA  1 
ATOM   2065 C  C   . ASP A 1 253 ? -15.033 -2.723  -0.569  1.00 33.70 ? 253 ASP A C   1 
ATOM   2066 O  O   . ASP A 1 253 ? -15.534 -1.627  -0.312  1.00 31.65 ? 253 ASP A O   1 
ATOM   2067 C  CB  . ASP A 1 253 ? -13.339 -3.319  1.201   1.00 31.02 ? 253 ASP A CB  1 
ATOM   2068 C  CG  . ASP A 1 253 ? -11.859 -3.696  1.544   1.00 36.31 ? 253 ASP A CG  1 
ATOM   2069 O  OD1 . ASP A 1 253 ? -11.224 -4.513  0.808   1.00 42.84 ? 253 ASP A OD1 1 
ATOM   2070 O  OD2 . ASP A 1 253 ? -11.348 -3.213  2.590   1.00 33.22 ? 253 ASP A OD2 1 
ATOM   2071 N  N   . GLU A 1 254 ? -15.720 -3.749  -1.071  1.00 38.66 ? 254 GLU A N   1 
ATOM   2072 C  CA  . GLU A 1 254 ? -17.149 -3.678  -1.480  1.00 39.02 ? 254 GLU A CA  1 
ATOM   2073 C  C   . GLU A 1 254 ? -17.502 -2.498  -2.403  1.00 35.80 ? 254 GLU A C   1 
ATOM   2074 O  O   . GLU A 1 254 ? -18.621 -1.951  -2.353  1.00 34.39 ? 254 GLU A O   1 
ATOM   2075 C  CB  . GLU A 1 254 ? -18.123 -3.812  -0.278  1.00 46.72 ? 254 GLU A CB  1 
ATOM   2076 C  CG  . GLU A 1 254 ? -18.305 -5.239  0.278   1.00 53.05 ? 254 GLU A CG  1 
ATOM   2077 C  CD  . GLU A 1 254 ? -18.900 -6.250  -0.720  1.00 59.24 ? 254 GLU A CD  1 
ATOM   2078 O  OE1 . GLU A 1 254 ? -20.065 -6.673  -0.519  1.00 60.88 ? 254 GLU A OE1 1 
ATOM   2079 O  OE2 . GLU A 1 254 ? -18.211 -6.647  -1.699  1.00 58.97 ? 254 GLU A OE2 1 
ATOM   2080 N  N   A ARG A 1 255 ? -16.520 -2.095  -3.212  0.50 32.87 ? 255 ARG A N   1 
ATOM   2081 N  N   B ARG A 1 255 ? -16.546 -2.131  -3.253  0.50 33.35 ? 255 ARG A N   1 
ATOM   2082 C  CA  A ARG A 1 255 ? -16.681 -1.029  -4.212  0.50 29.46 ? 255 ARG A CA  1 
ATOM   2083 C  CA  B ARG A 1 255 ? -16.738 -1.071  -4.248  0.50 29.99 ? 255 ARG A CA  1 
ATOM   2084 C  C   A ARG A 1 255 ? -16.223 -1.548  -5.580  0.50 26.59 ? 255 ARG A C   1 
ATOM   2085 C  C   B ARG A 1 255 ? -16.114 -1.479  -5.575  0.50 26.97 ? 255 ARG A C   1 
ATOM   2086 O  O   A ARG A 1 255 ? -15.631 -2.626  -5.666  0.50 25.69 ? 255 ARG A O   1 
ATOM   2087 O  O   B ARG A 1 255 ? -15.289 -2.387  -5.629  0.50 25.69 ? 255 ARG A O   1 
ATOM   2088 C  CB  A ARG A 1 255 ? -15.877 0.237   -3.837  0.50 26.30 ? 255 ARG A CB  1 
ATOM   2089 C  CB  B ARG A 1 255 ? -16.125 0.256   -3.776  0.50 27.53 ? 255 ARG A CB  1 
ATOM   2090 C  CG  A ARG A 1 255 ? -15.925 0.688   -2.380  0.50 24.79 ? 255 ARG A CG  1 
ATOM   2091 C  CG  B ARG A 1 255 ? -17.012 1.130   -2.906  0.50 26.09 ? 255 ARG A CG  1 
ATOM   2092 C  CD  A ARG A 1 255 ? -15.417 2.123   -2.264  0.50 21.95 ? 255 ARG A CD  1 
ATOM   2093 C  CD  B ARG A 1 255 ? -16.253 2.420   -2.582  0.50 24.39 ? 255 ARG A CD  1 
ATOM   2094 N  NE  A ARG A 1 255 ? -15.870 2.903   -3.408  0.50 19.17 ? 255 ARG A NE  1 
ATOM   2095 N  NE  B ARG A 1 255 ? -15.308 2.257   -1.478  0.50 22.55 ? 255 ARG A NE  1 
ATOM   2096 C  CZ  A ARG A 1 255 ? -15.410 4.104   -3.740  0.50 17.62 ? 255 ARG A CZ  1 
ATOM   2097 C  CZ  B ARG A 1 255 ? -14.165 2.928   -1.368  0.50 20.44 ? 255 ARG A CZ  1 
ATOM   2098 N  NH1 A ARG A 1 255 ? -14.475 4.660   -3.002  0.50 17.94 ? 255 ARG A NH1 1 
ATOM   2099 N  NH1 B ARG A 1 255 ? -13.823 3.792   -2.312  0.50 19.50 ? 255 ARG A NH1 1 
ATOM   2100 N  NH2 A ARG A 1 255 ? -15.878 4.724   -4.810  0.50 14.69 ? 255 ARG A NH2 1 
ATOM   2101 N  NH2 B ARG A 1 255 ? -13.373 2.740   -0.319  0.50 17.06 ? 255 ARG A NH2 1 
ATOM   2102 N  N   . LEU A 1 256 ? -16.505 -0.770  -6.633  1.00 26.87 ? 256 LEU A N   1 
ATOM   2103 C  CA  . LEU A 1 256 ? -16.100 -1.078  -7.977  1.00 22.09 ? 256 LEU A CA  1 
ATOM   2104 C  C   . LEU A 1 256 ? -15.541 0.156   -8.723  1.00 18.78 ? 256 LEU A C   1 
ATOM   2105 O  O   . LEU A 1 256 ? -15.929 1.312   -8.529  1.00 19.16 ? 256 LEU A O   1 
ATOM   2106 C  CB  . LEU A 1 256 ? -17.254 -1.753  -8.765  1.00 23.75 ? 256 LEU A CB  1 
ATOM   2107 C  CG  . LEU A 1 256 ? -17.775 -3.176  -8.466  1.00 25.11 ? 256 LEU A CG  1 
ATOM   2108 C  CD1 . LEU A 1 256 ? -18.773 -3.589  -9.541  1.00 26.20 ? 256 LEU A CD1 1 
ATOM   2109 C  CD2 . LEU A 1 256 ? -16.684 -4.247  -8.367  1.00 23.57 ? 256 LEU A CD2 1 
ATOM   2110 N  N   . VAL A 1 257 ? -14.541 -0.116  -9.516  1.00 16.82 ? 257 VAL A N   1 
ATOM   2111 C  CA  . VAL A 1 257 ? -13.964 0.847   -10.407 1.00 15.40 ? 257 VAL A CA  1 
ATOM   2112 C  C   . VAL A 1 257 ? -14.555 0.443   -11.739 1.00 14.89 ? 257 VAL A C   1 
ATOM   2113 O  O   . VAL A 1 257 ? -14.637 -0.762  -12.067 1.00 14.90 ? 257 VAL A O   1 
ATOM   2114 C  CB  . VAL A 1 257 ? -12.418 0.718   -10.428 1.00 15.18 ? 257 VAL A CB  1 
ATOM   2115 C  CG1 . VAL A 1 257 ? -11.786 1.573   -11.521 1.00 15.15 ? 257 VAL A CG1 1 
ATOM   2116 C  CG2 . VAL A 1 257 ? -11.843 1.105   -9.081  1.00 17.31 ? 257 VAL A CG2 1 
ATOM   2117 N  N   . TYR A 1 258 ? -15.026 1.411   -12.492 1.00 14.82 ? 258 TYR A N   1 
ATOM   2118 C  CA  . TYR A 1 258 ? -15.622 1.060   -13.835 1.00 14.60 ? 258 TYR A CA  1 
ATOM   2119 C  C   . TYR A 1 258 ? -14.661 1.354   -14.940 1.00 13.02 ? 258 TYR A C   1 
ATOM   2120 O  O   . TYR A 1 258 ? -13.938 2.374   -14.872 1.00 12.63 ? 258 TYR A O   1 
ATOM   2121 C  CB  . TYR A 1 258 ? -16.942 1.820   -14.058 1.00 16.15 ? 258 TYR A CB  1 
ATOM   2122 C  CG  . TYR A 1 258 ? -17.918 1.484   -12.950 1.00 20.47 ? 258 TYR A CG  1 
ATOM   2123 C  CD1 . TYR A 1 258 ? -18.062 2.347   -11.885 1.00 21.28 ? 258 TYR A CD1 1 
ATOM   2124 C  CD2 . TYR A 1 258 ? -18.609 0.248   -12.923 1.00 21.38 ? 258 TYR A CD2 1 
ATOM   2125 C  CE1 . TYR A 1 258 ? -18.915 2.056   -10.830 1.00 24.51 ? 258 TYR A CE1 1 
ATOM   2126 C  CE2 . TYR A 1 258 ? -19.490 -0.048  -11.887 1.00 24.67 ? 258 TYR A CE2 1 
ATOM   2127 C  CZ  . TYR A 1 258 ? -19.633 0.880   -10.840 1.00 25.77 ? 258 TYR A CZ  1 
ATOM   2128 O  OH  . TYR A 1 258 ? -20.463 0.686   -9.752  1.00 29.54 ? 258 TYR A OH  1 
ATOM   2129 N  N   . THR A 1 259 ? -14.659 0.541   -15.990 1.00 10.89 ? 259 THR A N   1 
ATOM   2130 C  CA  . THR A 1 259 ? -13.712 0.774   -17.066 1.00 11.60 ? 259 THR A CA  1 
ATOM   2131 C  C   . THR A 1 259 ? -14.409 1.078   -18.349 1.00 12.08 ? 259 THR A C   1 
ATOM   2132 O  O   . THR A 1 259 ? -15.491 0.571   -18.574 1.00 11.29 ? 259 THR A O   1 
ATOM   2133 C  CB  . THR A 1 259 ? -12.766 -0.408  -17.278 1.00 11.37 ? 259 THR A CB  1 
ATOM   2134 O  OG1 . THR A 1 259 ? -13.578 -1.583  -17.560 1.00 11.65 ? 259 THR A OG1 1 
ATOM   2135 C  CG2 . THR A 1 259 ? -11.962 -0.700  -15.988 1.00 12.68 ? 259 THR A CG2 1 
ATOM   2136 N  N   . SER A 1 260 ? -13.811 1.925   -19.179 1.00 12.15 ? 260 SER A N   1 
ATOM   2137 C  CA  . SER A 1 260 ? -14.474 2.219   -20.488 1.00 13.91 ? 260 SER A CA  1 
ATOM   2138 C  C   . SER A 1 260 ? -13.984 1.334   -21.619 1.00 14.71 ? 260 SER A C   1 
ATOM   2139 O  O   . SER A 1 260 ? -14.357 1.534   -22.772 1.00 15.06 ? 260 SER A O   1 
ATOM   2140 C  CB  . SER A 1 260 ? -14.242 3.673   -20.871 1.00 13.31 ? 260 SER A CB  1 
ATOM   2141 O  OG  . SER A 1 260 ? -12.860 3.918   -21.127 1.00 11.02 ? 260 SER A OG  1 
ATOM   2142 N  N   . PHE A 1 261 ? -13.103 0.408   -21.284 1.00 15.24 ? 261 PHE A N   1 
ATOM   2143 C  CA  . PHE A 1 261 ? -12.550 -0.536  -22.240 1.00 15.22 ? 261 PHE A CA  1 
ATOM   2144 C  C   . PHE A 1 261 ? -12.952 -1.879  -21.648 1.00 16.53 ? 261 PHE A C   1 
ATOM   2145 O  O   . PHE A 1 261 ? -13.271 -1.958  -20.442 1.00 14.87 ? 261 PHE A O   1 
ATOM   2146 C  CB  . PHE A 1 261 ? -11.029 -0.393  -22.335 1.00 14.82 ? 261 PHE A CB  1 
ATOM   2147 C  CG  . PHE A 1 261 ? -10.295 -0.519  -20.972 1.00 15.21 ? 261 PHE A CG  1 
ATOM   2148 C  CD1 . PHE A 1 261 ? -9.836  -1.758  -20.509 1.00 15.74 ? 261 PHE A CD1 1 
ATOM   2149 C  CD2 . PHE A 1 261 ? -10.052 0.607   -20.208 1.00 15.22 ? 261 PHE A CD2 1 
ATOM   2150 C  CE1 . PHE A 1 261 ? -9.165  -1.871  -19.297 1.00 15.43 ? 261 PHE A CE1 1 
ATOM   2151 C  CE2 . PHE A 1 261 ? -9.341  0.518   -18.997 1.00 14.16 ? 261 PHE A CE2 1 
ATOM   2152 C  CZ  . PHE A 1 261 ? -8.913  -0.717  -18.548 1.00 15.42 ? 261 PHE A CZ  1 
ATOM   2153 N  N   . SER A 1 262 ? -12.961 -2.943  -22.472 1.00 16.85 ? 262 SER A N   1 
ATOM   2154 C  CA  . SER A 1 262 ? -13.384 -4.229  -21.938 1.00 19.48 ? 262 SER A CA  1 
ATOM   2155 C  C   . SER A 1 262 ? -12.115 -5.020  -21.776 1.00 22.22 ? 262 SER A C   1 
ATOM   2156 O  O   . SER A 1 262 ? -11.115 -4.709  -22.377 1.00 24.27 ? 262 SER A O   1 
ATOM   2157 C  CB  . SER A 1 262 ? -14.364 -4.960  -22.901 1.00 18.51 ? 262 SER A CB  1 
ATOM   2158 O  OG  . SER A 1 262 ? -13.672 -5.255  -24.081 1.00 18.26 ? 262 SER A OG  1 
ATOM   2159 N  N   . GLN A 1 263 ? -12.153 -6.040  -20.949 1.00 25.86 ? 263 GLN A N   1 
ATOM   2160 C  CA  . GLN A 1 263 ? -10.998 -6.904  -20.851 1.00 31.39 ? 263 GLN A CA  1 
ATOM   2161 C  C   . GLN A 1 263 ? -11.394 -8.388  -20.860 1.00 32.69 ? 263 GLN A C   1 
ATOM   2162 O  O   . GLN A 1 263 ? -10.528 -9.267  -20.751 1.00 28.99 ? 263 GLN A O   1 
ATOM   2163 C  CB  . GLN A 1 263 ? -10.121 -6.513  -19.658 1.00 33.82 ? 263 GLN A CB  1 
ATOM   2164 C  CG  . GLN A 1 263 ? -10.879 -6.323  -18.369 1.00 34.19 ? 263 GLN A CG  1 
ATOM   2165 C  CD  . GLN A 1 263 ? -10.228 -5.328  -17.391 1.00 36.10 ? 263 GLN A CD  1 
ATOM   2166 O  OE1 . GLN A 1 263 ? -9.084  -4.843  -17.565 1.00 36.86 ? 263 GLN A OE1 1 
ATOM   2167 N  NE2 . GLN A 1 263 ? -10.972 -5.018  -16.346 1.00 33.29 ? 263 GLN A NE2 1 
ATOM   2168 O  OXT . GLN A 1 263 ? -12.585 -8.700  -21.076 1.00 30.82 ? 263 GLN A OXT 1 
ATOM   2169 N  N   . TRP B 1 4   ? -9.866  -0.185  18.069  1.00 16.32 ? 4   TRP B N   1 
ATOM   2170 C  CA  . TRP B 1 4   ? -9.316  -0.091  16.635  1.00 14.96 ? 4   TRP B CA  1 
ATOM   2171 C  C   . TRP B 1 4   ? -9.904  -1.161  15.723  1.00 15.55 ? 4   TRP B C   1 
ATOM   2172 O  O   . TRP B 1 4   ? -10.287 -2.224  16.199  1.00 15.42 ? 4   TRP B O   1 
ATOM   2173 C  CB  . TRP B 1 4   ? -7.790  -0.094  16.680  1.00 15.51 ? 4   TRP B CB  1 
ATOM   2174 C  CG  . TRP B 1 4   ? -7.206  -1.389  17.156  1.00 14.31 ? 4   TRP B CG  1 
ATOM   2175 C  CD1 . TRP B 1 4   ? -6.921  -1.735  18.445  1.00 14.50 ? 4   TRP B CD1 1 
ATOM   2176 C  CD2 . TRP B 1 4   ? -6.836  -2.513  16.347  1.00 13.66 ? 4   TRP B CD2 1 
ATOM   2177 N  NE1 . TRP B 1 4   ? -6.397  -3.004  18.489  1.00 13.92 ? 4   TRP B NE1 1 
ATOM   2178 C  CE2 . TRP B 1 4   ? -6.335  -3.503  17.215  1.00 13.45 ? 4   TRP B CE2 1 
ATOM   2179 C  CE3 . TRP B 1 4   ? -6.881  -2.777  14.975  1.00 12.76 ? 4   TRP B CE3 1 
ATOM   2180 C  CZ2 . TRP B 1 4   ? -5.880  -4.738  16.754  1.00 12.95 ? 4   TRP B CZ2 1 
ATOM   2181 C  CZ3 . TRP B 1 4   ? -6.429  -4.003  14.520  1.00 13.45 ? 4   TRP B CZ3 1 
ATOM   2182 C  CH2 . TRP B 1 4   ? -5.935  -4.968  15.407  1.00 14.41 ? 4   TRP B CH2 1 
ATOM   2183 N  N   . THR B 1 5   ? -9.981  -0.899  14.407  1.00 15.66 ? 5   THR B N   1 
ATOM   2184 C  CA  . THR B 1 5   ? -10.487 -1.852  13.420  1.00 15.54 ? 5   THR B CA  1 
ATOM   2185 C  C   . THR B 1 5   ? -9.675  -1.759  12.156  1.00 14.63 ? 5   THR B C   1 
ATOM   2186 O  O   . THR B 1 5   ? -8.717  -0.934  12.097  1.00 15.11 ? 5   THR B O   1 
ATOM   2187 C  CB  . THR B 1 5   ? -11.923 -1.475  13.003  1.00 17.00 ? 5   THR B CB  1 
ATOM   2188 O  OG1 . THR B 1 5   ? -11.894 -0.189  12.346  1.00 16.60 ? 5   THR B OG1 1 
ATOM   2189 C  CG2 . THR B 1 5   ? -12.854 -1.381  14.213  1.00 17.77 ? 5   THR B CG2 1 
ATOM   2190 N  N   . TYR B 1 6   ? -10.100 -2.511  11.118  1.00 13.57 ? 6   TYR B N   1 
ATOM   2191 C  CA  . TYR B 1 6   ? -9.557  -2.334  9.738   1.00 14.03 ? 6   TYR B CA  1 
ATOM   2192 C  C   . TYR B 1 6   ? -10.508 -1.640  8.751   1.00 14.74 ? 6   TYR B C   1 
ATOM   2193 O  O   . TYR B 1 6   ? -10.346 -1.686  7.524   1.00 12.80 ? 6   TYR B O   1 
ATOM   2194 C  CB  . TYR B 1 6   ? -9.181  -3.695  9.134   1.00 13.28 ? 6   TYR B CB  1 
ATOM   2195 C  CG  . TYR B 1 6   ? -8.068  -4.435  9.869   1.00 13.71 ? 6   TYR B CG  1 
ATOM   2196 C  CD1 . TYR B 1 6   ? -8.343  -5.265  10.976  1.00 13.29 ? 6   TYR B CD1 1 
ATOM   2197 C  CD2 . TYR B 1 6   ? -6.770  -4.409  9.371   1.00 13.93 ? 6   TYR B CD2 1 
ATOM   2198 C  CE1 . TYR B 1 6   ? -7.316  -5.984  11.585  1.00 12.83 ? 6   TYR B CE1 1 
ATOM   2199 C  CE2 . TYR B 1 6   ? -5.743  -5.105  9.967   1.00 13.52 ? 6   TYR B CE2 1 
ATOM   2200 C  CZ  . TYR B 1 6   ? -6.003  -5.888  11.069  1.00 13.13 ? 6   TYR B CZ  1 
ATOM   2201 O  OH  . TYR B 1 6   ? -4.972  -6.610  11.626  1.00 11.78 ? 6   TYR B OH  1 
ATOM   2202 N  N   . PHE B 1 7   ? -11.515 -0.964  9.248   1.00 16.75 ? 7   PHE B N   1 
ATOM   2203 C  CA  . PHE B 1 7   ? -12.488 -0.408  8.299   1.00 21.91 ? 7   PHE B CA  1 
ATOM   2204 C  C   . PHE B 1 7   ? -13.198 0.694   8.992   1.00 23.24 ? 7   PHE B C   1 
ATOM   2205 O  O   . PHE B 1 7   ? -13.692 0.474   10.082  1.00 24.02 ? 7   PHE B O   1 
ATOM   2206 C  CB  . PHE B 1 7   ? -13.515 -1.481  7.935   1.00 24.49 ? 7   PHE B CB  1 
ATOM   2207 C  CG  . PHE B 1 7   ? -14.645 -1.002  7.042   1.00 34.39 ? 7   PHE B CG  1 
ATOM   2208 C  CD1 . PHE B 1 7   ? -14.403 -0.620  5.705   1.00 33.89 ? 7   PHE B CD1 1 
ATOM   2209 C  CD2 . PHE B 1 7   ? -15.974 -0.991  7.517   1.00 37.54 ? 7   PHE B CD2 1 
ATOM   2210 C  CE1 . PHE B 1 7   ? -15.451 -0.220  4.878   1.00 38.78 ? 7   PHE B CE1 1 
ATOM   2211 C  CE2 . PHE B 1 7   ? -17.024 -0.584  6.688   1.00 40.54 ? 7   PHE B CE2 1 
ATOM   2212 C  CZ  . PHE B 1 7   ? -16.761 -0.215  5.368   1.00 40.76 ? 7   PHE B CZ  1 
ATOM   2213 N  N   . GLY B 1 8   ? -13.344 1.838   8.327   1.00 25.69 ? 8   GLY B N   1 
ATOM   2214 C  CA  . GLY B 1 8   ? -14.203 2.882   8.869   1.00 21.97 ? 8   GLY B CA  1 
ATOM   2215 C  C   . GLY B 1 8   ? -13.313 3.822   9.650   1.00 27.10 ? 8   GLY B C   1 
ATOM   2216 O  O   . GLY B 1 8   ? -12.071 3.822   9.424   1.00 26.26 ? 8   GLY B O   1 
ATOM   2217 N  N   . PRO B 1 9   ? -13.918 4.588   10.592  1.00 24.32 ? 9   PRO B N   1 
ATOM   2218 C  CA  . PRO B 1 9   ? -13.293 5.712   11.263  1.00 27.09 ? 9   PRO B CA  1 
ATOM   2219 C  C   . PRO B 1 9   ? -12.175 5.342   12.202  1.00 25.29 ? 9   PRO B C   1 
ATOM   2220 O  O   . PRO B 1 9   ? -11.340 6.224   12.536  1.00 23.91 ? 9   PRO B O   1 
ATOM   2221 C  CB  . PRO B 1 9   ? -14.459 6.315   12.107  1.00 26.37 ? 9   PRO B CB  1 
ATOM   2222 C  CG  . PRO B 1 9   ? -15.700 5.826   11.429  1.00 26.70 ? 9   PRO B CG  1 
ATOM   2223 C  CD  . PRO B 1 9   ? -15.318 4.424   11.036  1.00 25.45 ? 9   PRO B CD  1 
ATOM   2224 N  N   . ASP B 1 10  ? -12.168 4.094   12.703  1.00 23.17 ? 10  ASP B N   1 
ATOM   2225 C  CA  . ASP B 1 10  ? -11.103 3.708   13.643  1.00 19.63 ? 10  ASP B CA  1 
ATOM   2226 C  C   . ASP B 1 10  ? -10.133 2.753   12.947  1.00 16.23 ? 10  ASP B C   1 
ATOM   2227 O  O   . ASP B 1 10  ? -9.366  2.041   13.622  1.00 17.01 ? 10  ASP B O   1 
ATOM   2228 C  CB  . ASP B 1 10  ? -11.628 3.107   14.968  1.00 23.37 ? 10  ASP B CB  1 
ATOM   2229 C  CG  . ASP B 1 10  ? -12.477 4.087   15.783  1.00 26.63 ? 10  ASP B CG  1 
ATOM   2230 O  OD1 . ASP B 1 10  ? -13.615 3.715   16.118  1.00 29.11 ? 10  ASP B OD1 1 
ATOM   2231 O  OD2 . ASP B 1 10  ? -12.014 5.210   16.088  1.00 31.60 ? 10  ASP B OD2 1 
ATOM   2232 N  N   . GLY B 1 11  ? -10.207 2.754   11.612  1.00 15.03 ? 11  GLY B N   1 
ATOM   2233 C  CA  . GLY B 1 11  ? -9.300  2.036   10.653  1.00 11.81 ? 11  GLY B CA  1 
ATOM   2234 C  C   . GLY B 1 11  ? -7.857  2.502   10.640  1.00 10.43 ? 11  GLY B C   1 
ATOM   2235 O  O   . GLY B 1 11  ? -7.483  3.399   11.389  1.00 10.20 ? 11  GLY B O   1 
ATOM   2236 N  N   . GLU B 1 12  ? -7.038  1.925   9.769   1.00 10.34 ? 12  GLU B N   1 
ATOM   2237 C  CA  . GLU B 1 12  ? -5.588  1.983   9.941   1.00 9.87  ? 12  GLU B CA  1 
ATOM   2238 C  C   . GLU B 1 12  ? -4.994  3.393   9.793   1.00 9.82  ? 12  GLU B C   1 
ATOM   2239 O  O   . GLU B 1 12  ? -3.972  3.719   10.440  1.00 11.27 ? 12  GLU B O   1 
ATOM   2240 C  CB  . GLU B 1 12  ? -4.873  0.971   9.033   1.00 9.47  ? 12  GLU B CB  1 
ATOM   2241 C  CG  . GLU B 1 12  ? -5.014  1.237   7.493   1.00 9.79  ? 12  GLU B CG  1 
ATOM   2242 C  CD  . GLU B 1 12  ? -4.597  0.035   6.679   1.00 10.16 ? 12  GLU B CD  1 
ATOM   2243 O  OE1 . GLU B 1 12  ? -3.415  -0.182  6.457   1.00 10.60 ? 12  GLU B OE1 1 
ATOM   2244 O  OE2 . GLU B 1 12  ? -5.489  -0.729  6.181   1.00 11.71 ? 12  GLU B OE2 1 
ATOM   2245 N  N   . ASN B 1 13  ? -5.605  4.255   8.981   1.00 9.03  ? 13  ASN B N   1 
ATOM   2246 C  CA  . ASN B 1 13  ? -5.075  5.614   8.894   1.00 10.27 ? 13  ASN B CA  1 
ATOM   2247 C  C   . ASN B 1 13  ? -5.300  6.396   10.220  1.00 10.75 ? 13  ASN B C   1 
ATOM   2248 O  O   . ASN B 1 13  ? -4.720  7.455   10.392  1.00 13.49 ? 13  ASN B O   1 
ATOM   2249 C  CB  . ASN B 1 13  ? -5.685  6.399   7.711   1.00 9.58  ? 13  ASN B CB  1 
ATOM   2250 C  CG  . ASN B 1 13  ? -5.279  5.861   6.331   1.00 9.25  ? 13  ASN B CG  1 
ATOM   2251 O  OD1 . ASN B 1 13  ? -4.314  5.045   6.165   1.00 8.92  ? 13  ASN B OD1 1 
ATOM   2252 N  ND2 . ASN B 1 13  ? -6.034  6.312   5.301   1.00 8.60  ? 13  ASN B ND2 1 
ATOM   2253 N  N   . SER B 1 14  ? -6.153  5.897   11.107  1.00 10.05 ? 14  SER B N   1 
ATOM   2254 C  CA  . SER B 1 14  ? -6.404  6.544   12.421  1.00 11.54 ? 14  SER B CA  1 
ATOM   2255 C  C   . SER B 1 14  ? -5.671  5.883   13.598  1.00 11.02 ? 14  SER B C   1 
ATOM   2256 O  O   . SER B 1 14  ? -5.637  6.428   14.717  1.00 10.20 ? 14  SER B O   1 
ATOM   2257 C  CB  . SER B 1 14  ? -7.914  6.587   12.699  1.00 11.68 ? 14  SER B CB  1 
ATOM   2258 O  OG  . SER B 1 14  ? -8.502  7.529   11.772  1.00 12.18 ? 14  SER B OG  1 
ATOM   2259 N  N   . TRP B 1 15  ? -5.064  4.726   13.337  1.00 10.86 ? 15  TRP B N   1 
ATOM   2260 C  CA  . TRP B 1 15  ? -4.325  4.022   14.416  1.00 11.33 ? 15  TRP B CA  1 
ATOM   2261 C  C   . TRP B 1 15  ? -3.357  4.928   15.158  1.00 11.91 ? 15  TRP B C   1 
ATOM   2262 O  O   . TRP B 1 15  ? -3.233  4.853   16.410  1.00 13.46 ? 15  TRP B O   1 
ATOM   2263 C  CB  . TRP B 1 15  ? -3.547  2.850   13.867  1.00 10.59 ? 15  TRP B CB  1 
ATOM   2264 C  CG  . TRP B 1 15  ? -4.406  1.660   13.391  1.00 10.02 ? 15  TRP B CG  1 
ATOM   2265 C  CD1 . TRP B 1 15  ? -5.769  1.551   13.455  1.00 10.08 ? 15  TRP B CD1 1 
ATOM   2266 C  CD2 . TRP B 1 15  ? -3.942  0.438   12.787  1.00 9.98  ? 15  TRP B CD2 1 
ATOM   2267 N  NE1 . TRP B 1 15  ? -6.178  0.343   12.930  1.00 9.67  ? 15  TRP B NE1 1 
ATOM   2268 C  CE2 . TRP B 1 15  ? -5.078  -0.355  12.514  1.00 9.90  ? 15  TRP B CE2 1 
ATOM   2269 C  CE3 . TRP B 1 15  ? -2.677  -0.058  12.452  1.00 10.25 ? 15  TRP B CE3 1 
ATOM   2270 C  CZ2 . TRP B 1 15  ? -4.981  -1.616  11.924  1.00 9.36  ? 15  TRP B CZ2 1 
ATOM   2271 C  CZ3 . TRP B 1 15  ? -2.590  -1.310  11.866  1.00 10.05 ? 15  TRP B CZ3 1 
ATOM   2272 C  CH2 . TRP B 1 15  ? -3.733  -2.073  11.609  1.00 9.92  ? 15  TRP B CH2 1 
ATOM   2273 N  N   . SER B 1 16  ? -2.663  5.787   14.422  1.00 11.92 ? 16  SER B N   1 
ATOM   2274 C  CA  . SER B 1 16  ? -1.630  6.723   15.074  1.00 11.78 ? 16  SER B CA  1 
ATOM   2275 C  C   . SER B 1 16  ? -2.171  7.672   16.126  1.00 12.51 ? 16  SER B C   1 
ATOM   2276 O  O   . SER B 1 16  ? -1.396  8.211   16.911  1.00 11.61 ? 16  SER B O   1 
ATOM   2277 C  CB  . SER B 1 16  ? -0.904  7.574   14.040  1.00 11.63 ? 16  SER B CB  1 
ATOM   2278 O  OG  . SER B 1 16  ? -1.841  8.402   13.336  1.00 12.80 ? 16  SER B OG  1 
ATOM   2279 N  N   . LYS B 1 17  ? -3.490  7.851   16.151  1.00 12.43 ? 17  LYS B N   1 
ATOM   2280 C  CA  . LYS B 1 17  ? -4.114  8.792   17.107  1.00 15.09 ? 17  LYS B CA  1 
ATOM   2281 C  C   . LYS B 1 17  ? -3.965  8.268   18.552  1.00 17.10 ? 17  LYS B C   1 
ATOM   2282 O  O   . LYS B 1 17  ? -3.450  8.989   19.428  1.00 20.94 ? 17  LYS B O   1 
ATOM   2283 C  CB  . LYS B 1 17  ? -5.569  9.068   16.764  1.00 13.64 ? 17  LYS B CB  1 
ATOM   2284 C  CG  . LYS B 1 17  ? -5.800  9.821   15.473  1.00 13.48 ? 17  LYS B CG  1 
ATOM   2285 C  CD  . LYS B 1 17  ? -7.247  9.550   15.015  1.00 11.78 ? 17  LYS B CD  1 
ATOM   2286 C  CE  . LYS B 1 17  ? -7.621  10.314  13.739  1.00 11.67 ? 17  LYS B CE  1 
ATOM   2287 N  NZ  . LYS B 1 17  ? -9.095  10.452  13.484  1.00 10.94 ? 17  LYS B NZ  1 
ATOM   2288 N  N   . LYS B 1 18  ? -4.280  6.987   18.757  1.00 16.18 ? 18  LYS B N   1 
ATOM   2289 C  CA  . LYS B 1 18  ? -4.258  6.380   20.083  1.00 17.20 ? 18  LYS B CA  1 
ATOM   2290 C  C   . LYS B 1 18  ? -2.952  5.594   20.307  1.00 15.41 ? 18  LYS B C   1 
ATOM   2291 O  O   . LYS B 1 18  ? -2.605  5.321   21.425  1.00 14.76 ? 18  LYS B O   1 
ATOM   2292 C  CB  . LYS B 1 18  ? -5.490  5.453   20.266  1.00 18.36 ? 18  LYS B CB  1 
ATOM   2293 C  CG  . LYS B 1 18  ? -5.422  4.401   21.376  1.00 25.22 ? 18  LYS B CG  1 
ATOM   2294 C  CD  . LYS B 1 18  ? -5.753  4.834   22.805  1.00 29.29 ? 18  LYS B CD  1 
ATOM   2295 C  CE  . LYS B 1 18  ? -7.197  4.478   23.226  1.00 32.70 ? 18  LYS B CE  1 
ATOM   2296 N  NZ  . LYS B 1 18  ? -7.501  3.003   23.289  1.00 30.40 ? 18  LYS B NZ  1 
ATOM   2297 N  N   . TYR B 1 19  ? -2.265  5.265   19.227  1.00 13.65 ? 19  TYR B N   1 
ATOM   2298 C  CA  . TYR B 1 19  ? -1.087  4.397   19.209  1.00 14.03 ? 19  TYR B CA  1 
ATOM   2299 C  C   . TYR B 1 19  ? -0.024  5.063   18.404  1.00 12.70 ? 19  TYR B C   1 
ATOM   2300 O  O   . TYR B 1 19  ? 0.134   4.781   17.253  1.00 11.63 ? 19  TYR B O   1 
ATOM   2301 C  CB  . TYR B 1 19  ? -1.417  3.017   18.597  1.00 14.54 ? 19  TYR B CB  1 
ATOM   2302 C  CG  . TYR B 1 19  ? -2.509  2.267   19.321  1.00 16.57 ? 19  TYR B CG  1 
ATOM   2303 C  CD1 . TYR B 1 19  ? -3.842  2.273   18.831  1.00 16.88 ? 19  TYR B CD1 1 
ATOM   2304 C  CD2 . TYR B 1 19  ? -2.241  1.571   20.535  1.00 15.92 ? 19  TYR B CD2 1 
ATOM   2305 C  CE1 . TYR B 1 19  ? -4.846  1.583   19.473  1.00 19.35 ? 19  TYR B CE1 1 
ATOM   2306 C  CE2 . TYR B 1 19  ? -3.273  0.906   21.210  1.00 19.62 ? 19  TYR B CE2 1 
ATOM   2307 C  CZ  . TYR B 1 19  ? -4.558  0.921   20.677  1.00 20.66 ? 19  TYR B CZ  1 
ATOM   2308 O  OH  . TYR B 1 19  ? -5.596  0.264   21.319  1.00 21.60 ? 19  TYR B OH  1 
ATOM   2309 N  N   . PRO B 1 20  ? 0.760   5.976   19.015  1.00 12.80 ? 20  PRO B N   1 
ATOM   2310 C  CA  . PRO B 1 20  ? 1.713   6.805   18.261  1.00 12.85 ? 20  PRO B CA  1 
ATOM   2311 C  C   . PRO B 1 20  ? 2.727   5.987   17.385  1.00 12.20 ? 20  PRO B C   1 
ATOM   2312 O  O   . PRO B 1 20  ? 3.085   6.423   16.288  1.00 13.11 ? 20  PRO B O   1 
ATOM   2313 C  CB  . PRO B 1 20  ? 2.445   7.599   19.371  1.00 13.24 ? 20  PRO B CB  1 
ATOM   2314 C  CG  . PRO B 1 20  ? 1.466   7.601   20.505  1.00 14.14 ? 20  PRO B CG  1 
ATOM   2315 C  CD  . PRO B 1 20  ? 0.751   6.266   20.453  1.00 13.14 ? 20  PRO B CD  1 
ATOM   2316 N  N   . SER B 1 21  ? 3.106   4.784   17.824  1.00 11.34 ? 21  SER B N   1 
ATOM   2317 C  CA  . SER B 1 21  ? 4.105   3.996   17.083  1.00 10.56 ? 21  SER B CA  1 
ATOM   2318 C  C   . SER B 1 21  ? 3.577   3.583   15.743  1.00 11.68 ? 21  SER B C   1 
ATOM   2319 O  O   . SER B 1 21  ? 4.381   3.346   14.821  1.00 11.07 ? 21  SER B O   1 
ATOM   2320 C  CB  . SER B 1 21  ? 4.694   2.814   17.894  1.00 10.99 ? 21  SER B CB  1 
ATOM   2321 O  OG  . SER B 1 21  ? 5.411   3.273   19.061  1.00 11.42 ? 21  SER B OG  1 
ATOM   2322 N  N   . CYS B 1 22  ? 2.242   3.589   15.578  1.00 10.88 ? 22  CYS B N   1 
ATOM   2323 C  CA  . CYS B 1 22  ? 1.677   3.226   14.242  1.00 11.14 ? 22  CYS B CA  1 
ATOM   2324 C  C   . CYS B 1 22  ? 2.011   4.271   13.133  1.00 10.95 ? 22  CYS B C   1 
ATOM   2325 O  O   . CYS B 1 22  ? 1.957   3.978   11.895  1.00 11.72 ? 22  CYS B O   1 
ATOM   2326 C  CB  . CYS B 1 22  ? 0.160   2.947   14.399  1.00 10.58 ? 22  CYS B CB  1 
ATOM   2327 S  SG  . CYS B 1 22  ? -0.327  1.523   15.438  1.00 10.75 ? 22  CYS B SG  1 
ATOM   2328 N  N   . GLY B 1 23  ? 2.350   5.492   13.561  1.00 12.07 ? 23  GLY B N   1 
ATOM   2329 C  CA  . GLY B 1 23  ? 2.994   6.457   12.665  1.00 11.56 ? 23  GLY B CA  1 
ATOM   2330 C  C   . GLY B 1 23  ? 4.484   6.728   12.926  1.00 13.38 ? 23  GLY B C   1 
ATOM   2331 O  O   . GLY B 1 23  ? 4.997   7.809   12.499  1.00 13.70 ? 23  GLY B O   1 
ATOM   2332 N  N   . GLY B 1 24  ? 5.199   5.771   13.522  1.00 13.48 ? 24  GLY B N   1 
ATOM   2333 C  CA  . GLY B 1 24  ? 6.646   5.904   13.832  1.00 13.30 ? 24  GLY B CA  1 
ATOM   2334 C  C   . GLY B 1 24  ? 7.527   5.113   12.872  1.00 13.19 ? 24  GLY B C   1 
ATOM   2335 O  O   . GLY B 1 24  ? 7.140   4.867   11.756  1.00 12.99 ? 24  GLY B O   1 
ATOM   2336 N  N   . LEU B 1 25  ? 8.680   4.674   13.337  1.00 11.87 ? 25  LEU B N   1 
ATOM   2337 C  CA  . LEU B 1 25  ? 9.737   4.079   12.527  1.00 12.18 ? 25  LEU B CA  1 
ATOM   2338 C  C   . LEU B 1 25  ? 9.499   2.598   12.377  1.00 11.31 ? 25  LEU B C   1 
ATOM   2339 O  O   . LEU B 1 25  ? 8.759   1.999   13.146  1.00 11.44 ? 25  LEU B O   1 
ATOM   2340 C  CB  . LEU B 1 25  ? 11.115  4.230   13.250  1.00 13.80 ? 25  LEU B CB  1 
ATOM   2341 C  CG  . LEU B 1 25  ? 11.537  5.665   13.539  1.00 13.41 ? 25  LEU B CG  1 
ATOM   2342 C  CD1 . LEU B 1 25  ? 12.622  5.664   14.589  1.00 12.99 ? 25  LEU B CD1 1 
ATOM   2343 C  CD2 . LEU B 1 25  ? 12.068  6.250   12.252  1.00 15.74 ? 25  LEU B CD2 1 
ATOM   2344 N  N   . LEU B 1 26  ? 10.217  2.030   11.417  1.00 11.07 ? 26  LEU B N   1 
ATOM   2345 C  CA  . LEU B 1 26  ? 10.278  0.606   11.210  1.00 10.92 ? 26  LEU B CA  1 
ATOM   2346 C  C   . LEU B 1 26  ? 8.918   -0.094  11.026  1.00 10.46 ? 26  LEU B C   1 
ATOM   2347 O  O   . LEU B 1 26  ? 8.801   -1.277  11.343  1.00 10.77 ? 26  LEU B O   1 
ATOM   2348 C  CB  . LEU B 1 26  ? 11.093  -0.122  12.268  1.00 11.69 ? 26  LEU B CB  1 
ATOM   2349 C  CG  . LEU B 1 26  ? 12.531  0.365   12.469  1.00 11.96 ? 26  LEU B CG  1 
ATOM   2350 C  CD1 . LEU B 1 26  ? 13.196  -0.309  13.676  1.00 13.27 ? 26  LEU B CD1 1 
ATOM   2351 C  CD2 . LEU B 1 26  ? 13.286  0.119   11.208  1.00 12.96 ? 26  LEU B CD2 1 
ATOM   2352 N  N   . GLN B 1 27  ? 7.943   0.546   10.394  1.00 9.27  ? 27  GLN B N   1 
ATOM   2353 C  CA  . GLN B 1 27  ? 6.639   -0.138  10.232  1.00 8.54  ? 27  GLN B CA  1 
ATOM   2354 C  C   . GLN B 1 27  ? 6.556   -1.304  9.204   1.00 8.56  ? 27  GLN B C   1 
ATOM   2355 O  O   . GLN B 1 27  ? 7.136   -1.208  8.142   1.00 8.26  ? 27  GLN B O   1 
ATOM   2356 C  CB  . GLN B 1 27  ? 5.598   0.973   9.919   1.00 9.38  ? 27  GLN B CB  1 
ATOM   2357 C  CG  . GLN B 1 27  ? 5.361   1.965   11.054  1.00 9.04  ? 27  GLN B CG  1 
ATOM   2358 C  CD  . GLN B 1 27  ? 4.859   1.270   12.293  1.00 9.86  ? 27  GLN B CD  1 
ATOM   2359 O  OE1 . GLN B 1 27  ? 3.717   0.768   12.300  1.00 11.08 ? 27  GLN B OE1 1 
ATOM   2360 N  NE2 . GLN B 1 27  ? 5.752   1.129   13.347  1.00 10.44 ? 27  GLN B NE2 1 
ATOM   2361 N  N   . SER B 1 28  ? 5.770   -2.345  9.514   1.00 8.08  ? 28  SER B N   1 
ATOM   2362 C  CA  . SER B 1 28  ? 5.458   -3.449  8.644   1.00 8.16  ? 28  SER B CA  1 
ATOM   2363 C  C   . SER B 1 28  ? 3.942   -3.496  8.428   1.00 7.62  ? 28  SER B C   1 
ATOM   2364 O  O   . SER B 1 28  ? 3.153   -2.844  9.166   1.00 7.84  ? 28  SER B O   1 
ATOM   2365 C  CB  . SER B 1 28  ? 5.896   -4.782  9.378   1.00 8.37  ? 28  SER B CB  1 
ATOM   2366 O  OG  . SER B 1 28  ? 7.253   -4.704  9.831   1.00 9.51  ? 28  SER B OG  1 
ATOM   2367 N  N   . PRO B 1 29  ? 3.511   -4.215  7.413   1.00 7.88  ? 29  PRO B N   1 
ATOM   2368 C  CA  . PRO B 1 29  ? 4.306   -4.997  6.450   1.00 8.40  ? 29  PRO B CA  1 
ATOM   2369 C  C   . PRO B 1 29  ? 4.860   -4.116  5.311   1.00 9.01  ? 29  PRO B C   1 
ATOM   2370 O  O   . PRO B 1 29  ? 4.585   -2.913  5.269   1.00 10.02 ? 29  PRO B O   1 
ATOM   2371 C  CB  . PRO B 1 29  ? 3.255   -5.969  5.911   1.00 8.26  ? 29  PRO B CB  1 
ATOM   2372 C  CG  . PRO B 1 29  ? 2.037   -5.106  5.871   1.00 7.94  ? 29  PRO B CG  1 
ATOM   2373 C  CD  . PRO B 1 29  ? 2.071   -4.415  7.190   1.00 7.86  ? 29  PRO B CD  1 
ATOM   2374 N  N   . ILE B 1 30  ? 5.593   -4.737  4.378   1.00 9.90  ? 30  ILE B N   1 
ATOM   2375 C  CA  . ILE B 1 30  ? 6.183   -4.035  3.242   1.00 10.57 ? 30  ILE B CA  1 
ATOM   2376 C  C   . ILE B 1 30  ? 6.035   -4.811  1.995   1.00 11.73 ? 30  ILE B C   1 
ATOM   2377 O  O   . ILE B 1 30  ? 5.636   -6.019  2.037   1.00 12.79 ? 30  ILE B O   1 
ATOM   2378 C  CB  . ILE B 1 30  ? 7.680   -3.798  3.435   1.00 11.36 ? 30  ILE B CB  1 
ATOM   2379 C  CG1 . ILE B 1 30  ? 8.451   -5.133  3.689   1.00 11.06 ? 30  ILE B CG1 1 
ATOM   2380 C  CG2 . ILE B 1 30  ? 7.857   -2.766  4.544   1.00 10.43 ? 30  ILE B CG2 1 
ATOM   2381 C  CD1 . ILE B 1 30  ? 9.971   -4.954  3.664   1.00 11.19 ? 30  ILE B CD1 1 
ATOM   2382 N  N   . ASP B 1 31  ? 6.353   -4.162  0.876   1.00 11.86 ? 31  ASP B N   1 
ATOM   2383 C  CA  . ASP B 1 31  ? 6.363   -4.913  -0.396  1.00 12.97 ? 31  ASP B CA  1 
ATOM   2384 C  C   . ASP B 1 31  ? 7.790   -5.358  -0.621  1.00 13.60 ? 31  ASP B C   1 
ATOM   2385 O  O   . ASP B 1 31  ? 8.702   -4.537  -0.610  1.00 12.04 ? 31  ASP B O   1 
ATOM   2386 C  CB  . ASP B 1 31  ? 5.933   -4.027  -1.577  1.00 13.32 ? 31  ASP B CB  1 
ATOM   2387 C  CG  . ASP B 1 31  ? 6.126   -4.709  -2.912  1.00 13.48 ? 31  ASP B CG  1 
ATOM   2388 O  OD1 . ASP B 1 31  ? 5.612   -5.847  -3.108  1.00 13.92 ? 31  ASP B OD1 1 
ATOM   2389 O  OD2 . ASP B 1 31  ? 6.728   -4.115  -3.803  1.00 14.11 ? 31  ASP B OD2 1 
ATOM   2390 N  N   . LEU B 1 32  ? 7.957   -6.665  -0.833  1.00 13.72 ? 32  LEU B N   1 
ATOM   2391 C  CA  . LEU B 1 32  ? 9.266   -7.311  -1.131  1.00 13.83 ? 32  LEU B CA  1 
ATOM   2392 C  C   . LEU B 1 32  ? 9.508   -7.282  -2.644  1.00 15.07 ? 32  LEU B C   1 
ATOM   2393 O  O   . LEU B 1 32  ? 8.823   -8.012  -3.420  1.00 14.07 ? 32  LEU B O   1 
ATOM   2394 C  CB  . LEU B 1 32  ? 9.282   -8.762  -0.555  1.00 12.91 ? 32  LEU B CB  1 
ATOM   2395 C  CG  . LEU B 1 32  ? 8.959   -8.891  0.969   1.00 12.67 ? 32  LEU B CG  1 
ATOM   2396 C  CD1 . LEU B 1 32  ? 8.574   -10.306 1.364   1.00 13.95 ? 32  LEU B CD1 1 
ATOM   2397 C  CD2 . LEU B 1 32  ? 10.071  -8.375  1.894   1.00 12.71 ? 32  LEU B CD2 1 
ATOM   2398 N  N   . HIS B 1 33  ? 10.400  -6.374  -3.071  1.00 15.77 ? 33  HIS B N   1 
ATOM   2399 C  CA  . HIS B 1 33  ? 10.706  -6.140  -4.531  1.00 15.56 ? 33  HIS B CA  1 
ATOM   2400 C  C   . HIS B 1 33  ? 12.186  -5.878  -4.770  1.00 15.49 ? 33  HIS B C   1 
ATOM   2401 O  O   . HIS B 1 33  ? 12.942  -5.517  -3.830  1.00 14.41 ? 33  HIS B O   1 
ATOM   2402 C  CB  . HIS B 1 33  ? 9.827   -4.998  -5.145  1.00 16.14 ? 33  HIS B CB  1 
ATOM   2403 C  CG  . HIS B 1 33  ? 10.090  -3.637  -4.565  1.00 16.29 ? 33  HIS B CG  1 
ATOM   2404 N  ND1 . HIS B 1 33  ? 9.770   -3.299  -3.267  1.00 17.88 ? 33  HIS B ND1 1 
ATOM   2405 C  CD2 . HIS B 1 33  ? 10.628  -2.524  -5.120  1.00 15.99 ? 33  HIS B CD2 1 
ATOM   2406 C  CE1 . HIS B 1 33  ? 10.101  -2.038  -3.046  1.00 18.00 ? 33  HIS B CE1 1 
ATOM   2407 N  NE2 . HIS B 1 33  ? 10.627  -1.547  -4.153  1.00 17.19 ? 33  HIS B NE2 1 
ATOM   2408 N  N   . SER B 1 34  ? 12.640  -6.035  -6.006  1.00 17.87 ? 34  SER B N   1 
ATOM   2409 C  CA  . SER B 1 34  ? 14.084  -6.157  -6.275  1.00 19.16 ? 34  SER B CA  1 
ATOM   2410 C  C   . SER B 1 34  ? 14.909  -4.939  -5.830  1.00 20.79 ? 34  SER B C   1 
ATOM   2411 O  O   . SER B 1 34  ? 16.019  -5.101  -5.354  1.00 18.75 ? 34  SER B O   1 
ATOM   2412 C  CB  . SER B 1 34  ? 14.318  -6.461  -7.755  1.00 23.50 ? 34  SER B CB  1 
ATOM   2413 O  OG  . SER B 1 34  ? 13.741  -5.468  -8.587  1.00 27.93 ? 34  SER B OG  1 
ATOM   2414 N  N   . ASP B 1 35  ? 14.335  -3.733  -5.915  1.00 19.24 ? 35  ASP B N   1 
ATOM   2415 C  CA  . ASP B 1 35  ? 15.088  -2.499  -5.653  1.00 18.53 ? 35  ASP B CA  1 
ATOM   2416 C  C   . ASP B 1 35  ? 15.562  -2.412  -4.222  1.00 18.36 ? 35  ASP B C   1 
ATOM   2417 O  O   . ASP B 1 35  ? 16.524  -1.677  -3.929  1.00 20.37 ? 35  ASP B O   1 
ATOM   2418 C  CB  . ASP B 1 35  ? 14.242  -1.250  -5.961  1.00 19.08 ? 35  ASP B CB  1 
ATOM   2419 C  CG  . ASP B 1 35  ? 13.634  -1.261  -7.372  1.00 21.29 ? 35  ASP B CG  1 
ATOM   2420 O  OD1 . ASP B 1 35  ? 14.042  -0.344  -8.168  1.00 17.37 ? 35  ASP B OD1 1 
ATOM   2421 O  OD2 . ASP B 1 35  ? 12.748  -2.168  -7.679  1.00 21.33 ? 35  ASP B OD2 1 
ATOM   2422 N  N   . ILE B 1 36  ? 14.874  -3.118  -3.307  1.00 15.90 ? 36  ILE B N   1 
ATOM   2423 C  CA  . ILE B 1 36  ? 15.202  -3.069  -1.872  1.00 15.06 ? 36  ILE B CA  1 
ATOM   2424 C  C   . ILE B 1 36  ? 15.808  -4.401  -1.331  1.00 15.69 ? 36  ILE B C   1 
ATOM   2425 O  O   . ILE B 1 36  ? 16.005  -4.513  -0.114  1.00 14.89 ? 36  ILE B O   1 
ATOM   2426 C  CB  . ILE B 1 36  ? 13.996  -2.632  -0.988  1.00 15.48 ? 36  ILE B CB  1 
ATOM   2427 C  CG1 . ILE B 1 36  ? 12.840  -3.711  -1.106  1.00 17.08 ? 36  ILE B CG1 1 
ATOM   2428 C  CG2 . ILE B 1 36  ? 13.560  -1.230  -1.382  1.00 16.25 ? 36  ILE B CG2 1 
ATOM   2429 C  CD1 . ILE B 1 36  ? 11.831  -3.815  0.046   1.00 20.65 ? 36  ILE B CD1 1 
ATOM   2430 N  N   . LEU B 1 37  ? 16.085  -5.388  -2.195  1.00 16.18 ? 37  LEU B N   1 
ATOM   2431 C  CA  . LEU B 1 37  ? 16.621  -6.695  -1.721  1.00 18.17 ? 37  LEU B CA  1 
ATOM   2432 C  C   . LEU B 1 37  ? 18.152  -6.740  -1.839  1.00 18.38 ? 37  LEU B C   1 
ATOM   2433 O  O   . LEU B 1 37  ? 18.743  -6.110  -2.760  1.00 18.22 ? 37  LEU B O   1 
ATOM   2434 C  CB  . LEU B 1 37  ? 16.005  -7.902  -2.453  1.00 18.38 ? 37  LEU B CB  1 
ATOM   2435 C  CG  . LEU B 1 37  ? 14.484  -8.082  -2.602  1.00 18.92 ? 37  LEU B CG  1 
ATOM   2436 C  CD1 . LEU B 1 37  ? 14.180  -9.320  -3.433  1.00 19.29 ? 37  LEU B CD1 1 
ATOM   2437 C  CD2 . LEU B 1 37  ? 13.810  -8.187  -1.244  1.00 17.18 ? 37  LEU B CD2 1 
ATOM   2438 N  N   . GLN B 1 38  ? 18.812  -7.430  -0.892  1.00 18.92 ? 38  GLN B N   1 
ATOM   2439 C  CA  . GLN B 1 38  ? 20.266  -7.636  -0.945  1.00 18.34 ? 38  GLN B CA  1 
ATOM   2440 C  C   . GLN B 1 38  ? 20.606  -9.037  -0.390  1.00 17.77 ? 38  GLN B C   1 
ATOM   2441 O  O   . GLN B 1 38  ? 20.303  -9.320  0.759   1.00 14.89 ? 38  GLN B O   1 
ATOM   2442 C  CB  . GLN B 1 38  ? 21.003  -6.557  -0.135  1.00 21.85 ? 38  GLN B CB  1 
ATOM   2443 C  CG  . GLN B 1 38  ? 22.533  -6.722  -0.100  1.00 24.51 ? 38  GLN B CG  1 
ATOM   2444 C  CD  . GLN B 1 38  ? 23.254  -5.512  0.477   1.00 30.32 ? 38  GLN B CD  1 
ATOM   2445 O  OE1 . GLN B 1 38  ? 23.848  -5.587  1.550   1.00 27.95 ? 38  GLN B OE1 1 
ATOM   2446 N  NE2 . GLN B 1 38  ? 23.148  -4.370  -0.213  1.00 29.74 ? 38  GLN B NE2 1 
ATOM   2447 N  N   . TYR B 1 39  ? 21.268  -9.880  -1.181  1.00 15.71 ? 39  TYR B N   1 
ATOM   2448 C  CA  . TYR B 1 39  ? 21.663  -11.224 -0.682  1.00 14.42 ? 39  TYR B CA  1 
ATOM   2449 C  C   . TYR B 1 39  ? 22.647  -11.072 0.472   1.00 14.63 ? 39  TYR B C   1 
ATOM   2450 O  O   . TYR B 1 39  ? 23.611  -10.293 0.357   1.00 14.14 ? 39  TYR B O   1 
ATOM   2451 C  CB  . TYR B 1 39  ? 22.321  -11.974 -1.819  1.00 14.40 ? 39  TYR B CB  1 
ATOM   2452 C  CG  . TYR B 1 39  ? 22.884  -13.313 -1.456  1.00 15.17 ? 39  TYR B CG  1 
ATOM   2453 C  CD1 . TYR B 1 39  ? 22.079  -14.300 -0.869  1.00 14.67 ? 39  TYR B CD1 1 
ATOM   2454 C  CD2 . TYR B 1 39  ? 24.209  -13.617 -1.768  1.00 14.38 ? 39  TYR B CD2 1 
ATOM   2455 C  CE1 . TYR B 1 39  ? 22.594  -15.545 -0.579  1.00 14.68 ? 39  TYR B CE1 1 
ATOM   2456 C  CE2 . TYR B 1 39  ? 24.733  -14.867 -1.500  1.00 15.56 ? 39  TYR B CE2 1 
ATOM   2457 C  CZ  . TYR B 1 39  ? 23.941  -15.805 -0.900  1.00 15.97 ? 39  TYR B CZ  1 
ATOM   2458 O  OH  . TYR B 1 39  ? 24.493  -17.018 -0.592  1.00 16.40 ? 39  TYR B OH  1 
ATOM   2459 N  N   . ASP B 1 40  ? 22.420  -11.799 1.578   1.00 13.68 ? 40  ASP B N   1 
ATOM   2460 C  CA  . ASP B 1 40  ? 23.379  -11.845 2.704   1.00 13.31 ? 40  ASP B CA  1 
ATOM   2461 C  C   . ASP B 1 40  ? 23.834  -13.316 2.874   1.00 14.15 ? 40  ASP B C   1 
ATOM   2462 O  O   . ASP B 1 40  ? 23.055  -14.165 3.356   1.00 13.78 ? 40  ASP B O   1 
ATOM   2463 C  CB  . ASP B 1 40  ? 22.718  -11.295 3.966   1.00 15.56 ? 40  ASP B CB  1 
ATOM   2464 C  CG  . ASP B 1 40  ? 23.681  -11.179 5.141   1.00 16.63 ? 40  ASP B CG  1 
ATOM   2465 O  OD1 . ASP B 1 40  ? 23.354  -10.504 6.148   1.00 18.52 ? 40  ASP B OD1 1 
ATOM   2466 O  OD2 . ASP B 1 40  ? 24.754  -11.785 5.065   1.00 17.75 ? 40  ASP B OD2 1 
ATOM   2467 N  N   . ALA B 1 41  ? 25.041  -13.665 2.405   1.00 12.53 ? 41  ALA B N   1 
ATOM   2468 C  CA  . ALA B 1 41  ? 25.505  -15.059 2.486   1.00 13.41 ? 41  ALA B CA  1 
ATOM   2469 C  C   . ALA B 1 41  ? 25.671  -15.549 3.933   1.00 13.19 ? 41  ALA B C   1 
ATOM   2470 O  O   . ALA B 1 41  ? 25.806  -16.759 4.156   1.00 15.31 ? 41  ALA B O   1 
ATOM   2471 C  CB  . ALA B 1 41  ? 26.817  -15.258 1.711   1.00 12.50 ? 41  ALA B CB  1 
ATOM   2472 N  N   . SER B 1 42  ? 25.740  -14.637 4.912   1.00 15.12 ? 42  SER B N   1 
ATOM   2473 C  CA  . SER B 1 42  ? 25.845  -15.070 6.322   1.00 16.90 ? 42  SER B CA  1 
ATOM   2474 C  C   . SER B 1 42  ? 24.524  -15.558 6.999   1.00 19.93 ? 42  SER B C   1 
ATOM   2475 O  O   . SER B 1 42  ? 24.536  -16.167 8.111   1.00 18.86 ? 42  SER B O   1 
ATOM   2476 C  CB  . SER B 1 42  ? 26.521  -14.001 7.169   1.00 18.11 ? 42  SER B CB  1 
ATOM   2477 O  OG  . SER B 1 42  ? 27.888  -13.807 6.825   1.00 17.77 ? 42  SER B OG  1 
ATOM   2478 N  N   . LEU B 1 43  ? 23.384  -15.347 6.348   1.00 17.04 ? 43  LEU B N   1 
ATOM   2479 C  CA  . LEU B 1 43  ? 22.110  -15.727 6.993   1.00 18.70 ? 43  LEU B CA  1 
ATOM   2480 C  C   . LEU B 1 43  ? 22.002  -17.263 6.990   1.00 20.47 ? 43  LEU B C   1 
ATOM   2481 O  O   . LEU B 1 43  ? 21.970  -17.808 5.952   1.00 21.37 ? 43  LEU B O   1 
ATOM   2482 C  CB  . LEU B 1 43  ? 20.907  -15.167 6.167   1.00 16.89 ? 43  LEU B CB  1 
ATOM   2483 C  CG  . LEU B 1 43  ? 20.747  -13.642 6.059   1.00 17.20 ? 43  LEU B CG  1 
ATOM   2484 C  CD1 . LEU B 1 43  ? 19.622  -13.263 5.075   1.00 15.48 ? 43  LEU B CD1 1 
ATOM   2485 C  CD2 . LEU B 1 43  ? 20.466  -13.087 7.437   1.00 17.88 ? 43  LEU B CD2 1 
ATOM   2486 N  N   . THR B 1 44  ? 21.861  -17.921 8.153   1.00 23.92 ? 44  THR B N   1 
ATOM   2487 C  CA  . THR B 1 44  ? 21.752  -19.411 8.218   1.00 24.21 ? 44  THR B CA  1 
ATOM   2488 C  C   . THR B 1 44  ? 20.314  -19.927 8.355   1.00 20.67 ? 44  THR B C   1 
ATOM   2489 O  O   . THR B 1 44  ? 19.435  -19.195 8.854   1.00 20.20 ? 44  THR B O   1 
ATOM   2490 C  CB  . THR B 1 44  ? 22.534  -19.989 9.397   1.00 26.56 ? 44  THR B CB  1 
ATOM   2491 O  OG1 . THR B 1 44  ? 22.064  -19.391 10.616  1.00 28.02 ? 44  THR B OG1 1 
ATOM   2492 C  CG2 . THR B 1 44  ? 24.045  -19.773 9.207   1.00 29.84 ? 44  THR B CG2 1 
ATOM   2493 N  N   . PRO B 1 45  ? 20.066  -21.174 7.930   1.00 19.48 ? 45  PRO B N   1 
ATOM   2494 C  CA  . PRO B 1 45  ? 18.697  -21.618 8.019   1.00 19.54 ? 45  PRO B CA  1 
ATOM   2495 C  C   . PRO B 1 45  ? 18.261  -21.730 9.458   1.00 19.82 ? 45  PRO B C   1 
ATOM   2496 O  O   . PRO B 1 45  ? 19.065  -22.120 10.370  1.00 18.15 ? 45  PRO B O   1 
ATOM   2497 C  CB  . PRO B 1 45  ? 18.696  -23.015 7.412   1.00 19.06 ? 45  PRO B CB  1 
ATOM   2498 C  CG  . PRO B 1 45  ? 20.050  -23.264 6.920   1.00 21.01 ? 45  PRO B CG  1 
ATOM   2499 C  CD  . PRO B 1 45  ? 20.942  -22.124 7.221   1.00 19.21 ? 45  PRO B CD  1 
ATOM   2500 N  N   . LEU B 1 46  ? 16.997  -21.399 9.683   1.00 18.09 ? 46  LEU B N   1 
ATOM   2501 C  CA  . LEU B 1 46  ? 16.435  -21.612 10.990  1.00 17.99 ? 46  LEU B CA  1 
ATOM   2502 C  C   . LEU B 1 46  ? 16.243  -23.107 11.290  1.00 17.27 ? 46  LEU B C   1 
ATOM   2503 O  O   . LEU B 1 46  ? 16.074  -23.954 10.389  1.00 18.89 ? 46  LEU B O   1 
ATOM   2504 C  CB  . LEU B 1 46  ? 15.124  -20.829 11.166  1.00 18.84 ? 46  LEU B CB  1 
ATOM   2505 C  CG  . LEU B 1 46  ? 15.252  -19.301 11.007  1.00 20.94 ? 46  LEU B CG  1 
ATOM   2506 C  CD1 . LEU B 1 46  ? 13.900  -18.657 11.094  1.00 23.48 ? 46  LEU B CD1 1 
ATOM   2507 C  CD2 . LEU B 1 46  ? 16.170  -18.683 12.050  1.00 22.93 ? 46  LEU B CD2 1 
ATOM   2508 N  N   . GLU B 1 47  ? 16.288  -23.397 12.584  1.00 19.38 ? 47  GLU B N   1 
ATOM   2509 C  CA  . GLU B 1 47  ? 15.951  -24.728 13.125  1.00 18.01 ? 47  GLU B CA  1 
ATOM   2510 C  C   . GLU B 1 47  ? 14.788  -24.538 14.083  1.00 17.45 ? 47  GLU B C   1 
ATOM   2511 O  O   . GLU B 1 47  ? 14.745  -23.577 14.886  1.00 18.46 ? 47  GLU B O   1 
ATOM   2512 C  CB  . GLU B 1 47  ? 17.184  -25.432 13.763  1.00 20.23 ? 47  GLU B CB  1 
ATOM   2513 C  CG  . GLU B 1 47  ? 18.394  -25.480 12.816  1.00 24.60 ? 47  GLU B CG  1 
ATOM   2514 C  CD  . GLU B 1 47  ? 19.663  -26.123 13.394  1.00 29.64 ? 47  GLU B CD  1 
ATOM   2515 O  OE1 . GLU B 1 47  ? 20.776  -25.552 13.261  1.00 33.69 ? 47  GLU B OE1 1 
ATOM   2516 O  OE2 . GLU B 1 47  ? 19.560  -27.205 13.979  1.00 32.16 ? 47  GLU B OE2 1 
ATOM   2517 N  N   . PHE B 1 48  ? 13.804  -25.437 13.938  1.00 17.99 ? 48  PHE B N   1 
ATOM   2518 C  CA  . PHE B 1 48  ? 12.514  -25.374 14.644  1.00 16.75 ? 48  PHE B CA  1 
ATOM   2519 C  C   . PHE B 1 48  ? 12.517  -26.517 15.651  1.00 18.62 ? 48  PHE B C   1 
ATOM   2520 O  O   . PHE B 1 48  ? 12.618  -27.693 15.248  1.00 19.55 ? 48  PHE B O   1 
ATOM   2521 C  CB  . PHE B 1 48  ? 11.410  -25.577 13.620  1.00 17.23 ? 48  PHE B CB  1 
ATOM   2522 C  CG  . PHE B 1 48  ? 11.523  -24.639 12.464  1.00 16.83 ? 48  PHE B CG  1 
ATOM   2523 C  CD1 . PHE B 1 48  ? 11.883  -25.108 11.232  1.00 18.13 ? 48  PHE B CD1 1 
ATOM   2524 C  CD2 . PHE B 1 48  ? 11.338  -23.269 12.647  1.00 17.15 ? 48  PHE B CD2 1 
ATOM   2525 C  CE1 . PHE B 1 48  ? 12.059  -24.245 10.165  1.00 18.46 ? 48  PHE B CE1 1 
ATOM   2526 C  CE2 . PHE B 1 48  ? 11.475  -22.389 11.582  1.00 16.80 ? 48  PHE B CE2 1 
ATOM   2527 C  CZ  . PHE B 1 48  ? 11.837  -22.876 10.341  1.00 16.20 ? 48  PHE B CZ  1 
ATOM   2528 N  N   . GLN B 1 49  ? 12.500  -26.155 16.942  1.00 17.64 ? 49  GLN B N   1 
ATOM   2529 C  CA  . GLN B 1 49  ? 12.647  -27.122 18.031  1.00 16.89 ? 49  GLN B CA  1 
ATOM   2530 C  C   . GLN B 1 49  ? 11.376  -27.128 18.872  1.00 15.66 ? 49  GLN B C   1 
ATOM   2531 O  O   . GLN B 1 49  ? 10.830  -26.079 19.224  1.00 14.90 ? 49  GLN B O   1 
ATOM   2532 C  CB  . GLN B 1 49  ? 13.837  -26.696 18.909  1.00 17.69 ? 49  GLN B CB  1 
ATOM   2533 C  CG  . GLN B 1 49  ? 15.212  -26.797 18.207  1.00 20.42 ? 49  GLN B CG  1 
ATOM   2534 C  CD  . GLN B 1 49  ? 16.297  -25.997 18.889  1.00 25.07 ? 49  GLN B CD  1 
ATOM   2535 O  OE1 . GLN B 1 49  ? 16.019  -25.088 19.690  1.00 24.09 ? 49  GLN B OE1 1 
ATOM   2536 N  NE2 . GLN B 1 49  ? 17.554  -26.301 18.556  1.00 28.56 ? 49  GLN B NE2 1 
ATOM   2537 N  N   . GLY B 1 50  ? 10.916  -28.327 19.210  1.00 14.45 ? 50  GLY B N   1 
ATOM   2538 C  CA  . GLY B 1 50  ? 9.768   -28.462 20.041  1.00 15.51 ? 50  GLY B CA  1 
ATOM   2539 C  C   . GLY B 1 50  ? 8.462   -28.115 19.318  1.00 15.36 ? 50  GLY B C   1 
ATOM   2540 O  O   . GLY B 1 50  ? 7.453   -27.937 19.981  1.00 14.71 ? 50  GLY B O   1 
ATOM   2541 N  N   . TYR B 1 51  ? 8.471   -28.038 17.984  1.00 13.40 ? 51  TYR B N   1 
ATOM   2542 C  CA  . TYR B 1 51  ? 7.249   -27.679 17.207  1.00 13.42 ? 51  TYR B CA  1 
ATOM   2543 C  C   . TYR B 1 51  ? 6.278   -28.860 17.116  1.00 14.28 ? 51  TYR B C   1 
ATOM   2544 O  O   . TYR B 1 51  ? 5.092   -28.678 16.823  1.00 14.39 ? 51  TYR B O   1 
ATOM   2545 C  CB  . TYR B 1 51  ? 7.652   -27.234 15.786  1.00 12.12 ? 51  TYR B CB  1 
ATOM   2546 C  CG  . TYR B 1 51  ? 7.955   -25.739 15.619  1.00 12.70 ? 51  TYR B CG  1 
ATOM   2547 C  CD1 . TYR B 1 51  ? 8.792   -25.073 16.494  1.00 13.18 ? 51  TYR B CD1 1 
ATOM   2548 C  CD2 . TYR B 1 51  ? 7.408   -25.022 14.550  1.00 12.97 ? 51  TYR B CD2 1 
ATOM   2549 C  CE1 . TYR B 1 51  ? 9.056   -23.716 16.338  1.00 12.94 ? 51  TYR B CE1 1 
ATOM   2550 C  CE2 . TYR B 1 51  ? 7.657   -23.660 14.366  1.00 12.28 ? 51  TYR B CE2 1 
ATOM   2551 C  CZ  . TYR B 1 51  ? 8.491   -23.018 15.259  1.00 13.24 ? 51  TYR B CZ  1 
ATOM   2552 O  OH  . TYR B 1 51  ? 8.691   -21.673 15.094  1.00 12.19 ? 51  TYR B OH  1 
ATOM   2553 N  N   . ASN B 1 52  ? 6.767   -30.091 17.344  1.00 14.32 ? 52  ASN B N   1 
ATOM   2554 C  CA  . ASN B 1 52  ? 5.873   -31.243 17.269  1.00 15.38 ? 52  ASN B CA  1 
ATOM   2555 C  C   . ASN B 1 52  ? 5.185   -31.370 18.654  1.00 16.18 ? 52  ASN B C   1 
ATOM   2556 O  O   . ASN B 1 52  ? 5.729   -31.984 19.630  1.00 14.50 ? 52  ASN B O   1 
ATOM   2557 C  CB  . ASN B 1 52  ? 6.668   -32.498 16.862  1.00 17.42 ? 52  ASN B CB  1 
ATOM   2558 C  CG  . ASN B 1 52  ? 5.782   -33.683 16.518  1.00 18.46 ? 52  ASN B CG  1 
ATOM   2559 O  OD1 . ASN B 1 52  ? 4.644   -33.707 16.844  1.00 19.19 ? 52  ASN B OD1 1 
ATOM   2560 N  ND2 . ASN B 1 52  ? 6.330   -34.662 15.833  1.00 22.43 ? 52  ASN B ND2 1 
ATOM   2561 N  N   . LEU B 1 53  ? 4.029   -30.695 18.783  1.00 14.05 ? 53  LEU B N   1 
ATOM   2562 C  CA  . LEU B 1 53  ? 3.311   -30.675 20.051  1.00 11.95 ? 53  LEU B CA  1 
ATOM   2563 C  C   . LEU B 1 53  ? 2.615   -31.988 20.321  1.00 12.98 ? 53  LEU B C   1 
ATOM   2564 O  O   . LEU B 1 53  ? 1.977   -32.569 19.415  1.00 11.40 ? 53  LEU B O   1 
ATOM   2565 C  CB  . LEU B 1 53  ? 2.307   -29.525 20.047  1.00 12.25 ? 53  LEU B CB  1 
ATOM   2566 C  CG  . LEU B 1 53  ? 2.842   -28.124 19.740  1.00 12.28 ? 53  LEU B CG  1 
ATOM   2567 C  CD1 . LEU B 1 53  ? 1.649   -27.139 19.748  1.00 13.37 ? 53  LEU B CD1 1 
ATOM   2568 C  CD2 . LEU B 1 53  ? 3.895   -27.593 20.707  1.00 12.48 ? 53  LEU B CD2 1 
ATOM   2569 N  N   . SER B 1 54  ? 2.711   -32.447 21.578  1.00 12.69 ? 54  SER B N   1 
ATOM   2570 C  CA  . SER B 1 54  ? 2.090   -33.715 21.971  1.00 13.35 ? 54  SER B CA  1 
ATOM   2571 C  C   . SER B 1 54  ? 0.555   -33.728 21.735  1.00 14.27 ? 54  SER B C   1 
ATOM   2572 O  O   . SER B 1 54  ? -0.176  -32.795 22.189  1.00 13.10 ? 54  SER B O   1 
ATOM   2573 C  CB  . SER B 1 54  ? 2.389   -33.979 23.471  1.00 13.48 ? 54  SER B CB  1 
ATOM   2574 O  OG  . SER B 1 54  ? 1.644   -35.093 23.971  1.00 14.05 ? 54  SER B OG  1 
ATOM   2575 N  N   . ALA B 1 55  ? 0.085   -34.791 21.056  1.00 15.12 ? 55  ALA B N   1 
ATOM   2576 C  CA  . ALA B 1 55  ? -1.367  -35.035 20.862  1.00 17.71 ? 55  ALA B CA  1 
ATOM   2577 C  C   . ALA B 1 55  ? -2.156  -35.189 22.159  1.00 17.54 ? 55  ALA B C   1 
ATOM   2578 O  O   . ALA B 1 55  ? -3.357  -34.968 22.139  1.00 18.31 ? 55  ALA B O   1 
ATOM   2579 C  CB  . ALA B 1 55  ? -1.627  -36.214 19.944  1.00 20.99 ? 55  ALA B CB  1 
ATOM   2580 N  N   . ASN B 1 56  ? -1.473  -35.510 23.283  1.00 17.25 ? 56  ASN B N   1 
ATOM   2581 C  CA  . ASN B 1 56  ? -2.119  -35.632 24.619  1.00 16.28 ? 56  ASN B CA  1 
ATOM   2582 C  C   . ASN B 1 56  ? -2.211  -34.308 25.348  1.00 16.62 ? 56  ASN B C   1 
ATOM   2583 O  O   . ASN B 1 56  ? -2.955  -34.187 26.334  1.00 14.36 ? 56  ASN B O   1 
ATOM   2584 C  CB  . ASN B 1 56  ? -1.424  -36.671 25.526  1.00 17.76 ? 56  ASN B CB  1 
ATOM   2585 C  CG  . ASN B 1 56  ? -1.744  -38.114 25.130  1.00 20.14 ? 56  ASN B CG  1 
ATOM   2586 O  OD1 . ASN B 1 56  ? -0.845  -39.003 25.156  1.00 22.90 ? 56  ASN B OD1 1 
ATOM   2587 N  ND2 . ASN B 1 56  ? -2.986  -38.354 24.687  1.00 17.95 ? 56  ASN B ND2 1 
ATOM   2588 N  N   . LYS B 1 57  ? -1.494  -33.297 24.838  1.00 15.37 ? 57  LYS B N   1 
ATOM   2589 C  CA  . LYS B 1 57  ? -1.662  -31.945 25.341  1.00 15.11 ? 57  LYS B CA  1 
ATOM   2590 C  C   . LYS B 1 57  ? -2.647  -31.183 24.484  1.00 15.24 ? 57  LYS B C   1 
ATOM   2591 O  O   . LYS B 1 57  ? -2.976  -31.603 23.358  1.00 15.01 ? 57  LYS B O   1 
ATOM   2592 C  CB  . LYS B 1 57  ? -0.301  -31.254 25.376  1.00 15.84 ? 57  LYS B CB  1 
ATOM   2593 C  CG  . LYS B 1 57  ? 0.628   -31.809 26.447  1.00 17.69 ? 57  LYS B CG  1 
ATOM   2594 C  CD  . LYS B 1 57  ? 1.969   -31.023 26.485  1.00 18.91 ? 57  LYS B CD  1 
ATOM   2595 C  CE  . LYS B 1 57  ? 3.079   -31.741 27.278  1.00 21.98 ? 57  LYS B CE  1 
ATOM   2596 N  NZ  . LYS B 1 57  ? 2.818   -31.572 28.741  1.00 21.11 ? 57  LYS B NZ  1 
ATOM   2597 N  N   . GLN B 1 58  ? -3.167  -30.089 25.020  1.00 15.36 ? 58  GLN B N   1 
ATOM   2598 C  CA  . GLN B 1 58  ? -3.998  -29.207 24.205  1.00 13.66 ? 58  GLN B CA  1 
ATOM   2599 C  C   . GLN B 1 58  ? -3.668  -27.721 24.408  1.00 13.09 ? 58  GLN B C   1 
ATOM   2600 O  O   . GLN B 1 58  ? -2.958  -27.358 25.363  1.00 11.18 ? 58  GLN B O   1 
ATOM   2601 C  CB  . GLN B 1 58  ? -5.460  -29.511 24.426  1.00 15.81 ? 58  GLN B CB  1 
ATOM   2602 C  CG  . GLN B 1 58  ? -5.999  -29.165 25.809  1.00 17.83 ? 58  GLN B CG  1 
ATOM   2603 C  CD  . GLN B 1 58  ? -7.468  -29.634 26.003  1.00 18.23 ? 58  GLN B CD  1 
ATOM   2604 O  OE1 . GLN B 1 58  ? -7.998  -29.368 27.019  1.00 20.13 ? 58  GLN B OE1 1 
ATOM   2605 N  NE2 . GLN B 1 58  ? -8.085  -30.375 25.013  1.00 19.74 ? 58  GLN B NE2 1 
ATOM   2606 N  N   . PHE B 1 59  ? -4.191  -26.883 23.506  1.00 12.01 ? 59  PHE B N   1 
ATOM   2607 C  CA  . PHE B 1 59  ? -3.638  -25.518 23.223  1.00 12.09 ? 59  PHE B CA  1 
ATOM   2608 C  C   . PHE B 1 59  ? -4.824  -24.624 22.952  1.00 11.54 ? 59  PHE B C   1 
ATOM   2609 O  O   . PHE B 1 59  ? -5.810  -25.047 22.338  1.00 11.23 ? 59  PHE B O   1 
ATOM   2610 C  CB  . PHE B 1 59  ? -2.638  -25.650 22.013  1.00 11.45 ? 59  PHE B CB  1 
ATOM   2611 C  CG  . PHE B 1 59  ? -1.490  -26.513 22.369  1.00 11.68 ? 59  PHE B CG  1 
ATOM   2612 C  CD1 . PHE B 1 59  ? -1.505  -27.871 22.117  1.00 11.69 ? 59  PHE B CD1 1 
ATOM   2613 C  CD2 . PHE B 1 59  ? -0.466  -25.979 23.158  1.00 12.01 ? 59  PHE B CD2 1 
ATOM   2614 C  CE1 . PHE B 1 59  ? -0.478  -28.705 22.587  1.00 12.59 ? 59  PHE B CE1 1 
ATOM   2615 C  CE2 . PHE B 1 59  ? 0.588   -26.821 23.628  1.00 13.31 ? 59  PHE B CE2 1 
ATOM   2616 C  CZ  . PHE B 1 59  ? 0.574   -28.184 23.321  1.00 12.20 ? 59  PHE B CZ  1 
ATOM   2617 N  N   . LEU B 1 60  ? -4.795  -23.420 23.483  1.00 12.31 ? 60  LEU B N   1 
ATOM   2618 C  CA  . LEU B 1 60  ? -6.043  -22.637 23.566  1.00 13.87 ? 60  LEU B CA  1 
ATOM   2619 C  C   . LEU B 1 60  ? -6.219  -21.819 22.265  1.00 14.49 ? 60  LEU B C   1 
ATOM   2620 O  O   . LEU B 1 60  ? -5.328  -21.033 21.891  1.00 12.62 ? 60  LEU B O   1 
ATOM   2621 C  CB  . LEU B 1 60  ? -5.989  -21.676 24.753  1.00 14.76 ? 60  LEU B CB  1 
ATOM   2622 C  CG  . LEU B 1 60  ? -7.221  -20.770 25.009  1.00 15.49 ? 60  LEU B CG  1 
ATOM   2623 C  CD1 . LEU B 1 60  ? -8.461  -21.637 25.280  1.00 13.98 ? 60  LEU B CD1 1 
ATOM   2624 C  CD2 . LEU B 1 60  ? -6.942  -19.781 26.142  1.00 17.66 ? 60  LEU B CD2 1 
ATOM   2625 N  N   . LEU B 1 61  ? -7.340  -22.023 21.569  1.00 12.43 ? 61  LEU B N   1 
ATOM   2626 C  CA  . LEU B 1 61  ? -7.665  -21.228 20.389  1.00 12.47 ? 61  LEU B CA  1 
ATOM   2627 C  C   . LEU B 1 61  ? -8.663  -20.092 20.812  1.00 12.83 ? 61  LEU B C   1 
ATOM   2628 O  O   . LEU B 1 61  ? -9.632  -20.371 21.537  1.00 12.67 ? 61  LEU B O   1 
ATOM   2629 C  CB  . LEU B 1 61  ? -8.291  -22.086 19.321  1.00 12.06 ? 61  LEU B CB  1 
ATOM   2630 C  CG  . LEU B 1 61  ? -8.500  -21.428 17.967  1.00 11.81 ? 61  LEU B CG  1 
ATOM   2631 C  CD1 . LEU B 1 61  ? -7.154  -21.489 17.220  1.00 10.95 ? 61  LEU B CD1 1 
ATOM   2632 C  CD2 . LEU B 1 61  ? -9.605  -22.153 17.196  1.00 12.76 ? 61  LEU B CD2 1 
ATOM   2633 N  N   . THR B 1 62  ? -8.373  -18.844 20.418  1.00 12.48 ? 62  THR B N   1 
ATOM   2634 C  CA  . THR B 1 62  ? -9.125  -17.638 20.891  1.00 12.90 ? 62  THR B CA  1 
ATOM   2635 C  C   . THR B 1 62  ? -9.440  -16.730 19.701  1.00 12.46 ? 62  THR B C   1 
ATOM   2636 O  O   . THR B 1 62  ? -8.570  -16.486 18.862  1.00 11.40 ? 62  THR B O   1 
ATOM   2637 C  CB  . THR B 1 62  ? -8.250  -16.788 21.862  1.00 14.73 ? 62  THR B CB  1 
ATOM   2638 O  OG1 . THR B 1 62  ? -7.991  -17.513 23.074  1.00 18.20 ? 62  THR B OG1 1 
ATOM   2639 C  CG2 . THR B 1 62  ? -8.949  -15.476 22.316  1.00 16.91 ? 62  THR B CG2 1 
ATOM   2640 N  N   . ASN B 1 63  ? -10.655 -16.184 19.652  1.00 11.98 ? 63  ASN B N   1 
ATOM   2641 C  CA  . ASN B 1 63  ? -10.984 -15.064 18.747  1.00 11.87 ? 63  ASN B CA  1 
ATOM   2642 C  C   . ASN B 1 63  ? -10.786 -13.827 19.592  1.00 12.08 ? 63  ASN B C   1 
ATOM   2643 O  O   . ASN B 1 63  ? -11.491 -13.628 20.615  1.00 12.10 ? 63  ASN B O   1 
ATOM   2644 C  CB  . ASN B 1 63  ? -12.462 -15.230 18.275  1.00 11.67 ? 63  ASN B CB  1 
ATOM   2645 C  CG  . ASN B 1 63  ? -13.010 -14.034 17.483  1.00 10.20 ? 63  ASN B CG  1 
ATOM   2646 O  OD1 . ASN B 1 63  ? -12.487 -12.902 17.497  1.00 9.60  ? 63  ASN B OD1 1 
ATOM   2647 N  ND2 . ASN B 1 63  ? -14.121 -14.310 16.767  1.00 9.50  ? 63  ASN B ND2 1 
ATOM   2648 N  N   . ASN B 1 64  ? -9.792  -12.999 19.231  1.00 11.95 ? 64  ASN B N   1 
ATOM   2649 C  CA  . ASN B 1 64  ? -9.413  -11.856 20.100  1.00 13.48 ? 64  ASN B CA  1 
ATOM   2650 C  C   . ASN B 1 64  ? -10.057 -10.562 19.525  1.00 12.59 ? 64  ASN B C   1 
ATOM   2651 O  O   . ASN B 1 64  ? -9.698  -9.436  19.869  1.00 13.22 ? 64  ASN B O   1 
ATOM   2652 C  CB  . ASN B 1 64  ? -7.873  -11.765 20.236  1.00 13.30 ? 64  ASN B CB  1 
ATOM   2653 C  CG  . ASN B 1 64  ? -7.155  -11.509 18.893  1.00 14.56 ? 64  ASN B CG  1 
ATOM   2654 O  OD1 . ASN B 1 64  ? -7.786  -11.178 17.840  1.00 13.43 ? 64  ASN B OD1 1 
ATOM   2655 N  ND2 . ASN B 1 64  ? -5.828  -11.627 18.916  1.00 14.39 ? 64  ASN B ND2 1 
ATOM   2656 N  N   . GLY B 1 65  ? -10.985 -10.759 18.575  1.00 11.57 ? 65  GLY B N   1 
ATOM   2657 C  CA  . GLY B 1 65  ? -11.674 -9.627  17.958  1.00 12.36 ? 65  GLY B CA  1 
ATOM   2658 C  C   . GLY B 1 65  ? -10.972 -9.052  16.720  1.00 11.84 ? 65  GLY B C   1 
ATOM   2659 O  O   . GLY B 1 65  ? -11.527 -8.181  16.058  1.00 12.31 ? 65  GLY B O   1 
ATOM   2660 N  N   . HIS B 1 66  ? -9.756  -9.536  16.408  1.00 12.09 ? 66  HIS B N   1 
ATOM   2661 C  CA  . HIS B 1 66  ? -8.945  -8.996  15.320  1.00 12.02 ? 66  HIS B CA  1 
ATOM   2662 C  C   . HIS B 1 66  ? -8.420  -10.061 14.437  1.00 11.15 ? 66  HIS B C   1 
ATOM   2663 O  O   . HIS B 1 66  ? -8.169  -9.818  13.240  1.00 11.14 ? 66  HIS B O   1 
ATOM   2664 C  CB  . HIS B 1 66  ? -7.777  -8.163  15.895  1.00 12.94 ? 66  HIS B CB  1 
ATOM   2665 C  CG  . HIS B 1 66  ? -8.227  -7.051  16.833  1.00 14.37 ? 66  HIS B CG  1 
ATOM   2666 N  ND1 . HIS B 1 66  ? -8.897  -5.962  16.389  1.00 14.12 ? 66  HIS B ND1 1 
ATOM   2667 C  CD2 . HIS B 1 66  ? -8.066  -6.879  18.211  1.00 14.99 ? 66  HIS B CD2 1 
ATOM   2668 C  CE1 . HIS B 1 66  ? -9.194  -5.134  17.433  1.00 15.42 ? 66  HIS B CE1 1 
ATOM   2669 N  NE2 . HIS B 1 66  ? -8.711  -5.699  18.554  1.00 16.26 ? 66  HIS B NE2 1 
ATOM   2670 N  N   . SER B 1 67  ? -8.229  -11.260 15.009  1.00 10.85 ? 67  SER B N   1 
ATOM   2671 C  CA  . SER B 1 67  ? -7.843  -12.467 14.234  1.00 10.69 ? 67  SER B CA  1 
ATOM   2672 C  C   . SER B 1 67  ? -8.271  -13.696 15.070  1.00 10.83 ? 67  SER B C   1 
ATOM   2673 O  O   . SER B 1 67  ? -8.961  -13.550 16.142  1.00 12.37 ? 67  SER B O   1 
ATOM   2674 C  CB  . SER B 1 67  ? -6.308  -12.404 14.018  1.00 11.22 ? 67  SER B CB  1 
ATOM   2675 O  OG  . SER B 1 67  ? -5.751  -13.511 13.375  1.00 10.72 ? 67  SER B OG  1 
ATOM   2676 N  N   . VAL B 1 68  ? -7.916  -14.880 14.621  1.00 11.39 ? 68  VAL B N   1 
ATOM   2677 C  CA  . VAL B 1 68  ? -8.040  -16.089 15.446  1.00 11.47 ? 68  VAL B CA  1 
ATOM   2678 C  C   . VAL B 1 68  ? -6.593  -16.448 15.836  1.00 11.45 ? 68  VAL B C   1 
ATOM   2679 O  O   . VAL B 1 68  ? -5.746  -16.581 14.942  1.00 11.01 ? 68  VAL B O   1 
ATOM   2680 C  CB  . VAL B 1 68  ? -8.782  -17.232 14.673  1.00 11.20 ? 68  VAL B CB  1 
ATOM   2681 C  CG1 . VAL B 1 68  ? -8.158  -17.505 13.296  1.00 11.38 ? 68  VAL B CG1 1 
ATOM   2682 C  CG2 . VAL B 1 68  ? -8.944  -18.524 15.531  1.00 11.88 ? 68  VAL B CG2 1 
ATOM   2683 N  N   . LYS B 1 69  ? -6.313  -16.522 17.141  1.00 12.16 ? 69  LYS B N   1 
ATOM   2684 C  CA  . LYS B 1 69  ? -4.984  -16.978 17.639  1.00 12.36 ? 69  LYS B CA  1 
ATOM   2685 C  C   . LYS B 1 69  ? -4.934  -18.380 18.256  1.00 11.88 ? 69  LYS B C   1 
ATOM   2686 O  O   . LYS B 1 69  ? -5.902  -18.816 18.816  1.00 13.13 ? 69  LYS B O   1 
ATOM   2687 C  CB  . LYS B 1 69  ? -4.342  -15.976 18.642  1.00 12.23 ? 69  LYS B CB  1 
ATOM   2688 C  CG  . LYS B 1 69  ? -5.043  -15.765 19.966  1.00 13.28 ? 69  LYS B CG  1 
ATOM   2689 C  CD  . LYS B 1 69  ? -4.206  -14.861 20.859  1.00 14.22 ? 69  LYS B CD  1 
ATOM   2690 C  CE  . LYS B 1 69  ? -4.817  -14.689 22.260  1.00 14.93 ? 69  LYS B CE  1 
ATOM   2691 N  NZ  . LYS B 1 69  ? -4.150  -13.595 23.064  1.00 14.61 ? 69  LYS B NZ  1 
ATOM   2692 N  N   A LEU B 1 70  ? -3.799  -19.071 18.106  0.50 11.90 ? 70  LEU B N   1 
ATOM   2693 N  N   B LEU B 1 70  ? -3.790  -19.068 18.155  0.50 12.46 ? 70  LEU B N   1 
ATOM   2694 C  CA  A LEU B 1 70  ? -3.500  -20.270 18.884  0.50 10.86 ? 70  LEU B CA  1 
ATOM   2695 C  CA  B LEU B 1 70  ? -3.567  -20.307 18.910  0.50 11.73 ? 70  LEU B CA  1 
ATOM   2696 C  C   A LEU B 1 70  ? -2.390  -19.870 19.889  0.50 11.07 ? 70  LEU B C   1 
ATOM   2697 C  C   B LEU B 1 70  ? -2.337  -20.147 19.828  0.50 12.05 ? 70  LEU B C   1 
ATOM   2698 O  O   A LEU B 1 70  ? -1.427  -19.185 19.530  0.50 10.14 ? 70  LEU B O   1 
ATOM   2699 O  O   B LEU B 1 70  ? -1.214  -19.926 19.330  0.50 11.83 ? 70  LEU B O   1 
ATOM   2700 C  CB  A LEU B 1 70  ? -3.105  -21.435 17.974  0.50 10.88 ? 70  LEU B CB  1 
ATOM   2701 C  CB  B LEU B 1 70  ? -3.437  -21.513 17.988  0.50 12.16 ? 70  LEU B CB  1 
ATOM   2702 C  CG  A LEU B 1 70  ? -2.846  -22.842 18.546  0.50 10.06 ? 70  LEU B CG  1 
ATOM   2703 C  CG  B LEU B 1 70  ? -3.297  -22.844 18.732  0.50 11.70 ? 70  LEU B CG  1 
ATOM   2704 C  CD1 A LEU B 1 70  ? -4.017  -23.419 19.334  0.50 9.83  ? 70  LEU B CD1 1 
ATOM   2705 C  CD1 B LEU B 1 70  ? -2.204  -22.755 19.777  0.50 12.16 ? 70  LEU B CD1 1 
ATOM   2706 C  CD2 A LEU B 1 70  ? -2.360  -23.831 17.487  0.50 9.23  ? 70  LEU B CD2 1 
ATOM   2707 C  CD2 B LEU B 1 70  ? -4.600  -23.262 19.388  0.50 11.79 ? 70  LEU B CD2 1 
ATOM   2708 N  N   . ASN B 1 71  ? -2.550  -20.251 21.148  1.00 10.83 ? 71  ASN B N   1 
ATOM   2709 C  CA  . ASN B 1 71  ? -1.428  -20.077 22.162  1.00 11.84 ? 71  ASN B CA  1 
ATOM   2710 C  C   . ASN B 1 71  ? -0.421  -21.182 21.991  1.00 12.32 ? 71  ASN B C   1 
ATOM   2711 O  O   . ASN B 1 71  ? -0.809  -22.329 21.748  1.00 11.97 ? 71  ASN B O   1 
ATOM   2712 C  CB  . ASN B 1 71  ? -1.921  -20.057 23.614  1.00 12.16 ? 71  ASN B CB  1 
ATOM   2713 C  CG  . ASN B 1 71  ? -2.601  -18.737 23.991  1.00 12.91 ? 71  ASN B CG  1 
ATOM   2714 O  OD1 . ASN B 1 71  ? -2.581  -17.789 23.238  1.00 15.02 ? 71  ASN B OD1 1 
ATOM   2715 N  ND2 . ASN B 1 71  ? -3.188  -18.682 25.181  1.00 15.44 ? 71  ASN B ND2 1 
ATOM   2716 N  N   . LEU B 1 72  ? 0.863   -20.872 22.116  1.00 11.39 ? 72  LEU B N   1 
ATOM   2717 C  CA  . LEU B 1 72  ? 1.891   -21.878 21.877  1.00 11.99 ? 72  LEU B CA  1 
ATOM   2718 C  C   . LEU B 1 72  ? 2.790   -21.891 23.085  1.00 12.30 ? 72  LEU B C   1 
ATOM   2719 O  O   . LEU B 1 72  ? 2.849   -20.837 23.794  1.00 13.66 ? 72  LEU B O   1 
ATOM   2720 C  CB  . LEU B 1 72  ? 2.721   -21.574 20.595  1.00 11.47 ? 72  LEU B CB  1 
ATOM   2721 C  CG  . LEU B 1 72  ? 1.927   -21.549 19.264  1.00 11.29 ? 72  LEU B CG  1 
ATOM   2722 C  CD1 . LEU B 1 72  ? 2.808   -21.049 18.109  1.00 11.23 ? 72  LEU B CD1 1 
ATOM   2723 C  CD2 . LEU B 1 72  ? 1.420   -22.938 18.956  1.00 11.72 ? 72  LEU B CD2 1 
ATOM   2724 N  N   . PRO B 1 73  ? 3.416   -23.068 23.370  1.00 12.52 ? 73  PRO B N   1 
ATOM   2725 C  CA  . PRO B 1 73  ? 4.164   -23.196 24.646  1.00 12.35 ? 73  PRO B CA  1 
ATOM   2726 C  C   . PRO B 1 73  ? 5.565   -22.628 24.571  1.00 11.98 ? 73  PRO B C   1 
ATOM   2727 O  O   . PRO B 1 73  ? 6.191   -22.750 23.524  1.00 12.36 ? 73  PRO B O   1 
ATOM   2728 C  CB  . PRO B 1 73  ? 4.238   -24.730 24.856  1.00 11.94 ? 73  PRO B CB  1 
ATOM   2729 C  CG  . PRO B 1 73  ? 3.956   -25.400 23.506  1.00 12.63 ? 73  PRO B CG  1 
ATOM   2730 C  CD  . PRO B 1 73  ? 3.215   -24.362 22.667  1.00 12.59 ? 73  PRO B CD  1 
ATOM   2731 N  N   . SER B 1 74  ? 6.077   -22.062 25.669  1.00 13.68 ? 74  SER B N   1 
ATOM   2732 C  CA  . SER B 1 74  ? 7.394   -21.489 25.667  1.00 13.44 ? 74  SER B CA  1 
ATOM   2733 C  C   . SER B 1 74  ? 8.523   -22.516 25.473  1.00 14.45 ? 74  SER B C   1 
ATOM   2734 O  O   . SER B 1 74  ? 9.665   -22.121 25.243  1.00 15.02 ? 74  SER B O   1 
ATOM   2735 C  CB  . SER B 1 74  ? 7.615   -20.676 26.956  1.00 15.43 ? 74  SER B CB  1 
ATOM   2736 O  OG  . SER B 1 74  ? 7.571   -21.560 28.050  1.00 15.99 ? 74  SER B OG  1 
ATOM   2737 N  N   . ASP B 1 75  ? 8.223   -23.822 25.547  1.00 15.80 ? 75  ASP B N   1 
ATOM   2738 C  CA  . ASP B 1 75  ? 9.204   -24.871 25.109  1.00 16.84 ? 75  ASP B CA  1 
ATOM   2739 C  C   . ASP B 1 75  ? 9.454   -25.010 23.576  1.00 17.36 ? 75  ASP B C   1 
ATOM   2740 O  O   . ASP B 1 75  ? 10.463  -25.621 23.143  1.00 16.46 ? 75  ASP B O   1 
ATOM   2741 C  CB  . ASP B 1 75  ? 8.931   -26.215 25.830  1.00 20.31 ? 75  ASP B CB  1 
ATOM   2742 C  CG  . ASP B 1 75  ? 7.700   -26.948 25.301  1.00 24.68 ? 75  ASP B CG  1 
ATOM   2743 O  OD1 . ASP B 1 75  ? 6.584   -26.384 25.296  1.00 28.31 ? 75  ASP B OD1 1 
ATOM   2744 O  OD2 . ASP B 1 75  ? 7.829   -28.121 24.904  1.00 29.49 ? 75  ASP B OD2 1 
ATOM   2745 N  N   . MET B 1 76  ? 8.544   -24.499 22.733  1.00 15.59 ? 76  MET B N   1 
ATOM   2746 C  CA  . MET B 1 76  ? 8.849   -24.276 21.320  1.00 15.30 ? 76  MET B CA  1 
ATOM   2747 C  C   . MET B 1 76  ? 9.829   -23.131 21.116  1.00 15.01 ? 76  MET B C   1 
ATOM   2748 O  O   . MET B 1 76  ? 9.589   -22.028 21.578  1.00 14.41 ? 76  MET B O   1 
ATOM   2749 C  CB  . MET B 1 76  ? 7.597   -23.854 20.531  1.00 16.73 ? 76  MET B CB  1 
ATOM   2750 C  CG  . MET B 1 76  ? 6.926   -24.915 19.721  1.00 19.43 ? 76  MET B CG  1 
ATOM   2751 S  SD  . MET B 1 76  ? 5.353   -24.272 19.032  1.00 18.13 ? 76  MET B SD  1 
ATOM   2752 C  CE  . MET B 1 76  ? 5.859   -23.379 17.577  1.00 16.72 ? 76  MET B CE  1 
ATOM   2753 N  N   . HIS B 1 77  ? 10.909  -23.397 20.405  1.00 16.51 ? 77  HIS B N   1 
ATOM   2754 C  CA  . HIS B 1 77  ? 11.995  -22.413 20.175  1.00 16.12 ? 77  HIS B CA  1 
ATOM   2755 C  C   . HIS B 1 77  ? 12.449  -22.364 18.724  1.00 16.90 ? 77  HIS B C   1 
ATOM   2756 O  O   . HIS B 1 77  ? 12.282  -23.322 17.969  1.00 15.68 ? 77  HIS B O   1 
ATOM   2757 C  CB  . HIS B 1 77  ? 13.275  -22.754 20.953  1.00 19.57 ? 77  HIS B CB  1 
ATOM   2758 C  CG  . HIS B 1 77  ? 13.074  -23.286 22.330  1.00 21.10 ? 77  HIS B CG  1 
ATOM   2759 N  ND1 . HIS B 1 77  ? 12.489  -22.562 23.315  1.00 22.74 ? 77  HIS B ND1 1 
ATOM   2760 C  CD2 . HIS B 1 77  ? 13.488  -24.478 22.911  1.00 21.77 ? 77  HIS B CD2 1 
ATOM   2761 C  CE1 . HIS B 1 77  ? 12.489  -23.269 24.455  1.00 19.23 ? 77  HIS B CE1 1 
ATOM   2762 N  NE2 . HIS B 1 77  ? 13.103  -24.437 24.210  1.00 22.49 ? 77  HIS B NE2 1 
ATOM   2763 N  N   . ILE B 1 78  ? 13.073  -21.257 18.325  1.00 15.85 ? 78  ILE B N   1 
ATOM   2764 C  CA  . ILE B 1 78  ? 13.790  -21.254 17.055  1.00 16.95 ? 78  ILE B CA  1 
ATOM   2765 C  C   . ILE B 1 78  ? 15.271  -21.062 17.336  1.00 17.20 ? 78  ILE B C   1 
ATOM   2766 O  O   . ILE B 1 78  ? 15.645  -20.269 18.228  1.00 16.61 ? 78  ILE B O   1 
ATOM   2767 C  CB  . ILE B 1 78  ? 13.275  -20.205 16.035  1.00 19.20 ? 78  ILE B CB  1 
ATOM   2768 C  CG1 . ILE B 1 78  ? 13.206  -18.802 16.632  1.00 18.59 ? 78  ILE B CG1 1 
ATOM   2769 C  CG2 . ILE B 1 78  ? 11.930  -20.617 15.481  1.00 19.35 ? 78  ILE B CG2 1 
ATOM   2770 C  CD1 . ILE B 1 78  ? 12.312  -17.840 15.823  1.00 20.20 ? 78  ILE B CD1 1 
ATOM   2771 N  N   . GLN B 1 79  ? 16.086  -21.809 16.609  1.00 18.72 ? 79  GLN B N   1 
ATOM   2772 C  CA  . GLN B 1 79  ? 17.515  -21.579 16.645  1.00 22.36 ? 79  GLN B CA  1 
ATOM   2773 C  C   . GLN B 1 79  ? 18.012  -21.002 15.317  1.00 20.93 ? 79  GLN B C   1 
ATOM   2774 O  O   . GLN B 1 79  ? 17.449  -21.262 14.268  1.00 19.69 ? 79  GLN B O   1 
ATOM   2775 C  CB  . GLN B 1 79  ? 18.224  -22.870 16.962  1.00 27.98 ? 79  GLN B CB  1 
ATOM   2776 C  CG  . GLN B 1 79  ? 19.728  -22.718 16.977  1.00 31.52 ? 79  GLN B CG  1 
ATOM   2777 C  CD  . GLN B 1 79  ? 20.375  -24.047 17.169  1.00 34.15 ? 79  GLN B CD  1 
ATOM   2778 O  OE1 . GLN B 1 79  ? 20.155  -24.683 18.196  1.00 33.84 ? 79  GLN B OE1 1 
ATOM   2779 N  NE2 . GLN B 1 79  ? 21.112  -24.515 16.161  1.00 34.02 ? 79  GLN B NE2 1 
ATOM   2780 N  N   . GLY B 1 80  ? 19.058  -20.187 15.389  1.00 21.64 ? 80  GLY B N   1 
ATOM   2781 C  CA  . GLY B 1 80  ? 19.617  -19.621 14.176  1.00 22.93 ? 80  GLY B CA  1 
ATOM   2782 C  C   . GLY B 1 80  ? 19.590  -18.114 14.178  1.00 22.26 ? 80  GLY B C   1 
ATOM   2783 O  O   . GLY B 1 80  ? 20.126  -17.487 13.223  1.00 24.43 ? 80  GLY B O   1 
ATOM   2784 N  N   . LEU B 1 81  ? 18.980  -17.529 15.223  1.00 18.22 ? 81  LEU B N   1 
ATOM   2785 C  CA  . LEU B 1 81  ? 19.083  -16.088 15.469  1.00 18.96 ? 81  LEU B CA  1 
ATOM   2786 C  C   . LEU B 1 81  ? 20.104  -15.892 16.588  1.00 18.89 ? 81  LEU B C   1 
ATOM   2787 O  O   . LEU B 1 81  ? 20.535  -16.868 17.234  1.00 17.98 ? 81  LEU B O   1 
ATOM   2788 C  CB  . LEU B 1 81  ? 17.731  -15.500 15.906  1.00 16.39 ? 81  LEU B CB  1 
ATOM   2789 C  CG  . LEU B 1 81  ? 16.622  -15.645 14.863  1.00 17.16 ? 81  LEU B CG  1 
ATOM   2790 C  CD1 . LEU B 1 81  ? 15.359  -15.053 15.476  1.00 17.77 ? 81  LEU B CD1 1 
ATOM   2791 C  CD2 . LEU B 1 81  ? 16.968  -14.986 13.543  1.00 18.42 ? 81  LEU B CD2 1 
ATOM   2792 N  N   . GLN B 1 82  ? 20.469  -14.654 16.855  1.00 19.75 ? 82  GLN B N   1 
ATOM   2793 C  CA  . GLN B 1 82  ? 21.539  -14.466 17.841  1.00 20.16 ? 82  GLN B CA  1 
ATOM   2794 C  C   . GLN B 1 82  ? 21.173  -14.879 19.267  1.00 23.39 ? 82  GLN B C   1 
ATOM   2795 O  O   . GLN B 1 82  ? 22.025  -15.458 19.954  1.00 24.41 ? 82  GLN B O   1 
ATOM   2796 C  CB  . GLN B 1 82  ? 22.162  -13.078 17.765  1.00 20.46 ? 82  GLN B CB  1 
ATOM   2797 C  CG  . GLN B 1 82  ? 21.214  -11.920 17.837  1.00 23.26 ? 82  GLN B CG  1 
ATOM   2798 C  CD  . GLN B 1 82  ? 21.923  -10.614 17.617  1.00 26.27 ? 82  GLN B CD  1 
ATOM   2799 O  OE1 . GLN B 1 82  ? 22.777  -10.481 16.713  1.00 29.05 ? 82  GLN B OE1 1 
ATOM   2800 N  NE2 . GLN B 1 82  ? 21.599  -9.630  18.445  1.00 27.68 ? 82  GLN B NE2 1 
ATOM   2801 N  N   . SER B 1 83  ? 19.922  -14.592 19.699  1.00 21.62 ? 83  SER B N   1 
ATOM   2802 C  CA  . SER B 1 83  ? 19.398  -15.014 20.996  1.00 20.26 ? 83  SER B CA  1 
ATOM   2803 C  C   . SER B 1 83  ? 18.432  -16.144 20.716  1.00 20.44 ? 83  SER B C   1 
ATOM   2804 O  O   . SER B 1 83  ? 17.880  -16.237 19.589  1.00 19.37 ? 83  SER B O   1 
ATOM   2805 C  CB  . SER B 1 83  ? 18.617  -13.895 21.730  1.00 20.00 ? 83  SER B CB  1 
ATOM   2806 O  OG  . SER B 1 83  ? 19.280  -12.629 21.737  1.00 21.14 ? 83  SER B OG  1 
ATOM   2807 N  N   . ARG B 1 84  ? 18.167  -16.978 21.725  1.00 19.54 ? 84  ARG B N   1 
ATOM   2808 C  CA  . ARG B 1 84  ? 17.021  -17.936 21.576  1.00 18.23 ? 84  ARG B CA  1 
ATOM   2809 C  C   . ARG B 1 84  ? 15.687  -17.184 21.725  1.00 15.97 ? 84  ARG B C   1 
ATOM   2810 O  O   . ARG B 1 84  ? 15.565  -16.261 22.532  1.00 18.06 ? 84  ARG B O   1 
ATOM   2811 C  CB  . ARG B 1 84  ? 17.117  -19.103 22.542  1.00 20.54 ? 84  ARG B CB  1 
ATOM   2812 C  CG  . ARG B 1 84  ? 16.412  -20.346 21.994  1.00 22.62 ? 84  ARG B CG  1 
ATOM   2813 C  CD  . ARG B 1 84  ? 16.847  -21.576 22.783  1.00 24.29 ? 84  ARG B CD  1 
ATOM   2814 N  NE  . ARG B 1 84  ? 16.400  -21.525 24.177  1.00 26.60 ? 84  ARG B NE  1 
ATOM   2815 C  CZ  . ARG B 1 84  ? 16.447  -22.581 24.989  1.00 29.12 ? 84  ARG B CZ  1 
ATOM   2816 N  NH1 . ARG B 1 84  ? 16.944  -23.724 24.530  1.00 27.14 ? 84  ARG B NH1 1 
ATOM   2817 N  NH2 . ARG B 1 84  ? 16.009  -22.492 26.238  1.00 25.56 ? 84  ARG B NH2 1 
ATOM   2818 N  N   . TYR B 1 85  ? 14.717  -17.513 20.851  1.00 15.05 ? 85  TYR B N   1 
ATOM   2819 C  CA  . TYR B 1 85  ? 13.379  -16.935 20.852  1.00 14.09 ? 85  TYR B CA  1 
ATOM   2820 C  C   . TYR B 1 85  ? 12.398  -18.120 21.079  1.00 12.88 ? 85  TYR B C   1 
ATOM   2821 O  O   . TYR B 1 85  ? 12.574  -19.156 20.470  1.00 14.55 ? 85  TYR B O   1 
ATOM   2822 C  CB  . TYR B 1 85  ? 13.071  -16.240 19.487  1.00 14.06 ? 85  TYR B CB  1 
ATOM   2823 C  CG  . TYR B 1 85  ? 13.704  -14.858 19.315  1.00 13.76 ? 85  TYR B CG  1 
ATOM   2824 C  CD1 . TYR B 1 85  ? 15.024  -14.717 18.867  1.00 13.56 ? 85  TYR B CD1 1 
ATOM   2825 C  CD2 . TYR B 1 85  ? 13.026  -13.713 19.697  1.00 13.12 ? 85  TYR B CD2 1 
ATOM   2826 C  CE1 . TYR B 1 85  ? 15.625  -13.442 18.768  1.00 13.56 ? 85  TYR B CE1 1 
ATOM   2827 C  CE2 . TYR B 1 85  ? 13.618  -12.419 19.562  1.00 13.06 ? 85  TYR B CE2 1 
ATOM   2828 C  CZ  . TYR B 1 85  ? 14.919  -12.309 19.061  1.00 14.07 ? 85  TYR B CZ  1 
ATOM   2829 O  OH  . TYR B 1 85  ? 15.533  -11.065 18.963  1.00 14.36 ? 85  TYR B OH  1 
ATOM   2830 N  N   . SER B 1 86  ? 11.457  -17.982 22.019  1.00 13.04 ? 86  SER B N   1 
ATOM   2831 C  CA  . SER B 1 86  ? 10.508  -19.061 22.327  1.00 13.14 ? 86  SER B CA  1 
ATOM   2832 C  C   . SER B 1 86  ? 9.132   -18.660 21.834  1.00 12.45 ? 86  SER B C   1 
ATOM   2833 O  O   . SER B 1 86  ? 8.791   -17.491 21.872  1.00 12.42 ? 86  SER B O   1 
ATOM   2834 C  CB  . SER B 1 86  ? 10.401  -19.278 23.844  1.00 15.25 ? 86  SER B CB  1 
ATOM   2835 O  OG  . SER B 1 86  ? 11.656  -19.744 24.398  1.00 17.23 ? 86  SER B OG  1 
ATOM   2836 N  N   . ALA B 1 87  ? 8.326   -19.638 21.483  1.00 11.97 ? 87  ALA B N   1 
ATOM   2837 C  CA  . ALA B 1 87  ? 7.014   -19.299 20.908  1.00 12.85 ? 87  ALA B CA  1 
ATOM   2838 C  C   . ALA B 1 87  ? 6.019   -18.700 21.939  1.00 13.68 ? 87  ALA B C   1 
ATOM   2839 O  O   . ALA B 1 87  ? 6.096   -18.957 23.185  1.00 12.52 ? 87  ALA B O   1 
ATOM   2840 C  CB  . ALA B 1 87  ? 6.429   -20.541 20.248  1.00 13.94 ? 87  ALA B CB  1 
ATOM   2841 N  N   . THR B 1 88  ? 5.063   -17.910 21.410  1.00 13.33 ? 88  THR B N   1 
ATOM   2842 C  CA  . THR B 1 88  ? 3.936   -17.423 22.234  1.00 11.53 ? 88  THR B CA  1 
ATOM   2843 C  C   . THR B 1 88  ? 2.538   -17.690 21.617  1.00 12.63 ? 88  THR B C   1 
ATOM   2844 O  O   . THR B 1 88  ? 1.605   -18.080 22.347  1.00 11.60 ? 88  THR B O   1 
ATOM   2845 C  CB  . THR B 1 88  ? 4.150   -15.950 22.636  1.00 12.59 ? 88  THR B CB  1 
ATOM   2846 O  OG1 . THR B 1 88  ? 3.062   -15.467 23.417  1.00 12.47 ? 88  THR B OG1 1 
ATOM   2847 C  CG2 . THR B 1 88  ? 4.344   -14.946 21.433  1.00 11.47 ? 88  THR B CG2 1 
ATOM   2848 N  N   . GLN B 1 89  ? 2.371   -17.402 20.321  1.00 10.75 ? 89  GLN B N   1 
ATOM   2849 C  CA  . GLN B 1 89  ? 1.103   -17.660 19.650  1.00 11.58 ? 89  GLN B CA  1 
ATOM   2850 C  C   . GLN B 1 89  ? 1.308   -17.707 18.142  1.00 10.85 ? 89  GLN B C   1 
ATOM   2851 O  O   . GLN B 1 89  ? 2.328   -17.217 17.607  1.00 11.44 ? 89  GLN B O   1 
ATOM   2852 C  CB  . GLN B 1 89  ? 0.102   -16.542 20.013  1.00 12.99 ? 89  GLN B CB  1 
ATOM   2853 C  CG  . GLN B 1 89  ? 0.578   -15.149 19.604  1.00 16.08 ? 89  GLN B CG  1 
ATOM   2854 C  CD  . GLN B 1 89  ? -0.291  -14.619 18.493  1.00 17.90 ? 89  GLN B CD  1 
ATOM   2855 O  OE1 . GLN B 1 89  ? -0.200  -15.072 17.355  1.00 23.21 ? 89  GLN B OE1 1 
ATOM   2856 N  NE2 . GLN B 1 89  ? -1.169  -13.710 18.813  1.00 17.36 ? 89  GLN B NE2 1 
ATOM   2857 N  N   . LEU B 1 90  ? 0.314   -18.227 17.438  1.00 10.23 ? 90  LEU B N   1 
ATOM   2858 C  CA  . LEU B 1 90  ? 0.210   -18.063 16.002  1.00 10.94 ? 90  LEU B CA  1 
ATOM   2859 C  C   . LEU B 1 90  ? -1.207  -17.533 15.602  1.00 11.03 ? 90  LEU B C   1 
ATOM   2860 O  O   . LEU B 1 90  ? -2.187  -17.665 16.386  1.00 9.79  ? 90  LEU B O   1 
ATOM   2861 C  CB  . LEU B 1 90  ? 0.654   -19.335 15.195  1.00 11.27 ? 90  LEU B CB  1 
ATOM   2862 C  CG  . LEU B 1 90  ? -0.127  -20.679 15.344  1.00 11.84 ? 90  LEU B CG  1 
ATOM   2863 C  CD1 . LEU B 1 90  ? -1.581  -20.617 14.756  1.00 12.19 ? 90  LEU B CD1 1 
ATOM   2864 C  CD2 . LEU B 1 90  ? 0.684   -21.799 14.742  1.00 11.06 ? 90  LEU B CD2 1 
ATOM   2865 N  N   . HIS B 1 91  ? -1.276  -16.855 14.454  1.00 10.62 ? 91  HIS B N   1 
ATOM   2866 C  CA  . HIS B 1 91  ? -2.550  -16.265 13.990  1.00 10.74 ? 91  HIS B CA  1 
ATOM   2867 C  C   . HIS B 1 91  ? -2.519  -16.022 12.507  1.00 10.93 ? 91  HIS B C   1 
ATOM   2868 O  O   . HIS B 1 91  ? -1.461  -16.212 11.876  1.00 11.31 ? 91  HIS B O   1 
ATOM   2869 C  CB  . HIS B 1 91  ? -2.849  -14.971 14.761  1.00 10.09 ? 91  HIS B CB  1 
ATOM   2870 C  CG  . HIS B 1 91  ? -1.824  -13.908 14.530  1.00 10.37 ? 91  HIS B CG  1 
ATOM   2871 N  ND1 . HIS B 1 91  ? -0.785  -13.691 15.401  1.00 10.95 ? 91  HIS B ND1 1 
ATOM   2872 C  CD2 . HIS B 1 91  ? -1.634  -13.031 13.447  1.00 10.74 ? 91  HIS B CD2 1 
ATOM   2873 C  CE1 . HIS B 1 91  ? -0.028  -12.665 14.943  1.00 10.60 ? 91  HIS B CE1 1 
ATOM   2874 N  NE2 . HIS B 1 91  ? -0.541  -12.261 13.732  1.00 10.48 ? 91  HIS B NE2 1 
ATOM   2875 N  N   . LEU B 1 92  ? -3.680  -15.688 11.915  1.00 10.12 ? 92  LEU B N   1 
ATOM   2876 C  CA  . LEU B 1 92  ? -3.787  -15.454 10.469  1.00 10.58 ? 92  LEU B CA  1 
ATOM   2877 C  C   . LEU B 1 92  ? -4.315  -14.050 10.055  1.00 9.33  ? 92  LEU B C   1 
ATOM   2878 O  O   . LEU B 1 92  ? -5.006  -13.388 10.805  1.00 9.53  ? 92  LEU B O   1 
ATOM   2879 C  CB  . LEU B 1 92  ? -4.676  -16.507 9.808   1.00 11.40 ? 92  LEU B CB  1 
ATOM   2880 C  CG  . LEU B 1 92  ? -3.996  -17.848 10.031  1.00 13.24 ? 92  LEU B CG  1 
ATOM   2881 C  CD1 . LEU B 1 92  ? -4.889  -18.629 10.984  1.00 13.88 ? 92  LEU B CD1 1 
ATOM   2882 C  CD2 . LEU B 1 92  ? -3.746  -18.596 8.745   1.00 13.49 ? 92  LEU B CD2 1 
ATOM   2883 N  N   . HIS B 1 93  ? -3.986  -13.638 8.850   1.00 9.52  ? 93  HIS B N   1 
ATOM   2884 C  CA  . HIS B 1 93  ? -4.590  -12.467 8.193   1.00 9.83  ? 93  HIS B CA  1 
ATOM   2885 C  C   . HIS B 1 93  ? -5.170  -12.910 6.866   1.00 9.56  ? 93  HIS B C   1 
ATOM   2886 O  O   . HIS B 1 93  ? -4.592  -13.784 6.191   1.00 9.19  ? 93  HIS B O   1 
ATOM   2887 C  CB  . HIS B 1 93  ? -3.515  -11.409 7.965   1.00 9.83  ? 93  HIS B CB  1 
ATOM   2888 C  CG  . HIS B 1 93  ? -2.863  -10.994 9.253   1.00 8.57  ? 93  HIS B CG  1 
ATOM   2889 N  ND1 . HIS B 1 93  ? -3.346  -9.979  10.019  1.00 8.98  ? 93  HIS B ND1 1 
ATOM   2890 C  CD2 . HIS B 1 93  ? -1.735  -11.468 9.902   1.00 9.52  ? 93  HIS B CD2 1 
ATOM   2891 C  CE1 . HIS B 1 93  ? -2.547  -9.849  11.097  1.00 8.25  ? 93  HIS B CE1 1 
ATOM   2892 N  NE2 . HIS B 1 93  ? -1.625  -10.789 11.054  1.00 8.23  ? 93  HIS B NE2 1 
ATOM   2893 N  N   . TRP B 1 94  ? -6.297  -12.336 6.504   1.00 9.65  ? 94  TRP B N   1 
ATOM   2894 C  CA  . TRP B 1 94  ? -6.947  -12.722 5.214   1.00 9.71  ? 94  TRP B CA  1 
ATOM   2895 C  C   . TRP B 1 94  ? -7.762  -11.638 4.579   1.00 9.71  ? 94  TRP B C   1 
ATOM   2896 O  O   . TRP B 1 94  ? -7.959  -10.592 5.154   1.00 9.56  ? 94  TRP B O   1 
ATOM   2897 C  CB  . TRP B 1 94  ? -7.814  -14.027 5.412   1.00 10.02 ? 94  TRP B CB  1 
ATOM   2898 C  CG  . TRP B 1 94  ? -8.874  -13.881 6.476   1.00 9.75  ? 94  TRP B CG  1 
ATOM   2899 C  CD1 . TRP B 1 94  ? -10.175 -13.418 6.299   1.00 9.84  ? 94  TRP B CD1 1 
ATOM   2900 C  CD2 . TRP B 1 94  ? -8.736  -14.148 7.927   1.00 10.21 ? 94  TRP B CD2 1 
ATOM   2901 N  NE1 . TRP B 1 94  ? -10.848 -13.332 7.524   1.00 10.85 ? 94  TRP B NE1 1 
ATOM   2902 C  CE2 . TRP B 1 94  ? -10.032 -13.800 8.533   1.00 9.75  ? 94  TRP B CE2 1 
ATOM   2903 C  CE3 . TRP B 1 94  ? -7.696  -14.662 8.765   1.00 8.83  ? 94  TRP B CE3 1 
ATOM   2904 C  CZ2 . TRP B 1 94  ? -10.286 -13.980 9.890   1.00 9.57  ? 94  TRP B CZ2 1 
ATOM   2905 C  CZ3 . TRP B 1 94  ? -7.955  -14.798 10.144  1.00 9.33  ? 94  TRP B CZ3 1 
ATOM   2906 C  CH2 . TRP B 1 94  ? -9.225  -14.504 10.696  1.00 9.12  ? 94  TRP B CH2 1 
ATOM   2907 N  N   . GLY B 1 95  ? -8.340  -11.903 3.398   1.00 9.86  ? 95  GLY B N   1 
ATOM   2908 C  CA  . GLY B 1 95  ? -9.083  -10.864 2.664   1.00 10.06 ? 95  GLY B CA  1 
ATOM   2909 C  C   . GLY B 1 95  ? -10.601 -11.041 2.761   1.00 9.74  ? 95  GLY B C   1 
ATOM   2910 O  O   . GLY B 1 95  ? -11.202 -11.064 3.855   1.00 9.40  ? 95  GLY B O   1 
ATOM   2911 N  N   . ASN B 1 96  ? -11.242 -11.187 1.602   1.00 10.72 ? 96  ASN B N   1 
ATOM   2912 C  CA  . ASN B 1 96  ? -12.708 -11.403 1.604   1.00 11.30 ? 96  ASN B CA  1 
ATOM   2913 C  C   . ASN B 1 96  ? -13.114 -12.180 0.361   1.00 11.92 ? 96  ASN B C   1 
ATOM   2914 O  O   . ASN B 1 96  ? -12.344 -12.248 -0.561  1.00 13.26 ? 96  ASN B O   1 
ATOM   2915 C  CB  . ASN B 1 96  ? -13.482 -10.047 1.653   1.00 12.08 ? 96  ASN B CB  1 
ATOM   2916 C  CG  . ASN B 1 96  ? -13.437 -9.294  0.347   1.00 12.53 ? 96  ASN B CG  1 
ATOM   2917 O  OD1 . ASN B 1 96  ? -14.281 -9.480  -0.578  1.00 13.60 ? 96  ASN B OD1 1 
ATOM   2918 N  ND2 . ASN B 1 96  ? -12.490 -8.395  0.267   1.00 12.74 ? 96  ASN B ND2 1 
ATOM   2919 N  N   . PRO B 1 97  ? -14.308 -12.796 0.354   1.00 13.11 ? 97  PRO B N   1 
ATOM   2920 C  CA  . PRO B 1 97  ? -14.670 -13.699 -0.765  1.00 14.15 ? 97  PRO B CA  1 
ATOM   2921 C  C   . PRO B 1 97  ? -14.687 -13.021 -2.147  1.00 16.00 ? 97  PRO B C   1 
ATOM   2922 O  O   . PRO B 1 97  ? -14.358 -13.653 -3.153  1.00 16.99 ? 97  PRO B O   1 
ATOM   2923 C  CB  . PRO B 1 97  ? -16.074 -14.182 -0.368  1.00 15.32 ? 97  PRO B CB  1 
ATOM   2924 C  CG  . PRO B 1 97  ? -16.007 -14.145 1.150   1.00 15.81 ? 97  PRO B CG  1 
ATOM   2925 C  CD  . PRO B 1 97  ? -15.345 -12.782 1.391   1.00 13.53 ? 97  PRO B CD  1 
ATOM   2926 N  N   . ASN B 1 98  ? -15.045 -11.738 -2.213  1.00 16.60 ? 98  ASN B N   1 
ATOM   2927 C  CA  . ASN B 1 98  ? -14.987 -11.028 -3.505  1.00 19.68 ? 98  ASN B CA  1 
ATOM   2928 C  C   . ASN B 1 98  ? -13.600 -10.576 -3.949  1.00 19.95 ? 98  ASN B C   1 
ATOM   2929 O  O   . ASN B 1 98  ? -13.432 -10.131 -5.100  1.00 21.88 ? 98  ASN B O   1 
ATOM   2930 C  CB  . ASN B 1 98  ? -15.941 -9.843  -3.418  1.00 22.28 ? 98  ASN B CB  1 
ATOM   2931 C  CG  . ASN B 1 98  ? -17.411 -10.305 -3.468  1.00 25.88 ? 98  ASN B CG  1 
ATOM   2932 O  OD1 . ASN B 1 98  ? -17.717 -11.384 -4.030  1.00 26.79 ? 98  ASN B OD1 1 
ATOM   2933 N  ND2 . ASN B 1 98  ? -18.298 -9.512  -2.928  1.00 26.36 ? 98  ASN B ND2 1 
ATOM   2934 N  N   . ASP B 1 99  ? -12.640 -10.634 -3.015  1.00 17.76 ? 99  ASP B N   1 
ATOM   2935 C  CA  . ASP B 1 99  ? -11.248 -10.209 -3.237  1.00 17.26 ? 99  ASP B CA  1 
ATOM   2936 C  C   . ASP B 1 99  ? -10.310 -10.976 -2.286  1.00 16.15 ? 99  ASP B C   1 
ATOM   2937 O  O   . ASP B 1 99  ? -9.898  -10.428 -1.216  1.00 15.31 ? 99  ASP B O   1 
ATOM   2938 C  CB  . ASP B 1 99  ? -11.103 -8.689  -3.040  1.00 17.87 ? 99  ASP B CB  1 
ATOM   2939 C  CG  . ASP B 1 99  ? -9.874  -8.118  -3.768  1.00 17.72 ? 99  ASP B CG  1 
ATOM   2940 O  OD1 . ASP B 1 99  ? -9.094  -8.880  -4.391  1.00 18.14 ? 99  ASP B OD1 1 
ATOM   2941 O  OD2 . ASP B 1 99  ? -9.710  -6.892  -3.748  1.00 19.20 ? 99  ASP B OD2 1 
ATOM   2942 N  N   . PRO B 1 100 ? -10.026 -12.258 -2.615  1.00 14.72 ? 100 PRO B N   1 
ATOM   2943 C  CA  . PRO B 1 100 ? -9.380  -13.188 -1.676  1.00 13.61 ? 100 PRO B CA  1 
ATOM   2944 C  C   . PRO B 1 100 ? -7.886  -13.066 -1.789  1.00 13.59 ? 100 PRO B C   1 
ATOM   2945 O  O   . PRO B 1 100 ? -7.201  -13.998 -2.211  1.00 13.24 ? 100 PRO B O   1 
ATOM   2946 C  CB  . PRO B 1 100 ? -9.934  -14.553 -2.134  1.00 13.57 ? 100 PRO B CB  1 
ATOM   2947 C  CG  . PRO B 1 100 ? -10.166 -14.380 -3.571  1.00 14.33 ? 100 PRO B CG  1 
ATOM   2948 C  CD  . PRO B 1 100 ? -10.551 -12.974 -3.797  1.00 14.42 ? 100 PRO B CD  1 
ATOM   2949 N  N   . HIS B 1 101 ? -7.423  -11.850 -1.508  1.00 13.63 ? 101 HIS B N   1 
ATOM   2950 C  CA  . HIS B 1 101 ? -6.030  -11.502 -1.621  1.00 15.43 ? 101 HIS B CA  1 
ATOM   2951 C  C   . HIS B 1 101 ? -5.641  -10.694 -0.414  1.00 15.46 ? 101 HIS B C   1 
ATOM   2952 O  O   . HIS B 1 101 ? -5.394  -9.483  -0.535  1.00 17.69 ? 101 HIS B O   1 
ATOM   2953 C  CB  . HIS B 1 101 ? -5.757  -10.750 -2.968  1.00 16.76 ? 101 HIS B CB  1 
ATOM   2954 C  CG  . HIS B 1 101 ? -6.250  -11.515 -4.176  1.00 18.00 ? 101 HIS B CG  1 
ATOM   2955 N  ND1 . HIS B 1 101 ? -5.523  -12.534 -4.754  1.00 18.52 ? 101 HIS B ND1 1 
ATOM   2956 C  CD2 . HIS B 1 101 ? -7.410  -11.450 -4.877  1.00 17.47 ? 101 HIS B CD2 1 
ATOM   2957 C  CE1 . HIS B 1 101 ? -6.197  -13.057 -5.767  1.00 17.88 ? 101 HIS B CE1 1 
ATOM   2958 N  NE2 . HIS B 1 101 ? -7.347  -12.415 -5.866  1.00 17.99 ? 101 HIS B NE2 1 
ATOM   2959 N  N   . GLY B 1 102 ? -5.591  -11.342 0.760   1.00 13.23 ? 102 GLY B N   1 
ATOM   2960 C  CA  . GLY B 1 102 ? -5.373  -10.620 2.021   1.00 11.10 ? 102 GLY B CA  1 
ATOM   2961 C  C   . GLY B 1 102 ? -4.125  -10.914 2.837   1.00 10.29 ? 102 GLY B C   1 
ATOM   2962 O  O   . GLY B 1 102 ? -4.164  -10.787 4.063   1.00 10.76 ? 102 GLY B O   1 
ATOM   2963 N  N   . SER B 1 103 ? -3.027  -11.323 2.200   1.00 9.33  ? 103 SER B N   1 
ATOM   2964 C  CA  . SER B 1 103 ? -1.734  -11.381 2.906   1.00 9.54  ? 103 SER B CA  1 
ATOM   2965 C  C   . SER B 1 103 ? -1.358  -9.935  3.304   1.00 9.23  ? 103 SER B C   1 
ATOM   2966 O  O   . SER B 1 103 ? -1.883  -8.976  2.768   1.00 10.16 ? 103 SER B O   1 
ATOM   2967 C  CB  . SER B 1 103 ? -0.642  -11.977 1.997   1.00 9.63  ? 103 SER B CB  1 
ATOM   2968 O  OG  . SER B 1 103 ? -0.310  -11.139 0.859   1.00 10.79 ? 103 SER B OG  1 
ATOM   2969 N  N   . GLU B 1 104 ? -0.479  -9.813  4.260   1.00 9.03  ? 104 GLU B N   1 
ATOM   2970 C  CA  . GLU B 1 104 ? 0.103   -8.522  4.701   1.00 9.37  ? 104 GLU B CA  1 
ATOM   2971 C  C   . GLU B 1 104 ? 1.303   -8.141  3.836   1.00 8.99  ? 104 GLU B C   1 
ATOM   2972 O  O   . GLU B 1 104 ? 1.297   -7.110  3.170   1.00 8.90  ? 104 GLU B O   1 
ATOM   2973 C  CB  . GLU B 1 104 ? 0.491   -8.665  6.194   1.00 9.40  ? 104 GLU B CB  1 
ATOM   2974 C  CG  . GLU B 1 104 ? -0.663  -9.070  7.131   1.00 9.57  ? 104 GLU B CG  1 
ATOM   2975 C  CD  . GLU B 1 104 ? -0.734  -8.238  8.375   1.00 9.73  ? 104 GLU B CD  1 
ATOM   2976 O  OE1 . GLU B 1 104 ? -0.015  -8.511  9.366   1.00 11.32 ? 104 GLU B OE1 1 
ATOM   2977 O  OE2 . GLU B 1 104 ? -1.475  -7.235  8.402   1.00 9.89  ? 104 GLU B OE2 1 
ATOM   2978 N  N   . HIS B 1 105 ? 2.356   -8.977  3.832   1.00 9.56  ? 105 HIS B N   1 
ATOM   2979 C  CA  . HIS B 1 105 ? 3.508   -8.768  2.916   1.00 9.04  ? 105 HIS B CA  1 
ATOM   2980 C  C   . HIS B 1 105 ? 3.100   -9.078  1.489   1.00 9.66  ? 105 HIS B C   1 
ATOM   2981 O  O   . HIS B 1 105 ? 2.201   -9.947  1.266   1.00 9.40  ? 105 HIS B O   1 
ATOM   2982 C  CB  . HIS B 1 105 ? 4.684   -9.628  3.326   1.00 9.00  ? 105 HIS B CB  1 
ATOM   2983 C  CG  . HIS B 1 105 ? 5.308   -9.191  4.621   1.00 7.92  ? 105 HIS B CG  1 
ATOM   2984 N  ND1 . HIS B 1 105 ? 4.915   -9.682  5.819   1.00 7.85  ? 105 HIS B ND1 1 
ATOM   2985 C  CD2 . HIS B 1 105 ? 6.193   -8.189  4.864   1.00 7.85  ? 105 HIS B CD2 1 
ATOM   2986 C  CE1 . HIS B 1 105 ? 5.650   -9.068  6.803   1.00 8.42  ? 105 HIS B CE1 1 
ATOM   2987 N  NE2 . HIS B 1 105 ? 6.457   -8.177  6.207   1.00 7.96  ? 105 HIS B NE2 1 
ATOM   2988 N  N   . THR B 1 106 ? 3.613   -8.267  0.565   1.00 10.61 ? 106 THR B N   1 
ATOM   2989 C  CA  . THR B 1 106 ? 3.474   -8.516  -0.923  1.00 11.27 ? 106 THR B CA  1 
ATOM   2990 C  C   . THR B 1 106 ? 4.870   -8.827  -1.507  1.00 11.42 ? 106 THR B C   1 
ATOM   2991 O  O   . THR B 1 106 ? 5.902   -8.490  -0.927  1.00 11.68 ? 106 THR B O   1 
ATOM   2992 C  CB  . THR B 1 106 ? 2.718   -7.364  -1.660  1.00 11.19 ? 106 THR B CB  1 
ATOM   2993 O  OG1 . THR B 1 106 ? 3.423   -6.111  -1.511  1.00 11.95 ? 106 THR B OG1 1 
ATOM   2994 C  CG2 . THR B 1 106 ? 1.343   -7.152  -1.029  1.00 11.44 ? 106 THR B CG2 1 
ATOM   2995 N  N   . VAL B 1 107 ? 4.892   -9.511  -2.646  1.00 12.43 ? 107 VAL B N   1 
ATOM   2996 C  CA  . VAL B 1 107 ? 6.142   -9.859  -3.360  1.00 12.79 ? 107 VAL B CA  1 
ATOM   2997 C  C   . VAL B 1 107 ? 5.972   -9.300  -4.787  1.00 12.13 ? 107 VAL B C   1 
ATOM   2998 O  O   . VAL B 1 107 ? 5.034   -9.704  -5.528  1.00 13.26 ? 107 VAL B O   1 
ATOM   2999 C  CB  . VAL B 1 107 ? 6.355   -11.397 -3.406  1.00 12.13 ? 107 VAL B CB  1 
ATOM   3000 C  CG1 . VAL B 1 107 ? 7.657   -11.705 -4.082  1.00 13.91 ? 107 VAL B CG1 1 
ATOM   3001 C  CG2 . VAL B 1 107 ? 6.321   -12.034 -1.989  1.00 14.66 ? 107 VAL B CG2 1 
ATOM   3002 N  N   . SER B 1 108 ? 6.819   -8.332  -5.134  1.00 13.96 ? 108 SER B N   1 
ATOM   3003 C  CA  . SER B 1 108 ? 6.771   -7.680  -6.464  1.00 15.10 ? 108 SER B CA  1 
ATOM   3004 C  C   . SER B 1 108 ? 5.352   -7.167  -6.696  1.00 14.88 ? 108 SER B C   1 
ATOM   3005 O  O   . SER B 1 108 ? 4.806   -7.302  -7.776  1.00 16.58 ? 108 SER B O   1 
ATOM   3006 C  CB  . SER B 1 108 ? 7.284   -8.621  -7.583  1.00 15.86 ? 108 SER B CB  1 
ATOM   3007 O  OG  . SER B 1 108 ? 8.668   -8.927  -7.442  1.00 18.18 ? 108 SER B OG  1 
ATOM   3008 N  N   . GLY B 1 109 ? 4.749   -6.576  -5.633  1.00 16.36 ? 109 GLY B N   1 
ATOM   3009 C  CA  . GLY B 1 109 ? 3.440   -5.915  -5.701  1.00 15.65 ? 109 GLY B CA  1 
ATOM   3010 C  C   . GLY B 1 109 ? 2.194   -6.809  -5.624  1.00 18.39 ? 109 GLY B C   1 
ATOM   3011 O  O   . GLY B 1 109 ? 1.044   -6.300  -5.606  1.00 18.27 ? 109 GLY B O   1 
ATOM   3012 N  N   . GLN B 1 110 ? 2.429   -8.114  -5.581  1.00 16.75 ? 110 GLN B N   1 
ATOM   3013 C  CA  . GLN B 1 110 ? 1.356   -9.134  -5.613  1.00 17.14 ? 110 GLN B CA  1 
ATOM   3014 C  C   . GLN B 1 110 ? 0.995   -9.617  -4.196  1.00 16.57 ? 110 GLN B C   1 
ATOM   3015 O  O   . GLN B 1 110 ? 1.863   -10.033 -3.393  1.00 15.04 ? 110 GLN B O   1 
ATOM   3016 C  CB  . GLN B 1 110 ? 1.724   -10.334 -6.463  1.00 18.38 ? 110 GLN B CB  1 
ATOM   3017 C  CG  . GLN B 1 110 ? 2.162   -10.035 -7.923  1.00 19.26 ? 110 GLN B CG  1 
ATOM   3018 C  CD  . GLN B 1 110 ? 1.246   -9.033  -8.606  1.00 19.51 ? 110 GLN B CD  1 
ATOM   3019 O  OE1 . GLN B 1 110 ? 0.095   -9.355  -8.944  1.00 18.39 ? 110 GLN B OE1 1 
ATOM   3020 N  NE2 . GLN B 1 110 ? 1.751   -7.795  -8.811  1.00 18.86 ? 110 GLN B NE2 1 
ATOM   3021 N  N   . HIS B 1 111 ? -0.293  -9.578  -3.907  1.00 15.25 ? 111 HIS B N   1 
ATOM   3022 C  CA  . HIS B 1 111 ? -0.790  -10.094 -2.607  1.00 15.87 ? 111 HIS B CA  1 
ATOM   3023 C  C   . HIS B 1 111 ? -0.932  -11.587 -2.790  1.00 15.78 ? 111 HIS B C   1 
ATOM   3024 O  O   . HIS B 1 111 ? -1.121  -12.060 -3.921  1.00 18.92 ? 111 HIS B O   1 
ATOM   3025 C  CB  . HIS B 1 111 ? -2.138  -9.492  -2.311  1.00 17.24 ? 111 HIS B CB  1 
ATOM   3026 C  CG  . HIS B 1 111 ? -2.093  -8.298  -1.431  1.00 18.02 ? 111 HIS B CG  1 
ATOM   3027 N  ND1 . HIS B 1 111 ? -1.978  -7.046  -1.911  1.00 20.26 ? 111 HIS B ND1 1 
ATOM   3028 C  CD2 . HIS B 1 111 ? -2.151  -8.194  -0.043  1.00 16.68 ? 111 HIS B CD2 1 
ATOM   3029 C  CE1 . HIS B 1 111 ? -1.964  -6.183  -0.883  1.00 18.64 ? 111 HIS B CE1 1 
ATOM   3030 N  NE2 . HIS B 1 111 ? -2.067  -6.893  0.254   1.00 21.05 ? 111 HIS B NE2 1 
ATOM   3031 N  N   . PHE B 1 112 ? -0.774  -12.343 -1.718  1.00 14.26 ? 112 PHE B N   1 
ATOM   3032 C  CA  . PHE B 1 112 ? -1.255  -13.718 -1.650  1.00 13.34 ? 112 PHE B CA  1 
ATOM   3033 C  C   . PHE B 1 112 ? -2.634  -13.786 -0.959  1.00 11.97 ? 112 PHE B C   1 
ATOM   3034 O  O   . PHE B 1 112 ? -3.180  -12.778 -0.471  1.00 10.79 ? 112 PHE B O   1 
ATOM   3035 C  CB  . PHE B 1 112 ? -0.221  -14.646 -0.958  1.00 14.56 ? 112 PHE B CB  1 
ATOM   3036 C  CG  . PHE B 1 112 ? 1.064   -14.842 -1.746  1.00 16.47 ? 112 PHE B CG  1 
ATOM   3037 C  CD1 . PHE B 1 112 ? 1.996   -13.804 -1.859  1.00 17.38 ? 112 PHE B CD1 1 
ATOM   3038 C  CD2 . PHE B 1 112 ? 1.347   -16.059 -2.341  1.00 17.68 ? 112 PHE B CD2 1 
ATOM   3039 C  CE1 . PHE B 1 112 ? 3.169   -13.973 -2.593  1.00 17.23 ? 112 PHE B CE1 1 
ATOM   3040 C  CE2 . PHE B 1 112 ? 2.522   -16.237 -3.069  1.00 17.40 ? 112 PHE B CE2 1 
ATOM   3041 C  CZ  . PHE B 1 112 ? 3.411   -15.197 -3.198  1.00 16.76 ? 112 PHE B CZ  1 
ATOM   3042 N  N   . ALA B 1 113 ? -3.229  -14.985 -0.937  1.00 11.41 ? 113 ALA B N   1 
ATOM   3043 C  CA  . ALA B 1 113 ? -4.602  -15.127 -0.417  1.00 11.47 ? 113 ALA B CA  1 
ATOM   3044 C  C   . ALA B 1 113 ? -4.667  -14.802 1.031   1.00 10.26 ? 113 ALA B C   1 
ATOM   3045 O  O   . ALA B 1 113 ? -5.662  -14.243 1.485   1.00 9.53  ? 113 ALA B O   1 
ATOM   3046 C  CB  . ALA B 1 113 ? -5.147  -16.546 -0.612  1.00 10.47 ? 113 ALA B CB  1 
ATOM   3047 N  N   . ALA B 1 114 ? -3.589  -15.142 1.756   1.00 10.46 ? 114 ALA B N   1 
ATOM   3048 C  CA  . ALA B 1 114 ? -3.586  -15.003 3.195   1.00 9.46  ? 114 ALA B CA  1 
ATOM   3049 C  C   . ALA B 1 114 ? -2.170  -15.104 3.795   1.00 8.87  ? 114 ALA B C   1 
ATOM   3050 O  O   . ALA B 1 114 ? -1.206  -15.366 3.084   1.00 8.87  ? 114 ALA B O   1 
ATOM   3051 C  CB  . ALA B 1 114 ? -4.548  -16.071 3.813   1.00 8.89  ? 114 ALA B CB  1 
ATOM   3052 N  N   . GLU B 1 115 ? -2.042  -15.002 5.119   1.00 8.77  ? 115 GLU B N   1 
ATOM   3053 C  CA  . GLU B 1 115 ? -0.676  -15.031 5.691   1.00 8.71  ? 115 GLU B CA  1 
ATOM   3054 C  C   . GLU B 1 115 ? -0.754  -15.558 7.131   1.00 9.05  ? 115 GLU B C   1 
ATOM   3055 O  O   . GLU B 1 115 ? -1.671  -15.126 7.947   1.00 8.75  ? 115 GLU B O   1 
ATOM   3056 C  CB  . GLU B 1 115 ? -0.059  -13.587 5.699   1.00 9.42  ? 115 GLU B CB  1 
ATOM   3057 C  CG  . GLU B 1 115 ? 1.396   -13.524 6.196   1.00 9.16  ? 115 GLU B CG  1 
ATOM   3058 C  CD  . GLU B 1 115 ? 2.133   -12.241 5.753   1.00 10.21 ? 115 GLU B CD  1 
ATOM   3059 O  OE1 . GLU B 1 115 ? 3.124   -11.831 6.447   1.00 9.67  ? 115 GLU B OE1 1 
ATOM   3060 O  OE2 . GLU B 1 115 ? 1.766   -11.693 4.653   1.00 10.29 ? 115 GLU B OE2 1 
ATOM   3061 N  N   . LEU B 1 116 ? 0.166   -16.469 7.467   1.00 8.77  ? 116 LEU B N   1 
ATOM   3062 C  CA  . LEU B 1 116 ? 0.214   -16.997 8.855   1.00 8.96  ? 116 LEU B CA  1 
ATOM   3063 C  C   . LEU B 1 116 ? 1.412   -16.318 9.551   1.00 9.51  ? 116 LEU B C   1 
ATOM   3064 O  O   . LEU B 1 116 ? 2.472   -16.166 8.932   1.00 10.09 ? 116 LEU B O   1 
ATOM   3065 C  CB  . LEU B 1 116 ? 0.358   -18.549 8.847   1.00 9.62  ? 116 LEU B CB  1 
ATOM   3066 C  CG  . LEU B 1 116 ? 0.769   -19.244 10.205  1.00 9.95  ? 116 LEU B CG  1 
ATOM   3067 C  CD1 . LEU B 1 116 ? -0.464  -19.426 11.097  1.00 9.71  ? 116 LEU B CD1 1 
ATOM   3068 C  CD2 . LEU B 1 116 ? 1.476   -20.615 9.985   1.00 10.40 ? 116 LEU B CD2 1 
ATOM   3069 N  N   . HIS B 1 117 ? 1.276   -15.988 10.840  1.00 9.79  ? 117 HIS B N   1 
ATOM   3070 C  CA  . HIS B 1 117 ? 2.364   -15.436 11.635  1.00 10.33 ? 117 HIS B CA  1 
ATOM   3071 C  C   . HIS B 1 117 ? 2.609   -16.326 12.823  1.00 11.82 ? 117 HIS B C   1 
ATOM   3072 O  O   . HIS B 1 117 ? 1.645   -16.616 13.555  1.00 12.11 ? 117 HIS B O   1 
ATOM   3073 C  CB  . HIS B 1 117 ? 2.031   -14.002 12.104  1.00 10.68 ? 117 HIS B CB  1 
ATOM   3074 C  CG  . HIS B 1 117 ? 2.036   -12.992 10.981  1.00 10.90 ? 117 HIS B CG  1 
ATOM   3075 N  ND1 . HIS B 1 117 ? 1.356   -11.794 11.035  1.00 9.46  ? 117 HIS B ND1 1 
ATOM   3076 C  CD2 . HIS B 1 117 ? 2.690   -13.022 9.756   1.00 10.00 ? 117 HIS B CD2 1 
ATOM   3077 C  CE1 . HIS B 1 117 ? 1.601   -11.133 9.886   1.00 9.69  ? 117 HIS B CE1 1 
ATOM   3078 N  NE2 . HIS B 1 117 ? 2.370   -11.901 9.109   1.00 9.57  ? 117 HIS B NE2 1 
ATOM   3079 N  N   . ILE B 1 118 ? 3.866   -16.767 13.036  1.00 11.16 ? 118 ILE B N   1 
ATOM   3080 C  CA  . ILE B 1 118 ? 4.261   -17.541 14.271  1.00 11.21 ? 118 ILE B CA  1 
ATOM   3081 C  C   . ILE B 1 118 ? 5.138   -16.633 15.125  1.00 11.73 ? 118 ILE B C   1 
ATOM   3082 O  O   . ILE B 1 118 ? 6.257   -16.319 14.748  1.00 10.87 ? 118 ILE B O   1 
ATOM   3083 C  CB  . ILE B 1 118 ? 4.942   -18.899 13.973  1.00 12.83 ? 118 ILE B CB  1 
ATOM   3084 C  CG1 . ILE B 1 118 ? 4.072   -19.664 12.984  1.00 11.71 ? 118 ILE B CG1 1 
ATOM   3085 C  CG2 . ILE B 1 118 ? 5.099   -19.748 15.279  1.00 12.12 ? 118 ILE B CG2 1 
ATOM   3086 C  CD1 . ILE B 1 118 ? 4.766   -20.894 12.400  1.00 11.42 ? 118 ILE B CD1 1 
ATOM   3087 N  N   . VAL B 1 119 ? 4.568   -16.207 16.261  1.00 11.16 ? 119 VAL B N   1 
ATOM   3088 C  CA  . VAL B 1 119 ? 5.164   -15.155 17.066  1.00 11.68 ? 119 VAL B CA  1 
ATOM   3089 C  C   . VAL B 1 119 ? 6.017   -15.792 18.176  1.00 11.68 ? 119 VAL B C   1 
ATOM   3090 O  O   . VAL B 1 119 ? 5.566   -16.785 18.824  1.00 11.95 ? 119 VAL B O   1 
ATOM   3091 C  CB  . VAL B 1 119 ? 4.065   -14.174 17.635  1.00 10.94 ? 119 VAL B CB  1 
ATOM   3092 C  CG1 . VAL B 1 119 ? 4.746   -13.026 18.368  1.00 9.69  ? 119 VAL B CG1 1 
ATOM   3093 C  CG2 . VAL B 1 119 ? 3.160   -13.611 16.495  1.00 11.13 ? 119 VAL B CG2 1 
ATOM   3094 N  N   . HIS B 1 120 ? 7.216   -15.221 18.392  1.00 11.43 ? 120 HIS B N   1 
ATOM   3095 C  CA  . HIS B 1 120 ? 8.211   -15.687 19.383  1.00 10.89 ? 120 HIS B CA  1 
ATOM   3096 C  C   . HIS B 1 120 ? 8.735   -14.463 20.100  1.00 11.99 ? 120 HIS B C   1 
ATOM   3097 O  O   . HIS B 1 120 ? 8.787   -13.350 19.534  1.00 11.81 ? 120 HIS B O   1 
ATOM   3098 C  CB  . HIS B 1 120 ? 9.431   -16.434 18.725  1.00 10.97 ? 120 HIS B CB  1 
ATOM   3099 C  CG  . HIS B 1 120 ? 9.074   -17.636 17.880  1.00 10.81 ? 120 HIS B CG  1 
ATOM   3100 N  ND1 . HIS B 1 120 ? 8.507   -17.526 16.637  1.00 11.88 ? 120 HIS B ND1 1 
ATOM   3101 C  CD2 . HIS B 1 120 ? 9.277   -18.996 18.091  1.00 11.24 ? 120 HIS B CD2 1 
ATOM   3102 C  CE1 . HIS B 1 120 ? 8.336   -18.749 16.117  1.00 11.44 ? 120 HIS B CE1 1 
ATOM   3103 N  NE2 . HIS B 1 120 ? 8.817   -19.645 17.002  1.00 11.44 ? 120 HIS B NE2 1 
ATOM   3104 N  N   . TYR B 1 121 ? 9.204   -14.652 21.358  1.00 13.05 ? 121 TYR B N   1 
ATOM   3105 C  CA  . TYR B 1 121 ? 9.837   -13.570 22.079  1.00 13.08 ? 121 TYR B CA  1 
ATOM   3106 C  C   . TYR B 1 121 ? 11.233  -14.000 22.495  1.00 13.98 ? 121 TYR B C   1 
ATOM   3107 O  O   . TYR B 1 121 ? 11.490  -15.192 22.649  1.00 14.75 ? 121 TYR B O   1 
ATOM   3108 C  CB  . TYR B 1 121 ? 9.013   -13.163 23.323  1.00 13.18 ? 121 TYR B CB  1 
ATOM   3109 C  CG  . TYR B 1 121 ? 8.936   -14.255 24.402  1.00 13.78 ? 121 TYR B CG  1 
ATOM   3110 C  CD1 . TYR B 1 121 ? 9.760   -14.216 25.564  1.00 13.13 ? 121 TYR B CD1 1 
ATOM   3111 C  CD2 . TYR B 1 121 ? 8.054   -15.329 24.274  1.00 12.39 ? 121 TYR B CD2 1 
ATOM   3112 C  CE1 . TYR B 1 121 ? 9.658   -15.214 26.533  1.00 13.47 ? 121 TYR B CE1 1 
ATOM   3113 C  CE2 . TYR B 1 121 ? 7.980   -16.344 25.231  1.00 14.55 ? 121 TYR B CE2 1 
ATOM   3114 C  CZ  . TYR B 1 121 ? 8.774   -16.293 26.356  1.00 14.26 ? 121 TYR B CZ  1 
ATOM   3115 O  OH  . TYR B 1 121 ? 8.613   -17.358 27.254  1.00 14.91 ? 121 TYR B OH  1 
ATOM   3116 N  N   . ASN B 1 122 ? 12.077  -13.004 22.788  1.00 15.43 ? 122 ASN B N   1 
ATOM   3117 C  CA  . ASN B 1 122 ? 13.473  -13.212 23.249  1.00 15.14 ? 122 ASN B CA  1 
ATOM   3118 C  C   . ASN B 1 122 ? 13.522  -13.716 24.722  1.00 16.15 ? 122 ASN B C   1 
ATOM   3119 O  O   . ASN B 1 122 ? 13.488  -12.944 25.685  1.00 15.88 ? 122 ASN B O   1 
ATOM   3120 C  CB  . ASN B 1 122 ? 14.256  -11.938 23.015  1.00 15.02 ? 122 ASN B CB  1 
ATOM   3121 C  CG  . ASN B 1 122 ? 15.769  -12.103 23.203  1.00 16.13 ? 122 ASN B CG  1 
ATOM   3122 O  OD1 . ASN B 1 122 ? 16.226  -12.895 24.013  1.00 15.87 ? 122 ASN B OD1 1 
ATOM   3123 N  ND2 . ASN B 1 122 ? 16.536  -11.295 22.487  1.00 14.90 ? 122 ASN B ND2 1 
ATOM   3124 N  N   . SER B 1 123 ? 13.565  -15.029 24.859  1.00 16.40 ? 123 SER B N   1 
ATOM   3125 C  CA  . SER B 1 123 ? 13.531  -15.676 26.159  1.00 18.41 ? 123 SER B CA  1 
ATOM   3126 C  C   . SER B 1 123 ? 14.903  -15.657 26.906  1.00 20.29 ? 123 SER B C   1 
ATOM   3127 O  O   . SER B 1 123 ? 14.987  -15.990 28.095  1.00 21.72 ? 123 SER B O   1 
ATOM   3128 C  CB  . SER B 1 123 ? 12.969  -17.082 26.006  1.00 17.54 ? 123 SER B CB  1 
ATOM   3129 O  OG  . SER B 1 123 ? 13.588  -17.879 24.984  1.00 19.50 ? 123 SER B OG  1 
ATOM   3130 N  N   . ASP B 1 124 ? 15.970  -15.291 26.214  1.00 21.83 ? 124 ASP B N   1 
ATOM   3131 C  CA  . ASP B 1 124 ? 17.266  -15.102 26.904  1.00 21.79 ? 124 ASP B CA  1 
ATOM   3132 C  C   . ASP B 1 124 ? 17.269  -13.773 27.639  1.00 23.37 ? 124 ASP B C   1 
ATOM   3133 O  O   . ASP B 1 124 ? 17.971  -13.626 28.676  1.00 23.49 ? 124 ASP B O   1 
ATOM   3134 C  CB  . ASP B 1 124 ? 18.455  -15.073 25.905  1.00 25.32 ? 124 ASP B CB  1 
ATOM   3135 C  CG  . ASP B 1 124 ? 18.698  -16.377 25.170  1.00 27.48 ? 124 ASP B CG  1 
ATOM   3136 O  OD1 . ASP B 1 124 ? 18.316  -17.486 25.615  1.00 30.81 ? 124 ASP B OD1 1 
ATOM   3137 O  OD2 . ASP B 1 124 ? 19.357  -16.294 24.110  1.00 30.04 ? 124 ASP B OD2 1 
ATOM   3138 N  N   . LEU B 1 125 ? 16.556  -12.776 27.096  1.00 20.18 ? 125 LEU B N   1 
ATOM   3139 C  CA  . LEU B 1 125 ? 16.498  -11.434 27.675  1.00 20.61 ? 125 LEU B CA  1 
ATOM   3140 C  C   . LEU B 1 125 ? 15.286  -11.202 28.563  1.00 21.48 ? 125 LEU B C   1 
ATOM   3141 O  O   . LEU B 1 125 ? 15.354  -10.446 29.524  1.00 20.96 ? 125 LEU B O   1 
ATOM   3142 C  CB  . LEU B 1 125 ? 16.579  -10.318 26.609  1.00 20.58 ? 125 LEU B CB  1 
ATOM   3143 C  CG  . LEU B 1 125 ? 17.946  -10.041 25.924  1.00 21.53 ? 125 LEU B CG  1 
ATOM   3144 C  CD1 . LEU B 1 125 ? 17.885  -8.824  25.009  1.00 21.88 ? 125 LEU B CD1 1 
ATOM   3145 C  CD2 . LEU B 1 125 ? 19.087  -9.863  26.945  1.00 22.08 ? 125 LEU B CD2 1 
ATOM   3146 N  N   . TYR B 1 126 ? 14.172  -11.866 28.245  1.00 22.73 ? 126 TYR B N   1 
ATOM   3147 C  CA  . TYR B 1 126 ? 12.880  -11.460 28.811  1.00 19.22 ? 126 TYR B CA  1 
ATOM   3148 C  C   . TYR B 1 126 ? 12.087  -12.664 29.321  1.00 17.28 ? 126 TYR B C   1 
ATOM   3149 O  O   . TYR B 1 126 ? 12.235  -13.749 28.790  1.00 18.76 ? 126 TYR B O   1 
ATOM   3150 C  CB  . TYR B 1 126 ? 12.071  -10.596 27.797  1.00 19.47 ? 126 TYR B CB  1 
ATOM   3151 C  CG  . TYR B 1 126 ? 12.812  -9.371  27.233  1.00 19.48 ? 126 TYR B CG  1 
ATOM   3152 C  CD1 . TYR B 1 126 ? 13.091  -9.274  25.853  1.00 18.41 ? 126 TYR B CD1 1 
ATOM   3153 C  CD2 . TYR B 1 126 ? 13.272  -8.362  28.068  1.00 18.55 ? 126 TYR B CD2 1 
ATOM   3154 C  CE1 . TYR B 1 126 ? 13.785  -8.184  25.325  1.00 18.65 ? 126 TYR B CE1 1 
ATOM   3155 C  CE2 . TYR B 1 126 ? 13.949  -7.254  27.561  1.00 20.01 ? 126 TYR B CE2 1 
ATOM   3156 C  CZ  . TYR B 1 126 ? 14.206  -7.170  26.186  1.00 20.53 ? 126 TYR B CZ  1 
ATOM   3157 O  OH  . TYR B 1 126 ? 14.878  -6.070  25.672  1.00 20.81 ? 126 TYR B OH  1 
ATOM   3158 N  N   . PRO B 1 127 ? 11.280  -12.485 30.399  1.00 19.54 ? 127 PRO B N   1 
ATOM   3159 C  CA  . PRO B 1 127 ? 10.548  -13.604 31.023  1.00 18.90 ? 127 PRO B CA  1 
ATOM   3160 C  C   . PRO B 1 127 ? 9.332   -14.112 30.227  1.00 19.50 ? 127 PRO B C   1 
ATOM   3161 O  O   . PRO B 1 127 ? 9.010   -15.285 30.288  1.00 18.08 ? 127 PRO B O   1 
ATOM   3162 C  CB  . PRO B 1 127 ? 10.126  -13.046 32.398  1.00 18.45 ? 127 PRO B CB  1 
ATOM   3163 C  CG  . PRO B 1 127 ? 10.071  -11.553 32.227  1.00 20.27 ? 127 PRO B CG  1 
ATOM   3164 C  CD  . PRO B 1 127 ? 11.148  -11.238 31.185  1.00 19.88 ? 127 PRO B CD  1 
ATOM   3165 N  N   . ASP B 1 128 ? 8.729   -13.237 29.437  1.00 18.44 ? 128 ASP B N   1 
ATOM   3166 C  CA  . ASP B 1 128 ? 7.484   -13.521 28.728  1.00 17.66 ? 128 ASP B CA  1 
ATOM   3167 C  C   . ASP B 1 128 ? 7.295   -12.559 27.573  1.00 16.75 ? 128 ASP B C   1 
ATOM   3168 O  O   . ASP B 1 128 ? 8.002   -11.521 27.481  1.00 14.71 ? 128 ASP B O   1 
ATOM   3169 C  CB  . ASP B 1 128 ? 6.246   -13.575 29.668  1.00 19.10 ? 128 ASP B CB  1 
ATOM   3170 C  CG  . ASP B 1 128 ? 6.043   -12.315 30.543  1.00 21.71 ? 128 ASP B CG  1 
ATOM   3171 O  OD1 . ASP B 1 128 ? 6.153   -11.168 30.057  1.00 24.17 ? 128 ASP B OD1 1 
ATOM   3172 O  OD2 . ASP B 1 128 ? 5.677   -12.447 31.758  1.00 21.59 ? 128 ASP B OD2 1 
ATOM   3173 N  N   . ALA B 1 129 ? 6.285   -12.866 26.746  1.00 15.66 ? 129 ALA B N   1 
ATOM   3174 C  CA  . ALA B 1 129 ? 6.009   -12.075 25.524  1.00 16.36 ? 129 ALA B CA  1 
ATOM   3175 C  C   . ALA B 1 129 ? 5.529   -10.642 25.801  1.00 16.38 ? 129 ALA B C   1 
ATOM   3176 O  O   . ALA B 1 129 ? 5.944   -9.701  25.101  1.00 15.16 ? 129 ALA B O   1 
ATOM   3177 C  CB  . ALA B 1 129 ? 5.038   -12.844 24.598  1.00 17.18 ? 129 ALA B CB  1 
ATOM   3178 N  N   A SER B 1 130 ? 4.707   -10.478 26.844  0.50 16.28 ? 130 SER B N   1 
ATOM   3179 N  N   B SER B 1 130 ? 4.652   -10.445 26.796  0.50 15.27 ? 130 SER B N   1 
ATOM   3180 C  CA  A SER B 1 130 ? 4.151   -9.196  27.211  0.50 16.97 ? 130 SER B CA  1 
ATOM   3181 C  CA  B SER B 1 130 ? 4.165   -9.106  27.068  0.50 15.31 ? 130 SER B CA  1 
ATOM   3182 C  C   A SER B 1 130 ? 5.229   -8.166  27.582  0.50 17.74 ? 130 SER B C   1 
ATOM   3183 C  C   B SER B 1 130 ? 5.348   -8.179  27.435  0.50 16.37 ? 130 SER B C   1 
ATOM   3184 O  O   A SER B 1 130 ? 5.137   -6.979  27.231  0.50 16.45 ? 130 SER B O   1 
ATOM   3185 O  O   B SER B 1 130 ? 5.471   -7.077  26.902  0.50 15.11 ? 130 SER B O   1 
ATOM   3186 C  CB  A SER B 1 130 ? 3.220   -9.378  28.414  0.50 17.27 ? 130 SER B CB  1 
ATOM   3187 C  CB  B SER B 1 130 ? 3.084   -9.100  28.176  0.50 14.74 ? 130 SER B CB  1 
ATOM   3188 O  OG  A SER B 1 130 ? 2.214   -8.408  28.365  0.50 17.86 ? 130 SER B OG  1 
ATOM   3189 O  OG  B SER B 1 130 ? 3.626   -9.496  29.418  0.50 12.53 ? 130 SER B OG  1 
ATOM   3190 N  N   . THR B 1 131 ? 6.211   -8.641  28.339  1.00 17.02 ? 131 THR B N   1 
ATOM   3191 C  CA  . THR B 1 131 ? 7.357   -7.842  28.785  1.00 19.06 ? 131 THR B CA  1 
ATOM   3192 C  C   . THR B 1 131 ? 8.263   -7.555  27.586  1.00 18.45 ? 131 THR B C   1 
ATOM   3193 O  O   . THR B 1 131 ? 8.671   -6.395  27.373  1.00 21.37 ? 131 THR B O   1 
ATOM   3194 C  CB  . THR B 1 131 ? 8.048   -8.605  29.938  1.00 20.35 ? 131 THR B CB  1 
ATOM   3195 O  OG1 . THR B 1 131 ? 7.059   -8.761  30.997  1.00 19.79 ? 131 THR B OG1 1 
ATOM   3196 C  CG2 . THR B 1 131 ? 9.266   -7.847  30.457  1.00 23.33 ? 131 THR B CG2 1 
ATOM   3197 N  N   . ALA B 1 132 ? 8.482   -8.577  26.773  1.00 17.35 ? 132 ALA B N   1 
ATOM   3198 C  CA  . ALA B 1 132 ? 9.352   -8.482  25.571  1.00 18.17 ? 132 ALA B CA  1 
ATOM   3199 C  C   . ALA B 1 132 ? 8.811   -7.550  24.470  1.00 17.84 ? 132 ALA B C   1 
ATOM   3200 O  O   . ALA B 1 132 ? 9.594   -6.997  23.743  1.00 17.08 ? 132 ALA B O   1 
ATOM   3201 C  CB  . ALA B 1 132 ? 9.589   -9.837  24.954  1.00 16.34 ? 132 ALA B CB  1 
ATOM   3202 N  N   A SER B 1 133 ? 7.488   -7.413  24.395  0.50 17.88 ? 133 SER B N   1 
ATOM   3203 N  N   B SER B 1 133 ? 7.492   -7.431  24.348  0.50 17.38 ? 133 SER B N   1 
ATOM   3204 C  CA  A SER B 1 133 ? 6.814   -6.757  23.261  0.50 18.10 ? 133 SER B CA  1 
ATOM   3205 C  CA  B SER B 1 133 ? 6.878   -6.759  23.183  0.50 17.10 ? 133 SER B CA  1 
ATOM   3206 C  C   A SER B 1 133 ? 7.209   -5.301  22.972  0.50 17.51 ? 133 SER B C   1 
ATOM   3207 C  C   B SER B 1 133 ? 7.309   -5.305  22.940  0.50 16.92 ? 133 SER B C   1 
ATOM   3208 O  O   A SER B 1 133 ? 7.126   -4.866  21.822  0.50 17.60 ? 133 SER B O   1 
ATOM   3209 O  O   B SER B 1 133 ? 7.347   -4.870  21.787  0.50 16.93 ? 133 SER B O   1 
ATOM   3210 C  CB  A SER B 1 133 ? 5.292   -6.854  23.433  0.50 17.71 ? 133 SER B CB  1 
ATOM   3211 C  CB  B SER B 1 133 ? 5.355   -6.815  23.300  0.50 16.24 ? 133 SER B CB  1 
ATOM   3212 O  OG  A SER B 1 133 ? 4.631   -6.364  22.288  0.50 17.43 ? 133 SER B OG  1 
ATOM   3213 O  OG  B SER B 1 133 ? 4.977   -6.249  24.533  0.50 15.03 ? 133 SER B OG  1 
ATOM   3214 N  N   . ASN B 1 134 ? 7.612   -4.549  23.997  1.00 17.64 ? 134 ASN B N   1 
ATOM   3215 C  CA  . ASN B 1 134 ? 8.009   -3.148  23.803  1.00 17.37 ? 134 ASN B CA  1 
ATOM   3216 C  C   . ASN B 1 134 ? 9.434   -2.879  24.229  1.00 19.79 ? 134 ASN B C   1 
ATOM   3217 O  O   . ASN B 1 134 ? 9.759   -1.774  24.668  1.00 19.59 ? 134 ASN B O   1 
ATOM   3218 C  CB  . ASN B 1 134 ? 6.992   -2.144  24.423  1.00 18.92 ? 134 ASN B CB  1 
ATOM   3219 C  CG  . ASN B 1 134 ? 6.900   -2.264  25.925  1.00 19.98 ? 134 ASN B CG  1 
ATOM   3220 O  OD1 . ASN B 1 134 ? 7.298   -3.313  26.504  1.00 18.15 ? 134 ASN B OD1 1 
ATOM   3221 N  ND2 . ASN B 1 134 ? 6.368   -1.205  26.589  1.00 17.16 ? 134 ASN B ND2 1 
ATOM   3222 N  N   . LYS B 1 135 ? 10.286  -3.885  24.082  1.00 17.71 ? 135 LYS B N   1 
ATOM   3223 C  CA  . LYS B 1 135 ? 11.677  -3.753  24.469  1.00 20.44 ? 135 LYS B CA  1 
ATOM   3224 C  C   . LYS B 1 135 ? 12.596  -4.148  23.343  1.00 18.77 ? 135 LYS B C   1 
ATOM   3225 O  O   . LYS B 1 135 ? 12.181  -4.848  22.370  1.00 18.96 ? 135 LYS B O   1 
ATOM   3226 C  CB  . LYS B 1 135 ? 11.979  -4.524  25.773  1.00 22.06 ? 135 LYS B CB  1 
ATOM   3227 C  CG  . LYS B 1 135 ? 11.102  -4.051  26.928  1.00 24.77 ? 135 LYS B CG  1 
ATOM   3228 C  CD  . LYS B 1 135 ? 11.500  -4.662  28.274  1.00 27.46 ? 135 LYS B CD  1 
ATOM   3229 C  CE  . LYS B 1 135 ? 10.655  -4.009  29.370  1.00 28.62 ? 135 LYS B CE  1 
ATOM   3230 N  NZ  . LYS B 1 135 ? 9.180   -4.228  29.143  1.00 33.71 ? 135 LYS B NZ  1 
ATOM   3231 N  N   . SER B 1 136 ? 13.819  -3.606  23.401  1.00 20.08 ? 136 SER B N   1 
ATOM   3232 C  CA  . SER B 1 136 ? 14.816  -3.873  22.352  1.00 21.08 ? 136 SER B CA  1 
ATOM   3233 C  C   . SER B 1 136 ? 14.966  -5.349  22.122  1.00 20.96 ? 136 SER B C   1 
ATOM   3234 O  O   . SER B 1 136 ? 15.132  -6.106  23.091  1.00 21.70 ? 136 SER B O   1 
ATOM   3235 C  CB  . SER B 1 136 ? 16.219  -3.330  22.756  1.00 23.42 ? 136 SER B CB  1 
ATOM   3236 O  OG  . SER B 1 136 ? 17.121  -3.583  21.688  1.00 23.77 ? 136 SER B OG  1 
ATOM   3237 N  N   . GLU B 1 137 ? 14.909  -5.756  20.854  1.00 18.52 ? 137 GLU B N   1 
ATOM   3238 C  CA  . GLU B 1 137 ? 15.152  -7.139  20.451  1.00 20.04 ? 137 GLU B CA  1 
ATOM   3239 C  C   . GLU B 1 137 ? 14.028  -8.087  20.917  1.00 18.59 ? 137 GLU B C   1 
ATOM   3240 O  O   . GLU B 1 137 ? 14.216  -9.303  21.000  1.00 19.98 ? 137 GLU B O   1 
ATOM   3241 C  CB  . GLU B 1 137 ? 16.523  -7.634  20.979  1.00 21.63 ? 137 GLU B CB  1 
ATOM   3242 C  CG  . GLU B 1 137 ? 17.685  -6.804  20.472  1.00 22.83 ? 137 GLU B CG  1 
ATOM   3243 C  CD  . GLU B 1 137 ? 19.026  -7.270  21.016  1.00 27.26 ? 137 GLU B CD  1 
ATOM   3244 O  OE1 . GLU B 1 137 ? 19.740  -6.397  21.549  1.00 24.41 ? 137 GLU B OE1 1 
ATOM   3245 O  OE2 . GLU B 1 137 ? 19.332  -8.504  20.927  1.00 26.84 ? 137 GLU B OE2 1 
ATOM   3246 N  N   . GLY B 1 138 ? 12.868  -7.540  21.259  1.00 16.79 ? 138 GLY B N   1 
ATOM   3247 C  CA  . GLY B 1 138 ? 11.940  -8.373  21.981  1.00 13.69 ? 138 GLY B CA  1 
ATOM   3248 C  C   . GLY B 1 138 ? 11.293  -9.522  21.236  1.00 12.15 ? 138 GLY B C   1 
ATOM   3249 O  O   . GLY B 1 138 ? 11.011  -10.595 21.844  1.00 11.98 ? 138 GLY B O   1 
ATOM   3250 N  N   . LEU B 1 139 ? 10.981  -9.313  19.945  1.00 11.39 ? 139 LEU B N   1 
ATOM   3251 C  CA  . LEU B 1 139 ? 10.117  -10.277 19.210  1.00 11.18 ? 139 LEU B CA  1 
ATOM   3252 C  C   . LEU B 1 139 ? 10.711  -10.758 17.849  1.00 11.95 ? 139 LEU B C   1 
ATOM   3253 O  O   . LEU B 1 139 ? 11.535  -10.042 17.211  1.00 11.80 ? 139 LEU B O   1 
ATOM   3254 C  CB  . LEU B 1 139 ? 8.711   -9.709  18.962  1.00 11.69 ? 139 LEU B CB  1 
ATOM   3255 C  CG  . LEU B 1 139 ? 7.903   -9.265  20.189  1.00 12.27 ? 139 LEU B CG  1 
ATOM   3256 C  CD1 . LEU B 1 139 ? 6.638   -8.528  19.780  1.00 14.19 ? 139 LEU B CD1 1 
ATOM   3257 C  CD2 . LEU B 1 139 ? 7.494   -10.495 21.036  1.00 11.39 ? 139 LEU B CD2 1 
ATOM   3258 N  N   . ALA B 1 140 ? 10.332  -11.973 17.445  1.00 11.51 ? 140 ALA B N   1 
ATOM   3259 C  CA  . ALA B 1 140 ? 10.734  -12.526 16.135  1.00 12.62 ? 140 ALA B CA  1 
ATOM   3260 C  C   . ALA B 1 140 ? 9.517   -13.245 15.553  1.00 11.94 ? 140 ALA B C   1 
ATOM   3261 O  O   . ALA B 1 140 ? 8.993   -14.175 16.159  1.00 13.29 ? 140 ALA B O   1 
ATOM   3262 C  CB  . ALA B 1 140 ? 11.925  -13.494 16.314  1.00 12.84 ? 140 ALA B CB  1 
ATOM   3263 N  N   . VAL B 1 141 ? 9.042   -12.789 14.407  1.00 11.04 ? 141 VAL B N   1 
ATOM   3264 C  CA  . VAL B 1 141 ? 7.864   -13.403 13.802  1.00 9.75  ? 141 VAL B CA  1 
ATOM   3265 C  C   . VAL B 1 141 ? 8.254   -14.162 12.564  1.00 9.57  ? 141 VAL B C   1 
ATOM   3266 O  O   . VAL B 1 141 ? 9.048   -13.661 11.787  1.00 10.00 ? 141 VAL B O   1 
ATOM   3267 C  CB  . VAL B 1 141 ? 6.766   -12.356 13.569  1.00 9.74  ? 141 VAL B CB  1 
ATOM   3268 C  CG1 . VAL B 1 141 ? 5.501   -13.017 12.982  1.00 8.84  ? 141 VAL B CG1 1 
ATOM   3269 C  CG2 . VAL B 1 141 ? 6.359   -11.709 14.902  1.00 9.63  ? 141 VAL B CG2 1 
ATOM   3270 N  N   . LEU B 1 142 ? 7.695   -15.370 12.355  1.00 9.05  ? 142 LEU B N   1 
ATOM   3271 C  CA  . LEU B 1 142 ? 7.893   -16.069 11.096  1.00 9.78  ? 142 LEU B CA  1 
ATOM   3272 C  C   . LEU B 1 142 ? 6.600   -15.875 10.326  1.00 9.96  ? 142 LEU B C   1 
ATOM   3273 O  O   . LEU B 1 142 ? 5.524   -16.009 10.917  1.00 10.22 ? 142 LEU B O   1 
ATOM   3274 C  CB  . LEU B 1 142 ? 8.081   -17.620 11.305  1.00 10.06 ? 142 LEU B CB  1 
ATOM   3275 C  CG  . LEU B 1 142 ? 9.057   -18.115 12.383  1.00 10.17 ? 142 LEU B CG  1 
ATOM   3276 C  CD1 . LEU B 1 142 ? 9.172   -19.640 12.364  1.00 11.35 ? 142 LEU B CD1 1 
ATOM   3277 C  CD2 . LEU B 1 142 ? 10.374  -17.410 12.096  1.00 12.37 ? 142 LEU B CD2 1 
ATOM   3278 N  N   . ALA B 1 143 ? 6.694   -15.619 9.029   1.00 9.98  ? 143 ALA B N   1 
ATOM   3279 C  CA  . ALA B 1 143 ? 5.529   -15.352 8.172   1.00 10.36 ? 143 ALA B CA  1 
ATOM   3280 C  C   . ALA B 1 143 ? 5.516   -16.336 7.021   1.00 10.73 ? 143 ALA B C   1 
ATOM   3281 O  O   . ALA B 1 143 ? 6.494   -16.496 6.277   1.00 10.68 ? 143 ALA B O   1 
ATOM   3282 C  CB  . ALA B 1 143 ? 5.569   -13.908 7.613   1.00 10.70 ? 143 ALA B CB  1 
ATOM   3283 N  N   . VAL B 1 144 ? 4.362   -16.954 6.807   1.00 10.93 ? 144 VAL B N   1 
ATOM   3284 C  CA  . VAL B 1 144 ? 4.188   -17.898 5.719   1.00 9.97  ? 144 VAL B CA  1 
ATOM   3285 C  C   . VAL B 1 144 ? 3.101   -17.375 4.819   1.00 10.07 ? 144 VAL B C   1 
ATOM   3286 O  O   . VAL B 1 144 ? 2.023   -17.075 5.305   1.00 9.89  ? 144 VAL B O   1 
ATOM   3287 C  CB  . VAL B 1 144 ? 3.651   -19.239 6.252   1.00 10.50 ? 144 VAL B CB  1 
ATOM   3288 C  CG1 . VAL B 1 144 ? 3.426   -20.231 5.117   1.00 11.05 ? 144 VAL B CG1 1 
ATOM   3289 C  CG2 . VAL B 1 144 ? 4.666   -19.831 7.224   1.00 11.89 ? 144 VAL B CG2 1 
ATOM   3290 N  N   . LEU B 1 145 ? 3.380   -17.278 3.521   1.00 9.70  ? 145 LEU B N   1 
ATOM   3291 C  CA  . LEU B 1 145 ? 2.409   -16.717 2.521   1.00 10.03 ? 145 LEU B CA  1 
ATOM   3292 C  C   . LEU B 1 145 ? 1.573   -17.906 2.137   1.00 10.42 ? 145 LEU B C   1 
ATOM   3293 O  O   . LEU B 1 145 ? 2.151   -18.980 1.925   1.00 12.09 ? 145 LEU B O   1 
ATOM   3294 C  CB  . LEU B 1 145 ? 3.162   -16.170 1.266   1.00 9.61  ? 145 LEU B CB  1 
ATOM   3295 C  CG  . LEU B 1 145 ? 4.129   -14.981 1.566   1.00 9.96  ? 145 LEU B CG  1 
ATOM   3296 C  CD1 . LEU B 1 145 ? 5.006   -14.634 0.340   1.00 11.59 ? 145 LEU B CD1 1 
ATOM   3297 C  CD2 . LEU B 1 145 ? 3.350   -13.735 2.011   1.00 11.27 ? 145 LEU B CD2 1 
ATOM   3298 N  N   . ILE B 1 146 ? 0.249   -17.703 1.971   1.00 10.84 ? 146 ILE B N   1 
ATOM   3299 C  CA  . ILE B 1 146 ? -0.693  -18.795 1.652   1.00 10.50 ? 146 ILE B CA  1 
ATOM   3300 C  C   . ILE B 1 146 ? -1.426  -18.492 0.332   1.00 12.71 ? 146 ILE B C   1 
ATOM   3301 O  O   . ILE B 1 146 ? -2.034  -17.425 0.217   1.00 13.27 ? 146 ILE B O   1 
ATOM   3302 C  CB  . ILE B 1 146 ? -1.784  -18.882 2.779   1.00 10.42 ? 146 ILE B CB  1 
ATOM   3303 C  CG1 . ILE B 1 146 ? -1.087  -19.170 4.138   1.00 9.06  ? 146 ILE B CG1 1 
ATOM   3304 C  CG2 . ILE B 1 146 ? -2.840  -19.983 2.474   1.00 10.31 ? 146 ILE B CG2 1 
ATOM   3305 C  CD1 . ILE B 1 146 ? -1.925  -18.849 5.365   1.00 9.42  ? 146 ILE B CD1 1 
ATOM   3306 N  N   . GLU B 1 147 ? -1.385  -19.406 -0.623  1.00 12.50 ? 147 GLU B N   1 
ATOM   3307 C  CA  . GLU B 1 147 ? -2.220  -19.314 -1.852  1.00 13.96 ? 147 GLU B CA  1 
ATOM   3308 C  C   . GLU B 1 147 ? -3.264  -20.436 -1.989  1.00 15.85 ? 147 GLU B C   1 
ATOM   3309 O  O   . GLU B 1 147 ? -3.180  -21.439 -1.267  1.00 15.32 ? 147 GLU B O   1 
ATOM   3310 C  CB  . GLU B 1 147 ? -1.288  -19.268 -3.084  1.00 15.21 ? 147 GLU B CB  1 
ATOM   3311 C  CG  . GLU B 1 147 ? -0.445  -20.528 -3.274  1.00 14.96 ? 147 GLU B CG  1 
ATOM   3312 C  CD  . GLU B 1 147 ? 0.620   -20.460 -4.353  1.00 17.74 ? 147 GLU B CD  1 
ATOM   3313 O  OE1 . GLU B 1 147 ? 1.108   -19.377 -4.752  1.00 17.19 ? 147 GLU B OE1 1 
ATOM   3314 O  OE2 . GLU B 1 147 ? 1.008   -21.552 -4.782  1.00 20.90 ? 147 GLU B OE2 1 
ATOM   3315 N  N   . MET B 1 148 ? -4.245  -20.253 -2.889  1.00 17.17 ? 148 MET B N   1 
ATOM   3316 C  CA  . MET B 1 148 ? -5.223  -21.329 -3.231  1.00 19.01 ? 148 MET B CA  1 
ATOM   3317 C  C   . MET B 1 148 ? -4.521  -22.488 -3.908  1.00 18.76 ? 148 MET B C   1 
ATOM   3318 O  O   . MET B 1 148 ? -3.682  -22.299 -4.802  1.00 19.90 ? 148 MET B O   1 
ATOM   3319 C  CB  . MET B 1 148 ? -6.293  -20.811 -4.194  1.00 24.73 ? 148 MET B CB  1 
ATOM   3320 C  CG  . MET B 1 148 ? -7.379  -19.868 -3.699  1.00 31.02 ? 148 MET B CG  1 
ATOM   3321 S  SD  . MET B 1 148 ? -8.344  -19.125 -5.087  1.00 46.07 ? 148 MET B SD  1 
ATOM   3322 C  CE  . MET B 1 148 ? -8.372  -20.466 -6.284  1.00 39.26 ? 148 MET B CE  1 
ATOM   3323 N  N   . GLY B 1 149 ? -4.831  -23.712 -3.495  1.00 19.14 ? 149 GLY B N   1 
ATOM   3324 C  CA  . GLY B 1 149 ? -4.284  -24.878 -4.133  1.00 19.25 ? 149 GLY B CA  1 
ATOM   3325 C  C   . GLY B 1 149 ? -5.002  -26.113 -3.687  1.00 17.85 ? 149 GLY B C   1 
ATOM   3326 O  O   . GLY B 1 149 ? -6.204  -26.093 -3.539  1.00 17.14 ? 149 GLY B O   1 
ATOM   3327 N  N   . SER B 1 150 ? -4.236  -27.176 -3.473  1.00 19.47 ? 150 SER B N   1 
ATOM   3328 C  CA  . SER B 1 150 ? -4.677  -28.427 -2.835  1.00 20.99 ? 150 SER B CA  1 
ATOM   3329 C  C   . SER B 1 150 ? -5.041  -28.244 -1.342  1.00 20.47 ? 150 SER B C   1 
ATOM   3330 O  O   . SER B 1 150 ? -4.479  -27.393 -0.639  1.00 18.48 ? 150 SER B O   1 
ATOM   3331 C  CB  . SER B 1 150 ? -3.532  -29.449 -2.956  1.00 22.45 ? 150 SER B CB  1 
ATOM   3332 O  OG  . SER B 1 150 ? -2.303  -28.871 -2.458  1.00 25.98 ? 150 SER B OG  1 
ATOM   3333 N  N   . PHE B 1 151 ? -5.989  -29.060 -0.888  1.00 18.03 ? 151 PHE B N   1 
ATOM   3334 C  CA  . PHE B 1 151 ? -6.395  -29.157 0.500   1.00 16.80 ? 151 PHE B CA  1 
ATOM   3335 C  C   . PHE B 1 151 ? -5.195  -29.486 1.376   1.00 16.57 ? 151 PHE B C   1 
ATOM   3336 O  O   . PHE B 1 151 ? -4.363  -30.378 1.053   1.00 16.65 ? 151 PHE B O   1 
ATOM   3337 C  CB  . PHE B 1 151 ? -7.443  -30.298 0.635   1.00 16.05 ? 151 PHE B CB  1 
ATOM   3338 C  CG  . PHE B 1 151 ? -7.894  -30.575 2.060   1.00 15.39 ? 151 PHE B CG  1 
ATOM   3339 C  CD1 . PHE B 1 151 ? -8.814  -29.730 2.680   1.00 16.24 ? 151 PHE B CD1 1 
ATOM   3340 C  CD2 . PHE B 1 151 ? -7.399  -31.674 2.766   1.00 16.45 ? 151 PHE B CD2 1 
ATOM   3341 C  CE1 . PHE B 1 151 ? -9.238  -29.981 3.967   1.00 16.83 ? 151 PHE B CE1 1 
ATOM   3342 C  CE2 . PHE B 1 151 ? -7.815  -31.967 4.056   1.00 16.57 ? 151 PHE B CE2 1 
ATOM   3343 C  CZ  . PHE B 1 151 ? -8.757  -31.110 4.658   1.00 18.18 ? 151 PHE B CZ  1 
ATOM   3344 N  N   . ASN B 1 152 ? -5.140  -28.824 2.507   1.00 17.02 ? 152 ASN B N   1 
ATOM   3345 C  CA  . ASN B 1 152 ? -4.022  -28.930 3.401   1.00 16.16 ? 152 ASN B CA  1 
ATOM   3346 C  C   . ASN B 1 152 ? -4.506  -29.492 4.769   1.00 18.04 ? 152 ASN B C   1 
ATOM   3347 O  O   . ASN B 1 152 ? -5.157  -28.796 5.579   1.00 16.75 ? 152 ASN B O   1 
ATOM   3348 C  CB  . ASN B 1 152 ? -3.385  -27.554 3.492   1.00 15.17 ? 152 ASN B CB  1 
ATOM   3349 C  CG  . ASN B 1 152 ? -2.056  -27.539 4.234   1.00 16.25 ? 152 ASN B CG  1 
ATOM   3350 O  OD1 . ASN B 1 152 ? -1.897  -28.105 5.347   1.00 15.99 ? 152 ASN B OD1 1 
ATOM   3351 N  ND2 . ASN B 1 152 ? -1.094  -26.834 3.645   1.00 15.16 ? 152 ASN B ND2 1 
ATOM   3352 N  N   . PRO B 1 153 ? -4.184  -30.772 5.035   1.00 18.07 ? 153 PRO B N   1 
ATOM   3353 C  CA  . PRO B 1 153 ? -4.648  -31.454 6.267   1.00 18.12 ? 153 PRO B CA  1 
ATOM   3354 C  C   . PRO B 1 153 ? -4.151  -30.719 7.513   1.00 17.02 ? 153 PRO B C   1 
ATOM   3355 O  O   . PRO B 1 153 ? -4.898  -30.571 8.489   1.00 16.04 ? 153 PRO B O   1 
ATOM   3356 C  CB  . PRO B 1 153 ? -4.013  -32.853 6.153   1.00 19.77 ? 153 PRO B CB  1 
ATOM   3357 C  CG  . PRO B 1 153 ? -3.797  -33.044 4.670   1.00 19.97 ? 153 PRO B CG  1 
ATOM   3358 C  CD  . PRO B 1 153 ? -3.435  -31.671 4.126   1.00 17.92 ? 153 PRO B CD  1 
ATOM   3359 N  N   . SER B 1 154 ? -2.929  -30.187 7.441   1.00 15.57 ? 154 SER B N   1 
ATOM   3360 C  CA  . SER B 1 154 ? -2.331  -29.511 8.607   1.00 15.88 ? 154 SER B CA  1 
ATOM   3361 C  C   . SER B 1 154 ? -2.993  -28.189 8.967   1.00 15.45 ? 154 SER B C   1 
ATOM   3362 O  O   . SER B 1 154 ? -3.301  -27.919 10.148  1.00 15.24 ? 154 SER B O   1 
ATOM   3363 C  CB  . SER B 1 154 ? -0.841  -29.367 8.381   1.00 16.92 ? 154 SER B CB  1 
ATOM   3364 O  OG  . SER B 1 154 ? -0.365  -30.707 8.154   1.00 18.64 ? 154 SER B OG  1 
ATOM   3365 N  N   . TYR B 1 155 ? -3.227  -27.344 7.965   1.00 14.38 ? 155 TYR B N   1 
ATOM   3366 C  CA  . TYR B 1 155 ? -4.027  -26.118 8.267   1.00 14.27 ? 155 TYR B CA  1 
ATOM   3367 C  C   . TYR B 1 155 ? -5.460  -26.477 8.717   1.00 15.06 ? 155 TYR B C   1 
ATOM   3368 O  O   . TYR B 1 155 ? -6.045  -25.752 9.517   1.00 16.06 ? 155 TYR B O   1 
ATOM   3369 C  CB  . TYR B 1 155 ? -4.010  -25.143 7.065   1.00 15.68 ? 155 TYR B CB  1 
ATOM   3370 C  CG  . TYR B 1 155 ? -2.761  -24.300 7.034   1.00 15.02 ? 155 TYR B CG  1 
ATOM   3371 C  CD1 . TYR B 1 155 ? -1.554  -24.822 6.521   1.00 14.79 ? 155 TYR B CD1 1 
ATOM   3372 C  CD2 . TYR B 1 155 ? -2.776  -22.987 7.522   1.00 14.39 ? 155 TYR B CD2 1 
ATOM   3373 C  CE1 . TYR B 1 155 ? -0.395  -24.041 6.493   1.00 14.55 ? 155 TYR B CE1 1 
ATOM   3374 C  CE2 . TYR B 1 155 ? -1.605  -22.215 7.547   1.00 15.30 ? 155 TYR B CE2 1 
ATOM   3375 C  CZ  . TYR B 1 155 ? -0.416  -22.760 6.993   1.00 15.39 ? 155 TYR B CZ  1 
ATOM   3376 O  OH  . TYR B 1 155 ? 0.777   -22.017 7.003   1.00 14.84 ? 155 TYR B OH  1 
ATOM   3377 N  N   . ASP B 1 156 ? -6.031  -27.592 8.238   1.00 16.22 ? 156 ASP B N   1 
ATOM   3378 C  CA  . ASP B 1 156 ? -7.324  -28.029 8.749   1.00 15.47 ? 156 ASP B CA  1 
ATOM   3379 C  C   . ASP B 1 156 ? -7.356  -28.379 10.252  1.00 15.41 ? 156 ASP B C   1 
ATOM   3380 O  O   . ASP B 1 156 ? -8.414  -28.271 10.884  1.00 13.94 ? 156 ASP B O   1 
ATOM   3381 C  CB  . ASP B 1 156 ? -8.012  -29.098 7.869   1.00 17.44 ? 156 ASP B CB  1 
ATOM   3382 C  CG  . ASP B 1 156 ? -9.403  -28.639 7.424   1.00 21.06 ? 156 ASP B CG  1 
ATOM   3383 O  OD1 . ASP B 1 156 ? -10.342 -29.467 7.433   1.00 20.42 ? 156 ASP B OD1 1 
ATOM   3384 O  OD2 . ASP B 1 156 ? -9.566  -27.415 7.090   1.00 18.19 ? 156 ASP B OD2 1 
ATOM   3385 N  N   . LYS B 1 157 ? -6.197  -28.688 10.841  1.00 13.12 ? 157 LYS B N   1 
ATOM   3386 C  CA  . LYS B 1 157 ? -6.063  -28.831 12.270  1.00 14.52 ? 157 LYS B CA  1 
ATOM   3387 C  C   . LYS B 1 157 ? -6.419  -27.589 13.081  1.00 13.74 ? 157 LYS B C   1 
ATOM   3388 O  O   . LYS B 1 157 ? -6.868  -27.712 14.221  1.00 14.18 ? 157 LYS B O   1 
ATOM   3389 C  CB  . LYS B 1 157 ? -4.704  -29.440 12.638  1.00 16.52 ? 157 LYS B CB  1 
ATOM   3390 C  CG  . LYS B 1 157 ? -4.527  -30.843 11.979  1.00 18.67 ? 157 LYS B CG  1 
ATOM   3391 C  CD  . LYS B 1 157 ? -3.317  -31.628 12.479  1.00 21.83 ? 157 LYS B CD  1 
ATOM   3392 C  CE  . LYS B 1 157 ? -3.004  -32.800 11.540  1.00 21.26 ? 157 LYS B CE  1 
ATOM   3393 N  NZ  . LYS B 1 157 ? -1.553  -33.210 11.706  1.00 26.54 ? 157 LYS B NZ  1 
ATOM   3394 N  N   . ILE B 1 158 ? -6.265  -26.406 12.468  1.00 12.77 ? 158 ILE B N   1 
ATOM   3395 C  CA  . ILE B 1 158 ? -6.824  -25.147 13.012  1.00 13.80 ? 158 ILE B CA  1 
ATOM   3396 C  C   . ILE B 1 158 ? -8.269  -24.869 12.512  1.00 13.14 ? 158 ILE B C   1 
ATOM   3397 O  O   . ILE B 1 158 ? -9.174  -24.544 13.312  1.00 12.05 ? 158 ILE B O   1 
ATOM   3398 C  CB  . ILE B 1 158 ? -5.897  -23.929 12.664  1.00 13.45 ? 158 ILE B CB  1 
ATOM   3399 C  CG1 . ILE B 1 158 ? -4.496  -24.130 13.285  1.00 14.41 ? 158 ILE B CG1 1 
ATOM   3400 C  CG2 . ILE B 1 158 ? -6.438  -22.657 13.284  1.00 14.88 ? 158 ILE B CG2 1 
ATOM   3401 C  CD1 . ILE B 1 158 ? -3.379  -23.300 12.677  1.00 14.55 ? 158 ILE B CD1 1 
ATOM   3402 N  N   . PHE B 1 159 ? -8.456  -24.944 11.188  1.00 12.92 ? 159 PHE B N   1 
ATOM   3403 C  CA  . PHE B 1 159 ? -9.723  -24.515 10.568  1.00 13.99 ? 159 PHE B CA  1 
ATOM   3404 C  C   . PHE B 1 159 ? -10.954 -25.324 10.990  1.00 13.43 ? 159 PHE B C   1 
ATOM   3405 O  O   . PHE B 1 159 ? -12.074 -24.792 11.074  1.00 12.74 ? 159 PHE B O   1 
ATOM   3406 C  CB  . PHE B 1 159 ? -9.644  -24.501 9.019   1.00 12.77 ? 159 PHE B CB  1 
ATOM   3407 C  CG  . PHE B 1 159 ? -8.594  -23.588 8.466   1.00 13.77 ? 159 PHE B CG  1 
ATOM   3408 C  CD1 . PHE B 1 159 ? -8.123  -22.518 9.196   1.00 13.93 ? 159 PHE B CD1 1 
ATOM   3409 C  CD2 . PHE B 1 159 ? -8.063  -23.824 7.210   1.00 13.54 ? 159 PHE B CD2 1 
ATOM   3410 C  CE1 . PHE B 1 159 ? -7.178  -21.659 8.682   1.00 14.26 ? 159 PHE B CE1 1 
ATOM   3411 C  CE2 . PHE B 1 159 ? -7.096  -22.988 6.694   1.00 13.93 ? 159 PHE B CE2 1 
ATOM   3412 C  CZ  . PHE B 1 159 ? -6.647  -21.906 7.424   1.00 13.82 ? 159 PHE B CZ  1 
ATOM   3413 N  N   . SER B 1 160 ? -10.783 -26.604 11.291  1.00 14.59 ? 160 SER B N   1 
ATOM   3414 C  CA  . SER B 1 160 ? -11.941 -27.378 11.711  1.00 15.98 ? 160 SER B CA  1 
ATOM   3415 C  C   . SER B 1 160 ? -12.570 -26.907 13.049  1.00 16.28 ? 160 SER B C   1 
ATOM   3416 O  O   . SER B 1 160 ? -13.667 -27.354 13.356  1.00 19.42 ? 160 SER B O   1 
ATOM   3417 C  CB  . SER B 1 160 ? -11.601 -28.870 11.802  1.00 16.29 ? 160 SER B CB  1 
ATOM   3418 O  OG  . SER B 1 160 ? -10.601 -28.993 12.805  1.00 17.01 ? 160 SER B OG  1 
ATOM   3419 N  N   . HIS B 1 161 ? -11.898 -26.072 13.848  1.00 14.07 ? 161 HIS B N   1 
ATOM   3420 C  CA  . HIS B 1 161 ? -12.439 -25.634 15.139  1.00 14.98 ? 161 HIS B CA  1 
ATOM   3421 C  C   . HIS B 1 161 ? -13.098 -24.279 15.056  1.00 13.59 ? 161 HIS B C   1 
ATOM   3422 O  O   . HIS B 1 161 ? -13.538 -23.780 16.083  1.00 14.21 ? 161 HIS B O   1 
ATOM   3423 C  CB  . HIS B 1 161 ? -11.338 -25.570 16.242  1.00 16.59 ? 161 HIS B CB  1 
ATOM   3424 C  CG  . HIS B 1 161 ? -10.676 -26.894 16.493  1.00 19.39 ? 161 HIS B CG  1 
ATOM   3425 N  ND1 . HIS B 1 161 ? -11.118 -27.766 17.442  1.00 21.06 ? 161 HIS B ND1 1 
ATOM   3426 C  CD2 . HIS B 1 161 ? -9.603  -27.515 15.843  1.00 18.61 ? 161 HIS B CD2 1 
ATOM   3427 C  CE1 . HIS B 1 161 ? -10.346 -28.891 17.389  1.00 24.04 ? 161 HIS B CE1 1 
ATOM   3428 N  NE2 . HIS B 1 161 ? -9.442  -28.741 16.398  1.00 21.48 ? 161 HIS B NE2 1 
ATOM   3429 N  N   . LEU B 1 162 ? -13.123 -23.682 13.851  1.00 13.02 ? 162 LEU B N   1 
ATOM   3430 C  CA  . LEU B 1 162 ? -13.423 -22.230 13.684  1.00 14.73 ? 162 LEU B CA  1 
ATOM   3431 C  C   . LEU B 1 162 ? -14.833 -21.907 14.173  1.00 15.04 ? 162 LEU B C   1 
ATOM   3432 O  O   . LEU B 1 162 ? -15.052 -20.849 14.782  1.00 13.89 ? 162 LEU B O   1 
ATOM   3433 C  CB  . LEU B 1 162 ? -13.187 -21.751 12.199  1.00 15.00 ? 162 LEU B CB  1 
ATOM   3434 C  CG  . LEU B 1 162 ? -11.766 -21.471 11.629  1.00 14.61 ? 162 LEU B CG  1 
ATOM   3435 C  CD1 . LEU B 1 162 ? -11.747 -20.930 10.200  1.00 14.65 ? 162 LEU B CD1 1 
ATOM   3436 C  CD2 . LEU B 1 162 ? -10.937 -20.512 12.497  1.00 16.63 ? 162 LEU B CD2 1 
ATOM   3437 N  N   . GLN B 1 163 ? -15.791 -22.834 13.945  1.00 15.61 ? 163 GLN B N   1 
ATOM   3438 C  CA  . GLN B 1 163 ? -17.202 -22.577 14.338  1.00 15.78 ? 163 GLN B CA  1 
ATOM   3439 C  C   . GLN B 1 163 ? -17.409 -22.505 15.869  1.00 15.35 ? 163 GLN B C   1 
ATOM   3440 O  O   . GLN B 1 163 ? -18.467 -22.114 16.351  1.00 16.73 ? 163 GLN B O   1 
ATOM   3441 C  CB  . GLN B 1 163 ? -18.188 -23.548 13.613  1.00 18.50 ? 163 GLN B CB  1 
ATOM   3442 C  CG  . GLN B 1 163 ? -17.935 -23.639 12.087  1.00 17.78 ? 163 GLN B CG  1 
ATOM   3443 C  CD  . GLN B 1 163 ? -18.061 -22.293 11.323  1.00 19.81 ? 163 GLN B CD  1 
ATOM   3444 O  OE1 . GLN B 1 163 ? -19.009 -21.542 11.512  1.00 21.81 ? 163 GLN B OE1 1 
ATOM   3445 N  NE2 . GLN B 1 163 ? -17.101 -22.019 10.442  1.00 20.90 ? 163 GLN B NE2 1 
ATOM   3446 N  N   . HIS B 1 164 ? -16.404 -22.859 16.659  1.00 14.41 ? 164 HIS B N   1 
ATOM   3447 C  CA  . HIS B 1 164 ? -16.516 -22.661 18.128  1.00 14.13 ? 164 HIS B CA  1 
ATOM   3448 C  C   . HIS B 1 164 ? -15.901 -21.433 18.650  1.00 14.77 ? 164 HIS B C   1 
ATOM   3449 O  O   . HIS B 1 164 ? -15.928 -21.200 19.880  1.00 15.29 ? 164 HIS B O   1 
ATOM   3450 C  CB  . HIS B 1 164 ? -15.963 -23.858 18.902  1.00 14.50 ? 164 HIS B CB  1 
ATOM   3451 C  CG  . HIS B 1 164 ? -16.494 -25.175 18.354  1.00 15.43 ? 164 HIS B CG  1 
ATOM   3452 N  ND1 . HIS B 1 164 ? -17.799 -25.535 18.464  1.00 17.38 ? 164 HIS B ND1 1 
ATOM   3453 C  CD2 . HIS B 1 164 ? -15.860 -26.200 17.669  1.00 15.72 ? 164 HIS B CD2 1 
ATOM   3454 C  CE1 . HIS B 1 164 ? -17.975 -26.749 17.858  1.00 16.65 ? 164 HIS B CE1 1 
ATOM   3455 N  NE2 . HIS B 1 164 ? -16.809 -27.121 17.333  1.00 15.98 ? 164 HIS B NE2 1 
ATOM   3456 N  N   . VAL B 1 165 ? -15.346 -20.619 17.759  1.00 13.54 ? 165 VAL B N   1 
ATOM   3457 C  CA  . VAL B 1 165 ? -14.764 -19.361 18.206  1.00 12.59 ? 165 VAL B CA  1 
ATOM   3458 C  C   . VAL B 1 165 ? -15.313 -18.205 17.348  1.00 13.30 ? 165 VAL B C   1 
ATOM   3459 O  O   . VAL B 1 165 ? -14.614 -17.210 17.087  1.00 12.99 ? 165 VAL B O   1 
ATOM   3460 C  CB  . VAL B 1 165 ? -13.184 -19.416 18.339  1.00 12.54 ? 165 VAL B CB  1 
ATOM   3461 C  CG1 . VAL B 1 165 ? -12.768 -20.351 19.468  1.00 12.70 ? 165 VAL B CG1 1 
ATOM   3462 C  CG2 . VAL B 1 165 ? -12.443 -19.859 17.063  1.00 12.98 ? 165 VAL B CG2 1 
ATOM   3463 N  N   . LYS B 1 166 ? -16.586 -18.308 16.932  1.00 12.84 ? 166 LYS B N   1 
ATOM   3464 C  CA  . LYS B 1 166 ? -17.154 -17.276 16.045  1.00 13.93 ? 166 LYS B CA  1 
ATOM   3465 C  C   . LYS B 1 166 ? -17.160 -15.820 16.507  1.00 13.20 ? 166 LYS B C   1 
ATOM   3466 O  O   . LYS B 1 166 ? -17.022 -14.879 15.669  1.00 13.00 ? 166 LYS B O   1 
ATOM   3467 C  CB  . LYS B 1 166 ? -18.543 -17.689 15.494  1.00 14.46 ? 166 LYS B CB  1 
ATOM   3468 C  CG  . LYS B 1 166 ? -18.573 -19.061 14.797  1.00 18.02 ? 166 LYS B CG  1 
ATOM   3469 C  CD  . LYS B 1 166 ? -19.987 -19.366 14.275  1.00 18.68 ? 166 LYS B CD  1 
ATOM   3470 C  CE  . LYS B 1 166 ? -20.469 -18.437 13.162  1.00 20.01 ? 166 LYS B CE  1 
ATOM   3471 N  NZ  . LYS B 1 166 ? -19.891 -18.791 11.823  1.00 19.92 ? 166 LYS B NZ  1 
ATOM   3472 N  N   . TYR B 1 167 ? -17.288 -15.585 17.803  1.00 13.32 ? 167 TYR B N   1 
ATOM   3473 C  CA  . TYR B 1 167 ? -17.416 -14.199 18.298  1.00 13.70 ? 167 TYR B CA  1 
ATOM   3474 C  C   . TYR B 1 167 ? -16.252 -13.846 19.176  1.00 13.85 ? 167 TYR B C   1 
ATOM   3475 O  O   . TYR B 1 167 ? -15.629 -14.735 19.755  1.00 12.92 ? 167 TYR B O   1 
ATOM   3476 C  CB  . TYR B 1 167 ? -18.745 -14.060 19.053  1.00 13.88 ? 167 TYR B CB  1 
ATOM   3477 C  CG  . TYR B 1 167 ? -19.859 -14.214 18.083  1.00 14.63 ? 167 TYR B CG  1 
ATOM   3478 C  CD1 . TYR B 1 167 ? -20.449 -15.437 17.865  1.00 14.55 ? 167 TYR B CD1 1 
ATOM   3479 C  CD2 . TYR B 1 167 ? -20.279 -13.116 17.340  1.00 14.73 ? 167 TYR B CD2 1 
ATOM   3480 C  CE1 . TYR B 1 167 ? -21.454 -15.584 16.901  1.00 17.55 ? 167 TYR B CE1 1 
ATOM   3481 C  CE2 . TYR B 1 167 ? -21.271 -13.252 16.370  1.00 15.73 ? 167 TYR B CE2 1 
ATOM   3482 C  CZ  . TYR B 1 167 ? -21.857 -14.472 16.179  1.00 16.63 ? 167 TYR B CZ  1 
ATOM   3483 O  OH  . TYR B 1 167 ? -22.857 -14.576 15.217  1.00 20.39 ? 167 TYR B OH  1 
ATOM   3484 N  N   . LYS B 1 168 ? -15.985 -12.543 19.305  1.00 13.69 ? 168 LYS B N   1 
ATOM   3485 C  CA  . LYS B 1 168 ? -14.860 -12.073 20.129  1.00 15.01 ? 168 LYS B CA  1 
ATOM   3486 C  C   . LYS B 1 168 ? -14.881 -12.589 21.569  1.00 15.13 ? 168 LYS B C   1 
ATOM   3487 O  O   . LYS B 1 168 ? -15.913 -12.538 22.261  1.00 14.69 ? 168 LYS B O   1 
ATOM   3488 C  CB  . LYS B 1 168 ? -14.859 -10.538 20.134  1.00 14.31 ? 168 LYS B CB  1 
ATOM   3489 C  CG  . LYS B 1 168 ? -13.682 -9.955  20.886  1.00 17.59 ? 168 LYS B CG  1 
ATOM   3490 C  CD  . LYS B 1 168 ? -13.763 -8.459  20.863  1.00 18.76 ? 168 LYS B CD  1 
ATOM   3491 C  CE  . LYS B 1 168 ? -12.855 -7.905  21.922  1.00 21.63 ? 168 LYS B CE  1 
ATOM   3492 N  NZ  . LYS B 1 168 ? -12.575 -6.514  21.500  1.00 22.72 ? 168 LYS B NZ  1 
ATOM   3493 N  N   . GLY B 1 169 ? -13.759 -13.126 22.022  1.00 15.58 ? 169 GLY B N   1 
ATOM   3494 C  CA  . GLY B 1 169 ? -13.660 -13.558 23.386  1.00 15.98 ? 169 GLY B CA  1 
ATOM   3495 C  C   . GLY B 1 169 ? -13.861 -15.039 23.536  1.00 16.76 ? 169 GLY B C   1 
ATOM   3496 O  O   . GLY B 1 169 ? -13.456 -15.585 24.561  1.00 19.37 ? 169 GLY B O   1 
ATOM   3497 N  N   . GLN B 1 170 ? -14.530 -15.699 22.572  1.00 14.95 ? 170 GLN B N   1 
ATOM   3498 C  CA  . GLN B 1 170 ? -14.725 -17.126 22.654  1.00 15.52 ? 170 GLN B CA  1 
ATOM   3499 C  C   . GLN B 1 170 ? -13.417 -17.963 22.494  1.00 16.32 ? 170 GLN B C   1 
ATOM   3500 O  O   . GLN B 1 170 ? -12.467 -17.544 21.782  1.00 14.87 ? 170 GLN B O   1 
ATOM   3501 C  CB  . GLN B 1 170 ? -15.792 -17.575 21.650  1.00 14.23 ? 170 GLN B CB  1 
ATOM   3502 C  CG  . GLN B 1 170 ? -17.141 -16.851 21.828  1.00 13.98 ? 170 GLN B CG  1 
ATOM   3503 C  CD  . GLN B 1 170 ? -18.226 -17.390 20.937  1.00 12.60 ? 170 GLN B CD  1 
ATOM   3504 O  OE1 . GLN B 1 170 ? -17.989 -17.681 19.801  1.00 13.30 ? 170 GLN B OE1 1 
ATOM   3505 N  NE2 . GLN B 1 170 ? -19.463 -17.486 21.475  1.00 14.85 ? 170 GLN B NE2 1 
ATOM   3506 N  N   . GLU B 1 171 ? -13.413 -19.151 23.121  1.00 15.51 ? 171 GLU B N   1 
ATOM   3507 C  CA  . GLU B 1 171 ? -12.218 -19.974 23.243  1.00 16.62 ? 171 GLU B CA  1 
ATOM   3508 C  C   . GLU B 1 171 ? -12.587 -21.422 22.997  1.00 16.53 ? 171 GLU B C   1 
ATOM   3509 O  O   . GLU B 1 171 ? -13.713 -21.841 23.249  1.00 15.89 ? 171 GLU B O   1 
ATOM   3510 C  CB  . GLU B 1 171 ? -11.607 -19.863 24.652  1.00 17.62 ? 171 GLU B CB  1 
ATOM   3511 C  CG  . GLU B 1 171 ? -11.160 -18.482 25.099  1.00 18.80 ? 171 GLU B CG  1 
ATOM   3512 C  CD  . GLU B 1 171 ? -10.735 -18.483 26.580  1.00 18.96 ? 171 GLU B CD  1 
ATOM   3513 O  OE1 . GLU B 1 171 ? -10.023 -17.601 27.039  1.00 22.59 ? 171 GLU B OE1 1 
ATOM   3514 O  OE2 . GLU B 1 171 ? -11.103 -19.361 27.313  1.00 21.38 ? 171 GLU B OE2 1 
ATOM   3515 N  N   . ALA B 1 172 ? -11.618 -22.190 22.502  1.00 15.92 ? 172 ALA B N   1 
ATOM   3516 C  CA  . ALA B 1 172 ? -11.764 -23.646 22.403  1.00 16.62 ? 172 ALA B CA  1 
ATOM   3517 C  C   . ALA B 1 172 ? -10.367 -24.251 22.503  1.00 16.54 ? 172 ALA B C   1 
ATOM   3518 O  O   . ALA B 1 172 ? -9.396  -23.558 22.215  1.00 17.58 ? 172 ALA B O   1 
ATOM   3519 C  CB  . ALA B 1 172 ? -12.419 -24.062 21.103  1.00 14.87 ? 172 ALA B CB  1 
ATOM   3520 N  N   . PHE B 1 173 ? -10.238 -25.506 22.961  1.00 16.13 ? 173 PHE B N   1 
ATOM   3521 C  CA  . PHE B 1 173 ? -8.915  -26.166 22.922  1.00 15.82 ? 173 PHE B CA  1 
ATOM   3522 C  C   . PHE B 1 173 ? -8.705  -26.967 21.665  1.00 15.83 ? 173 PHE B C   1 
ATOM   3523 O  O   . PHE B 1 173 ? -9.674  -27.492 21.069  1.00 17.12 ? 173 PHE B O   1 
ATOM   3524 C  CB  . PHE B 1 173 ? -8.641  -27.050 24.167  1.00 17.11 ? 173 PHE B CB  1 
ATOM   3525 C  CG  . PHE B 1 173 ? -8.465  -26.285 25.452  1.00 16.45 ? 173 PHE B CG  1 
ATOM   3526 C  CD1 . PHE B 1 173 ? -9.455  -26.299 26.447  1.00 17.82 ? 173 PHE B CD1 1 
ATOM   3527 C  CD2 . PHE B 1 173 ? -7.281  -25.595 25.712  1.00 17.45 ? 173 PHE B CD2 1 
ATOM   3528 C  CE1 . PHE B 1 173 ? -9.270  -25.626 27.654  1.00 17.66 ? 173 PHE B CE1 1 
ATOM   3529 C  CE2 . PHE B 1 173 ? -7.102  -24.919 26.925  1.00 17.23 ? 173 PHE B CE2 1 
ATOM   3530 C  CZ  . PHE B 1 173 ? -8.101  -24.914 27.882  1.00 17.85 ? 173 PHE B CZ  1 
ATOM   3531 N  N   . VAL B 1 174 ? -7.446  -27.024 21.242  1.00 13.61 ? 174 VAL B N   1 
ATOM   3532 C  CA  . VAL B 1 174 ? -7.019  -27.747 20.057  1.00 14.19 ? 174 VAL B CA  1 
ATOM   3533 C  C   . VAL B 1 174 ? -5.927  -28.743 20.524  1.00 13.31 ? 174 VAL B C   1 
ATOM   3534 O  O   . VAL B 1 174 ? -4.965  -28.346 21.156  1.00 14.40 ? 174 VAL B O   1 
ATOM   3535 C  CB  . VAL B 1 174 ? -6.481  -26.738 18.957  1.00 14.70 ? 174 VAL B CB  1 
ATOM   3536 C  CG1 . VAL B 1 174 ? -5.910  -27.470 17.752  1.00 16.01 ? 174 VAL B CG1 1 
ATOM   3537 C  CG2 . VAL B 1 174 ? -7.576  -25.762 18.517  1.00 16.90 ? 174 VAL B CG2 1 
ATOM   3538 N  N   . PRO B 1 175 ? -6.110  -30.035 20.270  1.00 13.02 ? 175 PRO B N   1 
ATOM   3539 C  CA  . PRO B 1 175 ? -5.067  -31.032 20.610  1.00 13.62 ? 175 PRO B CA  1 
ATOM   3540 C  C   . PRO B 1 175 ? -3.761  -30.740 19.898  1.00 13.19 ? 175 PRO B C   1 
ATOM   3541 O  O   . PRO B 1 175 ? -3.761  -30.235 18.759  1.00 13.07 ? 175 PRO B O   1 
ATOM   3542 C  CB  . PRO B 1 175 ? -5.635  -32.335 20.022  1.00 13.36 ? 175 PRO B CB  1 
ATOM   3543 C  CG  . PRO B 1 175 ? -7.118  -32.074 19.825  1.00 14.10 ? 175 PRO B CG  1 
ATOM   3544 C  CD  . PRO B 1 175 ? -7.153  -30.630 19.402  1.00 12.66 ? 175 PRO B CD  1 
ATOM   3545 N  N   . GLY B 1 176 ? -2.653  -31.041 20.575  1.00 13.36 ? 176 GLY B N   1 
ATOM   3546 C  CA  . GLY B 1 176 ? -1.347  -30.869 19.971  1.00 14.04 ? 176 GLY B CA  1 
ATOM   3547 C  C   . GLY B 1 176 ? -1.208  -31.522 18.615  1.00 14.26 ? 176 GLY B C   1 
ATOM   3548 O  O   . GLY B 1 176 ? -1.666  -32.664 18.399  1.00 12.80 ? 176 GLY B O   1 
ATOM   3549 N  N   . PHE B 1 177 ? -0.573  -30.765 17.714  1.00 14.13 ? 177 PHE B N   1 
ATOM   3550 C  CA  . PHE B 1 177 ? -0.120  -31.247 16.381  1.00 14.76 ? 177 PHE B CA  1 
ATOM   3551 C  C   . PHE B 1 177 ? 1.265   -30.663 15.987  1.00 15.86 ? 177 PHE B C   1 
ATOM   3552 O  O   . PHE B 1 177 ? 1.841   -29.793 16.700  1.00 14.61 ? 177 PHE B O   1 
ATOM   3553 C  CB  . PHE B 1 177 ? -1.226  -31.001 15.324  1.00 15.17 ? 177 PHE B CB  1 
ATOM   3554 C  CG  . PHE B 1 177 ? -1.390  -29.536 14.883  1.00 13.83 ? 177 PHE B CG  1 
ATOM   3555 C  CD1 . PHE B 1 177 ? -0.778  -29.106 13.694  1.00 14.30 ? 177 PHE B CD1 1 
ATOM   3556 C  CD2 . PHE B 1 177 ? -2.197  -28.638 15.577  1.00 13.12 ? 177 PHE B CD2 1 
ATOM   3557 C  CE1 . PHE B 1 177 ? -0.918  -27.785 13.235  1.00 13.45 ? 177 PHE B CE1 1 
ATOM   3558 C  CE2 . PHE B 1 177 ? -2.354  -27.319 15.131  1.00 13.37 ? 177 PHE B CE2 1 
ATOM   3559 C  CZ  . PHE B 1 177 ? -1.717  -26.901 13.959  1.00 12.95 ? 177 PHE B CZ  1 
ATOM   3560 N  N   . ASN B 1 178 ? 1.832   -31.132 14.879  1.00 16.00 ? 178 ASN B N   1 
ATOM   3561 C  CA  . ASN B 1 178 ? 3.168   -30.696 14.461  1.00 16.06 ? 178 ASN B CA  1 
ATOM   3562 C  C   . ASN B 1 178 ? 3.096   -29.293 13.747  1.00 15.08 ? 178 ASN B C   1 
ATOM   3563 O  O   . ASN B 1 178 ? 2.683   -29.183 12.570  1.00 16.14 ? 178 ASN B O   1 
ATOM   3564 C  CB  . ASN B 1 178 ? 3.859   -31.760 13.538  1.00 16.05 ? 178 ASN B CB  1 
ATOM   3565 C  CG  . ASN B 1 178 ? 5.344   -31.429 13.255  1.00 17.80 ? 178 ASN B CG  1 
ATOM   3566 O  OD1 . ASN B 1 178 ? 5.867   -30.408 13.722  1.00 16.34 ? 178 ASN B OD1 1 
ATOM   3567 N  ND2 . ASN B 1 178 ? 6.030   -32.301 12.494  1.00 19.90 ? 178 ASN B ND2 1 
ATOM   3568 N  N   . ILE B 1 179 ? 3.505   -28.251 14.454  1.00 13.73 ? 179 ILE B N   1 
ATOM   3569 C  CA  . ILE B 1 179 ? 3.420   -26.897 13.931  1.00 13.77 ? 179 ILE B CA  1 
ATOM   3570 C  C   . ILE B 1 179 ? 4.293   -26.768 12.646  1.00 15.42 ? 179 ILE B C   1 
ATOM   3571 O  O   . ILE B 1 179 ? 4.007   -25.977 11.747  1.00 14.55 ? 179 ILE B O   1 
ATOM   3572 C  CB  . ILE B 1 179 ? 3.660   -25.845 15.024  1.00 14.30 ? 179 ILE B CB  1 
ATOM   3573 C  CG1 . ILE B 1 179 ? 2.742   -26.050 16.266  1.00 12.96 ? 179 ILE B CG1 1 
ATOM   3574 C  CG2 . ILE B 1 179 ? 3.566   -24.436 14.440  1.00 13.72 ? 179 ILE B CG2 1 
ATOM   3575 C  CD1 . ILE B 1 179 ? 1.225   -25.792 16.074  1.00 14.04 ? 179 ILE B CD1 1 
ATOM   3576 N  N   . GLU B 1 180 ? 5.329   -27.599 12.539  1.00 15.76 ? 180 GLU B N   1 
ATOM   3577 C  CA  . GLU B 1 180 ? 6.239   -27.498 11.391  1.00 16.07 ? 180 GLU B CA  1 
ATOM   3578 C  C   . GLU B 1 180 ? 5.563   -27.855 10.059  1.00 15.54 ? 180 GLU B C   1 
ATOM   3579 O  O   . GLU B 1 180 ? 6.058   -27.481 8.971   1.00 17.12 ? 180 GLU B O   1 
ATOM   3580 C  CB  . GLU B 1 180 ? 7.492   -28.348 11.640  1.00 18.24 ? 180 GLU B CB  1 
ATOM   3581 C  CG  . GLU B 1 180 ? 8.618   -28.050 10.664  1.00 19.30 ? 180 GLU B CG  1 
ATOM   3582 C  CD  . GLU B 1 180 ? 9.939   -28.652 11.066  1.00 21.69 ? 180 GLU B CD  1 
ATOM   3583 O  OE1 . GLU B 1 180 ? 10.039  -29.291 12.142  1.00 22.31 ? 180 GLU B OE1 1 
ATOM   3584 O  OE2 . GLU B 1 180 ? 10.895  -28.427 10.299  1.00 24.79 ? 180 GLU B OE2 1 
ATOM   3585 N  N   . GLU B 1 181 ? 4.463   -28.584 10.125  1.00 14.68 ? 181 GLU B N   1 
ATOM   3586 C  CA  . GLU B 1 181 ? 3.687   -28.890 8.927   1.00 16.63 ? 181 GLU B CA  1 
ATOM   3587 C  C   . GLU B 1 181 ? 2.989   -27.687 8.309   1.00 14.66 ? 181 GLU B C   1 
ATOM   3588 O  O   . GLU B 1 181 ? 2.527   -27.779 7.185   1.00 16.81 ? 181 GLU B O   1 
ATOM   3589 C  CB  . GLU B 1 181 ? 2.664   -29.986 9.200   1.00 18.81 ? 181 GLU B CB  1 
ATOM   3590 C  CG  . GLU B 1 181 ? 3.352   -31.274 9.614   1.00 23.04 ? 181 GLU B CG  1 
ATOM   3591 C  CD  . GLU B 1 181 ? 2.396   -32.408 9.808   1.00 30.05 ? 181 GLU B CD  1 
ATOM   3592 O  OE1 . GLU B 1 181 ? 2.631   -33.440 9.132   1.00 36.95 ? 181 GLU B OE1 1 
ATOM   3593 O  OE2 . GLU B 1 181 ? 1.424   -32.271 10.612  1.00 34.89 ? 181 GLU B OE2 1 
ATOM   3594 N  N   . LEU B 1 182 ? 2.875   -26.592 9.062   1.00 14.37 ? 182 LEU B N   1 
ATOM   3595 C  CA  . LEU B 1 182 ? 2.325   -25.321 8.517   1.00 13.76 ? 182 LEU B CA  1 
ATOM   3596 C  C   . LEU B 1 182 ? 3.333   -24.543 7.652   1.00 15.14 ? 182 LEU B C   1 
ATOM   3597 O  O   . LEU B 1 182 ? 2.965   -23.563 6.964   1.00 15.88 ? 182 LEU B O   1 
ATOM   3598 C  CB  . LEU B 1 182 ? 1.831   -24.392 9.652   1.00 12.94 ? 182 LEU B CB  1 
ATOM   3599 C  CG  . LEU B 1 182 ? 0.865   -24.983 10.648  1.00 11.92 ? 182 LEU B CG  1 
ATOM   3600 C  CD1 . LEU B 1 182 ? 0.465   -24.052 11.810  1.00 12.15 ? 182 LEU B CD1 1 
ATOM   3601 C  CD2 . LEU B 1 182 ? -0.349  -25.510 9.892   1.00 12.55 ? 182 LEU B CD2 1 
ATOM   3602 N  N   . LEU B 1 183 ? 4.605   -24.940 7.740   1.00 14.16 ? 183 LEU B N   1 
ATOM   3603 C  CA  . LEU B 1 183 ? 5.697   -24.228 7.068   1.00 14.96 ? 183 LEU B CA  1 
ATOM   3604 C  C   . LEU B 1 183 ? 5.851   -24.739 5.656   1.00 15.91 ? 183 LEU B C   1 
ATOM   3605 O  O   . LEU B 1 183 ? 5.495   -25.884 5.383   1.00 17.10 ? 183 LEU B O   1 
ATOM   3606 C  CB  . LEU B 1 183 ? 7.013   -24.381 7.839   1.00 15.37 ? 183 LEU B CB  1 
ATOM   3607 C  CG  . LEU B 1 183 ? 7.038   -23.913 9.311   1.00 15.02 ? 183 LEU B CG  1 
ATOM   3608 C  CD1 . LEU B 1 183 ? 8.410   -24.132 9.944   1.00 14.01 ? 183 LEU B CD1 1 
ATOM   3609 C  CD2 . LEU B 1 183 ? 6.607   -22.448 9.475   1.00 15.63 ? 183 LEU B CD2 1 
ATOM   3610 N  N   . PRO B 1 184 ? 6.349   -23.877 4.752   1.00 15.31 ? 184 PRO B N   1 
ATOM   3611 C  CA  . PRO B 1 184 ? 6.578   -24.344 3.411   1.00 16.64 ? 184 PRO B CA  1 
ATOM   3612 C  C   . PRO B 1 184 ? 7.809   -25.210 3.237   1.00 20.04 ? 184 PRO B C   1 
ATOM   3613 O  O   . PRO B 1 184 ? 8.602   -25.444 4.182   1.00 19.40 ? 184 PRO B O   1 
ATOM   3614 C  CB  . PRO B 1 184 ? 6.754   -23.031 2.638   1.00 16.45 ? 184 PRO B CB  1 
ATOM   3615 C  CG  . PRO B 1 184 ? 7.436   -22.134 3.607   1.00 14.95 ? 184 PRO B CG  1 
ATOM   3616 C  CD  . PRO B 1 184 ? 6.852   -22.487 4.949   1.00 14.08 ? 184 PRO B CD  1 
ATOM   3617 N  N   . GLU B 1 185 ? 7.957   -25.602 1.969   1.00 25.00 ? 185 GLU B N   1 
ATOM   3618 C  CA  . GLU B 1 185 ? 9.220   -26.042 1.338   1.00 25.62 ? 185 GLU B CA  1 
ATOM   3619 C  C   . GLU B 1 185 ? 10.452  -25.147 1.443   1.00 27.51 ? 185 GLU B C   1 
ATOM   3620 O  O   . GLU B 1 185 ? 10.365  -23.890 1.373   1.00 25.99 ? 185 GLU B O   1 
ATOM   3621 C  CB  . GLU B 1 185 ? 8.918   -26.298 -0.122  1.00 26.31 ? 185 GLU B CB  1 
ATOM   3622 C  CG  . GLU B 1 185 ? 7.903   -27.437 -0.250  1.00 32.47 ? 185 GLU B CG  1 
ATOM   3623 C  CD  . GLU B 1 185 ? 7.894   -28.062 -1.620  1.00 37.71 ? 185 GLU B CD  1 
ATOM   3624 O  OE1 . GLU B 1 185 ? 7.860   -27.320 -2.641  1.00 36.35 ? 185 GLU B OE1 1 
ATOM   3625 O  OE2 . GLU B 1 185 ? 7.923   -29.310 -1.656  1.00 40.48 ? 185 GLU B OE2 1 
ATOM   3626 N  N   A ARG B 1 186 ? 11.580  -25.816 1.669   0.50 25.17 ? 186 ARG B N   1 
ATOM   3627 N  N   B ARG B 1 186 ? 11.639  -25.752 1.512   0.50 25.58 ? 186 ARG B N   1 
ATOM   3628 C  CA  A ARG B 1 186 ? 12.864  -25.180 1.626   0.50 24.78 ? 186 ARG B CA  1 
ATOM   3629 C  CA  B ARG B 1 186 ? 12.876  -24.968 1.530   0.50 25.28 ? 186 ARG B CA  1 
ATOM   3630 C  C   A ARG B 1 186 ? 12.821  -23.881 2.449   0.50 22.90 ? 186 ARG B C   1 
ATOM   3631 C  C   B ARG B 1 186 ? 12.741  -23.770 2.454   0.50 23.02 ? 186 ARG B C   1 
ATOM   3632 O  O   A ARG B 1 186 ? 13.107  -22.779 1.912   0.50 22.71 ? 186 ARG B O   1 
ATOM   3633 O  O   B ARG B 1 186 ? 12.907  -22.606 1.991   0.50 21.73 ? 186 ARG B O   1 
ATOM   3634 C  CB  A ARG B 1 186 ? 13.273  -24.913 0.158   0.50 26.20 ? 186 ARG B CB  1 
ATOM   3635 C  CB  B ARG B 1 186 ? 13.239  -24.384 0.142   0.50 27.03 ? 186 ARG B CB  1 
ATOM   3636 C  CG  A ARG B 1 186 ? 13.732  -26.136 -0.649  0.50 25.99 ? 186 ARG B CG  1 
ATOM   3637 C  CG  B ARG B 1 186 ? 13.813  -25.334 -0.896  0.50 27.98 ? 186 ARG B CG  1 
ATOM   3638 C  CD  A ARG B 1 186 ? 12.595  -26.784 -1.447  0.50 25.61 ? 186 ARG B CD  1 
ATOM   3639 C  CD  B ARG B 1 186 ? 12.727  -25.672 -1.897  0.50 29.63 ? 186 ARG B CD  1 
ATOM   3640 N  NE  A ARG B 1 186 ? 12.151  -25.957 -2.574  0.50 24.88 ? 186 ARG B NE  1 
ATOM   3641 N  NE  B ARG B 1 186 ? 13.202  -26.597 -2.911  0.50 31.32 ? 186 ARG B NE  1 
ATOM   3642 C  CZ  A ARG B 1 186 ? 12.874  -24.982 -3.123  0.50 24.48 ? 186 ARG B CZ  1 
ATOM   3643 C  CZ  B ARG B 1 186 ? 12.492  -27.618 -3.362  0.50 31.68 ? 186 ARG B CZ  1 
ATOM   3644 N  NH1 A ARG B 1 186 ? 12.374  -24.271 -4.130  0.50 23.67 ? 186 ARG B NH1 1 
ATOM   3645 N  NH1 B ARG B 1 186 ? 13.008  -28.417 -4.284  0.50 32.35 ? 186 ARG B NH1 1 
ATOM   3646 N  NH2 A ARG B 1 186 ? 14.103  -24.731 -2.683  0.50 23.36 ? 186 ARG B NH2 1 
ATOM   3647 N  NH2 B ARG B 1 186 ? 11.274  -27.835 -2.885  0.50 31.50 ? 186 ARG B NH2 1 
ATOM   3648 N  N   . THR B 1 187 ? 12.458  -23.998 3.736   1.00 20.19 ? 187 THR B N   1 
ATOM   3649 C  CA  . THR B 1 187 ? 12.476  -22.840 4.656   1.00 18.09 ? 187 THR B CA  1 
ATOM   3650 C  C   . THR B 1 187 ? 13.811  -22.122 4.632   1.00 17.25 ? 187 THR B C   1 
ATOM   3651 O  O   . THR B 1 187 ? 13.945  -21.037 5.202   1.00 14.96 ? 187 THR B O   1 
ATOM   3652 C  CB  . THR B 1 187 ? 12.170  -23.210 6.138   1.00 19.41 ? 187 THR B CB  1 
ATOM   3653 O  OG1 . THR B 1 187 ? 12.960  -24.356 6.500   1.00 18.62 ? 187 THR B OG1 1 
ATOM   3654 C  CG2 . THR B 1 187 ? 10.638  -23.502 6.296   1.00 19.70 ? 187 THR B CG2 1 
ATOM   3655 N  N   . ALA B 1 188 ? 14.847  -22.708 3.998   1.00 15.64 ? 188 ALA B N   1 
ATOM   3656 C  CA  . ALA B 1 188 ? 16.158  -22.074 4.110   1.00 16.76 ? 188 ALA B CA  1 
ATOM   3657 C  C   . ALA B 1 188 ? 16.181  -20.781 3.294   1.00 15.75 ? 188 ALA B C   1 
ATOM   3658 O  O   . ALA B 1 188 ? 17.028  -19.938 3.529   1.00 15.61 ? 188 ALA B O   1 
ATOM   3659 C  CB  . ALA B 1 188 ? 17.294  -23.010 3.642   1.00 18.83 ? 188 ALA B CB  1 
ATOM   3660 N  N   . GLU B 1 189 ? 15.258  -20.677 2.327   1.00 15.02 ? 189 GLU B N   1 
ATOM   3661 C  CA  . GLU B 1 189 ? 15.142  -19.479 1.473   1.00 15.66 ? 189 GLU B CA  1 
ATOM   3662 C  C   . GLU B 1 189 ? 14.124  -18.491 2.064   1.00 12.60 ? 189 GLU B C   1 
ATOM   3663 O  O   . GLU B 1 189 ? 12.973  -18.838 2.167   1.00 12.38 ? 189 GLU B O   1 
ATOM   3664 C  CB  . GLU B 1 189 ? 14.781  -19.871 0.049   1.00 18.03 ? 189 GLU B CB  1 
ATOM   3665 C  CG  . GLU B 1 189 ? 15.717  -20.943 -0.515  1.00 23.13 ? 189 GLU B CG  1 
ATOM   3666 C  CD  . GLU B 1 189 ? 15.356  -21.340 -1.915  1.00 28.01 ? 189 GLU B CD  1 
ATOM   3667 O  OE1 . GLU B 1 189 ? 14.764  -20.518 -2.631  1.00 27.19 ? 189 GLU B OE1 1 
ATOM   3668 O  OE2 . GLU B 1 189 ? 15.671  -22.495 -2.303  1.00 33.31 ? 189 GLU B OE2 1 
ATOM   3669 N  N   . TYR B 1 190 ? 14.585  -17.326 2.505   1.00 11.64 ? 190 TYR B N   1 
ATOM   3670 C  CA  . TYR B 1 190 ? 13.707  -16.332 3.145   1.00 11.47 ? 190 TYR B CA  1 
ATOM   3671 C  C   . TYR B 1 190 ? 14.193  -14.881 2.968   1.00 11.94 ? 190 TYR B C   1 
ATOM   3672 O  O   . TYR B 1 190 ? 15.363  -14.634 2.613   1.00 12.53 ? 190 TYR B O   1 
ATOM   3673 C  CB  . TYR B 1 190 ? 13.515  -16.634 4.650   1.00 10.21 ? 190 TYR B CB  1 
ATOM   3674 C  CG  . TYR B 1 190 ? 14.820  -16.731 5.448   1.00 10.62 ? 190 TYR B CG  1 
ATOM   3675 C  CD1 . TYR B 1 190 ? 15.469  -15.584 5.891   1.00 9.90  ? 190 TYR B CD1 1 
ATOM   3676 C  CD2 . TYR B 1 190 ? 15.430  -17.974 5.714   1.00 10.18 ? 190 TYR B CD2 1 
ATOM   3677 C  CE1 . TYR B 1 190 ? 16.665  -15.661 6.542   1.00 10.60 ? 190 TYR B CE1 1 
ATOM   3678 C  CE2 . TYR B 1 190 ? 16.639  -18.037 6.441   1.00 10.15 ? 190 TYR B CE2 1 
ATOM   3679 C  CZ  . TYR B 1 190 ? 17.256  -16.862 6.819   1.00 11.16 ? 190 TYR B CZ  1 
ATOM   3680 O  OH  . TYR B 1 190 ? 18.432  -16.806 7.575   1.00 12.18 ? 190 TYR B OH  1 
ATOM   3681 N  N   . TYR B 1 191 ? 13.303  -13.926 3.281   1.00 11.80 ? 191 TYR B N   1 
ATOM   3682 C  CA  . TYR B 1 191 ? 13.599  -12.500 3.394   1.00 12.10 ? 191 TYR B CA  1 
ATOM   3683 C  C   . TYR B 1 191 ? 13.705  -12.120 4.892   1.00 12.17 ? 191 TYR B C   1 
ATOM   3684 O  O   . TYR B 1 191 ? 12.903  -12.577 5.713   1.00 13.81 ? 191 TYR B O   1 
ATOM   3685 C  CB  . TYR B 1 191 ? 12.440  -11.657 2.788   1.00 11.17 ? 191 TYR B CB  1 
ATOM   3686 C  CG  . TYR B 1 191 ? 11.972  -12.008 1.402   1.00 11.34 ? 191 TYR B CG  1 
ATOM   3687 C  CD1 . TYR B 1 191 ? 11.047  -13.018 1.188   1.00 11.39 ? 191 TYR B CD1 1 
ATOM   3688 C  CD2 . TYR B 1 191 ? 12.416  -11.276 0.288   1.00 11.59 ? 191 TYR B CD2 1 
ATOM   3689 C  CE1 . TYR B 1 191 ? 10.618  -13.312 -0.107  1.00 12.61 ? 191 TYR B CE1 1 
ATOM   3690 C  CE2 . TYR B 1 191 ? 11.989  -11.572 -1.010  1.00 11.98 ? 191 TYR B CE2 1 
ATOM   3691 C  CZ  . TYR B 1 191 ? 11.113  -12.585 -1.180  1.00 12.28 ? 191 TYR B CZ  1 
ATOM   3692 O  OH  . TYR B 1 191 ? 10.643  -12.882 -2.457  1.00 15.84 ? 191 TYR B OH  1 
ATOM   3693 N  N   . ARG B 1 192 ? 14.684  -11.318 5.286   1.00 11.41 ? 192 ARG B N   1 
ATOM   3694 C  CA  . ARG B 1 192 ? 14.807  -10.971 6.682   1.00 11.19 ? 192 ARG B CA  1 
ATOM   3695 C  C   . ARG B 1 192 ? 14.896  -9.442  6.805   1.00 10.82 ? 192 ARG B C   1 
ATOM   3696 O  O   . ARG B 1 192 ? 15.626  -8.844  6.056   1.00 12.21 ? 192 ARG B O   1 
ATOM   3697 C  CB  . ARG B 1 192 ? 16.103  -11.618 7.185   1.00 11.27 ? 192 ARG B CB  1 
ATOM   3698 C  CG  . ARG B 1 192 ? 16.692  -11.162 8.494   1.00 14.49 ? 192 ARG B CG  1 
ATOM   3699 C  CD  . ARG B 1 192 ? 15.975  -11.683 9.714   1.00 12.93 ? 192 ARG B CD  1 
ATOM   3700 N  NE  . ARG B 1 192 ? 15.750  -13.175 9.810   1.00 14.44 ? 192 ARG B NE  1 
ATOM   3701 C  CZ  . ARG B 1 192 ? 16.649  -14.134 10.029  1.00 13.63 ? 192 ARG B CZ  1 
ATOM   3702 N  NH1 . ARG B 1 192 ? 16.241  -15.383 10.119  1.00 14.20 ? 192 ARG B NH1 1 
ATOM   3703 N  NH2 . ARG B 1 192 ? 17.950  -13.885 10.155  1.00 16.26 ? 192 ARG B NH2 1 
ATOM   3704 N  N   . TYR B 1 193 ? 14.174  -8.822  7.728   1.00 11.29 ? 193 TYR B N   1 
ATOM   3705 C  CA  . TYR B 1 193 ? 14.269  -7.364  7.924   1.00 11.31 ? 193 TYR B CA  1 
ATOM   3706 C  C   . TYR B 1 193 ? 13.761  -6.948  9.327   1.00 11.63 ? 193 TYR B C   1 
ATOM   3707 O  O   . TYR B 1 193 ? 12.968  -7.684  9.947   1.00 11.48 ? 193 TYR B O   1 
ATOM   3708 C  CB  . TYR B 1 193 ? 13.540  -6.622  6.762   1.00 11.12 ? 193 TYR B CB  1 
ATOM   3709 C  CG  . TYR B 1 193 ? 12.020  -6.546  6.894   1.00 11.06 ? 193 TYR B CG  1 
ATOM   3710 C  CD1 . TYR B 1 193 ? 11.418  -5.457  7.516   1.00 11.05 ? 193 TYR B CD1 1 
ATOM   3711 C  CD2 . TYR B 1 193 ? 11.205  -7.580  6.450   1.00 10.91 ? 193 TYR B CD2 1 
ATOM   3712 C  CE1 . TYR B 1 193 ? 10.024  -5.372  7.694   1.00 10.60 ? 193 TYR B CE1 1 
ATOM   3713 C  CE2 . TYR B 1 193 ? 9.814   -7.512  6.605   1.00 10.01 ? 193 TYR B CE2 1 
ATOM   3714 C  CZ  . TYR B 1 193 ? 9.234   -6.441  7.240   1.00 10.57 ? 193 TYR B CZ  1 
ATOM   3715 O  OH  . TYR B 1 193 ? 7.888   -6.434  7.398   1.00 9.90  ? 193 TYR B OH  1 
ATOM   3716 N  N   . ARG B 1 194 ? 14.224  -5.780  9.825   1.00 12.00 ? 194 ARG B N   1 
ATOM   3717 C  CA  . ARG B 1 194 ? 13.734  -5.221  11.067  1.00 14.21 ? 194 ARG B CA  1 
ATOM   3718 C  C   . ARG B 1 194 ? 12.453  -4.386  10.860  1.00 13.20 ? 194 ARG B C   1 
ATOM   3719 O  O   . ARG B 1 194 ? 12.421  -3.433  10.103  1.00 11.71 ? 194 ARG B O   1 
ATOM   3720 C  CB  . ARG B 1 194 ? 14.800  -4.332  11.761  1.00 15.24 ? 194 ARG B CB  1 
ATOM   3721 C  CG  . ARG B 1 194 ? 15.997  -5.132  12.307  1.00 20.79 ? 194 ARG B CG  1 
ATOM   3722 C  CD  . ARG B 1 194 ? 17.047  -4.217  12.958  1.00 25.26 ? 194 ARG B CD  1 
ATOM   3723 N  NE  . ARG B 1 194 ? 16.586  -3.624  14.223  1.00 30.38 ? 194 ARG B NE  1 
ATOM   3724 C  CZ  . ARG B 1 194 ? 16.638  -2.309  14.489  1.00 36.38 ? 194 ARG B CZ  1 
ATOM   3725 N  NH1 . ARG B 1 194 ? 16.208  -1.827  15.658  1.00 33.49 ? 194 ARG B NH1 1 
ATOM   3726 N  NH2 . ARG B 1 194 ? 17.159  -1.469  13.584  1.00 34.03 ? 194 ARG B NH2 1 
ATOM   3727 N  N   . GLY B 1 195 ? 11.404  -4.720  11.613  1.00 13.73 ? 195 GLY B N   1 
ATOM   3728 C  CA  . GLY B 1 195 ? 10.132  -4.012  11.458  1.00 12.51 ? 195 GLY B CA  1 
ATOM   3729 C  C   . GLY B 1 195 ? 9.348   -3.967  12.742  1.00 12.41 ? 195 GLY B C   1 
ATOM   3730 O  O   . GLY B 1 195 ? 9.918   -3.845  13.819  1.00 11.78 ? 195 GLY B O   1 
ATOM   3731 N  N   . SER B 1 196 ? 8.024   -4.068  12.630  1.00 10.85 ? 196 SER B N   1 
ATOM   3732 C  CA  . SER B 1 196 ? 7.096   -3.791  13.764  1.00 9.42  ? 196 SER B CA  1 
ATOM   3733 C  C   . SER B 1 196 ? 5.996   -4.813  13.866  1.00 9.69  ? 196 SER B C   1 
ATOM   3734 O  O   . SER B 1 196 ? 5.808   -5.625  12.954  1.00 8.33  ? 196 SER B O   1 
ATOM   3735 C  CB  . SER B 1 196 ? 6.366   -2.450  13.623  1.00 10.12 ? 196 SER B CB  1 
ATOM   3736 O  OG  . SER B 1 196 ? 5.460   -2.448  12.437  1.00 9.56  ? 196 SER B OG  1 
ATOM   3737 N  N   . LEU B 1 197 ? 5.214   -4.720  14.969  1.00 9.71  ? 197 LEU B N   1 
ATOM   3738 C  CA  . LEU B 1 197 ? 3.862   -5.346  14.919  1.00 9.73  ? 197 LEU B CA  1 
ATOM   3739 C  C   . LEU B 1 197 ? 3.025   -4.713  13.768  1.00 8.75  ? 197 LEU B C   1 
ATOM   3740 O  O   . LEU B 1 197 ? 3.104   -3.498  13.517  1.00 9.73  ? 197 LEU B O   1 
ATOM   3741 C  CB  . LEU B 1 197 ? 3.129   -5.103  16.258  1.00 9.99  ? 197 LEU B CB  1 
ATOM   3742 C  CG  . LEU B 1 197 ? 3.913   -5.596  17.505  1.00 11.15 ? 197 LEU B CG  1 
ATOM   3743 C  CD1 . LEU B 1 197 ? 3.178   -5.178  18.743  1.00 11.82 ? 197 LEU B CD1 1 
ATOM   3744 C  CD2 . LEU B 1 197 ? 4.106   -7.140  17.515  1.00 12.47 ? 197 LEU B CD2 1 
ATOM   3745 N  N   . THR B 1 198 ? 2.193   -5.513  13.075  1.00 8.91  ? 198 THR B N   1 
ATOM   3746 C  CA  . THR B 1 198 ? 1.393   -4.957  12.002  1.00 8.20  ? 198 THR B CA  1 
ATOM   3747 C  C   . THR B 1 198 ? -0.016  -4.532  12.519  1.00 8.60  ? 198 THR B C   1 
ATOM   3748 O  O   . THR B 1 198 ? -0.937  -4.226  11.679  1.00 8.47  ? 198 THR B O   1 
ATOM   3749 C  CB  . THR B 1 198 ? 1.168   -5.951  10.878  1.00 7.86  ? 198 THR B CB  1 
ATOM   3750 O  OG1 . THR B 1 198 ? 0.463   -7.042  11.437  1.00 7.43  ? 198 THR B OG1 1 
ATOM   3751 C  CG2 . THR B 1 198 ? 2.523   -6.468  10.212  1.00 8.29  ? 198 THR B CG2 1 
ATOM   3752 N  N   . THR B 1 199 ? -0.236  -4.592  13.836  1.00 9.32  ? 199 THR B N   1 
ATOM   3753 C  CA  . THR B 1 199 ? -1.443  -4.033  14.442  1.00 10.83 ? 199 THR B CA  1 
ATOM   3754 C  C   . THR B 1 199 ? -1.031  -3.159  15.596  1.00 10.74 ? 199 THR B C   1 
ATOM   3755 O  O   . THR B 1 199 ? 0.137   -3.254  16.063  1.00 11.80 ? 199 THR B O   1 
ATOM   3756 C  CB  . THR B 1 199 ? -2.478  -5.077  15.016  1.00 12.13 ? 199 THR B CB  1 
ATOM   3757 O  OG1 . THR B 1 199 ? -1.988  -5.587  16.256  1.00 14.17 ? 199 THR B OG1 1 
ATOM   3758 C  CG2 . THR B 1 199 ? -2.784  -6.218  14.063  1.00 13.52 ? 199 THR B CG2 1 
ATOM   3759 N  N   . PRO B 1 200 ? -1.976  -2.319  16.096  1.00 10.67 ? 200 PRO B N   1 
ATOM   3760 C  CA  . PRO B 1 200 ? -1.722  -1.604  17.336  1.00 10.49 ? 200 PRO B CA  1 
ATOM   3761 C  C   . PRO B 1 200 ? -1.311  -2.590  18.413  1.00 10.64 ? 200 PRO B C   1 
ATOM   3762 O  O   . PRO B 1 200 ? -1.868  -3.712  18.493  1.00 10.96 ? 200 PRO B O   1 
ATOM   3763 C  CB  . PRO B 1 200 ? -3.100  -0.974  17.686  1.00 10.66 ? 200 PRO B CB  1 
ATOM   3764 C  CG  . PRO B 1 200 ? -3.704  -0.687  16.335  1.00 10.81 ? 200 PRO B CG  1 
ATOM   3765 C  CD  . PRO B 1 200 ? -3.253  -1.880  15.477  1.00 11.28 ? 200 PRO B CD  1 
ATOM   3766 N  N   . PRO B 1 201 ? -0.336  -2.198  19.243  1.00 10.22 ? 201 PRO B N   1 
ATOM   3767 C  CA  . PRO B 1 201 ? 0.331   -0.887  19.319  1.00 10.18 ? 201 PRO B CA  1 
ATOM   3768 C  C   . PRO B 1 201 ? 1.494   -0.595  18.300  1.00 10.70 ? 201 PRO B C   1 
ATOM   3769 O  O   . PRO B 1 201 ? 2.215   0.435   18.504  1.00 10.60 ? 201 PRO B O   1 
ATOM   3770 C  CB  . PRO B 1 201 ? 0.956   -0.937  20.741  1.00 11.43 ? 201 PRO B CB  1 
ATOM   3771 C  CG  . PRO B 1 201 ? 1.278   -2.405  20.915  1.00 11.12 ? 201 PRO B CG  1 
ATOM   3772 C  CD  . PRO B 1 201 ? 0.094   -3.136  20.303  1.00 11.12 ? 201 PRO B CD  1 
ATOM   3773 N  N   . CYS B 1 202 ? 1.789   -1.528  17.370  1.00 10.42 ? 202 CYS B N   1 
ATOM   3774 C  CA  . CYS B 1 202 ? 2.782   -1.340  16.222  1.00 11.46 ? 202 CYS B CA  1 
ATOM   3775 C  C   . CYS B 1 202 ? 4.251   -1.110  16.736  1.00 11.20 ? 202 CYS B C   1 
ATOM   3776 O  O   . CYS B 1 202 ? 5.024   -0.394  16.082  1.00 10.73 ? 202 CYS B O   1 
ATOM   3777 C  CB  . CYS B 1 202 ? 2.403   -0.122  15.333  1.00 11.29 ? 202 CYS B CB  1 
ATOM   3778 S  SG  . CYS B 1 202 ? 0.711   0.007   14.643  1.00 12.14 ? 202 CYS B SG  1 
ATOM   3779 N  N   . ASN B 1 203 ? 4.572   -1.654  17.911  1.00 10.81 ? 203 ASN B N   1 
ATOM   3780 C  CA  . ASN B 1 203 ? 5.926   -1.589  18.454  1.00 10.80 ? 203 ASN B CA  1 
ATOM   3781 C  C   . ASN B 1 203 ? 6.984   -1.969  17.394  1.00 11.00 ? 203 ASN B C   1 
ATOM   3782 O  O   . ASN B 1 203 ? 6.889   -3.025  16.765  1.00 10.03 ? 203 ASN B O   1 
ATOM   3783 C  CB  . ASN B 1 203 ? 6.120   -2.497  19.678  1.00 11.39 ? 203 ASN B CB  1 
ATOM   3784 C  CG  . ASN B 1 203 ? 5.090   -2.259  20.779  1.00 11.08 ? 203 ASN B CG  1 
ATOM   3785 O  OD1 . ASN B 1 203 ? 4.494   -1.190  20.915  1.00 11.66 ? 203 ASN B OD1 1 
ATOM   3786 N  ND2 . ASN B 1 203 ? 4.849   -3.298  21.570  1.00 11.77 ? 203 ASN B ND2 1 
ATOM   3787 N  N   . PRO B 1 204 ? 7.998   -1.080  17.209  1.00 10.93 ? 204 PRO B N   1 
ATOM   3788 C  CA  . PRO B 1 204 ? 9.055   -1.316  16.206  1.00 11.08 ? 204 PRO B CA  1 
ATOM   3789 C  C   . PRO B 1 204 ? 10.072  -2.298  16.805  1.00 12.72 ? 204 PRO B C   1 
ATOM   3790 O  O   . PRO B 1 204 ? 11.281  -1.974  16.927  1.00 11.78 ? 204 PRO B O   1 
ATOM   3791 C  CB  . PRO B 1 204 ? 9.645   0.121   16.018  1.00 10.93 ? 204 PRO B CB  1 
ATOM   3792 C  CG  . PRO B 1 204 ? 9.511   0.735   17.365  1.00 10.93 ? 204 PRO B CG  1 
ATOM   3793 C  CD  . PRO B 1 204 ? 8.106   0.261   17.802  1.00 10.95 ? 204 PRO B CD  1 
ATOM   3794 N  N   . THR B 1 205 ? 9.605   -3.491  17.166  1.00 12.83 ? 205 THR B N   1 
ATOM   3795 C  CA  . THR B 1 205 ? 10.414  -4.378  17.991  1.00 14.20 ? 205 THR B CA  1 
ATOM   3796 C  C   . THR B 1 205 ? 10.522  -5.748  17.401  1.00 13.03 ? 205 THR B C   1 
ATOM   3797 O  O   . THR B 1 205 ? 10.982  -6.659  18.109  1.00 13.23 ? 205 THR B O   1 
ATOM   3798 C  CB  . THR B 1 205 ? 9.822   -4.555  19.407  1.00 13.11 ? 205 THR B CB  1 
ATOM   3799 O  OG1 . THR B 1 205 ? 8.454   -4.976  19.278  1.00 12.87 ? 205 THR B OG1 1 
ATOM   3800 C  CG2 . THR B 1 205 ? 9.913   -3.255  20.191  1.00 12.48 ? 205 THR B CG2 1 
ATOM   3801 N  N   . VAL B 1 206 ? 10.127  -5.917  16.126  1.00 12.41 ? 206 VAL B N   1 
ATOM   3802 C  CA  . VAL B 1 206 ? 10.067  -7.239  15.508  1.00 11.55 ? 206 VAL B CA  1 
ATOM   3803 C  C   . VAL B 1 206 ? 11.158  -7.573  14.497  1.00 11.44 ? 206 VAL B C   1 
ATOM   3804 O  O   . VAL B 1 206 ? 11.406  -6.822  13.575  1.00 11.61 ? 206 VAL B O   1 
ATOM   3805 C  CB  . VAL B 1 206 ? 8.667   -7.511  14.757  1.00 11.56 ? 206 VAL B CB  1 
ATOM   3806 C  CG1 . VAL B 1 206 ? 8.628   -8.890  14.083  1.00 11.89 ? 206 VAL B CG1 1 
ATOM   3807 C  CG2 . VAL B 1 206 ? 7.478   -7.358  15.702  1.00 13.05 ? 206 VAL B CG2 1 
ATOM   3808 N  N   . LEU B 1 207 ? 11.743  -8.761  14.608  1.00 11.84 ? 207 LEU B N   1 
ATOM   3809 C  CA  . LEU B 1 207 ? 12.653  -9.273  13.575  1.00 12.57 ? 207 LEU B CA  1 
ATOM   3810 C  C   . LEU B 1 207 ? 11.788  -10.190 12.679  1.00 11.63 ? 207 LEU B C   1 
ATOM   3811 O  O   . LEU B 1 207 ? 11.330  -11.244 13.133  1.00 11.45 ? 207 LEU B O   1 
ATOM   3812 C  CB  . LEU B 1 207 ? 13.807  -10.063 14.215  1.00 14.34 ? 207 LEU B CB  1 
ATOM   3813 C  CG  . LEU B 1 207 ? 14.961  -10.446 13.228  1.00 16.21 ? 207 LEU B CG  1 
ATOM   3814 C  CD1 . LEU B 1 207 ? 15.436  -9.322  12.311  1.00 16.57 ? 207 LEU B CD1 1 
ATOM   3815 C  CD2 . LEU B 1 207 ? 16.160  -10.943 14.044  1.00 19.14 ? 207 LEU B CD2 1 
ATOM   3816 N  N   . TRP B 1 208 ? 11.603  -9.802  11.420  1.00 11.17 ? 208 TRP B N   1 
ATOM   3817 C  CA  . TRP B 1 208 ? 10.726  -10.535 10.487  1.00 10.28 ? 208 TRP B CA  1 
ATOM   3818 C  C   . TRP B 1 208 ? 11.505  -11.525 9.657   1.00 10.64 ? 208 TRP B C   1 
ATOM   3819 O  O   . TRP B 1 208 ? 12.554  -11.177 9.152   1.00 10.41 ? 208 TRP B O   1 
ATOM   3820 C  CB  . TRP B 1 208 ? 10.041  -9.536  9.556   1.00 9.65  ? 208 TRP B CB  1 
ATOM   3821 C  CG  . TRP B 1 208 ? 8.841   -8.877  10.243  1.00 9.52  ? 208 TRP B CG  1 
ATOM   3822 C  CD1 . TRP B 1 208 ? 8.766   -7.612  10.788  1.00 8.99  ? 208 TRP B CD1 1 
ATOM   3823 C  CD2 . TRP B 1 208 ? 7.493   -9.439  10.363  1.00 9.00  ? 208 TRP B CD2 1 
ATOM   3824 N  NE1 . TRP B 1 208 ? 7.538   -7.370  11.337  1.00 8.70  ? 208 TRP B NE1 1 
ATOM   3825 C  CE2 . TRP B 1 208 ? 6.708   -8.442  11.102  1.00 9.09  ? 208 TRP B CE2 1 
ATOM   3826 C  CE3 . TRP B 1 208 ? 6.895   -10.674 10.007  1.00 8.63  ? 208 TRP B CE3 1 
ATOM   3827 C  CZ2 . TRP B 1 208 ? 5.385   -8.656  11.444  1.00 9.79  ? 208 TRP B CZ2 1 
ATOM   3828 C  CZ3 . TRP B 1 208 ? 5.559   -10.881 10.351  1.00 8.70  ? 208 TRP B CZ3 1 
ATOM   3829 C  CH2 . TRP B 1 208 ? 4.816   -9.894  11.073  1.00 8.70  ? 208 TRP B CH2 1 
ATOM   3830 N  N   . THR B 1 209 ? 10.999  -12.763 9.526   1.00 10.20 ? 209 THR B N   1 
ATOM   3831 C  CA  . THR B 1 209 ? 11.512  -13.707 8.582   1.00 11.14 ? 209 THR B CA  1 
ATOM   3832 C  C   . THR B 1 209 ? 10.269  -14.086 7.766   1.00 11.78 ? 209 THR B C   1 
ATOM   3833 O  O   . THR B 1 209 ? 9.353   -14.667 8.325   1.00 12.16 ? 209 THR B O   1 
ATOM   3834 C  CB  . THR B 1 209 ? 12.074  -14.957 9.300   1.00 11.01 ? 209 THR B CB  1 
ATOM   3835 O  OG1 . THR B 1 209 ? 13.197  -14.569 10.154  1.00 11.96 ? 209 THR B OG1 1 
ATOM   3836 C  CG2 . THR B 1 209 ? 12.535  -16.033 8.276   1.00 11.90 ? 209 THR B CG2 1 
ATOM   3837 N  N   . VAL B 1 210 ? 10.250  -13.737 6.480   1.00 12.21 ? 210 VAL B N   1 
ATOM   3838 C  CA  . VAL B 1 210 ? 9.167   -14.133 5.580   1.00 10.58 ? 210 VAL B CA  1 
ATOM   3839 C  C   . VAL B 1 210 ? 9.713   -15.215 4.641   1.00 11.65 ? 210 VAL B C   1 
ATOM   3840 O  O   . VAL B 1 210 ? 10.619  -14.967 3.873   1.00 11.69 ? 210 VAL B O   1 
ATOM   3841 C  CB  . VAL B 1 210 ? 8.656   -12.908 4.722   1.00 10.96 ? 210 VAL B CB  1 
ATOM   3842 C  CG1 . VAL B 1 210 ? 7.471   -13.348 3.833   1.00 9.16  ? 210 VAL B CG1 1 
ATOM   3843 C  CG2 . VAL B 1 210 ? 8.220   -11.694 5.563   1.00 10.30 ? 210 VAL B CG2 1 
ATOM   3844 N  N   . PHE B 1 211 ? 9.151   -16.429 4.660   1.00 11.64 ? 211 PHE B N   1 
ATOM   3845 C  CA  . PHE B 1 211 ? 9.706   -17.501 3.828   1.00 12.39 ? 211 PHE B CA  1 
ATOM   3846 C  C   . PHE B 1 211 ? 9.422   -17.209 2.350   1.00 12.08 ? 211 PHE B C   1 
ATOM   3847 O  O   . PHE B 1 211 ? 8.413   -16.610 2.036   1.00 13.96 ? 211 PHE B O   1 
ATOM   3848 C  CB  . PHE B 1 211 ? 9.165   -18.888 4.260   1.00 12.43 ? 211 PHE B CB  1 
ATOM   3849 C  CG  . PHE B 1 211 ? 9.536   -19.265 5.687   1.00 13.04 ? 211 PHE B CG  1 
ATOM   3850 C  CD1 . PHE B 1 211 ? 8.574   -19.302 6.690   1.00 13.02 ? 211 PHE B CD1 1 
ATOM   3851 C  CD2 . PHE B 1 211 ? 10.860  -19.552 6.026   1.00 13.76 ? 211 PHE B CD2 1 
ATOM   3852 C  CE1 . PHE B 1 211 ? 8.921   -19.636 8.005   1.00 15.19 ? 211 PHE B CE1 1 
ATOM   3853 C  CE2 . PHE B 1 211 ? 11.215  -19.876 7.345   1.00 13.42 ? 211 PHE B CE2 1 
ATOM   3854 C  CZ  . PHE B 1 211 ? 10.244  -19.891 8.339   1.00 14.91 ? 211 PHE B CZ  1 
ATOM   3855 N  N   . ARG B 1 212 ? 10.332  -17.608 1.456   1.00 11.48 ? 212 ARG B N   1 
ATOM   3856 C  CA  . ARG B 1 212 ? 10.182  -17.278 0.061   1.00 12.45 ? 212 ARG B CA  1 
ATOM   3857 C  C   . ARG B 1 212 ? 9.033   -18.077 -0.545  1.00 13.66 ? 212 ARG B C   1 
ATOM   3858 O  O   . ARG B 1 212 ? 8.349   -17.594 -1.419  1.00 12.73 ? 212 ARG B O   1 
ATOM   3859 C  CB  . ARG B 1 212 ? 11.507  -17.640 -0.661  1.00 13.60 ? 212 ARG B CB  1 
ATOM   3860 C  CG  . ARG B 1 212 ? 11.586  -17.184 -2.115  1.00 14.49 ? 212 ARG B CG  1 
ATOM   3861 C  CD  . ARG B 1 212 ? 12.674  -17.929 -2.907  1.00 16.99 ? 212 ARG B CD  1 
ATOM   3862 N  NE  . ARG B 1 212 ? 12.852  -17.339 -4.238  1.00 18.19 ? 212 ARG B NE  1 
ATOM   3863 C  CZ  . ARG B 1 212 ? 13.875  -17.579 -5.076  1.00 21.43 ? 212 ARG B CZ  1 
ATOM   3864 N  NH1 . ARG B 1 212 ? 14.839  -18.433 -4.766  1.00 22.55 ? 212 ARG B NH1 1 
ATOM   3865 N  NH2 . ARG B 1 212 ? 13.932  -16.939 -6.256  1.00 21.88 ? 212 ARG B NH2 1 
ATOM   3866 N  N   . ASN B 1 213 ? 8.868   -19.331 -0.126  1.00 13.83 ? 213 ASN B N   1 
ATOM   3867 C  CA  . ASN B 1 213 ? 7.888   -20.253 -0.793  1.00 14.27 ? 213 ASN B CA  1 
ATOM   3868 C  C   . ASN B 1 213 ? 6.559   -20.286 -0.028  1.00 13.88 ? 213 ASN B C   1 
ATOM   3869 O  O   . ASN B 1 213 ? 6.560   -20.314 1.197   1.00 13.57 ? 213 ASN B O   1 
ATOM   3870 C  CB  . ASN B 1 213 ? 8.446   -21.699 -0.952  1.00 16.26 ? 213 ASN B CB  1 
ATOM   3871 C  CG  . ASN B 1 213 ? 9.725   -21.772 -1.826  1.00 18.26 ? 213 ASN B CG  1 
ATOM   3872 O  OD1 . ASN B 1 213 ? 9.830   -21.158 -2.888  1.00 20.08 ? 213 ASN B OD1 1 
ATOM   3873 N  ND2 . ASN B 1 213 ? 10.707  -22.507 -1.349  1.00 18.41 ? 213 ASN B ND2 1 
ATOM   3874 N  N   . PRO B 1 214 ? 5.414   -20.210 -0.758  1.00 15.25 ? 214 PRO B N   1 
ATOM   3875 C  CA  . PRO B 1 214 ? 4.083   -20.179 -0.173  1.00 14.45 ? 214 PRO B CA  1 
ATOM   3876 C  C   . PRO B 1 214 ? 3.618   -21.623 0.083   1.00 13.55 ? 214 PRO B C   1 
ATOM   3877 O  O   . PRO B 1 214 ? 4.164   -22.604 -0.493  1.00 14.02 ? 214 PRO B O   1 
ATOM   3878 C  CB  . PRO B 1 214 ? 3.202   -19.554 -1.312  1.00 15.43 ? 214 PRO B CB  1 
ATOM   3879 C  CG  . PRO B 1 214 ? 3.894   -20.030 -2.574  1.00 15.68 ? 214 PRO B CG  1 
ATOM   3880 C  CD  . PRO B 1 214 ? 5.378   -20.047 -2.232  1.00 14.17 ? 214 PRO B CD  1 
ATOM   3881 N  N   . VAL B 1 215 ? 2.649   -21.750 0.965   1.00 12.20 ? 215 VAL B N   1 
ATOM   3882 C  CA  . VAL B 1 215 ? 1.919   -23.008 1.104   1.00 11.57 ? 215 VAL B CA  1 
ATOM   3883 C  C   . VAL B 1 215 ? 0.619   -22.861 0.347   1.00 12.31 ? 215 VAL B C   1 
ATOM   3884 O  O   . VAL B 1 215 ? 0.186   -21.694 0.086   1.00 12.57 ? 215 VAL B O   1 
ATOM   3885 C  CB  . VAL B 1 215 ? 1.717   -23.418 2.557   1.00 11.00 ? 215 VAL B CB  1 
ATOM   3886 C  CG1 . VAL B 1 215 ? 3.091   -23.476 3.261   1.00 9.48  ? 215 VAL B CG1 1 
ATOM   3887 C  CG2 . VAL B 1 215 ? 0.682   -22.495 3.277   1.00 9.84  ? 215 VAL B CG2 1 
ATOM   3888 N  N   . GLN B 1 216 ? -0.054  -23.992 0.142   1.00 13.41 ? 216 GLN B N   1 
ATOM   3889 C  CA  . GLN B 1 216 ? -1.421  -24.074 -0.487  1.00 15.34 ? 216 GLN B CA  1 
ATOM   3890 C  C   . GLN B 1 216 ? -2.493  -24.561 0.482   1.00 15.73 ? 216 GLN B C   1 
ATOM   3891 O  O   . GLN B 1 216 ? -2.261  -25.473 1.289   1.00 16.00 ? 216 GLN B O   1 
ATOM   3892 C  CB  . GLN B 1 216 ? -1.443  -24.975 -1.729  1.00 18.89 ? 216 GLN B CB  1 
ATOM   3893 C  CG  . GLN B 1 216 ? -0.593  -24.462 -2.885  1.00 21.91 ? 216 GLN B CG  1 
ATOM   3894 C  CD  . GLN B 1 216 ? -0.682  -25.257 -4.180  1.00 25.23 ? 216 GLN B CD  1 
ATOM   3895 O  OE1 . GLN B 1 216 ? -0.175  -24.793 -5.207  1.00 31.64 ? 216 GLN B OE1 1 
ATOM   3896 N  NE2 . GLN B 1 216 ? -1.303  -26.458 -4.160  1.00 24.29 ? 216 GLN B NE2 1 
ATOM   3897 N  N   . ILE B 1 217 ? -3.656  -23.895 0.446   1.00 15.97 ? 217 ILE B N   1 
ATOM   3898 C  CA  . ILE B 1 217 ? -4.876  -24.396 1.109   1.00 13.26 ? 217 ILE B CA  1 
ATOM   3899 C  C   . ILE B 1 217 ? -5.948  -24.444 0.009   1.00 13.60 ? 217 ILE B C   1 
ATOM   3900 O  O   . ILE B 1 217 ? -5.833  -23.690 -0.967  1.00 13.37 ? 217 ILE B O   1 
ATOM   3901 C  CB  . ILE B 1 217 ? -5.331  -23.580 2.321   1.00 12.92 ? 217 ILE B CB  1 
ATOM   3902 C  CG1 . ILE B 1 217 ? -5.706  -22.129 1.954   1.00 13.67 ? 217 ILE B CG1 1 
ATOM   3903 C  CG2 . ILE B 1 217 ? -4.296  -23.575 3.445   1.00 12.39 ? 217 ILE B CG2 1 
ATOM   3904 C  CD1 . ILE B 1 217 ? -6.367  -21.451 3.157   1.00 13.09 ? 217 ILE B CD1 1 
ATOM   3905 N  N   . SER B 1 218 ? -6.948  -25.332 0.133   1.00 14.18 ? 218 SER B N   1 
ATOM   3906 C  CA  . SER B 1 218 ? -8.041  -25.329 -0.876  1.00 14.99 ? 218 SER B CA  1 
ATOM   3907 C  C   . SER B 1 218 ? -8.901  -24.046 -0.886  1.00 16.55 ? 218 SER B C   1 
ATOM   3908 O  O   . SER B 1 218 ? -8.902  -23.224 0.063   1.00 15.28 ? 218 SER B O   1 
ATOM   3909 C  CB  . SER B 1 218 ? -8.956  -26.557 -0.782  1.00 15.16 ? 218 SER B CB  1 
ATOM   3910 O  OG  . SER B 1 218 ? -9.759  -26.506 0.408   1.00 14.27 ? 218 SER B OG  1 
ATOM   3911 N  N   . GLN B 1 219 ? -9.672  -23.900 -1.967  1.00 17.94 ? 219 GLN B N   1 
ATOM   3912 C  CA  . GLN B 1 219 ? -10.636 -22.814 -2.074  1.00 17.23 ? 219 GLN B CA  1 
ATOM   3913 C  C   . GLN B 1 219 ? -11.620 -22.915 -0.983  1.00 17.28 ? 219 GLN B C   1 
ATOM   3914 O  O   . GLN B 1 219 ? -12.059 -21.906 -0.486  1.00 16.91 ? 219 GLN B O   1 
ATOM   3915 C  CB  . GLN B 1 219 ? -11.403 -22.932 -3.385  1.00 21.38 ? 219 GLN B CB  1 
ATOM   3916 C  CG  . GLN B 1 219 ? -10.713 -22.345 -4.582  1.00 26.50 ? 219 GLN B CG  1 
ATOM   3917 C  CD  . GLN B 1 219 ? -11.701 -22.236 -5.733  1.00 29.61 ? 219 GLN B CD  1 
ATOM   3918 O  OE1 . GLN B 1 219 ? -12.439 -23.204 -6.033  1.00 28.98 ? 219 GLN B OE1 1 
ATOM   3919 N  NE2 . GLN B 1 219 ? -11.787 -21.037 -6.323  1.00 30.54 ? 219 GLN B NE2 1 
ATOM   3920 N  N   . GLU B 1 220 ? -11.985 -24.152 -0.591  1.00 17.47 ? 220 GLU B N   1 
ATOM   3921 C  CA  . GLU B 1 220 ? -13.039 -24.303 0.375   1.00 18.00 ? 220 GLU B CA  1 
ATOM   3922 C  C   . GLU B 1 220 ? -12.530 -23.938 1.745   1.00 14.68 ? 220 GLU B C   1 
ATOM   3923 O  O   . GLU B 1 220 ? -13.271 -23.322 2.490   1.00 15.06 ? 220 GLU B O   1 
ATOM   3924 C  CB  . GLU B 1 220 ? -13.651 -25.729 0.362   1.00 22.37 ? 220 GLU B CB  1 
ATOM   3925 C  CG  . GLU B 1 220 ? -14.363 -26.022 -0.946  1.00 25.88 ? 220 GLU B CG  1 
ATOM   3926 C  CD  . GLU B 1 220 ? -13.508 -26.681 -2.041  1.00 30.27 ? 220 GLU B CD  1 
ATOM   3927 O  OE1 . GLU B 1 220 ? -12.256 -26.513 -2.155  1.00 29.71 ? 220 GLU B OE1 1 
ATOM   3928 O  OE2 . GLU B 1 220 ? -14.126 -27.386 -2.861  1.00 34.26 ? 220 GLU B OE2 1 
ATOM   3929 N  N   . GLN B 1 221 ? -11.271 -24.284 2.040   1.00 13.27 ? 221 GLN B N   1 
ATOM   3930 C  CA  . GLN B 1 221 ? -10.609 -23.923 3.304   1.00 13.23 ? 221 GLN B CA  1 
ATOM   3931 C  C   . GLN B 1 221 ? -10.470 -22.392 3.410   1.00 13.16 ? 221 GLN B C   1 
ATOM   3932 O  O   . GLN B 1 221 ? -10.720 -21.825 4.446   1.00 12.54 ? 221 GLN B O   1 
ATOM   3933 C  CB  . GLN B 1 221 ? -9.210  -24.518 3.390   1.00 13.25 ? 221 GLN B CB  1 
ATOM   3934 C  CG  . GLN B 1 221 ? -9.222  -25.998 3.752   1.00 13.34 ? 221 GLN B CG  1 
ATOM   3935 C  CD  . GLN B 1 221 ? -7.837  -26.577 3.847   1.00 13.47 ? 221 GLN B CD  1 
ATOM   3936 O  OE1 . GLN B 1 221 ? -7.083  -26.579 2.872   1.00 13.48 ? 221 GLN B OE1 1 
ATOM   3937 N  NE2 . GLN B 1 221 ? -7.486  -27.083 5.031   1.00 13.50 ? 221 GLN B NE2 1 
ATOM   3938 N  N   . LEU B 1 222 ? -10.035 -21.768 2.338   1.00 13.45 ? 222 LEU B N   1 
ATOM   3939 C  CA  . LEU B 1 222 ? -9.928  -20.302 2.320   1.00 13.07 ? 222 LEU B CA  1 
ATOM   3940 C  C   . LEU B 1 222 ? -11.304 -19.609 2.518   1.00 13.98 ? 222 LEU B C   1 
ATOM   3941 O  O   . LEU B 1 222 ? -11.414 -18.630 3.291   1.00 12.96 ? 222 LEU B O   1 
ATOM   3942 C  CB  . LEU B 1 222 ? -9.194  -19.841 1.048   1.00 12.49 ? 222 LEU B CB  1 
ATOM   3943 C  CG  . LEU B 1 222 ? -9.047  -18.331 0.889   1.00 13.27 ? 222 LEU B CG  1 
ATOM   3944 C  CD1 . LEU B 1 222 ? -7.976  -17.850 1.899   1.00 12.27 ? 222 LEU B CD1 1 
ATOM   3945 C  CD2 . LEU B 1 222 ? -8.637  -17.979 -0.554  1.00 13.94 ? 222 LEU B CD2 1 
ATOM   3946 N  N   . LEU B 1 223 ? -12.355 -20.101 1.825   1.00 12.04 ? 223 LEU B N   1 
ATOM   3947 C  CA  . LEU B 1 223 ? -13.665 -19.523 1.966   1.00 11.74 ? 223 LEU B CA  1 
ATOM   3948 C  C   . LEU B 1 223 ? -14.189 -19.679 3.432   1.00 12.27 ? 223 LEU B C   1 
ATOM   3949 O  O   . LEU B 1 223 ? -14.770 -18.748 3.964   1.00 12.09 ? 223 LEU B O   1 
ATOM   3950 C  CB  . LEU B 1 223 ? -14.648 -20.125 0.949   1.00 12.06 ? 223 LEU B CB  1 
ATOM   3951 C  CG  . LEU B 1 223 ? -16.041 -19.543 0.935   1.00 13.36 ? 223 LEU B CG  1 
ATOM   3952 C  CD1 . LEU B 1 223 ? -15.967 -18.158 0.342   1.00 13.30 ? 223 LEU B CD1 1 
ATOM   3953 C  CD2 . LEU B 1 223 ? -17.036 -20.395 0.127   1.00 13.37 ? 223 LEU B CD2 1 
ATOM   3954 N  N   . ALA B 1 224 ? -13.888 -20.827 4.063   1.00 12.21 ? 224 ALA B N   1 
ATOM   3955 C  CA  . ALA B 1 224 ? -14.239 -21.098 5.441   1.00 11.98 ? 224 ALA B CA  1 
ATOM   3956 C  C   . ALA B 1 224 ? -13.621 -20.118 6.364   1.00 12.24 ? 224 ALA B C   1 
ATOM   3957 O  O   . ALA B 1 224 ? -14.311 -19.630 7.263   1.00 12.61 ? 224 ALA B O   1 
ATOM   3958 C  CB  . ALA B 1 224 ? -13.845 -22.509 5.864   1.00 11.42 ? 224 ALA B CB  1 
ATOM   3959 N  N   . LEU B 1 225 ? -12.340 -19.829 6.140   1.00 12.24 ? 225 LEU B N   1 
ATOM   3960 C  CA  . LEU B 1 225 ? -11.629 -18.888 6.994   1.00 10.76 ? 225 LEU B CA  1 
ATOM   3961 C  C   . LEU B 1 225 ? -12.188 -17.458 6.831   1.00 10.41 ? 225 LEU B C   1 
ATOM   3962 O  O   . LEU B 1 225 ? -12.413 -16.764 7.811   1.00 10.93 ? 225 LEU B O   1 
ATOM   3963 C  CB  . LEU B 1 225 ? -10.116 -18.919 6.694   1.00 10.91 ? 225 LEU B CB  1 
ATOM   3964 C  CG  . LEU B 1 225 ? -9.245  -17.952 7.518   1.00 11.10 ? 225 LEU B CG  1 
ATOM   3965 C  CD1 . LEU B 1 225 ? -9.306  -18.172 9.027   1.00 11.07 ? 225 LEU B CD1 1 
ATOM   3966 C  CD2 . LEU B 1 225 ? -7.788  -17.955 7.025   1.00 11.49 ? 225 LEU B CD2 1 
ATOM   3967 N  N   . GLU B 1 226 ? -12.444 -17.056 5.602   1.00 9.87  ? 226 GLU B N   1 
ATOM   3968 C  CA  . GLU B 1 226 ? -13.025 -15.750 5.294   1.00 11.54 ? 226 GLU B CA  1 
ATOM   3969 C  C   . GLU B 1 226 ? -14.450 -15.469 5.844   1.00 11.60 ? 226 GLU B C   1 
ATOM   3970 O  O   . GLU B 1 226 ? -14.837 -14.291 5.924   1.00 12.08 ? 226 GLU B O   1 
ATOM   3971 C  CB  . GLU B 1 226 ? -13.039 -15.538 3.770   1.00 11.41 ? 226 GLU B CB  1 
ATOM   3972 C  CG  . GLU B 1 226 ? -11.621 -15.382 3.169   1.00 11.96 ? 226 GLU B CG  1 
ATOM   3973 C  CD  . GLU B 1 226 ? -11.607 -15.624 1.677   1.00 13.94 ? 226 GLU B CD  1 
ATOM   3974 O  OE1 . GLU B 1 226 ? -12.614 -16.198 1.122   1.00 15.67 ? 226 GLU B OE1 1 
ATOM   3975 O  OE2 . GLU B 1 226 ? -10.593 -15.289 1.029   1.00 12.99 ? 226 GLU B OE2 1 
ATOM   3976 N  N   . THR B 1 227 ? -15.227 -16.521 6.129   1.00 13.18 ? 227 THR B N   1 
ATOM   3977 C  CA  . THR B 1 227 ? -16.659 -16.387 6.452   1.00 12.68 ? 227 THR B CA  1 
ATOM   3978 C  C   . THR B 1 227 ? -17.036 -16.850 7.882   1.00 14.78 ? 227 THR B C   1 
ATOM   3979 O  O   . THR B 1 227 ? -18.222 -16.766 8.262   1.00 14.79 ? 227 THR B O   1 
ATOM   3980 C  CB  . THR B 1 227 ? -17.530 -17.169 5.454   1.00 13.22 ? 227 THR B CB  1 
ATOM   3981 O  OG1 . THR B 1 227 ? -17.104 -18.548 5.411   1.00 13.31 ? 227 THR B OG1 1 
ATOM   3982 C  CG2 . THR B 1 227 ? -17.414 -16.503 4.003   1.00 12.86 ? 227 THR B CG2 1 
ATOM   3983 N  N   . ALA B 1 228 ? -16.071 -17.385 8.640   1.00 13.82 ? 228 ALA B N   1 
ATOM   3984 C  CA  . ALA B 1 228 ? -16.372 -18.027 9.967   1.00 13.61 ? 228 ALA B CA  1 
ATOM   3985 C  C   . ALA B 1 228 ? -16.561 -17.082 11.119  1.00 13.88 ? 228 ALA B C   1 
ATOM   3986 O  O   . ALA B 1 228 ? -17.402 -17.321 12.058  1.00 14.90 ? 228 ALA B O   1 
ATOM   3987 C  CB  . ALA B 1 228 ? -15.289 -19.066 10.324  1.00 14.71 ? 228 ALA B CB  1 
ATOM   3988 N  N   . LEU B 1 229 ? -15.797 -15.970 11.077  1.00 13.39 ? 229 LEU B N   1 
ATOM   3989 C  CA  . LEU B 1 229 ? -15.578 -15.204 12.271  1.00 12.75 ? 229 LEU B CA  1 
ATOM   3990 C  C   . LEU B 1 229 ? -16.155 -13.802 12.194  1.00 13.03 ? 229 LEU B C   1 
ATOM   3991 O  O   . LEU B 1 229 ? -16.361 -13.227 11.077  1.00 12.53 ? 229 LEU B O   1 
ATOM   3992 C  CB  . LEU B 1 229 ? -14.059 -15.132 12.600  1.00 13.12 ? 229 LEU B CB  1 
ATOM   3993 C  CG  . LEU B 1 229 ? -13.251 -16.441 12.623  1.00 13.73 ? 229 LEU B CG  1 
ATOM   3994 C  CD1 . LEU B 1 229 ? -11.726 -16.219 12.873  1.00 13.09 ? 229 LEU B CD1 1 
ATOM   3995 C  CD2 . LEU B 1 229 ? -13.872 -17.458 13.590  1.00 14.54 ? 229 LEU B CD2 1 
ATOM   3996 N  N   . TYR B 1 230 ? -16.425 -13.294 13.392  1.00 12.04 ? 230 TYR B N   1 
ATOM   3997 C  CA  . TYR B 1 230 ? -16.880 -11.918 13.678  1.00 14.08 ? 230 TYR B CA  1 
ATOM   3998 C  C   . TYR B 1 230 ? -15.926 -11.207 14.633  1.00 13.61 ? 230 TYR B C   1 
ATOM   3999 O  O   . TYR B 1 230 ? -15.355 -11.847 15.525  1.00 14.19 ? 230 TYR B O   1 
ATOM   4000 C  CB  . TYR B 1 230 ? -18.308 -11.959 14.252  1.00 13.55 ? 230 TYR B CB  1 
ATOM   4001 C  CG  . TYR B 1 230 ? -19.325 -12.398 13.222  1.00 14.03 ? 230 TYR B CG  1 
ATOM   4002 C  CD1 . TYR B 1 230 ? -19.597 -13.758 13.007  1.00 15.26 ? 230 TYR B CD1 1 
ATOM   4003 C  CD2 . TYR B 1 230 ? -20.004 -11.476 12.471  1.00 16.04 ? 230 TYR B CD2 1 
ATOM   4004 C  CE1 . TYR B 1 230 ? -20.494 -14.153 12.032  1.00 16.82 ? 230 TYR B CE1 1 
ATOM   4005 C  CE2 . TYR B 1 230 ? -20.951 -11.884 11.505  1.00 16.26 ? 230 TYR B CE2 1 
ATOM   4006 C  CZ  . TYR B 1 230 ? -21.154 -13.226 11.309  1.00 17.88 ? 230 TYR B CZ  1 
ATOM   4007 O  OH  . TYR B 1 230 ? -22.032 -13.670 10.359  1.00 21.05 ? 230 TYR B OH  1 
ATOM   4008 N  N   . CYS B 1 231 ? -15.690 -9.907  14.396  1.00 14.31 ? 231 CYS B N   1 
ATOM   4009 C  CA  . CYS B 1 231 ? -14.852 -9.077  15.321  1.00 13.35 ? 231 CYS B CA  1 
ATOM   4010 C  C   . CYS B 1 231 ? -15.513 -8.728  16.652  1.00 14.26 ? 231 CYS B C   1 
ATOM   4011 O  O   . CYS B 1 231 ? -14.833 -8.193  17.582  1.00 15.77 ? 231 CYS B O   1 
ATOM   4012 C  CB  . CYS B 1 231 ? -14.581 -7.725  14.651  1.00 14.59 ? 231 CYS B CB  1 
ATOM   4013 S  SG  . CYS B 1 231 ? -13.688 -7.839  13.095  1.00 16.93 ? 231 CYS B SG  1 
ATOM   4014 N  N   . THR B 1 232 ? -16.829 -8.912  16.726  1.00 13.76 ? 232 THR B N   1 
ATOM   4015 C  CA  . THR B 1 232 ? -17.659 -8.416  17.861  1.00 14.95 ? 232 THR B CA  1 
ATOM   4016 C  C   . THR B 1 232 ? -18.051 -9.549  18.783  1.00 15.51 ? 232 THR B C   1 
ATOM   4017 O  O   . THR B 1 232 ? -18.106 -10.726 18.374  1.00 15.64 ? 232 THR B O   1 
ATOM   4018 C  CB  . THR B 1 232 ? -18.948 -7.753  17.332  1.00 16.20 ? 232 THR B CB  1 
ATOM   4019 O  OG1 . THR B 1 232 ? -19.453 -8.531  16.237  1.00 16.67 ? 232 THR B OG1 1 
ATOM   4020 C  CG2 . THR B 1 232 ? -18.656 -6.319  16.864  1.00 14.66 ? 232 THR B CG2 1 
ATOM   4021 N  N   . HIS B 1 233 ? -18.412 -9.167  20.007  1.00 19.07 ? 233 HIS B N   1 
ATOM   4022 C  CA  . HIS B 1 233 ? -18.827 -10.065 21.063  1.00 18.51 ? 233 HIS B CA  1 
ATOM   4023 C  C   . HIS B 1 233 ? -20.209 -10.579 20.708  1.00 19.89 ? 233 HIS B C   1 
ATOM   4024 O  O   . HIS B 1 233 ? -20.951 -9.933  19.939  1.00 20.18 ? 233 HIS B O   1 
ATOM   4025 C  CB  . HIS B 1 233 ? -18.918 -9.289  22.379  1.00 19.45 ? 233 HIS B CB  1 
ATOM   4026 C  CG  . HIS B 1 233 ? -17.567 -8.979  23.046  1.00 20.90 ? 233 HIS B CG  1 
ATOM   4027 N  ND1 . HIS B 1 233 ? -16.838 -9.926  23.670  1.00 21.42 ? 233 HIS B ND1 1 
ATOM   4028 C  CD2 . HIS B 1 233 ? -16.873 -7.779  23.219  1.00 21.36 ? 233 HIS B CD2 1 
ATOM   4029 C  CE1 . HIS B 1 233 ? -15.719 -9.372  24.212  1.00 22.19 ? 233 HIS B CE1 1 
ATOM   4030 N  NE2 . HIS B 1 233 ? -15.732 -8.066  23.938  1.00 20.96 ? 233 HIS B NE2 1 
ATOM   4031 N  N   . MET B 1 234 ? -20.567 -11.745 21.231  1.00 18.41 ? 234 MET B N   1 
ATOM   4032 C  CA  . MET B 1 234 ? -21.895 -12.322 20.949  1.00 23.27 ? 234 MET B CA  1 
ATOM   4033 C  C   . MET B 1 234 ? -23.136 -11.465 21.342  1.00 23.32 ? 234 MET B C   1 
ATOM   4034 O  O   . MET B 1 234 ? -24.253 -11.672 20.826  1.00 24.05 ? 234 MET B O   1 
ATOM   4035 C  CB  . MET B 1 234 ? -21.986 -13.709 21.557  1.00 25.79 ? 234 MET B CB  1 
ATOM   4036 C  CG  . MET B 1 234 ? -21.804 -13.717 23.067  1.00 26.88 ? 234 MET B CG  1 
ATOM   4037 S  SD  . MET B 1 234 ? -21.703 -15.404 23.724  1.00 36.29 ? 234 MET B SD  1 
ATOM   4038 C  CE  . MET B 1 234 ? -22.993 -16.146 22.698  1.00 28.53 ? 234 MET B CE  1 
ATOM   4039 N  N   . ASP B 1 235 ? -22.959 -10.470 22.171  1.00 24.61 ? 235 ASP B N   1 
ATOM   4040 C  CA  . ASP B 1 235 ? -24.120 -9.573  22.407  1.00 28.26 ? 235 ASP B CA  1 
ATOM   4041 C  C   . ASP B 1 235 ? -23.999 -8.129  21.838  1.00 26.35 ? 235 ASP B C   1 
ATOM   4042 O  O   . ASP B 1 235 ? -24.726 -7.216  22.266  1.00 27.64 ? 235 ASP B O   1 
ATOM   4043 C  CB  . ASP B 1 235 ? -24.527 -9.657  23.904  1.00 30.28 ? 235 ASP B CB  1 
ATOM   4044 C  CG  . ASP B 1 235 ? -24.845 -11.110 24.332  1.00 36.80 ? 235 ASP B CG  1 
ATOM   4045 O  OD1 . ASP B 1 235 ? -24.437 -11.567 25.432  1.00 42.62 ? 235 ASP B OD1 1 
ATOM   4046 O  OD2 . ASP B 1 235 ? -25.501 -11.835 23.537  1.00 39.54 ? 235 ASP B OD2 1 
ATOM   4047 N  N   . ASP B 1 236 ? -23.114 -7.932  20.851  1.00 23.24 ? 236 ASP B N   1 
ATOM   4048 C  CA  . ASP B 1 236 ? -22.945 -6.629  20.205  1.00 24.93 ? 236 ASP B CA  1 
ATOM   4049 C  C   . ASP B 1 236 ? -24.141 -6.323  19.288  1.00 25.70 ? 236 ASP B C   1 
ATOM   4050 O  O   . ASP B 1 236 ? -24.445 -7.108  18.370  1.00 24.66 ? 236 ASP B O   1 
ATOM   4051 C  CB  . ASP B 1 236 ? -21.619 -6.548  19.417  1.00 22.81 ? 236 ASP B CB  1 
ATOM   4052 C  CG  . ASP B 1 236 ? -21.147 -5.132  19.208  1.00 25.76 ? 236 ASP B CG  1 
ATOM   4053 O  OD1 . ASP B 1 236 ? -21.879 -4.329  18.576  1.00 26.52 ? 236 ASP B OD1 1 
ATOM   4054 O  OD2 . ASP B 1 236 ? -20.022 -4.804  19.669  1.00 26.65 ? 236 ASP B OD2 1 
ATOM   4055 N  N   . PRO B 1 237 ? -24.816 -5.176  19.526  1.00 27.90 ? 237 PRO B N   1 
ATOM   4056 C  CA  . PRO B 1 237 ? -25.935 -4.790  18.667  1.00 28.10 ? 237 PRO B CA  1 
ATOM   4057 C  C   . PRO B 1 237 ? -25.540 -4.389  17.221  1.00 29.37 ? 237 PRO B C   1 
ATOM   4058 O  O   . PRO B 1 237 ? -26.417 -4.358  16.326  1.00 27.26 ? 237 PRO B O   1 
ATOM   4059 C  CB  . PRO B 1 237 ? -26.537 -3.610  19.416  1.00 26.72 ? 237 PRO B CB  1 
ATOM   4060 C  CG  . PRO B 1 237 ? -25.339 -2.961  20.047  1.00 27.12 ? 237 PRO B CG  1 
ATOM   4061 C  CD  . PRO B 1 237 ? -24.476 -4.098  20.486  1.00 27.30 ? 237 PRO B CD  1 
ATOM   4062 N  N   . SER B 1 238 ? -24.251 -4.103  16.987  1.00 29.08 ? 238 SER B N   1 
ATOM   4063 C  CA  . SER B 1 238 ? -23.745 -3.854  15.620  1.00 25.66 ? 238 SER B CA  1 
ATOM   4064 C  C   . SER B 1 238 ? -22.609 -4.841  15.289  1.00 23.35 ? 238 SER B C   1 
ATOM   4065 O  O   . SER B 1 238 ? -21.429 -4.486  15.440  1.00 21.92 ? 238 SER B O   1 
ATOM   4066 C  CB  . SER B 1 238 ? -23.218 -2.426  15.472  1.00 28.28 ? 238 SER B CB  1 
ATOM   4067 O  OG  . SER B 1 238 ? -24.103 -1.495  16.045  1.00 34.55 ? 238 SER B OG  1 
ATOM   4068 N  N   . PRO B 1 239 ? -22.973 -6.061  14.831  1.00 21.35 ? 239 PRO B N   1 
ATOM   4069 C  CA  . PRO B 1 239 ? -21.991 -7.129  14.504  1.00 22.54 ? 239 PRO B CA  1 
ATOM   4070 C  C   . PRO B 1 239 ? -21.171 -6.785  13.295  1.00 22.12 ? 239 PRO B C   1 
ATOM   4071 O  O   . PRO B 1 239 ? -21.690 -6.207  12.311  1.00 20.94 ? 239 PRO B O   1 
ATOM   4072 C  CB  . PRO B 1 239 ? -22.866 -8.348  14.170  1.00 22.82 ? 239 PRO B CB  1 
ATOM   4073 C  CG  . PRO B 1 239 ? -24.235 -7.996  14.648  1.00 24.47 ? 239 PRO B CG  1 
ATOM   4074 C  CD  . PRO B 1 239 ? -24.351 -6.514  14.583  1.00 21.37 ? 239 PRO B CD  1 
ATOM   4075 N  N   . ARG B 1 240 ? -19.900 -7.165  13.306  1.00 20.59 ? 240 ARG B N   1 
ATOM   4076 C  CA  . ARG B 1 240 ? -19.080 -6.901  12.146  1.00 20.28 ? 240 ARG B CA  1 
ATOM   4077 C  C   . ARG B 1 240 ? -18.292 -8.170  11.827  1.00 19.24 ? 240 ARG B C   1 
ATOM   4078 O  O   . ARG B 1 240 ? -17.659 -8.734  12.722  1.00 16.53 ? 240 ARG B O   1 
ATOM   4079 C  CB  . ARG B 1 240 ? -18.141 -5.715  12.437  1.00 22.77 ? 240 ARG B CB  1 
ATOM   4080 C  CG  . ARG B 1 240 ? -18.828 -4.346  12.257  1.00 28.16 ? 240 ARG B CG  1 
ATOM   4081 C  CD  . ARG B 1 240 ? -18.063 -3.260  12.984  1.00 29.81 ? 240 ARG B CD  1 
ATOM   4082 N  NE  . ARG B 1 240 ? -16.702 -3.704  13.208  1.00 32.33 ? 240 ARG B NE  1 
ATOM   4083 C  CZ  . ARG B 1 240 ? -16.154 -3.900  14.403  1.00 30.83 ? 240 ARG B CZ  1 
ATOM   4084 N  NH1 . ARG B 1 240 ? -16.837 -3.619  15.485  1.00 27.48 ? 240 ARG B NH1 1 
ATOM   4085 N  NH2 . ARG B 1 240 ? -14.908 -4.338  14.491  1.00 26.43 ? 240 ARG B NH2 1 
ATOM   4086 N  N   . GLU B 1 241 ? -18.334 -8.594  10.560  1.00 17.28 ? 241 GLU B N   1 
ATOM   4087 C  CA  . GLU B 1 241 ? -17.616 -9.828  10.104  1.00 15.15 ? 241 GLU B CA  1 
ATOM   4088 C  C   . GLU B 1 241 ? -16.131 -9.602  10.144  1.00 13.08 ? 241 GLU B C   1 
ATOM   4089 O  O   . GLU B 1 241 ? -15.659 -8.481  9.876   1.00 11.87 ? 241 GLU B O   1 
ATOM   4090 C  CB  . GLU B 1 241 ? -17.977 -10.142 8.674   1.00 17.75 ? 241 GLU B CB  1 
ATOM   4091 C  CG  . GLU B 1 241 ? -19.290 -10.826 8.504   1.00 21.85 ? 241 GLU B CG  1 
ATOM   4092 C  CD  . GLU B 1 241 ? -19.972 -10.431 7.202   1.00 26.17 ? 241 GLU B CD  1 
ATOM   4093 O  OE1 . GLU B 1 241 ? -21.199 -10.554 7.209   1.00 29.87 ? 241 GLU B OE1 1 
ATOM   4094 O  OE2 . GLU B 1 241 ? -19.312 -9.960  6.226   1.00 25.80 ? 241 GLU B OE2 1 
ATOM   4095 N  N   . MET B 1 242 ? -15.372 -10.670 10.414  1.00 11.15 ? 242 MET B N   1 
ATOM   4096 C  CA  . MET B 1 242 ? -13.932 -10.592 10.438  1.00 11.17 ? 242 MET B CA  1 
ATOM   4097 C  C   . MET B 1 242 ? -13.393 -10.865 9.050   1.00 10.43 ? 242 MET B C   1 
ATOM   4098 O  O   . MET B 1 242 ? -13.123 -12.021 8.688   1.00 10.57 ? 242 MET B O   1 
ATOM   4099 C  CB  . MET B 1 242 ? -13.291 -11.492 11.531  1.00 12.45 ? 242 MET B CB  1 
ATOM   4100 C  CG  . MET B 1 242 ? -11.775 -11.210 11.697  1.00 12.63 ? 242 MET B CG  1 
ATOM   4101 S  SD  . MET B 1 242 ? -11.055 -12.336 12.919  1.00 12.85 ? 242 MET B SD  1 
ATOM   4102 C  CE  . MET B 1 242 ? -11.968 -11.901 14.377  1.00 12.20 ? 242 MET B CE  1 
ATOM   4103 N  N   A ILE B 1 243 ? -13.246 -9.790  8.277   0.50 9.84  ? 243 ILE B N   1 
ATOM   4104 N  N   B ILE B 1 243 ? -13.238 -9.796  8.274   0.50 10.22 ? 243 ILE B N   1 
ATOM   4105 C  CA  A ILE B 1 243 ? -12.708 -9.832  6.916   0.50 9.24  ? 243 ILE B CA  1 
ATOM   4106 C  CA  B ILE B 1 243 ? -12.701 -9.857  6.916   0.50 9.88  ? 243 ILE B CA  1 
ATOM   4107 C  C   A ILE B 1 243 ? -11.688 -8.702  6.683   0.50 9.53  ? 243 ILE B C   1 
ATOM   4108 C  C   B ILE B 1 243 ? -11.700 -8.708  6.675   0.50 9.90  ? 243 ILE B C   1 
ATOM   4109 O  O   A ILE B 1 243 ? -11.685 -7.704  7.414   0.50 9.52  ? 243 ILE B O   1 
ATOM   4110 O  O   B ILE B 1 243 ? -11.722 -7.702  7.394   0.50 9.83  ? 243 ILE B O   1 
ATOM   4111 C  CB  A ILE B 1 243 ? -13.840 -9.722  5.861   0.50 8.96  ? 243 ILE B CB  1 
ATOM   4112 C  CB  B ILE B 1 243 ? -13.838 -9.780  5.864   0.50 10.10 ? 243 ILE B CB  1 
ATOM   4113 C  CG1 A ILE B 1 243 ? -14.675 -8.433  6.077   0.50 8.55  ? 243 ILE B CG1 1 
ATOM   4114 C  CG1 B ILE B 1 243 ? -14.811 -8.635  6.206   0.50 10.18 ? 243 ILE B CG1 1 
ATOM   4115 C  CG2 A ILE B 1 243 ? -14.754 -10.913 5.960   0.50 8.19  ? 243 ILE B CG2 1 
ATOM   4116 C  CG2 B ILE B 1 243 ? -14.632 -11.057 5.834   0.50 9.20  ? 243 ILE B CG2 1 
ATOM   4117 C  CD1 A ILE B 1 243 ? -15.752 -8.191  5.035   0.50 8.20  ? 243 ILE B CD1 1 
ATOM   4118 C  CD1 B ILE B 1 243 ? -14.130 -7.303  6.354   0.50 11.18 ? 243 ILE B CD1 1 
ATOM   4119 N  N   . ASN B 1 244 ? -10.830 -8.861  5.673   1.00 9.37  ? 244 ASN B N   1 
ATOM   4120 C  CA  . ASN B 1 244 ? -9.775  -7.822  5.329   1.00 9.73  ? 244 ASN B CA  1 
ATOM   4121 C  C   . ASN B 1 244 ? -8.974  -7.366  6.531   1.00 9.71  ? 244 ASN B C   1 
ATOM   4122 O  O   . ASN B 1 244 ? -8.746  -6.128  6.725   1.00 8.50  ? 244 ASN B O   1 
ATOM   4123 C  CB  . ASN B 1 244 ? -10.391 -6.636  4.602   1.00 11.11 ? 244 ASN B CB  1 
ATOM   4124 C  CG  . ASN B 1 244 ? -11.275 -7.074  3.424   1.00 13.15 ? 244 ASN B CG  1 
ATOM   4125 O  OD1 . ASN B 1 244 ? -10.871 -7.915  2.658   1.00 15.06 ? 244 ASN B OD1 1 
ATOM   4126 N  ND2 . ASN B 1 244 ? -12.526 -6.549  3.344   1.00 15.07 ? 244 ASN B ND2 1 
ATOM   4127 N  N   . ASN B 1 245 ? -8.637  -8.352  7.381   1.00 9.80  ? 245 ASN B N   1 
ATOM   4128 C  CA  . ASN B 1 245 ? -7.906  -8.053  8.649   1.00 9.52  ? 245 ASN B CA  1 
ATOM   4129 C  C   . ASN B 1 245 ? -6.370  -8.007  8.392   1.00 9.45  ? 245 ASN B C   1 
ATOM   4130 O  O   . ASN B 1 245 ? -5.576  -8.674  9.064   1.00 8.83  ? 245 ASN B O   1 
ATOM   4131 C  CB  . ASN B 1 245 ? -8.311  -8.997  9.824   1.00 9.53  ? 245 ASN B CB  1 
ATOM   4132 C  CG  . ASN B 1 245 ? -7.970  -10.511 9.547   1.00 9.69  ? 245 ASN B CG  1 
ATOM   4133 O  OD1 . ASN B 1 245 ? -7.815  -10.952 8.398   1.00 9.93  ? 245 ASN B OD1 1 
ATOM   4134 N  ND2 . ASN B 1 245 ? -7.887  -11.287 10.595  1.00 10.23 ? 245 ASN B ND2 1 
ATOM   4135 N  N   . PHE B 1 246 ? -5.963  -7.272  7.361   1.00 10.42 ? 246 PHE B N   1 
ATOM   4136 C  CA  . PHE B 1 246 ? -4.527  -7.075  7.039   1.00 9.17  ? 246 PHE B CA  1 
ATOM   4137 C  C   . PHE B 1 246 ? -4.242  -5.537  6.895   1.00 8.84  ? 246 PHE B C   1 
ATOM   4138 O  O   . PHE B 1 246 ? -5.138  -4.785  6.512   1.00 9.34  ? 246 PHE B O   1 
ATOM   4139 C  CB  . PHE B 1 246 ? -4.208  -7.880  5.750   1.00 9.51  ? 246 PHE B CB  1 
ATOM   4140 C  CG  . PHE B 1 246 ? -4.890  -7.362  4.512   1.00 9.54  ? 246 PHE B CG  1 
ATOM   4141 C  CD1 . PHE B 1 246 ? -4.262  -6.371  3.720   1.00 9.17  ? 246 PHE B CD1 1 
ATOM   4142 C  CD2 . PHE B 1 246 ? -6.195  -7.797  4.142   1.00 9.57  ? 246 PHE B CD2 1 
ATOM   4143 C  CE1 . PHE B 1 246 ? -4.890  -5.829  2.617   1.00 10.08 ? 246 PHE B CE1 1 
ATOM   4144 C  CE2 . PHE B 1 246 ? -6.817  -7.241  3.004   1.00 9.63  ? 246 PHE B CE2 1 
ATOM   4145 C  CZ  . PHE B 1 246 ? -6.145  -6.291  2.224   1.00 9.66  ? 246 PHE B CZ  1 
ATOM   4146 N  N   . ARG B 1 247 ? -3.056  -5.097  7.308   1.00 7.45  ? 247 ARG B N   1 
ATOM   4147 C  CA  . ARG B 1 247 ? -2.606  -3.732  7.079   1.00 7.52  ? 247 ARG B CA  1 
ATOM   4148 C  C   . ARG B 1 247 ? -2.117  -3.508  5.629   1.00 8.15  ? 247 ARG B C   1 
ATOM   4149 O  O   . ARG B 1 247 ? -1.433  -4.395  5.036   1.00 8.67  ? 247 ARG B O   1 
ATOM   4150 C  CB  . ARG B 1 247 ? -1.499  -3.412  8.117   1.00 7.10  ? 247 ARG B CB  1 
ATOM   4151 C  CG  . ARG B 1 247 ? -1.167  -1.920  8.215   1.00 6.92  ? 247 ARG B CG  1 
ATOM   4152 C  CD  . ARG B 1 247 ? -0.054  -1.701  9.271   1.00 7.04  ? 247 ARG B CD  1 
ATOM   4153 N  NE  . ARG B 1 247 ? -0.017  -0.302  9.673   1.00 7.02  ? 247 ARG B NE  1 
ATOM   4154 C  CZ  . ARG B 1 247 ? 0.987   0.163   10.432  1.00 7.31  ? 247 ARG B CZ  1 
ATOM   4155 N  NH1 . ARG B 1 247 ? 1.998   -0.657  10.750  1.00 7.12  ? 247 ARG B NH1 1 
ATOM   4156 N  NH2 . ARG B 1 247 ? 0.945   1.410   10.850  1.00 7.20  ? 247 ARG B NH2 1 
ATOM   4157 N  N   . GLN B 1 248 ? -2.391  -2.334  5.036   1.00 8.49  ? 248 GLN B N   1 
ATOM   4158 C  CA  . GLN B 1 248 ? -1.678  -1.930  3.765   1.00 9.14  ? 248 GLN B CA  1 
ATOM   4159 C  C   . GLN B 1 248 ? -0.169  -1.915  3.924   1.00 9.23  ? 248 GLN B C   1 
ATOM   4160 O  O   . GLN B 1 248 ? 0.337   -1.701  5.044   1.00 9.70  ? 248 GLN B O   1 
ATOM   4161 C  CB  . GLN B 1 248 ? -2.101  -0.520  3.328   1.00 8.70  ? 248 GLN B CB  1 
ATOM   4162 C  CG  . GLN B 1 248 ? -3.567  -0.420  2.998   1.00 9.42  ? 248 GLN B CG  1 
ATOM   4163 C  CD  . GLN B 1 248 ? -4.003  -1.351  1.856   1.00 9.39  ? 248 GLN B CD  1 
ATOM   4164 O  OE1 . GLN B 1 248 ? -4.460  -2.507  2.064   1.00 9.22  ? 248 GLN B OE1 1 
ATOM   4165 N  NE2 . GLN B 1 248 ? -3.858  -0.862  0.639   1.00 8.89  ? 248 GLN B NE2 1 
ATOM   4166 N  N   . VAL B 1 249 ? 0.573   -2.126  2.821   1.00 9.75  ? 249 VAL B N   1 
ATOM   4167 C  CA  . VAL B 1 249 ? 2.022   -2.094  2.966   1.00 9.26  ? 249 VAL B CA  1 
ATOM   4168 C  C   . VAL B 1 249 ? 2.500   -0.673  3.240   1.00 9.13  ? 249 VAL B C   1 
ATOM   4169 O  O   . VAL B 1 249 ? 1.841   0.278   2.840   1.00 8.48  ? 249 VAL B O   1 
ATOM   4170 C  CB  . VAL B 1 249 ? 2.783   -2.674  1.750   1.00 9.89  ? 249 VAL B CB  1 
ATOM   4171 C  CG1 . VAL B 1 249 ? 2.459   -4.162  1.616   1.00 11.27 ? 249 VAL B CG1 1 
ATOM   4172 C  CG2 . VAL B 1 249 ? 2.450   -1.920  0.468   1.00 10.88 ? 249 VAL B CG2 1 
ATOM   4173 N  N   . GLN B 1 250 ? 3.666   -0.575  3.891   1.00 8.50  ? 250 GLN B N   1 
ATOM   4174 C  CA  . GLN B 1 250 ? 4.227   0.687   4.416   1.00 9.58  ? 250 GLN B CA  1 
ATOM   4175 C  C   . GLN B 1 250 ? 5.330   1.218   3.520   1.00 10.03 ? 250 GLN B C   1 
ATOM   4176 O  O   . GLN B 1 250 ? 5.975   0.445   2.866   1.00 10.71 ? 250 GLN B O   1 
ATOM   4177 C  CB  . GLN B 1 250 ? 4.827   0.433   5.837   1.00 8.54  ? 250 GLN B CB  1 
ATOM   4178 C  CG  . GLN B 1 250 ? 3.855   -0.186  6.825   1.00 7.79  ? 250 GLN B CG  1 
ATOM   4179 C  CD  . GLN B 1 250 ? 2.719   0.812   7.193   1.00 8.34  ? 250 GLN B CD  1 
ATOM   4180 O  OE1 . GLN B 1 250 ? 2.993   1.890   7.713   1.00 8.28  ? 250 GLN B OE1 1 
ATOM   4181 N  NE2 . GLN B 1 250 ? 1.471   0.489   6.827   1.00 6.80  ? 250 GLN B NE2 1 
ATOM   4182 N  N   . LYS B 1 251 ? 5.596   2.527   3.543   1.00 11.15 ? 251 LYS B N   1 
ATOM   4183 C  CA  . LYS B 1 251 ? 6.811   3.018   2.890   1.00 12.87 ? 251 LYS B CA  1 
ATOM   4184 C  C   . LYS B 1 251 ? 8.052   2.341   3.489   1.00 13.26 ? 251 LYS B C   1 
ATOM   4185 O  O   . LYS B 1 251 ? 8.105   2.052   4.697   1.00 12.54 ? 251 LYS B O   1 
ATOM   4186 C  CB  . LYS B 1 251 ? 7.010   4.537   3.080   1.00 13.67 ? 251 LYS B CB  1 
ATOM   4187 C  CG  . LYS B 1 251 ? 5.991   5.437   2.371   1.00 12.85 ? 251 LYS B CG  1 
ATOM   4188 C  CD  . LYS B 1 251 ? 6.385   5.782   0.936   1.00 12.96 ? 251 LYS B CD  1 
ATOM   4189 C  CE  . LYS B 1 251 ? 5.449   6.914   0.403   1.00 11.92 ? 251 LYS B CE  1 
ATOM   4190 N  NZ  . LYS B 1 251 ? 4.017   6.435   0.324   1.00 10.22 ? 251 LYS B NZ  1 
ATOM   4191 N  N   . PHE B 1 252 ? 9.031   2.105   2.613   1.00 14.50 ? 252 PHE B N   1 
ATOM   4192 C  CA  . PHE B 1 252 ? 10.289  1.428   2.959   1.00 17.44 ? 252 PHE B CA  1 
ATOM   4193 C  C   . PHE B 1 252 ? 11.419  1.990   2.141   1.00 20.77 ? 252 PHE B C   1 
ATOM   4194 O  O   . PHE B 1 252 ? 11.580  1.643   0.954   1.00 18.74 ? 252 PHE B O   1 
ATOM   4195 C  CB  . PHE B 1 252 ? 10.179  -0.087  2.748   1.00 17.65 ? 252 PHE B CB  1 
ATOM   4196 C  CG  . PHE B 1 252 ? 11.271  -0.863  3.416   1.00 17.40 ? 252 PHE B CG  1 
ATOM   4197 C  CD1 . PHE B 1 252 ? 11.159  -1.213  4.755   1.00 15.93 ? 252 PHE B CD1 1 
ATOM   4198 C  CD2 . PHE B 1 252 ? 12.367  -1.321  2.676   1.00 16.75 ? 252 PHE B CD2 1 
ATOM   4199 C  CE1 . PHE B 1 252 ? 12.137  -1.971  5.384   1.00 17.82 ? 252 PHE B CE1 1 
ATOM   4200 C  CE2 . PHE B 1 252 ? 13.351  -2.096  3.292   1.00 17.92 ? 252 PHE B CE2 1 
ATOM   4201 C  CZ  . PHE B 1 252 ? 13.243  -2.405  4.663   1.00 18.80 ? 252 PHE B CZ  1 
ATOM   4202 N  N   . ASP B 1 253 ? 12.205  2.864   2.794   1.00 22.64 ? 253 ASP B N   1 
ATOM   4203 C  CA  . ASP B 1 253 ? 13.056  3.853   2.073   1.00 30.76 ? 253 ASP B CA  1 
ATOM   4204 C  C   . ASP B 1 253 ? 14.426  4.003   2.710   1.00 35.04 ? 253 ASP B C   1 
ATOM   4205 O  O   . ASP B 1 253 ? 14.530  4.105   3.934   1.00 35.53 ? 253 ASP B O   1 
ATOM   4206 C  CB  . ASP B 1 253 ? 12.355  5.220   2.066   1.00 33.16 ? 253 ASP B CB  1 
ATOM   4207 C  CG  . ASP B 1 253 ? 11.313  5.363   0.910   1.00 36.75 ? 253 ASP B CG  1 
ATOM   4208 O  OD1 . ASP B 1 253 ? 11.686  5.049   -0.270  1.00 39.19 ? 253 ASP B OD1 1 
ATOM   4209 O  OD2 . ASP B 1 253 ? 10.154  5.813   1.177   1.00 30.68 ? 253 ASP B OD2 1 
ATOM   4210 N  N   . GLU B 1 254 ? 15.472  4.006   1.878   1.00 42.87 ? 254 GLU B N   1 
ATOM   4211 C  CA  . GLU B 1 254 ? 16.867  4.072   2.342   1.00 40.87 ? 254 GLU B CA  1 
ATOM   4212 C  C   . GLU B 1 254 ? 17.158  2.960   3.375   1.00 40.87 ? 254 GLU B C   1 
ATOM   4213 O  O   . GLU B 1 254 ? 17.858  3.135   4.383   1.00 39.91 ? 254 GLU B O   1 
ATOM   4214 C  CB  . GLU B 1 254 ? 17.224  5.484   2.833   1.00 46.62 ? 254 GLU B CB  1 
ATOM   4215 C  CG  . GLU B 1 254 ? 17.256  6.507   1.704   1.00 47.99 ? 254 GLU B CG  1 
ATOM   4216 C  CD  . GLU B 1 254 ? 17.249  7.956   2.188   1.00 56.13 ? 254 GLU B CD  1 
ATOM   4217 O  OE1 . GLU B 1 254 ? 16.715  8.828   1.455   1.00 53.96 ? 254 GLU B OE1 1 
ATOM   4218 O  OE2 . GLU B 1 254 ? 17.782  8.229   3.293   1.00 56.05 ? 254 GLU B OE2 1 
ATOM   4219 N  N   . ARG B 1 255 ? 16.584  1.801   3.085   1.00 40.39 ? 255 ARG B N   1 
ATOM   4220 C  CA  . ARG B 1 255 ? 16.676  0.633   3.950   1.00 36.68 ? 255 ARG B CA  1 
ATOM   4221 C  C   . ARG B 1 255 ? 16.570  -0.592  3.101   1.00 31.91 ? 255 ARG B C   1 
ATOM   4222 O  O   . ARG B 1 255 ? 16.019  -0.544  1.968   1.00 27.65 ? 255 ARG B O   1 
ATOM   4223 C  CB  . ARG B 1 255 ? 15.528  0.610   4.948   1.00 37.97 ? 255 ARG B CB  1 
ATOM   4224 C  CG  . ARG B 1 255 ? 15.932  0.814   6.396   1.00 40.15 ? 255 ARG B CG  1 
ATOM   4225 C  CD  . ARG B 1 255 ? 14.801  0.361   7.326   1.00 38.06 ? 255 ARG B CD  1 
ATOM   4226 N  NE  . ARG B 1 255 ? 13.670  1.295   7.370   1.00 38.20 ? 255 ARG B NE  1 
ATOM   4227 C  CZ  . ARG B 1 255 ? 12.425  0.947   7.704   1.00 36.13 ? 255 ARG B CZ  1 
ATOM   4228 N  NH1 . ARG B 1 255 ? 11.444  1.855   7.732   1.00 29.79 ? 255 ARG B NH1 1 
ATOM   4229 N  NH2 . ARG B 1 255 ? 12.164  -0.324  7.998   1.00 34.56 ? 255 ARG B NH2 1 
ATOM   4230 N  N   . LEU B 1 256 ? 17.070  -1.698  3.640   1.00 26.77 ? 256 LEU B N   1 
ATOM   4231 C  CA  . LEU B 1 256 ? 17.204  -2.885  2.848   1.00 22.31 ? 256 LEU B CA  1 
ATOM   4232 C  C   . LEU B 1 256 ? 16.611  -4.161  3.551   1.00 19.89 ? 256 LEU B C   1 
ATOM   4233 O  O   . LEU B 1 256 ? 16.483  -4.258  4.769   1.00 20.29 ? 256 LEU B O   1 
ATOM   4234 C  CB  . LEU B 1 256 ? 18.675  -3.045  2.380   1.00 25.11 ? 256 LEU B CB  1 
ATOM   4235 C  CG  . LEU B 1 256 ? 19.142  -2.333  1.076   1.00 26.87 ? 256 LEU B CG  1 
ATOM   4236 C  CD1 . LEU B 1 256 ? 19.072  -3.212  -0.160  1.00 29.52 ? 256 LEU B CD1 1 
ATOM   4237 C  CD2 . LEU B 1 256 ? 18.431  -1.026  0.734   1.00 27.37 ? 256 LEU B CD2 1 
ATOM   4238 N  N   . VAL B 1 257 ? 16.138  -5.065  2.726   1.00 15.80 ? 257 VAL B N   1 
ATOM   4239 C  CA  . VAL B 1 257 ? 15.668  -6.364  3.153   1.00 14.28 ? 257 VAL B CA  1 
ATOM   4240 C  C   . VAL B 1 257 ? 16.757  -7.329  2.726   1.00 14.41 ? 257 VAL B C   1 
ATOM   4241 O  O   . VAL B 1 257 ? 17.216  -7.285  1.552   1.00 16.12 ? 257 VAL B O   1 
ATOM   4242 C  CB  . VAL B 1 257 ? 14.329  -6.695  2.386   1.00 12.31 ? 257 VAL B CB  1 
ATOM   4243 C  CG1 . VAL B 1 257 ? 13.883  -8.141  2.587   1.00 11.78 ? 257 VAL B CG1 1 
ATOM   4244 C  CG2 . VAL B 1 257 ? 13.239  -5.745  2.848   1.00 11.21 ? 257 VAL B CG2 1 
ATOM   4245 N  N   . TYR B 1 258 ? 17.182  -8.226  3.621   1.00 14.57 ? 258 TYR B N   1 
ATOM   4246 C  CA  . TYR B 1 258 ? 18.237  -9.151  3.254   1.00 14.78 ? 258 TYR B CA  1 
ATOM   4247 C  C   . TYR B 1 258 ? 17.681  -10.527 2.859   1.00 14.49 ? 258 TYR B C   1 
ATOM   4248 O  O   . TYR B 1 258 ? 16.758  -10.996 3.484   1.00 14.34 ? 258 TYR B O   1 
ATOM   4249 C  CB  . TYR B 1 258 ? 19.301  -9.258  4.376   1.00 15.72 ? 258 TYR B CB  1 
ATOM   4250 C  CG  . TYR B 1 258 ? 19.856  -7.881  4.768   1.00 19.65 ? 258 TYR B CG  1 
ATOM   4251 C  CD1 . TYR B 1 258 ? 19.187  -7.094  5.707   1.00 21.09 ? 258 TYR B CD1 1 
ATOM   4252 C  CD2 . TYR B 1 258 ? 20.992  -7.347  4.175   1.00 21.71 ? 258 TYR B CD2 1 
ATOM   4253 C  CE1 . TYR B 1 258 ? 19.645  -5.829  6.059   1.00 24.25 ? 258 TYR B CE1 1 
ATOM   4254 C  CE2 . TYR B 1 258 ? 21.488  -6.085  4.549   1.00 21.90 ? 258 TYR B CE2 1 
ATOM   4255 C  CZ  . TYR B 1 258 ? 20.794  -5.332  5.479   1.00 25.96 ? 258 TYR B CZ  1 
ATOM   4256 O  OH  . TYR B 1 258 ? 21.233  -4.088  5.894   1.00 28.90 ? 258 TYR B OH  1 
ATOM   4257 N  N   . THR B 1 259 ? 18.244  -11.175 1.840   1.00 12.87 ? 259 THR B N   1 
ATOM   4258 C  CA  . THR B 1 259 ? 17.731  -12.461 1.421   1.00 12.86 ? 259 THR B CA  1 
ATOM   4259 C  C   . THR B 1 259 ? 18.745  -13.558 1.663   1.00 13.83 ? 259 THR B C   1 
ATOM   4260 O  O   . THR B 1 259 ? 19.933  -13.343 1.508   1.00 13.27 ? 259 THR B O   1 
ATOM   4261 C  CB  . THR B 1 259 ? 17.260  -12.493 -0.043  1.00 14.12 ? 259 THR B CB  1 
ATOM   4262 O  OG1 . THR B 1 259 ? 18.340  -12.174 -0.937  1.00 14.97 ? 259 THR B OG1 1 
ATOM   4263 C  CG2 . THR B 1 259 ? 16.125  -11.472 -0.259  1.00 14.80 ? 259 THR B CG2 1 
ATOM   4264 N  N   . SER B 1 260 ? 18.252  -14.759 1.943   1.00 14.45 ? 260 SER B N   1 
ATOM   4265 C  CA  . SER B 1 260 ? 19.183  -15.906 2.137   1.00 14.93 ? 260 SER B CA  1 
ATOM   4266 C  C   . SER B 1 260 ? 19.386  -16.680 0.828   1.00 16.85 ? 260 SER B C   1 
ATOM   4267 O  O   . SER B 1 260 ? 19.952  -17.777 0.810   1.00 19.19 ? 260 SER B O   1 
ATOM   4268 C  CB  . SER B 1 260 ? 18.646  -16.781 3.247   1.00 13.90 ? 260 SER B CB  1 
ATOM   4269 O  OG  . SER B 1 260 ? 17.559  -17.524 2.752   1.00 13.32 ? 260 SER B OG  1 
ATOM   4270 N  N   . PHE B 1 261 ? 18.909  -16.109 -0.276  1.00 16.85 ? 261 PHE B N   1 
ATOM   4271 C  CA  . PHE B 1 261 ? 18.936  -16.755 -1.589  1.00 17.69 ? 261 PHE B CA  1 
ATOM   4272 C  C   . PHE B 1 261 ? 19.382  -15.667 -2.555  1.00 20.34 ? 261 PHE B C   1 
ATOM   4273 O  O   . PHE B 1 261 ? 18.996  -14.490 -2.404  1.00 17.24 ? 261 PHE B O   1 
ATOM   4274 C  CB  . PHE B 1 261 ? 17.550  -17.331 -1.998  1.00 17.05 ? 261 PHE B CB  1 
ATOM   4275 C  CG  . PHE B 1 261 ? 16.429  -16.304 -2.020  1.00 17.16 ? 261 PHE B CG  1 
ATOM   4276 C  CD1 . PHE B 1 261 ? 16.147  -15.576 -3.182  1.00 17.77 ? 261 PHE B CD1 1 
ATOM   4277 C  CD2 . PHE B 1 261 ? 15.667  -16.066 -0.884  1.00 16.18 ? 261 PHE B CD2 1 
ATOM   4278 C  CE1 . PHE B 1 261 ? 15.135  -14.611 -3.205  1.00 17.31 ? 261 PHE B CE1 1 
ATOM   4279 C  CE2 . PHE B 1 261 ? 14.663  -15.097 -0.888  1.00 17.86 ? 261 PHE B CE2 1 
ATOM   4280 C  CZ  . PHE B 1 261 ? 14.379  -14.369 -2.049  1.00 17.82 ? 261 PHE B CZ  1 
ATOM   4281 N  N   . SER B 1 262 ? 20.193  -16.039 -3.549  1.00 21.18 ? 262 SER B N   1 
ATOM   4282 C  CA  . SER B 1 262 ? 20.799  -15.014 -4.399  1.00 24.31 ? 262 SER B CA  1 
ATOM   4283 C  C   . SER B 1 262 ? 20.119  -15.064 -5.730  1.00 29.08 ? 262 SER B C   1 
ATOM   4284 O  O   . SER B 1 262 ? 19.254  -15.956 -5.946  1.00 28.66 ? 262 SER B O   1 
ATOM   4285 C  CB  . SER B 1 262 ? 22.301  -15.223 -4.560  1.00 26.07 ? 262 SER B CB  1 
ATOM   4286 O  OG  . SER B 1 262 ? 22.547  -16.489 -5.124  1.00 26.14 ? 262 SER B OG  1 
ATOM   4287 N  N   . LYS C 1 3   ? 32.134  24.890  51.174  1.00 37.19 ? 3   LYS C N   1 
ATOM   4288 C  CA  . LYS C 1 3   ? 31.761  24.950  49.758  1.00 35.39 ? 3   LYS C CA  1 
ATOM   4289 C  C   . LYS C 1 3   ? 31.884  23.549  49.155  1.00 31.57 ? 3   LYS C C   1 
ATOM   4290 O  O   . LYS C 1 3   ? 32.864  22.813  49.404  1.00 32.57 ? 3   LYS C O   1 
ATOM   4291 C  CB  . LYS C 1 3   ? 32.682  25.911  49.017  1.00 40.80 ? 3   LYS C CB  1 
ATOM   4292 C  CG  . LYS C 1 3   ? 31.984  26.927  48.124  1.00 48.05 ? 3   LYS C CG  1 
ATOM   4293 C  CD  . LYS C 1 3   ? 32.837  27.308  46.909  1.00 50.34 ? 3   LYS C CD  1 
ATOM   4294 C  CE  . LYS C 1 3   ? 34.345  27.320  47.186  1.00 54.69 ? 3   LYS C CE  1 
ATOM   4295 N  NZ  . LYS C 1 3   ? 34.791  28.347  48.174  1.00 60.03 ? 3   LYS C NZ  1 
ATOM   4296 N  N   . TRP C 1 4   ? 30.931  23.190  48.307  1.00 23.52 ? 4   TRP C N   1 
ATOM   4297 C  CA  . TRP C 1 4   ? 30.895  21.826  47.829  1.00 18.79 ? 4   TRP C CA  1 
ATOM   4298 C  C   . TRP C 1 4   ? 31.963  21.642  46.761  1.00 17.08 ? 4   TRP C C   1 
ATOM   4299 O  O   . TRP C 1 4   ? 32.392  22.621  46.121  1.00 15.37 ? 4   TRP C O   1 
ATOM   4300 C  CB  . TRP C 1 4   ? 29.488  21.542  47.326  1.00 16.75 ? 4   TRP C CB  1 
ATOM   4301 C  CG  . TRP C 1 4   ? 29.054  22.410  46.148  1.00 15.22 ? 4   TRP C CG  1 
ATOM   4302 C  CD1 . TRP C 1 4   ? 28.370  23.620  46.175  1.00 15.93 ? 4   TRP C CD1 1 
ATOM   4303 C  CD2 . TRP C 1 4   ? 29.198  22.069  44.721  1.00 15.28 ? 4   TRP C CD2 1 
ATOM   4304 N  NE1 . TRP C 1 4   ? 28.113  24.079  44.892  1.00 16.20 ? 4   TRP C NE1 1 
ATOM   4305 C  CE2 . TRP C 1 4   ? 28.632  23.177  43.967  1.00 16.15 ? 4   TRP C CE2 1 
ATOM   4306 C  CE3 . TRP C 1 4   ? 29.770  20.980  44.016  1.00 14.08 ? 4   TRP C CE3 1 
ATOM   4307 C  CZ2 . TRP C 1 4   ? 28.586  23.172  42.548  1.00 16.03 ? 4   TRP C CZ2 1 
ATOM   4308 C  CZ3 . TRP C 1 4   ? 29.731  21.003  42.602  1.00 13.28 ? 4   TRP C CZ3 1 
ATOM   4309 C  CH2 . TRP C 1 4   ? 29.161  22.071  41.889  1.00 13.93 ? 4   TRP C CH2 1 
ATOM   4310 N  N   . THR C 1 5   ? 32.354  20.384  46.532  1.00 15.19 ? 5   THR C N   1 
ATOM   4311 C  CA  . THR C 1 5   ? 33.470  19.971  45.660  1.00 14.62 ? 5   THR C CA  1 
ATOM   4312 C  C   . THR C 1 5   ? 33.116  18.614  45.055  1.00 14.02 ? 5   THR C C   1 
ATOM   4313 O  O   . THR C 1 5   ? 32.083  18.052  45.396  1.00 13.49 ? 5   THR C O   1 
ATOM   4314 C  CB  . THR C 1 5   ? 34.812  19.720  46.414  1.00 15.34 ? 5   THR C CB  1 
ATOM   4315 O  OG1 . THR C 1 5   ? 34.673  18.594  47.289  1.00 15.74 ? 5   THR C OG1 1 
ATOM   4316 C  CG2 . THR C 1 5   ? 35.260  20.939  47.213  1.00 14.88 ? 5   THR C CG2 1 
ATOM   4317 N  N   . TYR C 1 6   ? 33.940  18.120  44.122  1.00 13.27 ? 6   TYR C N   1 
ATOM   4318 C  CA  . TYR C 1 6   ? 33.833  16.762  43.645  1.00 13.20 ? 6   TYR C CA  1 
ATOM   4319 C  C   . TYR C 1 6   ? 34.792  15.754  44.290  1.00 14.13 ? 6   TYR C C   1 
ATOM   4320 O  O   . TYR C 1 6   ? 34.808  14.587  43.924  1.00 11.90 ? 6   TYR C O   1 
ATOM   4321 C  CB  . TYR C 1 6   ? 34.032  16.761  42.113  1.00 11.68 ? 6   TYR C CB  1 
ATOM   4322 C  CG  . TYR C 1 6   ? 32.930  17.435  41.339  1.00 10.68 ? 6   TYR C CG  1 
ATOM   4323 C  CD1 . TYR C 1 6   ? 32.972  18.796  41.027  1.00 10.03 ? 6   TYR C CD1 1 
ATOM   4324 C  CD2 . TYR C 1 6   ? 31.853  16.668  40.851  1.00 9.72  ? 6   TYR C CD2 1 
ATOM   4325 C  CE1 . TYR C 1 6   ? 31.938  19.379  40.258  1.00 9.54  ? 6   TYR C CE1 1 
ATOM   4326 C  CE2 . TYR C 1 6   ? 30.843  17.224  40.075  1.00 10.33 ? 6   TYR C CE2 1 
ATOM   4327 C  CZ  . TYR C 1 6   ? 30.878  18.602  39.806  1.00 10.63 ? 6   TYR C CZ  1 
ATOM   4328 O  OH  . TYR C 1 6   ? 29.844  19.159  39.026  1.00 9.85  ? 6   TYR C OH  1 
ATOM   4329 N  N   . PHE C 1 7   ? 35.539  16.163  45.322  1.00 15.37 ? 7   PHE C N   1 
ATOM   4330 C  CA  . PHE C 1 7   ? 36.580  15.276  45.819  1.00 19.57 ? 7   PHE C CA  1 
ATOM   4331 C  C   . PHE C 1 7   ? 36.852  15.610  47.275  1.00 19.25 ? 7   PHE C C   1 
ATOM   4332 O  O   . PHE C 1 7   ? 37.146  16.757  47.565  1.00 20.35 ? 7   PHE C O   1 
ATOM   4333 C  CB  . PHE C 1 7   ? 37.858  15.454  44.923  1.00 24.22 ? 7   PHE C CB  1 
ATOM   4334 C  CG  . PHE C 1 7   ? 39.107  14.730  45.417  1.00 27.06 ? 7   PHE C CG  1 
ATOM   4335 C  CD1 . PHE C 1 7   ? 39.140  13.330  45.527  1.00 28.20 ? 7   PHE C CD1 1 
ATOM   4336 C  CD2 . PHE C 1 7   ? 40.283  15.446  45.699  1.00 32.49 ? 7   PHE C CD2 1 
ATOM   4337 C  CE1 . PHE C 1 7   ? 40.291  12.671  45.944  1.00 29.00 ? 7   PHE C CE1 1 
ATOM   4338 C  CE2 . PHE C 1 7   ? 41.444  14.780  46.115  1.00 31.72 ? 7   PHE C CE2 1 
ATOM   4339 C  CZ  . PHE C 1 7   ? 41.444  13.398  46.247  1.00 29.43 ? 7   PHE C CZ  1 
ATOM   4340 N  N   . GLY C 1 8   ? 36.803  14.602  48.157  1.00 19.06 ? 8   GLY C N   1 
ATOM   4341 C  CA  . GLY C 1 8   ? 37.206  14.751  49.587  1.00 17.94 ? 8   GLY C CA  1 
ATOM   4342 C  C   . GLY C 1 8   ? 35.953  14.901  50.448  1.00 18.43 ? 8   GLY C C   1 
ATOM   4343 O  O   . GLY C 1 8   ? 34.851  14.611  49.984  1.00 15.94 ? 8   GLY C O   1 
ATOM   4344 N  N   . PRO C 1 9   ? 36.092  15.354  51.720  1.00 18.36 ? 9   PRO C N   1 
ATOM   4345 C  CA  . PRO C 1 9   ? 34.898  15.284  52.625  1.00 19.86 ? 9   PRO C CA  1 
ATOM   4346 C  C   . PRO C 1 9   ? 33.715  16.148  52.230  1.00 21.29 ? 9   PRO C C   1 
ATOM   4347 O  O   . PRO C 1 9   ? 32.669  16.003  52.842  1.00 22.62 ? 9   PRO C O   1 
ATOM   4348 C  CB  . PRO C 1 9   ? 35.458  15.698  54.022  1.00 18.64 ? 9   PRO C CB  1 
ATOM   4349 C  CG  . PRO C 1 9   ? 36.783  16.332  53.742  1.00 17.43 ? 9   PRO C CG  1 
ATOM   4350 C  CD  . PRO C 1 9   ? 37.294  15.866  52.399  1.00 18.89 ? 9   PRO C CD  1 
ATOM   4351 N  N   . ASP C 1 10  ? 33.869  17.045  51.234  1.00 19.32 ? 10  ASP C N   1 
ATOM   4352 C  CA  . ASP C 1 10  ? 32.739  17.900  50.843  1.00 19.13 ? 10  ASP C CA  1 
ATOM   4353 C  C   . ASP C 1 10  ? 32.216  17.490  49.470  1.00 16.89 ? 10  ASP C C   1 
ATOM   4354 O  O   . ASP C 1 10  ? 31.468  18.253  48.814  1.00 16.82 ? 10  ASP C O   1 
ATOM   4355 C  CB  . ASP C 1 10  ? 33.080  19.399  50.890  1.00 20.45 ? 10  ASP C CB  1 
ATOM   4356 C  CG  . ASP C 1 10  ? 33.234  19.904  52.296  1.00 23.67 ? 10  ASP C CG  1 
ATOM   4357 O  OD1 . ASP C 1 10  ? 32.239  19.843  53.056  1.00 23.54 ? 10  ASP C OD1 1 
ATOM   4358 O  OD2 . ASP C 1 10  ? 34.342  20.369  52.664  1.00 24.86 ? 10  ASP C OD2 1 
ATOM   4359 N  N   . GLY C 1 11  ? 32.641  16.279  49.074  1.00 13.76 ? 11  GLY C N   1 
ATOM   4360 C  CA  . GLY C 1 11  ? 32.307  15.701  47.805  1.00 12.74 ? 11  GLY C CA  1 
ATOM   4361 C  C   . GLY C 1 11  ? 30.892  15.185  47.747  1.00 10.82 ? 11  GLY C C   1 
ATOM   4362 O  O   . GLY C 1 11  ? 30.071  15.451  48.656  1.00 9.43  ? 11  GLY C O   1 
ATOM   4363 N  N   . GLU C 1 12  ? 30.572  14.510  46.640  1.00 10.57 ? 12  GLU C N   1 
ATOM   4364 C  CA  . GLU C 1 12  ? 29.169  14.308  46.274  1.00 10.54 ? 12  GLU C CA  1 
ATOM   4365 C  C   . GLU C 1 12  ? 28.220  13.510  47.216  1.00 10.82 ? 12  GLU C C   1 
ATOM   4366 O  O   . GLU C 1 12  ? 27.012  13.778  47.232  1.00 10.97 ? 12  GLU C O   1 
ATOM   4367 C  CB  . GLU C 1 12  ? 29.079  13.776  44.837  1.00 9.96  ? 12  GLU C CB  1 
ATOM   4368 C  CG  . GLU C 1 12  ? 29.400  12.259  44.750  1.00 9.41  ? 12  GLU C CG  1 
ATOM   4369 C  CD  . GLU C 1 12  ? 29.712  11.904  43.318  1.00 10.17 ? 12  GLU C CD  1 
ATOM   4370 O  OE1 . GLU C 1 12  ? 28.724  11.593  42.638  1.00 9.25  ? 12  GLU C OE1 1 
ATOM   4371 O  OE2 . GLU C 1 12  ? 30.855  12.002  42.830  1.00 9.48  ? 12  GLU C OE2 1 
ATOM   4372 N  N   . ASN C 1 13  ? 28.761  12.530  47.947  1.00 9.83  ? 13  ASN C N   1 
ATOM   4373 C  CA  . ASN C 1 13  ? 28.052  11.810  49.001  1.00 9.10  ? 13  ASN C CA  1 
ATOM   4374 C  C   . ASN C 1 13  ? 27.597  12.669  50.175  1.00 8.64  ? 13  ASN C C   1 
ATOM   4375 O  O   . ASN C 1 13  ? 26.709  12.242  50.936  1.00 8.40  ? 13  ASN C O   1 
ATOM   4376 C  CB  . ASN C 1 13  ? 28.875  10.597  49.528  1.00 9.02  ? 13  ASN C CB  1 
ATOM   4377 C  CG  . ASN C 1 13  ? 29.015  9.512   48.486  1.00 9.17  ? 13  ASN C CG  1 
ATOM   4378 O  OD1 . ASN C 1 13  ? 28.460  9.659   47.401  1.00 8.17  ? 13  ASN C OD1 1 
ATOM   4379 N  ND2 . ASN C 1 13  ? 29.709  8.359   48.831  1.00 7.60  ? 13  ASN C ND2 1 
ATOM   4380 N  N   . SER C 1 14  ? 28.210  13.835  50.378  1.00 8.86  ? 14  SER C N   1 
ATOM   4381 C  CA  . SER C 1 14  ? 27.724  14.706  51.412  1.00 9.27  ? 14  SER C CA  1 
ATOM   4382 C  C   . SER C 1 14  ? 27.060  15.985  50.916  1.00 9.59  ? 14  SER C C   1 
ATOM   4383 O  O   . SER C 1 14  ? 26.650  16.859  51.748  1.00 9.09  ? 14  SER C O   1 
ATOM   4384 C  CB  . SER C 1 14  ? 28.823  15.047  52.482  1.00 10.75 ? 14  SER C CB  1 
ATOM   4385 O  OG  . SER C 1 14  ? 29.828  15.725  51.832  1.00 12.03 ? 14  SER C OG  1 
ATOM   4386 N  N   . TRP C 1 15  ? 26.920  16.151  49.606  1.00 9.62  ? 15  TRP C N   1 
ATOM   4387 C  CA  . TRP C 1 15  ? 26.041  17.301  49.111  1.00 9.24  ? 15  TRP C CA  1 
ATOM   4388 C  C   . TRP C 1 15  ? 24.684  17.424  49.791  1.00 10.08 ? 15  TRP C C   1 
ATOM   4389 O  O   . TRP C 1 15  ? 24.228  18.565  50.074  1.00 9.99  ? 15  TRP C O   1 
ATOM   4390 C  CB  . TRP C 1 15  ? 25.780  17.215  47.599  1.00 8.81  ? 15  TRP C CB  1 
ATOM   4391 C  CG  . TRP C 1 15  ? 26.978  17.395  46.707  1.00 8.76  ? 15  TRP C CG  1 
ATOM   4392 C  CD1 . TRP C 1 15  ? 28.297  17.749  47.084  1.00 9.12  ? 15  TRP C CD1 1 
ATOM   4393 C  CD2 . TRP C 1 15  ? 27.054  17.195  45.257  1.00 9.95  ? 15  TRP C CD2 1 
ATOM   4394 N  NE1 . TRP C 1 15  ? 29.115  17.800  45.983  1.00 9.25  ? 15  TRP C NE1 1 
ATOM   4395 C  CE2 . TRP C 1 15  ? 28.435  17.534  44.862  1.00 9.43  ? 15  TRP C CE2 1 
ATOM   4396 C  CE3 . TRP C 1 15  ? 26.129  16.886  44.261  1.00 9.38  ? 15  TRP C CE3 1 
ATOM   4397 C  CZ2 . TRP C 1 15  ? 28.864  17.450  43.566  1.00 9.39  ? 15  TRP C CZ2 1 
ATOM   4398 C  CZ3 . TRP C 1 15  ? 26.595  16.838  42.927  1.00 8.82  ? 15  TRP C CZ3 1 
ATOM   4399 C  CH2 . TRP C 1 15  ? 27.907  17.117  42.597  1.00 9.52  ? 15  TRP C CH2 1 
ATOM   4400 N  N   . SER C 1 16  ? 23.998  16.295  50.038  1.00 10.29 ? 16  SER C N   1 
ATOM   4401 C  CA  . SER C 1 16  ? 22.729  16.309  50.755  1.00 10.81 ? 16  SER C CA  1 
ATOM   4402 C  C   . SER C 1 16  ? 22.781  16.976  52.148  1.00 11.41 ? 16  SER C C   1 
ATOM   4403 O  O   . SER C 1 16  ? 21.755  17.320  52.649  1.00 10.30 ? 16  SER C O   1 
ATOM   4404 C  CB  . SER C 1 16  ? 22.170  14.880  50.938  1.00 11.74 ? 16  SER C CB  1 
ATOM   4405 O  OG  . SER C 1 16  ? 22.891  14.111  51.915  1.00 12.20 ? 16  SER C OG  1 
ATOM   4406 N  N   . LYS C 1 17  ? 23.946  17.061  52.807  1.00 11.65 ? 17  LYS C N   1 
ATOM   4407 C  CA  . LYS C 1 17  ? 23.992  17.714  54.117  1.00 12.62 ? 17  LYS C CA  1 
ATOM   4408 C  C   . LYS C 1 17  ? 23.847  19.228  53.994  1.00 12.59 ? 17  LYS C C   1 
ATOM   4409 O  O   . LYS C 1 17  ? 23.451  19.907  54.951  1.00 10.48 ? 17  LYS C O   1 
ATOM   4410 C  CB  . LYS C 1 17  ? 25.288  17.375  54.851  1.00 14.15 ? 17  LYS C CB  1 
ATOM   4411 C  CG  . LYS C 1 17  ? 25.494  15.880  55.111  1.00 16.70 ? 17  LYS C CG  1 
ATOM   4412 C  CD  . LYS C 1 17  ? 26.793  15.793  55.956  1.00 19.53 ? 17  LYS C CD  1 
ATOM   4413 C  CE  . LYS C 1 17  ? 27.470  14.428  55.831  1.00 20.12 ? 17  LYS C CE  1 
ATOM   4414 N  NZ  . LYS C 1 17  ? 28.801  14.402  56.545  1.00 22.80 ? 17  LYS C NZ  1 
ATOM   4415 N  N   . LYS C 1 18  ? 24.147  19.740  52.802  1.00 13.89 ? 18  LYS C N   1 
ATOM   4416 C  CA  . LYS C 1 18  ? 24.147  21.159  52.542  1.00 14.75 ? 18  LYS C CA  1 
ATOM   4417 C  C   . LYS C 1 18  ? 23.005  21.614  51.645  1.00 14.23 ? 18  LYS C C   1 
ATOM   4418 O  O   . LYS C 1 18  ? 22.597  22.799  51.688  1.00 13.09 ? 18  LYS C O   1 
ATOM   4419 C  CB  . LYS C 1 18  ? 25.495  21.566  51.937  1.00 17.32 ? 18  LYS C CB  1 
ATOM   4420 C  CG  . LYS C 1 18  ? 26.646  21.603  52.950  1.00 21.16 ? 18  LYS C CG  1 
ATOM   4421 C  CD  . LYS C 1 18  ? 27.676  20.491  52.674  1.00 26.94 ? 18  LYS C CD  1 
ATOM   4422 C  CE  . LYS C 1 18  ? 27.996  19.520  53.844  1.00 27.86 ? 18  LYS C CE  1 
ATOM   4423 N  NZ  . LYS C 1 18  ? 28.140  20.021  55.261  1.00 24.30 ? 18  LYS C NZ  1 
ATOM   4424 N  N   . TYR C 1 19  ? 22.520  20.684  50.837  1.00 12.65 ? 19  TYR C N   1 
ATOM   4425 C  CA  . TYR C 1 19  ? 21.473  20.958  49.836  1.00 12.23 ? 19  TYR C CA  1 
ATOM   4426 C  C   . TYR C 1 19  ? 20.430  19.836  49.849  1.00 11.22 ? 19  TYR C C   1 
ATOM   4427 O  O   . TYR C 1 19  ? 20.698  18.767  49.350  1.00 10.58 ? 19  TYR C O   1 
ATOM   4428 C  CB  . TYR C 1 19  ? 22.083  21.124  48.379  1.00 12.36 ? 19  TYR C CB  1 
ATOM   4429 C  CG  . TYR C 1 19  ? 23.158  22.192  48.312  1.00 13.24 ? 19  TYR C CG  1 
ATOM   4430 C  CD1 . TYR C 1 19  ? 24.506  21.872  48.548  1.00 14.93 ? 19  TYR C CD1 1 
ATOM   4431 C  CD2 . TYR C 1 19  ? 22.807  23.514  48.089  1.00 14.72 ? 19  TYR C CD2 1 
ATOM   4432 C  CE1 . TYR C 1 19  ? 25.470  22.861  48.557  1.00 16.48 ? 19  TYR C CE1 1 
ATOM   4433 C  CE2 . TYR C 1 19  ? 23.734  24.504  48.061  1.00 15.57 ? 19  TYR C CE2 1 
ATOM   4434 C  CZ  . TYR C 1 19  ? 25.060  24.190  48.285  1.00 17.09 ? 19  TYR C CZ  1 
ATOM   4435 O  OH  . TYR C 1 19  ? 25.969  25.217  48.286  1.00 17.66 ? 19  TYR C OH  1 
ATOM   4436 N  N   . PRO C 1 20  ? 19.247  20.085  50.407  1.00 11.27 ? 20  PRO C N   1 
ATOM   4437 C  CA  . PRO C 1 20  ? 18.308  18.983  50.615  1.00 11.61 ? 20  PRO C CA  1 
ATOM   4438 C  C   . PRO C 1 20  ? 17.938  18.199  49.342  1.00 11.36 ? 20  PRO C C   1 
ATOM   4439 O  O   . PRO C 1 20  ? 17.792  16.981  49.409  1.00 11.66 ? 20  PRO C O   1 
ATOM   4440 C  CB  . PRO C 1 20  ? 17.063  19.667  51.232  1.00 13.18 ? 20  PRO C CB  1 
ATOM   4441 C  CG  . PRO C 1 20  ? 17.311  21.169  51.107  1.00 12.86 ? 20  PRO C CG  1 
ATOM   4442 C  CD  . PRO C 1 20  ? 18.794  21.354  51.031  1.00 11.20 ? 20  PRO C CD  1 
ATOM   4443 N  N   . SER C 1 21  ? 17.772  18.881  48.200  1.00 11.06 ? 21  SER C N   1 
ATOM   4444 C  CA  . SER C 1 21  ? 17.277  18.194  46.990  1.00 9.72  ? 21  SER C CA  1 
ATOM   4445 C  C   . SER C 1 21  ? 18.312  17.200  46.426  1.00 9.45  ? 21  SER C C   1 
ATOM   4446 O  O   . SER C 1 21  ? 17.926  16.334  45.675  1.00 8.55  ? 21  SER C O   1 
ATOM   4447 C  CB  . SER C 1 21  ? 16.856  19.187  45.845  1.00 10.32 ? 21  SER C CB  1 
ATOM   4448 O  OG  . SER C 1 21  ? 15.680  19.867  46.285  1.00 10.40 ? 21  SER C OG  1 
ATOM   4449 N  N   . CYS C 1 22  ? 19.591  17.339  46.764  1.00 8.94  ? 22  CYS C N   1 
ATOM   4450 C  CA  . CYS C 1 22  ? 20.638  16.357  46.355  1.00 10.32 ? 22  CYS C CA  1 
ATOM   4451 C  C   . CYS C 1 22  ? 20.431  14.953  46.914  1.00 10.06 ? 22  CYS C C   1 
ATOM   4452 O  O   . CYS C 1 22  ? 20.948  13.999  46.315  1.00 10.21 ? 22  CYS C O   1 
ATOM   4453 C  CB  . CYS C 1 22  ? 22.112  16.832  46.627  1.00 9.88  ? 22  CYS C CB  1 
ATOM   4454 S  SG  . CYS C 1 22  ? 22.514  18.413  45.890  1.00 11.68 ? 22  CYS C SG  1 
ATOM   4455 N  N   . GLY C 1 23  ? 19.682  14.825  48.039  1.00 10.41 ? 23  GLY C N   1 
ATOM   4456 C  CA  . GLY C 1 23  ? 19.288  13.483  48.555  1.00 10.32 ? 23  GLY C CA  1 
ATOM   4457 C  C   . GLY C 1 23  ? 17.840  13.084  48.214  1.00 11.43 ? 23  GLY C C   1 
ATOM   4458 O  O   . GLY C 1 23  ? 17.324  12.089  48.717  1.00 12.37 ? 23  GLY C O   1 
ATOM   4459 N  N   . GLY C 1 24  ? 17.215  13.824  47.323  1.00 10.93 ? 24  GLY C N   1 
ATOM   4460 C  CA  . GLY C 1 24  ? 15.789  13.606  47.012  1.00 13.66 ? 24  GLY C CA  1 
ATOM   4461 C  C   . GLY C 1 24  ? 15.490  12.796  45.807  1.00 12.86 ? 24  GLY C C   1 
ATOM   4462 O  O   . GLY C 1 24  ? 16.319  12.059  45.304  1.00 13.14 ? 24  GLY C O   1 
ATOM   4463 N  N   . LEU C 1 25  ? 14.279  12.973  45.322  1.00 14.15 ? 25  LEU C N   1 
ATOM   4464 C  CA  . LEU C 1 25  ? 13.829  12.273  44.126  1.00 16.03 ? 25  LEU C CA  1 
ATOM   4465 C  C   . LEU C 1 25  ? 14.384  12.815  42.807  1.00 15.32 ? 25  LEU C C   1 
ATOM   4466 O  O   . LEU C 1 25  ? 14.850  13.967  42.720  1.00 15.86 ? 25  LEU C O   1 
ATOM   4467 C  CB  . LEU C 1 25  ? 12.298  12.338  44.099  1.00 18.00 ? 25  LEU C CB  1 
ATOM   4468 C  CG  . LEU C 1 25  ? 11.604  11.679  45.295  1.00 20.02 ? 25  LEU C CG  1 
ATOM   4469 C  CD1 . LEU C 1 25  ? 10.095  11.814  45.141  1.00 24.06 ? 25  LEU C CD1 1 
ATOM   4470 C  CD2 . LEU C 1 25  ? 12.061  10.219  45.347  1.00 19.24 ? 25  LEU C CD2 1 
ATOM   4471 N  N   . LEU C 1 26  ? 14.305  12.000  41.769  1.00 16.27 ? 26  LEU C N   1 
ATOM   4472 C  CA  . LEU C 1 26  ? 14.467  12.489  40.336  1.00 16.78 ? 26  LEU C CA  1 
ATOM   4473 C  C   . LEU C 1 26  ? 15.911  13.010  40.023  1.00 14.41 ? 26  LEU C C   1 
ATOM   4474 O  O   . LEU C 1 26  ? 16.094  13.893  39.181  1.00 13.08 ? 26  LEU C O   1 
ATOM   4475 C  CB  . LEU C 1 26  ? 13.429  13.611  40.014  1.00 17.14 ? 26  LEU C CB  1 
ATOM   4476 C  CG  . LEU C 1 26  ? 11.915  13.307  39.888  1.00 20.23 ? 26  LEU C CG  1 
ATOM   4477 C  CD1 . LEU C 1 26  ? 11.102  14.537  39.478  1.00 20.40 ? 26  LEU C CD1 1 
ATOM   4478 C  CD2 . LEU C 1 26  ? 11.648  12.153  38.947  1.00 18.35 ? 26  LEU C CD2 1 
ATOM   4479 N  N   . GLN C 1 27  ? 16.917  12.444  40.689  1.00 11.82 ? 27  GLN C N   1 
ATOM   4480 C  CA  . GLN C 1 27  ? 18.299  12.893  40.507  1.00 10.50 ? 27  GLN C CA  1 
ATOM   4481 C  C   . GLN C 1 27  ? 18.936  12.438  39.173  1.00 9.22  ? 27  GLN C C   1 
ATOM   4482 O  O   . GLN C 1 27  ? 18.603  11.379  38.671  1.00 10.87 ? 27  GLN C O   1 
ATOM   4483 C  CB  . GLN C 1 27  ? 19.173  12.503  41.697  1.00 10.48 ? 27  GLN C CB  1 
ATOM   4484 C  CG  . GLN C 1 27  ? 18.679  13.170  42.980  1.00 10.10 ? 27  GLN C CG  1 
ATOM   4485 C  CD  . GLN C 1 27  ? 18.854  14.686  42.916  1.00 9.66  ? 27  GLN C CD  1 
ATOM   4486 O  OE1 . GLN C 1 27  ? 19.978  15.221  43.096  1.00 8.49  ? 27  GLN C OE1 1 
ATOM   4487 N  NE2 . GLN C 1 27  ? 17.746  15.394  42.645  1.00 8.54  ? 27  GLN C NE2 1 
ATOM   4488 N  N   . SER C 1 28  ? 19.774  13.316  38.591  1.00 8.94  ? 28  SER C N   1 
ATOM   4489 C  CA  . SER C 1 28  ? 20.593  13.028  37.385  1.00 8.92  ? 28  SER C CA  1 
ATOM   4490 C  C   . SER C 1 28  ? 22.051  13.160  37.730  1.00 8.51  ? 28  SER C C   1 
ATOM   4491 O  O   . SER C 1 28  ? 22.342  13.754  38.753  1.00 9.17  ? 28  SER C O   1 
ATOM   4492 C  CB  . SER C 1 28  ? 20.244  14.134  36.389  1.00 10.26 ? 28  SER C CB  1 
ATOM   4493 O  OG  . SER C 1 28  ? 18.883  13.969  35.949  1.00 10.12 ? 28  SER C OG  1 
ATOM   4494 N  N   . PRO C 1 29  ? 22.995  12.606  36.930  1.00 8.81  ? 29  PRO C N   1 
ATOM   4495 C  CA  . PRO C 1 29  ? 22.882  11.848  35.688  1.00 8.48  ? 29  PRO C CA  1 
ATOM   4496 C  C   . PRO C 1 29  ? 22.474  10.380  35.910  1.00 9.22  ? 29  PRO C C   1 
ATOM   4497 O  O   . PRO C 1 29  ? 22.414  9.963   37.062  1.00 8.59  ? 29  PRO C O   1 
ATOM   4498 C  CB  . PRO C 1 29  ? 24.275  11.949  35.105  1.00 9.01  ? 29  PRO C CB  1 
ATOM   4499 C  CG  . PRO C 1 29  ? 25.222  11.995  36.318  1.00 8.39  ? 29  PRO C CG  1 
ATOM   4500 C  CD  . PRO C 1 29  ? 24.411  12.678  37.408  1.00 8.52  ? 29  PRO C CD  1 
ATOM   4501 N  N   . ILE C 1 30  ? 22.188  9.643   34.820  1.00 8.32  ? 30  ILE C N   1 
ATOM   4502 C  CA  . ILE C 1 30  ? 21.837  8.229   34.872  1.00 9.19  ? 30  ILE C CA  1 
ATOM   4503 C  C   . ILE C 1 30  ? 22.621  7.450   33.817  1.00 9.39  ? 30  ILE C C   1 
ATOM   4504 O  O   . ILE C 1 30  ? 23.208  8.041   32.897  1.00 8.90  ? 30  ILE C O   1 
ATOM   4505 C  CB  . ILE C 1 30  ? 20.326  7.966   34.664  1.00 8.88  ? 30  ILE C CB  1 
ATOM   4506 C  CG1 . ILE C 1 30  ? 19.771  8.677   33.416  1.00 8.59  ? 30  ILE C CG1 1 
ATOM   4507 C  CG2 . ILE C 1 30  ? 19.543  8.435   35.918  1.00 9.51  ? 30  ILE C CG2 1 
ATOM   4508 C  CD1 . ILE C 1 30  ? 18.333  8.257   33.024  1.00 9.75  ? 30  ILE C CD1 1 
ATOM   4509 N  N   . ASP C 1 31  ? 22.566  6.114   33.933  1.00 9.82  ? 31  ASP C N   1 
ATOM   4510 C  CA  . ASP C 1 31  ? 23.127  5.249   32.930  1.00 10.07 ? 31  ASP C CA  1 
ATOM   4511 C  C   . ASP C 1 31  ? 21.990  4.884   31.966  1.00 10.44 ? 31  ASP C C   1 
ATOM   4512 O  O   . ASP C 1 31  ? 20.939  4.460   32.421  1.00 10.89 ? 31  ASP C O   1 
ATOM   4513 C  CB  . ASP C 1 31  ? 23.714  3.985   33.548  1.00 11.55 ? 31  ASP C CB  1 
ATOM   4514 C  CG  . ASP C 1 31  ? 24.277  3.049   32.474  1.00 13.48 ? 31  ASP C CG  1 
ATOM   4515 O  OD1 . ASP C 1 31  ? 25.088  3.491   31.654  1.00 12.64 ? 31  ASP C OD1 1 
ATOM   4516 O  OD2 . ASP C 1 31  ? 23.781  1.935   32.339  1.00 16.20 ? 31  ASP C OD2 1 
ATOM   4517 N  N   . LEU C 1 32  ? 22.224  5.034   30.669  1.00 9.76  ? 32  LEU C N   1 
ATOM   4518 C  CA  . LEU C 1 32  ? 21.175  4.849   29.653  1.00 10.80 ? 32  LEU C CA  1 
ATOM   4519 C  C   . LEU C 1 32  ? 21.446  3.477   29.124  1.00 11.22 ? 32  LEU C C   1 
ATOM   4520 O  O   . LEU C 1 32  ? 22.516  3.255   28.470  1.00 11.89 ? 32  LEU C O   1 
ATOM   4521 C  CB  . LEU C 1 32  ? 21.326  5.930   28.531  1.00 10.85 ? 32  LEU C CB  1 
ATOM   4522 C  CG  . LEU C 1 32  ? 21.258  7.384   29.042  1.00 11.62 ? 32  LEU C CG  1 
ATOM   4523 C  CD1 . LEU C 1 32  ? 21.756  8.354   27.991  1.00 12.10 ? 32  LEU C CD1 1 
ATOM   4524 C  CD2 . LEU C 1 32  ? 19.880  7.845   29.585  1.00 11.91 ? 32  LEU C CD2 1 
ATOM   4525 N  N   . HIS C 1 33  ? 20.539  2.522   29.425  1.00 13.06 ? 33  HIS C N   1 
ATOM   4526 C  CA  . HIS C 1 33  ? 20.774  1.130   29.048  1.00 14.03 ? 33  HIS C CA  1 
ATOM   4527 C  C   . HIS C 1 33  ? 19.466  0.466   28.655  1.00 13.56 ? 33  HIS C C   1 
ATOM   4528 O  O   . HIS C 1 33  ? 18.370  0.969   28.993  1.00 12.58 ? 33  HIS C O   1 
ATOM   4529 C  CB  . HIS C 1 33  ? 21.572  0.344   30.101  1.00 14.23 ? 33  HIS C CB  1 
ATOM   4530 C  CG  . HIS C 1 33  ? 20.854  0.180   31.419  1.00 15.61 ? 33  HIS C CG  1 
ATOM   4531 N  ND1 . HIS C 1 33  ? 20.904  1.107   32.388  1.00 15.27 ? 33  HIS C ND1 1 
ATOM   4532 C  CD2 . HIS C 1 33  ? 20.053  -0.852  31.902  1.00 15.50 ? 33  HIS C CD2 1 
ATOM   4533 C  CE1 . HIS C 1 33  ? 20.123  0.700   33.416  1.00 18.52 ? 33  HIS C CE1 1 
ATOM   4534 N  NE2 . HIS C 1 33  ? 19.609  -0.486  33.105  1.00 16.30 ? 33  HIS C NE2 1 
ATOM   4535 N  N   A SER C 1 34  ? 19.564  -0.653  27.938  0.50 14.53 ? 34  SER C N   1 
ATOM   4536 N  N   B SER C 1 34  ? 19.568  -0.653  27.946  0.50 14.57 ? 34  SER C N   1 
ATOM   4537 C  CA  A SER C 1 34  ? 18.393  -1.259  27.224  0.50 15.70 ? 34  SER C CA  1 
ATOM   4538 C  CA  B SER C 1 34  ? 18.398  -1.243  27.240  0.50 15.81 ? 34  SER C CA  1 
ATOM   4539 C  C   A SER C 1 34  ? 17.131  -1.510  28.045  0.50 16.06 ? 34  SER C C   1 
ATOM   4540 C  C   B SER C 1 34  ? 17.142  -1.432  28.078  0.50 16.07 ? 34  SER C C   1 
ATOM   4541 O  O   A SER C 1 34  ? 16.006  -1.281  27.568  0.50 14.81 ? 34  SER C O   1 
ATOM   4542 O  O   B SER C 1 34  ? 16.034  -1.082  27.642  0.50 14.99 ? 34  SER C O   1 
ATOM   4543 C  CB  A SER C 1 34  ? 18.786  -2.567  26.514  0.50 16.23 ? 34  SER C CB  1 
ATOM   4544 C  CB  B SER C 1 34  ? 18.761  -2.588  26.602  0.50 16.38 ? 34  SER C CB  1 
ATOM   4545 O  OG  A SER C 1 34  ? 19.438  -3.465  27.395  0.50 16.32 ? 34  SER C OG  1 
ATOM   4546 O  OG  B SER C 1 34  ? 17.961  -2.821  25.461  0.50 16.89 ? 34  SER C OG  1 
ATOM   4547 N  N   . ASP C 1 35  ? 17.325  -2.029  29.259  1.00 16.19 ? 35  ASP C N   1 
ATOM   4548 C  CA  . ASP C 1 35  ? 16.222  -2.474  30.134  1.00 16.90 ? 35  ASP C CA  1 
ATOM   4549 C  C   . ASP C 1 35  ? 15.287  -1.337  30.487  1.00 15.91 ? 35  ASP C C   1 
ATOM   4550 O  O   . ASP C 1 35  ? 14.141  -1.586  30.782  1.00 15.70 ? 35  ASP C O   1 
ATOM   4551 C  CB  . ASP C 1 35  ? 16.793  -2.997  31.484  1.00 18.02 ? 35  ASP C CB  1 
ATOM   4552 C  CG  . ASP C 1 35  ? 17.823  -4.114  31.288  1.00 20.99 ? 35  ASP C CG  1 
ATOM   4553 O  OD1 . ASP C 1 35  ? 18.925  -3.847  30.679  1.00 21.77 ? 35  ASP C OD1 1 
ATOM   4554 O  OD2 . ASP C 1 35  ? 17.494  -5.265  31.689  1.00 19.46 ? 35  ASP C OD2 1 
ATOM   4555 N  N   . ILE C 1 36  ? 15.797  -0.108  30.539  1.00 15.44 ? 36  ILE C N   1 
ATOM   4556 C  CA  . ILE C 1 36  ? 14.974  1.061   30.958  1.00 17.17 ? 36  ILE C CA  1 
ATOM   4557 C  C   . ILE C 1 36  ? 14.634  2.013   29.782  1.00 16.62 ? 36  ILE C C   1 
ATOM   4558 O  O   . ILE C 1 36  ? 14.018  3.055   29.970  1.00 19.60 ? 36  ILE C O   1 
ATOM   4559 C  CB  . ILE C 1 36  ? 15.619  1.832   32.146  1.00 16.51 ? 36  ILE C CB  1 
ATOM   4560 C  CG1 . ILE C 1 36  ? 16.965  2.432   31.753  1.00 18.43 ? 36  ILE C CG1 1 
ATOM   4561 C  CG2 . ILE C 1 36  ? 15.695  0.951   33.419  1.00 19.25 ? 36  ILE C CG2 1 
ATOM   4562 C  CD1 . ILE C 1 36  ? 17.626  3.246   32.860  1.00 21.37 ? 36  ILE C CD1 1 
ATOM   4563 N  N   . LEU C 1 37  ? 14.980  1.619   28.560  1.00 16.81 ? 37  LEU C N   1 
ATOM   4564 C  CA  . LEU C 1 37  ? 14.641  2.412   27.364  1.00 15.63 ? 37  LEU C CA  1 
ATOM   4565 C  C   . LEU C 1 37  ? 13.244  2.041   26.792  1.00 15.49 ? 37  LEU C C   1 
ATOM   4566 O  O   . LEU C 1 37  ? 12.900  0.824   26.676  1.00 15.14 ? 37  LEU C O   1 
ATOM   4567 C  CB  . LEU C 1 37  ? 15.713  2.155   26.272  1.00 17.69 ? 37  LEU C CB  1 
ATOM   4568 C  CG  . LEU C 1 37  ? 17.156  2.565   26.551  1.00 17.06 ? 37  LEU C CG  1 
ATOM   4569 C  CD1 . LEU C 1 37  ? 17.923  2.499   25.244  1.00 16.97 ? 37  LEU C CD1 1 
ATOM   4570 C  CD2 . LEU C 1 37  ? 17.210  3.975   27.066  1.00 17.66 ? 37  LEU C CD2 1 
ATOM   4571 N  N   . GLN C 1 38  ? 12.442  3.052   26.424  1.00 13.73 ? 38  GLN C N   1 
ATOM   4572 C  CA  . GLN C 1 38  ? 11.178  2.754   25.686  1.00 15.93 ? 38  GLN C CA  1 
ATOM   4573 C  C   . GLN C 1 38  ? 11.017  3.677   24.468  1.00 15.53 ? 38  GLN C C   1 
ATOM   4574 O  O   . GLN C 1 38  ? 11.104  4.927   24.624  1.00 15.21 ? 38  GLN C O   1 
ATOM   4575 C  CB  . GLN C 1 38  ? 9.981   2.958   26.604  1.00 17.81 ? 38  GLN C CB  1 
ATOM   4576 C  CG  . GLN C 1 38  ? 8.621   2.645   25.948  1.00 19.57 ? 38  GLN C CG  1 
ATOM   4577 C  CD  . GLN C 1 38  ? 7.568   2.398   26.995  1.00 22.47 ? 38  GLN C CD  1 
ATOM   4578 O  OE1 . GLN C 1 38  ? 7.601   1.373   27.720  1.00 25.09 ? 38  GLN C OE1 1 
ATOM   4579 N  NE2 . GLN C 1 38  ? 6.639   3.330   27.110  1.00 21.68 ? 38  GLN C NE2 1 
ATOM   4580 N  N   . TYR C 1 39  ? 10.810  3.109   23.286  1.00 14.49 ? 39  TYR C N   1 
ATOM   4581 C  CA  . TYR C 1 39  ? 10.597  3.957   22.098  1.00 14.02 ? 39  TYR C CA  1 
ATOM   4582 C  C   . TYR C 1 39  ? 9.323   4.808   22.259  1.00 13.47 ? 39  TYR C C   1 
ATOM   4583 O  O   . TYR C 1 39  ? 8.288   4.290   22.663  1.00 13.09 ? 39  TYR C O   1 
ATOM   4584 C  CB  . TYR C 1 39  ? 10.474  3.121   20.850  1.00 13.76 ? 39  TYR C CB  1 
ATOM   4585 C  CG  . TYR C 1 39  ? 10.094  3.926   19.568  1.00 13.40 ? 39  TYR C CG  1 
ATOM   4586 C  CD1 . TYR C 1 39  ? 10.985  4.854   19.022  1.00 13.33 ? 39  TYR C CD1 1 
ATOM   4587 C  CD2 . TYR C 1 39  ? 8.861   3.706   18.905  1.00 14.39 ? 39  TYR C CD2 1 
ATOM   4588 C  CE1 . TYR C 1 39  ? 10.710  5.563   17.859  1.00 14.08 ? 39  TYR C CE1 1 
ATOM   4589 C  CE2 . TYR C 1 39  ? 8.553   4.454   17.753  1.00 14.70 ? 39  TYR C CE2 1 
ATOM   4590 C  CZ  . TYR C 1 39  ? 9.486   5.353   17.218  1.00 15.34 ? 39  TYR C CZ  1 
ATOM   4591 O  OH  . TYR C 1 39  ? 9.242   6.116   16.072  1.00 14.21 ? 39  TYR C OH  1 
ATOM   4592 N  N   . ASP C 1 40  ? 9.394   6.086   21.887  1.00 13.59 ? 40  ASP C N   1 
ATOM   4593 C  CA  . ASP C 1 40  ? 8.240   7.008   21.966  1.00 14.31 ? 40  ASP C CA  1 
ATOM   4594 C  C   . ASP C 1 40  ? 8.141   7.782   20.651  1.00 14.47 ? 40  ASP C C   1 
ATOM   4595 O  O   . ASP C 1 40  ? 8.918   8.704   20.454  1.00 12.53 ? 40  ASP C O   1 
ATOM   4596 C  CB  . ASP C 1 40  ? 8.423   8.009   23.106  1.00 15.53 ? 40  ASP C CB  1 
ATOM   4597 C  CG  . ASP C 1 40  ? 7.177   8.923   23.292  1.00 17.45 ? 40  ASP C CG  1 
ATOM   4598 O  OD1 . ASP C 1 40  ? 7.036   9.555   24.366  1.00 22.24 ? 40  ASP C OD1 1 
ATOM   4599 O  OD2 . ASP C 1 40  ? 6.313   8.984   22.406  1.00 14.81 ? 40  ASP C OD2 1 
ATOM   4600 N  N   . ALA C 1 41  ? 7.235   7.391   19.738  1.00 13.70 ? 41  ALA C N   1 
ATOM   4601 C  CA  . ALA C 1 41  ? 7.139   8.055   18.440  1.00 15.38 ? 41  ALA C CA  1 
ATOM   4602 C  C   . ALA C 1 41  ? 6.675   9.524   18.564  1.00 15.31 ? 41  ALA C C   1 
ATOM   4603 O  O   . ALA C 1 41  ? 6.800   10.291  17.614  1.00 15.33 ? 41  ALA C O   1 
ATOM   4604 C  CB  . ALA C 1 41  ? 6.236   7.246   17.449  1.00 15.05 ? 41  ALA C CB  1 
ATOM   4605 N  N   . SER C 1 42  ? 6.112   9.913   19.713  1.00 15.82 ? 42  SER C N   1 
ATOM   4606 C  CA  . SER C 1 42  ? 5.725   11.307  19.913  1.00 17.75 ? 42  SER C CA  1 
ATOM   4607 C  C   . SER C 1 42  ? 6.922   12.270  20.066  1.00 16.12 ? 42  SER C C   1 
ATOM   4608 O  O   . SER C 1 42  ? 6.736   13.502  20.050  1.00 18.38 ? 42  SER C O   1 
ATOM   4609 C  CB  . SER C 1 42  ? 4.722   11.464  21.106  1.00 18.15 ? 42  SER C CB  1 
ATOM   4610 O  OG  . SER C 1 42  ? 5.396   11.716  22.349  1.00 26.29 ? 42  SER C OG  1 
ATOM   4611 N  N   . LEU C 1 43  ? 8.137   11.733  20.187  1.00 14.71 ? 43  LEU C N   1 
ATOM   4612 C  CA  . LEU C 1 43  ? 9.320   12.595  20.374  1.00 14.46 ? 43  LEU C CA  1 
ATOM   4613 C  C   . LEU C 1 43  ? 9.855   13.118  19.049  1.00 15.15 ? 43  LEU C C   1 
ATOM   4614 O  O   . LEU C 1 43  ? 10.678  12.480  18.387  1.00 15.69 ? 43  LEU C O   1 
ATOM   4615 C  CB  . LEU C 1 43  ? 10.436  11.895  21.176  1.00 14.73 ? 43  LEU C CB  1 
ATOM   4616 C  CG  . LEU C 1 43  ? 10.084  11.446  22.625  1.00 15.55 ? 43  LEU C CG  1 
ATOM   4617 C  CD1 . LEU C 1 43  ? 11.163  10.513  23.147  1.00 14.75 ? 43  LEU C CD1 1 
ATOM   4618 C  CD2 . LEU C 1 43  ? 9.815   12.579  23.623  1.00 15.82 ? 43  LEU C CD2 1 
ATOM   4619 N  N   . THR C 1 44  ? 9.437   14.336  18.703  1.00 15.97 ? 44  THR C N   1 
ATOM   4620 C  CA  . THR C 1 44  ? 9.706   14.927  17.378  1.00 16.06 ? 44  THR C CA  1 
ATOM   4621 C  C   . THR C 1 44  ? 10.966  15.817  17.460  1.00 16.34 ? 44  THR C C   1 
ATOM   4622 O  O   . THR C 1 44  ? 11.484  16.049  18.547  1.00 15.76 ? 44  THR C O   1 
ATOM   4623 C  CB  . THR C 1 44  ? 8.475   15.778  16.919  1.00 18.27 ? 44  THR C CB  1 
ATOM   4624 O  OG1 . THR C 1 44  ? 8.085   16.669  17.977  1.00 20.34 ? 44  THR C OG1 1 
ATOM   4625 C  CG2 . THR C 1 44  ? 7.277   14.876  16.550  1.00 19.91 ? 44  THR C CG2 1 
ATOM   4626 N  N   . PRO C 1 45  ? 11.519  16.251  16.311  1.00 16.20 ? 45  PRO C N   1 
ATOM   4627 C  CA  . PRO C 1 45  ? 12.794  17.009  16.417  1.00 16.65 ? 45  PRO C CA  1 
ATOM   4628 C  C   . PRO C 1 45  ? 12.597  18.317  17.126  1.00 16.03 ? 45  PRO C C   1 
ATOM   4629 O  O   . PRO C 1 45  ? 11.538  18.935  16.979  1.00 16.59 ? 45  PRO C O   1 
ATOM   4630 C  CB  . PRO C 1 45  ? 13.178  17.260  14.952  1.00 16.63 ? 45  PRO C CB  1 
ATOM   4631 C  CG  . PRO C 1 45  ? 12.532  16.091  14.219  1.00 18.35 ? 45  PRO C CG  1 
ATOM   4632 C  CD  . PRO C 1 45  ? 11.170  15.951  14.903  1.00 16.33 ? 45  PRO C CD  1 
ATOM   4633 N  N   . LEU C 1 46  ? 13.606  18.748  17.881  1.00 14.81 ? 46  LEU C N   1 
ATOM   4634 C  CA  . LEU C 1 46  ? 13.591  20.077  18.478  1.00 16.35 ? 46  LEU C CA  1 
ATOM   4635 C  C   . LEU C 1 46  ? 13.980  21.075  17.393  1.00 16.00 ? 46  LEU C C   1 
ATOM   4636 O  O   . LEU C 1 46  ? 14.733  20.720  16.490  1.00 18.11 ? 46  LEU C O   1 
ATOM   4637 C  CB  . LEU C 1 46  ? 14.627  20.152  19.634  1.00 15.73 ? 46  LEU C CB  1 
ATOM   4638 C  CG  . LEU C 1 46  ? 14.283  19.423  20.964  1.00 16.85 ? 46  LEU C CG  1 
ATOM   4639 C  CD1 . LEU C 1 46  ? 15.351  19.720  22.008  1.00 16.11 ? 46  LEU C CD1 1 
ATOM   4640 C  CD2 . LEU C 1 46  ? 12.904  19.863  21.498  1.00 16.70 ? 46  LEU C CD2 1 
ATOM   4641 N  N   . GLU C 1 47  ? 13.498  22.311  17.468  1.00 17.35 ? 47  GLU C N   1 
ATOM   4642 C  CA  . GLU C 1 47  ? 14.038  23.360  16.605  1.00 19.07 ? 47  GLU C CA  1 
ATOM   4643 C  C   . GLU C 1 47  ? 14.838  24.356  17.441  1.00 17.28 ? 47  GLU C C   1 
ATOM   4644 O  O   . GLU C 1 47  ? 14.349  24.821  18.433  1.00 16.34 ? 47  GLU C O   1 
ATOM   4645 C  CB  . GLU C 1 47  ? 12.905  24.056  15.837  1.00 24.95 ? 47  GLU C CB  1 
ATOM   4646 C  CG  . GLU C 1 47  ? 12.124  23.106  14.921  1.00 30.81 ? 47  GLU C CG  1 
ATOM   4647 C  CD  . GLU C 1 47  ? 12.898  22.713  13.652  1.00 38.77 ? 47  GLU C CD  1 
ATOM   4648 O  OE1 . GLU C 1 47  ? 13.491  23.613  12.997  1.00 42.13 ? 47  GLU C OE1 1 
ATOM   4649 O  OE2 . GLU C 1 47  ? 12.902  21.505  13.290  1.00 42.87 ? 47  GLU C OE2 1 
ATOM   4650 N  N   . PHE C 1 48  ? 16.071  24.619  17.022  1.00 16.57 ? 48  PHE C N   1 
ATOM   4651 C  CA  . PHE C 1 48  ? 17.017  25.460  17.722  1.00 18.03 ? 48  PHE C CA  1 
ATOM   4652 C  C   . PHE C 1 48  ? 16.995  26.850  17.085  1.00 18.64 ? 48  PHE C C   1 
ATOM   4653 O  O   . PHE C 1 48  ? 17.683  27.094  16.081  1.00 21.23 ? 48  PHE C O   1 
ATOM   4654 C  CB  . PHE C 1 48  ? 18.404  24.836  17.616  1.00 17.02 ? 48  PHE C CB  1 
ATOM   4655 C  CG  . PHE C 1 48  ? 18.404  23.358  17.923  1.00 16.37 ? 48  PHE C CG  1 
ATOM   4656 C  CD1 . PHE C 1 48  ? 18.364  22.421  16.916  1.00 17.29 ? 48  PHE C CD1 1 
ATOM   4657 C  CD2 . PHE C 1 48  ? 18.376  22.928  19.226  1.00 15.61 ? 48  PHE C CD2 1 
ATOM   4658 C  CE1 . PHE C 1 48  ? 18.314  21.029  17.189  1.00 16.70 ? 48  PHE C CE1 1 
ATOM   4659 C  CE2 . PHE C 1 48  ? 18.331  21.561  19.516  1.00 18.14 ? 48  PHE C CE2 1 
ATOM   4660 C  CZ  . PHE C 1 48  ? 18.328  20.606  18.490  1.00 15.72 ? 48  PHE C CZ  1 
ATOM   4661 N  N   . GLN C 1 49  ? 16.257  27.769  17.702  1.00 18.47 ? 49  GLN C N   1 
ATOM   4662 C  CA  . GLN C 1 49  ? 16.121  29.124  17.141  1.00 17.61 ? 49  GLN C CA  1 
ATOM   4663 C  C   . GLN C 1 49  ? 17.023  30.151  17.779  1.00 14.80 ? 49  GLN C C   1 
ATOM   4664 O  O   . GLN C 1 49  ? 17.173  30.166  18.999  1.00 13.27 ? 49  GLN C O   1 
ATOM   4665 C  CB  . GLN C 1 49  ? 14.688  29.577  17.256  1.00 21.69 ? 49  GLN C CB  1 
ATOM   4666 C  CG  . GLN C 1 49  ? 13.776  28.508  16.680  1.00 24.08 ? 49  GLN C CG  1 
ATOM   4667 C  CD  . GLN C 1 49  ? 12.323  28.924  16.662  1.00 27.40 ? 49  GLN C CD  1 
ATOM   4668 O  OE1 . GLN C 1 49  ? 11.866  29.726  17.496  1.00 27.54 ? 49  GLN C OE1 1 
ATOM   4669 N  NE2 . GLN C 1 49  ? 11.566  28.344  15.710  1.00 29.51 ? 49  GLN C NE2 1 
ATOM   4670 N  N   . GLY C 1 50  ? 17.598  31.016  16.942  1.00 12.83 ? 50  GLY C N   1 
ATOM   4671 C  CA  . GLY C 1 50  ? 18.573  32.020  17.395  1.00 12.81 ? 50  GLY C CA  1 
ATOM   4672 C  C   . GLY C 1 50  ? 19.854  31.425  17.988  1.00 13.03 ? 50  GLY C C   1 
ATOM   4673 O  O   . GLY C 1 50  ? 20.557  32.111  18.755  1.00 13.25 ? 50  GLY C O   1 
ATOM   4674 N  N   . TYR C 1 51  ? 20.133  30.162  17.675  1.00 12.99 ? 51  TYR C N   1 
ATOM   4675 C  CA  . TYR C 1 51  ? 21.445  29.530  18.007  1.00 13.39 ? 51  TYR C CA  1 
ATOM   4676 C  C   . TYR C 1 51  ? 22.593  30.097  17.200  1.00 14.15 ? 51  TYR C C   1 
ATOM   4677 O  O   . TYR C 1 51  ? 23.766  29.985  17.615  1.00 12.77 ? 51  TYR C O   1 
ATOM   4678 C  CB  . TYR C 1 51  ? 21.387  28.010  17.770  1.00 12.62 ? 51  TYR C CB  1 
ATOM   4679 C  CG  . TYR C 1 51  ? 20.848  27.221  18.958  1.00 12.74 ? 51  TYR C CG  1 
ATOM   4680 C  CD1 . TYR C 1 51  ? 19.747  27.655  19.690  1.00 12.36 ? 51  TYR C CD1 1 
ATOM   4681 C  CD2 . TYR C 1 51  ? 21.469  26.020  19.352  1.00 12.54 ? 51  TYR C CD2 1 
ATOM   4682 C  CE1 . TYR C 1 51  ? 19.284  26.940  20.816  1.00 13.48 ? 51  TYR C CE1 1 
ATOM   4683 C  CE2 . TYR C 1 51  ? 21.003  25.296  20.452  1.00 12.62 ? 51  TYR C CE2 1 
ATOM   4684 C  CZ  . TYR C 1 51  ? 19.933  25.768  21.194  1.00 12.99 ? 51  TYR C CZ  1 
ATOM   4685 O  OH  . TYR C 1 51  ? 19.534  25.042  22.304  1.00 13.27 ? 51  TYR C OH  1 
ATOM   4686 N  N   . ASN C 1 52  ? 22.282  30.685  16.038  1.00 14.91 ? 52  ASN C N   1 
ATOM   4687 C  CA  . ASN C 1 52  ? 23.340  31.351  15.216  1.00 17.26 ? 52  ASN C CA  1 
ATOM   4688 C  C   . ASN C 1 52  ? 23.712  32.741  15.780  1.00 15.09 ? 52  ASN C C   1 
ATOM   4689 O  O   . ASN C 1 52  ? 23.313  33.787  15.236  1.00 14.61 ? 52  ASN C O   1 
ATOM   4690 C  CB  . ASN C 1 52  ? 22.971  31.376  13.719  1.00 17.75 ? 52  ASN C CB  1 
ATOM   4691 C  CG  . ASN C 1 52  ? 24.167  31.723  12.812  1.00 22.49 ? 52  ASN C CG  1 
ATOM   4692 O  OD1 . ASN C 1 52  ? 25.328  31.826  13.266  1.00 21.78 ? 52  ASN C OD1 1 
ATOM   4693 N  ND2 . ASN C 1 52  ? 23.882  31.915  11.494  1.00 23.34 ? 52  ASN C ND2 1 
ATOM   4694 N  N   . LEU C 1 53  ? 24.408  32.753  16.911  1.00 13.31 ? 53  LEU C N   1 
ATOM   4695 C  CA  . LEU C 1 53  ? 24.775  33.990  17.588  1.00 14.24 ? 53  LEU C CA  1 
ATOM   4696 C  C   . LEU C 1 53  ? 25.573  34.974  16.709  1.00 15.28 ? 53  LEU C C   1 
ATOM   4697 O  O   . LEU C 1 53  ? 26.499  34.583  15.977  1.00 15.90 ? 53  LEU C O   1 
ATOM   4698 C  CB  . LEU C 1 53  ? 25.588  33.679  18.888  1.00 13.93 ? 53  LEU C CB  1 
ATOM   4699 C  CG  . LEU C 1 53  ? 24.920  32.772  19.940  1.00 13.67 ? 53  LEU C CG  1 
ATOM   4700 C  CD1 . LEU C 1 53  ? 25.794  32.625  21.191  1.00 13.68 ? 53  LEU C CD1 1 
ATOM   4701 C  CD2 . LEU C 1 53  ? 23.465  33.158  20.276  1.00 14.09 ? 53  LEU C CD2 1 
ATOM   4702 N  N   . SER C 1 54  ? 25.227  36.242  16.836  1.00 15.66 ? 54  SER C N   1 
ATOM   4703 C  CA  . SER C 1 54  ? 25.802  37.312  16.024  1.00 17.73 ? 54  SER C CA  1 
ATOM   4704 C  C   . SER C 1 54  ? 27.332  37.351  16.207  1.00 16.37 ? 54  SER C C   1 
ATOM   4705 O  O   . SER C 1 54  ? 27.812  37.493  17.335  1.00 15.19 ? 54  SER C O   1 
ATOM   4706 C  CB  . SER C 1 54  ? 25.204  38.644  16.517  1.00 16.93 ? 54  SER C CB  1 
ATOM   4707 O  OG  . SER C 1 54  ? 25.730  39.738  15.771  1.00 20.83 ? 54  SER C OG  1 
ATOM   4708 N  N   . ALA C 1 55  ? 28.067  37.184  15.122  1.00 17.13 ? 55  ALA C N   1 
ATOM   4709 C  CA  . ALA C 1 55  ? 29.541  37.335  15.162  1.00 17.96 ? 55  ALA C CA  1 
ATOM   4710 C  C   . ALA C 1 55  ? 29.946  38.752  15.594  1.00 16.59 ? 55  ALA C C   1 
ATOM   4711 O  O   . ALA C 1 55  ? 31.089  38.963  16.029  1.00 18.05 ? 55  ALA C O   1 
ATOM   4712 C  CB  . ALA C 1 55  ? 30.166  36.982  13.817  1.00 18.77 ? 55  ALA C CB  1 
ATOM   4713 N  N   . ASN C 1 56  ? 29.007  39.699  15.519  1.00 16.96 ? 56  ASN C N   1 
ATOM   4714 C  CA  . ASN C 1 56  ? 29.284  41.107  15.894  1.00 18.31 ? 56  ASN C CA  1 
ATOM   4715 C  C   . ASN C 1 56  ? 29.027  41.383  17.397  1.00 17.76 ? 56  ASN C C   1 
ATOM   4716 O  O   . ASN C 1 56  ? 29.247  42.487  17.894  1.00 18.09 ? 56  ASN C O   1 
ATOM   4717 C  CB  . ASN C 1 56  ? 28.513  42.076  14.963  1.00 20.31 ? 56  ASN C CB  1 
ATOM   4718 C  CG  . ASN C 1 56  ? 28.967  42.004  13.499  1.00 22.16 ? 56  ASN C CG  1 
ATOM   4719 O  OD1 . ASN C 1 56  ? 30.114  41.685  13.176  1.00 24.10 ? 56  ASN C OD1 1 
ATOM   4720 N  ND2 . ASN C 1 56  ? 28.051  42.277  12.605  1.00 23.86 ? 56  ASN C ND2 1 
ATOM   4721 N  N   . LYS C 1 57  ? 28.618  40.356  18.146  1.00 17.51 ? 57  LYS C N   1 
ATOM   4722 C  CA  . LYS C 1 57  ? 28.377  40.513  19.562  1.00 17.55 ? 57  LYS C CA  1 
ATOM   4723 C  C   . LYS C 1 57  ? 29.431  39.684  20.277  1.00 16.22 ? 57  LYS C C   1 
ATOM   4724 O  O   . LYS C 1 57  ? 30.075  38.828  19.662  1.00 15.56 ? 57  LYS C O   1 
ATOM   4725 C  CB  . LYS C 1 57  ? 26.997  39.966  19.945  1.00 20.80 ? 57  LYS C CB  1 
ATOM   4726 C  CG  . LYS C 1 57  ? 25.825  40.955  20.062  1.00 24.74 ? 57  LYS C CG  1 
ATOM   4727 C  CD  . LYS C 1 57  ? 24.566  40.204  20.542  1.00 26.25 ? 57  LYS C CD  1 
ATOM   4728 C  CE  . LYS C 1 57  ? 24.310  40.252  22.055  1.00 23.79 ? 57  LYS C CE  1 
ATOM   4729 N  NZ  . LYS C 1 57  ? 22.949  39.744  22.394  1.00 21.38 ? 57  LYS C NZ  1 
ATOM   4730 N  N   . GLN C 1 58  ? 29.562  39.899  21.576  1.00 14.94 ? 58  GLN C N   1 
ATOM   4731 C  CA  . GLN C 1 58  ? 30.481  39.122  22.437  1.00 15.61 ? 58  GLN C CA  1 
ATOM   4732 C  C   . GLN C 1 58  ? 29.767  38.581  23.665  1.00 14.84 ? 58  GLN C C   1 
ATOM   4733 O  O   . GLN C 1 58  ? 28.922  39.282  24.246  1.00 13.34 ? 58  GLN C O   1 
ATOM   4734 C  CB  . GLN C 1 58  ? 31.620  40.021  22.902  1.00 18.48 ? 58  GLN C CB  1 
ATOM   4735 C  CG  . GLN C 1 58  ? 32.521  40.482  21.776  1.00 23.73 ? 58  GLN C CG  1 
ATOM   4736 C  CD  . GLN C 1 58  ? 33.493  41.544  22.272  1.00 26.21 ? 58  GLN C CD  1 
ATOM   4737 O  OE1 . GLN C 1 58  ? 33.091  42.534  22.893  1.00 33.55 ? 58  GLN C OE1 1 
ATOM   4738 N  NE2 . GLN C 1 58  ? 34.757  41.330  22.024  1.00 26.27 ? 58  GLN C NE2 1 
ATOM   4739 N  N   . PHE C 1 59  ? 30.117  37.345  24.053  1.00 14.19 ? 59  PHE C N   1 
ATOM   4740 C  CA  . PHE C 1 59  ? 29.436  36.612  25.095  1.00 13.84 ? 59  PHE C CA  1 
ATOM   4741 C  C   . PHE C 1 59  ? 30.414  36.287  26.240  1.00 13.59 ? 59  PHE C C   1 
ATOM   4742 O  O   . PHE C 1 59  ? 31.545  35.916  26.002  1.00 14.41 ? 59  PHE C O   1 
ATOM   4743 C  CB  . PHE C 1 59  ? 28.726  35.399  24.497  1.00 14.46 ? 59  PHE C CB  1 
ATOM   4744 C  CG  . PHE C 1 59  ? 27.722  35.792  23.422  1.00 14.79 ? 59  PHE C CG  1 
ATOM   4745 C  CD1 . PHE C 1 59  ? 28.125  35.920  22.096  1.00 14.51 ? 59  PHE C CD1 1 
ATOM   4746 C  CD2 . PHE C 1 59  ? 26.389  36.149  23.772  1.00 15.86 ? 59  PHE C CD2 1 
ATOM   4747 C  CE1 . PHE C 1 59  ? 27.258  36.336  21.103  1.00 14.63 ? 59  PHE C CE1 1 
ATOM   4748 C  CE2 . PHE C 1 59  ? 25.510  36.597  22.789  1.00 15.21 ? 59  PHE C CE2 1 
ATOM   4749 C  CZ  . PHE C 1 59  ? 25.949  36.683  21.441  1.00 16.50 ? 59  PHE C CZ  1 
ATOM   4750 N  N   . LEU C 1 60  ? 29.970  36.463  27.484  1.00 14.08 ? 60  LEU C N   1 
ATOM   4751 C  CA  . LEU C 1 60  ? 30.856  36.305  28.636  1.00 13.46 ? 60  LEU C CA  1 
ATOM   4752 C  C   . LEU C 1 60  ? 31.156  34.813  28.963  1.00 13.83 ? 60  LEU C C   1 
ATOM   4753 O  O   . LEU C 1 60  ? 30.225  34.033  29.183  1.00 12.66 ? 60  LEU C O   1 
ATOM   4754 C  CB  . LEU C 1 60  ? 30.213  36.942  29.878  1.00 14.42 ? 60  LEU C CB  1 
ATOM   4755 C  CG  . LEU C 1 60  ? 31.138  37.220  31.064  1.00 14.68 ? 60  LEU C CG  1 
ATOM   4756 C  CD1 . LEU C 1 60  ? 32.250  38.228  30.762  1.00 14.60 ? 60  LEU C CD1 1 
ATOM   4757 C  CD2 . LEU C 1 60  ? 30.326  37.630  32.310  1.00 16.12 ? 60  LEU C CD2 1 
ATOM   4758 N  N   . LEU C 1 61  ? 32.445  34.477  29.096  1.00 14.07 ? 61  LEU C N   1 
ATOM   4759 C  CA  . LEU C 1 61  ? 32.920  33.161  29.550  1.00 13.89 ? 61  LEU C CA  1 
ATOM   4760 C  C   . LEU C 1 61  ? 33.512  33.357  30.964  1.00 14.42 ? 61  LEU C C   1 
ATOM   4761 O  O   . LEU C 1 61  ? 34.246  34.311  31.234  1.00 16.67 ? 61  LEU C O   1 
ATOM   4762 C  CB  . LEU C 1 61  ? 34.007  32.628  28.598  1.00 13.46 ? 61  LEU C CB  1 
ATOM   4763 C  CG  . LEU C 1 61  ? 34.515  31.208  28.781  1.00 13.28 ? 61  LEU C CG  1 
ATOM   4764 C  CD1 . LEU C 1 61  ? 33.544  30.152  28.246  1.00 13.71 ? 61  LEU C CD1 1 
ATOM   4765 C  CD2 . LEU C 1 61  ? 35.874  31.127  28.085  1.00 13.22 ? 61  LEU C CD2 1 
ATOM   4766 N  N   . THR C 1 62  ? 33.104  32.489  31.883  1.00 14.30 ? 62  THR C N   1 
ATOM   4767 C  CA  . THR C 1 62  ? 33.441  32.648  33.293  1.00 14.93 ? 62  THR C CA  1 
ATOM   4768 C  C   . THR C 1 62  ? 33.882  31.300  33.866  1.00 13.52 ? 62  THR C C   1 
ATOM   4769 O  O   . THR C 1 62  ? 33.211  30.258  33.689  1.00 12.62 ? 62  THR C O   1 
ATOM   4770 C  CB  . THR C 1 62  ? 32.223  33.154  34.127  1.00 15.34 ? 62  THR C CB  1 
ATOM   4771 O  OG1 . THR C 1 62  ? 31.684  34.347  33.530  1.00 17.75 ? 62  THR C OG1 1 
ATOM   4772 C  CG2 . THR C 1 62  ? 32.648  33.497  35.556  1.00 17.68 ? 62  THR C CG2 1 
ATOM   4773 N  N   . ASN C 1 63  ? 34.978  31.345  34.605  1.00 13.72 ? 63  ASN C N   1 
ATOM   4774 C  CA  . ASN C 1 63  ? 35.347  30.222  35.485  1.00 13.94 ? 63  ASN C CA  1 
ATOM   4775 C  C   . ASN C 1 63  ? 34.613  30.460  36.835  1.00 13.01 ? 63  ASN C C   1 
ATOM   4776 O  O   . ASN C 1 63  ? 34.944  31.379  37.560  1.00 11.96 ? 63  ASN C O   1 
ATOM   4777 C  CB  . ASN C 1 63  ? 36.899  30.149  35.658  1.00 13.36 ? 63  ASN C CB  1 
ATOM   4778 C  CG  . ASN C 1 63  ? 37.353  29.133  36.711  1.00 12.99 ? 63  ASN C CG  1 
ATOM   4779 O  OD1 . ASN C 1 63  ? 36.591  28.767  37.619  1.00 11.28 ? 63  ASN C OD1 1 
ATOM   4780 N  ND2 . ASN C 1 63  ? 38.648  28.710  36.639  1.00 13.12 ? 63  ASN C ND2 1 
ATOM   4781 N  N   . ASN C 1 64  ? 33.639  29.592  37.164  1.00 12.23 ? 64  ASN C N   1 
ATOM   4782 C  CA  . ASN C 1 64  ? 32.856  29.771  38.404  1.00 13.57 ? 64  ASN C CA  1 
ATOM   4783 C  C   . ASN C 1 64  ? 33.300  28.937  39.602  1.00 14.25 ? 64  ASN C C   1 
ATOM   4784 O  O   . ASN C 1 64  ? 32.617  28.912  40.643  1.00 13.70 ? 64  ASN C O   1 
ATOM   4785 C  CB  . ASN C 1 64  ? 31.340  29.646  38.123  1.00 13.83 ? 64  ASN C CB  1 
ATOM   4786 C  CG  . ASN C 1 64  ? 30.914  28.243  37.741  1.00 15.44 ? 64  ASN C CG  1 
ATOM   4787 O  OD1 . ASN C 1 64  ? 31.673  27.275  37.894  1.00 14.41 ? 64  ASN C OD1 1 
ATOM   4788 N  ND2 . ASN C 1 64  ? 29.669  28.123  37.178  1.00 17.79 ? 64  ASN C ND2 1 
ATOM   4789 N  N   . GLY C 1 65  ? 34.452  28.256  39.467  1.00 13.81 ? 65  GLY C N   1 
ATOM   4790 C  CA  . GLY C 1 65  ? 34.964  27.475  40.568  1.00 13.03 ? 65  GLY C CA  1 
ATOM   4791 C  C   . GLY C 1 65  ? 34.567  26.015  40.444  1.00 13.59 ? 65  GLY C C   1 
ATOM   4792 O  O   . GLY C 1 65  ? 35.181  25.211  41.057  1.00 14.69 ? 65  GLY C O   1 
ATOM   4793 N  N   . HIS C 1 66  ? 33.580  25.707  39.594  1.00 13.12 ? 66  HIS C N   1 
ATOM   4794 C  CA  . HIS C 1 66  ? 33.037  24.352  39.427  1.00 13.32 ? 66  HIS C CA  1 
ATOM   4795 C  C   . HIS C 1 66  ? 33.091  23.894  37.959  1.00 12.98 ? 66  HIS C C   1 
ATOM   4796 O  O   . HIS C 1 66  ? 33.086  22.682  37.667  1.00 11.45 ? 66  HIS C O   1 
ATOM   4797 C  CB  . HIS C 1 66  ? 31.588  24.326  39.945  1.00 15.20 ? 66  HIS C CB  1 
ATOM   4798 C  CG  . HIS C 1 66  ? 31.435  24.744  41.429  1.00 17.19 ? 66  HIS C CG  1 
ATOM   4799 N  ND1 . HIS C 1 66  ? 31.975  24.025  42.464  1.00 19.04 ? 66  HIS C ND1 1 
ATOM   4800 C  CD2 . HIS C 1 66  ? 30.770  25.819  42.016  1.00 18.45 ? 66  HIS C CD2 1 
ATOM   4801 C  CE1 . HIS C 1 66  ? 31.657  24.604  43.640  1.00 18.08 ? 66  HIS C CE1 1 
ATOM   4802 N  NE2 . HIS C 1 66  ? 30.949  25.710  43.378  1.00 20.16 ? 66  HIS C NE2 1 
ATOM   4803 N  N   . SER C 1 67  ? 33.021  24.841  37.027  1.00 12.13 ? 67  SER C N   1 
ATOM   4804 C  CA  . SER C 1 67  ? 33.058  24.546  35.580  1.00 12.13 ? 67  SER C CA  1 
ATOM   4805 C  C   . SER C 1 67  ? 33.523  25.832  34.893  1.00 13.18 ? 67  SER C C   1 
ATOM   4806 O  O   . SER C 1 67  ? 33.906  26.796  35.579  1.00 12.28 ? 67  SER C O   1 
ATOM   4807 C  CB  . SER C 1 67  ? 31.671  24.085  35.034  1.00 12.22 ? 67  SER C CB  1 
ATOM   4808 O  OG  . SER C 1 67  ? 31.749  23.657  33.670  1.00 12.45 ? 67  SER C OG  1 
ATOM   4809 N  N   . VAL C 1 68  ? 33.532  25.820  33.557  1.00 12.54 ? 68  VAL C N   1 
ATOM   4810 C  CA  . VAL C 1 68  ? 33.708  26.992  32.747  1.00 11.93 ? 68  VAL C CA  1 
ATOM   4811 C  C   . VAL C 1 68  ? 32.374  27.149  31.976  1.00 12.64 ? 68  VAL C C   1 
ATOM   4812 O  O   . VAL C 1 68  ? 31.853  26.162  31.403  1.00 11.72 ? 68  VAL C O   1 
ATOM   4813 C  CB  . VAL C 1 68  ? 34.965  26.920  31.793  1.00 12.35 ? 68  VAL C CB  1 
ATOM   4814 C  CG1 . VAL C 1 68  ? 34.965  25.690  30.928  1.00 12.69 ? 68  VAL C CG1 1 
ATOM   4815 C  CG2 . VAL C 1 68  ? 35.074  28.173  30.915  1.00 11.94 ? 68  VAL C CG2 1 
ATOM   4816 N  N   . LYS C 1 69  ? 31.776  28.336  32.084  1.00 13.16 ? 69  LYS C N   1 
ATOM   4817 C  CA  . LYS C 1 69  ? 30.412  28.555  31.540  1.00 13.15 ? 69  LYS C CA  1 
ATOM   4818 C  C   . LYS C 1 69  ? 30.395  29.766  30.550  1.00 13.08 ? 69  LYS C C   1 
ATOM   4819 O  O   . LYS C 1 69  ? 31.031  30.755  30.795  1.00 12.36 ? 69  LYS C O   1 
ATOM   4820 C  CB  . LYS C 1 69  ? 29.391  28.788  32.690  1.00 14.98 ? 69  LYS C CB  1 
ATOM   4821 C  CG  . LYS C 1 69  ? 29.537  30.071  33.492  1.00 17.15 ? 69  LYS C CG  1 
ATOM   4822 C  CD  . LYS C 1 69  ? 28.267  30.361  34.369  1.00 18.51 ? 69  LYS C CD  1 
ATOM   4823 C  CE  . LYS C 1 69  ? 28.402  31.730  35.097  1.00 20.61 ? 69  LYS C CE  1 
ATOM   4824 N  NZ  . LYS C 1 69  ? 27.223  32.066  35.965  1.00 18.46 ? 69  LYS C NZ  1 
ATOM   4825 N  N   . LEU C 1 70  ? 29.639  29.642  29.492  1.00 10.84 ? 70  LEU C N   1 
ATOM   4826 C  CA  . LEU C 1 70  ? 29.386  30.716  28.602  1.00 11.41 ? 70  LEU C CA  1 
ATOM   4827 C  C   . LEU C 1 70  ? 27.931  31.234  28.792  1.00 10.79 ? 70  LEU C C   1 
ATOM   4828 O  O   . LEU C 1 70  ? 26.948  30.479  28.661  1.00 10.10 ? 70  LEU C O   1 
ATOM   4829 C  CB  . LEU C 1 70  ? 29.596  30.227  27.162  1.00 10.40 ? 70  LEU C CB  1 
ATOM   4830 C  CG  . LEU C 1 70  ? 29.406  31.239  26.009  1.00 10.84 ? 70  LEU C CG  1 
ATOM   4831 C  CD1 . LEU C 1 70  ? 30.541  32.244  26.053  1.00 10.72 ? 70  LEU C CD1 1 
ATOM   4832 C  CD2 . LEU C 1 70  ? 29.361  30.584  24.643  1.00 10.89 ? 70  LEU C CD2 1 
ATOM   4833 N  N   . ASN C 1 71  ? 27.805  32.526  29.051  1.00 11.13 ? 71  ASN C N   1 
ATOM   4834 C  CA  . ASN C 1 71  ? 26.506  33.152  29.092  1.00 12.64 ? 71  ASN C CA  1 
ATOM   4835 C  C   . ASN C 1 71  ? 25.849  33.170  27.690  1.00 11.75 ? 71  ASN C C   1 
ATOM   4836 O  O   . ASN C 1 71  ? 26.511  33.400  26.646  1.00 12.42 ? 71  ASN C O   1 
ATOM   4837 C  CB  . ASN C 1 71  ? 26.566  34.549  29.720  1.00 14.14 ? 71  ASN C CB  1 
ATOM   4838 C  CG  . ASN C 1 71  ? 26.794  34.521  31.258  1.00 17.29 ? 71  ASN C CG  1 
ATOM   4839 O  OD1 . ASN C 1 71  ? 26.685  33.496  31.891  1.00 17.62 ? 71  ASN C OD1 1 
ATOM   4840 N  ND2 . ASN C 1 71  ? 27.112  35.676  31.827  1.00 19.81 ? 71  ASN C ND2 1 
ATOM   4841 N  N   . LEU C 1 72  ? 24.576  32.836  27.661  1.00 11.96 ? 72  LEU C N   1 
ATOM   4842 C  CA  . LEU C 1 72  ? 23.758  32.794  26.409  1.00 11.41 ? 72  LEU C CA  1 
ATOM   4843 C  C   . LEU C 1 72  ? 22.613  33.814  26.505  1.00 11.76 ? 72  LEU C C   1 
ATOM   4844 O  O   . LEU C 1 72  ? 22.096  34.033  27.600  1.00 12.46 ? 72  LEU C O   1 
ATOM   4845 C  CB  . LEU C 1 72  ? 23.198  31.361  26.148  1.00 10.59 ? 72  LEU C CB  1 
ATOM   4846 C  CG  . LEU C 1 72  ? 24.308  30.328  25.863  1.00 9.04  ? 72  LEU C CG  1 
ATOM   4847 C  CD1 . LEU C 1 72  ? 23.733  28.883  26.011  1.00 9.83  ? 72  LEU C CD1 1 
ATOM   4848 C  CD2 . LEU C 1 72  ? 25.121  30.482  24.532  1.00 8.21  ? 72  LEU C CD2 1 
ATOM   4849 N  N   . PRO C 1 73  ? 22.193  34.424  25.361  1.00 12.58 ? 73  PRO C N   1 
ATOM   4850 C  CA  . PRO C 1 73  ? 21.158  35.479  25.402  1.00 12.38 ? 73  PRO C CA  1 
ATOM   4851 C  C   . PRO C 1 73  ? 19.735  34.884  25.399  1.00 14.20 ? 73  PRO C C   1 
ATOM   4852 O  O   . PRO C 1 73  ? 19.516  33.833  24.798  1.00 12.81 ? 73  PRO C O   1 
ATOM   4853 C  CB  . PRO C 1 73  ? 21.412  36.229  24.079  1.00 13.87 ? 73  PRO C CB  1 
ATOM   4854 C  CG  . PRO C 1 73  ? 21.822  35.118  23.102  1.00 11.90 ? 73  PRO C CG  1 
ATOM   4855 C  CD  . PRO C 1 73  ? 22.717  34.217  23.973  1.00 11.84 ? 73  PRO C CD  1 
ATOM   4856 N  N   . SER C 1 74  ? 18.783  35.548  26.064  1.00 14.95 ? 74  SER C N   1 
ATOM   4857 C  CA  . SER C 1 74  ? 17.426  35.029  26.167  1.00 15.85 ? 74  SER C CA  1 
ATOM   4858 C  C   . SER C 1 74  ? 16.691  34.953  24.828  1.00 15.28 ? 74  SER C C   1 
ATOM   4859 O  O   . SER C 1 74  ? 15.679  34.261  24.750  1.00 16.78 ? 74  SER C O   1 
ATOM   4860 C  CB  . SER C 1 74  ? 16.585  35.843  27.159  1.00 18.12 ? 74  SER C CB  1 
ATOM   4861 O  OG  . SER C 1 74  ? 16.532  37.201  26.772  1.00 20.74 ? 74  SER C OG  1 
ATOM   4862 N  N   . ASP C 1 75  ? 17.206  35.562  23.746  1.00 14.52 ? 75  ASP C N   1 
ATOM   4863 C  CA  . ASP C 1 75  ? 16.529  35.358  22.430  1.00 15.03 ? 75  ASP C CA  1 
ATOM   4864 C  C   . ASP C 1 75  ? 16.742  33.983  21.809  1.00 15.64 ? 75  ASP C C   1 
ATOM   4865 O  O   . ASP C 1 75  ? 15.996  33.593  20.945  1.00 16.15 ? 75  ASP C O   1 
ATOM   4866 C  CB  . ASP C 1 75  ? 16.835  36.441  21.369  1.00 15.58 ? 75  ASP C CB  1 
ATOM   4867 C  CG  . ASP C 1 75  ? 18.255  36.438  20.939  1.00 16.19 ? 75  ASP C CG  1 
ATOM   4868 O  OD1 . ASP C 1 75  ? 19.106  36.836  21.756  1.00 15.08 ? 75  ASP C OD1 1 
ATOM   4869 O  OD2 . ASP C 1 75  ? 18.547  36.007  19.792  1.00 16.04 ? 75  ASP C OD2 1 
ATOM   4870 N  N   . MET C 1 76  ? 17.786  33.274  22.237  1.00 13.73 ? 76  MET C N   1 
ATOM   4871 C  CA  . MET C 1 76  ? 18.061  31.927  21.815  1.00 13.93 ? 76  MET C CA  1 
ATOM   4872 C  C   . MET C 1 76  ? 17.113  30.968  22.565  1.00 13.83 ? 76  MET C C   1 
ATOM   4873 O  O   . MET C 1 76  ? 17.005  31.058  23.792  1.00 13.08 ? 76  MET C O   1 
ATOM   4874 C  CB  . MET C 1 76  ? 19.533  31.634  22.211  1.00 14.08 ? 76  MET C CB  1 
ATOM   4875 C  CG  . MET C 1 76  ? 20.052  30.230  21.924  1.00 14.87 ? 76  MET C CG  1 
ATOM   4876 S  SD  . MET C 1 76  ? 21.839  30.115  22.348  1.00 14.30 ? 76  MET C SD  1 
ATOM   4877 C  CE  . MET C 1 76  ? 22.020  28.350  22.489  1.00 13.88 ? 76  MET C CE  1 
ATOM   4878 N  N   . HIS C 1 77  ? 16.485  30.026  21.859  1.00 13.73 ? 77  HIS C N   1 
ATOM   4879 C  CA  . HIS C 1 77  ? 15.480  29.157  22.477  1.00 15.69 ? 77  HIS C CA  1 
ATOM   4880 C  C   . HIS C 1 77  ? 15.265  27.831  21.790  1.00 15.94 ? 77  HIS C C   1 
ATOM   4881 O  O   . HIS C 1 77  ? 15.610  27.641  20.585  1.00 16.23 ? 77  HIS C O   1 
ATOM   4882 C  CB  . HIS C 1 77  ? 14.160  29.906  22.689  1.00 18.53 ? 77  HIS C CB  1 
ATOM   4883 C  CG  . HIS C 1 77  ? 13.507  30.379  21.426  1.00 18.09 ? 77  HIS C CG  1 
ATOM   4884 N  ND1 . HIS C 1 77  ? 13.549  31.671  21.023  1.00 19.19 ? 77  HIS C ND1 1 
ATOM   4885 C  CD2 . HIS C 1 77  ? 12.721  29.693  20.493  1.00 17.35 ? 77  HIS C CD2 1 
ATOM   4886 C  CE1 . HIS C 1 77  ? 12.850  31.797  19.868  1.00 17.17 ? 77  HIS C CE1 1 
ATOM   4887 N  NE2 . HIS C 1 77  ? 12.357  30.588  19.534  1.00 17.12 ? 77  HIS C NE2 1 
ATOM   4888 N  N   . ILE C 1 78  ? 14.712  26.883  22.525  1.00 15.52 ? 78  ILE C N   1 
ATOM   4889 C  CA  . ILE C 1 78  ? 14.180  25.678  21.869  1.00 16.83 ? 78  ILE C CA  1 
ATOM   4890 C  C   . ILE C 1 78  ? 12.683  25.743  21.738  1.00 18.46 ? 78  ILE C C   1 
ATOM   4891 O  O   . ILE C 1 78  ? 11.983  26.069  22.718  1.00 17.85 ? 78  ILE C O   1 
ATOM   4892 C  CB  . ILE C 1 78  ? 14.356  24.417  22.715  1.00 18.27 ? 78  ILE C CB  1 
ATOM   4893 C  CG1 . ILE C 1 78  ? 15.816  24.116  23.060  1.00 19.70 ? 78  ILE C CG1 1 
ATOM   4894 C  CG2 . ILE C 1 78  ? 13.704  23.210  22.021  1.00 17.48 ? 78  ILE C CG2 1 
ATOM   4895 C  CD1 . ILE C 1 78  ? 15.812  23.203  24.289  1.00 19.58 ? 78  ILE C CD1 1 
ATOM   4896 N  N   . GLN C 1 79  ? 12.203  25.414  20.551  1.00 19.71 ? 79  GLN C N   1 
ATOM   4897 C  CA  . GLN C 1 79  ? 10.805  25.310  20.300  1.00 23.91 ? 79  GLN C CA  1 
ATOM   4898 C  C   . GLN C 1 79  ? 10.517  23.841  19.939  1.00 23.45 ? 79  GLN C C   1 
ATOM   4899 O  O   . GLN C 1 79  ? 11.396  23.096  19.490  1.00 25.73 ? 79  GLN C O   1 
ATOM   4900 C  CB  . GLN C 1 79  ? 10.369  26.299  19.218  1.00 30.23 ? 79  GLN C CB  1 
ATOM   4901 C  CG  . GLN C 1 79  ? 10.502  25.824  17.778  1.00 36.94 ? 79  GLN C CG  1 
ATOM   4902 C  CD  . GLN C 1 79  ? 9.225   25.182  17.253  1.00 39.52 ? 79  GLN C CD  1 
ATOM   4903 O  OE1 . GLN C 1 79  ? 8.126   25.728  17.438  1.00 45.55 ? 79  GLN C OE1 1 
ATOM   4904 N  NE2 . GLN C 1 79  ? 9.357   23.996  16.608  1.00 36.73 ? 79  GLN C NE2 1 
ATOM   4905 N  N   . GLY C 1 80  ? 9.299   23.409  20.187  1.00 22.81 ? 80  GLY C N   1 
ATOM   4906 C  CA  . GLY C 1 80  ? 8.957   22.008  20.029  1.00 23.56 ? 80  GLY C CA  1 
ATOM   4907 C  C   . GLY C 1 80  ? 8.488   21.362  21.323  1.00 23.15 ? 80  GLY C C   1 
ATOM   4908 O  O   . GLY C 1 80  ? 7.745   20.387  21.304  1.00 21.64 ? 80  GLY C O   1 
ATOM   4909 N  N   . LEU C 1 81  ? 8.917   21.895  22.459  1.00 21.31 ? 81  LEU C N   1 
ATOM   4910 C  CA  . LEU C 1 81  ? 8.369   21.434  23.735  1.00 21.75 ? 81  LEU C CA  1 
ATOM   4911 C  C   . LEU C 1 81  ? 7.022   22.136  24.002  1.00 22.10 ? 81  LEU C C   1 
ATOM   4912 O  O   . LEU C 1 81  ? 6.643   23.014  23.220  1.00 21.33 ? 81  LEU C O   1 
ATOM   4913 C  CB  . LEU C 1 81  ? 9.378   21.661  24.878  1.00 19.02 ? 81  LEU C CB  1 
ATOM   4914 C  CG  . LEU C 1 81  ? 10.757  20.930  24.702  1.00 18.69 ? 81  LEU C CG  1 
ATOM   4915 C  CD1 . LEU C 1 81  ? 11.782  21.403  25.716  1.00 16.14 ? 81  LEU C CD1 1 
ATOM   4916 C  CD2 . LEU C 1 81  ? 10.662  19.409  24.717  1.00 18.46 ? 81  LEU C CD2 1 
ATOM   4917 N  N   . GLN C 1 82  ? 6.326   21.781  25.092  1.00 21.59 ? 82  GLN C N   1 
ATOM   4918 C  CA  . GLN C 1 82  ? 4.968   22.354  25.331  1.00 26.72 ? 82  GLN C CA  1 
ATOM   4919 C  C   . GLN C 1 82  ? 4.990   23.892  25.621  1.00 24.30 ? 82  GLN C C   1 
ATOM   4920 O  O   . GLN C 1 82  ? 4.168   24.666  25.129  1.00 26.98 ? 82  GLN C O   1 
ATOM   4921 C  CB  . GLN C 1 82  ? 4.151   21.459  26.293  1.00 30.03 ? 82  GLN C CB  1 
ATOM   4922 C  CG  . GLN C 1 82  ? 4.133   21.753  27.784  1.00 33.83 ? 82  GLN C CG  1 
ATOM   4923 C  CD  . GLN C 1 82  ? 5.471   22.093  28.438  1.00 36.42 ? 82  GLN C CD  1 
ATOM   4924 O  OE1 . GLN C 1 82  ? 6.565   21.654  28.011  1.00 40.56 ? 82  GLN C OE1 1 
ATOM   4925 N  NE2 . GLN C 1 82  ? 5.385   22.884  29.518  1.00 30.32 ? 82  GLN C NE2 1 
ATOM   4926 N  N   . SER C 1 83  ? 6.029   24.327  26.335  1.00 20.34 ? 83  SER C N   1 
ATOM   4927 C  CA  . SER C 1 83  ? 6.392   25.724  26.443  1.00 17.45 ? 83  SER C CA  1 
ATOM   4928 C  C   . SER C 1 83  ? 7.683   26.030  25.710  1.00 16.92 ? 83  SER C C   1 
ATOM   4929 O  O   . SER C 1 83  ? 8.479   25.136  25.416  1.00 15.00 ? 83  SER C O   1 
ATOM   4930 C  CB  . SER C 1 83  ? 6.639   26.088  27.894  1.00 16.45 ? 83  SER C CB  1 
ATOM   4931 O  OG  . SER C 1 83  ? 5.654   25.536  28.759  1.00 18.79 ? 83  SER C OG  1 
ATOM   4932 N  N   . ARG C 1 84  ? 7.911   27.330  25.485  1.00 15.92 ? 84  ARG C N   1 
ATOM   4933 C  CA  . ARG C 1 84  ? 9.209   27.803  25.070  1.00 14.88 ? 84  ARG C CA  1 
ATOM   4934 C  C   . ARG C 1 84  ? 10.199  27.738  26.226  1.00 14.16 ? 84  ARG C C   1 
ATOM   4935 O  O   . ARG C 1 84  ? 9.888   28.164  27.321  1.00 14.94 ? 84  ARG C O   1 
ATOM   4936 C  CB  . ARG C 1 84  ? 9.126   29.268  24.594  1.00 15.64 ? 84  ARG C CB  1 
ATOM   4937 C  CG  . ARG C 1 84  ? 10.473  29.802  24.078  1.00 14.38 ? 84  ARG C CG  1 
ATOM   4938 C  CD  . ARG C 1 84  ? 10.305  31.239  23.535  1.00 15.33 ? 84  ARG C CD  1 
ATOM   4939 N  NE  . ARG C 1 84  ? 9.773   31.176  22.172  1.00 14.50 ? 84  ARG C NE  1 
ATOM   4940 C  CZ  . ARG C 1 84  ? 9.729   32.222  21.346  1.00 14.61 ? 84  ARG C CZ  1 
ATOM   4941 N  NH1 . ARG C 1 84  ? 10.086  33.398  21.805  1.00 14.01 ? 84  ARG C NH1 1 
ATOM   4942 N  NH2 . ARG C 1 84  ? 9.272   32.108  20.092  1.00 12.67 ? 84  ARG C NH2 1 
ATOM   4943 N  N   . TYR C 1 85  ? 11.409  27.251  25.932  1.00 13.39 ? 85  TYR C N   1 
ATOM   4944 C  CA  . TYR C 1 85  ? 12.538  27.345  26.877  1.00 13.32 ? 85  TYR C CA  1 
ATOM   4945 C  C   . TYR C 1 85  ? 13.620  28.263  26.327  1.00 12.88 ? 85  TYR C C   1 
ATOM   4946 O  O   . TYR C 1 85  ? 14.153  27.985  25.264  1.00 13.93 ? 85  TYR C O   1 
ATOM   4947 C  CB  . TYR C 1 85  ? 13.112  25.950  27.143  1.00 13.89 ? 85  TYR C CB  1 
ATOM   4948 C  CG  . TYR C 1 85  ? 12.217  25.160  28.045  1.00 13.69 ? 85  TYR C CG  1 
ATOM   4949 C  CD1 . TYR C 1 85  ? 11.175  24.421  27.506  1.00 13.71 ? 85  TYR C CD1 1 
ATOM   4950 C  CD2 . TYR C 1 85  ? 12.432  25.130  29.422  1.00 13.37 ? 85  TYR C CD2 1 
ATOM   4951 C  CE1 . TYR C 1 85  ? 10.313  23.686  28.327  1.00 15.11 ? 85  TYR C CE1 1 
ATOM   4952 C  CE2 . TYR C 1 85  ? 11.591  24.400  30.246  1.00 13.87 ? 85  TYR C CE2 1 
ATOM   4953 C  CZ  . TYR C 1 85  ? 10.536  23.672  29.679  1.00 14.40 ? 85  TYR C CZ  1 
ATOM   4954 O  OH  . TYR C 1 85  ? 9.686   22.942  30.462  1.00 14.76 ? 85  TYR C OH  1 
ATOM   4955 N  N   . SER C 1 86  ? 13.988  29.307  27.037  1.00 12.32 ? 86  SER C N   1 
ATOM   4956 C  CA  . SER C 1 86  ? 15.054  30.213  26.527  1.00 13.09 ? 86  SER C CA  1 
ATOM   4957 C  C   . SER C 1 86  ? 16.446  29.903  27.125  1.00 13.41 ? 86  SER C C   1 
ATOM   4958 O  O   . SER C 1 86  ? 16.522  29.578  28.294  1.00 11.99 ? 86  SER C O   1 
ATOM   4959 C  CB  . SER C 1 86  ? 14.641  31.684  26.794  1.00 13.09 ? 86  SER C CB  1 
ATOM   4960 O  OG  . SER C 1 86  ? 13.321  31.912  26.224  1.00 12.34 ? 86  SER C OG  1 
ATOM   4961 N  N   . ALA C 1 87  ? 17.535  29.999  26.331  1.00 13.61 ? 87  ALA C N   1 
ATOM   4962 C  CA  . ALA C 1 87  ? 18.880  29.697  26.827  1.00 12.66 ? 87  ALA C CA  1 
ATOM   4963 C  C   . ALA C 1 87  ? 19.347  30.633  27.918  1.00 13.64 ? 87  ALA C C   1 
ATOM   4964 O  O   . ALA C 1 87  ? 18.961  31.814  27.969  1.00 12.60 ? 87  ALA C O   1 
ATOM   4965 C  CB  . ALA C 1 87  ? 19.909  29.650  25.667  1.00 12.35 ? 87  ALA C CB  1 
ATOM   4966 N  N   . THR C 1 88  ? 20.146  30.090  28.834  1.00 11.68 ? 88  THR C N   1 
ATOM   4967 C  CA  . THR C 1 88  ? 20.741  30.924  29.861  1.00 13.35 ? 88  THR C CA  1 
ATOM   4968 C  C   . THR C 1 88  ? 22.276  30.783  29.906  1.00 13.04 ? 88  THR C C   1 
ATOM   4969 O  O   . THR C 1 88  ? 23.003  31.807  30.073  1.00 13.24 ? 88  THR C O   1 
ATOM   4970 C  CB  . THR C 1 88  ? 20.045  30.675  31.248  1.00 13.32 ? 88  THR C CB  1 
ATOM   4971 O  OG1 . THR C 1 88  ? 20.695  31.470  32.253  1.00 14.43 ? 88  THR C OG1 1 
ATOM   4972 C  CG2 . THR C 1 88  ? 20.174  29.220  31.711  1.00 11.67 ? 88  THR C CG2 1 
ATOM   4973 N  N   . GLN C 1 89  ? 22.787  29.556  29.732  1.00 12.27 ? 89  GLN C N   1 
ATOM   4974 C  CA  . GLN C 1 89  ? 24.247  29.332  29.727  1.00 11.65 ? 89  GLN C CA  1 
ATOM   4975 C  C   . GLN C 1 89  ? 24.610  27.953  29.206  1.00 11.44 ? 89  GLN C C   1 
ATOM   4976 O  O   . GLN C 1 89  ? 23.715  27.033  29.171  1.00 10.60 ? 89  GLN C O   1 
ATOM   4977 C  CB  . GLN C 1 89  ? 24.811  29.528  31.138  1.00 14.24 ? 89  GLN C CB  1 
ATOM   4978 C  CG  . GLN C 1 89  ? 24.044  28.840  32.232  1.00 17.02 ? 89  GLN C CG  1 
ATOM   4979 C  CD  . GLN C 1 89  ? 24.755  27.636  32.804  1.00 20.39 ? 89  GLN C CD  1 
ATOM   4980 O  OE1 . GLN C 1 89  ? 25.561  27.005  32.155  1.00 22.82 ? 89  GLN C OE1 1 
ATOM   4981 N  NE2 . GLN C 1 89  ? 24.429  27.309  34.023  1.00 25.94 ? 89  GLN C NE2 1 
ATOM   4982 N  N   . LEU C 1 90  ? 25.870  27.773  28.800  1.00 10.15 ? 90  LEU C N   1 
ATOM   4983 C  CA  . LEU C 1 90  ? 26.364  26.401  28.592  1.00 10.22 ? 90  LEU C CA  1 
ATOM   4984 C  C   . LEU C 1 90  ? 27.622  26.185  29.371  1.00 10.17 ? 90  LEU C C   1 
ATOM   4985 O  O   . LEU C 1 90  ? 28.363  27.179  29.673  1.00 9.97  ? 90  LEU C O   1 
ATOM   4986 C  CB  . LEU C 1 90  ? 26.551  26.114  27.087  1.00 10.95 ? 90  LEU C CB  1 
ATOM   4987 C  CG  . LEU C 1 90  ? 27.416  27.035  26.236  1.00 10.46 ? 90  LEU C CG  1 
ATOM   4988 C  CD1 . LEU C 1 90  ? 28.891  26.747  26.496  1.00 10.88 ? 90  LEU C CD1 1 
ATOM   4989 C  CD2 . LEU C 1 90  ? 27.108  26.722  24.762  1.00 11.21 ? 90  LEU C CD2 1 
ATOM   4990 N  N   . HIS C 1 91  ? 27.943  24.909  29.619  1.00 10.06 ? 91  HIS C N   1 
ATOM   4991 C  CA  . HIS C 1 91  ? 29.122  24.598  30.424  1.00 9.68  ? 91  HIS C CA  1 
ATOM   4992 C  C   . HIS C 1 91  ? 29.515  23.144  30.178  1.00 9.37  ? 91  HIS C C   1 
ATOM   4993 O  O   . HIS C 1 91  ? 28.802  22.365  29.477  1.00 9.02  ? 91  HIS C O   1 
ATOM   4994 C  CB  . HIS C 1 91  ? 28.831  24.864  31.931  1.00 10.14 ? 91  HIS C CB  1 
ATOM   4995 C  CG  . HIS C 1 91  ? 27.750  23.964  32.507  1.00 10.78 ? 91  HIS C CG  1 
ATOM   4996 N  ND1 . HIS C 1 91  ? 26.475  24.377  32.733  1.00 10.75 ? 91  HIS C ND1 1 
ATOM   4997 C  CD2 . HIS C 1 91  ? 27.791  22.600  32.844  1.00 9.97  ? 91  HIS C CD2 1 
ATOM   4998 C  CE1 . HIS C 1 91  ? 25.740  23.319  33.167  1.00 11.01 ? 91  HIS C CE1 1 
ATOM   4999 N  NE2 . HIS C 1 91  ? 26.579  22.248  33.268  1.00 9.94  ? 91  HIS C NE2 1 
ATOM   5000 N  N   . LEU C 1 92  ? 30.652  22.779  30.738  1.00 9.47  ? 92  LEU C N   1 
ATOM   5001 C  CA  . LEU C 1 92  ? 31.235  21.434  30.530  1.00 9.35  ? 92  LEU C CA  1 
ATOM   5002 C  C   . LEU C 1 92  ? 31.571  20.624  31.782  1.00 9.68  ? 92  LEU C C   1 
ATOM   5003 O  O   . LEU C 1 92  ? 31.756  21.164  32.882  1.00 8.53  ? 92  LEU C O   1 
ATOM   5004 C  CB  . LEU C 1 92  ? 32.413  21.505  29.548  1.00 10.31 ? 92  LEU C CB  1 
ATOM   5005 C  CG  . LEU C 1 92  ? 32.066  21.962  28.098  1.00 11.10 ? 92  LEU C CG  1 
ATOM   5006 C  CD1 . LEU C 1 92  ? 32.669  23.377  28.023  1.00 9.81  ? 92  LEU C CD1 1 
ATOM   5007 C  CD2 . LEU C 1 92  ? 32.758  21.088  27.083  1.00 11.62 ? 92  LEU C CD2 1 
ATOM   5008 N  N   . HIS C 1 93  ? 31.602  19.297  31.594  1.00 10.00 ? 93  HIS C N   1 
ATOM   5009 C  CA  . HIS C 1 93  ? 32.080  18.334  32.647  1.00 10.14 ? 93  HIS C CA  1 
ATOM   5010 C  C   . HIS C 1 93  ? 33.145  17.411  32.040  1.00 10.48 ? 93  HIS C C   1 
ATOM   5011 O  O   . HIS C 1 93  ? 33.005  17.010  30.881  1.00 11.53 ? 93  HIS C O   1 
ATOM   5012 C  CB  . HIS C 1 93  ? 30.909  17.487  33.178  1.00 9.27  ? 93  HIS C CB  1 
ATOM   5013 C  CG  . HIS C 1 93  ? 29.737  18.318  33.745  1.00 9.43  ? 93  HIS C CG  1 
ATOM   5014 N  ND1 . HIS C 1 93  ? 29.634  18.673  35.048  1.00 9.81  ? 93  HIS C ND1 1 
ATOM   5015 C  CD2 . HIS C 1 93  ? 28.641  18.824  33.121  1.00 9.53  ? 93  HIS C CD2 1 
ATOM   5016 C  CE1 . HIS C 1 93  ? 28.523  19.385  35.243  1.00 10.26 ? 93  HIS C CE1 1 
ATOM   5017 N  NE2 . HIS C 1 93  ? 27.880  19.462  34.060  1.00 10.60 ? 93  HIS C NE2 1 
ATOM   5018 N  N   . TRP C 1 94  ? 34.205  17.127  32.807  1.00 10.05 ? 94  TRP C N   1 
ATOM   5019 C  CA  . TRP C 1 94  ? 35.325  16.266  32.336  1.00 9.22  ? 94  TRP C CA  1 
ATOM   5020 C  C   . TRP C 1 94  ? 36.099  15.534  33.413  1.00 8.57  ? 94  TRP C C   1 
ATOM   5021 O  O   . TRP C 1 94  ? 35.861  15.687  34.619  1.00 9.06  ? 94  TRP C O   1 
ATOM   5022 C  CB  . TRP C 1 94  ? 36.314  17.116  31.541  1.00 9.21  ? 94  TRP C CB  1 
ATOM   5023 C  CG  . TRP C 1 94  ? 36.890  18.302  32.368  1.00 8.87  ? 94  TRP C CG  1 
ATOM   5024 C  CD1 . TRP C 1 94  ? 38.002  18.272  33.167  1.00 9.19  ? 94  TRP C CD1 1 
ATOM   5025 C  CD2 . TRP C 1 94  ? 36.365  19.642  32.477  1.00 9.52  ? 94  TRP C CD2 1 
ATOM   5026 N  NE1 . TRP C 1 94  ? 38.204  19.508  33.749  1.00 9.66  ? 94  TRP C NE1 1 
ATOM   5027 C  CE2 . TRP C 1 94  ? 37.218  20.361  33.343  1.00 9.62  ? 94  TRP C CE2 1 
ATOM   5028 C  CE3 . TRP C 1 94  ? 35.270  20.305  31.918  1.00 9.29  ? 94  TRP C CE3 1 
ATOM   5029 C  CZ2 . TRP C 1 94  ? 37.000  21.705  33.665  1.00 9.70  ? 94  TRP C CZ2 1 
ATOM   5030 C  CZ3 . TRP C 1 94  ? 35.056  21.644  32.243  1.00 9.42  ? 94  TRP C CZ3 1 
ATOM   5031 C  CH2 . TRP C 1 94  ? 35.916  22.324  33.105  1.00 9.68  ? 94  TRP C CH2 1 
ATOM   5032 N  N   . GLY C 1 95  ? 37.007  14.657  32.988  1.00 9.22  ? 95  GLY C N   1 
ATOM   5033 C  CA  . GLY C 1 95  ? 37.722  13.749  33.921  1.00 11.31 ? 95  GLY C CA  1 
ATOM   5034 C  C   . GLY C 1 95  ? 39.121  14.283  34.230  1.00 11.70 ? 95  GLY C C   1 
ATOM   5035 O  O   . GLY C 1 95  ? 39.279  15.439  34.657  1.00 11.02 ? 95  GLY C O   1 
ATOM   5036 N  N   . ASN C 1 96  ? 40.154  13.490  33.917  1.00 12.20 ? 96  ASN C N   1 
ATOM   5037 C  CA  . ASN C 1 96  ? 41.544  13.940  34.208  1.00 14.53 ? 96  ASN C CA  1 
ATOM   5038 C  C   . ASN C 1 96  ? 42.485  13.110  33.331  1.00 13.98 ? 96  ASN C C   1 
ATOM   5039 O  O   . ASN C 1 96  ? 42.054  12.050  32.818  1.00 13.34 ? 96  ASN C O   1 
ATOM   5040 C  CB  . ASN C 1 96  ? 41.886  13.811  35.726  1.00 14.56 ? 96  ASN C CB  1 
ATOM   5041 C  CG  . ASN C 1 96  ? 42.178  12.340  36.160  1.00 17.67 ? 96  ASN C CG  1 
ATOM   5042 O  OD1 . ASN C 1 96  ? 43.341  11.841  36.122  1.00 17.81 ? 96  ASN C OD1 1 
ATOM   5043 N  ND2 . ASN C 1 96  ? 41.147  11.666  36.600  1.00 15.53 ? 96  ASN C ND2 1 
ATOM   5044 N  N   . PRO C 1 97  ? 43.723  13.587  33.117  1.00 15.26 ? 97  PRO C N   1 
ATOM   5045 C  CA  . PRO C 1 97  ? 44.632  12.935  32.134  1.00 16.36 ? 97  PRO C CA  1 
ATOM   5046 C  C   . PRO C 1 97  ? 44.942  11.449  32.447  1.00 16.82 ? 97  PRO C C   1 
ATOM   5047 O  O   . PRO C 1 97  ? 45.171  10.649  31.502  1.00 18.53 ? 97  PRO C O   1 
ATOM   5048 C  CB  . PRO C 1 97  ? 45.917  13.801  32.199  1.00 17.15 ? 97  PRO C CB  1 
ATOM   5049 C  CG  . PRO C 1 97  ? 45.412  15.170  32.659  1.00 18.20 ? 97  PRO C CG  1 
ATOM   5050 C  CD  . PRO C 1 97  ? 44.342  14.812  33.685  1.00 16.22 ? 97  PRO C CD  1 
ATOM   5051 N  N   . ASN C 1 98  ? 44.930  11.079  33.727  1.00 16.03 ? 98  ASN C N   1 
ATOM   5052 C  CA  . ASN C 1 98  ? 45.059  9.687   34.119  1.00 17.70 ? 98  ASN C CA  1 
ATOM   5053 C  C   . ASN C 1 98  ? 43.803  8.788   33.858  1.00 18.40 ? 98  ASN C C   1 
ATOM   5054 O  O   . ASN C 1 98  ? 43.931  7.553   33.751  1.00 20.43 ? 98  ASN C O   1 
ATOM   5055 C  CB  . ASN C 1 98  ? 45.386  9.610   35.597  1.00 20.62 ? 98  ASN C CB  1 
ATOM   5056 C  CG  . ASN C 1 98  ? 46.626  10.395  35.966  1.00 26.10 ? 98  ASN C CG  1 
ATOM   5057 O  OD1 . ASN C 1 98  ? 47.628  10.401  35.239  1.00 30.04 ? 98  ASN C OD1 1 
ATOM   5058 N  ND2 . ASN C 1 98  ? 46.571  11.056  37.101  1.00 29.84 ? 98  ASN C ND2 1 
ATOM   5059 N  N   . ASP C 1 99  ? 42.613  9.387   33.829  1.00 16.09 ? 99  ASP C N   1 
ATOM   5060 C  CA  . ASP C 1 99  ? 41.355  8.641   33.595  1.00 17.54 ? 99  ASP C CA  1 
ATOM   5061 C  C   . ASP C 1 99  ? 40.375  9.536   32.822  1.00 16.58 ? 99  ASP C C   1 
ATOM   5062 O  O   . ASP C 1 99  ? 39.456  10.107  33.411  1.00 19.27 ? 99  ASP C O   1 
ATOM   5063 C  CB  . ASP C 1 99  ? 40.746  8.132   34.917  1.00 19.12 ? 99  ASP C CB  1 
ATOM   5064 C  CG  . ASP C 1 99  ? 39.717  6.988   34.711  1.00 21.12 ? 99  ASP C CG  1 
ATOM   5065 O  OD1 . ASP C 1 99  ? 39.143  6.853   33.603  1.00 20.87 ? 99  ASP C OD1 1 
ATOM   5066 O  OD2 . ASP C 1 99  ? 39.475  6.220   35.681  1.00 21.49 ? 99  ASP C OD2 1 
ATOM   5067 N  N   . PRO C 1 100 ? 40.633  9.745   31.519  1.00 14.79 ? 100 PRO C N   1 
ATOM   5068 C  CA  . PRO C 1 100 ? 39.975  10.797  30.742  1.00 14.30 ? 100 PRO C CA  1 
ATOM   5069 C  C   . PRO C 1 100 ? 38.560  10.337  30.284  1.00 13.67 ? 100 PRO C C   1 
ATOM   5070 O  O   . PRO C 1 100 ? 38.235  10.278  29.072  1.00 13.13 ? 100 PRO C O   1 
ATOM   5071 C  CB  . PRO C 1 100 ? 40.875  10.959  29.527  1.00 14.62 ? 100 PRO C CB  1 
ATOM   5072 C  CG  . PRO C 1 100 ? 41.453  9.596   29.312  1.00 14.77 ? 100 PRO C CG  1 
ATOM   5073 C  CD  . PRO C 1 100 ? 41.547  8.945   30.686  1.00 16.04 ? 100 PRO C CD  1 
ATOM   5074 N  N   . HIS C 1 101 ? 37.737  10.061  31.280  1.00 13.70 ? 101 HIS C N   1 
ATOM   5075 C  CA  . HIS C 1 101 ? 36.374  9.587   31.053  1.00 14.59 ? 101 HIS C CA  1 
ATOM   5076 C  C   . HIS C 1 101 ? 35.445  10.269  32.037  1.00 14.38 ? 101 HIS C C   1 
ATOM   5077 O  O   . HIS C 1 101 ? 34.961  9.631   32.980  1.00 15.68 ? 101 HIS C O   1 
ATOM   5078 C  CB  . HIS C 1 101 ? 36.302  8.069   31.201  1.00 17.50 ? 101 HIS C CB  1 
ATOM   5079 C  CG  . HIS C 1 101 ? 37.311  7.345   30.360  1.00 19.48 ? 101 HIS C CG  1 
ATOM   5080 N  ND1 . HIS C 1 101 ? 38.451  6.847   30.873  1.00 22.14 ? 101 HIS C ND1 1 
ATOM   5081 C  CD2 . HIS C 1 101 ? 37.360  7.119   28.991  1.00 22.84 ? 101 HIS C CD2 1 
ATOM   5082 C  CE1 . HIS C 1 101 ? 39.181  6.315   29.891  1.00 21.57 ? 101 HIS C CE1 1 
ATOM   5083 N  NE2 . HIS C 1 101 ? 38.507  6.477   28.735  1.00 24.59 ? 101 HIS C NE2 1 
ATOM   5084 N  N   . GLY C 1 102 ? 35.141  11.545  31.808  1.00 11.68 ? 102 GLY C N   1 
ATOM   5085 C  CA  . GLY C 1 102 ? 34.289  12.260  32.765  1.00 10.58 ? 102 GLY C CA  1 
ATOM   5086 C  C   . GLY C 1 102 ? 33.004  12.868  32.205  1.00 10.62 ? 102 GLY C C   1 
ATOM   5087 O  O   . GLY C 1 102 ? 32.602  13.922  32.639  1.00 11.49 ? 102 GLY C O   1 
ATOM   5088 N  N   . SER C 1 103 ? 32.348  12.187  31.260  1.00 10.67 ? 103 SER C N   1 
ATOM   5089 C  CA  . SER C 1 103 ? 30.913  12.495  31.040  1.00 10.58 ? 103 SER C CA  1 
ATOM   5090 C  C   . SER C 1 103 ? 30.091  12.256  32.308  1.00 9.71  ? 103 SER C C   1 
ATOM   5091 O  O   . SER C 1 103 ? 30.525  11.558  33.230  1.00 10.76 ? 103 SER C O   1 
ATOM   5092 C  CB  . SER C 1 103 ? 30.365  11.722  29.822  1.00 9.29  ? 103 SER C CB  1 
ATOM   5093 O  OG  . SER C 1 103 ? 30.248  10.304  30.058  1.00 11.34 ? 103 SER C OG  1 
ATOM   5094 N  N   . GLU C 1 104 ? 28.902  12.836  32.370  1.00 8.47  ? 104 GLU C N   1 
ATOM   5095 C  CA  . GLU C 1 104 ? 27.977  12.575  33.454  1.00 8.52  ? 104 GLU C CA  1 
ATOM   5096 C  C   . GLU C 1 104 ? 27.068  11.386  33.131  1.00 8.65  ? 104 GLU C C   1 
ATOM   5097 O  O   . GLU C 1 104 ? 27.087  10.369  33.862  1.00 9.99  ? 104 GLU C O   1 
ATOM   5098 C  CB  . GLU C 1 104 ? 27.208  13.863  33.720  1.00 8.28  ? 104 GLU C CB  1 
ATOM   5099 C  CG  . GLU C 1 104 ? 28.180  15.015  34.132  1.00 9.10  ? 104 GLU C CG  1 
ATOM   5100 C  CD  . GLU C 1 104 ? 27.549  15.870  35.222  1.00 9.39  ? 104 GLU C CD  1 
ATOM   5101 O  OE1 . GLU C 1 104 ? 26.618  16.591  34.842  1.00 9.13  ? 104 GLU C OE1 1 
ATOM   5102 O  OE2 . GLU C 1 104 ? 27.951  15.830  36.441  1.00 9.18  ? 104 GLU C OE2 1 
ATOM   5103 N  N   . HIS C 1 105 ? 26.333  11.494  32.018  1.00 8.10  ? 105 HIS C N   1 
ATOM   5104 C  CA  . HIS C 1 105 ? 25.534  10.387  31.542  1.00 8.98  ? 105 HIS C CA  1 
ATOM   5105 C  C   . HIS C 1 105 ? 26.463  9.322   30.986  1.00 9.09  ? 105 HIS C C   1 
ATOM   5106 O  O   . HIS C 1 105 ? 27.512  9.605   30.426  1.00 9.76  ? 105 HIS C O   1 
ATOM   5107 C  CB  . HIS C 1 105 ? 24.526  10.857  30.482  1.00 8.52  ? 105 HIS C CB  1 
ATOM   5108 C  CG  . HIS C 1 105 ? 23.420  11.684  31.068  1.00 8.49  ? 105 HIS C CG  1 
ATOM   5109 N  ND1 . HIS C 1 105 ? 23.472  13.061  31.142  1.00 8.54  ? 105 HIS C ND1 1 
ATOM   5110 C  CD2 . HIS C 1 105 ? 22.257  11.321  31.659  1.00 9.11  ? 105 HIS C CD2 1 
ATOM   5111 C  CE1 . HIS C 1 105 ? 22.376  13.511  31.727  1.00 8.01  ? 105 HIS C CE1 1 
ATOM   5112 N  NE2 . HIS C 1 105 ? 21.623  12.475  32.050  1.00 9.13  ? 105 HIS C NE2 1 
ATOM   5113 N  N   . THR C 1 106 ? 26.061  8.066   31.139  1.00 10.50 ? 106 THR C N   1 
ATOM   5114 C  CA  . THR C 1 106 ? 26.826  6.965   30.616  1.00 10.33 ? 106 THR C CA  1 
ATOM   5115 C  C   . THR C 1 106 ? 25.889  6.168   29.678  1.00 10.34 ? 106 THR C C   1 
ATOM   5116 O  O   . THR C 1 106 ? 24.689  6.366   29.721  1.00 9.96  ? 106 THR C O   1 
ATOM   5117 C  CB  . THR C 1 106 ? 27.450  6.096   31.708  1.00 10.98 ? 106 THR C CB  1 
ATOM   5118 O  OG1 . THR C 1 106 ? 26.455  5.461   32.532  1.00 10.60 ? 106 THR C OG1 1 
ATOM   5119 C  CG2 . THR C 1 106 ? 28.427  6.873   32.598  1.00 10.90 ? 106 THR C CG2 1 
ATOM   5120 N  N   . VAL C 1 107 ? 26.442  5.378   28.770  1.00 11.60 ? 107 VAL C N   1 
ATOM   5121 C  CA  . VAL C 1 107 ? 25.593  4.583   27.827  1.00 12.21 ? 107 VAL C CA  1 
ATOM   5122 C  C   . VAL C 1 107 ? 26.048  3.145   27.907  1.00 14.32 ? 107 VAL C C   1 
ATOM   5123 O  O   . VAL C 1 107 ? 27.227  2.832   27.638  1.00 15.60 ? 107 VAL C O   1 
ATOM   5124 C  CB  . VAL C 1 107 ? 25.719  5.059   26.355  1.00 12.36 ? 107 VAL C CB  1 
ATOM   5125 C  CG1 . VAL C 1 107 ? 24.969  4.087   25.441  1.00 13.05 ? 107 VAL C CG1 1 
ATOM   5126 C  CG2 . VAL C 1 107 ? 25.231  6.521   26.126  1.00 12.64 ? 107 VAL C CG2 1 
ATOM   5127 N  N   . SER C 1 108 ? 25.123  2.248   28.240  1.00 15.75 ? 108 SER C N   1 
ATOM   5128 C  CA  . SER C 1 108 ? 25.467  0.837   28.476  1.00 17.43 ? 108 SER C CA  1 
ATOM   5129 C  C   . SER C 1 108 ? 26.721  0.701   29.350  1.00 17.78 ? 108 SER C C   1 
ATOM   5130 O  O   . SER C 1 108 ? 27.619  -0.080  29.031  1.00 17.55 ? 108 SER C O   1 
ATOM   5131 C  CB  . SER C 1 108 ? 25.629  0.097   27.134  1.00 19.40 ? 108 SER C CB  1 
ATOM   5132 O  OG  . SER C 1 108 ? 24.454  0.281   26.345  1.00 20.50 ? 108 SER C OG  1 
ATOM   5133 N  N   . GLY C 1 109 ? 26.774  1.479   30.440  1.00 14.83 ? 109 GLY C N   1 
ATOM   5134 C  CA  . GLY C 1 109 ? 27.913  1.481   31.304  1.00 16.22 ? 109 GLY C CA  1 
ATOM   5135 C  C   . GLY C 1 109 ? 29.124  2.329   30.922  1.00 17.41 ? 109 GLY C C   1 
ATOM   5136 O  O   . GLY C 1 109 ? 29.988  2.563   31.813  1.00 19.86 ? 109 GLY C O   1 
ATOM   5137 N  N   . GLN C 1 110 ? 29.234  2.725   29.641  1.00 17.53 ? 110 GLN C N   1 
ATOM   5138 C  CA  . GLN C 1 110 ? 30.443  3.404   29.098  1.00 18.47 ? 110 GLN C CA  1 
ATOM   5139 C  C   . GLN C 1 110 ? 30.435  4.933   29.377  1.00 17.60 ? 110 GLN C C   1 
ATOM   5140 O  O   . GLN C 1 110 ? 29.457  5.600   29.050  1.00 12.53 ? 110 GLN C O   1 
ATOM   5141 C  CB  . GLN C 1 110 ? 30.691  3.080   27.605  1.00 21.39 ? 110 GLN C CB  1 
ATOM   5142 C  CG  . GLN C 1 110 ? 30.313  4.196   26.590  1.00 25.27 ? 110 GLN C CG  1 
ATOM   5143 C  CD  . GLN C 1 110 ? 31.157  4.291   25.279  1.00 28.26 ? 110 GLN C CD  1 
ATOM   5144 O  OE1 . GLN C 1 110 ? 32.182  5.027   25.199  1.00 30.00 ? 110 GLN C OE1 1 
ATOM   5145 N  NE2 . GLN C 1 110 ? 30.683  3.605   24.222  1.00 23.78 ? 110 GLN C NE2 1 
ATOM   5146 N  N   . HIS C 1 111 ? 31.496  5.471   30.017  1.00 16.31 ? 111 HIS C N   1 
ATOM   5147 C  CA  . HIS C 1 111 ? 31.625  6.937   30.189  1.00 16.28 ? 111 HIS C CA  1 
ATOM   5148 C  C   . HIS C 1 111 ? 32.203  7.484   28.919  1.00 16.04 ? 111 HIS C C   1 
ATOM   5149 O  O   . HIS C 1 111 ? 33.074  6.824   28.334  1.00 18.61 ? 111 HIS C O   1 
ATOM   5150 C  CB  . HIS C 1 111 ? 32.694  7.291   31.221  1.00 17.20 ? 111 HIS C CB  1 
ATOM   5151 C  CG  . HIS C 1 111 ? 32.130  7.530   32.588  1.00 17.30 ? 111 HIS C CG  1 
ATOM   5152 N  ND1 . HIS C 1 111 ? 31.564  8.731   32.956  1.00 17.95 ? 111 HIS C ND1 1 
ATOM   5153 C  CD2 . HIS C 1 111 ? 32.027  6.719   33.668  1.00 19.99 ? 111 HIS C CD2 1 
ATOM   5154 C  CE1 . HIS C 1 111 ? 31.143  8.653   34.206  1.00 18.54 ? 111 HIS C CE1 1 
ATOM   5155 N  NE2 . HIS C 1 111 ? 31.414  7.443   34.662  1.00 19.35 ? 111 HIS C NE2 1 
ATOM   5156 N  N   . PHE C 1 112 ? 31.788  8.693   28.499  1.00 14.05 ? 112 PHE C N   1 
ATOM   5157 C  CA  . PHE C 1 112 ? 32.438  9.366   27.416  1.00 12.48 ? 112 PHE C CA  1 
ATOM   5158 C  C   . PHE C 1 112 ? 33.485  10.267  28.017  1.00 10.67 ? 112 PHE C C   1 
ATOM   5159 O  O   . PHE C 1 112 ? 33.601  10.313  29.191  1.00 10.71 ? 112 PHE C O   1 
ATOM   5160 C  CB  . PHE C 1 112 ? 31.414  10.080  26.494  1.00 13.81 ? 112 PHE C CB  1 
ATOM   5161 C  CG  . PHE C 1 112 ? 30.635  9.124   25.661  1.00 15.50 ? 112 PHE C CG  1 
ATOM   5162 C  CD1 . PHE C 1 112 ? 29.559  8.410   26.208  1.00 17.61 ? 112 PHE C CD1 1 
ATOM   5163 C  CD2 . PHE C 1 112 ? 31.007  8.879   24.312  1.00 18.68 ? 112 PHE C CD2 1 
ATOM   5164 C  CE1 . PHE C 1 112 ? 28.836  7.484   25.455  1.00 18.33 ? 112 PHE C CE1 1 
ATOM   5165 C  CE2 . PHE C 1 112 ? 30.252  7.962   23.548  1.00 18.75 ? 112 PHE C CE2 1 
ATOM   5166 C  CZ  . PHE C 1 112 ? 29.190  7.248   24.139  1.00 19.17 ? 112 PHE C CZ  1 
ATOM   5167 N  N   . ALA C 1 113 ? 34.377  10.846  27.200  1.00 10.39 ? 113 ALA C N   1 
ATOM   5168 C  CA  . ALA C 1 113 ? 35.468  11.728  27.672  1.00 9.70  ? 113 ALA C CA  1 
ATOM   5169 C  C   . ALA C 1 113 ? 34.977  12.945  28.421  1.00 8.99  ? 113 ALA C C   1 
ATOM   5170 O  O   . ALA C 1 113 ? 35.592  13.348  29.442  1.00 10.26 ? 113 ALA C O   1 
ATOM   5171 C  CB  . ALA C 1 113 ? 36.412  12.138  26.505  1.00 9.86  ? 113 ALA C CB  1 
ATOM   5172 N  N   . ALA C 1 114 ? 33.894  13.559  27.941  1.00 9.60  ? 114 ALA C N   1 
ATOM   5173 C  CA  . ALA C 1 114 ? 33.374  14.792  28.520  1.00 8.74  ? 114 ALA C CA  1 
ATOM   5174 C  C   . ALA C 1 114 ? 31.914  14.989  28.144  1.00 9.17  ? 114 ALA C C   1 
ATOM   5175 O  O   . ALA C 1 114 ? 31.374  14.190  27.373  1.00 8.55  ? 114 ALA C O   1 
ATOM   5176 C  CB  . ALA C 1 114 ? 34.189  16.022  28.052  1.00 8.72  ? 114 ALA C CB  1 
ATOM   5177 N  N   . GLU C 1 115 ? 31.276  16.052  28.690  1.00 9.94  ? 115 GLU C N   1 
ATOM   5178 C  CA  . GLU C 1 115 ? 29.892  16.338  28.362  1.00 9.31  ? 115 GLU C CA  1 
ATOM   5179 C  C   . GLU C 1 115 ? 29.615  17.847  28.328  1.00 10.08 ? 115 GLU C C   1 
ATOM   5180 O  O   . GLU C 1 115 ? 30.118  18.619  29.186  1.00 10.48 ? 115 GLU C O   1 
ATOM   5181 C  CB  . GLU C 1 115 ? 28.928  15.649  29.383  1.00 10.62 ? 115 GLU C CB  1 
ATOM   5182 C  CG  . GLU C 1 115 ? 27.431  15.590  28.981  1.00 9.81  ? 115 GLU C CG  1 
ATOM   5183 C  CD  . GLU C 1 115 ? 26.637  14.584  29.816  1.00 9.94  ? 115 GLU C CD  1 
ATOM   5184 O  OE1 . GLU C 1 115 ? 25.513  14.890  30.240  1.00 10.51 ? 115 GLU C OE1 1 
ATOM   5185 O  OE2 . GLU C 1 115 ? 27.164  13.506  30.104  1.00 11.09 ? 115 GLU C OE2 1 
ATOM   5186 N  N   . LEU C 1 116 ? 28.815  18.246  27.356  1.00 8.77  ? 116 LEU C N   1 
ATOM   5187 C  CA  . LEU C 1 116 ? 28.381  19.668  27.199  1.00 9.77  ? 116 LEU C CA  1 
ATOM   5188 C  C   . LEU C 1 116 ? 26.933  19.776  27.611  1.00 9.81  ? 116 LEU C C   1 
ATOM   5189 O  O   . LEU C 1 116 ? 26.112  18.962  27.172  1.00 10.53 ? 116 LEU C O   1 
ATOM   5190 C  CB  . LEU C 1 116 ? 28.487  20.081  25.723  1.00 10.03 ? 116 LEU C CB  1 
ATOM   5191 C  CG  . LEU C 1 116 ? 27.876  21.483  25.358  1.00 9.83  ? 116 LEU C CG  1 
ATOM   5192 C  CD1 . LEU C 1 116 ? 28.816  22.548  25.802  1.00 10.45 ? 116 LEU C CD1 1 
ATOM   5193 C  CD2 . LEU C 1 116 ? 27.711  21.596  23.839  1.00 10.64 ? 116 LEU C CD2 1 
ATOM   5194 N  N   . HIS C 1 117 ? 26.597  20.780  28.419  1.00 9.89  ? 117 HIS C N   1 
ATOM   5195 C  CA  . HIS C 1 117 ? 25.210  21.056  28.820  1.00 9.35  ? 117 HIS C CA  1 
ATOM   5196 C  C   . HIS C 1 117 ? 24.839  22.422  28.344  1.00 10.09 ? 117 HIS C C   1 
ATOM   5197 O  O   . HIS C 1 117 ? 25.610  23.372  28.536  1.00 9.03  ? 117 HIS C O   1 
ATOM   5198 C  CB  . HIS C 1 117 ? 25.007  20.990  30.329  1.00 9.22  ? 117 HIS C CB  1 
ATOM   5199 C  CG  . HIS C 1 117 ? 25.134  19.592  30.897  1.00 8.75  ? 117 HIS C CG  1 
ATOM   5200 N  ND1 . HIS C 1 117 ? 25.353  19.366  32.239  1.00 8.43  ? 117 HIS C ND1 1 
ATOM   5201 C  CD2 . HIS C 1 117 ? 24.964  18.339  30.298  1.00 8.54  ? 117 HIS C CD2 1 
ATOM   5202 C  CE1 . HIS C 1 117 ? 25.468  18.006  32.420  1.00 9.05  ? 117 HIS C CE1 1 
ATOM   5203 N  NE2 . HIS C 1 117 ? 25.153  17.395  31.263  1.00 7.90  ? 117 HIS C NE2 1 
ATOM   5204 N  N   . ILE C 1 118 ? 23.725  22.497  27.608  1.00 9.59  ? 118 ILE C N   1 
ATOM   5205 C  CA  . ILE C 1 118 ? 23.189  23.813  27.200  1.00 9.91  ? 118 ILE C CA  1 
ATOM   5206 C  C   . ILE C 1 118 ? 21.875  24.014  28.002  1.00 10.19 ? 118 ILE C C   1 
ATOM   5207 O  O   . ILE C 1 118 ? 20.844  23.313  27.745  1.00 10.57 ? 118 ILE C O   1 
ATOM   5208 C  CB  . ILE C 1 118 ? 22.919  23.858  25.679  1.00 10.91 ? 118 ILE C CB  1 
ATOM   5209 C  CG1 . ILE C 1 118 ? 24.161  23.366  24.897  1.00 10.77 ? 118 ILE C CG1 1 
ATOM   5210 C  CG2 . ILE C 1 118 ? 22.396  25.263  25.270  1.00 10.90 ? 118 ILE C CG2 1 
ATOM   5211 C  CD1 . ILE C 1 118 ? 23.942  23.340  23.384  1.00 12.29 ? 118 ILE C CD1 1 
ATOM   5212 N  N   . VAL C 1 119 ? 21.905  24.941  28.957  1.00 10.62 ? 119 VAL C N   1 
ATOM   5213 C  CA  . VAL C 1 119 ? 20.845  25.082  29.982  1.00 10.56 ? 119 VAL C CA  1 
ATOM   5214 C  C   . VAL C 1 119 ? 19.792  26.125  29.500  1.00 10.90 ? 119 VAL C C   1 
ATOM   5215 O  O   . VAL C 1 119 ? 20.181  27.190  29.010  1.00 12.87 ? 119 VAL C O   1 
ATOM   5216 C  CB  . VAL C 1 119 ? 21.470  25.502  31.376  1.00 10.01 ? 119 VAL C CB  1 
ATOM   5217 C  CG1 . VAL C 1 119 ? 20.406  25.743  32.441  1.00 9.91  ? 119 VAL C CG1 1 
ATOM   5218 C  CG2 . VAL C 1 119 ? 22.402  24.423  31.846  1.00 11.58 ? 119 VAL C CG2 1 
ATOM   5219 N  N   . HIS C 1 120 ? 18.500  25.793  29.608  1.00 10.56 ? 120 HIS C N   1 
ATOM   5220 C  CA  . HIS C 1 120 ? 17.398  26.695  29.194  1.00 11.14 ? 120 HIS C CA  1 
ATOM   5221 C  C   . HIS C 1 120 ? 16.376  26.766  30.305  1.00 11.57 ? 120 HIS C C   1 
ATOM   5222 O  O   . HIS C 1 120 ? 16.261  25.827  31.044  1.00 12.44 ? 120 HIS C O   1 
ATOM   5223 C  CB  . HIS C 1 120 ? 16.682  26.194  27.911  1.00 10.95 ? 120 HIS C CB  1 
ATOM   5224 C  CG  . HIS C 1 120 ? 17.587  25.936  26.696  1.00 10.99 ? 120 HIS C CG  1 
ATOM   5225 N  ND1 . HIS C 1 120 ? 18.397  24.848  26.601  1.00 11.70 ? 120 HIS C ND1 1 
ATOM   5226 C  CD2 . HIS C 1 120 ? 17.653  26.562  25.473  1.00 10.96 ? 120 HIS C CD2 1 
ATOM   5227 C  CE1 . HIS C 1 120 ? 19.017  24.824  25.404  1.00 11.15 ? 120 HIS C CE1 1 
ATOM   5228 N  NE2 . HIS C 1 120 ? 18.588  25.882  24.706  1.00 11.31 ? 120 HIS C NE2 1 
ATOM   5229 N  N   . TYR C 1 121 ? 15.589  27.835  30.381  1.00 11.27 ? 121 TYR C N   1 
ATOM   5230 C  CA  . TYR C 1 121 ? 14.506  27.930  31.397  1.00 13.51 ? 121 TYR C CA  1 
ATOM   5231 C  C   . TYR C 1 121 ? 13.166  28.202  30.715  1.00 13.54 ? 121 TYR C C   1 
ATOM   5232 O  O   . TYR C 1 121 ? 13.134  28.725  29.606  1.00 13.47 ? 121 TYR C O   1 
ATOM   5233 C  CB  . TYR C 1 121 ? 14.814  29.030  32.417  1.00 13.62 ? 121 TYR C CB  1 
ATOM   5234 C  CG  . TYR C 1 121 ? 14.750  30.457  31.833  1.00 15.41 ? 121 TYR C CG  1 
ATOM   5235 C  CD1 . TYR C 1 121 ? 13.633  31.271  32.023  1.00 17.21 ? 121 TYR C CD1 1 
ATOM   5236 C  CD2 . TYR C 1 121 ? 15.829  30.997  31.132  1.00 16.41 ? 121 TYR C CD2 1 
ATOM   5237 C  CE1 . TYR C 1 121 ? 13.595  32.592  31.500  1.00 18.44 ? 121 TYR C CE1 1 
ATOM   5238 C  CE2 . TYR C 1 121 ? 15.785  32.300  30.599  1.00 18.90 ? 121 TYR C CE2 1 
ATOM   5239 C  CZ  . TYR C 1 121 ? 14.677  33.089  30.801  1.00 19.34 ? 121 TYR C CZ  1 
ATOM   5240 O  OH  . TYR C 1 121 ? 14.680  34.364  30.275  1.00 19.23 ? 121 TYR C OH  1 
ATOM   5241 N  N   . ASN C 1 122 ? 12.079  27.903  31.421  1.00 13.64 ? 122 ASN C N   1 
ATOM   5242 C  CA  . ASN C 1 122 ? 10.750  27.985  30.872  1.00 14.75 ? 122 ASN C CA  1 
ATOM   5243 C  C   . ASN C 1 122 ? 10.308  29.450  30.952  1.00 13.95 ? 122 ASN C C   1 
ATOM   5244 O  O   . ASN C 1 122 ? 9.838   29.919  32.014  1.00 16.08 ? 122 ASN C O   1 
ATOM   5245 C  CB  . ASN C 1 122 ? 9.767   27.072  31.671  1.00 14.19 ? 122 ASN C CB  1 
ATOM   5246 C  CG  . ASN C 1 122 ? 8.417   26.963  30.979  1.00 14.56 ? 122 ASN C CG  1 
ATOM   5247 O  OD1 . ASN C 1 122 ? 7.982   27.923  30.292  1.00 15.40 ? 122 ASN C OD1 1 
ATOM   5248 N  ND2 . ASN C 1 122 ? 7.783   25.790  31.065  1.00 16.11 ? 122 ASN C ND2 1 
ATOM   5249 N  N   . SER C 1 123 ? 10.450  30.153  29.847  1.00 13.63 ? 123 SER C N   1 
ATOM   5250 C  CA  . SER C 1 123 ? 10.195  31.581  29.827  1.00 13.86 ? 123 SER C CA  1 
ATOM   5251 C  C   . SER C 1 123 ? 8.731   31.962  29.565  1.00 13.87 ? 123 SER C C   1 
ATOM   5252 O  O   . SER C 1 123 ? 8.399   33.149  29.573  1.00 15.36 ? 123 SER C O   1 
ATOM   5253 C  CB  . SER C 1 123 ? 11.145  32.248  28.811  1.00 14.49 ? 123 SER C CB  1 
ATOM   5254 O  OG  . SER C 1 123 ? 10.983  31.727  27.496  1.00 14.73 ? 123 SER C OG  1 
ATOM   5255 N  N   . ASP C 1 124 ? 7.894   30.970  29.260  1.00 14.39 ? 124 ASP C N   1 
ATOM   5256 C  CA  . ASP C 1 124 ? 6.446   31.160  29.178  1.00 16.05 ? 124 ASP C CA  1 
ATOM   5257 C  C   . ASP C 1 124 ? 5.851   31.224  30.565  1.00 16.56 ? 124 ASP C C   1 
ATOM   5258 O  O   . ASP C 1 124 ? 4.922   32.007  30.802  1.00 14.59 ? 124 ASP C O   1 
ATOM   5259 C  CB  . ASP C 1 124 ? 5.801   30.035  28.370  1.00 15.31 ? 124 ASP C CB  1 
ATOM   5260 C  CG  . ASP C 1 124 ? 6.011   30.215  26.848  1.00 15.90 ? 124 ASP C CG  1 
ATOM   5261 O  OD1 . ASP C 1 124 ? 6.281   31.349  26.356  1.00 17.25 ? 124 ASP C OD1 1 
ATOM   5262 O  OD2 . ASP C 1 124 ? 5.863   29.208  26.146  1.00 16.47 ? 124 ASP C OD2 1 
ATOM   5263 N  N   . LEU C 1 125 ? 6.412   30.416  31.483  1.00 16.50 ? 125 LEU C N   1 
ATOM   5264 C  CA  . LEU C 1 125 ? 5.946   30.351  32.875  1.00 17.02 ? 125 LEU C CA  1 
ATOM   5265 C  C   . LEU C 1 125 ? 6.711   31.258  33.830  1.00 17.79 ? 125 LEU C C   1 
ATOM   5266 O  O   . LEU C 1 125 ? 6.092   31.770  34.798  1.00 18.33 ? 125 LEU C O   1 
ATOM   5267 C  CB  . LEU C 1 125 ? 5.914   28.899  33.429  1.00 16.97 ? 125 LEU C CB  1 
ATOM   5268 C  CG  . LEU C 1 125 ? 5.051   27.841  32.729  1.00 17.55 ? 125 LEU C CG  1 
ATOM   5269 C  CD1 . LEU C 1 125 ? 5.266   26.448  33.342  1.00 18.76 ? 125 LEU C CD1 1 
ATOM   5270 C  CD2 . LEU C 1 125 ? 3.536   28.211  32.681  1.00 16.76 ? 125 LEU C CD2 1 
ATOM   5271 N  N   . TYR C 1 126 ? 8.004   31.506  33.590  1.00 17.51 ? 126 TYR C N   1 
ATOM   5272 C  CA  . TYR C 1 126 ? 8.801   32.274  34.529  1.00 18.19 ? 126 TYR C CA  1 
ATOM   5273 C  C   . TYR C 1 126 ? 9.597   33.396  33.876  1.00 20.79 ? 126 TYR C C   1 
ATOM   5274 O  O   . TYR C 1 126 ? 9.932   33.307  32.704  1.00 21.24 ? 126 TYR C O   1 
ATOM   5275 C  CB  . TYR C 1 126 ? 9.720   31.330  35.358  1.00 18.21 ? 126 TYR C CB  1 
ATOM   5276 C  CG  . TYR C 1 126 ? 8.987   30.126  35.896  1.00 17.26 ? 126 TYR C CG  1 
ATOM   5277 C  CD1 . TYR C 1 126 ? 9.186   28.874  35.318  1.00 17.16 ? 126 TYR C CD1 1 
ATOM   5278 C  CD2 . TYR C 1 126 ? 8.060   30.233  36.959  1.00 17.90 ? 126 TYR C CD2 1 
ATOM   5279 C  CE1 . TYR C 1 126 ? 8.489   27.753  35.744  1.00 19.63 ? 126 TYR C CE1 1 
ATOM   5280 C  CE2 . TYR C 1 126 ? 7.346   29.129  37.395  1.00 18.65 ? 126 TYR C CE2 1 
ATOM   5281 C  CZ  . TYR C 1 126 ? 7.575   27.875  36.809  1.00 20.17 ? 126 TYR C CZ  1 
ATOM   5282 O  OH  . TYR C 1 126 ? 6.895   26.722  37.201  1.00 19.49 ? 126 TYR C OH  1 
ATOM   5283 N  N   . PRO C 1 127 ? 9.941   34.461  34.646  1.00 24.59 ? 127 PRO C N   1 
ATOM   5284 C  CA  . PRO C 1 127 ? 10.595  35.645  34.061  1.00 25.74 ? 127 PRO C CA  1 
ATOM   5285 C  C   . PRO C 1 127 ? 12.096  35.537  33.771  1.00 27.90 ? 127 PRO C C   1 
ATOM   5286 O  O   . PRO C 1 127 ? 12.585  36.252  32.904  1.00 25.31 ? 127 PRO C O   1 
ATOM   5287 C  CB  . PRO C 1 127 ? 10.386  36.719  35.133  1.00 27.80 ? 127 PRO C CB  1 
ATOM   5288 C  CG  . PRO C 1 127 ? 10.283  35.955  36.394  1.00 24.65 ? 127 PRO C CG  1 
ATOM   5289 C  CD  . PRO C 1 127 ? 9.507   34.728  36.029  1.00 24.11 ? 127 PRO C CD  1 
ATOM   5290 N  N   . ASP C 1 128 ? 12.811  34.682  34.505  1.00 26.12 ? 128 ASP C N   1 
ATOM   5291 C  CA  . ASP C 1 128 ? 14.279  34.474  34.327  1.00 25.01 ? 128 ASP C CA  1 
ATOM   5292 C  C   . ASP C 1 128 ? 14.716  33.083  34.849  1.00 22.58 ? 128 ASP C C   1 
ATOM   5293 O  O   . ASP C 1 128 ? 13.921  32.392  35.489  1.00 21.67 ? 128 ASP C O   1 
ATOM   5294 C  CB  . ASP C 1 128 ? 15.100  35.599  35.008  1.00 24.26 ? 128 ASP C CB  1 
ATOM   5295 C  CG  . ASP C 1 128 ? 14.631  35.909  36.411  1.00 28.72 ? 128 ASP C CG  1 
ATOM   5296 O  OD1 . ASP C 1 128 ? 14.277  37.084  36.693  1.00 29.30 ? 128 ASP C OD1 1 
ATOM   5297 O  OD2 . ASP C 1 128 ? 14.605  34.988  37.257  1.00 28.56 ? 128 ASP C OD2 1 
ATOM   5298 N  N   . ALA C 1 129 ? 15.961  32.684  34.558  1.00 23.38 ? 129 ALA C N   1 
ATOM   5299 C  CA  . ALA C 1 129 ? 16.515  31.377  34.987  1.00 21.24 ? 129 ALA C CA  1 
ATOM   5300 C  C   . ALA C 1 129 ? 16.508  31.193  36.521  1.00 22.53 ? 129 ALA C C   1 
ATOM   5301 O  O   . ALA C 1 129 ? 16.155  30.110  36.994  1.00 19.37 ? 129 ALA C O   1 
ATOM   5302 C  CB  . ALA C 1 129 ? 17.920  31.178  34.428  1.00 19.78 ? 129 ALA C CB  1 
ATOM   5303 N  N   . SER C 1 130 ? 16.877  32.248  37.266  1.00 23.33 ? 130 SER C N   1 
ATOM   5304 C  CA  . SER C 1 130 ? 16.926  32.213  38.734  1.00 26.16 ? 130 SER C CA  1 
ATOM   5305 C  C   . SER C 1 130 ? 15.548  31.871  39.332  1.00 26.96 ? 130 SER C C   1 
ATOM   5306 O  O   . SER C 1 130 ? 15.447  30.968  40.173  1.00 27.87 ? 130 SER C O   1 
ATOM   5307 C  CB  . SER C 1 130 ? 17.514  33.520  39.313  1.00 30.79 ? 130 SER C CB  1 
ATOM   5308 O  OG  . SER C 1 130 ? 17.750  33.409  40.717  1.00 32.08 ? 130 SER C OG  1 
ATOM   5309 N  N   . THR C 1 131 ? 14.471  32.528  38.908  1.00 24.47 ? 131 THR C N   1 
ATOM   5310 C  CA  . THR C 1 131 ? 13.175  32.124  39.449  1.00 23.83 ? 131 THR C CA  1 
ATOM   5311 C  C   . THR C 1 131 ? 12.583  30.798  38.893  1.00 22.64 ? 131 THR C C   1 
ATOM   5312 O  O   . THR C 1 131 ? 11.871  30.084  39.595  1.00 23.09 ? 131 THR C O   1 
ATOM   5313 C  CB  . THR C 1 131 ? 12.174  33.318  39.663  1.00 27.34 ? 131 THR C CB  1 
ATOM   5314 O  OG1 . THR C 1 131 ? 10.860  32.994  39.206  1.00 31.44 ? 131 THR C OG1 1 
ATOM   5315 C  CG2 . THR C 1 131 ? 12.676  34.627  39.070  1.00 22.72 ? 131 THR C CG2 1 
ATOM   5316 N  N   . ALA C 1 132 ? 12.941  30.419  37.672  1.00 19.83 ? 132 ALA C N   1 
ATOM   5317 C  CA  . ALA C 1 132 ? 12.518  29.099  37.139  1.00 18.58 ? 132 ALA C CA  1 
ATOM   5318 C  C   . ALA C 1 132 ? 13.178  27.895  37.846  1.00 20.63 ? 132 ALA C C   1 
ATOM   5319 O  O   . ALA C 1 132 ? 12.582  26.812  37.953  1.00 18.08 ? 132 ALA C O   1 
ATOM   5320 C  CB  . ALA C 1 132 ? 12.786  29.026  35.630  1.00 18.68 ? 132 ALA C CB  1 
ATOM   5321 N  N   . SER C 1 133 ? 14.394  28.116  38.350  1.00 22.57 ? 133 SER C N   1 
ATOM   5322 C  CA  . SER C 1 133 ? 15.313  27.009  38.638  1.00 25.45 ? 133 SER C CA  1 
ATOM   5323 C  C   . SER C 1 133 ? 14.750  26.022  39.634  1.00 23.05 ? 133 SER C C   1 
ATOM   5324 O  O   . SER C 1 133 ? 14.965  24.812  39.500  1.00 21.77 ? 133 SER C O   1 
ATOM   5325 C  CB  . SER C 1 133 ? 16.669  27.544  39.114  1.00 26.05 ? 133 SER C CB  1 
ATOM   5326 O  OG  . SER C 1 133 ? 16.534  28.247  40.337  1.00 32.61 ? 133 SER C OG  1 
ATOM   5327 N  N   . ASN C 1 134 ? 14.070  26.553  40.661  1.00 23.54 ? 134 ASN C N   1 
ATOM   5328 C  CA  . ASN C 1 134 ? 13.494  25.726  41.704  1.00 23.47 ? 134 ASN C CA  1 
ATOM   5329 C  C   . ASN C 1 134 ? 11.989  25.472  41.557  1.00 23.10 ? 134 ASN C C   1 
ATOM   5330 O  O   . ASN C 1 134 ? 11.351  25.006  42.483  1.00 22.91 ? 134 ASN C O   1 
ATOM   5331 C  CB  . ASN C 1 134 ? 13.831  26.261  43.118  1.00 23.88 ? 134 ASN C CB  1 
ATOM   5332 C  CG  . ASN C 1 134 ? 13.062  27.531  43.480  1.00 27.88 ? 134 ASN C CG  1 
ATOM   5333 O  OD1 . ASN C 1 134 ? 12.425  28.166  42.629  1.00 29.73 ? 134 ASN C OD1 1 
ATOM   5334 N  ND2 . ASN C 1 134 ? 13.111  27.897  44.763  1.00 27.35 ? 134 ASN C ND2 1 
ATOM   5335 N  N   . LYS C 1 135 ? 11.448  25.727  40.371  1.00 23.06 ? 135 LYS C N   1 
ATOM   5336 C  CA  . LYS C 1 135 ? 10.022  25.657  40.146  1.00 23.37 ? 135 LYS C CA  1 
ATOM   5337 C  C   . LYS C 1 135 ? 9.591   24.626  39.089  1.00 23.83 ? 135 LYS C C   1 
ATOM   5338 O  O   . LYS C 1 135 ? 10.405  24.156  38.249  1.00 20.72 ? 135 LYS C O   1 
ATOM   5339 C  CB  . LYS C 1 135 ? 9.422   27.081  39.885  1.00 24.71 ? 135 LYS C CB  1 
ATOM   5340 C  CG  . LYS C 1 135 ? 9.338   27.937  41.164  1.00 27.86 ? 135 LYS C CG  1 
ATOM   5341 C  CD  . LYS C 1 135 ? 8.898   29.375  40.936  1.00 27.82 ? 135 LYS C CD  1 
ATOM   5342 C  CE  . LYS C 1 135 ? 9.251   30.317  42.103  1.00 30.45 ? 135 LYS C CE  1 
ATOM   5343 N  NZ  . LYS C 1 135 ? 10.704  30.649  42.335  1.00 27.48 ? 135 LYS C NZ  1 
ATOM   5344 N  N   . SER C 1 136 ? 8.315   24.231  39.195  1.00 21.07 ? 136 SER C N   1 
ATOM   5345 C  CA  . SER C 1 136 ? 7.697   23.213  38.341  1.00 22.22 ? 136 SER C CA  1 
ATOM   5346 C  C   . SER C 1 136 ? 7.948   23.449  36.841  1.00 22.42 ? 136 SER C C   1 
ATOM   5347 O  O   . SER C 1 136 ? 7.680   24.567  36.352  1.00 21.90 ? 136 SER C O   1 
ATOM   5348 C  CB  . SER C 1 136 ? 6.196   23.227  38.605  1.00 25.70 ? 136 SER C CB  1 
ATOM   5349 O  OG  . SER C 1 136 ? 5.606   22.192  37.859  1.00 29.61 ? 136 SER C OG  1 
ATOM   5350 N  N   . GLU C 1 137 ? 8.421   22.416  36.123  1.00 19.28 ? 137 GLU C N   1 
ATOM   5351 C  CA  . GLU C 1 137 ? 8.857   22.529  34.706  1.00 20.94 ? 137 GLU C CA  1 
ATOM   5352 C  C   . GLU C 1 137 ? 9.783   23.749  34.394  1.00 19.63 ? 137 GLU C C   1 
ATOM   5353 O  O   . GLU C 1 137 ? 9.762   24.351  33.294  1.00 19.42 ? 137 GLU C O   1 
ATOM   5354 C  CB  . GLU C 1 137 ? 7.619   22.463  33.788  1.00 23.52 ? 137 GLU C CB  1 
ATOM   5355 C  CG  . GLU C 1 137 ? 7.088   21.027  33.683  1.00 29.20 ? 137 GLU C CG  1 
ATOM   5356 C  CD  . GLU C 1 137 ? 5.802   20.906  32.881  1.00 34.48 ? 137 GLU C CD  1 
ATOM   5357 O  OE1 . GLU C 1 137 ? 5.031   21.900  32.805  1.00 34.12 ? 137 GLU C OE1 1 
ATOM   5358 O  OE2 . GLU C 1 137 ? 5.556   19.801  32.336  1.00 38.61 ? 137 GLU C OE2 1 
ATOM   5359 N  N   . GLY C 1 138 ? 10.622  24.090  35.360  1.00 15.94 ? 138 GLY C N   1 
ATOM   5360 C  CA  . GLY C 1 138 ? 11.425  25.314  35.259  1.00 14.24 ? 138 GLY C CA  1 
ATOM   5361 C  C   . GLY C 1 138 ? 12.509  25.248  34.182  1.00 13.76 ? 138 GLY C C   1 
ATOM   5362 O  O   . GLY C 1 138 ? 12.850  26.288  33.596  1.00 13.93 ? 138 GLY C O   1 
ATOM   5363 N  N   . LEU C 1 139 ? 13.099  24.063  33.986  1.00 12.12 ? 139 LEU C N   1 
ATOM   5364 C  CA  . LEU C 1 139 ? 14.369  23.947  33.213  1.00 11.24 ? 139 LEU C CA  1 
ATOM   5365 C  C   . LEU C 1 139 ? 14.366  22.871  32.182  1.00 10.82 ? 139 LEU C C   1 
ATOM   5366 O  O   . LEU C 1 139 ? 13.670  21.822  32.317  1.00 12.17 ? 139 LEU C O   1 
ATOM   5367 C  CB  . LEU C 1 139 ? 15.621  23.777  34.157  1.00 11.07 ? 139 LEU C CB  1 
ATOM   5368 C  CG  . LEU C 1 139 ? 15.887  24.823  35.240  1.00 11.47 ? 139 LEU C CG  1 
ATOM   5369 C  CD1 . LEU C 1 139 ? 16.846  24.226  36.291  1.00 11.89 ? 139 LEU C CD1 1 
ATOM   5370 C  CD2 . LEU C 1 139 ? 16.368  26.181  34.721  1.00 11.69 ? 139 LEU C CD2 1 
ATOM   5371 N  N   . ALA C 1 140 ? 15.119  23.107  31.086  1.00 11.77 ? 140 ALA C N   1 
ATOM   5372 C  CA  . ALA C 1 140 ? 15.382  22.084  30.081  1.00 11.07 ? 140 ALA C CA  1 
ATOM   5373 C  C   . ALA C 1 140 ? 16.848  22.115  29.656  1.00 11.39 ? 140 ALA C C   1 
ATOM   5374 O  O   . ALA C 1 140 ? 17.389  23.197  29.320  1.00 11.39 ? 140 ALA C O   1 
ATOM   5375 C  CB  . ALA C 1 140 ? 14.475  22.237  28.833  1.00 10.53 ? 140 ALA C CB  1 
ATOM   5376 N  N   . VAL C 1 141 ? 17.500  20.947  29.707  1.00 10.91 ? 141 VAL C N   1 
ATOM   5377 C  CA  . VAL C 1 141 ? 18.934  20.856  29.383  1.00 11.99 ? 141 VAL C CA  1 
ATOM   5378 C  C   . VAL C 1 141 ? 19.177  19.936  28.190  1.00 11.01 ? 141 VAL C C   1 
ATOM   5379 O  O   . VAL C 1 141 ? 18.573  18.820  28.082  1.00 10.24 ? 141 VAL C O   1 
ATOM   5380 C  CB  . VAL C 1 141 ? 19.839  20.506  30.640  1.00 12.67 ? 141 VAL C CB  1 
ATOM   5381 C  CG1 . VAL C 1 141 ? 21.321  20.605  30.261  1.00 12.26 ? 141 VAL C CG1 1 
ATOM   5382 C  CG2 . VAL C 1 141 ? 19.513  21.409  31.785  1.00 13.48 ? 141 VAL C CG2 1 
ATOM   5383 N  N   . LEU C 1 142 ? 20.029  20.386  27.269  1.00 11.19 ? 142 LEU C N   1 
ATOM   5384 C  CA  . LEU C 1 142 ? 20.450  19.563  26.145  1.00 12.15 ? 142 LEU C CA  1 
ATOM   5385 C  C   . LEU C 1 142 ? 21.814  19.071  26.534  1.00 11.95 ? 142 LEU C C   1 
ATOM   5386 O  O   . LEU C 1 142 ? 22.673  19.881  26.916  1.00 12.44 ? 142 LEU C O   1 
ATOM   5387 C  CB  . LEU C 1 142 ? 20.550  20.359  24.840  1.00 13.17 ? 142 LEU C CB  1 
ATOM   5388 C  CG  . LEU C 1 142 ? 19.335  21.197  24.408  1.00 13.82 ? 142 LEU C CG  1 
ATOM   5389 C  CD1 . LEU C 1 142 ? 19.610  21.733  22.996  1.00 14.59 ? 142 LEU C CD1 1 
ATOM   5390 C  CD2 . LEU C 1 142 ? 18.110  20.296  24.316  1.00 13.52 ? 142 LEU C CD2 1 
ATOM   5391 N  N   . ALA C 1 143 ? 22.021  17.759  26.421  1.00 10.29 ? 143 ALA C N   1 
ATOM   5392 C  CA  . ALA C 1 143 ? 23.354  17.143  26.746  1.00 10.85 ? 143 ALA C CA  1 
ATOM   5393 C  C   . ALA C 1 143 ? 24.009  16.574  25.481  1.00 10.03 ? 143 ALA C C   1 
ATOM   5394 O  O   . ALA C 1 143 ? 23.384  15.765  24.729  1.00 10.58 ? 143 ALA C O   1 
ATOM   5395 C  CB  . ALA C 1 143 ? 23.248  16.054  27.831  1.00 10.63 ? 143 ALA C CB  1 
ATOM   5396 N  N   A VAL C 1 144 ? 25.246  16.995  25.235  0.50 9.56  ? 144 VAL C N   1 
ATOM   5397 N  N   B VAL C 1 144 ? 25.241  16.993  25.231  0.50 9.79  ? 144 VAL C N   1 
ATOM   5398 C  CA  A VAL C 1 144 ? 26.086  16.442  24.150  0.50 9.61  ? 144 VAL C CA  1 
ATOM   5399 C  CA  B VAL C 1 144 ? 26.063  16.413  24.158  0.50 10.04 ? 144 VAL C CA  1 
ATOM   5400 C  C   A VAL C 1 144 ? 27.260  15.653  24.694  0.50 9.71  ? 144 VAL C C   1 
ATOM   5401 C  C   B VAL C 1 144 ? 27.209  15.631  24.750  0.50 9.95  ? 144 VAL C C   1 
ATOM   5402 O  O   A VAL C 1 144 ? 28.116  16.222  25.415  0.50 10.38 ? 144 VAL C O   1 
ATOM   5403 O  O   B VAL C 1 144 ? 27.998  16.187  25.549  0.50 10.60 ? 144 VAL C O   1 
ATOM   5404 C  CB  A VAL C 1 144 ? 26.628  17.537  23.188  0.50 9.55  ? 144 VAL C CB  1 
ATOM   5405 C  CB  B VAL C 1 144 ? 26.694  17.485  23.248  0.50 10.32 ? 144 VAL C CB  1 
ATOM   5406 C  CG1 A VAL C 1 144 ? 27.507  16.899  22.110  0.50 8.62  ? 144 VAL C CG1 1 
ATOM   5407 C  CG1 B VAL C 1 144 ? 25.667  18.522  22.794  0.50 10.27 ? 144 VAL C CG1 1 
ATOM   5408 C  CG2 A VAL C 1 144 ? 25.480  18.338  22.567  0.50 9.45  ? 144 VAL C CG2 1 
ATOM   5409 C  CG2 B VAL C 1 144 ? 27.862  18.115  23.973  0.50 9.97  ? 144 VAL C CG2 1 
ATOM   5410 N  N   . LEU C 1 145 ? 27.298  14.353  24.350  1.00 9.91  ? 145 LEU C N   1 
ATOM   5411 C  CA  . LEU C 1 145 ? 28.383  13.456  24.736  1.00 10.47 ? 145 LEU C CA  1 
ATOM   5412 C  C   . LEU C 1 145 ? 29.590  13.730  23.874  1.00 10.42 ? 145 LEU C C   1 
ATOM   5413 O  O   . LEU C 1 145 ? 29.460  13.825  22.663  1.00 10.49 ? 145 LEU C O   1 
ATOM   5414 C  CB  . LEU C 1 145 ? 27.954  11.939  24.618  1.00 10.91 ? 145 LEU C CB  1 
ATOM   5415 C  CG  . LEU C 1 145 ? 26.705  11.517  25.430  1.00 11.39 ? 145 LEU C CG  1 
ATOM   5416 C  CD1 . LEU C 1 145 ? 26.182  10.151  25.086  1.00 11.10 ? 145 LEU C CD1 1 
ATOM   5417 C  CD2 . LEU C 1 145 ? 27.048  11.522  26.920  1.00 10.97 ? 145 LEU C CD2 1 
ATOM   5418 N  N   . ILE C 1 146 ? 30.767  13.886  24.517  1.00 12.10 ? 146 ILE C N   1 
ATOM   5419 C  CA  . ILE C 1 146 ? 32.039  14.170  23.836  1.00 11.15 ? 146 ILE C CA  1 
ATOM   5420 C  C   . ILE C 1 146 ? 33.062  12.993  23.929  1.00 13.60 ? 146 ILE C C   1 
ATOM   5421 O  O   . ILE C 1 146 ? 33.398  12.498  25.000  1.00 11.65 ? 146 ILE C O   1 
ATOM   5422 C  CB  . ILE C 1 146 ? 32.680  15.418  24.442  1.00 11.80 ? 146 ILE C CB  1 
ATOM   5423 C  CG1 . ILE C 1 146 ? 31.709  16.627  24.307  1.00 11.34 ? 146 ILE C CG1 1 
ATOM   5424 C  CG2 . ILE C 1 146 ? 34.033  15.702  23.802  1.00 10.31 ? 146 ILE C CG2 1 
ATOM   5425 C  CD1 . ILE C 1 146 ? 32.188  17.842  25.031  1.00 11.47 ? 146 ILE C CD1 1 
ATOM   5426 N  N   . GLU C 1 147 ? 33.570  12.576  22.799  1.00 14.31 ? 147 GLU C N   1 
ATOM   5427 C  CA  . GLU C 1 147 ? 34.632  11.563  22.769  1.00 17.83 ? 147 GLU C CA  1 
ATOM   5428 C  C   . GLU C 1 147 ? 35.928  12.095  22.175  1.00 17.77 ? 147 GLU C C   1 
ATOM   5429 O  O   . GLU C 1 147 ? 35.936  13.124  21.493  1.00 18.11 ? 147 GLU C O   1 
ATOM   5430 C  CB  . GLU C 1 147 ? 34.166  10.252  22.066  1.00 19.88 ? 147 GLU C CB  1 
ATOM   5431 C  CG  . GLU C 1 147 ? 33.666  10.365  20.648  1.00 23.39 ? 147 GLU C CG  1 
ATOM   5432 C  CD  . GLU C 1 147 ? 33.297  9.012   20.040  1.00 26.90 ? 147 GLU C CD  1 
ATOM   5433 O  OE1 . GLU C 1 147 ? 32.726  8.169   20.746  1.00 28.39 ? 147 GLU C OE1 1 
ATOM   5434 O  OE2 . GLU C 1 147 ? 33.578  8.801   18.829  1.00 28.07 ? 147 GLU C OE2 1 
ATOM   5435 N  N   . MET C 1 148 ? 37.040  11.408  22.426  1.00 16.65 ? 148 MET C N   1 
ATOM   5436 C  CA  . MET C 1 148 ? 38.317  11.880  21.954  1.00 17.49 ? 148 MET C CA  1 
ATOM   5437 C  C   . MET C 1 148 ? 38.488  11.366  20.512  1.00 17.40 ? 148 MET C C   1 
ATOM   5438 O  O   . MET C 1 148 ? 38.293  10.172  20.221  1.00 17.09 ? 148 MET C O   1 
ATOM   5439 C  CB  . MET C 1 148 ? 39.435  11.413  22.906  1.00 20.36 ? 148 MET C CB  1 
ATOM   5440 C  CG  . MET C 1 148 ? 40.707  12.245  22.799  1.00 22.57 ? 148 MET C CG  1 
ATOM   5441 S  SD  . MET C 1 148 ? 41.779  11.532  21.540  1.00 30.03 ? 148 MET C SD  1 
ATOM   5442 C  CE  . MET C 1 148 ? 42.333  10.141  22.524  1.00 22.49 ? 148 MET C CE  1 
ATOM   5443 N  N   . GLY C 1 149 ? 38.822  12.272  19.607  1.00 15.58 ? 149 GLY C N   1 
ATOM   5444 C  CA  . GLY C 1 149 ? 38.936  11.903  18.164  1.00 15.84 ? 149 GLY C CA  1 
ATOM   5445 C  C   . GLY C 1 149 ? 39.426  13.044  17.292  1.00 13.74 ? 149 GLY C C   1 
ATOM   5446 O  O   . GLY C 1 149 ? 40.498  13.608  17.533  1.00 14.77 ? 149 GLY C O   1 
ATOM   5447 N  N   . SER C 1 150 ? 38.633  13.405  16.280  1.00 14.21 ? 150 SER C N   1 
ATOM   5448 C  CA  . SER C 1 150 ? 38.988  14.537  15.408  1.00 15.08 ? 150 SER C CA  1 
ATOM   5449 C  C   . SER C 1 150 ? 39.010  15.895  16.118  1.00 14.13 ? 150 SER C C   1 
ATOM   5450 O  O   . SER C 1 150 ? 38.153  16.171  16.999  1.00 13.74 ? 150 SER C O   1 
ATOM   5451 C  CB  . SER C 1 150 ? 38.062  14.604  14.189  1.00 15.88 ? 150 SER C CB  1 
ATOM   5452 O  OG  . SER C 1 150 ? 38.177  13.385  13.482  1.00 15.57 ? 150 SER C OG  1 
ATOM   5453 N  N   . PHE C 1 151 ? 39.952  16.760  15.729  1.00 13.81 ? 151 PHE C N   1 
ATOM   5454 C  CA  . PHE C 1 151 ? 39.924  18.200  16.159  1.00 13.63 ? 151 PHE C CA  1 
ATOM   5455 C  C   . PHE C 1 151 ? 38.577  18.805  15.769  1.00 13.66 ? 151 PHE C C   1 
ATOM   5456 O  O   . PHE C 1 151 ? 38.046  18.541  14.649  1.00 12.78 ? 151 PHE C O   1 
ATOM   5457 C  CB  . PHE C 1 151 ? 41.006  19.003  15.405  1.00 14.86 ? 151 PHE C CB  1 
ATOM   5458 C  CG  . PHE C 1 151 ? 41.080  20.460  15.812  1.00 14.25 ? 151 PHE C CG  1 
ATOM   5459 C  CD1 . PHE C 1 151 ? 41.730  20.822  17.002  1.00 15.53 ? 151 PHE C CD1 1 
ATOM   5460 C  CD2 . PHE C 1 151 ? 40.509  21.441  15.019  1.00 14.60 ? 151 PHE C CD2 1 
ATOM   5461 C  CE1 . PHE C 1 151 ? 41.808  22.187  17.383  1.00 15.81 ? 151 PHE C CE1 1 
ATOM   5462 C  CE2 . PHE C 1 151 ? 40.595  22.799  15.374  1.00 15.68 ? 151 PHE C CE2 1 
ATOM   5463 C  CZ  . PHE C 1 151 ? 41.223  23.157  16.568  1.00 14.63 ? 151 PHE C CZ  1 
ATOM   5464 N  N   . ASN C 1 152 ? 38.035  19.669  16.635  1.00 13.97 ? 152 ASN C N   1 
ATOM   5465 C  CA  . ASN C 1 152 ? 36.695  20.187  16.438  1.00 14.72 ? 152 ASN C CA  1 
ATOM   5466 C  C   . ASN C 1 152 ? 36.849  21.722  16.427  1.00 15.01 ? 152 ASN C C   1 
ATOM   5467 O  O   . ASN C 1 152 ? 37.051  22.313  17.500  1.00 14.90 ? 152 ASN C O   1 
ATOM   5468 C  CB  . ASN C 1 152 ? 35.752  19.767  17.623  1.00 13.45 ? 152 ASN C CB  1 
ATOM   5469 C  CG  . ASN C 1 152 ? 34.278  19.986  17.293  1.00 13.89 ? 152 ASN C CG  1 
ATOM   5470 O  OD1 . ASN C 1 152 ? 33.891  21.103  16.911  1.00 13.81 ? 152 ASN C OD1 1 
ATOM   5471 N  ND2 . ASN C 1 152 ? 33.447  18.934  17.411  1.00 12.31 ? 152 ASN C ND2 1 
ATOM   5472 N  N   . PRO C 1 153 ? 36.811  22.352  15.232  1.00 15.03 ? 153 PRO C N   1 
ATOM   5473 C  CA  . PRO C 1 153 ? 36.956  23.814  15.213  1.00 16.25 ? 153 PRO C CA  1 
ATOM   5474 C  C   . PRO C 1 153 ? 35.956  24.593  16.056  1.00 14.03 ? 153 PRO C C   1 
ATOM   5475 O  O   . PRO C 1 153 ? 36.301  25.653  16.576  1.00 13.97 ? 153 PRO C O   1 
ATOM   5476 C  CB  . PRO C 1 153 ? 36.676  24.151  13.745  1.00 17.69 ? 153 PRO C CB  1 
ATOM   5477 C  CG  . PRO C 1 153 ? 37.253  22.958  13.007  1.00 19.52 ? 153 PRO C CG  1 
ATOM   5478 C  CD  . PRO C 1 153 ? 36.794  21.788  13.859  1.00 17.18 ? 153 PRO C CD  1 
ATOM   5479 N  N   . SER C 1 154 ? 34.701  24.142  16.070  1.00 13.91 ? 154 SER C N   1 
ATOM   5480 C  CA  . SER C 1 154 ? 33.589  24.793  16.766  1.00 13.42 ? 154 SER C CA  1 
ATOM   5481 C  C   . SER C 1 154 ? 33.787  24.811  18.296  1.00 13.58 ? 154 SER C C   1 
ATOM   5482 O  O   . SER C 1 154 ? 33.630  25.865  18.884  1.00 12.69 ? 154 SER C O   1 
ATOM   5483 C  CB  . SER C 1 154 ? 32.252  24.156  16.351  1.00 15.70 ? 154 SER C CB  1 
ATOM   5484 O  OG  . SER C 1 154 ? 32.153  24.383  14.924  1.00 20.44 ? 154 SER C OG  1 
ATOM   5485 N  N   . TYR C 1 155 ? 34.117  23.653  18.908  1.00 11.99 ? 155 TYR C N   1 
ATOM   5486 C  CA  . TYR C 1 155 ? 34.485  23.637  20.366  1.00 11.64 ? 155 TYR C CA  1 
ATOM   5487 C  C   . TYR C 1 155 ? 35.710  24.531  20.628  1.00 11.91 ? 155 TYR C C   1 
ATOM   5488 O  O   . TYR C 1 155 ? 35.823  25.171  21.680  1.00 11.47 ? 155 TYR C O   1 
ATOM   5489 C  CB  . TYR C 1 155 ? 34.652  22.204  20.855  1.00 11.44 ? 155 TYR C CB  1 
ATOM   5490 C  CG  . TYR C 1 155 ? 33.310  21.525  21.142  1.00 11.32 ? 155 TYR C CG  1 
ATOM   5491 C  CD1 . TYR C 1 155 ? 32.483  21.042  20.109  1.00 11.99 ? 155 TYR C CD1 1 
ATOM   5492 C  CD2 . TYR C 1 155 ? 32.844  21.385  22.447  1.00 10.91 ? 155 TYR C CD2 1 
ATOM   5493 C  CE1 . TYR C 1 155 ? 31.270  20.404  20.405  1.00 10.87 ? 155 TYR C CE1 1 
ATOM   5494 C  CE2 . TYR C 1 155 ? 31.621  20.765  22.731  1.00 11.43 ? 155 TYR C CE2 1 
ATOM   5495 C  CZ  . TYR C 1 155 ? 30.829  20.328  21.705  1.00 10.65 ? 155 TYR C CZ  1 
ATOM   5496 O  OH  . TYR C 1 155 ? 29.595  19.713  21.976  1.00 11.83 ? 155 TYR C OH  1 
ATOM   5497 N  N   . ASP C 1 156 ? 36.622  24.646  19.633  1.00 12.78 ? 156 ASP C N   1 
ATOM   5498 C  CA  . ASP C 1 156 ? 37.811  25.508  19.850  1.00 12.64 ? 156 ASP C CA  1 
ATOM   5499 C  C   . ASP C 1 156 ? 37.498  27.019  19.969  1.00 11.81 ? 156 ASP C C   1 
ATOM   5500 O  O   . ASP C 1 156 ? 38.290  27.815  20.480  1.00 11.11 ? 156 ASP C O   1 
ATOM   5501 C  CB  . ASP C 1 156 ? 38.939  25.192  18.829  1.00 14.77 ? 156 ASP C CB  1 
ATOM   5502 C  CG  . ASP C 1 156 ? 40.294  25.037  19.553  1.00 16.10 ? 156 ASP C CG  1 
ATOM   5503 O  OD1 . ASP C 1 156 ? 41.263  25.705  19.106  1.00 17.85 ? 156 ASP C OD1 1 
ATOM   5504 O  OD2 . ASP C 1 156 ? 40.338  24.327  20.612  1.00 14.58 ? 156 ASP C OD2 1 
ATOM   5505 N  N   . LYS C 1 157 ? 36.327  27.381  19.474  1.00 13.06 ? 157 LYS C N   1 
ATOM   5506 C  CA  . LYS C 1 157 ? 35.796  28.766  19.666  1.00 14.16 ? 157 LYS C CA  1 
ATOM   5507 C  C   . LYS C 1 157 ? 35.637  29.067  21.152  1.00 13.19 ? 157 LYS C C   1 
ATOM   5508 O  O   . LYS C 1 157 ? 35.850  30.210  21.540  1.00 14.73 ? 157 LYS C O   1 
ATOM   5509 C  CB  . LYS C 1 157 ? 34.512  29.035  18.841  1.00 14.89 ? 157 LYS C CB  1 
ATOM   5510 C  CG  . LYS C 1 157 ? 34.862  29.166  17.378  1.00 18.21 ? 157 LYS C CG  1 
ATOM   5511 C  CD  . LYS C 1 157 ? 33.608  29.042  16.484  1.00 20.11 ? 157 LYS C CD  1 
ATOM   5512 C  CE  . LYS C 1 157 ? 34.031  28.802  15.037  1.00 20.72 ? 157 LYS C CE  1 
ATOM   5513 N  NZ  . LYS C 1 157 ? 32.814  28.823  14.162  1.00 19.42 ? 157 LYS C NZ  1 
ATOM   5514 N  N   . ILE C 1 158 ? 35.319  28.058  21.976  1.00 12.10 ? 158 ILE C N   1 
ATOM   5515 C  CA  . ILE C 1 158 ? 35.406  28.157  23.469  1.00 12.30 ? 158 ILE C CA  1 
ATOM   5516 C  C   . ILE C 1 158 ? 36.818  27.882  24.020  1.00 12.34 ? 158 ILE C C   1 
ATOM   5517 O  O   . ILE C 1 158 ? 37.385  28.702  24.799  1.00 11.67 ? 158 ILE C O   1 
ATOM   5518 C  CB  . ILE C 1 158 ? 34.397  27.196  24.133  1.00 13.54 ? 158 ILE C CB  1 
ATOM   5519 C  CG1 . ILE C 1 158 ? 32.969  27.598  23.713  1.00 13.40 ? 158 ILE C CG1 1 
ATOM   5520 C  CG2 . ILE C 1 158 ? 34.522  27.222  25.678  1.00 12.71 ? 158 ILE C CG2 1 
ATOM   5521 C  CD1 . ILE C 1 158 ? 31.940  26.526  23.915  1.00 14.91 ? 158 ILE C CD1 1 
ATOM   5522 N  N   . PHE C 1 159 ? 37.397  26.753  23.600  1.00 11.54 ? 159 PHE C N   1 
ATOM   5523 C  CA  . PHE C 1 159 ? 38.618  26.252  24.258  1.00 12.81 ? 159 PHE C CA  1 
ATOM   5524 C  C   . PHE C 1 159 ? 39.835  27.209  24.099  1.00 12.79 ? 159 PHE C C   1 
ATOM   5525 O  O   . PHE C 1 159 ? 40.732  27.263  24.956  1.00 11.67 ? 159 PHE C O   1 
ATOM   5526 C  CB  . PHE C 1 159 ? 38.968  24.837  23.763  1.00 11.62 ? 159 PHE C CB  1 
ATOM   5527 C  CG  . PHE C 1 159 ? 37.914  23.760  24.092  1.00 12.42 ? 159 PHE C CG  1 
ATOM   5528 C  CD1 . PHE C 1 159 ? 36.989  23.912  25.144  1.00 12.85 ? 159 PHE C CD1 1 
ATOM   5529 C  CD2 . PHE C 1 159 ? 37.904  22.542  23.375  1.00 13.60 ? 159 PHE C CD2 1 
ATOM   5530 C  CE1 . PHE C 1 159 ? 36.059  22.882  25.464  1.00 14.14 ? 159 PHE C CE1 1 
ATOM   5531 C  CE2 . PHE C 1 159 ? 36.986  21.511  23.693  1.00 13.62 ? 159 PHE C CE2 1 
ATOM   5532 C  CZ  . PHE C 1 159 ? 36.068  21.689  24.749  1.00 14.02 ? 159 PHE C CZ  1 
ATOM   5533 N  N   . SER C 1 160 ? 39.844  27.970  23.019  1.00 13.44 ? 160 SER C N   1 
ATOM   5534 C  CA  . SER C 1 160 ? 40.992  28.875  22.729  1.00 14.39 ? 160 SER C CA  1 
ATOM   5535 C  C   . SER C 1 160 ? 41.106  30.005  23.763  1.00 14.53 ? 160 SER C C   1 
ATOM   5536 O  O   . SER C 1 160 ? 42.176  30.665  23.862  1.00 14.93 ? 160 SER C O   1 
ATOM   5537 C  CB  . SER C 1 160 ? 40.905  29.399  21.268  1.00 14.93 ? 160 SER C CB  1 
ATOM   5538 O  OG  . SER C 1 160 ? 39.753  30.187  21.073  1.00 16.54 ? 160 SER C OG  1 
ATOM   5539 N  N   . HIS C 1 161 ? 40.055  30.194  24.589  1.00 13.63 ? 161 HIS C N   1 
ATOM   5540 C  CA  . HIS C 1 161 ? 40.049  31.178  25.697  1.00 13.47 ? 161 HIS C CA  1 
ATOM   5541 C  C   . HIS C 1 161 ? 40.396  30.639  27.057  1.00 13.98 ? 161 HIS C C   1 
ATOM   5542 O  O   . HIS C 1 161 ? 40.426  31.385  28.048  1.00 13.22 ? 161 HIS C O   1 
ATOM   5543 C  CB  . HIS C 1 161 ? 38.681  31.897  25.746  1.00 12.88 ? 161 HIS C CB  1 
ATOM   5544 C  CG  . HIS C 1 161 ? 38.359  32.603  24.464  1.00 14.28 ? 161 HIS C CG  1 
ATOM   5545 N  ND1 . HIS C 1 161 ? 38.835  33.846  24.188  1.00 13.45 ? 161 HIS C ND1 1 
ATOM   5546 C  CD2 . HIS C 1 161 ? 37.646  32.194  23.345  1.00 14.18 ? 161 HIS C CD2 1 
ATOM   5547 C  CE1 . HIS C 1 161 ? 38.406  34.227  22.990  1.00 14.67 ? 161 HIS C CE1 1 
ATOM   5548 N  NE2 . HIS C 1 161 ? 37.669  33.204  22.451  1.00 14.46 ? 161 HIS C NE2 1 
ATOM   5549 N  N   . LEU C 1 162 ? 40.610  29.316  27.144  1.00 13.20 ? 162 LEU C N   1 
ATOM   5550 C  CA  . LEU C 1 162 ? 40.792  28.677  28.438  1.00 13.15 ? 162 LEU C CA  1 
ATOM   5551 C  C   . LEU C 1 162 ? 41.935  29.228  29.289  1.00 13.60 ? 162 LEU C C   1 
ATOM   5552 O  O   . LEU C 1 162 ? 41.751  29.418  30.491  1.00 13.27 ? 162 LEU C O   1 
ATOM   5553 C  CB  . LEU C 1 162 ? 40.937  27.171  28.313  1.00 14.36 ? 162 LEU C CB  1 
ATOM   5554 C  CG  . LEU C 1 162 ? 39.633  26.488  27.890  1.00 12.64 ? 162 LEU C CG  1 
ATOM   5555 C  CD1 . LEU C 1 162 ? 39.999  25.047  27.635  1.00 14.62 ? 162 LEU C CD1 1 
ATOM   5556 C  CD2 . LEU C 1 162 ? 38.625  26.594  29.014  1.00 15.49 ? 162 LEU C CD2 1 
ATOM   5557 N  N   . GLN C 1 163 ? 43.069  29.487  28.649  1.00 13.80 ? 163 GLN C N   1 
ATOM   5558 C  CA  . GLN C 1 163 ? 44.257  30.088  29.301  1.00 15.05 ? 163 GLN C CA  1 
ATOM   5559 C  C   . GLN C 1 163 ? 44.063  31.498  29.806  1.00 15.60 ? 163 GLN C C   1 
ATOM   5560 O  O   . GLN C 1 163 ? 44.993  32.050  30.446  1.00 14.40 ? 163 GLN C O   1 
ATOM   5561 C  CB  . GLN C 1 163 ? 45.477  30.075  28.366  1.00 16.44 ? 163 GLN C CB  1 
ATOM   5562 C  CG  . GLN C 1 163 ? 45.880  28.654  27.974  1.00 18.47 ? 163 GLN C CG  1 
ATOM   5563 C  CD  . GLN C 1 163 ? 46.206  27.711  29.144  1.00 18.84 ? 163 GLN C CD  1 
ATOM   5564 O  OE1 . GLN C 1 163 ? 46.760  28.099  30.189  1.00 20.81 ? 163 GLN C OE1 1 
ATOM   5565 N  NE2 . GLN C 1 163 ? 45.865  26.428  28.966  1.00 20.99 ? 163 GLN C NE2 1 
ATOM   5566 N  N   . HIS C 1 164 ? 42.888  32.081  29.562  1.00 14.20 ? 164 HIS C N   1 
ATOM   5567 C  CA  . HIS C 1 164 ? 42.570  33.429  30.102  1.00 14.87 ? 164 HIS C CA  1 
ATOM   5568 C  C   . HIS C 1 164 ? 41.473  33.477  31.163  1.00 15.16 ? 164 HIS C C   1 
ATOM   5569 O  O   . HIS C 1 164 ? 41.183  34.533  31.715  1.00 15.70 ? 164 HIS C O   1 
ATOM   5570 C  CB  . HIS C 1 164 ? 42.343  34.409  28.945  1.00 13.90 ? 164 HIS C CB  1 
ATOM   5571 C  CG  . HIS C 1 164 ? 43.519  34.448  28.045  1.00 13.61 ? 164 HIS C CG  1 
ATOM   5572 N  ND1 . HIS C 1 164 ? 43.495  33.902  26.826  1.00 14.77 ? 164 HIS C ND1 1 
ATOM   5573 C  CD2 . HIS C 1 164 ? 44.832  34.854  28.287  1.00 13.29 ? 164 HIS C CD2 1 
ATOM   5574 C  CE1 . HIS C 1 164 ? 44.747  33.973  26.279  1.00 14.62 ? 164 HIS C CE1 1 
ATOM   5575 N  NE2 . HIS C 1 164 ? 45.560  34.543  27.184  1.00 15.95 ? 164 HIS C NE2 1 
ATOM   5576 N  N   . VAL C 1 165 ? 40.918  32.309  31.480  1.00 14.52 ? 165 VAL C N   1 
ATOM   5577 C  CA  . VAL C 1 165 ? 40.017  32.160  32.622  1.00 14.43 ? 165 VAL C CA  1 
ATOM   5578 C  C   . VAL C 1 165 ? 40.514  31.015  33.562  1.00 14.67 ? 165 VAL C C   1 
ATOM   5579 O  O   . VAL C 1 165 ? 39.705  30.231  34.074  1.00 14.59 ? 165 VAL C O   1 
ATOM   5580 C  CB  . VAL C 1 165 ? 38.551  31.920  32.122  1.00 15.57 ? 165 VAL C CB  1 
ATOM   5581 C  CG1 . VAL C 1 165 ? 38.011  33.158  31.383  1.00 14.93 ? 165 VAL C CG1 1 
ATOM   5582 C  CG2 . VAL C 1 165 ? 38.460  30.674  31.239  1.00 14.02 ? 165 VAL C CG2 1 
ATOM   5583 N  N   . LYS C 1 166 ? 41.827  30.943  33.833  1.00 14.55 ? 166 LYS C N   1 
ATOM   5584 C  CA  . LYS C 1 166 ? 42.399  29.800  34.574  1.00 14.08 ? 166 LYS C CA  1 
ATOM   5585 C  C   . LYS C 1 166 ? 41.878  29.709  36.035  1.00 13.12 ? 166 LYS C C   1 
ATOM   5586 O  O   . LYS C 1 166 ? 41.840  28.635  36.609  1.00 11.99 ? 166 LYS C O   1 
ATOM   5587 C  CB  . LYS C 1 166 ? 43.940  29.866  34.580  1.00 14.14 ? 166 LYS C CB  1 
ATOM   5588 C  CG  . LYS C 1 166 ? 44.541  29.788  33.173  1.00 16.37 ? 166 LYS C CG  1 
ATOM   5589 C  CD  . LYS C 1 166 ? 46.073  29.838  33.183  1.00 17.17 ? 166 LYS C CD  1 
ATOM   5590 C  CE  . LYS C 1 166 ? 46.629  28.547  33.796  1.00 16.44 ? 166 LYS C CE  1 
ATOM   5591 N  NZ  . LYS C 1 166 ? 46.401  27.330  32.933  1.00 17.37 ? 166 LYS C NZ  1 
ATOM   5592 N  N   . TYR C 1 167 ? 41.465  30.831  36.628  1.00 13.05 ? 167 TYR C N   1 
ATOM   5593 C  CA  . TYR C 1 167 ? 41.227  30.853  38.056  1.00 13.66 ? 167 TYR C CA  1 
ATOM   5594 C  C   . TYR C 1 167 ? 39.812  31.307  38.328  1.00 13.12 ? 167 TYR C C   1 
ATOM   5595 O  O   . TYR C 1 167 ? 39.213  32.027  37.518  1.00 13.08 ? 167 TYR C O   1 
ATOM   5596 C  CB  . TYR C 1 167 ? 42.238  31.807  38.763  1.00 17.23 ? 167 TYR C CB  1 
ATOM   5597 C  CG  . TYR C 1 167 ? 43.656  31.299  38.712  1.00 21.11 ? 167 TYR C CG  1 
ATOM   5598 C  CD1 . TYR C 1 167 ? 44.572  31.752  37.736  1.00 21.60 ? 167 TYR C CD1 1 
ATOM   5599 C  CD2 . TYR C 1 167 ? 44.089  30.353  39.646  1.00 21.36 ? 167 TYR C CD2 1 
ATOM   5600 C  CE1 . TYR C 1 167 ? 45.864  31.250  37.682  1.00 24.06 ? 167 TYR C CE1 1 
ATOM   5601 C  CE2 . TYR C 1 167 ? 45.375  29.854  39.608  1.00 23.19 ? 167 TYR C CE2 1 
ATOM   5602 C  CZ  . TYR C 1 167 ? 46.249  30.296  38.629  1.00 26.94 ? 167 TYR C CZ  1 
ATOM   5603 O  OH  . TYR C 1 167 ? 47.512  29.788  38.636  1.00 29.68 ? 167 TYR C OH  1 
ATOM   5604 N  N   . LYS C 1 168 ? 39.298  30.912  39.486  1.00 12.36 ? 168 LYS C N   1 
ATOM   5605 C  CA  . LYS C 1 168 ? 37.896  31.211  39.886  1.00 14.17 ? 168 LYS C CA  1 
ATOM   5606 C  C   . LYS C 1 168 ? 37.598  32.694  39.822  1.00 15.47 ? 168 LYS C C   1 
ATOM   5607 O  O   . LYS C 1 168 ? 38.399  33.497  40.323  1.00 15.69 ? 168 LYS C O   1 
ATOM   5608 C  CB  . LYS C 1 168 ? 37.613  30.717  41.305  1.00 16.19 ? 168 LYS C CB  1 
ATOM   5609 C  CG  . LYS C 1 168 ? 36.151  30.913  41.676  1.00 16.60 ? 168 LYS C CG  1 
ATOM   5610 C  CD  . LYS C 1 168 ? 35.810  30.231  43.003  1.00 19.98 ? 168 LYS C CD  1 
ATOM   5611 C  CE  . LYS C 1 168 ? 34.384  30.549  43.414  1.00 22.72 ? 168 LYS C CE  1 
ATOM   5612 N  NZ  . LYS C 1 168 ? 34.195  30.250  44.886  1.00 24.12 ? 168 LYS C NZ  1 
ATOM   5613 N  N   . GLY C 1 169 ? 36.470  33.050  39.187  1.00 14.06 ? 169 GLY C N   1 
ATOM   5614 C  CA  . GLY C 1 169 ? 36.063  34.464  39.078  1.00 16.01 ? 169 GLY C CA  1 
ATOM   5615 C  C   . GLY C 1 169 ? 36.546  35.140  37.811  1.00 16.46 ? 169 GLY C C   1 
ATOM   5616 O  O   . GLY C 1 169 ? 36.020  36.190  37.432  1.00 17.84 ? 169 GLY C O   1 
ATOM   5617 N  N   . GLN C 1 170 ? 37.528  34.550  37.123  1.00 14.44 ? 170 GLN C N   1 
ATOM   5618 C  CA  . GLN C 1 170 ? 38.065  35.148  35.896  1.00 14.18 ? 170 GLN C CA  1 
ATOM   5619 C  C   . GLN C 1 170 ? 37.084  35.048  34.721  1.00 15.39 ? 170 GLN C C   1 
ATOM   5620 O  O   . GLN C 1 170 ? 36.306  34.081  34.638  1.00 13.25 ? 170 GLN C O   1 
ATOM   5621 C  CB  . GLN C 1 170 ? 39.457  34.585  35.550  1.00 13.93 ? 170 GLN C CB  1 
ATOM   5622 C  CG  . GLN C 1 170 ? 40.507  35.023  36.598  1.00 14.68 ? 170 GLN C CG  1 
ATOM   5623 C  CD  . GLN C 1 170 ? 41.936  34.609  36.292  1.00 17.14 ? 170 GLN C CD  1 
ATOM   5624 O  OE1 . GLN C 1 170 ? 42.188  33.560  35.727  1.00 17.17 ? 170 GLN C OE1 1 
ATOM   5625 N  NE2 . GLN C 1 170 ? 42.899  35.432  36.730  1.00 17.21 ? 170 GLN C NE2 1 
ATOM   5626 N  N   . GLU C 1 171 ? 37.128  36.057  33.849  1.00 13.48 ? 171 GLU C N   1 
ATOM   5627 C  CA  . GLU C 1 171 ? 36.160  36.215  32.726  1.00 13.98 ? 171 GLU C CA  1 
ATOM   5628 C  C   . GLU C 1 171 ? 36.857  36.575  31.426  1.00 14.51 ? 171 GLU C C   1 
ATOM   5629 O  O   . GLU C 1 171 ? 37.914  37.250  31.434  1.00 14.66 ? 171 GLU C O   1 
ATOM   5630 C  CB  . GLU C 1 171 ? 35.170  37.383  33.021  1.00 13.90 ? 171 GLU C CB  1 
ATOM   5631 C  CG  . GLU C 1 171 ? 34.153  37.143  34.123  1.00 18.03 ? 171 GLU C CG  1 
ATOM   5632 C  CD  . GLU C 1 171 ? 33.376  38.378  34.602  1.00 19.49 ? 171 GLU C CD  1 
ATOM   5633 O  OE1 . GLU C 1 171 ? 32.419  38.172  35.376  1.00 23.58 ? 171 GLU C OE1 1 
ATOM   5634 O  OE2 . GLU C 1 171 ? 33.691  39.528  34.222  1.00 20.06 ? 171 GLU C OE2 1 
ATOM   5635 N  N   . ALA C 1 172 ? 36.241  36.195  30.307  1.00 14.75 ? 172 ALA C N   1 
ATOM   5636 C  CA  . ALA C 1 172 ? 36.744  36.515  28.980  1.00 16.10 ? 172 ALA C CA  1 
ATOM   5637 C  C   . ALA C 1 172 ? 35.566  36.687  28.059  1.00 16.11 ? 172 ALA C C   1 
ATOM   5638 O  O   . ALA C 1 172 ? 34.531  36.113  28.301  1.00 16.57 ? 172 ALA C O   1 
ATOM   5639 C  CB  . ALA C 1 172 ? 37.657  35.386  28.441  1.00 16.87 ? 172 ALA C CB  1 
ATOM   5640 N  N   . PHE C 1 173 ? 35.731  37.469  26.992  1.00 15.41 ? 173 PHE C N   1 
ATOM   5641 C  CA  . PHE C 1 173 ? 34.717  37.583  25.955  1.00 15.15 ? 173 PHE C CA  1 
ATOM   5642 C  C   . PHE C 1 173 ? 34.964  36.642  24.802  1.00 16.84 ? 173 PHE C C   1 
ATOM   5643 O  O   . PHE C 1 173 ? 36.103  36.518  24.315  1.00 14.10 ? 173 PHE C O   1 
ATOM   5644 C  CB  . PHE C 1 173 ? 34.610  39.026  25.428  1.00 17.69 ? 173 PHE C CB  1 
ATOM   5645 C  CG  . PHE C 1 173 ? 33.966  39.958  26.408  1.00 16.76 ? 173 PHE C CG  1 
ATOM   5646 C  CD1 . PHE C 1 173 ? 34.705  40.972  27.024  1.00 20.73 ? 173 PHE C CD1 1 
ATOM   5647 C  CD2 . PHE C 1 173 ? 32.635  39.793  26.734  1.00 19.33 ? 173 PHE C CD2 1 
ATOM   5648 C  CE1 . PHE C 1 173 ? 34.092  41.815  27.960  1.00 21.61 ? 173 PHE C CE1 1 
ATOM   5649 C  CE2 . PHE C 1 173 ? 32.001  40.628  27.657  1.00 20.66 ? 173 PHE C CE2 1 
ATOM   5650 C  CZ  . PHE C 1 173 ? 32.742  41.626  28.276  1.00 20.87 ? 173 PHE C CZ  1 
ATOM   5651 N  N   . VAL C 1 174 ? 33.881  35.988  24.354  1.00 14.79 ? 174 VAL C N   1 
ATOM   5652 C  CA  . VAL C 1 174 ? 33.917  35.133  23.197  1.00 13.73 ? 174 VAL C CA  1 
ATOM   5653 C  C   . VAL C 1 174 ? 32.954  35.682  22.144  1.00 13.29 ? 174 VAL C C   1 
ATOM   5654 O  O   . VAL C 1 174 ? 31.781  35.887  22.444  1.00 12.01 ? 174 VAL C O   1 
ATOM   5655 C  CB  . VAL C 1 174 ? 33.391  33.709  23.561  1.00 14.31 ? 174 VAL C CB  1 
ATOM   5656 C  CG1 . VAL C 1 174 ? 33.236  32.860  22.293  1.00 13.27 ? 174 VAL C CG1 1 
ATOM   5657 C  CG2 . VAL C 1 174 ? 34.286  33.052  24.604  1.00 13.89 ? 174 VAL C CG2 1 
ATOM   5658 N  N   . PRO C 1 175 ? 33.445  35.928  20.890  1.00 13.06 ? 175 PRO C N   1 
ATOM   5659 C  CA  . PRO C 1 175 ? 32.489  36.437  19.876  1.00 14.04 ? 175 PRO C CA  1 
ATOM   5660 C  C   . PRO C 1 175 ? 31.444  35.415  19.529  1.00 13.50 ? 175 PRO C C   1 
ATOM   5661 O  O   . PRO C 1 175 ? 31.708  34.209  19.639  1.00 13.16 ? 175 PRO C O   1 
ATOM   5662 C  CB  . PRO C 1 175 ? 33.338  36.707  18.640  1.00 14.83 ? 175 PRO C CB  1 
ATOM   5663 C  CG  . PRO C 1 175 ? 34.731  36.599  19.052  1.00 16.13 ? 175 PRO C CG  1 
ATOM   5664 C  CD  . PRO C 1 175 ? 34.833  35.954  20.433  1.00 14.94 ? 175 PRO C CD  1 
ATOM   5665 N  N   . GLY C 1 176 ? 30.264  35.897  19.124  1.00 13.59 ? 176 GLY C N   1 
ATOM   5666 C  CA  . GLY C 1 176 ? 29.181  35.003  18.695  1.00 13.56 ? 176 GLY C CA  1 
ATOM   5667 C  C   . GLY C 1 176 ? 29.601  34.011  17.613  1.00 13.43 ? 176 GLY C C   1 
ATOM   5668 O  O   . GLY C 1 176 ? 30.359  34.365  16.696  1.00 12.65 ? 176 GLY C O   1 
ATOM   5669 N  N   . PHE C 1 177 ? 29.134  32.765  17.755  1.00 14.55 ? 177 PHE C N   1 
ATOM   5670 C  CA  . PHE C 1 177 ? 29.231  31.787  16.711  1.00 14.45 ? 177 PHE C CA  1 
ATOM   5671 C  C   . PHE C 1 177 ? 27.980  30.943  16.733  1.00 14.48 ? 177 PHE C C   1 
ATOM   5672 O  O   . PHE C 1 177 ? 27.197  31.009  17.685  1.00 16.20 ? 177 PHE C O   1 
ATOM   5673 C  CB  . PHE C 1 177 ? 30.483  30.898  16.882  1.00 14.83 ? 177 PHE C CB  1 
ATOM   5674 C  CG  . PHE C 1 177 ? 30.499  29.996  18.136  1.00 15.23 ? 177 PHE C CG  1 
ATOM   5675 C  CD1 . PHE C 1 177 ? 30.111  28.651  18.069  1.00 15.89 ? 177 PHE C CD1 1 
ATOM   5676 C  CD2 . PHE C 1 177 ? 30.980  30.474  19.346  1.00 15.27 ? 177 PHE C CD2 1 
ATOM   5677 C  CE1 . PHE C 1 177 ? 30.186  27.822  19.178  1.00 13.09 ? 177 PHE C CE1 1 
ATOM   5678 C  CE2 . PHE C 1 177 ? 31.039  29.653  20.468  1.00 14.94 ? 177 PHE C CE2 1 
ATOM   5679 C  CZ  . PHE C 1 177 ? 30.657  28.303  20.370  1.00 13.79 ? 177 PHE C CZ  1 
ATOM   5680 N  N   . ASN C 1 178 ? 27.814  30.107  15.739  1.00 12.60 ? 178 ASN C N   1 
ATOM   5681 C  CA  . ASN C 1 178 ? 26.640  29.248  15.704  1.00 13.61 ? 178 ASN C CA  1 
ATOM   5682 C  C   . ASN C 1 178 ? 26.737  28.056  16.663  1.00 12.83 ? 178 ASN C C   1 
ATOM   5683 O  O   . ASN C 1 178 ? 27.456  27.101  16.413  1.00 12.66 ? 178 ASN C O   1 
ATOM   5684 C  CB  . ASN C 1 178 ? 26.380  28.808  14.252  1.00 14.24 ? 178 ASN C CB  1 
ATOM   5685 C  CG  . ASN C 1 178 ? 25.178  27.939  14.118  1.00 15.42 ? 178 ASN C CG  1 
ATOM   5686 O  OD1 . ASN C 1 178 ? 24.343  27.753  15.075  1.00 14.22 ? 178 ASN C OD1 1 
ATOM   5687 N  ND2 . ASN C 1 178 ? 25.041  27.365  12.899  1.00 17.77 ? 178 ASN C ND2 1 
ATOM   5688 N  N   . ILE C 1 179 ? 26.024  28.146  17.794  1.00 13.16 ? 179 ILE C N   1 
ATOM   5689 C  CA  . ILE C 1 179 ? 25.965  27.087  18.845  1.00 12.78 ? 179 ILE C CA  1 
ATOM   5690 C  C   . ILE C 1 179 ? 25.513  25.713  18.328  1.00 12.86 ? 179 ILE C C   1 
ATOM   5691 O  O   . ILE C 1 179 ? 25.883  24.653  18.890  1.00 13.54 ? 179 ILE C O   1 
ATOM   5692 C  CB  . ILE C 1 179 ? 25.067  27.541  20.055  1.00 12.02 ? 179 ILE C CB  1 
ATOM   5693 C  CG1 . ILE C 1 179 ? 25.547  28.907  20.637  1.00 11.30 ? 179 ILE C CG1 1 
ATOM   5694 C  CG2 . ILE C 1 179 ? 24.959  26.468  21.160  1.00 10.88 ? 179 ILE C CG2 1 
ATOM   5695 C  CD1 . ILE C 1 179 ? 26.991  28.916  21.143  1.00 12.19 ? 179 ILE C CD1 1 
ATOM   5696 N  N   . GLU C 1 180 ? 24.697  25.713  17.281  1.00 12.89 ? 180 GLU C N   1 
ATOM   5697 C  CA  . GLU C 1 180 ? 24.316  24.484  16.666  1.00 14.88 ? 180 GLU C CA  1 
ATOM   5698 C  C   . GLU C 1 180 ? 25.504  23.628  16.121  1.00 13.57 ? 180 GLU C C   1 
ATOM   5699 O  O   . GLU C 1 180 ? 25.353  22.425  15.960  1.00 14.03 ? 180 GLU C O   1 
ATOM   5700 C  CB  . GLU C 1 180 ? 23.234  24.716  15.554  1.00 17.37 ? 180 GLU C CB  1 
ATOM   5701 C  CG  . GLU C 1 180 ? 22.195  23.593  15.529  1.00 22.77 ? 180 GLU C CG  1 
ATOM   5702 C  CD  . GLU C 1 180 ? 21.186  23.711  14.397  1.00 25.55 ? 180 GLU C CD  1 
ATOM   5703 O  OE1 . GLU C 1 180 ? 20.809  24.848  14.022  1.00 26.49 ? 180 GLU C OE1 1 
ATOM   5704 O  OE2 . GLU C 1 180 ? 20.765  22.649  13.908  1.00 28.86 ? 180 GLU C OE2 1 
ATOM   5705 N  N   . GLU C 1 181 ? 26.624  24.268  15.805  1.00 14.38 ? 181 GLU C N   1 
ATOM   5706 C  CA  . GLU C 1 181 ? 27.865  23.566  15.431  1.00 15.70 ? 181 GLU C CA  1 
ATOM   5707 C  C   . GLU C 1 181 ? 28.430  22.707  16.630  1.00 14.26 ? 181 GLU C C   1 
ATOM   5708 O  O   . GLU C 1 181 ? 29.325  21.879  16.410  1.00 13.09 ? 181 GLU C O   1 
ATOM   5709 C  CB  . GLU C 1 181 ? 28.942  24.546  14.967  1.00 18.01 ? 181 GLU C CB  1 
ATOM   5710 C  CG  . GLU C 1 181 ? 28.695  25.317  13.664  1.00 19.65 ? 181 GLU C CG  1 
ATOM   5711 C  CD  . GLU C 1 181 ? 29.659  26.514  13.516  1.00 24.11 ? 181 GLU C CD  1 
ATOM   5712 O  OE1 . GLU C 1 181 ? 30.652  26.603  14.303  1.00 23.93 ? 181 GLU C OE1 1 
ATOM   5713 O  OE2 . GLU C 1 181 ? 29.418  27.376  12.612  1.00 23.14 ? 181 GLU C OE2 1 
ATOM   5714 N  N   . LEU C 1 182 ? 27.923  22.914  17.860  1.00 13.23 ? 182 LEU C N   1 
ATOM   5715 C  CA  . LEU C 1 182 ? 28.385  22.082  19.009  1.00 12.11 ? 182 LEU C CA  1 
ATOM   5716 C  C   . LEU C 1 182 ? 27.563  20.793  19.152  1.00 12.40 ? 182 LEU C C   1 
ATOM   5717 O  O   . LEU C 1 182 ? 27.818  19.974  20.032  1.00 12.43 ? 182 LEU C O   1 
ATOM   5718 C  CB  . LEU C 1 182 ? 28.362  22.856  20.356  1.00 13.72 ? 182 LEU C CB  1 
ATOM   5719 C  CG  . LEU C 1 182 ? 29.076  24.209  20.382  1.00 13.44 ? 182 LEU C CG  1 
ATOM   5720 C  CD1 . LEU C 1 182 ? 28.946  24.769  21.807  1.00 14.25 ? 182 LEU C CD1 1 
ATOM   5721 C  CD2 . LEU C 1 182 ? 30.549  24.072  20.030  1.00 14.06 ? 182 LEU C CD2 1 
ATOM   5722 N  N   . LEU C 1 183 ? 26.543  20.657  18.306  1.00 11.89 ? 183 LEU C N   1 
ATOM   5723 C  CA  . LEU C 1 183 ? 25.595  19.550  18.391  1.00 12.16 ? 183 LEU C CA  1 
ATOM   5724 C  C   . LEU C 1 183 ? 26.096  18.449  17.474  1.00 13.36 ? 183 LEU C C   1 
ATOM   5725 O  O   . LEU C 1 183 ? 26.796  18.728  16.464  1.00 11.93 ? 183 LEU C O   1 
ATOM   5726 C  CB  . LEU C 1 183 ? 24.154  20.020  17.993  1.00 13.23 ? 183 LEU C CB  1 
ATOM   5727 C  CG  . LEU C 1 183 ? 23.530  21.088  18.934  1.00 14.38 ? 183 LEU C CG  1 
ATOM   5728 C  CD1 . LEU C 1 183 ? 22.047  21.345  18.628  1.00 16.74 ? 183 LEU C CD1 1 
ATOM   5729 C  CD2 . LEU C 1 183 ? 23.739  20.842  20.464  1.00 14.64 ? 183 LEU C CD2 1 
ATOM   5730 N  N   . PRO C 1 184 ? 25.681  17.198  17.752  1.00 12.73 ? 184 PRO C N   1 
ATOM   5731 C  CA  . PRO C 1 184 ? 26.210  16.088  16.958  1.00 14.07 ? 184 PRO C CA  1 
ATOM   5732 C  C   . PRO C 1 184 ? 25.330  15.844  15.718  1.00 16.19 ? 184 PRO C C   1 
ATOM   5733 O  O   . PRO C 1 184 ? 24.338  16.537  15.516  1.00 16.72 ? 184 PRO C O   1 
ATOM   5734 C  CB  . PRO C 1 184 ? 26.001  14.893  17.909  1.00 13.59 ? 184 PRO C CB  1 
ATOM   5735 C  CG  . PRO C 1 184 ? 24.746  15.254  18.673  1.00 12.95 ? 184 PRO C CG  1 
ATOM   5736 C  CD  . PRO C 1 184 ? 24.927  16.746  18.936  1.00 13.12 ? 184 PRO C CD  1 
ATOM   5737 N  N   A GLU C 1 185 ? 25.724  14.853  14.911  0.50 17.73 ? 185 GLU C N   1 
ATOM   5738 N  N   B GLU C 1 185 ? 25.707  14.859  14.906  0.50 17.34 ? 185 GLU C N   1 
ATOM   5739 C  CA  A GLU C 1 185 ? 24.919  14.357  13.791  0.50 18.99 ? 185 GLU C CA  1 
ATOM   5740 C  CA  B GLU C 1 185 ? 24.884  14.443  13.777  0.50 18.26 ? 185 GLU C CA  1 
ATOM   5741 C  C   A GLU C 1 185 ? 23.587  13.783  14.268  0.50 18.10 ? 185 GLU C C   1 
ATOM   5742 C  C   B GLU C 1 185 ? 23.590  13.803  14.260  0.50 17.73 ? 185 GLU C C   1 
ATOM   5743 O  O   A GLU C 1 185 ? 23.491  13.328  15.418  0.50 16.95 ? 185 GLU C O   1 
ATOM   5744 O  O   B GLU C 1 185 ? 23.523  13.321  15.401  0.50 16.64 ? 185 GLU C O   1 
ATOM   5745 C  CB  A GLU C 1 185 ? 25.701  13.282  13.001  0.50 21.18 ? 185 GLU C CB  1 
ATOM   5746 C  CB  B GLU C 1 185 ? 25.662  13.462  12.886  0.50 19.83 ? 185 GLU C CB  1 
ATOM   5747 C  CG  A GLU C 1 185 ? 26.372  13.823  11.750  0.50 22.55 ? 185 GLU C CG  1 
ATOM   5748 C  CG  B GLU C 1 185 ? 26.910  14.082  12.308  0.50 20.18 ? 185 GLU C CG  1 
ATOM   5749 C  CD  A GLU C 1 185 ? 27.149  12.779  10.972  0.50 23.91 ? 185 GLU C CD  1 
ATOM   5750 C  CD  B GLU C 1 185 ? 26.625  15.382  11.576  0.50 21.34 ? 185 GLU C CD  1 
ATOM   5751 O  OE1 A GLU C 1 185 ? 26.701  12.376  9.877   0.50 25.11 ? 185 GLU C OE1 1 
ATOM   5752 O  OE1 B GLU C 1 185 ? 25.629  15.458  10.811  0.50 22.31 ? 185 GLU C OE1 1 
ATOM   5753 O  OE2 A GLU C 1 185 ? 28.228  12.387  11.443  0.50 26.23 ? 185 GLU C OE2 1 
ATOM   5754 O  OE2 B GLU C 1 185 ? 27.402  16.339  11.741  0.50 21.18 ? 185 GLU C OE2 1 
ATOM   5755 N  N   . ARG C 1 186 ? 22.568  13.864  13.393  1.00 18.38 ? 186 ARG C N   1 
ATOM   5756 C  CA  . ARG C 1 186 ? 21.242  13.310  13.637  1.00 19.46 ? 186 ARG C CA  1 
ATOM   5757 C  C   . ARG C 1 186 ? 20.618  13.725  15.013  1.00 18.81 ? 186 ARG C C   1 
ATOM   5758 O  O   . ARG C 1 186 ? 20.243  12.865  15.866  1.00 17.01 ? 186 ARG C O   1 
ATOM   5759 C  CB  . ARG C 1 186 ? 21.287  11.791  13.399  1.00 22.61 ? 186 ARG C CB  1 
ATOM   5760 C  CG  . ARG C 1 186 ? 21.669  11.427  11.948  1.00 28.96 ? 186 ARG C CG  1 
ATOM   5761 C  CD  . ARG C 1 186 ? 22.224  10.010  11.738  1.00 34.23 ? 186 ARG C CD  1 
ATOM   5762 N  NE  . ARG C 1 186 ? 21.794  9.085   12.780  1.00 38.82 ? 186 ARG C NE  1 
ATOM   5763 C  CZ  . ARG C 1 186 ? 22.615  8.430   13.597  1.00 37.95 ? 186 ARG C CZ  1 
ATOM   5764 N  NH1 . ARG C 1 186 ? 22.111  7.638   14.538  1.00 32.03 ? 186 ARG C NH1 1 
ATOM   5765 N  NH2 . ARG C 1 186 ? 23.942  8.568   13.476  1.00 41.71 ? 186 ARG C NH2 1 
ATOM   5766 N  N   . THR C 1 187 ? 20.523  15.037  15.234  1.00 17.06 ? 187 THR C N   1 
ATOM   5767 C  CA  . THR C 1 187 ? 19.892  15.534  16.483  1.00 16.11 ? 187 THR C CA  1 
ATOM   5768 C  C   . THR C 1 187 ? 18.447  15.088  16.703  1.00 15.29 ? 187 THR C C   1 
ATOM   5769 O  O   . THR C 1 187 ? 17.949  15.183  17.827  1.00 14.82 ? 187 THR C O   1 
ATOM   5770 C  CB  . THR C 1 187 ? 19.949  17.082  16.602  1.00 15.97 ? 187 THR C CB  1 
ATOM   5771 O  OG1 . THR C 1 187 ? 19.475  17.624  15.384  1.00 15.32 ? 187 THR C OG1 1 
ATOM   5772 C  CG2 . THR C 1 187 ? 21.405  17.606  16.886  1.00 17.92 ? 187 THR C CG2 1 
ATOM   5773 N  N   . ALA C 1 188 ? 17.746  14.642  15.646  1.00 13.58 ? 188 ALA C N   1 
ATOM   5774 C  CA  . ALA C 1 188 ? 16.397  14.086  15.842  1.00 12.59 ? 188 ALA C CA  1 
ATOM   5775 C  C   . ALA C 1 188 ? 16.388  12.786  16.740  1.00 12.96 ? 188 ALA C C   1 
ATOM   5776 O  O   . ALA C 1 188 ? 15.321  12.358  17.218  1.00 11.30 ? 188 ALA C O   1 
ATOM   5777 C  CB  . ALA C 1 188 ? 15.714  13.825  14.456  1.00 13.14 ? 188 ALA C CB  1 
ATOM   5778 N  N   . GLU C 1 189 ? 17.569  12.159  16.928  1.00 12.54 ? 189 GLU C N   1 
ATOM   5779 C  CA  . GLU C 1 189 ? 17.752  10.913  17.651  1.00 12.23 ? 189 GLU C CA  1 
ATOM   5780 C  C   . GLU C 1 189 ? 18.274  11.191  19.042  1.00 11.73 ? 189 GLU C C   1 
ATOM   5781 O  O   . GLU C 1 189 ? 19.403  11.753  19.171  1.00 11.06 ? 189 GLU C O   1 
ATOM   5782 C  CB  . GLU C 1 189 ? 18.711  9.976   16.931  1.00 14.40 ? 189 GLU C CB  1 
ATOM   5783 C  CG  . GLU C 1 189 ? 18.175  9.540   15.549  1.00 16.85 ? 189 GLU C CG  1 
ATOM   5784 C  CD  . GLU C 1 189 ? 18.993  8.442   14.929  1.00 19.02 ? 189 GLU C CD  1 
ATOM   5785 O  OE1 . GLU C 1 189 ? 19.971  8.016   15.513  1.00 20.50 ? 189 GLU C OE1 1 
ATOM   5786 O  OE2 . GLU C 1 189 ? 18.648  7.977   13.835  1.00 24.32 ? 189 GLU C OE2 1 
ATOM   5787 N  N   . TYR C 1 190 ? 17.404  10.998  20.043  1.00 10.31 ? 190 TYR C N   1 
ATOM   5788 C  CA  . TYR C 1 190 ? 17.770  11.414  21.445  1.00 10.33 ? 190 TYR C CA  1 
ATOM   5789 C  C   . TYR C 1 190 ? 17.084  10.581  22.514  1.00 9.96  ? 190 TYR C C   1 
ATOM   5790 O  O   . TYR C 1 190 ? 16.045  9.911   22.273  1.00 9.94  ? 190 TYR C O   1 
ATOM   5791 C  CB  . TYR C 1 190 ? 17.495  12.913  21.734  1.00 10.51 ? 190 TYR C CB  1 
ATOM   5792 C  CG  . TYR C 1 190 ? 16.049  13.415  21.497  1.00 11.29 ? 190 TYR C CG  1 
ATOM   5793 C  CD1 . TYR C 1 190 ? 15.091  13.332  22.492  1.00 10.84 ? 190 TYR C CD1 1 
ATOM   5794 C  CD2 . TYR C 1 190 ? 15.659  13.950  20.239  1.00 12.60 ? 190 TYR C CD2 1 
ATOM   5795 C  CE1 . TYR C 1 190 ? 13.765  13.774  22.259  1.00 11.84 ? 190 TYR C CE1 1 
ATOM   5796 C  CE2 . TYR C 1 190 ? 14.325  14.378  19.982  1.00 11.75 ? 190 TYR C CE2 1 
ATOM   5797 C  CZ  . TYR C 1 190 ? 13.384  14.270  20.998  1.00 11.96 ? 190 TYR C CZ  1 
ATOM   5798 O  OH  . TYR C 1 190 ? 12.085  14.775  20.844  1.00 11.89 ? 190 TYR C OH  1 
ATOM   5799 N  N   . TYR C 1 191 ? 17.654  10.677  23.722  1.00 9.17  ? 191 TYR C N   1 
ATOM   5800 C  CA  . TYR C 1 191 ? 17.070  10.173  24.924  1.00 9.38  ? 191 TYR C CA  1 
ATOM   5801 C  C   . TYR C 1 191 ? 16.364  11.333  25.643  1.00 9.35  ? 191 TYR C C   1 
ATOM   5802 O  O   . TYR C 1 191 ? 16.864  12.472  25.683  1.00 11.17 ? 191 TYR C O   1 
ATOM   5803 C  CB  . TYR C 1 191 ? 18.129  9.585   25.887  1.00 9.19  ? 191 TYR C CB  1 
ATOM   5804 C  CG  . TYR C 1 191 ? 19.075  8.563   25.328  1.00 9.66  ? 191 TYR C CG  1 
ATOM   5805 C  CD1 . TYR C 1 191 ? 20.332  8.976   24.772  1.00 9.42  ? 191 TYR C CD1 1 
ATOM   5806 C  CD2 . TYR C 1 191 ? 18.800  7.202   25.470  1.00 9.01  ? 191 TYR C CD2 1 
ATOM   5807 C  CE1 . TYR C 1 191 ? 21.228  8.020   24.260  1.00 10.38 ? 191 TYR C CE1 1 
ATOM   5808 C  CE2 . TYR C 1 191 ? 19.727  6.237   25.013  1.00 9.39  ? 191 TYR C CE2 1 
ATOM   5809 C  CZ  . TYR C 1 191 ? 20.912  6.662   24.393  1.00 9.81  ? 191 TYR C CZ  1 
ATOM   5810 O  OH  . TYR C 1 191 ? 21.852  5.763   23.936  1.00 10.37 ? 191 TYR C OH  1 
ATOM   5811 N  N   . ARG C 1 192 ? 15.201  11.034  26.188  1.00 9.11  ? 192 ARG C N   1 
ATOM   5812 C  CA  . ARG C 1 192 ? 14.392  12.014  26.957  1.00 9.51  ? 192 ARG C CA  1 
ATOM   5813 C  C   . ARG C 1 192 ? 13.906  11.525  28.358  1.00 10.20 ? 192 ARG C C   1 
ATOM   5814 O  O   . ARG C 1 192 ? 13.218  10.499  28.473  1.00 11.04 ? 192 ARG C O   1 
ATOM   5815 C  CB  . ARG C 1 192 ? 13.199  12.451  26.086  1.00 9.62  ? 192 ARG C CB  1 
ATOM   5816 C  CG  . ARG C 1 192 ? 12.094  13.192  26.862  1.00 11.10 ? 192 ARG C CG  1 
ATOM   5817 C  CD  . ARG C 1 192 ? 12.399  14.640  27.172  1.00 13.20 ? 192 ARG C CD  1 
ATOM   5818 N  NE  . ARG C 1 192 ? 13.003  15.444  26.102  1.00 14.86 ? 192 ARG C NE  1 
ATOM   5819 C  CZ  . ARG C 1 192 ? 12.390  15.952  25.034  1.00 16.36 ? 192 ARG C CZ  1 
ATOM   5820 N  NH1 . ARG C 1 192 ? 13.101  16.704  24.219  1.00 16.11 ? 192 ARG C NH1 1 
ATOM   5821 N  NH2 . ARG C 1 192 ? 11.090  15.750  24.779  1.00 18.61 ? 192 ARG C NH2 1 
ATOM   5822 N  N   . TYR C 1 193 ? 14.254  12.238  29.437  1.00 10.30 ? 193 TYR C N   1 
ATOM   5823 C  CA  . TYR C 1 193 ? 13.680  11.856  30.782  1.00 10.99 ? 193 TYR C CA  1 
ATOM   5824 C  C   . TYR C 1 193 ? 13.543  13.034  31.726  1.00 11.71 ? 193 TYR C C   1 
ATOM   5825 O  O   . TYR C 1 193 ? 14.177  14.076  31.514  1.00 10.72 ? 193 TYR C O   1 
ATOM   5826 C  CB  . TYR C 1 193 ? 14.501  10.711  31.434  1.00 10.04 ? 193 TYR C CB  1 
ATOM   5827 C  CG  . TYR C 1 193 ? 15.825  11.170  32.044  1.00 9.45  ? 193 TYR C CG  1 
ATOM   5828 C  CD1 . TYR C 1 193 ? 15.953  11.371  33.407  1.00 9.44  ? 193 TYR C CD1 1 
ATOM   5829 C  CD2 . TYR C 1 193 ? 16.953  11.366  31.228  1.00 8.69  ? 193 TYR C CD2 1 
ATOM   5830 C  CE1 . TYR C 1 193 ? 17.150  11.831  33.943  1.00 9.24  ? 193 TYR C CE1 1 
ATOM   5831 C  CE2 . TYR C 1 193 ? 18.157  11.835  31.750  1.00 8.61  ? 193 TYR C CE2 1 
ATOM   5832 C  CZ  . TYR C 1 193 ? 18.246  12.039  33.107  1.00 9.39  ? 193 TYR C CZ  1 
ATOM   5833 O  OH  . TYR C 1 193 ? 19.433  12.472  33.662  1.00 8.74  ? 193 TYR C OH  1 
ATOM   5834 N  N   . ARG C 1 194 ? 12.750  12.861  32.784  1.00 12.03 ? 194 ARG C N   1 
ATOM   5835 C  CA  . ARG C 1 194 ? 12.644  13.898  33.768  1.00 14.09 ? 194 ARG C CA  1 
ATOM   5836 C  C   . ARG C 1 194 ? 13.662  13.678  34.864  1.00 11.96 ? 194 ARG C C   1 
ATOM   5837 O  O   . ARG C 1 194 ? 13.777  12.579  35.423  1.00 12.43 ? 194 ARG C O   1 
ATOM   5838 C  CB  . ARG C 1 194 ? 11.210  14.031  34.367  1.00 17.02 ? 194 ARG C CB  1 
ATOM   5839 C  CG  . ARG C 1 194 ? 10.132  14.225  33.265  1.00 23.57 ? 194 ARG C CG  1 
ATOM   5840 C  CD  . ARG C 1 194 ? 8.723   14.570  33.781  1.00 29.89 ? 194 ARG C CD  1 
ATOM   5841 N  NE  . ARG C 1 194 ? 8.343   13.723  34.902  1.00 37.83 ? 194 ARG C NE  1 
ATOM   5842 C  CZ  . ARG C 1 194 ? 8.323   14.120  36.179  1.00 41.81 ? 194 ARG C CZ  1 
ATOM   5843 N  NH1 . ARG C 1 194 ? 8.611   15.394  36.528  1.00 41.24 ? 194 ARG C NH1 1 
ATOM   5844 N  NH2 . ARG C 1 194 ? 8.011   13.229  37.106  1.00 38.77 ? 194 ARG C NH2 1 
ATOM   5845 N  N   . GLY C 1 195 ? 14.419  14.725  35.148  1.00 10.62 ? 195 GLY C N   1 
ATOM   5846 C  CA  . GLY C 1 195 ? 15.465  14.613  36.189  1.00 10.42 ? 195 GLY C CA  1 
ATOM   5847 C  C   . GLY C 1 195 ? 15.824  15.941  36.845  1.00 10.84 ? 195 GLY C C   1 
ATOM   5848 O  O   . GLY C 1 195 ? 14.909  16.753  37.156  1.00 12.04 ? 195 GLY C O   1 
ATOM   5849 N  N   . SER C 1 196 ? 17.125  16.162  37.128  1.00 10.29 ? 196 SER C N   1 
ATOM   5850 C  CA  . SER C 1 196 ? 17.576  17.215  38.048  1.00 9.89  ? 196 SER C CA  1 
ATOM   5851 C  C   . SER C 1 196 ? 18.837  17.869  37.551  1.00 9.36  ? 196 SER C C   1 
ATOM   5852 O  O   . SER C 1 196 ? 19.530  17.357  36.613  1.00 9.65  ? 196 SER C O   1 
ATOM   5853 C  CB  . SER C 1 196 ? 17.857  16.691  39.476  1.00 9.53  ? 196 SER C CB  1 
ATOM   5854 O  OG  . SER C 1 196 ? 19.147  16.068  39.502  1.00 9.52  ? 196 SER C OG  1 
ATOM   5855 N  N   . LEU C 1 197 ? 19.148  18.989  38.182  1.00 10.41 ? 197 LEU C N   1 
ATOM   5856 C  CA  . LEU C 1 197 ? 20.472  19.581  37.996  1.00 11.14 ? 197 LEU C CA  1 
ATOM   5857 C  C   . LEU C 1 197 ? 21.463  18.580  38.563  1.00 10.09 ? 197 LEU C C   1 
ATOM   5858 O  O   . LEU C 1 197 ? 21.187  17.955  39.597  1.00 10.83 ? 197 LEU C O   1 
ATOM   5859 C  CB  . LEU C 1 197 ? 20.615  20.845  38.823  1.00 11.99 ? 197 LEU C CB  1 
ATOM   5860 C  CG  . LEU C 1 197 ? 19.792  22.100  38.475  1.00 12.70 ? 197 LEU C CG  1 
ATOM   5861 C  CD1 . LEU C 1 197 ? 19.908  23.238  39.494  1.00 14.18 ? 197 LEU C CD1 1 
ATOM   5862 C  CD2 . LEU C 1 197 ? 20.107  22.564  37.067  1.00 13.34 ? 197 LEU C CD2 1 
ATOM   5863 N  N   . THR C 1 198 ? 22.643  18.486  37.960  1.00 9.60  ? 198 THR C N   1 
ATOM   5864 C  CA  . THR C 1 198 ? 23.631  17.494  38.400  1.00 8.83  ? 198 THR C CA  1 
ATOM   5865 C  C   . THR C 1 198 ? 24.610  18.102  39.378  1.00 9.17  ? 198 THR C C   1 
ATOM   5866 O  O   . THR C 1 198 ? 25.543  17.409  39.874  1.00 9.45  ? 198 THR C O   1 
ATOM   5867 C  CB  . THR C 1 198 ? 24.458  16.934  37.225  1.00 8.54  ? 198 THR C CB  1 
ATOM   5868 O  OG1 . THR C 1 198 ? 25.254  18.011  36.660  1.00 10.18 ? 198 THR C OG1 1 
ATOM   5869 C  CG2 . THR C 1 198 ? 23.472  16.258  36.193  1.00 8.10  ? 198 THR C CG2 1 
ATOM   5870 N  N   . THR C 1 199 ? 24.417  19.377  39.658  1.00 8.77  ? 199 THR C N   1 
ATOM   5871 C  CA  . THR C 1 199 ? 25.238  20.012  40.697  1.00 10.20 ? 199 THR C CA  1 
ATOM   5872 C  C   . THR C 1 199 ? 24.298  20.594  41.780  1.00 9.34  ? 199 THR C C   1 
ATOM   5873 O  O   . THR C 1 199 ? 23.138  20.771  41.522  1.00 8.13  ? 199 THR C O   1 
ATOM   5874 C  CB  . THR C 1 199 ? 26.148  21.104  40.133  1.00 11.87 ? 199 THR C CB  1 
ATOM   5875 O  OG1 . THR C 1 199 ? 25.370  22.259  39.800  1.00 13.95 ? 199 THR C OG1 1 
ATOM   5876 C  CG2 . THR C 1 199 ? 26.858  20.662  38.840  1.00 11.15 ? 199 THR C CG2 1 
ATOM   5877 N  N   . PRO C 1 200 ? 24.818  20.885  42.991  1.00 9.68  ? 200 PRO C N   1 
ATOM   5878 C  CA  . PRO C 1 200 ? 23.965  21.632  43.952  1.00 10.04 ? 200 PRO C CA  1 
ATOM   5879 C  C   . PRO C 1 200 ? 23.394  22.907  43.288  1.00 10.85 ? 200 PRO C C   1 
ATOM   5880 O  O   . PRO C 1 200 ? 24.131  23.609  42.574  1.00 10.79 ? 200 PRO C O   1 
ATOM   5881 C  CB  . PRO C 1 200 ? 24.972  21.967  45.080  1.00 9.80  ? 200 PRO C CB  1 
ATOM   5882 C  CG  . PRO C 1 200 ? 25.884  20.710  45.066  1.00 9.52  ? 200 PRO C CG  1 
ATOM   5883 C  CD  . PRO C 1 200 ? 26.129  20.561  43.569  1.00 10.44 ? 200 PRO C CD  1 
ATOM   5884 N  N   . PRO C 1 201 ? 22.112  23.274  43.568  1.00 11.72 ? 201 PRO C N   1 
ATOM   5885 C  CA  . PRO C 1 201 ? 21.248  22.701  44.602  1.00 11.36 ? 201 PRO C CA  1 
ATOM   5886 C  C   . PRO C 1 201 ? 20.472  21.399  44.200  1.00 11.04 ? 201 PRO C C   1 
ATOM   5887 O  O   . PRO C 1 201 ? 19.618  20.951  44.977  1.00 12.39 ? 201 PRO C O   1 
ATOM   5888 C  CB  . PRO C 1 201 ? 20.275  23.849  44.944  1.00 12.42 ? 201 PRO C CB  1 
ATOM   5889 C  CG  . PRO C 1 201 ? 20.307  24.754  43.767  1.00 14.02 ? 201 PRO C CG  1 
ATOM   5890 C  CD  . PRO C 1 201 ? 21.529  24.479  42.921  1.00 11.87 ? 201 PRO C CD  1 
ATOM   5891 N  N   . CYS C 1 202 ? 20.841  20.805  43.061  1.00 10.42 ? 202 CYS C N   1 
ATOM   5892 C  CA  . CYS C 1 202 ? 20.240  19.556  42.521  1.00 10.37 ? 202 CYS C CA  1 
ATOM   5893 C  C   . CYS C 1 202 ? 18.683  19.551  42.333  1.00 10.23 ? 202 CYS C C   1 
ATOM   5894 O  O   . CYS C 1 202 ? 17.990  18.481  42.528  1.00 8.52  ? 202 CYS C O   1 
ATOM   5895 C  CB  . CYS C 1 202 ? 20.599  18.379  43.427  1.00 11.75 ? 202 CYS C CB  1 
ATOM   5896 S  SG  . CYS C 1 202 ? 22.333  18.108  43.838  1.00 12.32 ? 202 CYS C SG  1 
ATOM   5897 N  N   . ASN C 1 203 ? 18.104  20.732  42.045  1.00 10.85 ? 203 ASN C N   1 
ATOM   5898 C  CA  . ASN C 1 203 ? 16.648  20.840  41.978  1.00 11.64 ? 203 ASN C CA  1 
ATOM   5899 C  C   . ASN C 1 203 ? 16.109  19.839  40.972  1.00 11.53 ? 203 ASN C C   1 
ATOM   5900 O  O   . ASN C 1 203 ? 16.650  19.766  39.863  1.00 11.24 ? 203 ASN C O   1 
ATOM   5901 C  CB  . ASN C 1 203 ? 16.148  22.197  41.471  1.00 13.86 ? 203 ASN C CB  1 
ATOM   5902 C  CG  . ASN C 1 203 ? 16.792  23.389  42.114  1.00 17.13 ? 203 ASN C CG  1 
ATOM   5903 O  OD1 . ASN C 1 203 ? 17.218  24.266  41.396  1.00 25.00 ? 203 ASN C OD1 1 
ATOM   5904 N  ND2 . ASN C 1 203 ? 16.741  23.520  43.426  1.00 20.28 ? 203 ASN C ND2 1 
ATOM   5905 N  N   . PRO C 1 204 ? 15.016  19.129  41.316  1.00 11.22 ? 204 PRO C N   1 
ATOM   5906 C  CA  . PRO C 1 204 ? 14.399  18.099  40.468  1.00 10.84 ? 204 PRO C CA  1 
ATOM   5907 C  C   . PRO C 1 204 ? 13.436  18.672  39.381  1.00 11.70 ? 204 PRO C C   1 
ATOM   5908 O  O   . PRO C 1 204 ? 12.298  18.168  39.202  1.00 11.86 ? 204 PRO C O   1 
ATOM   5909 C  CB  . PRO C 1 204 ? 13.656  17.227  41.501  1.00 10.01 ? 204 PRO C CB  1 
ATOM   5910 C  CG  . PRO C 1 204 ? 13.184  18.230  42.490  1.00 10.00 ? 204 PRO C CG  1 
ATOM   5911 C  CD  . PRO C 1 204 ? 14.409  19.125  42.677  1.00 10.56 ? 204 PRO C CD  1 
ATOM   5912 N  N   . THR C 1 205 ? 13.928  19.632  38.603  1.00 12.33 ? 205 THR C N   1 
ATOM   5913 C  CA  . THR C 1 205 ? 13.089  20.481  37.754  1.00 12.34 ? 205 THR C CA  1 
ATOM   5914 C  C   . THR C 1 205 ? 13.531  20.477  36.282  1.00 12.37 ? 205 THR C C   1 
ATOM   5915 O  O   . THR C 1 205 ? 13.191  21.393  35.532  1.00 11.25 ? 205 THR C O   1 
ATOM   5916 C  CB  . THR C 1 205 ? 13.138  21.937  38.257  1.00 12.27 ? 205 THR C CB  1 
ATOM   5917 O  OG1 . THR C 1 205 ? 14.507  22.349  38.345  1.00 13.44 ? 205 THR C OG1 1 
ATOM   5918 C  CG2 . THR C 1 205 ? 12.458  22.076  39.667  1.00 13.33 ? 205 THR C CG2 1 
ATOM   5919 N  N   . VAL C 1 206 ? 14.316  19.482  35.888  1.00 11.16 ? 206 VAL C N   1 
ATOM   5920 C  CA  . VAL C 1 206 ? 14.942  19.482  34.536  1.00 11.16 ? 206 VAL C CA  1 
ATOM   5921 C  C   . VAL C 1 206 ? 14.315  18.457  33.607  1.00 11.45 ? 206 VAL C C   1 
ATOM   5922 O  O   . VAL C 1 206 ? 14.330  17.256  33.882  1.00 11.24 ? 206 VAL C O   1 
ATOM   5923 C  CB  . VAL C 1 206 ? 16.475  19.192  34.631  1.00 10.73 ? 206 VAL C CB  1 
ATOM   5924 C  CG1 . VAL C 1 206 ? 17.105  19.099  33.245  1.00 10.84 ? 206 VAL C CG1 1 
ATOM   5925 C  CG2 . VAL C 1 206 ? 17.167  20.284  35.501  1.00 11.85 ? 206 VAL C CG2 1 
ATOM   5926 N  N   . LEU C 1 207 ? 13.903  18.921  32.440  1.00 12.90 ? 207 LEU C N   1 
ATOM   5927 C  CA  . LEU C 1 207 ? 13.560  18.023  31.382  1.00 12.92 ? 207 LEU C CA  1 
ATOM   5928 C  C   . LEU C 1 207 ? 14.878  17.756  30.565  1.00 11.87 ? 207 LEU C C   1 
ATOM   5929 O  O   . LEU C 1 207 ? 15.466  18.663  29.962  1.00 11.29 ? 207 LEU C O   1 
ATOM   5930 C  CB  . LEU C 1 207 ? 12.389  18.611  30.534  1.00 14.92 ? 207 LEU C CB  1 
ATOM   5931 C  CG  . LEU C 1 207 ? 11.910  17.622  29.448  1.00 16.70 ? 207 LEU C CG  1 
ATOM   5932 C  CD1 . LEU C 1 207 ? 11.305  16.367  30.059  1.00 18.15 ? 207 LEU C CD1 1 
ATOM   5933 C  CD2 . LEU C 1 207 ? 10.883  18.269  28.522  1.00 18.17 ? 207 LEU C CD2 1 
ATOM   5934 N  N   . TRP C 1 208 ? 15.366  16.513  30.608  1.00 10.75 ? 208 TRP C N   1 
ATOM   5935 C  CA  . TRP C 1 208 ? 16.606  16.167  29.931  1.00 10.59 ? 208 TRP C CA  1 
ATOM   5936 C  C   . TRP C 1 208 ? 16.421  15.701  28.483  1.00 10.56 ? 208 TRP C C   1 
ATOM   5937 O  O   . TRP C 1 208 ? 15.614  14.849  28.249  1.00 9.78  ? 208 TRP C O   1 
ATOM   5938 C  CB  . TRP C 1 208 ? 17.376  15.096  30.695  1.00 9.21  ? 208 TRP C CB  1 
ATOM   5939 C  CG  . TRP C 1 208 ? 18.170  15.683  31.875  1.00 9.57  ? 208 TRP C CG  1 
ATOM   5940 C  CD1 . TRP C 1 208 ? 17.793  15.717  33.221  1.00 9.88  ? 208 TRP C CD1 1 
ATOM   5941 C  CD2 . TRP C 1 208 ? 19.471  16.351  31.815  1.00 10.46 ? 208 TRP C CD2 1 
ATOM   5942 N  NE1 . TRP C 1 208 ? 18.764  16.370  33.990  1.00 9.80  ? 208 TRP C NE1 1 
ATOM   5943 C  CE2 . TRP C 1 208 ? 19.800  16.766  33.188  1.00 9.59  ? 208 TRP C CE2 1 
ATOM   5944 C  CE3 . TRP C 1 208 ? 20.391  16.618  30.794  1.00 9.87  ? 208 TRP C CE3 1 
ATOM   5945 C  CZ2 . TRP C 1 208 ? 21.003  17.458  33.501  1.00 9.91  ? 208 TRP C CZ2 1 
ATOM   5946 C  CZ3 . TRP C 1 208 ? 21.591  17.313  31.139  1.00 10.17 ? 208 TRP C CZ3 1 
ATOM   5947 C  CH2 . TRP C 1 208 ? 21.855  17.750  32.463  1.00 9.91  ? 208 TRP C CH2 1 
ATOM   5948 N  N   . THR C 1 209 ? 17.229  16.215  27.575  1.00 11.08 ? 209 THR C N   1 
ATOM   5949 C  CA  . THR C 1 209 ? 17.434  15.593  26.182  1.00 11.38 ? 209 THR C CA  1 
ATOM   5950 C  C   . THR C 1 209 ? 18.941  15.323  25.977  1.00 11.24 ? 209 THR C C   1 
ATOM   5951 O  O   . THR C 1 209 ? 19.761  16.258  25.926  1.00 10.34 ? 209 THR C O   1 
ATOM   5952 C  CB  . THR C 1 209 ? 16.973  16.592  25.075  1.00 11.69 ? 209 THR C CB  1 
ATOM   5953 O  OG1 . THR C 1 209 ? 15.625  17.015  25.349  1.00 11.38 ? 209 THR C OG1 1 
ATOM   5954 C  CG2 . THR C 1 209 ? 17.065  16.000  23.638  1.00 12.59 ? 209 THR C CG2 1 
ATOM   5955 N  N   . VAL C 1 210 ? 19.316  14.048  25.955  1.00 10.19 ? 210 VAL C N   1 
ATOM   5956 C  CA  . VAL C 1 210 ? 20.694  13.662  25.687  1.00 10.45 ? 210 VAL C CA  1 
ATOM   5957 C  C   . VAL C 1 210 ? 20.774  13.172  24.250  1.00 10.66 ? 210 VAL C C   1 
ATOM   5958 O  O   . VAL C 1 210 ? 20.024  12.216  23.865  1.00 10.80 ? 210 VAL C O   1 
ATOM   5959 C  CB  . VAL C 1 210 ? 21.083  12.481  26.584  1.00 10.64 ? 210 VAL C CB  1 
ATOM   5960 C  CG1 . VAL C 1 210 ? 22.532  12.097  26.369  1.00 11.37 ? 210 VAL C CG1 1 
ATOM   5961 C  CG2 . VAL C 1 210 ? 20.834  12.823  28.037  1.00 10.76 ? 210 VAL C CG2 1 
ATOM   5962 N  N   . PHE C 1 211 ? 21.616  13.804  23.430  1.00 10.84 ? 211 PHE C N   1 
ATOM   5963 C  CA  . PHE C 1 211 ? 21.656  13.333  22.014  1.00 10.99 ? 211 PHE C CA  1 
ATOM   5964 C  C   . PHE C 1 211 ? 22.252  11.947  21.910  1.00 11.80 ? 211 PHE C C   1 
ATOM   5965 O  O   . PHE C 1 211 ? 23.129  11.589  22.676  1.00 10.46 ? 211 PHE C O   1 
ATOM   5966 C  CB  . PHE C 1 211 ? 22.255  14.367  21.037  1.00 11.03 ? 211 PHE C CB  1 
ATOM   5967 C  CG  . PHE C 1 211 ? 21.471  15.635  21.006  1.00 10.09 ? 211 PHE C CG  1 
ATOM   5968 C  CD1 . PHE C 1 211 ? 21.983  16.775  21.592  1.00 9.61  ? 211 PHE C CD1 1 
ATOM   5969 C  CD2 . PHE C 1 211 ? 20.182  15.684  20.403  1.00 10.08 ? 211 PHE C CD2 1 
ATOM   5970 C  CE1 . PHE C 1 211 ? 21.248  17.954  21.640  1.00 10.52 ? 211 PHE C CE1 1 
ATOM   5971 C  CE2 . PHE C 1 211 ? 19.439  16.870  20.426  1.00 10.33 ? 211 PHE C CE2 1 
ATOM   5972 C  CZ  . PHE C 1 211 ? 19.985  18.029  21.006  1.00 9.96  ? 211 PHE C CZ  1 
ATOM   5973 N  N   . ARG C 1 212 ? 21.707  11.149  20.993  1.00 11.70 ? 212 ARG C N   1 
ATOM   5974 C  CA  . ARG C 1 212 ? 22.188  9.773   20.798  1.00 13.71 ? 212 ARG C CA  1 
ATOM   5975 C  C   . ARG C 1 212 ? 23.690  9.680   20.383  1.00 13.30 ? 212 ARG C C   1 
ATOM   5976 O  O   . ARG C 1 212 ? 24.457  8.796   20.859  1.00 14.32 ? 212 ARG C O   1 
ATOM   5977 C  CB  . ARG C 1 212 ? 21.329  9.055   19.727  1.00 13.14 ? 212 ARG C CB  1 
ATOM   5978 C  CG  . ARG C 1 212 ? 21.763  7.592   19.604  1.00 15.76 ? 212 ARG C CG  1 
ATOM   5979 C  CD  . ARG C 1 212 ? 21.077  6.894   18.442  1.00 16.07 ? 212 ARG C CD  1 
ATOM   5980 N  NE  . ARG C 1 212 ? 21.200  5.447   18.593  1.00 18.08 ? 212 ARG C NE  1 
ATOM   5981 C  CZ  . ARG C 1 212 ? 20.719  4.576   17.708  1.00 20.16 ? 212 ARG C CZ  1 
ATOM   5982 N  NH1 . ARG C 1 212 ? 20.165  5.014   16.574  1.00 19.26 ? 212 ARG C NH1 1 
ATOM   5983 N  NH2 . ARG C 1 212 ? 20.828  3.269   17.944  1.00 19.41 ? 212 ARG C NH2 1 
ATOM   5984 N  N   . ASN C 1 213 ? 24.121  10.574  19.495  1.00 13.82 ? 213 ASN C N   1 
ATOM   5985 C  CA  . ASN C 1 213 ? 25.457  10.492  18.942  1.00 14.03 ? 213 ASN C CA  1 
ATOM   5986 C  C   . ASN C 1 213 ? 26.397  11.466  19.607  1.00 14.09 ? 213 ASN C C   1 
ATOM   5987 O  O   . ASN C 1 213 ? 25.997  12.623  19.866  1.00 13.53 ? 213 ASN C O   1 
ATOM   5988 C  CB  . ASN C 1 213 ? 25.433  10.787  17.452  1.00 16.37 ? 213 ASN C CB  1 
ATOM   5989 C  CG  . ASN C 1 213 ? 24.540  9.847   16.724  1.00 19.71 ? 213 ASN C CG  1 
ATOM   5990 O  OD1 . ASN C 1 213 ? 24.651  8.627   16.895  1.00 20.92 ? 213 ASN C OD1 1 
ATOM   5991 N  ND2 . ASN C 1 213 ? 23.609  10.393  15.971  1.00 20.34 ? 213 ASN C ND2 1 
ATOM   5992 N  N   . PRO C 1 214 ? 27.634  11.016  19.892  1.00 13.85 ? 214 PRO C N   1 
ATOM   5993 C  CA  . PRO C 1 214 ? 28.653  11.913  20.434  1.00 13.12 ? 214 PRO C CA  1 
ATOM   5994 C  C   . PRO C 1 214 ? 29.252  12.789  19.367  1.00 14.24 ? 214 PRO C C   1 
ATOM   5995 O  O   . PRO C 1 214 ? 29.105  12.486  18.164  1.00 13.57 ? 214 PRO C O   1 
ATOM   5996 C  CB  . PRO C 1 214 ? 29.727  10.947  20.951  1.00 13.91 ? 214 PRO C CB  1 
ATOM   5997 C  CG  . PRO C 1 214 ? 29.591  9.726   20.079  1.00 14.62 ? 214 PRO C CG  1 
ATOM   5998 C  CD  . PRO C 1 214 ? 28.126  9.620   19.753  1.00 13.72 ? 214 PRO C CD  1 
ATOM   5999 N  N   . VAL C 1 215 ? 29.903  13.870  19.801  1.00 13.60 ? 215 VAL C N   1 
ATOM   6000 C  CA  . VAL C 1 215 ? 30.825  14.684  18.949  1.00 13.14 ? 215 VAL C CA  1 
ATOM   6001 C  C   . VAL C 1 215 ? 32.255  14.288  19.330  1.00 12.77 ? 215 VAL C C   1 
ATOM   6002 O  O   . VAL C 1 215 ? 32.435  13.671  20.422  1.00 15.36 ? 215 VAL C O   1 
ATOM   6003 C  CB  . VAL C 1 215 ? 30.642  16.213  19.134  1.00 12.95 ? 215 VAL C CB  1 
ATOM   6004 C  CG1 . VAL C 1 215 ? 29.230  16.659  18.764  1.00 14.40 ? 215 VAL C CG1 1 
ATOM   6005 C  CG2 . VAL C 1 215 ? 30.967  16.634  20.596  1.00 12.87 ? 215 VAL C CG2 1 
ATOM   6006 N  N   . GLN C 1 216 ? 33.256  14.605  18.463  1.00 12.18 ? 216 GLN C N   1 
ATOM   6007 C  CA  . GLN C 1 216 ? 34.649  14.434  18.798  1.00 11.43 ? 216 GLN C CA  1 
ATOM   6008 C  C   . GLN C 1 216 ? 35.401  15.750  18.973  1.00 10.33 ? 216 GLN C C   1 
ATOM   6009 O  O   . GLN C 1 216 ? 35.138  16.693  18.265  1.00 10.24 ? 216 GLN C O   1 
ATOM   6010 C  CB  . GLN C 1 216 ? 35.390  13.617  17.724  1.00 13.23 ? 216 GLN C CB  1 
ATOM   6011 C  CG  . GLN C 1 216 ? 34.712  12.260  17.521  1.00 14.48 ? 216 GLN C CG  1 
ATOM   6012 C  CD  . GLN C 1 216 ? 35.348  11.442  16.460  1.00 16.82 ? 216 GLN C CD  1 
ATOM   6013 O  OE1 . GLN C 1 216 ? 36.367  11.850  15.853  1.00 14.94 ? 216 GLN C OE1 1 
ATOM   6014 N  NE2 . GLN C 1 216 ? 34.737  10.245  16.202  1.00 17.68 ? 216 GLN C NE2 1 
ATOM   6015 N  N   . ILE C 1 217 ? 36.330  15.766  19.909  1.00 10.91 ? 217 ILE C N   1 
ATOM   6016 C  CA  . ILE C 1 217 ? 37.355  16.825  20.084  1.00 11.86 ? 217 ILE C CA  1 
ATOM   6017 C  C   . ILE C 1 217 ? 38.715  16.089  20.080  1.00 13.35 ? 217 ILE C C   1 
ATOM   6018 O  O   . ILE C 1 217 ? 38.789  14.888  20.328  1.00 13.08 ? 217 ILE C O   1 
ATOM   6019 C  CB  . ILE C 1 217 ? 37.204  17.664  21.398  1.00 11.56 ? 217 ILE C CB  1 
ATOM   6020 C  CG1 . ILE C 1 217 ? 37.300  16.817  22.688  1.00 13.76 ? 217 ILE C CG1 1 
ATOM   6021 C  CG2 . ILE C 1 217 ? 35.881  18.459  21.386  1.00 12.48 ? 217 ILE C CG2 1 
ATOM   6022 C  CD1 . ILE C 1 217 ? 37.294  17.677  23.953  1.00 12.12 ? 217 ILE C CD1 1 
ATOM   6023 N  N   . SER C 1 218 ? 39.801  16.794  19.826  1.00 14.46 ? 218 SER C N   1 
ATOM   6024 C  CA  . SER C 1 218 ? 41.100  16.103  19.705  1.00 15.38 ? 218 SER C CA  1 
ATOM   6025 C  C   . SER C 1 218 ? 41.698  15.810  21.067  1.00 16.39 ? 218 SER C C   1 
ATOM   6026 O  O   . SER C 1 218 ? 41.266  16.365  22.096  1.00 14.97 ? 218 SER C O   1 
ATOM   6027 C  CB  . SER C 1 218 ? 42.103  16.927  18.873  1.00 14.81 ? 218 SER C CB  1 
ATOM   6028 O  OG  . SER C 1 218 ? 42.507  18.058  19.630  1.00 14.28 ? 218 SER C OG  1 
ATOM   6029 N  N   . GLN C 1 219 ? 42.742  14.973  21.076  1.00 15.90 ? 219 GLN C N   1 
ATOM   6030 C  CA  . GLN C 1 219 ? 43.421  14.646  22.344  1.00 20.13 ? 219 GLN C CA  1 
ATOM   6031 C  C   . GLN C 1 219 ? 43.987  15.938  22.947  1.00 18.67 ? 219 GLN C C   1 
ATOM   6032 O  O   . GLN C 1 219 ? 43.982  16.123  24.196  1.00 18.89 ? 219 GLN C O   1 
ATOM   6033 C  CB  . GLN C 1 219 ? 44.481  13.510  22.118  1.00 23.89 ? 219 GLN C CB  1 
ATOM   6034 C  CG  . GLN C 1 219 ? 45.711  13.434  23.044  1.00 28.18 ? 219 GLN C CG  1 
ATOM   6035 C  CD  . GLN C 1 219 ? 45.430  13.288  24.556  1.00 35.09 ? 219 GLN C CD  1 
ATOM   6036 O  OE1 . GLN C 1 219 ? 46.345  13.512  25.399  1.00 38.44 ? 219 GLN C OE1 1 
ATOM   6037 N  NE2 . GLN C 1 219 ? 44.197  12.920  24.918  1.00 34.82 ? 219 GLN C NE2 1 
ATOM   6038 N  N   . GLU C 1 220 ? 44.443  16.844  22.082  1.00 16.47 ? 220 GLU C N   1 
ATOM   6039 C  CA  . GLU C 1 220 ? 45.034  18.100  22.572  1.00 17.40 ? 220 GLU C CA  1 
ATOM   6040 C  C   . GLU C 1 220 ? 43.979  19.012  23.165  1.00 15.37 ? 220 GLU C C   1 
ATOM   6041 O  O   . GLU C 1 220 ? 44.244  19.674  24.174  1.00 13.32 ? 220 GLU C O   1 
ATOM   6042 C  CB  . GLU C 1 220 ? 45.884  18.885  21.544  1.00 20.16 ? 220 GLU C CB  1 
ATOM   6043 C  CG  . GLU C 1 220 ? 45.746  18.538  20.073  1.00 28.84 ? 220 GLU C CG  1 
ATOM   6044 C  CD  . GLU C 1 220 ? 46.376  17.190  19.701  1.00 29.89 ? 220 GLU C CD  1 
ATOM   6045 O  OE1 . GLU C 1 220 ? 45.619  16.318  19.286  1.00 27.94 ? 220 GLU C OE1 1 
ATOM   6046 O  OE2 . GLU C 1 220 ? 47.613  16.992  19.852  1.00 34.51 ? 220 GLU C OE2 1 
ATOM   6047 N  N   . GLN C 1 221 ? 42.792  19.049  22.543  1.00 12.55 ? 221 GLN C N   1 
ATOM   6048 C  CA  . GLN C 1 221 ? 41.667  19.863  23.115  1.00 12.67 ? 221 GLN C CA  1 
ATOM   6049 C  C   . GLN C 1 221 ? 41.202  19.281  24.451  1.00 12.72 ? 221 GLN C C   1 
ATOM   6050 O  O   . GLN C 1 221 ? 40.984  20.022  25.423  1.00 12.41 ? 221 GLN C O   1 
ATOM   6051 C  CB  . GLN C 1 221 ? 40.484  19.948  22.149  1.00 12.84 ? 221 GLN C CB  1 
ATOM   6052 C  CG  . GLN C 1 221 ? 40.798  20.698  20.846  1.00 12.54 ? 221 GLN C CG  1 
ATOM   6053 C  CD  . GLN C 1 221 ? 39.626  20.703  19.869  1.00 12.85 ? 221 GLN C CD  1 
ATOM   6054 O  OE1 . GLN C 1 221 ? 39.252  19.684  19.291  1.00 12.90 ? 221 GLN C OE1 1 
ATOM   6055 N  NE2 . GLN C 1 221 ? 39.055  21.893  19.651  1.00 13.48 ? 221 GLN C NE2 1 
ATOM   6056 N  N   . LEU C 1 222 ? 41.035  17.955  24.488  1.00 11.50 ? 222 LEU C N   1 
ATOM   6057 C  CA  . LEU C 1 222 ? 40.686  17.312  25.736  1.00 11.39 ? 222 LEU C CA  1 
ATOM   6058 C  C   . LEU C 1 222 ? 41.754  17.590  26.820  1.00 12.12 ? 222 LEU C C   1 
ATOM   6059 O  O   . LEU C 1 222 ? 41.399  17.921  27.969  1.00 10.74 ? 222 LEU C O   1 
ATOM   6060 C  CB  . LEU C 1 222 ? 40.407  15.839  25.537  1.00 11.62 ? 222 LEU C CB  1 
ATOM   6061 C  CG  . LEU C 1 222 ? 39.947  15.038  26.762  1.00 11.42 ? 222 LEU C CG  1 
ATOM   6062 C  CD1 . LEU C 1 222 ? 38.578  15.519  27.233  1.00 12.17 ? 222 LEU C CD1 1 
ATOM   6063 C  CD2 . LEU C 1 222 ? 39.890  13.516  26.487  1.00 11.79 ? 222 LEU C CD2 1 
ATOM   6064 N  N   . LEU C 1 223 ? 43.047  17.509  26.492  1.00 12.90 ? 223 LEU C N   1 
ATOM   6065 C  CA  . LEU C 1 223 ? 44.078  17.687  27.544  1.00 13.72 ? 223 LEU C CA  1 
ATOM   6066 C  C   . LEU C 1 223 ? 44.035  19.125  28.054  1.00 13.92 ? 223 LEU C C   1 
ATOM   6067 O  O   . LEU C 1 223 ? 44.175  19.371  29.276  1.00 14.35 ? 223 LEU C O   1 
ATOM   6068 C  CB  . LEU C 1 223 ? 45.481  17.358  27.065  1.00 15.09 ? 223 LEU C CB  1 
ATOM   6069 C  CG  . LEU C 1 223 ? 46.604  17.388  28.118  1.00 15.74 ? 223 LEU C CG  1 
ATOM   6070 C  CD1 . LEU C 1 223 ? 46.408  16.220  29.115  1.00 15.95 ? 223 LEU C CD1 1 
ATOM   6071 C  CD2 . LEU C 1 223 ? 47.920  17.230  27.360  1.00 17.59 ? 223 LEU C CD2 1 
ATOM   6072 N  N   . ALA C 1 224 ? 43.776  20.048  27.130  1.00 13.79 ? 224 ALA C N   1 
ATOM   6073 C  CA  . ALA C 1 224 ? 43.627  21.501  27.495  1.00 12.74 ? 224 ALA C CA  1 
ATOM   6074 C  C   . ALA C 1 224 ? 42.487  21.728  28.464  1.00 13.00 ? 224 ALA C C   1 
ATOM   6075 O  O   . ALA C 1 224 ? 42.634  22.406  29.458  1.00 12.56 ? 224 ALA C O   1 
ATOM   6076 C  CB  . ALA C 1 224 ? 43.475  22.371  26.260  1.00 12.66 ? 224 ALA C CB  1 
ATOM   6077 N  N   . LEU C 1 225 ? 41.306  21.178  28.138  1.00 12.80 ? 225 LEU C N   1 
ATOM   6078 C  CA  . LEU C 1 225 ? 40.171  21.296  29.025  1.00 12.24 ? 225 LEU C CA  1 
ATOM   6079 C  C   . LEU C 1 225 ? 40.492  20.730  30.455  1.00 13.73 ? 225 LEU C C   1 
ATOM   6080 O  O   . LEU C 1 225 ? 40.088  21.323  31.489  1.00 13.71 ? 225 LEU C O   1 
ATOM   6081 C  CB  . LEU C 1 225 ? 38.949  20.545  28.382  1.00 11.35 ? 225 LEU C CB  1 
ATOM   6082 C  CG  . LEU C 1 225 ? 37.620  20.648  29.164  1.00 10.77 ? 225 LEU C CG  1 
ATOM   6083 C  CD1 . LEU C 1 225 ? 37.170  22.104  29.348  1.00 10.95 ? 225 LEU C CD1 1 
ATOM   6084 C  CD2 . LEU C 1 225 ? 36.554  19.762  28.454  1.00 11.18 ? 225 LEU C CD2 1 
ATOM   6085 N  N   . GLU C 1 226 ? 41.256  19.619  30.512  1.00 12.69 ? 226 GLU C N   1 
ATOM   6086 C  CA  . GLU C 1 226 ? 41.480  18.914  31.771  1.00 13.48 ? 226 GLU C CA  1 
ATOM   6087 C  C   . GLU C 1 226 ? 42.619  19.568  32.567  1.00 13.56 ? 226 GLU C C   1 
ATOM   6088 O  O   . GLU C 1 226 ? 42.808  19.204  33.695  1.00 18.15 ? 226 GLU C O   1 
ATOM   6089 C  CB  . GLU C 1 226 ? 41.898  17.424  31.541  1.00 13.21 ? 226 GLU C CB  1 
ATOM   6090 C  CG  . GLU C 1 226 ? 40.859  16.545  30.860  1.00 13.20 ? 226 GLU C CG  1 
ATOM   6091 C  CD  . GLU C 1 226 ? 41.418  15.250  30.278  1.00 13.80 ? 226 GLU C CD  1 
ATOM   6092 O  OE1 . GLU C 1 226 ? 42.644  15.238  29.970  1.00 13.61 ? 226 GLU C OE1 1 
ATOM   6093 O  OE2 . GLU C 1 226 ? 40.640  14.272  30.043  1.00 12.57 ? 226 GLU C OE2 1 
ATOM   6094 N  N   . THR C 1 227 ? 43.424  20.445  31.970  1.00 14.26 ? 227 THR C N   1 
ATOM   6095 C  CA  . THR C 1 227 ? 44.659  20.899  32.657  1.00 14.52 ? 227 THR C CA  1 
ATOM   6096 C  C   . THR C 1 227 ? 44.740  22.412  32.778  1.00 15.47 ? 227 THR C C   1 
ATOM   6097 O  O   . THR C 1 227 ? 45.625  22.898  33.460  1.00 14.70 ? 227 THR C O   1 
ATOM   6098 C  CB  . THR C 1 227 ? 45.981  20.409  31.935  1.00 13.53 ? 227 THR C CB  1 
ATOM   6099 O  OG1 . THR C 1 227 ? 45.997  20.888  30.578  1.00 13.92 ? 227 THR C OG1 1 
ATOM   6100 C  CG2 . THR C 1 227 ? 46.092  18.871  31.837  1.00 14.73 ? 227 THR C CG2 1 
ATOM   6101 N  N   . ALA C 1 228 ? 43.854  23.149  32.108  1.00 14.89 ? 228 ALA C N   1 
ATOM   6102 C  CA  . ALA C 1 228 ? 43.931  24.635  32.063  1.00 14.38 ? 228 ALA C CA  1 
ATOM   6103 C  C   . ALA C 1 228 ? 43.412  25.349  33.307  1.00 12.65 ? 228 ALA C C   1 
ATOM   6104 O  O   . ALA C 1 228 ? 43.897  26.436  33.661  1.00 14.22 ? 228 ALA C O   1 
ATOM   6105 C  CB  . ALA C 1 228 ? 43.174  25.151  30.819  1.00 16.11 ? 228 ALA C CB  1 
ATOM   6106 N  N   . LEU C 1 229 ? 42.452  24.739  34.001  1.00 12.63 ? 229 LEU C N   1 
ATOM   6107 C  CA  . LEU C 1 229 ? 41.581  25.499  34.958  1.00 11.39 ? 229 LEU C CA  1 
ATOM   6108 C  C   . LEU C 1 229 ? 41.745  25.087  36.421  1.00 11.83 ? 229 LEU C C   1 
ATOM   6109 O  O   . LEU C 1 229 ? 41.962  23.915  36.725  1.00 11.13 ? 229 LEU C O   1 
ATOM   6110 C  CB  . LEU C 1 229 ? 40.090  25.430  34.559  1.00 12.08 ? 229 LEU C CB  1 
ATOM   6111 C  CG  . LEU C 1 229 ? 39.760  25.707  33.093  1.00 11.52 ? 229 LEU C CG  1 
ATOM   6112 C  CD1 . LEU C 1 229 ? 38.265  25.444  32.889  1.00 11.17 ? 229 LEU C CD1 1 
ATOM   6113 C  CD2 . LEU C 1 229 ? 40.160  27.177  32.881  1.00 11.58 ? 229 LEU C CD2 1 
ATOM   6114 N  N   . TYR C 1 230 ? 41.695  26.070  37.322  1.00 13.00 ? 230 TYR C N   1 
ATOM   6115 C  CA  . TYR C 1 230 ? 41.699  25.791  38.763  1.00 14.41 ? 230 TYR C CA  1 
ATOM   6116 C  C   . TYR C 1 230 ? 40.358  26.127  39.401  1.00 16.59 ? 230 TYR C C   1 
ATOM   6117 O  O   . TYR C 1 230 ? 39.630  26.977  38.914  1.00 13.73 ? 230 TYR C O   1 
ATOM   6118 C  CB  . TYR C 1 230 ? 42.837  26.592  39.432  1.00 16.85 ? 230 TYR C CB  1 
ATOM   6119 C  CG  . TYR C 1 230 ? 44.200  26.115  38.941  1.00 20.61 ? 230 TYR C CG  1 
ATOM   6120 C  CD1 . TYR C 1 230 ? 44.696  26.528  37.694  1.00 22.39 ? 230 TYR C CD1 1 
ATOM   6121 C  CD2 . TYR C 1 230 ? 44.977  25.247  39.707  1.00 21.89 ? 230 TYR C CD2 1 
ATOM   6122 C  CE1 . TYR C 1 230 ? 45.905  26.071  37.209  1.00 26.23 ? 230 TYR C CE1 1 
ATOM   6123 C  CE2 . TYR C 1 230 ? 46.205  24.793  39.223  1.00 23.74 ? 230 TYR C CE2 1 
ATOM   6124 C  CZ  . TYR C 1 230 ? 46.659  25.221  37.984  1.00 26.89 ? 230 TYR C CZ  1 
ATOM   6125 O  OH  . TYR C 1 230 ? 47.877  24.790  37.481  1.00 31.40 ? 230 TYR C OH  1 
ATOM   6126 N  N   . CYS C 1 231 ? 40.008  25.425  40.480  1.00 17.98 ? 231 CYS C N   1 
ATOM   6127 C  CA  . CYS C 1 231 ? 38.780  25.699  41.247  1.00 17.70 ? 231 CYS C CA  1 
ATOM   6128 C  C   . CYS C 1 231 ? 38.891  26.940  42.092  1.00 19.34 ? 231 CYS C C   1 
ATOM   6129 O  O   . CYS C 1 231 ? 37.871  27.562  42.436  1.00 20.25 ? 231 CYS C O   1 
ATOM   6130 C  CB  . CYS C 1 231 ? 38.490  24.526  42.189  1.00 19.09 ? 231 CYS C CB  1 
ATOM   6131 S  SG  . CYS C 1 231 ? 37.910  23.047  41.335  1.00 19.22 ? 231 CYS C SG  1 
ATOM   6132 N  N   . THR C 1 232 ? 40.123  27.258  42.472  1.00 19.62 ? 232 THR C N   1 
ATOM   6133 C  CA  . THR C 1 232 ? 40.462  28.331  43.424  1.00 22.35 ? 232 THR C CA  1 
ATOM   6134 C  C   . THR C 1 232 ? 40.873  29.715  42.811  1.00 23.70 ? 232 THR C C   1 
ATOM   6135 O  O   . THR C 1 232 ? 41.173  29.822  41.608  1.00 19.69 ? 232 THR C O   1 
ATOM   6136 C  CB  . THR C 1 232 ? 41.663  27.827  44.232  1.00 24.50 ? 232 THR C CB  1 
ATOM   6137 O  OG1 . THR C 1 232 ? 42.606  27.255  43.321  1.00 23.64 ? 232 THR C OG1 1 
ATOM   6138 C  CG2 . THR C 1 232 ? 41.246  26.732  45.205  1.00 25.15 ? 232 THR C CG2 1 
ATOM   6139 N  N   . HIS C 1 233 ? 40.914  30.761  43.638  1.00 26.82 ? 233 HIS C N   1 
ATOM   6140 C  CA  . HIS C 1 233 ? 41.311  32.103  43.173  1.00 30.94 ? 233 HIS C CA  1 
ATOM   6141 C  C   . HIS C 1 233 ? 42.779  32.177  42.860  1.00 33.35 ? 233 HIS C C   1 
ATOM   6142 O  O   . HIS C 1 233 ? 43.573  31.332  43.321  1.00 32.66 ? 233 HIS C O   1 
ATOM   6143 C  CB  . HIS C 1 233 ? 40.960  33.168  44.199  1.00 33.05 ? 233 HIS C CB  1 
ATOM   6144 C  CG  . HIS C 1 233 ? 39.483  33.349  44.404  1.00 37.23 ? 233 HIS C CG  1 
ATOM   6145 N  ND1 . HIS C 1 233 ? 38.701  34.023  43.519  1.00 38.49 ? 233 HIS C ND1 1 
ATOM   6146 C  CD2 . HIS C 1 233 ? 38.648  32.948  45.449  1.00 36.59 ? 233 HIS C CD2 1 
ATOM   6147 C  CE1 . HIS C 1 233 ? 37.425  34.027  43.964  1.00 37.96 ? 233 HIS C CE1 1 
ATOM   6148 N  NE2 . HIS C 1 233 ? 37.388  33.364  45.144  1.00 37.89 ? 233 HIS C NE2 1 
ATOM   6149 N  N   . MET C 1 234 ? 43.167  33.177  42.066  1.00 36.99 ? 234 MET C N   1 
ATOM   6150 C  CA  . MET C 1 234 ? 44.574  33.333  41.650  1.00 39.69 ? 234 MET C CA  1 
ATOM   6151 C  C   . MET C 1 234 ? 45.581  33.313  42.829  1.00 39.61 ? 234 MET C C   1 
ATOM   6152 O  O   . MET C 1 234 ? 46.702  32.858  42.672  1.00 40.74 ? 234 MET C O   1 
ATOM   6153 C  CB  . MET C 1 234 ? 44.777  34.557  40.728  1.00 41.45 ? 234 MET C CB  1 
ATOM   6154 C  CG  . MET C 1 234 ? 46.118  34.579  39.981  1.00 43.99 ? 234 MET C CG  1 
ATOM   6155 S  SD  . MET C 1 234 ? 46.352  35.911  38.770  1.00 51.11 ? 234 MET C SD  1 
ATOM   6156 C  CE  . MET C 1 234 ? 46.217  35.029  37.219  1.00 41.48 ? 234 MET C CE  1 
ATOM   6157 N  N   . ASP C 1 235 ? 45.176  33.747  44.012  1.00 39.93 ? 235 ASP C N   1 
ATOM   6158 C  CA  . ASP C 1 235 ? 46.146  33.810  45.127  1.00 44.60 ? 235 ASP C CA  1 
ATOM   6159 C  C   . ASP C 1 235 ? 45.944  32.760  46.236  1.00 44.13 ? 235 ASP C C   1 
ATOM   6160 O  O   . ASP C 1 235 ? 46.428  32.940  47.361  1.00 43.06 ? 235 ASP C O   1 
ATOM   6161 C  CB  . ASP C 1 235 ? 46.200  35.234  45.714  1.00 47.68 ? 235 ASP C CB  1 
ATOM   6162 C  CG  . ASP C 1 235 ? 44.945  35.611  46.520  1.00 51.72 ? 235 ASP C CG  1 
ATOM   6163 O  OD1 . ASP C 1 235 ? 43.890  34.929  46.410  1.00 52.93 ? 235 ASP C OD1 1 
ATOM   6164 O  OD2 . ASP C 1 235 ? 45.017  36.610  47.277  1.00 52.50 ? 235 ASP C OD2 1 
ATOM   6165 N  N   . ASP C 1 236 ? 45.248  31.669  45.920  1.00 40.71 ? 236 ASP C N   1 
ATOM   6166 C  CA  . ASP C 1 236 ? 44.776  30.733  46.953  1.00 42.78 ? 236 ASP C CA  1 
ATOM   6167 C  C   . ASP C 1 236 ? 45.882  29.824  47.503  1.00 42.36 ? 236 ASP C C   1 
ATOM   6168 O  O   . ASP C 1 236 ? 46.468  29.044  46.750  1.00 41.99 ? 236 ASP C O   1 
ATOM   6169 C  CB  . ASP C 1 236 ? 43.586  29.907  46.448  1.00 41.64 ? 236 ASP C CB  1 
ATOM   6170 C  CG  . ASP C 1 236 ? 42.715  29.385  47.578  1.00 39.71 ? 236 ASP C CG  1 
ATOM   6171 O  OD1 . ASP C 1 236 ? 43.243  28.736  48.502  1.00 32.30 ? 236 ASP C OD1 1 
ATOM   6172 O  OD2 . ASP C 1 236 ? 41.489  29.640  47.550  1.00 42.81 ? 236 ASP C OD2 1 
ATOM   6173 N  N   . PRO C 1 237 ? 46.164  29.925  48.798  1.00 41.60 ? 237 PRO C N   1 
ATOM   6174 C  CA  . PRO C 1 237 ? 47.228  29.125  49.416  1.00 39.54 ? 237 PRO C CA  1 
ATOM   6175 C  C   . PRO C 1 237 ? 47.063  27.626  49.163  1.00 40.62 ? 237 PRO C C   1 
ATOM   6176 O  O   . PRO C 1 237 ? 48.051  26.917  48.976  1.00 37.97 ? 237 PRO C O   1 
ATOM   6177 C  CB  . PRO C 1 237 ? 47.066  29.427  50.907  1.00 44.47 ? 237 PRO C CB  1 
ATOM   6178 C  CG  . PRO C 1 237 ? 45.625  29.764  51.062  1.00 44.62 ? 237 PRO C CG  1 
ATOM   6179 C  CD  . PRO C 1 237 ? 45.231  30.474  49.797  1.00 42.40 ? 237 PRO C CD  1 
ATOM   6180 N  N   . SER C 1 238 ? 45.819  27.160  49.164  1.00 35.30 ? 238 SER C N   1 
ATOM   6181 C  CA  . SER C 1 238 ? 45.505  25.735  48.971  1.00 33.78 ? 238 SER C CA  1 
ATOM   6182 C  C   . SER C 1 238 ? 44.812  25.575  47.595  1.00 33.37 ? 238 SER C C   1 
ATOM   6183 O  O   . SER C 1 238 ? 43.565  25.465  47.545  1.00 30.43 ? 238 SER C O   1 
ATOM   6184 C  CB  . SER C 1 238 ? 44.569  25.225  50.089  1.00 34.98 ? 238 SER C CB  1 
ATOM   6185 O  OG  . SER C 1 238 ? 45.131  25.341  51.401  1.00 33.48 ? 238 SER C OG  1 
ATOM   6186 N  N   . PRO C 1 239 ? 45.610  25.608  46.485  1.00 29.14 ? 239 PRO C N   1 
ATOM   6187 C  CA  . PRO C 1 239 ? 45.116  25.499  45.063  1.00 30.14 ? 239 PRO C CA  1 
ATOM   6188 C  C   . PRO C 1 239 ? 44.520  24.137  44.802  1.00 30.28 ? 239 PRO C C   1 
ATOM   6189 O  O   . PRO C 1 239 ? 44.949  23.174  45.431  1.00 31.03 ? 239 PRO C O   1 
ATOM   6190 C  CB  . PRO C 1 239 ? 46.392  25.607  44.224  1.00 29.23 ? 239 PRO C CB  1 
ATOM   6191 C  CG  . PRO C 1 239 ? 47.398  26.242  45.116  1.00 29.21 ? 239 PRO C CG  1 
ATOM   6192 C  CD  . PRO C 1 239 ? 47.056  25.869  46.535  1.00 30.11 ? 239 PRO C CD  1 
ATOM   6193 N  N   . ARG C 1 240 ? 43.533  24.044  43.902  1.00 26.97 ? 240 ARG C N   1 
ATOM   6194 C  CA  . ARG C 1 240 ? 42.895  22.766  43.626  1.00 23.43 ? 240 ARG C CA  1 
ATOM   6195 C  C   . ARG C 1 240 ? 42.647  22.808  42.116  1.00 22.53 ? 240 ARG C C   1 
ATOM   6196 O  O   . ARG C 1 240 ? 42.011  23.766  41.632  1.00 16.76 ? 240 ARG C O   1 
ATOM   6197 C  CB  . ARG C 1 240 ? 41.552  22.654  44.372  1.00 24.29 ? 240 ARG C CB  1 
ATOM   6198 C  CG  . ARG C 1 240 ? 41.665  22.512  45.893  1.00 26.36 ? 240 ARG C CG  1 
ATOM   6199 C  CD  . ARG C 1 240 ? 40.311  22.353  46.588  1.00 23.07 ? 240 ARG C CD  1 
ATOM   6200 N  NE  . ARG C 1 240 ? 39.599  23.626  46.720  1.00 24.66 ? 240 ARG C NE  1 
ATOM   6201 C  CZ  . ARG C 1 240 ? 38.462  23.929  46.090  1.00 29.40 ? 240 ARG C CZ  1 
ATOM   6202 N  NH1 . ARG C 1 240 ? 37.884  23.039  45.281  1.00 23.70 ? 240 ARG C NH1 1 
ATOM   6203 N  NH2 . ARG C 1 240 ? 37.901  25.135  46.261  1.00 28.91 ? 240 ARG C NH2 1 
ATOM   6204 N  N   . GLU C 1 241 ? 43.189  21.840  41.368  1.00 19.05 ? 241 GLU C N   1 
ATOM   6205 C  CA  . GLU C 1 241 ? 42.937  21.785  39.938  1.00 19.24 ? 241 GLU C CA  1 
ATOM   6206 C  C   . GLU C 1 241 ? 41.480  21.455  39.709  1.00 18.75 ? 241 GLU C C   1 
ATOM   6207 O  O   . GLU C 1 241 ? 40.880  20.814  40.546  1.00 17.19 ? 241 GLU C O   1 
ATOM   6208 C  CB  . GLU C 1 241 ? 43.764  20.666  39.306  1.00 22.80 ? 241 GLU C CB  1 
ATOM   6209 C  CG  . GLU C 1 241 ? 45.254  20.847  39.391  1.00 26.35 ? 241 GLU C CG  1 
ATOM   6210 C  CD  . GLU C 1 241 ? 45.950  19.537  39.097  1.00 30.58 ? 241 GLU C CD  1 
ATOM   6211 O  OE1 . GLU C 1 241 ? 45.314  18.478  39.307  1.00 34.25 ? 241 GLU C OE1 1 
ATOM   6212 O  OE2 . GLU C 1 241 ? 47.125  19.558  38.677  1.00 30.96 ? 241 GLU C OE2 1 
ATOM   6213 N  N   . MET C 1 242 ? 40.915  21.887  38.572  1.00 15.51 ? 242 MET C N   1 
ATOM   6214 C  CA  . MET C 1 242 ? 39.526  21.646  38.203  1.00 14.43 ? 242 MET C CA  1 
ATOM   6215 C  C   . MET C 1 242 ? 39.494  20.436  37.285  1.00 13.51 ? 242 MET C C   1 
ATOM   6216 O  O   . MET C 1 242 ? 39.706  20.527  36.054  1.00 13.18 ? 242 MET C O   1 
ATOM   6217 C  CB  . MET C 1 242 ? 38.877  22.897  37.528  1.00 14.42 ? 242 MET C CB  1 
ATOM   6218 C  CG  . MET C 1 242 ? 37.373  22.690  37.186  1.00 14.77 ? 242 MET C CG  1 
ATOM   6219 S  SD  . MET C 1 242 ? 36.453  24.028  36.386  1.00 13.56 ? 242 MET C SD  1 
ATOM   6220 C  CE  . MET C 1 242 ? 36.737  25.442  37.480  1.00 13.47 ? 242 MET C CE  1 
ATOM   6221 N  N   . ILE C 1 243 ? 39.301  19.289  37.945  1.00 12.82 ? 243 ILE C N   1 
ATOM   6222 C  CA  . ILE C 1 243 ? 39.309  17.969  37.320  1.00 11.75 ? 243 ILE C CA  1 
ATOM   6223 C  C   . ILE C 1 243 ? 38.216  17.112  37.886  1.00 10.37 ? 243 ILE C C   1 
ATOM   6224 O  O   . ILE C 1 243 ? 37.763  17.372  39.001  1.00 10.67 ? 243 ILE C O   1 
ATOM   6225 C  CB  . ILE C 1 243 ? 40.678  17.255  37.507  1.00 12.10 ? 243 ILE C CB  1 
ATOM   6226 C  CG1 . ILE C 1 243 ? 41.062  17.189  39.012  1.00 11.76 ? 243 ILE C CG1 1 
ATOM   6227 C  CG2 . ILE C 1 243 ? 41.748  17.856  36.611  1.00 11.31 ? 243 ILE C CG2 1 
ATOM   6228 C  CD1 . ILE C 1 243 ? 42.216  16.196  39.237  1.00 13.53 ? 243 ILE C CD1 1 
ATOM   6229 N  N   . ASN C 1 244 ? 37.736  16.134  37.112  1.00 10.64 ? 244 ASN C N   1 
ATOM   6230 C  CA  . ASN C 1 244 ? 36.761  15.138  37.633  1.00 9.71  ? 244 ASN C CA  1 
ATOM   6231 C  C   . ASN C 1 244 ? 35.531  15.883  38.204  1.00 9.82  ? 244 ASN C C   1 
ATOM   6232 O  O   . ASN C 1 244 ? 35.015  15.538  39.286  1.00 9.71  ? 244 ASN C O   1 
ATOM   6233 C  CB  . ASN C 1 244 ? 37.405  14.273  38.745  1.00 11.26 ? 244 ASN C CB  1 
ATOM   6234 C  CG  . ASN C 1 244 ? 38.693  13.605  38.263  1.00 11.56 ? 244 ASN C CG  1 
ATOM   6235 O  OD1 . ASN C 1 244 ? 38.775  13.219  37.110  1.00 10.77 ? 244 ASN C OD1 1 
ATOM   6236 N  ND2 . ASN C 1 244 ? 39.744  13.533  39.150  1.00 11.99 ? 244 ASN C ND2 1 
ATOM   6237 N  N   . ASN C 1 245 ? 35.086  16.919  37.475  1.00 8.38  ? 245 ASN C N   1 
ATOM   6238 C  CA  . ASN C 1 245 ? 33.878  17.696  37.865  1.00 8.56  ? 245 ASN C CA  1 
ATOM   6239 C  C   . ASN C 1 245 ? 32.581  17.103  37.266  1.00 8.76  ? 245 ASN C C   1 
ATOM   6240 O  O   . ASN C 1 245 ? 31.781  17.829  36.672  1.00 8.28  ? 245 ASN C O   1 
ATOM   6241 C  CB  . ASN C 1 245 ? 34.050  19.197  37.490  1.00 8.25  ? 245 ASN C CB  1 
ATOM   6242 C  CG  . ASN C 1 245 ? 34.255  19.460  35.980  1.00 8.97  ? 245 ASN C CG  1 
ATOM   6243 O  OD1 . ASN C 1 245 ? 34.650  18.589  35.204  1.00 9.36  ? 245 ASN C OD1 1 
ATOM   6244 N  ND2 . ASN C 1 245 ? 34.078  20.730  35.583  1.00 8.69  ? 245 ASN C ND2 1 
ATOM   6245 N  N   . PHE C 1 246 ? 32.406  15.788  37.417  1.00 8.88  ? 246 PHE C N   1 
ATOM   6246 C  CA  . PHE C 1 246 ? 31.188  15.032  36.996  1.00 9.29  ? 246 PHE C CA  1 
ATOM   6247 C  C   . PHE C 1 246 ? 30.633  14.250  38.221  1.00 10.07 ? 246 PHE C C   1 
ATOM   6248 O  O   . PHE C 1 246 ? 31.410  13.857  39.173  1.00 10.08 ? 246 PHE C O   1 
ATOM   6249 C  CB  . PHE C 1 246 ? 31.494  14.095  35.855  1.00 9.96  ? 246 PHE C CB  1 
ATOM   6250 C  CG  . PHE C 1 246 ? 32.460  13.000  36.233  1.00 10.67 ? 246 PHE C CG  1 
ATOM   6251 C  CD1 . PHE C 1 246 ? 31.972  11.695  36.511  1.00 10.79 ? 246 PHE C CD1 1 
ATOM   6252 C  CD2 . PHE C 1 246 ? 33.840  13.244  36.307  1.00 10.42 ? 246 PHE C CD2 1 
ATOM   6253 C  CE1 . PHE C 1 246 ? 32.829  10.668  36.874  1.00 10.86 ? 246 PHE C CE1 1 
ATOM   6254 C  CE2 . PHE C 1 246 ? 34.743  12.208  36.621  1.00 11.16 ? 246 PHE C CE2 1 
ATOM   6255 C  CZ  . PHE C 1 246 ? 34.226  10.915  36.932  1.00 11.76 ? 246 PHE C CZ  1 
ATOM   6256 N  N   . ARG C 1 247 ? 29.299  14.142  38.264  1.00 8.86  ? 247 ARG C N   1 
ATOM   6257 C  CA  . ARG C 1 247 ? 28.590  13.376  39.308  1.00 8.76  ? 247 ARG C CA  1 
ATOM   6258 C  C   . ARG C 1 247 ? 28.505  11.896  38.867  1.00 8.21  ? 247 ARG C C   1 
ATOM   6259 O  O   . ARG C 1 247 ? 28.334  11.652  37.687  1.00 8.83  ? 247 ARG C O   1 
ATOM   6260 C  CB  . ARG C 1 247 ? 27.165  13.924  39.487  1.00 8.61  ? 247 ARG C CB  1 
ATOM   6261 C  CG  . ARG C 1 247 ? 26.492  13.492  40.816  1.00 8.56  ? 247 ARG C CG  1 
ATOM   6262 C  CD  . ARG C 1 247 ? 25.123  14.111  40.931  1.00 7.83  ? 247 ARG C CD  1 
ATOM   6263 N  NE  . ARG C 1 247 ? 24.565  13.976  42.289  1.00 8.35  ? 247 ARG C NE  1 
ATOM   6264 C  CZ  . ARG C 1 247 ? 23.306  14.261  42.620  1.00 7.99  ? 247 ARG C CZ  1 
ATOM   6265 N  NH1 . ARG C 1 247 ? 22.416  14.639  41.694  1.00 8.86  ? 247 ARG C NH1 1 
ATOM   6266 N  NH2 . ARG C 1 247 ? 22.889  14.103  43.869  1.00 7.87  ? 247 ARG C NH2 1 
ATOM   6267 N  N   . GLN C 1 248 ? 28.585  10.953  39.813  1.00 7.85  ? 248 GLN C N   1 
ATOM   6268 C  CA  . GLN C 1 248 ? 28.356  9.513   39.557  1.00 8.16  ? 248 GLN C CA  1 
ATOM   6269 C  C   . GLN C 1 248 ? 26.902  9.345   39.094  1.00 7.99  ? 248 GLN C C   1 
ATOM   6270 O  O   . GLN C 1 248 ? 26.025  10.156  39.484  1.00 7.90  ? 248 GLN C O   1 
ATOM   6271 C  CB  . GLN C 1 248 ? 28.565  8.727   40.851  1.00 8.58  ? 248 GLN C CB  1 
ATOM   6272 C  CG  . GLN C 1 248 ? 30.038  8.714   41.335  1.00 8.08  ? 248 GLN C CG  1 
ATOM   6273 C  CD  . GLN C 1 248 ? 30.991  8.133   40.283  1.00 8.78  ? 248 GLN C CD  1 
ATOM   6274 O  OE1 . GLN C 1 248 ? 31.580  8.893   39.470  1.00 8.77  ? 248 GLN C OE1 1 
ATOM   6275 N  NE2 . GLN C 1 248 ? 31.114  6.767   40.264  1.00 9.33  ? 248 GLN C NE2 1 
ATOM   6276 N  N   . VAL C 1 249 ? 26.618  8.302   38.307  1.00 9.01  ? 249 VAL C N   1 
ATOM   6277 C  CA  . VAL C 1 249 ? 25.223  8.057   37.935  1.00 9.23  ? 249 VAL C CA  1 
ATOM   6278 C  C   . VAL C 1 249 ? 24.352  7.709   39.178  1.00 9.33  ? 249 VAL C C   1 
ATOM   6279 O  O   . VAL C 1 249 ? 24.871  7.152   40.158  1.00 9.85  ? 249 VAL C O   1 
ATOM   6280 C  CB  . VAL C 1 249 ? 25.047  6.964   36.849  1.00 9.11  ? 249 VAL C CB  1 
ATOM   6281 C  CG1 . VAL C 1 249 ? 25.646  7.464   35.488  1.00 9.54  ? 249 VAL C CG1 1 
ATOM   6282 C  CG2 . VAL C 1 249 ? 25.688  5.625   37.282  1.00 9.06  ? 249 VAL C CG2 1 
ATOM   6283 N  N   . GLN C 1 250 ? 23.037  7.994   39.084  1.00 8.78  ? 250 GLN C N   1 
ATOM   6284 C  CA  . GLN C 1 250 ? 22.089  7.868   40.157  1.00 8.62  ? 250 GLN C CA  1 
ATOM   6285 C  C   . GLN C 1 250 ? 21.227  6.600   39.963  1.00 8.98  ? 250 GLN C C   1 
ATOM   6286 O  O   . GLN C 1 250 ? 21.109  6.076   38.833  1.00 8.62  ? 250 GLN C O   1 
ATOM   6287 C  CB  . GLN C 1 250 ? 21.180  9.133   40.179  1.00 8.77  ? 250 GLN C CB  1 
ATOM   6288 C  CG  . GLN C 1 250 ? 21.907  10.492  40.262  1.00 9.26  ? 250 GLN C CG  1 
ATOM   6289 C  CD  . GLN C 1 250 ? 22.631  10.590  41.621  1.00 10.15 ? 250 GLN C CD  1 
ATOM   6290 O  OE1 . GLN C 1 250 ? 21.995  10.716  42.684  1.00 9.99  ? 250 GLN C OE1 1 
ATOM   6291 N  NE2 . GLN C 1 250 ? 23.943  10.578  41.583  1.00 10.55 ? 250 GLN C NE2 1 
ATOM   6292 N  N   . LYS C 1 251 ? 20.620  6.125   41.049  1.00 9.26  ? 251 LYS C N   1 
ATOM   6293 C  CA  . LYS C 1 251 ? 19.607  5.048   40.952  1.00 10.30 ? 251 LYS C CA  1 
ATOM   6294 C  C   . LYS C 1 251 ? 18.453  5.561   40.077  1.00 10.65 ? 251 LYS C C   1 
ATOM   6295 O  O   . LYS C 1 251 ? 18.074  6.755   40.122  1.00 9.35  ? 251 LYS C O   1 
ATOM   6296 C  CB  . LYS C 1 251 ? 19.026  4.659   42.348  1.00 10.95 ? 251 LYS C CB  1 
ATOM   6297 C  CG  . LYS C 1 251 ? 19.917  3.811   43.261  1.00 11.86 ? 251 LYS C CG  1 
ATOM   6298 C  CD  . LYS C 1 251 ? 20.081  2.363   42.714  1.00 11.40 ? 251 LYS C CD  1 
ATOM   6299 C  CE  . LYS C 1 251 ? 20.742  1.450   43.746  1.00 10.58 ? 251 LYS C CE  1 
ATOM   6300 N  NZ  . LYS C 1 251 ? 22.065  2.054   44.127  1.00 10.13 ? 251 LYS C NZ  1 
ATOM   6301 N  N   . PHE C 1 252 ? 17.844  4.665   39.313  1.00 12.84 ? 252 PHE C N   1 
ATOM   6302 C  CA  . PHE C 1 252 ? 16.769  5.060   38.398  1.00 16.64 ? 252 PHE C CA  1 
ATOM   6303 C  C   . PHE C 1 252 ? 15.924  3.830   38.272  1.00 22.43 ? 252 PHE C C   1 
ATOM   6304 O  O   . PHE C 1 252 ? 16.181  2.991   37.392  1.00 25.00 ? 252 PHE C O   1 
ATOM   6305 C  CB  . PHE C 1 252 ? 17.311  5.281   37.002  1.00 17.87 ? 252 PHE C CB  1 
ATOM   6306 C  CG  . PHE C 1 252 ? 16.340  5.929   36.056  1.00 17.17 ? 252 PHE C CG  1 
ATOM   6307 C  CD1 . PHE C 1 252 ? 16.014  7.277   36.198  1.00 16.87 ? 252 PHE C CD1 1 
ATOM   6308 C  CD2 . PHE C 1 252 ? 15.743  5.191   35.043  1.00 17.48 ? 252 PHE C CD2 1 
ATOM   6309 C  CE1 . PHE C 1 252 ? 15.151  7.903   35.305  1.00 18.11 ? 252 PHE C CE1 1 
ATOM   6310 C  CE2 . PHE C 1 252 ? 14.867  5.800   34.153  1.00 18.75 ? 252 PHE C CE2 1 
ATOM   6311 C  CZ  . PHE C 1 252 ? 14.568  7.146   34.282  1.00 18.35 ? 252 PHE C CZ  1 
ATOM   6312 N  N   . ASP C 1 253 ? 14.966  3.710   39.176  1.00 24.56 ? 253 ASP C N   1 
ATOM   6313 C  CA  . ASP C 1 253 ? 14.142  2.489   39.344  1.00 31.70 ? 253 ASP C CA  1 
ATOM   6314 C  C   . ASP C 1 253 ? 12.673  2.837   39.158  1.00 30.26 ? 253 ASP C C   1 
ATOM   6315 O  O   . ASP C 1 253 ? 12.243  3.936   39.548  1.00 31.71 ? 253 ASP C O   1 
ATOM   6316 C  CB  . ASP C 1 253 ? 14.348  1.887   40.737  1.00 31.87 ? 253 ASP C CB  1 
ATOM   6317 C  CG  . ASP C 1 253 ? 15.774  1.381   40.962  1.00 36.23 ? 253 ASP C CG  1 
ATOM   6318 O  OD1 . ASP C 1 253 ? 16.205  0.474   40.208  1.00 46.43 ? 253 ASP C OD1 1 
ATOM   6319 O  OD2 . ASP C 1 253 ? 16.444  1.850   41.903  1.00 30.00 ? 253 ASP C OD2 1 
ATOM   6320 N  N   . GLU C 1 254 ? 11.953  1.862   38.587  1.00 35.38 ? 254 GLU C N   1 
ATOM   6321 C  CA  . GLU C 1 254 ? 10.568  1.913   38.072  1.00 31.95 ? 254 GLU C CA  1 
ATOM   6322 C  C   . GLU C 1 254 ? 10.467  2.710   36.744  1.00 33.15 ? 254 GLU C C   1 
ATOM   6323 O  O   . GLU C 1 254 ? 9.850   2.253   35.759  1.00 34.58 ? 254 GLU C O   1 
ATOM   6324 C  CB  . GLU C 1 254 ? 9.542   2.371   39.149  1.00 37.10 ? 254 GLU C CB  1 
ATOM   6325 C  CG  . GLU C 1 254 ? 9.018   3.799   39.019  0.01 35.42 ? 254 GLU C CG  1 
ATOM   6326 C  CD  . GLU C 1 254 ? 9.522   4.730   40.109  0.01 35.52 ? 254 GLU C CD  1 
ATOM   6327 O  OE1 . GLU C 1 254 ? 9.917   5.868   39.781  0.01 35.42 ? 254 GLU C OE1 1 
ATOM   6328 O  OE2 . GLU C 1 254 ? 9.525   4.328   41.293  0.01 35.64 ? 254 GLU C OE2 1 
ATOM   6329 N  N   A ARG C 1 255 ? 11.099  3.872   36.730  0.50 28.31 ? 255 ARG C N   1 
ATOM   6330 N  N   B ARG C 1 255 ? 11.126  3.868   36.754  0.50 29.98 ? 255 ARG C N   1 
ATOM   6331 C  CA  A ARG C 1 255 ? 10.983  4.835   35.640  0.50 26.78 ? 255 ARG C CA  1 
ATOM   6332 C  CA  B ARG C 1 255 ? 11.146  4.878   35.684  0.50 29.30 ? 255 ARG C CA  1 
ATOM   6333 C  C   A ARG C 1 255 ? 11.801  4.532   34.386  0.50 24.35 ? 255 ARG C C   1 
ATOM   6334 C  C   B ARG C 1 255 ? 11.760  4.455   34.352  0.50 26.12 ? 255 ARG C C   1 
ATOM   6335 O  O   A ARG C 1 255 ? 12.762  3.768   34.416  0.50 23.85 ? 255 ARG C O   1 
ATOM   6336 O  O   B ARG C 1 255 ? 12.548  3.515   34.290  0.50 26.22 ? 255 ARG C O   1 
ATOM   6337 C  CB  A ARG C 1 255 ? 11.415  6.185   36.150  0.50 23.05 ? 255 ARG C CB  1 
ATOM   6338 C  CB  B ARG C 1 255 ? 11.942  6.079   36.168  0.50 26.92 ? 255 ARG C CB  1 
ATOM   6339 C  CG  A ARG C 1 255 ? 11.035  6.459   37.583  0.50 21.41 ? 255 ARG C CG  1 
ATOM   6340 C  CG  B ARG C 1 255 ? 11.807  6.372   37.641  0.50 28.48 ? 255 ARG C CG  1 
ATOM   6341 C  CD  A ARG C 1 255 ? 11.842  7.683   37.960  0.50 18.40 ? 255 ARG C CD  1 
ATOM   6342 C  CD  B ARG C 1 255 ? 12.729  7.513   38.022  0.50 25.41 ? 255 ARG C CD  1 
ATOM   6343 N  NE  A ARG C 1 255 ? 11.655  8.663   36.904  0.50 16.57 ? 255 ARG C NE  1 
ATOM   6344 N  NE  B ARG C 1 255 ? 13.863  7.071   38.830  0.50 24.37 ? 255 ARG C NE  1 
ATOM   6345 C  CZ  A ARG C 1 255 ? 12.556  9.564   36.546  0.50 16.35 ? 255 ARG C CZ  1 
ATOM   6346 C  CZ  B ARG C 1 255 ? 14.512  7.873   39.664  0.50 23.70 ? 255 ARG C CZ  1 
ATOM   6347 N  NH1 A ARG C 1 255 ? 13.756  9.561   37.160  0.50 15.89 ? 255 ARG C NH1 1 
ATOM   6348 N  NH1 B ARG C 1 255 ? 14.143  9.130   39.769  0.50 23.77 ? 255 ARG C NH1 1 
ATOM   6349 N  NH2 A ARG C 1 255 ? 12.272  10.424  35.571  0.50 13.54 ? 255 ARG C NH2 1 
ATOM   6350 N  NH2 B ARG C 1 255 ? 15.512  7.428   40.404  0.50 24.85 ? 255 ARG C NH2 1 
ATOM   6351 N  N   . LEU C 1 256 ? 11.418  5.198   33.299  1.00 24.11 ? 256 LEU C N   1 
ATOM   6352 C  CA  . LEU C 1 256 ? 11.920  4.925   31.962  1.00 22.00 ? 256 LEU C CA  1 
ATOM   6353 C  C   . LEU C 1 256 ? 12.567  6.154   31.336  1.00 19.14 ? 256 LEU C C   1 
ATOM   6354 O  O   . LEU C 1 256 ? 12.323  7.274   31.708  1.00 17.60 ? 256 LEU C O   1 
ATOM   6355 C  CB  . LEU C 1 256 ? 10.776  4.442   31.017  1.00 23.08 ? 256 LEU C CB  1 
ATOM   6356 C  CG  . LEU C 1 256 ? 10.181  3.054   31.342  1.00 24.66 ? 256 LEU C CG  1 
ATOM   6357 C  CD1 . LEU C 1 256 ? 9.060   2.624   30.393  1.00 25.33 ? 256 LEU C CD1 1 
ATOM   6358 C  CD2 . LEU C 1 256 ? 11.243  1.970   31.450  1.00 27.02 ? 256 LEU C CD2 1 
ATOM   6359 N  N   . VAL C 1 257 ? 13.405  5.883   30.357  1.00 17.39 ? 257 VAL C N   1 
ATOM   6360 C  CA  . VAL C 1 257 ? 13.976  6.919   29.519  1.00 15.47 ? 257 VAL C CA  1 
ATOM   6361 C  C   . VAL C 1 257 ? 13.264  6.664   28.199  1.00 14.51 ? 257 VAL C C   1 
ATOM   6362 O  O   . VAL C 1 257 ? 13.130  5.499   27.734  1.00 13.09 ? 257 VAL C O   1 
ATOM   6363 C  CB  . VAL C 1 257 ? 15.476  6.673   29.386  1.00 15.87 ? 257 VAL C CB  1 
ATOM   6364 C  CG1 . VAL C 1 257 ? 16.116  7.615   28.352  1.00 15.57 ? 257 VAL C CG1 1 
ATOM   6365 C  CG2 . VAL C 1 257 ? 16.110  6.806   30.764  1.00 17.17 ? 257 VAL C CG2 1 
ATOM   6366 N  N   . TYR C 1 258 ? 12.758  7.746   27.614  1.00 13.82 ? 258 TYR C N   1 
ATOM   6367 C  CA  . TYR C 1 258 ? 12.012  7.625   26.346  1.00 14.31 ? 258 TYR C CA  1 
ATOM   6368 C  C   . TYR C 1 258 ? 12.973  7.910   25.175  1.00 13.40 ? 258 TYR C C   1 
ATOM   6369 O  O   . TYR C 1 258 ? 13.752  8.875   25.243  1.00 12.16 ? 258 TYR C O   1 
ATOM   6370 C  CB  . TYR C 1 258 ? 10.759  8.564   26.368  1.00 15.85 ? 258 TYR C CB  1 
ATOM   6371 C  CG  . TYR C 1 258 ? 9.868   8.121   27.513  1.00 18.82 ? 258 TYR C CG  1 
ATOM   6372 C  CD1 . TYR C 1 258 ? 9.988   8.694   28.783  1.00 21.30 ? 258 TYR C CD1 1 
ATOM   6373 C  CD2 . TYR C 1 258 ? 9.020   7.005   27.363  1.00 19.21 ? 258 TYR C CD2 1 
ATOM   6374 C  CE1 . TYR C 1 258 ? 9.220   8.209   29.843  1.00 23.18 ? 258 TYR C CE1 1 
ATOM   6375 C  CE2 . TYR C 1 258 ? 8.248   6.522   28.409  1.00 21.09 ? 258 TYR C CE2 1 
ATOM   6376 C  CZ  . TYR C 1 258 ? 8.370   7.104   29.645  1.00 24.39 ? 258 TYR C CZ  1 
ATOM   6377 O  OH  . TYR C 1 258 ? 7.621   6.604   30.696  1.00 27.89 ? 258 TYR C OH  1 
ATOM   6378 N  N   . THR C 1 259 ? 12.912  7.121   24.108  1.00 11.83 ? 259 THR C N   1 
ATOM   6379 C  CA  . THR C 1 259 ? 13.807  7.369   22.971  1.00 11.75 ? 259 THR C CA  1 
ATOM   6380 C  C   . THR C 1 259 ? 13.068  7.695   21.674  1.00 11.54 ? 259 THR C C   1 
ATOM   6381 O  O   . THR C 1 259 ? 12.050  7.096   21.416  1.00 10.60 ? 259 THR C O   1 
ATOM   6382 C  CB  . THR C 1 259 ? 14.756  6.177   22.696  1.00 12.88 ? 259 THR C CB  1 
ATOM   6383 O  OG1 . THR C 1 259 ? 13.965  4.986   22.500  1.00 14.20 ? 259 THR C OG1 1 
ATOM   6384 C  CG2 . THR C 1 259 ? 15.751  5.915   23.884  1.00 12.57 ? 259 THR C CG2 1 
ATOM   6385 N  N   . SER C 1 260 ? 13.626  8.599   20.864  1.00 12.57 ? 260 SER C N   1 
ATOM   6386 C  CA  . SER C 1 260 ? 13.077  8.934   19.492  1.00 13.72 ? 260 SER C CA  1 
ATOM   6387 C  C   . SER C 1 260 ? 13.553  7.992   18.361  1.00 15.78 ? 260 SER C C   1 
ATOM   6388 O  O   . SER C 1 260 ? 13.188  8.172   17.144  1.00 14.88 ? 260 SER C O   1 
ATOM   6389 C  CB  . SER C 1 260 ? 13.409  10.395  19.109  1.00 13.40 ? 260 SER C CB  1 
ATOM   6390 O  OG  . SER C 1 260 ? 14.817  10.571  19.031  1.00 12.39 ? 260 SER C OG  1 
ATOM   6391 N  N   . PHE C 1 261 ? 14.405  7.047   18.738  1.00 14.69 ? 261 PHE C N   1 
ATOM   6392 C  CA  . PHE C 1 261 ? 14.970  6.065   17.833  1.00 16.09 ? 261 PHE C CA  1 
ATOM   6393 C  C   . PHE C 1 261 ? 14.642  4.698   18.416  1.00 16.80 ? 261 PHE C C   1 
ATOM   6394 O  O   . PHE C 1 261 ? 14.422  4.607   19.615  1.00 15.58 ? 261 PHE C O   1 
ATOM   6395 C  CB  . PHE C 1 261 ? 16.479  6.278   17.689  1.00 14.74 ? 261 PHE C CB  1 
ATOM   6396 C  CG  . PHE C 1 261 ? 17.253  6.195   19.005  1.00 14.75 ? 261 PHE C CG  1 
ATOM   6397 C  CD1 . PHE C 1 261 ? 17.811  4.976   19.425  1.00 14.65 ? 261 PHE C CD1 1 
ATOM   6398 C  CD2 . PHE C 1 261 ? 17.447  7.328   19.785  1.00 15.22 ? 261 PHE C CD2 1 
ATOM   6399 C  CE1 . PHE C 1 261 ? 18.548  4.893   20.612  1.00 17.31 ? 261 PHE C CE1 1 
ATOM   6400 C  CE2 . PHE C 1 261 ? 18.180  7.247   21.006  1.00 15.09 ? 261 PHE C CE2 1 
ATOM   6401 C  CZ  . PHE C 1 261 ? 18.718  6.026   21.396  1.00 16.22 ? 261 PHE C CZ  1 
ATOM   6402 N  N   . SER C 1 262 ? 14.555  3.631   17.608  1.00 19.30 ? 262 SER C N   1 
ATOM   6403 C  CA  . SER C 1 262 ? 14.226  2.338   18.219  1.00 22.29 ? 262 SER C CA  1 
ATOM   6404 C  C   . SER C 1 262 ? 15.440  1.547   18.741  1.00 29.01 ? 262 SER C C   1 
ATOM   6405 O  O   . SER C 1 262 ? 15.611  1.391   19.959  1.00 32.35 ? 262 SER C O   1 
ATOM   6406 C  CB  . SER C 1 262 ? 13.288  1.455   17.361  1.00 23.95 ? 262 SER C CB  1 
ATOM   6407 O  OG  . SER C 1 262 ? 12.868  0.274   18.117  1.00 22.41 ? 262 SER C OG  1 
ATOM   6408 N  N   . GLN C 1 263 ? 16.286  1.031   17.881  1.00 30.84 ? 263 GLN C N   1 
ATOM   6409 C  CA  . GLN C 1 263 ? 17.488  0.302   18.431  1.00 35.00 ? 263 GLN C CA  1 
ATOM   6410 C  C   . GLN C 1 263 ? 17.243  -1.179  18.801  1.00 34.81 ? 263 GLN C C   1 
ATOM   6411 O  O   . GLN C 1 263 ? 16.364  -1.517  19.625  1.00 30.98 ? 263 GLN C O   1 
ATOM   6412 C  CB  . GLN C 1 263 ? 18.144  1.070   19.604  1.00 38.00 ? 263 GLN C CB  1 
ATOM   6413 C  CG  . GLN C 1 263 ? 19.450  0.488   20.160  1.00 38.71 ? 263 GLN C CG  1 
ATOM   6414 C  CD  . GLN C 1 263 ? 20.328  1.502   20.921  1.00 44.69 ? 263 GLN C CD  1 
ATOM   6415 O  OE1 . GLN C 1 263 ? 21.324  2.005   20.372  1.00 47.64 ? 263 GLN C OE1 1 
ATOM   6416 N  NE2 . GLN C 1 263 ? 19.989  1.781   22.196  1.00 35.18 ? 263 GLN C NE2 1 
ATOM   6417 N  N   . TRP D 1 4   ? 18.009  3.741   57.576  1.00 17.69 ? 4   TRP D N   1 
ATOM   6418 C  CA  . TRP D 1 4   ? 18.480  3.850   56.153  1.00 15.16 ? 4   TRP D CA  1 
ATOM   6419 C  C   . TRP D 1 4   ? 17.878  2.835   55.206  1.00 16.63 ? 4   TRP D C   1 
ATOM   6420 O  O   . TRP D 1 4   ? 17.476  1.720   55.635  1.00 16.40 ? 4   TRP D O   1 
ATOM   6421 C  CB  . TRP D 1 4   ? 20.018  3.787   56.108  1.00 15.59 ? 4   TRP D CB  1 
ATOM   6422 C  CG  . TRP D 1 4   ? 20.669  2.454   56.501  1.00 13.36 ? 4   TRP D CG  1 
ATOM   6423 C  CD1 . TRP D 1 4   ? 21.034  2.012   57.773  1.00 13.49 ? 4   TRP D CD1 1 
ATOM   6424 C  CD2 . TRP D 1 4   ? 21.025  1.381   55.608  1.00 13.23 ? 4   TRP D CD2 1 
ATOM   6425 N  NE1 . TRP D 1 4   ? 21.618  0.767   57.718  1.00 13.95 ? 4   TRP D NE1 1 
ATOM   6426 C  CE2 . TRP D 1 4   ? 21.617  0.326   56.424  1.00 12.78 ? 4   TRP D CE2 1 
ATOM   6427 C  CE3 . TRP D 1 4   ? 20.924  1.196   54.225  1.00 12.89 ? 4   TRP D CE3 1 
ATOM   6428 C  CZ2 . TRP D 1 4   ? 22.097  -0.857  55.873  1.00 12.30 ? 4   TRP D CZ2 1 
ATOM   6429 C  CZ3 . TRP D 1 4   ? 21.432  -0.013  53.677  1.00 12.57 ? 4   TRP D CZ3 1 
ATOM   6430 C  CH2 . TRP D 1 4   ? 21.999  -0.994  54.482  1.00 12.32 ? 4   TRP D CH2 1 
ATOM   6431 N  N   . THR D 1 5   ? 17.878  3.187   53.916  1.00 14.07 ? 5   THR D N   1 
ATOM   6432 C  CA  . THR D 1 5   ? 17.314  2.408   52.805  1.00 16.04 ? 5   THR D CA  1 
ATOM   6433 C  C   . THR D 1 5   ? 18.149  2.557   51.518  1.00 14.41 ? 5   THR D C   1 
ATOM   6434 O  O   . THR D 1 5   ? 19.131  3.342   51.462  1.00 15.21 ? 5   THR D O   1 
ATOM   6435 C  CB  . THR D 1 5   ? 15.860  2.847   52.474  1.00 16.13 ? 5   THR D CB  1 
ATOM   6436 O  OG1 . THR D 1 5   ? 15.883  4.018   51.638  1.00 18.60 ? 5   THR D OG1 1 
ATOM   6437 C  CG2 . THR D 1 5   ? 15.015  3.178   53.767  1.00 16.31 ? 5   THR D CG2 1 
ATOM   6438 N  N   . TYR D 1 6   ? 17.722  1.900   50.448  1.00 13.41 ? 6   TYR D N   1 
ATOM   6439 C  CA  . TYR D 1 6   ? 18.307  2.133   49.121  1.00 14.84 ? 6   TYR D CA  1 
ATOM   6440 C  C   . TYR D 1 6   ? 17.401  2.955   48.170  1.00 14.33 ? 6   TYR D C   1 
ATOM   6441 O  O   . TYR D 1 6   ? 17.660  3.031   46.971  1.00 12.72 ? 6   TYR D O   1 
ATOM   6442 C  CB  . TYR D 1 6   ? 18.609  0.811   48.451  1.00 13.91 ? 6   TYR D CB  1 
ATOM   6443 C  CG  . TYR D 1 6   ? 19.716  0.015   49.070  1.00 13.96 ? 6   TYR D CG  1 
ATOM   6444 C  CD1 . TYR D 1 6   ? 19.481  -0.851  50.155  1.00 15.10 ? 6   TYR D CD1 1 
ATOM   6445 C  CD2 . TYR D 1 6   ? 20.997  0.052   48.529  1.00 14.16 ? 6   TYR D CD2 1 
ATOM   6446 C  CE1 . TYR D 1 6   ? 20.511  -1.627  50.692  1.00 13.99 ? 6   TYR D CE1 1 
ATOM   6447 C  CE2 . TYR D 1 6   ? 22.045  -0.709  49.082  1.00 14.53 ? 6   TYR D CE2 1 
ATOM   6448 C  CZ  . TYR D 1 6   ? 21.796  -1.553  50.136  1.00 15.06 ? 6   TYR D CZ  1 
ATOM   6449 O  OH  . TYR D 1 6   ? 22.827  -2.302  50.633  1.00 13.92 ? 6   TYR D OH  1 
ATOM   6450 N  N   . PHE D 1 7   ? 16.324  3.517   48.692  1.00 18.07 ? 7   PHE D N   1 
ATOM   6451 C  CA  . PHE D 1 7   ? 15.291  4.132   47.824  1.00 21.22 ? 7   PHE D CA  1 
ATOM   6452 C  C   . PHE D 1 7   ? 14.725  5.330   48.521  1.00 22.63 ? 7   PHE D C   1 
ATOM   6453 O  O   . PHE D 1 7   ? 14.244  5.181   49.640  1.00 27.54 ? 7   PHE D O   1 
ATOM   6454 C  CB  . PHE D 1 7   ? 14.075  3.235   47.715  1.00 23.84 ? 7   PHE D CB  1 
ATOM   6455 C  CG  . PHE D 1 7   ? 14.262  1.964   46.941  1.00 27.22 ? 7   PHE D CG  1 
ATOM   6456 C  CD1 . PHE D 1 7   ? 14.049  1.931   45.553  1.00 27.83 ? 7   PHE D CD1 1 
ATOM   6457 C  CD2 . PHE D 1 7   ? 14.484  0.747   47.614  1.00 29.50 ? 7   PHE D CD2 1 
ATOM   6458 C  CE1 . PHE D 1 7   ? 14.159  0.730   44.836  1.00 22.81 ? 7   PHE D CE1 1 
ATOM   6459 C  CE2 . PHE D 1 7   ? 14.585  -0.440  46.918  1.00 24.22 ? 7   PHE D CE2 1 
ATOM   6460 C  CZ  . PHE D 1 7   ? 14.398  -0.439  45.535  1.00 26.65 ? 7   PHE D CZ  1 
ATOM   6461 N  N   . GLY D 1 8   ? 14.734  6.493   47.890  1.00 21.78 ? 8   GLY D N   1 
ATOM   6462 C  CA  . GLY D 1 8   ? 13.838  7.569   48.362  1.00 22.61 ? 8   GLY D CA  1 
ATOM   6463 C  C   . GLY D 1 8   ? 14.598  8.535   49.247  1.00 24.08 ? 8   GLY D C   1 
ATOM   6464 O  O   . GLY D 1 8   ? 15.839  8.651   49.135  1.00 25.38 ? 8   GLY D O   1 
ATOM   6465 N  N   . PRO D 1 9   ? 13.879  9.195   50.163  1.00 24.48 ? 9   PRO D N   1 
ATOM   6466 C  CA  . PRO D 1 9   ? 14.498  10.213  51.055  1.00 22.68 ? 9   PRO D CA  1 
ATOM   6467 C  C   . PRO D 1 9   ? 15.626  9.695   51.924  1.00 22.82 ? 9   PRO D C   1 
ATOM   6468 O  O   . PRO D 1 9   ? 16.532  10.471  52.235  1.00 17.28 ? 9   PRO D O   1 
ATOM   6469 C  CB  . PRO D 1 9   ? 13.323  10.699  51.933  1.00 23.35 ? 9   PRO D CB  1 
ATOM   6470 C  CG  . PRO D 1 9   ? 12.098  10.362  51.155  1.00 27.18 ? 9   PRO D CG  1 
ATOM   6471 C  CD  . PRO D 1 9   ? 12.408  9.134   50.326  1.00 23.94 ? 9   PRO D CD  1 
ATOM   6472 N  N   . ASP D 1 10  ? 15.593  8.401   52.308  1.00 20.22 ? 10  ASP D N   1 
ATOM   6473 C  CA  . ASP D 1 10  ? 16.580  7.928   53.266  1.00 20.29 ? 10  ASP D CA  1 
ATOM   6474 C  C   . ASP D 1 10  ? 17.593  7.019   52.545  1.00 17.49 ? 10  ASP D C   1 
ATOM   6475 O  O   . ASP D 1 10  ? 18.358  6.266   53.193  1.00 18.70 ? 10  ASP D O   1 
ATOM   6476 C  CB  . ASP D 1 10  ? 15.913  7.247   54.479  1.00 21.08 ? 10  ASP D CB  1 
ATOM   6477 C  CG  . ASP D 1 10  ? 15.121  8.225   55.351  1.00 25.22 ? 10  ASP D CG  1 
ATOM   6478 O  OD1 . ASP D 1 10  ? 15.574  9.358   55.598  1.00 23.47 ? 10  ASP D OD1 1 
ATOM   6479 O  OD2 . ASP D 1 10  ? 14.012  7.857   55.765  1.00 26.88 ? 10  ASP D OD2 1 
ATOM   6480 N  N   . GLY D 1 11  ? 17.602  7.132   51.210  1.00 16.33 ? 11  GLY D N   1 
ATOM   6481 C  CA  . GLY D 1 11  ? 18.570  6.438   50.331  1.00 13.27 ? 11  GLY D CA  1 
ATOM   6482 C  C   . GLY D 1 11  ? 20.016  6.853   50.371  1.00 12.60 ? 11  GLY D C   1 
ATOM   6483 O  O   . GLY D 1 11  ? 20.398  7.705   51.179  1.00 10.44 ? 11  GLY D O   1 
ATOM   6484 N  N   . GLU D 1 12  ? 20.851  6.274   49.478  1.00 10.48 ? 12  GLU D N   1 
ATOM   6485 C  CA  . GLU D 1 12  ? 22.301  6.333   49.691  1.00 9.93  ? 12  GLU D CA  1 
ATOM   6486 C  C   . GLU D 1 12  ? 22.929  7.727   49.688  1.00 9.36  ? 12  GLU D C   1 
ATOM   6487 O  O   . GLU D 1 12  ? 23.962  7.896   50.321  1.00 10.41 ? 12  GLU D O   1 
ATOM   6488 C  CB  . GLU D 1 12  ? 23.092  5.405   48.712  1.00 10.02 ? 12  GLU D CB  1 
ATOM   6489 C  CG  . GLU D 1 12  ? 23.072  5.887   47.243  1.00 9.96  ? 12  GLU D CG  1 
ATOM   6490 C  CD  . GLU D 1 12  ? 23.415  4.789   46.268  1.00 10.46 ? 12  GLU D CD  1 
ATOM   6491 O  OE1 . GLU D 1 12  ? 24.589  4.577   45.957  1.00 10.05 ? 12  GLU D OE1 1 
ATOM   6492 O  OE2 . GLU D 1 12  ? 22.463  4.077   45.791  1.00 12.81 ? 12  GLU D OE2 1 
ATOM   6493 N  N   . ASN D 1 13  ? 22.358  8.708   48.987  1.00 9.35  ? 13  ASN D N   1 
ATOM   6494 C  CA  . ASN D 1 13  ? 22.962  10.053  49.006  1.00 9.27  ? 13  ASN D CA  1 
ATOM   6495 C  C   . ASN D 1 13  ? 22.778  10.729  50.352  1.00 9.47  ? 13  ASN D C   1 
ATOM   6496 O  O   . ASN D 1 13  ? 23.503  11.736  50.649  1.00 10.25 ? 13  ASN D O   1 
ATOM   6497 C  CB  . ASN D 1 13  ? 22.393  10.972  47.935  1.00 9.38  ? 13  ASN D CB  1 
ATOM   6498 C  CG  . ASN D 1 13  ? 22.814  10.592  46.537  1.00 8.49  ? 13  ASN D CG  1 
ATOM   6499 O  OD1 . ASN D 1 13  ? 23.658  9.673   46.270  1.00 8.94  ? 13  ASN D OD1 1 
ATOM   6500 N  ND2 . ASN D 1 13  ? 22.184  11.260  45.609  1.00 8.76  ? 13  ASN D ND2 1 
ATOM   6501 N  N   . SER D 1 14  ? 21.856  10.209  51.177  1.00 9.86  ? 14  SER D N   1 
ATOM   6502 C  CA  . SER D 1 14  ? 21.606  10.795  52.519  1.00 10.26 ? 14  SER D CA  1 
ATOM   6503 C  C   . SER D 1 14  ? 22.276  10.010  53.644  1.00 10.52 ? 14  SER D C   1 
ATOM   6504 O  O   . SER D 1 14  ? 22.175  10.422  54.807  1.00 11.36 ? 14  SER D O   1 
ATOM   6505 C  CB  . SER D 1 14  ? 20.086  10.871  52.830  1.00 11.82 ? 14  SER D CB  1 
ATOM   6506 O  OG  . SER D 1 14  ? 19.459  11.790  51.909  1.00 10.40 ? 14  SER D OG  1 
ATOM   6507 N  N   . TRP D 1 15  ? 22.941  8.872   53.338  1.00 9.97  ? 15  TRP D N   1 
ATOM   6508 C  CA  . TRP D 1 15  ? 23.585  8.051   54.398  1.00 9.61  ? 15  TRP D CA  1 
ATOM   6509 C  C   . TRP D 1 15  ? 24.606  8.811   55.234  1.00 10.19 ? 15  TRP D C   1 
ATOM   6510 O  O   . TRP D 1 15  ? 24.722  8.603   56.483  1.00 9.83  ? 15  TRP D O   1 
ATOM   6511 C  CB  . TRP D 1 15  ? 24.305  6.819   53.825  1.00 10.08 ? 15  TRP D CB  1 
ATOM   6512 C  CG  . TRP D 1 15  ? 23.433  5.771   53.149  1.00 9.66  ? 15  TRP D CG  1 
ATOM   6513 C  CD1 . TRP D 1 15  ? 22.060  5.665   53.159  1.00 10.21 ? 15  TRP D CD1 1 
ATOM   6514 C  CD2 . TRP D 1 15  ? 23.910  4.588   52.494  1.00 9.54  ? 15  TRP D CD2 1 
ATOM   6515 N  NE1 . TRP D 1 15  ? 21.641  4.536   52.521  1.00 9.43  ? 15  TRP D NE1 1 
ATOM   6516 C  CE2 . TRP D 1 15  ? 22.711  3.861   52.050  1.00 9.82  ? 15  TRP D CE2 1 
ATOM   6517 C  CE3 . TRP D 1 15  ? 25.187  4.106   52.125  1.00 9.63  ? 15  TRP D CE3 1 
ATOM   6518 C  CZ2 . TRP D 1 15  ? 22.793  2.685   51.356  1.00 9.22  ? 15  TRP D CZ2 1 
ATOM   6519 C  CZ3 . TRP D 1 15  ? 25.263  2.904   51.400  1.00 9.70  ? 15  TRP D CZ3 1 
ATOM   6520 C  CH2 . TRP D 1 15  ? 24.095  2.215   51.011  1.00 9.68  ? 15  TRP D CH2 1 
ATOM   6521 N  N   . SER D 1 16  ? 25.321  9.711   54.586  1.00 9.95  ? 16  SER D N   1 
ATOM   6522 C  CA  . SER D 1 16  ? 26.336  10.516  55.350  1.00 10.09 ? 16  SER D CA  1 
ATOM   6523 C  C   . SER D 1 16  ? 25.826  11.424  56.461  1.00 10.53 ? 16  SER D C   1 
ATOM   6524 O  O   . SER D 1 16  ? 26.672  11.886  57.340  1.00 9.55  ? 16  SER D O   1 
ATOM   6525 C  CB  . SER D 1 16  ? 27.209  11.350  54.405  1.00 10.30 ? 16  SER D CB  1 
ATOM   6526 O  OG  . SER D 1 16  ? 26.422  12.316  53.762  1.00 10.16 ? 16  SER D OG  1 
ATOM   6527 N  N   . LYS D 1 17  ? 24.511  11.702  56.456  1.00 11.30 ? 17  LYS D N   1 
ATOM   6528 C  CA  . LYS D 1 17  ? 23.906  12.598  57.478  1.00 11.13 ? 17  LYS D CA  1 
ATOM   6529 C  C   . LYS D 1 17  ? 24.120  11.986  58.835  1.00 12.04 ? 17  LYS D C   1 
ATOM   6530 O  O   . LYS D 1 17  ? 24.698  12.648  59.729  1.00 11.31 ? 17  LYS D O   1 
ATOM   6531 C  CB  . LYS D 1 17  ? 22.423  12.882  57.254  1.00 11.73 ? 17  LYS D CB  1 
ATOM   6532 C  CG  . LYS D 1 17  ? 22.133  13.668  55.979  1.00 11.18 ? 17  LYS D CG  1 
ATOM   6533 C  CD  . LYS D 1 17  ? 20.639  13.568  55.623  1.00 12.12 ? 17  LYS D CD  1 
ATOM   6534 C  CE  . LYS D 1 17  ? 20.352  14.327  54.314  1.00 12.33 ? 17  LYS D CE  1 
ATOM   6535 N  NZ  . LYS D 1 17  ? 18.973  14.277  53.776  1.00 12.18 ? 17  LYS D NZ  1 
ATOM   6536 N  N   . LYS D 1 18  ? 23.767  10.702  58.970  1.00 12.23 ? 18  LYS D N   1 
ATOM   6537 C  CA  . LYS D 1 18  ? 23.885  9.963   60.233  1.00 13.99 ? 18  LYS D CA  1 
ATOM   6538 C  C   . LYS D 1 18  ? 25.124  9.051   60.371  1.00 14.66 ? 18  LYS D C   1 
ATOM   6539 O  O   . LYS D 1 18  ? 25.531  8.673   61.498  1.00 13.22 ? 18  LYS D O   1 
ATOM   6540 C  CB  . LYS D 1 18  ? 22.650  9.073   60.431  1.00 14.30 ? 18  LYS D CB  1 
ATOM   6541 C  CG  . LYS D 1 18  ? 22.530  8.611   61.874  1.00 16.27 ? 18  LYS D CG  1 
ATOM   6542 C  CD  . LYS D 1 18  ? 21.310  7.724   62.066  0.01 15.53 ? 18  LYS D CD  1 
ATOM   6543 C  CE  . LYS D 1 18  ? 21.180  7.263   63.508  0.01 15.61 ? 18  LYS D CE  1 
ATOM   6544 N  NZ  . LYS D 1 18  ? 19.970  6.418   63.707  0.01 15.61 ? 18  LYS D NZ  1 
ATOM   6545 N  N   . TYR D 1 19  ? 25.690  8.685   59.224  1.00 14.20 ? 19  TYR D N   1 
ATOM   6546 C  CA  . TYR D 1 19  ? 26.904  7.865   59.162  1.00 13.63 ? 19  TYR D CA  1 
ATOM   6547 C  C   . TYR D 1 19  ? 27.986  8.566   58.323  1.00 12.42 ? 19  TYR D C   1 
ATOM   6548 O  O   . TYR D 1 19  ? 28.082  8.309   57.106  1.00 10.87 ? 19  TYR D O   1 
ATOM   6549 C  CB  . TYR D 1 19  ? 26.556  6.522   58.508  1.00 13.39 ? 19  TYR D CB  1 
ATOM   6550 C  CG  . TYR D 1 19  ? 25.414  5.766   59.227  1.00 15.32 ? 19  TYR D CG  1 
ATOM   6551 C  CD1 . TYR D 1 19  ? 24.079  5.866   58.771  1.00 15.37 ? 19  TYR D CD1 1 
ATOM   6552 C  CD2 . TYR D 1 19  ? 25.667  5.000   60.370  1.00 16.08 ? 19  TYR D CD2 1 
ATOM   6553 C  CE1 . TYR D 1 19  ? 23.079  5.188   59.401  1.00 16.51 ? 19  TYR D CE1 1 
ATOM   6554 C  CE2 . TYR D 1 19  ? 24.645  4.296   61.009  1.00 17.13 ? 19  TYR D CE2 1 
ATOM   6555 C  CZ  . TYR D 1 19  ? 23.374  4.387   60.513  1.00 17.47 ? 19  TYR D CZ  1 
ATOM   6556 O  OH  . TYR D 1 19  ? 22.321  3.732   61.099  1.00 19.46 ? 19  TYR D OH  1 
ATOM   6557 N  N   . PRO D 1 20  ? 28.817  9.439   58.956  1.00 10.71 ? 20  PRO D N   1 
ATOM   6558 C  CA  . PRO D 1 20  ? 29.669  10.356  58.236  1.00 10.66 ? 20  PRO D CA  1 
ATOM   6559 C  C   . PRO D 1 20  ? 30.706  9.616   57.362  1.00 9.55  ? 20  PRO D C   1 
ATOM   6560 O  O   . PRO D 1 20  ? 31.093  10.164  56.361  1.00 11.10 ? 20  PRO D O   1 
ATOM   6561 C  CB  . PRO D 1 20  ? 30.369  11.166  59.343  1.00 10.32 ? 20  PRO D CB  1 
ATOM   6562 C  CG  . PRO D 1 20  ? 29.319  11.179  60.434  1.00 11.71 ? 20  PRO D CG  1 
ATOM   6563 C  CD  . PRO D 1 20  ? 28.698  9.794   60.388  1.00 11.75 ? 20  PRO D CD  1 
ATOM   6564 N  N   . SER D 1 21  ? 31.050  8.350   57.677  1.00 9.58  ? 21  SER D N   1 
ATOM   6565 C  CA  . SER D 1 21  ? 32.073  7.647   56.893  1.00 8.56  ? 21  SER D CA  1 
ATOM   6566 C  C   . SER D 1 21  ? 31.551  7.326   55.518  1.00 8.61  ? 21  SER D C   1 
ATOM   6567 O  O   . SER D 1 21  ? 32.323  7.084   54.581  1.00 8.04  ? 21  SER D O   1 
ATOM   6568 C  CB  . SER D 1 21  ? 32.660  6.454   57.613  1.00 9.01  ? 21  SER D CB  1 
ATOM   6569 O  OG  . SER D 1 21  ? 33.413  6.866   58.816  1.00 9.61  ? 21  SER D OG  1 
ATOM   6570 N  N   . CYS D 1 22  ? 30.230  7.357   55.383  1.00 8.98  ? 22  CYS D N   1 
ATOM   6571 C  CA  . CYS D 1 22  ? 29.634  7.173   54.058  1.00 8.52  ? 22  CYS D CA  1 
ATOM   6572 C  C   . CYS D 1 22  ? 29.991  8.282   53.062  1.00 9.47  ? 22  CYS D C   1 
ATOM   6573 O  O   . CYS D 1 22  ? 29.859  8.105   51.809  1.00 8.83  ? 22  CYS D O   1 
ATOM   6574 C  CB  . CYS D 1 22  ? 28.117  6.917   54.200  1.00 9.94  ? 22  CYS D CB  1 
ATOM   6575 S  SG  . CYS D 1 22  ? 27.668  5.372   55.059  1.00 9.76  ? 22  CYS D SG  1 
ATOM   6576 N  N   . GLY D 1 23  ? 30.424  9.441   53.608  1.00 9.69  ? 23  GLY D N   1 
ATOM   6577 C  CA  . GLY D 1 23  ? 30.933  10.538  52.785  1.00 9.81  ? 23  GLY D CA  1 
ATOM   6578 C  C   . GLY D 1 23  ? 32.451  10.721  52.913  1.00 10.57 ? 23  GLY D C   1 
ATOM   6579 O  O   . GLY D 1 23  ? 32.992  11.783  52.507  1.00 11.91 ? 23  GLY D O   1 
ATOM   6580 N  N   . GLY D 1 24  ? 33.138  9.694   53.430  1.00 10.58 ? 24  GLY D N   1 
ATOM   6581 C  CA  . GLY D 1 24  ? 34.567  9.799   53.769  1.00 10.50 ? 24  GLY D CA  1 
ATOM   6582 C  C   . GLY D 1 24  ? 35.426  9.108   52.733  1.00 10.90 ? 24  GLY D C   1 
ATOM   6583 O  O   . GLY D 1 24  ? 35.023  8.950   51.568  1.00 11.97 ? 24  GLY D O   1 
ATOM   6584 N  N   . LEU D 1 25  ? 36.611  8.666   53.164  1.00 11.66 ? 25  LEU D N   1 
ATOM   6585 C  CA  . LEU D 1 25  ? 37.623  8.097   52.326  1.00 11.55 ? 25  LEU D CA  1 
ATOM   6586 C  C   . LEU D 1 25  ? 37.378  6.646   51.965  1.00 12.16 ? 25  LEU D C   1 
ATOM   6587 O  O   . LEU D 1 25  ? 36.635  5.984   52.656  1.00 10.95 ? 25  LEU D O   1 
ATOM   6588 C  CB  . LEU D 1 25  ? 38.952  8.174   53.084  1.00 12.76 ? 25  LEU D CB  1 
ATOM   6589 C  CG  . LEU D 1 25  ? 39.463  9.575   53.340  1.00 14.32 ? 25  LEU D CG  1 
ATOM   6590 C  CD1 . LEU D 1 25  ? 40.400  9.560   54.586  1.00 14.85 ? 25  LEU D CD1 1 
ATOM   6591 C  CD2 . LEU D 1 25  ? 40.120  10.081  52.071  1.00 15.82 ? 25  LEU D CD2 1 
ATOM   6592 N  N   . LEU D 1 26  ? 38.112  6.152   50.944  1.00 10.25 ? 26  LEU D N   1 
ATOM   6593 C  CA  . LEU D 1 26  ? 38.177  4.729   50.618  1.00 11.13 ? 26  LEU D CA  1 
ATOM   6594 C  C   . LEU D 1 26  ? 36.834  4.030   50.360  1.00 10.56 ? 26  LEU D C   1 
ATOM   6595 O  O   . LEU D 1 26  ? 36.661  2.858   50.751  1.00 10.91 ? 26  LEU D O   1 
ATOM   6596 C  CB  . LEU D 1 26  ? 39.011  3.897   51.631  1.00 12.23 ? 26  LEU D CB  1 
ATOM   6597 C  CG  . LEU D 1 26  ? 40.492  4.319   51.808  1.00 12.69 ? 26  LEU D CG  1 
ATOM   6598 C  CD1 . LEU D 1 26  ? 41.190  3.504   52.885  1.00 13.32 ? 26  LEU D CD1 1 
ATOM   6599 C  CD2 . LEU D 1 26  ? 41.258  4.228   50.498  1.00 14.05 ? 26  LEU D CD2 1 
ATOM   6600 N  N   . GLN D 1 27  ? 35.878  4.724   49.743  1.00 10.90 ? 27  GLN D N   1 
ATOM   6601 C  CA  . GLN D 1 27  ? 34.516  4.098   49.614  1.00 9.72  ? 27  GLN D CA  1 
ATOM   6602 C  C   . GLN D 1 27  ? 34.412  3.070   48.517  1.00 9.87  ? 27  GLN D C   1 
ATOM   6603 O  O   . GLN D 1 27  ? 35.019  3.227   47.475  1.00 10.85 ? 27  GLN D O   1 
ATOM   6604 C  CB  . GLN D 1 27  ? 33.450  5.179   49.465  1.00 9.92  ? 27  GLN D CB  1 
ATOM   6605 C  CG  . GLN D 1 27  ? 33.239  6.069   50.708  1.00 9.50  ? 27  GLN D CG  1 
ATOM   6606 C  CD  . GLN D 1 27  ? 32.780  5.255   51.881  1.00 9.61  ? 27  GLN D CD  1 
ATOM   6607 O  OE1 . GLN D 1 27  ? 31.604  4.863   51.974  1.00 9.65  ? 27  GLN D OE1 1 
ATOM   6608 N  NE2 . GLN D 1 27  ? 33.728  4.967   52.827  1.00 9.77  ? 27  GLN D NE2 1 
ATOM   6609 N  N   . SER D 1 28  ? 33.611  2.024   48.789  1.00 9.79  ? 28  SER D N   1 
ATOM   6610 C  CA  . SER D 1 28  ? 33.277  0.921   47.885  1.00 8.87  ? 28  SER D CA  1 
ATOM   6611 C  C   . SER D 1 28  ? 31.781  0.942   47.573  1.00 8.46  ? 28  SER D C   1 
ATOM   6612 O  O   . SER D 1 28  ? 30.973  1.402   48.335  1.00 8.17  ? 28  SER D O   1 
ATOM   6613 C  CB  . SER D 1 28  ? 33.631  -0.436  48.543  1.00 8.44  ? 28  SER D CB  1 
ATOM   6614 O  OG  . SER D 1 28  ? 35.029  -0.494  48.867  1.00 8.86  ? 28  SER D OG  1 
ATOM   6615 N  N   . PRO D 1 29  ? 31.373  0.301   46.468  1.00 8.83  ? 29  PRO D N   1 
ATOM   6616 C  CA  . PRO D 1 29  ? 32.061  -0.467  45.494  1.00 9.21  ? 29  PRO D CA  1 
ATOM   6617 C  C   . PRO D 1 29  ? 32.623  0.447   44.365  1.00 10.09 ? 29  PRO D C   1 
ATOM   6618 O  O   . PRO D 1 29  ? 32.426  1.643   44.444  1.00 10.60 ? 29  PRO D O   1 
ATOM   6619 C  CB  . PRO D 1 29  ? 30.937  -1.328  44.950  1.00 8.77  ? 29  PRO D CB  1 
ATOM   6620 C  CG  . PRO D 1 29  ? 29.785  -0.321  44.891  1.00 8.69  ? 29  PRO D CG  1 
ATOM   6621 C  CD  . PRO D 1 29  ? 29.912  0.294   46.260  1.00 8.65  ? 29  PRO D CD  1 
ATOM   6622 N  N   . ILE D 1 30  ? 33.311  -0.124  43.373  1.00 10.51 ? 30  ILE D N   1 
ATOM   6623 C  CA  . ILE D 1 30  ? 33.945  0.684   42.329  1.00 10.81 ? 30  ILE D CA  1 
ATOM   6624 C  C   . ILE D 1 30  ? 33.757  0.009   40.991  1.00 11.34 ? 30  ILE D C   1 
ATOM   6625 O  O   . ILE D 1 30  ? 33.377  -1.185  40.943  1.00 11.28 ? 30  ILE D O   1 
ATOM   6626 C  CB  . ILE D 1 30  ? 35.428  0.899   42.606  1.00 11.77 ? 30  ILE D CB  1 
ATOM   6627 C  CG1 . ILE D 1 30  ? 36.134  -0.488  42.667  1.00 11.71 ? 30  ILE D CG1 1 
ATOM   6628 C  CG2 . ILE D 1 30  ? 35.616  1.711   43.901  1.00 11.85 ? 30  ILE D CG2 1 
ATOM   6629 C  CD1 . ILE D 1 30  ? 37.643  -0.375  42.838  1.00 11.99 ? 30  ILE D CD1 1 
ATOM   6630 N  N   . ASP D 1 31  ? 34.021  0.773   39.927  1.00 11.18 ? 31  ASP D N   1 
ATOM   6631 C  CA  . ASP D 1 31  ? 34.117  0.181   38.595  1.00 12.24 ? 31  ASP D CA  1 
ATOM   6632 C  C   . ASP D 1 31  ? 35.551  -0.306  38.363  1.00 12.85 ? 31  ASP D C   1 
ATOM   6633 O  O   . ASP D 1 31  ? 36.529  0.462   38.513  1.00 11.77 ? 31  ASP D O   1 
ATOM   6634 C  CB  . ASP D 1 31  ? 33.729  1.173   37.503  1.00 13.25 ? 31  ASP D CB  1 
ATOM   6635 C  CG  . ASP D 1 31  ? 33.857  0.565   36.098  1.00 13.48 ? 31  ASP D CG  1 
ATOM   6636 O  OD1 . ASP D 1 31  ? 33.432  -0.587  35.876  1.00 14.82 ? 31  ASP D OD1 1 
ATOM   6637 O  OD2 . ASP D 1 31  ? 34.368  1.223   35.200  1.00 14.77 ? 31  ASP D OD2 1 
ATOM   6638 N  N   . LEU D 1 32  ? 35.672  -1.603  38.104  1.00 11.54 ? 32  LEU D N   1 
ATOM   6639 C  CA  . LEU D 1 32  ? 36.967  -2.258  37.765  1.00 13.76 ? 32  LEU D CA  1 
ATOM   6640 C  C   . LEU D 1 32  ? 37.221  -2.169  36.261  1.00 15.17 ? 32  LEU D C   1 
ATOM   6641 O  O   . LEU D 1 32  ? 36.556  -2.892  35.465  1.00 15.30 ? 32  LEU D O   1 
ATOM   6642 C  CB  . LEU D 1 32  ? 36.962  -3.742  38.214  1.00 12.71 ? 32  LEU D CB  1 
ATOM   6643 C  CG  . LEU D 1 32  ? 36.550  -3.919  39.686  1.00 12.01 ? 32  LEU D CG  1 
ATOM   6644 C  CD1 . LEU D 1 32  ? 36.192  -5.373  40.048  1.00 12.70 ? 32  LEU D CD1 1 
ATOM   6645 C  CD2 . LEU D 1 32  ? 37.648  -3.405  40.618  1.00 11.21 ? 32  LEU D CD2 1 
ATOM   6646 N  N   . HIS D 1 33  ? 38.097  -1.215  35.902  1.00 15.58 ? 33  HIS D N   1 
ATOM   6647 C  CA  . HIS D 1 33  ? 38.419  -0.839  34.517  1.00 15.89 ? 33  HIS D CA  1 
ATOM   6648 C  C   . HIS D 1 33  ? 39.886  -0.513  34.293  1.00 17.16 ? 33  HIS D C   1 
ATOM   6649 O  O   . HIS D 1 33  ? 40.566  -0.048  35.226  1.00 14.80 ? 33  HIS D O   1 
ATOM   6650 C  CB  . HIS D 1 33  ? 37.520  0.289   34.029  1.00 16.98 ? 33  HIS D CB  1 
ATOM   6651 C  CG  . HIS D 1 33  ? 37.795  1.659   34.670  1.00 17.75 ? 33  HIS D CG  1 
ATOM   6652 N  ND1 . HIS D 1 33  ? 37.437  1.951   35.934  1.00 17.89 ? 33  HIS D ND1 1 
ATOM   6653 C  CD2 . HIS D 1 33  ? 38.380  2.825   34.152  1.00 19.12 ? 33  HIS D CD2 1 
ATOM   6654 C  CE1 . HIS D 1 33  ? 37.808  3.234   36.236  1.00 20.03 ? 33  HIS D CE1 1 
ATOM   6655 N  NE2 . HIS D 1 33  ? 38.346  3.782   35.146  1.00 18.98 ? 33  HIS D NE2 1 
ATOM   6656 N  N   . SER D 1 34  ? 40.333  -0.650  33.034  1.00 18.27 ? 34  SER D N   1 
ATOM   6657 C  CA  . SER D 1 34  ? 41.761  -0.627  32.696  1.00 21.48 ? 34  SER D CA  1 
ATOM   6658 C  C   . SER D 1 34  ? 42.530  0.528   33.299  1.00 22.31 ? 34  SER D C   1 
ATOM   6659 O  O   . SER D 1 34  ? 43.634  0.318   33.819  1.00 21.75 ? 34  SER D O   1 
ATOM   6660 C  CB  . SER D 1 34  ? 41.975  -0.633  31.162  1.00 23.82 ? 34  SER D CB  1 
ATOM   6661 O  OG  . SER D 1 34  ? 41.437  0.576   30.659  1.00 25.04 ? 34  SER D OG  1 
ATOM   6662 N  N   . ASP D 1 35  ? 41.974  1.754   33.266  1.00 23.49 ? 35  ASP D N   1 
ATOM   6663 C  CA  . ASP D 1 35  ? 42.767  2.923   33.728  1.00 22.13 ? 35  ASP D CA  1 
ATOM   6664 C  C   . ASP D 1 35  ? 43.219  2.854   35.189  1.00 22.64 ? 35  ASP D C   1 
ATOM   6665 O  O   . ASP D 1 35  ? 44.153  3.579   35.558  1.00 19.23 ? 35  ASP D O   1 
ATOM   6666 C  CB  . ASP D 1 35  ? 42.060  4.290   33.508  1.00 23.93 ? 35  ASP D CB  1 
ATOM   6667 C  CG  . ASP D 1 35  ? 41.502  4.450   32.107  1.00 27.76 ? 35  ASP D CG  1 
ATOM   6668 O  OD1 . ASP D 1 35  ? 41.904  5.413   31.420  1.00 29.30 ? 35  ASP D OD1 1 
ATOM   6669 O  OD2 . ASP D 1 35  ? 40.641  3.620   31.685  1.00 30.43 ? 35  ASP D OD2 1 
ATOM   6670 N  N   . ILE D 1 36  ? 42.551  2.034   36.018  1.00 20.70 ? 36  ILE D N   1 
ATOM   6671 C  CA  . ILE D 1 36  ? 42.904  1.926   37.448  1.00 20.09 ? 36  ILE D CA  1 
ATOM   6672 C  C   . ILE D 1 36  ? 43.528  0.546   37.853  1.00 21.72 ? 36  ILE D C   1 
ATOM   6673 O  O   . ILE D 1 36  ? 43.793  0.337   39.039  1.00 22.45 ? 36  ILE D O   1 
ATOM   6674 C  CB  . ILE D 1 36  ? 41.739  2.267   38.405  1.00 21.23 ? 36  ILE D CB  1 
ATOM   6675 C  CG1 . ILE D 1 36  ? 40.594  1.200   38.298  1.00 20.41 ? 36  ILE D CG1 1 
ATOM   6676 C  CG2 . ILE D 1 36  ? 41.279  3.708   38.205  1.00 22.13 ? 36  ILE D CG2 1 
ATOM   6677 C  CD1 . ILE D 1 36  ? 39.429  1.333   39.290  1.00 23.97 ? 36  ILE D CD1 1 
ATOM   6678 N  N   . LEU D 1 37  ? 43.778  -0.346  36.885  1.00 20.28 ? 37  LEU D N   1 
ATOM   6679 C  CA  . LEU D 1 37  ? 44.274  -1.705  37.164  1.00 20.44 ? 37  LEU D CA  1 
ATOM   6680 C  C   . LEU D 1 37  ? 45.811  -1.823  36.981  1.00 21.94 ? 37  LEU D C   1 
ATOM   6681 O  O   . LEU D 1 37  ? 46.381  -1.324  35.988  1.00 22.23 ? 37  LEU D O   1 
ATOM   6682 C  CB  . LEU D 1 37  ? 43.585  -2.764  36.285  1.00 20.93 ? 37  LEU D CB  1 
ATOM   6683 C  CG  . LEU D 1 37  ? 42.063  -3.027  36.288  1.00 21.14 ? 37  LEU D CG  1 
ATOM   6684 C  CD1 . LEU D 1 37  ? 41.687  -4.092  35.265  1.00 20.94 ? 37  LEU D CD1 1 
ATOM   6685 C  CD2 . LEU D 1 37  ? 41.602  -3.440  37.689  1.00 17.88 ? 37  LEU D CD2 1 
ATOM   6686 N  N   . GLN D 1 38  ? 46.463  -2.507  37.917  1.00 19.59 ? 38  GLN D N   1 
ATOM   6687 C  CA  . GLN D 1 38  ? 47.870  -2.792  37.794  1.00 18.67 ? 38  GLN D CA  1 
ATOM   6688 C  C   . GLN D 1 38  ? 48.173  -4.193  38.287  1.00 16.98 ? 38  GLN D C   1 
ATOM   6689 O  O   . GLN D 1 38  ? 47.812  -4.532  39.433  1.00 15.01 ? 38  GLN D O   1 
ATOM   6690 C  CB  . GLN D 1 38  ? 48.614  -1.769  38.640  1.00 19.13 ? 38  GLN D CB  1 
ATOM   6691 C  CG  . GLN D 1 38  ? 50.105  -1.960  38.724  1.00 24.24 ? 38  GLN D CG  1 
ATOM   6692 C  CD  . GLN D 1 38  ? 50.766  -0.753  39.346  1.00 27.08 ? 38  GLN D CD  1 
ATOM   6693 O  OE1 . GLN D 1 38  ? 51.272  -0.800  40.466  1.00 29.18 ? 38  GLN D OE1 1 
ATOM   6694 N  NE2 . GLN D 1 38  ? 50.734  0.361   38.620  1.00 30.31 ? 38  GLN D NE2 1 
ATOM   6695 N  N   . TYR D 1 39  ? 48.876  -4.976  37.462  1.00 15.70 ? 39  TYR D N   1 
ATOM   6696 C  CA  . TYR D 1 39  ? 49.300  -6.344  37.839  1.00 15.40 ? 39  TYR D CA  1 
ATOM   6697 C  C   . TYR D 1 39  ? 50.274  -6.283  39.000  1.00 16.68 ? 39  TYR D C   1 
ATOM   6698 O  O   . TYR D 1 39  ? 51.189  -5.446  38.988  1.00 15.91 ? 39  TYR D O   1 
ATOM   6699 C  CB  . TYR D 1 39  ? 49.917  -7.042  36.626  1.00 16.55 ? 39  TYR D CB  1 
ATOM   6700 C  CG  . TYR D 1 39  ? 50.541  -8.406  36.956  1.00 15.56 ? 39  TYR D CG  1 
ATOM   6701 C  CD1 . TYR D 1 39  ? 49.818  -9.406  37.600  1.00 17.11 ? 39  TYR D CD1 1 
ATOM   6702 C  CD2 . TYR D 1 39  ? 51.830  -8.679  36.590  1.00 16.66 ? 39  TYR D CD2 1 
ATOM   6703 C  CE1 . TYR D 1 39  ? 50.392  -10.631 37.886  1.00 15.40 ? 39  TYR D CE1 1 
ATOM   6704 C  CE2 . TYR D 1 39  ? 52.421  -9.890  36.876  1.00 15.34 ? 39  TYR D CE2 1 
ATOM   6705 C  CZ  . TYR D 1 39  ? 51.700  -10.854 37.529  1.00 14.88 ? 39  TYR D CZ  1 
ATOM   6706 O  OH  . TYR D 1 39  ? 52.347  -12.046 37.802  1.00 15.00 ? 39  TYR D OH  1 
ATOM   6707 N  N   . ASP D 1 40  ? 50.043  -7.113  40.031  1.00 15.99 ? 40  ASP D N   1 
ATOM   6708 C  CA  . ASP D 1 40  ? 50.965  -7.177  41.184  1.00 16.32 ? 40  ASP D CA  1 
ATOM   6709 C  C   . ASP D 1 40  ? 51.394  -8.651  41.310  1.00 17.02 ? 40  ASP D C   1 
ATOM   6710 O  O   . ASP D 1 40  ? 50.594  -9.504  41.696  1.00 15.98 ? 40  ASP D O   1 
ATOM   6711 C  CB  . ASP D 1 40  ? 50.347  -6.577  42.460  1.00 15.91 ? 40  ASP D CB  1 
ATOM   6712 C  CG  . ASP D 1 40  ? 51.290  -6.671  43.674  1.00 18.69 ? 40  ASP D CG  1 
ATOM   6713 O  OD1 . ASP D 1 40  ? 50.952  -6.139  44.743  1.00 19.05 ? 40  ASP D OD1 1 
ATOM   6714 O  OD2 . ASP D 1 40  ? 52.309  -7.360  43.563  1.00 17.03 ? 40  ASP D OD2 1 
ATOM   6715 N  N   . ALA D 1 41  ? 52.620  -8.932  40.855  1.00 15.26 ? 41  ALA D N   1 
ATOM   6716 C  CA  . ALA D 1 41  ? 53.179  -10.274 40.872  1.00 15.41 ? 41  ALA D CA  1 
ATOM   6717 C  C   . ALA D 1 41  ? 53.319  -10.900 42.280  1.00 15.23 ? 41  ALA D C   1 
ATOM   6718 O  O   . ALA D 1 41  ? 53.501  -12.119 42.352  1.00 14.61 ? 41  ALA D O   1 
ATOM   6719 C  CB  . ALA D 1 41  ? 54.523  -10.329 40.102  1.00 16.44 ? 41  ALA D CB  1 
ATOM   6720 N  N   . SER D 1 42  ? 53.214  -10.102 43.360  1.00 15.33 ? 42  SER D N   1 
ATOM   6721 C  CA  . SER D 1 42  ? 53.403  -10.599 44.755  1.00 16.95 ? 42  SER D CA  1 
ATOM   6722 C  C   . SER D 1 42  ? 52.082  -11.116 45.395  1.00 17.80 ? 42  SER D C   1 
ATOM   6723 O  O   . SER D 1 42  ? 52.094  -11.680 46.499  1.00 18.06 ? 42  SER D O   1 
ATOM   6724 C  CB  . SER D 1 42  ? 54.029  -9.532  45.681  1.00 19.58 ? 42  SER D CB  1 
ATOM   6725 O  OG  . SER D 1 42  ? 55.329  -9.129  45.235  1.00 19.76 ? 42  SER D OG  1 
ATOM   6726 N  N   . LEU D 1 43  ? 50.958  -10.902 44.704  1.00 17.46 ? 43  LEU D N   1 
ATOM   6727 C  CA  . LEU D 1 43  ? 49.652  -11.407 45.173  1.00 16.89 ? 43  LEU D CA  1 
ATOM   6728 C  C   . LEU D 1 43  ? 49.657  -12.922 45.088  1.00 18.37 ? 43  LEU D C   1 
ATOM   6729 O  O   . LEU D 1 43  ? 50.017  -13.473 44.049  1.00 21.57 ? 43  LEU D O   1 
ATOM   6730 C  CB  . LEU D 1 43  ? 48.547  -10.844 44.307  1.00 15.04 ? 43  LEU D CB  1 
ATOM   6731 C  CG  . LEU D 1 43  ? 48.309  -9.329  44.509  1.00 13.79 ? 43  LEU D CG  1 
ATOM   6732 C  CD1 . LEU D 1 43  ? 47.229  -8.857  43.520  1.00 12.83 ? 43  LEU D CD1 1 
ATOM   6733 C  CD2 . LEU D 1 43  ? 47.859  -9.058  45.925  1.00 13.87 ? 43  LEU D CD2 1 
ATOM   6734 N  N   . THR D 1 44  ? 49.333  -13.599 46.190  1.00 18.62 ? 44  THR D N   1 
ATOM   6735 C  CA  . THR D 1 44  ? 49.323  -15.096 46.171  1.00 18.53 ? 44  THR D CA  1 
ATOM   6736 C  C   . THR D 1 44  ? 47.905  -15.678 46.247  1.00 17.02 ? 44  THR D C   1 
ATOM   6737 O  O   . THR D 1 44  ? 46.971  -14.981 46.593  1.00 17.02 ? 44  THR D O   1 
ATOM   6738 C  CB  . THR D 1 44  ? 50.097  -15.661 47.381  1.00 20.90 ? 44  THR D CB  1 
ATOM   6739 O  OG1 . THR D 1 44  ? 49.587  -15.097 48.598  1.00 19.69 ? 44  THR D OG1 1 
ATOM   6740 C  CG2 . THR D 1 44  ? 51.619  -15.437 47.254  1.00 23.04 ? 44  THR D CG2 1 
ATOM   6741 N  N   . PRO D 1 45  ? 47.731  -16.952 45.945  1.00 16.09 ? 45  PRO D N   1 
ATOM   6742 C  CA  . PRO D 1 45  ? 46.339  -17.373 46.024  1.00 17.24 ? 45  PRO D CA  1 
ATOM   6743 C  C   . PRO D 1 45  ? 45.866  -17.565 47.478  1.00 18.26 ? 45  PRO D C   1 
ATOM   6744 O  O   . PRO D 1 45  ? 46.655  -18.028 48.334  1.00 16.31 ? 45  PRO D O   1 
ATOM   6745 C  CB  . PRO D 1 45  ? 46.317  -18.697 45.272  1.00 17.71 ? 45  PRO D CB  1 
ATOM   6746 C  CG  . PRO D 1 45  ? 47.628  -18.811 44.529  1.00 19.01 ? 45  PRO D CG  1 
ATOM   6747 C  CD  . PRO D 1 45  ? 48.603  -17.898 45.235  1.00 17.91 ? 45  PRO D CD  1 
ATOM   6748 N  N   . LEU D 1 46  ? 44.607  -17.192 47.764  1.00 14.85 ? 46  LEU D N   1 
ATOM   6749 C  CA  . LEU D 1 46  ? 44.058  -17.425 49.091  1.00 15.20 ? 46  LEU D CA  1 
ATOM   6750 C  C   . LEU D 1 46  ? 43.851  -18.930 49.328  1.00 15.11 ? 46  LEU D C   1 
ATOM   6751 O  O   . LEU D 1 46  ? 43.634  -19.690 48.400  1.00 14.79 ? 46  LEU D O   1 
ATOM   6752 C  CB  . LEU D 1 46  ? 42.780  -16.622 49.335  1.00 15.42 ? 46  LEU D CB  1 
ATOM   6753 C  CG  . LEU D 1 46  ? 42.993  -15.128 49.262  1.00 15.35 ? 46  LEU D CG  1 
ATOM   6754 C  CD1 . LEU D 1 46  ? 41.633  -14.472 49.080  1.00 15.63 ? 46  LEU D CD1 1 
ATOM   6755 C  CD2 . LEU D 1 46  ? 43.715  -14.654 50.537  1.00 16.02 ? 46  LEU D CD2 1 
ATOM   6756 N  N   . GLU D 1 47  ? 43.951  -19.321 50.582  1.00 15.83 ? 47  GLU D N   1 
ATOM   6757 C  CA  . GLU D 1 47  ? 43.608  -20.686 50.947  1.00 17.28 ? 47  GLU D CA  1 
ATOM   6758 C  C   . GLU D 1 47  ? 42.382  -20.600 51.851  1.00 15.90 ? 47  GLU D C   1 
ATOM   6759 O  O   . GLU D 1 47  ? 42.341  -19.772 52.752  1.00 14.42 ? 47  GLU D O   1 
ATOM   6760 C  CB  . GLU D 1 47  ? 44.851  -21.413 51.544  1.00 20.58 ? 47  GLU D CB  1 
ATOM   6761 C  CG  . GLU D 1 47  ? 46.040  -21.345 50.546  1.00 22.70 ? 47  GLU D CG  1 
ATOM   6762 C  CD  . GLU D 1 47  ? 47.377  -21.983 51.012  1.00 28.84 ? 47  GLU D CD  1 
ATOM   6763 O  OE1 . GLU D 1 47  ? 48.470  -21.374 50.761  1.00 31.84 ? 47  GLU D OE1 1 
ATOM   6764 O  OE2 . GLU D 1 47  ? 47.356  -23.085 51.594  1.00 27.04 ? 47  GLU D OE2 1 
ATOM   6765 N  N   . PHE D 1 48  ? 41.372  -21.452 51.578  1.00 14.02 ? 48  PHE D N   1 
ATOM   6766 C  CA  . PHE D 1 48  ? 40.110  -21.448 52.345  1.00 15.69 ? 48  PHE D CA  1 
ATOM   6767 C  C   . PHE D 1 48  ? 40.113  -22.609 53.321  1.00 15.78 ? 48  PHE D C   1 
ATOM   6768 O  O   . PHE D 1 48  ? 40.246  -23.755 52.891  1.00 15.91 ? 48  PHE D O   1 
ATOM   6769 C  CB  . PHE D 1 48  ? 38.931  -21.529 51.364  1.00 14.37 ? 48  PHE D CB  1 
ATOM   6770 C  CG  . PHE D 1 48  ? 39.084  -20.568 50.238  1.00 14.64 ? 48  PHE D CG  1 
ATOM   6771 C  CD1 . PHE D 1 48  ? 39.538  -20.978 49.001  1.00 14.02 ? 48  PHE D CD1 1 
ATOM   6772 C  CD2 . PHE D 1 48  ? 38.869  -19.192 50.466  1.00 13.79 ? 48  PHE D CD2 1 
ATOM   6773 C  CE1 . PHE D 1 48  ? 39.741  -20.051 47.977  1.00 14.36 ? 48  PHE D CE1 1 
ATOM   6774 C  CE2 . PHE D 1 48  ? 39.067  -18.262 49.454  1.00 14.06 ? 48  PHE D CE2 1 
ATOM   6775 C  CZ  . PHE D 1 48  ? 39.488  -18.697 48.194  1.00 13.63 ? 48  PHE D CZ  1 
ATOM   6776 N  N   . GLN D 1 49  ? 40.053  -22.277 54.605  1.00 14.89 ? 49  GLN D N   1 
ATOM   6777 C  CA  . GLN D 1 49  ? 40.177  -23.246 55.704  1.00 13.95 ? 49  GLN D CA  1 
ATOM   6778 C  C   . GLN D 1 49  ? 38.913  -23.328 56.522  1.00 12.89 ? 49  GLN D C   1 
ATOM   6779 O  O   . GLN D 1 49  ? 38.387  -22.299 56.983  1.00 13.54 ? 49  GLN D O   1 
ATOM   6780 C  CB  . GLN D 1 49  ? 41.363  -22.837 56.636  1.00 15.68 ? 49  GLN D CB  1 
ATOM   6781 C  CG  . GLN D 1 49  ? 42.731  -23.103 56.013  1.00 15.55 ? 49  GLN D CG  1 
ATOM   6782 C  CD  . GLN D 1 49  ? 43.850  -22.212 56.561  1.00 16.67 ? 49  GLN D CD  1 
ATOM   6783 O  OE1 . GLN D 1 49  ? 43.596  -21.332 57.399  1.00 16.96 ? 49  GLN D OE1 1 
ATOM   6784 N  NE2 . GLN D 1 49  ? 45.090  -22.411 56.051  1.00 17.22 ? 49  GLN D NE2 1 
ATOM   6785 N  N   . GLY D 1 50  ? 38.407  -24.551 56.749  1.00 12.39 ? 50  GLY D N   1 
ATOM   6786 C  CA  . GLY D 1 50  ? 37.248  -24.617 57.629  1.00 11.77 ? 50  GLY D CA  1 
ATOM   6787 C  C   . GLY D 1 50  ? 35.947  -24.218 56.923  1.00 11.63 ? 50  GLY D C   1 
ATOM   6788 O  O   . GLY D 1 50  ? 34.938  -24.093 57.595  1.00 11.21 ? 50  GLY D O   1 
ATOM   6789 N  N   . TYR D 1 51  ? 35.982  -24.034 55.593  1.00 11.03 ? 51  TYR D N   1 
ATOM   6790 C  CA  . TYR D 1 51  ? 34.793  -23.684 54.765  1.00 11.78 ? 51  TYR D CA  1 
ATOM   6791 C  C   . TYR D 1 51  ? 33.819  -24.873 54.613  1.00 12.17 ? 51  TYR D C   1 
ATOM   6792 O  O   . TYR D 1 51  ? 32.640  -24.671 54.322  1.00 12.41 ? 51  TYR D O   1 
ATOM   6793 C  CB  . TYR D 1 51  ? 35.219  -23.240 53.338  1.00 10.79 ? 51  TYR D CB  1 
ATOM   6794 C  CG  . TYR D 1 51  ? 35.492  -21.723 53.236  1.00 12.14 ? 51  TYR D CG  1 
ATOM   6795 C  CD1 . TYR D 1 51  ? 36.400  -21.086 54.111  1.00 12.81 ? 51  TYR D CD1 1 
ATOM   6796 C  CD2 . TYR D 1 51  ? 34.913  -20.950 52.199  1.00 12.74 ? 51  TYR D CD2 1 
ATOM   6797 C  CE1 . TYR D 1 51  ? 36.663  -19.709 54.006  1.00 12.75 ? 51  TYR D CE1 1 
ATOM   6798 C  CE2 . TYR D 1 51  ? 35.188  -19.561 52.079  1.00 12.41 ? 51  TYR D CE2 1 
ATOM   6799 C  CZ  . TYR D 1 51  ? 36.042  -18.961 52.999  1.00 12.16 ? 51  TYR D CZ  1 
ATOM   6800 O  OH  . TYR D 1 51  ? 36.281  -17.593 52.934  1.00 12.08 ? 51  TYR D OH  1 
ATOM   6801 N  N   . ASN D 1 52  ? 34.292  -26.103 54.786  1.00 13.41 ? 52  ASN D N   1 
ATOM   6802 C  CA  . ASN D 1 52  ? 33.371  -27.270 54.770  1.00 14.39 ? 52  ASN D CA  1 
ATOM   6803 C  C   . ASN D 1 52  ? 32.646  -27.419 56.117  1.00 14.69 ? 52  ASN D C   1 
ATOM   6804 O  O   . ASN D 1 52  ? 33.048  -28.259 56.940  1.00 15.86 ? 52  ASN D O   1 
ATOM   6805 C  CB  . ASN D 1 52  ? 34.127  -28.557 54.415  1.00 16.95 ? 52  ASN D CB  1 
ATOM   6806 C  CG  . ASN D 1 52  ? 33.185  -29.749 54.226  1.00 19.45 ? 52  ASN D CG  1 
ATOM   6807 O  OD1 . ASN D 1 52  ? 32.029  -29.568 53.900  1.00 24.84 ? 52  ASN D OD1 1 
ATOM   6808 N  ND2 . ASN D 1 52  ? 33.680  -30.955 54.419  1.00 21.79 ? 52  ASN D ND2 1 
ATOM   6809 N  N   . LEU D 1 53  ? 31.589  -26.619 56.350  1.00 13.92 ? 53  LEU D N   1 
ATOM   6810 C  CA  . LEU D 1 53  ? 30.864  -26.561 57.636  1.00 13.83 ? 53  LEU D CA  1 
ATOM   6811 C  C   . LEU D 1 53  ? 30.153  -27.904 57.940  1.00 13.86 ? 53  LEU D C   1 
ATOM   6812 O  O   . LEU D 1 53  ? 29.506  -28.489 57.024  1.00 14.91 ? 53  LEU D O   1 
ATOM   6813 C  CB  . LEU D 1 53  ? 29.798  -25.450 57.603  1.00 12.94 ? 53  LEU D CB  1 
ATOM   6814 C  CG  . LEU D 1 53  ? 30.195  -24.040 57.193  1.00 12.68 ? 53  LEU D CG  1 
ATOM   6815 C  CD1 . LEU D 1 53  ? 28.983  -23.117 57.058  1.00 13.72 ? 53  LEU D CD1 1 
ATOM   6816 C  CD2 . LEU D 1 53  ? 31.192  -23.473 58.189  1.00 12.71 ? 53  LEU D CD2 1 
ATOM   6817 N  N   . SER D 1 54  ? 30.241  -28.345 59.201  1.00 14.15 ? 54  SER D N   1 
ATOM   6818 C  CA  . SER D 1 54  ? 29.688  -29.655 59.558  1.00 15.54 ? 54  SER D CA  1 
ATOM   6819 C  C   . SER D 1 54  ? 28.171  -29.692 59.277  1.00 16.17 ? 54  SER D C   1 
ATOM   6820 O  O   . SER D 1 54  ? 27.421  -28.800 59.723  1.00 15.21 ? 54  SER D O   1 
ATOM   6821 C  CB  . SER D 1 54  ? 29.961  -30.002 61.022  1.00 15.17 ? 54  SER D CB  1 
ATOM   6822 O  OG  . SER D 1 54  ? 29.206  -31.151 61.337  1.00 13.10 ? 54  SER D OG  1 
ATOM   6823 N  N   . ALA D 1 55  ? 27.744  -30.745 58.591  1.00 18.11 ? 55  ALA D N   1 
ATOM   6824 C  CA  . ALA D 1 55  ? 26.339  -30.927 58.267  1.00 21.00 ? 55  ALA D CA  1 
ATOM   6825 C  C   . ALA D 1 55  ? 25.464  -31.136 59.529  1.00 22.15 ? 55  ALA D C   1 
ATOM   6826 O  O   . ALA D 1 55  ? 24.215  -30.903 59.488  1.00 22.15 ? 55  ALA D O   1 
ATOM   6827 C  CB  . ALA D 1 55  ? 26.203  -32.075 57.266  1.00 25.49 ? 55  ALA D CB  1 
ATOM   6828 N  N   . ASN D 1 56  ? 26.117  -31.521 60.639  1.00 20.35 ? 56  ASN D N   1 
ATOM   6829 C  CA  . ASN D 1 56  ? 25.478  -31.718 61.963  1.00 20.61 ? 56  ASN D CA  1 
ATOM   6830 C  C   . ASN D 1 56  ? 25.345  -30.459 62.848  1.00 21.72 ? 56  ASN D C   1 
ATOM   6831 O  O   . ASN D 1 56  ? 24.638  -30.467 63.902  1.00 20.08 ? 56  ASN D O   1 
ATOM   6832 C  CB  . ASN D 1 56  ? 26.152  -32.861 62.766  1.00 24.77 ? 56  ASN D CB  1 
ATOM   6833 C  CG  . ASN D 1 56  ? 26.301  -34.165 61.962  1.00 26.89 ? 56  ASN D CG  1 
ATOM   6834 O  OD1 . ASN D 1 56  ? 27.369  -34.780 61.956  1.00 31.30 ? 56  ASN D OD1 1 
ATOM   6835 N  ND2 . ASN D 1 56  ? 25.268  -34.568 61.272  1.00 24.93 ? 56  ASN D ND2 1 
ATOM   6836 N  N   . LYS D 1 57  ? 25.996  -29.369 62.421  1.00 18.56 ? 57  LYS D N   1 
ATOM   6837 C  CA  . LYS D 1 57  ? 25.841  -28.097 63.087  1.00 17.14 ? 57  LYS D CA  1 
ATOM   6838 C  C   . LYS D 1 57  ? 24.840  -27.271 62.262  1.00 16.65 ? 57  LYS D C   1 
ATOM   6839 O  O   . LYS D 1 57  ? 24.556  -27.611 61.132  1.00 18.65 ? 57  LYS D O   1 
ATOM   6840 C  CB  . LYS D 1 57  ? 27.210  -27.390 63.256  1.00 19.96 ? 57  LYS D CB  1 
ATOM   6841 C  CG  . LYS D 1 57  ? 28.247  -28.220 64.022  1.00 20.73 ? 57  LYS D CG  1 
ATOM   6842 C  CD  . LYS D 1 57  ? 29.636  -27.585 64.007  1.00 22.70 ? 57  LYS D CD  1 
ATOM   6843 C  CE  . LYS D 1 57  ? 29.992  -27.081 65.400  1.00 24.13 ? 57  LYS D CE  1 
ATOM   6844 N  NZ  . LYS D 1 57  ? 31.364  -26.521 65.484  1.00 26.92 ? 57  LYS D NZ  1 
ATOM   6845 N  N   . GLN D 1 58  ? 24.324  -26.220 62.876  1.00 15.75 ? 58  GLN D N   1 
ATOM   6846 C  CA  . GLN D 1 58  ? 23.321  -25.284 62.325  1.00 15.59 ? 58  GLN D CA  1 
ATOM   6847 C  C   . GLN D 1 58  ? 23.827  -23.851 62.312  1.00 14.46 ? 58  GLN D C   1 
ATOM   6848 O  O   . GLN D 1 58  ? 24.571  -23.425 63.247  1.00 13.52 ? 58  GLN D O   1 
ATOM   6849 C  CB  . GLN D 1 58  ? 22.010  -25.352 63.177  1.00 14.30 ? 58  GLN D CB  1 
ATOM   6850 C  CG  . GLN D 1 58  ? 22.104  -24.884 64.641  1.00 15.82 ? 58  GLN D CG  1 
ATOM   6851 C  CD  . GLN D 1 58  ? 20.736  -24.806 65.397  1.00 17.13 ? 58  GLN D CD  1 
ATOM   6852 O  OE1 . GLN D 1 58  ? 20.624  -24.258 66.543  1.00 17.14 ? 58  GLN D OE1 1 
ATOM   6853 N  NE2 . GLN D 1 58  ? 19.715  -25.332 64.768  1.00 16.02 ? 58  GLN D NE2 1 
ATOM   6854 N  N   . PHE D 1 59  ? 23.399  -23.092 61.279  1.00 12.55 ? 59  PHE D N   1 
ATOM   6855 C  CA  . PHE D 1 59  ? 23.861  -21.681 61.115  1.00 13.22 ? 59  PHE D CA  1 
ATOM   6856 C  C   . PHE D 1 59  ? 22.701  -20.743 60.893  1.00 11.84 ? 59  PHE D C   1 
ATOM   6857 O  O   . PHE D 1 59  ? 21.745  -21.109 60.158  1.00 14.15 ? 59  PHE D O   1 
ATOM   6858 C  CB  . PHE D 1 59  ? 24.936  -21.615 59.999  1.00 11.47 ? 59  PHE D CB  1 
ATOM   6859 C  CG  . PHE D 1 59  ? 26.106  -22.521 60.307  1.00 12.22 ? 59  PHE D CG  1 
ATOM   6860 C  CD1 . PHE D 1 59  ? 26.010  -23.902 60.051  1.00 12.27 ? 59  PHE D CD1 1 
ATOM   6861 C  CD2 . PHE D 1 59  ? 27.219  -22.049 60.977  1.00 12.39 ? 59  PHE D CD2 1 
ATOM   6862 C  CE1 . PHE D 1 59  ? 27.069  -24.766 60.380  1.00 13.20 ? 59  PHE D CE1 1 
ATOM   6863 C  CE2 . PHE D 1 59  ? 28.263  -22.921 61.330  1.00 14.19 ? 59  PHE D CE2 1 
ATOM   6864 C  CZ  . PHE D 1 59  ? 28.202  -24.270 61.026  1.00 13.06 ? 59  PHE D CZ  1 
ATOM   6865 N  N   . LEU D 1 60  ? 22.723  -19.581 61.535  1.00 12.30 ? 60  LEU D N   1 
ATOM   6866 C  CA  . LEU D 1 60  ? 21.498  -18.757 61.534  1.00 11.68 ? 60  LEU D CA  1 
ATOM   6867 C  C   . LEU D 1 60  ? 21.342  -17.936 60.243  1.00 12.53 ? 60  LEU D C   1 
ATOM   6868 O  O   . LEU D 1 60  ? 22.233  -17.148 59.908  1.00 12.15 ? 60  LEU D O   1 
ATOM   6869 C  CB  . LEU D 1 60  ? 21.471  -17.852 62.721  1.00 12.69 ? 60  LEU D CB  1 
ATOM   6870 C  CG  . LEU D 1 60  ? 20.224  -17.017 63.019  1.00 12.07 ? 60  LEU D CG  1 
ATOM   6871 C  CD1 . LEU D 1 60  ? 19.109  -17.985 63.466  1.00 12.75 ? 60  LEU D CD1 1 
ATOM   6872 C  CD2 . LEU D 1 60  ? 20.582  -15.976 64.079  1.00 13.02 ? 60  LEU D CD2 1 
ATOM   6873 N  N   . LEU D 1 61  ? 20.246  -18.125 59.502  1.00 12.29 ? 61  LEU D N   1 
ATOM   6874 C  CA  . LEU D 1 61  ? 19.912  -17.245 58.368  1.00 13.74 ? 61  LEU D CA  1 
ATOM   6875 C  C   . LEU D 1 61  ? 18.955  -16.115 58.868  1.00 14.52 ? 61  LEU D C   1 
ATOM   6876 O  O   . LEU D 1 61  ? 17.970  -16.392 59.569  1.00 14.13 ? 61  LEU D O   1 
ATOM   6877 C  CB  . LEU D 1 61  ? 19.179  -18.024 57.260  1.00 13.05 ? 61  LEU D CB  1 
ATOM   6878 C  CG  . LEU D 1 61  ? 19.044  -17.489 55.854  1.00 12.95 ? 61  LEU D CG  1 
ATOM   6879 C  CD1 . LEU D 1 61  ? 20.413  -17.533 55.126  1.00 13.05 ? 61  LEU D CD1 1 
ATOM   6880 C  CD2 . LEU D 1 61  ? 18.073  -18.414 55.118  1.00 13.56 ? 61  LEU D CD2 1 
ATOM   6881 N  N   . THR D 1 62  ? 19.265  -14.849 58.556  1.00 15.93 ? 62  THR D N   1 
ATOM   6882 C  CA  . THR D 1 62  ? 18.473  -13.723 59.126  1.00 15.91 ? 62  THR D CA  1 
ATOM   6883 C  C   . THR D 1 62  ? 18.138  -12.752 57.999  1.00 14.90 ? 62  THR D C   1 
ATOM   6884 O  O   . THR D 1 62  ? 18.981  -12.508 57.145  1.00 15.96 ? 62  THR D O   1 
ATOM   6885 C  CB  . THR D 1 62  ? 19.282  -12.883 60.188  1.00 18.70 ? 62  THR D CB  1 
ATOM   6886 O  OG1 . THR D 1 62  ? 19.663  -13.686 61.302  1.00 21.41 ? 62  THR D OG1 1 
ATOM   6887 C  CG2 . THR D 1 62  ? 18.412  -11.824 60.807  1.00 19.92 ? 62  THR D CG2 1 
ATOM   6888 N  N   . ASN D 1 63  ? 16.916  -12.208 57.970  1.00 13.32 ? 63  ASN D N   1 
ATOM   6889 C  CA  . ASN D 1 63  ? 16.626  -11.051 57.096  1.00 13.00 ? 63  ASN D CA  1 
ATOM   6890 C  C   . ASN D 1 63  ? 16.864  -9.833  58.021  1.00 12.86 ? 63  ASN D C   1 
ATOM   6891 O  O   . ASN D 1 63  ? 16.163  -9.648  59.046  1.00 12.63 ? 63  ASN D O   1 
ATOM   6892 C  CB  . ASN D 1 63  ? 15.186  -11.192 56.491  1.00 12.74 ? 63  ASN D CB  1 
ATOM   6893 C  CG  . ASN D 1 63  ? 14.639  -9.901  55.866  1.00 12.65 ? 63  ASN D CG  1 
ATOM   6894 O  OD1 . ASN D 1 63  ? 15.155  -8.786  56.101  1.00 12.68 ? 63  ASN D OD1 1 
ATOM   6895 N  ND2 . ASN D 1 63  ? 13.521  -10.045 55.112  1.00 12.39 ? 63  ASN D ND2 1 
ATOM   6896 N  N   . ASN D 1 64  ? 17.907  -9.070  57.741  1.00 12.29 ? 64  ASN D N   1 
ATOM   6897 C  CA  . ASN D 1 64  ? 18.257  -7.903  58.620  1.00 13.27 ? 64  ASN D CA  1 
ATOM   6898 C  C   . ASN D 1 64  ? 17.556  -6.585  58.209  1.00 14.09 ? 64  ASN D C   1 
ATOM   6899 O  O   . ASN D 1 64  ? 17.892  -5.513  58.676  1.00 12.35 ? 64  ASN D O   1 
ATOM   6900 C  CB  . ASN D 1 64  ? 19.805  -7.724  58.777  1.00 13.43 ? 64  ASN D CB  1 
ATOM   6901 C  CG  . ASN D 1 64  ? 20.513  -7.419  57.460  1.00 14.54 ? 64  ASN D CG  1 
ATOM   6902 O  OD1 . ASN D 1 64  ? 19.869  -7.083  56.445  1.00 13.46 ? 64  ASN D OD1 1 
ATOM   6903 N  ND2 . ASN D 1 64  ? 21.872  -7.498  57.472  1.00 14.67 ? 64  ASN D ND2 1 
ATOM   6904 N  N   . GLY D 1 65  ? 16.638  -6.687  57.258  1.00 13.77 ? 65  GLY D N   1 
ATOM   6905 C  CA  . GLY D 1 65  ? 16.022  -5.472  56.673  1.00 15.04 ? 65  GLY D CA  1 
ATOM   6906 C  C   . GLY D 1 65  ? 16.751  -4.897  55.423  1.00 13.60 ? 65  GLY D C   1 
ATOM   6907 O  O   . GLY D 1 65  ? 16.172  -4.075  54.702  1.00 12.15 ? 65  GLY D O   1 
ATOM   6908 N  N   . HIS D 1 66  ? 17.972  -5.330  55.142  1.00 13.05 ? 66  HIS D N   1 
ATOM   6909 C  CA  . HIS D 1 66  ? 18.794  -4.782  54.054  1.00 13.11 ? 66  HIS D CA  1 
ATOM   6910 C  C   . HIS D 1 66  ? 19.325  -5.828  53.125  1.00 12.14 ? 66  HIS D C   1 
ATOM   6911 O  O   . HIS D 1 66  ? 19.650  -5.557  51.914  1.00 11.88 ? 66  HIS D O   1 
ATOM   6912 C  CB  . HIS D 1 66  ? 19.993  -4.009  54.698  1.00 15.14 ? 66  HIS D CB  1 
ATOM   6913 C  CG  . HIS D 1 66  ? 19.596  -3.036  55.789  1.00 15.97 ? 66  HIS D CG  1 
ATOM   6914 N  ND1 . HIS D 1 66  ? 18.922  -1.858  55.535  1.00 17.01 ? 66  HIS D ND1 1 
ATOM   6915 C  CD2 . HIS D 1 66  ? 19.799  -3.059  57.131  1.00 17.00 ? 66  HIS D CD2 1 
ATOM   6916 C  CE1 . HIS D 1 66  ? 18.719  -1.205  56.667  1.00 17.24 ? 66  HIS D CE1 1 
ATOM   6917 N  NE2 . HIS D 1 66  ? 19.241  -1.913  57.652  1.00 17.86 ? 66  HIS D NE2 1 
ATOM   6918 N  N   . SER D 1 67  ? 19.472  -7.040  53.656  1.00 11.61 ? 67  SER D N   1 
ATOM   6919 C  CA  . SER D 1 67  ? 19.892  -8.197  52.824  1.00 11.35 ? 67  SER D CA  1 
ATOM   6920 C  C   . SER D 1 67  ? 19.460  -9.477  53.529  1.00 10.97 ? 67  SER D C   1 
ATOM   6921 O  O   . SER D 1 67  ? 18.799  -9.389  54.587  1.00 12.25 ? 67  SER D O   1 
ATOM   6922 C  CB  . SER D 1 67  ? 21.421  -8.169  52.639  1.00 12.19 ? 67  SER D CB  1 
ATOM   6923 O  OG  . SER D 1 67  ? 21.837  -9.270  51.830  1.00 11.37 ? 67  SER D OG  1 
ATOM   6924 N  N   . VAL D 1 68  ? 19.808  -10.639 52.976  1.00 11.20 ? 68  VAL D N   1 
ATOM   6925 C  CA  . VAL D 1 68  ? 19.677  -11.909 53.713  1.00 11.24 ? 68  VAL D CA  1 
ATOM   6926 C  C   . VAL D 1 68  ? 21.070  -12.330 54.082  1.00 10.81 ? 68  VAL D C   1 
ATOM   6927 O  O   . VAL D 1 68  ? 21.914  -12.428 53.201  1.00 11.15 ? 68  VAL D O   1 
ATOM   6928 C  CB  . VAL D 1 68  ? 18.924  -13.022 52.950  1.00 11.56 ? 68  VAL D CB  1 
ATOM   6929 C  CG1 . VAL D 1 68  ? 19.527  -13.333 51.551  1.00 11.69 ? 68  VAL D CG1 1 
ATOM   6930 C  CG2 . VAL D 1 68  ? 18.842  -14.323 53.778  1.00 11.44 ? 68  VAL D CG2 1 
ATOM   6931 N  N   . LYS D 1 69  ? 21.295  -12.558 55.386  1.00 11.18 ? 69  LYS D N   1 
ATOM   6932 C  CA  . LYS D 1 69  ? 22.617  -12.970 55.838  1.00 12.54 ? 69  LYS D CA  1 
ATOM   6933 C  C   . LYS D 1 69  ? 22.630  -14.364 56.502  1.00 12.29 ? 69  LYS D C   1 
ATOM   6934 O  O   . LYS D 1 69  ? 21.686  -14.714 57.184  1.00 12.36 ? 69  LYS D O   1 
ATOM   6935 C  CB  . LYS D 1 69  ? 23.217  -11.905 56.772  1.00 13.44 ? 69  LYS D CB  1 
ATOM   6936 C  CG  . LYS D 1 69  ? 22.592  -11.766 58.140  1.00 16.73 ? 69  LYS D CG  1 
ATOM   6937 C  CD  . LYS D 1 69  ? 23.422  -10.798 58.996  1.00 17.77 ? 69  LYS D CD  1 
ATOM   6938 C  CE  . LYS D 1 69  ? 23.005  -11.006 60.447  1.00 18.67 ? 69  LYS D CE  1 
ATOM   6939 N  NZ  . LYS D 1 69  ? 23.506  -10.063 61.505  1.00 19.48 ? 69  LYS D NZ  1 
ATOM   6940 N  N   . LEU D 1 70  ? 23.706  -15.141 56.275  1.00 11.47 ? 70  LEU D N   1 
ATOM   6941 C  CA  . LEU D 1 70  ? 23.957  -16.355 56.990  1.00 10.94 ? 70  LEU D CA  1 
ATOM   6942 C  C   . LEU D 1 70  ? 25.159  -16.101 57.938  1.00 10.43 ? 70  LEU D C   1 
ATOM   6943 O  O   . LEU D 1 70  ? 26.263  -15.745 57.480  1.00 9.69  ? 70  LEU D O   1 
ATOM   6944 C  CB  . LEU D 1 70  ? 24.305  -17.422 55.990  1.00 11.61 ? 70  LEU D CB  1 
ATOM   6945 C  CG  . LEU D 1 70  ? 24.541  -18.841 56.532  1.00 12.81 ? 70  LEU D CG  1 
ATOM   6946 C  CD1 . LEU D 1 70  ? 23.284  -19.473 57.156  1.00 13.10 ? 70  LEU D CD1 1 
ATOM   6947 C  CD2 . LEU D 1 70  ? 25.073  -19.640 55.375  1.00 13.13 ? 70  LEU D CD2 1 
ATOM   6948 N  N   . ASN D 1 71  ? 24.955  -16.325 59.229  1.00 10.16 ? 71  ASN D N   1 
ATOM   6949 C  CA  . ASN D 1 71  ? 26.066  -16.197 60.197  1.00 11.64 ? 71  ASN D CA  1 
ATOM   6950 C  C   . ASN D 1 71  ? 27.053  -17.346 59.932  1.00 12.53 ? 71  ASN D C   1 
ATOM   6951 O  O   . ASN D 1 71  ? 26.623  -18.457 59.581  1.00 13.09 ? 71  ASN D O   1 
ATOM   6952 C  CB  . ASN D 1 71  ? 25.511  -16.227 61.608  1.00 13.55 ? 71  ASN D CB  1 
ATOM   6953 C  CG  . ASN D 1 71  ? 24.934  -14.900 62.049  1.00 16.40 ? 71  ASN D CG  1 
ATOM   6954 O  OD1 . ASN D 1 71  ? 24.902  -13.928 61.292  1.00 18.98 ? 71  ASN D OD1 1 
ATOM   6955 N  ND2 . ASN D 1 71  ? 24.529  -14.837 63.321  1.00 18.48 ? 71  ASN D ND2 1 
ATOM   6956 N  N   . LEU D 1 72  ? 28.353  -17.040 60.019  1.00 11.18 ? 72  LEU D N   1 
ATOM   6957 C  CA  . LEU D 1 72  ? 29.419  -18.025 59.786  1.00 11.00 ? 72  LEU D CA  1 
ATOM   6958 C  C   . LEU D 1 72  ? 30.277  -18.138 61.039  1.00 11.83 ? 72  LEU D C   1 
ATOM   6959 O  O   . LEU D 1 72  ? 30.398  -17.175 61.759  1.00 11.47 ? 72  LEU D O   1 
ATOM   6960 C  CB  . LEU D 1 72  ? 30.323  -17.633 58.594  1.00 10.33 ? 72  LEU D CB  1 
ATOM   6961 C  CG  . LEU D 1 72  ? 29.527  -17.575 57.269  1.00 10.46 ? 72  LEU D CG  1 
ATOM   6962 C  CD1 . LEU D 1 72  ? 30.414  -16.985 56.160  1.00 9.16  ? 72  LEU D CD1 1 
ATOM   6963 C  CD2 . LEU D 1 72  ? 29.072  -19.012 57.028  1.00 10.49 ? 72  LEU D CD2 1 
ATOM   6964 N  N   . PRO D 1 73  ? 30.895  -19.327 61.290  1.00 12.65 ? 73  PRO D N   1 
ATOM   6965 C  CA  . PRO D 1 73  ? 31.661  -19.522 62.524  1.00 12.08 ? 73  PRO D CA  1 
ATOM   6966 C  C   . PRO D 1 73  ? 33.078  -18.927 62.418  1.00 12.76 ? 73  PRO D C   1 
ATOM   6967 O  O   . PRO D 1 73  ? 33.665  -18.911 61.293  1.00 11.35 ? 73  PRO D O   1 
ATOM   6968 C  CB  . PRO D 1 73  ? 31.754  -21.049 62.622  1.00 12.39 ? 73  PRO D CB  1 
ATOM   6969 C  CG  . PRO D 1 73  ? 31.733  -21.511 61.215  1.00 12.46 ? 73  PRO D CG  1 
ATOM   6970 C  CD  . PRO D 1 73  ? 30.772  -20.572 60.497  1.00 12.48 ? 73  PRO D CD  1 
ATOM   6971 N  N   . SER D 1 74  ? 33.650  -18.536 63.564  1.00 12.88 ? 74  SER D N   1 
ATOM   6972 C  CA  . SER D 1 74  ? 35.034  -17.997 63.617  1.00 15.58 ? 74  SER D CA  1 
ATOM   6973 C  C   . SER D 1 74  ? 36.130  -19.052 63.347  1.00 17.21 ? 74  SER D C   1 
ATOM   6974 O  O   . SER D 1 74  ? 37.305  -18.693 63.141  1.00 16.75 ? 74  SER D O   1 
ATOM   6975 C  CB  . SER D 1 74  ? 35.283  -17.286 64.937  1.00 15.75 ? 74  SER D CB  1 
ATOM   6976 O  OG  . SER D 1 74  ? 35.186  -18.164 66.045  1.00 14.68 ? 74  SER D OG  1 
ATOM   6977 N  N   . ASP D 1 75  ? 35.752  -20.343 63.312  1.00 15.88 ? 75  ASP D N   1 
ATOM   6978 C  CA  . ASP D 1 75  ? 36.704  -21.381 62.908  1.00 17.64 ? 75  ASP D CA  1 
ATOM   6979 C  C   . ASP D 1 75  ? 36.891  -21.558 61.375  1.00 18.33 ? 75  ASP D C   1 
ATOM   6980 O  O   . ASP D 1 75  ? 37.639  -22.426 60.904  1.00 19.67 ? 75  ASP D O   1 
ATOM   6981 C  CB  . ASP D 1 75  ? 36.397  -22.731 63.612  1.00 19.21 ? 75  ASP D CB  1 
ATOM   6982 C  CG  . ASP D 1 75  ? 35.056  -23.314 63.232  1.00 20.55 ? 75  ASP D CG  1 
ATOM   6983 O  OD1 . ASP D 1 75  ? 34.358  -23.807 64.124  1.00 25.70 ? 75  ASP D OD1 1 
ATOM   6984 O  OD2 . ASP D 1 75  ? 34.685  -23.321 62.063  1.00 24.35 ? 75  ASP D OD2 1 
ATOM   6985 N  N   . MET D 1 76  ? 36.212  -20.721 60.615  1.00 15.96 ? 76  MET D N   1 
ATOM   6986 C  CA  . MET D 1 76  ? 36.340  -20.674 59.194  1.00 15.60 ? 76  MET D CA  1 
ATOM   6987 C  C   . MET D 1 76  ? 37.397  -19.499 58.943  1.00 14.50 ? 76  MET D C   1 
ATOM   6988 O  O   . MET D 1 76  ? 37.229  -18.413 59.473  1.00 16.71 ? 76  MET D O   1 
ATOM   6989 C  CB  . MET D 1 76  ? 34.966  -20.418 58.662  1.00 14.58 ? 76  MET D CB  1 
ATOM   6990 C  CG  . MET D 1 76  ? 34.839  -20.276 57.224  1.00 16.43 ? 76  MET D CG  1 
ATOM   6991 S  SD  . MET D 1 76  ? 33.127  -20.221 56.762  1.00 18.77 ? 76  MET D SD  1 
ATOM   6992 C  CE  . MET D 1 76  ? 33.376  -19.579 55.124  1.00 14.72 ? 76  MET D CE  1 
ATOM   6993 N  N   . HIS D 1 77  ? 38.462  -19.745 58.170  1.00 14.23 ? 77  HIS D N   1 
ATOM   6994 C  CA  . HIS D 1 77  ? 39.542  -18.731 58.007  1.00 13.78 ? 77  HIS D CA  1 
ATOM   6995 C  C   . HIS D 1 77  ? 39.967  -18.548 56.568  1.00 13.23 ? 77  HIS D C   1 
ATOM   6996 O  O   . HIS D 1 77  ? 39.843  -19.443 55.766  1.00 11.17 ? 77  HIS D O   1 
ATOM   6997 C  CB  . HIS D 1 77  ? 40.819  -19.133 58.781  1.00 15.24 ? 77  HIS D CB  1 
ATOM   6998 C  CG  . HIS D 1 77  ? 40.597  -19.584 60.202  1.00 16.66 ? 77  HIS D CG  1 
ATOM   6999 N  ND1 . HIS D 1 77  ? 40.188  -18.758 61.172  1.00 17.97 ? 77  HIS D ND1 1 
ATOM   7000 C  CD2 . HIS D 1 77  ? 40.804  -20.823 60.809  1.00 17.69 ? 77  HIS D CD2 1 
ATOM   7001 C  CE1 . HIS D 1 77  ? 40.105  -19.415 62.338  1.00 18.30 ? 77  HIS D CE1 1 
ATOM   7002 N  NE2 . HIS D 1 77  ? 40.482  -20.677 62.123  1.00 17.82 ? 77  HIS D NE2 1 
ATOM   7003 N  N   . ILE D 1 78  ? 40.576  -17.404 56.243  1.00 12.70 ? 78  ILE D N   1 
ATOM   7004 C  CA  . ILE D 1 78  ? 41.380  -17.350 55.038  1.00 13.70 ? 78  ILE D CA  1 
ATOM   7005 C  C   . ILE D 1 78  ? 42.848  -17.174 55.401  1.00 14.60 ? 78  ILE D C   1 
ATOM   7006 O  O   . ILE D 1 78  ? 43.207  -16.430 56.357  1.00 12.82 ? 78  ILE D O   1 
ATOM   7007 C  CB  . ILE D 1 78  ? 40.884  -16.297 54.049  1.00 14.39 ? 78  ILE D CB  1 
ATOM   7008 C  CG1 . ILE D 1 78  ? 40.783  -14.917 54.691  1.00 15.15 ? 78  ILE D CG1 1 
ATOM   7009 C  CG2 . ILE D 1 78  ? 39.489  -16.658 53.508  1.00 13.99 ? 78  ILE D CG2 1 
ATOM   7010 C  CD1 . ILE D 1 78  ? 39.991  -13.931 53.798  1.00 14.65 ? 78  ILE D CD1 1 
ATOM   7011 N  N   . GLN D 1 79  ? 43.684  -17.848 54.627  1.00 15.86 ? 79  GLN D N   1 
ATOM   7012 C  CA  . GLN D 1 79  ? 45.125  -17.646 54.703  1.00 16.85 ? 79  GLN D CA  1 
ATOM   7013 C  C   . GLN D 1 79  ? 45.628  -17.082 53.368  1.00 18.11 ? 79  GLN D C   1 
ATOM   7014 O  O   . GLN D 1 79  ? 45.123  -17.445 52.293  1.00 17.47 ? 79  GLN D O   1 
ATOM   7015 C  CB  . GLN D 1 79  ? 45.814  -18.978 55.005  1.00 18.02 ? 79  GLN D CB  1 
ATOM   7016 C  CG  . GLN D 1 79  ? 47.346  -18.911 55.166  1.00 16.39 ? 79  GLN D CG  1 
ATOM   7017 C  CD  . GLN D 1 79  ? 47.920  -20.294 55.217  1.00 17.83 ? 79  GLN D CD  1 
ATOM   7018 O  OE1 . GLN D 1 79  ? 47.725  -20.996 56.195  1.00 18.83 ? 79  GLN D OE1 1 
ATOM   7019 N  NE2 . GLN D 1 79  ? 48.610  -20.723 54.138  1.00 17.28 ? 79  GLN D NE2 1 
ATOM   7020 N  N   . GLY D 1 80  ? 46.639  -16.210 53.460  1.00 16.64 ? 80  GLY D N   1 
ATOM   7021 C  CA  . GLY D 1 80  ? 47.205  -15.529 52.261  1.00 17.61 ? 80  GLY D CA  1 
ATOM   7022 C  C   . GLY D 1 80  ? 47.220  -13.995 52.323  1.00 17.15 ? 80  GLY D C   1 
ATOM   7023 O  O   . GLY D 1 80  ? 47.731  -13.341 51.392  1.00 16.29 ? 80  GLY D O   1 
ATOM   7024 N  N   . LEU D 1 81  ? 46.667  -13.425 53.402  1.00 15.51 ? 81  LEU D N   1 
ATOM   7025 C  CA  . LEU D 1 81  ? 46.793  -11.987 53.639  1.00 15.98 ? 81  LEU D CA  1 
ATOM   7026 C  C   . LEU D 1 81  ? 47.843  -11.838 54.737  1.00 16.64 ? 81  LEU D C   1 
ATOM   7027 O  O   . LEU D 1 81  ? 48.230  -12.830 55.370  1.00 19.27 ? 81  LEU D O   1 
ATOM   7028 C  CB  . LEU D 1 81  ? 45.449  -11.376 54.084  1.00 15.71 ? 81  LEU D CB  1 
ATOM   7029 C  CG  . LEU D 1 81  ? 44.351  -11.605 53.026  1.00 16.38 ? 81  LEU D CG  1 
ATOM   7030 C  CD1 . LEU D 1 81  ? 43.023  -11.076 53.585  1.00 17.63 ? 81  LEU D CD1 1 
ATOM   7031 C  CD2 . LEU D 1 81  ? 44.683  -10.998 51.673  1.00 15.85 ? 81  LEU D CD2 1 
ATOM   7032 N  N   . GLN D 1 82  ? 48.248  -10.623 55.025  1.00 15.33 ? 82  GLN D N   1 
ATOM   7033 C  CA  . GLN D 1 82  ? 49.314  -10.492 56.009  1.00 18.87 ? 82  GLN D CA  1 
ATOM   7034 C  C   . GLN D 1 82  ? 48.935  -10.941 57.435  1.00 18.30 ? 82  GLN D C   1 
ATOM   7035 O  O   . GLN D 1 82  ? 49.799  -11.449 58.188  1.00 20.04 ? 82  GLN D O   1 
ATOM   7036 C  CB  . GLN D 1 82  ? 49.901  -9.087  55.991  1.00 18.63 ? 82  GLN D CB  1 
ATOM   7037 C  CG  . GLN D 1 82  ? 48.977  -7.927  56.285  1.00 19.35 ? 82  GLN D CG  1 
ATOM   7038 C  CD  . GLN D 1 82  ? 49.716  -6.607  56.130  1.00 19.97 ? 82  GLN D CD  1 
ATOM   7039 O  OE1 . GLN D 1 82  ? 50.441  -6.420  55.155  1.00 19.91 ? 82  GLN D OE1 1 
ATOM   7040 N  NE2 . GLN D 1 82  ? 49.534  -5.688  57.083  1.00 22.10 ? 82  GLN D NE2 1 
ATOM   7041 N  N   . SER D 1 83  ? 47.670  -10.703 57.822  1.00 17.33 ? 83  SER D N   1 
ATOM   7042 C  CA  . SER D 1 83  ? 47.132  -11.257 59.079  1.00 15.64 ? 83  SER D CA  1 
ATOM   7043 C  C   . SER D 1 83  ? 46.143  -12.374 58.720  1.00 15.46 ? 83  SER D C   1 
ATOM   7044 O  O   . SER D 1 83  ? 45.598  -12.394 57.581  1.00 15.24 ? 83  SER D O   1 
ATOM   7045 C  CB  . SER D 1 83  ? 46.364  -10.197 59.938  1.00 15.01 ? 83  SER D CB  1 
ATOM   7046 O  OG  . SER D 1 83  ? 47.095  -8.964  60.174  1.00 19.70 ? 83  SER D OG  1 
ATOM   7047 N  N   . ARG D 1 84  ? 45.879  -13.251 59.683  1.00 15.56 ? 84  ARG D N   1 
ATOM   7048 C  CA  . ARG D 1 84  ? 44.815  -14.278 59.516  1.00 14.70 ? 84  ARG D CA  1 
ATOM   7049 C  C   . ARG D 1 84  ? 43.449  -13.618 59.728  1.00 13.35 ? 84  ARG D C   1 
ATOM   7050 O  O   . ARG D 1 84  ? 43.309  -12.736 60.593  1.00 13.73 ? 84  ARG D O   1 
ATOM   7051 C  CB  . ARG D 1 84  ? 44.975  -15.517 60.433  1.00 15.55 ? 84  ARG D CB  1 
ATOM   7052 C  CG  . ARG D 1 84  ? 44.087  -16.685 59.947  1.00 18.38 ? 84  ARG D CG  1 
ATOM   7053 C  CD  . ARG D 1 84  ? 44.346  -18.041 60.596  1.00 20.84 ? 84  ARG D CD  1 
ATOM   7054 N  NE  . ARG D 1 84  ? 43.893  -17.975 61.973  1.00 24.57 ? 84  ARG D NE  1 
ATOM   7055 C  CZ  . ARG D 1 84  ? 43.782  -18.987 62.810  1.00 25.10 ? 84  ARG D CZ  1 
ATOM   7056 N  NH1 . ARG D 1 84  ? 44.113  -20.212 62.416  1.00 24.17 ? 84  ARG D NH1 1 
ATOM   7057 N  NH2 . ARG D 1 84  ? 43.343  -18.743 64.052  1.00 23.70 ? 84  ARG D NH2 1 
ATOM   7058 N  N   . TYR D 1 85  ? 42.477  -13.965 58.857  1.00 12.06 ? 85  TYR D N   1 
ATOM   7059 C  CA  . TYR D 1 85  ? 41.137  -13.448 58.983  1.00 12.97 ? 85  TYR D CA  1 
ATOM   7060 C  C   . TYR D 1 85  ? 40.149  -14.608 59.214  1.00 13.10 ? 85  TYR D C   1 
ATOM   7061 O  O   . TYR D 1 85  ? 40.339  -15.672 58.654  1.00 14.95 ? 85  TYR D O   1 
ATOM   7062 C  CB  . TYR D 1 85  ? 40.727  -12.628 57.723  1.00 11.98 ? 85  TYR D CB  1 
ATOM   7063 C  CG  . TYR D 1 85  ? 41.389  -11.259 57.612  1.00 11.76 ? 85  TYR D CG  1 
ATOM   7064 C  CD1 . TYR D 1 85  ? 42.724  -11.141 57.237  1.00 11.74 ? 85  TYR D CD1 1 
ATOM   7065 C  CD2 . TYR D 1 85  ? 40.656  -10.102 57.893  1.00 10.19 ? 85  TYR D CD2 1 
ATOM   7066 C  CE1 . TYR D 1 85  ? 43.322  -9.864  57.113  1.00 11.96 ? 85  TYR D CE1 1 
ATOM   7067 C  CE2 . TYR D 1 85  ? 41.242  -8.839  57.799  1.00 11.43 ? 85  TYR D CE2 1 
ATOM   7068 C  CZ  . TYR D 1 85  ? 42.563  -8.726  57.384  1.00 11.22 ? 85  TYR D CZ  1 
ATOM   7069 O  OH  . TYR D 1 85  ? 43.140  -7.483  57.234  1.00 11.08 ? 85  TYR D OH  1 
ATOM   7070 N  N   . SER D 1 86  ? 39.139  -14.402 60.071  1.00 12.38 ? 86  SER D N   1 
ATOM   7071 C  CA  . SER D 1 86  ? 38.125  -15.453 60.349  1.00 12.04 ? 86  SER D CA  1 
ATOM   7072 C  C   . SER D 1 86  ? 36.725  -14.969 59.922  1.00 11.25 ? 86  SER D C   1 
ATOM   7073 O  O   . SER D 1 86  ? 36.399  -13.767 60.071  1.00 10.31 ? 86  SER D O   1 
ATOM   7074 C  CB  . SER D 1 86  ? 38.142  -15.831 61.856  1.00 14.10 ? 86  SER D CB  1 
ATOM   7075 O  OG  . SER D 1 86  ? 39.488  -16.177 62.320  1.00 13.00 ? 86  SER D OG  1 
ATOM   7076 N  N   . ALA D 1 87  ? 35.892  -15.881 59.422  1.00 10.10 ? 87  ALA D N   1 
ATOM   7077 C  CA  . ALA D 1 87  ? 34.541  -15.523 58.956  1.00 11.09 ? 87  ALA D CA  1 
ATOM   7078 C  C   . ALA D 1 87  ? 33.612  -14.975 60.058  1.00 10.93 ? 87  ALA D C   1 
ATOM   7079 O  O   . ALA D 1 87  ? 33.750  -15.325 61.263  1.00 9.95  ? 87  ALA D O   1 
ATOM   7080 C  CB  . ALA D 1 87  ? 33.863  -16.742 58.337  1.00 10.64 ? 87  ALA D CB  1 
ATOM   7081 N  N   . THR D 1 88  ? 32.677  -14.109 59.632  1.00 10.96 ? 88  THR D N   1 
ATOM   7082 C  CA  . THR D 1 88  ? 31.535  -13.691 60.481  1.00 9.86  ? 88  THR D CA  1 
ATOM   7083 C  C   . THR D 1 88  ? 30.134  -13.862 59.813  1.00 10.27 ? 88  THR D C   1 
ATOM   7084 O  O   . THR D 1 88  ? 29.193  -14.213 60.500  1.00 10.96 ? 88  THR D O   1 
ATOM   7085 C  CB  . THR D 1 88  ? 31.750  -12.262 61.031  1.00 11.55 ? 88  THR D CB  1 
ATOM   7086 O  OG1 . THR D 1 88  ? 30.657  -11.821 61.853  1.00 11.66 ? 88  THR D OG1 1 
ATOM   7087 C  CG2 . THR D 1 88  ? 32.023  -11.257 59.840  1.00 9.83  ? 88  THR D CG2 1 
ATOM   7088 N  N   . GLN D 1 89  ? 29.991  -13.570 58.506  1.00 9.72  ? 89  GLN D N   1 
ATOM   7089 C  CA  . GLN D 1 89  ? 28.678  -13.725 57.799  1.00 10.29 ? 89  GLN D CA  1 
ATOM   7090 C  C   . GLN D 1 89  ? 28.906  -13.706 56.285  1.00 9.06  ? 89  GLN D C   1 
ATOM   7091 O  O   . GLN D 1 89  ? 29.914  -13.232 55.817  1.00 9.77  ? 89  GLN D O   1 
ATOM   7092 C  CB  . GLN D 1 89  ? 27.716  -12.580 58.185  1.00 11.49 ? 89  GLN D CB  1 
ATOM   7093 C  CG  . GLN D 1 89  ? 28.263  -11.169 57.846  1.00 14.17 ? 89  GLN D CG  1 
ATOM   7094 C  CD  . GLN D 1 89  ? 27.238  -10.097 57.748  1.00 18.48 ? 89  GLN D CD  1 
ATOM   7095 O  OE1 . GLN D 1 89  ? 26.585  -9.955  56.727  1.00 18.54 ? 89  GLN D OE1 1 
ATOM   7096 N  NE2 . GLN D 1 89  ? 27.084  -9.304  58.838  1.00 20.35 ? 89  GLN D NE2 1 
ATOM   7097 N  N   . LEU D 1 90  ? 27.947  -14.209 55.518  1.00 9.50  ? 90  LEU D N   1 
ATOM   7098 C  CA  . LEU D 1 90  ? 27.876  -13.997 54.067  1.00 9.18  ? 90  LEU D CA  1 
ATOM   7099 C  C   . LEU D 1 90  ? 26.444  -13.443 53.789  1.00 9.48  ? 90  LEU D C   1 
ATOM   7100 O  O   . LEU D 1 90  ? 25.547  -13.510 54.671  1.00 8.48  ? 90  LEU D O   1 
ATOM   7101 C  CB  . LEU D 1 90  ? 28.221  -15.272 53.270  1.00 9.31  ? 90  LEU D CB  1 
ATOM   7102 C  CG  . LEU D 1 90  ? 27.314  -16.503 53.388  1.00 9.36  ? 90  LEU D CG  1 
ATOM   7103 C  CD1 . LEU D 1 90  ? 25.952  -16.371 52.684  1.00 9.67  ? 90  LEU D CD1 1 
ATOM   7104 C  CD2 . LEU D 1 90  ? 28.101  -17.643 52.768  1.00 10.11 ? 90  LEU D CD2 1 
ATOM   7105 N  N   . HIS D 1 91  ? 26.280  -12.779 52.651  1.00 9.47  ? 91  HIS D N   1 
ATOM   7106 C  CA  . HIS D 1 91  ? 25.014  -12.132 52.288  1.00 9.23  ? 91  HIS D CA  1 
ATOM   7107 C  C   . HIS D 1 91  ? 25.065  -11.752 50.821  1.00 9.51  ? 91  HIS D C   1 
ATOM   7108 O  O   . HIS D 1 91  ? 26.105  -11.971 50.141  1.00 9.42  ? 91  HIS D O   1 
ATOM   7109 C  CB  . HIS D 1 91  ? 24.778  -10.935 53.222  1.00 8.72  ? 91  HIS D CB  1 
ATOM   7110 C  CG  . HIS D 1 91  ? 25.772  -9.823  53.006  1.00 9.18  ? 91  HIS D CG  1 
ATOM   7111 N  ND1 . HIS D 1 91  ? 26.782  -9.555  53.893  1.00 8.71  ? 91  HIS D ND1 1 
ATOM   7112 C  CD2 . HIS D 1 91  ? 25.931  -8.959  51.938  1.00 8.93  ? 91  HIS D CD2 1 
ATOM   7113 C  CE1 . HIS D 1 91  ? 27.544  -8.572  53.378  1.00 8.97  ? 91  HIS D CE1 1 
ATOM   7114 N  NE2 . HIS D 1 91  ? 27.019  -8.201  52.183  1.00 9.15  ? 91  HIS D NE2 1 
ATOM   7115 N  N   . LEU D 1 92  ? 23.968  -11.239 50.252  1.00 9.39  ? 92  LEU D N   1 
ATOM   7116 C  CA  . LEU D 1 92  ? 23.929  -10.978 48.784  1.00 9.35  ? 92  LEU D CA  1 
ATOM   7117 C  C   . LEU D 1 92  ? 23.407  -9.579  48.474  1.00 8.28  ? 92  LEU D C   1 
ATOM   7118 O  O   . LEU D 1 92  ? 22.768  -8.943  49.350  1.00 8.34  ? 92  LEU D O   1 
ATOM   7119 C  CB  . LEU D 1 92  ? 22.996  -11.992 48.052  1.00 9.39  ? 92  LEU D CB  1 
ATOM   7120 C  CG  . LEU D 1 92  ? 23.609  -13.416 48.144  1.00 10.40 ? 92  LEU D CG  1 
ATOM   7121 C  CD1 . LEU D 1 92  ? 22.849  -14.245 49.177  1.00 10.46 ? 92  LEU D CD1 1 
ATOM   7122 C  CD2 . LEU D 1 92  ? 23.656  -14.118 46.793  1.00 11.34 ? 92  LEU D CD2 1 
ATOM   7123 N  N   . HIS D 1 93  ? 23.600  -9.140  47.234  1.00 8.25  ? 93  HIS D N   1 
ATOM   7124 C  CA  . HIS D 1 93  ? 23.034  -7.875  46.715  1.00 8.08  ? 93  HIS D CA  1 
ATOM   7125 C  C   . HIS D 1 93  ? 22.484  -8.200  45.341  1.00 8.19  ? 93  HIS D C   1 
ATOM   7126 O  O   . HIS D 1 93  ? 23.076  -9.010  44.629  1.00 9.49  ? 93  HIS D O   1 
ATOM   7127 C  CB  . HIS D 1 93  ? 24.083  -6.806  46.562  1.00 7.78  ? 93  HIS D CB  1 
ATOM   7128 C  CG  . HIS D 1 93  ? 24.768  -6.492  47.843  1.00 7.85  ? 93  HIS D CG  1 
ATOM   7129 N  ND1 . HIS D 1 93  ? 24.339  -5.477  48.701  1.00 8.20  ? 93  HIS D ND1 1 
ATOM   7130 C  CD2 . HIS D 1 93  ? 25.904  -7.058  48.415  1.00 8.18  ? 93  HIS D CD2 1 
ATOM   7131 C  CE1 . HIS D 1 93  ? 25.175  -5.472  49.792  1.00 7.69  ? 93  HIS D CE1 1 
ATOM   7132 N  NE2 . HIS D 1 93  ? 26.093  -6.474  49.627  1.00 7.13  ? 93  HIS D NE2 1 
ATOM   7133 N  N   . TRP D 1 94  ? 21.381  -7.563  44.983  1.00 8.47  ? 94  TRP D N   1 
ATOM   7134 C  CA  . TRP D 1 94  ? 20.710  -7.815  43.702  1.00 8.64  ? 94  TRP D CA  1 
ATOM   7135 C  C   . TRP D 1 94  ? 19.851  -6.640  43.219  1.00 9.90  ? 94  TRP D C   1 
ATOM   7136 O  O   . TRP D 1 94  ? 19.711  -5.585  43.905  1.00 10.36 ? 94  TRP D O   1 
ATOM   7137 C  CB  . TRP D 1 94  ? 19.892  -9.139  43.822  1.00 8.45  ? 94  TRP D CB  1 
ATOM   7138 C  CG  . TRP D 1 94  ? 18.803  -9.070  44.908  1.00 8.19  ? 94  TRP D CG  1 
ATOM   7139 C  CD1 . TRP D 1 94  ? 17.510  -8.588  44.777  1.00 8.59  ? 94  TRP D CD1 1 
ATOM   7140 C  CD2 . TRP D 1 94  ? 18.922  -9.489  46.307  1.00 8.33  ? 94  TRP D CD2 1 
ATOM   7141 N  NE1 . TRP D 1 94  ? 16.812  -8.675  45.971  1.00 8.63  ? 94  TRP D NE1 1 
ATOM   7142 C  CE2 . TRP D 1 94  ? 17.614  -9.204  46.940  1.00 8.47  ? 94  TRP D CE2 1 
ATOM   7143 C  CE3 . TRP D 1 94  ? 19.962  -10.058 47.099  1.00 7.86  ? 94  TRP D CE3 1 
ATOM   7144 C  CZ2 . TRP D 1 94  ? 17.366  -9.488  48.265  1.00 7.98  ? 94  TRP D CZ2 1 
ATOM   7145 C  CZ3 . TRP D 1 94  ? 19.671  -10.321 48.475  1.00 8.25  ? 94  TRP D CZ3 1 
ATOM   7146 C  CH2 . TRP D 1 94  ? 18.418  -10.017 49.035  1.00 7.68  ? 94  TRP D CH2 1 
ATOM   7147 N  N   . GLY D 1 95  ? 19.328  -6.779  42.002  1.00 10.65 ? 95  GLY D N   1 
ATOM   7148 C  CA  . GLY D 1 95  ? 18.538  -5.700  41.369  1.00 10.71 ? 95  GLY D CA  1 
ATOM   7149 C  C   . GLY D 1 95  ? 17.067  -5.943  41.451  1.00 10.90 ? 95  GLY D C   1 
ATOM   7150 O  O   . GLY D 1 95  ? 16.499  -6.008  42.547  1.00 10.80 ? 95  GLY D O   1 
ATOM   7151 N  N   . ASN D 1 96  ? 16.396  -6.068  40.297  1.00 11.50 ? 96  ASN D N   1 
ATOM   7152 C  CA  . ASN D 1 96  ? 14.950  -6.292  40.323  1.00 12.53 ? 96  ASN D CA  1 
ATOM   7153 C  C   . ASN D 1 96  ? 14.458  -6.942  39.009  1.00 12.67 ? 96  ASN D C   1 
ATOM   7154 O  O   . ASN D 1 96  ? 15.168  -6.966  38.033  1.00 12.94 ? 96  ASN D O   1 
ATOM   7155 C  CB  . ASN D 1 96  ? 14.176  -4.977  40.574  1.00 14.69 ? 96  ASN D CB  1 
ATOM   7156 C  CG  . ASN D 1 96  ? 14.129  -4.109  39.352  1.00 16.86 ? 96  ASN D CG  1 
ATOM   7157 O  OD1 . ASN D 1 96  ? 13.267  -4.276  38.512  1.00 17.47 ? 96  ASN D OD1 1 
ATOM   7158 N  ND2 . ASN D 1 96  ? 15.080  -3.177  39.242  1.00 16.89 ? 96  ASN D ND2 1 
ATOM   7159 N  N   . PRO D 1 97  ? 13.254  -7.495  38.997  1.00 13.14 ? 97  PRO D N   1 
ATOM   7160 C  CA  . PRO D 1 97  ? 12.867  -8.273  37.789  1.00 15.15 ? 97  PRO D CA  1 
ATOM   7161 C  C   . PRO D 1 97  ? 12.892  -7.500  36.422  1.00 15.39 ? 97  PRO D C   1 
ATOM   7162 O  O   . PRO D 1 97  ? 13.167  -8.107  35.380  1.00 15.84 ? 97  PRO D O   1 
ATOM   7163 C  CB  . PRO D 1 97  ? 11.444  -8.743  38.142  1.00 14.35 ? 97  PRO D CB  1 
ATOM   7164 C  CG  . PRO D 1 97  ? 11.420  -8.800  39.661  1.00 13.98 ? 97  PRO D CG  1 
ATOM   7165 C  CD  . PRO D 1 97  ? 12.236  -7.575  40.060  1.00 13.69 ? 97  PRO D CD  1 
ATOM   7166 N  N   . ASN D 1 98  ? 12.595  -6.195  36.439  1.00 17.28 ? 98  ASN D N   1 
ATOM   7167 C  CA  . ASN D 1 98  ? 12.633  -5.334  35.217  1.00 19.55 ? 98  ASN D CA  1 
ATOM   7168 C  C   . ASN D 1 98  ? 14.079  -4.953  34.800  1.00 19.00 ? 98  ASN D C   1 
ATOM   7169 O  O   . ASN D 1 98  ? 14.346  -4.641  33.634  1.00 20.03 ? 98  ASN D O   1 
ATOM   7170 C  CB  . ASN D 1 98  ? 11.880  -3.996  35.464  1.00 22.99 ? 98  ASN D CB  1 
ATOM   7171 C  CG  . ASN D 1 98  ? 10.369  -4.164  35.668  1.00 31.72 ? 98  ASN D CG  1 
ATOM   7172 O  OD1 . ASN D 1 98  ? 9.768   -5.208  35.315  1.00 30.09 ? 98  ASN D OD1 1 
ATOM   7173 N  ND2 . ASN D 1 98  ? 9.732   -3.105  36.231  1.00 32.55 ? 98  ASN D ND2 1 
ATOM   7174 N  N   . ASP D 1 99  ? 15.012  -5.011  35.769  1.00 17.17 ? 99  ASP D N   1 
ATOM   7175 C  CA  . ASP D 1 99  ? 16.395  -4.612  35.559  1.00 14.58 ? 99  ASP D CA  1 
ATOM   7176 C  C   . ASP D 1 99  ? 17.315  -5.473  36.421  1.00 14.34 ? 99  ASP D C   1 
ATOM   7177 O  O   . ASP D 1 99  ? 17.795  -5.024  37.482  1.00 14.09 ? 99  ASP D O   1 
ATOM   7178 C  CB  . ASP D 1 99  ? 16.556  -3.136  35.887  1.00 16.11 ? 99  ASP D CB  1 
ATOM   7179 C  CG  . ASP D 1 99  ? 17.831  -2.531  35.270  1.00 17.25 ? 99  ASP D CG  1 
ATOM   7180 O  OD1 . ASP D 1 99  ? 18.642  -3.233  34.618  1.00 18.80 ? 99  ASP D OD1 1 
ATOM   7181 O  OD2 . ASP D 1 99  ? 18.023  -1.322  35.396  1.00 18.15 ? 99  ASP D OD2 1 
ATOM   7182 N  N   . PRO D 1 100 ? 17.539  -6.748  35.992  1.00 13.39 ? 100 PRO D N   1 
ATOM   7183 C  CA  . PRO D 1 100 ? 18.163  -7.804  36.817  1.00 12.18 ? 100 PRO D CA  1 
ATOM   7184 C  C   . PRO D 1 100 ? 19.686  -7.702  36.771  1.00 12.20 ? 100 PRO D C   1 
ATOM   7185 O  O   . PRO D 1 100 ? 20.406  -8.675  36.366  1.00 11.99 ? 100 PRO D O   1 
ATOM   7186 C  CB  . PRO D 1 100 ? 17.601  -9.089  36.171  1.00 13.40 ? 100 PRO D CB  1 
ATOM   7187 C  CG  . PRO D 1 100 ? 17.463  -8.751  34.739  1.00 14.14 ? 100 PRO D CG  1 
ATOM   7188 C  CD  . PRO D 1 100 ? 17.106  -7.281  34.673  1.00 14.24 ? 100 PRO D CD  1 
ATOM   7189 N  N   . HIS D 1 101 ? 20.193  -6.507  37.157  1.00 11.16 ? 101 HIS D N   1 
ATOM   7190 C  CA  . HIS D 1 101 ? 21.603  -6.201  37.025  1.00 11.86 ? 101 HIS D CA  1 
ATOM   7191 C  C   . HIS D 1 101 ? 22.062  -5.477  38.262  1.00 11.87 ? 101 HIS D C   1 
ATOM   7192 O  O   . HIS D 1 101 ? 22.361  -4.280  38.208  1.00 14.57 ? 101 HIS D O   1 
ATOM   7193 C  CB  . HIS D 1 101 ? 21.852  -5.343  35.740  1.00 14.39 ? 101 HIS D CB  1 
ATOM   7194 C  CG  . HIS D 1 101 ? 21.412  -6.050  34.455  1.00 15.30 ? 101 HIS D CG  1 
ATOM   7195 N  ND1 . HIS D 1 101 ? 20.254  -5.723  33.803  1.00 16.67 ? 101 HIS D ND1 1 
ATOM   7196 C  CD2 . HIS D 1 101 ? 21.963  -7.119  33.772  1.00 15.47 ? 101 HIS D CD2 1 
ATOM   7197 C  CE1 . HIS D 1 101 ? 20.089  -6.538  32.746  1.00 17.33 ? 101 HIS D CE1 1 
ATOM   7198 N  NE2 . HIS D 1 101 ? 21.135  -7.409  32.726  1.00 20.02 ? 101 HIS D NE2 1 
ATOM   7199 N  N   . GLY D 1 102 ? 22.120  -6.183  39.396  1.00 10.64 ? 102 GLY D N   1 
ATOM   7200 C  CA  . GLY D 1 102 ? 22.364  -5.550  40.672  1.00 9.91  ? 102 GLY D CA  1 
ATOM   7201 C  C   . GLY D 1 102 ? 23.591  -5.917  41.485  1.00 9.96  ? 102 GLY D C   1 
ATOM   7202 O  O   . GLY D 1 102 ? 23.544  -5.857  42.704  1.00 10.14 ? 102 GLY D O   1 
ATOM   7203 N  N   . SER D 1 103 ? 24.672  -6.327  40.835  1.00 8.96  ? 103 SER D N   1 
ATOM   7204 C  CA  . SER D 1 103 ? 25.986  -6.421  41.500  1.00 8.71  ? 103 SER D CA  1 
ATOM   7205 C  C   . SER D 1 103 ? 26.397  -5.044  42.012  1.00 9.06  ? 103 SER D C   1 
ATOM   7206 O  O   . SER D 1 103 ? 25.876  -4.034  41.607  1.00 10.48 ? 103 SER D O   1 
ATOM   7207 C  CB  . SER D 1 103 ? 27.042  -7.056  40.562  1.00 8.47  ? 103 SER D CB  1 
ATOM   7208 O  OG  . SER D 1 103 ? 27.431  -6.230  39.434  1.00 8.09  ? 103 SER D OG  1 
ATOM   7209 N  N   . GLU D 1 104 ? 27.264  -5.054  43.005  1.00 9.10  ? 104 GLU D N   1 
ATOM   7210 C  CA  . GLU D 1 104 ? 27.860  -3.869  43.565  1.00 9.57  ? 104 GLU D CA  1 
ATOM   7211 C  C   . GLU D 1 104 ? 29.023  -3.455  42.691  1.00 8.93  ? 104 GLU D C   1 
ATOM   7212 O  O   . GLU D 1 104 ? 29.008  -2.372  42.173  1.00 9.69  ? 104 GLU D O   1 
ATOM   7213 C  CB  . GLU D 1 104 ? 28.240  -4.074  45.066  1.00 9.14  ? 104 GLU D CB  1 
ATOM   7214 C  CG  . GLU D 1 104 ? 26.994  -4.448  45.963  1.00 9.10  ? 104 GLU D CG  1 
ATOM   7215 C  CD  . GLU D 1 104 ? 27.002  -3.739  47.268  1.00 9.84  ? 104 GLU D CD  1 
ATOM   7216 O  OE1 . GLU D 1 104 ? 27.766  -4.150  48.175  1.00 9.74  ? 104 GLU D OE1 1 
ATOM   7217 O  OE2 . GLU D 1 104 ? 26.253  -2.768  47.429  1.00 10.34 ? 104 GLU D OE2 1 
ATOM   7218 N  N   . HIS D 1 105 ? 30.065  -4.286  42.563  1.00 9.32  ? 105 HIS D N   1 
ATOM   7219 C  CA  . HIS D 1 105 ? 31.151  -4.019  41.649  1.00 9.63  ? 105 HIS D CA  1 
ATOM   7220 C  C   . HIS D 1 105 ? 30.677  -4.171  40.252  1.00 10.40 ? 105 HIS D C   1 
ATOM   7221 O  O   . HIS D 1 105 ? 29.772  -5.007  40.004  1.00 11.82 ? 105 HIS D O   1 
ATOM   7222 C  CB  . HIS D 1 105 ? 32.329  -4.938  42.003  1.00 9.06  ? 105 HIS D CB  1 
ATOM   7223 C  CG  . HIS D 1 105 ? 32.914  -4.592  43.355  1.00 9.45  ? 105 HIS D CG  1 
ATOM   7224 N  ND1 . HIS D 1 105 ? 32.520  -5.176  44.506  1.00 9.53  ? 105 HIS D ND1 1 
ATOM   7225 C  CD2 . HIS D 1 105 ? 33.842  -3.635  43.690  1.00 9.15  ? 105 HIS D CD2 1 
ATOM   7226 C  CE1 . HIS D 1 105 ? 33.184  -4.602  45.541  1.00 10.32 ? 105 HIS D CE1 1 
ATOM   7227 N  NE2 . HIS D 1 105 ? 33.989  -3.655  45.038  1.00 9.30  ? 105 HIS D NE2 1 
ATOM   7228 N  N   . THR D 1 106 ? 31.225  -3.313  39.387  1.00 10.46 ? 106 THR D N   1 
ATOM   7229 C  CA  . THR D 1 106 ? 31.166  -3.397  37.893  1.00 10.46 ? 106 THR D CA  1 
ATOM   7230 C  C   . THR D 1 106 ? 32.523  -3.682  37.248  1.00 10.50 ? 106 THR D C   1 
ATOM   7231 O  O   . THR D 1 106 ? 33.571  -3.392  37.824  1.00 11.39 ? 106 THR D O   1 
ATOM   7232 C  CB  . THR D 1 106 ? 30.484  -2.175  37.252  1.00 10.53 ? 106 THR D CB  1 
ATOM   7233 O  OG1 . THR D 1 106 ? 31.256  -1.020  37.533  1.00 9.36  ? 106 THR D OG1 1 
ATOM   7234 C  CG2 . THR D 1 106 ? 29.072  -1.962  37.846  1.00 10.49 ? 106 THR D CG2 1 
ATOM   7235 N  N   . VAL D 1 107 ? 32.521  -4.257  36.060  1.00 10.75 ? 107 VAL D N   1 
ATOM   7236 C  CA  . VAL D 1 107 ? 33.789  -4.592  35.359  1.00 11.67 ? 107 VAL D CA  1 
ATOM   7237 C  C   . VAL D 1 107 ? 33.653  -3.942  33.975  1.00 12.58 ? 107 VAL D C   1 
ATOM   7238 O  O   . VAL D 1 107 ? 32.735  -4.304  33.205  1.00 11.91 ? 107 VAL D O   1 
ATOM   7239 C  CB  . VAL D 1 107 ? 34.003  -6.135  35.195  1.00 11.56 ? 107 VAL D CB  1 
ATOM   7240 C  CG1 . VAL D 1 107 ? 35.270  -6.460  34.380  1.00 11.90 ? 107 VAL D CG1 1 
ATOM   7241 C  CG2 . VAL D 1 107 ? 34.094  -6.833  36.521  1.00 12.72 ? 107 VAL D CG2 1 
ATOM   7242 N  N   . SER D 1 108 ? 34.505  -2.953  33.704  1.00 13.83 ? 108 SER D N   1 
ATOM   7243 C  CA  . SER D 1 108 ? 34.433  -2.163  32.445  1.00 15.21 ? 108 SER D CA  1 
ATOM   7244 C  C   . SER D 1 108 ? 33.003  -1.638  32.212  1.00 15.68 ? 108 SER D C   1 
ATOM   7245 O  O   . SER D 1 108 ? 32.450  -1.728  31.092  1.00 15.08 ? 108 SER D O   1 
ATOM   7246 C  CB  . SER D 1 108 ? 34.921  -3.038  31.265  1.00 15.86 ? 108 SER D CB  1 
ATOM   7247 O  OG  . SER D 1 108 ? 36.273  -3.485  31.512  1.00 19.29 ? 108 SER D OG  1 
ATOM   7248 N  N   . GLY D 1 109 ? 32.390  -1.168  33.312  1.00 14.38 ? 109 GLY D N   1 
ATOM   7249 C  CA  . GLY D 1 109 ? 31.153  -0.415  33.253  1.00 16.24 ? 109 GLY D CA  1 
ATOM   7250 C  C   . GLY D 1 109 ? 29.938  -1.339  33.366  1.00 17.18 ? 109 GLY D C   1 
ATOM   7251 O  O   . GLY D 1 109 ? 28.839  -0.842  33.606  1.00 17.80 ? 109 GLY D O   1 
ATOM   7252 N  N   . GLN D 1 110 ? 30.161  -2.664  33.302  1.00 15.97 ? 110 GLN D N   1 
ATOM   7253 C  CA  . GLN D 1 110 ? 29.042  -3.654  33.276  1.00 15.80 ? 110 GLN D CA  1 
ATOM   7254 C  C   . GLN D 1 110 ? 28.666  -4.224  34.644  1.00 15.32 ? 110 GLN D C   1 
ATOM   7255 O  O   . GLN D 1 110 ? 29.552  -4.736  35.372  1.00 12.55 ? 110 GLN D O   1 
ATOM   7256 C  CB  . GLN D 1 110 ? 29.373  -4.822  32.350  1.00 16.73 ? 110 GLN D CB  1 
ATOM   7257 C  CG  . GLN D 1 110 ? 29.764  -4.421  30.906  1.00 17.95 ? 110 GLN D CG  1 
ATOM   7258 C  CD  . GLN D 1 110 ? 29.033  -3.192  30.359  1.00 18.61 ? 110 GLN D CD  1 
ATOM   7259 O  OE1 . GLN D 1 110 ? 27.825  -3.214  30.115  1.00 17.37 ? 110 GLN D OE1 1 
ATOM   7260 N  NE2 . GLN D 1 110 ? 29.782  -2.102  30.176  1.00 20.86 ? 110 GLN D NE2 1 
ATOM   7261 N  N   . HIS D 1 111 ? 27.356  -4.198  34.957  1.00 14.55 ? 111 HIS D N   1 
ATOM   7262 C  CA  . HIS D 1 111 ? 26.863  -4.847  36.186  1.00 14.41 ? 111 HIS D CA  1 
ATOM   7263 C  C   . HIS D 1 111 ? 26.711  -6.314  35.888  1.00 15.14 ? 111 HIS D C   1 
ATOM   7264 O  O   . HIS D 1 111 ? 26.463  -6.709  34.709  1.00 16.51 ? 111 HIS D O   1 
ATOM   7265 C  CB  . HIS D 1 111 ? 25.487  -4.324  36.618  1.00 15.67 ? 111 HIS D CB  1 
ATOM   7266 C  CG  . HIS D 1 111 ? 25.531  -3.090  37.434  1.00 14.76 ? 111 HIS D CG  1 
ATOM   7267 N  ND1 . HIS D 1 111 ? 25.581  -3.121  38.797  1.00 15.11 ? 111 HIS D ND1 1 
ATOM   7268 C  CD2 . HIS D 1 111 ? 25.551  -1.766  37.066  1.00 16.03 ? 111 HIS D CD2 1 
ATOM   7269 C  CE1 . HIS D 1 111 ? 25.621  -1.858  39.273  1.00 16.14 ? 111 HIS D CE1 1 
ATOM   7270 N  NE2 . HIS D 1 111 ? 25.607  -1.018  38.224  1.00 16.75 ? 111 HIS D NE2 1 
ATOM   7271 N  N   . PHE D 1 112 ? 26.875  -7.129  36.921  1.00 13.93 ? 112 PHE D N   1 
ATOM   7272 C  CA  . PHE D 1 112 ? 26.397  -8.501  36.896  1.00 13.80 ? 112 PHE D CA  1 
ATOM   7273 C  C   . PHE D 1 112 ? 25.044  -8.593  37.576  1.00 11.73 ? 112 PHE D C   1 
ATOM   7274 O  O   . PHE D 1 112 ? 24.488  -7.576  38.065  1.00 10.94 ? 112 PHE D O   1 
ATOM   7275 C  CB  . PHE D 1 112 ? 27.420  -9.501  37.483  1.00 14.59 ? 112 PHE D CB  1 
ATOM   7276 C  CG  . PHE D 1 112 ? 28.659  -9.655  36.642  1.00 17.15 ? 112 PHE D CG  1 
ATOM   7277 C  CD1 . PHE D 1 112 ? 29.562  -8.597  36.531  1.00 17.25 ? 112 PHE D CD1 1 
ATOM   7278 C  CD2 . PHE D 1 112 ? 28.890  -10.817 35.935  1.00 17.57 ? 112 PHE D CD2 1 
ATOM   7279 C  CE1 . PHE D 1 112 ? 30.708  -8.704  35.761  1.00 19.13 ? 112 PHE D CE1 1 
ATOM   7280 C  CE2 . PHE D 1 112 ? 30.036  -10.933 35.140  1.00 19.09 ? 112 PHE D CE2 1 
ATOM   7281 C  CZ  . PHE D 1 112 ? 30.932  -9.875  35.057  1.00 17.99 ? 112 PHE D CZ  1 
ATOM   7282 N  N   . ALA D 1 113 ? 24.427  -9.789  37.501  1.00 10.86 ? 113 ALA D N   1 
ATOM   7283 C  CA  . ALA D 1 113 ? 23.044  -9.959  37.967  1.00 10.70 ? 113 ALA D CA  1 
ATOM   7284 C  C   . ALA D 1 113 ? 22.957  -9.738  39.490  1.00 10.21 ? 113 ALA D C   1 
ATOM   7285 O  O   . ALA D 1 113 ? 22.043  -9.087  39.982  1.00 11.57 ? 113 ALA D O   1 
ATOM   7286 C  CB  . ALA D 1 113 ? 22.500  -11.364 37.578  1.00 10.45 ? 113 ALA D CB  1 
ATOM   7287 N  N   . ALA D 1 114 ? 24.017  -10.157 40.196  1.00 9.51  ? 114 ALA D N   1 
ATOM   7288 C  CA  . ALA D 1 114 ? 24.008  -10.144 41.632  1.00 9.18  ? 114 ALA D CA  1 
ATOM   7289 C  C   . ALA D 1 114 ? 25.424  -10.345 42.145  1.00 8.70  ? 114 ALA D C   1 
ATOM   7290 O  O   . ALA D 1 114 ? 26.374  -10.593 41.375  1.00 8.53  ? 114 ALA D O   1 
ATOM   7291 C  CB  . ALA D 1 114 ? 23.078  -11.266 42.145  1.00 9.61  ? 114 ALA D CB  1 
ATOM   7292 N  N   . GLU D 1 115 ? 25.581  -10.235 43.453  1.00 8.18  ? 115 GLU D N   1 
ATOM   7293 C  CA  . GLU D 1 115 ? 26.923  -10.344 44.017  1.00 8.27  ? 115 GLU D CA  1 
ATOM   7294 C  C   . GLU D 1 115 ? 26.842  -10.977 45.425  1.00 8.25  ? 115 GLU D C   1 
ATOM   7295 O  O   . GLU D 1 115 ? 25.966  -10.574 46.274  1.00 9.18  ? 115 GLU D O   1 
ATOM   7296 C  CB  . GLU D 1 115 ? 27.576  -8.911  44.034  1.00 7.97  ? 115 GLU D CB  1 
ATOM   7297 C  CG  . GLU D 1 115 ? 29.036  -8.902  44.563  1.00 8.01  ? 115 GLU D CG  1 
ATOM   7298 C  CD  . GLU D 1 115 ? 29.767  -7.618  44.259  1.00 8.19  ? 115 GLU D CD  1 
ATOM   7299 O  OE1 . GLU D 1 115 ? 30.675  -7.212  45.044  1.00 8.34  ? 115 GLU D OE1 1 
ATOM   7300 O  OE2 . GLU D 1 115 ? 29.415  -6.968  43.245  1.00 9.53  ? 115 GLU D OE2 1 
ATOM   7301 N  N   . LEU D 1 116 ? 27.762  -11.920 45.720  1.00 8.13  ? 116 LEU D N   1 
ATOM   7302 C  CA  . LEU D 1 116 ? 27.881  -12.562 47.041  1.00 8.15  ? 116 LEU D CA  1 
ATOM   7303 C  C   . LEU D 1 116 ? 29.072  -11.933 47.801  1.00 8.00  ? 116 LEU D C   1 
ATOM   7304 O  O   . LEU D 1 116 ? 30.078  -11.780 47.224  1.00 8.04  ? 116 LEU D O   1 
ATOM   7305 C  CB  . LEU D 1 116 ? 28.144  -14.087 46.899  1.00 8.39  ? 116 LEU D CB  1 
ATOM   7306 C  CG  . LEU D 1 116 ? 28.469  -14.773 48.253  1.00 7.59  ? 116 LEU D CG  1 
ATOM   7307 C  CD1 . LEU D 1 116 ? 27.234  -14.773 49.183  1.00 8.10  ? 116 LEU D CD1 1 
ATOM   7308 C  CD2 . LEU D 1 116 ? 29.101  -16.190 48.046  1.00 7.69  ? 116 LEU D CD2 1 
ATOM   7309 N  N   . HIS D 1 117 ? 28.933  -11.673 49.101  1.00 8.18  ? 117 HIS D N   1 
ATOM   7310 C  CA  . HIS D 1 117 ? 30.038  -11.199 49.960  1.00 8.27  ? 117 HIS D CA  1 
ATOM   7311 C  C   . HIS D 1 117 ? 30.204  -12.148 51.102  1.00 8.42  ? 117 HIS D C   1 
ATOM   7312 O  O   . HIS D 1 117 ? 29.241  -12.375 51.849  1.00 9.81  ? 117 HIS D O   1 
ATOM   7313 C  CB  . HIS D 1 117 ? 29.766  -9.791  50.530  1.00 8.09  ? 117 HIS D CB  1 
ATOM   7314 C  CG  . HIS D 1 117 ? 29.765  -8.719  49.479  1.00 8.18  ? 117 HIS D CG  1 
ATOM   7315 N  ND1 . HIS D 1 117 ? 29.072  -7.556  49.621  1.00 7.71  ? 117 HIS D ND1 1 
ATOM   7316 C  CD2 . HIS D 1 117 ? 30.298  -8.732  48.192  1.00 7.89  ? 117 HIS D CD2 1 
ATOM   7317 C  CE1 . HIS D 1 117 ? 29.227  -6.846  48.474  1.00 8.03  ? 117 HIS D CE1 1 
ATOM   7318 N  NE2 . HIS D 1 117 ? 29.991  -7.578  47.621  1.00 9.07  ? 117 HIS D NE2 1 
ATOM   7319 N  N   . ILE D 1 118 ? 31.428  -12.617 51.337  1.00 8.90  ? 118 ILE D N   1 
ATOM   7320 C  CA  . ILE D 1 118 ? 31.771  -13.471 52.512  1.00 8.34  ? 118 ILE D CA  1 
ATOM   7321 C  C   . ILE D 1 118 ? 32.729  -12.596 53.356  1.00 9.40  ? 118 ILE D C   1 
ATOM   7322 O  O   . ILE D 1 118 ? 33.870  -12.302 52.900  1.00 8.67  ? 118 ILE D O   1 
ATOM   7323 C  CB  . ILE D 1 118 ? 32.503  -14.742 52.084  1.00 8.80  ? 118 ILE D CB  1 
ATOM   7324 C  CG1 . ILE D 1 118 ? 31.625  -15.578 51.073  1.00 8.69  ? 118 ILE D CG1 1 
ATOM   7325 C  CG2 . ILE D 1 118 ? 32.678  -15.667 53.303  1.00 8.97  ? 118 ILE D CG2 1 
ATOM   7326 C  CD1 . ILE D 1 118 ? 32.329  -16.817 50.454  1.00 8.94  ? 118 ILE D CD1 1 
ATOM   7327 N  N   . VAL D 1 119 ? 32.251  -12.179 54.527  1.00 9.10  ? 119 VAL D N   1 
ATOM   7328 C  CA  . VAL D 1 119 ? 32.928  -11.179 55.365  1.00 9.52  ? 119 VAL D CA  1 
ATOM   7329 C  C   . VAL D 1 119 ? 33.701  -11.862 56.460  1.00 10.06 ? 119 VAL D C   1 
ATOM   7330 O  O   . VAL D 1 119 ? 33.203  -12.856 57.050  1.00 10.27 ? 119 VAL D O   1 
ATOM   7331 C  CB  . VAL D 1 119 ? 31.851  -10.211 55.974  1.00 9.72  ? 119 VAL D CB  1 
ATOM   7332 C  CG1 . VAL D 1 119 ? 32.512  -9.089  56.774  1.00 10.01 ? 119 VAL D CG1 1 
ATOM   7333 C  CG2 . VAL D 1 119 ? 30.963  -9.695  54.812  1.00 10.09 ? 119 VAL D CG2 1 
ATOM   7334 N  N   . HIS D 1 120 ? 34.905  -11.320 56.727  1.00 10.64 ? 120 HIS D N   1 
ATOM   7335 C  CA  . HIS D 1 120 ? 35.826  -11.927 57.679  1.00 10.41 ? 120 HIS D CA  1 
ATOM   7336 C  C   . HIS D 1 120 ? 36.367  -10.768 58.451  1.00 10.42 ? 120 HIS D C   1 
ATOM   7337 O  O   . HIS D 1 120 ? 36.341  -9.622  57.974  1.00 10.28 ? 120 HIS D O   1 
ATOM   7338 C  CB  . HIS D 1 120 ? 37.033  -12.637 56.989  1.00 10.76 ? 120 HIS D CB  1 
ATOM   7339 C  CG  . HIS D 1 120 ? 36.662  -13.741 56.026  1.00 10.96 ? 120 HIS D CG  1 
ATOM   7340 N  ND1 . HIS D 1 120 ? 36.053  -13.521 54.810  1.00 12.08 ? 120 HIS D ND1 1 
ATOM   7341 C  CD2 . HIS D 1 120 ? 36.842  -15.087 56.130  1.00 10.42 ? 120 HIS D CD2 1 
ATOM   7342 C  CE1 . HIS D 1 120 ? 35.878  -14.694 54.196  1.00 11.33 ? 120 HIS D CE1 1 
ATOM   7343 N  NE2 . HIS D 1 120 ? 36.372  -15.662 54.987  1.00 10.91 ? 120 HIS D NE2 1 
ATOM   7344 N  N   . TYR D 1 121 ? 36.818  -11.059 59.676  1.00 10.74 ? 121 TYR D N   1 
ATOM   7345 C  CA  . TYR D 1 121 ? 37.463  -10.054 60.492  1.00 11.62 ? 121 TYR D CA  1 
ATOM   7346 C  C   . TYR D 1 121 ? 38.892  -10.486 60.834  1.00 11.63 ? 121 TYR D C   1 
ATOM   7347 O  O   . TYR D 1 121 ? 39.202  -11.718 60.906  1.00 11.87 ? 121 TYR D O   1 
ATOM   7348 C  CB  . TYR D 1 121 ? 36.627  -9.765  61.778  1.00 11.69 ? 121 TYR D CB  1 
ATOM   7349 C  CG  . TYR D 1 121 ? 36.582  -10.884 62.798  1.00 11.86 ? 121 TYR D CG  1 
ATOM   7350 C  CD1 . TYR D 1 121 ? 37.474  -10.919 63.890  1.00 13.29 ? 121 TYR D CD1 1 
ATOM   7351 C  CD2 . TYR D 1 121 ? 35.700  -11.961 62.647  1.00 12.02 ? 121 TYR D CD2 1 
ATOM   7352 C  CE1 . TYR D 1 121 ? 37.445  -11.959 64.816  1.00 13.00 ? 121 TYR D CE1 1 
ATOM   7353 C  CE2 . TYR D 1 121 ? 35.676  -13.004 63.586  1.00 13.53 ? 121 TYR D CE2 1 
ATOM   7354 C  CZ  . TYR D 1 121 ? 36.537  -13.011 64.647  1.00 13.95 ? 121 TYR D CZ  1 
ATOM   7355 O  OH  . TYR D 1 121 ? 36.441  -14.113 65.521  1.00 16.55 ? 121 TYR D OH  1 
ATOM   7356 N  N   . ASN D 1 122 ? 39.732  -9.491  61.157  1.00 12.05 ? 122 ASN D N   1 
ATOM   7357 C  CA  . ASN D 1 122 ? 41.127  -9.753  61.535  1.00 12.19 ? 122 ASN D CA  1 
ATOM   7358 C  C   . ASN D 1 122 ? 41.222  -10.322 62.961  1.00 13.09 ? 122 ASN D C   1 
ATOM   7359 O  O   . ASN D 1 122 ? 41.176  -9.527  63.920  1.00 10.06 ? 122 ASN D O   1 
ATOM   7360 C  CB  . ASN D 1 122 ? 41.968  -8.455  61.502  1.00 12.44 ? 122 ASN D CB  1 
ATOM   7361 C  CG  . ASN D 1 122 ? 43.473  -8.739  61.591  1.00 12.54 ? 122 ASN D CG  1 
ATOM   7362 O  OD1 . ASN D 1 122 ? 43.894  -9.661  62.313  1.00 12.96 ? 122 ASN D OD1 1 
ATOM   7363 N  ND2 . ASN D 1 122 ? 44.281  -8.016  60.800  1.00 11.97 ? 122 ASN D ND2 1 
ATOM   7364 N  N   . SER D 1 123 ? 41.316  -11.658 63.054  1.00 12.86 ? 123 SER D N   1 
ATOM   7365 C  CA  . SER D 1 123 ? 41.318  -12.387 64.318  1.00 13.49 ? 123 SER D CA  1 
ATOM   7366 C  C   . SER D 1 123 ? 42.730  -12.446 64.982  1.00 14.83 ? 123 SER D C   1 
ATOM   7367 O  O   . SER D 1 123 ? 42.890  -12.865 66.106  1.00 15.63 ? 123 SER D O   1 
ATOM   7368 C  CB  . SER D 1 123 ? 40.686  -13.786 64.139  1.00 12.80 ? 123 SER D CB  1 
ATOM   7369 O  OG  . SER D 1 123 ? 41.255  -14.489 63.067  1.00 11.74 ? 123 SER D OG  1 
ATOM   7370 N  N   . ASP D 1 124 ? 43.730  -11.958 64.289  1.00 15.56 ? 124 ASP D N   1 
ATOM   7371 C  CA  . ASP D 1 124 ? 45.060  -11.841 64.874  1.00 17.93 ? 124 ASP D CA  1 
ATOM   7372 C  C   . ASP D 1 124 ? 45.012  -10.567 65.711  1.00 17.70 ? 124 ASP D C   1 
ATOM   7373 O  O   . ASP D 1 124 ? 45.652  -10.491 66.769  1.00 18.81 ? 124 ASP D O   1 
ATOM   7374 C  CB  . ASP D 1 124 ? 46.119  -11.710 63.765  1.00 16.76 ? 124 ASP D CB  1 
ATOM   7375 C  CG  . ASP D 1 124 ? 46.590  -13.056 63.183  1.00 17.45 ? 124 ASP D CG  1 
ATOM   7376 O  OD1 . ASP D 1 124 ? 46.240  -14.136 63.677  1.00 18.44 ? 124 ASP D OD1 1 
ATOM   7377 O  OD2 . ASP D 1 124 ? 47.312  -13.002 62.171  1.00 20.41 ? 124 ASP D OD2 1 
ATOM   7378 N  N   . LEU D 1 125 ? 44.248  -9.572  65.287  1.00 17.64 ? 125 LEU D N   1 
ATOM   7379 C  CA  . LEU D 1 125 ? 44.281  -8.270  66.015  1.00 17.20 ? 125 LEU D CA  1 
ATOM   7380 C  C   . LEU D 1 125 ? 43.139  -8.024  66.993  1.00 19.33 ? 125 LEU D C   1 
ATOM   7381 O  O   . LEU D 1 125 ? 43.283  -7.268  67.979  1.00 17.67 ? 125 LEU D O   1 
ATOM   7382 C  CB  . LEU D 1 125 ? 44.366  -7.093  65.046  1.00 17.65 ? 125 LEU D CB  1 
ATOM   7383 C  CG  . LEU D 1 125 ? 45.633  -6.835  64.200  1.00 19.23 ? 125 LEU D CG  1 
ATOM   7384 C  CD1 . LEU D 1 125 ? 45.416  -5.559  63.409  1.00 20.06 ? 125 LEU D CD1 1 
ATOM   7385 C  CD2 . LEU D 1 125 ? 46.855  -6.694  65.113  1.00 20.66 ? 125 LEU D CD2 1 
ATOM   7386 N  N   . TYR D 1 126 ? 41.981  -8.601  66.677  1.00 16.45 ? 126 TYR D N   1 
ATOM   7387 C  CA  . TYR D 1 126 ? 40.743  -8.234  67.311  1.00 14.75 ? 126 TYR D CA  1 
ATOM   7388 C  C   . TYR D 1 126 ? 39.986  -9.530  67.681  1.00 15.48 ? 126 TYR D C   1 
ATOM   7389 O  O   . TYR D 1 126 ? 40.056  -10.533 66.951  1.00 13.74 ? 126 TYR D O   1 
ATOM   7390 C  CB  . TYR D 1 126 ? 39.848  -7.320  66.407  1.00 14.30 ? 126 TYR D CB  1 
ATOM   7391 C  CG  . TYR D 1 126 ? 40.607  -6.118  65.859  1.00 13.99 ? 126 TYR D CG  1 
ATOM   7392 C  CD1 . TYR D 1 126 ? 40.993  -6.058  64.498  1.00 13.34 ? 126 TYR D CD1 1 
ATOM   7393 C  CD2 . TYR D 1 126 ? 40.987  -5.088  66.706  1.00 13.90 ? 126 TYR D CD2 1 
ATOM   7394 C  CE1 . TYR D 1 126 ? 41.705  -4.938  64.016  1.00 13.15 ? 126 TYR D CE1 1 
ATOM   7395 C  CE2 . TYR D 1 126 ? 41.726  -3.987  66.248  1.00 13.59 ? 126 TYR D CE2 1 
ATOM   7396 C  CZ  . TYR D 1 126 ? 42.110  -3.946  64.901  1.00 13.24 ? 126 TYR D CZ  1 
ATOM   7397 O  OH  . TYR D 1 126 ? 42.808  -2.868  64.420  1.00 13.26 ? 126 TYR D OH  1 
ATOM   7398 N  N   . PRO D 1 127 ? 39.227  -9.454  68.790  1.00 15.58 ? 127 PRO D N   1 
ATOM   7399 C  CA  . PRO D 1 127 ? 38.491  -10.556 69.401  1.00 16.35 ? 127 PRO D CA  1 
ATOM   7400 C  C   . PRO D 1 127 ? 37.273  -11.014 68.575  1.00 16.82 ? 127 PRO D C   1 
ATOM   7401 O  O   . PRO D 1 127 ? 36.939  -12.212 68.574  1.00 15.58 ? 127 PRO D O   1 
ATOM   7402 C  CB  . PRO D 1 127 ? 37.999  -9.949  70.737  1.00 17.34 ? 127 PRO D CB  1 
ATOM   7403 C  CG  . PRO D 1 127 ? 38.009  -8.471  70.549  1.00 18.25 ? 127 PRO D CG  1 
ATOM   7404 C  CD  . PRO D 1 127 ? 39.187  -8.229  69.620  1.00 16.43 ? 127 PRO D CD  1 
ATOM   7405 N  N   . ASP D 1 128 ? 36.598  -10.057 67.912  1.00 15.47 ? 128 ASP D N   1 
ATOM   7406 C  CA  . ASP D 1 128 ? 35.326  -10.343 67.194  1.00 15.09 ? 128 ASP D CA  1 
ATOM   7407 C  C   . ASP D 1 128 ? 35.090  -9.295  66.069  1.00 14.13 ? 128 ASP D C   1 
ATOM   7408 O  O   . ASP D 1 128 ? 35.738  -8.237  66.032  1.00 13.22 ? 128 ASP D O   1 
ATOM   7409 C  CB  . ASP D 1 128 ? 34.116  -10.357 68.167  1.00 17.98 ? 128 ASP D CB  1 
ATOM   7410 C  CG  . ASP D 1 128 ? 34.072  -9.177  69.100  1.00 20.73 ? 128 ASP D CG  1 
ATOM   7411 O  OD1 . ASP D 1 128 ? 34.176  -8.017  68.664  1.00 20.73 ? 128 ASP D OD1 1 
ATOM   7412 O  OD2 . ASP D 1 128 ? 33.951  -9.398  70.321  1.00 25.42 ? 128 ASP D OD2 1 
ATOM   7413 N  N   . ALA D 1 129 ? 34.130  -9.568  65.189  1.00 12.17 ? 129 ALA D N   1 
ATOM   7414 C  CA  . ALA D 1 129 ? 33.835  -8.635  64.084  1.00 13.66 ? 129 ALA D CA  1 
ATOM   7415 C  C   . ALA D 1 129 ? 33.318  -7.279  64.553  1.00 14.17 ? 129 ALA D C   1 
ATOM   7416 O  O   . ALA D 1 129 ? 33.696  -6.245  63.962  1.00 15.81 ? 129 ALA D O   1 
ATOM   7417 C  CB  . ALA D 1 129 ? 32.836  -9.298  63.106  1.00 12.80 ? 129 ALA D CB  1 
ATOM   7418 N  N   . SER D 1 130 ? 32.466  -7.260  65.615  1.00 15.58 ? 130 SER D N   1 
ATOM   7419 C  CA  . SER D 1 130 ? 31.991  -5.987  66.199  1.00 16.43 ? 130 SER D CA  1 
ATOM   7420 C  C   . SER D 1 130 ? 33.138  -5.051  66.605  1.00 17.16 ? 130 SER D C   1 
ATOM   7421 O  O   . SER D 1 130 ? 33.132  -3.826  66.271  1.00 16.22 ? 130 SER D O   1 
ATOM   7422 C  CB  . SER D 1 130 ? 31.045  -6.252  67.388  1.00 20.19 ? 130 SER D CB  1 
ATOM   7423 O  OG  . SER D 1 130 ? 30.827  -5.033  68.138  1.00 23.96 ? 130 SER D OG  1 
ATOM   7424 N  N   . THR D 1 131 ? 34.149  -5.608  67.286  1.00 16.84 ? 131 THR D N   1 
ATOM   7425 C  CA  . THR D 1 131 ? 35.344  -4.819  67.660  1.00 16.54 ? 131 THR D CA  1 
ATOM   7426 C  C   . THR D 1 131 ? 36.135  -4.433  66.428  1.00 15.25 ? 131 THR D C   1 
ATOM   7427 O  O   . THR D 1 131 ? 36.555  -3.283  66.319  1.00 16.59 ? 131 THR D O   1 
ATOM   7428 C  CB  . THR D 1 131 ? 36.262  -5.551  68.688  1.00 17.83 ? 131 THR D CB  1 
ATOM   7429 O  OG1 . THR D 1 131 ? 35.476  -5.966  69.810  1.00 18.46 ? 131 THR D OG1 1 
ATOM   7430 C  CG2 . THR D 1 131 ? 37.407  -4.650  69.179  1.00 17.66 ? 131 THR D CG2 1 
ATOM   7431 N  N   . ALA D 1 132 ? 36.296  -5.364  65.466  1.00 15.10 ? 132 ALA D N   1 
ATOM   7432 C  CA  . ALA D 1 132 ? 37.176  -5.144  64.303  1.00 14.64 ? 132 ALA D CA  1 
ATOM   7433 C  C   . ALA D 1 132 ? 36.662  -4.112  63.306  1.00 15.30 ? 132 ALA D C   1 
ATOM   7434 O  O   . ALA D 1 132 ? 37.456  -3.449  62.671  1.00 15.09 ? 132 ALA D O   1 
ATOM   7435 C  CB  . ALA D 1 132 ? 37.496  -6.448  63.571  1.00 13.49 ? 132 ALA D CB  1 
ATOM   7436 N  N   . SER D 1 133 ? 35.349  -3.938  63.248  1.00 15.03 ? 133 SER D N   1 
ATOM   7437 C  CA  . SER D 1 133 ? 34.728  -3.335  62.073  1.00 15.57 ? 133 SER D CA  1 
ATOM   7438 C  C   . SER D 1 133 ? 35.200  -1.902  61.839  1.00 15.51 ? 133 SER D C   1 
ATOM   7439 O  O   . SER D 1 133 ? 35.384  -1.492  60.675  1.00 14.64 ? 133 SER D O   1 
ATOM   7440 C  CB  . SER D 1 133 ? 33.228  -3.319  62.263  1.00 15.69 ? 133 SER D CB  1 
ATOM   7441 O  OG  . SER D 1 133 ? 32.585  -2.988  61.047  1.00 15.46 ? 133 SER D OG  1 
ATOM   7442 N  N   . ASN D 1 134 ? 35.336  -1.122  62.921  1.00 14.88 ? 134 ASN D N   1 
ATOM   7443 C  CA  . ASN D 1 134 ? 35.708  0.277   62.769  1.00 15.92 ? 134 ASN D CA  1 
ATOM   7444 C  C   . ASN D 1 134 ? 37.182  0.570   63.116  1.00 16.14 ? 134 ASN D C   1 
ATOM   7445 O  O   . ASN D 1 134 ? 37.539  1.705   63.376  1.00 15.99 ? 134 ASN D O   1 
ATOM   7446 C  CB  . ASN D 1 134 ? 34.724  1.211   63.515  1.00 16.44 ? 134 ASN D CB  1 
ATOM   7447 C  CG  . ASN D 1 134 ? 34.800  1.090   65.016  1.00 17.01 ? 134 ASN D CG  1 
ATOM   7448 O  OD1 . ASN D 1 134 ? 35.222  0.078   65.542  1.00 19.67 ? 134 ASN D OD1 1 
ATOM   7449 N  ND2 . ASN D 1 134 ? 34.388  2.144   65.722  1.00 18.39 ? 134 ASN D ND2 1 
ATOM   7450 N  N   . LYS D 1 135 ? 38.032  -0.453  63.067  1.00 16.08 ? 135 LYS D N   1 
ATOM   7451 C  CA  . LYS D 1 135 ? 39.425  -0.313  63.403  1.00 17.10 ? 135 LYS D CA  1 
ATOM   7452 C  C   . LYS D 1 135 ? 40.352  -0.646  62.207  1.00 16.51 ? 135 LYS D C   1 
ATOM   7453 O  O   . LYS D 1 135 ? 39.930  -1.293  61.232  1.00 14.22 ? 135 LYS D O   1 
ATOM   7454 C  CB  . LYS D 1 135 ? 39.757  -1.120  64.708  1.00 16.51 ? 135 LYS D CB  1 
ATOM   7455 C  CG  . LYS D 1 135 ? 38.809  -0.715  65.866  1.00 18.14 ? 135 LYS D CG  1 
ATOM   7456 C  CD  . LYS D 1 135 ? 39.066  -1.371  67.209  1.00 19.56 ? 135 LYS D CD  1 
ATOM   7457 C  CE  . LYS D 1 135 ? 38.168  -0.724  68.291  1.00 19.93 ? 135 LYS D CE  1 
ATOM   7458 N  NZ  . LYS D 1 135 ? 36.711  -1.050  68.089  1.00 21.75 ? 135 LYS D NZ  1 
ATOM   7459 N  N   . SER D 1 136 ? 41.587  -0.141  62.274  1.00 16.34 ? 136 SER D N   1 
ATOM   7460 C  CA  . SER D 1 136 ? 42.651  -0.394  61.267  1.00 16.63 ? 136 SER D CA  1 
ATOM   7461 C  C   . SER D 1 136 ? 42.774  -1.858  60.890  1.00 15.93 ? 136 SER D C   1 
ATOM   7462 O  O   . SER D 1 136 ? 42.873  -2.687  61.773  1.00 15.10 ? 136 SER D O   1 
ATOM   7463 C  CB  . SER D 1 136 ? 44.022  0.018   61.825  1.00 16.98 ? 136 SER D CB  1 
ATOM   7464 O  OG  . SER D 1 136 ? 45.025  -0.185  60.839  1.00 16.20 ? 136 SER D OG  1 
ATOM   7465 N  N   . GLU D 1 137 ? 42.810  -2.155  59.578  1.00 14.03 ? 137 GLU D N   1 
ATOM   7466 C  CA  . GLU D 1 137 ? 42.966  -3.518  59.092  1.00 14.97 ? 137 GLU D CA  1 
ATOM   7467 C  C   . GLU D 1 137 ? 41.882  -4.483  59.615  1.00 13.83 ? 137 GLU D C   1 
ATOM   7468 O  O   . GLU D 1 137 ? 42.139  -5.664  59.740  1.00 12.32 ? 137 GLU D O   1 
ATOM   7469 C  CB  . GLU D 1 137 ? 44.379  -4.078  59.439  1.00 15.53 ? 137 GLU D CB  1 
ATOM   7470 C  CG  . GLU D 1 137 ? 45.502  -3.099  59.106  1.00 18.36 ? 137 GLU D CG  1 
ATOM   7471 C  CD  . GLU D 1 137 ? 46.801  -3.332  59.869  1.00 19.55 ? 137 GLU D CD  1 
ATOM   7472 O  OE1 . GLU D 1 137 ? 47.249  -4.487  59.926  1.00 24.82 ? 137 GLU D OE1 1 
ATOM   7473 O  OE2 . GLU D 1 137 ? 47.390  -2.353  60.385  1.00 21.05 ? 137 GLU D OE2 1 
ATOM   7474 N  N   . GLY D 1 138 ? 40.719  -3.978  59.964  1.00 12.68 ? 138 GLY D N   1 
ATOM   7475 C  CA  . GLY D 1 138 ? 39.712  -4.807  60.686  1.00 12.20 ? 138 GLY D CA  1 
ATOM   7476 C  C   . GLY D 1 138 ? 39.024  -5.890  59.889  1.00 10.90 ? 138 GLY D C   1 
ATOM   7477 O  O   . GLY D 1 138 ? 38.713  -6.958  60.436  1.00 10.07 ? 138 GLY D O   1 
ATOM   7478 N  N   . LEU D 1 139 ? 38.784  -5.631  58.601  1.00 10.34 ? 139 LEU D N   1 
ATOM   7479 C  CA  . LEU D 1 139 ? 37.901  -6.563  57.772  1.00 10.93 ? 139 LEU D CA  1 
ATOM   7480 C  C   . LEU D 1 139 ? 38.464  -7.012  56.419  1.00 10.07 ? 139 LEU D C   1 
ATOM   7481 O  O   . LEU D 1 139 ? 39.216  -6.286  55.792  1.00 10.37 ? 139 LEU D O   1 
ATOM   7482 C  CB  . LEU D 1 139 ? 36.541  -5.884  57.498  1.00 10.11 ? 139 LEU D CB  1 
ATOM   7483 C  CG  . LEU D 1 139 ? 35.740  -5.443  58.720  1.00 10.62 ? 139 LEU D CG  1 
ATOM   7484 C  CD1 . LEU D 1 139 ? 34.495  -4.719  58.259  1.00 11.03 ? 139 LEU D CD1 1 
ATOM   7485 C  CD2 . LEU D 1 139 ? 35.402  -6.646  59.638  1.00 10.64 ? 139 LEU D CD2 1 
ATOM   7486 N  N   . ALA D 1 140 ? 38.049  -8.193  55.940  1.00 10.51 ? 140 ALA D N   1 
ATOM   7487 C  CA  . ALA D 1 140 ? 38.345  -8.624  54.579  1.00 9.71  ? 140 ALA D CA  1 
ATOM   7488 C  C   . ALA D 1 140 ? 37.115  -9.331  53.991  1.00 10.36 ? 140 ALA D C   1 
ATOM   7489 O  O   . ALA D 1 140 ? 36.522  -10.206 54.669  1.00 10.31 ? 140 ALA D O   1 
ATOM   7490 C  CB  . ALA D 1 140 ? 39.581  -9.527  54.592  1.00 9.58  ? 140 ALA D CB  1 
ATOM   7491 N  N   . VAL D 1 141 ? 36.696  -8.892  52.814  1.00 8.89  ? 141 VAL D N   1 
ATOM   7492 C  CA  . VAL D 1 141 ? 35.483  -9.446  52.164  1.00 9.88  ? 141 VAL D CA  1 
ATOM   7493 C  C   . VAL D 1 141 ? 35.848  -10.078 50.827  1.00 10.04 ? 141 VAL D C   1 
ATOM   7494 O  O   . VAL D 1 141 ? 36.567  -9.480  49.999  1.00 9.61  ? 141 VAL D O   1 
ATOM   7495 C  CB  . VAL D 1 141 ? 34.366  -8.383  52.014  1.00 10.11 ? 141 VAL D CB  1 
ATOM   7496 C  CG1 . VAL D 1 141 ? 33.107  -8.970  51.355  1.00 9.72  ? 141 VAL D CG1 1 
ATOM   7497 C  CG2 . VAL D 1 141 ? 34.050  -7.783  53.365  1.00 10.58 ? 141 VAL D CG2 1 
ATOM   7498 N  N   . LEU D 1 142 ? 35.361  -11.304 50.596  1.00 9.96  ? 142 LEU D N   1 
ATOM   7499 C  CA  . LEU D 1 142 ? 35.497  -11.912 49.295  1.00 9.98  ? 142 LEU D CA  1 
ATOM   7500 C  C   . LEU D 1 142 ? 34.199  -11.598 48.523  1.00 10.00 ? 142 LEU D C   1 
ATOM   7501 O  O   . LEU D 1 142 ? 33.124  -11.753 49.082  1.00 10.65 ? 142 LEU D O   1 
ATOM   7502 C  CB  . LEU D 1 142 ? 35.578  -13.457 49.430  1.00 9.56  ? 142 LEU D CB  1 
ATOM   7503 C  CG  . LEU D 1 142 ? 36.670  -13.954 50.389  1.00 9.79  ? 142 LEU D CG  1 
ATOM   7504 C  CD1 . LEU D 1 142 ? 36.685  -15.509 50.299  1.00 10.01 ? 142 LEU D CD1 1 
ATOM   7505 C  CD2 . LEU D 1 142 ? 38.020  -13.376 49.954  1.00 9.57  ? 142 LEU D CD2 1 
ATOM   7506 N  N   . ALA D 1 143 ? 34.306  -11.220 47.250  1.00 10.51 ? 143 ALA D N   1 
ATOM   7507 C  CA  . ALA D 1 143 ? 33.128  -10.895 46.428  1.00 10.48 ? 143 ALA D CA  1 
ATOM   7508 C  C   . ALA D 1 143 ? 33.062  -11.826 45.251  1.00 9.87  ? 143 ALA D C   1 
ATOM   7509 O  O   . ALA D 1 143 ? 34.044  -11.932 44.530  1.00 11.09 ? 143 ALA D O   1 
ATOM   7510 C  CB  . ALA D 1 143 ? 33.284  -9.436  45.941  1.00 10.35 ? 143 ALA D CB  1 
ATOM   7511 N  N   . VAL D 1 144 ? 31.933  -12.526 45.064  1.00 10.15 ? 144 VAL D N   1 
ATOM   7512 C  CA  . VAL D 1 144 ? 31.711  -13.367 43.906  1.00 10.23 ? 144 VAL D CA  1 
ATOM   7513 C  C   . VAL D 1 144 ? 30.656  -12.701 43.035  1.00 10.44 ? 144 VAL D C   1 
ATOM   7514 O  O   . VAL D 1 144 ? 29.573  -12.378 43.548  1.00 10.95 ? 144 VAL D O   1 
ATOM   7515 C  CB  . VAL D 1 144 ? 31.243  -14.780 44.352  1.00 10.69 ? 144 VAL D CB  1 
ATOM   7516 C  CG1 . VAL D 1 144 ? 31.035  -15.686 43.130  1.00 10.63 ? 144 VAL D CG1 1 
ATOM   7517 C  CG2 . VAL D 1 144 ? 32.266  -15.439 45.325  1.00 10.24 ? 144 VAL D CG2 1 
ATOM   7518 N  N   . LEU D 1 145 ? 30.972  -12.488 41.753  1.00 10.34 ? 145 LEU D N   1 
ATOM   7519 C  CA  . LEU D 1 145 ? 30.003  -11.940 40.771  1.00 10.14 ? 145 LEU D CA  1 
ATOM   7520 C  C   . LEU D 1 145 ? 29.102  -13.062 40.285  1.00 9.38  ? 145 LEU D C   1 
ATOM   7521 O  O   . LEU D 1 145 ? 29.603  -14.176 40.079  1.00 10.01 ? 145 LEU D O   1 
ATOM   7522 C  CB  . LEU D 1 145 ? 30.757  -11.251 39.620  1.00 10.13 ? 145 LEU D CB  1 
ATOM   7523 C  CG  . LEU D 1 145 ? 31.719  -10.098 40.103  1.00 10.69 ? 145 LEU D CG  1 
ATOM   7524 C  CD1 . LEU D 1 145 ? 32.710  -9.801  38.982  1.00 10.97 ? 145 LEU D CD1 1 
ATOM   7525 C  CD2 . LEU D 1 145 ? 31.011  -8.800  40.464  1.00 11.47 ? 145 LEU D CD2 1 
ATOM   7526 N  N   . ILE D 1 146 ? 27.803  -12.770 40.094  1.00 8.98  ? 146 ILE D N   1 
ATOM   7527 C  CA  . ILE D 1 146 ? 26.804  -13.847 39.754  1.00 9.37  ? 146 ILE D CA  1 
ATOM   7528 C  C   . ILE D 1 146 ? 26.131  -13.445 38.454  1.00 10.11 ? 146 ILE D C   1 
ATOM   7529 O  O   . ILE D 1 146 ? 25.649  -12.310 38.371  1.00 10.56 ? 146 ILE D O   1 
ATOM   7530 C  CB  . ILE D 1 146 ? 25.695  -13.941 40.841  1.00 8.61  ? 146 ILE D CB  1 
ATOM   7531 C  CG1 . ILE D 1 146 ? 26.357  -14.285 42.188  1.00 7.87  ? 146 ILE D CG1 1 
ATOM   7532 C  CG2 . ILE D 1 146 ? 24.648  -15.068 40.523  1.00 7.96  ? 146 ILE D CG2 1 
ATOM   7533 C  CD1 . ILE D 1 146 ? 25.415  -14.196 43.352  1.00 8.78  ? 146 ILE D CD1 1 
ATOM   7534 N  N   . GLU D 1 147 ? 25.989  -14.356 37.501  1.00 11.66 ? 147 GLU D N   1 
ATOM   7535 C  CA  . GLU D 1 147 ? 25.224  -14.035 36.260  1.00 12.19 ? 147 GLU D CA  1 
ATOM   7536 C  C   . GLU D 1 147 ? 24.204  -15.124 36.009  1.00 13.85 ? 147 GLU D C   1 
ATOM   7537 O  O   . GLU D 1 147 ? 24.266  -16.193 36.626  1.00 12.35 ? 147 GLU D O   1 
ATOM   7538 C  CB  . GLU D 1 147 ? 26.181  -13.887 35.026  1.00 14.21 ? 147 GLU D CB  1 
ATOM   7539 C  CG  . GLU D 1 147 ? 26.928  -15.211 34.707  1.00 16.71 ? 147 GLU D CG  1 
ATOM   7540 C  CD  . GLU D 1 147 ? 27.976  -15.114 33.610  1.00 18.55 ? 147 GLU D CD  1 
ATOM   7541 O  OE1 . GLU D 1 147 ? 28.436  -13.993 33.244  1.00 18.10 ? 147 GLU D OE1 1 
ATOM   7542 O  OE2 . GLU D 1 147 ? 28.334  -16.204 33.133  1.00 22.31 ? 147 GLU D OE2 1 
ATOM   7543 N  N   . MET D 1 148 ? 23.246  -14.842 35.112  1.00 14.88 ? 148 MET D N   1 
ATOM   7544 C  CA  . MET D 1 148 ? 22.245  -15.843 34.716  1.00 15.82 ? 148 MET D CA  1 
ATOM   7545 C  C   . MET D 1 148 ? 22.882  -16.938 33.892  1.00 16.50 ? 148 MET D C   1 
ATOM   7546 O  O   . MET D 1 148 ? 23.772  -16.685 33.055  1.00 16.49 ? 148 MET D O   1 
ATOM   7547 C  CB  . MET D 1 148 ? 21.074  -15.143 33.970  1.00 19.31 ? 148 MET D CB  1 
ATOM   7548 C  CG  . MET D 1 148 ? 19.809  -15.974 33.822  1.00 24.05 ? 148 MET D CG  1 
ATOM   7549 S  SD  . MET D 1 148 ? 18.424  -15.155 32.972  1.00 33.41 ? 148 MET D SD  1 
ATOM   7550 C  CE  . MET D 1 148 ? 18.043  -13.823 34.142  1.00 26.66 ? 148 MET D CE  1 
ATOM   7551 N  N   . GLY D 1 149 ? 22.450  -18.173 34.119  1.00 15.24 ? 149 GLY D N   1 
ATOM   7552 C  CA  . GLY D 1 149 ? 23.083  -19.280 33.433  1.00 14.80 ? 149 GLY D CA  1 
ATOM   7553 C  C   . GLY D 1 149 ? 22.485  -20.575 33.899  1.00 14.43 ? 149 GLY D C   1 
ATOM   7554 O  O   . GLY D 1 149 ? 21.268  -20.656 34.079  1.00 14.50 ? 149 GLY D O   1 
ATOM   7555 N  N   . SER D 1 150 ? 23.297  -21.595 34.150  1.00 13.86 ? 150 SER D N   1 
ATOM   7556 C  CA  . SER D 1 150 ? 22.666  -22.853 34.535  1.00 16.32 ? 150 SER D CA  1 
ATOM   7557 C  C   . SER D 1 150 ? 22.164  -22.888 36.022  1.00 15.85 ? 150 SER D C   1 
ATOM   7558 O  O   . SER D 1 150 ? 22.729  -22.207 36.900  1.00 15.78 ? 150 SER D O   1 
ATOM   7559 C  CB  . SER D 1 150 ? 23.612  -24.008 34.237  1.00 15.67 ? 150 SER D CB  1 
ATOM   7560 O  OG  . SER D 1 150 ? 24.681  -23.940 35.155  1.00 21.56 ? 150 SER D OG  1 
ATOM   7561 N  N   . PHE D 1 151 ? 21.199  -23.748 36.334  1.00 15.06 ? 151 PHE D N   1 
ATOM   7562 C  CA  . PHE D 1 151 ? 20.815  -23.985 37.781  1.00 15.13 ? 151 PHE D CA  1 
ATOM   7563 C  C   . PHE D 1 151 ? 22.010  -24.338 38.712  1.00 15.55 ? 151 PHE D C   1 
ATOM   7564 O  O   . PHE D 1 151 ? 22.881  -25.151 38.344  1.00 15.60 ? 151 PHE D O   1 
ATOM   7565 C  CB  . PHE D 1 151 ? 19.693  -25.042 37.884  1.00 15.26 ? 151 PHE D CB  1 
ATOM   7566 C  CG  . PHE D 1 151 ? 19.269  -25.368 39.315  1.00 15.49 ? 151 PHE D CG  1 
ATOM   7567 C  CD1 . PHE D 1 151 ? 18.423  -24.498 40.026  1.00 15.57 ? 151 PHE D CD1 1 
ATOM   7568 C  CD2 . PHE D 1 151 ? 19.703  -26.528 39.930  1.00 15.15 ? 151 PHE D CD2 1 
ATOM   7569 C  CE1 . PHE D 1 151 ? 18.022  -24.820 41.336  1.00 14.15 ? 151 PHE D CE1 1 
ATOM   7570 C  CE2 . PHE D 1 151 ? 19.356  -26.837 41.244  1.00 15.30 ? 151 PHE D CE2 1 
ATOM   7571 C  CZ  . PHE D 1 151 ? 18.506  -25.971 41.952  1.00 15.86 ? 151 PHE D CZ  1 
ATOM   7572 N  N   . ASN D 1 152 ? 22.061  -23.728 39.913  1.00 13.77 ? 152 ASN D N   1 
ATOM   7573 C  CA  . ASN D 1 152 ? 23.206  -23.923 40.844  1.00 13.07 ? 152 ASN D CA  1 
ATOM   7574 C  C   . ASN D 1 152 ? 22.764  -24.577 42.165  1.00 13.98 ? 152 ASN D C   1 
ATOM   7575 O  O   . ASN D 1 152 ? 22.181  -23.914 43.069  1.00 12.46 ? 152 ASN D O   1 
ATOM   7576 C  CB  . ASN D 1 152 ? 23.923  -22.576 41.046  1.00 13.05 ? 152 ASN D CB  1 
ATOM   7577 C  CG  . ASN D 1 152 ? 25.276  -22.688 41.798  1.00 12.83 ? 152 ASN D CG  1 
ATOM   7578 O  OD1 . ASN D 1 152 ? 25.391  -23.370 42.826  1.00 11.76 ? 152 ASN D OD1 1 
ATOM   7579 N  ND2 . ASN D 1 152 ? 26.294  -21.957 41.291  1.00 12.76 ? 152 ASN D ND2 1 
ATOM   7580 N  N   . PRO D 1 153 ? 22.929  -25.916 42.269  1.00 13.68 ? 153 PRO D N   1 
ATOM   7581 C  CA  . PRO D 1 153 ? 22.506  -26.584 43.502  1.00 13.54 ? 153 PRO D CA  1 
ATOM   7582 C  C   . PRO D 1 153 ? 23.130  -26.014 44.780  1.00 12.50 ? 153 PRO D C   1 
ATOM   7583 O  O   . PRO D 1 153 ? 22.477  -25.991 45.839  1.00 12.90 ? 153 PRO D O   1 
ATOM   7584 C  CB  . PRO D 1 153 ? 22.948  -28.070 43.311  1.00 14.47 ? 153 PRO D CB  1 
ATOM   7585 C  CG  . PRO D 1 153 ? 23.345  -28.194 41.891  1.00 15.52 ? 153 PRO D CG  1 
ATOM   7586 C  CD  . PRO D 1 153 ? 23.539  -26.839 41.281  1.00 13.75 ? 153 PRO D CD  1 
ATOM   7587 N  N   . SER D 1 154 ? 24.367  -25.542 44.704  1.00 12.10 ? 154 SER D N   1 
ATOM   7588 C  CA  . SER D 1 154 ? 25.022  -24.990 45.885  1.00 11.83 ? 154 SER D CA  1 
ATOM   7589 C  C   . SER D 1 154 ? 24.400  -23.670 46.389  1.00 11.15 ? 154 SER D C   1 
ATOM   7590 O  O   . SER D 1 154 ? 24.110  -23.522 47.562  1.00 11.87 ? 154 SER D O   1 
ATOM   7591 C  CB  . SER D 1 154 ? 26.515  -24.863 45.630  1.00 13.75 ? 154 SER D CB  1 
ATOM   7592 O  OG  . SER D 1 154 ? 27.100  -26.140 45.188  1.00 15.11 ? 154 SER D OG  1 
ATOM   7593 N  N   . TYR D 1 155 ? 24.164  -22.723 45.507  1.00 11.82 ? 155 TYR D N   1 
ATOM   7594 C  CA  . TYR D 1 155 ? 23.372  -21.527 45.883  1.00 11.74 ? 155 TYR D CA  1 
ATOM   7595 C  C   . TYR D 1 155 ? 21.965  -21.877 46.366  1.00 11.66 ? 155 TYR D C   1 
ATOM   7596 O  O   . TYR D 1 155 ? 21.367  -21.152 47.201  1.00 11.54 ? 155 TYR D O   1 
ATOM   7597 C  CB  . TYR D 1 155 ? 23.417  -20.469 44.732  1.00 11.55 ? 155 TYR D CB  1 
ATOM   7598 C  CG  . TYR D 1 155 ? 24.734  -19.675 44.718  1.00 10.65 ? 155 TYR D CG  1 
ATOM   7599 C  CD1 . TYR D 1 155 ? 25.946  -20.205 44.158  1.00 10.63 ? 155 TYR D CD1 1 
ATOM   7600 C  CD2 . TYR D 1 155 ? 24.758  -18.410 45.220  1.00 11.03 ? 155 TYR D CD2 1 
ATOM   7601 C  CE1 . TYR D 1 155 ? 27.139  -19.466 44.149  1.00 10.34 ? 155 TYR D CE1 1 
ATOM   7602 C  CE2 . TYR D 1 155 ? 25.947  -17.637 45.212  1.00 11.12 ? 155 TYR D CE2 1 
ATOM   7603 C  CZ  . TYR D 1 155 ? 27.126  -18.189 44.702  1.00 10.57 ? 155 TYR D CZ  1 
ATOM   7604 O  OH  . TYR D 1 155 ? 28.249  -17.397 44.751  1.00 10.03 ? 155 TYR D OH  1 
ATOM   7605 N  N   . ASP D 1 156 ? 21.383  -22.981 45.849  1.00 12.62 ? 156 ASP D N   1 
ATOM   7606 C  CA  . ASP D 1 156 ? 20.117  -23.390 46.344  1.00 13.45 ? 156 ASP D CA  1 
ATOM   7607 C  C   . ASP D 1 156 ? 20.086  -23.783 47.826  1.00 14.25 ? 156 ASP D C   1 
ATOM   7608 O  O   . ASP D 1 156 ? 19.011  -23.698 48.439  1.00 14.63 ? 156 ASP D O   1 
ATOM   7609 C  CB  . ASP D 1 156 ? 19.376  -24.400 45.402  1.00 13.35 ? 156 ASP D CB  1 
ATOM   7610 C  CG  . ASP D 1 156 ? 17.941  -23.873 45.005  1.00 15.88 ? 156 ASP D CG  1 
ATOM   7611 O  OD1 . ASP D 1 156 ? 16.942  -24.664 45.002  1.00 15.70 ? 156 ASP D OD1 1 
ATOM   7612 O  OD2 . ASP D 1 156 ? 17.812  -22.649 44.666  1.00 13.52 ? 156 ASP D OD2 1 
ATOM   7613 N  N   . LYS D 1 157 ? 21.243  -24.147 48.417  1.00 13.30 ? 157 LYS D N   1 
ATOM   7614 C  CA  . LYS D 1 157 ? 21.395  -24.396 49.844  1.00 14.38 ? 157 LYS D CA  1 
ATOM   7615 C  C   . LYS D 1 157 ? 21.087  -23.175 50.751  1.00 15.10 ? 157 LYS D C   1 
ATOM   7616 O  O   . LYS D 1 157 ? 20.852  -23.357 51.936  1.00 15.79 ? 157 LYS D O   1 
ATOM   7617 C  CB  . LYS D 1 157 ? 22.759  -25.067 50.166  1.00 14.36 ? 157 LYS D CB  1 
ATOM   7618 C  CG  . LYS D 1 157 ? 22.924  -26.415 49.422  1.00 14.71 ? 157 LYS D CG  1 
ATOM   7619 C  CD  . LYS D 1 157 ? 24.351  -26.925 49.269  1.00 16.27 ? 157 LYS D CD  1 
ATOM   7620 C  CE  . LYS D 1 157 ? 24.332  -28.430 48.981  1.00 16.86 ? 157 LYS D CE  1 
ATOM   7621 N  NZ  . LYS D 1 157 ? 25.711  -29.002 48.836  1.00 13.02 ? 157 LYS D NZ  1 
ATOM   7622 N  N   . ILE D 1 158 ? 21.135  -21.957 50.169  1.00 13.17 ? 158 ILE D N   1 
ATOM   7623 C  CA  . ILE D 1 158 ? 20.627  -20.702 50.739  1.00 12.80 ? 158 ILE D CA  1 
ATOM   7624 C  C   . ILE D 1 158 ? 19.188  -20.432 50.235  1.00 11.82 ? 158 ILE D C   1 
ATOM   7625 O  O   . ILE D 1 158 ? 18.301  -20.270 51.043  1.00 12.30 ? 158 ILE D O   1 
ATOM   7626 C  CB  . ILE D 1 158 ? 21.568  -19.494 50.391  1.00 12.12 ? 158 ILE D CB  1 
ATOM   7627 C  CG1 . ILE D 1 158 ? 22.974  -19.691 51.030  1.00 11.44 ? 158 ILE D CG1 1 
ATOM   7628 C  CG2 . ILE D 1 158 ? 21.010  -18.160 50.900  1.00 11.88 ? 158 ILE D CG2 1 
ATOM   7629 C  CD1 . ILE D 1 158 ? 24.031  -18.916 50.308  1.00 12.25 ? 158 ILE D CD1 1 
ATOM   7630 N  N   . PHE D 1 159 ? 18.974  -20.456 48.924  1.00 12.29 ? 159 PHE D N   1 
ATOM   7631 C  CA  . PHE D 1 159 ? 17.743  -19.906 48.315  1.00 13.92 ? 159 PHE D CA  1 
ATOM   7632 C  C   . PHE D 1 159 ? 16.491  -20.741 48.663  1.00 14.38 ? 159 PHE D C   1 
ATOM   7633 O  O   . PHE D 1 159 ? 15.348  -20.237 48.718  1.00 12.87 ? 159 PHE D O   1 
ATOM   7634 C  CB  . PHE D 1 159 ? 17.864  -19.830 46.758  1.00 14.34 ? 159 PHE D CB  1 
ATOM   7635 C  CG  . PHE D 1 159 ? 18.955  -18.913 46.249  1.00 13.39 ? 159 PHE D CG  1 
ATOM   7636 C  CD1 . PHE D 1 159 ? 19.559  -17.959 47.078  1.00 13.20 ? 159 PHE D CD1 1 
ATOM   7637 C  CD2 . PHE D 1 159 ? 19.381  -19.029 44.936  1.00 13.77 ? 159 PHE D CD2 1 
ATOM   7638 C  CE1 . PHE D 1 159 ? 20.534  -17.114 46.552  1.00 12.72 ? 159 PHE D CE1 1 
ATOM   7639 C  CE2 . PHE D 1 159 ? 20.332  -18.177 44.403  1.00 13.97 ? 159 PHE D CE2 1 
ATOM   7640 C  CZ  . PHE D 1 159 ? 20.921  -17.227 45.241  1.00 12.69 ? 159 PHE D CZ  1 
ATOM   7641 N  N   . SER D 1 160 ? 16.704  -22.027 48.895  1.00 14.59 ? 160 SER D N   1 
ATOM   7642 C  CA  . SER D 1 160 ? 15.602  -22.930 49.270  1.00 14.09 ? 160 SER D CA  1 
ATOM   7643 C  C   . SER D 1 160 ? 14.954  -22.601 50.634  1.00 14.59 ? 160 SER D C   1 
ATOM   7644 O  O   . SER D 1 160 ? 13.863  -23.126 50.940  1.00 15.48 ? 160 SER D O   1 
ATOM   7645 C  CB  . SER D 1 160 ? 16.116  -24.371 49.243  1.00 14.86 ? 160 SER D CB  1 
ATOM   7646 O  OG  . SER D 1 160 ? 16.873  -24.609 50.442  1.00 16.43 ? 160 SER D OG  1 
ATOM   7647 N  N   . HIS D 1 161 ? 15.580  -21.734 51.451  1.00 13.22 ? 161 HIS D N   1 
ATOM   7648 C  CA  . HIS D 1 161 ? 15.054  -21.385 52.785  1.00 13.69 ? 161 HIS D CA  1 
ATOM   7649 C  C   . HIS D 1 161 ? 14.469  -19.966 52.858  1.00 13.02 ? 161 HIS D C   1 
ATOM   7650 O  O   . HIS D 1 161 ? 14.065  -19.516 53.929  1.00 12.69 ? 161 HIS D O   1 
ATOM   7651 C  CB  . HIS D 1 161 ? 16.161  -21.489 53.834  1.00 16.25 ? 161 HIS D CB  1 
ATOM   7652 C  CG  . HIS D 1 161 ? 16.841  -22.843 53.855  1.00 19.66 ? 161 HIS D CG  1 
ATOM   7653 N  ND1 . HIS D 1 161 ? 16.190  -23.977 54.212  1.00 23.40 ? 161 HIS D ND1 1 
ATOM   7654 C  CD2 . HIS D 1 161 ? 18.147  -23.223 53.539  1.00 21.62 ? 161 HIS D CD2 1 
ATOM   7655 C  CE1 . HIS D 1 161 ? 17.035  -25.030 54.106  1.00 24.38 ? 161 HIS D CE1 1 
ATOM   7656 N  NE2 . HIS D 1 161 ? 18.230  -24.568 53.702  1.00 22.23 ? 161 HIS D NE2 1 
ATOM   7657 N  N   . LEU D 1 162 ? 14.424  -19.280 51.742  1.00 11.89 ? 162 LEU D N   1 
ATOM   7658 C  CA  . LEU D 1 162 ? 14.050  -17.837 51.775  1.00 12.56 ? 162 LEU D CA  1 
ATOM   7659 C  C   . LEU D 1 162 ? 12.630  -17.558 52.192  1.00 12.09 ? 162 LEU D C   1 
ATOM   7660 O  O   . LEU D 1 162 ? 12.343  -16.493 52.732  1.00 11.68 ? 162 LEU D O   1 
ATOM   7661 C  CB  . LEU D 1 162 ? 14.329  -17.138 50.430  1.00 11.51 ? 162 LEU D CB  1 
ATOM   7662 C  CG  . LEU D 1 162 ? 15.756  -17.135 49.854  1.00 11.39 ? 162 LEU D CG  1 
ATOM   7663 C  CD1 . LEU D 1 162 ? 15.779  -16.672 48.377  1.00 12.80 ? 162 LEU D CD1 1 
ATOM   7664 C  CD2 . LEU D 1 162 ? 16.762  -16.353 50.740  1.00 12.09 ? 162 LEU D CD2 1 
ATOM   7665 N  N   . GLN D 1 163 ? 11.710  -18.474 51.917  1.00 12.20 ? 163 GLN D N   1 
ATOM   7666 C  CA  . GLN D 1 163 ? 10.324  -18.231 52.340  1.00 12.75 ? 163 GLN D CA  1 
ATOM   7667 C  C   . GLN D 1 163 ? 10.091  -18.229 53.862  1.00 13.28 ? 163 GLN D C   1 
ATOM   7668 O  O   . GLN D 1 163 ? 8.996   -17.880 54.357  1.00 12.85 ? 163 GLN D O   1 
ATOM   7669 C  CB  . GLN D 1 163 ? 9.301   -19.128 51.606  1.00 13.39 ? 163 GLN D CB  1 
ATOM   7670 C  CG  . GLN D 1 163 ? 9.483   -19.274 50.080  1.00 15.09 ? 163 GLN D CG  1 
ATOM   7671 C  CD  . GLN D 1 163 ? 9.446   -17.928 49.364  1.00 15.80 ? 163 GLN D CD  1 
ATOM   7672 O  OE1 . GLN D 1 163 ? 8.603   -17.075 49.679  1.00 16.64 ? 163 GLN D OE1 1 
ATOM   7673 N  NE2 . GLN D 1 163 ? 10.423  -17.709 48.461  1.00 17.07 ? 163 GLN D NE2 1 
ATOM   7674 N  N   . HIS D 1 164 ? 11.105  -18.618 54.632  1.00 13.95 ? 164 HIS D N   1 
ATOM   7675 C  CA  . HIS D 1 164 ? 10.992  -18.508 56.074  1.00 12.98 ? 164 HIS D CA  1 
ATOM   7676 C  C   . HIS D 1 164 ? 11.660  -17.293 56.620  1.00 13.49 ? 164 HIS D C   1 
ATOM   7677 O  O   . HIS D 1 164 ? 11.649  -17.091 57.823  1.00 13.87 ? 164 HIS D O   1 
ATOM   7678 C  CB  . HIS D 1 164 ? 11.655  -19.688 56.712  1.00 14.55 ? 164 HIS D CB  1 
ATOM   7679 C  CG  . HIS D 1 164 ? 11.106  -20.973 56.212  1.00 15.33 ? 164 HIS D CG  1 
ATOM   7680 N  ND1 . HIS D 1 164 ? 9.791   -21.281 56.340  1.00 15.47 ? 164 HIS D ND1 1 
ATOM   7681 C  CD2 . HIS D 1 164 ? 11.704  -22.007 55.495  1.00 16.78 ? 164 HIS D CD2 1 
ATOM   7682 C  CE1 . HIS D 1 164 ? 9.568   -22.501 55.765  1.00 15.62 ? 164 HIS D CE1 1 
ATOM   7683 N  NE2 . HIS D 1 164 ? 10.728  -22.927 55.218  1.00 17.60 ? 164 HIS D NE2 1 
ATOM   7684 N  N   . VAL D 1 165 ? 12.225  -16.466 55.768  1.00 13.44 ? 165 VAL D N   1 
ATOM   7685 C  CA  . VAL D 1 165 ? 12.831  -15.194 56.278  1.00 12.55 ? 165 VAL D CA  1 
ATOM   7686 C  C   . VAL D 1 165 ? 12.345  -13.987 55.466  1.00 12.18 ? 165 VAL D C   1 
ATOM   7687 O  O   . VAL D 1 165 ? 13.079  -13.025 55.189  1.00 11.53 ? 165 VAL D O   1 
ATOM   7688 C  CB  . VAL D 1 165 ? 14.376  -15.319 56.378  1.00 12.12 ? 165 VAL D CB  1 
ATOM   7689 C  CG1 . VAL D 1 165 ? 14.758  -16.418 57.392  1.00 13.15 ? 165 VAL D CG1 1 
ATOM   7690 C  CG2 . VAL D 1 165 ? 14.986  -15.662 55.013  1.00 13.49 ? 165 VAL D CG2 1 
ATOM   7691 N  N   . LYS D 1 166 ? 11.071  -14.033 55.079  1.00 12.40 ? 166 LYS D N   1 
ATOM   7692 C  CA  . LYS D 1 166 ? 10.486  -13.002 54.175  1.00 12.85 ? 166 LYS D CA  1 
ATOM   7693 C  C   . LYS D 1 166 ? 10.516  -11.592 54.727  1.00 12.20 ? 166 LYS D C   1 
ATOM   7694 O  O   . LYS D 1 166 ? 10.725  -10.641 53.953  1.00 11.96 ? 166 LYS D O   1 
ATOM   7695 C  CB  . LYS D 1 166 ? 9.037   -13.382 53.769  1.00 11.86 ? 166 LYS D CB  1 
ATOM   7696 C  CG  . LYS D 1 166 ? 8.979   -14.687 52.984  1.00 13.11 ? 166 LYS D CG  1 
ATOM   7697 C  CD  . LYS D 1 166 ? 7.562   -15.062 52.473  1.00 13.07 ? 166 LYS D CD  1 
ATOM   7698 C  CE  . LYS D 1 166 ? 7.010   -14.067 51.439  1.00 12.35 ? 166 LYS D CE  1 
ATOM   7699 N  NZ  . LYS D 1 166 ? 7.826   -14.214 50.158  1.00 14.67 ? 166 LYS D NZ  1 
ATOM   7700 N  N   . TYR D 1 167 ? 10.323  -11.428 56.057  1.00 12.18 ? 167 TYR D N   1 
ATOM   7701 C  CA  . TYR D 1 167 ? 10.189  -10.070 56.665  1.00 12.48 ? 167 TYR D CA  1 
ATOM   7702 C  C   . TYR D 1 167 ? 11.356  -9.724  57.609  1.00 13.85 ? 167 TYR D C   1 
ATOM   7703 O  O   . TYR D 1 167 ? 12.033  -10.631 58.119  1.00 13.46 ? 167 TYR D O   1 
ATOM   7704 C  CB  . TYR D 1 167 ? 8.821   -9.906  57.368  1.00 12.09 ? 167 TYR D CB  1 
ATOM   7705 C  CG  . TYR D 1 167 ? 7.721   -9.989  56.329  1.00 12.71 ? 167 TYR D CG  1 
ATOM   7706 C  CD1 . TYR D 1 167 ? 7.067   -11.198 56.049  1.00 13.44 ? 167 TYR D CD1 1 
ATOM   7707 C  CD2 . TYR D 1 167 ? 7.381   -8.862  55.586  1.00 12.27 ? 167 TYR D CD2 1 
ATOM   7708 C  CE1 . TYR D 1 167 ? 6.119   -11.267 55.031  1.00 14.09 ? 167 TYR D CE1 1 
ATOM   7709 C  CE2 . TYR D 1 167 ? 6.415   -8.921  54.599  1.00 14.20 ? 167 TYR D CE2 1 
ATOM   7710 C  CZ  . TYR D 1 167 ? 5.793   -10.131 54.342  1.00 14.67 ? 167 TYR D CZ  1 
ATOM   7711 O  OH  . TYR D 1 167 ? 4.885   -10.181 53.300  1.00 18.13 ? 167 TYR D OH  1 
ATOM   7712 N  N   . LYS D 1 168 ? 11.622  -8.419  57.802  1.00 13.01 ? 168 LYS D N   1 
ATOM   7713 C  CA  . LYS D 1 168 ? 12.702  -7.993  58.746  1.00 13.33 ? 168 LYS D CA  1 
ATOM   7714 C  C   . LYS D 1 168 ? 12.678  -8.663  60.133  1.00 14.71 ? 168 LYS D C   1 
ATOM   7715 O  O   . LYS D 1 168 ? 11.647  -8.701  60.785  1.00 14.71 ? 168 LYS D O   1 
ATOM   7716 C  CB  . LYS D 1 168 ? 12.675  -6.458  58.891  1.00 13.25 ? 168 LYS D CB  1 
ATOM   7717 C  CG  . LYS D 1 168 ? 13.771  -5.884  59.822  1.00 14.13 ? 168 LYS D CG  1 
ATOM   7718 C  CD  . LYS D 1 168 ? 13.876  -4.375  59.655  1.00 14.94 ? 168 LYS D CD  1 
ATOM   7719 C  CE  . LYS D 1 168 ? 14.887  -3.798  60.659  1.00 20.04 ? 168 LYS D CE  1 
ATOM   7720 N  NZ  . LYS D 1 168 ? 15.237  -2.410  60.243  1.00 20.59 ? 168 LYS D NZ  1 
ATOM   7721 N  N   . GLY D 1 169 ? 13.839  -9.116  60.619  1.00 15.07 ? 169 GLY D N   1 
ATOM   7722 C  CA  . GLY D 1 169 ? 13.927  -9.728  61.933  1.00 16.73 ? 169 GLY D CA  1 
ATOM   7723 C  C   . GLY D 1 169 ? 13.616  -11.213 61.963  1.00 16.34 ? 169 GLY D C   1 
ATOM   7724 O  O   . GLY D 1 169 ? 13.873  -11.868 62.991  1.00 17.15 ? 169 GLY D O   1 
ATOM   7725 N  N   . GLN D 1 170 ? 13.037  -11.762 60.881  1.00 15.79 ? 170 GLN D N   1 
ATOM   7726 C  CA  . GLN D 1 170 ? 12.778  -13.210 60.818  1.00 13.81 ? 170 GLN D CA  1 
ATOM   7727 C  C   . GLN D 1 170 ? 14.081  -14.032 60.570  1.00 15.47 ? 170 GLN D C   1 
ATOM   7728 O  O   . GLN D 1 170 ? 15.010  -13.548 59.925  1.00 14.00 ? 170 GLN D O   1 
ATOM   7729 C  CB  . GLN D 1 170 ? 11.703  -13.515 59.751  1.00 13.63 ? 170 GLN D CB  1 
ATOM   7730 C  CG  . GLN D 1 170 ? 10.307  -12.990 60.153  1.00 13.02 ? 170 GLN D CG  1 
ATOM   7731 C  CD  . GLN D 1 170 ? 9.231   -13.298 59.086  1.00 13.68 ? 170 GLN D CD  1 
ATOM   7732 O  OE1 . GLN D 1 170 ? 9.546   -13.632 57.930  1.00 13.87 ? 170 GLN D OE1 1 
ATOM   7733 N  NE2 . GLN D 1 170 ? 7.952   -13.091 59.458  1.00 14.88 ? 170 GLN D NE2 1 
ATOM   7734 N  N   . GLU D 1 171 ? 14.143  -15.249 61.117  1.00 14.89 ? 171 GLU D N   1 
ATOM   7735 C  CA  . GLU D 1 171 ? 15.392  -16.044 61.194  1.00 16.10 ? 171 GLU D CA  1 
ATOM   7736 C  C   . GLU D 1 171 ? 15.019  -17.492 60.989  1.00 16.00 ? 171 GLU D C   1 
ATOM   7737 O  O   . GLU D 1 171 ? 13.891  -17.868 61.262  1.00 16.10 ? 171 GLU D O   1 
ATOM   7738 C  CB  . GLU D 1 171 ? 16.083  -15.905 62.569  1.00 17.49 ? 171 GLU D CB  1 
ATOM   7739 C  CG  . GLU D 1 171 ? 16.412  -14.448 62.942  1.00 22.55 ? 171 GLU D CG  1 
ATOM   7740 C  CD  . GLU D 1 171 ? 16.891  -14.220 64.380  1.00 26.50 ? 171 GLU D CD  1 
ATOM   7741 O  OE1 . GLU D 1 171 ? 17.488  -13.141 64.626  1.00 32.53 ? 171 GLU D OE1 1 
ATOM   7742 O  OE2 . GLU D 1 171 ? 16.694  -15.083 65.258  1.00 23.24 ? 171 GLU D OE2 1 
ATOM   7743 N  N   . ALA D 1 172 ? 15.988  -18.294 60.532  1.00 15.18 ? 172 ALA D N   1 
ATOM   7744 C  CA  . ALA D 1 172 ? 15.838  -19.726 60.336  1.00 15.18 ? 172 ALA D CA  1 
ATOM   7745 C  C   . ALA D 1 172 ? 17.237  -20.359 60.329  1.00 16.26 ? 172 ALA D C   1 
ATOM   7746 O  O   . ALA D 1 172 ? 18.187  -19.805 59.770  1.00 15.50 ? 172 ALA D O   1 
ATOM   7747 C  CB  . ALA D 1 172 ? 15.044  -20.080 59.066  1.00 14.03 ? 172 ALA D CB  1 
ATOM   7748 N  N   . PHE D 1 173 ? 17.372  -21.499 60.999  1.00 18.31 ? 173 PHE D N   1 
ATOM   7749 C  CA  . PHE D 1 173 ? 18.679  -22.191 61.106  1.00 17.83 ? 173 PHE D CA  1 
ATOM   7750 C  C   . PHE D 1 173 ? 18.808  -23.083 59.903  1.00 19.85 ? 173 PHE D C   1 
ATOM   7751 O  O   . PHE D 1 173 ? 17.831  -23.748 59.541  1.00 22.51 ? 173 PHE D O   1 
ATOM   7752 C  CB  . PHE D 1 173 ? 18.842  -23.015 62.421  1.00 18.24 ? 173 PHE D CB  1 
ATOM   7753 C  CG  . PHE D 1 173 ? 19.259  -22.212 63.635  1.00 17.64 ? 173 PHE D CG  1 
ATOM   7754 C  CD1 . PHE D 1 173 ? 18.315  -21.916 64.644  1.00 17.38 ? 173 PHE D CD1 1 
ATOM   7755 C  CD2 . PHE D 1 173 ? 20.589  -21.801 63.815  1.00 17.51 ? 173 PHE D CD2 1 
ATOM   7756 C  CE1 . PHE D 1 173 ? 18.674  -21.202 65.781  1.00 19.90 ? 173 PHE D CE1 1 
ATOM   7757 C  CE2 . PHE D 1 173 ? 20.953  -21.095 64.960  1.00 19.09 ? 173 PHE D CE2 1 
ATOM   7758 C  CZ  . PHE D 1 173 ? 20.012  -20.789 65.943  1.00 19.55 ? 173 PHE D CZ  1 
ATOM   7759 N  N   . VAL D 1 174 ? 19.996  -23.079 59.282  1.00 19.23 ? 174 VAL D N   1 
ATOM   7760 C  CA  . VAL D 1 174 ? 20.307  -23.786 58.024  1.00 19.17 ? 174 VAL D CA  1 
ATOM   7761 C  C   . VAL D 1 174 ? 21.362  -24.794 58.445  1.00 18.20 ? 174 VAL D C   1 
ATOM   7762 O  O   . VAL D 1 174 ? 22.298  -24.390 59.153  1.00 18.21 ? 174 VAL D O   1 
ATOM   7763 C  CB  . VAL D 1 174 ? 20.985  -22.790 56.988  1.00 20.47 ? 174 VAL D CB  1 
ATOM   7764 C  CG1 . VAL D 1 174 ? 21.499  -23.521 55.766  1.00 21.06 ? 174 VAL D CG1 1 
ATOM   7765 C  CG2 . VAL D 1 174 ? 20.062  -21.654 56.560  1.00 25.54 ? 174 VAL D CG2 1 
ATOM   7766 N  N   . PRO D 1 175 ? 21.261  -26.084 58.041  1.00 17.55 ? 175 PRO D N   1 
ATOM   7767 C  CA  . PRO D 1 175 ? 22.444  -26.972 58.281  1.00 17.24 ? 175 PRO D CA  1 
ATOM   7768 C  C   . PRO D 1 175 ? 23.737  -26.611 57.500  1.00 16.99 ? 175 PRO D C   1 
ATOM   7769 O  O   . PRO D 1 175 ? 23.712  -26.055 56.377  1.00 17.57 ? 175 PRO D O   1 
ATOM   7770 C  CB  . PRO D 1 175 ? 21.956  -28.372 57.825  1.00 18.15 ? 175 PRO D CB  1 
ATOM   7771 C  CG  . PRO D 1 175 ? 20.486  -28.215 57.477  1.00 18.75 ? 175 PRO D CG  1 
ATOM   7772 C  CD  . PRO D 1 175 ? 20.252  -26.750 57.197  1.00 16.45 ? 175 PRO D CD  1 
ATOM   7773 N  N   . GLY D 1 176 ? 24.883  -26.916 58.102  1.00 17.20 ? 176 GLY D N   1 
ATOM   7774 C  CA  . GLY D 1 176 ? 26.159  -26.668 57.439  1.00 16.51 ? 176 GLY D CA  1 
ATOM   7775 C  C   . GLY D 1 176 ? 26.259  -27.258 56.043  1.00 13.79 ? 176 GLY D C   1 
ATOM   7776 O  O   . GLY D 1 176 ? 25.798  -28.408 55.792  1.00 13.49 ? 176 GLY D O   1 
ATOM   7777 N  N   . PHE D 1 177 ? 26.944  -26.531 55.162  1.00 13.41 ? 177 PHE D N   1 
ATOM   7778 C  CA  . PHE D 1 177 ? 27.363  -27.051 53.882  1.00 13.13 ? 177 PHE D CA  1 
ATOM   7779 C  C   . PHE D 1 177 ? 28.733  -26.447 53.521  1.00 12.92 ? 177 PHE D C   1 
ATOM   7780 O  O   . PHE D 1 177 ? 29.247  -25.619 54.291  1.00 12.05 ? 177 PHE D O   1 
ATOM   7781 C  CB  . PHE D 1 177 ? 26.262  -26.799 52.804  1.00 14.35 ? 177 PHE D CB  1 
ATOM   7782 C  CG  . PHE D 1 177 ? 26.043  -25.323 52.483  1.00 14.33 ? 177 PHE D CG  1 
ATOM   7783 C  CD1 . PHE D 1 177 ? 26.659  -24.754 51.371  1.00 15.87 ? 177 PHE D CD1 1 
ATOM   7784 C  CD2 . PHE D 1 177 ? 25.217  -24.554 53.250  1.00 14.90 ? 177 PHE D CD2 1 
ATOM   7785 C  CE1 . PHE D 1 177 ? 26.488  -23.400 51.075  1.00 14.70 ? 177 PHE D CE1 1 
ATOM   7786 C  CE2 . PHE D 1 177 ? 25.028  -23.193 52.978  1.00 14.84 ? 177 PHE D CE2 1 
ATOM   7787 C  CZ  . PHE D 1 177 ? 25.662  -22.639 51.886  1.00 14.25 ? 177 PHE D CZ  1 
ATOM   7788 N  N   . ASN D 1 178 ? 29.345  -26.949 52.451  1.00 12.58 ? 178 ASN D N   1 
ATOM   7789 C  CA  . ASN D 1 178 ? 30.679  -26.479 52.051  1.00 13.24 ? 178 ASN D CA  1 
ATOM   7790 C  C   . ASN D 1 178 ? 30.555  -25.112 51.354  1.00 12.70 ? 178 ASN D C   1 
ATOM   7791 O  O   . ASN D 1 178 ? 30.154  -25.050 50.199  1.00 12.05 ? 178 ASN D O   1 
ATOM   7792 C  CB  . ASN D 1 178 ? 31.358  -27.470 51.109  1.00 13.27 ? 178 ASN D CB  1 
ATOM   7793 C  CG  . ASN D 1 178 ? 32.809  -27.145 50.835  1.00 16.11 ? 178 ASN D CG  1 
ATOM   7794 O  OD1 . ASN D 1 178 ? 33.368  -26.138 51.331  1.00 15.17 ? 178 ASN D OD1 1 
ATOM   7795 N  ND2 . ASN D 1 178 ? 33.458  -28.034 50.064  1.00 17.41 ? 178 ASN D ND2 1 
ATOM   7796 N  N   A ILE D 1 179 ? 30.946  -24.046 52.053  0.50 12.24 ? 179 ILE D N   1 
ATOM   7797 N  N   B ILE D 1 179 ? 30.956  -24.055 52.067  0.50 11.81 ? 179 ILE D N   1 
ATOM   7798 C  CA  A ILE D 1 179 ? 30.928  -22.697 51.488  0.50 13.02 ? 179 ILE D CA  1 
ATOM   7799 C  CA  B ILE D 1 179 ? 30.924  -22.685 51.555  0.50 12.27 ? 179 ILE D CA  1 
ATOM   7800 C  C   A ILE D 1 179 ? 31.727  -22.537 50.196  0.50 13.15 ? 179 ILE D C   1 
ATOM   7801 C  C   B ILE D 1 179 ? 31.809  -22.443 50.302  0.50 12.77 ? 179 ILE D C   1 
ATOM   7802 O  O   A ILE D 1 179 ? 31.356  -21.752 49.306  0.50 13.61 ? 179 ILE D O   1 
ATOM   7803 O  O   B ILE D 1 179 ? 31.558  -21.515 49.525  0.50 13.57 ? 179 ILE D O   1 
ATOM   7804 C  CB  A ILE D 1 179 ? 31.424  -21.667 52.518  0.50 12.84 ? 179 ILE D CB  1 
ATOM   7805 C  CB  B ILE D 1 179 ? 31.192  -21.660 52.708  0.50 11.26 ? 179 ILE D CB  1 
ATOM   7806 C  CG1 A ILE D 1 179 ? 30.696  -21.832 53.846  0.50 12.85 ? 179 ILE D CG1 1 
ATOM   7807 C  CG1 B ILE D 1 179 ? 30.281  -21.925 53.930  0.50 10.83 ? 179 ILE D CG1 1 
ATOM   7808 C  CG2 A ILE D 1 179 ? 31.293  -20.243 51.963  0.50 12.81 ? 179 ILE D CG2 1 
ATOM   7809 C  CG2 B ILE D 1 179 ? 31.046  -20.222 52.210  0.50 11.60 ? 179 ILE D CG2 1 
ATOM   7810 C  CD1 A ILE D 1 179 ? 30.811  -20.590 54.686  0.50 14.55 ? 179 ILE D CD1 1 
ATOM   7811 C  CD1 B ILE D 1 179 ? 28.811  -21.539 53.740  0.50 10.62 ? 179 ILE D CD1 1 
ATOM   7812 N  N   . GLU D 1 180 ? 32.819  -23.297 50.077  1.00 13.52 ? 180 GLU D N   1 
ATOM   7813 C  CA  . GLU D 1 180 ? 33.710  -23.174 48.944  1.00 14.17 ? 180 GLU D CA  1 
ATOM   7814 C  C   . GLU D 1 180 ? 32.999  -23.534 47.635  1.00 13.63 ? 180 GLU D C   1 
ATOM   7815 O  O   . GLU D 1 180 ? 33.416  -23.115 46.561  1.00 12.80 ? 180 GLU D O   1 
ATOM   7816 C  CB  . GLU D 1 180 ? 34.966  -24.037 49.161  1.00 17.43 ? 180 GLU D CB  1 
ATOM   7817 C  CG  . GLU D 1 180 ? 36.173  -23.532 48.383  1.00 18.52 ? 180 GLU D CG  1 
ATOM   7818 C  CD  . GLU D 1 180 ? 37.395  -24.410 48.505  1.00 20.40 ? 180 GLU D CD  1 
ATOM   7819 O  OE1 . GLU D 1 180 ? 37.556  -25.092 49.571  1.00 19.58 ? 180 GLU D OE1 1 
ATOM   7820 O  OE2 . GLU D 1 180 ? 38.168  -24.390 47.510  1.00 22.77 ? 180 GLU D OE2 1 
ATOM   7821 N  N   . GLU D 1 181 ? 31.901  -24.273 47.734  1.00 13.14 ? 181 GLU D N   1 
ATOM   7822 C  CA  . GLU D 1 181 ? 31.047  -24.558 46.552  1.00 13.91 ? 181 GLU D CA  1 
ATOM   7823 C  C   . GLU D 1 181 ? 30.388  -23.268 45.934  1.00 13.82 ? 181 GLU D C   1 
ATOM   7824 O  O   . GLU D 1 181 ? 29.936  -23.296 44.804  1.00 12.31 ? 181 GLU D O   1 
ATOM   7825 C  CB  . GLU D 1 181 ? 29.914  -25.489 46.965  1.00 14.95 ? 181 GLU D CB  1 
ATOM   7826 C  CG  . GLU D 1 181 ? 30.239  -26.990 47.109  1.00 18.86 ? 181 GLU D CG  1 
ATOM   7827 C  CD  . GLU D 1 181 ? 29.102  -27.790 47.780  1.00 19.84 ? 181 GLU D CD  1 
ATOM   7828 O  OE1 . GLU D 1 181 ? 27.962  -27.282 47.932  1.00 21.29 ? 181 GLU D OE1 1 
ATOM   7829 O  OE2 . GLU D 1 181 ? 29.321  -28.942 48.212  1.00 21.69 ? 181 GLU D OE2 1 
ATOM   7830 N  N   . LEU D 1 182 ? 30.291  -22.175 46.701  1.00 13.18 ? 182 LEU D N   1 
ATOM   7831 C  CA  . LEU D 1 182 ? 29.754  -20.868 46.185  1.00 13.69 ? 182 LEU D CA  1 
ATOM   7832 C  C   . LEU D 1 182 ? 30.823  -20.059 45.441  1.00 16.23 ? 182 LEU D C   1 
ATOM   7833 O  O   . LEU D 1 182 ? 30.544  -18.990 44.852  1.00 14.21 ? 182 LEU D O   1 
ATOM   7834 C  CB  . LEU D 1 182 ? 29.183  -20.012 47.361  1.00 13.47 ? 182 LEU D CB  1 
ATOM   7835 C  CG  . LEU D 1 182 ? 28.210  -20.708 48.326  1.00 12.34 ? 182 LEU D CG  1 
ATOM   7836 C  CD1 . LEU D 1 182 ? 27.881  -19.736 49.476  1.00 12.15 ? 182 LEU D CD1 1 
ATOM   7837 C  CD2 . LEU D 1 182 ? 26.932  -21.214 47.599  1.00 13.20 ? 182 LEU D CD2 1 
ATOM   7838 N  N   . LEU D 1 183 ? 32.071  -20.555 45.473  1.00 15.70 ? 183 LEU D N   1 
ATOM   7839 C  CA  . LEU D 1 183 ? 33.189  -19.809 44.826  1.00 15.36 ? 183 LEU D CA  1 
ATOM   7840 C  C   . LEU D 1 183 ? 33.345  -20.151 43.344  1.00 14.65 ? 183 LEU D C   1 
ATOM   7841 O  O   . LEU D 1 183 ? 33.087  -21.279 42.966  1.00 15.82 ? 183 LEU D O   1 
ATOM   7842 C  CB  . LEU D 1 183 ? 34.540  -20.042 45.549  1.00 15.12 ? 183 LEU D CB  1 
ATOM   7843 C  CG  . LEU D 1 183 ? 34.593  -19.657 47.018  1.00 14.92 ? 183 LEU D CG  1 
ATOM   7844 C  CD1 . LEU D 1 183 ? 36.024  -19.837 47.581  1.00 14.46 ? 183 LEU D CD1 1 
ATOM   7845 C  CD2 . LEU D 1 183 ? 34.078  -18.229 47.304  1.00 14.26 ? 183 LEU D CD2 1 
ATOM   7846 N  N   . PRO D 1 184 ? 33.879  -19.221 42.534  1.00 13.72 ? 184 PRO D N   1 
ATOM   7847 C  CA  . PRO D 1 184 ? 33.986  -19.564 41.135  1.00 14.94 ? 184 PRO D CA  1 
ATOM   7848 C  C   . PRO D 1 184 ? 35.242  -20.362 40.839  1.00 17.62 ? 184 PRO D C   1 
ATOM   7849 O  O   . PRO D 1 184 ? 36.046  -20.686 41.778  1.00 16.77 ? 184 PRO D O   1 
ATOM   7850 C  CB  . PRO D 1 184 ? 34.046  -18.203 40.480  1.00 14.60 ? 184 PRO D CB  1 
ATOM   7851 C  CG  . PRO D 1 184 ? 34.877  -17.400 41.451  1.00 13.03 ? 184 PRO D CG  1 
ATOM   7852 C  CD  . PRO D 1 184 ? 34.322  -17.820 42.776  1.00 13.46 ? 184 PRO D CD  1 
ATOM   7853 N  N   . GLU D 1 185 ? 35.390  -20.682 39.553  1.00 20.87 ? 185 GLU D N   1 
ATOM   7854 C  CA  . GLU D 1 185 ? 36.618  -21.267 38.991  1.00 21.93 ? 185 GLU D CA  1 
ATOM   7855 C  C   . GLU D 1 185 ? 37.843  -20.321 39.147  1.00 22.86 ? 185 GLU D C   1 
ATOM   7856 O  O   . GLU D 1 185 ? 37.729  -19.060 39.142  1.00 22.54 ? 185 GLU D O   1 
ATOM   7857 C  CB  . GLU D 1 185 ? 36.419  -21.543 37.519  1.00 25.03 ? 185 GLU D CB  1 
ATOM   7858 C  CG  . GLU D 1 185 ? 35.667  -22.829 37.170  1.00 32.39 ? 185 GLU D CG  1 
ATOM   7859 C  CD  . GLU D 1 185 ? 35.794  -23.222 35.690  1.00 37.19 ? 185 GLU D CD  1 
ATOM   7860 O  OE1 . GLU D 1 185 ? 36.516  -22.530 34.923  1.00 44.65 ? 185 GLU D OE1 1 
ATOM   7861 O  OE2 . GLU D 1 185 ? 35.179  -24.244 35.277  1.00 41.82 ? 185 GLU D OE2 1 
ATOM   7862 N  N   . ARG D 1 186 ? 39.018  -20.942 39.283  1.00 20.86 ? 186 ARG D N   1 
ATOM   7863 C  CA  . ARG D 1 186 ? 40.284  -20.237 39.235  1.00 20.39 ? 186 ARG D CA  1 
ATOM   7864 C  C   . ARG D 1 186 ? 40.284  -19.031 40.221  1.00 20.78 ? 186 ARG D C   1 
ATOM   7865 O  O   . ARG D 1 186 ? 40.587  -17.858 39.834  1.00 23.43 ? 186 ARG D O   1 
ATOM   7866 C  CB  . ARG D 1 186 ? 40.646  -19.906 37.769  1.00 22.67 ? 186 ARG D CB  1 
ATOM   7867 C  CG  . ARG D 1 186 ? 40.972  -21.119 36.908  0.01 21.75 ? 186 ARG D CG  1 
ATOM   7868 C  CD  . ARG D 1 186 ? 41.448  -20.707 35.514  0.01 21.73 ? 186 ARG D CD  1 
ATOM   7869 N  NE  . ARG D 1 186 ? 40.382  -20.080 34.714  0.01 21.62 ? 186 ARG D NE  1 
ATOM   7870 C  CZ  . ARG D 1 186 ? 39.517  -20.755 33.948  0.01 21.56 ? 186 ARG D CZ  1 
ATOM   7871 N  NH1 . ARG D 1 186 ? 38.579  -20.101 33.254  0.01 21.48 ? 186 ARG D NH1 1 
ATOM   7872 N  NH2 . ARG D 1 186 ? 39.589  -22.083 33.875  0.01 21.56 ? 186 ARG D NH2 1 
ATOM   7873 N  N   . THR D 1 187 ? 39.993  -19.325 41.489  1.00 16.04 ? 187 THR D N   1 
ATOM   7874 C  CA  . THR D 1 187 ? 40.015  -18.262 42.520  1.00 16.84 ? 187 THR D CA  1 
ATOM   7875 C  C   . THR D 1 187 ? 41.383  -17.544 42.617  1.00 15.64 ? 187 THR D C   1 
ATOM   7876 O  O   . THR D 1 187 ? 41.455  -16.467 43.199  1.00 12.69 ? 187 THR D O   1 
ATOM   7877 C  CB  . THR D 1 187 ? 39.687  -18.763 43.944  1.00 16.14 ? 187 THR D CB  1 
ATOM   7878 O  OG1 . THR D 1 187 ? 40.501  -19.901 44.208  1.00 16.98 ? 187 THR D OG1 1 
ATOM   7879 C  CG2 . THR D 1 187 ? 38.102  -19.065 44.140  1.00 16.46 ? 187 THR D CG2 1 
ATOM   7880 N  N   . ALA D 1 188 ? 42.465  -18.150 42.074  1.00 13.97 ? 188 ALA D N   1 
ATOM   7881 C  CA  . ALA D 1 188 ? 43.775  -17.488 42.124  1.00 14.45 ? 188 ALA D CA  1 
ATOM   7882 C  C   . ALA D 1 188 ? 43.751  -16.147 41.348  1.00 13.61 ? 188 ALA D C   1 
ATOM   7883 O  O   . ALA D 1 188 ? 44.624  -15.322 41.562  1.00 13.67 ? 188 ALA D O   1 
ATOM   7884 C  CB  . ALA D 1 188 ? 44.863  -18.376 41.505  1.00 15.17 ? 188 ALA D CB  1 
ATOM   7885 N  N   . GLU D 1 189 ? 42.828  -16.010 40.402  1.00 12.99 ? 189 GLU D N   1 
ATOM   7886 C  CA  . GLU D 1 189 ? 42.688  -14.777 39.639  1.00 14.41 ? 189 GLU D CA  1 
ATOM   7887 C  C   . GLU D 1 189 ? 41.692  -13.818 40.244  1.00 12.30 ? 189 GLU D C   1 
ATOM   7888 O  O   . GLU D 1 189 ? 40.483  -14.117 40.290  1.00 12.98 ? 189 GLU D O   1 
ATOM   7889 C  CB  . GLU D 1 189 ? 42.287  -15.107 38.218  1.00 16.24 ? 189 GLU D CB  1 
ATOM   7890 C  CG  . GLU D 1 189 ? 43.300  -16.016 37.547  1.00 18.57 ? 189 GLU D CG  1 
ATOM   7891 C  CD  . GLU D 1 189 ? 42.917  -16.415 36.132  1.00 23.79 ? 189 GLU D CD  1 
ATOM   7892 O  OE1 . GLU D 1 189 ? 42.260  -15.626 35.436  1.00 23.76 ? 189 GLU D OE1 1 
ATOM   7893 O  OE2 . GLU D 1 189 ? 43.298  -17.535 35.689  1.00 27.37 ? 189 GLU D OE2 1 
ATOM   7894 N  N   . TYR D 1 190 ? 42.174  -12.655 40.661  1.00 11.46 ? 190 TYR D N   1 
ATOM   7895 C  CA  . TYR D 1 190 ? 41.283  -11.719 41.352  1.00 10.57 ? 190 TYR D CA  1 
ATOM   7896 C  C   . TYR D 1 190 ? 41.768  -10.258 41.237  1.00 10.59 ? 190 TYR D C   1 
ATOM   7897 O  O   . TYR D 1 190 ? 42.905  -10.007 40.803  1.00 10.57 ? 190 TYR D O   1 
ATOM   7898 C  CB  . TYR D 1 190 ? 41.139  -12.138 42.813  1.00 9.62  ? 190 TYR D CB  1 
ATOM   7899 C  CG  . TYR D 1 190 ? 42.436  -12.215 43.616  1.00 10.08 ? 190 TYR D CG  1 
ATOM   7900 C  CD1 . TYR D 1 190 ? 43.081  -11.064 44.069  1.00 9.57  ? 190 TYR D CD1 1 
ATOM   7901 C  CD2 . TYR D 1 190 ? 43.049  -13.466 43.885  1.00 11.02 ? 190 TYR D CD2 1 
ATOM   7902 C  CE1 . TYR D 1 190 ? 44.302  -11.125 44.800  1.00 9.88  ? 190 TYR D CE1 1 
ATOM   7903 C  CE2 . TYR D 1 190 ? 44.241  -13.516 44.642  1.00 10.37 ? 190 TYR D CE2 1 
ATOM   7904 C  CZ  . TYR D 1 190 ? 44.883  -12.343 45.055  1.00 10.36 ? 190 TYR D CZ  1 
ATOM   7905 O  OH  . TYR D 1 190 ? 46.058  -12.433 45.836  1.00 9.70  ? 190 TYR D OH  1 
ATOM   7906 N  N   . TYR D 1 191 ? 40.913  -9.332  41.685  1.00 11.66 ? 191 TYR D N   1 
ATOM   7907 C  CA  . TYR D 1 191 ? 41.197  -7.889  41.830  1.00 11.33 ? 191 TYR D CA  1 
ATOM   7908 C  C   . TYR D 1 191 ? 41.299  -7.616  43.320  1.00 11.23 ? 191 TYR D C   1 
ATOM   7909 O  O   . TYR D 1 191 ? 40.450  -8.098  44.114  1.00 11.34 ? 191 TYR D O   1 
ATOM   7910 C  CB  . TYR D 1 191 ? 39.999  -7.051  41.262  1.00 11.20 ? 191 TYR D CB  1 
ATOM   7911 C  CG  . TYR D 1 191 ? 39.566  -7.317  39.814  1.00 10.99 ? 191 TYR D CG  1 
ATOM   7912 C  CD1 . TYR D 1 191 ? 38.637  -8.312  39.517  1.00 12.40 ? 191 TYR D CD1 1 
ATOM   7913 C  CD2 . TYR D 1 191 ? 40.014  -6.508  38.750  1.00 11.37 ? 191 TYR D CD2 1 
ATOM   7914 C  CE1 . TYR D 1 191 ? 38.193  -8.509  38.213  1.00 12.25 ? 191 TYR D CE1 1 
ATOM   7915 C  CE2 . TYR D 1 191 ? 39.593  -6.720  37.430  1.00 12.28 ? 191 TYR D CE2 1 
ATOM   7916 C  CZ  . TYR D 1 191 ? 38.689  -7.741  37.196  1.00 12.78 ? 191 TYR D CZ  1 
ATOM   7917 O  OH  . TYR D 1 191 ? 38.246  -7.967  35.915  1.00 14.81 ? 191 TYR D OH  1 
ATOM   7918 N  N   . ARG D 1 192 ? 42.284  -6.796  43.751  1.00 10.49 ? 192 ARG D N   1 
ATOM   7919 C  CA  . ARG D 1 192 ? 42.427  -6.530  45.173  1.00 10.68 ? 192 ARG D CA  1 
ATOM   7920 C  C   . ARG D 1 192 ? 42.553  -4.998  45.404  1.00 10.41 ? 192 ARG D C   1 
ATOM   7921 O  O   . ARG D 1 192 ? 43.270  -4.342  44.675  1.00 10.23 ? 192 ARG D O   1 
ATOM   7922 C  CB  . ARG D 1 192 ? 43.647  -7.210  45.822  1.00 12.04 ? 192 ARG D CB  1 
ATOM   7923 C  CG  . ARG D 1 192 ? 43.653  -6.928  47.348  1.00 12.10 ? 192 ARG D CG  1 
ATOM   7924 C  CD  . ARG D 1 192 ? 44.228  -7.925  48.287  1.00 15.00 ? 192 ARG D CD  1 
ATOM   7925 N  NE  . ARG D 1 192 ? 43.606  -9.255  48.149  1.00 15.45 ? 192 ARG D NE  1 
ATOM   7926 C  CZ  . ARG D 1 192 ? 44.284  -10.378 48.317  1.00 17.54 ? 192 ARG D CZ  1 
ATOM   7927 N  NH1 . ARG D 1 192 ? 43.665  -11.574 48.210  1.00 17.53 ? 192 ARG D NH1 1 
ATOM   7928 N  NH2 . ARG D 1 192 ? 45.604  -10.321 48.612  1.00 19.68 ? 192 ARG D NH2 1 
ATOM   7929 N  N   . TYR D 1 193 ? 41.850  -4.439  46.397  1.00 9.91  ? 193 TYR D N   1 
ATOM   7930 C  CA  . TYR D 1 193 ? 42.044  -3.007  46.737  1.00 10.55 ? 193 TYR D CA  1 
ATOM   7931 C  C   . TYR D 1 193 ? 41.533  -2.726  48.162  1.00 10.98 ? 193 TYR D C   1 
ATOM   7932 O  O   . TYR D 1 193 ? 40.772  -3.528  48.726  1.00 11.37 ? 193 TYR D O   1 
ATOM   7933 C  CB  . TYR D 1 193 ? 41.332  -2.115  45.681  1.00 9.80  ? 193 TYR D CB  1 
ATOM   7934 C  CG  . TYR D 1 193 ? 39.802  -2.030  45.826  1.00 9.65  ? 193 TYR D CG  1 
ATOM   7935 C  CD1 . TYR D 1 193 ? 39.189  -0.896  46.371  1.00 9.50  ? 193 TYR D CD1 1 
ATOM   7936 C  CD2 . TYR D 1 193 ? 38.984  -3.104  45.412  1.00 9.44  ? 193 TYR D CD2 1 
ATOM   7937 C  CE1 . TYR D 1 193 ? 37.791  -0.836  46.566  1.00 9.78  ? 193 TYR D CE1 1 
ATOM   7938 C  CE2 . TYR D 1 193 ? 37.609  -3.051  45.541  1.00 10.09 ? 193 TYR D CE2 1 
ATOM   7939 C  CZ  . TYR D 1 193 ? 37.008  -1.935  46.137  1.00 9.93  ? 193 TYR D CZ  1 
ATOM   7940 O  OH  . TYR D 1 193 ? 35.649  -1.918  46.292  1.00 10.06 ? 193 TYR D OH  1 
ATOM   7941 N  N   A ARG D 1 194 ? 41.965  -1.626  48.739  0.50 10.69 ? 194 ARG D N   1 
ATOM   7942 N  N   B ARG D 1 194 ? 41.967  -1.592  48.715  0.50 11.42 ? 194 ARG D N   1 
ATOM   7943 C  CA  A ARG D 1 194 ? 41.434  -1.249  50.002  0.50 10.74 ? 194 ARG D CA  1 
ATOM   7944 C  CA  B ARG D 1 194 ? 41.589  -1.057  50.023  0.50 11.94 ? 194 ARG D CA  1 
ATOM   7945 C  C   A ARG D 1 194 ? 40.224  -0.374  49.805  0.50 10.69 ? 194 ARG D C   1 
ATOM   7946 C  C   B ARG D 1 194 ? 40.259  -0.277  49.876  0.50 11.50 ? 194 ARG D C   1 
ATOM   7947 O  O   A ARG D 1 194 ? 40.228  0.626   49.058  0.50 10.00 ? 194 ARG D O   1 
ATOM   7948 O  O   B ARG D 1 194 ? 40.205  0.752   49.180  0.50 10.73 ? 194 ARG D O   1 
ATOM   7949 C  CB  A ARG D 1 194 ? 42.510  -0.595  50.866  0.50 10.73 ? 194 ARG D CB  1 
ATOM   7950 C  CB  B ARG D 1 194 ? 42.797  -0.195  50.563  0.50 12.78 ? 194 ARG D CB  1 
ATOM   7951 C  CG  A ARG D 1 194 ? 43.693  -1.534  51.051  0.50 10.82 ? 194 ARG D CG  1 
ATOM   7952 C  CG  B ARG D 1 194 ? 42.635  0.687   51.821  0.50 15.08 ? 194 ARG D CG  1 
ATOM   7953 C  CD  A ARG D 1 194 ? 44.202  -1.537  52.474  0.50 12.29 ? 194 ARG D CD  1 
ATOM   7954 C  CD  B ARG D 1 194 ? 43.882  0.801   52.747  0.50 15.28 ? 194 ARG D CD  1 
ATOM   7955 N  NE  A ARG D 1 194 ? 43.112  -1.497  53.441  0.50 12.58 ? 194 ARG D NE  1 
ATOM   7956 N  NE  B ARG D 1 194 ? 44.719  1.970   52.454  0.50 15.78 ? 194 ARG D NE  1 
ATOM   7957 C  CZ  A ARG D 1 194 ? 42.758  -2.466  54.287  0.50 13.19 ? 194 ARG D CZ  1 
ATOM   7958 C  CZ  B ARG D 1 194 ? 44.621  3.158   53.036  0.50 17.58 ? 194 ARG D CZ  1 
ATOM   7959 N  NH1 A ARG D 1 194 ? 41.742  -2.235  55.110  0.50 12.42 ? 194 ARG D NH1 1 
ATOM   7960 N  NH1 B ARG D 1 194 ? 45.416  4.147   52.660  0.50 20.46 ? 194 ARG D NH1 1 
ATOM   7961 N  NH2 A ARG D 1 194 ? 43.439  -3.606  54.382  0.50 11.97 ? 194 ARG D NH2 1 
ATOM   7962 N  NH2 B ARG D 1 194 ? 43.732  3.383   53.999  0.50 18.66 ? 194 ARG D NH2 1 
ATOM   7963 N  N   . GLY D 1 195 ? 39.178  -0.763  50.504  1.00 10.83 ? 195 GLY D N   1 
ATOM   7964 C  CA  . GLY D 1 195 ? 37.919  0.022   50.494  1.00 10.51 ? 195 GLY D CA  1 
ATOM   7965 C  C   . GLY D 1 195 ? 37.165  -0.026  51.798  1.00 10.84 ? 195 GLY D C   1 
ATOM   7966 O  O   . GLY D 1 195 ? 37.764  -0.039  52.881  1.00 10.62 ? 195 GLY D O   1 
ATOM   7967 N  N   . SER D 1 196 ? 35.841  -0.007  51.690  1.00 9.35  ? 196 SER D N   1 
ATOM   7968 C  CA  . SER D 1 196 ? 34.951  0.217   52.833  1.00 8.69  ? 196 SER D CA  1 
ATOM   7969 C  C   . SER D 1 196 ? 33.813  -0.790  52.852  1.00 8.39  ? 196 SER D C   1 
ATOM   7970 O  O   . SER D 1 196 ? 33.651  -1.515  51.878  1.00 8.46  ? 196 SER D O   1 
ATOM   7971 C  CB  . SER D 1 196 ? 34.348  1.607   52.744  1.00 8.28  ? 196 SER D CB  1 
ATOM   7972 O  OG  . SER D 1 196 ? 33.349  1.580   51.686  1.00 8.82  ? 196 SER D OG  1 
ATOM   7973 N  N   . LEU D 1 197 ? 33.048  -0.869  53.963  1.00 8.21  ? 197 LEU D N   1 
ATOM   7974 C  CA  . LEU D 1 197 ? 31.744  -1.533  53.901  1.00 8.73  ? 197 LEU D CA  1 
ATOM   7975 C  C   . LEU D 1 197 ? 30.886  -0.762  52.871  1.00 7.91  ? 197 LEU D C   1 
ATOM   7976 O  O   . LEU D 1 197 ? 30.973  0.430   52.777  1.00 8.68  ? 197 LEU D O   1 
ATOM   7977 C  CB  . LEU D 1 197 ? 31.039  -1.466  55.279  1.00 9.26  ? 197 LEU D CB  1 
ATOM   7978 C  CG  . LEU D 1 197 ? 31.785  -2.168  56.414  1.00 9.85  ? 197 LEU D CG  1 
ATOM   7979 C  CD1 . LEU D 1 197 ? 31.098  -1.778  57.681  1.00 9.75  ? 197 LEU D CD1 1 
ATOM   7980 C  CD2 . LEU D 1 197 ? 31.765  -3.680  56.178  1.00 10.07 ? 197 LEU D CD2 1 
ATOM   7981 N  N   . THR D 1 198 ? 29.998  -1.413  52.135  1.00 7.80  ? 198 THR D N   1 
ATOM   7982 C  CA  . THR D 1 198 ? 29.232  -0.715  51.107  1.00 8.41  ? 198 THR D CA  1 
ATOM   7983 C  C   . THR D 1 198 ? 27.812  -0.295  51.616  1.00 9.05  ? 198 THR D C   1 
ATOM   7984 O  O   . THR D 1 198 ? 26.930  0.086   50.809  1.00 9.24  ? 198 THR D O   1 
ATOM   7985 C  CB  . THR D 1 198 ? 29.025  -1.649  49.924  1.00 8.67  ? 198 THR D CB  1 
ATOM   7986 O  OG1 . THR D 1 198 ? 28.277  -2.808  50.389  1.00 8.36  ? 198 THR D OG1 1 
ATOM   7987 C  CG2 . THR D 1 198 ? 30.410  -2.125  49.237  1.00 8.68  ? 198 THR D CG2 1 
ATOM   7988 N  N   . THR D 1 199 ? 27.573  -0.497  52.919  1.00 9.22  ? 199 THR D N   1 
ATOM   7989 C  CA  . THR D 1 199 ? 26.368  -0.006  53.610  1.00 9.80  ? 199 THR D CA  1 
ATOM   7990 C  C   . THR D 1 199 ? 26.792  0.726   54.850  1.00 10.62 ? 199 THR D C   1 
ATOM   7991 O  O   . THR D 1 199 ? 27.943  0.552   55.270  1.00 10.35 ? 199 THR D O   1 
ATOM   7992 C  CB  . THR D 1 199 ? 25.350  -1.092  54.068  1.00 10.44 ? 199 THR D CB  1 
ATOM   7993 O  OG1 . THR D 1 199 ? 25.810  -1.763  55.227  1.00 10.98 ? 199 THR D OG1 1 
ATOM   7994 C  CG2 . THR D 1 199 ? 25.061  -2.121  52.977  1.00 9.85  ? 199 THR D CG2 1 
ATOM   7995 N  N   . PRO D 1 200 ? 25.875  1.567   55.438  1.00 9.84  ? 200 PRO D N   1 
ATOM   7996 C  CA  . PRO D 1 200 ? 26.192  2.199   56.750  1.00 10.42 ? 200 PRO D CA  1 
ATOM   7997 C  C   . PRO D 1 200 ? 26.619  1.108   57.730  1.00 9.49  ? 200 PRO D C   1 
ATOM   7998 O  O   . PRO D 1 200 ? 26.044  0.011   57.707  1.00 8.58  ? 200 PRO D O   1 
ATOM   7999 C  CB  . PRO D 1 200 ? 24.840  2.833   57.187  1.00 9.65  ? 200 PRO D CB  1 
ATOM   8000 C  CG  . PRO D 1 200 ? 24.134  3.140   55.830  1.00 11.21 ? 200 PRO D CG  1 
ATOM   8001 C  CD  . PRO D 1 200 ? 24.554  1.976   54.922  1.00 10.65 ? 200 PRO D CD  1 
ATOM   8002 N  N   . PRO D 1 201 ? 27.620  1.384   58.587  1.00 9.27  ? 201 PRO D N   1 
ATOM   8003 C  CA  . PRO D 1 201 ? 28.285  2.675   58.710  1.00 9.66  ? 201 PRO D CA  1 
ATOM   8004 C  C   . PRO D 1 201 ? 29.407  3.035   57.700  1.00 9.77  ? 201 PRO D C   1 
ATOM   8005 O  O   . PRO D 1 201 ? 30.049  4.104   57.890  1.00 10.62 ? 201 PRO D O   1 
ATOM   8006 C  CB  . PRO D 1 201 ? 28.822  2.644   60.175  1.00 9.94  ? 201 PRO D CB  1 
ATOM   8007 C  CG  . PRO D 1 201 ? 29.134  1.199   60.360  1.00 10.89 ? 201 PRO D CG  1 
ATOM   8008 C  CD  . PRO D 1 201 ? 27.892  0.528   59.744  1.00 10.63 ? 201 PRO D CD  1 
ATOM   8009 N  N   . CYS D 1 202 ? 29.631  2.196   56.661  1.00 10.06 ? 202 CYS D N   1 
ATOM   8010 C  CA  . CYS D 1 202 ? 30.578  2.486   55.555  1.00 10.16 ? 202 CYS D CA  1 
ATOM   8011 C  C   . CYS D 1 202 ? 32.042  2.536   56.040  1.00 9.65  ? 202 CYS D C   1 
ATOM   8012 O  O   . CYS D 1 202 ? 32.826  3.334   55.500  1.00 9.27  ? 202 CYS D O   1 
ATOM   8013 C  CB  . CYS D 1 202 ? 30.260  3.887   54.929  1.00 9.11  ? 202 CYS D CB  1 
ATOM   8014 S  SG  . CYS D 1 202 ? 28.572  3.874   54.127  1.00 9.82  ? 202 CYS D SG  1 
ATOM   8015 N  N   . ASN D 1 203 ? 32.390  1.806   57.123  1.00 10.22 ? 203 ASN D N   1 
ATOM   8016 C  CA  . ASN D 1 203 ? 33.751  1.998   57.721  1.00 10.22 ? 203 ASN D CA  1 
ATOM   8017 C  C   . ASN D 1 203 ? 34.806  1.677   56.632  1.00 10.47 ? 203 ASN D C   1 
ATOM   8018 O  O   . ASN D 1 203 ? 34.675  0.657   55.926  1.00 9.32  ? 203 ASN D O   1 
ATOM   8019 C  CB  . ASN D 1 203 ? 34.022  1.005   58.876  1.00 10.68 ? 203 ASN D CB  1 
ATOM   8020 C  CG  . ASN D 1 203 ? 33.091  1.242   60.065  1.00 11.33 ? 203 ASN D CG  1 
ATOM   8021 O  OD1 . ASN D 1 203 ? 32.754  2.388   60.354  1.00 12.13 ? 203 ASN D OD1 1 
ATOM   8022 N  ND2 . ASN D 1 203 ? 32.632  0.158   60.714  1.00 12.95 ? 203 ASN D ND2 1 
ATOM   8023 N  N   . PRO D 1 204 ? 35.873  2.501   56.542  1.00 10.04 ? 204 PRO D N   1 
ATOM   8024 C  CA  . PRO D 1 204 ? 36.889  2.356   55.448  1.00 9.69  ? 204 PRO D CA  1 
ATOM   8025 C  C   . PRO D 1 204 ? 37.950  1.333   55.874  1.00 10.18 ? 204 PRO D C   1 
ATOM   8026 O  O   . PRO D 1 204 ? 39.152  1.602   55.946  1.00 11.27 ? 204 PRO D O   1 
ATOM   8027 C  CB  . PRO D 1 204 ? 37.398  3.811   55.299  1.00 9.65  ? 204 PRO D CB  1 
ATOM   8028 C  CG  . PRO D 1 204 ? 37.352  4.297   56.697  1.00 10.22 ? 204 PRO D CG  1 
ATOM   8029 C  CD  . PRO D 1 204 ? 36.030  3.790   57.234  1.00 10.40 ? 204 PRO D CD  1 
ATOM   8030 N  N   . THR D 1 205 ? 37.488  0.145   56.206  1.00 11.32 ? 205 THR D N   1 
ATOM   8031 C  CA  . THR D 1 205 ? 38.327  -0.860  56.888  1.00 10.83 ? 205 THR D CA  1 
ATOM   8032 C  C   . THR D 1 205 ? 38.446  -2.164  56.193  1.00 10.42 ? 205 THR D C   1 
ATOM   8033 O  O   . THR D 1 205 ? 38.924  -3.117  56.804  1.00 11.31 ? 205 THR D O   1 
ATOM   8034 C  CB  . THR D 1 205 ? 37.803  -1.139  58.290  1.00 12.38 ? 205 THR D CB  1 
ATOM   8035 O  OG1 . THR D 1 205 ? 36.415  -1.471  58.203  1.00 10.91 ? 205 THR D OG1 1 
ATOM   8036 C  CG2 . THR D 1 205 ? 38.008  0.056   59.093  1.00 12.39 ? 205 THR D CG2 1 
ATOM   8037 N  N   . VAL D 1 206 ? 38.002  -2.226  54.932  1.00 9.98  ? 206 VAL D N   1 
ATOM   8038 C  CA  . VAL D 1 206 ? 37.884  -3.525  54.248  1.00 9.37  ? 206 VAL D CA  1 
ATOM   8039 C  C   . VAL D 1 206 ? 38.985  -3.758  53.196  1.00 8.79  ? 206 VAL D C   1 
ATOM   8040 O  O   . VAL D 1 206 ? 39.173  -2.970  52.265  1.00 8.91  ? 206 VAL D O   1 
ATOM   8041 C  CB  . VAL D 1 206 ? 36.480  -3.657  53.506  1.00 8.20  ? 206 VAL D CB  1 
ATOM   8042 C  CG1 . VAL D 1 206 ? 36.401  -5.012  52.827  1.00 8.39  ? 206 VAL D CG1 1 
ATOM   8043 C  CG2 . VAL D 1 206 ? 35.306  -3.425  54.469  1.00 9.32  ? 206 VAL D CG2 1 
ATOM   8044 N  N   A LEU D 1 207 ? 39.652  -4.896  53.296  0.50 8.76  ? 207 LEU D N   1 
ATOM   8045 N  N   B LEU D 1 207 ? 39.716  -4.851  53.321  0.50 9.09  ? 207 LEU D N   1 
ATOM   8046 C  CA  A LEU D 1 207 ? 40.507  -5.402  52.205  0.50 8.23  ? 207 LEU D CA  1 
ATOM   8047 C  CA  B LEU D 1 207 ? 40.481  -5.329  52.164  0.50 8.69  ? 207 LEU D CA  1 
ATOM   8048 C  C   A LEU D 1 207 ? 39.623  -6.225  51.255  0.50 8.29  ? 207 LEU D C   1 
ATOM   8049 C  C   B LEU D 1 207 ? 39.492  -6.124  51.324  0.50 8.56  ? 207 LEU D C   1 
ATOM   8050 O  O   A LEU D 1 207 ? 39.291  -7.360  51.590  0.50 7.96  ? 207 LEU D O   1 
ATOM   8051 O  O   B LEU D 1 207 ? 38.961  -7.127  51.808  0.50 8.25  ? 207 LEU D O   1 
ATOM   8052 C  CB  A LEU D 1 207 ? 41.571  -6.328  52.799  0.50 8.00  ? 207 LEU D CB  1 
ATOM   8053 C  CB  B LEU D 1 207 ? 41.625  -6.253  52.577  0.50 8.96  ? 207 LEU D CB  1 
ATOM   8054 C  CG  A LEU D 1 207 ? 42.850  -6.670  52.021  0.50 7.99  ? 207 LEU D CG  1 
ATOM   8055 C  CG  B LEU D 1 207 ? 42.533  -6.627  51.383  0.50 9.40  ? 207 LEU D CG  1 
ATOM   8056 C  CD1 A LEU D 1 207 ? 43.354  -5.491  51.168  0.50 7.85  ? 207 LEU D CD1 1 
ATOM   8057 C  CD1 B LEU D 1 207 ? 44.001  -6.409  51.715  0.50 9.88  ? 207 LEU D CD1 1 
ATOM   8058 C  CD2 A LEU D 1 207 ? 43.920  -7.185  52.983  0.50 7.94  ? 207 LEU D CD2 1 
ATOM   8059 C  CD2 B LEU D 1 207 ? 42.245  -8.041  50.893  0.50 9.28  ? 207 LEU D CD2 1 
ATOM   8060 N  N   . TRP D 1 208 ? 39.276  -5.664  50.088  1.00 8.15  ? 208 TRP D N   1 
ATOM   8061 C  CA  . TRP D 1 208 ? 38.435  -6.376  49.112  1.00 8.54  ? 208 TRP D CA  1 
ATOM   8062 C  C   . TRP D 1 208 ? 39.229  -7.302  48.222  1.00 8.70  ? 208 TRP D C   1 
ATOM   8063 O  O   . TRP D 1 208 ? 40.235  -6.891  47.665  1.00 8.92  ? 208 TRP D O   1 
ATOM   8064 C  CB  . TRP D 1 208 ? 37.719  -5.375  48.212  1.00 8.98  ? 208 TRP D CB  1 
ATOM   8065 C  CG  . TRP D 1 208 ? 36.564  -4.706  48.924  1.00 8.67  ? 208 TRP D CG  1 
ATOM   8066 C  CD1 . TRP D 1 208 ? 36.542  -3.477  49.569  1.00 8.81  ? 208 TRP D CD1 1 
ATOM   8067 C  CD2 . TRP D 1 208 ? 35.238  -5.248  49.028  1.00 8.67  ? 208 TRP D CD2 1 
ATOM   8068 N  NE1 . TRP D 1 208 ? 35.323  -3.251  50.146  1.00 8.53  ? 208 TRP D NE1 1 
ATOM   8069 C  CE2 . TRP D 1 208 ? 34.468  -4.295  49.821  1.00 8.99  ? 208 TRP D CE2 1 
ATOM   8070 C  CE3 . TRP D 1 208 ? 34.602  -6.441  48.554  1.00 9.09  ? 208 TRP D CE3 1 
ATOM   8071 C  CZ2 . TRP D 1 208 ? 33.120  -4.468  50.066  1.00 8.90  ? 208 TRP D CZ2 1 
ATOM   8072 C  CZ3 . TRP D 1 208 ? 33.256  -6.610  48.848  1.00 8.67  ? 208 TRP D CZ3 1 
ATOM   8073 C  CH2 . TRP D 1 208 ? 32.543  -5.669  49.663  1.00 8.86  ? 208 TRP D CH2 1 
ATOM   8074 N  N   . THR D 1 209 ? 38.671  -8.504  47.975  1.00 9.13  ? 209 THR D N   1 
ATOM   8075 C  CA  . THR D 1 209 ? 39.108  -9.416  46.947  1.00 8.80  ? 209 THR D CA  1 
ATOM   8076 C  C   . THR D 1 209 ? 37.843  -9.756  46.084  1.00 8.63  ? 209 THR D C   1 
ATOM   8077 O  O   . THR D 1 209 ? 36.962  -10.456 46.556  1.00 9.34  ? 209 THR D O   1 
ATOM   8078 C  CB  . THR D 1 209 ? 39.686  -10.683 47.615  1.00 9.54  ? 209 THR D CB  1 
ATOM   8079 O  OG1 . THR D 1 209 ? 40.861  -10.282 48.360  1.00 10.29 ? 209 THR D OG1 1 
ATOM   8080 C  CG2 . THR D 1 209 ? 40.077  -11.775 46.545  1.00 9.59  ? 209 THR D CG2 1 
ATOM   8081 N  N   . VAL D 1 210 ? 37.819  -9.279  44.843  1.00 8.68  ? 210 VAL D N   1 
ATOM   8082 C  CA  . VAL D 1 210 ? 36.769  -9.651  43.851  1.00 8.76  ? 210 VAL D CA  1 
ATOM   8083 C  C   . VAL D 1 210 ? 37.326  -10.685 42.893  1.00 9.24  ? 210 VAL D C   1 
ATOM   8084 O  O   . VAL D 1 210 ? 38.265  -10.421 42.130  1.00 10.02 ? 210 VAL D O   1 
ATOM   8085 C  CB  . VAL D 1 210 ? 36.299  -8.396  43.099  1.00 8.56  ? 210 VAL D CB  1 
ATOM   8086 C  CG1 . VAL D 1 210 ? 35.125  -8.709  42.155  1.00 7.58  ? 210 VAL D CG1 1 
ATOM   8087 C  CG2 . VAL D 1 210 ? 35.934  -7.278  44.075  1.00 8.32  ? 210 VAL D CG2 1 
ATOM   8088 N  N   . PHE D 1 211 ? 36.715  -11.875 42.838  1.00 10.32 ? 211 PHE D N   1 
ATOM   8089 C  CA  . PHE D 1 211 ? 37.248  -12.862 41.920  1.00 10.49 ? 211 PHE D CA  1 
ATOM   8090 C  C   . PHE D 1 211 ? 36.960  -12.508 40.472  1.00 10.31 ? 211 PHE D C   1 
ATOM   8091 O  O   . PHE D 1 211 ? 35.930  -11.913 40.147  1.00 10.69 ? 211 PHE D O   1 
ATOM   8092 C  CB  . PHE D 1 211 ? 36.710  -14.305 42.242  1.00 9.85  ? 211 PHE D CB  1 
ATOM   8093 C  CG  . PHE D 1 211 ? 37.105  -14.773 43.596  1.00 9.98  ? 211 PHE D CG  1 
ATOM   8094 C  CD1 . PHE D 1 211 ? 36.170  -14.757 44.672  1.00 9.76  ? 211 PHE D CD1 1 
ATOM   8095 C  CD2 . PHE D 1 211 ? 38.439  -15.172 43.859  1.00 10.31 ? 211 PHE D CD2 1 
ATOM   8096 C  CE1 . PHE D 1 211 ? 36.566  -15.132 45.966  1.00 10.41 ? 211 PHE D CE1 1 
ATOM   8097 C  CE2 . PHE D 1 211 ? 38.809  -15.480 45.153  1.00 10.06 ? 211 PHE D CE2 1 
ATOM   8098 C  CZ  . PHE D 1 211 ? 37.878  -15.496 46.203  1.00 9.95  ? 211 PHE D CZ  1 
ATOM   8099 N  N   . ARG D 1 212 ? 37.902  -12.849 39.601  1.00 10.02 ? 212 ARG D N   1 
ATOM   8100 C  CA  . ARG D 1 212 ? 37.804  -12.506 38.202  1.00 10.71 ? 212 ARG D CA  1 
ATOM   8101 C  C   . ARG D 1 212 ? 36.609  -13.131 37.504  1.00 10.47 ? 212 ARG D C   1 
ATOM   8102 O  O   . ARG D 1 212 ? 35.996  -12.515 36.634  1.00 11.36 ? 212 ARG D O   1 
ATOM   8103 C  CB  . ARG D 1 212 ? 39.078  -12.934 37.467  1.00 10.45 ? 212 ARG D CB  1 
ATOM   8104 C  CG  . ARG D 1 212 ? 39.154  -12.434 36.022  1.00 12.89 ? 212 ARG D CG  1 
ATOM   8105 C  CD  . ARG D 1 212 ? 40.269  -13.124 35.235  1.00 13.33 ? 212 ARG D CD  1 
ATOM   8106 N  NE  . ARG D 1 212 ? 40.543  -12.406 33.977  1.00 15.07 ? 212 ARG D NE  1 
ATOM   8107 C  CZ  . ARG D 1 212 ? 41.578  -12.670 33.160  1.00 16.47 ? 212 ARG D CZ  1 
ATOM   8108 N  NH1 . ARG D 1 212 ? 42.470  -13.642 33.440  1.00 16.92 ? 212 ARG D NH1 1 
ATOM   8109 N  NH2 . ARG D 1 212 ? 41.735  -11.929 32.049  1.00 17.11 ? 212 ARG D NH2 1 
ATOM   8110 N  N   . ASN D 1 213 ? 36.358  -14.391 37.821  1.00 11.39 ? 213 ASN D N   1 
ATOM   8111 C  CA  . ASN D 1 213 ? 35.363  -15.172 37.071  1.00 12.92 ? 213 ASN D CA  1 
ATOM   8112 C  C   . ASN D 1 213 ? 34.042  -15.215 37.854  1.00 13.18 ? 213 ASN D C   1 
ATOM   8113 O  O   . ASN D 1 213 ? 34.053  -15.328 39.096  1.00 13.09 ? 213 ASN D O   1 
ATOM   8114 C  CB  . ASN D 1 213 ? 35.908  -16.596 36.887  1.00 15.63 ? 213 ASN D CB  1 
ATOM   8115 C  CG  . ASN D 1 213 ? 37.122  -16.672 35.913  1.00 18.26 ? 213 ASN D CG  1 
ATOM   8116 O  OD1 . ASN D 1 213 ? 37.216  -15.945 34.925  1.00 21.11 ? 213 ASN D OD1 1 
ATOM   8117 N  ND2 . ASN D 1 213 ? 37.986  -17.620 36.156  1.00 18.43 ? 213 ASN D ND2 1 
ATOM   8118 N  N   . PRO D 1 214 ? 32.895  -15.160 37.137  1.00 12.25 ? 214 PRO D N   1 
ATOM   8119 C  CA  . PRO D 1 214 ? 31.596  -15.196 37.733  1.00 12.21 ? 214 PRO D CA  1 
ATOM   8120 C  C   . PRO D 1 214 ? 31.115  -16.642 37.995  1.00 12.32 ? 214 PRO D C   1 
ATOM   8121 O  O   . PRO D 1 214 ? 31.679  -17.617 37.407  1.00 13.05 ? 214 PRO D O   1 
ATOM   8122 C  CB  . PRO D 1 214 ? 30.698  -14.558 36.640  1.00 13.07 ? 214 PRO D CB  1 
ATOM   8123 C  CG  . PRO D 1 214 ? 31.354  -14.992 35.373  1.00 13.01 ? 214 PRO D CG  1 
ATOM   8124 C  CD  . PRO D 1 214 ? 32.829  -14.926 35.687  1.00 12.66 ? 214 PRO D CD  1 
ATOM   8125 N  N   . VAL D 1 215 ? 30.101  -16.772 38.844  1.00 10.24 ? 215 VAL D N   1 
ATOM   8126 C  CA  . VAL D 1 215 ? 29.367  -18.058 38.926  1.00 11.04 ? 215 VAL D CA  1 
ATOM   8127 C  C   . VAL D 1 215 ? 28.028  -17.901 38.166  1.00 10.79 ? 215 VAL D C   1 
ATOM   8128 O  O   . VAL D 1 215 ? 27.593  -16.782 37.962  1.00 11.36 ? 215 VAL D O   1 
ATOM   8129 C  CB  . VAL D 1 215 ? 29.165  -18.553 40.371  1.00 9.83  ? 215 VAL D CB  1 
ATOM   8130 C  CG1 . VAL D 1 215 ? 30.515  -18.800 41.082  1.00 10.38 ? 215 VAL D CG1 1 
ATOM   8131 C  CG2 . VAL D 1 215 ? 28.240  -17.615 41.159  1.00 8.95  ? 215 VAL D CG2 1 
ATOM   8132 N  N   . GLN D 1 216 ? 27.352  -19.002 37.847  1.00 12.23 ? 216 GLN D N   1 
ATOM   8133 C  CA  . GLN D 1 216 ? 25.998  -18.942 37.215  1.00 13.61 ? 216 GLN D CA  1 
ATOM   8134 C  C   . GLN D 1 216 ? 24.904  -19.414 38.174  1.00 13.91 ? 216 GLN D C   1 
ATOM   8135 O  O   . GLN D 1 216 ? 25.124  -20.378 38.903  1.00 14.04 ? 216 GLN D O   1 
ATOM   8136 C  CB  . GLN D 1 216 ? 25.967  -19.868 35.997  1.00 15.63 ? 216 GLN D CB  1 
ATOM   8137 C  CG  . GLN D 1 216 ? 26.726  -19.301 34.804  1.00 18.93 ? 216 GLN D CG  1 
ATOM   8138 C  CD  . GLN D 1 216 ? 26.804  -20.262 33.607  1.00 22.13 ? 216 GLN D CD  1 
ATOM   8139 O  OE1 . GLN D 1 216 ? 25.932  -21.160 33.384  1.00 22.78 ? 216 GLN D OE1 1 
ATOM   8140 N  NE2 . GLN D 1 216 ? 27.864  -20.093 32.814  1.00 24.10 ? 216 GLN D NE2 1 
ATOM   8141 N  N   . ILE D 1 217 ? 23.749  -18.738 38.211  1.00 13.40 ? 217 ILE D N   1 
ATOM   8142 C  CA  . ILE D 1 217 ? 22.545  -19.288 38.845  1.00 12.68 ? 217 ILE D CA  1 
ATOM   8143 C  C   . ILE D 1 217 ? 21.420  -19.229 37.796  1.00 13.35 ? 217 ILE D C   1 
ATOM   8144 O  O   . ILE D 1 217 ? 21.542  -18.454 36.868  1.00 14.35 ? 217 ILE D O   1 
ATOM   8145 C  CB  . ILE D 1 217 ? 22.122  -18.561 40.127  1.00 12.55 ? 217 ILE D CB  1 
ATOM   8146 C  CG1 . ILE D 1 217 ? 21.766  -17.050 39.868  1.00 12.05 ? 217 ILE D CG1 1 
ATOM   8147 C  CG2 . ILE D 1 217 ? 23.214  -18.687 41.183  1.00 12.09 ? 217 ILE D CG2 1 
ATOM   8148 C  CD1 . ILE D 1 217 ? 21.090  -16.392 41.077  1.00 11.78 ? 217 ILE D CD1 1 
ATOM   8149 N  N   . SER D 1 218 ? 20.365  -20.047 37.883  1.00 14.28 ? 218 SER D N   1 
ATOM   8150 C  CA  . SER D 1 218 ? 19.352  -20.014 36.814  1.00 15.41 ? 218 SER D CA  1 
ATOM   8151 C  C   . SER D 1 218 ? 18.458  -18.745 36.776  1.00 15.70 ? 218 SER D C   1 
ATOM   8152 O  O   . SER D 1 218 ? 18.298  -18.042 37.761  1.00 14.39 ? 218 SER D O   1 
ATOM   8153 C  CB  . SER D 1 218 ? 18.432  -21.237 36.923  1.00 13.80 ? 218 SER D CB  1 
ATOM   8154 O  OG  . SER D 1 218 ? 17.483  -21.130 38.008  1.00 15.61 ? 218 SER D OG  1 
ATOM   8155 N  N   . GLN D 1 219 ? 17.793  -18.494 35.649  1.00 16.02 ? 219 GLN D N   1 
ATOM   8156 C  CA  . GLN D 1 219 ? 16.770  -17.414 35.631  1.00 17.43 ? 219 GLN D CA  1 
ATOM   8157 C  C   . GLN D 1 219 ? 15.755  -17.528 36.807  1.00 16.31 ? 219 GLN D C   1 
ATOM   8158 O  O   . GLN D 1 219 ? 15.363  -16.528 37.399  1.00 15.69 ? 219 GLN D O   1 
ATOM   8159 C  CB  . GLN D 1 219 ? 16.047  -17.433 34.257  1.00 19.56 ? 219 GLN D CB  1 
ATOM   8160 C  CG  . GLN D 1 219 ? 14.681  -16.789 34.194  1.00 27.23 ? 219 GLN D CG  1 
ATOM   8161 C  CD  . GLN D 1 219 ? 14.070  -16.831 32.780  1.00 30.52 ? 219 GLN D CD  1 
ATOM   8162 O  OE1 . GLN D 1 219 ? 14.591  -17.499 31.868  1.00 33.88 ? 219 GLN D OE1 1 
ATOM   8163 N  NE2 . GLN D 1 219 ? 12.997  -16.079 32.582  1.00 32.46 ? 219 GLN D NE2 1 
ATOM   8164 N  N   . GLU D 1 220 ? 15.313  -18.743 37.118  1.00 17.18 ? 220 GLU D N   1 
ATOM   8165 C  CA  . GLU D 1 220 ? 14.329  -18.944 38.150  1.00 17.36 ? 220 GLU D CA  1 
ATOM   8166 C  C   . GLU D 1 220 ? 14.897  -18.661 39.540  1.00 15.99 ? 220 GLU D C   1 
ATOM   8167 O  O   . GLU D 1 220 ? 14.183  -18.138 40.405  1.00 15.79 ? 220 GLU D O   1 
ATOM   8168 C  CB  . GLU D 1 220 ? 13.768  -20.379 38.114  1.00 20.58 ? 220 GLU D CB  1 
ATOM   8169 C  CG  . GLU D 1 220 ? 12.828  -20.661 36.919  1.00 23.71 ? 220 GLU D CG  1 
ATOM   8170 C  CD  . GLU D 1 220 ? 13.587  -21.067 35.646  1.00 26.48 ? 220 GLU D CD  1 
ATOM   8171 O  OE1 . GLU D 1 220 ? 14.865  -21.127 35.602  1.00 23.78 ? 220 GLU D OE1 1 
ATOM   8172 O  OE2 . GLU D 1 220 ? 12.887  -21.330 34.638  1.00 30.86 ? 220 GLU D OE2 1 
ATOM   8173 N  N   . GLN D 1 221 ? 16.150  -19.043 39.762  1.00 13.99 ? 221 GLN D N   1 
ATOM   8174 C  CA  . GLN D 1 221 ? 16.817  -18.794 41.041  1.00 12.63 ? 221 GLN D CA  1 
ATOM   8175 C  C   . GLN D 1 221 ? 17.004  -17.304 41.221  1.00 11.05 ? 221 GLN D C   1 
ATOM   8176 O  O   . GLN D 1 221 ? 16.779  -16.822 42.299  1.00 9.78  ? 221 GLN D O   1 
ATOM   8177 C  CB  . GLN D 1 221 ? 18.198  -19.482 41.098  1.00 12.61 ? 221 GLN D CB  1 
ATOM   8178 C  CG  . GLN D 1 221 ? 18.155  -20.971 41.459  1.00 11.79 ? 221 GLN D CG  1 
ATOM   8179 C  CD  . GLN D 1 221 ? 19.552  -21.600 41.511  1.00 12.17 ? 221 GLN D CD  1 
ATOM   8180 O  OE1 . GLN D 1 221 ? 20.302  -21.595 40.516  1.00 11.88 ? 221 GLN D OE1 1 
ATOM   8181 N  NE2 . GLN D 1 221 ? 19.916  -22.123 42.688  1.00 11.38 ? 221 GLN D NE2 1 
ATOM   8182 N  N   . LEU D 1 222 ? 17.376  -16.591 40.154  1.00 10.69 ? 222 LEU D N   1 
ATOM   8183 C  CA  . LEU D 1 222 ? 17.572  -15.138 40.257  1.00 10.96 ? 222 LEU D CA  1 
ATOM   8184 C  C   . LEU D 1 222 ? 16.249  -14.414 40.612  1.00 10.50 ? 222 LEU D C   1 
ATOM   8185 O  O   . LEU D 1 222 ? 16.176  -13.542 41.485  1.00 9.02  ? 222 LEU D O   1 
ATOM   8186 C  CB  . LEU D 1 222 ? 18.157  -14.578 38.951  1.00 11.24 ? 222 LEU D CB  1 
ATOM   8187 C  CG  . LEU D 1 222 ? 18.516  -13.083 38.997  1.00 11.73 ? 222 LEU D CG  1 
ATOM   8188 C  CD1 . LEU D 1 222 ? 19.531  -12.858 40.115  1.00 12.39 ? 222 LEU D CD1 1 
ATOM   8189 C  CD2 . LEU D 1 222 ? 19.126  -12.695 37.653  1.00 13.28 ? 222 LEU D CD2 1 
ATOM   8190 N  N   . LEU D 1 223 ? 15.197  -14.753 39.880  1.00 10.43 ? 223 LEU D N   1 
ATOM   8191 C  CA  . LEU D 1 223 ? 13.888  -14.229 40.152  1.00 10.28 ? 223 LEU D CA  1 
ATOM   8192 C  C   . LEU D 1 223 ? 13.409  -14.546 41.574  1.00 10.45 ? 223 LEU D C   1 
ATOM   8193 O  O   . LEU D 1 223 ? 12.787  -13.692 42.182  1.00 9.86  ? 223 LEU D O   1 
ATOM   8194 C  CB  . LEU D 1 223 ? 12.870  -14.771 39.069  1.00 10.49 ? 223 LEU D CB  1 
ATOM   8195 C  CG  . LEU D 1 223 ? 11.482  -14.240 39.273  1.00 11.21 ? 223 LEU D CG  1 
ATOM   8196 C  CD1 . LEU D 1 223 ? 11.473  -12.771 38.935  1.00 10.63 ? 223 LEU D CD1 1 
ATOM   8197 C  CD2 . LEU D 1 223 ? 10.378  -14.930 38.403  1.00 12.54 ? 223 LEU D CD2 1 
ATOM   8198 N  N   . ALA D 1 224 ? 13.672  -15.761 42.095  1.00 9.63  ? 224 ALA D N   1 
ATOM   8199 C  CA  . ALA D 1 224 ? 13.250  -16.124 43.427  1.00 9.62  ? 224 ALA D CA  1 
ATOM   8200 C  C   . ALA D 1 224 ? 13.972  -15.198 44.390  1.00 9.66  ? 224 ALA D C   1 
ATOM   8201 O  O   . ALA D 1 224 ? 13.364  -14.734 45.349  1.00 10.49 ? 224 ALA D O   1 
ATOM   8202 C  CB  . ALA D 1 224 ? 13.591  -17.584 43.797  1.00 8.81  ? 224 ALA D CB  1 
ATOM   8203 N  N   . LEU D 1 225 ? 15.235  -14.947 44.123  1.00 9.57  ? 225 LEU D N   1 
ATOM   8204 C  CA  . LEU D 1 225 ? 16.016  -14.097 45.061  1.00 10.53 ? 225 LEU D CA  1 
ATOM   8205 C  C   . LEU D 1 225 ? 15.447  -12.664 45.039  1.00 11.61 ? 225 LEU D C   1 
ATOM   8206 O  O   . LEU D 1 225 ? 15.294  -12.049 46.080  1.00 14.21 ? 225 LEU D O   1 
ATOM   8207 C  CB  . LEU D 1 225 ? 17.494  -14.039 44.651  1.00 10.89 ? 225 LEU D CB  1 
ATOM   8208 C  CG  . LEU D 1 225 ? 18.397  -13.147 45.529  1.00 10.28 ? 225 LEU D CG  1 
ATOM   8209 C  CD1 . LEU D 1 225 ? 18.316  -13.483 47.014  1.00 11.29 ? 225 LEU D CD1 1 
ATOM   8210 C  CD2 . LEU D 1 225 ? 19.823  -13.332 44.997  1.00 12.09 ? 225 LEU D CD2 1 
ATOM   8211 N  N   . GLU D 1 226 ? 15.146  -12.144 43.848  1.00 11.08 ? 226 GLU D N   1 
ATOM   8212 C  CA  . GLU D 1 226 ? 14.633  -10.777 43.710  1.00 11.91 ? 226 GLU D CA  1 
ATOM   8213 C  C   . GLU D 1 226 ? 13.204  -10.582 44.267  1.00 12.65 ? 226 GLU D C   1 
ATOM   8214 O  O   . GLU D 1 226 ? 12.826  -9.461  44.551  1.00 14.48 ? 226 GLU D O   1 
ATOM   8215 C  CB  . GLU D 1 226 ? 14.654  -10.370 42.219  1.00 11.54 ? 226 GLU D CB  1 
ATOM   8216 C  CG  . GLU D 1 226 ? 16.047  -10.375 41.604  1.00 10.21 ? 226 GLU D CG  1 
ATOM   8217 C  CD  . GLU D 1 226 ? 15.996  -10.425 40.103  1.00 11.71 ? 226 GLU D CD  1 
ATOM   8218 O  OE1 . GLU D 1 226 ? 14.965  -10.913 39.521  1.00 11.84 ? 226 GLU D OE1 1 
ATOM   8219 O  OE2 . GLU D 1 226 ? 16.994  -10.053 39.498  1.00 13.00 ? 226 GLU D OE2 1 
ATOM   8220 N  N   . THR D 1 227 ? 12.414  -11.661 44.403  1.00 12.20 ? 227 THR D N   1 
ATOM   8221 C  CA  . THR D 1 227 ? 11.003  -11.571 44.771  1.00 12.56 ? 227 THR D CA  1 
ATOM   8222 C  C   . THR D 1 227 ? 10.645  -12.056 46.200  1.00 13.27 ? 227 THR D C   1 
ATOM   8223 O  O   . THR D 1 227 ? 9.521   -11.783 46.664  1.00 14.31 ? 227 THR D O   1 
ATOM   8224 C  CB  . THR D 1 227 ? 10.092  -12.256 43.735  1.00 11.47 ? 227 THR D CB  1 
ATOM   8225 O  OG1 . THR D 1 227 ? 10.413  -13.653 43.650  1.00 12.19 ? 227 THR D OG1 1 
ATOM   8226 C  CG2 . THR D 1 227 ? 10.274  -11.640 42.362  1.00 12.55 ? 227 THR D CG2 1 
ATOM   8227 N  N   . ALA D 1 228 ? 11.590  -12.681 46.925  1.00 13.35 ? 228 ALA D N   1 
ATOM   8228 C  CA  . ALA D 1 228 ? 11.255  -13.385 48.200  1.00 12.43 ? 228 ALA D CA  1 
ATOM   8229 C  C   . ALA D 1 228 ? 10.990  -12.499 49.409  1.00 13.24 ? 228 ALA D C   1 
ATOM   8230 O  O   . ALA D 1 228 ? 10.124  -12.811 50.293  1.00 13.57 ? 228 ALA D O   1 
ATOM   8231 C  CB  . ALA D 1 228 ? 12.320  -14.441 48.551  1.00 12.17 ? 228 ALA D CB  1 
ATOM   8232 N  N   . LEU D 1 229 ? 11.756  -11.397 49.479  1.00 11.78 ? 229 LEU D N   1 
ATOM   8233 C  CA  . LEU D 1 229 ? 12.019  -10.726 50.732  1.00 12.20 ? 229 LEU D CA  1 
ATOM   8234 C  C   . LEU D 1 229 ? 11.511  -9.269  50.709  1.00 12.32 ? 229 LEU D C   1 
ATOM   8235 O  O   . LEU D 1 229 ? 11.372  -8.641  49.656  1.00 13.18 ? 229 LEU D O   1 
ATOM   8236 C  CB  . LEU D 1 229 ? 13.550  -10.756 51.039  1.00 12.06 ? 229 LEU D CB  1 
ATOM   8237 C  CG  . LEU D 1 229 ? 14.323  -12.066 50.827  1.00 13.35 ? 229 LEU D CG  1 
ATOM   8238 C  CD1 . LEU D 1 229 ? 15.837  -11.828 51.066  1.00 14.77 ? 229 LEU D CD1 1 
ATOM   8239 C  CD2 . LEU D 1 229 ? 13.782  -13.168 51.740  1.00 13.94 ? 229 LEU D CD2 1 
ATOM   8240 N  N   . TYR D 1 230 ? 11.190  -8.798  51.885  1.00 11.99 ? 230 TYR D N   1 
ATOM   8241 C  CA  . TYR D 1 230 ? 10.773  -7.427  52.160  1.00 12.41 ? 230 TYR D CA  1 
ATOM   8242 C  C   . TYR D 1 230 ? 11.720  -6.812  53.163  1.00 12.47 ? 230 TYR D C   1 
ATOM   8243 O  O   . TYR D 1 230 ? 12.243  -7.530  54.055  1.00 13.63 ? 230 TYR D O   1 
ATOM   8244 C  CB  . TYR D 1 230 ? 9.384   -7.430  52.774  1.00 13.15 ? 230 TYR D CB  1 
ATOM   8245 C  CG  . TYR D 1 230 ? 8.357   -7.867  51.740  1.00 13.98 ? 230 TYR D CG  1 
ATOM   8246 C  CD1 . TYR D 1 230 ? 8.177   -9.236  51.468  1.00 15.28 ? 230 TYR D CD1 1 
ATOM   8247 C  CD2 . TYR D 1 230 ? 7.624   -6.932  51.001  1.00 14.88 ? 230 TYR D CD2 1 
ATOM   8248 C  CE1 . TYR D 1 230 ? 7.281   -9.663  50.541  1.00 15.81 ? 230 TYR D CE1 1 
ATOM   8249 C  CE2 . TYR D 1 230 ? 6.668   -7.371  50.052  1.00 16.49 ? 230 TYR D CE2 1 
ATOM   8250 C  CZ  . TYR D 1 230 ? 6.560   -8.754  49.833  1.00 16.72 ? 230 TYR D CZ  1 
ATOM   8251 O  OH  . TYR D 1 230 ? 5.694   -9.298  48.912  1.00 22.84 ? 230 TYR D OH  1 
ATOM   8252 N  N   . CYS D 1 231 ? 11.927  -5.493  53.061  1.00 13.05 ? 231 CYS D N   1 
ATOM   8253 C  CA  . CYS D 1 231 ? 12.805  -4.730  53.966  1.00 13.12 ? 231 CYS D CA  1 
ATOM   8254 C  C   . CYS D 1 231 ? 12.162  -4.432  55.310  1.00 14.68 ? 231 CYS D C   1 
ATOM   8255 O  O   . CYS D 1 231 ? 12.826  -3.959  56.276  1.00 13.30 ? 231 CYS D O   1 
ATOM   8256 C  CB  . CYS D 1 231 ? 13.092  -3.348  53.339  1.00 14.31 ? 231 CYS D CB  1 
ATOM   8257 S  SG  . CYS D 1 231 ? 14.068  -3.412  51.802  1.00 17.54 ? 231 CYS D SG  1 
ATOM   8258 N  N   . THR D 1 232 ? 10.850  -4.650  55.360  1.00 13.89 ? 232 THR D N   1 
ATOM   8259 C  CA  . THR D 1 232 ? 10.006  -4.192  56.486  1.00 14.97 ? 232 THR D CA  1 
ATOM   8260 C  C   . THR D 1 232 ? 9.619   -5.353  57.433  1.00 14.45 ? 232 THR D C   1 
ATOM   8261 O  O   . THR D 1 232 ? 9.624   -6.500  57.026  1.00 14.06 ? 232 THR D O   1 
ATOM   8262 C  CB  . THR D 1 232 ? 8.729   -3.509  55.901  1.00 15.13 ? 232 THR D CB  1 
ATOM   8263 O  OG1 . THR D 1 232 ? 8.349   -4.187  54.695  1.00 14.66 ? 232 THR D OG1 1 
ATOM   8264 C  CG2 . THR D 1 232 ? 8.994   -2.038  55.553  1.00 17.59 ? 232 THR D CG2 1 
ATOM   8265 N  N   . HIS D 1 233 ? 9.334   -5.040  58.715  1.00 16.66 ? 233 HIS D N   1 
ATOM   8266 C  CA  . HIS D 1 233 ? 8.773   -5.987  59.694  1.00 17.52 ? 233 HIS D CA  1 
ATOM   8267 C  C   . HIS D 1 233 ? 7.427   -6.527  59.268  1.00 17.91 ? 233 HIS D C   1 
ATOM   8268 O  O   . HIS D 1 233 ? 6.686   -5.851  58.587  1.00 18.98 ? 233 HIS D O   1 
ATOM   8269 C  CB  . HIS D 1 233 ? 8.626   -5.298  61.061  1.00 18.83 ? 233 HIS D CB  1 
ATOM   8270 C  CG  . HIS D 1 233 ? 9.945   -5.065  61.755  1.00 19.90 ? 233 HIS D CG  1 
ATOM   8271 N  ND1 . HIS D 1 233 ? 10.445  -3.836  61.978  1.00 23.83 ? 233 HIS D ND1 1 
ATOM   8272 C  CD2 . HIS D 1 233 ? 10.855  -5.956  62.280  1.00 20.10 ? 233 HIS D CD2 1 
ATOM   8273 C  CE1 . HIS D 1 233 ? 11.628  -3.940  62.587  1.00 21.90 ? 233 HIS D CE1 1 
ATOM   8274 N  NE2 . HIS D 1 233 ? 11.874  -5.235  62.783  1.00 22.58 ? 233 HIS D NE2 1 
ATOM   8275 N  N   . MET D 1 234 ? 7.107   -7.760  59.649  1.00 18.14 ? 234 MET D N   1 
ATOM   8276 C  CA  . MET D 1 234 ? 5.781   -8.338  59.329  1.00 20.78 ? 234 MET D CA  1 
ATOM   8277 C  C   . MET D 1 234 ? 4.538   -7.493  59.777  1.00 21.77 ? 234 MET D C   1 
ATOM   8278 O  O   . MET D 1 234 ? 3.406   -7.753  59.312  1.00 21.87 ? 234 MET D O   1 
ATOM   8279 C  CB  . MET D 1 234 ? 5.702   -9.763  59.894  1.00 23.07 ? 234 MET D CB  1 
ATOM   8280 C  CG  . MET D 1 234 ? 5.655   -9.758  61.431  1.00 24.36 ? 234 MET D CG  1 
ATOM   8281 S  SD  . MET D 1 234 ? 5.934   -11.346 62.230  1.00 26.75 ? 234 MET D SD  1 
ATOM   8282 C  CE  . MET D 1 234 ? 4.811   -12.365 61.233  1.00 23.55 ? 234 MET D CE  1 
ATOM   8283 N  N   . ASP D 1 235 ? 4.743   -6.500  60.654  1.00 20.82 ? 235 ASP D N   1 
ATOM   8284 C  CA  . ASP D 1 235 ? 3.636   -5.624  61.068  1.00 22.43 ? 235 ASP D CA  1 
ATOM   8285 C  C   . ASP D 1 235 ? 3.780   -4.151  60.620  1.00 22.27 ? 235 ASP D C   1 
ATOM   8286 O  O   . ASP D 1 235 ? 3.172   -3.207  61.256  1.00 22.08 ? 235 ASP D O   1 
ATOM   8287 C  CB  . ASP D 1 235 ? 3.383   -5.728  62.573  1.00 23.27 ? 235 ASP D CB  1 
ATOM   8288 C  CG  . ASP D 1 235 ? 4.527   -5.143  63.391  1.00 27.71 ? 235 ASP D CG  1 
ATOM   8289 O  OD1 . ASP D 1 235 ? 4.336   -4.862  64.599  1.00 30.78 ? 235 ASP D OD1 1 
ATOM   8290 O  OD2 . ASP D 1 235 ? 5.616   -4.935  62.802  1.00 25.42 ? 235 ASP D OD2 1 
ATOM   8291 N  N   . ASP D 1 236 ? 4.534   -3.930  59.538  1.00 20.39 ? 236 ASP D N   1 
ATOM   8292 C  CA  . ASP D 1 236 ? 4.679   -2.577  59.010  1.00 21.51 ? 236 ASP D CA  1 
ATOM   8293 C  C   . ASP D 1 236 ? 3.448   -2.262  58.135  1.00 20.88 ? 236 ASP D C   1 
ATOM   8294 O  O   . ASP D 1 236 ? 3.138   -3.037  57.192  1.00 22.97 ? 236 ASP D O   1 
ATOM   8295 C  CB  . ASP D 1 236 ? 5.974   -2.413  58.215  1.00 19.92 ? 236 ASP D CB  1 
ATOM   8296 C  CG  . ASP D 1 236 ? 6.387   -0.961  58.050  1.00 20.33 ? 236 ASP D CG  1 
ATOM   8297 O  OD1 . ASP D 1 236 ? 7.548   -0.646  58.363  1.00 21.21 ? 236 ASP D OD1 1 
ATOM   8298 O  OD2 . ASP D 1 236 ? 5.580   -0.103  57.604  1.00 19.33 ? 236 ASP D OD2 1 
ATOM   8299 N  N   . PRO D 1 237 ? 2.725   -1.149  58.464  1.00 24.40 ? 237 PRO D N   1 
ATOM   8300 C  CA  . PRO D 1 237 ? 1.656   -0.692  57.575  1.00 22.69 ? 237 PRO D CA  1 
ATOM   8301 C  C   . PRO D 1 237 ? 2.160   -0.237  56.185  1.00 22.79 ? 237 PRO D C   1 
ATOM   8302 O  O   . PRO D 1 237 ? 1.365   -0.191  55.250  1.00 24.86 ? 237 PRO D O   1 
ATOM   8303 C  CB  . PRO D 1 237 ? 0.987   0.450   58.381  1.00 25.34 ? 237 PRO D CB  1 
ATOM   8304 C  CG  . PRO D 1 237 ? 2.088   1.004   59.237  1.00 24.91 ? 237 PRO D CG  1 
ATOM   8305 C  CD  . PRO D 1 237 ? 2.969   -0.177  59.567  1.00 25.46 ? 237 PRO D CD  1 
ATOM   8306 N  N   . SER D 1 238 ? 3.452   0.039   56.003  1.00 21.53 ? 238 SER D N   1 
ATOM   8307 C  CA  . SER D 1 238 ? 3.932   0.438   54.656  1.00 20.07 ? 238 SER D CA  1 
ATOM   8308 C  C   . SER D 1 238 ? 5.071   -0.468  54.187  1.00 19.18 ? 238 SER D C   1 
ATOM   8309 O  O   . SER D 1 238 ? 6.235   -0.082  54.300  1.00 17.52 ? 238 SER D O   1 
ATOM   8310 C  CB  . SER D 1 238 ? 4.363   1.926   54.580  1.00 24.27 ? 238 SER D CB  1 
ATOM   8311 O  OG  . SER D 1 238 ? 3.283   2.809   54.841  1.00 24.84 ? 238 SER D OG  1 
ATOM   8312 N  N   . PRO D 1 239 ? 4.729   -1.661  53.626  1.00 19.36 ? 239 PRO D N   1 
ATOM   8313 C  CA  . PRO D 1 239 ? 5.763   -2.699  53.271  1.00 18.51 ? 239 PRO D CA  1 
ATOM   8314 C  C   . PRO D 1 239 ? 6.563   -2.306  52.048  1.00 20.25 ? 239 PRO D C   1 
ATOM   8315 O  O   . PRO D 1 239 ? 5.991   -1.730  51.086  1.00 17.41 ? 239 PRO D O   1 
ATOM   8316 C  CB  . PRO D 1 239 ? 4.919   -3.958  52.926  1.00 17.45 ? 239 PRO D CB  1 
ATOM   8317 C  CG  . PRO D 1 239 ? 3.494   -3.623  53.406  1.00 20.68 ? 239 PRO D CG  1 
ATOM   8318 C  CD  . PRO D 1 239 ? 3.353   -2.138  53.335  1.00 18.68 ? 239 PRO D CD  1 
ATOM   8319 N  N   . ARG D 1 240 ? 7.864   -2.615  52.068  1.00 17.48 ? 240 ARG D N   1 
ATOM   8320 C  CA  . ARG D 1 240 ? 8.712   -2.296  50.949  1.00 17.78 ? 240 ARG D CA  1 
ATOM   8321 C  C   . ARG D 1 240 ? 9.419   -3.627  50.553  1.00 15.71 ? 240 ARG D C   1 
ATOM   8322 O  O   . ARG D 1 240 ? 10.045  -4.230  51.389  1.00 15.14 ? 240 ARG D O   1 
ATOM   8323 C  CB  . ARG D 1 240 ? 9.677   -1.177  51.337  1.00 19.84 ? 240 ARG D CB  1 
ATOM   8324 C  CG  . ARG D 1 240 ? 8.928   0.140   51.744  1.00 23.38 ? 240 ARG D CG  1 
ATOM   8325 C  CD  . ARG D 1 240 ? 9.480   0.760   53.037  1.00 29.07 ? 240 ARG D CD  1 
ATOM   8326 N  NE  . ARG D 1 240 ? 10.906  0.449   53.013  1.00 32.63 ? 240 ARG D NE  1 
ATOM   8327 C  CZ  . ARG D 1 240 ? 11.735  0.498   54.056  1.00 32.04 ? 240 ARG D CZ  1 
ATOM   8328 N  NH1 . ARG D 1 240 ? 11.301  0.859   55.255  1.00 32.73 ? 240 ARG D NH1 1 
ATOM   8329 N  NH2 . ARG D 1 240 ? 13.009  0.185   53.877  1.00 24.96 ? 240 ARG D NH2 1 
ATOM   8330 N  N   . GLU D 1 241 ? 9.303   -4.025  49.287  1.00 15.25 ? 241 GLU D N   1 
ATOM   8331 C  CA  . GLU D 1 241 ? 10.057  -5.171  48.708  1.00 14.52 ? 241 GLU D CA  1 
ATOM   8332 C  C   . GLU D 1 241 ? 11.539  -4.935  48.752  1.00 12.43 ? 241 GLU D C   1 
ATOM   8333 O  O   . GLU D 1 241 ? 11.988  -3.817  48.517  1.00 11.16 ? 241 GLU D O   1 
ATOM   8334 C  CB  . GLU D 1 241 ? 9.646   -5.391  47.273  1.00 18.68 ? 241 GLU D CB  1 
ATOM   8335 C  CG  . GLU D 1 241 ? 8.275   -6.035  47.223  1.00 21.94 ? 241 GLU D CG  1 
ATOM   8336 C  CD  . GLU D 1 241 ? 7.516   -5.758  45.951  1.00 30.18 ? 241 GLU D CD  1 
ATOM   8337 O  OE1 . GLU D 1 241 ? 8.062   -5.100  45.047  1.00 32.73 ? 241 GLU D OE1 1 
ATOM   8338 O  OE2 . GLU D 1 241 ? 6.350   -6.195  45.878  1.00 33.07 ? 241 GLU D OE2 1 
ATOM   8339 N  N   . MET D 1 242 ? 12.292  -5.990  49.102  1.00 11.65 ? 242 MET D N   1 
ATOM   8340 C  CA  . MET D 1 242 ? 13.757  -5.994  49.095  1.00 11.93 ? 242 MET D CA  1 
ATOM   8341 C  C   . MET D 1 242 ? 14.334  -6.225  47.691  1.00 10.48 ? 242 MET D C   1 
ATOM   8342 O  O   . MET D 1 242 ? 14.552  -7.356  47.259  1.00 10.66 ? 242 MET D O   1 
ATOM   8343 C  CB  . MET D 1 242 ? 14.337  -6.983  50.126  1.00 11.82 ? 242 MET D CB  1 
ATOM   8344 C  CG  . MET D 1 242 ? 15.826  -6.702  50.381  1.00 11.96 ? 242 MET D CG  1 
ATOM   8345 S  SD  . MET D 1 242 ? 16.600  -7.900  51.500  1.00 10.62 ? 242 MET D SD  1 
ATOM   8346 C  CE  . MET D 1 242 ? 15.786  -7.511  53.070  1.00 9.85  ? 242 MET D CE  1 
ATOM   8347 N  N   . ILE D 1 243 ? 14.487  -5.096  46.975  1.00 10.27 ? 243 ILE D N   1 
ATOM   8348 C  CA  . ILE D 1 243 ? 15.009  -5.018  45.633  1.00 10.12 ? 243 ILE D CA  1 
ATOM   8349 C  C   . ILE D 1 243 ? 16.049  -3.859  45.531  1.00 9.62  ? 243 ILE D C   1 
ATOM   8350 O  O   . ILE D 1 243 ? 16.026  -2.923  46.345  1.00 9.41  ? 243 ILE D O   1 
ATOM   8351 C  CB  . ILE D 1 243 ? 13.876  -4.821  44.577  1.00 10.52 ? 243 ILE D CB  1 
ATOM   8352 C  CG1 . ILE D 1 243 ? 13.095  -3.541  44.883  1.00 11.83 ? 243 ILE D CG1 1 
ATOM   8353 C  CG2 . ILE D 1 243 ? 13.008  -6.116  44.404  1.00 10.24 ? 243 ILE D CG2 1 
ATOM   8354 C  CD1 . ILE D 1 243 ? 11.964  -3.254  43.893  1.00 15.22 ? 243 ILE D CD1 1 
ATOM   8355 N  N   . ASN D 1 244 ? 16.929  -3.935  44.532  1.00 9.73  ? 244 ASN D N   1 
ATOM   8356 C  CA  . ASN D 1 244 ? 17.943  -2.895  44.262  1.00 9.17  ? 244 ASN D CA  1 
ATOM   8357 C  C   . ASN D 1 244 ? 18.738  -2.553  45.502  1.00 9.08  ? 244 ASN D C   1 
ATOM   8358 O  O   . ASN D 1 244 ? 19.038  -1.380  45.768  1.00 9.24  ? 244 ASN D O   1 
ATOM   8359 C  CB  . ASN D 1 244 ? 17.279  -1.661  43.643  1.00 10.57 ? 244 ASN D CB  1 
ATOM   8360 C  CG  . ASN D 1 244 ? 16.351  -2.026  42.468  1.00 10.57 ? 244 ASN D CG  1 
ATOM   8361 O  OD1 . ASN D 1 244 ? 16.742  -2.751  41.592  1.00 11.75 ? 244 ASN D OD1 1 
ATOM   8362 N  ND2 . ASN D 1 244 ? 15.129  -1.525  42.484  1.00 11.34 ? 244 ASN D ND2 1 
ATOM   8363 N  N   . ASN D 1 245 ? 19.077  -3.592  46.268  1.00 8.77  ? 245 ASN D N   1 
ATOM   8364 C  CA  . ASN D 1 245 ? 19.846  -3.409  47.515  1.00 9.32  ? 245 ASN D CA  1 
ATOM   8365 C  C   . ASN D 1 245 ? 21.378  -3.443  47.241  1.00 9.54  ? 245 ASN D C   1 
ATOM   8366 O  O   . ASN D 1 245 ? 22.111  -4.164  47.917  1.00 9.47  ? 245 ASN D O   1 
ATOM   8367 C  CB  . ASN D 1 245 ? 19.402  -4.436  48.607  1.00 10.00 ? 245 ASN D CB  1 
ATOM   8368 C  CG  . ASN D 1 245 ? 19.735  -5.887  48.218  1.00 10.08 ? 245 ASN D CG  1 
ATOM   8369 O  OD1 . ASN D 1 245 ? 19.852  -6.220  47.027  1.00 8.56  ? 245 ASN D OD1 1 
ATOM   8370 N  ND2 . ASN D 1 245 ? 19.837  -6.750  49.192  1.00 10.49 ? 245 ASN D ND2 1 
ATOM   8371 N  N   . PHE D 1 246 ? 21.839  -2.624  46.274  1.00 8.92  ? 246 PHE D N   1 
ATOM   8372 C  CA  . PHE D 1 246 ? 23.230  -2.457  45.919  1.00 8.63  ? 246 PHE D CA  1 
ATOM   8373 C  C   . PHE D 1 246 ? 23.544  -0.929  45.967  1.00 8.36  ? 246 PHE D C   1 
ATOM   8374 O  O   . PHE D 1 246 ? 22.660  -0.086  45.658  1.00 9.07  ? 246 PHE D O   1 
ATOM   8375 C  CB  . PHE D 1 246 ? 23.567  -3.083  44.534  1.00 7.73  ? 246 PHE D CB  1 
ATOM   8376 C  CG  . PHE D 1 246 ? 22.869  -2.429  43.385  1.00 7.86  ? 246 PHE D CG  1 
ATOM   8377 C  CD1 . PHE D 1 246 ? 23.446  -1.334  42.729  1.00 7.73  ? 246 PHE D CD1 1 
ATOM   8378 C  CD2 . PHE D 1 246 ? 21.600  -2.843  43.011  1.00 7.77  ? 246 PHE D CD2 1 
ATOM   8379 C  CE1 . PHE D 1 246 ? 22.776  -0.679  41.683  1.00 8.56  ? 246 PHE D CE1 1 
ATOM   8380 C  CE2 . PHE D 1 246 ? 20.899  -2.178  42.027  1.00 7.82  ? 246 PHE D CE2 1 
ATOM   8381 C  CZ  . PHE D 1 246 ? 21.518  -1.121  41.308  1.00 8.14  ? 246 PHE D CZ  1 
ATOM   8382 N  N   . ARG D 1 247 ? 24.751  -0.593  46.422  1.00 7.51  ? 247 ARG D N   1 
ATOM   8383 C  CA  . ARG D 1 247 ? 25.192  0.793   46.315  1.00 7.82  ? 247 ARG D CA  1 
ATOM   8384 C  C   . ARG D 1 247 ? 25.729  1.163   44.892  1.00 7.88  ? 247 ARG D C   1 
ATOM   8385 O  O   . ARG D 1 247 ? 26.399  0.367   44.210  1.00 7.70  ? 247 ARG D O   1 
ATOM   8386 C  CB  . ARG D 1 247 ? 26.267  1.082   47.407  1.00 7.12  ? 247 ARG D CB  1 
ATOM   8387 C  CG  . ARG D 1 247 ? 26.609  2.574   47.576  1.00 7.31  ? 247 ARG D CG  1 
ATOM   8388 C  CD  . ARG D 1 247 ? 27.777  2.758   48.558  1.00 7.31  ? 247 ARG D CD  1 
ATOM   8389 N  NE  . ARG D 1 247 ? 27.822  4.103   49.191  1.00 6.88  ? 247 ARG D NE  1 
ATOM   8390 C  CZ  . ARG D 1 247 ? 28.823  4.450   50.035  1.00 7.70  ? 247 ARG D CZ  1 
ATOM   8391 N  NH1 . ARG D 1 247 ? 29.855  3.613   50.261  1.00 6.96  ? 247 ARG D NH1 1 
ATOM   8392 N  NH2 . ARG D 1 247 ? 28.829  5.663   50.616  1.00 7.36  ? 247 ARG D NH2 1 
ATOM   8393 N  N   . GLN D 1 248 ? 25.474  2.403   44.450  1.00 8.37  ? 248 GLN D N   1 
ATOM   8394 C  CA  . GLN D 1 248 ? 26.179  2.929   43.245  1.00 8.73  ? 248 GLN D CA  1 
ATOM   8395 C  C   . GLN D 1 248 ? 27.727  2.943   43.412  1.00 8.82  ? 248 GLN D C   1 
ATOM   8396 O  O   . GLN D 1 248 ? 28.244  3.075   44.538  1.00 8.61  ? 248 GLN D O   1 
ATOM   8397 C  CB  . GLN D 1 248 ? 25.700  4.357   42.935  1.00 9.80  ? 248 GLN D CB  1 
ATOM   8398 C  CG  . GLN D 1 248 ? 24.229  4.519   42.586  1.00 10.36 ? 248 GLN D CG  1 
ATOM   8399 C  CD  . GLN D 1 248 ? 23.776  3.783   41.328  1.00 10.32 ? 248 GLN D CD  1 
ATOM   8400 O  OE1 . GLN D 1 248 ? 23.211  2.672   41.388  1.00 9.90  ? 248 GLN D OE1 1 
ATOM   8401 N  NE2 . GLN D 1 248 ? 23.947  4.436   40.200  1.00 9.21  ? 248 GLN D NE2 1 
ATOM   8402 N  N   . VAL D 1 249 ? 28.437  2.731   42.301  1.00 9.70  ? 249 VAL D N   1 
ATOM   8403 C  CA  . VAL D 1 249 ? 29.877  2.750   42.268  1.00 8.67  ? 249 VAL D CA  1 
ATOM   8404 C  C   . VAL D 1 249 ? 30.372  4.171   42.638  1.00 8.72  ? 249 VAL D C   1 
ATOM   8405 O  O   . VAL D 1 249 ? 29.710  5.196   42.371  1.00 9.16  ? 249 VAL D O   1 
ATOM   8406 C  CB  . VAL D 1 249 ? 30.453  2.254   40.907  1.00 8.61  ? 249 VAL D CB  1 
ATOM   8407 C  CG1 . VAL D 1 249 ? 30.200  0.704   40.674  1.00 8.32  ? 249 VAL D CG1 1 
ATOM   8408 C  CG2 . VAL D 1 249 ? 29.841  3.051   39.758  1.00 9.05  ? 249 VAL D CG2 1 
ATOM   8409 N  N   . GLN D 1 250 ? 31.515  4.187   43.292  1.00 9.10  ? 250 GLN D N   1 
ATOM   8410 C  CA  . GLN D 1 250 ? 32.113  5.387   43.871  1.00 9.89  ? 250 GLN D CA  1 
ATOM   8411 C  C   . GLN D 1 250 ? 33.279  5.943   43.027  1.00 10.72 ? 250 GLN D C   1 
ATOM   8412 O  O   . GLN D 1 250 ? 33.976  5.187   42.306  1.00 10.58 ? 250 GLN D O   1 
ATOM   8413 C  CB  . GLN D 1 250 ? 32.662  5.068   45.300  1.00 9.32  ? 250 GLN D CB  1 
ATOM   8414 C  CG  . GLN D 1 250 ? 31.708  4.418   46.300  1.00 7.82  ? 250 GLN D CG  1 
ATOM   8415 C  CD  . GLN D 1 250 ? 30.564  5.371   46.694  1.00 8.51  ? 250 GLN D CD  1 
ATOM   8416 O  OE1 . GLN D 1 250 ? 30.775  6.389   47.306  1.00 7.14  ? 250 GLN D OE1 1 
ATOM   8417 N  NE2 . GLN D 1 250 ? 29.363  5.051   46.225  1.00 7.15  ? 250 GLN D NE2 1 
ATOM   8418 N  N   . LYS D 1 251 ? 33.554  7.249   43.175  1.00 10.93 ? 251 LYS D N   1 
ATOM   8419 C  CA  . LYS D 1 251 ? 34.759  7.846   42.598  1.00 12.68 ? 251 LYS D CA  1 
ATOM   8420 C  C   . LYS D 1 251 ? 35.937  7.040   43.085  1.00 14.03 ? 251 LYS D C   1 
ATOM   8421 O  O   . LYS D 1 251 ? 35.966  6.661   44.275  1.00 13.12 ? 251 LYS D O   1 
ATOM   8422 C  CB  . LYS D 1 251 ? 34.986  9.312   43.036  1.00 11.71 ? 251 LYS D CB  1 
ATOM   8423 C  CG  . LYS D 1 251 ? 33.952  10.329  42.457  1.00 11.95 ? 251 LYS D CG  1 
ATOM   8424 C  CD  . LYS D 1 251 ? 34.395  10.861  41.101  1.00 11.68 ? 251 LYS D CD  1 
ATOM   8425 C  CE  . LYS D 1 251 ? 33.450  11.945  40.518  1.00 11.18 ? 251 LYS D CE  1 
ATOM   8426 N  NZ  . LYS D 1 251 ? 32.005  11.542  40.428  1.00 9.71  ? 251 LYS D NZ  1 
ATOM   8427 N  N   . PHE D 1 252 ? 36.904  6.790   42.181  1.00 15.15 ? 252 PHE D N   1 
ATOM   8428 C  CA  . PHE D 1 252 ? 38.127  6.088   42.553  1.00 19.82 ? 252 PHE D CA  1 
ATOM   8429 C  C   . PHE D 1 252 ? 39.250  6.712   41.768  1.00 24.79 ? 252 PHE D C   1 
ATOM   8430 O  O   . PHE D 1 252 ? 39.333  6.463   40.564  1.00 25.64 ? 252 PHE D O   1 
ATOM   8431 C  CB  . PHE D 1 252 ? 38.017  4.613   42.124  1.00 20.90 ? 252 PHE D CB  1 
ATOM   8432 C  CG  . PHE D 1 252 ? 39.049  3.735   42.728  1.00 20.60 ? 252 PHE D CG  1 
ATOM   8433 C  CD1 . PHE D 1 252 ? 38.905  3.305   44.026  1.00 20.90 ? 252 PHE D CD1 1 
ATOM   8434 C  CD2 . PHE D 1 252 ? 40.164  3.331   42.003  1.00 20.87 ? 252 PHE D CD2 1 
ATOM   8435 C  CE1 . PHE D 1 252 ? 39.838  2.490   44.627  1.00 22.08 ? 252 PHE D CE1 1 
ATOM   8436 C  CE2 . PHE D 1 252 ? 41.095  2.513   42.590  1.00 22.30 ? 252 PHE D CE2 1 
ATOM   8437 C  CZ  . PHE D 1 252 ? 40.941  2.093   43.906  1.00 22.26 ? 252 PHE D CZ  1 
ATOM   8438 N  N   . ASP D 1 253 ? 40.078  7.527   42.423  1.00 27.84 ? 253 ASP D N   1 
ATOM   8439 C  CA  . ASP D 1 253 ? 40.854  8.592   41.736  1.00 35.20 ? 253 ASP D CA  1 
ATOM   8440 C  C   . ASP D 1 253 ? 42.205  8.668   42.391  1.00 38.47 ? 253 ASP D C   1 
ATOM   8441 O  O   . ASP D 1 253 ? 42.284  8.710   43.616  1.00 37.33 ? 253 ASP D O   1 
ATOM   8442 C  CB  . ASP D 1 253 ? 40.177  9.982   41.897  1.00 40.14 ? 253 ASP D CB  1 
ATOM   8443 C  CG  . ASP D 1 253 ? 38.931  10.203  40.962  1.00 40.97 ? 253 ASP D CG  1 
ATOM   8444 O  OD1 . ASP D 1 253 ? 38.740  9.507   39.932  1.00 42.29 ? 253 ASP D OD1 1 
ATOM   8445 O  OD2 . ASP D 1 253 ? 38.130  11.110  41.268  1.00 37.04 ? 253 ASP D OD2 1 
ATOM   8446 N  N   . GLU D 1 254 ? 43.262  8.668   41.577  1.00 46.46 ? 254 GLU D N   1 
ATOM   8447 C  CA  . GLU D 1 254 ? 44.661  8.560   42.047  1.00 48.93 ? 254 GLU D CA  1 
ATOM   8448 C  C   . GLU D 1 254 ? 44.887  7.400   43.033  1.00 44.75 ? 254 GLU D C   1 
ATOM   8449 O  O   . GLU D 1 254 ? 45.786  7.437   43.885  1.00 45.61 ? 254 GLU D O   1 
ATOM   8450 C  CB  . GLU D 1 254 ? 45.193  9.912   42.577  1.00 53.22 ? 254 GLU D CB  1 
ATOM   8451 C  CG  . GLU D 1 254 ? 44.507  10.466  43.828  1.00 57.82 ? 254 GLU D CG  1 
ATOM   8452 C  CD  . GLU D 1 254 ? 44.708  11.953  43.973  1.00 61.78 ? 254 GLU D CD  1 
ATOM   8453 O  OE1 . GLU D 1 254 ? 44.950  12.623  42.940  1.00 65.18 ? 254 GLU D OE1 1 
ATOM   8454 O  OE2 . GLU D 1 254 ? 44.632  12.449  45.118  1.00 67.20 ? 254 GLU D OE2 1 
ATOM   8455 N  N   . ARG D 1 255 ? 44.026  6.394   42.905  1.00 40.24 ? 255 ARG D N   1 
ATOM   8456 C  CA  . ARG D 1 255 ? 43.977  5.207   43.768  1.00 34.48 ? 255 ARG D CA  1 
ATOM   8457 C  C   . ARG D 1 255 ? 43.969  4.016   42.815  1.00 32.67 ? 255 ARG D C   1 
ATOM   8458 O  O   . ARG D 1 255 ? 43.631  4.172   41.622  1.00 23.39 ? 255 ARG D O   1 
ATOM   8459 C  CB  . ARG D 1 255 ? 42.659  5.307   44.608  1.00 35.39 ? 255 ARG D CB  1 
ATOM   8460 C  CG  . ARG D 1 255 ? 42.670  4.751   46.041  1.00 36.15 ? 255 ARG D CG  1 
ATOM   8461 C  CD  . ARG D 1 255 ? 41.843  5.487   47.115  1.00 33.64 ? 255 ARG D CD  1 
ATOM   8462 N  NE  . ARG D 1 255 ? 40.445  5.766   46.757  1.00 33.78 ? 255 ARG D NE  1 
ATOM   8463 C  CZ  . ARG D 1 255 ? 39.599  6.515   47.474  1.00 32.29 ? 255 ARG D CZ  1 
ATOM   8464 N  NH1 . ARG D 1 255 ? 38.352  6.693   47.053  1.00 32.78 ? 255 ARG D NH1 1 
ATOM   8465 N  NH2 . ARG D 1 255 ? 39.984  7.092   48.607  1.00 31.50 ? 255 ARG D NH2 1 
ATOM   8466 N  N   . LEU D 1 256 ? 44.355  2.837   43.308  1.00 31.45 ? 256 LEU D N   1 
ATOM   8467 C  CA  . LEU D 1 256 ? 44.637  1.696   42.410  1.00 26.50 ? 256 LEU D CA  1 
ATOM   8468 C  C   . LEU D 1 256 ? 44.137  0.300   42.893  1.00 22.32 ? 256 LEU D C   1 
ATOM   8469 O  O   . LEU D 1 256 ? 44.173  -0.078  44.080  1.00 24.60 ? 256 LEU D O   1 
ATOM   8470 C  CB  . LEU D 1 256 ? 46.136  1.648   42.091  1.00 29.10 ? 256 LEU D CB  1 
ATOM   8471 C  CG  . LEU D 1 256 ? 46.726  1.954   40.713  1.00 28.13 ? 256 LEU D CG  1 
ATOM   8472 C  CD1 . LEU D 1 256 ? 46.351  3.287   40.059  1.00 24.97 ? 256 LEU D CD1 1 
ATOM   8473 C  CD2 . LEU D 1 256 ? 48.228  1.776   40.818  1.00 31.12 ? 256 LEU D CD2 1 
ATOM   8474 N  N   . VAL D 1 257 ? 43.704  -0.487  41.924  1.00 18.96 ? 257 VAL D N   1 
ATOM   8475 C  CA  . VAL D 1 257 ? 43.289  -1.848  42.147  1.00 15.20 ? 257 VAL D CA  1 
ATOM   8476 C  C   . VAL D 1 257 ? 44.379  -2.742  41.558  1.00 15.80 ? 257 VAL D C   1 
ATOM   8477 O  O   . VAL D 1 257 ? 44.809  -2.549  40.395  1.00 18.81 ? 257 VAL D O   1 
ATOM   8478 C  CB  . VAL D 1 257 ? 42.024  -2.127  41.309  1.00 15.69 ? 257 VAL D CB  1 
ATOM   8479 C  CG1 . VAL D 1 257 ? 41.686  -3.628  41.346  1.00 13.58 ? 257 VAL D CG1 1 
ATOM   8480 C  CG2 . VAL D 1 257 ? 40.887  -1.202  41.747  1.00 15.18 ? 257 VAL D CG2 1 
ATOM   8481 N  N   . TYR D 1 258 ? 44.801  -3.746  42.319  1.00 14.66 ? 258 TYR D N   1 
ATOM   8482 C  CA  . TYR D 1 258 ? 45.856  -4.639  41.858  1.00 13.90 ? 258 TYR D CA  1 
ATOM   8483 C  C   . TYR D 1 258 ? 45.291  -5.952  41.387  1.00 13.88 ? 258 TYR D C   1 
ATOM   8484 O  O   . TYR D 1 258 ? 44.356  -6.451  42.019  1.00 16.40 ? 258 TYR D O   1 
ATOM   8485 C  CB  . TYR D 1 258 ? 46.870  -4.832  42.991  1.00 14.67 ? 258 TYR D CB  1 
ATOM   8486 C  CG  . TYR D 1 258 ? 47.378  -3.478  43.435  1.00 17.13 ? 258 TYR D CG  1 
ATOM   8487 C  CD1 . TYR D 1 258 ? 46.805  -2.818  44.538  1.00 19.75 ? 258 TYR D CD1 1 
ATOM   8488 C  CD2 . TYR D 1 258 ? 48.396  -2.843  42.742  1.00 19.02 ? 258 TYR D CD2 1 
ATOM   8489 C  CE1 . TYR D 1 258 ? 47.256  -1.552  44.945  1.00 19.97 ? 258 TYR D CE1 1 
ATOM   8490 C  CE2 . TYR D 1 258 ? 48.875  -1.563  43.161  1.00 20.06 ? 258 TYR D CE2 1 
ATOM   8491 C  CZ  . TYR D 1 258 ? 48.273  -0.935  44.242  1.00 21.64 ? 258 TYR D CZ  1 
ATOM   8492 O  OH  . TYR D 1 258 ? 48.720  0.306   44.692  1.00 25.75 ? 258 TYR D OH  1 
ATOM   8493 N  N   . THR D 1 259 ? 45.794  -6.504  40.271  1.00 13.01 ? 259 THR D N   1 
ATOM   8494 C  CA  . THR D 1 259 ? 45.286  -7.779  39.804  1.00 11.99 ? 259 THR D CA  1 
ATOM   8495 C  C   . THR D 1 259 ? 46.321  -8.864  39.980  1.00 12.41 ? 259 THR D C   1 
ATOM   8496 O  O   . THR D 1 259 ? 47.538  -8.592  39.910  1.00 12.17 ? 259 THR D O   1 
ATOM   8497 C  CB  . THR D 1 259 ? 44.886  -7.702  38.337  1.00 12.50 ? 259 THR D CB  1 
ATOM   8498 O  OG1 . THR D 1 259 ? 46.035  -7.337  37.538  1.00 14.22 ? 259 THR D OG1 1 
ATOM   8499 C  CG2 . THR D 1 259 ? 43.811  -6.633  38.154  1.00 12.61 ? 259 THR D CG2 1 
ATOM   8500 N  N   . SER D 1 260 ? 45.857  -10.096 40.187  1.00 12.10 ? 260 SER D N   1 
ATOM   8501 C  CA  . SER D 1 260 ? 46.789  -11.209 40.381  1.00 13.92 ? 260 SER D CA  1 
ATOM   8502 C  C   . SER D 1 260 ? 47.097  -11.858 39.034  1.00 14.74 ? 260 SER D C   1 
ATOM   8503 O  O   . SER D 1 260 ? 47.776  -12.888 39.006  1.00 17.06 ? 260 SER D O   1 
ATOM   8504 C  CB  . SER D 1 260 ? 46.208  -12.259 41.340  1.00 13.20 ? 260 SER D CB  1 
ATOM   8505 O  OG  . SER D 1 260 ? 45.018  -12.837 40.839  1.00 13.27 ? 260 SER D OG  1 
ATOM   8506 N  N   . PHE D 1 261 ? 46.587  -11.266 37.947  1.00 14.64 ? 261 PHE D N   1 
ATOM   8507 C  CA  . PHE D 1 261 ? 46.661  -11.832 36.589  1.00 17.72 ? 261 PHE D CA  1 
ATOM   8508 C  C   . PHE D 1 261 ? 47.141  -10.713 35.646  1.00 19.28 ? 261 PHE D C   1 
ATOM   8509 O  O   . PHE D 1 261 ? 46.677  -9.575  35.738  1.00 15.85 ? 261 PHE D O   1 
ATOM   8510 C  CB  . PHE D 1 261 ? 45.298  -12.459 36.159  1.00 16.10 ? 261 PHE D CB  1 
ATOM   8511 C  CG  . PHE D 1 261 ? 44.110  -11.515 36.255  1.00 16.42 ? 261 PHE D CG  1 
ATOM   8512 C  CD1 . PHE D 1 261 ? 43.734  -10.733 35.170  1.00 14.99 ? 261 PHE D CD1 1 
ATOM   8513 C  CD2 . PHE D 1 261 ? 43.382  -11.409 37.430  1.00 14.50 ? 261 PHE D CD2 1 
ATOM   8514 C  CE1 . PHE D 1 261 ? 42.641  -9.858  35.241  1.00 15.75 ? 261 PHE D CE1 1 
ATOM   8515 C  CE2 . PHE D 1 261 ? 42.331  -10.512 37.541  1.00 14.56 ? 261 PHE D CE2 1 
ATOM   8516 C  CZ  . PHE D 1 261 ? 41.944  -9.736  36.451  1.00 15.05 ? 261 PHE D CZ  1 
ATOM   8517 N  N   . SER D 1 262 ? 48.095  -10.991 34.769  1.00 21.10 ? 262 SER D N   1 
ATOM   8518 C  CA  . SER D 1 262 ? 48.629  -9.917  33.941  1.00 22.72 ? 262 SER D CA  1 
ATOM   8519 C  C   . SER D 1 262 ? 47.761  -9.833  32.694  1.00 24.38 ? 262 SER D C   1 
ATOM   8520 O  O   . SER D 1 262 ? 47.783  -8.855  31.956  1.00 24.21 ? 262 SER D O   1 
ATOM   8521 C  CB  . SER D 1 262 ? 50.089  -10.214 33.559  1.00 28.41 ? 262 SER D CB  1 
ATOM   8522 O  OG  . SER D 1 262 ? 50.224  -11.571 33.122  1.00 29.18 ? 262 SER D OG  1 
ATOM   8523 N  N   . GLN D 1 263 ? 46.963  -10.866 32.471  1.00 24.46 ? 263 GLN D N   1 
ATOM   8524 C  CA  . GLN D 1 263 ? 46.232  -10.992 31.210  1.00 22.96 ? 263 GLN D CA  1 
ATOM   8525 C  C   . GLN D 1 263 ? 45.181  -12.038 31.472  1.00 24.23 ? 263 GLN D C   1 
ATOM   8526 O  O   . GLN D 1 263 ? 44.265  -12.249 30.689  1.00 21.55 ? 263 GLN D O   1 
ATOM   8527 C  CB  . GLN D 1 263 ? 47.177  -11.497 30.090  1.00 26.17 ? 263 GLN D CB  1 
ATOM   8528 C  CG  . GLN D 1 263 ? 47.748  -12.915 30.310  1.00 26.65 ? 263 GLN D CG  1 
ATOM   8529 C  CD  . GLN D 1 263 ? 48.944  -13.286 29.396  1.00 28.09 ? 263 GLN D CD  1 
ATOM   8530 O  OE1 . GLN D 1 263 ? 49.641  -12.426 28.837  1.00 30.64 ? 263 GLN D OE1 1 
ATOM   8531 N  NE2 . GLN D 1 263 ? 49.194  -14.596 29.263  1.00 28.91 ? 263 GLN D NE2 1 
ATOM   8532 O  OXT . GLN D 1 263 ? 45.307  -12.770 32.460  1.00 24.29 ? 263 GLN D OXT 1 
HETATM 8533 ZN ZN  . ZN  E 2 .   ? -1.827  14.679  -7.199  1.00 10.89 ? 301 ZN  A ZN  1 
HETATM 8534 O  O19 . E1G F 3 .   ? -5.596  14.592  -5.496  1.00 23.96 ? 302 E1G A O19 1 
HETATM 8535 S  S17 . E1G F 3 .   ? -4.492  15.550  -5.994  1.00 25.44 ? 302 E1G A S17 1 
HETATM 8536 O  O18 . E1G F 3 .   ? -4.739  15.597  -7.524  1.00 23.26 ? 302 E1G A O18 1 
HETATM 8537 N  N20 . E1G F 3 .   ? -2.904  14.860  -5.734  1.00 16.12 ? 302 E1G A N20 1 
HETATM 8538 C  C4  . E1G F 3 .   ? -4.622  17.194  -5.282  1.00 26.23 ? 302 E1G A C4  1 
HETATM 8539 C  C5  . E1G F 3 .   ? -3.858  17.344  -4.138  1.00 27.68 ? 302 E1G A C5  1 
HETATM 8540 C  C6  . E1G F 3 .   ? -3.845  18.550  -3.429  1.00 32.61 ? 302 E1G A C6  1 
HETATM 8541 C  C1  . E1G F 3 .   ? -4.572  19.635  -3.902  1.00 35.27 ? 302 E1G A C1  1 
HETATM 8542 C  C3  . E1G F 3 .   ? -5.373  18.293  -5.784  1.00 29.93 ? 302 E1G A C3  1 
HETATM 8543 C  C2  . E1G F 3 .   ? -5.327  19.534  -5.073  1.00 34.37 ? 302 E1G A C2  1 
HETATM 8544 C  C7  . E1G F 3 .   ? -6.087  20.756  -5.423  1.00 40.72 ? 302 E1G A C7  1 
HETATM 8545 O  O13 . E1G F 3 .   ? -5.545  21.785  -5.830  1.00 48.52 ? 302 E1G A O13 1 
HETATM 8546 C  C8  . E1G F 3 .   ? -7.577  20.739  -5.210  1.00 47.46 ? 302 E1G A C8  1 
HETATM 8547 S  S9  . E1G F 3 .   ? -8.115  22.396  -4.704  1.00 60.23 ? 302 E1G A S9  1 
HETATM 8548 C  C10 . E1G F 3 .   ? -7.468  22.224  -3.019  1.00 59.70 ? 302 E1G A C10 1 
HETATM 8549 N  N12 . E1G F 3 .   ? -8.315  22.032  -1.948  1.00 56.78 ? 302 E1G A N12 1 
HETATM 8550 C  C15 . E1G F 3 .   ? -7.840  21.901  -0.675  1.00 52.06 ? 302 E1G A C15 1 
HETATM 8551 C  C16 . E1G F 3 .   ? -6.466  21.972  -0.435  1.00 53.22 ? 302 E1G A C16 1 
HETATM 8552 C  C14 . E1G F 3 .   ? -5.603  22.158  -1.514  1.00 56.66 ? 302 E1G A C14 1 
HETATM 8553 N  N11 . E1G F 3 .   ? -6.118  22.284  -2.778  1.00 60.86 ? 302 E1G A N11 1 
HETATM 8554 S  S   . DMS G 4 .   ? 17.205  14.528  -26.230 1.00 63.71 ? 303 DMS A S   1 
HETATM 8555 O  O   . DMS G 4 .   ? 17.032  13.100  -25.069 1.00 48.90 ? 303 DMS A O   1 
HETATM 8556 C  C1  . DMS G 4 .   ? 15.914  14.492  -27.451 1.00 50.29 ? 303 DMS A C1  1 
HETATM 8557 C  C2  . DMS G 4 .   ? 16.803  16.224  -25.693 1.00 55.29 ? 303 DMS A C2  1 
HETATM 8558 ZN ZN  . ZN  H 2 .   ? 0.050   -10.975 12.306  1.00 10.30 ? 301 ZN  B ZN  1 
HETATM 8559 O  O19 . E1G I 3 .   ? 2.775   -8.297  14.010  1.00 13.34 ? 302 E1G B O19 1 
HETATM 8560 S  S17 . E1G I 3 .   ? 1.754   -9.404  14.239  1.00 15.93 ? 302 E1G B S17 1 
HETATM 8561 O  O18 . E1G I 3 .   ? 2.431   -10.751 14.266  1.00 15.21 ? 302 E1G B O18 1 
HETATM 8562 N  N20 . E1G I 3 .   ? 0.527   -9.398  13.014  1.00 13.54 ? 302 E1G B N20 1 
HETATM 8563 C  C4  . E1G I 3 .   ? 1.128   -9.080  15.869  1.00 14.76 ? 302 E1G B C4  1 
HETATM 8564 C  C5  . E1G I 3 .   ? 0.402   -7.915  16.156  1.00 15.47 ? 302 E1G B C5  1 
HETATM 8565 C  C6  . E1G I 3 .   ? 0.018   -7.707  17.515  1.00 16.48 ? 302 E1G B C6  1 
HETATM 8566 C  C1  . E1G I 3 .   ? 0.305   -8.632  18.527  1.00 17.25 ? 302 E1G B C1  1 
HETATM 8567 C  C3  . E1G I 3 .   ? 1.460   -9.976  16.891  1.00 15.43 ? 302 E1G B C3  1 
HETATM 8568 C  C2  . E1G I 3 .   ? 1.053   -9.795  18.218  1.00 17.65 ? 302 E1G B C2  1 
HETATM 8569 C  C7  . E1G I 3 .   ? 1.424   -10.798 19.289  1.00 22.22 ? 302 E1G B C7  1 
HETATM 8570 O  O13 . E1G I 3 .   ? 1.828   -11.933 19.046  1.00 21.20 ? 302 E1G B O13 1 
HETATM 8571 C  C8  . E1G I 3 .   ? 1.317   -10.446 20.737  1.00 28.37 ? 302 E1G B C8  1 
HETATM 8572 S  S9  . E1G I 3 .   ? 2.609   -9.233  21.123  1.00 40.19 ? 302 E1G B S9  1 
HETATM 8573 C  C10 . E1G I 3 .   ? 1.516   -7.936  21.770  1.00 38.62 ? 302 E1G B C10 1 
HETATM 8574 N  N12 . E1G I 3 .   ? 2.043   -6.723  22.107  1.00 34.51 ? 302 E1G B N12 1 
HETATM 8575 C  C15 . E1G I 3 .   ? 1.256   -5.724  22.613  1.00 34.05 ? 302 E1G B C15 1 
HETATM 8576 C  C16 . E1G I 3 .   ? -0.115  -5.888  22.771  1.00 32.20 ? 302 E1G B C16 1 
HETATM 8577 C  C14 . E1G I 3 .   ? -0.652  -7.127  22.421  1.00 39.13 ? 302 E1G B C14 1 
HETATM 8578 N  N11 . E1G I 3 .   ? 0.161   -8.123  21.929  1.00 39.18 ? 302 E1G B N11 1 
HETATM 8579 C  C1  . PEG J 5 .   ? -4.345  -8.146  16.333  1.00 23.44 ? 303 PEG B C1  1 
HETATM 8580 O  O1  . PEG J 5 .   ? -3.916  -7.580  17.565  1.00 19.21 ? 303 PEG B O1  1 
HETATM 8581 C  C2  . PEG J 5 .   ? -4.458  -9.658  16.167  1.00 19.97 ? 303 PEG B C2  1 
HETATM 8582 O  O2  . PEG J 5 .   ? -3.440  -10.236 15.402  1.00 24.17 ? 303 PEG B O2  1 
HETATM 8583 C  C3  . PEG J 5 .   ? -2.534  -10.758 16.337  1.00 26.89 ? 303 PEG B C3  1 
HETATM 8584 C  C4  . PEG J 5 .   ? -3.119  -11.958 17.050  1.00 26.31 ? 303 PEG B C4  1 
HETATM 8585 O  O4  . PEG J 5 .   ? -2.780  -11.677 18.364  1.00 38.33 ? 303 PEG B O4  1 
HETATM 8586 C  C1  . EDO K 6 .   ? -12.976 -26.141 7.465   1.00 25.91 ? 304 EDO B C1  1 
HETATM 8587 O  O1  . EDO K 6 .   ? -12.037 -25.985 6.476   1.00 25.57 ? 304 EDO B O1  1 
HETATM 8588 C  C2  . EDO K 6 .   ? -13.568 -27.531 7.701   1.00 25.73 ? 304 EDO B C2  1 
HETATM 8589 O  O2  . EDO K 6 .   ? -12.760 -28.295 8.493   1.00 22.25 ? 304 EDO B O2  1 
HETATM 8590 ZN ZN  . ZN  L 2 .   ? 26.134  20.421  33.688  1.00 9.85  ? 301 ZN  C ZN  1 
HETATM 8591 ZN ZN  . ZN  M 2 .   ? 27.763  -6.744  50.935  1.00 9.94  ? 301 ZN  D ZN  1 
HETATM 8592 O  O19 . E1G N 3 .   ? 30.464  -4.259  52.739  1.00 13.90 ? 302 E1G D O19 1 
HETATM 8593 S  S17 . E1G N 3 .   ? 29.475  -5.389  52.973  1.00 17.60 ? 302 E1G D S17 1 
HETATM 8594 O  O18 . E1G N 3 .   ? 30.152  -6.754  52.729  1.00 15.38 ? 302 E1G D O18 1 
HETATM 8595 N  N20 . E1G N 3 .   ? 28.220  -5.231  51.812  1.00 14.14 ? 302 E1G D N20 1 
HETATM 8596 C  C4  . E1G N 3 .   ? 28.914  -5.236  54.668  1.00 18.96 ? 302 E1G D C4  1 
HETATM 8597 C  C5  . E1G N 3 .   ? 28.088  -4.154  54.988  1.00 19.09 ? 302 E1G D C5  1 
HETATM 8598 C  C6  . E1G N 3 .   ? 27.670  -4.031  56.326  1.00 21.32 ? 302 E1G D C6  1 
HETATM 8599 C  C1  . E1G N 3 .   ? 28.008  -5.007  57.299  1.00 21.79 ? 302 E1G D C1  1 
HETATM 8600 C  C3  . E1G N 3 .   ? 29.290  -6.196  55.640  1.00 19.60 ? 302 E1G D C3  1 
HETATM 8601 C  C2  . E1G N 3 .   ? 28.835  -6.101  56.962  1.00 22.13 ? 302 E1G D C2  1 
HETATM 8602 C  C7  . E1G N 3 .   ? 29.235  -7.128  57.976  1.00 26.09 ? 302 E1G D C7  1 
HETATM 8603 O  O13 . E1G N 3 .   ? 29.457  -8.273  57.597  1.00 25.16 ? 302 E1G D O13 1 
HETATM 8604 C  C8  . E1G N 3 .   ? 29.318  -6.876  59.456  1.00 29.94 ? 302 E1G D C8  1 
HETATM 8605 S  S9  . E1G N 3 .   ? 30.521  -5.572  59.897  1.00 33.01 ? 302 E1G D S9  1 
HETATM 8606 C  C10 . E1G N 3 .   ? 29.340  -4.393  60.614  1.00 35.20 ? 302 E1G D C10 1 
HETATM 8607 N  N12 . E1G N 3 .   ? 29.816  -3.269  61.256  1.00 33.60 ? 302 E1G D N12 1 
HETATM 8608 C  C15 . E1G N 3 .   ? 28.971  -2.351  61.820  1.00 35.29 ? 302 E1G D C15 1 
HETATM 8609 C  C16 . E1G N 3 .   ? 27.581  -2.541  61.757  1.00 35.77 ? 302 E1G D C16 1 
HETATM 8610 C  C14 . E1G N 3 .   ? 27.084  -3.687  61.095  1.00 35.60 ? 302 E1G D C14 1 
HETATM 8611 N  N11 . E1G N 3 .   ? 27.970  -4.582  60.539  1.00 34.47 ? 302 E1G D N11 1 
HETATM 8612 C  C1  . PEG O 5 .   ? 24.377  -7.831  55.356  1.00 21.66 ? 303 PEG D C1  1 
HETATM 8613 O  O1  . PEG O 5 .   ? 25.185  -7.408  56.356  1.00 24.99 ? 303 PEG D O1  1 
HETATM 8614 C  C2  . PEG O 5 .   ? 24.760  -6.731  54.341  1.00 21.99 ? 303 PEG D C2  1 
HETATM 8615 O  O2  . PEG O 5 .   ? 23.677  -5.897  54.066  1.00 22.20 ? 303 PEG D O2  1 
HETATM 8616 C  C3  . PEG O 5 .   ? 23.199  -5.297  55.201  1.00 19.15 ? 303 PEG D C3  1 
HETATM 8617 C  C4  . PEG O 5 .   ? 24.265  -4.294  55.616  1.00 23.57 ? 303 PEG D C4  1 
HETATM 8618 O  O4  . PEG O 5 .   ? 23.798  -3.560  56.669  1.00 21.75 ? 303 PEG D O4  1 
HETATM 8619 O  O   . HOH P 7 .   ? -2.748  8.194   4.735   1.00 9.55  ? 401 HOH A O   1 
HETATM 8620 O  O   . HOH P 7 .   ? 10.070  7.744   -9.458  1.00 9.20  ? 402 HOH A O   1 
HETATM 8621 O  O   . HOH P 7 .   ? 4.246   8.799   4.209   1.00 9.96  ? 403 HOH A O   1 
HETATM 8622 O  O   . HOH P 7 .   ? -0.049  12.250  -2.413  1.00 11.89 ? 404 HOH A O   1 
HETATM 8623 O  O   . HOH P 7 .   ? 15.732  6.760   -21.328 1.00 14.16 ? 405 HOH A O   1 
HETATM 8624 O  O   . HOH P 7 .   ? 9.836   3.990   -28.780 1.00 13.03 ? 406 HOH A O   1 
HETATM 8625 O  O   . HOH P 7 .   ? -1.718  5.751   3.368   1.00 11.81 ? 407 HOH A O   1 
HETATM 8626 O  O   . HOH P 7 .   ? -27.852 14.270  -15.504 1.00 16.56 ? 408 HOH A O   1 
HETATM 8627 O  O   . HOH P 7 .   ? -20.215 -4.319  -24.793 1.00 9.98  ? 409 HOH A O   1 
HETATM 8628 O  O   . HOH P 7 .   ? -3.495  9.386   8.452   1.00 10.06 ? 410 HOH A O   1 
HETATM 8629 O  O   . HOH P 7 .   ? -16.865 10.149  -18.713 1.00 17.00 ? 411 HOH A O   1 
HETATM 8630 O  O   . HOH P 7 .   ? -9.166  6.172   5.722   1.00 11.73 ? 412 HOH A O   1 
HETATM 8631 O  O   . HOH P 7 .   ? -11.373 0.018   -26.518 1.00 16.87 ? 413 HOH A O   1 
HETATM 8632 O  O   . HOH P 7 .   ? 8.123   9.903   -25.077 1.00 13.04 ? 414 HOH A O   1 
HETATM 8633 O  O   . HOH P 7 .   ? -2.143  2.937   2.897   1.00 7.33  ? 415 HOH A O   1 
HETATM 8634 O  O   . HOH P 7 .   ? -15.704 9.810   5.685   1.00 22.86 ? 416 HOH A O   1 
HETATM 8635 O  O   . HOH P 7 .   ? 0.920   4.166   -4.212  1.00 11.95 ? 417 HOH A O   1 
HETATM 8636 O  O   . HOH P 7 .   ? 3.599   9.500   10.706  1.00 16.43 ? 418 HOH A O   1 
HETATM 8637 O  O   . HOH P 7 .   ? -11.680 10.313  -22.839 1.00 19.15 ? 419 HOH A O   1 
HETATM 8638 O  O   . HOH P 7 .   ? -0.495  -1.527  -4.913  1.00 15.58 ? 420 HOH A O   1 
HETATM 8639 O  O   . HOH P 7 .   ? -2.274  6.885   -17.766 1.00 10.14 ? 421 HOH A O   1 
HETATM 8640 O  O   . HOH P 7 .   ? -5.411  5.612   -22.234 1.00 10.52 ? 422 HOH A O   1 
HETATM 8641 O  O   . HOH P 7 .   ? -6.173  -0.553  -3.358  1.00 16.12 ? 423 HOH A O   1 
HETATM 8642 O  O   . HOH P 7 .   ? -6.950  27.932  -23.684 1.00 17.36 ? 424 HOH A O   1 
HETATM 8643 O  O   . HOH P 7 .   ? 12.342  13.792  -29.008 1.00 14.88 ? 425 HOH A O   1 
HETATM 8644 O  O   . HOH P 7 .   ? 4.969   -0.262  -1.197  1.00 14.38 ? 426 HOH A O   1 
HETATM 8645 O  O   . HOH P 7 .   ? -21.044 -6.361  -19.922 1.00 14.85 ? 427 HOH A O   1 
HETATM 8646 O  O   . HOH P 7 .   ? 8.455   25.620  -21.401 1.00 20.06 ? 428 HOH A O   1 
HETATM 8647 O  O   . HOH P 7 .   ? 6.731   16.505  -0.728  1.00 19.28 ? 429 HOH A O   1 
HETATM 8648 O  O   . HOH P 7 .   ? 14.791  17.385  -18.346 1.00 25.12 ? 430 HOH A O   1 
HETATM 8649 O  O   . HOH P 7 .   ? -8.367  4.749   3.493   1.00 12.84 ? 431 HOH A O   1 
HETATM 8650 O  O   . HOH P 7 .   ? 8.762   14.677  -0.529  1.00 15.06 ? 432 HOH A O   1 
HETATM 8651 O  O   . HOH P 7 .   ? 2.886   12.411  -23.901 1.00 17.08 ? 433 HOH A O   1 
HETATM 8652 O  O   . HOH P 7 .   ? -24.853 1.782   -24.391 1.00 14.60 ? 434 HOH A O   1 
HETATM 8653 O  O   . HOH P 7 .   ? -12.882 11.112  3.822   1.00 12.15 ? 435 HOH A O   1 
HETATM 8654 O  O   . HOH P 7 .   ? -8.103  19.448  12.179  1.00 22.47 ? 436 HOH A O   1 
HETATM 8655 O  O   . HOH P 7 .   ? 2.032   8.116   -25.415 1.00 14.62 ? 437 HOH A O   1 
HETATM 8656 O  O   . HOH P 7 .   ? 15.866  27.375  -8.186  1.00 19.35 ? 438 HOH A O   1 
HETATM 8657 O  O   . HOH P 7 .   ? -15.024 6.205   -23.827 1.00 20.60 ? 439 HOH A O   1 
HETATM 8658 O  O   . HOH P 7 .   ? -12.562 -4.396  -26.415 1.00 19.19 ? 440 HOH A O   1 
HETATM 8659 O  O   . HOH P 7 .   ? 15.704  7.277   -11.562 1.00 12.98 ? 441 HOH A O   1 
HETATM 8660 O  O   . HOH P 7 .   ? -21.769 -1.911  -19.635 1.00 14.11 ? 442 HOH A O   1 
HETATM 8661 O  O   . HOH P 7 .   ? 1.475   4.255   4.979   1.00 10.30 ? 443 HOH A O   1 
HETATM 8662 O  O   . HOH P 7 .   ? -8.387  -3.505  -0.537  1.00 23.82 ? 444 HOH A O   1 
HETATM 8663 O  O   . HOH P 7 .   ? 3.509   7.845   8.590   1.00 16.38 ? 445 HOH A O   1 
HETATM 8664 O  O   . HOH P 7 .   ? 8.805   1.055   -25.169 1.00 18.01 ? 446 HOH A O   1 
HETATM 8665 O  O   . HOH P 7 .   ? 2.369   16.199  -3.402  1.00 15.72 ? 447 HOH A O   1 
HETATM 8666 O  O   . HOH P 7 .   ? 1.400   10.829  -25.641 1.00 17.83 ? 448 HOH A O   1 
HETATM 8667 O  O   . HOH P 7 .   ? -23.175 3.466   -24.828 1.00 13.51 ? 449 HOH A O   1 
HETATM 8668 O  O   . HOH P 7 .   ? 4.551   8.497   -24.487 1.00 16.47 ? 450 HOH A O   1 
HETATM 8669 O  O   . HOH P 7 .   ? -3.737  -0.065  -17.438 1.00 16.99 ? 451 HOH A O   1 
HETATM 8670 O  O   . HOH P 7 .   ? 15.520  15.950  -4.820  1.00 21.18 ? 452 HOH A O   1 
HETATM 8671 O  O   . HOH P 7 .   ? -18.832 8.593   -13.902 1.00 18.62 ? 453 HOH A O   1 
HETATM 8672 O  O   . HOH P 7 .   ? -11.049 11.008  -25.593 1.00 22.74 ? 454 HOH A O   1 
HETATM 8673 O  O   . HOH P 7 .   ? -6.924  2.220   3.731   1.00 10.73 ? 455 HOH A O   1 
HETATM 8674 O  O   . HOH P 7 .   ? 10.245  12.076  1.253   1.00 15.88 ? 456 HOH A O   1 
HETATM 8675 O  O   . HOH P 7 .   ? -12.018 12.933  -13.831 1.00 10.11 ? 457 HOH A O   1 
HETATM 8676 O  O   . HOH P 7 .   ? 17.024  4.270   -20.632 1.00 17.12 ? 458 HOH A O   1 
HETATM 8677 O  O   . HOH P 7 .   ? -7.709  28.063  -10.518 1.00 19.89 ? 459 HOH A O   1 
HETATM 8678 O  O   . HOH P 7 .   ? 11.504  22.846  -23.468 1.00 27.84 ? 460 HOH A O   1 
HETATM 8679 O  O   . HOH P 7 .   ? -11.407 -2.306  -25.136 1.00 15.65 ? 461 HOH A O   1 
HETATM 8680 O  O   . HOH P 7 .   ? -6.218  -3.591  -16.171 1.00 25.82 ? 462 HOH A O   1 
HETATM 8681 O  O   . HOH P 7 .   ? 1.189   1.854   -2.707  1.00 15.80 ? 463 HOH A O   1 
HETATM 8682 O  O   . HOH P 7 .   ? 10.315  14.804  6.275   1.00 18.63 ? 464 HOH A O   1 
HETATM 8683 O  O   . HOH P 7 .   ? -21.659 -6.335  -15.760 1.00 21.27 ? 465 HOH A O   1 
HETATM 8684 O  O   . HOH P 7 .   ? -12.933 1.701   -25.151 1.00 21.97 ? 466 HOH A O   1 
HETATM 8685 O  O   . HOH P 7 .   ? 7.591   22.298  3.157   1.00 29.01 ? 467 HOH A O   1 
HETATM 8686 O  O   . HOH P 7 .   ? -5.903  -9.815  -7.886  1.00 23.77 ? 468 HOH A O   1 
HETATM 8687 O  O   . HOH P 7 .   ? 11.171  3.451   -13.231 1.00 17.16 ? 469 HOH A O   1 
HETATM 8688 O  O   . HOH P 7 .   ? 8.048   14.899  2.369   1.00 21.34 ? 470 HOH A O   1 
HETATM 8689 O  O   . HOH P 7 .   ? 7.076   26.283  -25.681 1.00 23.52 ? 471 HOH A O   1 
HETATM 8690 O  O   . HOH P 7 .   ? 11.242  9.647   1.897   1.00 15.69 ? 472 HOH A O   1 
HETATM 8691 O  O   . HOH P 7 .   ? -3.156  -6.390  -7.078  1.00 17.23 ? 473 HOH A O   1 
HETATM 8692 O  O   . HOH P 7 .   ? 14.379  7.336   -0.368  1.00 21.22 ? 474 HOH A O   1 
HETATM 8693 O  O   . HOH P 7 .   ? -11.771 13.251  -26.809 1.00 21.22 ? 475 HOH A O   1 
HETATM 8694 O  O   . HOH P 7 .   ? 6.392   26.058  -23.037 1.00 14.66 ? 476 HOH A O   1 
HETATM 8695 O  O   . HOH P 7 .   ? -0.669  31.210  -14.408 1.00 23.63 ? 477 HOH A O   1 
HETATM 8696 O  O   . HOH P 7 .   ? 10.426  20.434  -25.649 1.00 16.77 ? 478 HOH A O   1 
HETATM 8697 O  O   . HOH P 7 .   ? -19.376 9.031   -19.579 1.00 22.26 ? 479 HOH A O   1 
HETATM 8698 O  O   . HOH P 7 .   ? 16.635  23.894  1.276   1.00 14.94 ? 480 HOH A O   1 
HETATM 8699 O  O   . HOH P 7 .   ? -11.837 -0.884  -29.060 1.00 18.09 ? 481 HOH A O   1 
HETATM 8700 O  O   . HOH P 7 .   ? 0.467   6.132   -24.543 1.00 17.40 ? 482 HOH A O   1 
HETATM 8701 O  O   . HOH P 7 .   ? 12.207  25.529  4.698   1.00 21.95 ? 483 HOH A O   1 
HETATM 8702 O  O   . HOH P 7 .   ? -10.150 19.467  6.680   1.00 19.16 ? 484 HOH A O   1 
HETATM 8703 O  O   . HOH P 7 .   ? 17.041  12.390  -5.141  1.00 26.44 ? 485 HOH A O   1 
HETATM 8704 O  O   . HOH P 7 .   ? -7.533  24.598  -27.286 1.00 19.53 ? 486 HOH A O   1 
HETATM 8705 O  O   . HOH P 7 .   ? -11.027 4.997   2.392   1.00 16.40 ? 487 HOH A O   1 
HETATM 8706 O  O   . HOH P 7 .   ? -5.905  20.444  -27.441 1.00 21.81 ? 488 HOH A O   1 
HETATM 8707 O  O   . HOH P 7 .   ? -15.970 11.093  -4.099  1.00 16.19 ? 489 HOH A O   1 
HETATM 8708 O  O   . HOH P 7 .   ? -9.296  16.745  6.500   1.00 12.53 ? 490 HOH A O   1 
HETATM 8709 O  O   . HOH P 7 .   ? -15.066 4.279   1.587   1.00 22.47 ? 491 HOH A O   1 
HETATM 8710 O  O   . HOH P 7 .   ? 7.752   14.484  8.937   1.00 17.25 ? 492 HOH A O   1 
HETATM 8711 O  O   . HOH P 7 .   ? -8.238  28.181  -13.234 1.00 19.13 ? 493 HOH A O   1 
HETATM 8712 O  O   . HOH P 7 .   ? 9.513   2.878   -15.369 1.00 16.74 ? 494 HOH A O   1 
HETATM 8713 O  O   . HOH P 7 .   ? -24.770 -5.031  -17.820 1.00 21.48 ? 495 HOH A O   1 
HETATM 8714 O  O   . HOH P 7 .   ? 1.955   13.759  13.694  1.00 25.15 ? 496 HOH A O   1 
HETATM 8715 O  O   . HOH P 7 .   ? 17.778  5.829   -11.051 1.00 26.56 ? 497 HOH A O   1 
HETATM 8716 O  O   . HOH P 7 .   ? -5.173  0.462   -25.538 1.00 26.17 ? 498 HOH A O   1 
HETATM 8717 O  O   . HOH P 7 .   ? 0.485   18.289  -4.226  1.00 26.99 ? 499 HOH A O   1 
HETATM 8718 O  O   . HOH P 7 .   ? -22.814 17.567  -11.784 1.00 24.19 ? 500 HOH A O   1 
HETATM 8719 O  O   . HOH P 7 .   ? 10.413  15.590  3.662   1.00 21.47 ? 501 HOH A O   1 
HETATM 8720 O  O   . HOH P 7 .   ? 13.627  17.387  9.149   1.00 32.61 ? 502 HOH A O   1 
HETATM 8721 O  O   . HOH P 7 .   ? -14.406 12.919  5.146   1.00 19.60 ? 503 HOH A O   1 
HETATM 8722 O  O   . HOH P 7 .   ? -14.242 14.033  8.960   1.00 26.86 ? 504 HOH A O   1 
HETATM 8723 O  O   . HOH P 7 .   ? 12.154  14.077  2.121   1.00 17.52 ? 505 HOH A O   1 
HETATM 8724 O  O   . HOH P 7 .   ? -8.346  21.442  -26.509 1.00 21.66 ? 506 HOH A O   1 
HETATM 8725 O  O   . HOH P 7 .   ? -23.614 -7.281  -17.362 1.00 18.12 ? 507 HOH A O   1 
HETATM 8726 O  O   . HOH P 7 .   ? -17.557 17.562  -17.792 1.00 18.48 ? 508 HOH A O   1 
HETATM 8727 O  O   . HOH P 7 .   ? -4.606  -8.426  -5.737  1.00 21.47 ? 509 HOH A O   1 
HETATM 8728 O  O   . HOH P 7 .   ? -19.742 -5.260  -17.318 1.00 20.13 ? 510 HOH A O   1 
HETATM 8729 O  O   . HOH P 7 .   ? 5.922   17.196  1.525   1.00 21.95 ? 511 HOH A O   1 
HETATM 8730 O  O   . HOH P 7 .   ? -9.759  3.110   -28.603 1.00 33.41 ? 512 HOH A O   1 
HETATM 8731 O  O   . HOH P 7 .   ? 6.015   2.348   -1.433  1.00 27.76 ? 513 HOH A O   1 
HETATM 8732 O  O   . HOH P 7 .   ? -0.105  24.874  -3.767  1.00 27.99 ? 514 HOH A O   1 
HETATM 8733 O  O   . HOH P 7 .   ? -11.366 9.500   -28.119 1.00 29.25 ? 515 HOH A O   1 
HETATM 8734 O  O   . HOH P 7 .   ? 13.523  16.114  -29.452 1.00 20.99 ? 516 HOH A O   1 
HETATM 8735 O  O   . HOH P 7 .   ? -25.438 -9.093  -15.869 1.00 28.51 ? 517 HOH A O   1 
HETATM 8736 O  O   . HOH P 7 .   ? -1.015  -1.439  -16.907 1.00 31.71 ? 518 HOH A O   1 
HETATM 8737 O  O   . HOH P 7 .   ? 7.644   2.238   -28.384 1.00 26.71 ? 519 HOH A O   1 
HETATM 8738 O  O   . HOH P 7 .   ? 5.140   6.995   5.876   1.00 24.49 ? 520 HOH A O   1 
HETATM 8739 O  O   . HOH P 7 .   ? 10.960  1.078   -17.132 1.00 22.90 ? 521 HOH A O   1 
HETATM 8740 O  O   . HOH P 7 .   ? -11.031 19.605  11.182  1.00 23.40 ? 522 HOH A O   1 
HETATM 8741 O  O   . HOH P 7 .   ? 5.857   20.165  5.117   1.00 21.54 ? 523 HOH A O   1 
HETATM 8742 O  O   . HOH P 7 .   ? -4.056  -8.846  -10.252 1.00 28.34 ? 524 HOH A O   1 
HETATM 8743 O  O   . HOH P 7 .   ? -12.992 -9.573  -15.294 1.00 25.06 ? 525 HOH A O   1 
HETATM 8744 O  O   . HOH P 7 .   ? -11.470 -11.627 -13.870 1.00 24.93 ? 526 HOH A O   1 
HETATM 8745 O  O   . HOH P 7 .   ? 12.100  18.631  -27.101 1.00 30.30 ? 527 HOH A O   1 
HETATM 8746 O  O   . HOH P 7 .   ? 12.024  12.051  9.741   1.00 22.26 ? 528 HOH A O   1 
HETATM 8747 O  O   . HOH P 7 .   ? -2.437  16.725  15.844  1.00 28.08 ? 529 HOH A O   1 
HETATM 8748 O  O   . HOH P 7 .   ? -10.815 22.322  1.105   1.00 29.52 ? 530 HOH A O   1 
HETATM 8749 O  O   . HOH P 7 .   ? -10.735 3.899   -0.516  1.00 17.54 ? 531 HOH A O   1 
HETATM 8750 O  O   . HOH P 7 .   ? -8.994  -3.551  -3.271  1.00 28.45 ? 532 HOH A O   1 
HETATM 8751 O  O   . HOH P 7 .   ? -16.743 4.666   -7.489  1.00 17.09 ? 533 HOH A O   1 
HETATM 8752 O  O   . HOH P 7 .   ? -24.467 2.179   -16.900 1.00 25.45 ? 534 HOH A O   1 
HETATM 8753 O  O   . HOH P 7 .   ? -22.075 5.641   -16.381 1.00 36.74 ? 535 HOH A O   1 
HETATM 8754 O  O   . HOH P 7 .   ? -14.946 4.919   -26.630 1.00 29.24 ? 536 HOH A O   1 
HETATM 8755 O  O   . HOH P 7 .   ? -20.421 18.059  -20.230 1.00 29.02 ? 537 HOH A O   1 
HETATM 8756 O  O   . HOH P 7 .   ? -11.366 16.340  -27.054 1.00 27.63 ? 538 HOH A O   1 
HETATM 8757 O  O   . HOH P 7 .   ? -3.501  28.495  -28.744 1.00 29.78 ? 539 HOH A O   1 
HETATM 8758 O  O   . HOH P 7 .   ? 0.711   35.856  -19.938 1.00 23.51 ? 540 HOH A O   1 
HETATM 8759 O  O   . HOH P 7 .   ? 10.721  32.360  -15.657 1.00 22.51 ? 541 HOH A O   1 
HETATM 8760 O  O   . HOH P 7 .   ? -8.122  31.517  -14.792 1.00 31.88 ? 542 HOH A O   1 
HETATM 8761 O  O   . HOH P 7 .   ? -25.797 12.350  -16.019 1.00 22.10 ? 543 HOH A O   1 
HETATM 8762 O  O   . HOH P 7 .   ? -9.775  28.772  -6.295  1.00 33.11 ? 544 HOH A O   1 
HETATM 8763 O  O   . HOH P 7 .   ? 9.605   4.464   -4.283  1.00 18.31 ? 545 HOH A O   1 
HETATM 8764 O  O   . HOH P 7 .   ? 1.335   -6.397  -14.483 1.00 28.50 ? 546 HOH A O   1 
HETATM 8765 O  O   . HOH P 7 .   ? 6.855   2.276   -15.006 1.00 19.71 ? 547 HOH A O   1 
HETATM 8766 O  O   . HOH P 7 .   ? -25.602 24.012  -13.480 1.00 37.44 ? 548 HOH A O   1 
HETATM 8767 O  O   . HOH P 7 .   ? -25.682 26.047  -9.068  1.00 33.10 ? 549 HOH A O   1 
HETATM 8768 O  O   . HOH P 7 .   ? 5.836   14.791  -26.599 1.00 23.66 ? 550 HOH A O   1 
HETATM 8769 O  O   . HOH P 7 .   ? 12.769  30.664  -11.519 1.00 25.00 ? 551 HOH A O   1 
HETATM 8770 O  O   . HOH P 7 .   ? 11.190  32.442  -7.668  1.00 25.79 ? 552 HOH A O   1 
HETATM 8771 O  O   . HOH P 7 .   ? 12.975  29.517  -1.226  1.00 20.86 ? 553 HOH A O   1 
HETATM 8772 O  O   . HOH P 7 .   ? 4.508   20.103  -27.029 1.00 38.89 ? 554 HOH A O   1 
HETATM 8773 O  O   . HOH P 7 .   ? 0.135   3.309   -25.552 1.00 33.36 ? 555 HOH A O   1 
HETATM 8774 O  O   . HOH P 7 .   ? -4.529  7.783   -29.636 1.00 27.65 ? 556 HOH A O   1 
HETATM 8775 O  O   . HOH P 7 .   ? -8.826  -3.326  -25.386 1.00 28.99 ? 557 HOH A O   1 
HETATM 8776 O  O   . HOH P 7 .   ? -17.641 2.382   4.437   1.00 35.44 ? 558 HOH A O   1 
HETATM 8777 O  O   . HOH P 7 .   ? -6.143  -7.285  -3.852  1.00 27.41 ? 559 HOH A O   1 
HETATM 8778 O  O   . HOH P 7 .   ? -0.624  29.460  -29.537 1.00 22.78 ? 560 HOH A O   1 
HETATM 8779 O  O   . HOH P 7 .   ? 12.544  28.568  -15.701 1.00 21.70 ? 561 HOH A O   1 
HETATM 8780 O  O   . HOH P 7 .   ? 13.261  26.035  -20.372 1.00 30.20 ? 562 HOH A O   1 
HETATM 8781 O  O   . HOH P 7 .   ? 17.886  8.275   -21.682 1.00 30.48 ? 563 HOH A O   1 
HETATM 8782 O  O   . HOH P 7 .   ? 1.901   38.199  -25.727 1.00 17.30 ? 564 HOH A O   1 
HETATM 8783 O  O   . HOH P 7 .   ? 3.411   36.211  -22.478 1.00 20.83 ? 565 HOH A O   1 
HETATM 8784 O  O   . HOH P 7 .   ? -5.111  29.959  -24.068 1.00 18.64 ? 566 HOH A O   1 
HETATM 8785 O  O   . HOH P 7 .   ? -6.196  30.897  -21.595 1.00 19.63 ? 567 HOH A O   1 
HETATM 8786 O  O   . HOH P 7 .   ? 18.158  29.538  -11.433 1.00 18.25 ? 568 HOH A O   1 
HETATM 8787 O  O   . HOH P 7 .   ? 21.234  27.639  -12.906 1.00 26.44 ? 569 HOH A O   1 
HETATM 8788 O  O   . HOH P 7 .   ? -23.378 -5.929  -13.338 1.00 26.98 ? 570 HOH A O   1 
HETATM 8789 O  O   . HOH P 7 .   ? 7.870   7.940   7.336   1.00 32.67 ? 571 HOH A O   1 
HETATM 8790 O  O   . HOH P 7 .   ? -16.920 14.059  4.300   1.00 25.34 ? 572 HOH A O   1 
HETATM 8791 O  O   . HOH P 7 .   ? -5.442  -7.740  -11.916 1.00 20.18 ? 573 HOH A O   1 
HETATM 8792 O  O   . HOH P 7 .   ? -12.958 -4.197  -17.001 1.00 22.94 ? 574 HOH A O   1 
HETATM 8793 O  O   . HOH P 7 .   ? -16.970 3.155   -23.234 1.00 30.88 ? 575 HOH A O   1 
HETATM 8794 O  O   . HOH P 7 .   ? -15.238 16.375  -30.790 1.00 30.49 ? 576 HOH A O   1 
HETATM 8795 O  O   . HOH P 7 .   ? 0.444   25.742  -1.348  1.00 34.15 ? 577 HOH A O   1 
HETATM 8796 O  O   . HOH P 7 .   ? -4.918  28.276  -11.432 1.00 23.57 ? 578 HOH A O   1 
HETATM 8797 O  O   . HOH P 7 .   ? 6.161   -1.861  -9.890  1.00 32.95 ? 579 HOH A O   1 
HETATM 8798 O  O   . HOH P 7 .   ? 1.021   -8.023  -12.171 1.00 29.77 ? 580 HOH A O   1 
HETATM 8799 O  O   . HOH P 7 .   ? 7.774   5.641   -26.744 1.00 31.39 ? 581 HOH A O   1 
HETATM 8800 O  O   . HOH P 7 .   ? 5.771   10.120  -26.497 1.00 20.87 ? 582 HOH A O   1 
HETATM 8801 O  O   . HOH P 7 .   ? 4.638   1.842   -22.971 1.00 23.80 ? 583 HOH A O   1 
HETATM 8802 O  O   . HOH P 7 .   ? 16.800  12.998  -22.065 1.00 27.45 ? 584 HOH A O   1 
HETATM 8803 O  O   . HOH P 7 .   ? 21.395  24.153  -5.014  1.00 29.91 ? 585 HOH A O   1 
HETATM 8804 O  O   . HOH P 7 .   ? 19.880  22.268  -0.895  1.00 30.66 ? 586 HOH A O   1 
HETATM 8805 O  O   . HOH P 7 .   ? -6.580  9.488   -27.797 1.00 22.77 ? 587 HOH A O   1 
HETATM 8806 O  O   . HOH P 7 .   ? 18.298  18.733  10.859  1.00 32.86 ? 588 HOH A O   1 
HETATM 8807 O  O   . HOH P 7 .   ? -17.762 -7.052  -18.631 1.00 30.63 ? 589 HOH A O   1 
HETATM 8808 O  O   . HOH P 7 .   ? 8.343   35.705  -17.866 1.00 25.11 ? 590 HOH A O   1 
HETATM 8809 O  O   . HOH P 7 .   ? 13.043  16.306  -6.971  1.00 16.47 ? 591 HOH A O   1 
HETATM 8810 O  O   . HOH P 7 .   ? -7.403  -0.993  -27.301 1.00 27.46 ? 592 HOH A O   1 
HETATM 8811 O  O   . HOH P 7 .   ? 8.254   32.383  -20.570 1.00 34.25 ? 593 HOH A O   1 
HETATM 8812 O  O   . HOH P 7 .   ? -12.298 5.284   -3.207  1.00 24.15 ? 594 HOH A O   1 
HETATM 8813 O  O   . HOH P 7 .   ? -9.011  7.736   -27.672 1.00 24.16 ? 595 HOH A O   1 
HETATM 8814 O  O   . HOH P 7 .   ? -21.306 -9.570  -1.479  1.00 28.41 ? 596 HOH A O   1 
HETATM 8815 O  O   . HOH P 7 .   ? -18.764 5.152   -4.378  1.00 34.47 ? 597 HOH A O   1 
HETATM 8816 O  O   . HOH P 7 .   ? 14.570  27.321  -18.242 1.00 32.87 ? 598 HOH A O   1 
HETATM 8817 O  O   . HOH P 7 .   ? 2.556   14.181  -27.154 1.00 29.85 ? 599 HOH A O   1 
HETATM 8818 O  O   . HOH P 7 .   ? 2.608   22.217  -27.857 1.00 26.33 ? 600 HOH A O   1 
HETATM 8819 O  O   . HOH P 7 .   ? -16.589 16.371  1.833   1.00 39.32 ? 601 HOH A O   1 
HETATM 8820 O  O   . HOH P 7 .   ? -9.111  -1.430  -29.777 1.00 28.27 ? 602 HOH A O   1 
HETATM 8821 O  O   . HOH P 7 .   ? 8.110   35.474  -9.888  1.00 34.83 ? 603 HOH A O   1 
HETATM 8822 O  O   . HOH P 7 .   ? 1.075   14.900  9.402   1.00 23.49 ? 604 HOH A O   1 
HETATM 8823 O  O   . HOH P 7 .   ? 7.285   19.224  2.999   1.00 29.34 ? 605 HOH A O   1 
HETATM 8824 O  O   . HOH P 7 .   ? 12.604  14.218  7.412   1.00 31.67 ? 606 HOH A O   1 
HETATM 8825 O  O   . HOH P 7 .   ? -18.615 0.771   -6.100  1.00 39.65 ? 607 HOH A O   1 
HETATM 8826 O  O   . HOH P 7 .   ? -21.417 -1.627  -15.389 1.00 30.59 ? 608 HOH A O   1 
HETATM 8827 O  O   . HOH P 7 .   ? -15.979 -7.886  -14.884 1.00 24.03 ? 609 HOH A O   1 
HETATM 8828 O  O   . HOH P 7 .   ? -17.958 0.970   -24.551 1.00 30.19 ? 610 HOH A O   1 
HETATM 8829 O  O   . HOH P 7 .   ? -20.627 8.594   -15.596 1.00 32.82 ? 611 HOH A O   1 
HETATM 8830 O  O   . HOH P 7 .   ? -17.634 12.029  -26.138 1.00 27.53 ? 612 HOH A O   1 
HETATM 8831 O  O   . HOH P 7 .   ? -10.477 23.378  -27.917 1.00 28.85 ? 613 HOH A O   1 
HETATM 8832 O  O   . HOH P 7 .   ? 0.010   19.607  -30.437 1.00 36.75 ? 614 HOH A O   1 
HETATM 8833 O  O   . HOH P 7 .   ? -0.154  25.798  -27.841 1.00 21.20 ? 615 HOH A O   1 
HETATM 8834 O  O   . HOH P 7 .   ? -5.740  35.451  -20.381 1.00 24.48 ? 616 HOH A O   1 
HETATM 8835 O  O   . HOH P 7 .   ? 1.725   27.549  -9.803  1.00 25.11 ? 617 HOH A O   1 
HETATM 8836 O  O   . HOH P 7 .   ? -24.147 13.706  -18.401 1.00 29.19 ? 618 HOH A O   1 
HETATM 8837 O  O   . HOH P 7 .   ? 17.950  2.050   -9.442  1.00 30.10 ? 619 HOH A O   1 
HETATM 8838 O  O   . HOH P 7 .   ? 4.209   -2.009  -6.415  1.00 27.16 ? 620 HOH A O   1 
HETATM 8839 O  O   . HOH P 7 .   ? -17.444 28.973  -11.952 1.00 30.70 ? 621 HOH A O   1 
HETATM 8840 O  O   . HOH P 7 .   ? -10.809 28.694  -8.883  1.00 28.46 ? 622 HOH A O   1 
HETATM 8841 O  O   . HOH P 7 .   ? 16.050  30.825  -9.408  1.00 38.61 ? 623 HOH A O   1 
HETATM 8842 O  O   . HOH P 7 .   ? -4.317  11.352  -26.927 1.00 29.33 ? 624 HOH A O   1 
HETATM 8843 O  O   . HOH P 7 .   ? 18.717  16.089  -16.960 1.00 31.00 ? 625 HOH A O   1 
HETATM 8844 O  O   . HOH P 7 .   ? 17.459  10.512  -2.987  1.00 27.87 ? 626 HOH A O   1 
HETATM 8845 O  O   . HOH P 7 .   ? -13.688 0.350   0.740   1.00 34.83 ? 627 HOH A O   1 
HETATM 8846 O  O   . HOH P 7 .   ? 18.281  16.025  -4.590  1.00 28.26 ? 628 HOH A O   1 
HETATM 8847 O  O   . HOH P 7 .   ? -4.341  -2.088  -19.471 1.00 29.14 ? 629 HOH A O   1 
HETATM 8848 O  O   . HOH P 7 .   ? -1.981  36.595  -19.131 1.00 24.45 ? 630 HOH A O   1 
HETATM 8849 O  O   . HOH P 7 .   ? 6.071   0.564   -16.627 1.00 27.95 ? 631 HOH A O   1 
HETATM 8850 O  O   . HOH P 7 .   ? -1.239  15.664  10.767  1.00 29.76 ? 632 HOH A O   1 
HETATM 8851 O  O   . HOH P 7 .   ? 8.585   34.473  -5.994  1.00 38.21 ? 633 HOH A O   1 
HETATM 8852 O  O   . HOH P 7 .   ? -0.784  30.384  -7.209  1.00 29.88 ? 634 HOH A O   1 
HETATM 8853 O  O   . HOH P 7 .   ? 14.594  32.357  -10.930 1.00 37.44 ? 635 HOH A O   1 
HETATM 8854 O  O   . HOH P 7 .   ? 13.063  33.188  -6.338  1.00 33.78 ? 636 HOH A O   1 
HETATM 8855 O  O   . HOH P 7 .   ? 0.905   14.326  16.036  1.00 35.52 ? 637 HOH A O   1 
HETATM 8856 O  O   . HOH P 7 .   ? -18.109 12.481  -0.504  1.00 21.09 ? 638 HOH A O   1 
HETATM 8857 O  O   . HOH P 7 .   ? -4.795  -4.854  -4.271  1.00 26.61 ? 639 HOH A O   1 
HETATM 8858 O  O   . HOH P 7 .   ? -14.910 -7.200  -5.512  1.00 28.01 ? 640 HOH A O   1 
HETATM 8859 O  O   . HOH P 7 .   ? -18.991 22.879  -26.679 1.00 33.89 ? 641 HOH A O   1 
HETATM 8860 O  O   . HOH P 7 .   ? 5.302   27.882  -29.155 1.00 30.21 ? 642 HOH A O   1 
HETATM 8861 O  O   . HOH P 7 .   ? 3.930   26.478  -27.417 1.00 31.30 ? 643 HOH A O   1 
HETATM 8862 O  O   . HOH P 7 .   ? 20.216  6.635   -10.909 1.00 28.79 ? 644 HOH A O   1 
HETATM 8863 O  O   . HOH P 7 .   ? 1.624   -1.788  -18.304 1.00 34.25 ? 645 HOH A O   1 
HETATM 8864 O  O   . HOH P 7 .   ? 7.621   1.140   -12.578 1.00 34.83 ? 646 HOH A O   1 
HETATM 8865 O  O   . HOH P 7 .   ? -17.292 28.231  0.794   1.00 32.72 ? 647 HOH A O   1 
HETATM 8866 O  O   . HOH P 7 .   ? 18.587  27.917  -8.710  1.00 31.11 ? 648 HOH A O   1 
HETATM 8867 O  O   . HOH P 7 .   ? -6.570  12.724  -26.465 1.00 32.25 ? 649 HOH A O   1 
HETATM 8868 O  O   . HOH P 7 .   ? 8.424   26.074  5.050   1.00 38.45 ? 650 HOH A O   1 
HETATM 8869 O  O   . HOH P 7 .   ? -12.642 -12.454 -7.319  1.00 35.14 ? 651 HOH A O   1 
HETATM 8870 O  O   . HOH P 7 .   ? -2.160  22.685  -3.887  1.00 31.27 ? 652 HOH A O   1 
HETATM 8871 O  O   . HOH P 7 .   ? -11.719 33.736  -15.399 1.00 32.83 ? 653 HOH A O   1 
HETATM 8872 O  O   . HOH P 7 .   ? -14.087 26.933  -19.419 1.00 30.77 ? 654 HOH A O   1 
HETATM 8873 O  O   . HOH P 7 .   ? -20.575 15.896  -12.426 1.00 31.09 ? 655 HOH A O   1 
HETATM 8874 O  O   . HOH P 7 .   ? 16.819  15.787  -20.902 1.00 26.84 ? 656 HOH A O   1 
HETATM 8875 O  O   . HOH P 7 .   ? 16.357  14.807  2.306   1.00 26.20 ? 657 HOH A O   1 
HETATM 8876 O  O   . HOH P 7 .   ? 17.030  9.988   -23.883 1.00 29.73 ? 658 HOH A O   1 
HETATM 8877 O  O   . HOH Q 7 .   ? -0.008  2.028   4.101   1.00 10.99 ? 401 HOH B O   1 
HETATM 8878 O  O   . HOH Q 7 .   ? -7.941  -0.171  7.484   1.00 11.45 ? 402 HOH B O   1 
HETATM 8879 O  O   . HOH Q 7 .   ? 4.845   5.477   9.976   1.00 12.44 ? 403 HOH B O   1 
HETATM 8880 O  O   . HOH Q 7 .   ? -2.496  -6.061  10.661  1.00 10.51 ? 404 HOH B O   1 
HETATM 8881 O  O   . HOH Q 7 .   ? -1.451  1.654   6.641   1.00 9.13  ? 405 HOH B O   1 
HETATM 8882 O  O   . HOH Q 7 .   ? -5.139  -31.074 16.534  1.00 14.31 ? 406 HOH B O   1 
HETATM 8883 O  O   . HOH Q 7 .   ? 4.227   4.428   5.221   1.00 12.37 ? 407 HOH B O   1 
HETATM 8884 O  O   . HOH Q 7 .   ? -2.308  5.517   11.505  1.00 11.10 ? 408 HOH B O   1 
HETATM 8885 O  O   . HOH Q 7 .   ? -1.624  2.329   9.756   1.00 12.50 ? 409 HOH B O   1 
HETATM 8886 O  O   . HOH Q 7 .   ? -9.900  10.537  10.891  1.00 16.84 ? 410 HOH B O   1 
HETATM 8887 O  O   . HOH Q 7 .   ? -4.575  -17.691 -4.247  1.00 12.50 ? 411 HOH B O   1 
HETATM 8888 O  O   . HOH Q 7 .   ? -7.416  -30.298 15.374  1.00 19.56 ? 412 HOH B O   1 
HETATM 8889 O  O   . HOH Q 7 .   ? -13.839 1.661   12.484  1.00 19.33 ? 413 HOH B O   1 
HETATM 8890 O  O   . HOH Q 7 .   ? -4.480  -2.394  -2.165  1.00 19.95 ? 414 HOH B O   1 
HETATM 8891 O  O   . HOH Q 7 .   ? 11.850  -13.818 12.524  1.00 12.77 ? 415 HOH B O   1 
HETATM 8892 O  O   . HOH Q 7 .   ? 3.220   -3.273  24.030  1.00 20.15 ? 416 HOH B O   1 
HETATM 8893 O  O   . HOH Q 7 .   ? 4.305   -30.613 23.402  1.00 21.72 ? 417 HOH B O   1 
HETATM 8894 O  O   . HOH Q 7 .   ? -13.942 -14.860 9.131   1.00 12.72 ? 418 HOH B O   1 
HETATM 8895 O  O   . HOH Q 7 .   ? -0.854  -5.459  2.635   1.00 9.20  ? 419 HOH B O   1 
HETATM 8896 O  O   . HOH Q 7 .   ? 6.664   -1.384  0.897   1.00 12.32 ? 420 HOH B O   1 
HETATM 8897 O  O   . HOH Q 7 .   ? 1.433   -21.031 26.516  1.00 16.30 ? 421 HOH B O   1 
HETATM 8898 O  O   . HOH Q 7 .   ? -12.454 -16.931 -1.332  1.00 16.66 ? 422 HOH B O   1 
HETATM 8899 O  O   . HOH Q 7 .   ? 15.349  -20.982 7.660   1.00 16.94 ? 423 HOH B O   1 
HETATM 8900 O  O   . HOH Q 7 .   ? 4.947   3.704   7.881   1.00 7.08  ? 424 HOH B O   1 
HETATM 8901 O  O   . HOH Q 7 .   ? -5.284  -8.938  13.205  1.00 11.59 ? 425 HOH B O   1 
HETATM 8902 O  O   . HOH Q 7 .   ? 4.651   -34.447 26.272  1.00 13.58 ? 426 HOH B O   1 
HETATM 8903 O  O   . HOH Q 7 .   ? -9.634  5.838   10.195  1.00 16.01 ? 427 HOH B O   1 
HETATM 8904 O  O   . HOH Q 7 .   ? 2.357   -4.051  -2.513  1.00 18.66 ? 428 HOH B O   1 
HETATM 8905 O  O   . HOH Q 7 .   ? 5.981   -24.722 -0.315  1.00 16.32 ? 429 HOH B O   1 
HETATM 8906 O  O   . HOH Q 7 .   ? 1.838   2.938   19.857  1.00 10.95 ? 430 HOH B O   1 
HETATM 8907 O  O   . HOH Q 7 .   ? 17.524  -29.319 21.032  1.00 20.28 ? 431 HOH B O   1 
HETATM 8908 O  O   . HOH Q 7 .   ? 10.711  -18.208 28.657  1.00 20.60 ? 432 HOH B O   1 
HETATM 8909 O  O   . HOH Q 7 .   ? -11.686 -7.305  10.364  1.00 15.78 ? 433 HOH B O   1 
HETATM 8910 O  O   . HOH Q 7 .   ? 14.265  -1.968  8.546   1.00 14.05 ? 434 HOH B O   1 
HETATM 8911 O  O   . HOH Q 7 .   ? 8.484   2.709   -0.313  1.00 16.59 ? 435 HOH B O   1 
HETATM 8912 O  O   . HOH Q 7 .   ? 1.634   -26.628 4.831   1.00 20.28 ? 436 HOH B O   1 
HETATM 8913 O  O   . HOH Q 7 .   ? -12.072 -19.571 -2.087  1.00 18.42 ? 437 HOH B O   1 
HETATM 8914 O  O   . HOH Q 7 .   ? -2.586  -22.898 25.496  1.00 18.18 ? 438 HOH B O   1 
HETATM 8915 O  O   . HOH Q 7 .   ? 6.800   -28.865 22.634  1.00 30.49 ? 439 HOH B O   1 
HETATM 8916 O  O   . HOH Q 7 .   ? -2.244  -16.309 -3.774  1.00 14.42 ? 440 HOH B O   1 
HETATM 8917 O  O   . HOH Q 7 .   ? -17.369 -13.166 4.575   1.00 17.85 ? 441 HOH B O   1 
HETATM 8918 O  O   . HOH Q 7 .   ? -2.486  -29.800 27.894  1.00 21.24 ? 442 HOH B O   1 
HETATM 8919 O  O   . HOH Q 7 .   ? -8.418  4.310   7.835   1.00 14.89 ? 443 HOH B O   1 
HETATM 8920 O  O   . HOH Q 7 .   ? 15.146  -23.710 7.565   1.00 20.27 ? 444 HOH B O   1 
HETATM 8921 O  O   . HOH Q 7 .   ? -4.541  2.831   4.574   1.00 7.42  ? 445 HOH B O   1 
HETATM 8922 O  O   . HOH Q 7 .   ? 6.272   -17.076 28.973  1.00 21.28 ? 446 HOH B O   1 
HETATM 8923 O  O   . HOH Q 7 .   ? -5.428  -18.237 22.294  1.00 14.68 ? 447 HOH B O   1 
HETATM 8924 O  O   . HOH Q 7 .   ? -6.895  -16.201 -3.782  1.00 13.25 ? 448 HOH B O   1 
HETATM 8925 O  O   . HOH Q 7 .   ? -1.641  -28.209 0.331   1.00 17.97 ? 449 HOH B O   1 
HETATM 8926 O  O   . HOH Q 7 .   ? -16.786 -13.540 8.357   1.00 15.42 ? 450 HOH B O   1 
HETATM 8927 O  O   . HOH Q 7 .   ? -1.543  -6.661  -4.845  1.00 29.05 ? 451 HOH B O   1 
HETATM 8928 O  O   . HOH Q 7 .   ? 5.905   -18.047 2.738   1.00 13.36 ? 452 HOH B O   1 
HETATM 8929 O  O   . HOH Q 7 .   ? 13.771  -8.834  17.710  1.00 22.11 ? 453 HOH B O   1 
HETATM 8930 O  O   . HOH Q 7 .   ? 12.746  -3.915  14.774  1.00 16.87 ? 454 HOH B O   1 
HETATM 8931 O  O   . HOH Q 7 .   ? -8.728  -7.990  -0.112  1.00 14.81 ? 455 HOH B O   1 
HETATM 8932 O  O   . HOH Q 7 .   ? 10.591  -2.923  -8.984  1.00 23.40 ? 456 HOH B O   1 
HETATM 8933 O  O   . HOH Q 7 .   ? -10.678 8.175   14.534  1.00 19.32 ? 457 HOH B O   1 
HETATM 8934 O  O   . HOH Q 7 .   ? 22.372  -16.927 2.999   1.00 17.85 ? 458 HOH B O   1 
HETATM 8935 O  O   . HOH Q 7 .   ? 8.086   -1.489  -7.501  1.00 22.80 ? 459 HOH B O   1 
HETATM 8936 O  O   . HOH Q 7 .   ? -0.884  -3.216  0.635   1.00 12.15 ? 460 HOH B O   1 
HETATM 8937 O  O   . HOH Q 7 .   ? 10.715  0.274   22.955  1.00 17.81 ? 461 HOH B O   1 
HETATM 8938 O  O   . HOH Q 7 .   ? -8.321  -13.828 1.386   1.00 13.87 ? 462 HOH B O   1 
HETATM 8939 O  O   . HOH Q 7 .   ? 12.616  -16.277 29.451  1.00 25.40 ? 463 HOH B O   1 
HETATM 8940 O  O   . HOH Q 7 .   ? 5.020   -12.196 -6.987  1.00 16.77 ? 464 HOH B O   1 
HETATM 8941 O  O   . HOH Q 7 .   ? -13.480 -4.482  5.286   1.00 20.12 ? 465 HOH B O   1 
HETATM 8942 O  O   . HOH Q 7 .   ? -12.741 -27.879 27.009  1.00 21.08 ? 466 HOH B O   1 
HETATM 8943 O  O   . HOH Q 7 .   ? 16.510  -32.252 18.778  1.00 20.74 ? 467 HOH B O   1 
HETATM 8944 O  O   . HOH Q 7 .   ? 10.641  -20.808 1.720   1.00 13.10 ? 468 HOH B O   1 
HETATM 8945 O  O   . HOH Q 7 .   ? 5.330   5.502   20.499  1.00 15.08 ? 469 HOH B O   1 
HETATM 8946 O  O   . HOH Q 7 .   ? -10.268 -7.927  12.426  1.00 15.07 ? 470 HOH B O   1 
HETATM 8947 O  O   . HOH Q 7 .   ? 10.678  -6.974  -7.760  1.00 20.45 ? 471 HOH B O   1 
HETATM 8948 O  O   . HOH Q 7 .   ? -23.892 -16.986 14.627  1.00 20.01 ? 472 HOH B O   1 
HETATM 8949 O  O   . HOH Q 7 .   ? -6.586  -32.614 9.176   1.00 19.40 ? 473 HOH B O   1 
HETATM 8950 O  O   . HOH Q 7 .   ? 5.254   1.078   24.837  1.00 15.96 ? 474 HOH B O   1 
HETATM 8951 O  O   . HOH Q 7 .   ? 18.505  -30.251 18.158  1.00 19.93 ? 475 HOH B O   1 
HETATM 8952 O  O   . HOH Q 7 .   ? 9.689   0.257   -0.622  1.00 24.61 ? 476 HOH B O   1 
HETATM 8953 O  O   . HOH Q 7 .   ? 10.266  -1.908  8.355   1.00 22.20 ? 477 HOH B O   1 
HETATM 8954 O  O   . HOH Q 7 .   ? -4.778  -11.374 21.584  1.00 25.40 ? 478 HOH B O   1 
HETATM 8955 O  O   . HOH Q 7 .   ? -18.097 -6.537  20.484  1.00 20.69 ? 479 HOH B O   1 
HETATM 8956 O  O   . HOH Q 7 .   ? 2.086   -34.659 17.552  1.00 24.26 ? 480 HOH B O   1 
HETATM 8957 O  O   . HOH Q 7 .   ? -18.860 -20.141 4.218   1.00 29.86 ? 481 HOH B O   1 
HETATM 8958 O  O   . HOH Q 7 .   ? -19.201 -19.794 18.507  1.00 21.16 ? 482 HOH B O   1 
HETATM 8959 O  O   . HOH Q 7 .   ? -10.437 -29.580 27.766  1.00 28.60 ? 483 HOH B O   1 
HETATM 8960 O  O   . HOH Q 7 .   ? 18.695  -17.231 10.748  1.00 31.96 ? 484 HOH B O   1 
HETATM 8961 O  O   . HOH Q 7 .   ? 3.515   -0.099  23.233  1.00 16.93 ? 485 HOH B O   1 
HETATM 8962 O  O   . HOH Q 7 .   ? 8.036   3.326   9.022   1.00 11.23 ? 486 HOH B O   1 
HETATM 8963 O  O   . HOH Q 7 .   ? -7.998  3.789   15.213  1.00 23.80 ? 487 HOH B O   1 
HETATM 8964 O  O   . HOH Q 7 .   ? -11.255 -28.699 0.390   1.00 29.81 ? 488 HOH B O   1 
HETATM 8965 O  O   . HOH Q 7 .   ? -17.654 -22.649 4.116   1.00 24.61 ? 489 HOH B O   1 
HETATM 8966 O  O   . HOH Q 7 .   ? -3.029  -13.776 -4.638  1.00 38.41 ? 490 HOH B O   1 
HETATM 8967 O  O   . HOH Q 7 .   ? -6.668  5.520   17.164  1.00 19.80 ? 491 HOH B O   1 
HETATM 8968 O  O   . HOH Q 7 .   ? 19.442  -20.047 5.056   1.00 25.67 ? 492 HOH B O   1 
HETATM 8969 O  O   . HOH Q 7 .   ? -14.181 -28.822 16.196  1.00 20.77 ? 493 HOH B O   1 
HETATM 8970 O  O   . HOH Q 7 .   ? -19.542 -24.192 19.788  1.00 28.18 ? 494 HOH B O   1 
HETATM 8971 O  O   . HOH Q 7 .   ? -11.753 8.799   11.290  1.00 20.36 ? 495 HOH B O   1 
HETATM 8972 O  O   . HOH Q 7 .   ? 15.346  -25.584 3.643   1.00 23.23 ? 496 HOH B O   1 
HETATM 8973 O  O   . HOH Q 7 .   ? -20.355 -17.439 9.722   1.00 18.77 ? 497 HOH B O   1 
HETATM 8974 O  O   . HOH Q 7 .   ? -12.448 -5.016  15.580  1.00 25.67 ? 498 HOH B O   1 
HETATM 8975 O  O   . HOH Q 7 .   ? -19.305 -11.602 -1.053  1.00 23.86 ? 499 HOH B O   1 
HETATM 8976 O  O   . HOH Q 7 .   ? 2.192   2.912   22.645  1.00 24.03 ? 500 HOH B O   1 
HETATM 8977 O  O   . HOH Q 7 .   ? 8.591   -30.421 14.412  1.00 12.74 ? 501 HOH B O   1 
HETATM 8978 O  O   . HOH Q 7 .   ? -19.931 -11.542 1.506   1.00 22.42 ? 502 HOH B O   1 
HETATM 8979 O  O   . HOH Q 7 .   ? -15.471 -1.559  11.161  1.00 23.79 ? 503 HOH B O   1 
HETATM 8980 O  O   . HOH Q 7 .   ? 10.263  -29.309 16.093  1.00 18.52 ? 504 HOH B O   1 
HETATM 8981 O  O   . HOH Q 7 .   ? 7.104   2.762   15.575  1.00 18.96 ? 505 HOH B O   1 
HETATM 8982 O  O   . HOH Q 7 .   ? -25.718 -14.184 23.748  1.00 38.25 ? 506 HOH B O   1 
HETATM 8983 O  O   . HOH Q 7 .   ? 4.400   -19.205 25.435  1.00 19.55 ? 507 HOH B O   1 
HETATM 8984 O  O   . HOH Q 7 .   ? -16.296 -21.769 22.519  1.00 23.36 ? 508 HOH B O   1 
HETATM 8985 O  O   . HOH Q 7 .   ? -10.502 -5.667  13.928  1.00 24.76 ? 509 HOH B O   1 
HETATM 8986 O  O   . HOH Q 7 .   ? -5.680  -37.587 24.413  1.00 25.46 ? 510 HOH B O   1 
HETATM 8987 O  O   . HOH Q 7 .   ? 6.762   9.605   14.236  1.00 37.08 ? 511 HOH B O   1 
HETATM 8988 O  O   . HOH Q 7 .   ? 10.875  -9.696  -5.272  1.00 25.48 ? 512 HOH B O   1 
HETATM 8989 O  O   . HOH Q 7 .   ? -12.900 -26.921 3.887   1.00 22.08 ? 513 HOH B O   1 
HETATM 8990 O  O   . HOH Q 7 .   ? 0.658   -33.040 13.215  1.00 19.95 ? 514 HOH B O   1 
HETATM 8991 O  O   . HOH Q 7 .   ? 2.049   -36.451 19.625  1.00 39.28 ? 515 HOH B O   1 
HETATM 8992 O  O   . HOH Q 7 .   ? -7.641  -16.183 25.500  1.00 28.29 ? 516 HOH B O   1 
HETATM 8993 O  O   . HOH Q 7 .   ? -17.000 -8.782  1.686   1.00 22.66 ? 517 HOH B O   1 
HETATM 8994 O  O   . HOH Q 7 .   ? 2.296   -27.478 26.735  1.00 22.19 ? 518 HOH B O   1 
HETATM 8995 O  O   . HOH Q 7 .   ? -0.138  -16.939 -5.336  1.00 23.87 ? 519 HOH B O   1 
HETATM 8996 O  O   . HOH Q 7 .   ? -13.102 -5.103  7.995   1.00 26.96 ? 520 HOH B O   1 
HETATM 8997 O  O   . HOH Q 7 .   ? -15.272 -6.743  1.793   1.00 24.58 ? 521 HOH B O   1 
HETATM 8998 O  O   . HOH Q 7 .   ? -5.075  -35.893 20.373  1.00 29.48 ? 522 HOH B O   1 
HETATM 8999 O  O   . HOH Q 7 .   ? 12.366  -21.610 -4.110  1.00 33.45 ? 523 HOH B O   1 
HETATM 9000 O  O   . HOH Q 7 .   ? 5.064   -8.541  -10.655 1.00 23.70 ? 524 HOH B O   1 
HETATM 9001 O  O   . HOH Q 7 .   ? -1.778  -15.298 23.550  1.00 26.49 ? 525 HOH B O   1 
HETATM 9002 O  O   . HOH Q 7 .   ? -3.341  13.614  18.625  1.00 20.58 ? 526 HOH B O   1 
HETATM 9003 O  O   . HOH Q 7 .   ? -1.905  11.088  19.270  1.00 21.19 ? 527 HOH B O   1 
HETATM 9004 O  O   . HOH Q 7 .   ? -11.770 -5.513  -2.414  1.00 24.50 ? 528 HOH B O   1 
HETATM 9005 O  O   . HOH Q 7 .   ? -16.090 -4.234  4.188   1.00 35.46 ? 529 HOH B O   1 
HETATM 9006 O  O   . HOH Q 7 .   ? -14.621 -4.095  11.594  1.00 18.65 ? 530 HOH B O   1 
HETATM 9007 O  O   . HOH Q 7 .   ? -12.105 0.125   19.610  1.00 28.50 ? 531 HOH B O   1 
HETATM 9008 O  O   . HOH Q 7 .   ? 10.793  -16.474 -5.350  1.00 25.70 ? 532 HOH B O   1 
HETATM 9009 O  O   . HOH Q 7 .   ? 7.149   -13.780 -7.106  1.00 24.61 ? 533 HOH B O   1 
HETATM 9010 O  O   . HOH Q 7 .   ? 14.352  -27.619 12.046  1.00 27.29 ? 534 HOH B O   1 
HETATM 9011 O  O   . HOH Q 7 .   ? -12.652 -26.764 24.185  1.00 22.19 ? 535 HOH B O   1 
HETATM 9012 O  O   . HOH Q 7 .   ? 10.598  -29.222 23.938  1.00 26.44 ? 536 HOH B O   1 
HETATM 9013 O  O   . HOH Q 7 .   ? 22.837  -12.086 13.996  1.00 25.49 ? 537 HOH B O   1 
HETATM 9014 O  O   . HOH Q 7 .   ? -21.207 -10.669 -4.367  1.00 43.08 ? 538 HOH B O   1 
HETATM 9015 O  O   . HOH Q 7 .   ? 2.495   -23.930 -2.730  1.00 23.00 ? 539 HOH B O   1 
HETATM 9016 O  O   . HOH Q 7 .   ? 1.170   -26.552 0.572   1.00 22.17 ? 540 HOH B O   1 
HETATM 9017 O  O   . HOH Q 7 .   ? -7.173  -30.786 -2.907  1.00 29.01 ? 541 HOH B O   1 
HETATM 9018 O  O   . HOH Q 7 .   ? -9.664  -32.158 16.813  1.00 23.35 ? 542 HOH B O   1 
HETATM 9019 O  O   . HOH Q 7 .   ? -21.281 -22.191 16.303  1.00 21.37 ? 543 HOH B O   1 
HETATM 9020 O  O   . HOH Q 7 .   ? -10.512 -27.194 -4.236  1.00 32.75 ? 544 HOH B O   1 
HETATM 9021 O  O   . HOH Q 7 .   ? 4.668   -15.273 27.229  1.00 18.47 ? 545 HOH B O   1 
HETATM 9022 O  O   . HOH Q 7 .   ? 3.126   -16.871 25.711  1.00 16.88 ? 546 HOH B O   1 
HETATM 9023 O  O   . HOH Q 7 .   ? 26.641  -18.069 -0.628  1.00 23.68 ? 547 HOH B O   1 
HETATM 9024 O  O   . HOH Q 7 .   ? -15.829 -25.811 13.942  1.00 22.19 ? 548 HOH B O   1 
HETATM 9025 O  O   . HOH Q 7 .   ? -17.996 -10.862 3.418   1.00 19.60 ? 549 HOH B O   1 
HETATM 9026 O  O   . HOH Q 7 .   ? -21.670 -19.174 17.339  1.00 27.84 ? 550 HOH B O   1 
HETATM 9027 O  O   . HOH Q 7 .   ? -18.644 -13.436 22.663  1.00 21.08 ? 551 HOH B O   1 
HETATM 9028 O  O   . HOH Q 7 .   ? -11.019 -14.694 25.918  1.00 25.89 ? 552 HOH B O   1 
HETATM 9029 O  O   . HOH Q 7 .   ? -2.057  4.027   7.325   1.00 20.91 ? 553 HOH B O   1 
HETATM 9030 O  O   . HOH Q 7 .   ? 6.633   -3.668  -6.467  1.00 19.90 ? 554 HOH B O   1 
HETATM 9031 O  O   . HOH Q 7 .   ? 24.333  -8.162  2.516   1.00 28.35 ? 555 HOH B O   1 
HETATM 9032 O  O   . HOH Q 7 .   ? 3.913   -21.701 27.850  1.00 21.53 ? 556 HOH B O   1 
HETATM 9033 O  O   . HOH Q 7 .   ? 4.664   -19.154 28.693  1.00 26.01 ? 557 HOH B O   1 
HETATM 9034 O  O   . HOH Q 7 .   ? -5.317  -33.500 23.624  1.00 23.57 ? 558 HOH B O   1 
HETATM 9035 O  O   . HOH Q 7 .   ? 0.230   -23.032 25.211  1.00 19.95 ? 559 HOH B O   1 
HETATM 9036 O  O   . HOH Q 7 .   ? 0.841   -18.531 24.879  1.00 18.63 ? 560 HOH B O   1 
HETATM 9037 O  O   . HOH Q 7 .   ? 15.864  -18.827 26.096  1.00 20.15 ? 561 HOH B O   1 
HETATM 9038 O  O   . HOH Q 7 .   ? 3.305   -18.877 -6.308  1.00 23.29 ? 562 HOH B O   1 
HETATM 9039 O  O   . HOH Q 7 .   ? 6.362   -17.713 -4.732  1.00 28.77 ? 563 HOH B O   1 
HETATM 9040 O  O   . HOH Q 7 .   ? -4.184  -32.301 -0.727  1.00 30.35 ? 564 HOH B O   1 
HETATM 9041 O  O   . HOH Q 7 .   ? 16.776  -17.447 -7.824  1.00 30.72 ? 565 HOH B O   1 
HETATM 9042 O  O   . HOH Q 7 .   ? -2.402  -10.854 21.060  1.00 26.96 ? 566 HOH B O   1 
HETATM 9043 O  O   . HOH Q 7 .   ? 11.836  3.530   9.601   1.00 18.17 ? 567 HOH B O   1 
HETATM 9044 O  O   . HOH Q 7 .   ? -2.943  -20.880 26.911  1.00 21.95 ? 568 HOH B O   1 
HETATM 9045 O  O   . HOH Q 7 .   ? 8.979   0.550   6.987   1.00 24.96 ? 569 HOH B O   1 
HETATM 9046 O  O   . HOH Q 7 .   ? 25.358  -9.768  17.028  1.00 25.53 ? 570 HOH B O   1 
HETATM 9047 O  O   . HOH Q 7 .   ? -21.975 -8.559  24.139  1.00 19.52 ? 571 HOH B O   1 
HETATM 9048 O  O   . HOH Q 7 .   ? 8.764   -15.065 -2.850  1.00 22.24 ? 572 HOH B O   1 
HETATM 9049 O  O   . HOH Q 7 .   ? 9.546   4.945   -1.368  1.00 30.87 ? 573 HOH B O   1 
HETATM 9050 O  O   . HOH Q 7 .   ? 12.552  -30.180 17.857  1.00 28.49 ? 574 HOH B O   1 
HETATM 9051 O  O   . HOH Q 7 .   ? 8.928   7.829   2.976   1.00 25.74 ? 575 HOH B O   1 
HETATM 9052 O  O   . HOH Q 7 .   ? -18.211 -27.178 13.800  1.00 25.03 ? 576 HOH B O   1 
HETATM 9053 O  O   . HOH Q 7 .   ? 11.163  5.991   8.789   1.00 28.02 ? 577 HOH B O   1 
HETATM 9054 O  O   . HOH Q 7 .   ? 5.896   -25.882 28.444  1.00 29.51 ? 578 HOH B O   1 
HETATM 9055 O  O   . HOH Q 7 .   ? 4.006   5.313   22.817  1.00 23.47 ? 579 HOH B O   1 
HETATM 9056 O  O   . HOH Q 7 .   ? 1.882   -9.234  24.283  1.00 40.95 ? 580 HOH B O   1 
HETATM 9057 O  O   . HOH Q 7 .   ? -19.925 -18.672 2.180   1.00 25.43 ? 581 HOH B O   1 
HETATM 9058 O  O   . HOH Q 7 .   ? -0.252  -21.698 30.771  1.00 36.27 ? 582 HOH B O   1 
HETATM 9059 O  O   . HOH Q 7 .   ? -5.494  -3.840  -0.063  1.00 24.82 ? 583 HOH B O   1 
HETATM 9060 O  O   . HOH Q 7 .   ? 5.722   -32.309 25.030  1.00 25.84 ? 584 HOH B O   1 
HETATM 9061 O  O   . HOH Q 7 .   ? 4.298   -28.523 25.137  1.00 23.59 ? 585 HOH B O   1 
HETATM 9062 O  O   . HOH Q 7 .   ? 5.347   -23.141 -3.142  1.00 33.04 ? 586 HOH B O   1 
HETATM 9063 O  O   . HOH Q 7 .   ? 13.655  5.024   5.984   1.00 27.67 ? 587 HOH B O   1 
HETATM 9064 O  O   . HOH Q 7 .   ? 2.720   -13.938 -6.905  1.00 24.79 ? 588 HOH B O   1 
HETATM 9065 O  O   . HOH Q 7 .   ? 4.338   -34.231 11.057  1.00 23.80 ? 589 HOH B O   1 
HETATM 9066 O  O   . HOH Q 7 .   ? 18.057  -24.320 21.268  1.00 33.24 ? 590 HOH B O   1 
HETATM 9067 O  O   . HOH Q 7 .   ? 17.502  -18.307 17.835  1.00 25.36 ? 591 HOH B O   1 
HETATM 9068 O  O   . HOH Q 7 .   ? -4.309  -18.236 -6.751  1.00 27.40 ? 592 HOH B O   1 
HETATM 9069 O  O   . HOH Q 7 .   ? -11.907 -4.706  11.113  1.00 22.17 ? 593 HOH B O   1 
HETATM 9070 O  O   . HOH Q 7 .   ? -13.895 -16.272 -3.337  1.00 19.37 ? 594 HOH B O   1 
HETATM 9071 O  O   . HOH Q 7 .   ? 17.509  -28.496 16.122  1.00 24.55 ? 595 HOH B O   1 
HETATM 9072 O  O   . HOH Q 7 .   ? 0.260   -2.462  -1.999  1.00 31.60 ? 596 HOH B O   1 
HETATM 9073 O  O   . HOH Q 7 .   ? 1.149   -25.136 26.995  1.00 24.70 ? 597 HOH B O   1 
HETATM 9074 O  O   . HOH Q 7 .   ? 2.544   9.017   15.428  1.00 25.56 ? 598 HOH B O   1 
HETATM 9075 O  O   . HOH Q 7 .   ? -1.915  -3.584  -3.434  1.00 34.17 ? 599 HOH B O   1 
HETATM 9076 O  O   . HOH Q 7 .   ? 6.972   -1.306  -3.689  1.00 24.72 ? 600 HOH B O   1 
HETATM 9077 O  O   . HOH Q 7 .   ? -18.136 5.759   8.357   1.00 44.41 ? 601 HOH B O   1 
HETATM 9078 O  O   . HOH Q 7 .   ? -12.516 -6.014  18.230  1.00 29.46 ? 602 HOH B O   1 
HETATM 9079 O  O   . HOH Q 7 .   ? -8.342  -8.306  21.944  1.00 29.59 ? 603 HOH B O   1 
HETATM 9080 O  O   . HOH Q 7 .   ? 5.671   1.300   20.805  1.00 24.62 ? 604 HOH B O   1 
HETATM 9081 O  O   . HOH Q 7 .   ? 8.758   5.971   9.253   1.00 35.64 ? 605 HOH B O   1 
HETATM 9082 O  O   . HOH Q 7 .   ? 17.686  -7.605  -6.168  1.00 38.71 ? 606 HOH B O   1 
HETATM 9083 O  O   . HOH Q 7 .   ? 16.550  -25.865 6.253   1.00 23.32 ? 607 HOH B O   1 
HETATM 9084 O  O   . HOH Q 7 .   ? 12.471  -27.213 6.340   1.00 35.60 ? 608 HOH B O   1 
HETATM 9085 O  O   . HOH Q 7 .   ? 10.491  -27.815 3.231   1.00 35.87 ? 609 HOH B O   1 
HETATM 9086 O  O   . HOH Q 7 .   ? 16.564  -22.860 -4.991  1.00 44.91 ? 610 HOH B O   1 
HETATM 9087 O  O   . HOH Q 7 .   ? 16.096  -26.376 9.737   1.00 29.63 ? 611 HOH B O   1 
HETATM 9088 O  O   . HOH Q 7 .   ? 25.085  -21.868 12.037  1.00 30.91 ? 612 HOH B O   1 
HETATM 9089 O  O   . HOH Q 7 .   ? 8.342   -31.846 10.685  1.00 28.54 ? 613 HOH B O   1 
HETATM 9090 O  O   . HOH Q 7 .   ? 0.202   -35.305 16.026  1.00 43.44 ? 614 HOH B O   1 
HETATM 9091 O  O   . HOH Q 7 .   ? -0.844  -20.353 28.398  1.00 29.47 ? 615 HOH B O   1 
HETATM 9092 O  O   . HOH Q 7 .   ? -3.144  -12.160 25.365  1.00 29.30 ? 616 HOH B O   1 
HETATM 9093 O  O   . HOH Q 7 .   ? 0.799   -14.174 22.922  1.00 28.54 ? 617 HOH B O   1 
HETATM 9094 O  O   . HOH Q 7 .   ? 11.580  -20.707 27.005  1.00 24.11 ? 618 HOH B O   1 
HETATM 9095 O  O   . HOH Q 7 .   ? -4.120  -34.160 1.286   1.00 29.06 ? 619 HOH B O   1 
HETATM 9096 O  O   . HOH Q 7 .   ? -14.869 -24.626 10.407  1.00 27.70 ? 620 HOH B O   1 
HETATM 9097 O  O   . HOH Q 7 .   ? -15.963 -23.382 2.761   1.00 26.86 ? 621 HOH B O   1 
HETATM 9098 O  O   . HOH Q 7 .   ? -19.353 -21.494 20.756  1.00 37.10 ? 622 HOH B O   1 
HETATM 9099 O  O   . HOH Q 7 .   ? -15.784 -19.457 24.989  1.00 28.06 ? 623 HOH B O   1 
HETATM 9100 O  O   . HOH Q 7 .   ? -10.786 -29.988 22.029  1.00 26.88 ? 624 HOH B O   1 
HETATM 9101 O  O   . HOH Q 7 .   ? -3.080  -34.214 16.857  1.00 39.33 ? 625 HOH B O   1 
HETATM 9102 O  O   . HOH Q 7 .   ? 4.073   -27.409 3.411   1.00 26.52 ? 626 HOH B O   1 
HETATM 9103 O  O   . HOH Q 7 .   ? 19.058  -12.121 11.336  1.00 35.27 ? 627 HOH B O   1 
HETATM 9104 O  O   . HOH Q 7 .   ? -17.043 -20.804 7.901   1.00 23.98 ? 628 HOH B O   1 
HETATM 9105 O  O   . HOH Q 7 .   ? -23.256 -11.367 27.473  1.00 39.98 ? 629 HOH B O   1 
HETATM 9106 O  O   . HOH Q 7 .   ? -19.556 -2.633  15.922  1.00 27.32 ? 630 HOH B O   1 
HETATM 9107 O  O   . HOH Q 7 .   ? 19.037  -1.438  5.463   1.00 27.94 ? 631 HOH B O   1 
HETATM 9108 O  O   . HOH Q 7 .   ? 9.777   -0.743  27.212  1.00 26.92 ? 632 HOH B O   1 
HETATM 9109 O  O   . HOH Q 7 .   ? 21.945  -8.837  -3.870  1.00 22.68 ? 633 HOH B O   1 
HETATM 9110 O  O   . HOH Q 7 .   ? -2.026  -34.751 14.306  1.00 29.56 ? 634 HOH B O   1 
HETATM 9111 O  O   . HOH Q 7 .   ? 18.926  -3.734  -4.031  1.00 31.84 ? 635 HOH B O   1 
HETATM 9112 O  O   . HOH Q 7 .   ? 20.868  -24.444 10.511  1.00 29.66 ? 636 HOH B O   1 
HETATM 9113 O  O   . HOH Q 7 .   ? 16.323  -31.636 16.056  1.00 31.71 ? 637 HOH B O   1 
HETATM 9114 O  O   . HOH Q 7 .   ? -6.851  -27.975 28.718  1.00 26.09 ? 638 HOH B O   1 
HETATM 9115 O  O   . HOH Q 7 .   ? 14.764  -20.676 27.651  1.00 25.85 ? 639 HOH B O   1 
HETATM 9116 O  O   . HOH Q 7 .   ? 17.084  -26.191 27.043  1.00 33.59 ? 640 HOH B O   1 
HETATM 9117 O  O   . HOH Q 7 .   ? 15.338  -11.071 32.508  1.00 24.92 ? 641 HOH B O   1 
HETATM 9118 O  O   . HOH Q 7 .   ? 6.902   -8.620  33.562  1.00 34.17 ? 642 HOH B O   1 
HETATM 9119 O  O   . HOH Q 7 .   ? -8.737  -25.571 -4.305  1.00 30.20 ? 643 HOH B O   1 
HETATM 9120 O  O   . HOH Q 7 .   ? -12.586 -31.286 20.081  1.00 37.52 ? 644 HOH B O   1 
HETATM 9121 O  O   . HOH Q 7 .   ? 16.338  -4.492  8.327   1.00 26.86 ? 645 HOH B O   1 
HETATM 9122 O  O   . HOH Q 7 .   ? -15.666 -26.080 3.761   1.00 28.87 ? 646 HOH B O   1 
HETATM 9123 O  O   . HOH Q 7 .   ? -18.035 -16.430 -2.114  1.00 27.17 ? 647 HOH B O   1 
HETATM 9124 O  O   . HOH Q 7 .   ? -15.495 -5.718  9.284   1.00 24.93 ? 648 HOH B O   1 
HETATM 9125 O  O   . HOH Q 7 .   ? -18.831 -12.220 25.369  1.00 29.26 ? 649 HOH B O   1 
HETATM 9126 O  O   . HOH Q 7 .   ? 24.000  -21.033 6.050   1.00 34.44 ? 650 HOH B O   1 
HETATM 9127 O  O   . HOH Q 7 .   ? 19.439  -20.506 20.435  1.00 26.30 ? 651 HOH B O   1 
HETATM 9128 O  O   . HOH Q 7 .   ? -4.037  -14.583 -7.261  1.00 29.00 ? 652 HOH B O   1 
HETATM 9129 O  O   . HOH Q 7 .   ? -16.441 -27.132 10.578  1.00 42.18 ? 653 HOH B O   1 
HETATM 9130 O  O   . HOH Q 7 .   ? 4.692   -5.266  -10.686 1.00 22.63 ? 654 HOH B O   1 
HETATM 9131 O  O   . HOH Q 7 .   ? 9.355   -34.086 16.776  1.00 31.61 ? 655 HOH B O   1 
HETATM 9132 O  O   . HOH R 7 .   ? 16.186  24.106  49.621  1.00 17.14 ? 401 HOH C O   1 
HETATM 9133 O  O   . HOH R 7 .   ? 19.124  24.181  48.821  1.00 21.32 ? 402 HOH C O   1 
HETATM 9134 O  O   . HOH R 7 .   ? 15.060  21.884  47.890  1.00 25.14 ? 403 HOH C O   1 
HETATM 9135 O  O   . HOH R 7 .   ? 18.706  26.297  47.158  1.00 21.04 ? 404 HOH C O   1 
HETATM 9136 O  O   . HOH R 7 .   ? 20.910  7.236   43.584  1.00 8.75  ? 405 HOH C O   1 
HETATM 9137 O  O   . HOH R 7 .   ? 26.159  10.660  43.655  1.00 12.65 ? 406 HOH C O   1 
HETATM 9138 O  O   . HOH R 7 .   ? 31.719  12.104  48.736  1.00 11.41 ? 407 HOH C O   1 
HETATM 9139 O  O   . HOH R 7 .   ? 18.742  21.562  47.538  1.00 9.54  ? 408 HOH C O   1 
HETATM 9140 O  O   . HOH R 7 .   ? 25.726  7.965   42.688  1.00 7.38  ? 409 HOH C O   1 
HETATM 9141 O  O   . HOH R 7 .   ? 28.815  9.640   35.912  1.00 8.75  ? 410 HOH C O   1 
HETATM 9142 O  O   . HOH R 7 .   ? 25.411  13.056  45.213  1.00 9.45  ? 411 HOH C O   1 
HETATM 9143 O  O   . HOH R 7 .   ? 24.678  13.753  48.975  1.00 8.21  ? 412 HOH C O   1 
HETATM 9144 O  O   . HOH R 7 .   ? 43.814  33.279  33.585  1.00 14.76 ? 413 HOH C O   1 
HETATM 9145 O  O   . HOH R 7 .   ? 36.253  32.404  20.142  1.00 15.40 ? 414 HOH C O   1 
HETATM 9146 O  O   . HOH R 7 .   ? 25.849  9.737   51.768  1.00 11.20 ? 415 HOH C O   1 
HETATM 9147 O  O   . HOH R 7 .   ? 32.466  13.558  44.319  1.00 10.38 ? 416 HOH C O   1 
HETATM 9148 O  O   . HOH R 7 .   ? 18.830  11.035  45.985  1.00 11.20 ? 417 HOH C O   1 
HETATM 9149 O  O   . HOH R 7 .   ? 21.746  5.012   36.447  1.00 12.09 ? 418 HOH C O   1 
HETATM 9150 O  O   . HOH R 7 .   ? 42.447  23.750  22.401  1.00 17.18 ? 419 HOH C O   1 
HETATM 9151 O  O   . HOH R 7 .   ? 30.296  21.647  37.574  1.00 12.54 ? 420 HOH C O   1 
HETATM 9152 O  O   . HOH R 7 .   ? 36.712  19.833  40.110  1.00 17.07 ? 421 HOH C O   1 
HETATM 9153 O  O   . HOH R 7 .   ? 43.533  13.388  28.481  1.00 12.88 ? 422 HOH C O   1 
HETATM 9154 O  O   . HOH R 7 .   ? 28.117  17.649  38.411  1.00 10.14 ? 423 HOH C O   1 
HETATM 9155 O  O   . HOH R 7 .   ? 34.881  21.826  40.017  1.00 14.96 ? 424 HOH C O   1 
HETATM 9156 O  O   . HOH R 7 .   ? 15.332  16.173  44.578  1.00 12.99 ? 425 HOH C O   1 
HETATM 9157 O  O   . HOH R 7 .   ? 38.035  13.606  30.638  1.00 11.09 ? 426 HOH C O   1 
HETATM 9158 O  O   . HOH R 7 .   ? 29.389  8.934   44.855  1.00 10.13 ? 427 HOH C O   1 
HETATM 9159 O  O   . HOH R 7 .   ? 19.636  9.706   43.614  1.00 12.91 ? 428 HOH C O   1 
HETATM 9160 O  O   . HOH R 7 .   ? 33.795  32.757  18.787  1.00 14.41 ? 429 HOH C O   1 
HETATM 9161 O  O   . HOH R 7 .   ? 28.061  13.250  15.739  1.00 17.03 ? 430 HOH C O   1 
HETATM 9162 O  O   . HOH R 7 .   ? 15.726  19.081  27.161  1.00 14.03 ? 431 HOH C O   1 
HETATM 9163 O  O   . HOH R 7 .   ? 20.136  34.054  31.705  1.00 19.33 ? 432 HOH C O   1 
HETATM 9164 O  O   . HOH R 7 .   ? 25.455  13.281  22.541  1.00 12.55 ? 433 HOH C O   1 
HETATM 9165 O  O   . HOH R 7 .   ? 19.246  28.793  15.013  1.00 21.86 ? 434 HOH C O   1 
HETATM 9166 O  O   . HOH R 7 .   ? 22.288  -1.552  27.261  1.00 16.71 ? 435 HOH C O   1 
HETATM 9167 O  O   . HOH R 7 .   ? 14.407  -1.478  25.359  1.00 18.38 ? 436 HOH C O   1 
HETATM 9168 O  O   . HOH R 7 .   ? 37.933  27.618  15.814  1.00 21.30 ? 437 HOH C O   1 
HETATM 9169 O  O   . HOH R 7 .   ? 38.674  18.968  47.025  1.00 20.07 ? 438 HOH C O   1 
HETATM 9170 O  O   . HOH R 7 .   ? 12.848  36.194  22.658  1.00 19.07 ? 439 HOH C O   1 
HETATM 9171 O  O   . HOH R 7 .   ? 24.045  6.534   22.412  1.00 17.23 ? 440 HOH C O   1 
HETATM 9172 O  O   . HOH R 7 .   ? 32.902  5.168   38.418  1.00 17.57 ? 441 HOH C O   1 
HETATM 9173 O  O   . HOH R 7 .   ? 40.792  22.125  33.924  1.00 12.08 ? 442 HOH C O   1 
HETATM 9174 O  O   . HOH R 7 .   ? 43.273  21.395  35.762  1.00 13.06 ? 443 HOH C O   1 
HETATM 9175 O  O   . HOH R 7 .   ? 29.840  29.918  13.487  1.00 19.78 ? 444 HOH C O   1 
HETATM 9176 O  O   . HOH R 7 .   ? 16.244  6.761   13.728  1.00 22.28 ? 445 HOH C O   1 
HETATM 9177 O  O   . HOH R 7 .   ? 24.486  -0.419  32.250  1.00 16.05 ? 446 HOH C O   1 
HETATM 9178 O  O   . HOH R 7 .   ? 16.078  17.159  17.782  1.00 19.42 ? 447 HOH C O   1 
HETATM 9179 O  O   . HOH R 7 .   ? 16.614  30.641  14.040  1.00 17.55 ? 448 HOH C O   1 
HETATM 9180 O  O   . HOH R 7 .   ? 21.431  2.997   24.087  1.00 33.98 ? 449 HOH C O   1 
HETATM 9181 O  O   . HOH R 7 .   ? 26.617  38.070  30.354  1.00 18.41 ? 450 HOH C O   1 
HETATM 9182 O  O   . HOH R 7 .   ? 35.987  11.728  47.076  1.00 18.42 ? 451 HOH C O   1 
HETATM 9183 O  O   . HOH R 7 .   ? 12.711  13.189  16.549  1.00 16.67 ? 452 HOH C O   1 
HETATM 9184 O  O   . HOH R 7 .   ? 14.477  15.192  11.222  1.00 20.69 ? 453 HOH C O   1 
HETATM 9185 O  O   . HOH R 7 .   ? 19.865  3.759   35.137  1.00 24.37 ? 454 HOH C O   1 
HETATM 9186 O  O   . HOH R 7 .   ? 31.056  6.375   19.701  1.00 27.02 ? 455 HOH C O   1 
HETATM 9187 O  O   . HOH R 7 .   ? 34.208  22.036  42.718  1.00 24.87 ? 456 HOH C O   1 
HETATM 9188 O  O   . HOH R 7 .   ? 40.292  19.015  42.656  1.00 17.64 ? 457 HOH C O   1 
HETATM 9189 O  O   . HOH R 7 .   ? 22.137  12.378  18.072  1.00 12.15 ? 458 HOH C O   1 
HETATM 9190 O  O   . HOH R 7 .   ? 14.724  8.624   15.024  1.00 24.78 ? 459 HOH C O   1 
HETATM 9191 O  O   . HOH R 7 .   ? 10.611  8.323   15.875  1.00 17.40 ? 460 HOH C O   1 
HETATM 9192 O  O   . HOH R 7 .   ? 11.077  21.179  32.793  1.00 22.10 ? 461 HOH C O   1 
HETATM 9193 O  O   . HOH R 7 .   ? 27.446  3.939   34.593  1.00 24.91 ? 462 HOH C O   1 
HETATM 9194 O  O   . HOH R 7 .   ? 17.131  -5.214  27.509  1.00 16.81 ? 463 HOH C O   1 
HETATM 9195 O  O   . HOH R 7 .   ? 35.838  18.323  49.677  1.00 17.01 ? 464 HOH C O   1 
HETATM 9196 O  O   . HOH R 7 .   ? 16.740  18.006  15.115  1.00 23.10 ? 465 HOH C O   1 
HETATM 9197 O  O   . HOH R 7 .   ? 33.295  11.682  46.241  1.00 21.69 ? 466 HOH C O   1 
HETATM 9198 O  O   . HOH R 7 .   ? 13.823  18.010  46.148  1.00 15.66 ? 467 HOH C O   1 
HETATM 9199 O  O   . HOH R 7 .   ? 29.042  7.189   37.104  1.00 13.64 ? 468 HOH C O   1 
HETATM 9200 O  O   . HOH R 7 .   ? 7.103   1.801   22.690  1.00 17.25 ? 469 HOH C O   1 
HETATM 9201 O  O   . HOH R 7 .   ? 34.351  33.109  15.999  1.00 18.73 ? 470 HOH C O   1 
HETATM 9202 O  O   . HOH R 7 .   ? 29.803  33.383  32.066  1.00 17.13 ? 471 HOH C O   1 
HETATM 9203 O  O   . HOH R 7 .   ? 15.936  16.935  12.619  1.00 23.39 ? 472 HOH C O   1 
HETATM 9204 O  O   . HOH R 7 .   ? 23.112  4.508   20.416  1.00 33.25 ? 473 HOH C O   1 
HETATM 9205 O  O   . HOH R 7 .   ? 27.467  33.489  13.940  1.00 19.65 ? 474 HOH C O   1 
HETATM 9206 O  O   . HOH R 7 .   ? 22.889  34.361  30.604  1.00 22.79 ? 475 HOH C O   1 
HETATM 9207 O  O   . HOH R 7 .   ? 10.036  24.284  23.192  1.00 16.46 ? 476 HOH C O   1 
HETATM 9208 O  O   . HOH R 7 .   ? 20.192  37.456  28.210  1.00 26.25 ? 477 HOH C O   1 
HETATM 9209 O  O   . HOH R 7 .   ? 14.790  2.020   22.042  1.00 23.46 ? 478 HOH C O   1 
HETATM 9210 O  O   . HOH R 7 .   ? 8.977   14.851  26.995  1.00 16.56 ? 479 HOH C O   1 
HETATM 9211 O  O   . HOH R 7 .   ? 25.167  32.545  34.156  1.00 25.11 ? 480 HOH C O   1 
HETATM 9212 O  O   . HOH R 7 .   ? 12.052  12.381  14.097  1.00 21.99 ? 481 HOH C O   1 
HETATM 9213 O  O   . HOH R 7 .   ? 40.365  26.189  15.069  1.00 20.22 ? 482 HOH C O   1 
HETATM 9214 O  O   . HOH R 7 .   ? 17.696  26.912  42.847  1.00 29.32 ? 483 HOH C O   1 
HETATM 9215 O  O   . HOH R 7 .   ? 11.132  16.729  22.225  1.00 23.69 ? 484 HOH C O   1 
HETATM 9216 O  O   . HOH R 7 .   ? 17.137  9.269   39.826  1.00 20.48 ? 485 HOH C O   1 
HETATM 9217 O  O   . HOH R 7 .   ? 39.465  14.293  41.772  1.00 21.52 ? 486 HOH C O   1 
HETATM 9218 O  O   . HOH R 7 .   ? 18.338  9.968   49.903  1.00 26.59 ? 487 HOH C O   1 
HETATM 9219 O  O   . HOH R 7 .   ? 12.202  16.824  36.470  1.00 14.98 ? 488 HOH C O   1 
HETATM 9220 O  O   . HOH R 7 .   ? 19.681  34.517  29.047  1.00 25.84 ? 489 HOH C O   1 
HETATM 9221 O  O   . HOH R 7 .   ? 15.784  4.049   15.103  1.00 19.32 ? 490 HOH C O   1 
HETATM 9222 O  O   . HOH R 7 .   ? 6.306   5.304   24.579  1.00 27.89 ? 491 HOH C O   1 
HETATM 9223 O  O   . HOH R 7 .   ? 36.125  19.593  43.211  1.00 19.81 ? 492 HOH C O   1 
HETATM 9224 O  O   . HOH R 7 .   ? 38.297  17.008  41.792  1.00 25.83 ? 493 HOH C O   1 
HETATM 9225 O  O   . HOH R 7 .   ? 16.211  23.879  14.135  1.00 26.89 ? 494 HOH C O   1 
HETATM 9226 O  O   . HOH R 7 .   ? 28.681  24.945  49.544  1.00 23.91 ? 495 HOH C O   1 
HETATM 9227 O  O   . HOH R 7 .   ? 23.344  -3.198  28.829  1.00 22.93 ? 496 HOH C O   1 
HETATM 9228 O  O   . HOH R 7 .   ? 9.536   28.642  21.089  1.00 29.04 ? 497 HOH C O   1 
HETATM 9229 O  O   . HOH R 7 .   ? 18.653  1.792   36.148  1.00 24.48 ? 498 HOH C O   1 
HETATM 9230 O  O   . HOH R 7 .   ? 26.630  5.625   22.122  1.00 26.67 ? 499 HOH C O   1 
HETATM 9231 O  O   . HOH R 7 .   ? 35.141  11.910  50.468  1.00 34.35 ? 500 HOH C O   1 
HETATM 9232 O  O   . HOH R 7 .   ? 29.160  18.250  50.440  1.00 23.01 ? 501 HOH C O   1 
HETATM 9233 O  O   . HOH R 7 .   ? 37.135  9.196   24.436  1.00 16.91 ? 502 HOH C O   1 
HETATM 9234 O  O   . HOH R 7 .   ? 38.668  9.597   26.481  1.00 21.20 ? 503 HOH C O   1 
HETATM 9235 O  O   . HOH R 7 .   ? 17.914  34.507  33.072  1.00 20.84 ? 504 HOH C O   1 
HETATM 9236 O  O   . HOH R 7 .   ? 33.694  7.403   37.727  1.00 29.97 ? 505 HOH C O   1 
HETATM 9237 O  O   . HOH R 7 .   ? 36.456  42.508  24.321  1.00 20.01 ? 506 HOH C O   1 
HETATM 9238 O  O   . HOH R 7 .   ? 27.785  30.248  37.903  1.00 23.99 ? 507 HOH C O   1 
HETATM 9239 O  O   . HOH R 7 .   ? 42.660  17.699  43.730  1.00 27.44 ? 508 HOH C O   1 
HETATM 9240 O  O   . HOH R 7 .   ? 23.102  25.840  11.571  1.00 35.07 ? 509 HOH C O   1 
HETATM 9241 O  O   . HOH R 7 .   ? 6.333   25.405  41.233  1.00 26.09 ? 510 HOH C O   1 
HETATM 9242 O  O   . HOH R 7 .   ? 11.998  13.802  11.793  1.00 25.93 ? 511 HOH C O   1 
HETATM 9243 O  O   . HOH R 7 .   ? 18.513  14.892  12.644  1.00 18.38 ? 512 HOH C O   1 
HETATM 9244 O  O   . HOH R 7 .   ? 21.029  19.993  14.535  1.00 25.70 ? 513 HOH C O   1 
HETATM 9245 O  O   . HOH R 7 .   ? 3.275   27.186  28.893  1.00 26.27 ? 514 HOH C O   1 
HETATM 9246 O  O   . HOH R 7 .   ? 35.514  24.254  44.237  1.00 30.35 ? 515 HOH C O   1 
HETATM 9247 O  O   . HOH R 7 .   ? 8.525   15.897  21.424  1.00 28.14 ? 516 HOH C O   1 
HETATM 9248 O  O   . HOH R 7 .   ? 19.808  31.457  14.602  1.00 20.06 ? 517 HOH C O   1 
HETATM 9249 O  O   . HOH R 7 .   ? 27.661  40.315  31.934  1.00 19.86 ? 518 HOH C O   1 
HETATM 9250 O  O   . HOH R 7 .   ? 24.686  37.154  26.943  1.00 27.81 ? 519 HOH C O   1 
HETATM 9251 O  O   . HOH R 7 .   ? 13.423  35.919  18.169  1.00 21.72 ? 520 HOH C O   1 
HETATM 9252 O  O   . HOH R 7 .   ? 38.883  38.522  34.772  1.00 25.24 ? 521 HOH C O   1 
HETATM 9253 O  O   . HOH R 7 .   ? 45.725  36.312  30.361  1.00 30.98 ? 522 HOH C O   1 
HETATM 9254 O  O   . HOH R 7 .   ? 27.467  27.055  10.963  1.00 24.70 ? 523 HOH C O   1 
HETATM 9255 O  O   . HOH R 7 .   ? 37.873  6.788   17.680  1.00 27.90 ? 524 HOH C O   1 
HETATM 9256 O  O   . HOH R 7 .   ? 39.980  7.103   38.028  1.00 26.13 ? 525 HOH C O   1 
HETATM 9257 O  O   . HOH R 7 .   ? 30.546  19.447  16.897  1.00 16.19 ? 526 HOH C O   1 
HETATM 9258 O  O   . HOH R 7 .   ? 28.937  17.816  15.123  1.00 26.49 ? 527 HOH C O   1 
HETATM 9259 O  O   . HOH R 7 .   ? 29.698  15.301  14.938  1.00 23.26 ? 528 HOH C O   1 
HETATM 9260 O  O   . HOH R 7 .   ? 32.274  15.579  15.972  1.00 13.89 ? 529 HOH C O   1 
HETATM 9261 O  O   . HOH R 7 .   ? 35.522  16.983  15.388  1.00 14.27 ? 530 HOH C O   1 
HETATM 9262 O  O   . HOH R 7 .   ? 19.570  -2.929  23.091  1.00 28.16 ? 531 HOH C O   1 
HETATM 9263 O  O   . HOH R 7 .   ? 46.760  20.569  25.098  1.00 16.90 ? 532 HOH C O   1 
HETATM 9264 O  O   . HOH R 7 .   ? 48.788  18.583  24.413  1.00 22.13 ? 533 HOH C O   1 
HETATM 9265 O  O   . HOH R 7 .   ? 44.588  25.647  27.058  1.00 27.45 ? 534 HOH C O   1 
HETATM 9266 O  O   . HOH R 7 .   ? 46.529  23.792  29.915  1.00 30.94 ? 535 HOH C O   1 
HETATM 9267 O  O   . HOH R 7 .   ? 49.036  29.403  29.632  1.00 20.51 ? 536 HOH C O   1 
HETATM 9268 O  O   . HOH R 7 .   ? 41.325  32.841  21.178  1.00 21.27 ? 537 HOH C O   1 
HETATM 9269 O  O   . HOH R 7 .   ? 42.623  33.683  23.396  1.00 20.68 ? 538 HOH C O   1 
HETATM 9270 O  O   . HOH R 7 .   ? 40.449  35.109  25.807  1.00 18.24 ? 539 HOH C O   1 
HETATM 9271 O  O   . HOH R 7 .   ? 34.011  7.002   22.894  1.00 19.81 ? 540 HOH C O   1 
HETATM 9272 O  O   . HOH R 7 .   ? 39.410  29.629  18.217  1.00 29.87 ? 541 HOH C O   1 
HETATM 9273 O  O   . HOH R 7 .   ? 37.256  28.361  12.947  1.00 30.06 ? 542 HOH C O   1 
HETATM 9274 O  O   . HOH R 7 .   ? 18.425  34.577  35.799  1.00 16.87 ? 543 HOH C O   1 
HETATM 9275 O  O   . HOH R 7 .   ? 3.475   2.809   26.437  1.00 32.34 ? 544 HOH C O   1 
HETATM 9276 O  O   . HOH R 7 .   ? 15.730  11.092  37.276  1.00 15.78 ? 545 HOH C O   1 
HETATM 9277 O  O   . HOH R 7 .   ? 11.370  9.675   32.833  1.00 31.57 ? 546 HOH C O   1 
HETATM 9278 O  O   . HOH R 7 .   ? 4.886   15.300  19.148  1.00 33.13 ? 547 HOH C O   1 
HETATM 9279 O  O   . HOH R 7 .   ? 18.125  22.276  13.565  1.00 32.33 ? 548 HOH C O   1 
HETATM 9280 O  O   . HOH R 7 .   ? 36.197  39.297  21.285  1.00 27.21 ? 549 HOH C O   1 
HETATM 9281 O  O   . HOH R 7 .   ? 27.232  37.568  27.952  1.00 17.56 ? 550 HOH C O   1 
HETATM 9282 O  O   . HOH R 7 .   ? 37.662  9.694   35.675  1.00 21.40 ? 551 HOH C O   1 
HETATM 9283 O  O   . HOH R 7 .   ? 2.008   29.730  36.085  1.00 24.90 ? 552 HOH C O   1 
HETATM 9284 O  O   . HOH R 7 .   ? 3.874   23.747  35.721  1.00 31.12 ? 553 HOH C O   1 
HETATM 9285 O  O   . HOH R 7 .   ? 33.489  22.105  14.061  1.00 23.70 ? 554 HOH C O   1 
HETATM 9286 O  O   . HOH R 7 .   ? 9.305   12.449  29.930  1.00 30.79 ? 555 HOH C O   1 
HETATM 9287 O  O   . HOH R 7 .   ? 19.998  6.500   12.182  1.00 24.48 ? 556 HOH C O   1 
HETATM 9288 O  O   . HOH R 7 .   ? 34.111  24.572  46.482  1.00 25.47 ? 557 HOH C O   1 
HETATM 9289 O  O   . HOH R 7 .   ? 45.266  14.802  17.553  1.00 23.66 ? 558 HOH C O   1 
HETATM 9290 O  O   . HOH R 7 .   ? 15.059  2.240   13.555  1.00 26.76 ? 559 HOH C O   1 
HETATM 9291 O  O   . HOH R 7 .   ? 25.760  44.255  14.338  1.00 31.43 ? 560 HOH C O   1 
HETATM 9292 O  O   . HOH R 7 .   ? 16.122  20.480  14.228  1.00 26.59 ? 561 HOH C O   1 
HETATM 9293 O  O   . HOH R 7 .   ? 35.534  39.582  30.016  1.00 23.88 ? 562 HOH C O   1 
HETATM 9294 O  O   . HOH R 7 .   ? 7.001   24.473  21.400  1.00 27.42 ? 563 HOH C O   1 
HETATM 9295 O  O   . HOH R 7 .   ? 40.296  37.118  30.449  1.00 24.37 ? 564 HOH C O   1 
HETATM 9296 O  O   . HOH R 7 .   ? 23.622  18.574  13.634  1.00 24.26 ? 565 HOH C O   1 
HETATM 9297 O  O   . HOH R 7 .   ? 8.890   6.721   33.447  1.00 30.01 ? 566 HOH C O   1 
HETATM 9298 O  O   . HOH R 7 .   ? 18.985  37.376  30.196  1.00 35.44 ? 567 HOH C O   1 
HETATM 9299 O  O   . HOH R 7 .   ? 16.870  10.026  42.792  1.00 14.90 ? 568 HOH C O   1 
HETATM 9300 O  O   . HOH R 7 .   ? 8.384   -0.449  21.336  1.00 18.54 ? 569 HOH C O   1 
HETATM 9301 O  O   . HOH R 7 .   ? 31.489  11.264  16.457  1.00 27.98 ? 570 HOH C O   1 
HETATM 9302 O  O   . HOH R 7 .   ? 34.652  8.653   24.881  1.00 23.41 ? 571 HOH C O   1 
HETATM 9303 O  O   . HOH R 7 .   ? 20.881  16.712  12.728  1.00 20.17 ? 572 HOH C O   1 
HETATM 9304 O  O   . HOH R 7 .   ? 44.881  21.839  19.261  1.00 25.94 ? 573 HOH C O   1 
HETATM 9305 O  O   . HOH R 7 .   ? 47.668  26.937  39.735  1.00 35.66 ? 574 HOH C O   1 
HETATM 9306 O  O   . HOH R 7 .   ? 34.508  40.860  32.014  1.00 25.84 ? 575 HOH C O   1 
HETATM 9307 O  O   . HOH R 7 .   ? 12.360  14.887  46.532  1.00 31.07 ? 576 HOH C O   1 
HETATM 9308 O  O   . HOH R 7 .   ? 45.069  18.057  35.223  1.00 28.39 ? 577 HOH C O   1 
HETATM 9309 O  O   . HOH R 7 .   ? 44.475  28.920  42.870  1.00 23.21 ? 578 HOH C O   1 
HETATM 9310 O  O   . HOH R 7 .   ? 12.911  9.803   41.710  1.00 28.49 ? 579 HOH C O   1 
HETATM 9311 O  O   . HOH R 7 .   ? 49.137  22.986  40.308  1.00 30.53 ? 580 HOH C O   1 
HETATM 9312 O  O   . HOH R 7 .   ? 10.276  9.709   18.216  1.00 26.83 ? 581 HOH C O   1 
HETATM 9313 O  O   . HOH R 7 .   ? 11.275  19.015  45.362  1.00 30.72 ? 582 HOH C O   1 
HETATM 9314 O  O   . HOH R 7 .   ? 31.943  42.218  31.867  1.00 26.00 ? 583 HOH C O   1 
HETATM 9315 O  O   . HOH R 7 .   ? 2.560   18.784  30.435  1.00 32.34 ? 584 HOH C O   1 
HETATM 9316 O  O   . HOH R 7 .   ? 47.772  21.243  27.613  1.00 28.77 ? 585 HOH C O   1 
HETATM 9317 O  O   . HOH R 7 .   ? 27.679  36.714  34.536  1.00 21.11 ? 586 HOH C O   1 
HETATM 9318 O  O   . HOH R 7 .   ? 45.385  16.114  37.459  1.00 30.48 ? 587 HOH C O   1 
HETATM 9319 O  O   . HOH R 7 .   ? 48.528  12.855  29.698  1.00 28.98 ? 588 HOH C O   1 
HETATM 9320 O  O   . HOH R 7 .   ? 10.862  18.714  34.952  1.00 20.68 ? 589 HOH C O   1 
HETATM 9321 O  O   . HOH R 7 .   ? 41.027  34.664  40.742  1.00 23.50 ? 590 HOH C O   1 
HETATM 9322 O  O   . HOH R 7 .   ? 34.390  33.772  45.623  1.00 38.80 ? 591 HOH C O   1 
HETATM 9323 O  O   . HOH R 7 .   ? 32.317  31.580  13.841  1.00 30.72 ? 592 HOH C O   1 
HETATM 9324 O  O   . HOH R 7 .   ? 22.914  15.409  10.825  1.00 26.57 ? 593 HOH C O   1 
HETATM 9325 O  O   . HOH R 7 .   ? 22.954  11.244  8.766   1.00 41.20 ? 594 HOH C O   1 
HETATM 9326 O  O   . HOH R 7 .   ? 49.026  32.720  40.116  1.00 40.93 ? 595 HOH C O   1 
HETATM 9327 O  O   . HOH R 7 .   ? 19.110  1.834   39.153  1.00 26.04 ? 596 HOH C O   1 
HETATM 9328 O  O   . HOH R 7 .   ? 18.092  -0.586  39.804  1.00 33.87 ? 597 HOH C O   1 
HETATM 9329 O  O   . HOH R 7 .   ? 13.847  1.900   36.197  1.00 28.53 ? 598 HOH C O   1 
HETATM 9330 O  O   . HOH R 7 .   ? 16.174  2.577   44.106  1.00 21.53 ? 599 HOH C O   1 
HETATM 9331 O  O   . HOH R 7 .   ? 30.667  17.663  54.535  1.00 36.65 ? 600 HOH C O   1 
HETATM 9332 O  O   . HOH R 7 .   ? 18.726  9.159   9.793   1.00 35.35 ? 601 HOH C O   1 
HETATM 9333 O  O   . HOH R 7 .   ? 22.813  36.816  28.921  1.00 22.77 ? 602 HOH C O   1 
HETATM 9334 O  O   . HOH R 7 .   ? 28.328  42.482  22.480  1.00 27.33 ? 603 HOH C O   1 
HETATM 9335 O  O   . HOH R 7 .   ? 8.071   17.620  32.025  1.00 40.14 ? 604 HOH C O   1 
HETATM 9336 O  O   . HOH R 7 .   ? 34.038  15.282  13.635  1.00 28.20 ? 605 HOH C O   1 
HETATM 9337 O  O   . HOH R 7 .   ? 41.591  37.042  33.123  1.00 33.06 ? 606 HOH C O   1 
HETATM 9338 O  O   . HOH R 7 .   ? 10.066  18.650  41.049  1.00 29.80 ? 607 HOH C O   1 
HETATM 9339 O  O   . HOH R 7 .   ? 37.599  12.409  52.380  1.00 27.66 ? 608 HOH C O   1 
HETATM 9340 O  O   . HOH R 7 .   ? 37.143  10.893  44.736  1.00 27.09 ? 609 HOH C O   1 
HETATM 9341 O  O   . HOH R 7 .   ? 39.829  17.642  50.865  1.00 34.22 ? 610 HOH C O   1 
HETATM 9342 O  O   . HOH R 7 .   ? 24.964  33.104  38.464  1.00 42.12 ? 611 HOH C O   1 
HETATM 9343 O  O   . HOH R 7 .   ? 35.052  6.215   26.612  1.00 36.44 ? 612 HOH C O   1 
HETATM 9344 O  O   . HOH R 7 .   ? 18.825  3.990   14.848  1.00 33.46 ? 613 HOH C O   1 
HETATM 9345 O  O   . HOH R 7 .   ? 49.782  15.630  22.163  1.00 32.06 ? 614 HOH C O   1 
HETATM 9346 O  O   . HOH R 7 .   ? 44.335  21.847  21.597  1.00 22.96 ? 615 HOH C O   1 
HETATM 9347 O  O   . HOH R 7 .   ? 41.311  24.809  48.553  1.00 30.94 ? 616 HOH C O   1 
HETATM 9348 O  O   . HOH R 7 .   ? 18.332  10.171  11.903  1.00 35.21 ? 617 HOH C O   1 
HETATM 9349 O  O   . HOH R 7 .   ? 26.802  36.693  12.728  1.00 31.32 ? 618 HOH C O   1 
HETATM 9350 O  O   . HOH R 7 .   ? 9.854   35.253  30.381  1.00 32.24 ? 619 HOH C O   1 
HETATM 9351 O  O   . HOH R 7 .   ? 28.273  2.197   24.659  1.00 24.40 ? 620 HOH C O   1 
HETATM 9352 O  O   . HOH S 7 .   ? 27.957  6.781   43.880  1.00 8.24  ? 401 HOH D O   1 
HETATM 9353 O  O   . HOH S 7 .   ? 26.867  -0.485  41.649  1.00 5.89  ? 402 HOH D O   1 
HETATM 9354 O  O   . HOH S 7 .   ? 26.384  6.725   49.375  1.00 9.01  ? 403 HOH D O   1 
HETATM 9355 O  O   . HOH S 7 .   ? 39.539  -9.945  50.884  1.00 7.36  ? 404 HOH D O   1 
HETATM 9356 O  O   . HOH S 7 .   ? 11.593  -21.480 51.866  1.00 16.16 ? 405 HOH D O   1 
HETATM 9357 O  O   . HOH S 7 .   ? 29.839  6.371   59.536  1.00 9.39  ? 406 HOH D O   1 
HETATM 9358 O  O   . HOH S 7 .   ? 20.010  4.582   47.219  1.00 12.89 ? 407 HOH D O   1 
HETATM 9359 O  O   . HOH S 7 .   ? 42.911  -16.670 45.768  1.00 14.38 ? 408 HOH D O   1 
HETATM 9360 O  O   . HOH S 7 .   ? 32.335  8.981   45.206  1.00 10.99 ? 409 HOH D O   1 
HETATM 9361 O  O   . HOH S 7 .   ? 26.630  6.238   46.254  1.00 9.64  ? 410 HOH D O   1 
HETATM 9362 O  O   . HOH S 7 .   ? 32.685  9.553   49.963  1.00 10.32 ? 411 HOH D O   1 
HETATM 9363 O  O   . HOH S 7 .   ? 25.179  -1.810  49.530  1.00 11.19 ? 412 HOH D O   1 
HETATM 9364 O  O   . HOH S 7 .   ? 32.162  -29.948 64.127  1.00 18.74 ? 413 HOH D O   1 
HETATM 9365 O  O   . HOH S 7 .   ? 34.510  3.634   40.249  1.00 13.75 ? 414 HOH D O   1 
HETATM 9366 O  O   . HOH S 7 .   ? 31.934  -26.553 60.923  1.00 18.82 ? 415 HOH D O   1 
HETATM 9367 O  O   . HOH S 7 .   ? 7.786   -6.820  40.143  1.00 15.55 ? 416 HOH D O   1 
HETATM 9368 O  O   . HOH S 7 .   ? 31.596  13.599  50.750  1.00 14.65 ? 417 HOH D O   1 
HETATM 9369 O  O   . HOH S 7 .   ? 22.804  -7.558  60.436  1.00 19.06 ? 418 HOH D O   1 
HETATM 9370 O  O   . HOH S 7 .   ? 25.182  -10.822 34.568  1.00 11.56 ? 419 HOH D O   1 
HETATM 9371 O  O   . HOH S 7 .   ? 36.214  -9.993  35.530  1.00 18.30 ? 420 HOH D O   1 
HETATM 9372 O  O   . HOH S 7 .   ? 23.504  7.694   44.509  1.00 8.49  ? 421 HOH D O   1 
HETATM 9373 O  O   . HOH S 7 .   ? 22.411  -4.573  52.071  1.00 15.05 ? 422 HOH D O   1 
HETATM 9374 O  O   . HOH S 7 .   ? 33.408  -13.416 40.858  1.00 14.73 ? 423 HOH D O   1 
HETATM 9375 O  O   . HOH S 7 .   ? 41.678  -5.103  56.546  1.00 10.61 ? 424 HOH D O   1 
HETATM 9376 O  O   . HOH S 7 .   ? 42.558  -21.092 41.523  1.00 17.07 ? 425 HOH D O   1 
HETATM 9377 O  O   . HOH S 7 .   ? 13.798  -10.108 47.623  1.00 11.36 ? 426 HOH D O   1 
HETATM 9378 O  O   . HOH S 7 .   ? 15.497  -14.122 36.081  1.00 13.57 ? 427 HOH D O   1 
HETATM 9379 O  O   . HOH S 7 .   ? 10.916  -8.836  46.675  1.00 16.19 ? 428 HOH D O   1 
HETATM 9380 O  O   . HOH S 7 .   ? 38.292  -16.059 39.620  1.00 11.77 ? 429 HOH D O   1 
HETATM 9381 O  O   . HOH S 7 .   ? 36.589  7.888   39.597  1.00 16.70 ? 430 HOH D O   1 
HETATM 9382 O  O   . HOH S 7 .   ? 41.967  -23.493 49.790  1.00 18.93 ? 431 HOH D O   1 
HETATM 9383 O  O   . HOH S 7 .   ? 42.245  2.126   47.747  1.00 12.46 ? 432 HOH D O   1 
HETATM 9384 O  O   . HOH S 7 .   ? 31.989  -15.792 63.544  1.00 13.69 ? 433 HOH D O   1 
HETATM 9385 O  O   . HOH S 7 .   ? 22.905  -2.754  33.180  1.00 27.33 ? 434 HOH D O   1 
HETATM 9386 O  O   . HOH S 7 .   ? 50.076  -12.109 41.361  1.00 18.34 ? 435 HOH D O   1 
HETATM 9387 O  O   . HOH S 7 .   ? 38.382  -14.842 66.848  1.00 20.21 ? 436 HOH D O   1 
HETATM 9388 O  O   . HOH S 7 .   ? 19.213  -8.672  39.950  1.00 10.39 ? 437 HOH D O   1 
HETATM 9389 O  O   . HOH S 7 .   ? 49.366  -18.870 51.959  1.00 21.05 ? 438 HOH D O   1 
HETATM 9390 O  O   . HOH S 7 .   ? 25.956  -11.542 61.944  1.00 19.08 ? 439 HOH D O   1 
HETATM 9391 O  O   . HOH S 7 .   ? 42.933  -19.449 45.318  1.00 18.87 ? 440 HOH D O   1 
HETATM 9392 O  O   . HOH S 7 .   ? 19.734  8.781   47.647  1.00 14.75 ? 441 HOH D O   1 
HETATM 9393 O  O   . HOH S 7 .   ? 43.946  -0.167  47.129  1.00 18.54 ? 442 HOH D O   1 
HETATM 9394 O  O   . HOH S 7 .   ? 24.898  -19.211 63.442  1.00 17.38 ? 443 HOH D O   1 
HETATM 9395 O  O   . HOH S 7 .   ? 20.514  -25.779 52.822  1.00 21.61 ? 444 HOH D O   1 
HETATM 9396 O  O   . HOH S 7 .   ? 7.281   -13.072 47.865  1.00 15.62 ? 445 HOH D O   1 
HETATM 9397 O  O   . HOH S 7 .   ? 28.186  -8.624  32.748  1.00 22.10 ? 446 HOH D O   1 
HETATM 9398 O  O   . HOH S 7 .   ? 17.544  -3.600  51.450  1.00 14.67 ? 447 HOH D O   1 
HETATM 9399 O  O   . HOH S 7 .   ? 22.527  -27.247 36.716  1.00 23.62 ? 448 HOH D O   1 
HETATM 9400 O  O   . HOH S 7 .   ? 45.152  -24.374 53.996  1.00 19.95 ? 449 HOH D O   1 
HETATM 9401 O  O   . HOH S 7 .   ? 11.257  -17.728 60.524  1.00 19.48 ? 450 HOH D O   1 
HETATM 9402 O  O   . HOH S 7 .   ? 34.721  3.937   35.781  1.00 23.44 ? 451 HOH D O   1 
HETATM 9403 O  O   . HOH S 7 .   ? 39.424  -17.097 65.197  1.00 19.95 ? 452 HOH D O   1 
HETATM 9404 O  O   . HOH S 7 .   ? 15.469  -21.373 43.915  1.00 21.40 ? 453 HOH D O   1 
HETATM 9405 O  O   . HOH S 7 .   ? 25.076  -26.151 65.706  1.00 26.09 ? 454 HOH D O   1 
HETATM 9406 O  O   . HOH S 7 .   ? 9.431   -2.357  59.293  1.00 20.17 ? 455 HOH D O   1 
HETATM 9407 O  O   . HOH S 7 .   ? 22.916  -12.337 34.013  1.00 15.27 ? 456 HOH D O   1 
HETATM 9408 O  O   . HOH S 7 .   ? 28.527  -14.955 63.156  1.00 20.21 ? 457 HOH D O   1 
HETATM 9409 O  O   . HOH S 7 .   ? 17.091  -25.295 65.678  1.00 20.47 ? 458 HOH D O   1 
HETATM 9410 O  O   . HOH S 7 .   ? 38.078  -25.249 53.733  1.00 14.37 ? 459 HOH D O   1 
HETATM 9411 O  O   . HOH S 7 .   ? 38.060  -10.956 33.090  1.00 25.02 ? 460 HOH D O   1 
HETATM 9412 O  O   . HOH S 7 .   ? 22.135  -29.412 61.666  1.00 18.09 ? 461 HOH D O   1 
HETATM 9413 O  O   . HOH S 7 .   ? 32.111  -21.805 38.445  1.00 28.99 ? 462 HOH D O   1 
HETATM 9414 O  O   . HOH S 7 .   ? 24.126  -27.762 34.446  1.00 21.63 ? 463 HOH D O   1 
HETATM 9415 O  O   . HOH S 7 .   ? 32.416  -11.930 65.629  1.00 23.49 ? 464 HOH D O   1 
HETATM 9416 O  O   . HOH S 7 .   ? 27.386  -11.504 32.900  1.00 21.62 ? 465 HOH D O   1 
HETATM 9417 O  O   . HOH S 7 .   ? 12.258  -11.268 35.438  1.00 25.14 ? 466 HOH D O   1 
HETATM 9418 O  O   . HOH S 7 .   ? 33.032  7.959   47.614  1.00 12.01 ? 467 HOH D O   1 
HETATM 9419 O  O   . HOH S 7 .   ? 20.620  -10.877 34.384  1.00 18.18 ? 468 HOH D O   1 
HETATM 9420 O  O   . HOH S 7 .   ? 18.683  -19.509 33.297  1.00 25.07 ? 469 HOH D O   1 
HETATM 9421 O  O   . HOH S 7 .   ? 44.851  -23.306 62.831  1.00 20.44 ? 470 HOH D O   1 
HETATM 9422 O  O   . HOH S 7 .   ? 19.095  6.658   45.989  1.00 13.58 ? 471 HOH D O   1 
HETATM 9423 O  O   . HOH S 7 .   ? 25.524  -23.100 37.725  1.00 17.85 ? 472 HOH D O   1 
HETATM 9424 O  O   . HOH S 7 .   ? 36.354  10.040  49.125  1.00 20.00 ? 473 HOH D O   1 
HETATM 9425 O  O   . HOH S 7 .   ? 43.572  -15.493 63.872  1.00 15.87 ? 474 HOH D O   1 
HETATM 9426 O  O   . HOH S 7 .   ? 34.482  -25.057 60.065  1.00 17.93 ? 475 HOH D O   1 
HETATM 9427 O  O   . HOH S 7 .   ? 29.475  -30.005 54.826  1.00 25.17 ? 476 HOH D O   1 
HETATM 9428 O  O   . HOH S 7 .   ? 8.404   -15.604 56.423  1.00 19.93 ? 477 HOH D O   1 
HETATM 9429 O  O   . HOH S 7 .   ? 35.740  7.623   48.550  1.00 13.50 ? 478 HOH D O   1 
HETATM 9430 O  O   . HOH S 7 .   ? 28.232  -29.018 50.881  1.00 16.62 ? 479 HOH D O   1 
HETATM 9431 O  O   . HOH S 7 .   ? 38.384  -25.122 61.179  1.00 17.97 ? 480 HOH D O   1 
HETATM 9432 O  O   . HOH S 7 .   ? 28.904  -22.028 42.453  1.00 15.58 ? 481 HOH D O   1 
HETATM 9433 O  O   . HOH S 7 .   ? 11.581  -18.366 40.332  1.00 18.39 ? 482 HOH D O   1 
HETATM 9434 O  O   . HOH S 7 .   ? 23.348  2.887   37.354  1.00 19.54 ? 483 HOH D O   1 
HETATM 9435 O  O   . HOH S 7 .   ? 19.056  -2.895  38.828  1.00 17.68 ? 484 HOH D O   1 
HETATM 9436 O  O   . HOH S 7 .   ? 22.359  -27.104 54.048  1.00 16.58 ? 485 HOH D O   1 
HETATM 9437 O  O   . HOH S 7 .   ? 16.137  -2.708  49.192  1.00 21.88 ? 486 HOH D O   1 
HETATM 9438 O  O   . HOH S 7 .   ? 45.093  -14.321 55.646  1.00 17.18 ? 487 HOH D O   1 
HETATM 9439 O  O   . HOH S 7 .   ? 33.901  -14.071 67.090  1.00 23.09 ? 488 HOH D O   1 
HETATM 9440 O  O   . HOH S 7 .   ? 48.332  -15.537 55.527  1.00 14.05 ? 489 HOH D O   1 
HETATM 9441 O  O   . HOH S 7 .   ? 28.350  -21.405 38.057  1.00 19.72 ? 490 HOH D O   1 
HETATM 9442 O  O   . HOH S 7 .   ? 45.609  -7.780  56.251  1.00 22.67 ? 491 HOH D O   1 
HETATM 9443 O  O   . HOH S 7 .   ? 5.976   -5.317  55.796  1.00 19.52 ? 492 HOH D O   1 
HETATM 9444 O  O   . HOH S 7 .   ? 28.501  -10.200 61.312  1.00 19.26 ? 493 HOH D O   1 
HETATM 9445 O  O   . HOH S 7 .   ? 8.278   -6.585  37.525  1.00 26.13 ? 494 HOH D O   1 
HETATM 9446 O  O   . HOH S 7 .   ? 34.170  -23.728 44.144  1.00 24.88 ? 495 HOH D O   1 
HETATM 9447 O  O   . HOH S 7 .   ? 32.120  -16.163 66.693  1.00 31.29 ? 496 HOH D O   1 
HETATM 9448 O  O   . HOH S 7 .   ? 36.022  -28.020 63.407  1.00 27.69 ? 497 HOH D O   1 
HETATM 9449 O  O   . HOH S 7 .   ? 14.925  -11.372 37.082  1.00 17.31 ? 498 HOH D O   1 
HETATM 9450 O  O   . HOH S 7 .   ? 2.992   -9.495  64.011  1.00 31.07 ? 499 HOH D O   1 
HETATM 9451 O  O   . HOH S 7 .   ? 19.631  -29.866 33.569  1.00 29.94 ? 500 HOH D O   1 
HETATM 9452 O  O   . HOH S 7 .   ? 13.841  6.308   51.988  1.00 16.74 ? 501 HOH D O   1 
HETATM 9453 O  O   . HOH S 7 .   ? 9.302   -22.822 51.622  1.00 26.13 ? 502 HOH D O   1 
HETATM 9454 O  O   . HOH S 7 .   ? 17.233  -1.453  52.839  1.00 24.26 ? 503 HOH D O   1 
HETATM 9455 O  O   . HOH S 7 .   ? 33.466  -28.444 62.100  1.00 18.86 ? 504 HOH D O   1 
HETATM 9456 O  O   . HOH S 7 .   ? 31.286  -0.011  63.298  1.00 24.13 ? 505 HOH D O   1 
HETATM 9457 O  O   . HOH S 7 .   ? 40.172  -26.579 55.462  1.00 18.79 ? 506 HOH D O   1 
HETATM 9458 O  O   . HOH S 7 .   ? 24.574  -8.106  34.366  1.00 25.52 ? 507 HOH D O   1 
HETATM 9459 O  O   . HOH S 7 .   ? 25.014  -22.283 31.272  1.00 24.84 ? 508 HOH D O   1 
HETATM 9460 O  O   . HOH S 7 .   ? 4.795   -17.364 51.870  1.00 26.16 ? 509 HOH D O   1 
HETATM 9461 O  O   . HOH S 7 .   ? 36.368  -26.853 60.343  1.00 20.45 ? 510 HOH D O   1 
HETATM 9462 O  O   . HOH S 7 .   ? 11.969  -15.691 63.287  1.00 20.31 ? 511 HOH D O   1 
HETATM 9463 O  O   . HOH S 7 .   ? 21.579  -1.946  35.305  1.00 26.31 ? 512 HOH D O   1 
HETATM 9464 O  O   . HOH S 7 .   ? 45.643  -1.574  33.029  1.00 23.58 ? 513 HOH D O   1 
HETATM 9465 O  O   . HOH S 7 .   ? 20.027  -25.155 34.409  1.00 19.97 ? 514 HOH D O   1 
HETATM 9466 O  O   . HOH S 7 .   ? 12.383  -1.188  48.416  1.00 20.01 ? 515 HOH D O   1 
HETATM 9467 O  O   . HOH S 7 .   ? 33.356  -19.877 37.457  1.00 20.37 ? 516 HOH D O   1 
HETATM 9468 O  O   . HOH S 7 .   ? 11.156  -25.009 53.356  1.00 20.71 ? 517 HOH D O   1 
HETATM 9469 O  O   . HOH S 7 .   ? 11.768  -18.226 64.145  1.00 28.63 ? 518 HOH D O   1 
HETATM 9470 O  O   . HOH S 7 .   ? 35.940  -27.518 48.226  1.00 29.11 ? 519 HOH D O   1 
HETATM 9471 O  O   . HOH S 7 .   ? 15.833  -0.210  50.549  1.00 22.29 ? 520 HOH D O   1 
HETATM 9472 O  O   . HOH S 7 .   ? 30.028  1.272   36.579  1.00 19.37 ? 521 HOH D O   1 
HETATM 9473 O  O   . HOH S 7 .   ? 3.886   -14.249 53.726  1.00 25.35 ? 522 HOH D O   1 
HETATM 9474 O  O   . HOH S 7 .   ? 39.535  -20.104 65.432  1.00 25.73 ? 523 HOH D O   1 
HETATM 9475 O  O   . HOH S 7 .   ? 32.503  -6.662  31.581  1.00 19.59 ? 524 HOH D O   1 
HETATM 9476 O  O   . HOH S 7 .   ? 34.331  -9.707  33.540  1.00 27.47 ? 525 HOH D O   1 
HETATM 9477 O  O   . HOH S 7 .   ? 36.966  -27.243 55.555  1.00 14.67 ? 526 HOH D O   1 
HETATM 9478 O  O   . HOH S 7 .   ? 20.789  -27.886 46.470  1.00 21.49 ? 527 HOH D O   1 
HETATM 9479 O  O   . HOH S 7 .   ? 12.636  -1.628  40.689  1.00 23.24 ? 528 HOH D O   1 
HETATM 9480 O  O   . HOH S 7 .   ? 36.135  -26.581 51.642  1.00 24.75 ? 529 HOH D O   1 
HETATM 9481 O  O   . HOH S 7 .   ? 29.832  -23.510 64.735  1.00 24.16 ? 530 HOH D O   1 
HETATM 9482 O  O   . HOH S 7 .   ? 43.233  -27.759 53.809  1.00 30.89 ? 531 HOH D O   1 
HETATM 9483 O  O   . HOH S 7 .   ? 28.815  -9.435  65.328  1.00 22.54 ? 532 HOH D O   1 
HETATM 9484 O  O   . HOH S 7 .   ? 24.732  -4.257  58.954  1.00 27.24 ? 533 HOH D O   1 
HETATM 9485 O  O   . HOH S 7 .   ? 26.156  -6.937  62.481  1.00 30.94 ? 534 HOH D O   1 
HETATM 9486 O  O   . HOH S 7 .   ? 29.789  -5.435  63.161  1.00 29.04 ? 535 HOH D O   1 
HETATM 9487 O  O   . HOH S 7 .   ? 38.303  3.139   30.447  1.00 24.00 ? 536 HOH D O   1 
HETATM 9488 O  O   . HOH S 7 .   ? 32.621  0.933   28.403  1.00 26.87 ? 537 HOH D O   1 
HETATM 9489 O  O   . HOH S 7 .   ? 15.438  -0.851  54.770  1.00 26.23 ? 538 HOH D O   1 
HETATM 9490 O  O   . HOH S 7 .   ? 12.357  3.121   50.646  1.00 28.14 ? 539 HOH D O   1 
HETATM 9491 O  O   . HOH S 7 .   ? 25.851  8.530   47.305  1.00 18.84 ? 540 HOH D O   1 
HETATM 9492 O  O   . HOH S 7 .   ? 38.819  -4.130  33.374  1.00 36.11 ? 541 HOH D O   1 
HETATM 9493 O  O   . HOH S 7 .   ? 39.218  -6.582  33.883  1.00 27.97 ? 542 HOH D O   1 
HETATM 9494 O  O   . HOH S 7 .   ? 38.173  -1.460  31.051  1.00 25.91 ? 543 HOH D O   1 
HETATM 9495 O  O   . HOH S 7 .   ? 48.844  -11.829 48.502  1.00 28.81 ? 544 HOH D O   1 
HETATM 9496 O  O   . HOH S 7 .   ? 50.519  -7.526  52.476  1.00 22.15 ? 545 HOH D O   1 
HETATM 9497 O  O   . HOH S 7 .   ? 31.583  -29.994 48.548  1.00 34.15 ? 546 HOH D O   1 
HETATM 9498 O  O   . HOH S 7 .   ? 26.580  -26.320 42.621  1.00 22.05 ? 547 HOH D O   1 
HETATM 9499 O  O   . HOH S 7 .   ? 14.958  -22.071 62.690  1.00 23.32 ? 548 HOH D O   1 
HETATM 9500 O  O   . HOH S 7 .   ? 24.546  -16.753 64.948  1.00 26.11 ? 549 HOH D O   1 
HETATM 9501 O  O   . HOH S 7 .   ? 42.318  -21.721 65.018  1.00 24.34 ? 550 HOH D O   1 
HETATM 9502 O  O   . HOH S 7 .   ? 10.468  -3.947  40.559  1.00 19.54 ? 551 HOH D O   1 
HETATM 9503 O  O   . HOH S 7 .   ? 25.562  -4.083  32.828  1.00 27.94 ? 552 HOH D O   1 
HETATM 9504 O  O   . HOH S 7 .   ? 19.442  -28.964 30.867  1.00 30.56 ? 553 HOH D O   1 
HETATM 9505 O  O   . HOH S 7 .   ? 44.965  -21.850 35.417  1.00 39.24 ? 554 HOH D O   1 
HETATM 9506 O  O   . HOH S 7 .   ? 40.545  -0.197  53.922  1.00 13.17 ? 555 HOH D O   1 
HETATM 9507 O  O   . HOH S 7 .   ? 54.606  -12.606 35.811  1.00 26.29 ? 556 HOH D O   1 
HETATM 9508 O  O   . HOH S 7 .   ? 48.957  -13.842 35.010  1.00 34.97 ? 557 HOH D O   1 
HETATM 9509 O  O   . HOH S 7 .   ? 6.046   -14.770 55.716  1.00 26.35 ? 558 HOH D O   1 
HETATM 9510 O  O   . HOH S 7 .   ? 38.969  10.267  48.607  1.00 26.01 ? 559 HOH D O   1 
HETATM 9511 O  O   . HOH S 7 .   ? 42.424  7.593   50.763  1.00 16.46 ? 560 HOH D O   1 
HETATM 9512 O  O   . HOH S 7 .   ? 44.495  6.080   49.197  1.00 26.76 ? 561 HOH D O   1 
HETATM 9513 O  O   . HOH S 7 .   ? 48.599  -15.106 60.969  1.00 23.69 ? 562 HOH D O   1 
HETATM 9514 O  O   . HOH S 7 .   ? 48.876  -10.505 61.843  1.00 25.22 ? 563 HOH D O   1 
HETATM 9515 O  O   . HOH S 7 .   ? 46.906  -6.929  58.597  1.00 25.82 ? 564 HOH D O   1 
HETATM 9516 O  O   . HOH S 7 .   ? 31.039  -9.646  66.588  1.00 18.04 ? 565 HOH D O   1 
HETATM 9517 O  O   . HOH S 7 .   ? 8.143   -17.417 58.340  1.00 23.38 ? 566 HOH D O   1 
HETATM 9518 O  O   . HOH S 7 .   ? 13.339  -24.615 54.150  1.00 18.66 ? 567 HOH D O   1 
HETATM 9519 O  O   . HOH S 7 .   ? 17.825  -28.084 55.025  1.00 29.80 ? 568 HOH D O   1 
HETATM 9520 O  O   . HOH S 7 .   ? 17.221  -27.071 45.808  1.00 27.84 ? 569 HOH D O   1 
HETATM 9521 O  O   . HOH S 7 .   ? 14.431  -23.238 46.122  1.00 26.17 ? 570 HOH D O   1 
HETATM 9522 O  O   . HOH S 7 .   ? 17.256  -24.456 33.796  1.00 27.03 ? 571 HOH D O   1 
HETATM 9523 O  O   . HOH S 7 .   ? 8.768   -15.198 42.269  1.00 30.81 ? 572 HOH D O   1 
HETATM 9524 O  O   . HOH S 7 .   ? 26.599  1.705   39.867  1.00 11.54 ? 573 HOH D O   1 
HETATM 9525 O  O   . HOH S 7 .   ? 21.452  9.399   57.326  1.00 14.98 ? 574 HOH D O   1 
HETATM 9526 O  O   . HOH S 7 .   ? 19.875  7.694   55.197  1.00 22.63 ? 575 HOH D O   1 
HETATM 9527 O  O   . HOH S 7 .   ? 16.320  6.901   45.350  1.00 16.84 ? 576 HOH D O   1 
HETATM 9528 O  O   . HOH S 7 .   ? 47.222  3.156   34.229  1.00 32.27 ? 577 HOH D O   1 
HETATM 9529 O  O   . HOH S 7 .   ? 52.813  -4.690  36.998  1.00 20.10 ? 578 HOH D O   1 
HETATM 9530 O  O   . HOH S 7 .   ? 22.803  -32.095 57.441  1.00 25.40 ? 579 HOH D O   1 
HETATM 9531 O  O   . HOH S 7 .   ? 15.061  -2.221  57.270  1.00 36.51 ? 580 HOH D O   1 
HETATM 9532 O  O   . HOH S 7 .   ? 28.683  -17.298 64.560  1.00 23.00 ? 581 HOH D O   1 
HETATM 9533 O  O   . HOH S 7 .   ? 30.755  -13.254 64.066  1.00 18.43 ? 582 HOH D O   1 
HETATM 9534 O  O   . HOH S 7 .   ? 47.788  -19.081 58.786  1.00 22.91 ? 583 HOH D O   1 
HETATM 9535 O  O   . HOH S 7 .   ? 30.380  -8.044  31.635  1.00 28.27 ? 584 HOH D O   1 
HETATM 9536 O  O   . HOH S 7 .   ? 42.385  -16.718 65.994  1.00 31.32 ? 585 HOH D O   1 
HETATM 9537 O  O   . HOH S 7 .   ? 19.057  -28.162 44.642  1.00 26.78 ? 586 HOH D O   1 
HETATM 9538 O  O   . HOH S 7 .   ? 15.316  -10.140 65.376  1.00 31.74 ? 587 HOH D O   1 
HETATM 9539 O  O   . HOH S 7 .   ? 39.672  3.508   60.311  1.00 27.13 ? 588 HOH D O   1 
HETATM 9540 O  O   . HOH S 7 .   ? 16.618  -21.915 33.473  1.00 31.12 ? 589 HOH D O   1 
HETATM 9541 O  O   . HOH S 7 .   ? 39.367  9.051   45.506  1.00 35.61 ? 590 HOH D O   1 
HETATM 9542 O  O   . HOH S 7 .   ? 49.546  -3.689  34.832  1.00 30.40 ? 591 HOH D O   1 
HETATM 9543 O  O   . HOH S 7 .   ? 25.236  -6.797  59.807  1.00 25.59 ? 592 HOH D O   1 
HETATM 9544 O  O   . HOH S 7 .   ? 36.612  5.118   46.605  1.00 20.32 ? 593 HOH D O   1 
HETATM 9545 O  O   . HOH S 7 .   ? 26.354  -24.959 39.486  1.00 20.54 ? 594 HOH D O   1 
HETATM 9546 O  O   . HOH S 7 .   ? 46.050  -13.231 48.924  1.00 35.50 ? 595 HOH D O   1 
HETATM 9547 O  O   . HOH S 7 .   ? 37.181  12.710  42.553  1.00 24.83 ? 596 HOH D O   1 
HETATM 9548 O  O   . HOH S 7 .   ? 46.937  -15.514 43.177  1.00 21.52 ? 597 HOH D O   1 
HETATM 9549 O  O   . HOH S 7 .   ? 34.180  1.737   32.732  1.00 24.17 ? 598 HOH D O   1 
HETATM 9550 O  O   . HOH S 7 .   ? 24.971  -1.807  30.428  1.00 26.16 ? 599 HOH D O   1 
HETATM 9551 O  O   . HOH S 7 .   ? 8.997   -9.309  61.011  1.00 20.56 ? 600 HOH D O   1 
HETATM 9552 O  O   . HOH S 7 .   ? 38.391  2.588   47.636  1.00 25.04 ? 601 HOH D O   1 
HETATM 9553 O  O   . HOH S 7 .   ? 27.481  1.725   37.570  1.00 33.68 ? 602 HOH D O   1 
HETATM 9554 O  O   . HOH S 7 .   ? 27.019  -16.853 66.473  1.00 25.71 ? 603 HOH D O   1 
HETATM 9555 O  O   . HOH S 7 .   ? 43.561  -17.802 32.727  1.00 29.56 ? 604 HOH D O   1 
HETATM 9556 O  O   . HOH S 7 .   ? 31.777  -18.372 65.946  1.00 26.14 ? 605 HOH D O   1 
HETATM 9557 O  O   . HOH S 7 .   ? 13.093  0.340   50.693  1.00 21.16 ? 606 HOH D O   1 
HETATM 9558 O  O   . HOH S 7 .   ? 27.771  -30.795 53.215  1.00 33.73 ? 607 HOH D O   1 
HETATM 9559 O  O   . HOH S 7 .   ? 46.300  3.018   45.038  1.00 38.16 ? 608 HOH D O   1 
HETATM 9560 O  O   . HOH S 7 .   ? 30.046  -18.599 35.225  1.00 25.54 ? 609 HOH D O   1 
HETATM 9561 O  O   . HOH S 7 .   ? 10.722  -16.141 45.798  1.00 20.99 ? 610 HOH D O   1 
HETATM 9562 O  O   . HOH S 7 .   ? 16.074  -23.463 37.834  1.00 26.26 ? 611 HOH D O   1 
HETATM 9563 O  O   . HOH S 7 .   ? 32.652  -3.230  28.632  1.00 34.41 ? 612 HOH D O   1 
HETATM 9564 O  O   . HOH S 7 .   ? 24.538  -21.230 64.825  1.00 30.34 ? 613 HOH D O   1 
HETATM 9565 O  O   . HOH S 7 .   ? 31.365  -4.675  71.453  1.00 40.23 ? 614 HOH D O   1 
HETATM 9566 O  O   . HOH S 7 .   ? 44.904  -19.216 37.469  1.00 28.69 ? 615 HOH D O   1 
HETATM 9567 O  O   . HOH S 7 .   ? 8.889   -8.236  35.156  1.00 33.91 ? 616 HOH D O   1 
HETATM 9568 O  O   . HOH S 7 .   ? 9.459   -10.903 36.072  1.00 24.36 ? 617 HOH D O   1 
HETATM 9569 O  O   . HOH S 7 .   ? 10.086  -6.102  32.955  1.00 28.04 ? 618 HOH D O   1 
HETATM 9570 O  O   . HOH S 7 .   ? 13.281  11.663  48.666  1.00 29.07 ? 619 HOH D O   1 
HETATM 9571 O  O   . HOH S 7 .   ? 17.557  0.778   58.924  1.00 36.54 ? 620 HOH D O   1 
HETATM 9572 O  O   . HOH S 7 .   ? 37.542  -6.196  31.401  1.00 37.19 ? 621 HOH D O   1 
HETATM 9573 O  O   . HOH S 7 .   ? 34.822  -8.460  31.028  1.00 31.51 ? 622 HOH D O   1 
HETATM 9574 O  O   . HOH S 7 .   ? 42.657  -25.273 53.221  1.00 31.78 ? 623 HOH D O   1 
HETATM 9575 O  O   . HOH S 7 .   ? 31.827  -24.720 63.114  1.00 23.28 ? 624 HOH D O   1 
HETATM 9576 O  O   . HOH S 7 .   ? 22.273  -14.631 60.608  1.00 31.81 ? 625 HOH D O   1 
HETATM 9577 O  O   . HOH S 7 .   ? 44.996  -5.049  68.490  1.00 23.52 ? 626 HOH D O   1 
HETATM 9578 O  O   . HOH S 7 .   ? 40.481  -13.364 67.796  1.00 21.28 ? 627 HOH D O   1 
HETATM 9579 O  O   . HOH S 7 .   ? 31.122  -2.612  64.749  1.00 35.29 ? 628 HOH D O   1 
HETATM 9580 O  O   . HOH S 7 .   ? 42.336  -0.395  57.537  1.00 26.62 ? 629 HOH D O   1 
HETATM 9581 O  O   . HOH S 7 .   ? 22.340  -22.575 30.912  1.00 23.55 ? 630 HOH D O   1 
HETATM 9582 O  O   . HOH S 7 .   ? 19.458  -27.632 34.967  1.00 25.73 ? 631 HOH D O   1 
HETATM 9583 O  O   . HOH S 7 .   ? 13.555  -18.241 66.219  1.00 36.79 ? 632 HOH D O   1 
HETATM 9584 O  O   . HOH S 7 .   ? 22.447  -31.232 55.045  1.00 41.08 ? 633 HOH D O   1 
HETATM 9585 O  O   . HOH S 7 .   ? 39.509  -23.821 39.354  1.00 28.97 ? 634 HOH D O   1 
HETATM 9586 O  O   . HOH S 7 .   ? 40.218  -16.938 34.448  1.00 34.58 ? 635 HOH D O   1 
HETATM 9587 O  O   . HOH S 7 .   ? 9.611   -18.019 42.307  1.00 28.27 ? 636 HOH D O   1 
HETATM 9588 O  O   . HOH S 7 .   ? 10.309  -8.092  43.084  1.00 20.51 ? 637 HOH D O   1 
HETATM 9589 O  O   . HOH S 7 .   ? 7.432   -1.739  61.977  1.00 39.05 ? 638 HOH D O   1 
HETATM 9590 O  O   . HOH S 7 .   ? 45.322  -6.907  34.616  1.00 37.57 ? 639 HOH D O   1 
HETATM 9591 O  O   . HOH S 7 .   ? 14.319  -21.337 41.695  1.00 29.13 ? 640 HOH D O   1 
HETATM 9592 O  O   . HOH S 7 .   ? 42.832  -13.512 29.528  1.00 31.36 ? 641 HOH D O   1 
HETATM 9593 O  O   . HOH S 7 .   ? 47.855  -8.734  52.599  1.00 25.21 ? 642 HOH D O   1 
HETATM 9594 O  O   . HOH S 7 .   ? 25.782  2.073   35.714  1.00 31.05 ? 643 HOH D O   1 
HETATM 9595 O  O   . HOH S 7 .   ? 10.088  -18.416 44.849  1.00 24.53 ? 644 HOH D O   1 
HETATM 9596 O  O   . HOH S 7 .   ? 54.888  -14.774 35.560  1.00 23.21 ? 645 HOH D O   1 
HETATM 9597 O  O   . HOH S 7 .   ? 13.251  -14.069 34.570  1.00 27.14 ? 646 HOH D O   1 
HETATM 9598 O  O   . HOH S 7 .   ? 19.376  4.359   60.551  1.00 35.92 ? 647 HOH D O   1 
HETATM 9599 O  O   . HOH S 7 .   ? 44.230  -21.264 43.887  1.00 26.95 ? 648 HOH D O   1 
HETATM 9600 O  O   . HOH S 7 .   ? 51.966  -13.079 58.218  1.00 28.17 ? 649 HOH D O   1 
HETATM 9601 O  O   . HOH S 7 .   ? 42.839  -10.712 69.769  1.00 36.15 ? 650 HOH D O   1 
HETATM 9602 O  O   . HOH S 7 .   ? 12.236  -24.629 49.283  1.00 26.40 ? 651 HOH D O   1 
HETATM 9603 O  O   . HOH S 7 .   ? 24.862  -30.174 53.807  1.00 31.85 ? 652 HOH D O   1 
HETATM 9604 O  O   . HOH S 7 .   ? 22.159  1.362   38.957  1.00 34.02 ? 653 HOH D O   1 
HETATM 9605 O  O   . HOH S 7 .   ? 51.529  -12.238 49.546  1.00 31.84 ? 654 HOH D O   1 
HETATM 9606 O  O   . HOH S 7 .   ? 51.182  -19.021 47.523  1.00 27.75 ? 655 HOH D O   1 
HETATM 9607 O  O   . HOH S 7 .   ? 19.339  -10.533 31.924  1.00 43.47 ? 656 HOH D O   1 
HETATM 9608 O  O   . HOH S 7 .   ? 41.954  -6.309  70.360  1.00 32.12 ? 657 HOH D O   1 
HETATM 9609 O  O   . HOH S 7 .   ? 14.444  -6.305  63.449  1.00 36.00 ? 658 HOH D O   1 
HETATM 9610 O  O   . HOH S 7 .   ? 15.311  -24.347 58.609  1.00 33.42 ? 659 HOH D O   1 
HETATM 9611 O  O   . HOH S 7 .   ? 35.335  -14.734 33.119  1.00 27.81 ? 660 HOH D O   1 
HETATM 9612 O  O   . HOH S 7 .   ? 3.179   -7.434  66.307  1.00 31.34 ? 661 HOH D O   1 
HETATM 9613 O  O   . HOH S 7 .   ? -0.747  -1.985  55.562  1.00 30.39 ? 662 HOH D O   1 
HETATM 9614 O  O   . HOH S 7 .   ? 32.097  8.503   62.587  1.00 25.81 ? 663 HOH D O   1 
HETATM 9615 O  O   . HOH S 7 .   ? 7.440   -19.725 41.943  1.00 29.98 ? 664 HOH D O   1 
# 
