data_6G7A
# 
_entry.id   6G7A 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   6G7A         pdb_00006g7a 10.2210/pdb6g7a/pdb 
WWPDB D_1200009520 ?            ?                   
# 
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 2019-03-13 
2 'Structure model' 1 1 2024-01-17 
3 'Structure model' 1 2 2024-11-06 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'        
2 2 'Structure model' 'Database references'    
3 2 'Structure model' 'Derived calculations'   
4 2 'Structure model' 'Refinement description' 
5 3 'Structure model' 'Structure summary'      
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' chem_comp_atom                
2 2 'Structure model' chem_comp_bond                
3 2 'Structure model' database_2                    
4 2 'Structure model' pdbx_initial_refinement_model 
5 2 'Structure model' struct_conn                   
6 3 'Structure model' pdbx_entry_details            
7 3 'Structure model' pdbx_modification_feature     
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_database_2.pdbx_DOI'                 
2  2 'Structure model' '_database_2.pdbx_database_accession'  
3  2 'Structure model' '_struct_conn.pdbx_dist_value'         
4  2 'Structure model' '_struct_conn.pdbx_ptnr2_label_alt_id' 
5  2 'Structure model' '_struct_conn.ptnr1_auth_asym_id'      
6  2 'Structure model' '_struct_conn.ptnr1_auth_comp_id'      
7  2 'Structure model' '_struct_conn.ptnr1_auth_seq_id'       
8  2 'Structure model' '_struct_conn.ptnr1_label_asym_id'     
9  2 'Structure model' '_struct_conn.ptnr1_label_atom_id'     
10 2 'Structure model' '_struct_conn.ptnr1_label_comp_id'     
11 2 'Structure model' '_struct_conn.ptnr1_label_seq_id'      
12 2 'Structure model' '_struct_conn.ptnr2_auth_asym_id'      
13 2 'Structure model' '_struct_conn.ptnr2_auth_comp_id'      
14 2 'Structure model' '_struct_conn.ptnr2_auth_seq_id'       
15 2 'Structure model' '_struct_conn.ptnr2_label_asym_id'     
16 2 'Structure model' '_struct_conn.ptnr2_label_atom_id'     
17 2 'Structure model' '_struct_conn.ptnr2_label_comp_id'     
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        6G7A 
_pdbx_database_status.recvd_initial_deposition_date   2018-04-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'PDB entries for the same citation' 6G5L unspecified 
PDB 'PDB entries for the same citation' 6G5U unspecified 
PDB 'PDB entries for the same citation' 6G6T unspecified 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Smirnov, A.'  1 ? 
'Manakova, E.' 2 ? 
'Grazulis, S.' 3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   FR 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Eur J Med Chem' 
_citation.journal_id_ASTM           EJMCA5 
_citation.journal_id_CSD            0493 
_citation.journal_id_ISSN           1768-3254 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            156 
_citation.language                  ? 
_citation.page_first                61 
_citation.page_last                 78 
_citation.title                     
'Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.' 
_citation.year                      2018 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2018.06.059 
_citation.pdbx_database_id_PubMed   30006175 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zaksauskas, A.'   1 ? 
primary 'Capkauskaite, E.' 2 ? 
primary 'Jezepcikas, L.'   3 ? 
primary 'Linkuviene, V.'   4 ? 
primary 'Kisonaite, M.'    5 ? 
primary 'Smirnov, A.'      6 ? 
primary 'Manakova, E.'     7 ? 
primary 'Grazulis, S.'     8 ? 
primary 'Matulis, D.'      9 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 12'                                                           29917.318 4    4.2.1.1 ? 
'human carbonic anhydrase XII'                                      ? 
2 non-polymer syn 'ZINC ION'                                                                        65.409    4    ?       ? 
'2-(benzylamino)-4-chloro-N-(2-hydroxyethyl)-5-sulfamoyl-benzamide' ? 
3 non-polymer syn 1,2-ETHANEDIOL                                                                    62.068    12   ?       ? Zn ? 
4 non-polymer syn '4-chloranyl-~{N}-(2-hydroxyethyl)-2-[(phenylmethyl)amino]-5-sulfamoyl-benzamide' 383.850   4    ?       ? 
1,2-ETHANEDIOL                                                      ? 
5 water       nat water                                                                             18.015    1356 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase XII,Carbonic anhydrase XII,CA-XII,Tumor antigen HOM-RCC-3.1.3' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSKWTYFGPDGENSWSKKYPSCGGLLQSPIDLHSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQG
LQSRYSATQLHLHWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFNPSYDKIFS
HLQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFRNPVQISQEQLLALETALYCTHMDDPSPR
EMINNFRQVQKFDERLVYTSFSQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSKWTYFGPDGENSWSKKYPSCGGLLQSPIDLHSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQG
LQSRYSATQLHLHWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFNPSYDKIFS
HLQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFRNPVQISQEQLLALETALYCTHMDDPSPR
EMINNFRQVQKFDERLVYTSFSQ
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                        ZN  
3 1,2-ETHANEDIOL                                                                    EDO 
4 '4-chloranyl-~{N}-(2-hydroxyethyl)-2-[(phenylmethyl)amino]-5-sulfamoyl-benzamide' EOQ 
5 water                                                                             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   LYS n 
1 4   TRP n 
1 5   THR n 
1 6   TYR n 
1 7   PHE n 
1 8   GLY n 
1 9   PRO n 
1 10  ASP n 
1 11  GLY n 
1 12  GLU n 
1 13  ASN n 
1 14  SER n 
1 15  TRP n 
1 16  SER n 
1 17  LYS n 
1 18  LYS n 
1 19  TYR n 
1 20  PRO n 
1 21  SER n 
1 22  CYS n 
1 23  GLY n 
1 24  GLY n 
1 25  LEU n 
1 26  LEU n 
1 27  GLN n 
1 28  SER n 
1 29  PRO n 
1 30  ILE n 
1 31  ASP n 
1 32  LEU n 
1 33  HIS n 
1 34  SER n 
1 35  ASP n 
1 36  ILE n 
1 37  LEU n 
1 38  GLN n 
1 39  TYR n 
1 40  ASP n 
1 41  ALA n 
1 42  SER n 
1 43  LEU n 
1 44  THR n 
1 45  PRO n 
1 46  LEU n 
1 47  GLU n 
1 48  PHE n 
1 49  GLN n 
1 50  GLY n 
1 51  TYR n 
1 52  ASN n 
1 53  LEU n 
1 54  SER n 
1 55  ALA n 
1 56  ASN n 
1 57  LYS n 
1 58  GLN n 
1 59  PHE n 
1 60  LEU n 
1 61  LEU n 
1 62  THR n 
1 63  ASN n 
1 64  ASN n 
1 65  GLY n 
1 66  HIS n 
1 67  SER n 
1 68  VAL n 
1 69  LYS n 
1 70  LEU n 
1 71  ASN n 
1 72  LEU n 
1 73  PRO n 
1 74  SER n 
1 75  ASP n 
1 76  MET n 
1 77  HIS n 
1 78  ILE n 
1 79  GLN n 
1 80  GLY n 
1 81  LEU n 
1 82  GLN n 
1 83  SER n 
1 84  ARG n 
1 85  TYR n 
1 86  SER n 
1 87  ALA n 
1 88  THR n 
1 89  GLN n 
1 90  LEU n 
1 91  HIS n 
1 92  LEU n 
1 93  HIS n 
1 94  TRP n 
1 95  GLY n 
1 96  ASN n 
1 97  PRO n 
1 98  ASN n 
1 99  ASP n 
1 100 PRO n 
1 101 HIS n 
1 102 GLY n 
1 103 SER n 
1 104 GLU n 
1 105 HIS n 
1 106 THR n 
1 107 VAL n 
1 108 SER n 
1 109 GLY n 
1 110 GLN n 
1 111 HIS n 
1 112 PHE n 
1 113 ALA n 
1 114 ALA n 
1 115 GLU n 
1 116 LEU n 
1 117 HIS n 
1 118 ILE n 
1 119 VAL n 
1 120 HIS n 
1 121 TYR n 
1 122 ASN n 
1 123 SER n 
1 124 ASP n 
1 125 LEU n 
1 126 TYR n 
1 127 PRO n 
1 128 ASP n 
1 129 ALA n 
1 130 SER n 
1 131 THR n 
1 132 ALA n 
1 133 SER n 
1 134 ASN n 
1 135 LYS n 
1 136 SER n 
1 137 GLU n 
1 138 GLY n 
1 139 LEU n 
1 140 ALA n 
1 141 VAL n 
1 142 LEU n 
1 143 ALA n 
1 144 VAL n 
1 145 LEU n 
1 146 ILE n 
1 147 GLU n 
1 148 MET n 
1 149 GLY n 
1 150 SER n 
1 151 PHE n 
1 152 ASN n 
1 153 PRO n 
1 154 SER n 
1 155 TYR n 
1 156 ASP n 
1 157 LYS n 
1 158 ILE n 
1 159 PHE n 
1 160 SER n 
1 161 HIS n 
1 162 LEU n 
1 163 GLN n 
1 164 HIS n 
1 165 VAL n 
1 166 LYS n 
1 167 TYR n 
1 168 LYS n 
1 169 GLY n 
1 170 GLN n 
1 171 GLU n 
1 172 ALA n 
1 173 PHE n 
1 174 VAL n 
1 175 PRO n 
1 176 GLY n 
1 177 PHE n 
1 178 ASN n 
1 179 ILE n 
1 180 GLU n 
1 181 GLU n 
1 182 LEU n 
1 183 LEU n 
1 184 PRO n 
1 185 GLU n 
1 186 ARG n 
1 187 THR n 
1 188 ALA n 
1 189 GLU n 
1 190 TYR n 
1 191 TYR n 
1 192 ARG n 
1 193 TYR n 
1 194 ARG n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 CYS n 
1 203 ASN n 
1 204 PRO n 
1 205 THR n 
1 206 VAL n 
1 207 LEU n 
1 208 TRP n 
1 209 THR n 
1 210 VAL n 
1 211 PHE n 
1 212 ARG n 
1 213 ASN n 
1 214 PRO n 
1 215 VAL n 
1 216 GLN n 
1 217 ILE n 
1 218 SER n 
1 219 GLN n 
1 220 GLU n 
1 221 GLN n 
1 222 LEU n 
1 223 LEU n 
1 224 ALA n 
1 225 LEU n 
1 226 GLU n 
1 227 THR n 
1 228 ALA n 
1 229 LEU n 
1 230 TYR n 
1 231 CYS n 
1 232 THR n 
1 233 HIS n 
1 234 MET n 
1 235 ASP n 
1 236 ASP n 
1 237 PRO n 
1 238 SER n 
1 239 PRO n 
1 240 ARG n 
1 241 GLU n 
1 242 MET n 
1 243 ILE n 
1 244 ASN n 
1 245 ASN n 
1 246 PHE n 
1 247 ARG n 
1 248 GLN n 
1 249 VAL n 
1 250 GLN n 
1 251 LYS n 
1 252 PHE n 
1 253 ASP n 
1 254 GLU n 
1 255 ARG n 
1 256 LEU n 
1 257 VAL n 
1 258 TYR n 
1 259 THR n 
1 260 SER n 
1 261 PHE n 
1 262 SER n 
1 263 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   263 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA12 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              Rosetta 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET21a 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                           ?                 
'C3 H7 N O2'         89.093  
ARG 'L-peptide linking' y ARGININE                                                                          ?                 
'C6 H15 N4 O2 1'     175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                        ?                 
'C4 H8 N2 O3'        132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                   ?                 
'C4 H7 N O4'         133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                          ?                 
'C3 H7 N O2 S'       121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                                                                    'ETHYLENE GLYCOL' 
'C2 H6 O2'           62.068  
EOQ non-polymer         . '4-chloranyl-~{N}-(2-hydroxyethyl)-2-[(phenylmethyl)amino]-5-sulfamoyl-benzamide' ?                 
'C16 H18 Cl N3 O4 S' 383.850 
GLN 'L-peptide linking' y GLUTAMINE                                                                         ?                 
'C5 H10 N2 O3'       146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                   ?                 
'C5 H9 N O4'         147.129 
GLY 'peptide linking'   y GLYCINE                                                                           ?                 
'C2 H5 N O2'         75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                         ?                 
'C6 H10 N3 O2 1'     156.162 
HOH non-polymer         . WATER                                                                             ?                 
'H2 O'               18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                        ?                 
'C6 H13 N O2'        131.173 
LEU 'L-peptide linking' y LEUCINE                                                                           ?                 
'C6 H13 N O2'        131.173 
LYS 'L-peptide linking' y LYSINE                                                                            ?                 
'C6 H15 N2 O2 1'     147.195 
MET 'L-peptide linking' y METHIONINE                                                                        ?                 
'C5 H11 N O2 S'      149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                                     ?                 
'C9 H11 N O2'        165.189 
PRO 'L-peptide linking' y PROLINE                                                                           ?                 
'C5 H9 N O2'         115.130 
SER 'L-peptide linking' y SERINE                                                                            ?                 
'C3 H7 N O3'         105.093 
THR 'L-peptide linking' y THREONINE                                                                         ?                 
'C4 H9 N O3'         119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                        ?                 
'C11 H12 N2 O2'      204.225 
TYR 'L-peptide linking' y TYROSINE                                                                          ?                 
'C9 H11 N O3'        181.189 
VAL 'L-peptide linking' y VALINE                                                                            ?                 
'C5 H11 N O2'        117.146 
ZN  non-polymer         . 'ZINC ION'                                                                        ?                 
'Zn 2'               65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   2   SER SER 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   2   SER SER B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   TRP 4   4   4   TRP TRP B . n 
B 1 5   THR 5   5   5   THR THR B . n 
B 1 6   TYR 6   6   6   TYR TYR B . n 
B 1 7   PHE 7   7   7   PHE PHE B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   PRO 9   9   9   PRO PRO B . n 
B 1 10  ASP 10  10  10  ASP ASP B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  GLU 12  12  12  GLU GLU B . n 
B 1 13  ASN 13  13  13  ASN ASN B . n 
B 1 14  SER 14  14  14  SER SER B . n 
B 1 15  TRP 15  15  15  TRP TRP B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  LYS 17  17  17  LYS LYS B . n 
B 1 18  LYS 18  18  18  LYS LYS B . n 
B 1 19  TYR 19  19  19  TYR TYR B . n 
B 1 20  PRO 20  20  20  PRO PRO B . n 
B 1 21  SER 21  21  21  SER SER B . n 
B 1 22  CYS 22  22  22  CYS CYS B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  GLY 24  24  24  GLY GLY B . n 
B 1 25  LEU 25  25  25  LEU LEU B . n 
B 1 26  LEU 26  26  26  LEU LEU B . n 
B 1 27  GLN 27  27  27  GLN GLN B . n 
B 1 28  SER 28  28  28  SER SER B . n 
B 1 29  PRO 29  29  29  PRO PRO B . n 
B 1 30  ILE 30  30  30  ILE ILE B . n 
B 1 31  ASP 31  31  31  ASP ASP B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  HIS 33  33  33  HIS HIS B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  ASP 35  35  35  ASP ASP B . n 
B 1 36  ILE 36  36  36  ILE ILE B . n 
B 1 37  LEU 37  37  37  LEU LEU B . n 
B 1 38  GLN 38  38  38  GLN GLN B . n 
B 1 39  TYR 39  39  39  TYR TYR B . n 
B 1 40  ASP 40  40  40  ASP ASP B . n 
B 1 41  ALA 41  41  41  ALA ALA B . n 
B 1 42  SER 42  42  42  SER SER B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  THR 44  44  44  THR THR B . n 
B 1 45  PRO 45  45  45  PRO PRO B . n 
B 1 46  LEU 46  46  46  LEU LEU B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  PHE 48  48  48  PHE PHE B . n 
B 1 49  GLN 49  49  49  GLN GLN B . n 
B 1 50  GLY 50  50  50  GLY GLY B . n 
B 1 51  TYR 51  51  51  TYR TYR B . n 
B 1 52  ASN 52  52  52  ASN ASN B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  SER 54  54  54  SER SER B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  ASN 56  56  56  ASN ASN B . n 
B 1 57  LYS 57  57  57  LYS LYS B . n 
B 1 58  GLN 58  58  58  GLN GLN B . n 
B 1 59  PHE 59  59  59  PHE PHE B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  LEU 61  61  61  LEU LEU B . n 
B 1 62  THR 62  62  62  THR THR B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  ASN 64  64  64  ASN ASN B . n 
B 1 65  GLY 65  65  65  GLY GLY B . n 
B 1 66  HIS 66  66  66  HIS HIS B . n 
B 1 67  SER 67  67  67  SER SER B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  ASN 71  71  71  ASN ASN B . n 
B 1 72  LEU 72  72  72  LEU LEU B . n 
B 1 73  PRO 73  73  73  PRO PRO B . n 
B 1 74  SER 74  74  74  SER SER B . n 
B 1 75  ASP 75  75  75  ASP ASP B . n 
B 1 76  MET 76  76  76  MET MET B . n 
B 1 77  HIS 77  77  77  HIS HIS B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  GLN 79  79  79  GLN GLN B . n 
B 1 80  GLY 80  80  80  GLY GLY B . n 
B 1 81  LEU 81  81  81  LEU LEU B . n 
B 1 82  GLN 82  82  82  GLN GLN B . n 
B 1 83  SER 83  83  83  SER SER B . n 
B 1 84  ARG 84  84  84  ARG ARG B . n 
B 1 85  TYR 85  85  85  TYR TYR B . n 
B 1 86  SER 86  86  86  SER SER B . n 
B 1 87  ALA 87  87  87  ALA ALA B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  GLN 89  89  89  GLN GLN B . n 
B 1 90  LEU 90  90  90  LEU LEU B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  LEU 92  92  92  LEU LEU B . n 
B 1 93  HIS 93  93  93  HIS HIS B . n 
B 1 94  TRP 94  94  94  TRP TRP B . n 
B 1 95  GLY 95  95  95  GLY GLY B . n 
B 1 96  ASN 96  96  96  ASN ASN B . n 
B 1 97  PRO 97  97  97  PRO PRO B . n 
B 1 98  ASN 98  98  98  ASN ASN B . n 
B 1 99  ASP 99  99  99  ASP ASP B . n 
B 1 100 PRO 100 100 100 PRO PRO B . n 
B 1 101 HIS 101 101 101 HIS HIS B . n 
B 1 102 GLY 102 102 102 GLY GLY B . n 
B 1 103 SER 103 103 103 SER SER B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 HIS 105 105 105 HIS HIS B . n 
B 1 106 THR 106 106 106 THR THR B . n 
B 1 107 VAL 107 107 107 VAL VAL B . n 
B 1 108 SER 108 108 108 SER SER B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 HIS 111 111 111 HIS HIS B . n 
B 1 112 PHE 112 112 112 PHE PHE B . n 
B 1 113 ALA 113 113 113 ALA ALA B . n 
B 1 114 ALA 114 114 114 ALA ALA B . n 
B 1 115 GLU 115 115 115 GLU GLU B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 HIS 117 117 117 HIS HIS B . n 
B 1 118 ILE 118 118 118 ILE ILE B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 HIS 120 120 120 HIS HIS B . n 
B 1 121 TYR 121 121 121 TYR TYR B . n 
B 1 122 ASN 122 122 122 ASN ASN B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 ASP 124 124 124 ASP ASP B . n 
B 1 125 LEU 125 125 125 LEU LEU B . n 
B 1 126 TYR 126 126 126 TYR TYR B . n 
B 1 127 PRO 127 127 127 PRO PRO B . n 
B 1 128 ASP 128 128 128 ASP ASP B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 SER 130 130 130 SER SER B . n 
B 1 131 THR 131 131 131 THR THR B . n 
B 1 132 ALA 132 132 132 ALA ALA B . n 
B 1 133 SER 133 133 133 SER SER B . n 
B 1 134 ASN 134 134 134 ASN ASN B . n 
B 1 135 LYS 135 135 135 LYS LYS B . n 
B 1 136 SER 136 136 136 SER SER B . n 
B 1 137 GLU 137 137 137 GLU GLU B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 LEU 139 139 139 LEU LEU B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 VAL 141 141 141 VAL VAL B . n 
B 1 142 LEU 142 142 142 LEU LEU B . n 
B 1 143 ALA 143 143 143 ALA ALA B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 LEU 145 145 145 LEU LEU B . n 
B 1 146 ILE 146 146 146 ILE ILE B . n 
B 1 147 GLU 147 147 147 GLU GLU B . n 
B 1 148 MET 148 148 148 MET MET B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 SER 150 150 150 SER SER B . n 
B 1 151 PHE 151 151 151 PHE PHE B . n 
B 1 152 ASN 152 152 152 ASN ASN B . n 
B 1 153 PRO 153 153 153 PRO PRO B . n 
B 1 154 SER 154 154 154 SER SER B . n 
B 1 155 TYR 155 155 155 TYR TYR B . n 
B 1 156 ASP 156 156 156 ASP ASP B . n 
B 1 157 LYS 157 157 157 LYS LYS B . n 
B 1 158 ILE 158 158 158 ILE ILE B . n 
B 1 159 PHE 159 159 159 PHE PHE B . n 
B 1 160 SER 160 160 160 SER SER B . n 
B 1 161 HIS 161 161 161 HIS HIS B . n 
B 1 162 LEU 162 162 162 LEU LEU B . n 
B 1 163 GLN 163 163 163 GLN GLN B . n 
B 1 164 HIS 164 164 164 HIS HIS B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 LYS 166 166 166 LYS LYS B . n 
B 1 167 TYR 167 167 167 TYR TYR B . n 
B 1 168 LYS 168 168 168 LYS LYS B . n 
B 1 169 GLY 169 169 169 GLY GLY B . n 
B 1 170 GLN 170 170 170 GLN GLN B . n 
B 1 171 GLU 171 171 171 GLU GLU B . n 
B 1 172 ALA 172 172 172 ALA ALA B . n 
B 1 173 PHE 173 173 173 PHE PHE B . n 
B 1 174 VAL 174 174 174 VAL VAL B . n 
B 1 175 PRO 175 175 175 PRO PRO B . n 
B 1 176 GLY 176 176 176 GLY GLY B . n 
B 1 177 PHE 177 177 177 PHE PHE B . n 
B 1 178 ASN 178 178 178 ASN ASN B . n 
B 1 179 ILE 179 179 179 ILE ILE B . n 
B 1 180 GLU 180 180 180 GLU GLU B . n 
B 1 181 GLU 181 181 181 GLU GLU B . n 
B 1 182 LEU 182 182 182 LEU LEU B . n 
B 1 183 LEU 183 183 183 LEU LEU B . n 
B 1 184 PRO 184 184 184 PRO PRO B . n 
B 1 185 GLU 185 185 185 GLU GLU B . n 
B 1 186 ARG 186 186 186 ARG ARG B . n 
B 1 187 THR 187 187 187 THR THR B . n 
B 1 188 ALA 188 188 188 ALA ALA B . n 
B 1 189 GLU 189 189 189 GLU GLU B . n 
B 1 190 TYR 190 190 190 TYR TYR B . n 
B 1 191 TYR 191 191 191 TYR TYR B . n 
B 1 192 ARG 192 192 192 ARG ARG B . n 
B 1 193 TYR 193 193 193 TYR TYR B . n 
B 1 194 ARG 194 194 194 ARG ARG B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 SER 196 196 196 SER SER B . n 
B 1 197 LEU 197 197 197 LEU LEU B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 PRO 200 200 200 PRO PRO B . n 
B 1 201 PRO 201 201 201 PRO PRO B . n 
B 1 202 CYS 202 202 202 CYS CYS B . n 
B 1 203 ASN 203 203 203 ASN ASN B . n 
B 1 204 PRO 204 204 204 PRO PRO B . n 
B 1 205 THR 205 205 205 THR THR B . n 
B 1 206 VAL 206 206 206 VAL VAL B . n 
B 1 207 LEU 207 207 207 LEU LEU B . n 
B 1 208 TRP 208 208 208 TRP TRP B . n 
B 1 209 THR 209 209 209 THR THR B . n 
B 1 210 VAL 210 210 210 VAL VAL B . n 
B 1 211 PHE 211 211 211 PHE PHE B . n 
B 1 212 ARG 212 212 212 ARG ARG B . n 
B 1 213 ASN 213 213 213 ASN ASN B . n 
B 1 214 PRO 214 214 214 PRO PRO B . n 
B 1 215 VAL 215 215 215 VAL VAL B . n 
B 1 216 GLN 216 216 216 GLN GLN B . n 
B 1 217 ILE 217 217 217 ILE ILE B . n 
B 1 218 SER 218 218 218 SER SER B . n 
B 1 219 GLN 219 219 219 GLN GLN B . n 
B 1 220 GLU 220 220 220 GLU GLU B . n 
B 1 221 GLN 221 221 221 GLN GLN B . n 
B 1 222 LEU 222 222 222 LEU LEU B . n 
B 1 223 LEU 223 223 223 LEU LEU B . n 
B 1 224 ALA 224 224 224 ALA ALA B . n 
B 1 225 LEU 225 225 225 LEU LEU B . n 
B 1 226 GLU 226 226 226 GLU GLU B . n 
B 1 227 THR 227 227 227 THR THR B . n 
B 1 228 ALA 228 228 228 ALA ALA B . n 
B 1 229 LEU 229 229 229 LEU LEU B . n 
B 1 230 TYR 230 230 230 TYR TYR B . n 
B 1 231 CYS 231 231 231 CYS CYS B . n 
B 1 232 THR 232 232 232 THR THR B . n 
B 1 233 HIS 233 233 233 HIS HIS B . n 
B 1 234 MET 234 234 234 MET MET B . n 
B 1 235 ASP 235 235 235 ASP ASP B . n 
B 1 236 ASP 236 236 236 ASP ASP B . n 
B 1 237 PRO 237 237 237 PRO PRO B . n 
B 1 238 SER 238 238 238 SER SER B . n 
B 1 239 PRO 239 239 239 PRO PRO B . n 
B 1 240 ARG 240 240 240 ARG ARG B . n 
B 1 241 GLU 241 241 241 GLU GLU B . n 
B 1 242 MET 242 242 242 MET MET B . n 
B 1 243 ILE 243 243 243 ILE ILE B . n 
B 1 244 ASN 244 244 244 ASN ASN B . n 
B 1 245 ASN 245 245 245 ASN ASN B . n 
B 1 246 PHE 246 246 246 PHE PHE B . n 
B 1 247 ARG 247 247 247 ARG ARG B . n 
B 1 248 GLN 248 248 248 GLN GLN B . n 
B 1 249 VAL 249 249 249 VAL VAL B . n 
B 1 250 GLN 250 250 250 GLN GLN B . n 
B 1 251 LYS 251 251 251 LYS LYS B . n 
B 1 252 PHE 252 252 252 PHE PHE B . n 
B 1 253 ASP 253 253 253 ASP ASP B . n 
B 1 254 GLU 254 254 254 GLU GLU B . n 
B 1 255 ARG 255 255 255 ARG ARG B . n 
B 1 256 LEU 256 256 256 LEU LEU B . n 
B 1 257 VAL 257 257 257 VAL VAL B . n 
B 1 258 TYR 258 258 258 TYR TYR B . n 
B 1 259 THR 259 259 259 THR THR B . n 
B 1 260 SER 260 260 260 SER SER B . n 
B 1 261 PHE 261 261 261 PHE PHE B . n 
B 1 262 SER 262 262 262 SER SER B . n 
B 1 263 GLN 263 263 263 GLN GLN B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   SER 2   2   2   SER SER C . n 
C 1 3   LYS 3   3   3   LYS LYS C . n 
C 1 4   TRP 4   4   4   TRP TRP C . n 
C 1 5   THR 5   5   5   THR THR C . n 
C 1 6   TYR 6   6   6   TYR TYR C . n 
C 1 7   PHE 7   7   7   PHE PHE C . n 
C 1 8   GLY 8   8   8   GLY GLY C . n 
C 1 9   PRO 9   9   9   PRO PRO C . n 
C 1 10  ASP 10  10  10  ASP ASP C . n 
C 1 11  GLY 11  11  11  GLY GLY C . n 
C 1 12  GLU 12  12  12  GLU GLU C . n 
C 1 13  ASN 13  13  13  ASN ASN C . n 
C 1 14  SER 14  14  14  SER SER C . n 
C 1 15  TRP 15  15  15  TRP TRP C . n 
C 1 16  SER 16  16  16  SER SER C . n 
C 1 17  LYS 17  17  17  LYS LYS C . n 
C 1 18  LYS 18  18  18  LYS LYS C . n 
C 1 19  TYR 19  19  19  TYR TYR C . n 
C 1 20  PRO 20  20  20  PRO PRO C . n 
C 1 21  SER 21  21  21  SER SER C . n 
C 1 22  CYS 22  22  22  CYS CYS C . n 
C 1 23  GLY 23  23  23  GLY GLY C . n 
C 1 24  GLY 24  24  24  GLY GLY C . n 
C 1 25  LEU 25  25  25  LEU LEU C . n 
C 1 26  LEU 26  26  26  LEU LEU C . n 
C 1 27  GLN 27  27  27  GLN GLN C . n 
C 1 28  SER 28  28  28  SER SER C . n 
C 1 29  PRO 29  29  29  PRO PRO C . n 
C 1 30  ILE 30  30  30  ILE ILE C . n 
C 1 31  ASP 31  31  31  ASP ASP C . n 
C 1 32  LEU 32  32  32  LEU LEU C . n 
C 1 33  HIS 33  33  33  HIS HIS C . n 
C 1 34  SER 34  34  34  SER SER C . n 
C 1 35  ASP 35  35  35  ASP ASP C . n 
C 1 36  ILE 36  36  36  ILE ILE C . n 
C 1 37  LEU 37  37  37  LEU LEU C . n 
C 1 38  GLN 38  38  38  GLN GLN C . n 
C 1 39  TYR 39  39  39  TYR TYR C . n 
C 1 40  ASP 40  40  40  ASP ASP C . n 
C 1 41  ALA 41  41  41  ALA ALA C . n 
C 1 42  SER 42  42  42  SER SER C . n 
C 1 43  LEU 43  43  43  LEU LEU C . n 
C 1 44  THR 44  44  44  THR THR C . n 
C 1 45  PRO 45  45  45  PRO PRO C . n 
C 1 46  LEU 46  46  46  LEU LEU C . n 
C 1 47  GLU 47  47  47  GLU GLU C . n 
C 1 48  PHE 48  48  48  PHE PHE C . n 
C 1 49  GLN 49  49  49  GLN GLN C . n 
C 1 50  GLY 50  50  50  GLY GLY C . n 
C 1 51  TYR 51  51  51  TYR TYR C . n 
C 1 52  ASN 52  52  52  ASN ASN C . n 
C 1 53  LEU 53  53  53  LEU LEU C . n 
C 1 54  SER 54  54  54  SER SER C . n 
C 1 55  ALA 55  55  55  ALA ALA C . n 
C 1 56  ASN 56  56  56  ASN ASN C . n 
C 1 57  LYS 57  57  57  LYS LYS C . n 
C 1 58  GLN 58  58  58  GLN GLN C . n 
C 1 59  PHE 59  59  59  PHE PHE C . n 
C 1 60  LEU 60  60  60  LEU LEU C . n 
C 1 61  LEU 61  61  61  LEU LEU C . n 
C 1 62  THR 62  62  62  THR THR C . n 
C 1 63  ASN 63  63  63  ASN ASN C . n 
C 1 64  ASN 64  64  64  ASN ASN C . n 
C 1 65  GLY 65  65  65  GLY GLY C . n 
C 1 66  HIS 66  66  66  HIS HIS C . n 
C 1 67  SER 67  67  67  SER SER C . n 
C 1 68  VAL 68  68  68  VAL VAL C . n 
C 1 69  LYS 69  69  69  LYS LYS C . n 
C 1 70  LEU 70  70  70  LEU LEU C . n 
C 1 71  ASN 71  71  71  ASN ASN C . n 
C 1 72  LEU 72  72  72  LEU LEU C . n 
C 1 73  PRO 73  73  73  PRO PRO C . n 
C 1 74  SER 74  74  74  SER SER C . n 
C 1 75  ASP 75  75  75  ASP ASP C . n 
C 1 76  MET 76  76  76  MET MET C . n 
C 1 77  HIS 77  77  77  HIS HIS C . n 
C 1 78  ILE 78  78  78  ILE ILE C . n 
C 1 79  GLN 79  79  79  GLN GLN C . n 
C 1 80  GLY 80  80  80  GLY GLY C . n 
C 1 81  LEU 81  81  81  LEU LEU C . n 
C 1 82  GLN 82  82  82  GLN GLN C . n 
C 1 83  SER 83  83  83  SER SER C . n 
C 1 84  ARG 84  84  84  ARG ARG C . n 
C 1 85  TYR 85  85  85  TYR TYR C . n 
C 1 86  SER 86  86  86  SER SER C . n 
C 1 87  ALA 87  87  87  ALA ALA C . n 
C 1 88  THR 88  88  88  THR THR C . n 
C 1 89  GLN 89  89  89  GLN GLN C . n 
C 1 90  LEU 90  90  90  LEU LEU C . n 
C 1 91  HIS 91  91  91  HIS HIS C . n 
C 1 92  LEU 92  92  92  LEU LEU C . n 
C 1 93  HIS 93  93  93  HIS HIS C . n 
C 1 94  TRP 94  94  94  TRP TRP C . n 
C 1 95  GLY 95  95  95  GLY GLY C . n 
C 1 96  ASN 96  96  96  ASN ASN C . n 
C 1 97  PRO 97  97  97  PRO PRO C . n 
C 1 98  ASN 98  98  98  ASN ASN C . n 
C 1 99  ASP 99  99  99  ASP ASP C . n 
C 1 100 PRO 100 100 100 PRO PRO C . n 
C 1 101 HIS 101 101 101 HIS HIS C . n 
C 1 102 GLY 102 102 102 GLY GLY C . n 
C 1 103 SER 103 103 103 SER SER C . n 
C 1 104 GLU 104 104 104 GLU GLU C . n 
C 1 105 HIS 105 105 105 HIS HIS C . n 
C 1 106 THR 106 106 106 THR THR C . n 
C 1 107 VAL 107 107 107 VAL VAL C . n 
C 1 108 SER 108 108 108 SER SER C . n 
C 1 109 GLY 109 109 109 GLY GLY C . n 
C 1 110 GLN 110 110 110 GLN GLN C . n 
C 1 111 HIS 111 111 111 HIS HIS C . n 
C 1 112 PHE 112 112 112 PHE PHE C . n 
C 1 113 ALA 113 113 113 ALA ALA C . n 
C 1 114 ALA 114 114 114 ALA ALA C . n 
C 1 115 GLU 115 115 115 GLU GLU C . n 
C 1 116 LEU 116 116 116 LEU LEU C . n 
C 1 117 HIS 117 117 117 HIS HIS C . n 
C 1 118 ILE 118 118 118 ILE ILE C . n 
C 1 119 VAL 119 119 119 VAL VAL C . n 
C 1 120 HIS 120 120 120 HIS HIS C . n 
C 1 121 TYR 121 121 121 TYR TYR C . n 
C 1 122 ASN 122 122 122 ASN ASN C . n 
C 1 123 SER 123 123 123 SER SER C . n 
C 1 124 ASP 124 124 124 ASP ASP C . n 
C 1 125 LEU 125 125 125 LEU LEU C . n 
C 1 126 TYR 126 126 126 TYR TYR C . n 
C 1 127 PRO 127 127 127 PRO PRO C . n 
C 1 128 ASP 128 128 128 ASP ASP C . n 
C 1 129 ALA 129 129 129 ALA ALA C . n 
C 1 130 SER 130 130 130 SER SER C . n 
C 1 131 THR 131 131 131 THR THR C . n 
C 1 132 ALA 132 132 132 ALA ALA C . n 
C 1 133 SER 133 133 133 SER SER C . n 
C 1 134 ASN 134 134 134 ASN ASN C . n 
C 1 135 LYS 135 135 135 LYS LYS C . n 
C 1 136 SER 136 136 136 SER SER C . n 
C 1 137 GLU 137 137 137 GLU GLU C . n 
C 1 138 GLY 138 138 138 GLY GLY C . n 
C 1 139 LEU 139 139 139 LEU LEU C . n 
C 1 140 ALA 140 140 140 ALA ALA C . n 
C 1 141 VAL 141 141 141 VAL VAL C . n 
C 1 142 LEU 142 142 142 LEU LEU C . n 
C 1 143 ALA 143 143 143 ALA ALA C . n 
C 1 144 VAL 144 144 144 VAL VAL C . n 
C 1 145 LEU 145 145 145 LEU LEU C . n 
C 1 146 ILE 146 146 146 ILE ILE C . n 
C 1 147 GLU 147 147 147 GLU GLU C . n 
C 1 148 MET 148 148 148 MET MET C . n 
C 1 149 GLY 149 149 149 GLY GLY C . n 
C 1 150 SER 150 150 150 SER SER C . n 
C 1 151 PHE 151 151 151 PHE PHE C . n 
C 1 152 ASN 152 152 152 ASN ASN C . n 
C 1 153 PRO 153 153 153 PRO PRO C . n 
C 1 154 SER 154 154 154 SER SER C . n 
C 1 155 TYR 155 155 155 TYR TYR C . n 
C 1 156 ASP 156 156 156 ASP ASP C . n 
C 1 157 LYS 157 157 157 LYS LYS C . n 
C 1 158 ILE 158 158 158 ILE ILE C . n 
C 1 159 PHE 159 159 159 PHE PHE C . n 
C 1 160 SER 160 160 160 SER SER C . n 
C 1 161 HIS 161 161 161 HIS HIS C . n 
C 1 162 LEU 162 162 162 LEU LEU C . n 
C 1 163 GLN 163 163 163 GLN GLN C . n 
C 1 164 HIS 164 164 164 HIS HIS C . n 
C 1 165 VAL 165 165 165 VAL VAL C . n 
C 1 166 LYS 166 166 166 LYS LYS C . n 
C 1 167 TYR 167 167 167 TYR TYR C . n 
C 1 168 LYS 168 168 168 LYS LYS C . n 
C 1 169 GLY 169 169 169 GLY GLY C . n 
C 1 170 GLN 170 170 170 GLN GLN C . n 
C 1 171 GLU 171 171 171 GLU GLU C . n 
C 1 172 ALA 172 172 172 ALA ALA C . n 
C 1 173 PHE 173 173 173 PHE PHE C . n 
C 1 174 VAL 174 174 174 VAL VAL C . n 
C 1 175 PRO 175 175 175 PRO PRO C . n 
C 1 176 GLY 176 176 176 GLY GLY C . n 
C 1 177 PHE 177 177 177 PHE PHE C . n 
C 1 178 ASN 178 178 178 ASN ASN C . n 
C 1 179 ILE 179 179 179 ILE ILE C . n 
C 1 180 GLU 180 180 180 GLU GLU C . n 
C 1 181 GLU 181 181 181 GLU GLU C . n 
C 1 182 LEU 182 182 182 LEU LEU C . n 
C 1 183 LEU 183 183 183 LEU LEU C . n 
C 1 184 PRO 184 184 184 PRO PRO C . n 
C 1 185 GLU 185 185 185 GLU GLU C . n 
C 1 186 ARG 186 186 186 ARG ARG C . n 
C 1 187 THR 187 187 187 THR THR C . n 
C 1 188 ALA 188 188 188 ALA ALA C . n 
C 1 189 GLU 189 189 189 GLU GLU C . n 
C 1 190 TYR 190 190 190 TYR TYR C . n 
C 1 191 TYR 191 191 191 TYR TYR C . n 
C 1 192 ARG 192 192 192 ARG ARG C . n 
C 1 193 TYR 193 193 193 TYR TYR C . n 
C 1 194 ARG 194 194 194 ARG ARG C . n 
C 1 195 GLY 195 195 195 GLY GLY C . n 
C 1 196 SER 196 196 196 SER SER C . n 
C 1 197 LEU 197 197 197 LEU LEU C . n 
C 1 198 THR 198 198 198 THR THR C . n 
C 1 199 THR 199 199 199 THR THR C . n 
C 1 200 PRO 200 200 200 PRO PRO C . n 
C 1 201 PRO 201 201 201 PRO PRO C . n 
C 1 202 CYS 202 202 202 CYS CYS C . n 
C 1 203 ASN 203 203 203 ASN ASN C . n 
C 1 204 PRO 204 204 204 PRO PRO C . n 
C 1 205 THR 205 205 205 THR THR C . n 
C 1 206 VAL 206 206 206 VAL VAL C . n 
C 1 207 LEU 207 207 207 LEU LEU C . n 
C 1 208 TRP 208 208 208 TRP TRP C . n 
C 1 209 THR 209 209 209 THR THR C . n 
C 1 210 VAL 210 210 210 VAL VAL C . n 
C 1 211 PHE 211 211 211 PHE PHE C . n 
C 1 212 ARG 212 212 212 ARG ARG C . n 
C 1 213 ASN 213 213 213 ASN ASN C . n 
C 1 214 PRO 214 214 214 PRO PRO C . n 
C 1 215 VAL 215 215 215 VAL VAL C . n 
C 1 216 GLN 216 216 216 GLN GLN C . n 
C 1 217 ILE 217 217 217 ILE ILE C . n 
C 1 218 SER 218 218 218 SER SER C . n 
C 1 219 GLN 219 219 219 GLN GLN C . n 
C 1 220 GLU 220 220 220 GLU GLU C . n 
C 1 221 GLN 221 221 221 GLN GLN C . n 
C 1 222 LEU 222 222 222 LEU LEU C . n 
C 1 223 LEU 223 223 223 LEU LEU C . n 
C 1 224 ALA 224 224 224 ALA ALA C . n 
C 1 225 LEU 225 225 225 LEU LEU C . n 
C 1 226 GLU 226 226 226 GLU GLU C . n 
C 1 227 THR 227 227 227 THR THR C . n 
C 1 228 ALA 228 228 228 ALA ALA C . n 
C 1 229 LEU 229 229 229 LEU LEU C . n 
C 1 230 TYR 230 230 230 TYR TYR C . n 
C 1 231 CYS 231 231 231 CYS CYS C . n 
C 1 232 THR 232 232 232 THR THR C . n 
C 1 233 HIS 233 233 233 HIS HIS C . n 
C 1 234 MET 234 234 234 MET MET C . n 
C 1 235 ASP 235 235 235 ASP ASP C . n 
C 1 236 ASP 236 236 236 ASP ASP C . n 
C 1 237 PRO 237 237 237 PRO PRO C . n 
C 1 238 SER 238 238 238 SER SER C . n 
C 1 239 PRO 239 239 239 PRO PRO C . n 
C 1 240 ARG 240 240 240 ARG ARG C . n 
C 1 241 GLU 241 241 241 GLU GLU C . n 
C 1 242 MET 242 242 242 MET MET C . n 
C 1 243 ILE 243 243 243 ILE ILE C . n 
C 1 244 ASN 244 244 244 ASN ASN C . n 
C 1 245 ASN 245 245 245 ASN ASN C . n 
C 1 246 PHE 246 246 246 PHE PHE C . n 
C 1 247 ARG 247 247 247 ARG ARG C . n 
C 1 248 GLN 248 248 248 GLN GLN C . n 
C 1 249 VAL 249 249 249 VAL VAL C . n 
C 1 250 GLN 250 250 250 GLN GLN C . n 
C 1 251 LYS 251 251 251 LYS LYS C . n 
C 1 252 PHE 252 252 252 PHE PHE C . n 
C 1 253 ASP 253 253 253 ASP ASP C . n 
C 1 254 GLU 254 254 254 GLU GLU C . n 
C 1 255 ARG 255 255 255 ARG ARG C . n 
C 1 256 LEU 256 256 256 LEU LEU C . n 
C 1 257 VAL 257 257 257 VAL VAL C . n 
C 1 258 TYR 258 258 258 TYR TYR C . n 
C 1 259 THR 259 259 259 THR THR C . n 
C 1 260 SER 260 260 260 SER SER C . n 
C 1 261 PHE 261 261 261 PHE PHE C . n 
C 1 262 SER 262 262 262 SER SER C . n 
C 1 263 GLN 263 263 263 GLN GLN C . n 
D 1 1   MET 1   1   ?   ?   ?   D . n 
D 1 2   SER 2   2   ?   ?   ?   D . n 
D 1 3   LYS 3   3   3   LYS LYS D . n 
D 1 4   TRP 4   4   4   TRP TRP D . n 
D 1 5   THR 5   5   5   THR THR D . n 
D 1 6   TYR 6   6   6   TYR TYR D . n 
D 1 7   PHE 7   7   7   PHE PHE D . n 
D 1 8   GLY 8   8   8   GLY GLY D . n 
D 1 9   PRO 9   9   9   PRO PRO D . n 
D 1 10  ASP 10  10  10  ASP ASP D . n 
D 1 11  GLY 11  11  11  GLY GLY D . n 
D 1 12  GLU 12  12  12  GLU GLU D . n 
D 1 13  ASN 13  13  13  ASN ASN D . n 
D 1 14  SER 14  14  14  SER SER D . n 
D 1 15  TRP 15  15  15  TRP TRP D . n 
D 1 16  SER 16  16  16  SER SER D . n 
D 1 17  LYS 17  17  17  LYS LYS D . n 
D 1 18  LYS 18  18  18  LYS LYS D . n 
D 1 19  TYR 19  19  19  TYR TYR D . n 
D 1 20  PRO 20  20  20  PRO PRO D . n 
D 1 21  SER 21  21  21  SER SER D . n 
D 1 22  CYS 22  22  22  CYS CYS D . n 
D 1 23  GLY 23  23  23  GLY GLY D . n 
D 1 24  GLY 24  24  24  GLY GLY D . n 
D 1 25  LEU 25  25  25  LEU LEU D . n 
D 1 26  LEU 26  26  26  LEU LEU D . n 
D 1 27  GLN 27  27  27  GLN GLN D . n 
D 1 28  SER 28  28  28  SER SER D . n 
D 1 29  PRO 29  29  29  PRO PRO D . n 
D 1 30  ILE 30  30  30  ILE ILE D . n 
D 1 31  ASP 31  31  31  ASP ASP D . n 
D 1 32  LEU 32  32  32  LEU LEU D . n 
D 1 33  HIS 33  33  33  HIS HIS D . n 
D 1 34  SER 34  34  34  SER SER D . n 
D 1 35  ASP 35  35  35  ASP ASP D . n 
D 1 36  ILE 36  36  36  ILE ILE D . n 
D 1 37  LEU 37  37  37  LEU LEU D . n 
D 1 38  GLN 38  38  38  GLN GLN D . n 
D 1 39  TYR 39  39  39  TYR TYR D . n 
D 1 40  ASP 40  40  40  ASP ASP D . n 
D 1 41  ALA 41  41  41  ALA ALA D . n 
D 1 42  SER 42  42  42  SER SER D . n 
D 1 43  LEU 43  43  43  LEU LEU D . n 
D 1 44  THR 44  44  44  THR THR D . n 
D 1 45  PRO 45  45  45  PRO PRO D . n 
D 1 46  LEU 46  46  46  LEU LEU D . n 
D 1 47  GLU 47  47  47  GLU GLU D . n 
D 1 48  PHE 48  48  48  PHE PHE D . n 
D 1 49  GLN 49  49  49  GLN GLN D . n 
D 1 50  GLY 50  50  50  GLY GLY D . n 
D 1 51  TYR 51  51  51  TYR TYR D . n 
D 1 52  ASN 52  52  52  ASN ASN D . n 
D 1 53  LEU 53  53  53  LEU LEU D . n 
D 1 54  SER 54  54  54  SER SER D . n 
D 1 55  ALA 55  55  55  ALA ALA D . n 
D 1 56  ASN 56  56  56  ASN ASN D . n 
D 1 57  LYS 57  57  57  LYS LYS D . n 
D 1 58  GLN 58  58  58  GLN GLN D . n 
D 1 59  PHE 59  59  59  PHE PHE D . n 
D 1 60  LEU 60  60  60  LEU LEU D . n 
D 1 61  LEU 61  61  61  LEU LEU D . n 
D 1 62  THR 62  62  62  THR THR D . n 
D 1 63  ASN 63  63  63  ASN ASN D . n 
D 1 64  ASN 64  64  64  ASN ASN D . n 
D 1 65  GLY 65  65  65  GLY GLY D . n 
D 1 66  HIS 66  66  66  HIS HIS D . n 
D 1 67  SER 67  67  67  SER SER D . n 
D 1 68  VAL 68  68  68  VAL VAL D . n 
D 1 69  LYS 69  69  69  LYS LYS D . n 
D 1 70  LEU 70  70  70  LEU LEU D . n 
D 1 71  ASN 71  71  71  ASN ASN D . n 
D 1 72  LEU 72  72  72  LEU LEU D . n 
D 1 73  PRO 73  73  73  PRO PRO D . n 
D 1 74  SER 74  74  74  SER SER D . n 
D 1 75  ASP 75  75  75  ASP ASP D . n 
D 1 76  MET 76  76  76  MET MET D . n 
D 1 77  HIS 77  77  77  HIS HIS D . n 
D 1 78  ILE 78  78  78  ILE ILE D . n 
D 1 79  GLN 79  79  79  GLN GLN D . n 
D 1 80  GLY 80  80  80  GLY GLY D . n 
D 1 81  LEU 81  81  81  LEU LEU D . n 
D 1 82  GLN 82  82  82  GLN GLN D . n 
D 1 83  SER 83  83  83  SER SER D . n 
D 1 84  ARG 84  84  84  ARG ARG D . n 
D 1 85  TYR 85  85  85  TYR TYR D . n 
D 1 86  SER 86  86  86  SER SER D . n 
D 1 87  ALA 87  87  87  ALA ALA D . n 
D 1 88  THR 88  88  88  THR THR D . n 
D 1 89  GLN 89  89  89  GLN GLN D . n 
D 1 90  LEU 90  90  90  LEU LEU D . n 
D 1 91  HIS 91  91  91  HIS HIS D . n 
D 1 92  LEU 92  92  92  LEU LEU D . n 
D 1 93  HIS 93  93  93  HIS HIS D . n 
D 1 94  TRP 94  94  94  TRP TRP D . n 
D 1 95  GLY 95  95  95  GLY GLY D . n 
D 1 96  ASN 96  96  96  ASN ASN D . n 
D 1 97  PRO 97  97  97  PRO PRO D . n 
D 1 98  ASN 98  98  98  ASN ASN D . n 
D 1 99  ASP 99  99  99  ASP ASP D . n 
D 1 100 PRO 100 100 100 PRO PRO D . n 
D 1 101 HIS 101 101 101 HIS HIS D . n 
D 1 102 GLY 102 102 102 GLY GLY D . n 
D 1 103 SER 103 103 103 SER SER D . n 
D 1 104 GLU 104 104 104 GLU GLU D . n 
D 1 105 HIS 105 105 105 HIS HIS D . n 
D 1 106 THR 106 106 106 THR THR D . n 
D 1 107 VAL 107 107 107 VAL VAL D . n 
D 1 108 SER 108 108 108 SER SER D . n 
D 1 109 GLY 109 109 109 GLY GLY D . n 
D 1 110 GLN 110 110 110 GLN GLN D . n 
D 1 111 HIS 111 111 111 HIS HIS D . n 
D 1 112 PHE 112 112 112 PHE PHE D . n 
D 1 113 ALA 113 113 113 ALA ALA D . n 
D 1 114 ALA 114 114 114 ALA ALA D . n 
D 1 115 GLU 115 115 115 GLU GLU D . n 
D 1 116 LEU 116 116 116 LEU LEU D . n 
D 1 117 HIS 117 117 117 HIS HIS D . n 
D 1 118 ILE 118 118 118 ILE ILE D . n 
D 1 119 VAL 119 119 119 VAL VAL D . n 
D 1 120 HIS 120 120 120 HIS HIS D . n 
D 1 121 TYR 121 121 121 TYR TYR D . n 
D 1 122 ASN 122 122 122 ASN ASN D . n 
D 1 123 SER 123 123 123 SER SER D . n 
D 1 124 ASP 124 124 124 ASP ASP D . n 
D 1 125 LEU 125 125 125 LEU LEU D . n 
D 1 126 TYR 126 126 126 TYR TYR D . n 
D 1 127 PRO 127 127 127 PRO PRO D . n 
D 1 128 ASP 128 128 128 ASP ASP D . n 
D 1 129 ALA 129 129 129 ALA ALA D . n 
D 1 130 SER 130 130 130 SER SER D . n 
D 1 131 THR 131 131 131 THR THR D . n 
D 1 132 ALA 132 132 132 ALA ALA D . n 
D 1 133 SER 133 133 133 SER SER D . n 
D 1 134 ASN 134 134 134 ASN ASN D . n 
D 1 135 LYS 135 135 135 LYS LYS D . n 
D 1 136 SER 136 136 136 SER SER D . n 
D 1 137 GLU 137 137 137 GLU GLU D . n 
D 1 138 GLY 138 138 138 GLY GLY D . n 
D 1 139 LEU 139 139 139 LEU LEU D . n 
D 1 140 ALA 140 140 140 ALA ALA D . n 
D 1 141 VAL 141 141 141 VAL VAL D . n 
D 1 142 LEU 142 142 142 LEU LEU D . n 
D 1 143 ALA 143 143 143 ALA ALA D . n 
D 1 144 VAL 144 144 144 VAL VAL D . n 
D 1 145 LEU 145 145 145 LEU LEU D . n 
D 1 146 ILE 146 146 146 ILE ILE D . n 
D 1 147 GLU 147 147 147 GLU GLU D . n 
D 1 148 MET 148 148 148 MET MET D . n 
D 1 149 GLY 149 149 149 GLY GLY D . n 
D 1 150 SER 150 150 150 SER SER D . n 
D 1 151 PHE 151 151 151 PHE PHE D . n 
D 1 152 ASN 152 152 152 ASN ASN D . n 
D 1 153 PRO 153 153 153 PRO PRO D . n 
D 1 154 SER 154 154 154 SER SER D . n 
D 1 155 TYR 155 155 155 TYR TYR D . n 
D 1 156 ASP 156 156 156 ASP ASP D . n 
D 1 157 LYS 157 157 157 LYS LYS D . n 
D 1 158 ILE 158 158 158 ILE ILE D . n 
D 1 159 PHE 159 159 159 PHE PHE D . n 
D 1 160 SER 160 160 160 SER SER D . n 
D 1 161 HIS 161 161 161 HIS HIS D . n 
D 1 162 LEU 162 162 162 LEU LEU D . n 
D 1 163 GLN 163 163 163 GLN GLN D . n 
D 1 164 HIS 164 164 164 HIS HIS D . n 
D 1 165 VAL 165 165 165 VAL VAL D . n 
D 1 166 LYS 166 166 166 LYS LYS D . n 
D 1 167 TYR 167 167 167 TYR TYR D . n 
D 1 168 LYS 168 168 168 LYS LYS D . n 
D 1 169 GLY 169 169 169 GLY GLY D . n 
D 1 170 GLN 170 170 170 GLN GLN D . n 
D 1 171 GLU 171 171 171 GLU GLU D . n 
D 1 172 ALA 172 172 172 ALA ALA D . n 
D 1 173 PHE 173 173 173 PHE PHE D . n 
D 1 174 VAL 174 174 174 VAL VAL D . n 
D 1 175 PRO 175 175 175 PRO PRO D . n 
D 1 176 GLY 176 176 176 GLY GLY D . n 
D 1 177 PHE 177 177 177 PHE PHE D . n 
D 1 178 ASN 178 178 178 ASN ASN D . n 
D 1 179 ILE 179 179 179 ILE ILE D . n 
D 1 180 GLU 180 180 180 GLU GLU D . n 
D 1 181 GLU 181 181 181 GLU GLU D . n 
D 1 182 LEU 182 182 182 LEU LEU D . n 
D 1 183 LEU 183 183 183 LEU LEU D . n 
D 1 184 PRO 184 184 184 PRO PRO D . n 
D 1 185 GLU 185 185 185 GLU GLU D . n 
D 1 186 ARG 186 186 186 ARG ARG D . n 
D 1 187 THR 187 187 187 THR THR D . n 
D 1 188 ALA 188 188 188 ALA ALA D . n 
D 1 189 GLU 189 189 189 GLU GLU D . n 
D 1 190 TYR 190 190 190 TYR TYR D . n 
D 1 191 TYR 191 191 191 TYR TYR D . n 
D 1 192 ARG 192 192 192 ARG ARG D . n 
D 1 193 TYR 193 193 193 TYR TYR D . n 
D 1 194 ARG 194 194 194 ARG ARG D . n 
D 1 195 GLY 195 195 195 GLY GLY D . n 
D 1 196 SER 196 196 196 SER SER D . n 
D 1 197 LEU 197 197 197 LEU LEU D . n 
D 1 198 THR 198 198 198 THR THR D . n 
D 1 199 THR 199 199 199 THR THR D . n 
D 1 200 PRO 200 200 200 PRO PRO D . n 
D 1 201 PRO 201 201 201 PRO PRO D . n 
D 1 202 CYS 202 202 202 CYS CYS D . n 
D 1 203 ASN 203 203 203 ASN ASN D . n 
D 1 204 PRO 204 204 204 PRO PRO D . n 
D 1 205 THR 205 205 205 THR THR D . n 
D 1 206 VAL 206 206 206 VAL VAL D . n 
D 1 207 LEU 207 207 207 LEU LEU D . n 
D 1 208 TRP 208 208 208 TRP TRP D . n 
D 1 209 THR 209 209 209 THR THR D . n 
D 1 210 VAL 210 210 210 VAL VAL D . n 
D 1 211 PHE 211 211 211 PHE PHE D . n 
D 1 212 ARG 212 212 212 ARG ARG D . n 
D 1 213 ASN 213 213 213 ASN ASN D . n 
D 1 214 PRO 214 214 214 PRO PRO D . n 
D 1 215 VAL 215 215 215 VAL VAL D . n 
D 1 216 GLN 216 216 216 GLN GLN D . n 
D 1 217 ILE 217 217 217 ILE ILE D . n 
D 1 218 SER 218 218 218 SER SER D . n 
D 1 219 GLN 219 219 219 GLN GLN D . n 
D 1 220 GLU 220 220 220 GLU GLU D . n 
D 1 221 GLN 221 221 221 GLN GLN D . n 
D 1 222 LEU 222 222 222 LEU LEU D . n 
D 1 223 LEU 223 223 223 LEU LEU D . n 
D 1 224 ALA 224 224 224 ALA ALA D . n 
D 1 225 LEU 225 225 225 LEU LEU D . n 
D 1 226 GLU 226 226 226 GLU GLU D . n 
D 1 227 THR 227 227 227 THR THR D . n 
D 1 228 ALA 228 228 228 ALA ALA D . n 
D 1 229 LEU 229 229 229 LEU LEU D . n 
D 1 230 TYR 230 230 230 TYR TYR D . n 
D 1 231 CYS 231 231 231 CYS CYS D . n 
D 1 232 THR 232 232 232 THR THR D . n 
D 1 233 HIS 233 233 233 HIS HIS D . n 
D 1 234 MET 234 234 234 MET MET D . n 
D 1 235 ASP 235 235 235 ASP ASP D . n 
D 1 236 ASP 236 236 236 ASP ASP D . n 
D 1 237 PRO 237 237 237 PRO PRO D . n 
D 1 238 SER 238 238 238 SER SER D . n 
D 1 239 PRO 239 239 239 PRO PRO D . n 
D 1 240 ARG 240 240 240 ARG ARG D . n 
D 1 241 GLU 241 241 241 GLU GLU D . n 
D 1 242 MET 242 242 242 MET MET D . n 
D 1 243 ILE 243 243 243 ILE ILE D . n 
D 1 244 ASN 244 244 244 ASN ASN D . n 
D 1 245 ASN 245 245 245 ASN ASN D . n 
D 1 246 PHE 246 246 246 PHE PHE D . n 
D 1 247 ARG 247 247 247 ARG ARG D . n 
D 1 248 GLN 248 248 248 GLN GLN D . n 
D 1 249 VAL 249 249 249 VAL VAL D . n 
D 1 250 GLN 250 250 250 GLN GLN D . n 
D 1 251 LYS 251 251 251 LYS LYS D . n 
D 1 252 PHE 252 252 252 PHE PHE D . n 
D 1 253 ASP 253 253 253 ASP ASP D . n 
D 1 254 GLU 254 254 254 GLU GLU D . n 
D 1 255 ARG 255 255 255 ARG ARG D . n 
D 1 256 LEU 256 256 256 LEU LEU D . n 
D 1 257 VAL 257 257 257 VAL VAL D . n 
D 1 258 TYR 258 258 258 TYR TYR D . n 
D 1 259 THR 259 259 259 THR THR D . n 
D 1 260 SER 260 260 260 SER SER D . n 
D 1 261 PHE 261 261 261 PHE PHE D . n 
D 1 262 SER 262 262 262 SER SER D . n 
D 1 263 GLN 263 263 263 GLN GLN D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E  2 ZN  1   301 1    ZN  ZN  A . 
F  3 EDO 1   302 3    EDO EDO A . 
G  4 EOQ 1   303 1    EOQ EA7 A . 
H  2 ZN  1   301 2    ZN  ZN  B . 
I  3 EDO 1   302 1    EDO EDO B . 
J  3 EDO 1   303 2    EDO EDO B . 
K  3 EDO 1   304 5    EDO EDO B . 
L  4 EOQ 1   305 2    EOQ EA7 B . 
M  2 ZN  1   301 3    ZN  ZN  C . 
N  3 EDO 1   302 4    EDO EDO C . 
O  3 EDO 1   303 7    EDO EDO C . 
P  3 EDO 1   304 8    EDO EDO C . 
Q  4 EOQ 1   305 3    EOQ EA7 C . 
R  2 ZN  1   301 4    ZN  ZN  D . 
S  3 EDO 1   302 6    EDO EDO D . 
T  3 EDO 1   303 9    EDO EDO D . 
U  3 EDO 1   304 10   EDO EDO D . 
V  3 EDO 1   305 11   EDO EDO D . 
W  3 EDO 1   306 12   EDO EDO D . 
X  4 EOQ 1   307 4    EOQ EA7 D . 
Y  5 HOH 1   401 639  HOH HOH A . 
Y  5 HOH 2   402 593  HOH HOH A . 
Y  5 HOH 3   403 1050 HOH HOH A . 
Y  5 HOH 4   404 1014 HOH HOH A . 
Y  5 HOH 5   405 961  HOH HOH A . 
Y  5 HOH 6   406 1090 HOH HOH A . 
Y  5 HOH 7   407 553  HOH HOH A . 
Y  5 HOH 8   408 566  HOH HOH A . 
Y  5 HOH 9   409 1035 HOH HOH A . 
Y  5 HOH 10  410 243  HOH HOH A . 
Y  5 HOH 11  411 1269 HOH HOH A . 
Y  5 HOH 12  412 1054 HOH HOH A . 
Y  5 HOH 13  413 1282 HOH HOH A . 
Y  5 HOH 14  414 781  HOH HOH A . 
Y  5 HOH 15  415 840  HOH HOH A . 
Y  5 HOH 16  416 171  HOH HOH A . 
Y  5 HOH 17  417 473  HOH HOH A . 
Y  5 HOH 18  418 1038 HOH HOH A . 
Y  5 HOH 19  419 186  HOH HOH A . 
Y  5 HOH 20  420 1076 HOH HOH A . 
Y  5 HOH 21  421 11   HOH HOH A . 
Y  5 HOH 22  422 1049 HOH HOH A . 
Y  5 HOH 23  423 1034 HOH HOH A . 
Y  5 HOH 24  424 1270 HOH HOH A . 
Y  5 HOH 25  425 699  HOH HOH A . 
Y  5 HOH 26  426 1255 HOH HOH A . 
Y  5 HOH 27  427 897  HOH HOH A . 
Y  5 HOH 28  428 585  HOH HOH A . 
Y  5 HOH 29  429 1099 HOH HOH A . 
Y  5 HOH 30  430 1057 HOH HOH A . 
Y  5 HOH 31  431 287  HOH HOH A . 
Y  5 HOH 32  432 1055 HOH HOH A . 
Y  5 HOH 33  433 614  HOH HOH A . 
Y  5 HOH 34  434 33   HOH HOH A . 
Y  5 HOH 35  435 1268 HOH HOH A . 
Y  5 HOH 36  436 431  HOH HOH A . 
Y  5 HOH 37  437 269  HOH HOH A . 
Y  5 HOH 38  438 1265 HOH HOH A . 
Y  5 HOH 39  439 475  HOH HOH A . 
Y  5 HOH 40  440 104  HOH HOH A . 
Y  5 HOH 41  441 198  HOH HOH A . 
Y  5 HOH 42  442 732  HOH HOH A . 
Y  5 HOH 43  443 819  HOH HOH A . 
Y  5 HOH 44  444 547  HOH HOH A . 
Y  5 HOH 45  445 257  HOH HOH A . 
Y  5 HOH 46  446 625  HOH HOH A . 
Y  5 HOH 47  447 290  HOH HOH A . 
Y  5 HOH 48  448 698  HOH HOH A . 
Y  5 HOH 49  449 371  HOH HOH A . 
Y  5 HOH 50  450 982  HOH HOH A . 
Y  5 HOH 51  451 1030 HOH HOH A . 
Y  5 HOH 52  452 204  HOH HOH A . 
Y  5 HOH 53  453 137  HOH HOH A . 
Y  5 HOH 54  454 135  HOH HOH A . 
Y  5 HOH 55  455 629  HOH HOH A . 
Y  5 HOH 56  456 1083 HOH HOH A . 
Y  5 HOH 57  457 88   HOH HOH A . 
Y  5 HOH 58  458 478  HOH HOH A . 
Y  5 HOH 59  459 69   HOH HOH A . 
Y  5 HOH 60  460 477  HOH HOH A . 
Y  5 HOH 61  461 1040 HOH HOH A . 
Y  5 HOH 62  462 127  HOH HOH A . 
Y  5 HOH 63  463 316  HOH HOH A . 
Y  5 HOH 64  464 315  HOH HOH A . 
Y  5 HOH 65  465 771  HOH HOH A . 
Y  5 HOH 66  466 284  HOH HOH A . 
Y  5 HOH 67  467 319  HOH HOH A . 
Y  5 HOH 68  468 838  HOH HOH A . 
Y  5 HOH 69  469 839  HOH HOH A . 
Y  5 HOH 70  470 1042 HOH HOH A . 
Y  5 HOH 71  471 670  HOH HOH A . 
Y  5 HOH 72  472 880  HOH HOH A . 
Y  5 HOH 73  473 332  HOH HOH A . 
Y  5 HOH 74  474 112  HOH HOH A . 
Y  5 HOH 75  475 397  HOH HOH A . 
Y  5 HOH 76  476 15   HOH HOH A . 
Y  5 HOH 77  477 18   HOH HOH A . 
Y  5 HOH 78  478 884  HOH HOH A . 
Y  5 HOH 79  479 22   HOH HOH A . 
Y  5 HOH 80  480 151  HOH HOH A . 
Y  5 HOH 81  481 572  HOH HOH A . 
Y  5 HOH 82  482 166  HOH HOH A . 
Y  5 HOH 83  483 32   HOH HOH A . 
Y  5 HOH 84  484 864  HOH HOH A . 
Y  5 HOH 85  485 583  HOH HOH A . 
Y  5 HOH 86  486 132  HOH HOH A . 
Y  5 HOH 87  487 497  HOH HOH A . 
Y  5 HOH 88  488 16   HOH HOH A . 
Y  5 HOH 89  489 116  HOH HOH A . 
Y  5 HOH 90  490 1061 HOH HOH A . 
Y  5 HOH 91  491 524  HOH HOH A . 
Y  5 HOH 92  492 843  HOH HOH A . 
Y  5 HOH 93  493 106  HOH HOH A . 
Y  5 HOH 94  494 334  HOH HOH A . 
Y  5 HOH 95  495 930  HOH HOH A . 
Y  5 HOH 96  496 458  HOH HOH A . 
Y  5 HOH 97  497 595  HOH HOH A . 
Y  5 HOH 98  498 301  HOH HOH A . 
Y  5 HOH 99  499 541  HOH HOH A . 
Y  5 HOH 100 500 271  HOH HOH A . 
Y  5 HOH 101 501 932  HOH HOH A . 
Y  5 HOH 102 502 1088 HOH HOH A . 
Y  5 HOH 103 503 952  HOH HOH A . 
Y  5 HOH 104 504 928  HOH HOH A . 
Y  5 HOH 105 505 1281 HOH HOH A . 
Y  5 HOH 106 506 101  HOH HOH A . 
Y  5 HOH 107 507 1089 HOH HOH A . 
Y  5 HOH 108 508 97   HOH HOH A . 
Y  5 HOH 109 509 31   HOH HOH A . 
Y  5 HOH 110 510 1044 HOH HOH A . 
Y  5 HOH 111 511 267  HOH HOH A . 
Y  5 HOH 112 512 189  HOH HOH A . 
Y  5 HOH 113 513 600  HOH HOH A . 
Y  5 HOH 114 514 831  HOH HOH A . 
Y  5 HOH 115 515 1267 HOH HOH A . 
Y  5 HOH 116 516 58   HOH HOH A . 
Y  5 HOH 117 517 1256 HOH HOH A . 
Y  5 HOH 118 518 282  HOH HOH A . 
Y  5 HOH 119 519 1011 HOH HOH A . 
Y  5 HOH 120 520 126  HOH HOH A . 
Y  5 HOH 121 521 713  HOH HOH A . 
Y  5 HOH 122 522 755  HOH HOH A . 
Y  5 HOH 123 523 229  HOH HOH A . 
Y  5 HOH 124 524 91   HOH HOH A . 
Y  5 HOH 125 525 29   HOH HOH A . 
Y  5 HOH 126 526 599  HOH HOH A . 
Y  5 HOH 127 527 335  HOH HOH A . 
Y  5 HOH 128 528 1051 HOH HOH A . 
Y  5 HOH 129 529 1355 HOH HOH A . 
Y  5 HOH 130 530 299  HOH HOH A . 
Y  5 HOH 131 531 202  HOH HOH A . 
Y  5 HOH 132 532 1360 HOH HOH A . 
Y  5 HOH 133 533 194  HOH HOH A . 
Y  5 HOH 134 534 393  HOH HOH A . 
Y  5 HOH 135 535 632  HOH HOH A . 
Y  5 HOH 136 536 963  HOH HOH A . 
Y  5 HOH 137 537 1043 HOH HOH A . 
Y  5 HOH 138 538 214  HOH HOH A . 
Y  5 HOH 139 539 285  HOH HOH A . 
Y  5 HOH 140 540 1264 HOH HOH A . 
Y  5 HOH 141 541 147  HOH HOH A . 
Y  5 HOH 142 542 39   HOH HOH A . 
Y  5 HOH 143 543 695  HOH HOH A . 
Y  5 HOH 144 544 326  HOH HOH A . 
Y  5 HOH 145 545 44   HOH HOH A . 
Y  5 HOH 146 546 1015 HOH HOH A . 
Y  5 HOH 147 547 548  HOH HOH A . 
Y  5 HOH 148 548 749  HOH HOH A . 
Y  5 HOH 149 549 6    HOH HOH A . 
Y  5 HOH 150 550 1041 HOH HOH A . 
Y  5 HOH 151 551 23   HOH HOH A . 
Y  5 HOH 152 552 281  HOH HOH A . 
Y  5 HOH 153 553 361  HOH HOH A . 
Y  5 HOH 154 554 941  HOH HOH A . 
Y  5 HOH 155 555 386  HOH HOH A . 
Y  5 HOH 156 556 320  HOH HOH A . 
Y  5 HOH 157 557 1093 HOH HOH A . 
Y  5 HOH 158 558 368  HOH HOH A . 
Y  5 HOH 159 559 495  HOH HOH A . 
Y  5 HOH 160 560 369  HOH HOH A . 
Y  5 HOH 161 561 1016 HOH HOH A . 
Y  5 HOH 162 562 1047 HOH HOH A . 
Y  5 HOH 163 563 413  HOH HOH A . 
Y  5 HOH 164 564 627  HOH HOH A . 
Y  5 HOH 165 565 142  HOH HOH A . 
Y  5 HOH 166 566 8    HOH HOH A . 
Y  5 HOH 167 567 612  HOH HOH A . 
Y  5 HOH 168 568 212  HOH HOH A . 
Y  5 HOH 169 569 559  HOH HOH A . 
Y  5 HOH 170 570 1357 HOH HOH A . 
Y  5 HOH 171 571 609  HOH HOH A . 
Y  5 HOH 172 572 557  HOH HOH A . 
Y  5 HOH 173 573 35   HOH HOH A . 
Y  5 HOH 174 574 163  HOH HOH A . 
Y  5 HOH 175 575 327  HOH HOH A . 
Y  5 HOH 176 576 568  HOH HOH A . 
Y  5 HOH 177 577 234  HOH HOH A . 
Y  5 HOH 178 578 1033 HOH HOH A . 
Y  5 HOH 179 579 719  HOH HOH A . 
Y  5 HOH 180 580 238  HOH HOH A . 
Y  5 HOH 181 581 741  HOH HOH A . 
Y  5 HOH 182 582 975  HOH HOH A . 
Y  5 HOH 183 583 310  HOH HOH A . 
Y  5 HOH 184 584 399  HOH HOH A . 
Y  5 HOH 185 585 521  HOH HOH A . 
Y  5 HOH 186 586 119  HOH HOH A . 
Y  5 HOH 187 587 907  HOH HOH A . 
Y  5 HOH 188 588 830  HOH HOH A . 
Y  5 HOH 189 589 1020 HOH HOH A . 
Y  5 HOH 190 590 682  HOH HOH A . 
Y  5 HOH 191 591 929  HOH HOH A . 
Y  5 HOH 192 592 1098 HOH HOH A . 
Y  5 HOH 193 593 148  HOH HOH A . 
Y  5 HOH 194 594 1249 HOH HOH A . 
Y  5 HOH 195 595 491  HOH HOH A . 
Y  5 HOH 196 596 862  HOH HOH A . 
Y  5 HOH 197 597 270  HOH HOH A . 
Y  5 HOH 198 598 77   HOH HOH A . 
Y  5 HOH 199 599 784  HOH HOH A . 
Y  5 HOH 200 600 730  HOH HOH A . 
Y  5 HOH 201 601 1010 HOH HOH A . 
Y  5 HOH 202 602 66   HOH HOH A . 
Y  5 HOH 203 603 1037 HOH HOH A . 
Y  5 HOH 204 604 1063 HOH HOH A . 
Y  5 HOH 205 605 1071 HOH HOH A . 
Y  5 HOH 206 606 384  HOH HOH A . 
Y  5 HOH 207 607 382  HOH HOH A . 
Y  5 HOH 208 608 457  HOH HOH A . 
Y  5 HOH 209 609 1271 HOH HOH A . 
Y  5 HOH 210 610 1027 HOH HOH A . 
Y  5 HOH 211 611 255  HOH HOH A . 
Y  5 HOH 212 612 182  HOH HOH A . 
Y  5 HOH 213 613 508  HOH HOH A . 
Y  5 HOH 214 614 718  HOH HOH A . 
Y  5 HOH 215 615 765  HOH HOH A . 
Y  5 HOH 216 616 273  HOH HOH A . 
Y  5 HOH 217 617 825  HOH HOH A . 
Y  5 HOH 218 618 608  HOH HOH A . 
Y  5 HOH 219 619 280  HOH HOH A . 
Y  5 HOH 220 620 904  HOH HOH A . 
Y  5 HOH 221 621 774  HOH HOH A . 
Y  5 HOH 222 622 244  HOH HOH A . 
Y  5 HOH 223 623 340  HOH HOH A . 
Y  5 HOH 224 624 1276 HOH HOH A . 
Y  5 HOH 225 625 1266 HOH HOH A . 
Y  5 HOH 226 626 685  HOH HOH A . 
Y  5 HOH 227 627 501  HOH HOH A . 
Y  5 HOH 228 628 415  HOH HOH A . 
Y  5 HOH 229 629 704  HOH HOH A . 
Y  5 HOH 230 630 955  HOH HOH A . 
Y  5 HOH 231 631 472  HOH HOH A . 
Y  5 HOH 232 632 530  HOH HOH A . 
Y  5 HOH 233 633 624  HOH HOH A . 
Y  5 HOH 234 634 808  HOH HOH A . 
Y  5 HOH 235 635 768  HOH HOH A . 
Y  5 HOH 236 636 916  HOH HOH A . 
Y  5 HOH 237 637 264  HOH HOH A . 
Y  5 HOH 238 638 538  HOH HOH A . 
Y  5 HOH 239 639 555  HOH HOH A . 
Y  5 HOH 240 640 712  HOH HOH A . 
Y  5 HOH 241 641 1257 HOH HOH A . 
Y  5 HOH 242 642 845  HOH HOH A . 
Y  5 HOH 243 643 1078 HOH HOH A . 
Y  5 HOH 244 644 621  HOH HOH A . 
Y  5 HOH 245 645 1029 HOH HOH A . 
Y  5 HOH 246 646 898  HOH HOH A . 
Y  5 HOH 247 647 355  HOH HOH A . 
Y  5 HOH 248 648 878  HOH HOH A . 
Y  5 HOH 249 649 576  HOH HOH A . 
Y  5 HOH 250 650 348  HOH HOH A . 
Y  5 HOH 251 651 164  HOH HOH A . 
Y  5 HOH 252 652 328  HOH HOH A . 
Y  5 HOH 253 653 1059 HOH HOH A . 
Y  5 HOH 254 654 1294 HOH HOH A . 
Y  5 HOH 255 655 925  HOH HOH A . 
Y  5 HOH 256 656 710  HOH HOH A . 
Y  5 HOH 257 657 507  HOH HOH A . 
Y  5 HOH 258 658 663  HOH HOH A . 
Y  5 HOH 259 659 742  HOH HOH A . 
Y  5 HOH 260 660 1056 HOH HOH A . 
Y  5 HOH 261 661 1048 HOH HOH A . 
Y  5 HOH 262 662 1039 HOH HOH A . 
Y  5 HOH 263 663 913  HOH HOH A . 
Y  5 HOH 264 664 482  HOH HOH A . 
Y  5 HOH 265 665 1092 HOH HOH A . 
Y  5 HOH 266 666 1082 HOH HOH A . 
Y  5 HOH 267 667 865  HOH HOH A . 
Y  5 HOH 268 668 1283 HOH HOH A . 
Y  5 HOH 269 669 855  HOH HOH A . 
Y  5 HOH 270 670 409  HOH HOH A . 
Y  5 HOH 271 671 659  HOH HOH A . 
Y  5 HOH 272 672 1087 HOH HOH A . 
Y  5 HOH 273 673 924  HOH HOH A . 
Y  5 HOH 274 674 1278 HOH HOH A . 
Y  5 HOH 275 675 1052 HOH HOH A . 
Y  5 HOH 276 676 1261 HOH HOH A . 
Y  5 HOH 277 677 1026 HOH HOH A . 
Y  5 HOH 278 678 1069 HOH HOH A . 
Y  5 HOH 279 679 636  HOH HOH A . 
Y  5 HOH 280 680 1081 HOH HOH A . 
Y  5 HOH 281 681 893  HOH HOH A . 
Y  5 HOH 282 682 834  HOH HOH A . 
Y  5 HOH 283 683 1359 HOH HOH A . 
Y  5 HOH 284 684 1094 HOH HOH A . 
Y  5 HOH 285 685 1062 HOH HOH A . 
Y  5 HOH 286 686 546  HOH HOH A . 
Y  5 HOH 287 687 1053 HOH HOH A . 
Y  5 HOH 288 688 876  HOH HOH A . 
Y  5 HOH 289 689 970  HOH HOH A . 
Y  5 HOH 290 690 1036 HOH HOH A . 
Y  5 HOH 291 691 1096 HOH HOH A . 
Y  5 HOH 292 692 770  HOH HOH A . 
Y  5 HOH 293 693 1117 HOH HOH A . 
Y  5 HOH 294 694 1279 HOH HOH A . 
Y  5 HOH 295 695 1070 HOH HOH A . 
Y  5 HOH 296 696 909  HOH HOH A . 
Y  5 HOH 297 697 469  HOH HOH A . 
Y  5 HOH 298 698 373  HOH HOH A . 
Y  5 HOH 299 699 1008 HOH HOH A . 
Y  5 HOH 300 700 867  HOH HOH A . 
Y  5 HOH 301 701 1095 HOH HOH A . 
Y  5 HOH 302 702 248  HOH HOH A . 
Y  5 HOH 303 703 786  HOH HOH A . 
Y  5 HOH 304 704 1345 HOH HOH A . 
Y  5 HOH 305 705 1260 HOH HOH A . 
Y  5 HOH 306 706 1084 HOH HOH A . 
Y  5 HOH 307 707 800  HOH HOH A . 
Y  5 HOH 308 708 579  HOH HOH A . 
Y  5 HOH 309 709 499  HOH HOH A . 
Y  5 HOH 310 710 841  HOH HOH A . 
Y  5 HOH 311 711 720  HOH HOH A . 
Y  5 HOH 312 712 594  HOH HOH A . 
Y  5 HOH 313 713 1277 HOH HOH A . 
Y  5 HOH 314 714 1086 HOH HOH A . 
Y  5 HOH 315 715 869  HOH HOH A . 
Y  5 HOH 316 716 1085 HOH HOH A . 
Y  5 HOH 317 717 1336 HOH HOH A . 
Y  5 HOH 318 718 1274 HOH HOH A . 
Y  5 HOH 319 719 1077 HOH HOH A . 
Y  5 HOH 320 720 971  HOH HOH A . 
Y  5 HOH 321 721 218  HOH HOH A . 
Y  5 HOH 322 722 1358 HOH HOH A . 
Y  5 HOH 323 723 1032 HOH HOH A . 
Y  5 HOH 324 724 751  HOH HOH A . 
Y  5 HOH 325 725 1263 HOH HOH A . 
Y  5 HOH 326 726 994  HOH HOH A . 
Y  5 HOH 327 727 965  HOH HOH A . 
Y  5 HOH 328 728 1018 HOH HOH A . 
Y  5 HOH 329 729 681  HOH HOH A . 
Y  5 HOH 330 730 543  HOH HOH A . 
Y  5 HOH 331 731 1028 HOH HOH A . 
Y  5 HOH 332 732 493  HOH HOH A . 
Y  5 HOH 333 733 483  HOH HOH A . 
Y  5 HOH 334 734 835  HOH HOH A . 
Y  5 HOH 335 735 872  HOH HOH A . 
Y  5 HOH 336 736 651  HOH HOH A . 
Y  5 HOH 337 737 1091 HOH HOH A . 
Y  5 HOH 338 738 1066 HOH HOH A . 
Y  5 HOH 339 739 728  HOH HOH A . 
Y  5 HOH 340 740 999  HOH HOH A . 
Y  5 HOH 341 741 1031 HOH HOH A . 
Y  5 HOH 342 742 1262 HOH HOH A . 
Z  5 HOH 1   401 812  HOH HOH B . 
Z  5 HOH 2   402 1300 HOH HOH B . 
Z  5 HOH 3   403 571  HOH HOH B . 
Z  5 HOH 4   404 1292 HOH HOH B . 
Z  5 HOH 5   405 1005 HOH HOH B . 
Z  5 HOH 6   406 1307 HOH HOH B . 
Z  5 HOH 7   407 933  HOH HOH B . 
Z  5 HOH 8   408 263  HOH HOH B . 
Z  5 HOH 9   409 1132 HOH HOH B . 
Z  5 HOH 10  410 740  HOH HOH B . 
Z  5 HOH 11  411 307  HOH HOH B . 
Z  5 HOH 12  412 1100 HOH HOH B . 
Z  5 HOH 13  413 1127 HOH HOH B . 
Z  5 HOH 14  414 974  HOH HOH B . 
Z  5 HOH 15  415 506  HOH HOH B . 
Z  5 HOH 16  416 1023 HOH HOH B . 
Z  5 HOH 17  417 239  HOH HOH B . 
Z  5 HOH 18  418 441  HOH HOH B . 
Z  5 HOH 19  419 9    HOH HOH B . 
Z  5 HOH 20  420 598  HOH HOH B . 
Z  5 HOH 21  421 806  HOH HOH B . 
Z  5 HOH 22  422 1148 HOH HOH B . 
Z  5 HOH 23  423 1289 HOH HOH B . 
Z  5 HOH 24  424 152  HOH HOH B . 
Z  5 HOH 25  425 156  HOH HOH B . 
Z  5 HOH 26  426 406  HOH HOH B . 
Z  5 HOH 27  427 1102 HOH HOH B . 
Z  5 HOH 28  428 124  HOH HOH B . 
Z  5 HOH 29  429 809  HOH HOH B . 
Z  5 HOH 30  430 1133 HOH HOH B . 
Z  5 HOH 31  431 374  HOH HOH B . 
Z  5 HOH 32  432 748  HOH HOH B . 
Z  5 HOH 33  433 700  HOH HOH B . 
Z  5 HOH 34  434 856  HOH HOH B . 
Z  5 HOH 35  435 967  HOH HOH B . 
Z  5 HOH 36  436 261  HOH HOH B . 
Z  5 HOH 37  437 737  HOH HOH B . 
Z  5 HOH 38  438 140  HOH HOH B . 
Z  5 HOH 39  439 185  HOH HOH B . 
Z  5 HOH 40  440 423  HOH HOH B . 
Z  5 HOH 41  441 463  HOH HOH B . 
Z  5 HOH 42  442 1124 HOH HOH B . 
Z  5 HOH 43  443 237  HOH HOH B . 
Z  5 HOH 44  444 1072 HOH HOH B . 
Z  5 HOH 45  445 80   HOH HOH B . 
Z  5 HOH 46  446 525  HOH HOH B . 
Z  5 HOH 47  447 250  HOH HOH B . 
Z  5 HOH 48  448 192  HOH HOH B . 
Z  5 HOH 49  449 735  HOH HOH B . 
Z  5 HOH 50  450 564  HOH HOH B . 
Z  5 HOH 51  451 232  HOH HOH B . 
Z  5 HOH 52  452 377  HOH HOH B . 
Z  5 HOH 53  453 804  HOH HOH B . 
Z  5 HOH 54  454 201  HOH HOH B . 
Z  5 HOH 55  455 1286 HOH HOH B . 
Z  5 HOH 56  456 889  HOH HOH B . 
Z  5 HOH 57  457 983  HOH HOH B . 
Z  5 HOH 58  458 1118 HOH HOH B . 
Z  5 HOH 59  459 86   HOH HOH B . 
Z  5 HOH 60  460 605  HOH HOH B . 
Z  5 HOH 61  461 641  HOH HOH B . 
Z  5 HOH 62  462 729  HOH HOH B . 
Z  5 HOH 63  463 1111 HOH HOH B . 
Z  5 HOH 64  464 48   HOH HOH B . 
Z  5 HOH 65  465 689  HOH HOH B . 
Z  5 HOH 66  466 776  HOH HOH B . 
Z  5 HOH 67  467 51   HOH HOH B . 
Z  5 HOH 68  468 360  HOH HOH B . 
Z  5 HOH 69  469 1045 HOH HOH B . 
Z  5 HOH 70  470 14   HOH HOH B . 
Z  5 HOH 71  471 288  HOH HOH B . 
Z  5 HOH 72  472 45   HOH HOH B . 
Z  5 HOH 73  473 79   HOH HOH B . 
Z  5 HOH 74  474 364  HOH HOH B . 
Z  5 HOH 75  475 365  HOH HOH B . 
Z  5 HOH 76  476 1116 HOH HOH B . 
Z  5 HOH 77  477 664  HOH HOH B . 
Z  5 HOH 78  478 169  HOH HOH B . 
Z  5 HOH 79  479 367  HOH HOH B . 
Z  5 HOH 80  480 175  HOH HOH B . 
Z  5 HOH 81  481 500  HOH HOH B . 
Z  5 HOH 82  482 570  HOH HOH B . 
Z  5 HOH 83  483 459  HOH HOH B . 
Z  5 HOH 84  484 818  HOH HOH B . 
Z  5 HOH 85  485 820  HOH HOH B . 
Z  5 HOH 86  486 630  HOH HOH B . 
Z  5 HOH 87  487 1259 HOH HOH B . 
Z  5 HOH 88  488 976  HOH HOH B . 
Z  5 HOH 89  489 50   HOH HOH B . 
Z  5 HOH 90  490 160  HOH HOH B . 
Z  5 HOH 91  491 203  HOH HOH B . 
Z  5 HOH 92  492 139  HOH HOH B . 
Z  5 HOH 93  493 105  HOH HOH B . 
Z  5 HOH 94  494 411  HOH HOH B . 
Z  5 HOH 95  495 199  HOH HOH B . 
Z  5 HOH 96  496 241  HOH HOH B . 
Z  5 HOH 97  497 115  HOH HOH B . 
Z  5 HOH 98  498 675  HOH HOH B . 
Z  5 HOH 99  499 304  HOH HOH B . 
Z  5 HOH 100 500 671  HOH HOH B . 
Z  5 HOH 101 501 174  HOH HOH B . 
Z  5 HOH 102 502 565  HOH HOH B . 
Z  5 HOH 103 503 82   HOH HOH B . 
Z  5 HOH 104 504 381  HOH HOH B . 
Z  5 HOH 105 505 829  HOH HOH B . 
Z  5 HOH 106 506 821  HOH HOH B . 
Z  5 HOH 107 507 1135 HOH HOH B . 
Z  5 HOH 108 508 73   HOH HOH B . 
Z  5 HOH 109 509 1013 HOH HOH B . 
Z  5 HOH 110 510 978  HOH HOH B . 
Z  5 HOH 111 511 87   HOH HOH B . 
Z  5 HOH 112 512 268  HOH HOH B . 
Z  5 HOH 113 513 370  HOH HOH B . 
Z  5 HOH 114 514 763  HOH HOH B . 
Z  5 HOH 115 515 1272 HOH HOH B . 
Z  5 HOH 116 516 618  HOH HOH B . 
Z  5 HOH 117 517 49   HOH HOH B . 
Z  5 HOH 118 518 828  HOH HOH B . 
Z  5 HOH 119 519 676  HOH HOH B . 
Z  5 HOH 120 520 37   HOH HOH B . 
Z  5 HOH 121 521 330  HOH HOH B . 
Z  5 HOH 122 522 54   HOH HOH B . 
Z  5 HOH 123 523 962  HOH HOH B . 
Z  5 HOH 124 524 1110 HOH HOH B . 
Z  5 HOH 125 525 81   HOH HOH B . 
Z  5 HOH 126 526 359  HOH HOH B . 
Z  5 HOH 127 527 61   HOH HOH B . 
Z  5 HOH 128 528 467  HOH HOH B . 
Z  5 HOH 129 529 336  HOH HOH B . 
Z  5 HOH 130 530 1291 HOH HOH B . 
Z  5 HOH 131 531 100  HOH HOH B . 
Z  5 HOH 132 532 470  HOH HOH B . 
Z  5 HOH 133 533 656  HOH HOH B . 
Z  5 HOH 134 534 96   HOH HOH B . 
Z  5 HOH 135 535 170  HOH HOH B . 
Z  5 HOH 136 536 38   HOH HOH B . 
Z  5 HOH 137 537 1046 HOH HOH B . 
Z  5 HOH 138 538 817  HOH HOH B . 
Z  5 HOH 139 539 40   HOH HOH B . 
Z  5 HOH 140 540 1024 HOH HOH B . 
Z  5 HOH 141 541 342  HOH HOH B . 
Z  5 HOH 142 542 790  HOH HOH B . 
Z  5 HOH 143 543 946  HOH HOH B . 
Z  5 HOH 144 544 697  HOH HOH B . 
Z  5 HOH 145 545 578  HOH HOH B . 
Z  5 HOH 146 546 297  HOH HOH B . 
Z  5 HOH 147 547 859  HOH HOH B . 
Z  5 HOH 148 548 211  HOH HOH B . 
Z  5 HOH 149 549 247  HOH HOH B . 
Z  5 HOH 150 550 950  HOH HOH B . 
Z  5 HOH 151 551 692  HOH HOH B . 
Z  5 HOH 152 552 733  HOH HOH B . 
Z  5 HOH 153 553 1288 HOH HOH B . 
Z  5 HOH 154 554 851  HOH HOH B . 
Z  5 HOH 155 555 168  HOH HOH B . 
Z  5 HOH 156 556 1309 HOH HOH B . 
Z  5 HOH 157 557 240  HOH HOH B . 
Z  5 HOH 158 558 63   HOH HOH B . 
Z  5 HOH 159 559 1120 HOH HOH B . 
Z  5 HOH 160 560 345  HOH HOH B . 
Z  5 HOH 161 561 980  HOH HOH B . 
Z  5 HOH 162 562 1115 HOH HOH B . 
Z  5 HOH 163 563 427  HOH HOH B . 
Z  5 HOH 164 564 1119 HOH HOH B . 
Z  5 HOH 165 565 778  HOH HOH B . 
Z  5 HOH 166 566 195  HOH HOH B . 
Z  5 HOH 167 567 274  HOH HOH B . 
Z  5 HOH 168 568 78   HOH HOH B . 
Z  5 HOH 169 569 514  HOH HOH B . 
Z  5 HOH 170 570 279  HOH HOH B . 
Z  5 HOH 171 571 1021 HOH HOH B . 
Z  5 HOH 172 572 318  HOH HOH B . 
Z  5 HOH 173 573 1121 HOH HOH B . 
Z  5 HOH 174 574 245  HOH HOH B . 
Z  5 HOH 175 575 43   HOH HOH B . 
Z  5 HOH 176 576 3    HOH HOH B . 
Z  5 HOH 177 577 617  HOH HOH B . 
Z  5 HOH 178 578 601  HOH HOH B . 
Z  5 HOH 179 579 388  HOH HOH B . 
Z  5 HOH 180 580 445  HOH HOH B . 
Z  5 HOH 181 581 686  HOH HOH B . 
Z  5 HOH 182 582 193  HOH HOH B . 
Z  5 HOH 183 583 363  HOH HOH B . 
Z  5 HOH 184 584 75   HOH HOH B . 
Z  5 HOH 185 585 914  HOH HOH B . 
Z  5 HOH 186 586 443  HOH HOH B . 
Z  5 HOH 187 587 1305 HOH HOH B . 
Z  5 HOH 188 588 517  HOH HOH B . 
Z  5 HOH 189 589 99   HOH HOH B . 
Z  5 HOH 190 590 2    HOH HOH B . 
Z  5 HOH 191 591 200  HOH HOH B . 
Z  5 HOH 192 592 1295 HOH HOH B . 
Z  5 HOH 193 593 1129 HOH HOH B . 
Z  5 HOH 194 594 701  HOH HOH B . 
Z  5 HOH 195 595 286  HOH HOH B . 
Z  5 HOH 196 596 108  HOH HOH B . 
Z  5 HOH 197 597 294  HOH HOH B . 
Z  5 HOH 198 598 437  HOH HOH B . 
Z  5 HOH 199 599 1103 HOH HOH B . 
Z  5 HOH 200 600 1001 HOH HOH B . 
Z  5 HOH 201 601 1112 HOH HOH B . 
Z  5 HOH 202 602 418  HOH HOH B . 
Z  5 HOH 203 603 158  HOH HOH B . 
Z  5 HOH 204 604 885  HOH HOH B . 
Z  5 HOH 205 605 1134 HOH HOH B . 
Z  5 HOH 206 606 276  HOH HOH B . 
Z  5 HOH 207 607 552  HOH HOH B . 
Z  5 HOH 208 608 644  HOH HOH B . 
Z  5 HOH 209 609 321  HOH HOH B . 
Z  5 HOH 210 610 826  HOH HOH B . 
Z  5 HOH 211 611 289  HOH HOH B . 
Z  5 HOH 212 612 1125 HOH HOH B . 
Z  5 HOH 213 613 344  HOH HOH B . 
Z  5 HOH 214 614 738  HOH HOH B . 
Z  5 HOH 215 615 226  HOH HOH B . 
Z  5 HOH 216 616 419  HOH HOH B . 
Z  5 HOH 217 617 109  HOH HOH B . 
Z  5 HOH 218 618 532  HOH HOH B . 
Z  5 HOH 219 619 465  HOH HOH B . 
Z  5 HOH 220 620 56   HOH HOH B . 
Z  5 HOH 221 621 1058 HOH HOH B . 
Z  5 HOH 222 622 1123 HOH HOH B . 
Z  5 HOH 223 623 652  HOH HOH B . 
Z  5 HOH 224 624 863  HOH HOH B . 
Z  5 HOH 225 625 1079 HOH HOH B . 
Z  5 HOH 226 626 1022 HOH HOH B . 
Z  5 HOH 227 627 402  HOH HOH B . 
Z  5 HOH 228 628 1068 HOH HOH B . 
Z  5 HOH 229 629 1145 HOH HOH B . 
Z  5 HOH 230 630 868  HOH HOH B . 
Z  5 HOH 231 631 711  HOH HOH B . 
Z  5 HOH 232 632 745  HOH HOH B . 
Z  5 HOH 233 633 120  HOH HOH B . 
Z  5 HOH 234 634 921  HOH HOH B . 
Z  5 HOH 235 635 1106 HOH HOH B . 
Z  5 HOH 236 636 1141 HOH HOH B . 
Z  5 HOH 237 637 661  HOH HOH B . 
Z  5 HOH 238 638 217  HOH HOH B . 
Z  5 HOH 239 639 222  HOH HOH B . 
Z  5 HOH 240 640 573  HOH HOH B . 
Z  5 HOH 241 641 587  HOH HOH B . 
Z  5 HOH 242 642 592  HOH HOH B . 
Z  5 HOH 243 643 992  HOH HOH B . 
Z  5 HOH 244 644 603  HOH HOH B . 
Z  5 HOH 245 645 1073 HOH HOH B . 
Z  5 HOH 246 646 351  HOH HOH B . 
Z  5 HOH 247 647 750  HOH HOH B . 
Z  5 HOH 248 648 1108 HOH HOH B . 
Z  5 HOH 249 649 1122 HOH HOH B . 
Z  5 HOH 250 650 1131 HOH HOH B . 
Z  5 HOH 251 651 1299 HOH HOH B . 
Z  5 HOH 252 652 668  HOH HOH B . 
Z  5 HOH 253 653 722  HOH HOH B . 
Z  5 HOH 254 654 252  HOH HOH B . 
Z  5 HOH 255 655 1136 HOH HOH B . 
Z  5 HOH 256 656 1126 HOH HOH B . 
Z  5 HOH 257 657 854  HOH HOH B . 
Z  5 HOH 258 658 563  HOH HOH B . 
Z  5 HOH 259 659 899  HOH HOH B . 
Z  5 HOH 260 660 1308 HOH HOH B . 
Z  5 HOH 261 661 1101 HOH HOH B . 
Z  5 HOH 262 662 977  HOH HOH B . 
Z  5 HOH 263 663 1109 HOH HOH B . 
Z  5 HOH 264 664 746  HOH HOH B . 
Z  5 HOH 265 665 461  HOH HOH B . 
Z  5 HOH 266 666 870  HOH HOH B . 
Z  5 HOH 267 667 960  HOH HOH B . 
Z  5 HOH 268 668 1356 HOH HOH B . 
Z  5 HOH 269 669 511  HOH HOH B . 
Z  5 HOH 270 670 1025 HOH HOH B . 
Z  5 HOH 271 671 596  HOH HOH B . 
Z  5 HOH 272 672 744  HOH HOH B . 
Z  5 HOH 273 673 714  HOH HOH B . 
Z  5 HOH 274 674 1293 HOH HOH B . 
Z  5 HOH 275 675 277  HOH HOH B . 
Z  5 HOH 276 676 1290 HOH HOH B . 
Z  5 HOH 277 677 615  HOH HOH B . 
Z  5 HOH 278 678 1080 HOH HOH B . 
Z  5 HOH 279 679 1301 HOH HOH B . 
Z  5 HOH 280 680 1303 HOH HOH B . 
Z  5 HOH 281 681 887  HOH HOH B . 
Z  5 HOH 282 682 796  HOH HOH B . 
Z  5 HOH 283 683 540  HOH HOH B . 
Z  5 HOH 284 684 1280 HOH HOH B . 
Z  5 HOH 285 685 490  HOH HOH B . 
Z  5 HOH 286 686 259  HOH HOH B . 
Z  5 HOH 287 687 421  HOH HOH B . 
Z  5 HOH 288 688 844  HOH HOH B . 
Z  5 HOH 289 689 667  HOH HOH B . 
Z  5 HOH 290 690 311  HOH HOH B . 
Z  5 HOH 291 691 1137 HOH HOH B . 
Z  5 HOH 292 692 1296 HOH HOH B . 
Z  5 HOH 293 693 795  HOH HOH B . 
Z  5 HOH 294 694 1017 HOH HOH B . 
Z  5 HOH 295 695 905  HOH HOH B . 
Z  5 HOH 296 696 479  HOH HOH B . 
Z  5 HOH 297 697 440  HOH HOH B . 
Z  5 HOH 298 698 788  HOH HOH B . 
Z  5 HOH 299 699 424  HOH HOH B . 
Z  5 HOH 300 700 1064 HOH HOH B . 
Z  5 HOH 301 701 1284 HOH HOH B . 
Z  5 HOH 302 702 1113 HOH HOH B . 
Z  5 HOH 303 703 1246 HOH HOH B . 
Z  5 HOH 304 704 358  HOH HOH B . 
Z  5 HOH 305 705 1002 HOH HOH B . 
Z  5 HOH 306 706 1114 HOH HOH B . 
Z  5 HOH 307 707 442  HOH HOH B . 
Z  5 HOH 308 708 296  HOH HOH B . 
Z  5 HOH 309 709 1304 HOH HOH B . 
Z  5 HOH 310 710 764  HOH HOH B . 
Z  5 HOH 311 711 522  HOH HOH B . 
Z  5 HOH 312 712 623  HOH HOH B . 
Z  5 HOH 313 713 452  HOH HOH B . 
Z  5 HOH 314 714 1104 HOH HOH B . 
Z  5 HOH 315 715 489  HOH HOH B . 
Z  5 HOH 316 716 550  HOH HOH B . 
Z  5 HOH 317 717 536  HOH HOH B . 
Z  5 HOH 318 718 687  HOH HOH B . 
Z  5 HOH 319 719 1067 HOH HOH B . 
Z  5 HOH 320 720 1128 HOH HOH B . 
Z  5 HOH 321 721 1245 HOH HOH B . 
Z  5 HOH 322 722 1285 HOH HOH B . 
Z  5 HOH 323 723 739  HOH HOH B . 
Z  5 HOH 324 724 780  HOH HOH B . 
Z  5 HOH 325 725 954  HOH HOH B . 
Z  5 HOH 326 726 1258 HOH HOH B . 
Z  5 HOH 327 727 1019 HOH HOH B . 
Z  5 HOH 328 728 991  HOH HOH B . 
Z  5 HOH 329 729 1139 HOH HOH B . 
Z  5 HOH 330 730 439  HOH HOH B . 
Z  5 HOH 331 731 1297 HOH HOH B . 
Z  5 HOH 332 732 1349 HOH HOH B . 
Z  5 HOH 333 733 969  HOH HOH B . 
Z  5 HOH 334 734 706  HOH HOH B . 
Z  5 HOH 335 735 1107 HOH HOH B . 
Z  5 HOH 336 736 504  HOH HOH B . 
Z  5 HOH 337 737 1298 HOH HOH B . 
Z  5 HOH 338 738 1074 HOH HOH B . 
Z  5 HOH 339 739 626  HOH HOH B . 
Z  5 HOH 340 740 1075 HOH HOH B . 
Z  5 HOH 341 741 717  HOH HOH B . 
Z  5 HOH 342 742 1105 HOH HOH B . 
Z  5 HOH 343 743 464  HOH HOH B . 
Z  5 HOH 344 744 591  HOH HOH B . 
Z  5 HOH 345 745 487  HOH HOH B . 
Z  5 HOH 346 746 947  HOH HOH B . 
Z  5 HOH 347 747 1140 HOH HOH B . 
Z  5 HOH 348 748 802  HOH HOH B . 
Z  5 HOH 349 749 799  HOH HOH B . 
Z  5 HOH 350 750 1302 HOH HOH B . 
Z  5 HOH 351 751 1130 HOH HOH B . 
AA 5 HOH 1   401 1329 HOH HOH C . 
AA 5 HOH 2   402 1185 HOH HOH C . 
AA 5 HOH 3   403 1181 HOH HOH C . 
AA 5 HOH 4   404 322  HOH HOH C . 
AA 5 HOH 5   405 726  HOH HOH C . 
AA 5 HOH 6   406 1328 HOH HOH C . 
AA 5 HOH 7   407 1177 HOH HOH C . 
AA 5 HOH 8   408 520  HOH HOH C . 
AA 5 HOH 9   409 1003 HOH HOH C . 
AA 5 HOH 10  410 486  HOH HOH C . 
AA 5 HOH 11  411 1190 HOH HOH C . 
AA 5 HOH 12  412 1350 HOH HOH C . 
AA 5 HOH 13  413 1167 HOH HOH C . 
AA 5 HOH 14  414 972  HOH HOH C . 
AA 5 HOH 15  415 398  HOH HOH C . 
AA 5 HOH 16  416 1000 HOH HOH C . 
AA 5 HOH 17  417 210  HOH HOH C . 
AA 5 HOH 18  418 1331 HOH HOH C . 
AA 5 HOH 19  419 1202 HOH HOH C . 
AA 5 HOH 20  420 165  HOH HOH C . 
AA 5 HOH 21  421 673  HOH HOH C . 
AA 5 HOH 22  422 1196 HOH HOH C . 
AA 5 HOH 23  423 551  HOH HOH C . 
AA 5 HOH 24  424 577  HOH HOH C . 
AA 5 HOH 25  425 1335 HOH HOH C . 
AA 5 HOH 26  426 759  HOH HOH C . 
AA 5 HOH 27  427 154  HOH HOH C . 
AA 5 HOH 28  428 52   HOH HOH C . 
AA 5 HOH 29  429 1313 HOH HOH C . 
AA 5 HOH 30  430 503  HOH HOH C . 
AA 5 HOH 31  431 366  HOH HOH C . 
AA 5 HOH 32  432 447  HOH HOH C . 
AA 5 HOH 33  433 215  HOH HOH C . 
AA 5 HOH 34  434 997  HOH HOH C . 
AA 5 HOH 35  435 948  HOH HOH C . 
AA 5 HOH 36  436 1327 HOH HOH C . 
AA 5 HOH 37  437 1206 HOH HOH C . 
AA 5 HOH 38  438 1151 HOH HOH C . 
AA 5 HOH 39  439 562  HOH HOH C . 
AA 5 HOH 40  440 1207 HOH HOH C . 
AA 5 HOH 41  441 28   HOH HOH C . 
AA 5 HOH 42  442 958  HOH HOH C . 
AA 5 HOH 43  443 882  HOH HOH C . 
AA 5 HOH 44  444 1330 HOH HOH C . 
AA 5 HOH 45  445 836  HOH HOH C . 
AA 5 HOH 46  446 888  HOH HOH C . 
AA 5 HOH 47  447 574  HOH HOH C . 
AA 5 HOH 48  448 42   HOH HOH C . 
AA 5 HOH 49  449 943  HOH HOH C . 
AA 5 HOH 50  450 642  HOH HOH C . 
AA 5 HOH 51  451 93   HOH HOH C . 
AA 5 HOH 52  452 167  HOH HOH C . 
AA 5 HOH 53  453 815  HOH HOH C . 
AA 5 HOH 54  454 761  HOH HOH C . 
AA 5 HOH 55  455 62   HOH HOH C . 
AA 5 HOH 56  456 857  HOH HOH C . 
AA 5 HOH 57  457 643  HOH HOH C . 
AA 5 HOH 58  458 560  HOH HOH C . 
AA 5 HOH 59  459 308  HOH HOH C . 
AA 5 HOH 60  460 896  HOH HOH C . 
AA 5 HOH 61  461 396  HOH HOH C . 
AA 5 HOH 62  462 102  HOH HOH C . 
AA 5 HOH 63  463 1324 HOH HOH C . 
AA 5 HOH 64  464 923  HOH HOH C . 
AA 5 HOH 65  465 117  HOH HOH C . 
AA 5 HOH 66  466 230  HOH HOH C . 
AA 5 HOH 67  467 190  HOH HOH C . 
AA 5 HOH 68  468 931  HOH HOH C . 
AA 5 HOH 69  469 188  HOH HOH C . 
AA 5 HOH 70  470 444  HOH HOH C . 
AA 5 HOH 71  471 1009 HOH HOH C . 
AA 5 HOH 72  472 1211 HOH HOH C . 
AA 5 HOH 73  473 113  HOH HOH C . 
AA 5 HOH 74  474 385  HOH HOH C . 
AA 5 HOH 75  475 561  HOH HOH C . 
AA 5 HOH 76  476 936  HOH HOH C . 
AA 5 HOH 77  477 317  HOH HOH C . 
AA 5 HOH 78  478 509  HOH HOH C . 
AA 5 HOH 79  479 816  HOH HOH C . 
AA 5 HOH 80  480 528  HOH HOH C . 
AA 5 HOH 81  481 278  HOH HOH C . 
AA 5 HOH 82  482 13   HOH HOH C . 
AA 5 HOH 83  483 1187 HOH HOH C . 
AA 5 HOH 84  484 702  HOH HOH C . 
AA 5 HOH 85  485 111  HOH HOH C . 
AA 5 HOH 86  486 684  HOH HOH C . 
AA 5 HOH 87  487 92   HOH HOH C . 
AA 5 HOH 88  488 159  HOH HOH C . 
AA 5 HOH 89  489 611  HOH HOH C . 
AA 5 HOH 90  490 474  HOH HOH C . 
AA 5 HOH 91  491 191  HOH HOH C . 
AA 5 HOH 92  492 1060 HOH HOH C . 
AA 5 HOH 93  493 622  HOH HOH C . 
AA 5 HOH 94  494 209  HOH HOH C . 
AA 5 HOH 95  495 1189 HOH HOH C . 
AA 5 HOH 96  496 68   HOH HOH C . 
AA 5 HOH 97  497 155  HOH HOH C . 
AA 5 HOH 98  498 1191 HOH HOH C . 
AA 5 HOH 99  499 1012 HOH HOH C . 
AA 5 HOH 100 500 85   HOH HOH C . 
AA 5 HOH 101 501 1306 HOH HOH C . 
AA 5 HOH 102 502 448  HOH HOH C . 
AA 5 HOH 103 503 224  HOH HOH C . 
AA 5 HOH 104 504 917  HOH HOH C . 
AA 5 HOH 105 505 395  HOH HOH C . 
AA 5 HOH 106 506 1176 HOH HOH C . 
AA 5 HOH 107 507 356  HOH HOH C . 
AA 5 HOH 108 508 1186 HOH HOH C . 
AA 5 HOH 109 509 266  HOH HOH C . 
AA 5 HOH 110 510 1192 HOH HOH C . 
AA 5 HOH 111 511 417  HOH HOH C . 
AA 5 HOH 112 512 1171 HOH HOH C . 
AA 5 HOH 113 513 235  HOH HOH C . 
AA 5 HOH 114 514 537  HOH HOH C . 
AA 5 HOH 115 515 129  HOH HOH C . 
AA 5 HOH 116 516 1201 HOH HOH C . 
AA 5 HOH 117 517 1326 HOH HOH C . 
AA 5 HOH 118 518 329  HOH HOH C . 
AA 5 HOH 119 519 696  HOH HOH C . 
AA 5 HOH 120 520 480  HOH HOH C . 
AA 5 HOH 121 521 25   HOH HOH C . 
AA 5 HOH 122 522 476  HOH HOH C . 
AA 5 HOH 123 523 513  HOH HOH C . 
AA 5 HOH 124 524 1150 HOH HOH C . 
AA 5 HOH 125 525 4    HOH HOH C . 
AA 5 HOH 126 526 772  HOH HOH C . 
AA 5 HOH 127 527 404  HOH HOH C . 
AA 5 HOH 128 528 485  HOH HOH C . 
AA 5 HOH 129 529 134  HOH HOH C . 
AA 5 HOH 130 530 426  HOH HOH C . 
AA 5 HOH 131 531 775  HOH HOH C . 
AA 5 HOH 132 532 1168 HOH HOH C . 
AA 5 HOH 133 533 272  HOH HOH C . 
AA 5 HOH 134 534 861  HOH HOH C . 
AA 5 HOH 135 535 26   HOH HOH C . 
AA 5 HOH 136 536 515  HOH HOH C . 
AA 5 HOH 137 537 72   HOH HOH C . 
AA 5 HOH 138 538 607  HOH HOH C . 
AA 5 HOH 139 539 481  HOH HOH C . 
AA 5 HOH 140 540 283  HOH HOH C . 
AA 5 HOH 141 541 149  HOH HOH C . 
AA 5 HOH 142 542 313  HOH HOH C . 
AA 5 HOH 143 543 680  HOH HOH C . 
AA 5 HOH 144 544 17   HOH HOH C . 
AA 5 HOH 145 545 391  HOH HOH C . 
AA 5 HOH 146 546 436  HOH HOH C . 
AA 5 HOH 147 547 179  HOH HOH C . 
AA 5 HOH 148 548 392  HOH HOH C . 
AA 5 HOH 149 549 118  HOH HOH C . 
AA 5 HOH 150 550 1210 HOH HOH C . 
AA 5 HOH 151 551 743  HOH HOH C . 
AA 5 HOH 152 552 919  HOH HOH C . 
AA 5 HOH 153 553 306  HOH HOH C . 
AA 5 HOH 154 554 150  HOH HOH C . 
AA 5 HOH 155 555 7    HOH HOH C . 
AA 5 HOH 156 556 228  HOH HOH C . 
AA 5 HOH 157 557 407  HOH HOH C . 
AA 5 HOH 158 558 110  HOH HOH C . 
AA 5 HOH 159 559 945  HOH HOH C . 
AA 5 HOH 160 560 602  HOH HOH C . 
AA 5 HOH 161 561 1352 HOH HOH C . 
AA 5 HOH 162 562 672  HOH HOH C . 
AA 5 HOH 163 563 253  HOH HOH C . 
AA 5 HOH 164 564 1341 HOH HOH C . 
AA 5 HOH 165 565 460  HOH HOH C . 
AA 5 HOH 166 566 957  HOH HOH C . 
AA 5 HOH 167 567 1180 HOH HOH C . 
AA 5 HOH 168 568 74   HOH HOH C . 
AA 5 HOH 169 569 131  HOH HOH C . 
AA 5 HOH 170 570 527  HOH HOH C . 
AA 5 HOH 171 571 582  HOH HOH C . 
AA 5 HOH 172 572 293  HOH HOH C . 
AA 5 HOH 173 573 291  HOH HOH C . 
AA 5 HOH 174 574 64   HOH HOH C . 
AA 5 HOH 175 575 512  HOH HOH C . 
AA 5 HOH 176 576 606  HOH HOH C . 
AA 5 HOH 177 577 1205 HOH HOH C . 
AA 5 HOH 178 578 1208 HOH HOH C . 
AA 5 HOH 179 579 1166 HOH HOH C . 
AA 5 HOH 180 580 496  HOH HOH C . 
AA 5 HOH 181 581 604  HOH HOH C . 
AA 5 HOH 182 582 654  HOH HOH C . 
AA 5 HOH 183 583 352  HOH HOH C . 
AA 5 HOH 184 584 986  HOH HOH C . 
AA 5 HOH 185 585 380  HOH HOH C . 
AA 5 HOH 186 586 534  HOH HOH C . 
AA 5 HOH 187 587 94   HOH HOH C . 
AA 5 HOH 188 588 669  HOH HOH C . 
AA 5 HOH 189 589 762  HOH HOH C . 
AA 5 HOH 190 590 678  HOH HOH C . 
AA 5 HOH 191 591 662  HOH HOH C . 
AA 5 HOH 192 592 544  HOH HOH C . 
AA 5 HOH 193 593 989  HOH HOH C . 
AA 5 HOH 194 594 883  HOH HOH C . 
AA 5 HOH 195 595 586  HOH HOH C . 
AA 5 HOH 196 596 387  HOH HOH C . 
AA 5 HOH 197 597 1204 HOH HOH C . 
AA 5 HOH 198 598 811  HOH HOH C . 
AA 5 HOH 199 599 531  HOH HOH C . 
AA 5 HOH 200 600 145  HOH HOH C . 
AA 5 HOH 201 601 233  HOH HOH C . 
AA 5 HOH 202 602 758  HOH HOH C . 
AA 5 HOH 203 603 219  HOH HOH C . 
AA 5 HOH 204 604 1193 HOH HOH C . 
AA 5 HOH 205 605 1194 HOH HOH C . 
AA 5 HOH 206 606 309  HOH HOH C . 
AA 5 HOH 207 607 354  HOH HOH C . 
AA 5 HOH 208 608 852  HOH HOH C . 
AA 5 HOH 209 609 1337 HOH HOH C . 
AA 5 HOH 210 610 403  HOH HOH C . 
AA 5 HOH 211 611 103  HOH HOH C . 
AA 5 HOH 212 612 176  HOH HOH C . 
AA 5 HOH 213 613 325  HOH HOH C . 
AA 5 HOH 214 614 650  HOH HOH C . 
AA 5 HOH 215 615 347  HOH HOH C . 
AA 5 HOH 216 616 1203 HOH HOH C . 
AA 5 HOH 217 617 1006 HOH HOH C . 
AA 5 HOH 218 618 1323 HOH HOH C . 
AA 5 HOH 219 619 1138 HOH HOH C . 
AA 5 HOH 220 620 922  HOH HOH C . 
AA 5 HOH 221 621 942  HOH HOH C . 
AA 5 HOH 222 622 1188 HOH HOH C . 
AA 5 HOH 223 623 323  HOH HOH C . 
AA 5 HOH 224 624 996  HOH HOH C . 
AA 5 HOH 225 625 433  HOH HOH C . 
AA 5 HOH 226 626 906  HOH HOH C . 
AA 5 HOH 227 627 757  HOH HOH C . 
AA 5 HOH 228 628 526  HOH HOH C . 
AA 5 HOH 229 629 655  HOH HOH C . 
AA 5 HOH 230 630 915  HOH HOH C . 
AA 5 HOH 231 631 666  HOH HOH C . 
AA 5 HOH 232 632 966  HOH HOH C . 
AA 5 HOH 233 633 258  HOH HOH C . 
AA 5 HOH 234 634 1310 HOH HOH C . 
AA 5 HOH 235 635 429  HOH HOH C . 
AA 5 HOH 236 636 910  HOH HOH C . 
AA 5 HOH 237 637 1212 HOH HOH C . 
AA 5 HOH 238 638 275  HOH HOH C . 
AA 5 HOH 239 639 847  HOH HOH C . 
AA 5 HOH 240 640 842  HOH HOH C . 
AA 5 HOH 241 641 556  HOH HOH C . 
AA 5 HOH 242 642 1170 HOH HOH C . 
AA 5 HOH 243 643 783  HOH HOH C . 
AA 5 HOH 244 644 753  HOH HOH C . 
AA 5 HOH 245 645 979  HOH HOH C . 
AA 5 HOH 246 646 1195 HOH HOH C . 
AA 5 HOH 247 647 1175 HOH HOH C . 
AA 5 HOH 248 648 575  HOH HOH C . 
AA 5 HOH 249 649 640  HOH HOH C . 
AA 5 HOH 250 650 1321 HOH HOH C . 
AA 5 HOH 251 651 1197 HOH HOH C . 
AA 5 HOH 252 652 1209 HOH HOH C . 
AA 5 HOH 253 653 1179 HOH HOH C . 
AA 5 HOH 254 654 471  HOH HOH C . 
AA 5 HOH 255 655 1178 HOH HOH C . 
AA 5 HOH 256 656 660  HOH HOH C . 
AA 5 HOH 257 657 1239 HOH HOH C . 
AA 5 HOH 258 658 653  HOH HOH C . 
AA 5 HOH 259 659 892  HOH HOH C . 
AA 5 HOH 260 660 1273 HOH HOH C . 
AA 5 HOH 261 661 362  HOH HOH C . 
AA 5 HOH 262 662 873  HOH HOH C . 
AA 5 HOH 263 663 998  HOH HOH C . 
AA 5 HOH 264 664 1314 HOH HOH C . 
AA 5 HOH 265 665 981  HOH HOH C . 
AA 5 HOH 266 666 523  HOH HOH C . 
AA 5 HOH 267 667 715  HOH HOH C . 
AA 5 HOH 268 668 1325 HOH HOH C . 
AA 5 HOH 269 669 754  HOH HOH C . 
AA 5 HOH 270 670 1173 HOH HOH C . 
AA 5 HOH 271 671 1165 HOH HOH C . 
AA 5 HOH 272 672 837  HOH HOH C . 
AA 5 HOH 273 673 376  HOH HOH C . 
AA 5 HOH 274 674 1311 HOH HOH C . 
AA 5 HOH 275 675 951  HOH HOH C . 
AA 5 HOH 276 676 891  HOH HOH C . 
AA 5 HOH 277 677 824  HOH HOH C . 
AA 5 HOH 278 678 1332 HOH HOH C . 
AA 5 HOH 279 679 708  HOH HOH C . 
AA 5 HOH 280 680 1163 HOH HOH C . 
AA 5 HOH 281 681 987  HOH HOH C . 
AA 5 HOH 282 682 990  HOH HOH C . 
AA 5 HOH 283 683 1149 HOH HOH C . 
AA 5 HOH 284 684 953  HOH HOH C . 
AA 5 HOH 285 685 727  HOH HOH C . 
AA 5 HOH 286 686 645  HOH HOH C . 
AA 5 HOH 287 687 908  HOH HOH C . 
AA 5 HOH 288 688 792  HOH HOH C . 
AA 5 HOH 289 689 1184 HOH HOH C . 
AA 5 HOH 290 690 1251 HOH HOH C . 
AA 5 HOH 291 691 688  HOH HOH C . 
AA 5 HOH 292 692 665  HOH HOH C . 
AA 5 HOH 293 693 985  HOH HOH C . 
AA 5 HOH 294 694 1275 HOH HOH C . 
AA 5 HOH 295 695 785  HOH HOH C . 
AA 5 HOH 296 696 1338 HOH HOH C . 
AA 5 HOH 297 697 1182 HOH HOH C . 
AA 5 HOH 298 698 333  HOH HOH C . 
AA 5 HOH 299 699 658  HOH HOH C . 
AA 5 HOH 300 700 877  HOH HOH C . 
AA 5 HOH 301 701 900  HOH HOH C . 
AA 5 HOH 302 702 1312 HOH HOH C . 
AA 5 HOH 303 703 648  HOH HOH C . 
AA 5 HOH 304 704 823  HOH HOH C . 
AA 5 HOH 305 705 1164 HOH HOH C . 
AA 5 HOH 306 706 1320 HOH HOH C . 
AA 5 HOH 307 707 1319 HOH HOH C . 
AA 5 HOH 308 708 721  HOH HOH C . 
AA 5 HOH 309 709 810  HOH HOH C . 
AA 5 HOH 310 710 1318 HOH HOH C . 
AA 5 HOH 311 711 1162 HOH HOH C . 
AA 5 HOH 312 712 432  HOH HOH C . 
AA 5 HOH 313 713 1183 HOH HOH C . 
AA 5 HOH 314 714 1316 HOH HOH C . 
AA 5 HOH 315 715 1152 HOH HOH C . 
AA 5 HOH 316 716 968  HOH HOH C . 
AA 5 HOH 317 717 1322 HOH HOH C . 
AA 5 HOH 318 718 1169 HOH HOH C . 
AA 5 HOH 319 719 1317 HOH HOH C . 
BA 5 HOH 1   401 405  HOH HOH D . 
BA 5 HOH 2   402 674  HOH HOH D . 
BA 5 HOH 3   403 1143 HOH HOH D . 
BA 5 HOH 4   404 1346 HOH HOH D . 
BA 5 HOH 5   405 178  HOH HOH D . 
BA 5 HOH 6   406 723  HOH HOH D . 
BA 5 HOH 7   407 734  HOH HOH D . 
BA 5 HOH 8   408 1144 HOH HOH D . 
BA 5 HOH 9   409 879  HOH HOH D . 
BA 5 HOH 10  410 1216 HOH HOH D . 
BA 5 HOH 11  411 1340 HOH HOH D . 
BA 5 HOH 12  412 390  HOH HOH D . 
BA 5 HOH 13  413 1226 HOH HOH D . 
BA 5 HOH 14  414 1174 HOH HOH D . 
BA 5 HOH 15  415 265  HOH HOH D . 
BA 5 HOH 16  416 5    HOH HOH D . 
BA 5 HOH 17  417 256  HOH HOH D . 
BA 5 HOH 18  418 693  HOH HOH D . 
BA 5 HOH 19  419 498  HOH HOH D . 
BA 5 HOH 20  420 314  HOH HOH D . 
BA 5 HOH 21  421 435  HOH HOH D . 
BA 5 HOH 22  422 939  HOH HOH D . 
BA 5 HOH 23  423 1236 HOH HOH D . 
BA 5 HOH 24  424 984  HOH HOH D . 
BA 5 HOH 25  425 1247 HOH HOH D . 
BA 5 HOH 26  426 90   HOH HOH D . 
BA 5 HOH 27  427 236  HOH HOH D . 
BA 5 HOH 28  428 1218 HOH HOH D . 
BA 5 HOH 29  429 1198 HOH HOH D . 
BA 5 HOH 30  430 184  HOH HOH D . 
BA 5 HOH 31  431 805  HOH HOH D . 
BA 5 HOH 32  432 337  HOH HOH D . 
BA 5 HOH 33  433 343  HOH HOH D . 
BA 5 HOH 34  434 425  HOH HOH D . 
BA 5 HOH 35  435 162  HOH HOH D . 
BA 5 HOH 36  436 516  HOH HOH D . 
BA 5 HOH 37  437 349  HOH HOH D . 
BA 5 HOH 38  438 716  HOH HOH D . 
BA 5 HOH 39  439 747  HOH HOH D . 
BA 5 HOH 40  440 122  HOH HOH D . 
BA 5 HOH 41  441 53   HOH HOH D . 
BA 5 HOH 42  442 107  HOH HOH D . 
BA 5 HOH 43  443 494  HOH HOH D . 
BA 5 HOH 44  444 1097 HOH HOH D . 
BA 5 HOH 45  445 394  HOH HOH D . 
BA 5 HOH 46  446 703  HOH HOH D . 
BA 5 HOH 47  447 871  HOH HOH D . 
BA 5 HOH 48  448 65   HOH HOH D . 
BA 5 HOH 49  449 911  HOH HOH D . 
BA 5 HOH 50  450 589  HOH HOH D . 
BA 5 HOH 51  451 453  HOH HOH D . 
BA 5 HOH 52  452 634  HOH HOH D . 
BA 5 HOH 53  453 935  HOH HOH D . 
BA 5 HOH 54  454 196  HOH HOH D . 
BA 5 HOH 55  455 339  HOH HOH D . 
BA 5 HOH 56  456 249  HOH HOH D . 
BA 5 HOH 57  457 251  HOH HOH D . 
BA 5 HOH 58  458 860  HOH HOH D . 
BA 5 HOH 59  459 213  HOH HOH D . 
BA 5 HOH 60  460 949  HOH HOH D . 
BA 5 HOH 61  461 694  HOH HOH D . 
BA 5 HOH 62  462 518  HOH HOH D . 
BA 5 HOH 63  463 47   HOH HOH D . 
BA 5 HOH 64  464 731  HOH HOH D . 
BA 5 HOH 65  465 462  HOH HOH D . 
BA 5 HOH 66  466 177  HOH HOH D . 
BA 5 HOH 67  467 766  HOH HOH D . 
BA 5 HOH 68  468 894  HOH HOH D . 
BA 5 HOH 69  469 1232 HOH HOH D . 
BA 5 HOH 70  470 926  HOH HOH D . 
BA 5 HOH 71  471 331  HOH HOH D . 
BA 5 HOH 72  472 125  HOH HOH D . 
BA 5 HOH 73  473 34   HOH HOH D . 
BA 5 HOH 74  474 46   HOH HOH D . 
BA 5 HOH 75  475 83   HOH HOH D . 
BA 5 HOH 76  476 902  HOH HOH D . 
BA 5 HOH 77  477 446  HOH HOH D . 
BA 5 HOH 78  478 143  HOH HOH D . 
BA 5 HOH 79  479 27   HOH HOH D . 
BA 5 HOH 80  480 55   HOH HOH D . 
BA 5 HOH 81  481 420  HOH HOH D . 
BA 5 HOH 82  482 1250 HOH HOH D . 
BA 5 HOH 83  483 324  HOH HOH D . 
BA 5 HOH 84  484 956  HOH HOH D . 
BA 5 HOH 85  485 41   HOH HOH D . 
BA 5 HOH 86  486 84   HOH HOH D . 
BA 5 HOH 87  487 303  HOH HOH D . 
BA 5 HOH 88  488 1240 HOH HOH D . 
BA 5 HOH 89  489 36   HOH HOH D . 
BA 5 HOH 90  490 141  HOH HOH D . 
BA 5 HOH 91  491 635  HOH HOH D . 
BA 5 HOH 92  492 146  HOH HOH D . 
BA 5 HOH 93  493 846  HOH HOH D . 
BA 5 HOH 94  494 1235 HOH HOH D . 
BA 5 HOH 95  495 610  HOH HOH D . 
BA 5 HOH 96  496 114  HOH HOH D . 
BA 5 HOH 97  497 709  HOH HOH D . 
BA 5 HOH 98  498 631  HOH HOH D . 
BA 5 HOH 99  499 767  HOH HOH D . 
BA 5 HOH 100 500 30   HOH HOH D . 
BA 5 HOH 101 501 807  HOH HOH D . 
BA 5 HOH 102 502 71   HOH HOH D . 
BA 5 HOH 103 503 300  HOH HOH D . 
BA 5 HOH 104 504 21   HOH HOH D . 
BA 5 HOH 105 505 1157 HOH HOH D . 
BA 5 HOH 106 506 181  HOH HOH D . 
BA 5 HOH 107 507 813  HOH HOH D . 
BA 5 HOH 108 508 161  HOH HOH D . 
BA 5 HOH 109 509 1    HOH HOH D . 
BA 5 HOH 110 510 138  HOH HOH D . 
BA 5 HOH 111 511 205  HOH HOH D . 
BA 5 HOH 112 512 468  HOH HOH D . 
BA 5 HOH 113 513 752  HOH HOH D . 
BA 5 HOH 114 514 292  HOH HOH D . 
BA 5 HOH 115 515 12   HOH HOH D . 
BA 5 HOH 116 516 57   HOH HOH D . 
BA 5 HOH 117 517 76   HOH HOH D . 
BA 5 HOH 118 518 558  HOH HOH D . 
BA 5 HOH 119 519 121  HOH HOH D . 
BA 5 HOH 120 520 1142 HOH HOH D . 
BA 5 HOH 121 521 295  HOH HOH D . 
BA 5 HOH 122 522 679  HOH HOH D . 
BA 5 HOH 123 523 1004 HOH HOH D . 
BA 5 HOH 124 524 172  HOH HOH D . 
BA 5 HOH 125 525 822  HOH HOH D . 
BA 5 HOH 126 526 408  HOH HOH D . 
BA 5 HOH 127 527 529  HOH HOH D . 
BA 5 HOH 128 528 449  HOH HOH D . 
BA 5 HOH 129 529 216  HOH HOH D . 
BA 5 HOH 130 530 183  HOH HOH D . 
BA 5 HOH 131 531 128  HOH HOH D . 
BA 5 HOH 132 532 60   HOH HOH D . 
BA 5 HOH 133 533 389  HOH HOH D . 
BA 5 HOH 134 534 1215 HOH HOH D . 
BA 5 HOH 135 535 98   HOH HOH D . 
BA 5 HOH 136 536 938  HOH HOH D . 
BA 5 HOH 137 537 519  HOH HOH D . 
BA 5 HOH 138 538 416  HOH HOH D . 
BA 5 HOH 139 539 1241 HOH HOH D . 
BA 5 HOH 140 540 67   HOH HOH D . 
BA 5 HOH 141 541 153  HOH HOH D . 
BA 5 HOH 142 542 777  HOH HOH D . 
BA 5 HOH 143 543 677  HOH HOH D . 
BA 5 HOH 144 544 637  HOH HOH D . 
BA 5 HOH 145 545 144  HOH HOH D . 
BA 5 HOH 146 546 1227 HOH HOH D . 
BA 5 HOH 147 547 1200 HOH HOH D . 
BA 5 HOH 148 548 20   HOH HOH D . 
BA 5 HOH 149 549 803  HOH HOH D . 
BA 5 HOH 150 550 379  HOH HOH D . 
BA 5 HOH 151 551 628  HOH HOH D . 
BA 5 HOH 152 552 223  HOH HOH D . 
BA 5 HOH 153 553 260  HOH HOH D . 
BA 5 HOH 154 554 769  HOH HOH D . 
BA 5 HOH 155 555 649  HOH HOH D . 
BA 5 HOH 156 556 197  HOH HOH D . 
BA 5 HOH 157 557 705  HOH HOH D . 
BA 5 HOH 158 558 173  HOH HOH D . 
BA 5 HOH 159 559 620  HOH HOH D . 
BA 5 HOH 160 560 341  HOH HOH D . 
BA 5 HOH 161 561 1214 HOH HOH D . 
BA 5 HOH 162 562 567  HOH HOH D . 
BA 5 HOH 163 563 136  HOH HOH D . 
BA 5 HOH 164 564 70   HOH HOH D . 
BA 5 HOH 165 565 492  HOH HOH D . 
BA 5 HOH 166 566 1153 HOH HOH D . 
BA 5 HOH 167 567 302  HOH HOH D . 
BA 5 HOH 168 568 1243 HOH HOH D . 
BA 5 HOH 169 569 690  HOH HOH D . 
BA 5 HOH 170 570 588  HOH HOH D . 
BA 5 HOH 171 571 412  HOH HOH D . 
BA 5 HOH 172 572 569  HOH HOH D . 
BA 5 HOH 173 573 833  HOH HOH D . 
BA 5 HOH 174 574 19   HOH HOH D . 
BA 5 HOH 175 575 220  HOH HOH D . 
BA 5 HOH 176 576 995  HOH HOH D . 
BA 5 HOH 177 577 312  HOH HOH D . 
BA 5 HOH 178 578 1221 HOH HOH D . 
BA 5 HOH 179 579 242  HOH HOH D . 
BA 5 HOH 180 580 1244 HOH HOH D . 
BA 5 HOH 181 581 350  HOH HOH D . 
BA 5 HOH 182 582 231  HOH HOH D . 
BA 5 HOH 183 583 484  HOH HOH D . 
BA 5 HOH 184 584 438  HOH HOH D . 
BA 5 HOH 185 585 848  HOH HOH D . 
BA 5 HOH 186 586 254  HOH HOH D . 
BA 5 HOH 187 587 187  HOH HOH D . 
BA 5 HOH 188 588 157  HOH HOH D . 
BA 5 HOH 189 589 1248 HOH HOH D . 
BA 5 HOH 190 590 724  HOH HOH D . 
BA 5 HOH 191 591 400  HOH HOH D . 
BA 5 HOH 192 592 10   HOH HOH D . 
BA 5 HOH 193 593 383  HOH HOH D . 
BA 5 HOH 194 594 338  HOH HOH D . 
BA 5 HOH 195 595 59   HOH HOH D . 
BA 5 HOH 196 596 89   HOH HOH D . 
BA 5 HOH 197 597 533  HOH HOH D . 
BA 5 HOH 198 598 505  HOH HOH D . 
BA 5 HOH 199 599 581  HOH HOH D . 
BA 5 HOH 200 600 1287 HOH HOH D . 
BA 5 HOH 201 601 725  HOH HOH D . 
BA 5 HOH 202 602 428  HOH HOH D . 
BA 5 HOH 203 603 791  HOH HOH D . 
BA 5 HOH 204 604 683  HOH HOH D . 
BA 5 HOH 205 605 206  HOH HOH D . 
BA 5 HOH 206 606 760  HOH HOH D . 
BA 5 HOH 207 607 638  HOH HOH D . 
BA 5 HOH 208 608 590  HOH HOH D . 
BA 5 HOH 209 609 208  HOH HOH D . 
BA 5 HOH 210 610 1199 HOH HOH D . 
BA 5 HOH 211 611 616  HOH HOH D . 
BA 5 HOH 212 612 1007 HOH HOH D . 
BA 5 HOH 213 613 633  HOH HOH D . 
BA 5 HOH 214 614 782  HOH HOH D . 
BA 5 HOH 215 615 1351 HOH HOH D . 
BA 5 HOH 216 616 95   HOH HOH D . 
BA 5 HOH 217 617 422  HOH HOH D . 
BA 5 HOH 218 618 372  HOH HOH D . 
BA 5 HOH 219 619 130  HOH HOH D . 
BA 5 HOH 220 620 850  HOH HOH D . 
BA 5 HOH 221 621 375  HOH HOH D . 
BA 5 HOH 222 622 180  HOH HOH D . 
BA 5 HOH 223 623 24   HOH HOH D . 
BA 5 HOH 224 624 207  HOH HOH D . 
BA 5 HOH 225 625 305  HOH HOH D . 
BA 5 HOH 226 626 410  HOH HOH D . 
BA 5 HOH 227 627 123  HOH HOH D . 
BA 5 HOH 228 628 346  HOH HOH D . 
BA 5 HOH 229 629 545  HOH HOH D . 
BA 5 HOH 230 630 1228 HOH HOH D . 
BA 5 HOH 231 631 988  HOH HOH D . 
BA 5 HOH 232 632 756  HOH HOH D . 
BA 5 HOH 233 633 298  HOH HOH D . 
BA 5 HOH 234 634 434  HOH HOH D . 
BA 5 HOH 235 635 454  HOH HOH D . 
BA 5 HOH 236 636 430  HOH HOH D . 
BA 5 HOH 237 637 707  HOH HOH D . 
BA 5 HOH 238 638 858  HOH HOH D . 
BA 5 HOH 239 639 414  HOH HOH D . 
BA 5 HOH 240 640 964  HOH HOH D . 
BA 5 HOH 241 641 647  HOH HOH D . 
BA 5 HOH 242 642 881  HOH HOH D . 
BA 5 HOH 243 643 793  HOH HOH D . 
BA 5 HOH 244 644 901  HOH HOH D . 
BA 5 HOH 245 645 619  HOH HOH D . 
BA 5 HOH 246 646 1347 HOH HOH D . 
BA 5 HOH 247 647 1339 HOH HOH D . 
BA 5 HOH 248 648 450  HOH HOH D . 
BA 5 HOH 249 649 357  HOH HOH D . 
BA 5 HOH 250 650 455  HOH HOH D . 
BA 5 HOH 251 651 580  HOH HOH D . 
BA 5 HOH 252 652 875  HOH HOH D . 
BA 5 HOH 253 653 1222 HOH HOH D . 
BA 5 HOH 254 654 262  HOH HOH D . 
BA 5 HOH 255 655 1238 HOH HOH D . 
BA 5 HOH 256 656 488  HOH HOH D . 
BA 5 HOH 257 657 937  HOH HOH D . 
BA 5 HOH 258 658 1252 HOH HOH D . 
BA 5 HOH 259 659 1354 HOH HOH D . 
BA 5 HOH 260 660 1233 HOH HOH D . 
BA 5 HOH 261 661 657  HOH HOH D . 
BA 5 HOH 262 662 554  HOH HOH D . 
BA 5 HOH 263 663 597  HOH HOH D . 
BA 5 HOH 264 664 1315 HOH HOH D . 
BA 5 HOH 265 665 849  HOH HOH D . 
BA 5 HOH 266 666 691  HOH HOH D . 
BA 5 HOH 267 667 918  HOH HOH D . 
BA 5 HOH 268 668 779  HOH HOH D . 
BA 5 HOH 269 669 1146 HOH HOH D . 
BA 5 HOH 270 670 1161 HOH HOH D . 
BA 5 HOH 271 671 890  HOH HOH D . 
BA 5 HOH 272 672 1219 HOH HOH D . 
BA 5 HOH 273 673 773  HOH HOH D . 
BA 5 HOH 274 674 1213 HOH HOH D . 
BA 5 HOH 275 675 934  HOH HOH D . 
BA 5 HOH 276 676 1224 HOH HOH D . 
BA 5 HOH 277 677 959  HOH HOH D . 
BA 5 HOH 278 678 944  HOH HOH D . 
BA 5 HOH 279 679 225  HOH HOH D . 
BA 5 HOH 280 680 378  HOH HOH D . 
BA 5 HOH 281 681 1348 HOH HOH D . 
BA 5 HOH 282 682 993  HOH HOH D . 
BA 5 HOH 283 683 903  HOH HOH D . 
BA 5 HOH 284 684 584  HOH HOH D . 
BA 5 HOH 285 685 1172 HOH HOH D . 
BA 5 HOH 286 686 535  HOH HOH D . 
BA 5 HOH 287 687 798  HOH HOH D . 
BA 5 HOH 288 688 1229 HOH HOH D . 
BA 5 HOH 289 689 1147 HOH HOH D . 
BA 5 HOH 290 690 542  HOH HOH D . 
BA 5 HOH 291 691 794  HOH HOH D . 
BA 5 HOH 292 692 1333 HOH HOH D . 
BA 5 HOH 293 693 1242 HOH HOH D . 
BA 5 HOH 294 694 549  HOH HOH D . 
BA 5 HOH 295 695 940  HOH HOH D . 
BA 5 HOH 296 696 814  HOH HOH D . 
BA 5 HOH 297 697 801  HOH HOH D . 
BA 5 HOH 298 698 927  HOH HOH D . 
BA 5 HOH 299 699 866  HOH HOH D . 
BA 5 HOH 300 700 920  HOH HOH D . 
BA 5 HOH 301 701 613  HOH HOH D . 
BA 5 HOH 302 702 1155 HOH HOH D . 
BA 5 HOH 303 703 1334 HOH HOH D . 
BA 5 HOH 304 704 510  HOH HOH D . 
BA 5 HOH 305 705 227  HOH HOH D . 
BA 5 HOH 306 706 401  HOH HOH D . 
BA 5 HOH 307 707 646  HOH HOH D . 
BA 5 HOH 308 708 1217 HOH HOH D . 
BA 5 HOH 309 709 874  HOH HOH D . 
BA 5 HOH 310 710 1225 HOH HOH D . 
BA 5 HOH 311 711 1344 HOH HOH D . 
BA 5 HOH 312 712 353  HOH HOH D . 
BA 5 HOH 313 713 539  HOH HOH D . 
BA 5 HOH 314 714 832  HOH HOH D . 
BA 5 HOH 315 715 789  HOH HOH D . 
BA 5 HOH 316 716 1231 HOH HOH D . 
BA 5 HOH 317 717 1237 HOH HOH D . 
BA 5 HOH 318 718 827  HOH HOH D . 
BA 5 HOH 319 719 736  HOH HOH D . 
BA 5 HOH 320 720 1343 HOH HOH D . 
BA 5 HOH 321 721 1353 HOH HOH D . 
BA 5 HOH 322 722 1156 HOH HOH D . 
BA 5 HOH 323 723 853  HOH HOH D . 
BA 5 HOH 324 724 502  HOH HOH D . 
BA 5 HOH 325 725 451  HOH HOH D . 
BA 5 HOH 326 726 797  HOH HOH D . 
BA 5 HOH 327 727 466  HOH HOH D . 
BA 5 HOH 328 728 133  HOH HOH D . 
BA 5 HOH 329 729 1159 HOH HOH D . 
BA 5 HOH 330 730 1342 HOH HOH D . 
BA 5 HOH 331 731 1223 HOH HOH D . 
BA 5 HOH 332 732 456  HOH HOH D . 
BA 5 HOH 333 733 1160 HOH HOH D . 
BA 5 HOH 334 734 1154 HOH HOH D . 
BA 5 HOH 335 735 246  HOH HOH D . 
BA 5 HOH 336 736 1065 HOH HOH D . 
BA 5 HOH 337 737 787  HOH HOH D . 
BA 5 HOH 338 738 895  HOH HOH D . 
BA 5 HOH 339 739 1220 HOH HOH D . 
BA 5 HOH 340 740 1234 HOH HOH D . 
BA 5 HOH 341 741 1158 HOH HOH D . 
BA 5 HOH 342 742 886  HOH HOH D . 
BA 5 HOH 343 743 973  HOH HOH D . 
BA 5 HOH 344 744 1230 HOH HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 C ASP 235 ? CG  ? C ASP 235 CG  
2 1 Y 1 C ASP 235 ? OD1 ? C ASP 235 OD1 
3 1 Y 1 C ASP 235 ? OD2 ? C ASP 235 OD2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? .      1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.20 2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.10   3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .      4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .      5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .      6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   108.920 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6G7A 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     77.296 
_cell.length_a_esd                 ? 
_cell.length_b                     73.925 
_cell.length_b_esd                 ? 
_cell.length_c                     91.217 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         6G7A 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   6G7A 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.06 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         39.9 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.2 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'Crystallization buffer: 0.1M ammonium citrate (pH 7.2), 0.2 M ammonium sulfate and 26% PEG4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment    ? 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.ambient_temp_esd       ? 
_diffrn.crystal_id             1 
_diffrn.crystal_support        ? 
_diffrn.crystal_treatment      ? 
_diffrn.details                ? 
_diffrn.id                     1 
_diffrn.ambient_pressure       ? 
_diffrn.ambient_pressure_esd   ? 
_diffrn.ambient_pressure_gt    ? 
_diffrn.ambient_pressure_lt    ? 
_diffrn.ambient_temp_gt        ? 
_diffrn.ambient_temp_lt        ? 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2015-06-26 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.033200 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.033200 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         6G7A 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.420 
_reflns.d_resolution_low                 86.290 
_reflns.details                          ? 
_reflns.limit_h_max                      ? 
_reflns.limit_h_min                      ? 
_reflns.limit_k_max                      ? 
_reflns.limit_k_min                      ? 
_reflns.limit_l_max                      ? 
_reflns.limit_l_min                      ? 
_reflns.number_all                       ? 
_reflns.number_obs                       173178 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             94.900 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.800 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.036 
_reflns.pdbx_netI_over_av_sigmaI         10.568 
_reflns.pdbx_netI_over_sigmaI            24.800 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  0.046 
_reflns.pdbx_Rpim_I_all                  0.017 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_R_split 
1.420 1.500  ? 4.1  ? ? ? ? 20503 77.200 ? ? ? ? 0.186 ? ? ? ? ? ? ? ? 6.000 0.186 ? ? ? 0.227 0.089 ? 1  1 ? ? 
1.500 1.590  ? 5.3  ? ? ? ? ?     96.500 ? ? ? ? 0.142 ? ? ? ? ? ? ? ? 7.000 0.142 ? ? ? 0.172 0.064 ? 2  1 ? ? 
1.590 1.700  ? 7.1  ? ? ? ? ?     96.800 ? ? ? ? 0.104 ? ? ? ? ? ? ? ? 6.700 0.104 ? ? ? 0.129 0.049 ? 3  1 ? ? 
1.700 1.830  ? 9.7  ? ? ? ? ?     97.500 ? ? ? ? 0.074 ? ? ? ? ? ? ? ? 7.100 0.074 ? ? ? 0.093 0.035 ? 4  1 ? ? 
1.830 2.010  ? 13.3 ? ? ? ? ?     97.900 ? ? ? ? 0.052 ? ? ? ? ? ? ? ? 6.700 0.052 ? ? ? 0.067 0.026 ? 5  1 ? ? 
2.010 2.250  ? 16.7 ? ? ? ? ?     98.300 ? ? ? ? 0.040 ? ? ? ? ? ? ? ? 7.200 0.040 ? ? ? 0.051 0.019 ? 6  1 ? ? 
2.250 2.590  ? 18.6 ? ? ? ? ?     98.700 ? ? ? ? 0.034 ? ? ? ? ? ? ? ? 6.800 0.034 ? ? ? 0.045 0.017 ? 7  1 ? ? 
2.590 3.180  ? 20.5 ? ? ? ? ?     99.400 ? ? ? ? 0.028 ? ? ? ? ? ? ? ? 7.200 0.028 ? ? ? 0.037 0.014 ? 8  1 ? ? 
3.180 4.490  ? 20.9 ? ? ? ? ?     99.500 ? ? ? ? 0.024 ? ? ? ? ? ? ? ? 6.800 0.024 ? ? ? 0.030 0.012 ? 9  1 ? ? 
4.490 86.290 ? 15.5 ? ? ? ? ?     99.500 ? ? ? ? 0.023 ? ? ? ? ? ? ? ? 6.800 0.023 ? ? ? 0.030 0.012 ? 10 1 ? ? 
# 
_refine.aniso_B[1][1]                            -0.0600 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.2000 
_refine.aniso_B[2][2]                            0.1600 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            -0.1900 
_refine.B_iso_max                                83.580 
_refine.B_iso_mean                               17.0153 
_refine.B_iso_min                                5.850 
_refine.correlation_coeff_Fo_to_Fc               0.9740 
_refine.correlation_coeff_Fo_to_Fc_free          0.9620 
_refine.details                                  
'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES      : REFINED INDIVIDUALLY' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 6G7A 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.4200 
_refine.ls_d_res_low                             73.1200 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     173152 
_refine.ls_number_reflns_R_free                  17232 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.6500 
_refine.ls_percent_reflns_R_free                 10.0000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1558 
_refine.ls_R_factor_R_free                       0.1859 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1525 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      5LL9 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.0680 
_refine.pdbx_overall_ESU_R_Free                  0.0710 
_refine.pdbx_solvent_vdw_probe_radii             1.4000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.0681 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        8408 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         152 
_refine_hist.number_atoms_solvent             1356 
_refine_hist.number_atoms_total               9916 
_refine_hist.d_res_high                       1.4200 
_refine_hist.d_res_low                        73.1200 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.025  0.019  9130  ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.332  1.959  12447 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 6.904  5.000  1103  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 37.725 24.583 456   ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 13.138 15.000 1426  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 14.818 15.000 37    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.167  0.200  1282  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.015  0.021  7250  ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 1.754  1.351  4343  ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 2.520  2.021  5469  ? r_mcangle_it           ? ? 
'X-RAY DIFFRACTION' ? 3.081  1.625  4787  ? r_scbond_it            ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.4200 
_refine_ls_shell.d_res_low                        1.4570 
_refine_ls_shell.number_reflns_all                8179 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             789 
_refine_ls_shell.number_reflns_R_work             7390 
_refine_ls_shell.percent_reflns_obs               60.6800 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free                  0.2280 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.1840 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     6G7A 
_struct.title                        
'Crystal structure of human carbonic anhydrase isozyme XII 2-(benzylamino)-4-chloro-N-(2-hydroxyethyl)-5-sulfamoyl-benzamide' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        6G7A 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor comple, lyase' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 2 ? 
F  N N 3 ? 
G  N N 4 ? 
H  N N 2 ? 
I  N N 3 ? 
J  N N 3 ? 
K  N N 3 ? 
L  N N 4 ? 
M  N N 2 ? 
N  N N 3 ? 
O  N N 3 ? 
P  N N 3 ? 
Q  N N 4 ? 
R  N N 2 ? 
S  N N 3 ? 
T  N N 3 ? 
U  N N 3 ? 
V  N N 3 ? 
W  N N 3 ? 
X  N N 4 ? 
Y  N N 5 ? 
Z  N N 5 ? 
AA N N 5 ? 
BA N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH12_HUMAN 
_struct_ref.pdbx_db_accession          O43570 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SKWTYFGPDGENSWSKKYPSCGGLLQSPIDLHSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQGL
QSRYSATQLHLHWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFNPSYDKIFSH
LQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFRNPVQISQEQLLALETALYCTHMDDPSPRE
MINNFRQVQKFDERLVYTSFSQ
;
_struct_ref.pdbx_align_begin           30 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 6G7A A 2 ? 263 ? O43570 30 ? 291 ? 2 263 
2 1 6G7A B 2 ? 263 ? O43570 30 ? 291 ? 2 263 
3 1 6G7A C 2 ? 263 ? O43570 30 ? 291 ? 2 263 
4 1 6G7A 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 6G7A MET A 1 ? UNP O43570 ? ? 'initiating methionine' 1 1 
2 6G7A MET B 1 ? UNP O43570 ? ? 'initiating methionine' 1 2 
3 6G7A MET C 1 ? UNP O43570 ? ? 'initiating methionine' 1 3 
4 6G7A MET D 1 ? UNP O43570 ? ? 'initiating methionine' 1 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? dimeric 2 
2 author_defined_assembly ? dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F,G,H,I,J,K,L,Y,Z           
2 1 C,D,M,N,O,P,Q,R,S,T,U,V,W,X,AA,BA 
# 
loop_
_pdbx_struct_assembly_auth_evidence.id 
_pdbx_struct_assembly_auth_evidence.assembly_id 
_pdbx_struct_assembly_auth_evidence.experimental_support 
_pdbx_struct_assembly_auth_evidence.details 
1 1 none ? 
2 2 none ? 
# 
_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 
# 
_struct_biol.id        1 
_struct_biol.details   'The asymmetric unit contains two dimers:' 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 11  ? ASN A 13  ? GLY A 11  ASN A 13  5 ? 3  
HELX_P HELX_P2  AA2 SER A 14  ? TYR A 19  ? SER A 14  TYR A 19  1 ? 6  
HELX_P HELX_P3  AA3 PRO A 20  ? GLY A 24  ? PRO A 20  GLY A 24  5 ? 5  
HELX_P HELX_P4  AA4 HIS A 33  ? ASP A 35  ? HIS A 33  ASP A 35  5 ? 3  
HELX_P HELX_P5  AA5 ASP A 128 ? SER A 133 ? ASP A 128 SER A 133 1 ? 6  
HELX_P HELX_P6  AA6 ASN A 152 ? SER A 160 ? ASN A 152 SER A 160 1 ? 9  
HELX_P HELX_P7  AA7 HIS A 161 ? LYS A 166 ? HIS A 161 LYS A 166 5 ? 6  
HELX_P HELX_P8  AA8 ASN A 178 ? LEU A 183 ? ASN A 178 LEU A 183 5 ? 6  
HELX_P HELX_P9  AA9 SER A 218 ? ALA A 228 ? SER A 218 ALA A 228 1 ? 11 
HELX_P HELX_P10 AB1 GLY B 11  ? LYS B 18  ? GLY B 11  LYS B 18  5 ? 8  
HELX_P HELX_P11 AB2 TYR B 19  ? GLY B 24  ? TYR B 19  GLY B 24  5 ? 6  
HELX_P HELX_P12 AB3 HIS B 33  ? ASP B 35  ? HIS B 33  ASP B 35  5 ? 3  
HELX_P HELX_P13 AB4 ASP B 128 ? SER B 133 ? ASP B 128 SER B 133 1 ? 6  
HELX_P HELX_P14 AB5 ASN B 152 ? SER B 160 ? ASN B 152 SER B 160 1 ? 9  
HELX_P HELX_P15 AB6 HIS B 161 ? VAL B 165 ? HIS B 161 VAL B 165 5 ? 5  
HELX_P HELX_P16 AB7 ASN B 178 ? LEU B 183 ? ASN B 178 LEU B 183 5 ? 6  
HELX_P HELX_P17 AB8 SER B 218 ? ALA B 228 ? SER B 218 ALA B 228 1 ? 11 
HELX_P HELX_P18 AB9 SER C 14  ? LYS C 18  ? SER C 14  LYS C 18  5 ? 5  
HELX_P HELX_P19 AC1 TYR C 19  ? GLY C 24  ? TYR C 19  GLY C 24  5 ? 6  
HELX_P HELX_P20 AC2 HIS C 33  ? ASP C 35  ? HIS C 33  ASP C 35  5 ? 3  
HELX_P HELX_P21 AC3 ASP C 128 ? SER C 133 ? ASP C 128 SER C 133 1 ? 6  
HELX_P HELX_P22 AC4 ASN C 152 ? SER C 160 ? ASN C 152 SER C 160 1 ? 9  
HELX_P HELX_P23 AC5 HIS C 161 ? VAL C 165 ? HIS C 161 VAL C 165 5 ? 5  
HELX_P HELX_P24 AC6 ASN C 178 ? LEU C 183 ? ASN C 178 LEU C 183 5 ? 6  
HELX_P HELX_P25 AC7 SER C 218 ? ALA C 228 ? SER C 218 ALA C 228 1 ? 11 
HELX_P HELX_P26 AC8 GLY D 11  ? LYS D 18  ? GLY D 11  LYS D 18  5 ? 8  
HELX_P HELX_P27 AC9 TYR D 19  ? GLY D 24  ? TYR D 19  GLY D 24  5 ? 6  
HELX_P HELX_P28 AD1 HIS D 33  ? ASP D 35  ? HIS D 33  ASP D 35  5 ? 3  
HELX_P HELX_P29 AD2 ASP D 128 ? ASN D 134 ? ASP D 128 ASN D 134 1 ? 7  
HELX_P HELX_P30 AD3 TYR D 155 ? SER D 160 ? TYR D 155 SER D 160 1 ? 6  
HELX_P HELX_P31 AD4 HIS D 161 ? VAL D 165 ? HIS D 161 VAL D 165 5 ? 5  
HELX_P HELX_P32 AD5 ASN D 178 ? LEU D 183 ? ASN D 178 LEU D 183 5 ? 6  
HELX_P HELX_P33 AD6 SER D 218 ? LEU D 229 ? SER D 218 LEU D 229 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 22  SG  ? ? ? 1_555 A CYS 202 SG ? ? A CYS 22  A CYS 202 1_555 ? ? ? ? ? ? ? 2.041 ? ? 
disulf2  disulf ? ? B CYS 22  SG  ? ? ? 1_555 B CYS 202 SG ? ? B CYS 22  B CYS 202 1_555 ? ? ? ? ? ? ? 2.057 ? ? 
disulf3  disulf ? ? C CYS 22  SG  ? ? ? 1_555 C CYS 202 SG ? ? C CYS 22  C CYS 202 1_555 ? ? ? ? ? ? ? 2.052 ? ? 
disulf4  disulf ? ? D CYS 22  SG  ? ? ? 1_555 D CYS 202 SG ? ? D CYS 22  D CYS 202 1_555 ? ? ? ? ? ? ? 2.023 ? ? 
metalc1  metalc ? ? A HIS 91  NE2 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 91  A ZN  301 1_555 ? ? ? ? ? ? ? 2.044 ? ? 
metalc2  metalc ? ? A HIS 93  NE2 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 93  A ZN  301 1_555 ? ? ? ? ? ? ? 2.017 ? ? 
metalc3  metalc ? ? A HIS 117 ND1 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 117 A ZN  301 1_555 ? ? ? ? ? ? ? 2.024 ? ? 
metalc4  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 G EOQ .   S1 A ? A ZN  301 A EOQ 303 1_555 ? ? ? ? ? ? ? 2.997 ? ? 
metalc5  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 G EOQ .   S1 B ? A ZN  301 A EOQ 303 1_555 ? ? ? ? ? ? ? 2.998 ? ? 
metalc6  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 G EOQ .   N5 A ? A ZN  301 A EOQ 303 1_555 ? ? ? ? ? ? ? 1.954 ? ? 
metalc7  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 G EOQ .   N5 B ? A ZN  301 A EOQ 303 1_555 ? ? ? ? ? ? ? 1.939 ? ? 
metalc8  metalc ? ? B HIS 91  NE2 ? ? ? 1_555 H ZN  .   ZN ? ? B HIS 91  B ZN  301 1_555 ? ? ? ? ? ? ? 2.011 ? ? 
metalc9  metalc ? ? B HIS 93  NE2 ? ? ? 1_555 H ZN  .   ZN ? ? B HIS 93  B ZN  301 1_555 ? ? ? ? ? ? ? 2.066 ? ? 
metalc10 metalc ? ? B HIS 117 ND1 ? ? ? 1_555 H ZN  .   ZN ? ? B HIS 117 B ZN  301 1_555 ? ? ? ? ? ? ? 2.027 ? ? 
metalc11 metalc ? ? H ZN  .   ZN  ? ? ? 1_555 L EOQ .   S1 ? ? B ZN  301 B EOQ 305 1_555 ? ? ? ? ? ? ? 2.984 ? ? 
metalc12 metalc ? ? H ZN  .   ZN  ? ? ? 1_555 L EOQ .   N5 ? ? B ZN  301 B EOQ 305 1_555 ? ? ? ? ? ? ? 1.877 ? ? 
metalc13 metalc ? ? C HIS 91  NE2 ? ? ? 1_555 M ZN  .   ZN ? ? C HIS 91  C ZN  301 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
metalc14 metalc ? ? C HIS 93  NE2 ? ? ? 1_555 M ZN  .   ZN ? ? C HIS 93  C ZN  301 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
metalc15 metalc ? ? C HIS 117 ND1 ? ? ? 1_555 M ZN  .   ZN ? ? C HIS 117 C ZN  301 1_555 ? ? ? ? ? ? ? 1.995 ? ? 
metalc16 metalc ? ? M ZN  .   ZN  ? ? ? 1_555 Q EOQ .   S1 ? ? C ZN  301 C EOQ 305 1_555 ? ? ? ? ? ? ? 2.985 ? ? 
metalc17 metalc ? ? M ZN  .   ZN  ? ? ? 1_555 Q EOQ .   N5 ? ? C ZN  301 C EOQ 305 1_555 ? ? ? ? ? ? ? 1.972 ? ? 
metalc18 metalc ? ? D HIS 91  NE2 ? ? ? 1_555 R ZN  .   ZN ? ? D HIS 91  D ZN  301 1_555 ? ? ? ? ? ? ? 2.007 ? ? 
metalc19 metalc ? ? D HIS 93  NE2 ? ? ? 1_555 R ZN  .   ZN ? ? D HIS 93  D ZN  301 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
metalc20 metalc ? ? D HIS 117 ND1 ? ? ? 1_555 R ZN  .   ZN ? ? D HIS 117 D ZN  301 1_555 ? ? ? ? ? ? ? 2.017 ? ? 
metalc21 metalc ? ? R ZN  .   ZN  ? ? ? 1_555 X EOQ .   N5 ? ? D ZN  301 D EOQ 307 1_555 ? ? ? ? ? ? ? 1.927 ? ? 
metalc22 metalc ? ? R ZN  .   ZN  ? ? ? 1_555 X EOQ .   S1 ? ? D ZN  301 D EOQ 307 1_555 ? ? ? ? ? ? ? 2.986 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 93  ? A HIS 93  ? 1_555 101.9 ? 
2  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 117 ? A HIS 117 ? 1_555 111.5 ? 
3  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 117 ? A HIS 117 ? 1_555 98.4  ? 
4  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 S1  A G EOQ .   ? A EOQ 303 ? 1_555 99.6  ? 
5  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 S1  A G EOQ .   ? A EOQ 303 ? 1_555 144.5 ? 
6  ND1 ? A HIS 117 ? A HIS 117 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 S1  A G EOQ .   ? A EOQ 303 ? 1_555 99.7  ? 
7  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 S1  B G EOQ .   ? A EOQ 303 ? 1_555 99.6  ? 
8  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 S1  B G EOQ .   ? A EOQ 303 ? 1_555 144.4 ? 
9  ND1 ? A HIS 117 ? A HIS 117 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 S1  B G EOQ .   ? A EOQ 303 ? 1_555 99.7  ? 
10 S1  A G EOQ .   ? A EOQ 303 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 S1  B G EOQ .   ? A EOQ 303 ? 1_555 0.0   ? 
11 NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N5  A G EOQ .   ? A EOQ 303 ? 1_555 110.1 ? 
12 NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N5  A G EOQ .   ? A EOQ 303 ? 1_555 115.9 ? 
13 ND1 ? A HIS 117 ? A HIS 117 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N5  A G EOQ .   ? A EOQ 303 ? 1_555 117.6 ? 
14 S1  A G EOQ .   ? A EOQ 303 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N5  A G EOQ .   ? A EOQ 303 ? 1_555 28.9  ? 
15 S1  B G EOQ .   ? A EOQ 303 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N5  A G EOQ .   ? A EOQ 303 ? 1_555 28.9  ? 
16 NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N5  B G EOQ .   ? A EOQ 303 ? 1_555 110.3 ? 
17 NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N5  B G EOQ .   ? A EOQ 303 ? 1_555 115.7 ? 
18 ND1 ? A HIS 117 ? A HIS 117 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N5  B G EOQ .   ? A EOQ 303 ? 1_555 117.6 ? 
19 S1  A G EOQ .   ? A EOQ 303 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N5  B G EOQ .   ? A EOQ 303 ? 1_555 29.1  ? 
20 S1  B G EOQ .   ? A EOQ 303 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N5  B G EOQ .   ? A EOQ 303 ? 1_555 29.1  ? 
21 N5  A G EOQ .   ? A EOQ 303 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N5  B G EOQ .   ? A EOQ 303 ? 1_555 0.2   ? 
22 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_555 103.5 ? 
23 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_555 112.2 ? 
24 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? H ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 99.7  ? 
25 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? H ZN . ? B ZN 301 ? 1_555 S1  ? L EOQ .   ? B EOQ 305 ? 1_555 98.8  ? 
26 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? H ZN . ? B ZN 301 ? 1_555 S1  ? L EOQ .   ? B EOQ 305 ? 1_555 143.4 ? 
27 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 ZN ? H ZN . ? B ZN 301 ? 1_555 S1  ? L EOQ .   ? B EOQ 305 ? 1_555 98.2  ? 
28 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? H ZN . ? B ZN 301 ? 1_555 N5  ? L EOQ .   ? B EOQ 305 ? 1_555 107.9 ? 
29 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? H ZN . ? B ZN 301 ? 1_555 N5  ? L EOQ .   ? B EOQ 305 ? 1_555 115.7 ? 
30 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 ZN ? H ZN . ? B ZN 301 ? 1_555 N5  ? L EOQ .   ? B EOQ 305 ? 1_555 117.0 ? 
31 S1  ? L EOQ .   ? B EOQ 305 ? 1_555 ZN ? H ZN . ? B ZN 301 ? 1_555 N5  ? L EOQ .   ? B EOQ 305 ? 1_555 28.3  ? 
32 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 100.5 ? 
33 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 113.5 ? 
34 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 99.3  ? 
35 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 S1  ? Q EOQ .   ? C EOQ 305 ? 1_555 99.8  ? 
36 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 S1  ? Q EOQ .   ? C EOQ 305 ? 1_555 145.1 ? 
37 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 S1  ? Q EOQ .   ? C EOQ 305 ? 1_555 98.1  ? 
38 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 N5  ? Q EOQ .   ? C EOQ 305 ? 1_555 109.8 ? 
39 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 N5  ? Q EOQ .   ? C EOQ 305 ? 1_555 116.1 ? 
40 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 N5  ? Q EOQ .   ? C EOQ 305 ? 1_555 116.2 ? 
41 S1  ? Q EOQ .   ? C EOQ 305 ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 N5  ? Q EOQ .   ? C EOQ 305 ? 1_555 29.4  ? 
42 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? R ZN . ? D ZN 301 ? 1_555 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 103.2 ? 
43 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? R ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 112.0 ? 
44 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? R ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 98.9  ? 
45 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? R ZN . ? D ZN 301 ? 1_555 N5  ? X EOQ .   ? D EOQ 307 ? 1_555 107.5 ? 
46 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? R ZN . ? D ZN 301 ? 1_555 N5  ? X EOQ .   ? D EOQ 307 ? 1_555 115.6 ? 
47 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 ZN ? R ZN . ? D ZN 301 ? 1_555 N5  ? X EOQ .   ? D EOQ 307 ? 1_555 118.6 ? 
48 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? R ZN . ? D ZN 301 ? 1_555 S1  ? X EOQ .   ? D EOQ 307 ? 1_555 99.7  ? 
49 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? R ZN . ? D ZN 301 ? 1_555 S1  ? X EOQ .   ? D EOQ 307 ? 1_555 143.6 ? 
50 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 ZN ? R ZN . ? D ZN 301 ? 1_555 S1  ? X EOQ .   ? D EOQ 307 ? 1_555 98.3  ? 
51 N5  ? X EOQ .   ? D EOQ 307 ? 1_555 ZN ? R ZN . ? D ZN 301 ? 1_555 S1  ? X EOQ .   ? D EOQ 307 ? 1_555 29.1  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 22 ? CYS A 202 ? CYS A 22 ? 1_555 CYS A 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS B 22 ? CYS B 202 ? CYS B 22 ? 1_555 CYS B 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS C 22 ? CYS C 202 ? CYS C 22 ? 1_555 CYS C 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS D 22 ? CYS D 202 ? CYS D 22 ? 1_555 CYS D 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 28  A . ? SER 28  A PRO 29  A ? PRO 29  A 1 2.65  
2 PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 8.08  
3 SER 28  B . ? SER 28  B PRO 29  B ? PRO 29  B 1 -1.21 
4 PRO 200 B . ? PRO 200 B PRO 201 B ? PRO 201 B 1 7.62  
5 PRO 200 B . ? PRO 200 B PRO 201 B ? PRO 201 B 1 -0.37 
6 SER 28  C . ? SER 28  C PRO 29  C ? PRO 29  C 1 -0.29 
7 PRO 200 C . ? PRO 200 C PRO 201 C ? PRO 201 C 1 4.43  
8 SER 28  D . ? SER 28  D PRO 29  D ? PRO 29  D 1 -2.65 
9 PRO 200 D . ? PRO 200 D PRO 201 D ? PRO 201 D 1 2.85  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
AA4 ? 2  ? 
AA5 ? 10 ? 
AA6 ? 6  ? 
AA7 ? 2  ? 
AA8 ? 10 ? 
AA9 ? 6  ? 
AB1 ? 2  ? 
AB2 ? 10 ? 
AB3 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
AA4 1 2  ? parallel      
AA5 1 2  ? parallel      
AA5 2 3  ? anti-parallel 
AA5 3 4  ? anti-parallel 
AA5 4 5  ? parallel      
AA5 5 6  ? anti-parallel 
AA5 6 7  ? anti-parallel 
AA5 7 8  ? anti-parallel 
AA5 8 9  ? anti-parallel 
AA5 9 10 ? anti-parallel 
AA6 1 2  ? anti-parallel 
AA6 2 3  ? anti-parallel 
AA6 3 4  ? anti-parallel 
AA6 4 5  ? anti-parallel 
AA6 5 6  ? parallel      
AA7 1 2  ? parallel      
AA8 1 2  ? parallel      
AA8 2 3  ? anti-parallel 
AA8 3 4  ? anti-parallel 
AA8 4 5  ? parallel      
AA8 5 6  ? anti-parallel 
AA8 6 7  ? anti-parallel 
AA8 7 8  ? anti-parallel 
AA8 8 9  ? anti-parallel 
AA8 9 10 ? anti-parallel 
AA9 1 2  ? anti-parallel 
AA9 2 3  ? anti-parallel 
AA9 3 4  ? anti-parallel 
AA9 4 5  ? anti-parallel 
AA9 5 6  ? parallel      
AB1 1 2  ? parallel      
AB2 1 2  ? parallel      
AB2 2 3  ? anti-parallel 
AB2 3 4  ? anti-parallel 
AB2 4 5  ? parallel      
AB2 5 6  ? anti-parallel 
AB2 6 7  ? anti-parallel 
AB2 7 8  ? anti-parallel 
AB2 8 9  ? anti-parallel 
AB2 9 10 ? anti-parallel 
AB3 1 2  ? anti-parallel 
AB3 2 3  ? anti-parallel 
AB3 3 4  ? anti-parallel 
AB3 4 5  ? anti-parallel 
AB3 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 31  ? LEU A 32  ? ASP A 31  LEU A 32  
AA1 2  THR A 106 ? VAL A 107 ? THR A 106 VAL A 107 
AA2 1  LEU A 37  ? TYR A 39  ? LEU A 37  TYR A 39  
AA2 2  VAL A 257 ? THR A 259 ? VAL A 257 THR A 259 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 190 GLY A 195 
AA2 4  VAL A 206 ? PHE A 211 ? VAL A 206 PHE A 211 
AA2 5  LEU A 139 ? MET A 148 ? LEU A 139 MET A 148 
AA2 6  ALA A 114 ? ASN A 122 ? ALA A 114 ASN A 122 
AA2 7  TYR A 85  ? TRP A 94  ? TYR A 85  TRP A 94  
AA2 8  VAL A 68  ? ASN A 71  ? VAL A 68  ASN A 71  
AA2 9  GLN A 58  ? ASN A 63  ? GLN A 58  ASN A 63  
AA2 10 GLU A 171 ? PRO A 175 ? GLU A 171 PRO A 175 
AA3 1  GLU A 47  ? GLN A 49  ? GLU A 47  GLN A 49  
AA3 2  HIS A 77  ? GLN A 79  ? HIS A 77  GLN A 79  
AA3 3  TYR A 85  ? TRP A 94  ? TYR A 85  TRP A 94  
AA3 4  ALA A 114 ? ASN A 122 ? ALA A 114 ASN A 122 
AA3 5  LEU A 139 ? MET A 148 ? LEU A 139 MET A 148 
AA3 6  VAL A 215 ? ILE A 217 ? VAL A 215 ILE A 217 
AA4 1  ASP B 31  ? LEU B 32  ? ASP B 31  LEU B 32  
AA4 2  THR B 106 ? VAL B 107 ? THR B 106 VAL B 107 
AA5 1  LEU B 37  ? TYR B 39  ? LEU B 37  TYR B 39  
AA5 2  VAL B 257 ? THR B 259 ? VAL B 257 THR B 259 
AA5 3  TYR B 190 ? GLY B 195 ? TYR B 190 GLY B 195 
AA5 4  VAL B 206 ? PHE B 211 ? VAL B 206 PHE B 211 
AA5 5  LEU B 139 ? MET B 148 ? LEU B 139 MET B 148 
AA5 6  ALA B 114 ? ASN B 122 ? ALA B 114 ASN B 122 
AA5 7  TYR B 85  ? TRP B 94  ? TYR B 85  TRP B 94  
AA5 8  VAL B 68  ? ASN B 71  ? VAL B 68  ASN B 71  
AA5 9  GLN B 58  ? ASN B 63  ? GLN B 58  ASN B 63  
AA5 10 GLU B 171 ? PRO B 175 ? GLU B 171 PRO B 175 
AA6 1  GLU B 47  ? GLN B 49  ? GLU B 47  GLN B 49  
AA6 2  HIS B 77  ? GLN B 79  ? HIS B 77  GLN B 79  
AA6 3  TYR B 85  ? TRP B 94  ? TYR B 85  TRP B 94  
AA6 4  ALA B 114 ? ASN B 122 ? ALA B 114 ASN B 122 
AA6 5  LEU B 139 ? MET B 148 ? LEU B 139 MET B 148 
AA6 6  VAL B 215 ? ILE B 217 ? VAL B 215 ILE B 217 
AA7 1  ASP C 31  ? LEU C 32  ? ASP C 31  LEU C 32  
AA7 2  THR C 106 ? VAL C 107 ? THR C 106 VAL C 107 
AA8 1  LEU C 37  ? TYR C 39  ? LEU C 37  TYR C 39  
AA8 2  VAL C 257 ? THR C 259 ? VAL C 257 THR C 259 
AA8 3  TYR C 190 ? GLY C 195 ? TYR C 190 GLY C 195 
AA8 4  VAL C 206 ? PHE C 211 ? VAL C 206 PHE C 211 
AA8 5  LEU C 139 ? MET C 148 ? LEU C 139 MET C 148 
AA8 6  ALA C 114 ? ASN C 122 ? ALA C 114 ASN C 122 
AA8 7  TYR C 85  ? TRP C 94  ? TYR C 85  TRP C 94  
AA8 8  VAL C 68  ? ASN C 71  ? VAL C 68  ASN C 71  
AA8 9  GLN C 58  ? ASN C 63  ? GLN C 58  ASN C 63  
AA8 10 GLU C 171 ? PRO C 175 ? GLU C 171 PRO C 175 
AA9 1  GLU C 47  ? GLN C 49  ? GLU C 47  GLN C 49  
AA9 2  HIS C 77  ? GLN C 79  ? HIS C 77  GLN C 79  
AA9 3  TYR C 85  ? TRP C 94  ? TYR C 85  TRP C 94  
AA9 4  ALA C 114 ? ASN C 122 ? ALA C 114 ASN C 122 
AA9 5  LEU C 139 ? MET C 148 ? LEU C 139 MET C 148 
AA9 6  VAL C 215 ? ILE C 217 ? VAL C 215 ILE C 217 
AB1 1  ASP D 31  ? LEU D 32  ? ASP D 31  LEU D 32  
AB1 2  THR D 106 ? VAL D 107 ? THR D 106 VAL D 107 
AB2 1  LEU D 37  ? TYR D 39  ? LEU D 37  TYR D 39  
AB2 2  VAL D 257 ? THR D 259 ? VAL D 257 THR D 259 
AB2 3  TYR D 190 ? GLY D 195 ? TYR D 190 GLY D 195 
AB2 4  VAL D 206 ? PHE D 211 ? VAL D 206 PHE D 211 
AB2 5  LEU D 139 ? MET D 148 ? LEU D 139 MET D 148 
AB2 6  ALA D 114 ? ASN D 122 ? ALA D 114 ASN D 122 
AB2 7  TYR D 85  ? TRP D 94  ? TYR D 85  TRP D 94  
AB2 8  VAL D 68  ? ASN D 71  ? VAL D 68  ASN D 71  
AB2 9  GLN D 58  ? ASN D 63  ? GLN D 58  ASN D 63  
AB2 10 GLU D 171 ? PRO D 175 ? GLU D 171 PRO D 175 
AB3 1  GLU D 47  ? GLN D 49  ? GLU D 47  GLN D 49  
AB3 2  HIS D 77  ? GLN D 79  ? HIS D 77  GLN D 79  
AB3 3  TYR D 85  ? TRP D 94  ? TYR D 85  TRP D 94  
AB3 4  ALA D 114 ? ASN D 122 ? ALA D 114 ASN D 122 
AB3 5  LEU D 139 ? MET D 148 ? LEU D 139 MET D 148 
AB3 6  VAL D 215 ? ILE D 217 ? VAL D 215 ILE D 217 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N LEU A 32  ? N LEU A 32  O THR A 106 ? O THR A 106 
AA2 1 2  N GLN A 38  ? N GLN A 38  O VAL A 257 ? O VAL A 257 
AA2 2 3  O TYR A 258 ? O TYR A 258 N ARG A 192 ? N ARG A 192 
AA2 3 4  N GLY A 195 ? N GLY A 195 O VAL A 206 ? O VAL A 206 
AA2 4 5  O THR A 209 ? O THR A 209 N ALA A 143 ? N ALA A 143 
AA2 5 6  O ILE A 146 ? O ILE A 146 N ALA A 114 ? N ALA A 114 
AA2 6 7  O VAL A 119 ? O VAL A 119 N GLN A 89  ? N GLN A 89  
AA2 7 8  O LEU A 90  ? O LEU A 90  N LEU A 70  ? N LEU A 70  
AA2 8 9  O ASN A 71  ? O ASN A 71  N LEU A 60  ? N LEU A 60  
AA2 9 10 N LEU A 61  ? N LEU A 61  O ALA A 172 ? O ALA A 172 
AA3 1 2  N GLN A 49  ? N GLN A 49  O HIS A 77  ? O HIS A 77  
AA3 2 3  N ILE A 78  ? N ILE A 78  O TYR A 85  ? O TYR A 85  
AA3 3 4  N GLN A 89  ? N GLN A 89  O VAL A 119 ? O VAL A 119 
AA3 4 5  N ALA A 114 ? N ALA A 114 O ILE A 146 ? O ILE A 146 
AA3 5 6  N GLU A 147 ? N GLU A 147 O VAL A 215 ? O VAL A 215 
AA4 1 2  N LEU B 32  ? N LEU B 32  O THR B 106 ? O THR B 106 
AA5 1 2  N GLN B 38  ? N GLN B 38  O THR B 259 ? O THR B 259 
AA5 2 3  O TYR B 258 ? O TYR B 258 N ARG B 192 ? N ARG B 192 
AA5 3 4  N GLY B 195 ? N GLY B 195 O VAL B 206 ? O VAL B 206 
AA5 4 5  O THR B 209 ? O THR B 209 N ALA B 143 ? N ALA B 143 
AA5 5 6  O LEU B 142 ? O LEU B 142 N ILE B 118 ? N ILE B 118 
AA5 6 7  O VAL B 119 ? O VAL B 119 N GLN B 89  ? N GLN B 89  
AA5 7 8  O LEU B 90  ? O LEU B 90  N LEU B 70  ? N LEU B 70  
AA5 8 9  O ASN B 71  ? O ASN B 71  N LEU B 60  ? N LEU B 60  
AA5 9 10 N LEU B 61  ? N LEU B 61  O ALA B 172 ? O ALA B 172 
AA6 1 2  N GLU B 47  ? N GLU B 47  O GLN B 79  ? O GLN B 79  
AA6 2 3  N ILE B 78  ? N ILE B 78  O TYR B 85  ? O TYR B 85  
AA6 3 4  N GLN B 89  ? N GLN B 89  O VAL B 119 ? O VAL B 119 
AA6 4 5  N ILE B 118 ? N ILE B 118 O LEU B 142 ? O LEU B 142 
AA6 5 6  N GLU B 147 ? N GLU B 147 O VAL B 215 ? O VAL B 215 
AA7 1 2  N LEU C 32  ? N LEU C 32  O THR C 106 ? O THR C 106 
AA8 1 2  N GLN C 38  ? N GLN C 38  O THR C 259 ? O THR C 259 
AA8 2 3  O TYR C 258 ? O TYR C 258 N ARG C 192 ? N ARG C 192 
AA8 3 4  N GLY C 195 ? N GLY C 195 O VAL C 206 ? O VAL C 206 
AA8 4 5  O THR C 209 ? O THR C 209 N ALA C 143 ? N ALA C 143 
AA8 5 6  O LEU C 142 ? O LEU C 142 N ILE C 118 ? N ILE C 118 
AA8 6 7  O VAL C 119 ? O VAL C 119 N GLN C 89  ? N GLN C 89  
AA8 7 8  O LEU C 90  ? O LEU C 90  N LEU C 70  ? N LEU C 70  
AA8 8 9  O ASN C 71  ? O ASN C 71  N LEU C 60  ? N LEU C 60  
AA8 9 10 N LEU C 61  ? N LEU C 61  O ALA C 172 ? O ALA C 172 
AA9 1 2  N GLU C 47  ? N GLU C 47  O GLN C 79  ? O GLN C 79  
AA9 2 3  N ILE C 78  ? N ILE C 78  O TYR C 85  ? O TYR C 85  
AA9 3 4  N GLN C 89  ? N GLN C 89  O VAL C 119 ? O VAL C 119 
AA9 4 5  N ILE C 118 ? N ILE C 118 O LEU C 142 ? O LEU C 142 
AA9 5 6  N GLU C 147 ? N GLU C 147 O VAL C 215 ? O VAL C 215 
AB1 1 2  N LEU D 32  ? N LEU D 32  O THR D 106 ? O THR D 106 
AB2 1 2  N GLN D 38  ? N GLN D 38  O VAL D 257 ? O VAL D 257 
AB2 2 3  O TYR D 258 ? O TYR D 258 N ARG D 192 ? N ARG D 192 
AB2 3 4  N TYR D 191 ? N TYR D 191 O VAL D 210 ? O VAL D 210 
AB2 4 5  O THR D 209 ? O THR D 209 N ALA D 143 ? N ALA D 143 
AB2 5 6  O ILE D 146 ? O ILE D 146 N ALA D 114 ? N ALA D 114 
AB2 6 7  O VAL D 119 ? O VAL D 119 N GLN D 89  ? N GLN D 89  
AB2 7 8  O LEU D 90  ? O LEU D 90  N LEU D 70  ? N LEU D 70  
AB2 8 9  O ASN D 71  ? O ASN D 71  N LEU D 60  ? N LEU D 60  
AB2 9 10 N LEU D 61  ? N LEU D 61  O ALA D 172 ? O ALA D 172 
AB3 1 2  N GLN D 49  ? N GLN D 49  O HIS D 77  ? O HIS D 77  
AB3 2 3  N ILE D 78  ? N ILE D 78  O TYR D 85  ? O TYR D 85  
AB3 3 4  N GLN D 89  ? N GLN D 89  O VAL D 119 ? O VAL D 119 
AB3 4 5  N ALA D 114 ? N ALA D 114 O ILE D 146 ? O ILE D 146 
AB3 5 6  N GLU D 147 ? N GLU D 147 O VAL D 215 ? O VAL D 215 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'binding site for residue ZN A 301'  
AC2 Software A EDO 302 ? 3  'binding site for residue EDO A 302' 
AC3 Software A EOQ 303 ? 17 'binding site for residue EOQ A 303' 
AC4 Software B ZN  301 ? 4  'binding site for residue ZN B 301'  
AC5 Software B EDO 302 ? 7  'binding site for residue EDO B 302' 
AC6 Software B EDO 303 ? 5  'binding site for residue EDO B 303' 
AC7 Software B EDO 304 ? 4  'binding site for residue EDO B 304' 
AC8 Software B EOQ 305 ? 15 'binding site for residue EOQ B 305' 
AC9 Software C ZN  301 ? 4  'binding site for residue ZN C 301'  
AD1 Software C EDO 302 ? 8  'binding site for residue EDO C 302' 
AD2 Software C EDO 303 ? 4  'binding site for residue EDO C 303' 
AD3 Software C EDO 304 ? 6  'binding site for residue EDO C 304' 
AD4 Software C EOQ 305 ? 17 'binding site for residue EOQ C 305' 
AD5 Software D ZN  301 ? 4  'binding site for residue ZN D 301'  
AD6 Software D EDO 302 ? 6  'binding site for residue EDO D 302' 
AD7 Software D EDO 303 ? 6  'binding site for residue EDO D 303' 
AD8 Software D EDO 304 ? 6  'binding site for residue EDO D 304' 
AD9 Software D EDO 305 ? 4  'binding site for residue EDO D 305' 
AE1 Software D EDO 306 ? 3  'binding site for residue EDO D 306' 
AE2 Software D EOQ 307 ? 15 'binding site for residue EOQ D 307' 
# 
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  EOQ G  .   ? EOQ A 303 . ? 1_555 ? 
5   AC2 3  ASP A  156 ? ASP A 156 . ? 1_555 ? 
6   AC2 3  SER A  160 ? SER A 160 . ? 1_555 ? 
7   AC2 3  HOH Y  .   ? HOH A 447 . ? 1_555 ? 
8   AC3 17 TRP A  4   ? TRP A 4   . ? 1_555 ? 
9   AC3 17 ASN A  64  ? ASN A 64  . ? 1_555 ? 
10  AC3 17 GLN A  89  ? GLN A 89  . ? 1_555 ? 
11  AC3 17 HIS A  91  ? HIS A 91  . ? 1_555 ? 
12  AC3 17 HIS A  93  ? HIS A 93  . ? 1_555 ? 
13  AC3 17 HIS A  117 ? HIS A 117 . ? 1_555 ? 
14  AC3 17 SER A  130 ? SER A 130 . ? 1_555 ? 
15  AC3 17 VAL A  141 ? VAL A 141 . ? 1_555 ? 
16  AC3 17 LEU A  197 ? LEU A 197 . ? 1_555 ? 
17  AC3 17 THR A  198 ? THR A 198 . ? 1_555 ? 
18  AC3 17 THR A  199 ? THR A 199 . ? 1_555 ? 
19  AC3 17 TRP A  208 ? TRP A 208 . ? 1_555 ? 
20  AC3 17 ZN  E  .   ? ZN  A 301 . ? 1_555 ? 
21  AC3 17 HOH Y  .   ? HOH A 407 . ? 1_555 ? 
22  AC3 17 HOH Y  .   ? HOH A 412 . ? 1_555 ? 
23  AC3 17 HOH Y  .   ? HOH A 426 . ? 1_555 ? 
24  AC3 17 HOH Y  .   ? HOH A 500 . ? 1_555 ? 
25  AC4 4  HIS B  91  ? HIS B 91  . ? 1_555 ? 
26  AC4 4  HIS B  93  ? HIS B 93  . ? 1_555 ? 
27  AC4 4  HIS B  117 ? HIS B 117 . ? 1_555 ? 
28  AC4 4  EOQ L  .   ? EOQ B 305 . ? 1_555 ? 
29  AC5 7  THR B  44  ? THR B 44  . ? 1_555 ? 
30  AC5 7  LEU B  46  ? LEU B 46  . ? 1_555 ? 
31  AC5 7  GLY B  80  ? GLY B 80  . ? 1_555 ? 
32  AC5 7  TYR B  190 ? TYR B 190 . ? 1_555 ? 
33  AC5 7  ARG B  192 ? ARG B 192 . ? 1_555 ? 
34  AC5 7  HOH Z  .   ? HOH B 423 . ? 1_555 ? 
35  AC5 7  HOH Z  .   ? HOH B 601 . ? 1_555 ? 
36  AC6 5  ASP B  156 ? ASP B 156 . ? 1_555 ? 
37  AC6 5  SER B  160 ? SER B 160 . ? 1_555 ? 
38  AC6 5  GLN B  221 ? GLN B 221 . ? 1_555 ? 
39  AC6 5  ALA B  224 ? ALA B 224 . ? 1_555 ? 
40  AC6 5  HOH Z  .   ? HOH B 519 . ? 1_555 ? 
41  AC7 4  LYS B  57  ? LYS B 57  . ? 1_555 ? 
42  AC7 4  GLN B  58  ? GLN B 58  . ? 1_555 ? 
43  AC7 4  HOH Z  .   ? HOH B 404 . ? 1_555 ? 
44  AC7 4  HOH Z  .   ? HOH B 632 . ? 1_555 ? 
45  AC8 15 ASN B  64  ? ASN B 64  . ? 1_555 ? 
46  AC8 15 GLN B  89  ? GLN B 89  . ? 1_555 ? 
47  AC8 15 HIS B  91  ? HIS B 91  . ? 1_555 ? 
48  AC8 15 HIS B  93  ? HIS B 93  . ? 1_555 ? 
49  AC8 15 HIS B  117 ? HIS B 117 . ? 1_555 ? 
50  AC8 15 SER B  130 ? SER B 130 . ? 1_555 ? 
51  AC8 15 SER B  133 ? SER B 133 . ? 1_555 ? 
52  AC8 15 VAL B  141 ? VAL B 141 . ? 1_555 ? 
53  AC8 15 LEU B  197 ? LEU B 197 . ? 1_555 ? 
54  AC8 15 THR B  198 ? THR B 198 . ? 1_555 ? 
55  AC8 15 THR B  199 ? THR B 199 . ? 1_555 ? 
56  AC8 15 TRP B  208 ? TRP B 208 . ? 1_555 ? 
57  AC8 15 ZN  H  .   ? ZN  B 301 . ? 1_555 ? 
58  AC8 15 HOH Z  .   ? HOH B 403 . ? 1_555 ? 
59  AC8 15 HOH Z  .   ? HOH B 581 . ? 1_555 ? 
60  AC9 4  HIS C  91  ? HIS C 91  . ? 1_555 ? 
61  AC9 4  HIS C  93  ? HIS C 93  . ? 1_555 ? 
62  AC9 4  HIS C  117 ? HIS C 117 . ? 1_555 ? 
63  AC9 4  EOQ Q  .   ? EOQ C 305 . ? 1_555 ? 
64  AD1 8  SER C  42  ? SER C 42  . ? 1_555 ? 
65  AD1 8  LEU C  46  ? LEU C 46  . ? 1_555 ? 
66  AD1 8  GLY C  80  ? GLY C 80  . ? 1_555 ? 
67  AD1 8  LEU C  81  ? LEU C 81  . ? 1_555 ? 
68  AD1 8  TYR C  190 ? TYR C 190 . ? 1_555 ? 
69  AD1 8  ARG C  192 ? ARG C 192 . ? 1_555 ? 
70  AD1 8  HOH AA .   ? HOH C 418 . ? 1_555 ? 
71  AD1 8  HOH AA .   ? HOH C 445 . ? 1_555 ? 
72  AD2 4  LEU C  46  ? LEU C 46  . ? 1_555 ? 
73  AD2 4  GLU C  47  ? GLU C 47  . ? 1_555 ? 
74  AD2 4  PHE C  48  ? PHE C 48  . ? 1_555 ? 
75  AD2 4  GLU C  180 ? GLU C 180 . ? 1_555 ? 
76  AD3 6  ASN C  71  ? ASN C 71  . ? 1_555 ? 
77  AD3 6  LEU C  72  ? LEU C 72  . ? 1_555 ? 
78  AD3 6  THR C  88  ? THR C 88  . ? 1_555 ? 
79  AD3 6  HOH AA .   ? HOH C 433 . ? 1_555 ? 
80  AD3 6  HOH AA .   ? HOH C 439 . ? 1_555 ? 
81  AD3 6  HOH AA .   ? HOH C 527 . ? 1_555 ? 
82  AD4 17 TRP C  4   ? TRP C 4   . ? 1_555 ? 
83  AD4 17 ASN C  64  ? ASN C 64  . ? 1_555 ? 
84  AD4 17 GLN C  89  ? GLN C 89  . ? 1_555 ? 
85  AD4 17 HIS C  91  ? HIS C 91  . ? 1_555 ? 
86  AD4 17 HIS C  93  ? HIS C 93  . ? 1_555 ? 
87  AD4 17 HIS C  117 ? HIS C 117 . ? 1_555 ? 
88  AD4 17 VAL C  119 ? VAL C 119 . ? 1_555 ? 
89  AD4 17 SER C  130 ? SER C 130 . ? 1_555 ? 
90  AD4 17 SER C  133 ? SER C 133 . ? 1_555 ? 
91  AD4 17 VAL C  141 ? VAL C 141 . ? 1_555 ? 
92  AD4 17 LEU C  197 ? LEU C 197 . ? 1_555 ? 
93  AD4 17 THR C  198 ? THR C 198 . ? 1_555 ? 
94  AD4 17 THR C  199 ? THR C 199 . ? 1_555 ? 
95  AD4 17 TRP C  208 ? TRP C 208 . ? 1_555 ? 
96  AD4 17 ZN  M  .   ? ZN  C 301 . ? 1_555 ? 
97  AD4 17 HOH AA .   ? HOH C 403 . ? 1_555 ? 
98  AD4 17 HOH AA .   ? HOH C 548 . ? 1_555 ? 
99  AD5 4  HIS D  91  ? HIS D 91  . ? 1_555 ? 
100 AD5 4  HIS D  93  ? HIS D 93  . ? 1_555 ? 
101 AD5 4  HIS D  117 ? HIS D 117 . ? 1_555 ? 
102 AD5 4  EOQ X  .   ? EOQ D 307 . ? 1_555 ? 
103 AD6 6  SER D  42  ? SER D 42  . ? 1_555 ? 
104 AD6 6  THR D  44  ? THR D 44  . ? 1_555 ? 
105 AD6 6  LEU D  46  ? LEU D 46  . ? 1_555 ? 
106 AD6 6  GLY D  80  ? GLY D 80  . ? 1_555 ? 
107 AD6 6  TYR D  190 ? TYR D 190 . ? 1_555 ? 
108 AD6 6  ARG D  192 ? ARG D 192 . ? 1_555 ? 
109 AD7 6  GLN D  110 ? GLN D 110 . ? 1_555 ? 
110 AD7 6  HIS D  111 ? HIS D 111 . ? 1_555 ? 
111 AD7 6  PHE D  112 ? PHE D 112 . ? 1_555 ? 
112 AD7 6  EDO U  .   ? EDO D 304 . ? 1_555 ? 
113 AD7 6  HOH BA .   ? HOH D 417 . ? 1_555 ? 
114 AD7 6  HOH BA .   ? HOH D 612 . ? 1_555 ? 
115 AD8 6  PHE D  112 ? PHE D 112 . ? 1_555 ? 
116 AD8 6  ALA D  113 ? ALA D 113 . ? 1_555 ? 
117 AD8 6  GLU D  147 ? GLU D 147 . ? 1_555 ? 
118 AD8 6  MET D  148 ? MET D 148 . ? 1_555 ? 
119 AD8 6  EDO T  .   ? EDO D 303 . ? 1_555 ? 
120 AD8 6  HOH BA .   ? HOH D 508 . ? 1_555 ? 
121 AD9 4  PRO D  100 ? PRO D 100 . ? 1_555 ? 
122 AD9 4  HIS D  101 ? HIS D 101 . ? 1_555 ? 
123 AD9 4  MET D  148 ? MET D 148 . ? 1_555 ? 
124 AD9 4  HOH BA .   ? HOH D 508 . ? 1_555 ? 
125 AE1 3  ASP D  156 ? ASP D 156 . ? 1_555 ? 
126 AE1 3  SER D  160 ? SER D 160 . ? 1_555 ? 
127 AE1 3  HOH BA .   ? HOH D 541 . ? 1_555 ? 
128 AE2 15 ASN D  64  ? ASN D 64  . ? 1_555 ? 
129 AE2 15 GLN D  89  ? GLN D 89  . ? 1_555 ? 
130 AE2 15 HIS D  91  ? HIS D 91  . ? 1_555 ? 
131 AE2 15 HIS D  93  ? HIS D 93  . ? 1_555 ? 
132 AE2 15 HIS D  117 ? HIS D 117 . ? 1_555 ? 
133 AE2 15 SER D  130 ? SER D 130 . ? 1_555 ? 
134 AE2 15 SER D  133 ? SER D 133 . ? 1_555 ? 
135 AE2 15 VAL D  141 ? VAL D 141 . ? 1_555 ? 
136 AE2 15 LEU D  197 ? LEU D 197 . ? 1_555 ? 
137 AE2 15 THR D  198 ? THR D 198 . ? 1_555 ? 
138 AE2 15 THR D  199 ? THR D 199 . ? 1_555 ? 
139 AE2 15 TRP D  208 ? TRP D 208 . ? 1_555 ? 
140 AE2 15 ZN  R  .   ? ZN  D 301 . ? 1_555 ? 
141 AE2 15 HOH BA .   ? HOH D 402 . ? 1_555 ? 
142 AE2 15 HOH BA .   ? HOH D 544 . ? 1_555 ? 
# 
_pdbx_entry_details.entry_id                   6G7A 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   D HOH 437 ? ? O D HOH 698 ? ? 2.01 
2 1 O   A HOH 666 ? ? O A HOH 705 ? ? 2.13 
3 1 OD2 A ASP 253 ? ? O A HOH 401 ? ? 2.14 
4 1 O   B HOH 571 ? ? O B HOH 720 ? ? 2.17 
5 1 O   C HOH 480 ? ? O C HOH 641 ? ? 2.18 
6 1 OE1 A GLN 79  ? ? O A HOH 402 ? ? 2.19 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CD A LYS 18  ? B CE A LYS 18  ? B NZ A LYS 18  ? B 95.78  111.70 -15.92 2.30 N 
2 1 CA A CYS 231 ? B CB A CYS 231 ? B SG A CYS 231 ? B 120.96 114.20 6.76   1.10 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 99  ? ? -150.61 77.21   
2  1 ASN A 245 ? ? -92.61  52.47   
3  1 ASP B 99  ? ? -154.09 85.91   
4  1 ASN B 245 ? ? -96.27  58.25   
5  1 ASP B 253 ? B 48.41   25.36   
6  1 GLU B 254 ? ? 73.57   -1.31   
7  1 GLU B 254 ? ? 88.35   -1.31   
8  1 PHE C 7   ? ? -156.06 -149.29 
9  1 ASP C 99  ? ? -153.00 78.03   
10 1 SER C 238 ? ? -112.77 79.89   
11 1 ASN C 245 ? ? -92.26  53.84   
12 1 HIS D 66  ? ? -131.74 -30.57  
13 1 ASP D 99  ? ? -152.92 81.40   
14 1 ASN D 245 ? ? -94.21  53.22   
# 
_phasing.method   MR 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? B HOH 750 ? 6.14 . 
2 1 O ? B HOH 751 ? 6.32 . 
3 1 O ? C HOH 718 ? 5.81 . 
4 1 O ? C HOH 719 ? 7.25 . 
5 1 O ? D HOH 744 ? 6.09 . 
# 
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 B MET 1 ? B MET 1 
3 1 Y 1 C MET 1 ? C MET 1 
4 1 Y 1 D MET 1 ? D MET 1 
5 1 Y 1 D SER 2 ? D SER 2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
EDO C1   C  N N 88  
EDO O1   O  N N 89  
EDO C2   C  N N 90  
EDO O2   O  N N 91  
EDO H11  H  N N 92  
EDO H12  H  N N 93  
EDO HO1  H  N N 94  
EDO H21  H  N N 95  
EDO H22  H  N N 96  
EDO HO2  H  N N 97  
EOQ C6   C  Y N 98  
EOQ C7   C  Y N 99  
EOQ C8   C  Y N 100 
EOQ C9   C  Y N 101 
EOQ C10  C  Y N 102 
EOQ C12  C  N N 103 
EOQ C2   C  Y N 104 
EOQ N5   N  N N 105 
EOQ C15  C  N N 106 
EOQ C16  C  N N 107 
EOQ O13  O  N N 108 
EOQ N14  N  N N 109 
EOQ O17  O  N N 110 
EOQ S1   S  N N 111 
EOQ O4   O  N N 112 
EOQ O3   O  N N 113 
EOQ CL1  CL N N 114 
EOQ N18  N  N N 115 
EOQ C19  C  N N 116 
EOQ C20  C  Y N 117 
EOQ C22  C  Y N 118 
EOQ C25  C  Y N 119 
EOQ C24  C  Y N 120 
EOQ C23  C  Y N 121 
EOQ C21  C  Y N 122 
EOQ H1   H  N N 123 
EOQ H2   H  N N 124 
EOQ H3   H  N N 125 
EOQ H4   H  N N 126 
EOQ H5   H  N N 127 
EOQ H6   H  N N 128 
EOQ H7   H  N N 129 
EOQ H8   H  N N 130 
EOQ H9   H  N N 131 
EOQ H10  H  N N 132 
EOQ H11  H  N N 133 
EOQ H12  H  N N 134 
EOQ H13  H  N N 135 
EOQ H14  H  N N 136 
EOQ H15  H  N N 137 
EOQ H16  H  N N 138 
EOQ H17  H  N N 139 
EOQ H18  H  N N 140 
GLN N    N  N N 141 
GLN CA   C  N S 142 
GLN C    C  N N 143 
GLN O    O  N N 144 
GLN CB   C  N N 145 
GLN CG   C  N N 146 
GLN CD   C  N N 147 
GLN OE1  O  N N 148 
GLN NE2  N  N N 149 
GLN OXT  O  N N 150 
GLN H    H  N N 151 
GLN H2   H  N N 152 
GLN HA   H  N N 153 
GLN HB2  H  N N 154 
GLN HB3  H  N N 155 
GLN HG2  H  N N 156 
GLN HG3  H  N N 157 
GLN HE21 H  N N 158 
GLN HE22 H  N N 159 
GLN HXT  H  N N 160 
GLU N    N  N N 161 
GLU CA   C  N S 162 
GLU C    C  N N 163 
GLU O    O  N N 164 
GLU CB   C  N N 165 
GLU CG   C  N N 166 
GLU CD   C  N N 167 
GLU OE1  O  N N 168 
GLU OE2  O  N N 169 
GLU OXT  O  N N 170 
GLU H    H  N N 171 
GLU H2   H  N N 172 
GLU HA   H  N N 173 
GLU HB2  H  N N 174 
GLU HB3  H  N N 175 
GLU HG2  H  N N 176 
GLU HG3  H  N N 177 
GLU HE2  H  N N 178 
GLU HXT  H  N N 179 
GLY N    N  N N 180 
GLY CA   C  N N 181 
GLY C    C  N N 182 
GLY O    O  N N 183 
GLY OXT  O  N N 184 
GLY H    H  N N 185 
GLY H2   H  N N 186 
GLY HA2  H  N N 187 
GLY HA3  H  N N 188 
GLY HXT  H  N N 189 
HIS N    N  N N 190 
HIS CA   C  N S 191 
HIS C    C  N N 192 
HIS O    O  N N 193 
HIS CB   C  N N 194 
HIS CG   C  Y N 195 
HIS ND1  N  Y N 196 
HIS CD2  C  Y N 197 
HIS CE1  C  Y N 198 
HIS NE2  N  Y N 199 
HIS OXT  O  N N 200 
HIS H    H  N N 201 
HIS H2   H  N N 202 
HIS HA   H  N N 203 
HIS HB2  H  N N 204 
HIS HB3  H  N N 205 
HIS HD1  H  N N 206 
HIS HD2  H  N N 207 
HIS HE1  H  N N 208 
HIS HE2  H  N N 209 
HIS HXT  H  N N 210 
HOH O    O  N N 211 
HOH H1   H  N N 212 
HOH H2   H  N N 213 
ILE N    N  N N 214 
ILE CA   C  N S 215 
ILE C    C  N N 216 
ILE O    O  N N 217 
ILE CB   C  N S 218 
ILE CG1  C  N N 219 
ILE CG2  C  N N 220 
ILE CD1  C  N N 221 
ILE OXT  O  N N 222 
ILE H    H  N N 223 
ILE H2   H  N N 224 
ILE HA   H  N N 225 
ILE HB   H  N N 226 
ILE HG12 H  N N 227 
ILE HG13 H  N N 228 
ILE HG21 H  N N 229 
ILE HG22 H  N N 230 
ILE HG23 H  N N 231 
ILE HD11 H  N N 232 
ILE HD12 H  N N 233 
ILE HD13 H  N N 234 
ILE HXT  H  N N 235 
LEU N    N  N N 236 
LEU CA   C  N S 237 
LEU C    C  N N 238 
LEU O    O  N N 239 
LEU CB   C  N N 240 
LEU CG   C  N N 241 
LEU CD1  C  N N 242 
LEU CD2  C  N N 243 
LEU OXT  O  N N 244 
LEU H    H  N N 245 
LEU H2   H  N N 246 
LEU HA   H  N N 247 
LEU HB2  H  N N 248 
LEU HB3  H  N N 249 
LEU HG   H  N N 250 
LEU HD11 H  N N 251 
LEU HD12 H  N N 252 
LEU HD13 H  N N 253 
LEU HD21 H  N N 254 
LEU HD22 H  N N 255 
LEU HD23 H  N N 256 
LEU HXT  H  N N 257 
LYS N    N  N N 258 
LYS CA   C  N S 259 
LYS C    C  N N 260 
LYS O    O  N N 261 
LYS CB   C  N N 262 
LYS CG   C  N N 263 
LYS CD   C  N N 264 
LYS CE   C  N N 265 
LYS NZ   N  N N 266 
LYS OXT  O  N N 267 
LYS H    H  N N 268 
LYS H2   H  N N 269 
LYS HA   H  N N 270 
LYS HB2  H  N N 271 
LYS HB3  H  N N 272 
LYS HG2  H  N N 273 
LYS HG3  H  N N 274 
LYS HD2  H  N N 275 
LYS HD3  H  N N 276 
LYS HE2  H  N N 277 
LYS HE3  H  N N 278 
LYS HZ1  H  N N 279 
LYS HZ2  H  N N 280 
LYS HZ3  H  N N 281 
LYS HXT  H  N N 282 
MET N    N  N N 283 
MET CA   C  N S 284 
MET C    C  N N 285 
MET O    O  N N 286 
MET CB   C  N N 287 
MET CG   C  N N 288 
MET SD   S  N N 289 
MET CE   C  N N 290 
MET OXT  O  N N 291 
MET H    H  N N 292 
MET H2   H  N N 293 
MET HA   H  N N 294 
MET HB2  H  N N 295 
MET HB3  H  N N 296 
MET HG2  H  N N 297 
MET HG3  H  N N 298 
MET HE1  H  N N 299 
MET HE2  H  N N 300 
MET HE3  H  N N 301 
MET HXT  H  N N 302 
PHE N    N  N N 303 
PHE CA   C  N S 304 
PHE C    C  N N 305 
PHE O    O  N N 306 
PHE CB   C  N N 307 
PHE CG   C  Y N 308 
PHE CD1  C  Y N 309 
PHE CD2  C  Y N 310 
PHE CE1  C  Y N 311 
PHE CE2  C  Y N 312 
PHE CZ   C  Y N 313 
PHE OXT  O  N N 314 
PHE H    H  N N 315 
PHE H2   H  N N 316 
PHE HA   H  N N 317 
PHE HB2  H  N N 318 
PHE HB3  H  N N 319 
PHE HD1  H  N N 320 
PHE HD2  H  N N 321 
PHE HE1  H  N N 322 
PHE HE2  H  N N 323 
PHE HZ   H  N N 324 
PHE HXT  H  N N 325 
PRO N    N  N N 326 
PRO CA   C  N S 327 
PRO C    C  N N 328 
PRO O    O  N N 329 
PRO CB   C  N N 330 
PRO CG   C  N N 331 
PRO CD   C  N N 332 
PRO OXT  O  N N 333 
PRO H    H  N N 334 
PRO HA   H  N N 335 
PRO HB2  H  N N 336 
PRO HB3  H  N N 337 
PRO HG2  H  N N 338 
PRO HG3  H  N N 339 
PRO HD2  H  N N 340 
PRO HD3  H  N N 341 
PRO HXT  H  N N 342 
SER N    N  N N 343 
SER CA   C  N S 344 
SER C    C  N N 345 
SER O    O  N N 346 
SER CB   C  N N 347 
SER OG   O  N N 348 
SER OXT  O  N N 349 
SER H    H  N N 350 
SER H2   H  N N 351 
SER HA   H  N N 352 
SER HB2  H  N N 353 
SER HB3  H  N N 354 
SER HG   H  N N 355 
SER HXT  H  N N 356 
THR N    N  N N 357 
THR CA   C  N S 358 
THR C    C  N N 359 
THR O    O  N N 360 
THR CB   C  N R 361 
THR OG1  O  N N 362 
THR CG2  C  N N 363 
THR OXT  O  N N 364 
THR H    H  N N 365 
THR H2   H  N N 366 
THR HA   H  N N 367 
THR HB   H  N N 368 
THR HG1  H  N N 369 
THR HG21 H  N N 370 
THR HG22 H  N N 371 
THR HG23 H  N N 372 
THR HXT  H  N N 373 
TRP N    N  N N 374 
TRP CA   C  N S 375 
TRP C    C  N N 376 
TRP O    O  N N 377 
TRP CB   C  N N 378 
TRP CG   C  Y N 379 
TRP CD1  C  Y N 380 
TRP CD2  C  Y N 381 
TRP NE1  N  Y N 382 
TRP CE2  C  Y N 383 
TRP CE3  C  Y N 384 
TRP CZ2  C  Y N 385 
TRP CZ3  C  Y N 386 
TRP CH2  C  Y N 387 
TRP OXT  O  N N 388 
TRP H    H  N N 389 
TRP H2   H  N N 390 
TRP HA   H  N N 391 
TRP HB2  H  N N 392 
TRP HB3  H  N N 393 
TRP HD1  H  N N 394 
TRP HE1  H  N N 395 
TRP HE3  H  N N 396 
TRP HZ2  H  N N 397 
TRP HZ3  H  N N 398 
TRP HH2  H  N N 399 
TRP HXT  H  N N 400 
TYR N    N  N N 401 
TYR CA   C  N S 402 
TYR C    C  N N 403 
TYR O    O  N N 404 
TYR CB   C  N N 405 
TYR CG   C  Y N 406 
TYR CD1  C  Y N 407 
TYR CD2  C  Y N 408 
TYR CE1  C  Y N 409 
TYR CE2  C  Y N 410 
TYR CZ   C  Y N 411 
TYR OH   O  N N 412 
TYR OXT  O  N N 413 
TYR H    H  N N 414 
TYR H2   H  N N 415 
TYR HA   H  N N 416 
TYR HB2  H  N N 417 
TYR HB3  H  N N 418 
TYR HD1  H  N N 419 
TYR HD2  H  N N 420 
TYR HE1  H  N N 421 
TYR HE2  H  N N 422 
TYR HH   H  N N 423 
TYR HXT  H  N N 424 
VAL N    N  N N 425 
VAL CA   C  N S 426 
VAL C    C  N N 427 
VAL O    O  N N 428 
VAL CB   C  N N 429 
VAL CG1  C  N N 430 
VAL CG2  C  N N 431 
VAL OXT  O  N N 432 
VAL H    H  N N 433 
VAL H2   H  N N 434 
VAL HA   H  N N 435 
VAL HB   H  N N 436 
VAL HG11 H  N N 437 
VAL HG12 H  N N 438 
VAL HG13 H  N N 439 
VAL HG21 H  N N 440 
VAL HG22 H  N N 441 
VAL HG23 H  N N 442 
VAL HXT  H  N N 443 
ZN  ZN   ZN N N 444 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
EOQ CL1 C6   sing N N 92  
EOQ O4  S1   doub N N 93  
EOQ C6  C7   doub Y N 94  
EOQ C6  C2   sing Y N 95  
EOQ C7  C8   sing Y N 96  
EOQ C22 C25  doub Y N 97  
EOQ C22 C20  sing Y N 98  
EOQ C19 C20  sing N N 99  
EOQ C19 N18  sing N N 100 
EOQ C25 C24  sing Y N 101 
EOQ C20 C21  doub Y N 102 
EOQ S1  O3   doub N N 103 
EOQ S1  C2   sing N N 104 
EOQ S1  N5   sing N N 105 
EOQ C2  C10  doub Y N 106 
EOQ C24 C23  doub Y N 107 
EOQ C21 C23  sing Y N 108 
EOQ C8  N18  sing N N 109 
EOQ C8  C9   doub Y N 110 
EOQ C10 C9   sing Y N 111 
EOQ C9  C12  sing N N 112 
EOQ C12 N14  sing N N 113 
EOQ C12 O13  doub N N 114 
EOQ N14 C15  sing N N 115 
EOQ C15 C16  sing N N 116 
EOQ C16 O17  sing N N 117 
EOQ C7  H1   sing N N 118 
EOQ C10 H2   sing N N 119 
EOQ N5  H3   sing N N 120 
EOQ N5  H4   sing N N 121 
EOQ C15 H5   sing N N 122 
EOQ C15 H6   sing N N 123 
EOQ C16 H7   sing N N 124 
EOQ C16 H8   sing N N 125 
EOQ N14 H9   sing N N 126 
EOQ O17 H10  sing N N 127 
EOQ N18 H11  sing N N 128 
EOQ C19 H12  sing N N 129 
EOQ C19 H13  sing N N 130 
EOQ C22 H14  sing N N 131 
EOQ C25 H15  sing N N 132 
EOQ C24 H16  sing N N 133 
EOQ C23 H17  sing N N 134 
EOQ C21 H18  sing N N 135 
GLN N   CA   sing N N 136 
GLN N   H    sing N N 137 
GLN N   H2   sing N N 138 
GLN CA  C    sing N N 139 
GLN CA  CB   sing N N 140 
GLN CA  HA   sing N N 141 
GLN C   O    doub N N 142 
GLN C   OXT  sing N N 143 
GLN CB  CG   sing N N 144 
GLN CB  HB2  sing N N 145 
GLN CB  HB3  sing N N 146 
GLN CG  CD   sing N N 147 
GLN CG  HG2  sing N N 148 
GLN CG  HG3  sing N N 149 
GLN CD  OE1  doub N N 150 
GLN CD  NE2  sing N N 151 
GLN NE2 HE21 sing N N 152 
GLN NE2 HE22 sing N N 153 
GLN OXT HXT  sing N N 154 
GLU N   CA   sing N N 155 
GLU N   H    sing N N 156 
GLU N   H2   sing N N 157 
GLU CA  C    sing N N 158 
GLU CA  CB   sing N N 159 
GLU CA  HA   sing N N 160 
GLU C   O    doub N N 161 
GLU C   OXT  sing N N 162 
GLU CB  CG   sing N N 163 
GLU CB  HB2  sing N N 164 
GLU CB  HB3  sing N N 165 
GLU CG  CD   sing N N 166 
GLU CG  HG2  sing N N 167 
GLU CG  HG3  sing N N 168 
GLU CD  OE1  doub N N 169 
GLU CD  OE2  sing N N 170 
GLU OE2 HE2  sing N N 171 
GLU OXT HXT  sing N N 172 
GLY N   CA   sing N N 173 
GLY N   H    sing N N 174 
GLY N   H2   sing N N 175 
GLY CA  C    sing N N 176 
GLY CA  HA2  sing N N 177 
GLY CA  HA3  sing N N 178 
GLY C   O    doub N N 179 
GLY C   OXT  sing N N 180 
GLY OXT HXT  sing N N 181 
HIS N   CA   sing N N 182 
HIS N   H    sing N N 183 
HIS N   H2   sing N N 184 
HIS CA  C    sing N N 185 
HIS CA  CB   sing N N 186 
HIS CA  HA   sing N N 187 
HIS C   O    doub N N 188 
HIS C   OXT  sing N N 189 
HIS CB  CG   sing N N 190 
HIS CB  HB2  sing N N 191 
HIS CB  HB3  sing N N 192 
HIS CG  ND1  sing Y N 193 
HIS CG  CD2  doub Y N 194 
HIS ND1 CE1  doub Y N 195 
HIS ND1 HD1  sing N N 196 
HIS CD2 NE2  sing Y N 197 
HIS CD2 HD2  sing N N 198 
HIS CE1 NE2  sing Y N 199 
HIS CE1 HE1  sing N N 200 
HIS NE2 HE2  sing N N 201 
HIS OXT HXT  sing N N 202 
HOH O   H1   sing N N 203 
HOH O   H2   sing N N 204 
ILE N   CA   sing N N 205 
ILE N   H    sing N N 206 
ILE N   H2   sing N N 207 
ILE CA  C    sing N N 208 
ILE CA  CB   sing N N 209 
ILE CA  HA   sing N N 210 
ILE C   O    doub N N 211 
ILE C   OXT  sing N N 212 
ILE CB  CG1  sing N N 213 
ILE CB  CG2  sing N N 214 
ILE CB  HB   sing N N 215 
ILE CG1 CD1  sing N N 216 
ILE CG1 HG12 sing N N 217 
ILE CG1 HG13 sing N N 218 
ILE CG2 HG21 sing N N 219 
ILE CG2 HG22 sing N N 220 
ILE CG2 HG23 sing N N 221 
ILE CD1 HD11 sing N N 222 
ILE CD1 HD12 sing N N 223 
ILE CD1 HD13 sing N N 224 
ILE OXT HXT  sing N N 225 
LEU N   CA   sing N N 226 
LEU N   H    sing N N 227 
LEU N   H2   sing N N 228 
LEU CA  C    sing N N 229 
LEU CA  CB   sing N N 230 
LEU CA  HA   sing N N 231 
LEU C   O    doub N N 232 
LEU C   OXT  sing N N 233 
LEU CB  CG   sing N N 234 
LEU CB  HB2  sing N N 235 
LEU CB  HB3  sing N N 236 
LEU CG  CD1  sing N N 237 
LEU CG  CD2  sing N N 238 
LEU CG  HG   sing N N 239 
LEU CD1 HD11 sing N N 240 
LEU CD1 HD12 sing N N 241 
LEU CD1 HD13 sing N N 242 
LEU CD2 HD21 sing N N 243 
LEU CD2 HD22 sing N N 244 
LEU CD2 HD23 sing N N 245 
LEU OXT HXT  sing N N 246 
LYS N   CA   sing N N 247 
LYS N   H    sing N N 248 
LYS N   H2   sing N N 249 
LYS CA  C    sing N N 250 
LYS CA  CB   sing N N 251 
LYS CA  HA   sing N N 252 
LYS C   O    doub N N 253 
LYS C   OXT  sing N N 254 
LYS CB  CG   sing N N 255 
LYS CB  HB2  sing N N 256 
LYS CB  HB3  sing N N 257 
LYS CG  CD   sing N N 258 
LYS CG  HG2  sing N N 259 
LYS CG  HG3  sing N N 260 
LYS CD  CE   sing N N 261 
LYS CD  HD2  sing N N 262 
LYS CD  HD3  sing N N 263 
LYS CE  NZ   sing N N 264 
LYS CE  HE2  sing N N 265 
LYS CE  HE3  sing N N 266 
LYS NZ  HZ1  sing N N 267 
LYS NZ  HZ2  sing N N 268 
LYS NZ  HZ3  sing N N 269 
LYS OXT HXT  sing N N 270 
MET N   CA   sing N N 271 
MET N   H    sing N N 272 
MET N   H2   sing N N 273 
MET CA  C    sing N N 274 
MET CA  CB   sing N N 275 
MET CA  HA   sing N N 276 
MET C   O    doub N N 277 
MET C   OXT  sing N N 278 
MET CB  CG   sing N N 279 
MET CB  HB2  sing N N 280 
MET CB  HB3  sing N N 281 
MET CG  SD   sing N N 282 
MET CG  HG2  sing N N 283 
MET CG  HG3  sing N N 284 
MET SD  CE   sing N N 285 
MET CE  HE1  sing N N 286 
MET CE  HE2  sing N N 287 
MET CE  HE3  sing N N 288 
MET OXT HXT  sing N N 289 
PHE N   CA   sing N N 290 
PHE N   H    sing N N 291 
PHE N   H2   sing N N 292 
PHE CA  C    sing N N 293 
PHE CA  CB   sing N N 294 
PHE CA  HA   sing N N 295 
PHE C   O    doub N N 296 
PHE C   OXT  sing N N 297 
PHE CB  CG   sing N N 298 
PHE CB  HB2  sing N N 299 
PHE CB  HB3  sing N N 300 
PHE CG  CD1  doub Y N 301 
PHE CG  CD2  sing Y N 302 
PHE CD1 CE1  sing Y N 303 
PHE CD1 HD1  sing N N 304 
PHE CD2 CE2  doub Y N 305 
PHE CD2 HD2  sing N N 306 
PHE CE1 CZ   doub Y N 307 
PHE CE1 HE1  sing N N 308 
PHE CE2 CZ   sing Y N 309 
PHE CE2 HE2  sing N N 310 
PHE CZ  HZ   sing N N 311 
PHE OXT HXT  sing N N 312 
PRO N   CA   sing N N 313 
PRO N   CD   sing N N 314 
PRO N   H    sing N N 315 
PRO CA  C    sing N N 316 
PRO CA  CB   sing N N 317 
PRO CA  HA   sing N N 318 
PRO C   O    doub N N 319 
PRO C   OXT  sing N N 320 
PRO CB  CG   sing N N 321 
PRO CB  HB2  sing N N 322 
PRO CB  HB3  sing N N 323 
PRO CG  CD   sing N N 324 
PRO CG  HG2  sing N N 325 
PRO CG  HG3  sing N N 326 
PRO CD  HD2  sing N N 327 
PRO CD  HD3  sing N N 328 
PRO OXT HXT  sing N N 329 
SER N   CA   sing N N 330 
SER N   H    sing N N 331 
SER N   H2   sing N N 332 
SER CA  C    sing N N 333 
SER CA  CB   sing N N 334 
SER CA  HA   sing N N 335 
SER C   O    doub N N 336 
SER C   OXT  sing N N 337 
SER CB  OG   sing N N 338 
SER CB  HB2  sing N N 339 
SER CB  HB3  sing N N 340 
SER OG  HG   sing N N 341 
SER OXT HXT  sing N N 342 
THR N   CA   sing N N 343 
THR N   H    sing N N 344 
THR N   H2   sing N N 345 
THR CA  C    sing N N 346 
THR CA  CB   sing N N 347 
THR CA  HA   sing N N 348 
THR C   O    doub N N 349 
THR C   OXT  sing N N 350 
THR CB  OG1  sing N N 351 
THR CB  CG2  sing N N 352 
THR CB  HB   sing N N 353 
THR OG1 HG1  sing N N 354 
THR CG2 HG21 sing N N 355 
THR CG2 HG22 sing N N 356 
THR CG2 HG23 sing N N 357 
THR OXT HXT  sing N N 358 
TRP N   CA   sing N N 359 
TRP N   H    sing N N 360 
TRP N   H2   sing N N 361 
TRP CA  C    sing N N 362 
TRP CA  CB   sing N N 363 
TRP CA  HA   sing N N 364 
TRP C   O    doub N N 365 
TRP C   OXT  sing N N 366 
TRP CB  CG   sing N N 367 
TRP CB  HB2  sing N N 368 
TRP CB  HB3  sing N N 369 
TRP CG  CD1  doub Y N 370 
TRP CG  CD2  sing Y N 371 
TRP CD1 NE1  sing Y N 372 
TRP CD1 HD1  sing N N 373 
TRP CD2 CE2  doub Y N 374 
TRP CD2 CE3  sing Y N 375 
TRP NE1 CE2  sing Y N 376 
TRP NE1 HE1  sing N N 377 
TRP CE2 CZ2  sing Y N 378 
TRP CE3 CZ3  doub Y N 379 
TRP CE3 HE3  sing N N 380 
TRP CZ2 CH2  doub Y N 381 
TRP CZ2 HZ2  sing N N 382 
TRP CZ3 CH2  sing Y N 383 
TRP CZ3 HZ3  sing N N 384 
TRP CH2 HH2  sing N N 385 
TRP OXT HXT  sing N N 386 
TYR N   CA   sing N N 387 
TYR N   H    sing N N 388 
TYR N   H2   sing N N 389 
TYR CA  C    sing N N 390 
TYR CA  CB   sing N N 391 
TYR CA  HA   sing N N 392 
TYR C   O    doub N N 393 
TYR C   OXT  sing N N 394 
TYR CB  CG   sing N N 395 
TYR CB  HB2  sing N N 396 
TYR CB  HB3  sing N N 397 
TYR CG  CD1  doub Y N 398 
TYR CG  CD2  sing Y N 399 
TYR CD1 CE1  sing Y N 400 
TYR CD1 HD1  sing N N 401 
TYR CD2 CE2  doub Y N 402 
TYR CD2 HD2  sing N N 403 
TYR CE1 CZ   doub Y N 404 
TYR CE1 HE1  sing N N 405 
TYR CE2 CZ   sing Y N 406 
TYR CE2 HE2  sing N N 407 
TYR CZ  OH   sing N N 408 
TYR OH  HH   sing N N 409 
TYR OXT HXT  sing N N 410 
VAL N   CA   sing N N 411 
VAL N   H    sing N N 412 
VAL N   H2   sing N N 413 
VAL CA  C    sing N N 414 
VAL CA  CB   sing N N 415 
VAL CA  HA   sing N N 416 
VAL C   O    doub N N 417 
VAL C   OXT  sing N N 418 
VAL CB  CG1  sing N N 419 
VAL CB  CG2  sing N N 420 
VAL CB  HB   sing N N 421 
VAL CG1 HG11 sing N N 422 
VAL CG1 HG12 sing N N 423 
VAL CG1 HG13 sing N N 424 
VAL CG2 HG21 sing N N 425 
VAL CG2 HG22 sing N N 426 
VAL CG2 HG23 sing N N 427 
VAL OXT HXT  sing N N 428 
# 
_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   5LL9 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    6G7A 
_atom_sites.fract_transf_matrix[1][1]   0.012937 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004434 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013527 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   -0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.011589 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   A SER A  1 2   ? 21.561  15.345  16.968  0.50 30.65 ? 2   SER A N   1 
ATOM   2     N  N   B SER A  1 2   ? 19.120  19.565  16.027  0.50 37.45 ? 2   SER A N   1 
ATOM   3     C  CA  A SER A  1 2   ? 21.262  14.098  17.715  0.50 33.89 ? 2   SER A CA  1 
ATOM   4     C  CA  B SER A  1 2   ? 19.490  18.324  15.284  0.50 32.49 ? 2   SER A CA  1 
ATOM   5     C  C   A SER A  1 2   ? 19.953  14.286  18.453  0.50 32.37 ? 2   SER A C   1 
ATOM   6     C  C   B SER A  1 2   ? 18.870  17.107  15.925  0.50 28.50 ? 2   SER A C   1 
ATOM   7     O  O   A SER A  1 2   ? 19.582  13.449  19.261  0.50 30.21 ? 2   SER A O   1 
ATOM   8     O  O   B SER A  1 2   ? 18.953  16.018  15.397  0.50 25.05 ? 2   SER A O   1 
ATOM   9     C  CB  A SER A  1 2   ? 22.386  13.777  18.683  0.50 33.05 ? 2   SER A CB  1 
ATOM   10    C  CB  B SER A  1 2   ? 21.019  18.168  15.159  0.50 36.11 ? 2   SER A CB  1 
ATOM   11    O  OG  A SER A  1 2   ? 23.245  12.831  18.087  0.50 32.68 ? 2   SER A OG  1 
ATOM   12    O  OG  B SER A  1 2   ? 21.666  18.060  16.427  0.50 39.20 ? 2   SER A OG  1 
ATOM   13    N  N   A LYS A  1 3   ? 19.276  15.415  18.159  0.50 31.31 ? 3   LYS A N   1 
ATOM   14    N  N   B LYS A  1 3   ? 18.186  17.295  17.036  0.50 28.52 ? 3   LYS A N   1 
ATOM   15    C  CA  A LYS A  1 3   ? 17.874  15.714  18.549  0.50 30.06 ? 3   LYS A CA  1 
ATOM   16    C  CA  B LYS A  1 3   ? 17.715  16.142  17.789  0.50 25.62 ? 3   LYS A CA  1 
ATOM   17    C  C   A LYS A  1 3   ? 16.792  14.678  18.151  0.50 26.75 ? 3   LYS A C   1 
ATOM   18    C  C   B LYS A  1 3   ? 16.849  15.225  16.925  0.50 21.70 ? 3   LYS A C   1 
ATOM   19    O  O   A LYS A  1 3   ? 15.721  14.587  18.778  0.50 25.79 ? 3   LYS A O   1 
ATOM   20    O  O   B LYS A  1 3   ? 16.108  15.681  16.040  0.50 21.07 ? 3   LYS A O   1 
ATOM   21    C  CB  A LYS A  1 3   ? 17.463  17.025  17.890  0.50 36.41 ? 3   LYS A CB  1 
ATOM   22    C  CB  B LYS A  1 3   ? 17.032  16.555  19.111  0.50 28.97 ? 3   LYS A CB  1 
ATOM   23    C  CG  A LYS A  1 3   ? 15.990  17.343  18.036  0.50 38.02 ? 3   LYS A CG  1 
ATOM   24    C  CG  B LYS A  1 3   ? 18.015  16.448  20.287  0.50 38.97 ? 3   LYS A CG  1 
ATOM   25    C  CD  A LYS A  1 3   ? 15.666  17.501  19.508  0.50 41.57 ? 3   LYS A CD  1 
ATOM   26    C  CD  B LYS A  1 3   ? 17.940  17.615  21.284  0.50 42.95 ? 3   LYS A CD  1 
ATOM   27    C  CE  A LYS A  1 3   ? 14.445  18.386  19.691  0.50 43.50 ? 3   LYS A CE  1 
ATOM   28    C  CE  B LYS A  1 3   ? 18.945  17.407  22.428  0.50 45.26 ? 3   LYS A CE  1 
ATOM   29    N  NZ  A LYS A  1 3   ? 14.435  19.501  18.696  0.50 47.95 ? 3   LYS A NZ  1 
ATOM   30    N  NZ  B LYS A  1 3   ? 18.575  18.192  23.642  0.50 48.70 ? 3   LYS A NZ  1 
ATOM   31    N  N   . TRP A  1 4   ? 17.082  13.925  17.088  1.00 17.85 ? 4   TRP A N   1 
ATOM   32    C  CA  . TRP A  1 4   ? 16.201  12.911  16.523  1.00 14.33 ? 4   TRP A CA  1 
ATOM   33    C  C   . TRP A  1 4   ? 16.163  11.755  17.522  1.00 13.99 ? 4   TRP A C   1 
ATOM   34    O  O   . TRP A  1 4   ? 17.118  11.490  18.309  1.00 14.30 ? 4   TRP A O   1 
ATOM   35    C  CB  . TRP A  1 4   ? 16.746  12.441  15.176  1.00 13.36 ? 4   TRP A CB  1 
ATOM   36    C  CG  . TRP A  1 4   ? 18.134  11.838  15.174  1.00 11.77 ? 4   TRP A CG  1 
ATOM   37    C  CD1 . TRP A  1 4   ? 19.297  12.437  14.949  1.00 11.96 ? 4   TRP A CD1 1 
ATOM   38    C  CD2 . TRP A  1 4   ? 18.436  10.439  15.274  1.00 10.51 ? 4   TRP A CD2 1 
ATOM   39    N  NE1 . TRP A  1 4   ? 20.345  11.556  14.923  1.00 12.76 ? 4   TRP A NE1 1 
ATOM   40    C  CE2 . TRP A  1 4   ? 19.820  10.281  15.094  1.00 10.50 ? 4   TRP A CE2 1 
ATOM   41    C  CE3 . TRP A  1 4   ? 17.613  9.277   15.392  1.00 9.84  ? 4   TRP A CE3 1 
ATOM   42    C  CZ2 . TRP A  1 4   ? 20.440  9.023   15.122  1.00 10.63 ? 4   TRP A CZ2 1 
ATOM   43    C  CZ3 . TRP A  1 4   ? 18.237  8.020   15.421  1.00 10.23 ? 4   TRP A CZ3 1 
ATOM   44    C  CH2 . TRP A  1 4   ? 19.619  7.903   15.275  1.00 9.74  ? 4   TRP A CH2 1 
ATOM   45    N  N   . THR A  1 5   ? 15.060  11.044  17.506  1.00 12.81 ? 5   THR A N   1 
ATOM   46    C  CA  . THR A  1 5   ? 14.820  9.892   18.427  1.00 12.91 ? 5   THR A CA  1 
ATOM   47    C  C   . THR A  1 5   ? 14.090  8.795   17.676  1.00 11.82 ? 5   THR A C   1 
ATOM   48    O  O   . THR A  1 5   ? 13.845  8.884   16.442  1.00 11.70 ? 5   THR A O   1 
ATOM   49    C  CB  . THR A  1 5   ? 13.916  10.239  19.635  1.00 14.82 ? 5   THR A CB  1 
ATOM   50    O  OG1 . THR A  1 5   ? 12.634  10.537  19.052  1.00 17.54 ? 5   THR A OG1 1 
ATOM   51    C  CG2 . THR A  1 5   ? 14.425  11.501  20.364  1.00 17.58 ? 5   THR A CG2 1 
ATOM   52    N  N   . TYR A  1 6   ? 13.680  7.707   18.350  1.00 12.34 ? 6   TYR A N   1 
ATOM   53    C  CA  . TYR A  1 6   ? 12.902  6.636   17.715  1.00 12.60 ? 6   TYR A CA  1 
ATOM   54    C  C   . TYR A  1 6   ? 11.454  6.609   18.338  1.00 12.98 ? 6   TYR A C   1 
ATOM   55    O  O   . TYR A  1 6   ? 10.644  5.734   18.175  1.00 14.74 ? 6   TYR A O   1 
ATOM   56    C  CB  . TYR A  1 6   ? 13.501  5.251   17.929  1.00 12.34 ? 6   TYR A CB  1 
ATOM   57    C  CG  . TYR A  1 6   ? 14.786  5.023   17.178  1.00 11.45 ? 6   TYR A CG  1 
ATOM   58    C  CD1 . TYR A  1 6   ? 16.021  5.361   17.731  1.00 10.30 ? 6   TYR A CD1 1 
ATOM   59    C  CD2 . TYR A  1 6   ? 14.765  4.437   15.919  1.00 10.66 ? 6   TYR A CD2 1 
ATOM   60    C  CE1 . TYR A  1 6   ? 17.194  5.120   17.035  1.00 11.21 ? 6   TYR A CE1 1 
ATOM   61    C  CE2 . TYR A  1 6   ? 15.928  4.197   15.228  1.00 9.95  ? 6   TYR A CE2 1 
ATOM   62    C  CZ  . TYR A  1 6   ? 17.134  4.536   15.783  1.00 9.70  ? 6   TYR A CZ  1 
ATOM   63    O  OH  . TYR A  1 6   ? 18.264  4.273   15.048  1.00 11.15 ? 6   TYR A OH  1 
ATOM   64    N  N   . PHE A  1 7   ? 11.146  7.659   19.137  1.00 21.47 ? 7   PHE A N   1 
ATOM   65    C  CA  . PHE A  1 7   ? 9.836   7.709   19.839  1.00 25.82 ? 7   PHE A CA  1 
ATOM   66    C  C   . PHE A  1 7   ? 9.472   9.152   20.132  1.00 28.90 ? 7   PHE A C   1 
ATOM   67    O  O   . PHE A  1 7   ? 10.336  9.911   20.661  1.00 31.26 ? 7   PHE A O   1 
ATOM   68    C  CB  . PHE A  1 7   ? 9.920   6.963   21.201  1.00 33.43 ? 7   PHE A CB  1 
ATOM   69    C  CG  . PHE A  1 7   ? 8.620   7.010   22.036  1.00 46.32 ? 7   PHE A CG  1 
ATOM   70    C  CD1 . PHE A  1 7   ? 8.350   8.093   22.925  1.00 51.08 ? 7   PHE A CD1 1 
ATOM   71    C  CD2 . PHE A  1 7   ? 7.663   5.958   21.954  1.00 49.40 ? 7   PHE A CD2 1 
ATOM   72    C  CE1 . PHE A  1 7   ? 7.163   8.128   23.679  1.00 45.44 ? 7   PHE A CE1 1 
ATOM   73    C  CE2 . PHE A  1 7   ? 6.488   5.997   22.717  1.00 40.86 ? 7   PHE A CE2 1 
ATOM   74    C  CZ  . PHE A  1 7   ? 6.239   7.084   23.566  1.00 53.28 ? 7   PHE A CZ  1 
ATOM   75    N  N   . GLY A  1 8   ? 8.198   9.478   19.907  1.00 24.81 ? 8   GLY A N   1 
ATOM   76    C  CA  . GLY A  1 8   ? 7.586   10.815  20.290  1.00 25.75 ? 8   GLY A CA  1 
ATOM   77    C  C   . GLY A  1 8   ? 7.753   11.740  19.075  1.00 29.72 ? 8   GLY A C   1 
ATOM   78    O  O   . GLY A  1 8   ? 7.928   11.262  17.941  1.00 29.79 ? 8   GLY A O   1 
ATOM   79    N  N   . PRO A  1 9   ? 7.748   13.038  19.278  1.00 22.91 ? 9   PRO A N   1 
ATOM   80    C  CA  . PRO A  1 9   ? 7.642   13.989  18.164  1.00 22.03 ? 9   PRO A CA  1 
ATOM   81    C  C   . PRO A  1 9   ? 8.806   14.056  17.234  1.00 22.09 ? 9   PRO A C   1 
ATOM   82    O  O   . PRO A  1 9   ? 8.673   14.521  16.142  1.00 19.34 ? 9   PRO A O   1 
ATOM   83    C  CB  . PRO A  1 9   ? 7.621   15.370  18.886  1.00 27.74 ? 9   PRO A CB  1 
ATOM   84    C  CG  . PRO A  1 9   ? 7.213   15.091  20.244  1.00 26.28 ? 9   PRO A CG  1 
ATOM   85    C  CD  . PRO A  1 9   ? 7.561   13.714  20.592  1.00 23.93 ? 9   PRO A CD  1 
ATOM   86    N  N   . ASP A  1 10  ? 9.973   13.568  17.707  1.00 18.64 ? 10  ASP A N   1 
ATOM   87    C  CA  . ASP A  1 10  ? 11.146  13.636  16.942  1.00 16.35 ? 10  ASP A CA  1 
ATOM   88    C  C   . ASP A  1 10  ? 11.577  12.268  16.402  1.00 14.98 ? 10  ASP A C   1 
ATOM   89    O  O   . ASP A  1 10  ? 12.768  12.082  16.032  1.00 14.46 ? 10  ASP A O   1 
ATOM   90    C  CB  . ASP A  1 10  ? 12.311  14.231  17.834  1.00 19.24 ? 10  ASP A CB  1 
ATOM   91    C  CG  . ASP A  1 10  ? 12.072  15.706  18.254  1.00 23.87 ? 10  ASP A CG  1 
ATOM   92    O  OD1 . ASP A  1 10  ? 11.637  16.511  17.388  1.00 28.42 ? 10  ASP A OD1 1 
ATOM   93    O  OD2 . ASP A  1 10  ? 12.254  15.954  19.495  1.00 30.46 ? 10  ASP A OD2 1 
ATOM   94    N  N   . GLY A  1 11  ? 10.584  11.372  16.359  1.00 16.05 ? 11  GLY A N   1 
ATOM   95    C  CA  . GLY A  1 11  ? 10.746  9.959   15.860  1.00 13.01 ? 11  GLY A CA  1 
ATOM   96    C  C   . GLY A  1 11  ? 10.810  9.922   14.355  1.00 12.16 ? 11  GLY A C   1 
ATOM   97    O  O   . GLY A  1 11  ? 10.881  10.939  13.654  1.00 11.76 ? 11  GLY A O   1 
ATOM   98    N  N   . GLU A  1 12  ? 10.897  8.688   13.838  1.00 9.75  ? 12  GLU A N   1 
ATOM   99    C  CA  . GLU A  1 12  ? 11.302  8.480   12.486  1.00 9.02  ? 12  GLU A CA  1 
ATOM   100   C  C   . GLU A  1 12  ? 10.436  9.152   11.374  1.00 9.00  ? 12  GLU A C   1 
ATOM   101   O  O   . GLU A  1 12  ? 10.965  9.474   10.336  1.00 8.99  ? 12  GLU A O   1 
ATOM   102   C  CB  . GLU A  1 12  ? 11.487  6.953   12.174  1.00 9.69  ? 12  GLU A CB  1 
ATOM   103   C  CG  . GLU A  1 12  ? 10.158  6.171   12.145  1.00 9.08  ? 12  GLU A CG  1 
ATOM   104   C  CD  . GLU A  1 12  ? 10.497  4.693   12.301  1.00 9.37  ? 12  GLU A CD  1 
ATOM   105   O  OE1 . GLU A  1 12  ? 10.745  4.067   11.298  1.00 9.08  ? 12  GLU A OE1 1 
ATOM   106   O  OE2 . GLU A  1 12  ? 10.412  4.266   13.453  1.00 11.07 ? 12  GLU A OE2 1 
ATOM   107   N  N   . ASN A  1 13  ? 9.140   9.328   11.653  1.00 9.25  ? 13  ASN A N   1 
ATOM   108   C  CA  . ASN A  1 13  ? 8.329   9.990   10.629  1.00 9.15  ? 13  ASN A CA  1 
ATOM   109   C  C   . ASN A  1 13  ? 8.651   11.455  10.495  1.00 10.31 ? 13  ASN A C   1 
ATOM   110   O  O   . ASN A  1 13  ? 8.262   12.009  9.475   1.00 10.71 ? 13  ASN A O   1 
ATOM   111   C  CB  . ASN A  1 13  ? 6.840   9.848   10.940  1.00 9.57  ? 13  ASN A CB  1 
ATOM   112   C  CG  . ASN A  1 13  ? 6.332   8.424   10.778  1.00 10.00 ? 13  ASN A CG  1 
ATOM   113   O  OD1 . ASN A  1 13  ? 7.006   7.551   10.235  1.00 11.19 ? 13  ASN A OD1 1 
ATOM   114   N  ND2 . ASN A  1 13  ? 5.148   8.216   11.289  1.00 10.22 ? 13  ASN A ND2 1 
ATOM   115   N  N   . SER A  1 14  ? 9.316   12.029  11.472  1.00 10.04 ? 14  SER A N   1 
ATOM   116   C  CA  . SER A  1 14  ? 9.752   13.460  11.462  1.00 9.98  ? 14  SER A CA  1 
ATOM   117   C  C   . SER A  1 14  ? 11.228  13.653  11.074  1.00 10.63 ? 14  SER A C   1 
ATOM   118   O  O   . SER A  1 14  ? 11.635  14.801  10.902  1.00 11.26 ? 14  SER A O   1 
ATOM   119   C  CB  . SER A  1 14  ? 9.614   14.074  12.843  1.00 12.02 ? 14  SER A CB  1 
ATOM   120   O  OG  . SER A  1 14  ? 8.171   14.146  13.092  1.00 18.21 ? 14  SER A OG  1 
ATOM   121   N  N   . TRP A  1 15  ? 11.988  12.579  10.884  1.00 9.77  ? 15  TRP A N   1 
ATOM   122   C  CA  . TRP A  1 15  ? 13.392  12.785  10.553  1.00 9.31  ? 15  TRP A CA  1 
ATOM   123   C  C   . TRP A  1 15  ? 13.581  13.613  9.266   1.00 10.42 ? 15  TRP A C   1 
ATOM   124   O  O   . TRP A  1 15  ? 14.538  14.390  9.159   1.00 10.15 ? 15  TRP A O   1 
ATOM   125   C  CB  . TRP A  1 15  ? 14.103  11.410  10.351  1.00 9.84  ? 15  TRP A CB  1 
ATOM   126   C  CG  . TRP A  1 15  ? 14.264  10.591  11.585  1.00 8.97  ? 15  TRP A CG  1 
ATOM   127   C  CD1 . TRP A  1 15  ? 13.992  10.911  12.863  1.00 9.64  ? 15  TRP A CD1 1 
ATOM   128   C  CD2 . TRP A  1 15  ? 14.672  9.217   11.578  1.00 8.37  ? 15  TRP A CD2 1 
ATOM   129   N  NE1 . TRP A  1 15  ? 14.312  9.823   13.697  1.00 9.92  ? 15  TRP A NE1 1 
ATOM   130   C  CE2 . TRP A  1 15  ? 14.735  8.797   12.904  1.00 8.05  ? 15  TRP A CE2 1 
ATOM   131   C  CE3 . TRP A  1 15  ? 15.128  8.375   10.568  1.00 7.77  ? 15  TRP A CE3 1 
ATOM   132   C  CZ2 . TRP A  1 15  ? 15.182  7.476   13.249  1.00 7.61  ? 15  TRP A CZ2 1 
ATOM   133   C  CZ3 . TRP A  1 15  ? 15.545  7.074   10.900  1.00 7.79  ? 15  TRP A CZ3 1 
ATOM   134   C  CH2 . TRP A  1 15  ? 15.564  6.673   12.204  1.00 7.97  ? 15  TRP A CH2 1 
ATOM   135   N  N   . SER A  1 16  ? 12.690  13.489  8.301   1.00 9.43  ? 16  SER A N   1 
ATOM   136   C  CA  . SER A  1 16  ? 12.873  14.124  7.025   1.00 9.78  ? 16  SER A CA  1 
ATOM   137   C  C   . SER A  1 16  ? 12.747  15.656  7.160   1.00 9.83  ? 16  SER A C   1 
ATOM   138   O  O   . SER A  1 16  ? 13.195  16.309  6.165   1.00 9.55  ? 16  SER A O   1 
ATOM   139   C  CB  . SER A  1 16  ? 11.805  13.667  6.021   1.00 9.75  ? 16  SER A CB  1 
ATOM   140   O  OG  . SER A  1 16  ? 10.497  14.039  6.544   1.00 10.56 ? 16  SER A OG  1 
ATOM   141   N  N   A LYS A  1 17  ? 12.182  16.181  8.229   0.50 9.53  ? 17  LYS A N   1 
ATOM   142   N  N   B LYS A  1 17  ? 12.241  16.143  8.315   0.50 10.35 ? 17  LYS A N   1 
ATOM   143   C  CA  A LYS A  1 17  ? 12.188  17.660  8.289   0.50 9.32  ? 17  LYS A CA  1 
ATOM   144   C  CA  B LYS A  1 17  ? 12.179  17.624  8.531   0.50 11.01 ? 17  LYS A CA  1 
ATOM   145   C  C   A LYS A  1 17  ? 13.681  18.182  8.285   0.50 9.58  ? 17  LYS A C   1 
ATOM   146   C  C   B LYS A  1 17  ? 13.546  18.276  8.571   0.50 11.30 ? 17  LYS A C   1 
ATOM   147   O  O   A LYS A  1 17  ? 14.122  19.023  7.400   0.50 8.21  ? 17  LYS A O   1 
ATOM   148   O  O   B LYS A  1 17  ? 13.712  19.314  7.973   0.50 10.60 ? 17  LYS A O   1 
ATOM   149   C  CB  A LYS A  1 17  ? 11.431  18.079  9.533   0.50 9.39  ? 17  LYS A CB  1 
ATOM   150   C  CB  B LYS A  1 17  ? 11.444  17.978  9.781   0.50 12.88 ? 17  LYS A CB  1 
ATOM   151   C  CG  A LYS A  1 17  ? 10.027  17.514  9.795   0.50 10.90 ? 17  LYS A CG  1 
ATOM   152   C  CG  B LYS A  1 17  ? 9.991   18.234  9.543   0.50 15.39 ? 17  LYS A CG  1 
ATOM   153   C  CD  A LYS A  1 17  ? 9.436   17.830  11.163  0.50 12.21 ? 17  LYS A CD  1 
ATOM   154   C  CD  B LYS A  1 17  ? 9.258   18.207  10.876  0.50 19.20 ? 17  LYS A CD  1 
ATOM   155   C  CE  A LYS A  1 17  ? 8.032   17.157  11.326  0.50 12.79 ? 17  LYS A CE  1 
ATOM   156   C  CE  B LYS A  1 17  ? 7.970   17.416  10.706  0.50 20.50 ? 17  LYS A CE  1 
ATOM   157   N  NZ  A LYS A  1 17  ? 7.449   17.318  12.693  0.50 12.48 ? 17  LYS A NZ  1 
ATOM   158   N  NZ  B LYS A  1 17  ? 8.392   16.160  10.080  0.50 21.46 ? 17  LYS A NZ  1 
ATOM   159   N  N   A LYS A  1 18  ? 14.442  17.710  9.273   0.50 9.97  ? 18  LYS A N   1 
ATOM   160   N  N   B LYS A  1 18  ? 14.494  17.686  9.300   0.50 10.47 ? 18  LYS A N   1 
ATOM   161   C  CA  A LYS A  1 18  ? 15.808  18.208  9.423   0.50 11.23 ? 18  LYS A CA  1 
ATOM   162   C  CA  B LYS A  1 18  ? 15.888  18.187  9.356   0.50 10.75 ? 18  LYS A CA  1 
ATOM   163   C  C   A LYS A  1 18  ? 16.860  17.414  8.637   0.50 10.66 ? 18  LYS A C   1 
ATOM   164   C  C   B LYS A  1 18  ? 16.830  17.478  8.367   0.50 10.54 ? 18  LYS A C   1 
ATOM   165   O  O   A LYS A  1 18  ? 18.043  17.854  8.553   0.50 11.71 ? 18  LYS A O   1 
ATOM   166   O  O   B LYS A  1 18  ? 17.886  17.966  7.886   0.50 10.98 ? 18  LYS A O   1 
ATOM   167   C  CB  A LYS A  1 18  ? 16.195  18.299  10.920  0.50 13.93 ? 18  LYS A CB  1 
ATOM   168   C  CB  B LYS A  1 18  ? 16.435  17.916  10.772  0.50 11.62 ? 18  LYS A CB  1 
ATOM   169   C  CG  A LYS A  1 18  ? 15.367  19.344  11.666  0.50 17.89 ? 18  LYS A CG  1 
ATOM   170   C  CG  B LYS A  1 18  ? 17.832  18.470  11.002  0.50 14.06 ? 18  LYS A CG  1 
ATOM   171   C  CD  A LYS A  1 18  ? 15.890  19.714  13.036  0.50 21.36 ? 18  LYS A CD  1 
ATOM   172   C  CD  B LYS A  1 18  ? 18.196  18.254  12.441  0.50 17.76 ? 18  LYS A CD  1 
ATOM   173   C  CE  A LYS A  1 18  ? 16.713  21.014  12.963  0.50 25.72 ? 18  LYS A CE  1 
ATOM   174   C  CE  B LYS A  1 18  ? 19.630  18.615  12.637  0.50 19.81 ? 18  LYS A CE  1 
ATOM   175   N  NZ  A LYS A  1 18  ? 15.954  22.210  12.471  0.50 28.49 ? 18  LYS A NZ  1 
ATOM   176   N  NZ  B LYS A  1 18  ? 19.372  19.958  13.178  0.50 23.26 ? 18  LYS A NZ  1 
ATOM   177   N  N   . TYR A  1 19  ? 16.487  16.232  8.079   1.00 10.46 ? 19  TYR A N   1 
ATOM   178   C  CA  . TYR A  1 19  ? 17.345  15.337  7.313   1.00 9.90  ? 19  TYR A CA  1 
ATOM   179   C  C   . TYR A  1 19  ? 16.632  14.948  6.057   1.00 10.42 ? 19  TYR A C   1 
ATOM   180   O  O   . TYR A  1 19  ? 16.000  13.864  6.035   1.00 9.51  ? 19  TYR A O   1 
ATOM   181   C  CB  . TYR A  1 19  ? 17.701  14.114  8.185   1.00 10.48 ? 19  TYR A CB  1 
ATOM   182   C  CG  . TYR A  1 19  ? 18.359  14.487  9.491   1.00 10.52 ? 19  TYR A CG  1 
ATOM   183   C  CD1 . TYR A  1 19  ? 19.744  14.789  9.498   1.00 11.85 ? 19  TYR A CD1 1 
ATOM   184   C  CD2 . TYR A  1 19  ? 17.646  14.531  10.648  1.00 10.63 ? 19  TYR A CD2 1 
ATOM   185   C  CE1 . TYR A  1 19  ? 20.384  15.105  10.717  1.00 12.01 ? 19  TYR A CE1 1 
ATOM   186   C  CE2 . TYR A  1 19  ? 18.263  14.824  11.864  1.00 11.38 ? 19  TYR A CE2 1 
ATOM   187   C  CZ  . TYR A  1 19  ? 19.618  15.106  11.851  1.00 12.02 ? 19  TYR A CZ  1 
ATOM   188   O  OH  . TYR A  1 19  ? 20.264  15.450  13.104  1.00 16.99 ? 19  TYR A OH  1 
ATOM   189   N  N   . PRO A  1 20  ? 16.687  15.739  4.997   1.00 9.47  ? 20  PRO A N   1 
ATOM   190   C  CA  . PRO A  1 20  ? 15.751  15.558  3.924   1.00 9.29  ? 20  PRO A CA  1 
ATOM   191   C  C   . PRO A  1 20  ? 16.011  14.222  3.272   1.00 10.48 ? 20  PRO A C   1 
ATOM   192   O  O   . PRO A  1 20  ? 15.090  13.656  2.619   1.00 11.09 ? 20  PRO A O   1 
ATOM   193   C  CB  . PRO A  1 20  ? 16.042  16.721  2.928   1.00 12.30 ? 20  PRO A CB  1 
ATOM   194   C  CG  . PRO A  1 20  ? 16.752  17.706  3.743   1.00 12.58 ? 20  PRO A CG  1 
ATOM   195   C  CD  . PRO A  1 20  ? 17.436  17.027  4.907   1.00 10.64 ? 20  PRO A CD  1 
ATOM   196   N  N   . SER A  1 21  ? 17.225  13.609  3.270   1.00 8.80  ? 21  SER A N   1 
ATOM   197   C  CA  . SER A  1 21  ? 17.385  12.305  2.626   1.00 8.66  ? 21  SER A CA  1 
ATOM   198   C  C   . SER A  1 21  ? 16.523  11.206  3.272   1.00 8.45  ? 21  SER A C   1 
ATOM   199   O  O   . SER A  1 21  ? 16.294  10.197  2.574   1.00 8.32  ? 21  SER A O   1 
ATOM   200   C  CB  . SER A  1 21  ? 18.930  11.906  2.653   1.00 10.12 ? 21  SER A CB  1 
ATOM   201   O  OG  . SER A  1 21  ? 19.639  12.755  1.702   1.00 12.38 ? 21  SER A OG  1 
ATOM   202   N  N   . CYS A  1 22  ? 16.079  11.413  4.510   1.00 8.25  ? 22  CYS A N   1 
ATOM   203   C  CA  . CYS A  1 22  ? 15.205  10.435  5.146   1.00 8.73  ? 22  CYS A CA  1 
ATOM   204   C  C   . CYS A  1 22  ? 13.889  10.265  4.426   1.00 10.42 ? 22  CYS A C   1 
ATOM   205   O  O   . CYS A  1 22  ? 13.224  9.252   4.670   1.00 10.51 ? 22  CYS A O   1 
ATOM   206   C  CB  . CYS A  1 22  ? 15.024  10.753  6.608   1.00 8.45  ? 22  CYS A CB  1 
ATOM   207   S  SG  . CYS A  1 22  ? 16.618  10.738  7.550   1.00 10.32 ? 22  CYS A SG  1 
ATOM   208   N  N   . GLY A  1 23  ? 13.513  11.254  3.597   1.00 11.52 ? 23  GLY A N   1 
ATOM   209   C  CA  . GLY A  1 23  ? 12.344  11.142  2.705   1.00 11.11 ? 23  GLY A CA  1 
ATOM   210   C  C   . GLY A  1 23  ? 12.659  10.948  1.319   1.00 10.46 ? 23  GLY A C   1 
ATOM   211   O  O   . GLY A  1 23  ? 11.742  11.005  0.483   1.00 11.16 ? 23  GLY A O   1 
ATOM   212   N  N   . GLY A  1 24  ? 13.878  10.651  0.965   1.00 10.57 ? 24  GLY A N   1 
ATOM   213   C  CA  . GLY A  1 24  ? 14.357  10.418  -0.408  1.00 10.80 ? 24  GLY A CA  1 
ATOM   214   C  C   . GLY A  1 24  ? 14.413  9.009   -0.876  1.00 11.00 ? 24  GLY A C   1 
ATOM   215   O  O   . GLY A  1 24  ? 13.693  8.184   -0.246  1.00 12.89 ? 24  GLY A O   1 
ATOM   216   N  N   . LEU A  1 25  ? 15.148  8.760   -1.921  1.00 11.60 ? 25  LEU A N   1 
ATOM   217   C  CA  . LEU A  1 25  ? 15.282  7.460   -2.487  1.00 13.27 ? 25  LEU A CA  1 
ATOM   218   C  C   . LEU A  1 25  ? 16.197  6.534   -1.703  1.00 14.21 ? 25  LEU A C   1 
ATOM   219   O  O   . LEU A  1 25  ? 17.006  6.930   -0.870  1.00 12.27 ? 25  LEU A O   1 
ATOM   220   C  CB  . LEU A  1 25  ? 15.808  7.600   -3.911  1.00 16.92 ? 25  LEU A CB  1 
ATOM   221   C  CG  . LEU A  1 25  ? 14.900  8.487   -4.837  1.00 19.79 ? 25  LEU A CG  1 
ATOM   222   C  CD1 . LEU A  1 25  ? 15.633  8.707   -6.144  1.00 25.67 ? 25  LEU A CD1 1 
ATOM   223   C  CD2 . LEU A  1 25  ? 13.502  7.913   -5.051  1.00 20.83 ? 25  LEU A CD2 1 
ATOM   224   N  N   . LEU A  1 26  ? 16.024  5.265   -2.045  1.00 12.58 ? 26  LEU A N   1 
ATOM   225   C  CA  . LEU A  1 26  ? 17.003  4.185   -1.748  1.00 14.02 ? 26  LEU A CA  1 
ATOM   226   C  C   . LEU A  1 26  ? 17.011  3.987   -0.184  1.00 13.16 ? 26  LEU A C   1 
ATOM   227   O  O   . LEU A  1 26  ? 18.025  3.609   0.358   1.00 13.23 ? 26  LEU A O   1 
ATOM   228   C  CB  . LEU A  1 26  ? 18.430  4.355   -2.283  1.00 14.86 ? 26  LEU A CB  1 
ATOM   229   C  CG  . LEU A  1 26  ? 18.596  4.314   -3.835  1.00 21.14 ? 26  LEU A CG  1 
ATOM   230   C  CD1 . LEU A  1 26  ? 20.087  4.407   -4.186  1.00 21.74 ? 26  LEU A CD1 1 
ATOM   231   C  CD2 . LEU A  1 26  ? 18.081  3.060   -4.496  1.00 21.27 ? 26  LEU A CD2 1 
ATOM   232   N  N   . GLN A  1 27  ? 15.911  4.186   0.518   1.00 9.46  ? 27  GLN A N   1 
ATOM   233   C  CA  . GLN A  1 27  ? 15.966  4.069   2.002   1.00 8.74  ? 27  GLN A CA  1 
ATOM   234   C  C   . GLN A  1 27  ? 15.965  2.639   2.504   1.00 8.89  ? 27  GLN A C   1 
ATOM   235   O  O   . GLN A  1 27  ? 15.358  1.738   1.957   1.00 10.81 ? 27  GLN A O   1 
ATOM   236   C  CB  . GLN A  1 27  ? 14.803  4.794   2.633   1.00 8.98  ? 27  GLN A CB  1 
ATOM   237   C  CG  . GLN A  1 27  ? 14.893  6.285   2.344   1.00 8.84  ? 27  GLN A CG  1 
ATOM   238   C  CD  . GLN A  1 27  ? 16.052  6.934   3.022   1.00 7.09  ? 27  GLN A CD  1 
ATOM   239   O  OE1 . GLN A  1 27  ? 16.020  7.142   4.229   1.00 8.49  ? 27  GLN A OE1 1 
ATOM   240   N  NE2 . GLN A  1 27  ? 17.067  7.216   2.267   1.00 8.20  ? 27  GLN A NE2 1 
ATOM   241   N  N   . SER A  1 28  ? 16.740  2.459   3.556   1.00 7.53  ? 28  SER A N   1 
ATOM   242   C  CA  . SER A  1 28  ? 16.849  1.200   4.325   1.00 7.55  ? 28  SER A CA  1 
ATOM   243   C  C   . SER A  1 28  ? 16.277  1.380   5.702   1.00 9.06  ? 28  SER A C   1 
ATOM   244   O  O   . SER A  1 28  ? 16.151  2.529   6.199   1.00 8.23  ? 28  SER A O   1 
ATOM   245   C  CB  . SER A  1 28  ? 18.340  0.942   4.450   1.00 8.54  ? 28  SER A CB  1 
ATOM   246   O  OG  . SER A  1 28  ? 18.925  0.653   3.202   1.00 8.09  ? 28  SER A OG  1 
ATOM   247   N  N   . PRO A  1 29  ? 15.892  0.319   6.419   1.00 8.36  ? 29  PRO A N   1 
ATOM   248   C  CA  . PRO A  1 29  ? 16.011  -1.063  6.031   1.00 8.33  ? 29  PRO A CA  1 
ATOM   249   C  C   . PRO A  1 29  ? 14.803  -1.499  5.232   1.00 7.61  ? 29  PRO A C   1 
ATOM   250   O  O   . PRO A  1 29  ? 13.856  -0.722  5.049   1.00 8.42  ? 29  PRO A O   1 
ATOM   251   C  CB  . PRO A  1 29  ? 16.049  -1.786  7.441   1.00 7.93  ? 29  PRO A CB  1 
ATOM   252   C  CG  . PRO A  1 29  ? 15.042  -0.973  8.214   1.00 7.72  ? 29  PRO A CG  1 
ATOM   253   C  CD  . PRO A  1 29  ? 15.353  0.517   7.803   1.00 8.08  ? 29  PRO A CD  1 
ATOM   254   N  N   . ILE A  1 30  ? 14.835  -2.771  4.799   1.00 8.24  ? 30  ILE A N   1 
ATOM   255   C  CA  . ILE A  1 30  ? 13.790  -3.343  3.951   1.00 8.73  ? 30  ILE A CA  1 
ATOM   256   C  C   . ILE A  1 30  ? 13.530  -4.791  4.392   1.00 9.97  ? 30  ILE A C   1 
ATOM   257   O  O   . ILE A  1 30  ? 14.306  -5.396  5.162   1.00 10.01 ? 30  ILE A O   1 
ATOM   258   C  CB  . ILE A  1 30  ? 14.237  -3.374  2.471   1.00 9.78  ? 30  ILE A CB  1 
ATOM   259   C  CG1 . ILE A  1 30  ? 15.542  -4.168  2.293   1.00 10.15 ? 30  ILE A CG1 1 
ATOM   260   C  CG2 . ILE A  1 30  ? 14.455  -1.890  1.999   1.00 10.67 ? 30  ILE A CG2 1 
ATOM   261   C  CD1 . ILE A  1 30  ? 15.837  -4.427  0.800   1.00 13.76 ? 30  ILE A CD1 1 
ATOM   262   N  N   . ASP A  1 31  ? 12.394  -5.288  3.969   1.00 9.62  ? 31  ASP A N   1 
ATOM   263   C  CA  . ASP A  1 31  ? 12.069  -6.681  4.125   1.00 10.10 ? 31  ASP A CA  1 
ATOM   264   C  C   . ASP A  1 31  ? 12.673  -7.440  3.004   1.00 10.42 ? 31  ASP A C   1 
ATOM   265   O  O   . ASP A  1 31  ? 12.539  -7.190  1.793   1.00 12.81 ? 31  ASP A O   1 
ATOM   266   C  CB  . ASP A  1 31  ? 10.564  -6.862  4.039   1.00 10.87 ? 31  ASP A CB  1 
ATOM   267   C  CG  . ASP A  1 31  ? 10.161  -8.286  4.314   1.00 14.35 ? 31  ASP A CG  1 
ATOM   268   O  OD1 . ASP A  1 31  ? 10.667  -8.958  5.214   1.00 11.69 ? 31  ASP A OD1 1 
ATOM   269   O  OD2 . ASP A  1 31  ? 9.141   -8.678  3.651   1.00 17.51 ? 31  ASP A OD2 1 
ATOM   270   N  N   . LEU A  1 32  ? 13.399  -8.455  3.388   1.00 10.55 ? 32  LEU A N   1 
ATOM   271   C  CA  . LEU A  1 32  ? 14.029  -9.408  2.460   1.00 12.62 ? 32  LEU A CA  1 
ATOM   272   C  C   . LEU A  1 32  ? 13.137  -10.633 2.261   1.00 12.25 ? 32  LEU A C   1 
ATOM   273   O  O   . LEU A  1 32  ? 12.960  -11.401 3.179   1.00 13.76 ? 32  LEU A O   1 
ATOM   274   C  CB  . LEU A  1 32  ? 15.396  -9.852  3.059   1.00 11.84 ? 32  LEU A CB  1 
ATOM   275   C  CG  . LEU A  1 32  ? 16.285  -8.658  3.483   1.00 11.54 ? 32  LEU A CG  1 
ATOM   276   C  CD1 . LEU A  1 32  ? 17.518  -9.120  4.297   1.00 12.41 ? 32  LEU A CD1 1 
ATOM   277   C  CD2 . LEU A  1 32  ? 16.811  -7.933  2.240   1.00 14.63 ? 32  LEU A CD2 1 
ATOM   278   N  N   . HIS A  1 33  ? 12.535  -10.729 1.094   1.00 16.35 ? 33  HIS A N   1 
ATOM   279   C  CA  . HIS A  1 33  ? 11.566  -11.827 0.916   1.00 18.77 ? 33  HIS A CA  1 
ATOM   280   C  C   . HIS A  1 33  ? 11.685  -12.369 -0.461  1.00 21.48 ? 33  HIS A C   1 
ATOM   281   O  O   . HIS A  1 33  ? 12.173  -11.652 -1.319  1.00 22.42 ? 33  HIS A O   1 
ATOM   282   C  CB  . HIS A  1 33  ? 10.144  -11.319 1.264   1.00 21.55 ? 33  HIS A CB  1 
ATOM   283   C  CG  . HIS A  1 33  ? 9.630   -10.235 0.357   1.00 25.36 ? 33  HIS A CG  1 
ATOM   284   N  ND1 . HIS A  1 33  ? 9.922   -8.895  0.527   1.00 25.48 ? 33  HIS A ND1 1 
ATOM   285   C  CD2 . HIS A  1 33  ? 8.877   -10.325 -0.774  1.00 25.77 ? 33  HIS A CD2 1 
ATOM   286   C  CE1 . HIS A  1 33  ? 9.358   -8.199  -0.463  1.00 29.92 ? 33  HIS A CE1 1 
ATOM   287   N  NE2 . HIS A  1 33  ? 8.756   -9.046  -1.277  1.00 29.97 ? 33  HIS A NE2 1 
ATOM   288   N  N   . SER A  1 34  ? 11.169  -13.575 -0.694  1.00 20.77 ? 34  SER A N   1 
ATOM   289   C  CA  . SER A  1 34  ? 11.588  -14.384 -1.841  1.00 25.05 ? 34  SER A CA  1 
ATOM   290   C  C   . SER A  1 34  ? 11.277  -13.756 -3.184  1.00 27.28 ? 34  SER A C   1 
ATOM   291   O  O   . SER A  1 34  ? 12.108  -13.887 -4.059  1.00 29.68 ? 34  SER A O   1 
ATOM   292   C  CB  . SER A  1 34  ? 10.981  -15.790 -1.766  1.00 36.37 ? 34  SER A CB  1 
ATOM   293   O  OG  . SER A  1 34  ? 9.606   -15.635 -1.467  1.00 42.85 ? 34  SER A OG  1 
ATOM   294   N  N   . ASP A  1 35  ? 10.157  -13.025 -3.269  1.00 30.13 ? 35  ASP A N   1 
ATOM   295   C  CA  . ASP A  1 35  ? 9.673   -12.356 -4.502  1.00 34.49 ? 35  ASP A CA  1 
ATOM   296   C  C   . ASP A  1 35  ? 10.741  -11.513 -5.141  1.00 32.41 ? 35  ASP A C   1 
ATOM   297   O  O   . ASP A  1 35  ? 10.802  -11.367 -6.387  1.00 30.14 ? 35  ASP A O   1 
ATOM   298   C  CB  . ASP A  1 35  ? 8.532   -11.368 -4.156  1.00 42.00 ? 35  ASP A CB  1 
ATOM   299   C  CG  . ASP A  1 35  ? 7.139   -11.994 -4.230  1.00 56.69 ? 35  ASP A CG  1 
ATOM   300   O  OD1 . ASP A  1 35  ? 6.977   -12.991 -4.978  1.00 63.23 ? 35  ASP A OD1 1 
ATOM   301   O  OD2 . ASP A  1 35  ? 6.203   -11.483 -3.536  1.00 59.96 ? 35  ASP A OD2 1 
ATOM   302   N  N   . ILE A  1 36  ? 11.547  -10.882 -4.276  1.00 26.52 ? 36  ILE A N   1 
ATOM   303   C  CA  . ILE A  1 36  ? 12.411  -9.792  -4.707  1.00 26.72 ? 36  ILE A CA  1 
ATOM   304   C  C   . ILE A  1 36  ? 13.838  -10.237 -4.626  1.00 22.04 ? 36  ILE A C   1 
ATOM   305   O  O   . ILE A  1 36  ? 14.765  -9.411  -4.832  1.00 26.24 ? 36  ILE A O   1 
ATOM   306   C  CB  . ILE A  1 36  ? 12.225  -8.487  -3.923  1.00 22.90 ? 36  ILE A CB  1 
ATOM   307   C  CG1 . ILE A  1 36  ? 12.504  -8.736  -2.401  1.00 24.08 ? 36  ILE A CG1 1 
ATOM   308   C  CG2 . ILE A  1 36  ? 10.875  -7.840  -4.224  1.00 25.02 ? 36  ILE A CG2 1 
ATOM   309   C  CD1 . ILE A  1 36  ? 12.770  -7.466  -1.629  1.00 21.28 ? 36  ILE A CD1 1 
ATOM   310   N  N   . LEU A  1 37  ? 14.028  -11.514 -4.347  1.00 20.71 ? 37  LEU A N   1 
ATOM   311   C  CA  . LEU A  1 37  ? 15.423  -12.032 -4.336  1.00 20.20 ? 37  LEU A CA  1 
ATOM   312   C  C   . LEU A  1 37  ? 15.889  -12.545 -5.679  1.00 22.66 ? 37  LEU A C   1 
ATOM   313   O  O   . LEU A  1 37  ? 15.146  -13.285 -6.380  1.00 24.78 ? 37  LEU A O   1 
ATOM   314   C  CB  . LEU A  1 37  ? 15.555  -13.158 -3.296  1.00 20.35 ? 37  LEU A CB  1 
ATOM   315   C  CG  . LEU A  1 37  ? 15.107  -12.828 -1.902  1.00 19.99 ? 37  LEU A CG  1 
ATOM   316   C  CD1 . LEU A  1 37  ? 15.421  -14.129 -1.101  1.00 24.36 ? 37  LEU A CD1 1 
ATOM   317   C  CD2 . LEU A  1 37  ? 15.905  -11.591 -1.392  1.00 18.65 ? 37  LEU A CD2 1 
ATOM   318   N  N   . GLN A  1 38  ? 17.123  -12.278 -6.047  1.00 20.91 ? 38  GLN A N   1 
ATOM   319   C  CA  . GLN A  1 38  ? 17.656  -12.856 -7.296  1.00 20.08 ? 38  GLN A CA  1 
ATOM   320   C  C   . GLN A  1 38  ? 19.097  -13.298 -7.105  1.00 18.06 ? 38  GLN A C   1 
ATOM   321   O  O   . GLN A  1 38  ? 19.937  -12.463 -6.661  1.00 16.27 ? 38  GLN A O   1 
ATOM   322   C  CB  . GLN A  1 38  ? 17.533  -11.873 -8.415  1.00 25.33 ? 38  GLN A CB  1 
ATOM   323   C  CG  . GLN A  1 38  ? 18.059  -12.506 -9.705  1.00 31.33 ? 38  GLN A CG  1 
ATOM   324   C  CD  . GLN A  1 38  ? 17.862  -11.593 -10.878 1.00 38.75 ? 38  GLN A CD  1 
ATOM   325   O  OE1 . GLN A  1 38  ? 16.724  -11.438 -11.364 1.00 40.18 ? 38  GLN A OE1 1 
ATOM   326   N  NE2 . GLN A  1 38  ? 18.961  -10.963 -11.327 1.00 32.74 ? 38  GLN A NE2 1 
ATOM   327   N  N   . TYR A  1 39  ? 19.421  -14.574 -7.394  1.00 18.26 ? 39  TYR A N   1 
ATOM   328   C  CA  . TYR A  1 39  ? 20.717  -15.094 -7.320  1.00 17.52 ? 39  TYR A CA  1 
ATOM   329   C  C   . TYR A  1 39  ? 21.580  -14.323 -8.297  1.00 21.01 ? 39  TYR A C   1 
ATOM   330   O  O   . TYR A  1 39  ? 21.144  -14.023 -9.439  1.00 22.82 ? 39  TYR A O   1 
ATOM   331   C  CB  . TYR A  1 39  ? 20.742  -16.639 -7.575  1.00 17.44 ? 39  TYR A CB  1 
ATOM   332   C  CG  . TYR A  1 39  ? 22.097  -17.197 -7.657  1.00 21.49 ? 39  TYR A CG  1 
ATOM   333   C  CD1 . TYR A  1 39  ? 22.931  -17.252 -6.514  1.00 20.18 ? 39  TYR A CD1 1 
ATOM   334   C  CD2 . TYR A  1 39  ? 22.576  -17.741 -8.848  1.00 23.22 ? 39  TYR A CD2 1 
ATOM   335   C  CE1 . TYR A  1 39  ? 24.167  -17.792 -6.546  1.00 23.72 ? 39  TYR A CE1 1 
ATOM   336   C  CE2 . TYR A  1 39  ? 23.865  -18.246 -8.915  1.00 27.65 ? 39  TYR A CE2 1 
ATOM   337   C  CZ  . TYR A  1 39  ? 24.645  -18.326 -7.762  1.00 26.88 ? 39  TYR A CZ  1 
ATOM   338   O  OH  . TYR A  1 39  ? 25.923  -18.809 -7.828  1.00 33.87 ? 39  TYR A OH  1 
ATOM   339   N  N   . ASP A  1 40  ? 22.745  -13.968 -7.835  1.00 18.37 ? 40  ASP A N   1 
ATOM   340   C  CA  . ASP A  1 40  ? 23.764  -13.346 -8.645  1.00 19.04 ? 40  ASP A CA  1 
ATOM   341   C  C   . ASP A  1 40  ? 25.083  -14.027 -8.369  1.00 25.30 ? 40  ASP A C   1 
ATOM   342   O  O   . ASP A  1 40  ? 25.678  -13.862 -7.308  1.00 19.43 ? 40  ASP A O   1 
ATOM   343   C  CB  . ASP A  1 40  ? 23.781  -11.836 -8.381  1.00 23.13 ? 40  ASP A CB  1 
ATOM   344   C  CG  . ASP A  1 40  ? 24.797  -11.042 -9.246  1.00 27.82 ? 40  ASP A CG  1 
ATOM   345   O  OD1 . ASP A  1 40  ? 25.705  -11.625 -9.849  1.00 28.80 ? 40  ASP A OD1 1 
ATOM   346   O  OD2 . ASP A  1 40  ? 24.647  -9.801  -9.241  1.00 33.22 ? 40  ASP A OD2 1 
ATOM   347   N  N   . ALA A  1 41  ? 25.533  -14.877 -9.323  1.00 27.10 ? 41  ALA A N   1 
ATOM   348   C  CA  . ALA A  1 41  ? 26.862  -15.537 -9.182  1.00 31.56 ? 41  ALA A CA  1 
ATOM   349   C  C   . ALA A  1 41  ? 28.072  -14.570 -9.116  1.00 26.54 ? 41  ALA A C   1 
ATOM   350   O  O   . ALA A  1 41  ? 29.165  -14.942 -8.718  1.00 34.07 ? 41  ALA A O   1 
ATOM   351   C  CB  . ALA A  1 41  ? 27.073  -16.625 -10.256 1.00 33.90 ? 41  ALA A CB  1 
ATOM   352   N  N   . SER A  1 42  ? 27.877  -13.320 -9.443  1.00 27.22 ? 42  SER A N   1 
ATOM   353   C  CA  . SER A  1 42  ? 28.922  -12.304 -9.269  1.00 28.29 ? 42  SER A CA  1 
ATOM   354   C  C   . SER A  1 42  ? 29.260  -12.084 -7.792  1.00 31.37 ? 42  SER A C   1 
ATOM   355   O  O   . SER A  1 42  ? 30.282  -11.486 -7.416  1.00 30.12 ? 42  SER A O   1 
ATOM   356   C  CB  . SER A  1 42  ? 28.429  -11.009 -9.941  1.00 30.38 ? 42  SER A CB  1 
ATOM   357   O  OG  . SER A  1 42  ? 28.537  -9.858  -9.098  1.00 37.63 ? 42  SER A OG  1 
ATOM   358   N  N   . LEU A  1 43  ? 28.346  -12.495 -6.930  1.00 21.00 ? 43  LEU A N   1 
ATOM   359   C  CA  . LEU A  1 43  ? 28.539  -12.223 -5.467  1.00 20.84 ? 43  LEU A CA  1 
ATOM   360   C  C   . LEU A  1 43  ? 29.430  -13.215 -4.709  1.00 21.21 ? 43  LEU A C   1 
ATOM   361   O  O   . LEU A  1 43  ? 28.998  -14.157 -3.992  1.00 20.84 ? 43  LEU A O   1 
ATOM   362   C  CB  . LEU A  1 43  ? 27.148  -12.104 -4.807  1.00 17.45 ? 43  LEU A CB  1 
ATOM   363   C  CG  . LEU A  1 43  ? 26.311  -10.957 -5.293  1.00 16.08 ? 43  LEU A CG  1 
ATOM   364   C  CD1 . LEU A  1 43  ? 24.958  -10.919 -4.599  1.00 14.36 ? 43  LEU A CD1 1 
ATOM   365   C  CD2 . LEU A  1 43  ? 26.971  -9.570  -5.144  1.00 16.29 ? 43  LEU A CD2 1 
ATOM   366   N  N   . THR A  1 44  ? 30.740  -13.050 -4.850  1.00 20.65 ? 44  THR A N   1 
ATOM   367   C  CA  . THR A  1 44  ? 31.681  -13.953 -4.277  1.00 19.53 ? 44  THR A CA  1 
ATOM   368   C  C   . THR A  1 44  ? 31.974  -13.647 -2.795  1.00 19.23 ? 44  THR A C   1 
ATOM   369   O  O   . THR A  1 44  ? 31.496  -12.589 -2.300  1.00 16.07 ? 44  THR A O   1 
ATOM   370   C  CB  . THR A  1 44  ? 32.981  -13.866 -5.095  1.00 23.74 ? 44  THR A CB  1 
ATOM   371   O  OG1 . THR A  1 44  ? 33.290  -12.478 -5.193  1.00 25.36 ? 44  THR A OG1 1 
ATOM   372   C  CG2 . THR A  1 44  ? 32.699  -14.418 -6.516  1.00 31.28 ? 44  THR A CG2 1 
ATOM   373   N  N   . PRO A  1 45  ? 32.604  -14.550 -2.034  1.00 17.83 ? 45  PRO A N   1 
ATOM   374   C  CA  . PRO A  1 45  ? 32.900  -14.266 -0.614  1.00 17.94 ? 45  PRO A CA  1 
ATOM   375   C  C   . PRO A  1 45  ? 33.725  -13.076 -0.345  1.00 19.24 ? 45  PRO A C   1 
ATOM   376   O  O   . PRO A  1 45  ? 34.710  -12.832 -1.062  1.00 22.03 ? 45  PRO A O   1 
ATOM   377   C  CB  . PRO A  1 45  ? 33.629  -15.522 -0.122  1.00 21.15 ? 45  PRO A CB  1 
ATOM   378   C  CG  . PRO A  1 45  ? 33.159  -16.619 -1.098  1.00 20.42 ? 45  PRO A CG  1 
ATOM   379   C  CD  . PRO A  1 45  ? 33.114  -15.916 -2.408  1.00 21.31 ? 45  PRO A CD  1 
ATOM   380   N  N   . LEU A  1 46  ? 33.346  -12.290 0.646   1.00 16.02 ? 46  LEU A N   1 
ATOM   381   C  CA  . LEU A  1 46  ? 34.162  -11.180 1.081   1.00 15.22 ? 46  LEU A CA  1 
ATOM   382   C  C   . LEU A  1 46  ? 35.278  -11.729 1.967   1.00 15.58 ? 46  LEU A C   1 
ATOM   383   O  O   . LEU A  1 46  ? 35.140  -12.833 2.592   1.00 18.36 ? 46  LEU A O   1 
ATOM   384   C  CB  . LEU A  1 46  ? 33.351  -10.171 1.905   1.00 14.66 ? 46  LEU A CB  1 
ATOM   385   C  CG  . LEU A  1 46  ? 32.187  -9.552  1.175   1.00 16.31 ? 46  LEU A CG  1 
ATOM   386   C  CD1 . LEU A  1 46  ? 31.465  -8.623  2.134   1.00 16.16 ? 46  LEU A CD1 1 
ATOM   387   C  CD2 . LEU A  1 46  ? 32.764  -8.738  0.005   1.00 19.59 ? 46  LEU A CD2 1 
ATOM   388   N  N   . GLU A  1 47  ? 36.354  -10.962 2.051   1.00 15.38 ? 47  GLU A N   1 
ATOM   389   C  CA  . GLU A  1 47  ? 37.394  -11.305 2.994   1.00 17.40 ? 47  GLU A CA  1 
ATOM   390   C  C   . GLU A  1 47  ? 37.551  -10.234 4.033   1.00 16.43 ? 47  GLU A C   1 
ATOM   391   O  O   . GLU A  1 47  ? 37.527  -8.983  3.735   1.00 17.46 ? 47  GLU A O   1 
ATOM   392   C  CB  . GLU A  1 47  ? 38.733  -11.458 2.263   1.00 23.66 ? 47  GLU A CB  1 
ATOM   393   C  CG  . GLU A  1 47  ? 38.783  -12.585 1.236   1.00 32.74 ? 47  GLU A CG  1 
ATOM   394   C  CD  . GLU A  1 47  ? 40.086  -12.520 0.442   1.00 45.44 ? 47  GLU A CD  1 
ATOM   395   O  OE1 . GLU A  1 47  ? 40.074  -11.937 -0.668  1.00 52.45 ? 47  GLU A OE1 1 
ATOM   396   O  OE2 . GLU A  1 47  ? 41.128  -13.004 0.956   1.00 49.77 ? 47  GLU A OE2 1 
ATOM   397   N  N   . PHE A  1 48  ? 37.724  -10.606 5.276   1.00 15.15 ? 48  PHE A N   1 
ATOM   398   C  CA  . PHE A  1 48  ? 37.732  -9.662  6.393   1.00 14.37 ? 48  PHE A CA  1 
ATOM   399   C  C   . PHE A  1 48  ? 39.138  -9.550  6.828   1.00 17.14 ? 48  PHE A C   1 
ATOM   400   O  O   . PHE A  1 48  ? 39.740  -10.534 7.320   1.00 20.09 ? 48  PHE A O   1 
ATOM   401   C  CB  . PHE A  1 48  ? 36.788  -10.236 7.455   1.00 15.86 ? 48  PHE A CB  1 
ATOM   402   C  CG  . PHE A  1 48  ? 35.431  -10.594 6.903   1.00 14.99 ? 48  PHE A CG  1 
ATOM   403   C  CD1 . PHE A  1 48  ? 34.581  -9.613  6.387   1.00 15.33 ? 48  PHE A CD1 1 
ATOM   404   C  CD2 . PHE A  1 48  ? 35.043  -11.970 6.735   1.00 15.07 ? 48  PHE A CD2 1 
ATOM   405   C  CE1 . PHE A  1 48  ? 33.360  -9.958  5.805   1.00 14.77 ? 48  PHE A CE1 1 
ATOM   406   C  CE2 . PHE A  1 48  ? 33.808  -12.292 6.166   1.00 14.44 ? 48  PHE A CE2 1 
ATOM   407   C  CZ  . PHE A  1 48  ? 32.987  -11.258 5.650   1.00 14.18 ? 48  PHE A CZ  1 
ATOM   408   N  N   . GLN A  1 49  ? 39.742  -8.439  6.579   1.00 14.14 ? 49  GLN A N   1 
ATOM   409   C  CA  . GLN A  1 49  ? 41.189  -8.311  6.797   1.00 14.80 ? 49  GLN A CA  1 
ATOM   410   C  C   . GLN A  1 49  ? 41.464  -7.324  7.884   1.00 12.91 ? 49  GLN A C   1 
ATOM   411   O  O   . GLN A  1 49  ? 40.789  -6.269  8.041   1.00 12.60 ? 49  GLN A O   1 
ATOM   412   C  CB  . GLN A  1 49  ? 41.790  -7.716  5.554   1.00 15.73 ? 49  GLN A CB  1 
ATOM   413   C  CG  . GLN A  1 49  ? 41.667  -8.699  4.420   1.00 22.98 ? 49  GLN A CG  1 
ATOM   414   C  CD  . GLN A  1 49  ? 42.585  -8.484  3.239   1.00 27.11 ? 49  GLN A CD  1 
ATOM   415   O  OE1 . GLN A  1 49  ? 42.993  -7.318  2.897   1.00 28.12 ? 49  GLN A OE1 1 
ATOM   416   N  NE2 . GLN A  1 49  ? 42.875  -9.612  2.553   1.00 27.19 ? 49  GLN A NE2 1 
ATOM   417   N  N   . GLY A  1 50  ? 42.408  -7.679  8.778   1.00 14.41 ? 50  GLY A N   1 
ATOM   418   C  CA  . GLY A  1 50  ? 42.673  -6.819  9.896   1.00 13.86 ? 50  GLY A CA  1 
ATOM   419   C  C   . GLY A  1 50  ? 41.530  -6.784  10.996  1.00 12.29 ? 50  GLY A C   1 
ATOM   420   O  O   . GLY A  1 50  ? 41.510  -5.946  11.838  1.00 14.62 ? 50  GLY A O   1 
ATOM   421   N  N   . TYR A  1 51  ? 40.670  -7.808  10.974  1.00 12.82 ? 51  TYR A N   1 
ATOM   422   C  CA  . TYR A  1 51  ? 39.575  -7.947  11.947  1.00 13.05 ? 51  TYR A CA  1 
ATOM   423   C  C   . TYR A  1 51  ? 40.120  -8.531  13.249  1.00 13.25 ? 51  TYR A C   1 
ATOM   424   O  O   . TYR A  1 51  ? 39.461  -8.347  14.259  1.00 13.36 ? 51  TYR A O   1 
ATOM   425   C  CB  . TYR A  1 51  ? 38.455  -8.882  11.426  1.00 11.81 ? 51  TYR A CB  1 
ATOM   426   C  CG  . TYR A  1 51  ? 37.408  -8.143  10.567  1.00 12.13 ? 51  TYR A CG  1 
ATOM   427   C  CD1 . TYR A  1 51  ? 37.779  -7.261  9.539   1.00 12.03 ? 51  TYR A CD1 1 
ATOM   428   C  CD2 . TYR A  1 51  ? 36.052  -8.326  10.795  1.00 11.35 ? 51  TYR A CD2 1 
ATOM   429   C  CE1 . TYR A  1 51  ? 36.817  -6.599  8.775   1.00 11.86 ? 51  TYR A CE1 1 
ATOM   430   C  CE2 . TYR A  1 51  ? 35.095  -7.673  10.040  1.00 12.23 ? 51  TYR A CE2 1 
ATOM   431   C  CZ  . TYR A  1 51  ? 35.471  -6.814  9.035   1.00 12.78 ? 51  TYR A CZ  1 
ATOM   432   O  OH  . TYR A  1 51  ? 34.474  -6.190  8.316   1.00 13.83 ? 51  TYR A OH  1 
ATOM   433   N  N   . ASN A  1 52  ? 41.303  -9.154  13.228  1.00 14.44 ? 52  ASN A N   1 
ATOM   434   C  CA  . ASN A  1 52  ? 41.794  -9.726  14.524  1.00 15.55 ? 52  ASN A CA  1 
ATOM   435   C  C   . ASN A  1 52  ? 42.533  -8.638  15.272  1.00 15.38 ? 52  ASN A C   1 
ATOM   436   O  O   . ASN A  1 52  ? 43.806  -8.511  15.136  1.00 18.52 ? 52  ASN A O   1 
ATOM   437   C  CB  . ASN A  1 52  ? 42.673  -10.938 14.226  1.00 16.31 ? 52  ASN A CB  1 
ATOM   438   C  CG  . ASN A  1 52  ? 42.950  -11.762 15.484  1.00 21.30 ? 52  ASN A CG  1 
ATOM   439   O  OD1 . ASN A  1 52  ? 42.415  -11.515 16.567  1.00 18.90 ? 52  ASN A OD1 1 
ATOM   440   N  ND2 . ASN A  1 52  ? 43.914  -12.711 15.345  1.00 28.30 ? 52  ASN A ND2 1 
ATOM   441   N  N   . LEU A  1 53  ? 41.810  -7.809  15.973  1.00 14.73 ? 53  LEU A N   1 
ATOM   442   C  CA  . LEU A  1 53  ? 42.353  -6.586  16.557  1.00 14.28 ? 53  LEU A CA  1 
ATOM   443   C  C   . LEU A  1 53  ? 43.349  -6.935  17.657  1.00 18.34 ? 53  LEU A C   1 
ATOM   444   O  O   . LEU A  1 53  ? 43.077  -7.823  18.466  1.00 18.81 ? 53  LEU A O   1 
ATOM   445   C  CB  . LEU A  1 53  ? 41.266  -5.624  17.152  1.00 15.70 ? 53  LEU A CB  1 
ATOM   446   C  CG  . LEU A  1 53  ? 40.169  -5.225  16.115  1.00 14.03 ? 53  LEU A CG  1 
ATOM   447   C  CD1 . LEU A  1 53  ? 39.175  -4.420  16.910  1.00 15.48 ? 53  LEU A CD1 1 
ATOM   448   C  CD2 . LEU A  1 53  ? 40.755  -4.507  14.911  1.00 16.36 ? 53  LEU A CD2 1 
ATOM   449   N  N   . SER A  1 54  ? 44.455  -6.185  17.648  1.00 17.97 ? 54  SER A N   1 
ATOM   450   C  CA  . SER A  1 54  ? 45.490  -6.396  18.654  1.00 18.85 ? 54  SER A CA  1 
ATOM   451   C  C   . SER A  1 54  ? 44.879  -6.392  20.067  1.00 18.99 ? 54  SER A C   1 
ATOM   452   O  O   . SER A  1 54  ? 44.281  -5.446  20.477  1.00 18.52 ? 54  SER A O   1 
ATOM   453   C  CB  . SER A  1 54  ? 46.454  -5.220  18.541  1.00 19.30 ? 54  SER A CB  1 
ATOM   454   O  OG  . SER A  1 54  ? 47.548  -5.487  19.466  1.00 23.19 ? 54  SER A OG  1 
ATOM   455   N  N   . ALA A  1 55  ? 45.086  -7.456  20.823  1.00 21.99 ? 55  ALA A N   1 
ATOM   456   C  CA  . ALA A  1 55  ? 44.710  -7.462  22.220  1.00 23.44 ? 55  ALA A CA  1 
ATOM   457   C  C   . ALA A  1 55  ? 45.542  -6.470  23.052  1.00 25.50 ? 55  ALA A C   1 
ATOM   458   O  O   . ALA A  1 55  ? 45.275  -6.244  24.169  1.00 24.83 ? 55  ALA A O   1 
ATOM   459   C  CB  . ALA A  1 55  ? 44.885  -8.873  22.786  1.00 30.58 ? 55  ALA A CB  1 
ATOM   460   N  N   . ASN A  1 56  ? 46.553  -5.871  22.454  1.00 24.41 ? 56  ASN A N   1 
ATOM   461   C  CA  . ASN A  1 56  ? 47.418  -4.858  23.155  1.00 26.01 ? 56  ASN A CA  1 
ATOM   462   C  C   . ASN A  1 56  ? 46.985  -3.440  22.809  1.00 25.82 ? 56  ASN A C   1 
ATOM   463   O  O   . ASN A  1 56  ? 47.670  -2.494  23.091  1.00 27.97 ? 56  ASN A O   1 
ATOM   464   C  CB  . ASN A  1 56  ? 48.883  -5.037  22.703  1.00 23.52 ? 56  ASN A CB  1 
ATOM   465   C  CG  . ASN A  1 56  ? 49.493  -6.312  23.220  1.00 31.18 ? 56  ASN A CG  1 
ATOM   466   O  OD1 . ASN A  1 56  ? 49.316  -6.644  24.401  1.00 35.51 ? 56  ASN A OD1 1 
ATOM   467   N  ND2 . ASN A  1 56  ? 50.132  -7.073  22.339  1.00 32.32 ? 56  ASN A ND2 1 
ATOM   468   N  N   . LYS A  1 57  ? 45.859  -3.306  22.074  1.00 21.87 ? 57  LYS A N   1 
ATOM   469   C  CA  . LYS A  1 57  ? 45.336  -2.017  21.712  1.00 19.87 ? 57  LYS A CA  1 
ATOM   470   C  C   . LYS A  1 57  ? 43.927  -1.970  22.323  1.00 19.85 ? 57  LYS A C   1 
ATOM   471   O  O   . LYS A  1 57  ? 43.323  -2.994  22.582  1.00 20.26 ? 57  LYS A O   1 
ATOM   472   C  CB  . LYS A  1 57  ? 45.289  -1.922  20.171  1.00 21.13 ? 57  LYS A CB  1 
ATOM   473   C  CG  . LYS A  1 57  ? 44.958  -0.562  19.628  1.00 24.13 ? 57  LYS A CG  1 
ATOM   474   C  CD  . LYS A  1 57  ? 45.450  -0.447  18.162  1.00 23.24 ? 57  LYS A CD  1 
ATOM   475   C  CE  . LYS A  1 57  ? 44.690  0.642   17.448  1.00 24.73 ? 57  LYS A CE  1 
ATOM   476   N  NZ  . LYS A  1 57  ? 45.138  0.938   16.085  1.00 28.81 ? 57  LYS A NZ  1 
ATOM   477   N  N   . GLN A  1 58  ? 43.516  -0.758  22.583  1.00 18.78 ? 58  GLN A N   1 
ATOM   478   C  CA  . GLN A  1 58  ? 42.135  -0.455  23.134  1.00 19.30 ? 58  GLN A CA  1 
ATOM   479   C  C   . GLN A  1 58  ? 41.268  0.297   22.176  1.00 19.18 ? 58  GLN A C   1 
ATOM   480   O  O   . GLN A  1 58  ? 41.721  1.172   21.450  1.00 19.89 ? 58  GLN A O   1 
ATOM   481   C  CB  . GLN A  1 58  ? 42.196  0.247   24.493  1.00 19.80 ? 58  GLN A CB  1 
ATOM   482   C  CG  . GLN A  1 58  ? 42.702  -0.727  25.470  1.00 23.65 ? 58  GLN A CG  1 
ATOM   483   C  CD  . GLN A  1 58  ? 42.974  -0.114  26.789  1.00 26.82 ? 58  GLN A CD  1 
ATOM   484   O  OE1 . GLN A  1 58  ? 43.400  -0.821  27.676  1.00 28.87 ? 58  GLN A OE1 1 
ATOM   485   N  NE2 . GLN A  1 58  ? 42.822  1.206   26.889  1.00 23.05 ? 58  GLN A NE2 1 
ATOM   486   N  N   . PHE A  1 59  ? 39.971  -0.092  22.164  1.00 17.30 ? 59  PHE A N   1 
ATOM   487   C  CA  . PHE A  1 59  ? 39.012  0.526   21.242  1.00 16.01 ? 59  PHE A CA  1 
ATOM   488   C  C   . PHE A  1 59  ? 37.877  1.197   21.986  1.00 15.16 ? 59  PHE A C   1 
ATOM   489   O  O   . PHE A  1 59  ? 37.376  0.604   22.954  1.00 15.37 ? 59  PHE A O   1 
ATOM   490   C  CB  . PHE A  1 59  ? 38.555  -0.563  20.264  1.00 16.22 ? 59  PHE A CB  1 
ATOM   491   C  CG  . PHE A  1 59  ? 39.702  -1.113  19.495  1.00 16.50 ? 59  PHE A CG  1 
ATOM   492   C  CD1 . PHE A  1 59  ? 40.117  -0.506  18.326  1.00 16.11 ? 59  PHE A CD1 1 
ATOM   493   C  CD2 . PHE A  1 59  ? 40.495  -2.134  20.041  1.00 17.33 ? 59  PHE A CD2 1 
ATOM   494   C  CE1 . PHE A  1 59  ? 41.274  -0.946  17.662  1.00 16.30 ? 59  PHE A CE1 1 
ATOM   495   C  CE2 . PHE A  1 59  ? 41.677  -2.597  19.344  1.00 13.99 ? 59  PHE A CE2 1 
ATOM   496   C  CZ  . PHE A  1 59  ? 42.023  -1.992  18.096  1.00 16.15 ? 59  PHE A CZ  1 
ATOM   497   N  N   . LEU A  1 60  ? 37.570  2.419   21.599  1.00 15.28 ? 60  LEU A N   1 
ATOM   498   C  CA  . LEU A  1 60  ? 36.634  3.250   22.394  1.00 14.54 ? 60  LEU A CA  1 
ATOM   499   C  C   . LEU A  1 60  ? 35.166  2.808   22.163  1.00 16.24 ? 60  LEU A C   1 
ATOM   500   O  O   . LEU A  1 60  ? 34.662  2.842   21.033  1.00 15.10 ? 60  LEU A O   1 
ATOM   501   C  CB  . LEU A  1 60  ? 36.770  4.703   22.019  1.00 16.56 ? 60  LEU A CB  1 
ATOM   502   C  CG  . LEU A  1 60  ? 36.010  5.640   22.868  1.00 20.11 ? 60  LEU A CG  1 
ATOM   503   C  CD1 . LEU A  1 60  ? 36.585  5.656   24.295  1.00 23.09 ? 60  LEU A CD1 1 
ATOM   504   C  CD2 . LEU A  1 60  ? 36.045  7.021   22.222  1.00 20.58 ? 60  LEU A CD2 1 
ATOM   505   N  N   . LEU A  1 61  ? 34.447  2.489   23.201  1.00 14.51 ? 61  LEU A N   1 
ATOM   506   C  CA  . LEU A  1 61  ? 33.016  2.163   23.244  1.00 14.05 ? 61  LEU A CA  1 
ATOM   507   C  C   . LEU A  1 61  ? 32.316  3.378   23.766  1.00 15.01 ? 61  LEU A C   1 
ATOM   508   O  O   . LEU A  1 61  ? 32.736  3.968   24.772  1.00 15.55 ? 61  LEU A O   1 
ATOM   509   C  CB  . LEU A  1 61  ? 32.761  0.994   24.181  1.00 15.08 ? 61  LEU A CB  1 
ATOM   510   C  CG  . LEU A  1 61  ? 31.358  0.315   24.127  1.00 15.61 ? 61  LEU A CG  1 
ATOM   511   C  CD1 . LEU A  1 61  ? 31.184  -0.529  22.838  1.00 14.65 ? 61  LEU A CD1 1 
ATOM   512   C  CD2 . LEU A  1 61  ? 31.155  -0.610  25.303  1.00 16.95 ? 61  LEU A CD2 1 
ATOM   513   N  N   A THR A  1 62  ? 31.341  3.902   23.036  0.50 14.05 ? 62  THR A N   1 
ATOM   514   N  N   B THR A  1 62  ? 31.271  3.824   23.092  0.50 13.87 ? 62  THR A N   1 
ATOM   515   C  CA  A THR A  1 62  ? 30.568  5.029   23.437  0.50 13.47 ? 62  THR A CA  1 
ATOM   516   C  CA  B THR A  1 62  ? 30.543  4.963   23.510  0.50 12.80 ? 62  THR A CA  1 
ATOM   517   C  C   A THR A  1 62  ? 29.039  4.709   23.509  0.50 15.05 ? 62  THR A C   1 
ATOM   518   C  C   B THR A  1 62  ? 29.045  4.866   23.376  0.50 14.74 ? 62  THR A C   1 
ATOM   519   O  O   A THR A  1 62  ? 28.512  3.804   22.798  0.50 13.69 ? 62  THR A O   1 
ATOM   520   O  O   B THR A  1 62  ? 28.556  4.265   22.406  0.50 12.68 ? 62  THR A O   1 
ATOM   521   C  CB  A THR A  1 62  ? 30.756  6.294   22.517  0.50 16.69 ? 62  THR A CB  1 
ATOM   522   C  CB  B THR A  1 62  ? 30.948  6.222   22.755  0.50 14.20 ? 62  THR A CB  1 
ATOM   523   O  OG1 A THR A  1 62  ? 32.125  6.676   22.303  0.50 18.27 ? 62  THR A OG1 1 
ATOM   524   O  OG1 B THR A  1 62  ? 30.595  6.082   21.340  0.50 14.13 ? 62  THR A OG1 1 
ATOM   525   C  CG2 A THR A  1 62  ? 30.020  7.497   23.050  0.50 14.95 ? 62  THR A CG2 1 
ATOM   526   C  CG2 B THR A  1 62  ? 32.386  6.497   22.974  0.50 16.80 ? 62  THR A CG2 1 
ATOM   527   N  N   . ASN A  1 63  ? 28.326  5.502   24.294  1.00 14.24 ? 63  ASN A N   1 
ATOM   528   C  CA  . ASN A  1 63  ? 26.876  5.652   24.152  1.00 13.74 ? 63  ASN A CA  1 
ATOM   529   C  C   . ASN A  1 63  ? 26.626  6.981   23.544  1.00 14.22 ? 63  ASN A C   1 
ATOM   530   O  O   . ASN A  1 63  ? 26.974  8.078   24.095  1.00 14.46 ? 63  ASN A O   1 
ATOM   531   C  CB  . ASN A  1 63  ? 26.271  5.573   25.551  1.00 13.28 ? 63  ASN A CB  1 
ATOM   532   C  CG  . ASN A  1 63  ? 24.764  5.853   25.570  1.00 13.74 ? 63  ASN A CG  1 
ATOM   533   O  OD1 . ASN A  1 63  ? 24.199  6.573   24.687  1.00 13.70 ? 63  ASN A OD1 1 
ATOM   534   N  ND2 . ASN A  1 63  ? 24.114  5.302   26.573  1.00 13.06 ? 63  ASN A ND2 1 
ATOM   535   N  N   . ASN A  1 64  ? 26.105  7.003   22.323  1.00 14.66 ? 64  ASN A N   1 
ATOM   536   C  CA  . ASN A  1 64  ? 25.939  8.287   21.642  1.00 15.92 ? 64  ASN A CA  1 
ATOM   537   C  C   . ASN A  1 64  ? 24.502  8.821   21.731  1.00 15.48 ? 64  ASN A C   1 
ATOM   538   O  O   . ASN A  1 64  ? 24.160  9.811   21.021  1.00 18.07 ? 64  ASN A O   1 
ATOM   539   C  CB  . ASN A  1 64  ? 26.417  8.201   20.169  1.00 16.75 ? 64  ASN A CB  1 
ATOM   540   C  CG  . ASN A  1 64  ? 25.607  7.208   19.339  1.00 16.73 ? 64  ASN A CG  1 
ATOM   541   O  OD1 . ASN A  1 64  ? 24.539  6.779   19.763  1.00 14.11 ? 64  ASN A OD1 1 
ATOM   542   N  ND2 . ASN A  1 64  ? 26.101  6.858   18.136  1.00 18.85 ? 64  ASN A ND2 1 
ATOM   543   N  N   . GLY A  1 65  ? 23.698  8.222   22.579  1.00 13.93 ? 65  GLY A N   1 
ATOM   544   C  CA  . GLY A  1 65  ? 22.336  8.636   22.778  1.00 16.15 ? 65  GLY A CA  1 
ATOM   545   C  C   . GLY A  1 65  ? 21.400  7.957   21.792  1.00 15.30 ? 65  GLY A C   1 
ATOM   546   O  O   . GLY A  1 65  ? 20.194  8.091   21.979  1.00 15.67 ? 65  GLY A O   1 
ATOM   547   N  N   . HIS A  1 66  ? 21.927  7.175   20.833  1.00 13.87 ? 66  HIS A N   1 
ATOM   548   C  CA  . HIS A  1 66  ? 21.104  6.422   19.826  1.00 12.50 ? 66  HIS A CA  1 
ATOM   549   C  C   . HIS A  1 66  ? 21.403  4.951   19.779  1.00 12.74 ? 66  HIS A C   1 
ATOM   550   O  O   . HIS A  1 66  ? 20.534  4.185   19.390  1.00 13.89 ? 66  HIS A O   1 
ATOM   551   C  CB  . HIS A  1 66  ? 21.285  7.024   18.414  1.00 14.12 ? 66  HIS A CB  1 
ATOM   552   C  CG  . HIS A  1 66  ? 21.053  8.515   18.366  1.00 13.13 ? 66  HIS A CG  1 
ATOM   553   N  ND1 . HIS A  1 66  ? 19.793  9.107   18.501  1.00 14.24 ? 66  HIS A ND1 1 
ATOM   554   C  CD2 . HIS A  1 66  ? 21.944  9.527   18.162  1.00 14.27 ? 66  HIS A CD2 1 
ATOM   555   C  CE1 . HIS A  1 66  ? 19.938  10.424  18.379  1.00 13.61 ? 66  HIS A CE1 1 
ATOM   556   N  NE2 . HIS A  1 66  ? 21.226  10.680  18.192  1.00 14.82 ? 66  HIS A NE2 1 
ATOM   557   N  N   . SER A  1 67  ? 22.635  4.535   20.110  1.00 11.36 ? 67  SER A N   1 
ATOM   558   C  CA  . SER A  1 67  ? 23.045  3.166   20.134  1.00 11.66 ? 67  SER A CA  1 
ATOM   559   C  C   . SER A  1 67  ? 24.319  3.112   21.014  1.00 11.10 ? 67  SER A C   1 
ATOM   560   O  O   . SER A  1 67  ? 24.741  4.133   21.557  1.00 13.01 ? 67  SER A O   1 
ATOM   561   C  CB  . SER A  1 67  ? 23.337  2.727   18.686  1.00 11.35 ? 67  SER A CB  1 
ATOM   562   O  OG  . SER A  1 67  ? 23.709  1.324   18.658  1.00 13.10 ? 67  SER A OG  1 
ATOM   563   N  N   . VAL A  1 68  ? 24.878  1.939   21.107  1.00 11.21 ? 68  VAL A N   1 
ATOM   564   C  CA  . VAL A  1 68  ? 26.225  1.736   21.617  1.00 12.23 ? 68  VAL A CA  1 
ATOM   565   C  C   . VAL A  1 68  ? 27.122  1.451   20.424  1.00 12.76 ? 68  VAL A C   1 
ATOM   566   O  O   . VAL A  1 68  ? 26.797  0.650   19.590  1.00 13.16 ? 68  VAL A O   1 
ATOM   567   C  CB  . VAL A  1 68  ? 26.226  0.640   22.706  1.00 13.16 ? 68  VAL A CB  1 
ATOM   568   C  CG1 . VAL A  1 68  ? 25.705  -0.706  22.225  1.00 14.30 ? 68  VAL A CG1 1 
ATOM   569   C  CG2 . VAL A  1 68  ? 27.685  0.442   23.160  1.00 16.41 ? 68  VAL A CG2 1 
ATOM   570   N  N   . LYS A  1 69  ? 28.199  2.199   20.366  1.00 13.14 ? 69  LYS A N   1 
ATOM   571   C  CA  . LYS A  1 69  ? 29.117  2.149   19.222  1.00 11.93 ? 69  LYS A CA  1 
ATOM   572   C  C   . LYS A  1 69  ? 30.501  1.759   19.719  1.00 12.14 ? 69  LYS A C   1 
ATOM   573   O  O   . LYS A  1 69  ? 30.998  2.327   20.705  1.00 14.14 ? 69  LYS A O   1 
ATOM   574   C  CB  . LYS A  1 69  ? 29.087  3.515   18.583  1.00 16.41 ? 69  LYS A CB  1 
ATOM   575   C  CG  . LYS A  1 69  ? 30.045  3.777   17.507  1.00 21.19 ? 69  LYS A CG  1 
ATOM   576   C  CD  . LYS A  1 69  ? 29.875  5.227   16.941  1.00 20.87 ? 69  LYS A CD  1 
ATOM   577   C  CE  . LYS A  1 69  ? 30.167  6.385   17.873  1.00 29.68 ? 69  LYS A CE  1 
ATOM   578   N  NZ  . LYS A  1 69  ? 30.412  7.550   16.900  1.00 31.05 ? 69  LYS A NZ  1 
ATOM   579   N  N   . LEU A  1 70  ? 31.177  0.978   18.938  1.00 10.67 ? 70  LEU A N   1 
ATOM   580   C  CA  . LEU A  1 70  ? 32.589  0.643   19.152  1.00 12.29 ? 70  LEU A CA  1 
ATOM   581   C  C   . LEU A  1 70  ? 33.412  1.203   18.005  1.00 11.76 ? 70  LEU A C   1 
ATOM   582   O  O   . LEU A  1 70  ? 33.155  0.862   16.851  1.00 11.46 ? 70  LEU A O   1 
ATOM   583   C  CB  . LEU A  1 70  ? 32.791  -0.833  19.303  1.00 12.07 ? 70  LEU A CB  1 
ATOM   584   C  CG  . LEU A  1 70  ? 34.259  -1.339  19.500  1.00 11.68 ? 70  LEU A CG  1 
ATOM   585   C  CD1 . LEU A  1 70  ? 34.829  -0.805  20.835  1.00 13.57 ? 70  LEU A CD1 1 
ATOM   586   C  CD2 . LEU A  1 70  ? 34.286  -2.844  19.389  1.00 13.14 ? 70  LEU A CD2 1 
ATOM   587   N  N   . ASN A  1 71  ? 34.342  2.124   18.268  1.00 11.67 ? 71  ASN A N   1 
ATOM   588   C  CA  . ASN A  1 71  ? 35.246  2.638   17.215  1.00 12.27 ? 71  ASN A CA  1 
ATOM   589   C  C   . ASN A  1 71  ? 36.154  1.560   16.736  1.00 13.51 ? 71  ASN A C   1 
ATOM   590   O  O   . ASN A  1 71  ? 36.697  0.731   17.487  1.00 15.14 ? 71  ASN A O   1 
ATOM   591   C  CB  . ASN A  1 71  ? 36.024  3.797   17.755  1.00 14.89 ? 71  ASN A CB  1 
ATOM   592   C  CG  . ASN A  1 71  ? 35.193  5.044   17.808  1.00 20.14 ? 71  ASN A CG  1 
ATOM   593   O  OD1 . ASN A  1 71  ? 33.962  5.094   17.495  1.00 22.31 ? 71  ASN A OD1 1 
ATOM   594   N  ND2 . ASN A  1 71  ? 35.849  6.132   18.214  1.00 26.15 ? 71  ASN A ND2 1 
ATOM   595   N  N   . LEU A  1 72  ? 36.371  1.525   15.434  1.00 11.67 ? 72  LEU A N   1 
ATOM   596   C  CA  . LEU A  1 72  ? 37.218  0.475   14.840  1.00 11.57 ? 72  LEU A CA  1 
ATOM   597   C  C   . LEU A  1 72  ? 38.404  1.178   14.099  1.00 13.94 ? 72  LEU A C   1 
ATOM   598   O  O   . LEU A  1 72  ? 38.224  2.291   13.573  1.00 15.04 ? 72  LEU A O   1 
ATOM   599   C  CB  . LEU A  1 72  ? 36.341  -0.360  13.860  1.00 10.61 ? 72  LEU A CB  1 
ATOM   600   C  CG  . LEU A  1 72  ? 35.296  -1.183  14.572  1.00 11.54 ? 72  LEU A CG  1 
ATOM   601   C  CD1 . LEU A  1 72  ? 34.407  -1.785  13.512  1.00 10.61 ? 72  LEU A CD1 1 
ATOM   602   C  CD2 . LEU A  1 72  ? 35.852  -2.252  15.540  1.00 11.91 ? 72  LEU A CD2 1 
ATOM   603   N  N   . PRO A  1 73  ? 39.520  0.477   13.878  1.00 13.62 ? 73  PRO A N   1 
ATOM   604   C  CA  . PRO A  1 73  ? 40.679  1.152   13.245  1.00 14.76 ? 73  PRO A CA  1 
ATOM   605   C  C   . PRO A  1 73  ? 40.656  1.047   11.741  1.00 14.95 ? 73  PRO A C   1 
ATOM   606   O  O   . PRO A  1 73  ? 40.099  0.088   11.178  1.00 16.16 ? 73  PRO A O   1 
ATOM   607   C  CB  . PRO A  1 73  ? 41.848  0.330   13.865  1.00 13.32 ? 73  PRO A CB  1 
ATOM   608   C  CG  . PRO A  1 73  ? 41.296  -1.082  13.980  1.00 12.85 ? 73  PRO A CG  1 
ATOM   609   C  CD  . PRO A  1 73  ? 39.814  -0.893  14.332  1.00 13.48 ? 73  PRO A CD  1 
ATOM   610   N  N   . SER A  1 74  ? 41.276  2.037   11.097  1.00 18.58 ? 74  SER A N   1 
ATOM   611   C  CA  . SER A  1 74  ? 41.174  2.021   9.619   1.00 20.94 ? 74  SER A CA  1 
ATOM   612   C  C   . SER A  1 74  ? 42.040  0.961   8.940   1.00 18.67 ? 74  SER A C   1 
ATOM   613   O  O   . SER A  1 74  ? 41.842  0.707   7.753   1.00 21.89 ? 74  SER A O   1 
ATOM   614   C  CB  . SER A  1 74  ? 41.501  3.341   8.975   1.00 23.38 ? 74  SER A CB  1 
ATOM   615   O  OG  . SER A  1 74  ? 42.764  3.640   9.459   1.00 25.41 ? 74  SER A OG  1 
ATOM   616   N  N   . ASP A  1 75  ? 42.901  0.227   9.687   1.00 16.41 ? 75  ASP A N   1 
ATOM   617   C  CA  . ASP A  1 75  ? 43.558  -0.926  9.040   1.00 17.92 ? 75  ASP A CA  1 
ATOM   618   C  C   . ASP A  1 75  ? 42.639  -2.165  8.877   1.00 14.89 ? 75  ASP A C   1 
ATOM   619   O  O   . ASP A  1 75  ? 42.955  -3.156  8.223   1.00 18.58 ? 75  ASP A O   1 
ATOM   620   C  CB  . ASP A  1 75  ? 44.881  -1.257  9.792   1.00 18.46 ? 75  ASP A CB  1 
ATOM   621   C  CG  . ASP A  1 75  ? 44.627  -1.725  11.176  1.00 19.47 ? 75  ASP A CG  1 
ATOM   622   O  OD1 . ASP A  1 75  ? 44.263  -0.849  11.992  1.00 22.50 ? 75  ASP A OD1 1 
ATOM   623   O  OD2 . ASP A  1 75  ? 45.023  -2.894  11.479  1.00 22.94 ? 75  ASP A OD2 1 
ATOM   624   N  N   . MET A  1 76  ? 41.441  -2.145  9.513   1.00 13.59 ? 76  MET A N   1 
ATOM   625   C  CA  . MET A  1 76  ? 40.485  -3.187  9.354   1.00 14.62 ? 76  MET A CA  1 
ATOM   626   C  C   . MET A  1 76  ? 39.673  -2.888  8.084   1.00 12.15 ? 76  MET A C   1 
ATOM   627   O  O   . MET A  1 76  ? 39.272  -1.728  7.905   1.00 13.47 ? 76  MET A O   1 
ATOM   628   C  CB  . MET A  1 76  ? 39.654  -3.052  10.590  1.00 18.01 ? 76  MET A CB  1 
ATOM   629   C  CG  . MET A  1 76  ? 38.535  -3.973  10.623  1.00 14.65 ? 76  MET A CG  1 
ATOM   630   S  SD  . MET A  1 76  ? 37.773  -3.953  12.294  1.00 14.97 ? 76  MET A SD  1 
ATOM   631   C  CE  . MET A  1 76  ? 36.197  -4.685  11.787  1.00 14.25 ? 76  MET A CE  1 
ATOM   632   N  N   . HIS A  1 77  ? 39.587  -3.830  7.214   1.00 11.94 ? 77  HIS A N   1 
ATOM   633   C  CA  . HIS A  1 77  ? 38.848  -3.584  5.945   1.00 13.53 ? 77  HIS A CA  1 
ATOM   634   C  C   . HIS A  1 77  ? 38.264  -4.792  5.333   1.00 12.45 ? 77  HIS A C   1 
ATOM   635   O  O   . HIS A  1 77  ? 38.573  -5.965  5.653   1.00 13.78 ? 77  HIS A O   1 
ATOM   636   C  CB  . HIS A  1 77  ? 39.726  -2.825  4.956   1.00 15.78 ? 77  HIS A CB  1 
ATOM   637   C  CG  . HIS A  1 77  ? 40.942  -3.616  4.569   1.00 17.52 ? 77  HIS A CG  1 
ATOM   638   N  ND1 . HIS A  1 77  ? 42.168  -3.351  5.118   1.00 20.69 ? 77  HIS A ND1 1 
ATOM   639   C  CD2 . HIS A  1 77  ? 41.126  -4.575  3.647   1.00 22.99 ? 77  HIS A CD2 1 
ATOM   640   C  CE1 . HIS A  1 77  ? 43.055  -4.171  4.607   1.00 19.07 ? 77  HIS A CE1 1 
ATOM   641   N  NE2 . HIS A  1 77  ? 42.469  -4.933  3.699   1.00 23.52 ? 77  HIS A NE2 1 
ATOM   642   N  N   . ILE A  1 78  ? 37.330  -4.545  4.408   1.00 12.28 ? 78  ILE A N   1 
ATOM   643   C  CA  . ILE A  1 78  ? 36.752  -5.579  3.543   1.00 13.36 ? 78  ILE A CA  1 
ATOM   644   C  C   . ILE A  1 78  ? 37.510  -5.642  2.296   1.00 14.13 ? 78  ILE A C   1 
ATOM   645   O  O   . ILE A  1 78  ? 37.751  -4.536  1.714   1.00 14.36 ? 78  ILE A O   1 
ATOM   646   C  CB  . ILE A  1 78  ? 35.253  -5.198  3.212   1.00 13.93 ? 78  ILE A CB  1 
ATOM   647   C  CG1 . ILE A  1 78  ? 34.371  -5.280  4.476   1.00 16.02 ? 78  ILE A CG1 1 
ATOM   648   C  CG2 . ILE A  1 78  ? 34.670  -6.155  2.163   1.00 18.09 ? 78  ILE A CG2 1 
ATOM   649   C  CD1 . ILE A  1 78  ? 33.017  -4.536  4.285   1.00 14.37 ? 78  ILE A CD1 1 
ATOM   650   N  N   . GLN A  1 79  ? 37.895  -6.844  1.884   1.00 14.23 ? 79  GLN A N   1 
ATOM   651   C  CA  . GLN A  1 79  ? 38.425  -7.005  0.568   1.00 17.22 ? 79  GLN A CA  1 
ATOM   652   C  C   . GLN A  1 79  ? 37.404  -7.827  -0.232  1.00 16.42 ? 79  GLN A C   1 
ATOM   653   O  O   . GLN A  1 79  ? 36.751  -8.741  0.297   1.00 17.61 ? 79  GLN A O   1 
ATOM   654   C  CB  . GLN A  1 79  ? 39.751  -7.799  0.761   1.00 21.78 ? 79  GLN A CB  1 
ATOM   655   C  CG  . GLN A  1 79  ? 40.388  -8.296  -0.559  1.00 29.42 ? 79  GLN A CG  1 
ATOM   656   C  CD  . GLN A  1 79  ? 41.267  -7.236  -1.196  1.00 42.69 ? 79  GLN A CD  1 
ATOM   657   O  OE1 . GLN A  1 79  ? 41.052  -6.024  -0.999  1.00 50.23 ? 79  GLN A OE1 1 
ATOM   658   N  NE2 . GLN A  1 79  ? 42.278  -7.673  -1.965  1.00 46.98 ? 79  GLN A NE2 1 
ATOM   659   N  N   . GLY A  1 80  ? 37.307  -7.553  -1.516  1.00 16.73 ? 80  GLY A N   1 
ATOM   660   C  CA  . GLY A  1 80  ? 36.330  -8.270  -2.381  1.00 17.62 ? 80  GLY A CA  1 
ATOM   661   C  C   . GLY A  1 80  ? 35.397  -7.358  -3.168  1.00 17.74 ? 80  GLY A C   1 
ATOM   662   O  O   . GLY A  1 80  ? 34.739  -7.760  -4.160  1.00 19.81 ? 80  GLY A O   1 
ATOM   663   N  N   . LEU A  1 81  ? 35.203  -6.142  -2.687  1.00 14.93 ? 81  LEU A N   1 
ATOM   664   C  CA  . LEU A  1 81  ? 34.414  -5.117  -3.365  1.00 16.93 ? 81  LEU A CA  1 
ATOM   665   C  C   . LEU A  1 81  ? 35.340  -4.412  -4.395  1.00 17.84 ? 81  LEU A C   1 
ATOM   666   O  O   . LEU A  1 81  ? 36.508  -4.676  -4.462  1.00 21.37 ? 81  LEU A O   1 
ATOM   667   C  CB  . LEU A  1 81  ? 33.752  -4.158  -2.356  1.00 15.49 ? 81  LEU A CB  1 
ATOM   668   C  CG  . LEU A  1 81  ? 32.760  -4.833  -1.349  1.00 15.50 ? 81  LEU A CG  1 
ATOM   669   C  CD1 . LEU A  1 81  ? 32.254  -3.940  -0.242  1.00 16.08 ? 81  LEU A CD1 1 
ATOM   670   C  CD2 . LEU A  1 81  ? 31.546  -5.478  -2.121  1.00 18.92 ? 81  LEU A CD2 1 
ATOM   671   N  N   . GLN A  1 82  ? 34.774  -3.521  -5.178  1.00 22.39 ? 82  GLN A N   1 
ATOM   672   C  CA  . GLN A  1 82  ? 35.642  -2.905  -6.217  1.00 23.75 ? 82  GLN A CA  1 
ATOM   673   C  C   . GLN A  1 82  ? 36.713  -1.994  -5.603  1.00 21.15 ? 82  GLN A C   1 
ATOM   674   O  O   . GLN A  1 82  ? 37.918  -1.973  -6.086  1.00 22.73 ? 82  GLN A O   1 
ATOM   675   C  CB  . GLN A  1 82  ? 34.768  -2.102  -7.153  1.00 30.00 ? 82  GLN A CB  1 
ATOM   676   C  CG  . GLN A  1 82  ? 34.071  -2.905  -8.256  1.00 44.39 ? 82  GLN A CG  1 
ATOM   677   C  CD  . GLN A  1 82  ? 34.949  -3.025  -9.508  1.00 50.33 ? 82  GLN A CD  1 
ATOM   678   O  OE1 . GLN A  1 82  ? 35.034  -2.088  -10.349 1.00 51.99 ? 82  GLN A OE1 1 
ATOM   679   N  NE2 . GLN A  1 82  ? 35.643  -4.158  -9.614  1.00 38.84 ? 82  GLN A NE2 1 
ATOM   680   N  N   . SER A  1 83  ? 36.314  -1.303  -4.532  1.00 17.57 ? 83  SER A N   1 
ATOM   681   C  CA  . SER A  1 83  ? 37.244  -0.458  -3.763  1.00 14.56 ? 83  SER A CA  1 
ATOM   682   C  C   . SER A  1 83  ? 37.422  -1.182  -2.423  1.00 13.29 ? 83  SER A C   1 
ATOM   683   O  O   . SER A  1 83  ? 36.550  -1.993  -2.015  1.00 11.68 ? 83  SER A O   1 
ATOM   684   C  CB  . SER A  1 83  ? 36.616  0.882   -3.458  1.00 13.01 ? 83  SER A CB  1 
ATOM   685   O  OG  . SER A  1 83  ? 36.508  1.655   -4.680  1.00 15.79 ? 83  SER A OG  1 
ATOM   686   N  N   . ARG A  1 84  ? 38.485  -0.758  -1.736  1.00 13.59 ? 84  ARG A N   1 
ATOM   687   C  CA  . ARG A  1 84  ? 38.697  -1.228  -0.375  1.00 12.29 ? 84  ARG A CA  1 
ATOM   688   C  C   . ARG A  1 84  ? 37.772  -0.333  0.481   1.00 10.44 ? 84  ARG A C   1 
ATOM   689   O  O   . ARG A  1 84  ? 37.651  0.866   0.330   1.00 11.44 ? 84  ARG A O   1 
ATOM   690   C  CB  . ARG A  1 84  ? 40.128  -0.897  0.038   1.00 11.30 ? 84  ARG A CB  1 
ATOM   691   C  CG  . ARG A  1 84  ? 40.322  -1.270  1.542   1.00 12.64 ? 84  ARG A CG  1 
ATOM   692   C  CD  . ARG A  1 84  ? 41.766  -0.995  2.071   1.00 13.23 ? 84  ARG A CD  1 
ATOM   693   N  NE  . ARG A  1 84  ? 42.552  -2.096  1.615   1.00 14.05 ? 84  ARG A NE  1 
ATOM   694   C  CZ  . ARG A  1 84  ? 43.832  -2.202  1.880   1.00 16.18 ? 84  ARG A CZ  1 
ATOM   695   N  NH1 . ARG A  1 84  ? 44.425  -1.249  2.584   1.00 17.08 ? 84  ARG A NH1 1 
ATOM   696   N  NH2 . ARG A  1 84  ? 44.495  -3.252  1.441   1.00 17.65 ? 84  ARG A NH2 1 
ATOM   697   N  N   . TYR A  1 85  ? 37.064  -1.055  1.444   1.00 10.46 ? 85  TYR A N   1 
ATOM   698   C  CA  . TYR A  1 85  ? 36.161  -0.326  2.399   1.00 10.54 ? 85  TYR A CA  1 
ATOM   699   C  C   . TYR A  1 85  ? 36.800  -0.579  3.789   1.00 10.10 ? 85  TYR A C   1 
ATOM   700   O  O   . TYR A  1 85  ? 36.908  -1.733  4.222   1.00 11.89 ? 85  TYR A O   1 
ATOM   701   C  CB  . TYR A  1 85  ? 34.706  -0.777  2.381   1.00 11.31 ? 85  TYR A CB  1 
ATOM   702   C  CG  . TYR A  1 85  ? 33.978  -0.260  1.175   1.00 9.50  ? 85  TYR A CG  1 
ATOM   703   C  CD1 . TYR A  1 85  ? 34.130  -0.849  -0.075  1.00 11.17 ? 85  TYR A CD1 1 
ATOM   704   C  CD2 . TYR A  1 85  ? 33.164  0.840   1.286   1.00 10.50 ? 85  TYR A CD2 1 
ATOM   705   C  CE1 . TYR A  1 85  ? 33.463  -0.348  -1.186  1.00 11.62 ? 85  TYR A CE1 1 
ATOM   706   C  CE2 . TYR A  1 85  ? 32.493  1.347   0.197   1.00 9.49  ? 85  TYR A CE2 1 
ATOM   707   C  CZ  . TYR A  1 85  ? 32.639  0.760   -1.045  1.00 10.19 ? 85  TYR A CZ  1 
ATOM   708   O  OH  . TYR A  1 85  ? 31.967  1.273   -2.128  1.00 16.07 ? 85  TYR A OH  1 
ATOM   709   N  N   . SER A  1 86  ? 37.188  0.488   4.448   1.00 9.99  ? 86  SER A N   1 
ATOM   710   C  CA  . SER A  1 86  ? 37.870  0.417   5.765   1.00 10.23 ? 86  SER A CA  1 
ATOM   711   C  C   . SER A  1 86  ? 36.861  0.611   6.872   1.00 10.40 ? 86  SER A C   1 
ATOM   712   O  O   . SER A  1 86  ? 35.964  1.430   6.745   1.00 10.88 ? 86  SER A O   1 
ATOM   713   C  CB  . SER A  1 86  ? 38.919  1.462   5.865   1.00 12.30 ? 86  SER A CB  1 
ATOM   714   O  OG  . SER A  1 86  ? 39.973  1.127   4.931   1.00 14.73 ? 86  SER A OG  1 
ATOM   715   N  N   . ALA A  1 87  ? 37.021  -0.100  8.000   1.00 10.39 ? 87  ALA A N   1 
ATOM   716   C  CA  . ALA A  1 87  ? 36.048  0.035   9.098   1.00 9.83  ? 87  ALA A CA  1 
ATOM   717   C  C   . ALA A  1 87  ? 36.145  1.362   9.763   1.00 10.67 ? 87  ALA A C   1 
ATOM   718   O  O   . ALA A  1 87  ? 37.245  1.992   9.830   1.00 12.88 ? 87  ALA A O   1 
ATOM   719   C  CB  . ALA A  1 87  ? 36.317  -1.057  10.085  1.00 12.93 ? 87  ALA A CB  1 
ATOM   720   N  N   . THR A  1 88  ? 35.041  1.828   10.288  1.00 10.19 ? 88  THR A N   1 
ATOM   721   C  CA  . THR A  1 88  ? 35.035  2.984   11.190  1.00 10.32 ? 88  THR A CA  1 
ATOM   722   C  C   . THR A  1 88  ? 34.396  2.693   12.518  1.00 10.06 ? 88  THR A C   1 
ATOM   723   O  O   . THR A  1 88  ? 34.862  3.221   13.513  1.00 11.34 ? 88  THR A O   1 
ATOM   724   C  CB  . THR A  1 88  ? 34.426  4.154   10.449  1.00 11.39 ? 88  THR A CB  1 
ATOM   725   O  OG1 . THR A  1 88  ? 34.346  5.295   11.275  1.00 15.64 ? 88  THR A OG1 1 
ATOM   726   C  CG2 . THR A  1 88  ? 33.015  3.916   10.027  1.00 12.39 ? 88  THR A CG2 1 
ATOM   727   N  N   . GLN A  1 89  ? 33.327  1.885   12.596  1.00 9.61  ? 89  GLN A N   1 
ATOM   728   C  CA  . GLN A  1 89  ? 32.627  1.649   13.854  1.00 9.60  ? 89  GLN A CA  1 
ATOM   729   C  C   . GLN A  1 89  ? 31.639  0.527   13.659  1.00 10.02 ? 89  GLN A C   1 
ATOM   730   O  O   . GLN A  1 89  ? 31.234  0.196   12.531  1.00 9.70  ? 89  GLN A O   1 
ATOM   731   C  CB  . GLN A  1 89  ? 31.886  2.880   14.383  1.00 10.42 ? 89  GLN A CB  1 
ATOM   732   C  CG  . GLN A  1 89  ? 30.970  3.569   13.391  1.00 12.95 ? 89  GLN A CG  1 
ATOM   733   C  CD  . GLN A  1 89  ? 29.513  3.338   13.751  1.00 13.51 ? 89  GLN A CD  1 
ATOM   734   O  OE1 . GLN A  1 89  ? 29.119  2.260   14.087  1.00 12.93 ? 89  GLN A OE1 1 
ATOM   735   N  NE2 . GLN A  1 89  ? 28.709  4.330   13.521  1.00 19.76 ? 89  GLN A NE2 1 
ATOM   736   N  N   . LEU A  1 90  ? 31.307  -0.093  14.780  1.00 9.33  ? 90  LEU A N   1 
ATOM   737   C  CA  . LEU A  1 90  ? 30.139  -1.003  14.851  1.00 9.20  ? 90  LEU A CA  1 
ATOM   738   C  C   . LEU A  1 90  ? 29.199  -0.594  15.866  1.00 8.29  ? 90  LEU A C   1 
ATOM   739   O  O   . LEU A  1 90  ? 29.531  0.103   16.798  1.00 9.77  ? 90  LEU A O   1 
ATOM   740   C  CB  . LEU A  1 90  ? 30.562  -2.495  14.936  1.00 9.92  ? 90  LEU A CB  1 
ATOM   741   C  CG  . LEU A  1 90  ? 31.340  -2.942  16.192  1.00 9.84  ? 90  LEU A CG  1 
ATOM   742   C  CD1 . LEU A  1 90  ? 30.472  -3.031  17.436  1.00 10.88 ? 90  LEU A CD1 1 
ATOM   743   C  CD2 . LEU A  1 90  ? 31.955  -4.296  15.832  1.00 11.23 ? 90  LEU A CD2 1 
ATOM   744   N  N   . HIS A  1 91  ? 27.934  -1.002  15.686  1.00 8.72  ? 91  HIS A N   1 
ATOM   745   C  CA  . HIS A  1 91  ? 26.881  -0.675  16.662  1.00 7.75  ? 91  HIS A CA  1 
ATOM   746   C  C   . HIS A  1 91  ? 25.706  -1.616  16.476  1.00 8.15  ? 91  HIS A C   1 
ATOM   747   O  O   . HIS A  1 91  ? 25.761  -2.463  15.583  1.00 8.13  ? 91  HIS A O   1 
ATOM   748   C  CB  . HIS A  1 91  ? 26.434  0.802   16.493  1.00 8.93  ? 91  HIS A CB  1 
ATOM   749   C  CG  . HIS A  1 91  ? 25.789  1.023   15.148  1.00 9.02  ? 91  HIS A CG  1 
ATOM   750   N  ND1 . HIS A  1 91  ? 26.517  1.429   14.053  1.00 9.23  ? 91  HIS A ND1 1 
ATOM   751   C  CD2 . HIS A  1 91  ? 24.552  0.710   14.712  1.00 9.37  ? 91  HIS A CD2 1 
ATOM   752   C  CE1 . HIS A  1 91  ? 25.724  1.415   12.960  1.00 9.26  ? 91  HIS A CE1 1 
ATOM   753   N  NE2 . HIS A  1 91  ? 24.522  0.961   13.338  1.00 7.40  ? 91  HIS A NE2 1 
ATOM   754   N  N   . LEU A  1 92  ? 24.734  -1.503  17.383  1.00 8.31  ? 92  LEU A N   1 
ATOM   755   C  CA  . LEU A  1 92  ? 23.621  -2.429  17.329  1.00 8.17  ? 92  LEU A CA  1 
ATOM   756   C  C   . LEU A  1 92  ? 22.243  -1.734  17.383  1.00 7.48  ? 92  LEU A C   1 
ATOM   757   O  O   . LEU A  1 92  ? 22.137  -0.582  17.699  1.00 8.53  ? 92  LEU A O   1 
ATOM   758   C  CB  . LEU A  1 92  ? 23.658  -3.409  18.542  1.00 10.87 ? 92  LEU A CB  1 
ATOM   759   C  CG  . LEU A  1 92  ? 24.925  -4.310  18.488  1.00 10.01 ? 92  LEU A CG  1 
ATOM   760   C  CD1 . LEU A  1 92  ? 25.984  -3.785  19.453  1.00 14.35 ? 92  LEU A CD1 1 
ATOM   761   C  CD2 . LEU A  1 92  ? 24.490  -5.697  18.794  1.00 13.32 ? 92  LEU A CD2 1 
ATOM   762   N  N   . HIS A  1 93  ? 21.215  -2.502  17.032  1.00 7.55  ? 93  HIS A N   1 
ATOM   763   C  CA  . HIS A  1 93  ? 19.796  -2.052  17.113  1.00 8.11  ? 93  HIS A CA  1 
ATOM   764   C  C   . HIS A  1 93  ? 19.025  -3.161  17.739  1.00 8.26  ? 93  HIS A C   1 
ATOM   765   O  O   . HIS A  1 93  ? 19.312  -4.347  17.486  1.00 9.13  ? 93  HIS A O   1 
ATOM   766   C  CB  . HIS A  1 93  ? 19.260  -1.851  15.647  1.00 8.17  ? 93  HIS A CB  1 
ATOM   767   C  CG  . HIS A  1 93  ? 20.043  -0.838  14.880  1.00 7.52  ? 93  HIS A CG  1 
ATOM   768   N  ND1 . HIS A  1 93  ? 19.693  0.509   14.841  1.00 7.85  ? 93  HIS A ND1 1 
ATOM   769   C  CD2 . HIS A  1 93  ? 21.146  -0.965  14.082  1.00 6.94  ? 93  HIS A CD2 1 
ATOM   770   C  CE1 . HIS A  1 93  ? 20.577  1.174   14.059  1.00 8.09  ? 93  HIS A CE1 1 
ATOM   771   N  NE2 . HIS A  1 93  ? 21.449  0.294   13.569  1.00 7.59  ? 93  HIS A NE2 1 
ATOM   772   N  N   . TRP A  1 94  ? 18.082  -2.805  18.567  1.00 8.77  ? 94  TRP A N   1 
ATOM   773   C  CA  . TRP A  1 94  ? 17.321  -3.834  19.306  1.00 8.35  ? 94  TRP A CA  1 
ATOM   774   C  C   . TRP A  1 94  ? 15.936  -3.323  19.677  1.00 9.04  ? 94  TRP A C   1 
ATOM   775   O  O   . TRP A  1 94  ? 15.616  -2.142  19.463  1.00 7.88  ? 94  TRP A O   1 
ATOM   776   C  CB  . TRP A  1 94  ? 18.069  -4.257  20.615  1.00 8.36  ? 94  TRP A CB  1 
ATOM   777   C  CG  . TRP A  1 94  ? 18.390  -3.098  21.535  1.00 8.67  ? 94  TRP A CG  1 
ATOM   778   C  CD1 . TRP A  1 94  ? 17.585  -2.620  22.527  1.00 9.12  ? 94  TRP A CD1 1 
ATOM   779   C  CD2 . TRP A  1 94  ? 19.573  -2.297  21.539  1.00 8.15  ? 94  TRP A CD2 1 
ATOM   780   N  NE1 . TRP A  1 94  ? 18.187  -1.543  23.150  1.00 9.58  ? 94  TRP A NE1 1 
ATOM   781   C  CE2 . TRP A  1 94  ? 19.438  -1.349  22.585  1.00 9.07  ? 94  TRP A CE2 1 
ATOM   782   C  CE3 . TRP A  1 94  ? 20.743  -2.285  20.752  1.00 8.30  ? 94  TRP A CE3 1 
ATOM   783   C  CZ2 . TRP A  1 94  ? 20.416  -0.386  22.887  1.00 8.93  ? 94  TRP A CZ2 1 
ATOM   784   C  CZ3 . TRP A  1 94  ? 21.736  -1.309  21.002  1.00 8.31  ? 94  TRP A CZ3 1 
ATOM   785   C  CH2 . TRP A  1 94  ? 21.587  -0.376  22.069  1.00 9.58  ? 94  TRP A CH2 1 
ATOM   786   N  N   . GLY A  1 95  ? 15.159  -4.211  20.267  1.00 8.13  ? 95  GLY A N   1 
ATOM   787   C  CA  . GLY A  1 95  ? 13.760  -3.911  20.643  1.00 9.27  ? 95  GLY A CA  1 
ATOM   788   C  C   . GLY A  1 95  ? 13.653  -3.568  22.124  1.00 8.80  ? 95  GLY A C   1 
ATOM   789   O  O   . GLY A  1 95  ? 14.285  -2.682  22.677  1.00 9.05  ? 95  GLY A O   1 
ATOM   790   N  N   . ASN A  1 96  ? 12.823  -4.384  22.814  1.00 9.94  ? 96  ASN A N   1 
ATOM   791   C  CA  . ASN A  1 96  ? 12.653  -4.141  24.290  1.00 10.26 ? 96  ASN A CA  1 
ATOM   792   C  C   . ASN A  1 96  ? 12.120  -5.481  24.866  1.00 11.23 ? 96  ASN A C   1 
ATOM   793   O  O   . ASN A  1 96  ? 11.667  -6.346  24.127  1.00 10.11 ? 96  ASN A O   1 
ATOM   794   C  CB  . ASN A  1 96  ? 11.648  -2.987  24.522  1.00 11.95 ? 96  ASN A CB  1 
ATOM   795   C  CG  . ASN A  1 96  ? 10.229  -3.365  24.213  1.00 14.34 ? 96  ASN A CG  1 
ATOM   796   O  OD1 . ASN A  1 96  ? 9.552   -3.921  25.125  1.00 17.07 ? 96  ASN A OD1 1 
ATOM   797   N  ND2 . ASN A  1 96  ? 9.722   -3.081  23.038  1.00 15.04 ? 96  ASN A ND2 1 
ATOM   798   N  N   . PRO A  1 97  ? 12.169  -5.622  26.214  1.00 11.03 ? 97  PRO A N   1 
ATOM   799   C  CA  . PRO A  1 97  ? 11.837  -6.926  26.731  1.00 11.56 ? 97  PRO A CA  1 
ATOM   800   C  C   . PRO A  1 97  ? 10.415  -7.369  26.539  1.00 11.08 ? 97  PRO A C   1 
ATOM   801   O  O   . PRO A  1 97  ? 10.203  -8.558  26.537  1.00 12.84 ? 97  PRO A O   1 
ATOM   802   C  CB  . PRO A  1 97  ? 12.177  -6.804  28.222  1.00 12.79 ? 97  PRO A CB  1 
ATOM   803   C  CG  . PRO A  1 97  ? 13.265  -5.725  28.272  1.00 13.02 ? 97  PRO A CG  1 
ATOM   804   C  CD  . PRO A  1 97  ? 12.751  -4.759  27.246  1.00 11.92 ? 97  PRO A CD  1 
ATOM   805   N  N   . ASN A  1 98  ? 9.472   -6.465  26.395  1.00 11.55 ? 98  ASN A N   1 
ATOM   806   C  CA  . ASN A  1 98  ? 8.095   -6.904  26.065  1.00 14.93 ? 98  ASN A CA  1 
ATOM   807   C  C   . ASN A  1 98  ? 7.857   -7.238  24.619  1.00 13.29 ? 98  ASN A C   1 
ATOM   808   O  O   . ASN A  1 98  ? 6.886   -7.886  24.279  1.00 15.55 ? 98  ASN A O   1 
ATOM   809   C  CB  . ASN A  1 98  ? 7.158   -5.743  26.433  1.00 15.25 ? 98  ASN A CB  1 
ATOM   810   C  CG  . ASN A  1 98  ? 6.987   -5.617  27.897  1.00 24.08 ? 98  ASN A CG  1 
ATOM   811   O  OD1 . ASN A  1 98  ? 6.965   -6.611  28.603  1.00 27.53 ? 98  ASN A OD1 1 
ATOM   812   N  ND2 . ASN A  1 98  ? 6.772   -4.385  28.356  1.00 26.11 ? 98  ASN A ND2 1 
ATOM   813   N  N   . ASP A  1 99  ? 8.778   -6.836  23.727  1.00 11.81 ? 99  ASP A N   1 
ATOM   814   C  CA  . ASP A  1 99  ? 8.643   -7.144  22.313  1.00 12.46 ? 99  ASP A CA  1 
ATOM   815   C  C   . ASP A  1 99  ? 10.081  -7.242  21.731  1.00 10.72 ? 99  ASP A C   1 
ATOM   816   O  O   . ASP A  1 99  ? 10.598  -6.309  21.144  1.00 11.35 ? 99  ASP A O   1 
ATOM   817   C  CB  . ASP A  1 99  ? 7.775   -6.062  21.573  1.00 12.56 ? 99  ASP A CB  1 
ATOM   818   C  CG  . ASP A  1 99  ? 7.284   -6.527  20.206  1.00 15.22 ? 99  ASP A CG  1 
ATOM   819   O  OD1 . ASP A  1 99  ? 7.659   -7.573  19.714  1.00 16.77 ? 99  ASP A OD1 1 
ATOM   820   O  OD2 . ASP A  1 99  ? 6.463   -5.794  19.660  1.00 19.76 ? 99  ASP A OD2 1 
ATOM   821   N  N   . PRO A  1 100 ? 10.755  -8.366  21.993  1.00 9.78  ? 100 PRO A N   1 
ATOM   822   C  CA  . PRO A  1 100 ? 12.202  -8.459  21.799  1.00 9.84  ? 100 PRO A CA  1 
ATOM   823   C  C   . PRO A  1 100 ? 12.578  -8.832  20.412  1.00 11.64 ? 100 PRO A C   1 
ATOM   824   O  O   . PRO A  1 100 ? 13.156  -9.845  20.072  1.00 11.02 ? 100 PRO A O   1 
ATOM   825   C  CB  . PRO A  1 100 ? 12.629  -9.487  22.864  1.00 11.27 ? 100 PRO A CB  1 
ATOM   826   C  CG  . PRO A  1 100 ? 11.411  -10.451 22.870  1.00 10.77 ? 100 PRO A CG  1 
ATOM   827   C  CD  . PRO A  1 100 ? 10.226  -9.515  22.792  1.00 11.14 ? 100 PRO A CD  1 
ATOM   828   N  N   . HIS A  1 101 ? 12.128  -7.955  19.513  1.00 10.77 ? 101 HIS A N   1 
ATOM   829   C  CA  . HIS A  1 101 ? 12.233  -8.254  18.025  1.00 11.78 ? 101 HIS A CA  1 
ATOM   830   C  C   . HIS A  1 101 ? 12.560  -6.968  17.313  1.00 12.54 ? 101 HIS A C   1 
ATOM   831   O  O   . HIS A  1 101 ? 11.778  -6.470  16.501  1.00 15.73 ? 101 HIS A O   1 
ATOM   832   C  CB  . HIS A  1 101 ? 10.900  -8.781  17.468  1.00 13.12 ? 101 HIS A CB  1 
ATOM   833   C  CG  . HIS A  1 101 ? 10.368  -9.911  18.274  1.00 13.61 ? 101 HIS A CG  1 
ATOM   834   N  ND1 . HIS A  1 101 ? 10.845  -11.198 18.204  1.00 14.89 ? 101 HIS A ND1 1 
ATOM   835   C  CD2 . HIS A  1 101 ? 9.339   -9.908  19.153  1.00 13.82 ? 101 HIS A CD2 1 
ATOM   836   C  CE1 . HIS A  1 101 ? 10.190  -11.942 19.096  1.00 15.19 ? 101 HIS A CE1 1 
ATOM   837   N  NE2 . HIS A  1 101 ? 9.282   -11.163 19.678  1.00 15.14 ? 101 HIS A NE2 1 
ATOM   838   N  N   . GLY A  1 102 ? 13.797  -6.512  17.502  1.00 8.91  ? 102 GLY A N   1 
ATOM   839   C  CA  . GLY A  1 102 ? 14.194  -5.197  17.092  1.00 9.58  ? 102 GLY A CA  1 
ATOM   840   C  C   . GLY A  1 102 ? 15.315  -5.154  16.038  1.00 8.48  ? 102 GLY A C   1 
ATOM   841   O  O   . GLY A  1 102 ? 16.041  -4.134  15.988  1.00 9.77  ? 102 GLY A O   1 
ATOM   842   N  N   . SER A  1 103 ? 15.456  -6.182  15.216  1.00 8.47  ? 103 SER A N   1 
ATOM   843   C  CA  . SER A  1 103 ? 16.326  -5.988  14.029  1.00 7.95  ? 103 SER A CA  1 
ATOM   844   C  C   . SER A  1 103 ? 15.741  -4.903  13.136  1.00 8.28  ? 103 SER A C   1 
ATOM   845   O  O   . SER A  1 103 ? 14.560  -4.530  13.232  1.00 10.03 ? 103 SER A O   1 
ATOM   846   C  CB  . SER A  1 103 ? 16.502  -7.295  13.271  1.00 8.02  ? 103 SER A CB  1 
ATOM   847   O  OG  . SER A  1 103 ? 15.232  -7.716  12.663  1.00 8.49  ? 103 SER A OG  1 
ATOM   848   N  N   . GLU A  1 104 ? 16.589  -4.405  12.259  1.00 7.48  ? 104 GLU A N   1 
ATOM   849   C  CA  . GLU A  1 104 ? 16.135  -3.401  11.247  1.00 7.51  ? 104 GLU A CA  1 
ATOM   850   C  C   . GLU A  1 104 ? 15.643  -4.107  10.008  1.00 7.69  ? 104 GLU A C   1 
ATOM   851   O  O   . GLU A  1 104 ? 14.487  -3.907  9.591   1.00 7.94  ? 104 GLU A O   1 
ATOM   852   C  CB  . GLU A  1 104 ? 17.288  -2.447  10.953  1.00 7.73  ? 104 GLU A CB  1 
ATOM   853   C  CG  . GLU A  1 104 ? 17.784  -1.727  12.219  1.00 7.85  ? 104 GLU A CG  1 
ATOM   854   C  CD  . GLU A  1 104 ? 18.155  -0.301  11.899  1.00 8.11  ? 104 GLU A CD  1 
ATOM   855   O  OE1 . GLU A  1 104 ? 19.233  -0.135  11.327  1.00 9.25  ? 104 GLU A OE1 1 
ATOM   856   O  OE2 . GLU A  1 104 ? 17.341  0.582   12.166  1.00 9.65  ? 104 GLU A OE2 1 
ATOM   857   N  N   . HIS A  1 105 ? 16.508  -4.896  9.379   1.00 7.05  ? 105 HIS A N   1 
ATOM   858   C  CA  . HIS A  1 105 ? 16.055  -5.757  8.280   1.00 7.28  ? 105 HIS A CA  1 
ATOM   859   C  C   . HIS A  1 105 ? 15.105  -6.827  8.832   1.00 7.73  ? 105 HIS A C   1 
ATOM   860   O  O   . HIS A  1 105 ? 15.283  -7.333  9.960   1.00 8.41  ? 105 HIS A O   1 
ATOM   861   C  CB  . HIS A  1 105 ? 17.224  -6.355  7.534   1.00 7.82  ? 105 HIS A CB  1 
ATOM   862   C  CG  . HIS A  1 105 ? 17.992  -5.316  6.801   1.00 8.21  ? 105 HIS A CG  1 
ATOM   863   N  ND1 . HIS A  1 105 ? 19.029  -4.593  7.351   1.00 8.21  ? 105 HIS A ND1 1 
ATOM   864   C  CD2 . HIS A  1 105 ? 17.774  -4.794  5.562   1.00 7.69  ? 105 HIS A CD2 1 
ATOM   865   C  CE1 . HIS A  1 105 ? 19.447  -3.674  6.457   1.00 9.10  ? 105 HIS A CE1 1 
ATOM   866   N  NE2 . HIS A  1 105 ? 18.707  -3.801  5.356   1.00 9.16  ? 105 HIS A NE2 1 
ATOM   867   N  N   . THR A  1 106 ? 14.185  -7.196  7.967   1.00 7.83  ? 106 THR A N   1 
ATOM   868   C  CA  . THR A  1 106 ? 13.315  -8.361  8.227   1.00 8.43  ? 106 THR A CA  1 
ATOM   869   C  C   . THR A  1 106 ? 13.490  -9.355  7.166   1.00 8.51  ? 106 THR A C   1 
ATOM   870   O  O   . THR A  1 106 ? 13.960  -9.096  6.071   1.00 8.99  ? 106 THR A O   1 
ATOM   871   C  CB  . THR A  1 106 ? 11.826  -7.965  8.454   1.00 8.82  ? 106 THR A CB  1 
ATOM   872   O  OG1 . THR A  1 106 ? 11.363  -7.356  7.207   1.00 9.54  ? 106 THR A OG1 1 
ATOM   873   C  CG2 . THR A  1 106 ? 11.698  -7.021  9.588   1.00 10.01 ? 106 THR A CG2 1 
ATOM   874   N  N   . VAL A  1 107 ? 13.139  -10.633 7.512   1.00 9.08  ? 107 VAL A N   1 
ATOM   875   C  CA  . VAL A  1 107 ? 13.219  -11.749 6.522   1.00 9.76  ? 107 VAL A CA  1 
ATOM   876   C  C   . VAL A  1 107 ? 11.819  -12.383 6.407   1.00 8.93  ? 107 VAL A C   1 
ATOM   877   O  O   . VAL A  1 107 ? 11.287  -12.831 7.411   1.00 10.24 ? 107 VAL A O   1 
ATOM   878   C  CB  . VAL A  1 107 ? 14.285  -12.801 6.838   1.00 10.11 ? 107 VAL A CB  1 
ATOM   879   C  CG1 . VAL A  1 107 ? 14.253  -13.885 5.812   1.00 11.40 ? 107 VAL A CG1 1 
ATOM   880   C  CG2 . VAL A  1 107 ? 15.730  -12.153 6.876   1.00 11.89 ? 107 VAL A CG2 1 
ATOM   881   N  N   . SER A  1 108 ? 11.231  -12.301 5.233   1.00 10.55 ? 108 SER A N   1 
ATOM   882   C  CA  . SER A  1 108 ? 9.832   -12.814 5.048   1.00 12.04 ? 108 SER A CA  1 
ATOM   883   C  C   . SER A  1 108 ? 8.926   -12.221 6.077   1.00 11.28 ? 108 SER A C   1 
ATOM   884   O  O   . SER A  1 108 ? 8.051   -12.904 6.668   1.00 11.28 ? 108 SER A O   1 
ATOM   885   C  CB  . SER A  1 108 ? 9.852   -14.363 5.168   1.00 12.12 ? 108 SER A CB  1 
ATOM   886   O  OG  . SER A  1 108 ? 10.754  -14.902 4.148   1.00 18.49 ? 108 SER A OG  1 
ATOM   887   N  N   . GLY A  1 109 ? 9.098   -10.919 6.325   1.00 9.63  ? 109 GLY A N   1 
ATOM   888   C  CA  . GLY A  1 109 ? 8.259   -10.134 7.211   1.00 11.21 ? 109 GLY A CA  1 
ATOM   889   C  C   . GLY A  1 109 ? 8.632   -10.236 8.700   1.00 12.33 ? 109 GLY A C   1 
ATOM   890   O  O   . GLY A  1 109 ? 7.993   -9.568  9.507   1.00 14.23 ? 109 GLY A O   1 
ATOM   891   N  N   . GLN A  1 110 ? 9.543   -11.127 9.073   1.00 10.87 ? 110 GLN A N   1 
ATOM   892   C  CA  . GLN A  1 110 ? 9.965   -11.343 10.453  1.00 10.96 ? 110 GLN A CA  1 
ATOM   893   C  C   . GLN A  1 110 ? 11.186  -10.585 10.946  1.00 9.71  ? 110 GLN A C   1 
ATOM   894   O  O   . GLN A  1 110 ? 12.206  -10.630 10.272  1.00 9.29  ? 110 GLN A O   1 
ATOM   895   C  CB  . GLN A  1 110 ? 10.235  -12.857 10.630  1.00 11.91 ? 110 GLN A CB  1 
ATOM   896   C  CG  . GLN A  1 110 ? 9.062   -13.761 10.090  1.00 12.20 ? 110 GLN A CG  1 
ATOM   897   C  CD  . GLN A  1 110 ? 7.684   -13.337 10.536  1.00 13.10 ? 110 GLN A CD  1 
ATOM   898   O  OE1 . GLN A  1 110 ? 7.410   -13.219 11.701  1.00 16.01 ? 110 GLN A OE1 1 
ATOM   899   N  NE2 . GLN A  1 110 ? 6.853   -12.986 9.559   1.00 16.75 ? 110 GLN A NE2 1 
ATOM   900   N  N   . HIS A  1 111 ? 11.052  -9.956  12.101  1.00 10.88 ? 111 HIS A N   1 
ATOM   901   C  CA  . HIS A  1 111 ? 12.143  -9.356  12.738  1.00 10.53 ? 111 HIS A CA  1 
ATOM   902   C  C   . HIS A  1 111 ? 12.937  -10.378 13.476  1.00 12.43 ? 111 HIS A C   1 
ATOM   903   O  O   . HIS A  1 111 ? 12.385  -11.390 13.929  1.00 16.59 ? 111 HIS A O   1 
ATOM   904   C  CB  . HIS A  1 111 ? 11.748  -8.380  13.818  1.00 12.37 ? 111 HIS A CB  1 
ATOM   905   C  CG  . HIS A  1 111 ? 11.360  -7.060  13.289  1.00 11.89 ? 111 HIS A CG  1 
ATOM   906   N  ND1 . HIS A  1 111 ? 10.130  -6.729  12.783  1.00 16.11 ? 111 HIS A ND1 1 
ATOM   907   C  CD2 . HIS A  1 111 ? 12.117  -5.948  13.142  1.00 11.46 ? 111 HIS A CD2 1 
ATOM   908   C  CE1 . HIS A  1 111 ? 10.115  -5.467  12.376  1.00 16.30 ? 111 HIS A CE1 1 
ATOM   909   N  NE2 . HIS A  1 111 ? 11.343  -4.974  12.563  1.00 15.79 ? 111 HIS A NE2 1 
ATOM   910   N  N   . PHE A  1 112 ? 14.231  -10.237 13.492  1.00 9.63  ? 112 PHE A N   1 
ATOM   911   C  CA  . PHE A  1 112 ? 15.105  -10.907 14.456  1.00 9.56  ? 112 PHE A CA  1 
ATOM   912   C  C   . PHE A  1 112 ? 15.170  -10.131 15.715  1.00 9.53  ? 112 PHE A C   1 
ATOM   913   O  O   . PHE A  1 112 ? 14.643  -8.979  15.839  1.00 9.94  ? 112 PHE A O   1 
ATOM   914   C  CB  . PHE A  1 112 ? 16.473  -11.119 13.819  1.00 10.13 ? 112 PHE A CB  1 
ATOM   915   C  CG  . PHE A  1 112 ? 16.455  -12.210 12.788  1.00 10.95 ? 112 PHE A CG  1 
ATOM   916   C  CD1 . PHE A  1 112 ? 15.870  -11.969 11.509  1.00 13.59 ? 112 PHE A CD1 1 
ATOM   917   C  CD2 . PHE A  1 112 ? 16.863  -13.524 13.095  1.00 12.98 ? 112 PHE A CD2 1 
ATOM   918   C  CE1 . PHE A  1 112 ? 15.788  -13.044 10.601  1.00 17.49 ? 112 PHE A CE1 1 
ATOM   919   C  CE2 . PHE A  1 112 ? 16.825  -14.557 12.181  1.00 14.05 ? 112 PHE A CE2 1 
ATOM   920   C  CZ  . PHE A  1 112 ? 16.290  -14.310 10.969  1.00 15.03 ? 112 PHE A CZ  1 
ATOM   921   N  N   . ALA A  1 113 ? 15.821  -10.680 16.734  1.00 9.60  ? 113 ALA A N   1 
ATOM   922   C  CA  . ALA A  1 113 ? 15.834  -10.031 18.035  1.00 10.06 ? 113 ALA A CA  1 
ATOM   923   C  C   . ALA A  1 113 ? 16.607  -8.722  18.011  1.00 9.20  ? 113 ALA A C   1 
ATOM   924   O  O   . ALA A  1 113 ? 16.253  -7.762  18.675  1.00 9.27  ? 113 ALA A O   1 
ATOM   925   C  CB  . ALA A  1 113 ? 16.473  -10.973 19.107  1.00 9.35  ? 113 ALA A CB  1 
ATOM   926   N  N   . ALA A  1 114 ? 17.733  -8.678  17.254  1.00 8.26  ? 114 ALA A N   1 
ATOM   927   C  CA  . ALA A  1 114 ? 18.578  -7.493  17.231  1.00 8.17  ? 114 ALA A CA  1 
ATOM   928   C  C   . ALA A  1 114 ? 19.406  -7.576  15.933  1.00 7.62  ? 114 ALA A C   1 
ATOM   929   O  O   . ALA A  1 114 ? 19.329  -8.566  15.170  1.00 8.21  ? 114 ALA A O   1 
ATOM   930   C  CB  . ALA A  1 114 ? 19.458  -7.475  18.505  1.00 9.01  ? 114 ALA A CB  1 
ATOM   931   N  N   . GLU A  1 115 ? 20.191  -6.532  15.706  1.00 8.09  ? 115 GLU A N   1 
ATOM   932   C  CA  . GLU A  1 115 ? 21.000  -6.515  14.470  1.00 7.82  ? 115 GLU A CA  1 
ATOM   933   C  C   . GLU A  1 115 ? 22.268  -5.728  14.780  1.00 7.50  ? 115 GLU A C   1 
ATOM   934   O  O   . GLU A  1 115 ? 22.229  -4.652  15.410  1.00 8.66  ? 115 GLU A O   1 
ATOM   935   C  CB  . GLU A  1 115 ? 20.171  -5.879  13.334  1.00 8.00  ? 115 GLU A CB  1 
ATOM   936   C  CG  . GLU A  1 115 ? 20.865  -5.907  11.951  1.00 8.22  ? 115 GLU A CG  1 
ATOM   937   C  CD  . GLU A  1 115 ? 19.900  -5.534  10.841  1.00 9.20  ? 115 GLU A CD  1 
ATOM   938   O  OE1 . GLU A  1 115 ? 18.682  -5.784  10.971  1.00 8.35  ? 115 GLU A OE1 1 
ATOM   939   O  OE2 . GLU A  1 115 ? 20.387  -5.025  9.822   1.00 7.91  ? 115 GLU A OE2 1 
ATOM   940   N  N   . LEU A  1 116 ? 23.431  -6.257  14.330  1.00 7.16  ? 116 LEU A N   1 
ATOM   941   C  CA  . LEU A  1 116 ? 24.760  -5.604  14.441  1.00 7.65  ? 116 LEU A CA  1 
ATOM   942   C  C   . LEU A  1 116 ? 25.102  -5.050  13.047  1.00 6.91  ? 116 LEU A C   1 
ATOM   943   O  O   . LEU A  1 116 ? 24.937  -5.727  12.022  1.00 7.32  ? 116 LEU A O   1 
ATOM   944   C  CB  . LEU A  1 116 ? 25.801  -6.688  14.838  1.00 9.22  ? 116 LEU A CB  1 
ATOM   945   C  CG  . LEU A  1 116 ? 27.307  -6.267  14.611  1.00 9.12  ? 116 LEU A CG  1 
ATOM   946   C  CD1 . LEU A  1 116 ? 27.635  -5.336  15.732  1.00 13.39 ? 116 LEU A CD1 1 
ATOM   947   C  CD2 . LEU A  1 116 ? 28.197  -7.495  14.609  1.00 10.55 ? 116 LEU A CD2 1 
ATOM   948   N  N   . HIS A  1 117 ? 25.596  -3.801  13.055  1.00 6.99  ? 117 HIS A N   1 
ATOM   949   C  CA  . HIS A  1 117 ? 26.114  -3.150  11.808  1.00 7.20  ? 117 HIS A CA  1 
ATOM   950   C  C   . HIS A  1 117 ? 27.563  -2.861  11.971  1.00 6.85  ? 117 HIS A C   1 
ATOM   951   O  O   . HIS A  1 117 ? 27.923  -2.214  12.952  1.00 8.06  ? 117 HIS A O   1 
ATOM   952   C  CB  . HIS A  1 117 ? 25.359  -1.858  11.565  1.00 7.10  ? 117 HIS A CB  1 
ATOM   953   C  CG  . HIS A  1 117 ? 23.953  -2.137  11.194  1.00 6.58  ? 117 HIS A CG  1 
ATOM   954   N  ND1 . HIS A  1 117 ? 22.913  -1.224  11.354  1.00 8.21  ? 117 HIS A ND1 1 
ATOM   955   C  CD2 . HIS A  1 117 ? 23.429  -3.223  10.608  1.00 7.70  ? 117 HIS A CD2 1 
ATOM   956   C  CE1 . HIS A  1 117 ? 21.794  -1.762  10.850  1.00 7.32  ? 117 HIS A CE1 1 
ATOM   957   N  NE2 . HIS A  1 117 ? 22.055  -2.998  10.469  1.00 7.17  ? 117 HIS A NE2 1 
ATOM   958   N  N   . ILE A  1 118 ? 28.382  -3.340  11.036  1.00 8.22  ? 118 ILE A N   1 
ATOM   959   C  CA  . ILE A  1 118 ? 29.810  -2.984  11.049  1.00 8.00  ? 118 ILE A CA  1 
ATOM   960   C  C   . ILE A  1 118 ? 29.967  -2.045  9.863   1.00 8.47  ? 118 ILE A C   1 
ATOM   961   O  O   . ILE A  1 118 ? 29.825  -2.430  8.673   1.00 8.30  ? 118 ILE A O   1 
ATOM   962   C  CB  . ILE A  1 118 ? 30.704  -4.200  10.880  1.00 8.59  ? 118 ILE A CB  1 
ATOM   963   C  CG1 . ILE A  1 118 ? 30.369  -5.260  11.923  1.00 9.25  ? 118 ILE A CG1 1 
ATOM   964   C  CG2 . ILE A  1 118 ? 32.213  -3.749  11.073  1.00 10.65 ? 118 ILE A CG2 1 
ATOM   965   C  CD1 . ILE A  1 118 ? 31.254  -6.496  11.831  1.00 11.00 ? 118 ILE A CD1 1 
ATOM   966   N  N   . VAL A  1 119 ? 30.206  -0.762  10.176  1.00 8.73  ? 119 VAL A N   1 
ATOM   967   C  CA  . VAL A  1 119 ? 30.183  0.327   9.146   1.00 8.90  ? 119 VAL A CA  1 
ATOM   968   C  C   . VAL A  1 119 ? 31.556  0.468   8.574   1.00 9.28  ? 119 VAL A C   1 
ATOM   969   O  O   . VAL A  1 119 ? 32.517  0.614   9.373   1.00 10.25 ? 119 VAL A O   1 
ATOM   970   C  CB  . VAL A  1 119 ? 29.732  1.661   9.785   1.00 8.99  ? 119 VAL A CB  1 
ATOM   971   C  CG1 . VAL A  1 119 ? 29.625  2.749   8.710   1.00 10.38 ? 119 VAL A CG1 1 
ATOM   972   C  CG2 . VAL A  1 119 ? 28.302  1.503   10.458  1.00 11.16 ? 119 VAL A CG2 1 
ATOM   973   N  N   . HIS A  1 120 ? 31.652  0.550   7.268   1.00 9.38  ? 120 HIS A N   1 
ATOM   974   C  CA  . HIS A  1 120 ? 32.967  0.815   6.596   1.00 9.67  ? 120 HIS A CA  1 
ATOM   975   C  C   . HIS A  1 120 ? 32.761  1.935   5.582   1.00 9.89  ? 120 HIS A C   1 
ATOM   976   O  O   . HIS A  1 120 ? 31.637  2.212   5.120   1.00 9.79  ? 120 HIS A O   1 
ATOM   977   C  CB  . HIS A  1 120 ? 33.402  -0.430  5.797   1.00 9.13  ? 120 HIS A CB  1 
ATOM   978   C  CG  . HIS A  1 120 ? 33.543  -1.702  6.593   1.00 10.10 ? 120 HIS A CG  1 
ATOM   979   N  ND1 . HIS A  1 120 ? 32.476  -2.408  7.177   1.00 9.46  ? 120 HIS A ND1 1 
ATOM   980   C  CD2 . HIS A  1 120 ? 34.656  -2.446  6.858   1.00 10.22 ? 120 HIS A CD2 1 
ATOM   981   C  CE1 . HIS A  1 120 ? 32.955  -3.530  7.720   1.00 9.61  ? 120 HIS A CE1 1 
ATOM   982   N  NE2 . HIS A  1 120 ? 34.283  -3.609  7.552   1.00 10.09 ? 120 HIS A NE2 1 
ATOM   983   N  N   . TYR A  1 121 ? 33.880  2.572   5.195   1.00 11.13 ? 121 TYR A N   1 
ATOM   984   C  CA  . TYR A  1 121 ? 33.810  3.630   4.180   1.00 10.10 ? 121 TYR A CA  1 
ATOM   985   C  C   . TYR A  1 121 ? 34.809  3.351   3.091   1.00 11.23 ? 121 TYR A C   1 
ATOM   986   O  O   . TYR A  1 121 ? 35.802  2.682   3.333   1.00 10.85 ? 121 TYR A O   1 
ATOM   987   C  CB  . TYR A  1 121 ? 34.065  5.039   4.821   1.00 12.08 ? 121 TYR A CB  1 
ATOM   988   C  CG  . TYR A  1 121 ? 35.490  5.296   5.322   1.00 13.58 ? 121 TYR A CG  1 
ATOM   989   C  CD1 . TYR A  1 121 ? 35.940  4.716   6.495   1.00 15.17 ? 121 TYR A CD1 1 
ATOM   990   C  CD2 . TYR A  1 121 ? 36.398  5.996   4.526   1.00 17.77 ? 121 TYR A CD2 1 
ATOM   991   C  CE1 . TYR A  1 121 ? 37.246  4.861   6.956   1.00 17.12 ? 121 TYR A CE1 1 
ATOM   992   C  CE2 . TYR A  1 121 ? 37.745  6.096   4.986   1.00 18.08 ? 121 TYR A CE2 1 
ATOM   993   C  CZ  . TYR A  1 121 ? 38.143  5.528   6.174   1.00 19.80 ? 121 TYR A CZ  1 
ATOM   994   O  OH  . TYR A  1 121 ? 39.465  5.630   6.706   1.00 20.93 ? 121 TYR A OH  1 
ATOM   995   N  N   . ASN A  1 122 ? 34.600  3.967   1.923   1.00 11.20 ? 122 ASN A N   1 
ATOM   996   C  CA  . ASN A  1 122 ? 35.480  3.715   0.740   1.00 11.83 ? 122 ASN A CA  1 
ATOM   997   C  C   . ASN A  1 122 ? 36.744  4.569   0.951   1.00 13.41 ? 122 ASN A C   1 
ATOM   998   O  O   . ASN A  1 122 ? 36.768  5.781   0.647   1.00 12.20 ? 122 ASN A O   1 
ATOM   999   C  CB  . ASN A  1 122 ? 34.767  4.194   -0.506  1.00 12.42 ? 122 ASN A CB  1 
ATOM   1000  C  CG  . ASN A  1 122 ? 35.489  3.810   -1.742  1.00 12.63 ? 122 ASN A CG  1 
ATOM   1001  O  OD1 . ASN A  1 122 ? 36.736  3.739   -1.755  1.00 12.66 ? 122 ASN A OD1 1 
ATOM   1002  N  ND2 . ASN A  1 122 ? 34.727  3.463   -2.819  1.00 15.03 ? 122 ASN A ND2 1 
ATOM   1003  N  N   . SER A  1 123 ? 37.789  3.907   1.452   1.00 11.40 ? 123 SER A N   1 
ATOM   1004  C  CA  . SER A  1 123 ? 39.023  4.621   1.763   1.00 13.10 ? 123 SER A CA  1 
ATOM   1005  C  C   . SER A  1 123 ? 39.881  4.780   0.514   1.00 12.82 ? 123 SER A C   1 
ATOM   1006  O  O   . SER A  1 123 ? 40.860  5.558   0.576   1.00 14.78 ? 123 SER A O   1 
ATOM   1007  C  CB  . SER A  1 123 ? 39.748  3.788   2.856   1.00 11.93 ? 123 SER A CB  1 
ATOM   1008  O  OG  . SER A  1 123 ? 39.840  2.459   2.526   1.00 12.91 ? 123 SER A OG  1 
ATOM   1009  N  N   . ASP A  1 124 ? 39.555  4.114   -0.576  1.00 12.54 ? 124 ASP A N   1 
ATOM   1010  C  CA  . ASP A  1 124 ? 40.327  4.320   -1.843  1.00 12.92 ? 124 ASP A CA  1 
ATOM   1011  C  C   . ASP A  1 124 ? 39.922  5.661   -2.398  1.00 13.97 ? 124 ASP A C   1 
ATOM   1012  O  O   . ASP A  1 124 ? 40.743  6.334   -3.043  1.00 16.70 ? 124 ASP A O   1 
ATOM   1013  C  CB  . ASP A  1 124 ? 39.953  3.229   -2.811  1.00 13.49 ? 124 ASP A CB  1 
ATOM   1014  C  CG  . ASP A  1 124 ? 40.652  1.947   -2.585  1.00 12.86 ? 124 ASP A CG  1 
ATOM   1015  O  OD1 . ASP A  1 124 ? 41.661  1.918   -1.847  1.00 14.34 ? 124 ASP A OD1 1 
ATOM   1016  O  OD2 . ASP A  1 124 ? 40.219  0.902   -3.049  1.00 12.89 ? 124 ASP A OD2 1 
ATOM   1017  N  N   . LEU A  1 125 ? 38.687  6.082   -2.186  1.00 11.29 ? 125 LEU A N   1 
ATOM   1018  C  CA  . LEU A  1 125 ? 38.175  7.344   -2.777  1.00 14.50 ? 125 LEU A CA  1 
ATOM   1019  C  C   . LEU A  1 125 ? 38.113  8.473   -1.829  1.00 14.55 ? 125 LEU A C   1 
ATOM   1020  O  O   . LEU A  1 125 ? 38.198  9.672   -2.300  1.00 17.61 ? 125 LEU A O   1 
ATOM   1021  C  CB  . LEU A  1 125 ? 36.781  7.153   -3.431  1.00 14.89 ? 125 LEU A CB  1 
ATOM   1022  C  CG  . LEU A  1 125 ? 36.777  6.101   -4.523  1.00 19.22 ? 125 LEU A CG  1 
ATOM   1023  C  CD1 . LEU A  1 125 ? 35.357  5.987   -5.095  1.00 20.25 ? 125 LEU A CD1 1 
ATOM   1024  C  CD2 . LEU A  1 125 ? 37.845  6.407   -5.602  1.00 21.60 ? 125 LEU A CD2 1 
ATOM   1025  N  N   . TYR A  1 126 ? 37.974  8.220   -0.524  1.00 14.10 ? 126 TYR A N   1 
ATOM   1026  C  CA  . TYR A  1 126 ? 37.701  9.262   0.475   1.00 15.58 ? 126 TYR A CA  1 
ATOM   1027  C  C   . TYR A  1 126 ? 38.563  9.119   1.702   1.00 17.01 ? 126 TYR A C   1 
ATOM   1028  O  O   . TYR A  1 126 ? 39.032  8.011   2.039   1.00 17.40 ? 126 TYR A O   1 
ATOM   1029  C  CB  . TYR A  1 126 ? 36.176  9.197   0.909   1.00 15.53 ? 126 TYR A CB  1 
ATOM   1030  C  CG  . TYR A  1 126 ? 35.277  9.238   -0.258  1.00 15.24 ? 126 TYR A CG  1 
ATOM   1031  C  CD1 . TYR A  1 126 ? 35.209  10.339  -1.127  1.00 19.27 ? 126 TYR A CD1 1 
ATOM   1032  C  CD2 . TYR A  1 126 ? 34.507  8.098   -0.583  1.00 15.61 ? 126 TYR A CD2 1 
ATOM   1033  C  CE1 . TYR A  1 126 ? 34.393  10.267  -2.281  1.00 20.42 ? 126 TYR A CE1 1 
ATOM   1034  C  CE2 . TYR A  1 126 ? 33.695  8.008   -1.717  1.00 16.62 ? 126 TYR A CE2 1 
ATOM   1035  C  CZ  . TYR A  1 126 ? 33.634  9.118   -2.587  1.00 18.57 ? 126 TYR A CZ  1 
ATOM   1036  O  OH  . TYR A  1 126 ? 32.809  9.057   -3.750  1.00 20.12 ? 126 TYR A OH  1 
ATOM   1037  N  N   . PRO A  1 127 ? 38.863  10.251  2.390   1.00 18.53 ? 127 PRO A N   1 
ATOM   1038  C  CA  . PRO A  1 127 ? 39.813  10.188  3.499   1.00 17.17 ? 127 PRO A CA  1 
ATOM   1039  C  C   . PRO A  1 127 ? 39.327  9.762   4.850   1.00 21.17 ? 127 PRO A C   1 
ATOM   1040  O  O   . PRO A  1 127 ? 40.134  9.307   5.690   1.00 25.52 ? 127 PRO A O   1 
ATOM   1041  C  CB  . PRO A  1 127 ? 40.345  11.624  3.608   1.00 21.90 ? 127 PRO A CB  1 
ATOM   1042  C  CG  . PRO A  1 127 ? 39.195  12.449  3.108   1.00 20.68 ? 127 PRO A CG  1 
ATOM   1043  C  CD  . PRO A  1 127 ? 38.581  11.624  1.988   1.00 20.41 ? 127 PRO A CD  1 
ATOM   1044  N  N   . ASP A  1 128 ? 38.011  9.816   5.026   1.00 21.10 ? 128 ASP A N   1 
ATOM   1045  C  CA  . ASP A  1 128 ? 37.392  9.404   6.280   1.00 21.20 ? 128 ASP A CA  1 
ATOM   1046  C  C   . ASP A  1 128 ? 35.925  9.117   6.078   1.00 19.58 ? 128 ASP A C   1 
ATOM   1047  O  O   . ASP A  1 128 ? 35.384  9.435   5.020   1.00 18.24 ? 128 ASP A O   1 
ATOM   1048  C  CB  . ASP A  1 128 ? 37.675  10.445  7.408   1.00 25.21 ? 128 ASP A CB  1 
ATOM   1049  C  CG  . ASP A  1 128 ? 37.369  11.835  6.964   1.00 29.47 ? 128 ASP A CG  1 
ATOM   1050  O  OD1 . ASP A  1 128 ? 38.181  12.791  7.231   1.00 33.89 ? 128 ASP A OD1 1 
ATOM   1051  O  OD2 . ASP A  1 128 ? 36.345  12.018  6.315   1.00 23.11 ? 128 ASP A OD2 1 
ATOM   1052  N  N   . ALA A  1 129 ? 35.335  8.476   7.061   1.00 19.75 ? 129 ALA A N   1 
ATOM   1053  C  CA  . ALA A  1 129 ? 33.949  8.090   6.960   1.00 19.15 ? 129 ALA A CA  1 
ATOM   1054  C  C   . ALA A  1 129 ? 33.037  9.313   6.844   1.00 21.40 ? 129 ALA A C   1 
ATOM   1055  O  O   . ALA A  1 129 ? 32.094  9.265   6.076   1.00 19.38 ? 129 ALA A O   1 
ATOM   1056  C  CB  . ALA A  1 129 ? 33.536  7.233   8.154   1.00 22.49 ? 129 ALA A CB  1 
ATOM   1057  N  N   . SER A  1 130 ? 33.345  10.362  7.598   1.00 21.26 ? 130 SER A N   1 
ATOM   1058  C  CA  . SER A  1 130 ? 32.518  11.590  7.560   1.00 22.29 ? 130 SER A CA  1 
ATOM   1059  C  C   . SER A  1 130 ? 32.420  12.087  6.096   1.00 23.11 ? 130 SER A C   1 
ATOM   1060  O  O   . SER A  1 130 ? 31.343  12.334  5.499   1.00 21.05 ? 130 SER A O   1 
ATOM   1061  C  CB  . SER A  1 130 ? 33.117  12.632  8.553   1.00 27.66 ? 130 SER A CB  1 
ATOM   1062  O  OG  . SER A  1 130 ? 32.294  13.792  8.534   1.00 30.71 ? 130 SER A OG  1 
ATOM   1063  N  N   . THR A  1 131 ? 33.568  12.223  5.480   1.00 20.57 ? 131 THR A N   1 
ATOM   1064  C  CA  . THR A  1 131 ? 33.566  12.741  4.140   1.00 19.69 ? 131 THR A CA  1 
ATOM   1065  C  C   . THR A  1 131 ? 32.893  11.753  3.205   1.00 19.32 ? 131 THR A C   1 
ATOM   1066  O  O   . THR A  1 131 ? 32.267  12.140  2.236   1.00 19.09 ? 131 THR A O   1 
ATOM   1067  C  CB  . THR A  1 131 ? 35.025  12.928  3.597   1.00 22.66 ? 131 THR A CB  1 
ATOM   1068  O  OG1 . THR A  1 131 ? 35.743  13.779  4.516   1.00 25.62 ? 131 THR A OG1 1 
ATOM   1069  C  CG2 . THR A  1 131 ? 35.066  13.605  2.252   1.00 22.63 ? 131 THR A CG2 1 
ATOM   1070  N  N   . ALA A  1 132 ? 33.132  10.435  3.342   1.00 17.33 ? 132 ALA A N   1 
ATOM   1071  C  CA  . ALA A  1 132 ? 32.523  9.484   2.467   1.00 16.15 ? 132 ALA A CA  1 
ATOM   1072  C  C   . ALA A  1 132 ? 30.989  9.377   2.647   1.00 16.67 ? 132 ALA A C   1 
ATOM   1073  O  O   . ALA A  1 132 ? 30.389  9.013   1.663   1.00 16.72 ? 132 ALA A O   1 
ATOM   1074  C  CB  . ALA A  1 132 ? 33.096  8.045   2.772   1.00 14.68 ? 132 ALA A CB  1 
ATOM   1075  N  N   . SER A  1 133 ? 30.475  9.706   3.806   1.00 16.67 ? 133 SER A N   1 
ATOM   1076  C  CA  . SER A  1 133 ? 29.070  9.322   4.174   1.00 18.47 ? 133 SER A CA  1 
ATOM   1077  C  C   . SER A  1 133 ? 28.024  9.867   3.225   1.00 19.47 ? 133 SER A C   1 
ATOM   1078  O  O   . SER A  1 133 ? 26.947  9.280   3.118   1.00 19.42 ? 133 SER A O   1 
ATOM   1079  C  CB  . SER A  1 133 ? 28.809  9.760   5.590   1.00 19.00 ? 133 SER A CB  1 
ATOM   1080  O  OG  . SER A  1 133 ? 28.777  11.218  5.691   1.00 19.65 ? 133 SER A OG  1 
ATOM   1081  N  N   . ASN A  1 134 ? 28.243  11.020  2.544   1.00 18.96 ? 134 ASN A N   1 
ATOM   1082  C  CA  . ASN A  1 134 ? 27.306  11.627  1.600   1.00 20.81 ? 134 ASN A CA  1 
ATOM   1083  C  C   . ASN A  1 134 ? 27.819  11.580  0.203   1.00 20.04 ? 134 ASN A C   1 
ATOM   1084  O  O   . ASN A  1 134 ? 27.340  12.256  -0.674  1.00 23.96 ? 134 ASN A O   1 
ATOM   1085  C  CB  . ASN A  1 134 ? 26.845  13.048  2.063   1.00 23.09 ? 134 ASN A CB  1 
ATOM   1086  C  CG  . ASN A  1 134 ? 27.996  14.061  2.032   1.00 28.65 ? 134 ASN A CG  1 
ATOM   1087  O  OD1 . ASN A  1 134 ? 29.206  13.663  1.990   1.00 28.14 ? 134 ASN A OD1 1 
ATOM   1088  N  ND2 . ASN A  1 134 ? 27.655  15.365  2.051   1.00 32.93 ? 134 ASN A ND2 1 
ATOM   1089  N  N   . LYS A  1 135 ? 28.714  10.674  -0.086  1.00 19.34 ? 135 LYS A N   1 
ATOM   1090  C  CA  . LYS A  1 135 ? 29.276  10.571  -1.391  1.00 21.16 ? 135 LYS A CA  1 
ATOM   1091  C  C   . LYS A  1 135 ? 29.040  9.313   -2.082  1.00 22.51 ? 135 LYS A C   1 
ATOM   1092  O  O   . LYS A  1 135 ? 28.802  8.270   -1.449  1.00 19.86 ? 135 LYS A O   1 
ATOM   1093  C  CB  . LYS A  1 135 ? 30.832  10.902  -1.320  1.00 22.19 ? 135 LYS A CB  1 
ATOM   1094  C  CG  . LYS A  1 135 ? 31.009  12.377  -0.907  1.00 23.22 ? 135 LYS A CG  1 
ATOM   1095  C  CD  . LYS A  1 135 ? 32.385  12.945  -1.208  1.00 24.69 ? 135 LYS A CD  1 
ATOM   1096  C  CE  . LYS A  1 135 ? 32.600  14.249  -0.496  1.00 23.58 ? 135 LYS A CE  1 
ATOM   1097  N  NZ  . LYS A  1 135 ? 31.751  14.473  0.733   1.00 25.90 ? 135 LYS A NZ  1 
ATOM   1098  N  N   . SER A  1 136 ? 29.151  9.352   -3.387  1.00 22.99 ? 136 SER A N   1 
ATOM   1099  C  CA  . SER A  1 136 ? 28.899  8.166   -4.227  1.00 22.90 ? 136 SER A CA  1 
ATOM   1100  C  C   . SER A  1 136 ? 29.805  7.008   -3.795  1.00 21.03 ? 136 SER A C   1 
ATOM   1101  O  O   . SER A  1 136 ? 31.009  7.173   -3.602  1.00 21.29 ? 136 SER A O   1 
ATOM   1102  C  CB  . SER A  1 136 ? 29.339  8.466   -5.654  1.00 25.10 ? 136 SER A CB  1 
ATOM   1103  O  OG  . SER A  1 136 ? 28.963  7.381   -6.444  1.00 31.29 ? 136 SER A OG  1 
ATOM   1104  N  N   . GLU A  1 137 ? 29.247  5.802   -3.721  1.00 17.70 ? 137 GLU A N   1 
ATOM   1105  C  CA  . GLU A  1 137 ? 30.070  4.642   -3.286  1.00 18.13 ? 137 GLU A CA  1 
ATOM   1106  C  C   . GLU A  1 137 ? 30.685  4.823   -1.890  1.00 17.23 ? 137 GLU A C   1 
ATOM   1107  O  O   . GLU A  1 137 ? 31.716  4.194   -1.556  1.00 18.08 ? 137 GLU A O   1 
ATOM   1108  C  CB  . GLU A  1 137 ? 31.117  4.204   -4.317  1.00 21.45 ? 137 GLU A CB  1 
ATOM   1109  C  CG  . GLU A  1 137 ? 30.524  3.851   -5.705  1.00 27.20 ? 137 GLU A CG  1 
ATOM   1110  C  CD  . GLU A  1 137 ? 31.511  3.018   -6.522  1.00 40.00 ? 137 GLU A CD  1 
ATOM   1111  O  OE1 . GLU A  1 137 ? 32.698  3.450   -6.651  1.00 45.25 ? 137 GLU A OE1 1 
ATOM   1112  O  OE2 . GLU A  1 137 ? 31.101  1.926   -7.020  1.00 49.18 ? 137 GLU A OE2 1 
ATOM   1113  N  N   . GLY A  1 138 ? 30.115  5.694   -1.121  1.00 13.75 ? 138 GLY A N   1 
ATOM   1114  C  CA  . GLY A  1 138 ? 30.788  6.013   0.120   1.00 13.60 ? 138 GLY A CA  1 
ATOM   1115  C  C   . GLY A  1 138 ? 30.896  5.039   1.257   1.00 11.63 ? 138 GLY A C   1 
ATOM   1116  O  O   . GLY A  1 138 ? 31.961  4.881   1.835   1.00 12.69 ? 138 GLY A O   1 
ATOM   1117  N  N   . LEU A  1 139 ? 29.812  4.221   1.440   1.00 10.45 ? 139 LEU A N   1 
ATOM   1118  C  CA  . LEU A  1 139 ? 29.766  3.373   2.641   1.00 10.34 ? 139 LEU A CA  1 
ATOM   1119  C  C   . LEU A  1 139 ? 29.416  1.934   2.267   1.00 8.79  ? 139 LEU A C   1 
ATOM   1120  O  O   . LEU A  1 139 ? 28.741  1.674   1.293   1.00 10.27 ? 139 LEU A O   1 
ATOM   1121  C  CB  . LEU A  1 139 ? 28.755  3.899   3.657   1.00 10.44 ? 139 LEU A CB  1 
ATOM   1122  C  CG  . LEU A  1 139 ? 28.989  5.320   4.169   1.00 11.67 ? 139 LEU A CG  1 
ATOM   1123  C  CD1 . LEU A  1 139 ? 27.800  5.788   5.025   1.00 12.50 ? 139 LEU A CD1 1 
ATOM   1124  C  CD2 . LEU A  1 139 ? 30.306  5.493   4.962   1.00 14.50 ? 139 LEU A CD2 1 
ATOM   1125  N  N   . ALA A  1 140 ? 29.827  1.016   3.155   1.00 8.58  ? 140 ALA A N   1 
ATOM   1126  C  CA  . ALA A  1 140 ? 29.462  -0.397  3.022   1.00 9.27  ? 140 ALA A CA  1 
ATOM   1127  C  C   . ALA A  1 140 ? 29.234  -0.848  4.442   1.00 9.32  ? 140 ALA A C   1 
ATOM   1128  O  O   . ALA A  1 140 ? 30.078  -0.682  5.334   1.00 10.35 ? 140 ALA A O   1 
ATOM   1129  C  CB  . ALA A  1 140 ? 30.539  -1.220  2.339   1.00 9.16  ? 140 ALA A CB  1 
ATOM   1130  N  N   . VAL A  1 141 ? 28.116  -1.516  4.676   1.00 9.15  ? 141 VAL A N   1 
ATOM   1131  C  CA  . VAL A  1 141 ? 27.778  -2.028  6.015   1.00 8.73  ? 141 VAL A CA  1 
ATOM   1132  C  C   . VAL A  1 141 ? 27.622  -3.524  5.957   1.00 8.08  ? 141 VAL A C   1 
ATOM   1133  O  O   . VAL A  1 141 ? 27.070  -4.091  4.996   1.00 9.19  ? 141 VAL A O   1 
ATOM   1134  C  CB  . VAL A  1 141 ? 26.504  -1.376  6.574   1.00 8.65  ? 141 VAL A CB  1 
ATOM   1135  C  CG1 . VAL A  1 141 ? 26.130  -2.041  7.955   1.00 10.78 ? 141 VAL A CG1 1 
ATOM   1136  C  CG2 . VAL A  1 141 ? 26.682  0.127   6.662   1.00 11.36 ? 141 VAL A CG2 1 
ATOM   1137  N  N   . LEU A  1 142 ? 28.211  -4.218  6.940   1.00 8.03  ? 142 LEU A N   1 
ATOM   1138  C  CA  . LEU A  1 142 ? 27.929  -5.642  7.124   1.00 8.67  ? 142 LEU A CA  1 
ATOM   1139  C  C   . LEU A  1 142 ? 26.873  -5.736  8.236   1.00 8.21  ? 142 LEU A C   1 
ATOM   1140  O  O   . LEU A  1 142 ? 27.072  -5.163  9.328   1.00 9.65  ? 142 LEU A O   1 
ATOM   1141  C  CB  . LEU A  1 142 ? 29.163  -6.361  7.617   1.00 9.53  ? 142 LEU A CB  1 
ATOM   1142  C  CG  . LEU A  1 142 ? 30.384  -6.274  6.659   1.00 10.66 ? 142 LEU A CG  1 
ATOM   1143  C  CD1 . LEU A  1 142 ? 31.539  -7.127  7.233   1.00 10.92 ? 142 LEU A CD1 1 
ATOM   1144  C  CD2 . LEU A  1 142 ? 30.088  -6.800  5.252   1.00 10.17 ? 142 LEU A CD2 1 
ATOM   1145  N  N   . ALA A  1 143 ? 25.791  -6.468  7.939   1.00 7.27  ? 143 ALA A N   1 
ATOM   1146  C  CA  . ALA A  1 143 ? 24.707  -6.585  8.953   1.00 7.77  ? 143 ALA A CA  1 
ATOM   1147  C  C   . ALA A  1 143 ? 24.593  -8.064  9.345   1.00 7.87  ? 143 ALA A C   1 
ATOM   1148  O  O   . ALA A  1 143 ? 24.528  -8.952  8.466   1.00 8.90  ? 143 ALA A O   1 
ATOM   1149  C  CB  . ALA A  1 143 ? 23.418  -6.070  8.296   1.00 8.77  ? 143 ALA A CB  1 
ATOM   1150  N  N   . VAL A  1 144 ? 24.602  -8.234  10.693  1.00 7.45  ? 144 VAL A N   1 
ATOM   1151  C  CA  . VAL A  1 144 ? 24.395  -9.577  11.227  1.00 8.28  ? 144 VAL A CA  1 
ATOM   1152  C  C   . VAL A  1 144 ? 23.062  -9.591  12.005  1.00 7.49  ? 144 VAL A C   1 
ATOM   1153  O  O   . VAL A  1 144 ? 22.850  -8.719  12.902  1.00 8.59  ? 144 VAL A O   1 
ATOM   1154  C  CB  . VAL A  1 144 ? 25.552  -9.876  12.223  1.00 9.26  ? 144 VAL A CB  1 
ATOM   1155  C  CG1 . VAL A  1 144 ? 25.353  -11.327 12.815  1.00 11.31 ? 144 VAL A CG1 1 
ATOM   1156  C  CG2 . VAL A  1 144 ? 26.917  -9.806  11.493  1.00 9.48  ? 144 VAL A CG2 1 
ATOM   1157  N  N   . LEU A  1 145 ? 22.225  -10.541 11.601  1.00 8.57  ? 145 LEU A N   1 
ATOM   1158  C  CA  . LEU A  1 145 ? 20.965  -10.745 12.329  1.00 8.31  ? 145 LEU A CA  1 
ATOM   1159  C  C   . LEU A  1 145 ? 21.218  -11.528 13.599  1.00 8.41  ? 145 LEU A C   1 
ATOM   1160  O  O   . LEU A  1 145 ? 22.001  -12.495 13.591  1.00 8.96  ? 145 LEU A O   1 
ATOM   1161  C  CB  . LEU A  1 145 ? 19.955  -11.451 11.405  1.00 9.22  ? 145 LEU A CB  1 
ATOM   1162  C  CG  . LEU A  1 145 ? 19.666  -10.708 10.124  1.00 10.93 ? 145 LEU A CG  1 
ATOM   1163  C  CD1 . LEU A  1 145 ? 18.982  -11.643 9.134   1.00 11.51 ? 145 LEU A CD1 1 
ATOM   1164  C  CD2 . LEU A  1 145 ? 18.836  -9.417  10.437  1.00 12.32 ? 145 LEU A CD2 1 
ATOM   1165  N  N   . ILE A  1 146 ? 20.573  -11.153 14.697  1.00 7.91  ? 146 ILE A N   1 
ATOM   1166  C  CA  . ILE A  1 146 ? 20.808  -11.786 16.009  1.00 8.82  ? 146 ILE A CA  1 
ATOM   1167  C  C   . ILE A  1 146 ? 19.548  -12.377 16.552  1.00 9.36  ? 146 ILE A C   1 
ATOM   1168  O  O   . ILE A  1 146 ? 18.506  -11.710 16.550  1.00 9.45  ? 146 ILE A O   1 
ATOM   1169  C  CB  . ILE A  1 146 ? 21.328  -10.738 16.985  1.00 9.03  ? 146 ILE A CB  1 
ATOM   1170  C  CG1 . ILE A  1 146 ? 22.693  -10.156 16.481  1.00 10.13 ? 146 ILE A CG1 1 
ATOM   1171  C  CG2 . ILE A  1 146 ? 21.576  -11.324 18.417  1.00 10.44 ? 146 ILE A CG2 1 
ATOM   1172  C  CD1 . ILE A  1 146 ? 23.104  -8.903  17.247  1.00 10.26 ? 146 ILE A CD1 1 
ATOM   1173  N  N   . GLU A  1 147 ? 19.622  -13.625 16.996  1.00 10.74 ? 147 GLU A N   1 
ATOM   1174  C  CA  . GLU A  1 147 ? 18.432  -14.304 17.579  1.00 11.62 ? 147 GLU A CA  1 
ATOM   1175  C  C   . GLU A  1 147 ? 18.872  -14.846 18.924  1.00 11.58 ? 147 GLU A C   1 
ATOM   1176  O  O   . GLU A  1 147 ? 20.053  -14.986 19.235  1.00 12.18 ? 147 GLU A O   1 
ATOM   1177  C  CB  . GLU A  1 147 ? 17.854  -15.395 16.725  1.00 13.76 ? 147 GLU A CB  1 
ATOM   1178  C  CG  . GLU A  1 147 ? 18.777  -16.572 16.593  1.00 12.55 ? 147 GLU A CG  1 
ATOM   1179  C  CD  . GLU A  1 147 ? 18.344  -17.572 15.529  1.00 15.46 ? 147 GLU A CD  1 
ATOM   1180  O  OE1 . GLU A  1 147 ? 17.371  -17.340 14.788  1.00 16.66 ? 147 GLU A OE1 1 
ATOM   1181  O  OE2 . GLU A  1 147 ? 19.002  -18.615 15.415  1.00 19.86 ? 147 GLU A OE2 1 
ATOM   1182  N  N   . MET A  1 148 ? 17.897  -15.224 19.703  1.00 13.11 ? 148 MET A N   1 
ATOM   1183  C  CA  . MET A  1 148 ? 18.163  -15.729 21.009  1.00 14.40 ? 148 MET A CA  1 
ATOM   1184  C  C   . MET A  1 148 ? 18.446  -17.157 21.037  1.00 14.65 ? 148 MET A C   1 
ATOM   1185  O  O   . MET A  1 148 ? 17.654  -17.903 20.472  1.00 16.85 ? 148 MET A O   1 
ATOM   1186  C  CB  . MET A  1 148 ? 16.845  -15.498 21.778  1.00 18.51 ? 148 MET A CB  1 
ATOM   1187  C  CG  . MET A  1 148 ? 16.897  -14.587 22.976  1.00 22.77 ? 148 MET A CG  1 
ATOM   1188  S  SD  . MET A  1 148 ? 17.703  -15.538 24.270  1.00 40.02 ? 148 MET A SD  1 
ATOM   1189  C  CE  . MET A  1 148 ? 17.008  -17.144 23.884  1.00 9.42  ? 148 MET A CE  1 
ATOM   1190  N  N   . GLY A  1 149 ? 19.527  -17.624 21.696  1.00 14.32 ? 149 GLY A N   1 
ATOM   1191  C  CA  . GLY A  1 149 ? 19.868  -19.024 21.760  1.00 14.28 ? 149 GLY A CA  1 
ATOM   1192  C  C   . GLY A  1 149 ? 20.970  -19.242 22.783  1.00 14.19 ? 149 GLY A C   1 
ATOM   1193  O  O   . GLY A  1 149 ? 20.863  -18.768 23.891  1.00 14.07 ? 149 GLY A O   1 
ATOM   1194  N  N   . SER A  1 150 ? 22.036  -19.903 22.366  1.00 15.33 ? 150 SER A N   1 
ATOM   1195  C  CA  . SER A  1 150 ? 23.127  -20.130 23.262  1.00 15.99 ? 150 SER A CA  1 
ATOM   1196  C  C   . SER A  1 150 ? 23.910  -18.855 23.588  1.00 15.01 ? 150 SER A C   1 
ATOM   1197  O  O   . SER A  1 150 ? 24.052  -17.894 22.770  1.00 13.43 ? 150 SER A O   1 
ATOM   1198  C  CB  . SER A  1 150 ? 24.088  -21.157 22.679  1.00 19.98 ? 150 SER A CB  1 
ATOM   1199  O  OG  . SER A  1 150 ? 24.497  -20.712 21.428  1.00 25.88 ? 150 SER A OG  1 
ATOM   1200  N  N   . PHE A  1 151 ? 24.509  -18.800 24.767  1.00 12.88 ? 151 PHE A N   1 
ATOM   1201  C  CA  . PHE A  1 151 ? 25.446  -17.746 25.175  1.00 13.36 ? 151 PHE A CA  1 
ATOM   1202  C  C   . PHE A  1 151 ? 26.572  -17.604 24.166  1.00 12.77 ? 151 PHE A C   1 
ATOM   1203  O  O   . PHE A  1 151 ? 27.143  -18.584 23.671  1.00 15.61 ? 151 PHE A O   1 
ATOM   1204  C  CB  . PHE A  1 151 ? 26.076  -18.128 26.555  1.00 13.20 ? 151 PHE A CB  1 
ATOM   1205  C  CG  . PHE A  1 151 ? 26.994  -17.127 27.064  1.00 14.09 ? 151 PHE A CG  1 
ATOM   1206  C  CD1 . PHE A  1 151 ? 26.546  -15.884 27.571  1.00 15.23 ? 151 PHE A CD1 1 
ATOM   1207  C  CD2 . PHE A  1 151 ? 28.413  -17.370 27.038  1.00 14.38 ? 151 PHE A CD2 1 
ATOM   1208  C  CE1 . PHE A  1 151 ? 27.471  -14.922 27.965  1.00 15.37 ? 151 PHE A CE1 1 
ATOM   1209  C  CE2 . PHE A  1 151 ? 29.298  -16.398 27.473  1.00 14.00 ? 151 PHE A CE2 1 
ATOM   1210  C  CZ  . PHE A  1 151 ? 28.841  -15.172 27.971  1.00 13.74 ? 151 PHE A CZ  1 
ATOM   1211  N  N   . ASN A  1 152 ? 26.907  -16.351 23.882  1.00 11.71 ? 152 ASN A N   1 
ATOM   1212  C  CA  . ASN A  1 152 ? 27.909  -16.071 22.875  1.00 11.74 ? 152 ASN A CA  1 
ATOM   1213  C  C   . ASN A  1 152 ? 29.078  -15.315 23.495  1.00 13.14 ? 152 ASN A C   1 
ATOM   1214  O  O   . ASN A  1 152 ? 29.005  -14.125 23.808  1.00 14.07 ? 152 ASN A O   1 
ATOM   1215  C  CB  . ASN A  1 152 ? 27.235  -15.206 21.737  1.00 11.67 ? 152 ASN A CB  1 
ATOM   1216  C  CG  . ASN A  1 152 ? 28.142  -15.149 20.517  1.00 11.31 ? 152 ASN A CG  1 
ATOM   1217  O  OD1 . ASN A  1 152 ? 29.313  -14.773 20.616  1.00 12.98 ? 152 ASN A OD1 1 
ATOM   1218  N  ND2 . ASN A  1 152 ? 27.536  -15.319 19.379  1.00 12.04 ? 152 ASN A ND2 1 
ATOM   1219  N  N   . PRO A  1 153 ? 30.204  -16.033 23.782  1.00 13.57 ? 153 PRO A N   1 
ATOM   1220  C  CA  . PRO A  1 153 ? 31.316  -15.379 24.397  1.00 13.40 ? 153 PRO A CA  1 
ATOM   1221  C  C   . PRO A  1 153 ? 31.876  -14.157 23.678  1.00 13.86 ? 153 PRO A C   1 
ATOM   1222  O  O   . PRO A  1 153 ? 32.389  -13.205 24.270  1.00 15.60 ? 153 PRO A O   1 
ATOM   1223  C  CB  . PRO A  1 153 ? 32.378  -16.550 24.461  1.00 15.92 ? 153 PRO A CB  1 
ATOM   1224  C  CG  . PRO A  1 153 ? 31.556  -17.761 24.561  1.00 17.93 ? 153 PRO A CG  1 
ATOM   1225  C  CD  . PRO A  1 153 ? 30.344  -17.494 23.630  1.00 13.32 ? 153 PRO A CD  1 
ATOM   1226  N  N   . SER A  1 154 ? 31.766  -14.248 22.360  1.00 13.41 ? 154 SER A N   1 
ATOM   1227  C  CA  . SER A  1 154 ? 32.390  -13.161 21.579  1.00 13.01 ? 154 SER A CA  1 
ATOM   1228  C  C   . SER A  1 154 ? 31.576  -11.889 21.686  1.00 11.44 ? 154 SER A C   1 
ATOM   1229  O  O   . SER A  1 154 ? 32.142  -10.856 21.854  1.00 13.23 ? 154 SER A O   1 
ATOM   1230  C  CB  . SER A  1 154 ? 32.542  -13.537 20.134  1.00 14.55 ? 154 SER A CB  1 
ATOM   1231  O  OG  . SER A  1 154 ? 33.431  -14.704 20.006  1.00 19.02 ? 154 SER A OG  1 
ATOM   1232  N  N   . TYR A  1 155 ? 30.216  -12.027 21.596  1.00 11.47 ? 155 TYR A N   1 
ATOM   1233  C  CA  . TYR A  1 155 ? 29.436  -10.776 21.855  1.00 11.91 ? 155 TYR A CA  1 
ATOM   1234  C  C   . TYR A  1 155 ? 29.597  -10.312 23.231  1.00 12.98 ? 155 TYR A C   1 
ATOM   1235  O  O   . TYR A  1 155 ? 29.540  -9.099  23.438  1.00 12.95 ? 155 TYR A O   1 
ATOM   1236  C  CB  . TYR A  1 155 ? 27.972  -10.981 21.511  1.00 10.70 ? 155 TYR A CB  1 
ATOM   1237  C  CG  . TYR A  1 155 ? 27.708  -10.871 19.998  1.00 11.77 ? 155 TYR A CG  1 
ATOM   1238  C  CD1 . TYR A  1 155 ? 28.031  -11.898 19.110  1.00 11.15 ? 155 TYR A CD1 1 
ATOM   1239  C  CD2 . TYR A  1 155 ? 27.048  -9.713  19.518  1.00 10.53 ? 155 TYR A CD2 1 
ATOM   1240  C  CE1 . TYR A  1 155 ? 27.818  -11.763 17.721  1.00 10.36 ? 155 TYR A CE1 1 
ATOM   1241  C  CE2 . TYR A  1 155 ? 26.875  -9.575  18.152  1.00 10.22 ? 155 TYR A CE2 1 
ATOM   1242  C  CZ  . TYR A  1 155 ? 27.243  -10.569 17.278  1.00 9.49  ? 155 TYR A CZ  1 
ATOM   1243  O  OH  . TYR A  1 155 ? 27.001  -10.330 15.925  1.00 10.97 ? 155 TYR A OH  1 
ATOM   1244  N  N   . ASP A  1 156 ? 29.873  -11.236 24.187  1.00 12.50 ? 156 ASP A N   1 
ATOM   1245  C  CA  . ASP A  1 156 ? 30.123  -10.711 25.496  1.00 13.19 ? 156 ASP A CA  1 
ATOM   1246  C  C   . ASP A  1 156 ? 31.386  -9.871  25.665  1.00 13.51 ? 156 ASP A C   1 
ATOM   1247  O  O   . ASP A  1 156 ? 31.442  -9.125  26.642  1.00 14.42 ? 156 ASP A O   1 
ATOM   1248  C  CB  . ASP A  1 156 ? 30.074  -11.804 26.558  1.00 15.23 ? 156 ASP A CB  1 
ATOM   1249  C  CG  . ASP A  1 156 ? 29.026  -11.468 27.631  1.00 17.58 ? 156 ASP A CG  1 
ATOM   1250  O  OD1 . ASP A  1 156 ? 27.876  -10.970 27.330  1.00 16.16 ? 156 ASP A OD1 1 
ATOM   1251  O  OD2 . ASP A  1 156 ? 29.407  -11.704 28.820  1.00 21.85 ? 156 ASP A OD2 1 
ATOM   1252  N  N   . LYS A  1 157 ? 32.343  -9.979  24.744  1.00 13.11 ? 157 LYS A N   1 
ATOM   1253  C  CA  . LYS A  1 157 ? 33.479  -9.084  24.747  1.00 14.64 ? 157 LYS A CA  1 
ATOM   1254  C  C   . LYS A  1 157 ? 33.053  -7.629  24.603  1.00 15.88 ? 157 LYS A C   1 
ATOM   1255  O  O   . LYS A  1 157 ? 33.773  -6.713  25.104  1.00 15.85 ? 157 LYS A O   1 
ATOM   1256  C  CB  . LYS A  1 157 ? 34.518  -9.502  23.688  1.00 15.48 ? 157 LYS A CB  1 
ATOM   1257  C  CG  . LYS A  1 157 ? 35.151  -10.874 24.081  1.00 17.11 ? 157 LYS A CG  1 
ATOM   1258  C  CD  . LYS A  1 157 ? 36.047  -11.402 22.951  1.00 17.07 ? 157 LYS A CD  1 
ATOM   1259  C  CE  . LYS A  1 157 ? 36.454  -12.872 23.189  1.00 18.93 ? 157 LYS A CE  1 
ATOM   1260  N  NZ  . LYS A  1 157 ? 37.386  -13.390 22.082  1.00 20.66 ? 157 LYS A NZ  1 
ATOM   1261  N  N   . ILE A  1 158 ? 31.902  -7.388  23.978  1.00 15.45 ? 158 ILE A N   1 
ATOM   1262  C  CA  . ILE A  1 158 ? 31.321  -6.046  23.945  1.00 15.21 ? 158 ILE A CA  1 
ATOM   1263  C  C   . ILE A  1 158 ? 30.321  -5.887  25.124  1.00 13.37 ? 158 ILE A C   1 
ATOM   1264  O  O   . ILE A  1 158 ? 30.389  -4.861  25.892  1.00 13.65 ? 158 ILE A O   1 
ATOM   1265  C  CB  . ILE A  1 158 ? 30.572  -5.744  22.645  1.00 15.05 ? 158 ILE A CB  1 
ATOM   1266  C  CG1 . ILE A  1 158 ? 31.534  -5.780  21.480  1.00 18.43 ? 158 ILE A CG1 1 
ATOM   1267  C  CG2 . ILE A  1 158 ? 29.798  -4.405  22.721  1.00 17.43 ? 158 ILE A CG2 1 
ATOM   1268  C  CD1 . ILE A  1 158 ? 30.936  -5.841  20.070  1.00 19.04 ? 158 ILE A CD1 1 
ATOM   1269  N  N   . PHE A  1 159 ? 29.377  -6.830  25.258  1.00 12.83 ? 159 PHE A N   1 
ATOM   1270  C  CA  . PHE A  1 159 ? 28.342  -6.669  26.279  1.00 12.89 ? 159 PHE A CA  1 
ATOM   1271  C  C   . PHE A  1 159 ? 28.811  -6.504  27.716  1.00 14.50 ? 159 PHE A C   1 
ATOM   1272  O  O   . PHE A  1 159 ? 28.146  -5.857  28.514  1.00 15.03 ? 159 PHE A O   1 
ATOM   1273  C  CB  . PHE A  1 159 ? 27.302  -7.717  26.194  1.00 13.12 ? 159 PHE A CB  1 
ATOM   1274  C  CG  . PHE A  1 159 ? 26.566  -7.838  24.864  1.00 13.52 ? 159 PHE A CG  1 
ATOM   1275  C  CD1 . PHE A  1 159 ? 26.484  -6.782  23.950  1.00 14.36 ? 159 PHE A CD1 1 
ATOM   1276  C  CD2 . PHE A  1 159 ? 25.936  -9.029  24.555  1.00 13.59 ? 159 PHE A CD2 1 
ATOM   1277  C  CE1 . PHE A  1 159 ? 25.788  -6.937  22.753  1.00 14.81 ? 159 PHE A CE1 1 
ATOM   1278  C  CE2 . PHE A  1 159 ? 25.250  -9.179  23.365  1.00 16.34 ? 159 PHE A CE2 1 
ATOM   1279  C  CZ  . PHE A  1 159 ? 25.164  -8.156  22.468  1.00 13.92 ? 159 PHE A CZ  1 
ATOM   1280  N  N   . SER A  1 160 ? 29.968  -7.095  28.006  1.00 14.26 ? 160 SER A N   1 
ATOM   1281  C  CA  . SER A  1 160 ? 30.522  -6.905  29.409  1.00 16.90 ? 160 SER A CA  1 
ATOM   1282  C  C   . SER A  1 160 ? 30.881  -5.522  29.804  1.00 19.10 ? 160 SER A C   1 
ATOM   1283  O  O   . SER A  1 160 ? 31.031  -5.230  31.025  1.00 21.00 ? 160 SER A O   1 
ATOM   1284  C  CB  . SER A  1 160 ? 31.689  -7.874  29.593  1.00 15.91 ? 160 SER A CB  1 
ATOM   1285  O  OG  . SER A  1 160 ? 32.811  -7.486  28.852  1.00 17.36 ? 160 SER A OG  1 
ATOM   1286  N  N   . HIS A  1 161 ? 31.003  -4.646  28.831  1.00 16.13 ? 161 HIS A N   1 
ATOM   1287  C  CA  . HIS A  1 161 ? 31.264  -3.292  29.068  1.00 16.19 ? 161 HIS A CA  1 
ATOM   1288  C  C   . HIS A  1 161 ? 30.041  -2.375  29.080  1.00 16.14 ? 161 HIS A C   1 
ATOM   1289  O  O   . HIS A  1 161 ? 30.217  -1.151  29.335  1.00 16.48 ? 161 HIS A O   1 
ATOM   1290  C  CB  . HIS A  1 161 ? 32.269  -2.720  28.062  1.00 17.04 ? 161 HIS A CB  1 
ATOM   1291  C  CG  . HIS A  1 161 ? 33.556  -3.453  28.078  1.00 16.80 ? 161 HIS A CG  1 
ATOM   1292  N  ND1 . HIS A  1 161 ? 34.647  -3.002  28.806  1.00 18.96 ? 161 HIS A ND1 1 
ATOM   1293  C  CD2 . HIS A  1 161 ? 33.968  -4.574  27.419  1.00 16.90 ? 161 HIS A CD2 1 
ATOM   1294  C  CE1 . HIS A  1 161 ? 35.673  -3.841  28.642  1.00 21.38 ? 161 HIS A CE1 1 
ATOM   1295  N  NE2 . HIS A  1 161 ? 35.290  -4.807  27.810  1.00 18.07 ? 161 HIS A NE2 1 
ATOM   1296  N  N   . LEU A  1 162 ? 28.832  -2.905  28.828  1.00 15.56 ? 162 LEU A N   1 
ATOM   1297  C  CA  . LEU A  1 162 ? 27.662  -2.027  28.689  1.00 15.57 ? 162 LEU A CA  1 
ATOM   1298  C  C   . LEU A  1 162 ? 27.406  -1.204  29.943  1.00 16.84 ? 162 LEU A C   1 
ATOM   1299  O  O   . LEU A  1 162 ? 27.006  -0.050  29.846  1.00 15.69 ? 162 LEU A O   1 
ATOM   1300  C  CB  . LEU A  1 162 ? 26.406  -2.813  28.405  1.00 15.70 ? 162 LEU A CB  1 
ATOM   1301  C  CG  . LEU A  1 162 ? 26.403  -3.450  27.015  1.00 15.46 ? 162 LEU A CG  1 
ATOM   1302  C  CD1 . LEU A  1 162 ? 25.167  -4.351  26.894  1.00 17.48 ? 162 LEU A CD1 1 
ATOM   1303  C  CD2 . LEU A  1 162 ? 26.377  -2.436  25.888  1.00 20.79 ? 162 LEU A CD2 1 
ATOM   1304  N  N   . GLN A  1 163 ? 27.685  -1.763  31.110  1.00 17.60 ? 163 GLN A N   1 
ATOM   1305  C  CA  . GLN A  1 163 ? 27.335  -0.960  32.291  1.00 20.08 ? 163 GLN A CA  1 
ATOM   1306  C  C   . GLN A  1 163 ? 28.134  0.307   32.410  1.00 21.84 ? 163 GLN A C   1 
ATOM   1307  O  O   . GLN A  1 163 ? 27.580  1.302   32.910  1.00 24.16 ? 163 GLN A O   1 
ATOM   1308  C  CB  . GLN A  1 163 ? 27.327  -1.830  33.542  1.00 31.28 ? 163 GLN A CB  1 
ATOM   1309  C  CG  . GLN A  1 163 ? 28.424  -1.590  34.576  1.00 47.10 ? 163 GLN A CG  1 
ATOM   1310  C  CD  . GLN A  1 163 ? 29.684  -2.450  34.414  1.00 51.37 ? 163 GLN A CD  1 
ATOM   1311  O  OE1 . GLN A  1 163 ? 30.288  -2.855  35.438  1.00 39.37 ? 163 GLN A OE1 1 
ATOM   1312  N  NE2 . GLN A  1 163 ? 30.103  -2.723  33.149  1.00 44.75 ? 163 GLN A NE2 1 
ATOM   1313  N  N   . HIS A  1 164 ? 29.331  0.337   31.811  1.00 16.78 ? 164 HIS A N   1 
ATOM   1314  C  CA  . HIS A  1 164 ? 30.135  1.556   31.847  1.00 16.18 ? 164 HIS A CA  1 
ATOM   1315  C  C   . HIS A  1 164 ? 29.776  2.580   30.837  1.00 15.86 ? 164 HIS A C   1 
ATOM   1316  O  O   . HIS A  1 164 ? 30.347  3.675   30.834  1.00 17.40 ? 164 HIS A O   1 
ATOM   1317  C  CB  . HIS A  1 164 ? 31.665  1.279   31.683  1.00 15.87 ? 164 HIS A CB  1 
ATOM   1318  C  CG  . HIS A  1 164 ? 32.275  0.418   32.759  1.00 17.40 ? 164 HIS A CG  1 
ATOM   1319  N  ND1 . HIS A  1 164 ? 32.050  0.611   34.096  1.00 19.70 ? 164 HIS A ND1 1 
ATOM   1320  C  CD2 . HIS A  1 164 ? 33.285  -0.477  32.679  1.00 22.25 ? 164 HIS A CD2 1 
ATOM   1321  C  CE1 . HIS A  1 164 ? 32.754  -0.262  34.793  1.00 17.44 ? 164 HIS A CE1 1 
ATOM   1322  N  NE2 . HIS A  1 164 ? 33.496  -0.958  33.964  1.00 25.93 ? 164 HIS A NE2 1 
ATOM   1323  N  N   . VAL A  1 165 ? 28.837  2.232   29.916  1.00 14.50 ? 165 VAL A N   1 
ATOM   1324  C  CA  . VAL A  1 165 ? 28.338  3.256   28.987  1.00 14.80 ? 165 VAL A CA  1 
ATOM   1325  C  C   . VAL A  1 165 ? 26.846  3.385   29.058  1.00 14.86 ? 165 VAL A C   1 
ATOM   1326  O  O   . VAL A  1 165 ? 26.145  3.713   28.101  1.00 14.29 ? 165 VAL A O   1 
ATOM   1327  C  CB  . VAL A  1 165 ? 28.757  2.950   27.518  1.00 15.22 ? 165 VAL A CB  1 
ATOM   1328  C  CG1 . VAL A  1 165 ? 30.306  3.113   27.359  1.00 16.89 ? 165 VAL A CG1 1 
ATOM   1329  C  CG2 . VAL A  1 165 ? 28.341  1.564   27.041  1.00 13.91 ? 165 VAL A CG2 1 
ATOM   1330  N  N   . LYS A  1 166 ? 26.327  3.284   30.277  1.00 14.53 ? 166 LYS A N   1 
ATOM   1331  C  CA  . LYS A  1 166 ? 24.901  3.439   30.538  1.00 15.06 ? 166 LYS A CA  1 
ATOM   1332  C  C   . LYS A  1 166 ? 24.235  4.705   29.978  1.00 13.30 ? 166 LYS A C   1 
ATOM   1333  O  O   . LYS A  1 166 ? 23.132  4.653   29.470  1.00 15.36 ? 166 LYS A O   1 
ATOM   1334  C  CB  . LYS A  1 166 ? 24.639  3.357   32.048  1.00 17.96 ? 166 LYS A CB  1 
ATOM   1335  C  CG  . LYS A  1 166 ? 23.171  3.413   32.510  1.00 18.82 ? 166 LYS A CG  1 
ATOM   1336  C  CD  . LYS A  1 166 ? 23.014  3.090   34.031  1.00 22.40 ? 166 LYS A CD  1 
ATOM   1337  C  CE  . LYS A  1 166 ? 23.602  1.699   34.310  1.00 31.31 ? 166 LYS A CE  1 
ATOM   1338  N  NZ  . LYS A  1 166 ? 22.990  0.496   33.613  1.00 44.82 ? 166 LYS A NZ  1 
ATOM   1339  N  N   . TYR A  1 167 ? 24.912  5.869   30.111  1.00 12.55 ? 167 TYR A N   1 
ATOM   1340  C  CA  . TYR A  1 167 ? 24.251  7.113   29.738  1.00 13.42 ? 167 TYR A CA  1 
ATOM   1341  C  C   . TYR A  1 167 ? 24.953  7.781   28.571  1.00 14.06 ? 167 TYR A C   1 
ATOM   1342  O  O   . TYR A  1 167 ? 26.129  7.564   28.311  1.00 13.50 ? 167 TYR A O   1 
ATOM   1343  C  CB  . TYR A  1 167 ? 24.340  8.067   30.957  1.00 13.60 ? 167 TYR A CB  1 
ATOM   1344  C  CG  . TYR A  1 167 ? 23.614  7.589   32.154  1.00 14.39 ? 167 TYR A CG  1 
ATOM   1345  C  CD1 . TYR A  1 167 ? 22.229  7.613   32.184  1.00 14.93 ? 167 TYR A CD1 1 
ATOM   1346  C  CD2 . TYR A  1 167 ? 24.322  7.052   33.238  1.00 14.25 ? 167 TYR A CD2 1 
ATOM   1347  C  CE1 . TYR A  1 167 ? 21.535  7.092   33.276  1.00 18.66 ? 167 TYR A CE1 1 
ATOM   1348  C  CE2 . TYR A  1 167 ? 23.618  6.534   34.348  1.00 17.88 ? 167 TYR A CE2 1 
ATOM   1349  C  CZ  . TYR A  1 167 ? 22.252  6.594   34.342  1.00 19.87 ? 167 TYR A CZ  1 
ATOM   1350  O  OH  . TYR A  1 167 ? 21.569  6.089   35.458  1.00 20.00 ? 167 TYR A OH  1 
ATOM   1351  N  N   . LYS A  1 168 ? 24.203  8.649   27.885  1.00 14.72 ? 168 LYS A N   1 
ATOM   1352  C  CA  . LYS A  1 168 ? 24.746  9.370   26.754  1.00 15.57 ? 168 LYS A CA  1 
ATOM   1353  C  C   . LYS A  1 168 ? 26.057  10.096  27.098  1.00 17.76 ? 168 LYS A C   1 
ATOM   1354  O  O   . LYS A  1 168 ? 26.118  10.678  28.198  1.00 17.54 ? 168 LYS A O   1 
ATOM   1355  C  CB  . LYS A  1 168 ? 23.682  10.383  26.247  1.00 15.94 ? 168 LYS A CB  1 
ATOM   1356  C  CG  . LYS A  1 168 ? 24.130  11.079  24.952  1.00 15.57 ? 168 LYS A CG  1 
ATOM   1357  C  CD  . LYS A  1 168 ? 23.159  12.114  24.395  1.00 21.31 ? 168 LYS A CD  1 
ATOM   1358  C  CE  . LYS A  1 168 ? 23.863  12.802  23.203  1.00 21.05 ? 168 LYS A CE  1 
ATOM   1359  N  NZ  . LYS A  1 168 ? 22.849  13.712  22.596  1.00 26.70 ? 168 LYS A NZ  1 
ATOM   1360  N  N   . GLY A  1 169 ? 27.092  10.088  26.237  1.00 16.88 ? 169 GLY A N   1 
ATOM   1361  C  CA  . GLY A  1 169 ? 28.353  10.759  26.542  1.00 18.77 ? 169 GLY A CA  1 
ATOM   1362  C  C   . GLY A  1 169 ? 29.369  9.903   27.273  1.00 18.67 ? 169 GLY A C   1 
ATOM   1363  O  O   . GLY A  1 169 ? 30.566  10.221  27.304  1.00 24.64 ? 169 GLY A O   1 
ATOM   1364  N  N   . GLN A  1 170 ? 28.925  8.804   27.833  1.00 16.89 ? 170 GLN A N   1 
ATOM   1365  C  CA  . GLN A  1 170 ? 29.877  7.964   28.549  1.00 14.34 ? 170 GLN A CA  1 
ATOM   1366  C  C   . GLN A  1 170 ? 30.677  7.061   27.640  1.00 16.91 ? 170 GLN A C   1 
ATOM   1367  O  O   . GLN A  1 170 ? 30.227  6.779   26.482  1.00 16.04 ? 170 GLN A O   1 
ATOM   1368  C  CB  . GLN A  1 170 ? 29.054  7.160   29.553  1.00 13.91 ? 170 GLN A CB  1 
ATOM   1369  C  CG  . GLN A  1 170 ? 28.646  7.977   30.733  1.00 14.01 ? 170 GLN A CG  1 
ATOM   1370  C  CD  . GLN A  1 170 ? 28.038  7.126   31.834  1.00 14.09 ? 170 GLN A CD  1 
ATOM   1371  O  OE1 . GLN A  1 170 ? 27.465  6.069   31.612  1.00 15.21 ? 170 GLN A OE1 1 
ATOM   1372  N  NE2 . GLN A  1 170 ? 28.162  7.593   33.095  1.00 15.11 ? 170 GLN A NE2 1 
ATOM   1373  N  N   A GLU A  1 171 ? 31.878  6.639   28.062  0.50 15.56 ? 171 GLU A N   1 
ATOM   1374  N  N   B GLU A  1 171 ? 31.845  6.596   28.090  0.50 14.62 ? 171 GLU A N   1 
ATOM   1375  C  CA  A GLU A  1 171 ? 32.816  5.922   27.207  0.50 16.32 ? 171 GLU A CA  1 
ATOM   1376  C  CA  B GLU A  1 171 ? 32.733  5.814   27.271  0.50 14.75 ? 171 GLU A CA  1 
ATOM   1377  C  C   A GLU A  1 171 ? 33.606  4.898   28.001  0.50 15.61 ? 171 GLU A C   1 
ATOM   1378  C  C   B GLU A  1 171 ? 33.420  4.735   28.073  0.50 15.43 ? 171 GLU A C   1 
ATOM   1379  O  O   A GLU A  1 171 ? 33.783  5.083   29.247  0.50 15.34 ? 171 GLU A O   1 
ATOM   1380  O  O   B GLU A  1 171 ? 33.374  4.716   29.348  0.50 15.67 ? 171 GLU A O   1 
ATOM   1381  C  CB  A GLU A  1 171 ? 33.770  6.913   26.505  0.50 19.99 ? 171 GLU A CB  1 
ATOM   1382  C  CB  B GLU A  1 171 ? 33.742  6.724   26.546  0.50 16.55 ? 171 GLU A CB  1 
ATOM   1383  C  CG  A GLU A  1 171 ? 33.147  8.253   26.168  0.50 22.30 ? 171 GLU A CG  1 
ATOM   1384  C  CG  B GLU A  1 171 ? 34.702  7.407   27.493  0.50 16.01 ? 171 GLU A CG  1 
ATOM   1385  C  CD  A GLU A  1 171 ? 33.966  9.157   25.239  0.50 24.02 ? 171 GLU A CD  1 
ATOM   1386  C  CD  B GLU A  1 171 ? 35.809  8.204   26.809  0.50 15.98 ? 171 GLU A CD  1 
ATOM   1387  O  OE1 A GLU A  1 171 ? 35.203  9.306   25.461  0.50 25.76 ? 171 GLU A OE1 1 
ATOM   1388  O  OE1 B GLU A  1 171 ? 35.618  8.730   25.690  0.50 17.86 ? 171 GLU A OE1 1 
ATOM   1389  O  OE2 A GLU A  1 171 ? 33.347  9.785   24.343  0.50 23.95 ? 171 GLU A OE2 1 
ATOM   1390  O  OE2 B GLU A  1 171 ? 36.903  8.351   27.419  0.50 14.46 ? 171 GLU A OE2 1 
ATOM   1391  N  N   . ALA A  1 172 ? 34.021  3.818   27.343  1.00 15.73 ? 172 ALA A N   1 
ATOM   1392  C  CA  . ALA A  1 172 ? 34.748  2.734   27.920  1.00 15.58 ? 172 ALA A CA  1 
ATOM   1393  C  C   . ALA A  1 172 ? 35.722  2.224   26.922  1.00 17.10 ? 172 ALA A C   1 
ATOM   1394  O  O   . ALA A  1 172 ? 35.608  2.483   25.705  1.00 18.53 ? 172 ALA A O   1 
ATOM   1395  C  CB  . ALA A  1 172 ? 33.792  1.615   28.336  1.00 17.22 ? 172 ALA A CB  1 
ATOM   1396  N  N   . PHE A  1 173 ? 36.754  1.530   27.380  1.00 18.47 ? 173 PHE A N   1 
ATOM   1397  C  CA  . PHE A  1 173 ? 37.780  0.954   26.521  1.00 19.35 ? 173 PHE A CA  1 
ATOM   1398  C  C   . PHE A  1 173 ? 37.628  -0.534  26.444  1.00 20.14 ? 173 PHE A C   1 
ATOM   1399  O  O   . PHE A  1 173 ? 37.417  -1.205  27.475  1.00 22.54 ? 173 PHE A O   1 
ATOM   1400  C  CB  . PHE A  1 173 ? 39.125  1.443   27.092  1.00 19.68 ? 173 PHE A CB  1 
ATOM   1401  C  CG  . PHE A  1 173 ? 39.434  2.859   26.646  1.00 25.50 ? 173 PHE A CG  1 
ATOM   1402  C  CD1 . PHE A  1 173 ? 39.766  3.144   25.284  1.00 27.81 ? 173 PHE A CD1 1 
ATOM   1403  C  CD2 . PHE A  1 173 ? 39.337  3.917   27.555  1.00 32.87 ? 173 PHE A CD2 1 
ATOM   1404  C  CE1 . PHE A  1 173 ? 40.027  4.450   24.871  1.00 29.71 ? 173 PHE A CE1 1 
ATOM   1405  C  CE2 . PHE A  1 173 ? 39.614  5.219   27.149  1.00 30.45 ? 173 PHE A CE2 1 
ATOM   1406  C  CZ  . PHE A  1 173 ? 39.958  5.497   25.819  1.00 30.02 ? 173 PHE A CZ  1 
ATOM   1407  N  N   . VAL A  1 174 ? 37.607  -1.090  25.207  1.00 15.63 ? 174 VAL A N   1 
ATOM   1408  C  CA  . VAL A  1 174 ? 37.499  -2.464  24.946  1.00 17.18 ? 174 VAL A CA  1 
ATOM   1409  C  C   . VAL A  1 174 ? 38.792  -2.982  24.369  1.00 18.79 ? 174 VAL A C   1 
ATOM   1410  O  O   . VAL A  1 174 ? 39.238  -2.469  23.363  1.00 18.53 ? 174 VAL A O   1 
ATOM   1411  C  CB  . VAL A  1 174 ? 36.319  -2.704  23.959  1.00 15.74 ? 174 VAL A CB  1 
ATOM   1412  C  CG1 . VAL A  1 174 ? 36.196  -4.170  23.748  1.00 16.08 ? 174 VAL A CG1 1 
ATOM   1413  C  CG2 . VAL A  1 174 ? 35.018  -2.158  24.547  1.00 17.08 ? 174 VAL A CG2 1 
ATOM   1414  N  N   . PRO A  1 175 ? 39.420  -3.984  25.021  1.00 16.48 ? 175 PRO A N   1 
ATOM   1415  C  CA  . PRO A  1 175 ? 40.643  -4.555  24.434  1.00 18.62 ? 175 PRO A CA  1 
ATOM   1416  C  C   . PRO A  1 175 ? 40.343  -5.244  23.107  1.00 17.12 ? 175 PRO A C   1 
ATOM   1417  O  O   . PRO A  1 175 ? 39.273  -5.843  22.945  1.00 18.00 ? 175 PRO A O   1 
ATOM   1418  C  CB  . PRO A  1 175 ? 41.072  -5.618  25.464  1.00 20.94 ? 175 PRO A CB  1 
ATOM   1419  C  CG  . PRO A  1 175 ? 40.368  -5.168  26.685  1.00 21.12 ? 175 PRO A CG  1 
ATOM   1420  C  CD  . PRO A  1 175 ? 39.022  -4.639  26.254  1.00 19.74 ? 175 PRO A CD  1 
ATOM   1421  N  N   . GLY A  1 176 ? 41.283  -5.149  22.209  1.00 17.70 ? 176 GLY A N   1 
ATOM   1422  C  CA  . GLY A  1 176 ? 41.097  -5.772  20.919  1.00 17.06 ? 176 GLY A CA  1 
ATOM   1423  C  C   . GLY A  1 176 ? 40.729  -7.217  21.011  1.00 19.20 ? 176 GLY A C   1 
ATOM   1424  O  O   . GLY A  1 176 ? 41.359  -7.989  21.776  1.00 19.30 ? 176 GLY A O   1 
ATOM   1425  N  N   . PHE A  1 177 ? 39.827  -7.681  20.125  1.00 15.75 ? 177 PHE A N   1 
ATOM   1426  C  CA  . PHE A  1 177 ? 39.525  -9.036  19.901  1.00 13.41 ? 177 PHE A CA  1 
ATOM   1427  C  C   . PHE A  1 177 ? 39.162  -9.281  18.441  1.00 13.02 ? 177 PHE A C   1 
ATOM   1428  O  O   . PHE A  1 177 ? 39.178  -8.296  17.705  1.00 13.69 ? 177 PHE A O   1 
ATOM   1429  C  CB  . PHE A  1 177 ? 38.380  -9.536  20.848  1.00 15.85 ? 177 PHE A CB  1 
ATOM   1430  C  CG  . PHE A  1 177 ? 37.008  -8.938  20.551  1.00 15.03 ? 177 PHE A CG  1 
ATOM   1431  C  CD1 . PHE A  1 177 ? 36.681  -7.644  20.997  1.00 14.48 ? 177 PHE A CD1 1 
ATOM   1432  C  CD2 . PHE A  1 177 ? 36.078  -9.694  19.789  1.00 15.12 ? 177 PHE A CD2 1 
ATOM   1433  C  CE1 . PHE A  1 177 ? 35.396  -7.078  20.698  1.00 16.80 ? 177 PHE A CE1 1 
ATOM   1434  C  CE2 . PHE A  1 177 ? 34.824  -9.118  19.519  1.00 14.52 ? 177 PHE A CE2 1 
ATOM   1435  C  CZ  . PHE A  1 177 ? 34.481  -7.859  19.940  1.00 15.43 ? 177 PHE A CZ  1 
ATOM   1436  N  N   . ASN A  1 178 ? 38.998  -10.534 18.064  1.00 13.55 ? 178 ASN A N   1 
ATOM   1437  C  CA  . ASN A  1 178 ? 38.768  -10.817 16.640  1.00 13.46 ? 178 ASN A CA  1 
ATOM   1438  C  C   . ASN A  1 178 ? 37.265  -10.522 16.319  1.00 13.94 ? 178 ASN A C   1 
ATOM   1439  O  O   . ASN A  1 178 ? 36.322  -11.364 16.599  1.00 12.81 ? 178 ASN A O   1 
ATOM   1440  C  CB  . ASN A  1 178 ? 39.137  -12.278 16.328  1.00 14.83 ? 178 ASN A CB  1 
ATOM   1441  C  CG  . ASN A  1 178 ? 38.950  -12.620 14.892  1.00 16.83 ? 178 ASN A CG  1 
ATOM   1442  O  OD1 . ASN A  1 178 ? 38.651  -11.784 14.022  1.00 14.74 ? 178 ASN A OD1 1 
ATOM   1443  N  ND2 . ASN A  1 178 ? 39.116  -13.852 14.586  1.00 19.69 ? 178 ASN A ND2 1 
ATOM   1444  N  N   . ILE A  1 179 ? 37.077  -9.381  15.629  1.00 12.44 ? 179 ILE A N   1 
ATOM   1445  C  CA  . ILE A  1 179 ? 35.722  -8.963  15.264  1.00 11.78 ? 179 ILE A CA  1 
ATOM   1446  C  C   . ILE A  1 179 ? 35.098  -10.019 14.349  1.00 12.00 ? 179 ILE A C   1 
ATOM   1447  O  O   . ILE A  1 179 ? 33.849  -10.088 14.272  1.00 11.09 ? 179 ILE A O   1 
ATOM   1448  C  CB  . ILE A  1 179 ? 35.793  -7.624  14.546  1.00 11.37 ? 179 ILE A CB  1 
ATOM   1449  C  CG1 . ILE A  1 179 ? 36.461  -6.564  15.471  1.00 11.62 ? 179 ILE A CG1 1 
ATOM   1450  C  CG2 . ILE A  1 179 ? 34.364  -7.215  14.149  1.00 12.37 ? 179 ILE A CG2 1 
ATOM   1451  C  CD1 . ILE A  1 179 ? 35.763  -6.362  16.827  1.00 13.69 ? 179 ILE A CD1 1 
ATOM   1452  N  N   . GLU A  1 180 ? 35.833  -10.858 13.594  1.00 11.71 ? 180 GLU A N   1 
ATOM   1453  C  CA  . GLU A  1 180 ? 35.189  -11.820 12.764  1.00 12.00 ? 180 GLU A CA  1 
ATOM   1454  C  C   . GLU A  1 180 ? 34.371  -12.837 13.601  1.00 11.22 ? 180 GLU A C   1 
ATOM   1455  O  O   . GLU A  1 180 ? 33.458  -13.482 13.072  1.00 12.73 ? 180 GLU A O   1 
ATOM   1456  C  CB  . GLU A  1 180 ? 36.215  -12.560 11.914  1.00 15.45 ? 180 GLU A CB  1 
ATOM   1457  C  CG  . GLU A  1 180 ? 35.667  -13.278 10.722  1.00 18.89 ? 180 GLU A CG  1 
ATOM   1458  C  CD  . GLU A  1 180 ? 36.719  -13.713 9.746   1.00 21.77 ? 180 GLU A CD  1 
ATOM   1459  O  OE1 . GLU A  1 180 ? 37.920  -13.451 9.923   1.00 21.59 ? 180 GLU A OE1 1 
ATOM   1460  O  OE2 . GLU A  1 180 ? 36.277  -14.426 8.868   1.00 25.76 ? 180 GLU A OE2 1 
ATOM   1461  N  N   . GLU A  1 181 ? 34.695  -12.929 14.915  1.00 12.10 ? 181 GLU A N   1 
ATOM   1462  C  CA  . GLU A  1 181 ? 33.962  -13.866 15.811  1.00 12.87 ? 181 GLU A CA  1 
ATOM   1463  C  C   . GLU A  1 181 ? 32.476  -13.377 15.909  1.00 11.93 ? 181 GLU A C   1 
ATOM   1464  O  O   . GLU A  1 181 ? 31.627  -14.169 16.359  1.00 14.13 ? 181 GLU A O   1 
ATOM   1465  C  CB  . GLU A  1 181 ? 34.528  -13.868 17.196  1.00 12.86 ? 181 GLU A CB  1 
ATOM   1466  C  CG  . GLU A  1 181 ? 35.959  -14.423 17.328  1.00 14.89 ? 181 GLU A CG  1 
ATOM   1467  C  CD  . GLU A  1 181 ? 36.599  -14.229 18.680  1.00 19.29 ? 181 GLU A CD  1 
ATOM   1468  O  OE1 . GLU A  1 181 ? 35.949  -13.722 19.619  1.00 19.00 ? 181 GLU A OE1 1 
ATOM   1469  O  OE2 . GLU A  1 181 ? 37.780  -14.602 18.781  1.00 19.67 ? 181 GLU A OE2 1 
ATOM   1470  N  N   . LEU A  1 182 ? 32.193  -12.094 15.590  1.00 10.72 ? 182 LEU A N   1 
ATOM   1471  C  CA  . LEU A  1 182 ? 30.798  -11.608 15.660  1.00 10.73 ? 182 LEU A CA  1 
ATOM   1472  C  C   . LEU A  1 182 ? 30.020  -11.996 14.451  1.00 11.25 ? 182 LEU A C   1 
ATOM   1473  O  O   . LEU A  1 182 ? 28.785  -11.807 14.434  1.00 11.44 ? 182 LEU A O   1 
ATOM   1474  C  CB  . LEU A  1 182 ? 30.805  -10.066 15.761  1.00 10.48 ? 182 LEU A CB  1 
ATOM   1475  C  CG  . LEU A  1 182 ? 31.611  -9.554  16.961  1.00 9.67  ? 182 LEU A CG  1 
ATOM   1476  C  CD1 . LEU A  1 182 ? 31.551  -7.994  16.985  1.00 11.50 ? 182 LEU A CD1 1 
ATOM   1477  C  CD2 . LEU A  1 182 ? 31.089  -10.064 18.268  1.00 11.63 ? 182 LEU A CD2 1 
ATOM   1478  N  N   . LEU A  1 183 ? 30.666  -12.481 13.375  1.00 11.46 ? 183 LEU A N   1 
ATOM   1479  C  CA  . LEU A  1 183 ? 29.969  -12.886 12.125  1.00 10.49 ? 183 LEU A CA  1 
ATOM   1480  C  C   . LEU A  1 183 ? 29.357  -14.264 12.217  1.00 11.86 ? 183 LEU A C   1 
ATOM   1481  O  O   . LEU A  1 183 ? 29.938  -15.079 12.990  1.00 13.11 ? 183 LEU A O   1 
ATOM   1482  C  CB  . LEU A  1 183 ? 31.000  -12.803 10.975  1.00 11.55 ? 183 LEU A CB  1 
ATOM   1483  C  CG  . LEU A  1 183 ? 31.626  -11.398 10.803  1.00 12.97 ? 183 LEU A CG  1 
ATOM   1484  C  CD1 . LEU A  1 183 ? 32.481  -11.419 9.515   1.00 14.90 ? 183 LEU A CD1 1 
ATOM   1485  C  CD2 . LEU A  1 183 ? 30.588  -10.275 10.723  1.00 13.62 ? 183 LEU A CD2 1 
ATOM   1486  N  N   . PRO A  1 184 ? 28.314  -14.576 11.498  1.00 10.72 ? 184 PRO A N   1 
ATOM   1487  C  CA  . PRO A  1 184 ? 27.678  -15.844 11.505  1.00 11.58 ? 184 PRO A CA  1 
ATOM   1488  C  C   . PRO A  1 184 ? 28.393  -16.844 10.665  1.00 14.59 ? 184 PRO A C   1 
ATOM   1489  O  O   . PRO A  1 184 ? 29.490  -16.596 10.076  1.00 14.52 ? 184 PRO A O   1 
ATOM   1490  C  CB  . PRO A  1 184 ? 26.233  -15.466 10.954  1.00 12.94 ? 184 PRO A CB  1 
ATOM   1491  C  CG  . PRO A  1 184 ? 26.672  -14.460 9.864   1.00 11.46 ? 184 PRO A CG  1 
ATOM   1492  C  CD  . PRO A  1 184 ? 27.693  -13.606 10.558  1.00 11.45 ? 184 PRO A CD  1 
ATOM   1493  N  N   . GLU A  1 185 ? 27.823  -18.051 10.755  1.00 16.72 ? 185 GLU A N   1 
ATOM   1494  C  CA  . GLU A  1 185 ? 28.245  -19.170 9.887   1.00 16.92 ? 185 GLU A CA  1 
ATOM   1495  C  C   . GLU A  1 185 ? 28.020  -18.902 8.443   1.00 17.64 ? 185 GLU A C   1 
ATOM   1496  O  O   . GLU A  1 185 ? 27.013  -18.179 8.074   1.00 17.38 ? 185 GLU A O   1 
ATOM   1497  C  CB  . GLU A  1 185 ? 27.371  -20.414 10.219  1.00 21.12 ? 185 GLU A CB  1 
ATOM   1498  C  CG  . GLU A  1 185 ? 27.718  -20.978 11.631  1.00 27.15 ? 185 GLU A CG  1 
ATOM   1499  C  CD  . GLU A  1 185 ? 29.232  -21.135 11.838  1.00 36.89 ? 185 GLU A CD  1 
ATOM   1500  O  OE1 . GLU A  1 185 ? 29.860  -21.931 11.099  1.00 36.50 ? 185 GLU A OE1 1 
ATOM   1501  O  OE2 . GLU A  1 185 ? 29.795  -20.464 12.742  1.00 44.17 ? 185 GLU A OE2 1 
ATOM   1502  N  N   . ARG A  1 186 ? 28.933  -19.407 7.587   1.00 16.30 ? 186 ARG A N   1 
ATOM   1503  C  CA  . ARG A  1 186 ? 28.747  -19.370 6.156   1.00 18.57 ? 186 ARG A CA  1 
ATOM   1504  C  C   . ARG A  1 186 ? 28.487  -17.901 5.705   1.00 14.60 ? 186 ARG A C   1 
ATOM   1505  O  O   . ARG A  1 186 ? 27.516  -17.500 5.023   1.00 15.53 ? 186 ARG A O   1 
ATOM   1506  C  CB  . ARG A  1 186 ? 27.595  -20.251 5.649   1.00 19.81 ? 186 ARG A CB  1 
ATOM   1507  C  CG  . ARG A  1 186 ? 27.750  -21.709 6.096   1.00 23.96 ? 186 ARG A CG  1 
ATOM   1508  C  CD  . ARG A  1 186 ? 26.823  -22.659 5.332   1.00 23.54 ? 186 ARG A CD  1 
ATOM   1509  N  NE  . ARG A  1 186 ? 25.394  -22.467 5.632   1.00 27.56 ? 186 ARG A NE  1 
ATOM   1510  C  CZ  . ARG A  1 186 ? 24.818  -22.673 6.817   1.00 29.90 ? 186 ARG A CZ  1 
ATOM   1511  N  NH1 . ARG A  1 186 ? 25.531  -23.055 7.865   1.00 30.68 ? 186 ARG A NH1 1 
ATOM   1512  N  NH2 . ARG A  1 186 ? 23.510  -22.480 6.992   1.00 37.97 ? 186 ARG A NH2 1 
ATOM   1513  N  N   . THR A  1 187 ? 29.480  -17.134 6.045   1.00 12.17 ? 187 THR A N   1 
ATOM   1514  C  CA  . THR A  1 187 ? 29.463  -15.742 5.543   1.00 12.94 ? 187 THR A CA  1 
ATOM   1515  C  C   . THR A  1 187 ? 29.521  -15.584 4.042   1.00 12.50 ? 187 THR A C   1 
ATOM   1516  O  O   . THR A  1 187 ? 29.178  -14.519 3.532   1.00 12.97 ? 187 THR A O   1 
ATOM   1517  C  CB  . THR A  1 187 ? 30.608  -14.880 6.116   1.00 12.79 ? 187 THR A CB  1 
ATOM   1518  O  OG1 . THR A  1 187 ? 31.857  -15.505 5.906   1.00 15.29 ? 187 THR A OG1 1 
ATOM   1519  C  CG2 . THR A  1 187 ? 30.444  -14.553 7.637   1.00 14.60 ? 187 THR A CG2 1 
ATOM   1520  N  N   . ALA A  1 188 ? 29.833  -16.666 3.298   1.00 14.18 ? 188 ALA A N   1 
ATOM   1521  C  CA  . ALA A  1 188 ? 29.598  -16.612 1.867   1.00 14.07 ? 188 ALA A CA  1 
ATOM   1522  C  C   . ALA A  1 188 ? 28.145  -16.396 1.416   1.00 13.37 ? 188 ALA A C   1 
ATOM   1523  O  O   . ALA A  1 188 ? 27.932  -15.989 0.291   1.00 13.81 ? 188 ALA A O   1 
ATOM   1524  C  CB  . ALA A  1 188 ? 30.155  -17.952 1.226   1.00 16.68 ? 188 ALA A CB  1 
ATOM   1525  N  N   . GLU A  1 189 ? 27.186  -16.683 2.341   1.00 13.71 ? 189 GLU A N   1 
ATOM   1526  C  CA  . GLU A  1 189 ? 25.749  -16.618 2.028   1.00 13.78 ? 189 GLU A CA  1 
ATOM   1527  C  C   . GLU A  1 189 ? 25.271  -15.243 2.533   1.00 12.02 ? 189 GLU A C   1 
ATOM   1528  O  O   . GLU A  1 189 ? 25.253  -14.972 3.740   1.00 11.28 ? 189 GLU A O   1 
ATOM   1529  C  CB  . GLU A  1 189 ? 24.957  -17.767 2.683   1.00 15.38 ? 189 GLU A CB  1 
ATOM   1530  C  CG  . GLU A  1 189 ? 25.418  -19.143 2.189   1.00 19.16 ? 189 GLU A CG  1 
ATOM   1531  C  CD  . GLU A  1 189 ? 24.878  -20.268 3.032   1.00 22.89 ? 189 GLU A CD  1 
ATOM   1532  O  OE1 . GLU A  1 189 ? 24.120  -20.091 3.988   1.00 20.80 ? 189 GLU A OE1 1 
ATOM   1533  O  OE2 . GLU A  1 189 ? 25.313  -21.437 2.801   1.00 28.68 ? 189 GLU A OE2 1 
ATOM   1534  N  N   . TYR A  1 190 ? 24.882  -14.353 1.603   1.00 10.54 ? 190 TYR A N   1 
ATOM   1535  C  CA  . TYR A  1 190 ? 24.416  -12.988 1.970   1.00 10.02 ? 190 TYR A CA  1 
ATOM   1536  C  C   . TYR A  1 190 ? 23.422  -12.401 1.004   1.00 9.88  ? 190 TYR A C   1 
ATOM   1537  O  O   . TYR A  1 190 ? 23.372  -12.809 -0.190  1.00 10.37 ? 190 TYR A O   1 
ATOM   1538  C  CB  . TYR A  1 190 ? 25.635  -12.049 2.236   1.00 9.86  ? 190 TYR A CB  1 
ATOM   1539  C  CG  . TYR A  1 190 ? 26.537  -11.943 1.035   1.00 10.31 ? 190 TYR A CG  1 
ATOM   1540  C  CD1 . TYR A  1 190 ? 26.265  -11.022 0.062   1.00 11.07 ? 190 TYR A CD1 1 
ATOM   1541  C  CD2 . TYR A  1 190 ? 27.738  -12.641 0.979   1.00 11.80 ? 190 TYR A CD2 1 
ATOM   1542  C  CE1 . TYR A  1 190 ? 27.099  -10.811 -1.036  1.00 12.55 ? 190 TYR A CE1 1 
ATOM   1543  C  CE2 . TYR A  1 190 ? 28.597  -12.424 -0.112  1.00 11.55 ? 190 TYR A CE2 1 
ATOM   1544  C  CZ  . TYR A  1 190 ? 28.256  -11.534 -1.060  1.00 12.54 ? 190 TYR A CZ  1 
ATOM   1545  O  OH  . TYR A  1 190 ? 29.202  -11.349 -2.135  1.00 13.94 ? 190 TYR A OH  1 
ATOM   1546  N  N   . TYR A  1 191 ? 22.709  -11.409 1.447   1.00 9.61  ? 191 TYR A N   1 
ATOM   1547  C  CA  . TYR A  1 191 ? 21.889  -10.528 0.633   1.00 9.51  ? 191 TYR A CA  1 
ATOM   1548  C  C   . TYR A  1 191 ? 22.654  -9.269  0.351   1.00 9.86  ? 191 TYR A C   1 
ATOM   1549  O  O   . TYR A  1 191 ? 23.427  -8.778  1.235   1.00 10.21 ? 191 TYR A O   1 
ATOM   1550  C  CB  . TYR A  1 191 ? 20.589  -10.108 1.372   1.00 10.28 ? 191 TYR A CB  1 
ATOM   1551  C  CG  . TYR A  1 191 ? 19.771  -11.260 1.953   1.00 10.32 ? 191 TYR A CG  1 
ATOM   1552  C  CD1 . TYR A  1 191 ? 18.752  -11.810 1.222   1.00 11.23 ? 191 TYR A CD1 1 
ATOM   1553  C  CD2 . TYR A  1 191 ? 20.010  -11.705 3.289   1.00 10.33 ? 191 TYR A CD2 1 
ATOM   1554  C  CE1 . TYR A  1 191 ? 17.944  -12.804 1.820   1.00 12.17 ? 191 TYR A CE1 1 
ATOM   1555  C  CE2 . TYR A  1 191 ? 19.188  -12.676 3.887   1.00 11.08 ? 191 TYR A CE2 1 
ATOM   1556  C  CZ  . TYR A  1 191 ? 18.205  -13.201 3.112   1.00 11.04 ? 191 TYR A CZ  1 
ATOM   1557  O  OH  . TYR A  1 191 ? 17.399  -14.234 3.670   1.00 13.68 ? 191 TYR A OH  1 
ATOM   1558  N  N   . ARG A  1 192 ? 22.498  -8.700  -0.828  1.00 10.25 ? 192 ARG A N   1 
ATOM   1559  C  CA  . ARG A  1 192 ? 23.196  -7.474  -1.184  1.00 10.07 ? 192 ARG A CA  1 
ATOM   1560  C  C   . ARG A  1 192 ? 22.290  -6.518  -1.918  1.00 10.54 ? 192 ARG A C   1 
ATOM   1561  O  O   . ARG A  1 192 ? 21.531  -6.930  -2.804  1.00 10.40 ? 192 ARG A O   1 
ATOM   1562  C  CB  . ARG A  1 192 ? 24.322  -7.866  -2.168  1.00 10.96 ? 192 ARG A CB  1 
ATOM   1563  C  CG  . ARG A  1 192 ? 24.917  -6.695  -2.995  1.00 12.06 ? 192 ARG A CG  1 
ATOM   1564  C  CD  . ARG A  1 192 ? 25.818  -5.753  -2.114  1.00 12.81 ? 192 ARG A CD  1 
ATOM   1565  N  NE  . ARG A  1 192 ? 26.778  -6.462  -1.247  1.00 13.04 ? 192 ARG A NE  1 
ATOM   1566  C  CZ  . ARG A  1 192 ? 27.905  -7.027  -1.668  1.00 12.86 ? 192 ARG A CZ  1 
ATOM   1567  N  NH1 . ARG A  1 192 ? 28.224  -6.972  -2.948  1.00 15.23 ? 192 ARG A NH1 1 
ATOM   1568  N  NH2 . ARG A  1 192 ? 28.713  -7.642  -0.819  1.00 12.78 ? 192 ARG A NH2 1 
ATOM   1569  N  N   . TYR A  1 193 ? 22.296  -5.241  -1.477  1.00 9.89  ? 193 TYR A N   1 
ATOM   1570  C  CA  . TYR A  1 193 ? 21.488  -4.238  -2.159  1.00 9.55  ? 193 TYR A CA  1 
ATOM   1571  C  C   . TYR A  1 193 ? 22.042  -2.876  -1.887  1.00 9.57  ? 193 TYR A C   1 
ATOM   1572  O  O   . TYR A  1 193 ? 22.746  -2.652  -0.896  1.00 10.10 ? 193 TYR A O   1 
ATOM   1573  C  CB  . TYR A  1 193 ? 19.983  -4.352  -1.820  1.00 9.33  ? 193 TYR A CB  1 
ATOM   1574  C  CG  . TYR A  1 193 ? 19.595  -3.806  -0.466  1.00 8.71  ? 193 TYR A CG  1 
ATOM   1575  C  CD1 . TYR A  1 193 ? 19.791  -4.529  0.719   1.00 8.13  ? 193 TYR A CD1 1 
ATOM   1576  C  CD2 . TYR A  1 193 ? 19.006  -2.544  -0.344  1.00 9.76  ? 193 TYR A CD2 1 
ATOM   1577  C  CE1 . TYR A  1 193 ? 19.483  -4.027  1.952   1.00 8.15  ? 193 TYR A CE1 1 
ATOM   1578  C  CE2 . TYR A  1 193 ? 18.700  -1.989  0.888   1.00 9.14  ? 193 TYR A CE2 1 
ATOM   1579  C  CZ  . TYR A  1 193 ? 18.960  -2.753  2.038   1.00 7.85  ? 193 TYR A CZ  1 
ATOM   1580  O  OH  . TYR A  1 193 ? 18.608  -2.180  3.235   1.00 8.97  ? 193 TYR A OH  1 
ATOM   1581  N  N   . ARG A  1 194 ? 21.711  -1.909  -2.718  1.00 10.48 ? 194 ARG A N   1 
ATOM   1582  C  CA  . ARG A  1 194 ? 22.074  -0.515  -2.500  1.00 10.01 ? 194 ARG A CA  1 
ATOM   1583  C  C   . ARG A  1 194 ? 20.998  0.170   -1.743  1.00 10.70 ? 194 ARG A C   1 
ATOM   1584  O  O   . ARG A  1 194 ? 19.780  0.180   -2.069  1.00 11.39 ? 194 ARG A O   1 
ATOM   1585  C  CB  . ARG A  1 194 ? 22.142  0.214   -3.900  1.00 12.71 ? 194 ARG A CB  1 
ATOM   1586  C  CG  . ARG A  1 194 ? 23.375  -0.332  -4.600  1.00 17.83 ? 194 ARG A CG  1 
ATOM   1587  C  CD  . ARG A  1 194 ? 24.684  0.425   -4.259  1.00 32.59 ? 194 ARG A CD  1 
ATOM   1588  N  NE  . ARG A  1 194 ? 25.906  -0.144  -4.902  1.00 45.93 ? 194 ARG A NE  1 
ATOM   1589  C  CZ  . ARG A  1 194 ? 27.114  0.453   -4.977  1.00 43.49 ? 194 ARG A CZ  1 
ATOM   1590  N  NH1 . ARG A  1 194 ? 27.299  1.681   -4.498  1.00 45.01 ? 194 ARG A NH1 1 
ATOM   1591  N  NH2 . ARG A  1 194 ? 28.150  -0.192  -5.534  1.00 41.46 ? 194 ARG A NH2 1 
ATOM   1592  N  N   . GLY A  1 195 ? 21.386  0.793   -0.623  1.00 9.20  ? 195 GLY A N   1 
ATOM   1593  C  CA  . GLY A  1 195 ? 20.411  1.510   0.202   1.00 10.14 ? 195 GLY A CA  1 
ATOM   1594  C  C   . GLY A  1 195 ? 21.008  2.662   0.911   1.00 9.05  ? 195 GLY A C   1 
ATOM   1595  O  O   . GLY A  1 195 ? 21.881  3.388   0.338   1.00 9.99  ? 195 GLY A O   1 
ATOM   1596  N  N   . SER A  1 196 ? 20.602  2.857   2.155   1.00 7.86  ? 196 SER A N   1 
ATOM   1597  C  CA  . SER A  1 196 ? 20.905  4.116   2.817   1.00 7.84  ? 196 SER A CA  1 
ATOM   1598  C  C   . SER A  1 196 ? 21.356  3.842   4.264   1.00 8.34  ? 196 SER A C   1 
ATOM   1599  O  O   . SER A  1 196 ? 21.180  2.710   4.804   1.00 8.03  ? 196 SER A O   1 
ATOM   1600  C  CB  . SER A  1 196 ? 19.724  5.072   2.949   1.00 8.51  ? 196 SER A CB  1 
ATOM   1601  O  OG  . SER A  1 196 ? 18.728  4.556   3.891   1.00 7.72  ? 196 SER A OG  1 
ATOM   1602  N  N   . LEU A  1 197 ? 21.864  4.888   4.921   1.00 8.58  ? 197 LEU A N   1 
ATOM   1603  C  CA  . LEU A  1 197 ? 21.943  4.822   6.387   1.00 9.25  ? 197 LEU A CA  1 
ATOM   1604  C  C   . LEU A  1 197 ? 20.503  4.582   6.929   1.00 7.85  ? 197 LEU A C   1 
ATOM   1605  O  O   . LEU A  1 197 ? 19.552  5.210   6.402   1.00 8.10  ? 197 LEU A O   1 
ATOM   1606  C  CB  . LEU A  1 197 ? 22.450  6.129   6.986   1.00 11.32 ? 197 LEU A CB  1 
ATOM   1607  C  CG  . LEU A  1 197 ? 23.950  6.372   7.028   1.00 12.32 ? 197 LEU A CG  1 
ATOM   1608  C  CD1 . LEU A  1 197 ? 24.477  6.860   5.738   1.00 15.65 ? 197 LEU A CD1 1 
ATOM   1609  C  CD2 . LEU A  1 197 ? 24.287  7.479   8.002   1.00 14.92 ? 197 LEU A CD2 1 
ATOM   1610  N  N   . THR A  1 198 ? 20.377  3.828   8.001   1.00 7.67  ? 198 THR A N   1 
ATOM   1611  C  CA  . THR A  1 198 ? 19.055  3.653   8.588   1.00 7.94  ? 198 THR A CA  1 
ATOM   1612  C  C   . THR A  1 198 ? 18.786  4.667   9.682   1.00 8.47  ? 198 THR A C   1 
ATOM   1613  O  O   . THR A  1 198 ? 17.740  4.602   10.345  1.00 8.57  ? 198 THR A O   1 
ATOM   1614  C  CB  . THR A  1 198 ? 18.898  2.237   9.187   1.00 7.90  ? 198 THR A CB  1 
ATOM   1615  O  OG1 . THR A  1 198 ? 19.848  2.144   10.283  1.00 8.85  ? 198 THR A OG1 1 
ATOM   1616  C  CG2 . THR A  1 198 ? 19.159  1.141   8.213   1.00 8.65  ? 198 THR A CG2 1 
ATOM   1617  N  N   . THR A  1 199 ? 19.757  5.579   9.943   1.00 8.03  ? 199 THR A N   1 
ATOM   1618  C  CA  . THR A  1 199 ? 19.615  6.670   10.861  1.00 8.94  ? 199 THR A CA  1 
ATOM   1619  C  C   . THR A  1 199 ? 19.821  7.959   10.095  1.00 8.89  ? 199 THR A C   1 
ATOM   1620  O  O   . THR A  1 199 ? 20.467  7.903   9.058   1.00 9.86  ? 199 THR A O   1 
ATOM   1621  C  CB  . THR A  1 199 ? 20.662  6.678   12.014  1.00 9.26  ? 199 THR A CB  1 
ATOM   1622  O  OG1 . THR A  1 199 ? 21.954  6.805   11.436  1.00 11.13 ? 199 THR A OG1 1 
ATOM   1623  C  CG2 . THR A  1 199 ? 20.632  5.324   12.806  1.00 10.59 ? 199 THR A CG2 1 
ATOM   1624  N  N   . PRO A  1 200 ? 19.349  9.055   10.693  1.00 8.21  ? 200 PRO A N   1 
ATOM   1625  C  CA  . PRO A  1 200 ? 19.750  10.348  10.113  1.00 9.10  ? 200 PRO A CA  1 
ATOM   1626  C  C   . PRO A  1 200 ? 21.287  10.414  9.974   1.00 10.32 ? 200 PRO A C   1 
ATOM   1627  O  O   . PRO A  1 200 ? 21.981  9.870   10.840  1.00 11.44 ? 200 PRO A O   1 
ATOM   1628  C  CB  . PRO A  1 200 ? 19.238  11.344  11.185  1.00 8.94  ? 200 PRO A CB  1 
ATOM   1629  C  CG  . PRO A  1 200 ? 17.977  10.705  11.678  1.00 7.93  ? 200 PRO A CG  1 
ATOM   1630  C  CD  . PRO A  1 200 ? 18.373  9.186   11.760  1.00 8.56  ? 200 PRO A CD  1 
ATOM   1631  N  N   . PRO A  1 201 ? 21.776  10.996  8.902   1.00 10.23 ? 201 PRO A N   1 
ATOM   1632  C  CA  . PRO A  1 201 ? 21.041  11.765  7.847   1.00 10.17 ? 201 PRO A CA  1 
ATOM   1633  C  C   . PRO A  1 201 ? 20.426  10.948  6.724   1.00 9.71  ? 201 PRO A C   1 
ATOM   1634  O  O   . PRO A  1 201 ? 19.925  11.505  5.742   1.00 10.35 ? 201 PRO A O   1 
ATOM   1635  C  CB  . PRO A  1 201 ? 22.064  12.725  7.245   1.00 10.83 ? 201 PRO A CB  1 
ATOM   1636  C  CG  . PRO A  1 201 ? 23.243  12.616  8.113   1.00 14.91 ? 201 PRO A CG  1 
ATOM   1637  C  CD  . PRO A  1 201 ? 23.210  11.238  8.778   1.00 11.05 ? 201 PRO A CD  1 
ATOM   1638  N  N   . CYS A  1 202 ? 20.463  9.609   6.802   1.00 9.38  ? 202 CYS A N   1 
ATOM   1639  C  CA  . CYS A  1 202 ? 19.792  8.644   5.840   1.00 8.08  ? 202 CYS A CA  1 
ATOM   1640  C  C   . CYS A  1 202 ? 20.306  8.766   4.427   1.00 8.95  ? 202 CYS A C   1 
ATOM   1641  O  O   . CYS A  1 202 ? 19.610  8.461   3.489   1.00 9.93  ? 202 CYS A O   1 
ATOM   1642  C  CB  . CYS A  1 202 ? 18.254  8.957   5.829   1.00 10.00 ? 202 CYS A CB  1 
ATOM   1643  S  SG  . CYS A  1 202 ? 17.377  8.851   7.386   1.00 9.30  ? 202 CYS A SG  1 
ATOM   1644  N  N   . ASN A  1 203 ? 21.583  9.134   4.296   1.00 9.79  ? 203 ASN A N   1 
ATOM   1645  C  CA  . ASN A  1 203 ? 22.105  9.281   2.968   1.00 10.08 ? 203 ASN A CA  1 
ATOM   1646  C  C   . ASN A  1 203 ? 22.034  7.994   2.205   1.00 10.21 ? 203 ASN A C   1 
ATOM   1647  O  O   . ASN A  1 203 ? 22.350  6.910   2.749   1.00 9.10  ? 203 ASN A O   1 
ATOM   1648  C  CB  . ASN A  1 203 ? 23.619  9.648   3.061   1.00 13.04 ? 203 ASN A CB  1 
ATOM   1649  C  CG  . ASN A  1 203 ? 23.837  10.838  3.940   1.00 17.68 ? 203 ASN A CG  1 
ATOM   1650  O  OD1 . ASN A  1 203 ? 23.867  10.736  5.172   1.00 22.08 ? 203 ASN A OD1 1 
ATOM   1651  N  ND2 . ASN A  1 203 ? 23.863  11.983  3.352   1.00 23.64 ? 203 ASN A ND2 1 
ATOM   1652  N  N   . PRO A  1 204 ? 21.688  8.037   0.907   1.00 10.07 ? 204 PRO A N   1 
ATOM   1653  C  CA  . PRO A  1 204 ? 21.552  6.841   0.087   1.00 10.44 ? 204 PRO A CA  1 
ATOM   1654  C  C   . PRO A  1 204 ? 22.860  6.355   -0.508  1.00 10.98 ? 204 PRO A C   1 
ATOM   1655  O  O   . PRO A  1 204 ? 23.017  6.172   -1.751  1.00 13.31 ? 204 PRO A O   1 
ATOM   1656  C  CB  . PRO A  1 204 ? 20.555  7.292   -0.988  1.00 11.02 ? 204 PRO A CB  1 
ATOM   1657  C  CG  . PRO A  1 204 ? 20.951  8.779   -1.200  1.00 11.11 ? 204 PRO A CG  1 
ATOM   1658  C  CD  . PRO A  1 204 ? 21.230  9.292   0.200   1.00 10.56 ? 204 PRO A CD  1 
ATOM   1659  N  N   . THR A  1 205 ? 23.789  6.102   0.394   1.00 10.73 ? 205 THR A N   1 
ATOM   1660  C  CA  . THR A  1 205 ? 25.151  5.879   -0.075  1.00 10.58 ? 205 THR A CA  1 
ATOM   1661  C  C   . THR A  1 205 ? 25.744  4.587   0.495   1.00 11.30 ? 205 THR A C   1 
ATOM   1662  O  O   . THR A  1 205 ? 26.948  4.413   0.499   1.00 10.83 ? 205 THR A O   1 
ATOM   1663  C  CB  . THR A  1 205 ? 26.055  6.982   0.525   1.00 11.12 ? 205 THR A CB  1 
ATOM   1664  O  OG1 . THR A  1 205 ? 25.850  7.057   1.886   1.00 11.46 ? 205 THR A OG1 1 
ATOM   1665  C  CG2 . THR A  1 205 ? 25.720  8.352   -0.170  1.00 13.43 ? 205 THR A CG2 1 
ATOM   1666  N  N   . VAL A  1 206 ? 24.876  3.627   0.900   1.00 9.98  ? 206 VAL A N   1 
ATOM   1667  C  CA  . VAL A  1 206 ? 25.373  2.387   1.532   1.00 10.06 ? 206 VAL A CA  1 
ATOM   1668  C  C   . VAL A  1 206 ? 25.169  1.208   0.698   1.00 10.16 ? 206 VAL A C   1 
ATOM   1669  O  O   . VAL A  1 206 ? 24.059  0.917   0.202   1.00 11.26 ? 206 VAL A O   1 
ATOM   1670  C  CB  . VAL A  1 206 ? 24.560  2.168   2.866   1.00 9.01  ? 206 VAL A CB  1 
ATOM   1671  C  CG1 . VAL A  1 206 ? 25.048  0.862   3.516   1.00 9.49  ? 206 VAL A CG1 1 
ATOM   1672  C  CG2 . VAL A  1 206 ? 24.812  3.322   3.879   1.00 9.09  ? 206 VAL A CG2 1 
ATOM   1673  N  N   . LEU A  1 207 ? 26.238  0.484   0.507   1.00 9.05  ? 207 LEU A N   1 
ATOM   1674  C  CA  . LEU A  1 207 ? 26.173  -0.836  -0.098  1.00 9.23  ? 207 LEU A CA  1 
ATOM   1675  C  C   . LEU A  1 207 ? 25.969  -1.847  1.061   1.00 8.82  ? 207 LEU A C   1 
ATOM   1676  O  O   . LEU A  1 207 ? 26.857  -2.025  1.916   1.00 9.68  ? 207 LEU A O   1 
ATOM   1677  C  CB  . LEU A  1 207 ? 27.485  -1.184  -0.836  1.00 10.86 ? 207 LEU A CB  1 
ATOM   1678  C  CG  . LEU A  1 207 ? 27.382  -2.501  -1.596  1.00 14.57 ? 207 LEU A CG  1 
ATOM   1679  C  CD1 . LEU A  1 207 ? 26.301  -2.350  -2.746  1.00 18.30 ? 207 LEU A CD1 1 
ATOM   1680  C  CD2 . LEU A  1 207 ? 28.688  -2.820  -2.274  1.00 20.80 ? 207 LEU A CD2 1 
ATOM   1681  N  N   . TRP A  1 208 ? 24.766  -2.403  1.136   1.00 8.42  ? 208 TRP A N   1 
ATOM   1682  C  CA  . TRP A  1 208 ? 24.395  -3.382  2.205   1.00 8.07  ? 208 TRP A CA  1 
ATOM   1683  C  C   . TRP A  1 208 ? 24.745  -4.802  1.927   1.00 8.28  ? 208 TRP A C   1 
ATOM   1684  O  O   . TRP A  1 208 ? 24.495  -5.277  0.813   1.00 9.66  ? 208 TRP A O   1 
ATOM   1685  C  CB  . TRP A  1 208 ? 22.812  -3.307  2.456   1.00 8.17  ? 208 TRP A CB  1 
ATOM   1686  C  CG  . TRP A  1 208 ? 22.497  -2.121  3.264   1.00 8.47  ? 208 TRP A CG  1 
ATOM   1687  C  CD1 . TRP A  1 208 ? 22.016  -0.883  2.811   1.00 7.07  ? 208 TRP A CD1 1 
ATOM   1688  C  CD2 . TRP A  1 208 ? 22.566  -1.977  4.691   1.00 7.91  ? 208 TRP A CD2 1 
ATOM   1689  N  NE1 . TRP A  1 208 ? 21.877  0.006   3.833   1.00 7.81  ? 208 TRP A NE1 1 
ATOM   1690  C  CE2 . TRP A  1 208 ? 22.194  -0.651  5.021   1.00 7.68  ? 208 TRP A CE2 1 
ATOM   1691  C  CE3 . TRP A  1 208 ? 22.951  -2.823  5.743   1.00 7.90  ? 208 TRP A CE3 1 
ATOM   1692  C  CZ2 . TRP A  1 208 ? 22.240  -0.156  6.344   1.00 7.76  ? 208 TRP A CZ2 1 
ATOM   1693  C  CZ3 . TRP A  1 208 ? 22.943  -2.366  7.020   1.00 8.11  ? 208 TRP A CZ3 1 
ATOM   1694  C  CH2 . TRP A  1 208 ? 22.627  -1.030  7.333   1.00 8.36  ? 208 TRP A CH2 1 
ATOM   1695  N  N   . THR A  1 209 ? 25.343  -5.485  2.929   1.00 7.95  ? 209 THR A N   1 
ATOM   1696  C  CA  . THR A  1 209 ? 25.571  -6.905  2.916   1.00 8.50  ? 209 THR A CA  1 
ATOM   1697  C  C   . THR A  1 209 ? 24.905  -7.420  4.164   1.00 8.33  ? 209 THR A C   1 
ATOM   1698  O  O   . THR A  1 209 ? 25.405  -7.115  5.251   1.00 9.56  ? 209 THR A O   1 
ATOM   1699  C  CB  . THR A  1 209 ? 27.061  -7.275  2.875   1.00 9.30  ? 209 THR A CB  1 
ATOM   1700  O  OG1 . THR A  1 209 ? 27.634  -6.700  1.656   1.00 9.42  ? 209 THR A OG1 1 
ATOM   1701  C  CG2 . THR A  1 209 ? 27.255  -8.759  2.870   1.00 9.94  ? 209 THR A CG2 1 
ATOM   1702  N  N   . VAL A  1 210 ? 23.824  -8.154  3.981   1.00 8.45  ? 210 VAL A N   1 
ATOM   1703  C  CA  . VAL A  1 210 ? 23.132  -8.725  5.183   1.00 8.40  ? 210 VAL A CA  1 
ATOM   1704  C  C   . VAL A  1 210 ? 23.404  -10.238 5.140   1.00 8.46  ? 210 VAL A C   1 
ATOM   1705  O  O   . VAL A  1 210 ? 23.031  -10.906 4.171   1.00 9.27  ? 210 VAL A O   1 
ATOM   1706  C  CB  . VAL A  1 210 ? 21.607  -8.417  5.127   1.00 8.71  ? 210 VAL A CB  1 
ATOM   1707  C  CG1 . VAL A  1 210 ? 20.979  -9.001  6.436   1.00 9.91  ? 210 VAL A CG1 1 
ATOM   1708  C  CG2 . VAL A  1 210 ? 21.311  -6.933  4.999   1.00 9.44  ? 210 VAL A CG2 1 
ATOM   1709  N  N   . PHE A  1 211 ? 24.122  -10.770 6.104   1.00 7.84  ? 211 PHE A N   1 
ATOM   1710  C  CA  . PHE A  1 211 ? 24.375  -12.219 6.044   1.00 8.77  ? 211 PHE A CA  1 
ATOM   1711  C  C   . PHE A  1 211 ? 23.118  -13.012 6.199   1.00 8.32  ? 211 PHE A C   1 
ATOM   1712  O  O   . PHE A  1 211 ? 22.195  -12.658 6.962   1.00 9.49  ? 211 PHE A O   1 
ATOM   1713  C  CB  . PHE A  1 211 ? 25.414  -12.574 7.132   1.00 8.47  ? 211 PHE A CB  1 
ATOM   1714  C  CG  . PHE A  1 211 ? 26.731  -11.934 6.872   1.00 8.69  ? 211 PHE A CG  1 
ATOM   1715  C  CD1 . PHE A  1 211 ? 27.534  -12.398 5.866   1.00 10.90 ? 211 PHE A CD1 1 
ATOM   1716  C  CD2 . PHE A  1 211 ? 27.208  -10.883 7.717   1.00 10.48 ? 211 PHE A CD2 1 
ATOM   1717  C  CE1 . PHE A  1 211 ? 28.774  -11.746 5.572   1.00 13.16 ? 211 PHE A CE1 1 
ATOM   1718  C  CE2 . PHE A  1 211 ? 28.486  -10.282 7.419   1.00 10.83 ? 211 PHE A CE2 1 
ATOM   1719  C  CZ  . PHE A  1 211 ? 29.199  -10.709 6.316   1.00 11.10 ? 211 PHE A CZ  1 
ATOM   1720  N  N   A ARG A  1 212 ? 23.088  -14.129 5.442   0.50 8.85  ? 212 ARG A N   1 
ATOM   1721  N  N   B ARG A  1 212 ? 23.055  -14.127 5.455   0.50 9.04  ? 212 ARG A N   1 
ATOM   1722  C  CA  A ARG A  1 212 ? 21.916  -15.009 5.440   0.50 9.09  ? 212 ARG A CA  1 
ATOM   1723  C  CA  B ARG A  1 212 ? 21.823  -14.918 5.478   0.50 9.30  ? 212 ARG A CA  1 
ATOM   1724  C  C   A ARG A  1 212 ? 21.589  -15.590 6.813   0.50 9.47  ? 212 ARG A C   1 
ATOM   1725  C  C   B ARG A  1 212 ? 21.568  -15.587 6.853   0.50 9.58  ? 212 ARG A C   1 
ATOM   1726  O  O   A ARG A  1 212 ? 20.383  -15.630 7.177   0.50 11.33 ? 212 ARG A O   1 
ATOM   1727  O  O   B ARG A  1 212 ? 20.391  -15.645 7.294   0.50 11.49 ? 212 ARG A O   1 
ATOM   1728  C  CB  A ARG A  1 212 ? 22.151  -16.184 4.525   0.50 10.41 ? 212 ARG A CB  1 
ATOM   1729  C  CB  B ARG A  1 212 ? 21.855  -15.943 4.366   0.50 10.81 ? 212 ARG A CB  1 
ATOM   1730  C  CG  A ARG A  1 212 ? 20.946  -17.105 4.377   0.50 10.93 ? 212 ARG A CG  1 
ATOM   1731  C  CG  B ARG A  1 212 ? 20.594  -16.791 4.230   0.50 11.82 ? 212 ARG A CG  1 
ATOM   1732  C  CD  A ARG A  1 212 ? 21.257  -18.372 3.579   0.50 14.00 ? 212 ARG A CD  1 
ATOM   1733  C  CD  B ARG A  1 212 ? 20.897  -18.024 3.415   0.50 15.05 ? 212 ARG A CD  1 
ATOM   1734  N  NE  A ARG A  1 212 ? 20.058  -19.202 3.473   0.50 15.59 ? 212 ARG A NE  1 
ATOM   1735  N  NE  B ARG A  1 212 ? 19.658  -18.636 2.971   0.50 17.52 ? 212 ARG A NE  1 
ATOM   1736  C  CZ  A ARG A  1 212 ? 19.717  -20.145 4.349   0.50 18.13 ? 212 ARG A CZ  1 
ATOM   1737  C  CZ  B ARG A  1 212 ? 19.604  -19.667 2.121   0.50 18.98 ? 212 ARG A CZ  1 
ATOM   1738  N  NH1 A ARG A  1 212 ? 20.524  -20.449 5.332   0.50 20.11 ? 212 ARG A NH1 1 
ATOM   1739  N  NH1 B ARG A  1 212 ? 20.711  -20.200 1.643   0.50 18.77 ? 212 ARG A NH1 1 
ATOM   1740  N  NH2 A ARG A  1 212 ? 18.630  -20.860 4.161   0.50 21.60 ? 212 ARG A NH2 1 
ATOM   1741  N  NH2 B ARG A  1 212 ? 18.413  -20.102 1.720   0.50 20.01 ? 212 ARG A NH2 1 
ATOM   1742  N  N   . ASN A  1 213 ? 22.625  -16.014 7.537   1.00 9.22  ? 213 ASN A N   1 
ATOM   1743  C  CA  . ASN A  1 213 ? 22.383  -16.806 8.765   1.00 10.15 ? 213 ASN A CA  1 
ATOM   1744  C  C   . ASN A  1 213 ? 22.566  -15.905 9.989   1.00 11.09 ? 213 ASN A C   1 
ATOM   1745  O  O   . ASN A  1 213 ? 23.498  -15.077 10.014  1.00 10.18 ? 213 ASN A O   1 
ATOM   1746  C  CB  . ASN A  1 213 ? 23.457  -17.932 8.786   1.00 11.81 ? 213 ASN A CB  1 
ATOM   1747  C  CG  . ASN A  1 213 ? 23.370  -18.820 7.568   1.00 13.74 ? 213 ASN A CG  1 
ATOM   1748  O  OD1 . ASN A  1 213 ? 24.404  -19.051 6.855   1.00 17.66 ? 213 ASN A OD1 1 
ATOM   1749  N  ND2 . ASN A  1 213 ? 22.186  -19.153 7.212   1.00 14.57 ? 213 ASN A ND2 1 
ATOM   1750  N  N   . PRO A  1 214 ? 21.720  -16.072 11.001  1.00 9.87  ? 214 PRO A N   1 
ATOM   1751  C  CA  . PRO A  1 214 ? 21.828  -15.294 12.168  1.00 10.97 ? 214 PRO A CA  1 
ATOM   1752  C  C   . PRO A  1 214 ? 22.918  -15.881 13.125  1.00 10.08 ? 214 PRO A C   1 
ATOM   1753  O  O   . PRO A  1 214 ? 23.310  -17.057 12.973  1.00 12.02 ? 214 PRO A O   1 
ATOM   1754  C  CB  . PRO A  1 214 ? 20.433  -15.416 12.793  1.00 12.17 ? 214 PRO A CB  1 
ATOM   1755  C  CG  . PRO A  1 214 ? 20.056  -16.844 12.415  1.00 14.22 ? 214 PRO A CG  1 
ATOM   1756  C  CD  . PRO A  1 214 ? 20.483  -16.903 10.981  1.00 12.07 ? 214 PRO A CD  1 
ATOM   1757  N  N   . VAL A  1 215 ? 23.332  -15.056 14.075  1.00 9.32  ? 215 VAL A N   1 
ATOM   1758  C  CA  . VAL A  1 215 ? 24.053  -15.541 15.239  1.00 9.78  ? 215 VAL A CA  1 
ATOM   1759  C  C   . VAL A  1 215 ? 23.068  -15.688 16.416  1.00 10.57 ? 215 VAL A C   1 
ATOM   1760  O  O   . VAL A  1 215 ? 21.974  -15.108 16.389  1.00 11.10 ? 215 VAL A O   1 
ATOM   1761  C  CB  . VAL A  1 215 ? 25.207  -14.610 15.615  1.00 10.42 ? 215 VAL A CB  1 
ATOM   1762  C  CG1 . VAL A  1 215 ? 26.278  -14.470 14.491  1.00 12.50 ? 215 VAL A CG1 1 
ATOM   1763  C  CG2 . VAL A  1 215 ? 24.751  -13.229 16.107  1.00 10.29 ? 215 VAL A CG2 1 
ATOM   1764  N  N   . GLN A  1 216 ? 23.556  -16.294 17.468  1.00 11.56 ? 216 GLN A N   1 
ATOM   1765  C  CA  . GLN A  1 216 ? 22.761  -16.464 18.711  1.00 11.49 ? 216 GLN A CA  1 
ATOM   1766  C  C   . GLN A  1 216 ? 23.426  -15.850 19.835  1.00 11.89 ? 216 GLN A C   1 
ATOM   1767  O  O   . GLN A  1 216 ? 24.686  -15.899 19.991  1.00 12.95 ? 216 GLN A O   1 
ATOM   1768  C  CB  . GLN A  1 216 ? 22.528  -17.958 19.053  1.00 13.64 ? 216 GLN A CB  1 
ATOM   1769  C  CG  . GLN A  1 216 ? 21.646  -18.624 18.039  1.00 14.71 ? 216 GLN A CG  1 
ATOM   1770  C  CD  . GLN A  1 216 ? 21.212  -19.979 18.410  1.00 23.24 ? 216 GLN A CD  1 
ATOM   1771  O  OE1 . GLN A  1 216 ? 21.697  -20.597 19.431  1.00 25.48 ? 216 GLN A OE1 1 
ATOM   1772  N  NE2 . GLN A  1 216 ? 20.182  -20.435 17.666  1.00 23.67 ? 216 GLN A NE2 1 
ATOM   1773  N  N   . ILE A  1 217 ? 22.681  -15.175 20.708  1.00 11.03 ? 217 ILE A N   1 
ATOM   1774  C  CA  . ILE A  1 217 ? 23.132  -14.711 22.036  1.00 11.70 ? 217 ILE A CA  1 
ATOM   1775  C  C   . ILE A  1 217 ? 22.127  -15.217 23.084  1.00 11.25 ? 217 ILE A C   1 
ATOM   1776  O  O   . ILE A  1 217 ? 21.000  -15.557 22.689  1.00 11.08 ? 217 ILE A O   1 
ATOM   1777  C  CB  . ILE A  1 217 ? 23.260  -13.153 22.054  1.00 11.76 ? 217 ILE A CB  1 
ATOM   1778  C  CG1 . ILE A  1 217 ? 21.844  -12.394 21.906  1.00 11.97 ? 217 ILE A CG1 1 
ATOM   1779  C  CG2 . ILE A  1 217 ? 24.290  -12.738 20.978  1.00 12.60 ? 217 ILE A CG2 1 
ATOM   1780  C  CD1 . ILE A  1 217 ? 21.984  -10.940 22.115  1.00 12.08 ? 217 ILE A CD1 1 
ATOM   1781  N  N   . SER A  1 218 ? 22.580  -15.289 24.335  1.00 11.57 ? 218 SER A N   1 
ATOM   1782  C  CA  . SER A  1 218 ? 21.589  -15.840 25.267  1.00 11.91 ? 218 SER A CA  1 
ATOM   1783  C  C   . SER A  1 218 ? 20.493  -14.899 25.658  1.00 12.85 ? 218 SER A C   1 
ATOM   1784  O  O   . SER A  1 218 ? 20.547  -13.676 25.428  1.00 12.31 ? 218 SER A O   1 
ATOM   1785  C  CB  . SER A  1 218 ? 22.321  -16.251 26.539  1.00 12.92 ? 218 SER A CB  1 
ATOM   1786  O  OG  . SER A  1 218 ? 22.771  -15.107 27.256  1.00 13.15 ? 218 SER A OG  1 
ATOM   1787  N  N   . GLN A  1 219 ? 19.446  -15.480 26.277  1.00 12.96 ? 219 GLN A N   1 
ATOM   1788  C  CA  . GLN A  1 219 ? 18.386  -14.602 26.830  1.00 13.18 ? 219 GLN A CA  1 
ATOM   1789  C  C   . GLN A  1 219 ? 18.887  -13.550 27.796  1.00 12.28 ? 219 GLN A C   1 
ATOM   1790  O  O   . GLN A  1 219 ? 18.464  -12.434 27.671  1.00 11.13 ? 219 GLN A O   1 
ATOM   1791  C  CB  . GLN A  1 219 ? 17.272  -15.464 27.385  1.00 18.87 ? 219 GLN A CB  1 
ATOM   1792  C  CG  . GLN A  1 219 ? 17.597  -16.160 28.647  1.00 23.55 ? 219 GLN A CG  1 
ATOM   1793  C  CD  . GLN A  1 219 ? 16.288  -16.733 29.158  1.00 37.51 ? 219 GLN A CD  1 
ATOM   1794  O  OE1 . GLN A  1 219 ? 15.716  -17.624 28.492  1.00 38.88 ? 219 GLN A OE1 1 
ATOM   1795  N  NE2 . GLN A  1 219 ? 15.744  -16.167 30.292  1.00 31.84 ? 219 GLN A NE2 1 
ATOM   1796  N  N   . GLU A  1 220 ? 19.877  -13.840 28.616  1.00 12.17 ? 220 GLU A N   1 
ATOM   1797  C  CA  . GLU A  1 220 ? 20.413  -12.907 29.504  1.00 12.42 ? 220 GLU A CA  1 
ATOM   1798  C  C   . GLU A  1 220 ? 21.204  -11.813 28.709  1.00 12.31 ? 220 GLU A C   1 
ATOM   1799  O  O   . GLU A  1 220 ? 21.166  -10.655 29.108  1.00 12.53 ? 220 GLU A O   1 
ATOM   1800  C  CB  . GLU A  1 220 ? 21.311  -13.511 30.584  1.00 15.63 ? 220 GLU A CB  1 
ATOM   1801  C  CG  . GLU A  1 220 ? 20.527  -14.502 31.518  1.00 18.31 ? 220 GLU A CG  1 
ATOM   1802  C  CD  . GLU A  1 220 ? 20.254  -15.890 30.907  1.00 21.67 ? 220 GLU A CD  1 
ATOM   1803  O  OE1 . GLU A  1 220 ? 20.851  -16.234 29.887  1.00 18.46 ? 220 GLU A OE1 1 
ATOM   1804  O  OE2 . GLU A  1 220 ? 19.480  -16.654 31.530  1.00 28.84 ? 220 GLU A OE2 1 
ATOM   1805  N  N   . GLN A  1 221 ? 21.980  -12.232 27.680  1.00 11.49 ? 221 GLN A N   1 
ATOM   1806  C  CA  . GLN A  1 221 ? 22.731  -11.216 26.931  1.00 10.79 ? 221 GLN A CA  1 
ATOM   1807  C  C   . GLN A  1 221 ? 21.735  -10.264 26.198  1.00 11.28 ? 221 GLN A C   1 
ATOM   1808  O  O   . GLN A  1 221 ? 21.970  -9.046  26.219  1.00 10.12 ? 221 GLN A O   1 
ATOM   1809  C  CB  . GLN A  1 221 ? 23.569  -11.897 25.882  1.00 11.28 ? 221 GLN A CB  1 
ATOM   1810  C  CG  . GLN A  1 221 ? 24.782  -12.690 26.504  1.00 12.16 ? 221 GLN A CG  1 
ATOM   1811  C  CD  . GLN A  1 221 ? 25.598  -13.354 25.406  1.00 9.67  ? 221 GLN A CD  1 
ATOM   1812  O  OE1 . GLN A  1 221 ? 25.206  -14.249 24.758  1.00 12.64 ? 221 GLN A OE1 1 
ATOM   1813  N  NE2 . GLN A  1 221 ? 26.844  -12.871 25.317  1.00 12.16 ? 221 GLN A NE2 1 
ATOM   1814  N  N   . LEU A  1 222 ? 20.672  -10.832 25.640  1.00 10.07 ? 222 LEU A N   1 
ATOM   1815  C  CA  . LEU A  1 222 ? 19.714  -9.987  24.910  1.00 10.64 ? 222 LEU A CA  1 
ATOM   1816  C  C   . LEU A  1 222 ? 19.050  -9.044  25.895  1.00 10.81 ? 222 LEU A C   1 
ATOM   1817  O  O   . LEU A  1 222 ? 18.865  -7.854  25.624  1.00 10.60 ? 222 LEU A O   1 
ATOM   1818  C  CB  . LEU A  1 222 ? 18.708  -10.831 24.218  1.00 10.31 ? 222 LEU A CB  1 
ATOM   1819  C  CG  . LEU A  1 222 ? 17.554  -10.076 23.524  1.00 11.46 ? 222 LEU A CG  1 
ATOM   1820  C  CD1 . LEU A  1 222 ? 18.102  -9.116  22.398  1.00 11.85 ? 222 LEU A CD1 1 
ATOM   1821  C  CD2 . LEU A  1 222 ? 16.531  -11.028 22.934  1.00 13.63 ? 222 LEU A CD2 1 
ATOM   1822  N  N   . LEU A  1 223 ? 18.676  -9.554  27.117  1.00 10.91 ? 223 LEU A N   1 
ATOM   1823  C  CA  . LEU A  1 223 ? 18.065  -8.651  28.121  1.00 11.59 ? 223 LEU A CA  1 
ATOM   1824  C  C   . LEU A  1 223 ? 19.048  -7.593  28.543  1.00 11.64 ? 223 LEU A C   1 
ATOM   1825  O  O   . LEU A  1 223 ? 18.614  -6.462  28.745  1.00 11.48 ? 223 LEU A O   1 
ATOM   1826  C  CB  . LEU A  1 223 ? 17.649  -9.508  29.328  1.00 12.26 ? 223 LEU A CB  1 
ATOM   1827  C  CG  . LEU A  1 223 ? 16.993  -8.725  30.401  1.00 12.86 ? 223 LEU A CG  1 
ATOM   1828  C  CD1 . LEU A  1 223 ? 15.615  -8.212  29.989  1.00 14.55 ? 223 LEU A CD1 1 
ATOM   1829  C  CD2 . LEU A  1 223 ? 16.899  -9.715  31.587  1.00 15.60 ? 223 LEU A CD2 1 
ATOM   1830  N  N   . ALA A  1 224 ? 20.374  -7.895  28.675  1.00 11.54 ? 224 ALA A N   1 
ATOM   1831  C  CA  . ALA A  1 224 ? 21.283  -6.872  29.058  1.00 11.22 ? 224 ALA A CA  1 
ATOM   1832  C  C   . ALA A  1 224 ? 21.373  -5.768  28.031  1.00 13.06 ? 224 ALA A C   1 
ATOM   1833  O  O   . ALA A  1 224 ? 21.359  -4.582  28.363  1.00 12.49 ? 224 ALA A O   1 
ATOM   1834  C  CB  . ALA A  1 224 ? 22.662  -7.539  29.360  1.00 11.75 ? 224 ALA A CB  1 
ATOM   1835  N  N   . LEU A  1 225 ? 21.460  -6.166  26.744  1.00 10.76 ? 225 LEU A N   1 
ATOM   1836  C  CA  . LEU A  1 225 ? 21.510  -5.149  25.678  1.00 12.14 ? 225 LEU A CA  1 
ATOM   1837  C  C   . LEU A  1 225 ? 20.246  -4.247  25.698  1.00 11.88 ? 225 LEU A C   1 
ATOM   1838  O  O   . LEU A  1 225 ? 20.373  -3.004  25.515  1.00 13.65 ? 225 LEU A O   1 
ATOM   1839  C  CB  . LEU A  1 225 ? 21.614  -5.916  24.381  1.00 11.16 ? 225 LEU A CB  1 
ATOM   1840  C  CG  . LEU A  1 225 ? 21.657  -4.965  23.167  1.00 10.64 ? 225 LEU A CG  1 
ATOM   1841  C  CD1 . LEU A  1 225 ? 22.915  -4.122  23.154  1.00 13.87 ? 225 LEU A CD1 1 
ATOM   1842  C  CD2 . LEU A  1 225 ? 21.629  -5.798  21.938  1.00 12.69 ? 225 LEU A CD2 1 
ATOM   1843  N  N   . GLU A  1 226 ? 19.070  -4.884  25.958  1.00 10.83 ? 226 GLU A N   1 
ATOM   1844  C  CA  . GLU A  1 226 ? 17.847  -4.089  25.985  1.00 11.99 ? 226 GLU A CA  1 
ATOM   1845  C  C   . GLU A  1 226 ? 17.632  -3.230  27.218  1.00 13.15 ? 226 GLU A C   1 
ATOM   1846  O  O   . GLU A  1 226 ? 16.778  -2.330  27.179  1.00 14.51 ? 226 GLU A O   1 
ATOM   1847  C  CB  . GLU A  1 226 ? 16.641  -5.075  25.932  1.00 11.16 ? 226 GLU A CB  1 
ATOM   1848  C  CG  . GLU A  1 226 ? 16.509  -5.819  24.622  1.00 10.26 ? 226 GLU A CG  1 
ATOM   1849  C  CD  . GLU A  1 226 ? 15.588  -7.025  24.717  1.00 11.27 ? 226 GLU A CD  1 
ATOM   1850  O  OE1 . GLU A  1 226 ? 15.328  -7.526  25.836  1.00 13.24 ? 226 GLU A OE1 1 
ATOM   1851  O  OE2 . GLU A  1 226 ? 15.164  -7.519  23.649  1.00 12.78 ? 226 GLU A OE2 1 
ATOM   1852  N  N   . THR A  1 227 ? 18.369  -3.451  28.304  1.00 12.66 ? 227 THR A N   1 
ATOM   1853  C  CA  . THR A  1 227 ? 18.032  -2.812  29.581  1.00 12.79 ? 227 THR A CA  1 
ATOM   1854  C  C   . THR A  1 227 ? 19.215  -2.011  30.107  1.00 14.80 ? 227 THR A C   1 
ATOM   1855  O  O   . THR A  1 227 ? 19.020  -1.259  31.076  1.00 16.79 ? 227 THR A O   1 
ATOM   1856  C  CB  . THR A  1 227 ? 17.594  -3.819  30.666  1.00 12.82 ? 227 THR A CB  1 
ATOM   1857  O  OG1 . THR A  1 227 ? 18.601  -4.770  30.933  1.00 14.98 ? 227 THR A OG1 1 
ATOM   1858  C  CG2 . THR A  1 227 ? 16.304  -4.472  30.290  1.00 14.55 ? 227 THR A CG2 1 
ATOM   1859  N  N   . ALA A  1 228 ? 20.410  -2.171  29.552  1.00 13.63 ? 228 ALA A N   1 
ATOM   1860  C  CA  . ALA A  1 228 ? 21.613  -1.541  30.133  1.00 12.64 ? 228 ALA A CA  1 
ATOM   1861  C  C   . ALA A  1 228 ? 21.736  -0.074  29.849  1.00 14.94 ? 228 ALA A C   1 
ATOM   1862  O  O   . ALA A  1 228 ? 22.452  0.645   30.617  1.00 16.34 ? 228 ALA A O   1 
ATOM   1863  C  CB  . ALA A  1 228 ? 22.852  -2.329  29.668  1.00 14.97 ? 228 ALA A CB  1 
ATOM   1864  N  N   . LEU A  1 229 ? 21.093  0.450   28.769  1.00 12.35 ? 229 LEU A N   1 
ATOM   1865  C  CA  . LEU A  1 229 ? 21.433  1.759   28.270  1.00 13.96 ? 229 LEU A CA  1 
ATOM   1866  C  C   . LEU A  1 229 ? 20.306  2.745   28.312  1.00 12.81 ? 229 LEU A C   1 
ATOM   1867  O  O   . LEU A  1 229 ? 19.141  2.370   28.142  1.00 11.80 ? 229 LEU A O   1 
ATOM   1868  C  CB  . LEU A  1 229 ? 21.999  1.732   26.861  1.00 13.50 ? 229 LEU A CB  1 
ATOM   1869  C  CG  . LEU A  1 229 ? 23.066  0.625   26.646  1.00 15.75 ? 229 LEU A CG  1 
ATOM   1870  C  CD1 . LEU A  1 229 ? 23.508  0.671   25.166  1.00 18.06 ? 229 LEU A CD1 1 
ATOM   1871  C  CD2 . LEU A  1 229 ? 24.251  0.847   27.551  1.00 15.77 ? 229 LEU A CD2 1 
ATOM   1872  N  N   . TYR A  1 230 ? 20.661  3.991   28.478  1.00 12.23 ? 230 TYR A N   1 
ATOM   1873  C  CA  . TYR A  1 230 ? 19.756  5.127   28.347  1.00 13.65 ? 230 TYR A CA  1 
ATOM   1874  C  C   . TYR A  1 230 ? 20.212  6.068   27.221  1.00 13.71 ? 230 TYR A C   1 
ATOM   1875  O  O   . TYR A  1 230 ? 21.373  6.221   26.913  1.00 15.26 ? 230 TYR A O   1 
ATOM   1876  C  CB  . TYR A  1 230 ? 19.754  5.938   29.696  1.00 15.95 ? 230 TYR A CB  1 
ATOM   1877  C  CG  . TYR A  1 230 ? 19.055  5.265   30.823  1.00 21.63 ? 230 TYR A CG  1 
ATOM   1878  C  CD1 . TYR A  1 230 ? 19.661  4.215   31.544  1.00 27.66 ? 230 TYR A CD1 1 
ATOM   1879  C  CD2 . TYR A  1 230 ? 17.846  5.729   31.252  1.00 25.57 ? 230 TYR A CD2 1 
ATOM   1880  C  CE1 . TYR A  1 230 ? 19.005  3.621   32.656  1.00 36.98 ? 230 TYR A CE1 1 
ATOM   1881  C  CE2 . TYR A  1 230 ? 17.185  5.165   32.368  1.00 30.07 ? 230 TYR A CE2 1 
ATOM   1882  C  CZ  . TYR A  1 230 ? 17.747  4.117   33.050  1.00 34.79 ? 230 TYR A CZ  1 
ATOM   1883  O  OH  . TYR A  1 230 ? 17.066  3.614   34.158  1.00 31.84 ? 230 TYR A OH  1 
ATOM   1884  N  N   A CYS A  1 231 ? 19.238  6.786   26.662  0.50 13.58 ? 231 CYS A N   1 
ATOM   1885  N  N   B CYS A  1 231 ? 19.248  6.781   26.663  0.50 17.20 ? 231 CYS A N   1 
ATOM   1886  C  CA  A CYS A  1 231 ? 19.469  7.724   25.585  0.50 12.72 ? 231 CYS A CA  1 
ATOM   1887  C  CA  B CYS A  1 231 ? 19.545  7.694   25.600  0.50 18.39 ? 231 CYS A CA  1 
ATOM   1888  C  C   A CYS A  1 231 ? 19.959  9.039   26.140  0.50 12.68 ? 231 CYS A C   1 
ATOM   1889  C  C   B CYS A  1 231 ? 19.773  9.104   26.106  0.50 15.69 ? 231 CYS A C   1 
ATOM   1890  O  O   A CYS A  1 231 ? 20.678  9.778   25.478  0.50 13.40 ? 231 CYS A O   1 
ATOM   1891  O  O   B CYS A  1 231 ? 20.123  10.020  25.355  0.50 17.40 ? 231 CYS A O   1 
ATOM   1892  C  CB  A CYS A  1 231 ? 18.153  8.034   24.838  0.50 10.50 ? 231 CYS A CB  1 
ATOM   1893  C  CB  B CYS A  1 231 ? 18.434  7.658   24.546  0.50 22.81 ? 231 CYS A CB  1 
ATOM   1894  S  SG  A CYS A  1 231 ? 17.554  6.684   23.806  0.50 9.14  ? 231 CYS A SG  1 
ATOM   1895  S  SG  B CYS A  1 231 ? 16.715  7.778   25.018  0.50 31.96 ? 231 CYS A SG  1 
ATOM   1896  N  N   . THR A  1 232 ? 19.640  9.250   27.430  1.00 14.25 ? 232 THR A N   1 
ATOM   1897  C  CA  . THR A  1 232 ? 19.813  10.523  28.102  1.00 15.53 ? 232 THR A CA  1 
ATOM   1898  C  C   . THR A  1 232 ? 21.119  10.614  28.879  1.00 16.93 ? 232 THR A C   1 
ATOM   1899  O  O   . THR A  1 232 ? 21.726  9.594   29.199  1.00 16.38 ? 232 THR A O   1 
ATOM   1900  C  CB  . THR A  1 232 ? 18.629  10.785  28.997  1.00 17.63 ? 232 THR A CB  1 
ATOM   1901  O  OG1 . THR A  1 232 ? 18.290  9.560   29.645  1.00 17.48 ? 232 THR A OG1 1 
ATOM   1902  C  CG2 . THR A  1 232 ? 17.447  11.359  28.166  1.00 17.47 ? 232 THR A CG2 1 
ATOM   1903  N  N   . HIS A  1 233 ? 21.577  11.850  29.170  1.00 15.72 ? 233 HIS A N   1 
ATOM   1904  C  CA  . HIS A  1 233 ? 22.744  12.033  30.020  1.00 16.52 ? 233 HIS A CA  1 
ATOM   1905  C  C   . HIS A  1 233 ? 22.378  11.641  31.459  1.00 15.89 ? 233 HIS A C   1 
ATOM   1906  O  O   . HIS A  1 233 ? 21.196  11.610  31.857  1.00 16.84 ? 233 HIS A O   1 
ATOM   1907  C  CB  . HIS A  1 233 ? 23.152  13.504  30.021  1.00 17.48 ? 233 HIS A CB  1 
ATOM   1908  C  CG  . HIS A  1 233 ? 23.806  13.899  28.745  1.00 22.26 ? 233 HIS A CG  1 
ATOM   1909  N  ND1 . HIS A  1 233 ? 23.149  14.614  27.754  1.00 30.82 ? 233 HIS A ND1 1 
ATOM   1910  C  CD2 . HIS A  1 233 ? 25.065  13.683  28.290  1.00 24.01 ? 233 HIS A CD2 1 
ATOM   1911  C  CE1 . HIS A  1 233 ? 23.968  14.800  26.739  1.00 26.68 ? 233 HIS A CE1 1 
ATOM   1912  N  NE2 . HIS A  1 233 ? 25.129  14.246  27.027  1.00 24.92 ? 233 HIS A NE2 1 
ATOM   1913  N  N   . MET A  1 234 ? 23.412  11.223  32.189  1.00 17.65 ? 234 MET A N   1 
ATOM   1914  C  CA  . MET A  1 234 ? 23.206  10.825  33.575  1.00 19.01 ? 234 MET A CA  1 
ATOM   1915  C  C   . MET A  1 234 ? 22.362  11.785  34.422  1.00 19.12 ? 234 MET A C   1 
ATOM   1916  O  O   . MET A  1 234 ? 21.577  11.308  35.200  1.00 20.31 ? 234 MET A O   1 
ATOM   1917  C  CB  . MET A  1 234 ? 24.573  10.649  34.193  1.00 22.11 ? 234 MET A CB  1 
ATOM   1918  C  CG  . MET A  1 234 ? 24.480  9.952   35.549  1.00 22.11 ? 234 MET A CG  1 
ATOM   1919  S  SD  . MET A  1 234 ? 26.149  9.517   36.197  1.00 31.59 ? 234 MET A SD  1 
ATOM   1920  C  CE  . MET A  1 234 ? 26.176  10.844  37.364  1.00 38.84 ? 234 MET A CE  1 
ATOM   1921  N  N   . ASP A  1 235 ? 22.557  13.101  34.275  1.00 20.85 ? 235 ASP A N   1 
ATOM   1922  C  CA  . ASP A  1 235 ? 21.894  14.017  35.193  1.00 24.03 ? 235 ASP A CA  1 
ATOM   1923  C  C   . ASP A  1 235 ? 20.592  14.492  34.662  1.00 22.77 ? 235 ASP A C   1 
ATOM   1924  O  O   . ASP A  1 235 ? 19.955  15.420  35.184  1.00 23.91 ? 235 ASP A O   1 
ATOM   1925  C  CB  . ASP A  1 235 ? 22.819  15.224  35.465  1.00 30.30 ? 235 ASP A CB  1 
ATOM   1926  C  CG  . ASP A  1 235 ? 22.961  16.159  34.246  1.00 35.44 ? 235 ASP A CG  1 
ATOM   1927  O  OD1 . ASP A  1 235 ? 22.376  15.918  33.122  1.00 36.62 ? 235 ASP A OD1 1 
ATOM   1928  O  OD2 . ASP A  1 235 ? 23.669  17.187  34.434  1.00 40.29 ? 235 ASP A OD2 1 
ATOM   1929  N  N   . ASP A  1 236 ? 20.121  13.894  33.588  1.00 20.62 ? 236 ASP A N   1 
ATOM   1930  C  CA  . ASP A  1 236 ? 18.816  14.242  33.037  1.00 19.14 ? 236 ASP A CA  1 
ATOM   1931  C  C   . ASP A  1 236 ? 17.701  13.896  33.988  1.00 21.82 ? 236 ASP A C   1 
ATOM   1932  O  O   . ASP A  1 236 ? 17.520  12.720  34.349  1.00 20.81 ? 236 ASP A O   1 
ATOM   1933  C  CB  . ASP A  1 236 ? 18.544  13.517  31.712  1.00 19.89 ? 236 ASP A CB  1 
ATOM   1934  C  CG  . ASP A  1 236 ? 17.441  14.208  30.880  1.00 24.61 ? 236 ASP A CG  1 
ATOM   1935  O  OD1 . ASP A  1 236 ? 16.420  14.657  31.453  1.00 28.38 ? 236 ASP A OD1 1 
ATOM   1936  O  OD2 . ASP A  1 236 ? 17.598  14.318  29.626  1.00 22.27 ? 236 ASP A OD2 1 
ATOM   1937  N  N   . PRO A  1 237 ? 16.900  14.881  34.431  1.00 23.86 ? 237 PRO A N   1 
ATOM   1938  C  CA  . PRO A  1 237 ? 15.788  14.529  35.334  1.00 22.12 ? 237 PRO A CA  1 
ATOM   1939  C  C   . PRO A  1 237 ? 14.600  13.746  34.688  1.00 25.40 ? 237 PRO A C   1 
ATOM   1940  O  O   . PRO A  1 237 ? 13.701  13.260  35.383  1.00 24.26 ? 237 PRO A O   1 
ATOM   1941  C  CB  . PRO A  1 237 ? 15.362  15.926  35.903  1.00 26.12 ? 237 PRO A CB  1 
ATOM   1942  C  CG  . PRO A  1 237 ? 15.614  16.817  34.703  1.00 27.79 ? 237 PRO A CG  1 
ATOM   1943  C  CD  . PRO A  1 237 ? 16.910  16.330  34.100  1.00 24.76 ? 237 PRO A CD  1 
ATOM   1944  N  N   . SER A  1 238 ? 14.639  13.549  33.372  1.00 25.06 ? 238 SER A N   1 
ATOM   1945  C  CA  . SER A  1 238 ? 13.643  12.761  32.649  1.00 27.57 ? 238 SER A CA  1 
ATOM   1946  C  C   . SER A  1 238 ? 14.338  11.663  31.820  1.00 23.69 ? 238 SER A C   1 
ATOM   1947  O  O   . SER A  1 238 ? 14.441  11.802  30.616  1.00 22.05 ? 238 SER A O   1 
ATOM   1948  C  CB  . SER A  1 238 ? 12.925  13.705  31.721  1.00 31.04 ? 238 SER A CB  1 
ATOM   1949  O  OG  . SER A  1 238 ? 11.971  14.422  32.489  1.00 38.59 ? 238 SER A OG  1 
ATOM   1950  N  N   . PRO A  1 239 ? 14.818  10.615  32.484  1.00 23.85 ? 239 PRO A N   1 
ATOM   1951  C  CA  . PRO A  1 239 ? 15.644  9.666   31.724  1.00 20.94 ? 239 PRO A CA  1 
ATOM   1952  C  C   . PRO A  1 239 ? 14.769  8.929   30.675  1.00 23.53 ? 239 PRO A C   1 
ATOM   1953  O  O   . PRO A  1 239 ? 13.561  8.708   30.883  1.00 25.15 ? 239 PRO A O   1 
ATOM   1954  C  CB  . PRO A  1 239 ? 16.110  8.709   32.796  1.00 20.80 ? 239 PRO A CB  1 
ATOM   1955  C  CG  . PRO A  1 239 ? 15.100  8.801   33.928  1.00 25.71 ? 239 PRO A CG  1 
ATOM   1956  C  CD  . PRO A  1 239 ? 14.789  10.266  33.913  1.00 21.12 ? 239 PRO A CD  1 
ATOM   1957  N  N   . ARG A  1 240 ? 15.408  8.477   29.593  1.00 20.80 ? 240 ARG A N   1 
ATOM   1958  C  CA  . ARG A  1 240 ? 14.697  7.756   28.582  1.00 19.06 ? 240 ARG A CA  1 
ATOM   1959  C  C   . ARG A  1 240 ? 15.541  6.470   28.289  1.00 16.99 ? 240 ARG A C   1 
ATOM   1960  O  O   . ARG A  1 240 ? 16.724  6.559   27.991  1.00 16.75 ? 240 ARG A O   1 
ATOM   1961  C  CB  . ARG A  1 240 ? 14.575  8.568   27.273  1.00 22.52 ? 240 ARG A CB  1 
ATOM   1962  C  CG  . ARG A  1 240 ? 13.625  9.797   27.256  1.00 26.55 ? 240 ARG A CG  1 
ATOM   1963  C  CD  . ARG A  1 240 ? 13.644  10.538  25.908  1.00 25.12 ? 240 ARG A CD  1 
ATOM   1964  N  NE  . ARG A  1 240 ? 14.836  11.383  25.647  1.00 29.55 ? 240 ARG A NE  1 
ATOM   1965  C  CZ  . ARG A  1 240 ? 15.766  11.204  24.690  1.00 25.99 ? 240 ARG A CZ  1 
ATOM   1966  N  NH1 . ARG A  1 240 ? 15.727  10.171  23.853  1.00 26.96 ? 240 ARG A NH1 1 
ATOM   1967  N  NH2 . ARG A  1 240 ? 16.769  12.074  24.580  1.00 28.87 ? 240 ARG A NH2 1 
ATOM   1968  N  N   . GLU A  1 241 ? 14.943  5.310   28.475  1.00 17.39 ? 241 GLU A N   1 
ATOM   1969  C  CA  . GLU A  1 241 ? 15.616  4.048   28.189  1.00 18.27 ? 241 GLU A CA  1 
ATOM   1970  C  C   . GLU A  1 241 ? 15.940  3.944   26.695  1.00 14.70 ? 241 GLU A C   1 
ATOM   1971  O  O   . GLU A  1 241 ? 15.129  4.365   25.852  1.00 17.07 ? 241 GLU A O   1 
ATOM   1972  C  CB  . GLU A  1 241 ? 14.718  2.903   28.554  1.00 20.80 ? 241 GLU A CB  1 
ATOM   1973  C  CG  . GLU A  1 241 ? 14.554  2.619   30.043  1.00 24.50 ? 241 GLU A CG  1 
ATOM   1974  C  CD  . GLU A  1 241 ? 13.462  1.526   30.313  1.00 31.75 ? 241 GLU A CD  1 
ATOM   1975  O  OE1 . GLU A  1 241 ? 12.844  0.945   29.355  1.00 38.35 ? 241 GLU A OE1 1 
ATOM   1976  O  OE2 . GLU A  1 241 ? 13.204  1.223   31.498  1.00 37.04 ? 241 GLU A OE2 1 
ATOM   1977  N  N   . MET A  1 242 ? 17.132  3.398   26.371  1.00 12.36 ? 242 MET A N   1 
ATOM   1978  C  CA  . MET A  1 242 ? 17.466  3.172   24.974  1.00 10.89 ? 242 MET A CA  1 
ATOM   1979  C  C   . MET A  1 242 ? 16.944  1.801   24.573  1.00 10.70 ? 242 MET A C   1 
ATOM   1980  O  O   . MET A  1 242 ? 17.564  0.773   24.790  1.00 11.04 ? 242 MET A O   1 
ATOM   1981  C  CB  . MET A  1 242 ? 18.976  3.250   24.783  1.00 10.49 ? 242 MET A CB  1 
ATOM   1982  C  CG  . MET A  1 242 ? 19.404  3.059   23.309  1.00 11.69 ? 242 MET A CG  1 
ATOM   1983  S  SD  . MET A  1 242 ? 21.177  3.115   23.051  1.00 12.76 ? 242 MET A SD  1 
ATOM   1984  C  CE  . MET A  1 242 ? 21.512  4.794   23.585  1.00 13.53 ? 242 MET A CE  1 
ATOM   1985  N  N   . ILE A  1 243 ? 15.740  1.841   23.979  1.00 10.36 ? 243 ILE A N   1 
ATOM   1986  C  CA  . ILE A  1 243 ? 15.032  0.640   23.505  1.00 10.59 ? 243 ILE A CA  1 
ATOM   1987  C  C   . ILE A  1 243 ? 14.389  0.973   22.156  1.00 10.66 ? 243 ILE A C   1 
ATOM   1988  O  O   . ILE A  1 243 ? 14.196  2.131   21.776  1.00 10.67 ? 243 ILE A O   1 
ATOM   1989  C  CB  . ILE A  1 243 ? 13.886  0.254   24.477  1.00 12.54 ? 243 ILE A CB  1 
ATOM   1990  C  CG1 . ILE A  1 243 ? 12.959  1.461   24.836  1.00 13.16 ? 243 ILE A CG1 1 
ATOM   1991  C  CG2 . ILE A  1 243 ? 14.475  -0.472  25.735  1.00 14.72 ? 243 ILE A CG2 1 
ATOM   1992  C  CD1 . ILE A  1 243 ? 11.713  1.036   25.620  1.00 15.12 ? 243 ILE A CD1 1 
ATOM   1993  N  N   . ASN A  1 244 ? 14.083  -0.067  21.397  1.00 8.88  ? 244 ASN A N   1 
ATOM   1994  C  CA  . ASN A  1 244 ? 13.342  0.105   20.153  1.00 9.84  ? 244 ASN A CA  1 
ATOM   1995  C  C   . ASN A  1 244 ? 14.079  1.041   19.180  1.00 10.05 ? 244 ASN A C   1 
ATOM   1996  O  O   . ASN A  1 244 ? 13.440  1.899   18.521  1.00 9.94  ? 244 ASN A O   1 
ATOM   1997  C  CB  . ASN A  1 244 ? 11.890  0.545   20.392  1.00 10.79 ? 244 ASN A CB  1 
ATOM   1998  C  CG  . ASN A  1 244 ? 11.184  -0.384  21.312  1.00 11.36 ? 244 ASN A CG  1 
ATOM   1999  O  OD1 . ASN A  1 244 ? 11.360  -1.560  21.255  1.00 13.18 ? 244 ASN A OD1 1 
ATOM   2000  N  ND2 . ASN A  1 244 ? 10.416  0.240   22.254  1.00 13.91 ? 244 ASN A ND2 1 
ATOM   2001  N  N   . ASN A  1 245 ? 15.412  0.915   19.143  1.00 9.27  ? 245 ASN A N   1 
ATOM   2002  C  CA  . ASN A  1 245 ? 16.256  1.871   18.381  1.00 9.00  ? 245 ASN A CA  1 
ATOM   2003  C  C   . ASN A  1 245 ? 16.450  1.281   16.991  1.00 7.96  ? 245 ASN A C   1 
ATOM   2004  O  O   . ASN A  1 245 ? 17.582  1.198   16.526  1.00 8.63  ? 245 ASN A O   1 
ATOM   2005  C  CB  . ASN A  1 245 ? 17.554  2.231   19.091  1.00 9.36  ? 245 ASN A CB  1 
ATOM   2006  C  CG  . ASN A  1 245 ? 18.432  1.032   19.367  1.00 9.69  ? 245 ASN A CG  1 
ATOM   2007  O  OD1 . ASN A  1 245 ? 18.019  -0.087  19.367  1.00 9.78  ? 245 ASN A OD1 1 
ATOM   2008  N  ND2 . ASN A  1 245 ? 19.715  1.309   19.680  1.00 11.09 ? 245 ASN A ND2 1 
ATOM   2009  N  N   . PHE A  1 246 ? 15.401  0.899   16.270  1.00 7.89  ? 246 PHE A N   1 
ATOM   2010  C  CA  . PHE A  1 246 ? 15.435  0.385   14.900  1.00 7.84  ? 246 PHE A CA  1 
ATOM   2011  C  C   . PHE A  1 246 ? 14.442  1.196   14.124  1.00 7.85  ? 246 PHE A C   1 
ATOM   2012  O  O   . PHE A  1 246 ? 13.445  1.648   14.659  1.00 8.97  ? 246 PHE A O   1 
ATOM   2013  C  CB  . PHE A  1 246 ? 15.092  -1.125  14.866  1.00 9.42  ? 246 PHE A CB  1 
ATOM   2014  C  CG  . PHE A  1 246 ? 13.683  -1.446  15.423  1.00 8.05  ? 246 PHE A CG  1 
ATOM   2015  C  CD1 . PHE A  1 246 ? 13.456  -1.656  16.749  1.00 8.40  ? 246 PHE A CD1 1 
ATOM   2016  C  CD2 . PHE A  1 246 ? 12.612  -1.571  14.529  1.00 8.91  ? 246 PHE A CD2 1 
ATOM   2017  C  CE1 . PHE A  1 246 ? 12.209  -1.950  17.229  1.00 9.60  ? 246 PHE A CE1 1 
ATOM   2018  C  CE2 . PHE A  1 246 ? 11.325  -1.861  15.007  1.00 9.92  ? 246 PHE A CE2 1 
ATOM   2019  C  CZ  . PHE A  1 246 ? 11.096  -2.066  16.382  1.00 9.85  ? 246 PHE A CZ  1 
ATOM   2020  N  N   . ARG A  1 247 ? 14.761  1.324   12.859  1.00 7.73  ? 247 ARG A N   1 
ATOM   2021  C  CA  . ARG A  1 247 ? 13.824  2.036   11.956  1.00 7.84  ? 247 ARG A CA  1 
ATOM   2022  C  C   . ARG A  1 247 ? 12.851  1.029   11.303  1.00 7.53  ? 247 ARG A C   1 
ATOM   2023  O  O   . ARG A  1 247 ? 13.237  -0.121  11.069  1.00 8.49  ? 247 ARG A O   1 
ATOM   2024  C  CB  . ARG A  1 247 ? 14.626  2.739   10.816  1.00 8.18  ? 247 ARG A CB  1 
ATOM   2025  C  CG  . ARG A  1 247 ? 13.826  3.707   9.922   1.00 7.78  ? 247 ARG A CG  1 
ATOM   2026  C  CD  . ARG A  1 247 ? 14.690  4.138   8.757   1.00 8.10  ? 247 ARG A CD  1 
ATOM   2027  N  NE  . ARG A  1 247 ? 14.096  5.320   8.169   1.00 7.08  ? 247 ARG A NE  1 
ATOM   2028  C  CZ  . ARG A  1 247 ? 14.537  5.924   7.069   1.00 8.06  ? 247 ARG A CZ  1 
ATOM   2029  N  NH1 . ARG A  1 247 ? 15.546  5.385   6.398   1.00 8.14  ? 247 ARG A NH1 1 
ATOM   2030  N  NH2 . ARG A  1 247 ? 13.955  7.024   6.632   1.00 7.95  ? 247 ARG A NH2 1 
ATOM   2031  N  N   . GLN A  1 248 ? 11.577  1.439   11.189  1.00 7.50  ? 248 GLN A N   1 
ATOM   2032  C  CA  . GLN A  1 248 ? 10.641  0.579   10.403  1.00 6.89  ? 248 GLN A CA  1 
ATOM   2033  C  C   . GLN A  1 248 ? 11.103  0.295   9.006   1.00 7.86  ? 248 GLN A C   1 
ATOM   2034  O  O   . GLN A  1 248 ? 11.827  1.101   8.387   1.00 8.32  ? 248 GLN A O   1 
ATOM   2035  C  CB  . GLN A  1 248 ? 9.227   1.259   10.307  1.00 7.60  ? 248 GLN A CB  1 
ATOM   2036  C  CG  . GLN A  1 248 ? 8.609   1.552   11.673  1.00 7.54  ? 248 GLN A CG  1 
ATOM   2037  C  CD  . GLN A  1 248 ? 8.240   0.316   12.418  1.00 9.11  ? 248 GLN A CD  1 
ATOM   2038  O  OE1 . GLN A  1 248 ? 8.983   -0.128  13.317  1.00 10.21 ? 248 GLN A OE1 1 
ATOM   2039  N  NE2 . GLN A  1 248 ? 7.091   -0.292  12.092  1.00 9.79  ? 248 GLN A NE2 1 
ATOM   2040  N  N   . VAL A  1 249 ? 10.741  -0.838  8.434   1.00 8.53  ? 249 VAL A N   1 
ATOM   2041  C  CA  . VAL A  1 249 ? 11.114  -1.172  7.055   1.00 9.53  ? 249 VAL A CA  1 
ATOM   2042  C  C   . VAL A  1 249 ? 10.468  -0.135  6.075   1.00 9.15  ? 249 VAL A C   1 
ATOM   2043  O  O   . VAL A  1 249 ? 9.333   0.380   6.328   1.00 8.69  ? 249 VAL A O   1 
ATOM   2044  C  CB  . VAL A  1 249 ? 10.744  -2.596  6.668   1.00 10.92 ? 249 VAL A CB  1 
ATOM   2045  C  CG1 . VAL A  1 249 ? 11.629  -3.594  7.386   1.00 10.77 ? 249 VAL A CG1 1 
ATOM   2046  C  CG2 . VAL A  1 249 ? 9.280   -2.874  6.818   1.00 13.70 ? 249 VAL A CG2 1 
ATOM   2047  N  N   . GLN A  1 250 ? 11.175  0.098   5.035   1.00 8.16  ? 250 GLN A N   1 
ATOM   2048  C  CA  . GLN A  1 250 ? 10.760  1.061   4.007   1.00 8.59  ? 250 GLN A CA  1 
ATOM   2049  C  C   . GLN A  1 250 ? 10.169  0.354   2.803   1.00 10.03 ? 250 GLN A C   1 
ATOM   2050  O  O   . GLN A  1 250 ? 10.522  -0.801  2.526   1.00 11.86 ? 250 GLN A O   1 
ATOM   2051  C  CB  . GLN A  1 250 ? 12.066  1.773   3.513   1.00 8.75  ? 250 GLN A CB  1 
ATOM   2052  C  CG  . GLN A  1 250 ? 12.898  2.404   4.681   1.00 9.25  ? 250 GLN A CG  1 
ATOM   2053  C  CD  . GLN A  1 250 ? 12.156  3.514   5.378   1.00 8.73  ? 250 GLN A CD  1 
ATOM   2054  O  OE1 . GLN A  1 250 ? 11.869  4.574   4.745   1.00 9.70  ? 250 GLN A OE1 1 
ATOM   2055  N  NE2 . GLN A  1 250 ? 11.787  3.370   6.603   1.00 8.21  ? 250 GLN A NE2 1 
ATOM   2056  N  N   . LYS A  1 251 ? 9.356   1.113   2.041   1.00 9.96  ? 251 LYS A N   1 
ATOM   2057  C  CA  . LYS A  1 251 ? 8.907   0.485   0.782   1.00 11.54 ? 251 LYS A CA  1 
ATOM   2058  C  C   . LYS A  1 251 ? 10.098  0.206   -0.098  1.00 11.66 ? 251 LYS A C   1 
ATOM   2059  O  O   . LYS A  1 251 ? 11.065  1.054   -0.106  1.00 12.25 ? 251 LYS A O   1 
ATOM   2060  C  CB  . LYS A  1 251 ? 7.946   1.411   0.097   1.00 10.94 ? 251 LYS A CB  1 
ATOM   2061  C  CG  . LYS A  1 251 ? 6.563   1.346   0.814   1.00 12.90 ? 251 LYS A CG  1 
ATOM   2062  C  CD  . LYS A  1 251 ? 5.603   2.222   0.098   1.00 12.77 ? 251 LYS A CD  1 
ATOM   2063  C  CE  . LYS A  1 251 ? 4.154   2.138   0.596   1.00 10.40 ? 251 LYS A CE  1 
ATOM   2064  N  NZ  . LYS A  1 251 ? 3.940   2.120   2.091   1.00 9.50  ? 251 LYS A NZ  1 
ATOM   2065  N  N   . PHE A  1 252 ? 10.018  -0.861  -0.911  1.00 12.15 ? 252 PHE A N   1 
ATOM   2066  C  CA  . PHE A  1 252 ? 11.145  -1.209  -1.799  1.00 14.39 ? 252 PHE A CA  1 
ATOM   2067  C  C   . PHE A  1 252 ? 10.480  -1.903  -3.016  1.00 21.88 ? 252 PHE A C   1 
ATOM   2068  O  O   . PHE A  1 252 ? 10.146  -3.079  -2.919  1.00 26.57 ? 252 PHE A O   1 
ATOM   2069  C  CB  . PHE A  1 252 ? 11.954  -2.279  -1.086  1.00 16.24 ? 252 PHE A CB  1 
ATOM   2070  C  CG  . PHE A  1 252 ? 13.224  -2.720  -1.813  1.00 18.23 ? 252 PHE A CG  1 
ATOM   2071  C  CD1 . PHE A  1 252 ? 14.352  -1.976  -1.735  1.00 16.43 ? 252 PHE A CD1 1 
ATOM   2072  C  CD2 . PHE A  1 252 ? 13.227  -3.963  -2.509  1.00 18.14 ? 252 PHE A CD2 1 
ATOM   2073  C  CE1 . PHE A  1 252 ? 15.555  -2.446  -2.389  1.00 18.36 ? 252 PHE A CE1 1 
ATOM   2074  C  CE2 . PHE A  1 252 ? 14.427  -4.440  -3.116  1.00 20.55 ? 252 PHE A CE2 1 
ATOM   2075  C  CZ  . PHE A  1 252 ? 15.564  -3.633  -3.057  1.00 20.73 ? 252 PHE A CZ  1 
ATOM   2076  N  N   . ASP A  1 253 ? 10.290  -1.172  -4.094  1.00 28.16 ? 253 ASP A N   1 
ATOM   2077  C  CA  . ASP A  1 253 ? 9.359   -1.599  -5.235  1.00 26.06 ? 253 ASP A CA  1 
ATOM   2078  C  C   . ASP A  1 253 ? 10.142  -1.451  -6.500  1.00 26.42 ? 253 ASP A C   1 
ATOM   2079  O  O   . ASP A  1 253 ? 10.878  -0.509  -6.653  1.00 24.52 ? 253 ASP A O   1 
ATOM   2080  C  CB  . ASP A  1 253 ? 8.092   -0.739  -5.358  1.00 30.46 ? 253 ASP A CB  1 
ATOM   2081  C  CG  . ASP A  1 253 ? 7.007   -1.390  -6.303  1.00 40.60 ? 253 ASP A CG  1 
ATOM   2082  O  OD1 . ASP A  1 253 ? 6.723   -2.648  -6.218  1.00 34.09 ? 253 ASP A OD1 1 
ATOM   2083  O  OD2 . ASP A  1 253 ? 6.426   -0.613  -7.128  1.00 38.68 ? 253 ASP A OD2 1 
ATOM   2084  N  N   . GLU A  1 254 ? 9.951   -2.435  -7.390  1.00 27.22 ? 254 GLU A N   1 
ATOM   2085  C  CA  . GLU A  1 254 ? 10.579  -2.503  -8.718  1.00 31.39 ? 254 GLU A CA  1 
ATOM   2086  C  C   . GLU A  1 254 ? 12.098  -2.634  -8.613  1.00 28.73 ? 254 GLU A C   1 
ATOM   2087  O  O   . GLU A  1 254 ? 12.818  -2.152  -9.456  1.00 30.63 ? 254 GLU A O   1 
ATOM   2088  C  CB  . GLU A  1 254 ? 10.168  -1.287  -9.575  1.00 35.37 ? 254 GLU A CB  1 
ATOM   2089  C  CG  . GLU A  1 254 ? 8.661   -1.284  -9.814  1.00 39.04 ? 254 GLU A CG  1 
ATOM   2090  C  CD  . GLU A  1 254 ? 8.161   -0.069  -10.593 1.00 49.79 ? 254 GLU A CD  1 
ATOM   2091  O  OE1 . GLU A  1 254 ? 8.899   0.926   -10.735 1.00 50.59 ? 254 GLU A OE1 1 
ATOM   2092  O  OE2 . GLU A  1 254 ? 6.997   -0.106  -11.056 1.00 55.09 ? 254 GLU A OE2 1 
ATOM   2093  N  N   . ARG A  1 255 ? 12.517  -3.282  -7.527  1.00 27.41 ? 255 ARG A N   1 
ATOM   2094  C  CA  . ARG A  1 255 ? 13.926  -3.518  -7.205  1.00 24.76 ? 255 ARG A CA  1 
ATOM   2095  C  C   . ARG A  1 255 ? 14.170  -4.901  -6.695  1.00 25.81 ? 255 ARG A C   1 
ATOM   2096  O  O   . ARG A  1 255 ? 13.258  -5.618  -6.204  1.00 26.64 ? 255 ARG A O   1 
ATOM   2097  C  CB  . ARG A  1 255 ? 14.361  -2.485  -6.154  1.00 21.59 ? 255 ARG A CB  1 
ATOM   2098  C  CG  . ARG A  1 255 ? 14.306  -1.012  -6.579  1.00 22.75 ? 255 ARG A CG  1 
ATOM   2099  C  CD  . ARG A  1 255 ? 14.832  -0.081  -5.471  1.00 24.86 ? 255 ARG A CD  1 
ATOM   2100  N  NE  . ARG A  1 255 ? 16.247  -0.365  -5.306  1.00 25.25 ? 255 ARG A NE  1 
ATOM   2101  C  CZ  . ARG A  1 255 ? 16.956  -0.098  -4.220  1.00 25.44 ? 255 ARG A CZ  1 
ATOM   2102  N  NH1 . ARG A  1 255 ? 16.393  0.487   -3.171  1.00 24.42 ? 255 ARG A NH1 1 
ATOM   2103  N  NH2 . ARG A  1 255 ? 18.240  -0.418  -4.195  1.00 18.34 ? 255 ARG A NH2 1 
ATOM   2104  N  N   . LEU A  1 256 ? 15.413  -5.322  -6.835  1.00 22.71 ? 256 LEU A N   1 
ATOM   2105  C  CA  . LEU A  1 256 ? 15.818  -6.610  -6.421  1.00 22.01 ? 256 LEU A CA  1 
ATOM   2106  C  C   . LEU A  1 256 ? 16.856  -6.446  -5.276  1.00 18.70 ? 256 LEU A C   1 
ATOM   2107  O  O   . LEU A  1 256 ? 17.660  -5.445  -5.165  1.00 20.93 ? 256 LEU A O   1 
ATOM   2108  C  CB  . LEU A  1 256 ? 16.408  -7.367  -7.618  1.00 28.02 ? 256 LEU A CB  1 
ATOM   2109  C  CG  . LEU A  1 256 ? 15.481  -7.701  -8.818  1.00 29.26 ? 256 LEU A CG  1 
ATOM   2110  C  CD1 . LEU A  1 256 ? 16.349  -8.249  -9.946  1.00 30.25 ? 256 LEU A CD1 1 
ATOM   2111  C  CD2 . LEU A  1 256 ? 14.384  -8.714  -8.406  1.00 33.62 ? 256 LEU A CD2 1 
ATOM   2112  N  N   . VAL A  1 257 ? 16.819  -7.502  -4.486  1.00 21.17 ? 257 VAL A N   1 
ATOM   2113  C  CA  . VAL A  1 257 ? 17.914  -7.812  -3.608  1.00 16.45 ? 257 VAL A CA  1 
ATOM   2114  C  C   . VAL A  1 257 ? 18.642  -8.998  -4.128  1.00 15.76 ? 257 VAL A C   1 
ATOM   2115  O  O   . VAL A  1 257 ? 18.051  -10.095 -4.413  1.00 19.29 ? 257 VAL A O   1 
ATOM   2116  C  CB  . VAL A  1 257 ? 17.404  -8.167  -2.199  1.00 15.99 ? 257 VAL A CB  1 
ATOM   2117  C  CG1 . VAL A  1 257 ? 18.486  -8.689  -1.220  1.00 16.79 ? 257 VAL A CG1 1 
ATOM   2118  C  CG2 . VAL A  1 257 ? 16.690  -6.993  -1.645  1.00 19.20 ? 257 VAL A CG2 1 
ATOM   2119  N  N   . TYR A  1 258 ? 19.895  -8.878  -4.317  1.00 14.07 ? 258 TYR A N   1 
ATOM   2120  C  CA  . TYR A  1 258 ? 20.685  -9.912  -4.938  1.00 15.39 ? 258 TYR A CA  1 
ATOM   2121  C  C   . TYR A  1 258 ? 21.138  -10.828 -3.865  1.00 15.29 ? 258 TYR A C   1 
ATOM   2122  O  O   . TYR A  1 258 ? 21.476  -10.389 -2.717  1.00 16.02 ? 258 TYR A O   1 
ATOM   2123  C  CB  . TYR A  1 258 ? 21.847  -9.323  -5.729  1.00 16.21 ? 258 TYR A CB  1 
ATOM   2124  C  CG  . TYR A  1 258 ? 21.293  -8.384  -6.797  1.00 19.88 ? 258 TYR A CG  1 
ATOM   2125  C  CD1 . TYR A  1 258 ? 20.813  -8.896  -7.996  1.00 21.01 ? 258 TYR A CD1 1 
ATOM   2126  C  CD2 . TYR A  1 258 ? 21.182  -7.041  -6.572  1.00 19.58 ? 258 TYR A CD2 1 
ATOM   2127  C  CE1 . TYR A  1 258 ? 20.240  -8.027  -8.990  1.00 25.43 ? 258 TYR A CE1 1 
ATOM   2128  C  CE2 . TYR A  1 258 ? 20.562  -6.185  -7.478  1.00 23.72 ? 258 TYR A CE2 1 
ATOM   2129  C  CZ  . TYR A  1 258 ? 20.114  -6.692  -8.683  1.00 22.77 ? 258 TYR A CZ  1 
ATOM   2130  O  OH  . TYR A  1 258 ? 19.535  -5.765  -9.573  1.00 27.68 ? 258 TYR A OH  1 
ATOM   2131  N  N   . THR A  1 259 ? 21.179  -12.124 -4.149  1.00 14.29 ? 259 THR A N   1 
ATOM   2132  C  CA  . THR A  1 259 ? 21.676  -13.092 -3.129  1.00 14.29 ? 259 THR A CA  1 
ATOM   2133  C  C   . THR A  1 259 ? 22.895  -13.846 -3.637  1.00 14.26 ? 259 THR A C   1 
ATOM   2134  O  O   . THR A  1 259 ? 23.011  -14.159 -4.871  1.00 14.95 ? 259 THR A O   1 
ATOM   2135  C  CB  . THR A  1 259 ? 20.583  -14.094 -2.704  1.00 13.75 ? 259 THR A CB  1 
ATOM   2136  O  OG1 . THR A  1 259 ? 20.169  -14.785 -3.928  1.00 16.85 ? 259 THR A OG1 1 
ATOM   2137  C  CG2 . THR A  1 259 ? 19.444  -13.366 -2.115  1.00 13.97 ? 259 THR A CG2 1 
ATOM   2138  N  N   . SER A  1 260 ? 23.819  -14.189 -2.774  1.00 14.25 ? 260 SER A N   1 
ATOM   2139  C  CA  . SER A  1 260 ? 24.957  -15.010 -3.181  1.00 15.53 ? 260 SER A CA  1 
ATOM   2140  C  C   . SER A  1 260 ? 24.618  -16.494 -3.132  1.00 15.07 ? 260 SER A C   1 
ATOM   2141  O  O   . SER A  1 260 ? 25.514  -17.297 -3.424  1.00 19.99 ? 260 SER A O   1 
ATOM   2142  C  CB  . SER A  1 260 ? 26.150  -14.726 -2.307  1.00 15.15 ? 260 SER A CB  1 
ATOM   2143  O  OG  . SER A  1 260 ? 25.818  -15.130 -0.968  1.00 14.37 ? 260 SER A OG  1 
ATOM   2144  N  N   . PHE A  1 261 ? 23.384  -16.826 -2.803  1.00 15.86 ? 261 PHE A N   1 
ATOM   2145  C  CA  . PHE A  1 261 ? 22.984  -18.220 -2.654  1.00 16.73 ? 261 PHE A CA  1 
ATOM   2146  C  C   . PHE A  1 261 ? 21.739  -18.357 -3.458  1.00 19.08 ? 261 PHE A C   1 
ATOM   2147  O  O   . PHE A  1 261 ? 20.960  -17.419 -3.687  1.00 20.82 ? 261 PHE A O   1 
ATOM   2148  C  CB  . PHE A  1 261 ? 22.786  -18.515 -1.157  1.00 15.75 ? 261 PHE A CB  1 
ATOM   2149  C  CG  . PHE A  1 261 ? 21.807  -17.588 -0.492  1.00 15.39 ? 261 PHE A CG  1 
ATOM   2150  C  CD1 . PHE A  1 261 ? 20.445  -17.851 -0.409  1.00 14.72 ? 261 PHE A CD1 1 
ATOM   2151  C  CD2 . PHE A  1 261 ? 22.273  -16.384 0.074   1.00 13.76 ? 261 PHE A CD2 1 
ATOM   2152  C  CE1 . PHE A  1 261 ? 19.539  -16.992 0.181   1.00 15.42 ? 261 PHE A CE1 1 
ATOM   2153  C  CE2 . PHE A  1 261 ? 21.367  -15.529 0.678   1.00 15.04 ? 261 PHE A CE2 1 
ATOM   2154  C  CZ  . PHE A  1 261 ? 20.027  -15.818 0.738   1.00 16.50 ? 261 PHE A CZ  1 
ATOM   2155  N  N   . SER A  1 262 ? 21.504  -19.589 -3.920  1.00 26.44 ? 262 SER A N   1 
ATOM   2156  C  CA  . SER A  1 262 ? 20.239  -19.822 -4.598  1.00 31.29 ? 262 SER A CA  1 
ATOM   2157  C  C   . SER A  1 262 ? 19.403  -20.776 -3.736  1.00 41.58 ? 262 SER A C   1 
ATOM   2158  O  O   . SER A  1 262 ? 18.252  -20.499 -3.450  1.00 46.34 ? 262 SER A O   1 
ATOM   2159  C  CB  . SER A  1 262 ? 20.483  -20.396 -5.988  1.00 35.26 ? 262 SER A CB  1 
ATOM   2160  O  OG  . SER A  1 262 ? 21.449  -21.426 -5.900  1.00 38.88 ? 262 SER A OG  1 
ATOM   2161  N  N   . GLN A  1 263 ? 20.027  -21.881 -3.309  1.00 47.80 ? 263 GLN A N   1 
ATOM   2162  C  CA  . GLN A  1 263 ? 19.332  -23.018 -2.668  1.00 54.43 ? 263 GLN A CA  1 
ATOM   2163  C  C   . GLN A  1 263 ? 18.440  -22.604 -1.467  1.00 59.36 ? 263 GLN A C   1 
ATOM   2164  O  O   . GLN A  1 263 ? 18.857  -21.811 -0.613  1.00 55.90 ? 263 GLN A O   1 
ATOM   2165  C  CB  . GLN A  1 263 ? 20.327  -24.122 -2.233  1.00 51.63 ? 263 GLN A CB  1 
ATOM   2166  C  CG  . GLN A  1 263 ? 21.565  -24.347 -3.099  1.00 48.33 ? 263 GLN A CG  1 
ATOM   2167  C  CD  . GLN A  1 263 ? 22.219  -25.699 -2.849  1.00 47.42 ? 263 GLN A CD  1 
ATOM   2168  O  OE1 . GLN A  1 263 ? 23.299  -25.809 -2.231  1.00 48.47 ? 263 GLN A OE1 1 
ATOM   2169  N  NE2 . GLN A  1 263 ? 21.574  -26.745 -3.348  1.00 27.22 ? 263 GLN A NE2 1 
ATOM   2170  N  N   . SER B  1 2   ? -4.334  18.839  -0.637  1.00 59.94 ? 2   SER B N   1 
ATOM   2171  C  CA  . SER B  1 2   ? -3.696  17.479  -0.614  1.00 43.85 ? 2   SER B CA  1 
ATOM   2172  C  C   . SER B  1 2   ? -2.834  17.218  -1.909  1.00 46.85 ? 2   SER B C   1 
ATOM   2173  O  O   . SER B  1 2   ? -3.395  16.959  -2.986  1.00 58.68 ? 2   SER B O   1 
ATOM   2174  C  CB  . SER B  1 2   ? -4.759  16.383  -0.327  1.00 44.91 ? 2   SER B CB  1 
ATOM   2175  O  OG  . SER B  1 2   ? -5.225  15.714  -1.506  1.00 43.30 ? 2   SER B OG  1 
ATOM   2176  N  N   . LYS B  1 3   ? -1.498  17.379  -1.830  1.00 40.46 ? 3   LYS B N   1 
ATOM   2177  C  CA  . LYS B  1 3   ? -0.569  16.798  -2.842  1.00 31.24 ? 3   LYS B CA  1 
ATOM   2178  C  C   . LYS B  1 3   ? 0.337   15.692  -2.262  1.00 23.97 ? 3   LYS B C   1 
ATOM   2179  O  O   . LYS B  1 3   ? 1.254   15.196  -2.943  1.00 20.67 ? 3   LYS B O   1 
ATOM   2180  C  CB  . LYS B  1 3   ? 0.268   17.797  -3.658  1.00 36.75 ? 3   LYS B CB  1 
ATOM   2181  C  CG  . LYS B  1 3   ? 1.374   18.493  -2.894  1.00 39.32 ? 3   LYS B CG  1 
ATOM   2182  C  CD  . LYS B  1 3   ? 1.828   19.784  -3.597  1.00 44.00 ? 3   LYS B CD  1 
ATOM   2183  C  CE  . LYS B  1 3   ? 3.041   19.556  -4.494  1.00 45.91 ? 3   LYS B CE  1 
ATOM   2184  N  NZ  . LYS B  1 3   ? 4.206   18.856  -3.851  1.00 36.50 ? 3   LYS B NZ  1 
ATOM   2185  N  N   . TRP B  1 4   ? 0.039   15.264  -1.025  1.00 14.28 ? 4   TRP B N   1 
ATOM   2186  C  CA  . TRP B  1 4   ? 0.746   14.148  -0.446  1.00 12.15 ? 4   TRP B CA  1 
ATOM   2187  C  C   . TRP B  1 4   ? 0.489   12.933  -1.328  1.00 11.39 ? 4   TRP B C   1 
ATOM   2188  O  O   . TRP B  1 4   ? -0.549  12.813  -2.060  1.00 12.52 ? 4   TRP B O   1 
ATOM   2189  C  CB  . TRP B  1 4   ? 0.245   13.892  0.994   1.00 12.11 ? 4   TRP B CB  1 
ATOM   2190  C  CG  . TRP B  1 4   ? -1.267  13.580  1.193   1.00 10.46 ? 4   TRP B CG  1 
ATOM   2191  C  CD1 . TRP B  1 4   ? -2.289  14.434  1.431   1.00 9.88  ? 4   TRP B CD1 1 
ATOM   2192  C  CD2 . TRP B  1 4   ? -1.863  12.271  1.137   1.00 8.50  ? 4   TRP B CD2 1 
ATOM   2193  N  NE1 . TRP B  1 4   ? -3.481  13.773  1.529   1.00 10.16 ? 4   TRP B NE1 1 
ATOM   2194  C  CE2 . TRP B  1 4   ? -3.250  12.437  1.395   1.00 9.76  ? 4   TRP B CE2 1 
ATOM   2195  C  CE3 . TRP B  1 4   ? -1.309  10.970  1.013   1.00 8.59  ? 4   TRP B CE3 1 
ATOM   2196  C  CZ2 . TRP B  1 4   ? -4.117  11.366  1.502   1.00 9.75  ? 4   TRP B CZ2 1 
ATOM   2197  C  CZ3 . TRP B  1 4   ? -2.159  9.913   1.087   1.00 8.11  ? 4   TRP B CZ3 1 
ATOM   2198  C  CH2 . TRP B  1 4   ? -3.512  10.113  1.328   1.00 9.61  ? 4   TRP B CH2 1 
ATOM   2199  N  N   . THR B  1 5   ? 1.425   12.008  -1.319  1.00 10.45 ? 5   THR B N   1 
ATOM   2200  C  CA  . THR B  1 5   ? 1.343   10.830  -2.147  1.00 9.71  ? 5   THR B CA  1 
ATOM   2201  C  C   . THR B  1 5   ? 1.860   9.626   -1.344  1.00 9.57  ? 5   THR B C   1 
ATOM   2202  O  O   . THR B  1 5   ? 2.199   9.739   -0.120  1.00 9.40  ? 5   THR B O   1 
ATOM   2203  C  CB  . THR B  1 5   ? 2.252   10.872  -3.375  1.00 10.91 ? 5   THR B CB  1 
ATOM   2204  O  OG1 . THR B  1 5   ? 3.595   10.900  -2.853  1.00 12.19 ? 5   THR B OG1 1 
ATOM   2205  C  CG2 . THR B  1 5   ? 1.961   12.204  -4.218  1.00 12.02 ? 5   THR B CG2 1 
ATOM   2206  N  N   . TYR B  1 6   ? 1.955   8.477   -1.972  1.00 10.03 ? 6   TYR B N   1 
ATOM   2207  C  CA  . TYR B  1 6   ? 2.594   7.298   -1.407  1.00 9.68  ? 6   TYR B CA  1 
ATOM   2208  C  C   . TYR B  1 6   ? 3.962   6.914   -1.958  1.00 10.43 ? 6   TYR B C   1 
ATOM   2209  O  O   . TYR B  1 6   ? 4.516   5.900   -1.699  1.00 11.55 ? 6   TYR B O   1 
ATOM   2210  C  CB  . TYR B  1 6   ? 1.694   6.074   -1.530  1.00 9.71  ? 6   TYR B CB  1 
ATOM   2211  C  CG  . TYR B  1 6   ? 0.423   6.185   -0.677  1.00 8.43  ? 6   TYR B CG  1 
ATOM   2212  C  CD1 . TYR B  1 6   ? -0.762  6.727   -1.176  1.00 7.94  ? 6   TYR B CD1 1 
ATOM   2213  C  CD2 . TYR B  1 6   ? 0.397   5.629   0.588   1.00 8.60  ? 6   TYR B CD2 1 
ATOM   2214  C  CE1 . TYR B  1 6   ? -1.906  6.736   -0.389  1.00 8.61  ? 6   TYR B CE1 1 
ATOM   2215  C  CE2 . TYR B  1 6   ? -0.725  5.622   1.402   1.00 7.96  ? 6   TYR B CE2 1 
ATOM   2216  C  CZ  . TYR B  1 6   ? -1.897  6.225   0.917   1.00 7.00  ? 6   TYR B CZ  1 
ATOM   2217  O  OH  . TYR B  1 6   ? -3.011  6.199   1.624   1.00 8.05  ? 6   TYR B OH  1 
ATOM   2218  N  N   . PHE B  1 7   ? 4.465   7.803   -2.817  1.00 12.47 ? 7   PHE B N   1 
ATOM   2219  C  CA  . PHE B  1 7   ? 5.649   7.485   -3.551  1.00 14.06 ? 7   PHE B CA  1 
ATOM   2220  C  C   . PHE B  1 7   ? 6.378   8.764   -3.933  1.00 15.78 ? 7   PHE B C   1 
ATOM   2221  O  O   . PHE B  1 7   ? 5.807   9.635   -4.544  1.00 14.94 ? 7   PHE B O   1 
ATOM   2222  C  CB  . PHE B  1 7   ? 5.357   6.737   -4.891  1.00 17.77 ? 7   PHE B CB  1 
ATOM   2223  C  CG  . PHE B  1 7   ? 6.644   6.371   -5.602  1.00 22.43 ? 7   PHE B CG  1 
ATOM   2224  C  CD1 . PHE B  1 7   ? 7.402   5.224   -5.233  1.00 24.58 ? 7   PHE B CD1 1 
ATOM   2225  C  CD2 . PHE B  1 7   ? 7.230   7.272   -6.552  1.00 28.69 ? 7   PHE B CD2 1 
ATOM   2226  C  CE1 . PHE B  1 7   ? 8.641   4.916   -5.850  1.00 30.38 ? 7   PHE B CE1 1 
ATOM   2227  C  CE2 . PHE B  1 7   ? 8.472   6.952   -7.167  1.00 32.68 ? 7   PHE B CE2 1 
ATOM   2228  C  CZ  . PHE B  1 7   ? 9.146   5.774   -6.840  1.00 32.43 ? 7   PHE B CZ  1 
ATOM   2229  N  N   . GLY B  1 8   ? 7.632   8.852   -3.583  1.00 17.96 ? 8   GLY B N   1 
ATOM   2230  C  CA  . GLY B  1 8   ? 8.521   9.960   -4.057  1.00 16.24 ? 8   GLY B CA  1 
ATOM   2231  C  C   . GLY B  1 8   ? 8.671   11.012  -2.967  1.00 18.18 ? 8   GLY B C   1 
ATOM   2232  O  O   . GLY B  1 8   ? 8.380   10.770  -1.784  1.00 18.29 ? 8   GLY B O   1 
ATOM   2233  N  N   . PRO B  1 9   ? 9.019   12.250  -3.297  1.00 17.98 ? 9   PRO B N   1 
ATOM   2234  C  CA  . PRO B  1 9   ? 9.250   13.314  -2.341  1.00 17.74 ? 9   PRO B CA  1 
ATOM   2235  C  C   . PRO B  1 9   ? 8.139   13.695  -1.438  1.00 16.25 ? 9   PRO B C   1 
ATOM   2236  O  O   . PRO B  1 9   ? 8.385   14.251  -0.388  1.00 19.93 ? 9   PRO B O   1 
ATOM   2237  C  CB  . PRO B  1 9   ? 9.622   14.563  -3.191  1.00 20.48 ? 9   PRO B CB  1 
ATOM   2238  C  CG  . PRO B  1 9   ? 9.659   14.040  -4.511  1.00 19.80 ? 9   PRO B CG  1 
ATOM   2239  C  CD  . PRO B  1 9   ? 9.215   12.663  -4.692  1.00 20.86 ? 9   PRO B CD  1 
ATOM   2240  N  N   . ASP B  1 10  ? 6.862   13.442  -1.857  1.00 14.39 ? 10  ASP B N   1 
ATOM   2241  C  CA  . ASP B  1 10  ? 5.726   13.755  -1.058  1.00 14.76 ? 10  ASP B CA  1 
ATOM   2242  C  C   . ASP B  1 10  ? 5.066   12.513  -0.399  1.00 10.96 ? 10  ASP B C   1 
ATOM   2243  O  O   . ASP B  1 10  ? 3.968   12.631  0.133   1.00 11.73 ? 10  ASP B O   1 
ATOM   2244  C  CB  . ASP B  1 10  ? 4.645   14.602  -1.809  1.00 17.97 ? 10  ASP B CB  1 
ATOM   2245  C  CG  . ASP B  1 10  ? 5.273   15.835  -2.497  1.00 21.38 ? 10  ASP B CG  1 
ATOM   2246  O  OD1 . ASP B  1 10  ? 5.896   16.578  -1.759  1.00 26.09 ? 10  ASP B OD1 1 
ATOM   2247  O  OD2 . ASP B  1 10  ? 5.262   15.947  -3.751  1.00 26.41 ? 10  ASP B OD2 1 
ATOM   2248  N  N   . GLY B  1 11  ? 5.917   11.470  -0.398  1.00 10.83 ? 11  GLY B N   1 
ATOM   2249  C  CA  . GLY B  1 11  ? 5.453   10.174  0.187   1.00 9.51  ? 11  GLY B CA  1 
ATOM   2250  C  C   . GLY B  1 11  ? 5.551   10.198  1.712   1.00 9.23  ? 11  GLY B C   1 
ATOM   2251  O  O   . GLY B  1 11  ? 5.711   11.205  2.405   1.00 8.94  ? 11  GLY B O   1 
ATOM   2252  N  N   . GLU B  1 12  ? 5.289   8.995   2.290   1.00 8.34  ? 12  GLU B N   1 
ATOM   2253  C  CA  . GLU B  1 12  ? 4.900   8.969   3.699   1.00 7.76  ? 12  GLU B CA  1 
ATOM   2254  C  C   . GLU B  1 12  ? 5.916   9.424   4.738   1.00 7.77  ? 12  GLU B C   1 
ATOM   2255  O  O   . GLU B  1 12  ? 5.522   9.863   5.790   1.00 8.60  ? 12  GLU B O   1 
ATOM   2256  C  CB  . GLU B  1 12  ? 4.418   7.507   4.028   1.00 8.94  ? 12  GLU B CB  1 
ATOM   2257  C  CG  . GLU B  1 12  ? 5.534   6.485   4.169   1.00 8.87  ? 12  GLU B CG  1 
ATOM   2258  C  CD  . GLU B  1 12  ? 4.932   5.101   4.080   1.00 7.92  ? 12  GLU B CD  1 
ATOM   2259  O  OE1 . GLU B  1 12  ? 4.548   4.620   5.152   1.00 8.23  ? 12  GLU B OE1 1 
ATOM   2260  O  OE2 . GLU B  1 12  ? 4.891   4.552   2.952   1.00 9.48  ? 12  GLU B OE2 1 
ATOM   2261  N  N   . ASN B  1 13  ? 7.221   9.308   4.346   1.00 8.36  ? 13  ASN B N   1 
ATOM   2262  C  CA  . ASN B  1 13  ? 8.185   9.819   5.306   1.00 9.09  ? 13  ASN B CA  1 
ATOM   2263  C  C   . ASN B  1 13  ? 8.252   11.336  5.367   1.00 9.66  ? 13  ASN B C   1 
ATOM   2264  O  O   . ASN B  1 13  ? 8.811   11.878  6.312   1.00 10.42 ? 13  ASN B O   1 
ATOM   2265  C  CB  . ASN B  1 13  ? 9.585   9.317   5.009   1.00 9.11  ? 13  ASN B CB  1 
ATOM   2266  C  CG  . ASN B  1 13  ? 9.775   7.807   5.242   1.00 9.35  ? 13  ASN B CG  1 
ATOM   2267  O  OD1 . ASN B  1 13  ? 8.850   7.137   5.730   1.00 9.72  ? 13  ASN B OD1 1 
ATOM   2268  N  ND2 . ASN B  1 13  ? 10.927  7.304   4.862   1.00 9.44  ? 13  ASN B ND2 1 
ATOM   2269  N  N   . SER B  1 14  ? 7.561   11.953  4.442   1.00 8.62  ? 14  SER B N   1 
ATOM   2270  C  CA  . SER B  1 14  ? 7.452   13.421  4.399   1.00 8.95  ? 14  SER B CA  1 
ATOM   2271  C  C   . SER B  1 14  ? 6.148   13.980  4.841   1.00 8.72  ? 14  SER B C   1 
ATOM   2272  O  O   . SER B  1 14  ? 6.010   15.221  4.964   1.00 9.30  ? 14  SER B O   1 
ATOM   2273  C  CB  . SER B  1 14  ? 7.762   13.878  2.999   1.00 9.43  ? 14  SER B CB  1 
ATOM   2274  O  OG  . SER B  1 14  ? 9.117   13.665  2.674   1.00 10.03 ? 14  SER B OG  1 
ATOM   2275  N  N   . TRP B  1 15  ? 5.110   13.154  5.092   1.00 7.81  ? 15  TRP B N   1 
ATOM   2276  C  CA  . TRP B  1 15  ? 3.816   13.719  5.419   1.00 8.53  ? 15  TRP B CA  1 
ATOM   2277  C  C   . TRP B  1 15  ? 3.887   14.596  6.649   1.00 9.10  ? 15  TRP B C   1 
ATOM   2278  O  O   . TRP B  1 15  ? 3.144   15.584  6.693   1.00 9.95  ? 15  TRP B O   1 
ATOM   2279  C  CB  . TRP B  1 15  ? 2.830   12.572  5.749   1.00 8.22  ? 15  TRP B CB  1 
ATOM   2280  C  CG  . TRP B  1 15  ? 2.454   11.728  4.626   1.00 8.23  ? 15  TRP B CG  1 
ATOM   2281  C  CD1 . TRP B  1 15  ? 2.737   11.890  3.290   1.00 8.49  ? 15  TRP B CD1 1 
ATOM   2282  C  CD2 . TRP B  1 15  ? 1.680   10.462  4.720   1.00 8.11  ? 15  TRP B CD2 1 
ATOM   2283  N  NE1 . TRP B  1 15  ? 2.164   10.794  2.542   1.00 8.74  ? 15  TRP B NE1 1 
ATOM   2284  C  CE2 . TRP B  1 15  ? 1.519   9.946   3.391   1.00 7.08  ? 15  TRP B CE2 1 
ATOM   2285  C  CE3 . TRP B  1 15  ? 1.101   9.761   5.799   1.00 6.87  ? 15  TRP B CE3 1 
ATOM   2286  C  CZ2 . TRP B  1 15  ? 0.810   8.749   3.106   1.00 8.07  ? 15  TRP B CZ2 1 
ATOM   2287  C  CZ3 . TRP B  1 15  ? 0.419   8.592   5.508   1.00 7.97  ? 15  TRP B CZ3 1 
ATOM   2288  C  CH2 . TRP B  1 15  ? 0.297   8.103   4.219   1.00 7.61  ? 15  TRP B CH2 1 
ATOM   2289  N  N   . SER B  1 16  ? 4.687   14.291  7.632   1.00 8.80  ? 16  SER B N   1 
ATOM   2290  C  CA  . SER B  1 16  ? 4.767   15.091  8.863   1.00 9.83  ? 16  SER B CA  1 
ATOM   2291  C  C   . SER B  1 16  ? 5.221   16.531  8.642   1.00 9.25  ? 16  SER B C   1 
ATOM   2292  O  O   . SER B  1 16  ? 5.007   17.328  9.547   1.00 11.16 ? 16  SER B O   1 
ATOM   2293  C  CB  . SER B  1 16  ? 5.742   14.409  9.835   1.00 10.44 ? 16  SER B CB  1 
ATOM   2294  O  OG  . SER B  1 16  ? 7.070   14.519  9.341   1.00 13.08 ? 16  SER B OG  1 
ATOM   2295  N  N   . LYS B  1 17  ? 5.831   16.807  7.482   1.00 9.18  ? 17  LYS B N   1 
ATOM   2296  C  CA  . LYS B  1 17  ? 6.286   18.174  7.191   1.00 9.70  ? 17  LYS B CA  1 
ATOM   2297  C  C   . LYS B  1 17  ? 5.103   19.074  7.072   1.00 10.68 ? 17  LYS B C   1 
ATOM   2298  O  O   . LYS B  1 17  ? 5.264   20.286  7.399   1.00 11.53 ? 17  LYS B O   1 
ATOM   2299  C  CB  . LYS B  1 17  ? 7.101   18.236  5.888   1.00 9.67  ? 17  LYS B CB  1 
ATOM   2300  C  CG  . LYS B  1 17  ? 8.368   17.370  5.833   1.00 11.97 ? 17  LYS B CG  1 
ATOM   2301  C  CD  . LYS B  1 17  ? 8.975   17.384  4.461   1.00 10.73 ? 17  LYS B CD  1 
ATOM   2302  C  CE  . LYS B  1 17  ? 10.187  16.424  4.321   1.00 9.71  ? 17  LYS B CE  1 
ATOM   2303  N  NZ  . LYS B  1 17  ? 10.748  16.535  3.000   1.00 10.29 ? 17  LYS B NZ  1 
ATOM   2304  N  N   . LYS B  1 18  ? 4.003   18.598  6.475   1.00 10.96 ? 18  LYS B N   1 
ATOM   2305  C  CA  . LYS B  1 18  ? 2.766   19.426  6.321   1.00 10.15 ? 18  LYS B CA  1 
ATOM   2306  C  C   . LYS B  1 18  ? 1.647   19.029  7.308   1.00 10.21 ? 18  LYS B C   1 
ATOM   2307  O  O   . LYS B  1 18  ? 0.722   19.832  7.508   1.00 12.84 ? 18  LYS B O   1 
ATOM   2308  C  CB  . LYS B  1 18  ? 2.205   19.241  4.912   1.00 12.24 ? 18  LYS B CB  1 
ATOM   2309  C  CG  . LYS B  1 18  ? 3.172   19.858  3.858   1.00 16.37 ? 18  LYS B CG  1 
ATOM   2310  C  CD  . LYS B  1 18  ? 2.675   19.596  2.429   1.00 18.11 ? 18  LYS B CD  1 
ATOM   2311  C  CE  . LYS B  1 18  ? 3.391   20.552  1.474   1.00 23.54 ? 18  LYS B CE  1 
ATOM   2312  N  NZ  . LYS B  1 18  ? 2.674   20.401  0.143   1.00 29.56 ? 18  LYS B NZ  1 
ATOM   2313  N  N   . TYR B  1 19  ? 1.711   17.794  7.891   1.00 9.56  ? 19  TYR B N   1 
ATOM   2314  C  CA  . TYR B  1 19  ? 0.592   17.247  8.740   1.00 10.01 ? 19  TYR B CA  1 
ATOM   2315  C  C   . TYR B  1 19  ? 1.259   16.779  10.000  1.00 10.13 ? 19  TYR B C   1 
ATOM   2316  O  O   . TYR B  1 19  ? 1.692   15.599  10.085  1.00 10.50 ? 19  TYR B O   1 
ATOM   2317  C  CB  . TYR B  1 19  ? -0.033  16.065  7.912   1.00 10.29 ? 19  TYR B CB  1 
ATOM   2318  C  CG  . TYR B  1 19  ? -0.641  16.524  6.617   1.00 9.73  ? 19  TYR B CG  1 
ATOM   2319  C  CD1 . TYR B  1 19  ? -1.855  17.188  6.591   1.00 11.46 ? 19  TYR B CD1 1 
ATOM   2320  C  CD2 . TYR B  1 19  ? 0.023   16.304  5.410   1.00 9.50  ? 19  TYR B CD2 1 
ATOM   2321  C  CE1 . TYR B  1 19  ? -2.411  17.579  5.403   1.00 13.80 ? 19  TYR B CE1 1 
ATOM   2322  C  CE2 . TYR B  1 19  ? -0.508  16.725  4.220   1.00 11.14 ? 19  TYR B CE2 1 
ATOM   2323  C  CZ  . TYR B  1 19  ? -1.722  17.350  4.208   1.00 12.69 ? 19  TYR B CZ  1 
ATOM   2324  O  OH  . TYR B  1 19  ? -2.232  17.735  3.001   1.00 17.27 ? 19  TYR B OH  1 
ATOM   2325  N  N   . PRO B  1 20  ? 1.366   17.641  11.014  1.00 10.39 ? 20  PRO B N   1 
ATOM   2326  C  CA  . PRO B  1 20  ? 2.161   17.268  12.191  1.00 11.10 ? 20  PRO B CA  1 
ATOM   2327  C  C   . PRO B  1 20  ? 1.657   16.012  12.846  1.00 10.09 ? 20  PRO B C   1 
ATOM   2328  O  O   . PRO B  1 20  ? 2.552   15.350  13.451  1.00 10.87 ? 20  PRO B O   1 
ATOM   2329  C  CB  . PRO B  1 20  ? 2.078   18.484  13.141  1.00 12.97 ? 20  PRO B CB  1 
ATOM   2330  C  CG  . PRO B  1 20  ? 1.748   19.601  12.168  1.00 14.31 ? 20  PRO B CG  1 
ATOM   2331  C  CD  . PRO B  1 20  ? 0.958   19.087  10.995  1.00 10.52 ? 20  PRO B CD  1 
ATOM   2332  N  N   . SER B  1 21  ? 0.356   15.683  12.827  1.00 9.75  ? 21  SER B N   1 
ATOM   2333  C  CA  . SER B  1 21  ? -0.076  14.496  13.555  1.00 9.98  ? 21  SER B CA  1 
ATOM   2334  C  C   . SER B  1 21  ? 0.483   13.235  12.895  1.00 10.29 ? 21  SER B C   1 
ATOM   2335  O  O   . SER B  1 21  ? 0.568   12.231  13.612  1.00 10.17 ? 21  SER B O   1 
ATOM   2336  C  CB  . SER B  1 21  ? -1.582  14.414  13.551  1.00 11.25 ? 21  SER B CB  1 
ATOM   2337  O  OG  . SER B  1 21  ? -2.100  15.447  14.375  1.00 14.85 ? 21  SER B OG  1 
ATOM   2338  N  N   . CYS B  1 22  ? 0.936   13.265  11.681  1.00 9.42  ? 22  CYS B N   1 
ATOM   2339  C  CA  . CYS B  1 22  ? 1.548   12.079  11.050  1.00 8.92  ? 22  CYS B CA  1 
ATOM   2340  C  C   . CYS B  1 22  ? 2.840   11.696  11.703  1.00 9.87  ? 22  CYS B C   1 
ATOM   2341  O  O   . CYS B  1 22  ? 3.321   10.567  11.505  1.00 10.77 ? 22  CYS B O   1 
ATOM   2342  C  CB  . CYS B  1 22  ? 1.738   12.254  9.502   1.00 9.05  ? 22  CYS B CB  1 
ATOM   2343  S  SG  . CYS B  1 22  ? 0.154   12.594  8.632   1.00 9.84  ? 22  CYS B SG  1 
ATOM   2344  N  N   . GLY B  1 23  ? 3.505   12.635  12.440  1.00 10.37 ? 23  GLY B N   1 
ATOM   2345  C  CA  . GLY B  1 23  ? 4.706   12.355  13.259  1.00 12.27 ? 23  GLY B CA  1 
ATOM   2346  C  C   . GLY B  1 23  ? 4.370   12.293  14.717  1.00 13.36 ? 23  GLY B C   1 
ATOM   2347  O  O   . GLY B  1 23  ? 5.330   12.313  15.531  1.00 14.88 ? 23  GLY B O   1 
ATOM   2348  N  N   . GLY B  1 24  ? 3.130   12.203  15.091  1.00 13.82 ? 24  GLY B N   1 
ATOM   2349  C  CA  . GLY B  1 24  ? 2.720   12.176  16.481  1.00 13.92 ? 24  GLY B CA  1 
ATOM   2350  C  C   . GLY B  1 24  ? 2.511   10.754  16.975  1.00 14.93 ? 24  GLY B C   1 
ATOM   2351  O  O   . GLY B  1 24  ? 3.057   9.830   16.409  1.00 17.27 ? 24  GLY B O   1 
ATOM   2352  N  N   . LEU B  1 25  ? 1.782   10.727  18.057  1.00 17.64 ? 25  LEU B N   1 
ATOM   2353  C  CA  . LEU B  1 25  ? 1.625   9.368   18.688  1.00 18.61 ? 25  LEU B CA  1 
ATOM   2354  C  C   . LEU B  1 25  ? 0.367   8.690   18.101  1.00 17.51 ? 25  LEU B C   1 
ATOM   2355  O  O   . LEU B  1 25  ? -0.407  9.328   17.321  1.00 15.80 ? 25  LEU B O   1 
ATOM   2356  C  CB  . LEU B  1 25  ? 1.586   9.470   20.203  1.00 25.03 ? 25  LEU B CB  1 
ATOM   2357  C  CG  . LEU B  1 25  ? 2.922   9.969   20.852  1.00 26.72 ? 25  LEU B CG  1 
ATOM   2358  C  CD1 . LEU B  1 25  ? 2.699   10.323  22.316  1.00 33.40 ? 25  LEU B CD1 1 
ATOM   2359  C  CD2 . LEU B  1 25  ? 4.104   9.015   20.687  1.00 33.44 ? 25  LEU B CD2 1 
ATOM   2360  N  N   . LEU B  1 26  ? 0.205   7.419   18.516  1.00 18.07 ? 26  LEU B N   1 
ATOM   2361  C  CA  . LEU B  1 26  ? -1.000  6.660   18.244  1.00 16.82 ? 26  LEU B CA  1 
ATOM   2362  C  C   . LEU B  1 26  ? -1.228  6.453   16.749  1.00 10.16 ? 26  LEU B C   1 
ATOM   2363  O  O   . LEU B  1 26  ? -2.382  6.313   16.348  1.00 12.35 ? 26  LEU B O   1 
ATOM   2364  C  CB  . LEU B  1 26  ? -2.259  7.256   18.853  1.00 17.17 ? 26  LEU B CB  1 
ATOM   2365  C  CG  . LEU B  1 26  ? -2.365  7.408   20.443  1.00 24.15 ? 26  LEU B CG  1 
ATOM   2366  C  CD1 . LEU B  1 26  ? -3.810  7.812   20.842  1.00 27.79 ? 26  LEU B CD1 1 
ATOM   2367  C  CD2 . LEU B  1 26  ? -1.953  6.148   21.172  1.00 25.85 ? 26  LEU B CD2 1 
ATOM   2368  N  N   . GLN B  1 27  ? -0.160  6.274   15.985  1.00 10.55 ? 27  GLN B N   1 
ATOM   2369  C  CA  . GLN B  1 27  ? -0.350  6.117   14.503  1.00 9.31  ? 27  GLN B CA  1 
ATOM   2370  C  C   . GLN B  1 27  ? -0.719  4.722   14.094  1.00 9.93  ? 27  GLN B C   1 
ATOM   2371  O  O   . GLN B  1 27  ? -0.253  3.711   14.652  1.00 10.98 ? 27  GLN B O   1 
ATOM   2372  C  CB  . GLN B  1 27  ? 0.903   6.587   13.743  1.00 9.80  ? 27  GLN B CB  1 
ATOM   2373  C  CG  . GLN B  1 27  ? 1.194   8.082   14.019  1.00 10.62 ? 27  GLN B CG  1 
ATOM   2374  C  CD  . GLN B  1 27  ? 0.103   8.961   13.414  1.00 8.87  ? 27  GLN B CD  1 
ATOM   2375  O  OE1 . GLN B  1 27  ? 0.122   9.077   12.140  1.00 9.41  ? 27  GLN B OE1 1 
ATOM   2376  N  NE2 . GLN B  1 27  ? -0.837  9.456   14.167  1.00 10.06 ? 27  GLN B NE2 1 
ATOM   2377  N  N   . SER B  1 28  ? -1.456  4.685   13.028  1.00 8.04  ? 28  SER B N   1 
ATOM   2378  C  CA  . SER B  1 28  ? -1.822  3.465   12.336  1.00 7.52  ? 28  SER B CA  1 
ATOM   2379  C  C   . SER B  1 28  ? -1.300  3.442   10.948  1.00 8.46  ? 28  SER B C   1 
ATOM   2380  O  O   . SER B  1 28  ? -1.025  4.523   10.387  1.00 8.76  ? 28  SER B O   1 
ATOM   2381  C  CB  . SER B  1 28  ? -3.344  3.404   12.270  1.00 8.81  ? 28  SER B CB  1 
ATOM   2382  O  OG  . SER B  1 28  ? -3.899  3.318   13.607  1.00 8.60  ? 28  SER B OG  1 
ATOM   2383  N  N   . PRO B  1 29  ? -1.180  2.329   10.262  1.00 6.99  ? 29  PRO B N   1 
ATOM   2384  C  CA  . PRO B  1 29  ? -1.508  0.971   10.752  1.00 7.89  ? 29  PRO B CA  1 
ATOM   2385  C  C   . PRO B  1 29  ? -0.378  0.367   11.553  1.00 7.38  ? 29  PRO B C   1 
ATOM   2386  O  O   . PRO B  1 29  ? 0.645   0.982   11.737  1.00 7.90  ? 29  PRO B O   1 
ATOM   2387  C  CB  . PRO B  1 29  ? -1.732  0.211   9.379   1.00 7.91  ? 29  PRO B CB  1 
ATOM   2388  C  CG  . PRO B  1 29  ? -0.564  0.787   8.524   1.00 7.75  ? 29  PRO B CG  1 
ATOM   2389  C  CD  . PRO B  1 29  ? -0.667  2.279   8.874   1.00 7.84  ? 29  PRO B CD  1 
ATOM   2390  N  N   . ILE B  1 30  ? -0.628  -0.869  11.968  1.00 7.52  ? 30  ILE B N   1 
ATOM   2391  C  CA  . ILE B  1 30  ? 0.349   -1.589  12.843  1.00 7.48  ? 30  ILE B CA  1 
ATOM   2392  C  C   . ILE B  1 30  ? 0.381   -3.057  12.401  1.00 8.10  ? 30  ILE B C   1 
ATOM   2393  O  O   . ILE B  1 30  ? -0.505  -3.543  11.709  1.00 7.35  ? 30  ILE B O   1 
ATOM   2394  C  CB  . ILE B  1 30  ? 0.023   -1.496  14.334  1.00 8.45  ? 30  ILE B CB  1 
ATOM   2395  C  CG1 . ILE B  1 30  ? -1.383  -2.017  14.594  1.00 9.19  ? 30  ILE B CG1 1 
ATOM   2396  C  CG2 . ILE B  1 30  ? 0.210   -0.023  14.801  1.00 10.39 ? 30  ILE B CG2 1 
ATOM   2397  C  CD1 . ILE B  1 30  ? -1.677  -2.141  16.091  1.00 11.58 ? 30  ILE B CD1 1 
ATOM   2398  N  N   . ASP B  1 31  ? 1.466   -3.715  12.860  1.00 7.55  ? 31  ASP B N   1 
ATOM   2399  C  CA  . ASP B  1 31  ? 1.651   -5.149  12.620  1.00 8.47  ? 31  ASP B CA  1 
ATOM   2400  C  C   . ASP B  1 31  ? 0.977   -5.833  13.857  1.00 10.48 ? 31  ASP B C   1 
ATOM   2401  O  O   . ASP B  1 31  ? 1.385   -5.614  14.997  1.00 11.02 ? 31  ASP B O   1 
ATOM   2402  C  CB  . ASP B  1 31  ? 3.133   -5.565  12.608  1.00 8.38  ? 31  ASP B CB  1 
ATOM   2403  C  CG  . ASP B  1 31  ? 3.273   -7.049  12.434  1.00 10.44 ? 31  ASP B CG  1 
ATOM   2404  O  OD1 . ASP B  1 31  ? 2.705   -7.635  11.476  1.00 10.32 ? 31  ASP B OD1 1 
ATOM   2405  O  OD2 . ASP B  1 31  ? 3.888   -7.651  13.324  1.00 13.97 ? 31  ASP B OD2 1 
ATOM   2406  N  N   . LEU B  1 32  ? 0.032   -6.706  13.563  1.00 10.51 ? 32  LEU B N   1 
ATOM   2407  C  CA  . LEU B  1 32  ? -0.710  -7.429  14.630  1.00 10.26 ? 32  LEU B CA  1 
ATOM   2408  C  C   . LEU B  1 32  ? 0.118   -8.697  14.885  1.00 10.44 ? 32  LEU B C   1 
ATOM   2409  O  O   . LEU B  1 32  ? 0.149   -9.576  14.047  1.00 11.02 ? 32  LEU B O   1 
ATOM   2410  C  CB  . LEU B  1 32  ? -2.120  -7.738  14.126  1.00 10.27 ? 32  LEU B CB  1 
ATOM   2411  C  CG  . LEU B  1 32  ? -2.893  -6.459  13.776  1.00 12.19 ? 32  LEU B CG  1 
ATOM   2412  C  CD1 . LEU B  1 32  ? -4.163  -6.841  13.045  1.00 13.58 ? 32  LEU B CD1 1 
ATOM   2413  C  CD2 . LEU B  1 32  ? -3.138  -5.616  14.987  1.00 13.15 ? 32  LEU B CD2 1 
ATOM   2414  N  N   . HIS B  1 33  ? 0.776   -8.786  16.048  1.00 10.86 ? 33  HIS B N   1 
ATOM   2415  C  CA  . HIS B  1 33  ? 1.676   -9.959  16.323  1.00 10.74 ? 33  HIS B CA  1 
ATOM   2416  C  C   . HIS B  1 33  ? 1.534   -10.293 17.797  1.00 10.37 ? 33  HIS B C   1 
ATOM   2417  O  O   . HIS B  1 33  ? 1.205   -9.414  18.614  1.00 11.03 ? 33  HIS B O   1 
ATOM   2418  C  CB  . HIS B  1 33  ? 3.192   -9.724  15.927  1.00 11.67 ? 33  HIS B CB  1 
ATOM   2419  C  CG  . HIS B  1 33  ? 3.855   -8.554  16.627  1.00 13.00 ? 33  HIS B CG  1 
ATOM   2420  N  ND1 . HIS B  1 33  ? 3.535   -7.260  16.347  1.00 16.13 ? 33  HIS B ND1 1 
ATOM   2421  C  CD2 . HIS B  1 33  ? 4.757   -8.488  17.663  1.00 12.59 ? 33  HIS B CD2 1 
ATOM   2422  C  CE1 . HIS B  1 33  ? 4.220   -6.431  17.145  1.00 18.51 ? 33  HIS B CE1 1 
ATOM   2423  N  NE2 . HIS B  1 33  ? 5.008   -7.161  17.910  1.00 15.58 ? 33  HIS B NE2 1 
ATOM   2424  N  N   . SER B  1 34  ? 1.901   -11.547 18.117  1.00 12.08 ? 34  SER B N   1 
ATOM   2425  C  CA  . SER B  1 34  ? 1.542   -12.059 19.460  1.00 12.56 ? 34  SER B CA  1 
ATOM   2426  C  C   . SER B  1 34  ? 2.039   -11.249 20.600  1.00 12.86 ? 34  SER B C   1 
ATOM   2427  O  O   . SER B  1 34  ? 1.312   -11.081 21.624  1.00 13.38 ? 34  SER B O   1 
ATOM   2428  C  CB  . SER B  1 34  ? 2.070   -13.502 19.546  1.00 15.71 ? 34  SER B CB  1 
ATOM   2429  O  OG  . SER B  1 34  ? 3.501   -13.546 19.467  1.00 18.45 ? 34  SER B OG  1 
ATOM   2430  N  N   . ASP B  1 35  ? 3.223   -10.640 20.539  1.00 12.32 ? 35  ASP B N   1 
ATOM   2431  C  CA  . ASP B  1 35  ? 3.759   -9.995  21.735  1.00 13.27 ? 35  ASP B CA  1 
ATOM   2432  C  C   . ASP B  1 35  ? 2.922   -8.878  22.247  1.00 13.58 ? 35  ASP B C   1 
ATOM   2433  O  O   . ASP B  1 35  ? 3.025   -8.407  23.408  1.00 17.33 ? 35  ASP B O   1 
ATOM   2434  C  CB  . ASP B  1 35  ? 5.196   -9.388  21.482  1.00 14.23 ? 35  ASP B CB  1 
ATOM   2435  C  CG  . ASP B  1 35  ? 6.098   -10.401 20.864  1.00 16.85 ? 35  ASP B CG  1 
ATOM   2436  O  OD1 . ASP B  1 35  ? 5.842   -10.911 19.741  1.00 15.60 ? 35  ASP B OD1 1 
ATOM   2437  O  OD2 . ASP B  1 35  ? 7.088   -10.830 21.546  1.00 15.29 ? 35  ASP B OD2 1 
ATOM   2438  N  N   . ILE B  1 36  ? 2.083   -8.306  21.375  1.00 13.04 ? 36  ILE B N   1 
ATOM   2439  C  CA  . ILE B  1 36  ? 1.356   -7.083  21.744  1.00 14.49 ? 36  ILE B CA  1 
ATOM   2440  C  C   . ILE B  1 36  ? -0.161  -7.335  21.809  1.00 13.48 ? 36  ILE B C   1 
ATOM   2441  O  O   . ILE B  1 36  ? -0.910  -6.392  21.992  1.00 14.24 ? 36  ILE B O   1 
ATOM   2442  C  CB  . ILE B  1 36  ? 1.675   -5.822  20.853  1.00 16.29 ? 36  ILE B CB  1 
ATOM   2443  C  CG1 . ILE B  1 36  ? 1.644   -6.109  19.350  1.00 20.02 ? 36  ILE B CG1 1 
ATOM   2444  C  CG2 . ILE B  1 36  ? 3.113   -5.346  21.121  1.00 20.60 ? 36  ILE B CG2 1 
ATOM   2445  C  CD1 . ILE B  1 36  ? 0.296   -6.368  18.864  1.00 19.09 ? 36  ILE B CD1 1 
ATOM   2446  N  N   . LEU B  1 37  ? -0.574  -8.579  21.665  1.00 12.27 ? 37  LEU B N   1 
ATOM   2447  C  CA  . LEU B  1 37  ? -1.996  -9.006  21.713  1.00 12.24 ? 37  LEU B CA  1 
ATOM   2448  C  C   . LEU B  1 37  ? -2.391  -9.356  23.077  1.00 14.89 ? 37  LEU B C   1 
ATOM   2449  O  O   . LEU B  1 37  ? -1.618  -10.000 23.797  1.00 17.45 ? 37  LEU B O   1 
ATOM   2450  C  CB  . LEU B  1 37  ? -2.280  -10.186 20.823  1.00 13.46 ? 37  LEU B CB  1 
ATOM   2451  C  CG  . LEU B  1 37  ? -2.005  -9.969  19.336  1.00 13.65 ? 37  LEU B CG  1 
ATOM   2452  C  CD1 . LEU B  1 37  ? -2.294  -11.190 18.473  1.00 17.52 ? 37  LEU B CD1 1 
ATOM   2453  C  CD2 . LEU B  1 37  ? -2.746  -8.777  18.722  1.00 12.57 ? 37  LEU B CD2 1 
ATOM   2454  N  N   . GLN B  1 38  ? -3.610  -9.017  23.473  1.00 13.06 ? 38  GLN B N   1 
ATOM   2455  C  CA  . GLN B  1 38  ? -4.138  -9.466  24.777  1.00 13.62 ? 38  GLN B CA  1 
ATOM   2456  C  C   . GLN B  1 38  ? -5.632  -9.628  24.678  1.00 14.76 ? 38  GLN B C   1 
ATOM   2457  O  O   . GLN B  1 38  ? -6.366  -8.721  24.264  1.00 12.58 ? 38  GLN B O   1 
ATOM   2458  C  CB  . GLN B  1 38  ? -3.868  -8.466  25.778  1.00 15.89 ? 38  GLN B CB  1 
ATOM   2459  C  CG  . GLN B  1 38  ? -4.226  -8.950  27.215  1.00 18.73 ? 38  GLN B CG  1 
ATOM   2460  C  CD  . GLN B  1 38  ? -3.652  -8.036  28.225  1.00 25.78 ? 38  GLN B CD  1 
ATOM   2461  O  OE1 . GLN B  1 38  ? -2.476  -8.168  28.576  1.00 32.95 ? 38  GLN B OE1 1 
ATOM   2462  N  NE2 . GLN B  1 38  ? -4.436  -7.106  28.699  1.00 25.83 ? 38  GLN B NE2 1 
ATOM   2463  N  N   . TYR B  1 39  ? -6.121  -10.775 25.111  1.00 14.06 ? 39  TYR B N   1 
ATOM   2464  C  CA  . TYR B  1 39  ? -7.551  -11.072 25.094  1.00 12.66 ? 39  TYR B CA  1 
ATOM   2465  C  C   . TYR B  1 39  ? -8.256  -10.129 26.065  1.00 12.25 ? 39  TYR B C   1 
ATOM   2466  O  O   . TYR B  1 39  ? -7.786  -9.830  27.184  1.00 14.04 ? 39  TYR B O   1 
ATOM   2467  C  CB  . TYR B  1 39  ? -7.688  -12.511 25.518  1.00 12.54 ? 39  TYR B CB  1 
ATOM   2468  C  CG  . TYR B  1 39  ? -9.119  -12.899 25.656  1.00 12.69 ? 39  TYR B CG  1 
ATOM   2469  C  CD1 . TYR B  1 39  ? -9.998  -12.890 24.599  1.00 12.83 ? 39  TYR B CD1 1 
ATOM   2470  C  CD2 . TYR B  1 39  ? -9.649  -13.299 26.903  1.00 14.47 ? 39  TYR B CD2 1 
ATOM   2471  C  CE1 . TYR B  1 39  ? -11.331 -13.247 24.721  1.00 13.57 ? 39  TYR B CE1 1 
ATOM   2472  C  CE2 . TYR B  1 39  ? -11.011 -13.652 27.014  1.00 14.40 ? 39  TYR B CE2 1 
ATOM   2473  C  CZ  . TYR B  1 39  ? -11.823 -13.671 25.943  1.00 15.15 ? 39  TYR B CZ  1 
ATOM   2474  O  OH  . TYR B  1 39  ? -13.162 -13.968 26.067  1.00 16.99 ? 39  TYR B OH  1 
ATOM   2475  N  N   . ASP B  1 40  ? -9.382  -9.627  25.615  1.00 11.85 ? 40  ASP B N   1 
ATOM   2476  C  CA  . ASP B  1 40  ? -10.281 -8.816  26.439  1.00 12.72 ? 40  ASP B CA  1 
ATOM   2477  C  C   . ASP B  1 40  ? -11.629 -9.374  26.236  1.00 12.98 ? 40  ASP B C   1 
ATOM   2478  O  O   . ASP B  1 40  ? -12.321 -9.120  25.228  1.00 11.95 ? 40  ASP B O   1 
ATOM   2479  C  CB  . ASP B  1 40  ? -10.156 -7.384  25.972  1.00 13.24 ? 40  ASP B CB  1 
ATOM   2480  C  CG  . ASP B  1 40  ? -10.956 -6.441  26.788  1.00 14.94 ? 40  ASP B CG  1 
ATOM   2481  O  OD1 . ASP B  1 40  ? -11.796 -6.877  27.566  1.00 16.68 ? 40  ASP B OD1 1 
ATOM   2482  O  OD2 . ASP B  1 40  ? -10.787 -5.205  26.565  1.00 19.96 ? 40  ASP B OD2 1 
ATOM   2483  N  N   . ALA B  1 41  ? -12.203 -10.036 27.268  1.00 13.14 ? 41  ALA B N   1 
ATOM   2484  C  CA  . ALA B  1 41  ? -13.548 -10.565 27.216  1.00 14.24 ? 41  ALA B CA  1 
ATOM   2485  C  C   . ALA B  1 41  ? -14.646 -9.541  27.158  1.00 13.62 ? 41  ALA B C   1 
ATOM   2486  O  O   . ALA B  1 41  ? -15.751 -9.921  26.772  1.00 16.41 ? 41  ALA B O   1 
ATOM   2487  C  CB  . ALA B  1 41  ? -13.715 -11.439 28.505  1.00 14.56 ? 41  ALA B CB  1 
ATOM   2488  N  N   . SER B  1 42  ? -14.361 -8.299  27.430  1.00 14.69 ? 42  SER B N   1 
ATOM   2489  C  CA  . SER B  1 42  ? -15.368 -7.256  27.255  1.00 15.45 ? 42  SER B CA  1 
ATOM   2490  C  C   . SER B  1 42  ? -15.628 -6.814  25.788  1.00 15.22 ? 42  SER B C   1 
ATOM   2491  O  O   . SER B  1 42  ? -16.530 -5.951  25.449  1.00 16.34 ? 42  SER B O   1 
ATOM   2492  C  CB  . SER B  1 42  ? -14.984 -5.992  28.007  1.00 20.20 ? 42  SER B CB  1 
ATOM   2493  O  OG  . SER B  1 42  ? -14.005 -5.207  27.388  1.00 22.58 ? 42  SER B OG  1 
ATOM   2494  N  N   . LEU B  1 43  ? -14.863 -7.366  24.867  1.00 11.92 ? 43  LEU B N   1 
ATOM   2495  C  CA  . LEU B  1 43  ? -15.026 -7.072  23.436  1.00 11.40 ? 43  LEU B CA  1 
ATOM   2496  C  C   . LEU B  1 43  ? -16.097 -7.927  22.885  1.00 11.24 ? 43  LEU B C   1 
ATOM   2497  O  O   . LEU B  1 43  ? -15.880 -8.961  22.240  1.00 12.97 ? 43  LEU B O   1 
ATOM   2498  C  CB  . LEU B  1 43  ? -13.711 -7.206  22.694  1.00 11.01 ? 43  LEU B CB  1 
ATOM   2499  C  CG  . LEU B  1 43  ? -12.647 -6.214  23.072  1.00 10.09 ? 43  LEU B CG  1 
ATOM   2500  C  CD1 . LEU B  1 43  ? -11.362 -6.513  22.337  1.00 12.16 ? 43  LEU B CD1 1 
ATOM   2501  C  CD2 . LEU B  1 43  ? -13.010 -4.736  22.871  1.00 11.99 ? 43  LEU B CD2 1 
ATOM   2502  N  N   . THR B  1 44  ? -17.352 -7.488  23.137  1.00 13.34 ? 44  THR B N   1 
ATOM   2503  C  CA  . THR B  1 44  ? -18.489 -8.235  22.679  1.00 13.82 ? 44  THR B CA  1 
ATOM   2504  C  C   . THR B  1 44  ? -18.866 -7.974  21.216  1.00 12.10 ? 44  THR B C   1 
ATOM   2505  O  O   . THR B  1 44  ? -18.239 -7.063  20.614  1.00 11.87 ? 44  THR B O   1 
ATOM   2506  C  CB  . THR B  1 44  ? -19.669 -7.825  23.590  1.00 15.44 ? 44  THR B CB  1 
ATOM   2507  O  OG1 . THR B  1 44  ? -19.677 -6.432  23.746  1.00 19.55 ? 44  THR B OG1 1 
ATOM   2508  C  CG2 . THR B  1 44  ? -19.419 -8.422  25.079  1.00 16.50 ? 44  THR B CG2 1 
ATOM   2509  N  N   . PRO B  1 45  ? -19.775 -8.715  20.629  1.00 12.31 ? 45  PRO B N   1 
ATOM   2510  C  CA  . PRO B  1 45  ? -19.976 -8.598  19.204  1.00 13.06 ? 45  PRO B CA  1 
ATOM   2511  C  C   . PRO B  1 45  ? -20.592 -7.257  18.775  1.00 13.62 ? 45  PRO B C   1 
ATOM   2512  O  O   . PRO B  1 45  ? -21.431 -6.703  19.515  1.00 16.60 ? 45  PRO B O   1 
ATOM   2513  C  CB  . PRO B  1 45  ? -20.938 -9.728  18.830  1.00 14.83 ? 45  PRO B CB  1 
ATOM   2514  C  CG  . PRO B  1 45  ? -20.658 -10.790 19.908  1.00 14.86 ? 45  PRO B CG  1 
ATOM   2515  C  CD  . PRO B  1 45  ? -20.385 -9.995  21.127  1.00 14.60 ? 45  PRO B CD  1 
ATOM   2516  N  N   . LEU B  1 46  ? -20.107 -6.680  17.665  1.00 11.49 ? 46  LEU B N   1 
ATOM   2517  C  CA  . LEU B  1 46  ? -20.777 -5.474  17.162  1.00 11.70 ? 46  LEU B CA  1 
ATOM   2518  C  C   . LEU B  1 46  ? -22.021 -5.926  16.370  1.00 11.59 ? 46  LEU B C   1 
ATOM   2519  O  O   . LEU B  1 46  ? -22.069 -7.032  15.858  1.00 13.02 ? 46  LEU B O   1 
ATOM   2520  C  CB  . LEU B  1 46  ? -19.857 -4.775  16.148  1.00 13.22 ? 46  LEU B CB  1 
ATOM   2521  C  CG  . LEU B  1 46  ? -18.613 -4.183  16.791  1.00 16.05 ? 46  LEU B CG  1 
ATOM   2522  C  CD1 . LEU B  1 46  ? -17.811 -3.567  15.650  1.00 15.66 ? 46  LEU B CD1 1 
ATOM   2523  C  CD2 . LEU B  1 46  ? -18.943 -3.106  17.844  1.00 19.74 ? 46  LEU B CD2 1 
ATOM   2524  N  N   . GLU B  1 47  ? -23.006 -5.033  16.294  1.00 12.84 ? 47  GLU B N   1 
ATOM   2525  C  CA  . GLU B  1 47  ? -24.130 -5.296  15.356  1.00 14.42 ? 47  GLU B CA  1 
ATOM   2526  C  C   . GLU B  1 47  ? -24.125 -4.178  14.265  1.00 12.86 ? 47  GLU B C   1 
ATOM   2527  O  O   . GLU B  1 47  ? -23.807 -2.970  14.554  1.00 16.52 ? 47  GLU B O   1 
ATOM   2528  C  CB  . GLU B  1 47  ? -25.475 -5.259  16.053  1.00 17.93 ? 47  GLU B CB  1 
ATOM   2529  C  CG  . GLU B  1 47  ? -25.600 -6.400  17.127  1.00 22.20 ? 47  GLU B CG  1 
ATOM   2530  C  CD  . GLU B  1 47  ? -26.999 -6.444  17.773  1.00 31.52 ? 47  GLU B CD  1 
ATOM   2531  O  OE1 . GLU B  1 47  ? -27.281 -5.589  18.641  1.00 43.95 ? 47  GLU B OE1 1 
ATOM   2532  O  OE2 . GLU B  1 47  ? -27.800 -7.309  17.403  1.00 44.33 ? 47  GLU B OE2 1 
ATOM   2533  N  N   . PHE B  1 48  ? -24.372 -4.649  13.073  1.00 14.54 ? 48  PHE B N   1 
ATOM   2534  C  CA  . PHE B  1 48  ? -24.321 -3.793  11.844  1.00 14.34 ? 48  PHE B CA  1 
ATOM   2535  C  C   . PHE B  1 48  ? -25.744 -3.444  11.412  1.00 14.91 ? 48  PHE B C   1 
ATOM   2536  O  O   . PHE B  1 48  ? -26.508 -4.397  11.066  1.00 18.89 ? 48  PHE B O   1 
ATOM   2537  C  CB  . PHE B  1 48  ? -23.484 -4.462  10.775  1.00 15.46 ? 48  PHE B CB  1 
ATOM   2538  C  CG  . PHE B  1 48  ? -22.203 -4.994  11.339  1.00 14.15 ? 48  PHE B CG  1 
ATOM   2539  C  CD1 . PHE B  1 48  ? -21.161 -4.172  11.683  1.00 13.75 ? 48  PHE B CD1 1 
ATOM   2540  C  CD2 . PHE B  1 48  ? -22.063 -6.390  11.552  1.00 14.75 ? 48  PHE B CD2 1 
ATOM   2541  C  CE1 . PHE B  1 48  ? -19.970 -4.716  12.311  1.00 14.48 ? 48  PHE B CE1 1 
ATOM   2542  C  CE2 . PHE B  1 48  ? -20.887 -6.895  12.129  1.00 16.25 ? 48  PHE B CE2 1 
ATOM   2543  C  CZ  . PHE B  1 48  ? -19.875 -6.068  12.473  1.00 14.63 ? 48  PHE B CZ  1 
ATOM   2544  N  N   . GLN B  1 49  ? -26.121 -2.176  11.644  1.00 13.92 ? 49  GLN B N   1 
ATOM   2545  C  CA  . GLN B  1 49  ? -27.531 -1.824  11.425  1.00 15.52 ? 49  GLN B CA  1 
ATOM   2546  C  C   . GLN B  1 49  ? -27.665 -0.932  10.213  1.00 13.00 ? 49  GLN B C   1 
ATOM   2547  O  O   . GLN B  1 49  ? -26.858 -0.024  10.050  1.00 13.26 ? 49  GLN B O   1 
ATOM   2548  C  CB  . GLN B  1 49  ? -28.043 -1.162  12.632  1.00 17.17 ? 49  GLN B CB  1 
ATOM   2549  C  CG  . GLN B  1 49  ? -28.279 -2.258  13.661  1.00 24.35 ? 49  GLN B CG  1 
ATOM   2550  C  CD  . GLN B  1 49  ? -28.397 -1.644  14.986  1.00 31.32 ? 49  GLN B CD  1 
ATOM   2551  O  OE1 . GLN B  1 49  ? -28.056 -0.460  15.167  1.00 32.44 ? 49  GLN B OE1 1 
ATOM   2552  N  NE2 . GLN B  1 49  ? -28.792 -2.448  15.958  1.00 30.33 ? 49  GLN B NE2 1 
ATOM   2553  N  N   . GLY B  1 50  ? -28.627 -1.250  9.378   1.00 15.48 ? 50  GLY B N   1 
ATOM   2554  C  CA  . GLY B  1 50  ? -28.857 -0.392  8.221   1.00 12.88 ? 50  GLY B CA  1 
ATOM   2555  C  C   . GLY B  1 50  ? -27.737 -0.542  7.207   1.00 14.26 ? 50  GLY B C   1 
ATOM   2556  O  O   . GLY B  1 50  ? -27.613 0.278   6.270   1.00 15.03 ? 50  GLY B O   1 
ATOM   2557  N  N   . TYR B  1 51  ? -27.061 -1.679  7.273   1.00 11.77 ? 51  TYR B N   1 
ATOM   2558  C  CA  . TYR B  1 51  ? -26.017 -1.965  6.268   1.00 11.32 ? 51  TYR B CA  1 
ATOM   2559  C  C   . TYR B  1 51  ? -26.595 -2.526  4.955   1.00 11.24 ? 51  TYR B C   1 
ATOM   2560  O  O   . TYR B  1 51  ? -25.970 -2.546  3.902   1.00 11.07 ? 51  TYR B O   1 
ATOM   2561  C  CB  . TYR B  1 51  ? -24.999 -3.073  6.779   1.00 11.37 ? 51  TYR B CB  1 
ATOM   2562  C  CG  . TYR B  1 51  ? -23.827 -2.493  7.531   1.00 11.22 ? 51  TYR B CG  1 
ATOM   2563  C  CD1 . TYR B  1 51  ? -23.997 -1.505  8.504   1.00 10.49 ? 51  TYR B CD1 1 
ATOM   2564  C  CD2 . TYR B  1 51  ? -22.538 -2.924  7.259   1.00 10.54 ? 51  TYR B CD2 1 
ATOM   2565  C  CE1 . TYR B  1 51  ? -22.909 -0.966  9.175   1.00 11.33 ? 51  TYR B CE1 1 
ATOM   2566  C  CE2 . TYR B  1 51  ? -21.454 -2.390  7.924   1.00 10.35 ? 51  TYR B CE2 1 
ATOM   2567  C  CZ  . TYR B  1 51  ? -21.639 -1.414  8.880   1.00 10.92 ? 51  TYR B CZ  1 
ATOM   2568  O  OH  . TYR B  1 51  ? -20.519 -0.908  9.519   1.00 11.59 ? 51  TYR B OH  1 
ATOM   2569  N  N   . ASN B  1 52  ? -27.872 -2.993  4.972   1.00 12.75 ? 52  ASN B N   1 
ATOM   2570  C  CA  . ASN B  1 52  ? -28.435 -3.548  3.775   1.00 12.03 ? 52  ASN B CA  1 
ATOM   2571  C  C   . ASN B  1 52  ? -29.092 -2.434  3.008   1.00 15.84 ? 52  ASN B C   1 
ATOM   2572  O  O   . ASN B  1 52  ? -30.249 -2.059  3.195   1.00 17.40 ? 52  ASN B O   1 
ATOM   2573  C  CB  . ASN B  1 52  ? -29.539 -4.604  4.163   1.00 14.07 ? 52  ASN B CB  1 
ATOM   2574  C  CG  . ASN B  1 52  ? -30.103 -5.295  2.977   1.00 19.25 ? 52  ASN B CG  1 
ATOM   2575  O  OD1 . ASN B  1 52  ? -29.650 -5.238  1.826   1.00 25.95 ? 52  ASN B OD1 1 
ATOM   2576  N  ND2 . ASN B  1 52  ? -31.193 -6.059  3.274   1.00 23.26 ? 52  ASN B ND2 1 
ATOM   2577  N  N   . LEU B  1 53  ? -28.288 -1.808  2.174   1.00 13.23 ? 53  LEU B N   1 
ATOM   2578  C  CA  . LEU B  1 53  ? -28.735 -0.602  1.469   1.00 12.19 ? 53  LEU B CA  1 
ATOM   2579  C  C   . LEU B  1 53  ? -29.699 -1.063  0.296   1.00 11.15 ? 53  LEU B C   1 
ATOM   2580  O  O   . LEU B  1 53  ? -29.438 -2.008  -0.437  1.00 12.71 ? 53  LEU B O   1 
ATOM   2581  C  CB  . LEU B  1 53  ? -27.517 0.108   0.830   1.00 12.16 ? 53  LEU B CB  1 
ATOM   2582  C  CG  . LEU B  1 53  ? -26.433 0.538   1.850   1.00 13.88 ? 53  LEU B CG  1 
ATOM   2583  C  CD1 . LEU B  1 53  ? -25.289 1.218   1.050   1.00 15.24 ? 53  LEU B CD1 1 
ATOM   2584  C  CD2 . LEU B  1 53  ? -27.002 1.375   2.968   1.00 13.83 ? 53  LEU B CD2 1 
ATOM   2585  N  N   . SER B  1 54  ? -30.747 -0.246  0.098   1.00 11.55 ? 54  SER B N   1 
ATOM   2586  C  CA  . SER B  1 54  ? -31.721 -0.611  -0.898  1.00 11.95 ? 54  SER B CA  1 
ATOM   2587  C  C   . SER B  1 54  ? -31.078 -0.615  -2.300  1.00 11.73 ? 54  SER B C   1 
ATOM   2588  O  O   . SER B  1 54  ? -30.492 0.423   -2.692  1.00 11.57 ? 54  SER B O   1 
ATOM   2589  C  CB  . SER B  1 54  ? -32.860 0.378   -0.856  1.00 12.92 ? 54  SER B CB  1 
ATOM   2590  O  OG  . SER B  1 54  ? -33.725 0.052   -1.936  1.00 13.96 ? 54  SER B OG  1 
ATOM   2591  N  N   . ALA B  1 55  ? -31.324 -1.645  -3.105  1.00 13.12 ? 55  ALA B N   1 
ATOM   2592  C  CA  . ALA B  1 55  ? -30.849 -1.685  -4.491  1.00 12.94 ? 55  ALA B CA  1 
ATOM   2593  C  C   . ALA B  1 55  ? -31.534 -0.682  -5.383  1.00 10.52 ? 55  ALA B C   1 
ATOM   2594  O  O   . ALA B  1 55  ? -31.068 -0.414  -6.485  1.00 13.78 ? 55  ALA B O   1 
ATOM   2595  C  CB  . ALA B  1 55  ? -30.979 -3.109  -5.118  1.00 16.83 ? 55  ALA B CB  1 
ATOM   2596  N  N   . ASN B  1 56  ? -32.611 -0.058  -4.913  1.00 12.55 ? 56  ASN B N   1 
ATOM   2597  C  CA  . ASN B  1 56  ? -33.298 0.950   -5.735  1.00 12.57 ? 56  ASN B CA  1 
ATOM   2598  C  C   . ASN B  1 56  ? -32.773 2.317   -5.408  1.00 13.40 ? 56  ASN B C   1 
ATOM   2599  O  O   . ASN B  1 56  ? -33.124 3.286   -6.080  1.00 15.09 ? 56  ASN B O   1 
ATOM   2600  C  CB  . ASN B  1 56  ? -34.833 0.941   -5.482  1.00 13.71 ? 56  ASN B CB  1 
ATOM   2601  C  CG  . ASN B  1 56  ? -35.460 -0.327  -5.937  1.00 16.57 ? 56  ASN B CG  1 
ATOM   2602  O  OD1 . ASN B  1 56  ? -34.913 -1.142  -6.682  1.00 17.25 ? 56  ASN B OD1 1 
ATOM   2603  N  ND2 . ASN B  1 56  ? -36.657 -0.492  -5.500  1.00 18.89 ? 56  ASN B ND2 1 
ATOM   2604  N  N   . LYS B  1 57  ? -31.940 2.450   -4.399  1.00 11.66 ? 57  LYS B N   1 
ATOM   2605  C  CA  . LYS B  1 57  ? -31.216 3.682   -4.115  1.00 11.66 ? 57  LYS B CA  1 
ATOM   2606  C  C   . LYS B  1 57  ? -29.799 3.582   -4.693  1.00 10.85 ? 57  LYS B C   1 
ATOM   2607  O  O   . LYS B  1 57  ? -29.358 2.520   -5.148  1.00 11.75 ? 57  LYS B O   1 
ATOM   2608  C  CB  . LYS B  1 57  ? -31.121 3.894   -2.575  1.00 11.07 ? 57  LYS B CB  1 
ATOM   2609  C  CG  . LYS B  1 57  ? -32.481 4.363   -2.004  1.00 14.54 ? 57  LYS B CG  1 
ATOM   2610  C  CD  . LYS B  1 57  ? -32.382 4.415   -0.475  1.00 21.62 ? 57  LYS B CD  1 
ATOM   2611  C  CE  . LYS B  1 57  ? -33.196 5.551   0.105   1.00 28.33 ? 57  LYS B CE  1 
ATOM   2612  N  NZ  . LYS B  1 57  ? -33.127 5.545   1.622   1.00 29.65 ? 57  LYS B NZ  1 
ATOM   2613  N  N   . GLN B  1 58  ? -29.109 4.696   -4.729  1.00 11.33 ? 58  GLN B N   1 
ATOM   2614  C  CA  . GLN B  1 58  ? -27.774 4.732   -5.310  1.00 11.21 ? 58  GLN B CA  1 
ATOM   2615  C  C   . GLN B  1 58  ? -26.906 5.654   -4.472  1.00 10.37 ? 58  GLN B C   1 
ATOM   2616  O  O   . GLN B  1 58  ? -27.314 6.601   -3.827  1.00 11.55 ? 58  GLN B O   1 
ATOM   2617  C  CB  . GLN B  1 58  ? -27.766 5.048   -6.785  1.00 15.75 ? 58  GLN B CB  1 
ATOM   2618  C  CG  . GLN B  1 58  ? -28.233 6.410   -7.001  1.00 14.41 ? 58  GLN B CG  1 
ATOM   2619  C  CD  . GLN B  1 58  ? -28.619 6.590   -8.489  1.00 19.00 ? 58  GLN B CD  1 
ATOM   2620  O  OE1 . GLN B  1 58  ? -28.450 5.723   -9.385  1.00 20.73 ? 58  GLN B OE1 1 
ATOM   2621  N  NE2 . GLN B  1 58  ? -29.140 7.809   -8.761  1.00 21.64 ? 58  GLN B NE2 1 
ATOM   2622  N  N   . PHE B  1 59  ? -25.609 5.246   -4.439  1.00 9.48  ? 59  PHE B N   1 
ATOM   2623  C  CA  . PHE B  1 59  ? -24.618 5.815   -3.542  1.00 8.65  ? 59  PHE B CA  1 
ATOM   2624  C  C   . PHE B  1 59  ? -23.397 6.281   -4.324  1.00 8.78  ? 59  PHE B C   1 
ATOM   2625  O  O   . PHE B  1 59  ? -22.965 5.597   -5.263  1.00 9.38  ? 59  PHE B O   1 
ATOM   2626  C  CB  . PHE B  1 59  ? -24.284 4.714   -2.506  1.00 10.20 ? 59  PHE B CB  1 
ATOM   2627  C  CG  . PHE B  1 59  ? -25.504 4.361   -1.700  1.00 10.48 ? 59  PHE B CG  1 
ATOM   2628  C  CD1 . PHE B  1 59  ? -26.412 3.361   -2.181  1.00 10.90 ? 59  PHE B CD1 1 
ATOM   2629  C  CD2 . PHE B  1 59  ? -25.805 5.101   -0.569  1.00 11.59 ? 59  PHE B CD2 1 
ATOM   2630  C  CE1 . PHE B  1 59  ? -27.622 3.194   -1.487  1.00 11.19 ? 59  PHE B CE1 1 
ATOM   2631  C  CE2 . PHE B  1 59  ? -27.054 4.882   0.117   1.00 11.78 ? 59  PHE B CE2 1 
ATOM   2632  C  CZ  . PHE B  1 59  ? -27.899 3.903   -0.365  1.00 11.07 ? 59  PHE B CZ  1 
ATOM   2633  N  N   . LEU B  1 60  ? -22.869 7.419   -3.907  1.00 8.92  ? 60  LEU B N   1 
ATOM   2634  C  CA  . LEU B  1 60  ? -21.820 8.043   -4.709  1.00 8.97  ? 60  LEU B CA  1 
ATOM   2635  C  C   . LEU B  1 60  ? -20.438 7.449   -4.487  1.00 8.16  ? 60  LEU B C   1 
ATOM   2636  O  O   . LEU B  1 60  ? -19.952 7.431   -3.376  1.00 9.87  ? 60  LEU B O   1 
ATOM   2637  C  CB  . LEU B  1 60  ? -21.759 9.530   -4.327  1.00 11.20 ? 60  LEU B CB  1 
ATOM   2638  C  CG  . LEU B  1 60  ? -20.908 10.420  -5.227  1.00 14.46 ? 60  LEU B CG  1 
ATOM   2639  C  CD1 . LEU B  1 60  ? -21.707 10.613  -6.467  1.00 16.48 ? 60  LEU B CD1 1 
ATOM   2640  C  CD2 . LEU B  1 60  ? -20.740 11.772  -4.486  1.00 17.59 ? 60  LEU B CD2 1 
ATOM   2641  N  N   . LEU B  1 61  ? -19.867 7.013   -5.584  1.00 8.77  ? 61  LEU B N   1 
ATOM   2642  C  CA  . LEU B  1 61  ? -18.476 6.506   -5.660  1.00 7.98  ? 61  LEU B CA  1 
ATOM   2643  C  C   . LEU B  1 61  ? -17.568 7.575   -6.240  1.00 9.80  ? 61  LEU B C   1 
ATOM   2644  O  O   . LEU B  1 61  ? -17.949 8.175   -7.215  1.00 12.42 ? 61  LEU B O   1 
ATOM   2645  C  CB  . LEU B  1 61  ? -18.442 5.285   -6.551  1.00 9.90  ? 61  LEU B CB  1 
ATOM   2646  C  CG  . LEU B  1 61  ? -17.171 4.460   -6.612  1.00 10.50 ? 61  LEU B CG  1 
ATOM   2647  C  CD1 . LEU B  1 61  ? -17.006 3.711   -5.285  1.00 11.81 ? 61  LEU B CD1 1 
ATOM   2648  C  CD2 . LEU B  1 61  ? -17.157 3.476   -7.813  1.00 11.89 ? 61  LEU B CD2 1 
ATOM   2649  N  N   . THR B  1 62  ? -16.468 7.874   -5.606  1.00 9.73  ? 62  THR B N   1 
ATOM   2650  C  CA  . THR B  1 62  ? -15.632 9.018   -6.024  1.00 10.40 ? 62  THR B CA  1 
ATOM   2651  C  C   . THR B  1 62  ? -14.168 8.566   -5.982  1.00 9.84  ? 62  THR B C   1 
ATOM   2652  O  O   . THR B  1 62  ? -13.713 7.892   -5.042  1.00 11.00 ? 62  THR B O   1 
ATOM   2653  C  CB  . THR B  1 62  ? -15.712 10.177  -5.044  1.00 13.32 ? 62  THR B CB  1 
ATOM   2654  O  OG1 . THR B  1 62  ? -17.085 10.627  -4.812  1.00 17.18 ? 62  THR B OG1 1 
ATOM   2655  C  CG2 . THR B  1 62  ? -14.894 11.412  -5.516  1.00 16.62 ? 62  THR B CG2 1 
ATOM   2656  N  N   . ASN B  1 63  ? -13.380 8.968   -6.938  1.00 8.72  ? 63  ASN B N   1 
ATOM   2657  C  CA  . ASN B  1 63  ? -11.923 8.902   -6.870  1.00 9.10  ? 63  ASN B CA  1 
ATOM   2658  C  C   . ASN B  1 63  ? -11.467 10.175  -6.277  1.00 9.33  ? 63  ASN B C   1 
ATOM   2659  O  O   . ASN B  1 63  ? -11.663 11.277  -6.832  1.00 8.68  ? 63  ASN B O   1 
ATOM   2660  C  CB  . ASN B  1 63  ? -11.417 8.752   -8.321  1.00 9.45  ? 63  ASN B CB  1 
ATOM   2661  C  CG  . ASN B  1 63  ? -9.920  8.773   -8.442  1.00 9.51  ? 63  ASN B CG  1 
ATOM   2662  O  OD1 . ASN B  1 63  ? -9.223  9.370   -7.618  1.00 9.12  ? 63  ASN B OD1 1 
ATOM   2663  N  ND2 . ASN B  1 63  ? -9.409  8.073   -9.474  1.00 9.12  ? 63  ASN B ND2 1 
ATOM   2664  N  N   . ASN B  1 64  ? -10.880 10.118  -5.078  1.00 9.40  ? 64  ASN B N   1 
ATOM   2665  C  CA  . ASN B  1 64  ? -10.444 11.366  -4.361  1.00 10.01 ? 64  ASN B CA  1 
ATOM   2666  C  C   . ASN B  1 64  ? -8.960  11.693  -4.546  1.00 10.12 ? 64  ASN B C   1 
ATOM   2667  O  O   . ASN B  1 64  ? -8.437  12.577  -3.897  1.00 11.51 ? 64  ASN B O   1 
ATOM   2668  C  CB  . ASN B  1 64  ? -10.839 11.303  -2.864  1.00 10.66 ? 64  ASN B CB  1 
ATOM   2669  C  CG  . ASN B  1 64  ? -10.080 10.224  -2.147  1.00 12.17 ? 64  ASN B CG  1 
ATOM   2670  O  OD1 . ASN B  1 64  ? -9.119  9.636   -2.686  1.00 10.62 ? 64  ASN B OD1 1 
ATOM   2671  N  ND2 . ASN B  1 64  ? -10.517 9.874   -0.897  1.00 14.85 ? 64  ASN B ND2 1 
ATOM   2672  N  N   . GLY B  1 65  ? -8.345  11.020  -5.501  1.00 8.34  ? 65  GLY B N   1 
ATOM   2673  C  CA  . GLY B  1 65  ? -6.910  11.252  -5.771  1.00 10.08 ? 65  GLY B CA  1 
ATOM   2674  C  C   . GLY B  1 65  ? -6.016  10.348  -4.919  1.00 9.20  ? 65  GLY B C   1 
ATOM   2675  O  O   . GLY B  1 65  ? -4.837  10.279  -5.205  1.00 9.54  ? 65  GLY B O   1 
ATOM   2676  N  N   . HIS B  1 66  ? -6.581  9.634   -3.933  1.00 9.28  ? 66  HIS B N   1 
ATOM   2677  C  CA  . HIS B  1 66  ? -5.767  8.766   -3.041  1.00 8.99  ? 66  HIS B CA  1 
ATOM   2678  C  C   . HIS B  1 66  ? -6.346  7.383   -2.889  1.00 9.48  ? 66  HIS B C   1 
ATOM   2679  O  O   . HIS B  1 66  ? -5.573  6.445   -2.512  1.00 9.64  ? 66  HIS B O   1 
ATOM   2680  C  CB  . HIS B  1 66  ? -5.689  9.425   -1.665  1.00 9.76  ? 66  HIS B CB  1 
ATOM   2681  C  CG  . HIS B  1 66  ? -5.141  10.802  -1.701  1.00 9.25  ? 66  HIS B CG  1 
ATOM   2682  N  ND1 . HIS B  1 66  ? -3.799  11.036  -1.884  1.00 9.98  ? 66  HIS B ND1 1 
ATOM   2683  C  CD2 . HIS B  1 66  ? -5.733  11.977  -1.529  1.00 9.57  ? 66  HIS B CD2 1 
ATOM   2684  C  CE1 . HIS B  1 66  ? -3.608  12.362  -1.879  1.00 9.76  ? 66  HIS B CE1 1 
ATOM   2685  N  NE2 . HIS B  1 66  ? -4.780  12.928  -1.613  1.00 11.47 ? 66  HIS B NE2 1 
ATOM   2686  N  N   . SER B  1 67  ? -7.664  7.221   -3.080  1.00 8.48  ? 67  SER B N   1 
ATOM   2687  C  CA  . SER B  1 67  ? -8.337  5.903   -3.036  1.00 8.31  ? 67  SER B CA  1 
ATOM   2688  C  C   . SER B  1 67  ? -9.611  6.062   -3.836  1.00 8.50  ? 67  SER B C   1 
ATOM   2689  O  O   . SER B  1 67  ? -9.837  7.126   -4.445  1.00 8.93  ? 67  SER B O   1 
ATOM   2690  C  CB  . SER B  1 67  ? -8.696  5.607   -1.562  1.00 9.46  ? 67  SER B CB  1 
ATOM   2691  O  OG  . SER B  1 67  ? -9.223  4.272   -1.463  1.00 9.87  ? 67  SER B OG  1 
ATOM   2692  N  N   . VAL B  1 68  ? -10.380 4.989   -3.869  1.00 8.98  ? 68  VAL B N   1 
ATOM   2693  C  CA  . VAL B  1 68  ? -11.733 5.094   -4.398  1.00 9.27  ? 68  VAL B CA  1 
ATOM   2694  C  C   . VAL B  1 68  ? -12.629 4.931   -3.136  1.00 8.84  ? 68  VAL B C   1 
ATOM   2695  O  O   . VAL B  1 68  ? -12.418 4.037   -2.323  1.00 9.47  ? 68  VAL B O   1 
ATOM   2696  C  CB  . VAL B  1 68  ? -11.973 4.007   -5.450  1.00 9.68  ? 68  VAL B CB  1 
ATOM   2697  C  CG1 . VAL B  1 68  ? -11.704 2.585   -4.979  1.00 11.73 ? 68  VAL B CG1 1 
ATOM   2698  C  CG2 . VAL B  1 68  ? -13.370 4.146   -6.065  1.00 13.11 ? 68  VAL B CG2 1 
ATOM   2699  N  N   . LYS B  1 69  ? -13.578 5.845   -3.017  1.00 8.91  ? 69  LYS B N   1 
ATOM   2700  C  CA  . LYS B  1 69  ? -14.482 5.890   -1.831  1.00 9.87  ? 69  LYS B CA  1 
ATOM   2701  C  C   . LYS B  1 69  ? -15.925 5.801   -2.247  1.00 9.24  ? 69  LYS B C   1 
ATOM   2702  O  O   . LYS B  1 69  ? -16.329 6.345   -3.244  1.00 10.63 ? 69  LYS B O   1 
ATOM   2703  C  CB  . LYS B  1 69  ? -14.118 7.051   -1.013  1.00 15.41 ? 69  LYS B CB  1 
ATOM   2704  C  CG  . LYS B  1 69  ? -14.602 8.372   -1.459  1.00 16.73 ? 69  LYS B CG  1 
ATOM   2705  C  CD  . LYS B  1 69  ? -14.719 9.350   -0.223  1.00 16.87 ? 69  LYS B CD  1 
ATOM   2706  C  CE  . LYS B  1 69  ? -14.919 10.653  -0.894  1.00 20.46 ? 69  LYS B CE  1 
ATOM   2707  N  NZ  . LYS B  1 69  ? -14.757 11.671  0.206   1.00 20.42 ? 69  LYS B NZ  1 
ATOM   2708  N  N   . LEU B  1 70  ? -16.704 5.075   -1.455  1.00 8.49  ? 70  LEU B N   1 
ATOM   2709  C  CA  . LEU B  1 70  ? -18.152 5.037   -1.576  1.00 8.84  ? 70  LEU B CA  1 
ATOM   2710  C  C   . LEU B  1 70  ? -18.746 5.782   -0.399  1.00 8.85  ? 70  LEU B C   1 
ATOM   2711  O  O   . LEU B  1 70  ? -18.529 5.406   0.762   1.00 9.57  ? 70  LEU B O   1 
ATOM   2712  C  CB  . LEU B  1 70  ? -18.577 3.570   -1.601  1.00 9.54  ? 70  LEU B CB  1 
ATOM   2713  C  CG  . LEU B  1 70  ? -20.123 3.347   -1.793  1.00 9.35  ? 70  LEU B CG  1 
ATOM   2714  C  CD1 . LEU B  1 70  ? -20.549 3.786   -3.188  1.00 11.16 ? 70  LEU B CD1 1 
ATOM   2715  C  CD2 . LEU B  1 70  ? -20.461 1.863   -1.577  1.00 11.07 ? 70  LEU B CD2 1 
ATOM   2716  N  N   . ASN B  1 71  ? -19.596 6.800   -0.641  1.00 9.88  ? 71  ASN B N   1 
ATOM   2717  C  CA  . ASN B  1 71  ? -20.312 7.486   0.496   1.00 9.66  ? 71  ASN B CA  1 
ATOM   2718  C  C   . ASN B  1 71  ? -21.454 6.595   0.974   1.00 10.15 ? 71  ASN B C   1 
ATOM   2719  O  O   . ASN B  1 71  ? -22.075 5.841   0.191   1.00 11.67 ? 71  ASN B O   1 
ATOM   2720  C  CB  . ASN B  1 71  ? -20.910 8.835   -0.050  1.00 11.79 ? 71  ASN B CB  1 
ATOM   2721  C  CG  . ASN B  1 71  ? -19.886 9.890   -0.293  1.00 14.35 ? 71  ASN B CG  1 
ATOM   2722  O  OD1 . ASN B  1 71  ? -18.721 9.783   -0.069  1.00 16.92 ? 71  ASN B OD1 1 
ATOM   2723  N  ND2 . ASN B  1 71  ? -20.445 11.060  -0.680  1.00 18.80 ? 71  ASN B ND2 1 
ATOM   2724  N  N   . LEU B  1 72  ? -21.604 6.641   2.278   1.00 9.79  ? 72  LEU B N   1 
ATOM   2725  C  CA  . LEU B  1 72  ? -22.574 5.808   2.911   1.00 10.06 ? 72  LEU B CA  1 
ATOM   2726  C  C   . LEU B  1 72  ? -23.549 6.725   3.707   1.00 10.71 ? 72  LEU B C   1 
ATOM   2727  O  O   . LEU B  1 72  ? -23.186 7.812   4.144   1.00 11.91 ? 72  LEU B O   1 
ATOM   2728  C  CB  . LEU B  1 72  ? -21.792 4.841   3.866   1.00 9.40  ? 72  LEU B CB  1 
ATOM   2729  C  CG  . LEU B  1 72  ? -20.909 3.832   3.165   1.00 10.08 ? 72  LEU B CG  1 
ATOM   2730  C  CD1 . LEU B  1 72  ? -19.986 3.172   4.268   1.00 9.99  ? 72  LEU B CD1 1 
ATOM   2731  C  CD2 . LEU B  1 72  ? -21.675 2.848   2.369   1.00 10.63 ? 72  LEU B CD2 1 
ATOM   2732  N  N   . PRO B  1 73  ? -24.747 6.184   3.911   1.00 11.05 ? 73  PRO B N   1 
ATOM   2733  C  CA  . PRO B  1 73  ? -25.790 7.020   4.557   1.00 12.02 ? 73  PRO B CA  1 
ATOM   2734  C  C   . PRO B  1 73  ? -25.675 6.974   6.075   1.00 14.17 ? 73  PRO B C   1 
ATOM   2735  O  O   . PRO B  1 73  ? -25.198 5.969   6.631   1.00 14.77 ? 73  PRO B O   1 
ATOM   2736  C  CB  . PRO B  1 73  ? -27.038 6.333   4.057   1.00 12.50 ? 73  PRO B CB  1 
ATOM   2737  C  CG  . PRO B  1 73  ? -26.675 4.857   3.952   1.00 11.35 ? 73  PRO B CG  1 
ATOM   2738  C  CD  . PRO B  1 73  ? -25.314 4.963   3.368   1.00 10.82 ? 73  PRO B CD  1 
ATOM   2739  N  N   . SER B  1 74  ? -26.096 8.057   6.727   1.00 18.12 ? 74  SER B N   1 
ATOM   2740  C  CA  . SER B  1 74  ? -25.887 8.100   8.199   1.00 17.76 ? 74  SER B CA  1 
ATOM   2741  C  C   . SER B  1 74  ? -26.896 7.224   8.941   1.00 16.20 ? 74  SER B C   1 
ATOM   2742  O  O   . SER B  1 74  ? -26.652 7.042   10.139  1.00 19.85 ? 74  SER B O   1 
ATOM   2743  C  CB  . SER B  1 74  ? -25.979 9.537   8.717   1.00 22.48 ? 74  SER B CB  1 
ATOM   2744  O  OG  . SER B  1 74  ? -27.250 10.059  8.314   1.00 25.67 ? 74  SER B OG  1 
ATOM   2745  N  N   . ASP B  1 75  ? -27.831 6.610   8.244   1.00 17.00 ? 75  ASP B N   1 
ATOM   2746  C  CA  . ASP B  1 75  ? -28.826 5.668   8.882   1.00 18.38 ? 75  ASP B CA  1 
ATOM   2747  C  C   . ASP B  1 75  ? -28.044 4.266   9.099   1.00 16.67 ? 75  ASP B C   1 
ATOM   2748  O  O   . ASP B  1 75  ? -28.581 3.343   9.708   1.00 19.83 ? 75  ASP B O   1 
ATOM   2749  C  CB  . ASP B  1 75  ? -30.233 5.497   8.228   1.00 21.77 ? 75  ASP B CB  1 
ATOM   2750  C  CG  . ASP B  1 75  ? -30.230 5.216   6.713   1.00 32.33 ? 75  ASP B CG  1 
ATOM   2751  O  OD1 . ASP B  1 75  ? -29.164 5.045   6.077   1.00 31.07 ? 75  ASP B OD1 1 
ATOM   2752  O  OD2 . ASP B  1 75  ? -31.360 5.252   6.146   1.00 42.02 ? 75  ASP B OD2 1 
ATOM   2753  N  N   . MET B  1 76  ? -26.878 4.108   8.465   1.00 14.43 ? 76  MET B N   1 
ATOM   2754  C  CA  . MET B  1 76  ? -26.071 2.903   8.618   1.00 14.07 ? 76  MET B CA  1 
ATOM   2755  C  C   . MET B  1 76  ? -25.222 3.097   9.885   1.00 13.59 ? 76  MET B C   1 
ATOM   2756  O  O   . MET B  1 76  ? -24.529 4.173   10.055  1.00 13.21 ? 76  MET B O   1 
ATOM   2757  C  CB  . MET B  1 76  ? -25.243 2.809   7.336   1.00 15.92 ? 76  MET B CB  1 
ATOM   2758  C  CG  . MET B  1 76  ? -24.329 1.691   7.373   1.00 17.49 ? 76  MET B CG  1 
ATOM   2759  S  SD  . MET B  1 76  ? -23.691 1.595   5.619   1.00 15.24 ? 76  MET B SD  1 
ATOM   2760  C  CE  . MET B  1 76  ? -22.295 0.651   6.076   1.00 15.16 ? 76  MET B CE  1 
ATOM   2761  N  N   . HIS B  1 77  ? -25.261 2.153   10.870  1.00 13.33 ? 77  HIS B N   1 
ATOM   2762  C  CA  . HIS B  1 77  ? -24.475 2.399   12.093  1.00 14.25 ? 77  HIS B CA  1 
ATOM   2763  C  C   . HIS B  1 77  ? -24.013 1.129   12.691  1.00 12.96 ? 77  HIS B C   1 
ATOM   2764  O  O   . HIS B  1 77  ? -24.425 0.068   12.298  1.00 13.48 ? 77  HIS B O   1 
ATOM   2765  C  CB  . HIS B  1 77  ? -25.192 3.270   13.139  1.00 21.46 ? 77  HIS B CB  1 
ATOM   2766  C  CG  . HIS B  1 77  ? -26.533 2.795   13.446  1.00 25.95 ? 77  HIS B CG  1 
ATOM   2767  N  ND1 . HIS B  1 77  ? -27.625 3.106   12.660  1.00 27.16 ? 77  HIS B ND1 1 
ATOM   2768  C  CD2 . HIS B  1 77  ? -27.014 2.106   14.515  1.00 35.08 ? 77  HIS B CD2 1 
ATOM   2769  C  CE1 . HIS B  1 77  ? -28.703 2.533   13.172  1.00 32.50 ? 77  HIS B CE1 1 
ATOM   2770  N  NE2 . HIS B  1 77  ? -28.363 1.926   14.294  1.00 32.91 ? 77  HIS B NE2 1 
ATOM   2771  N  N   . ILE B  1 78  ? -23.065 1.338   13.539  1.00 12.22 ? 78  ILE B N   1 
ATOM   2772  C  CA  . ILE B  1 78  ? -22.624 0.178   14.373  1.00 14.12 ? 78  ILE B CA  1 
ATOM   2773  C  C   . ILE B  1 78  ? -23.260 0.333   15.719  1.00 14.83 ? 78  ILE B C   1 
ATOM   2774  O  O   . ILE B  1 78  ? -23.264 1.473   16.275  1.00 15.62 ? 78  ILE B O   1 
ATOM   2775  C  CB  . ILE B  1 78  ? -21.079 0.241   14.565  1.00 16.74 ? 78  ILE B CB  1 
ATOM   2776  C  CG1 . ILE B  1 78  ? -20.155 0.124   13.350  1.00 23.31 ? 78  ILE B CG1 1 
ATOM   2777  C  CG2 . ILE B  1 78  ? -20.647 -0.836  15.623  1.00 19.68 ? 78  ILE B CG2 1 
ATOM   2778  C  CD1 . ILE B  1 78  ? -18.728 0.665   13.731  1.00 18.33 ? 78  ILE B CD1 1 
ATOM   2779  N  N   . GLN B  1 79  ? -23.750 -0.783  16.259  1.00 15.25 ? 79  GLN B N   1 
ATOM   2780  C  CA  . GLN B  1 79  ? -24.262 -0.834  17.653  1.00 17.50 ? 79  GLN B CA  1 
ATOM   2781  C  C   . GLN B  1 79  ? -23.268 -1.723  18.425  1.00 16.15 ? 79  GLN B C   1 
ATOM   2782  O  O   . GLN B  1 79  ? -22.846 -2.772  17.936  1.00 15.33 ? 79  GLN B O   1 
ATOM   2783  C  CB  . GLN B  1 79  ? -25.653 -1.464  17.677  1.00 19.26 ? 79  GLN B CB  1 
ATOM   2784  C  CG  . GLN B  1 79  ? -26.295 -1.304  19.104  1.00 25.89 ? 79  GLN B CG  1 
ATOM   2785  C  CD  . GLN B  1 79  ? -27.635 -1.961  19.170  1.00 30.43 ? 79  GLN B CD  1 
ATOM   2786  O  OE1 . GLN B  1 79  ? -28.635 -1.319  18.829  1.00 35.11 ? 79  GLN B OE1 1 
ATOM   2787  N  NE2 . GLN B  1 79  ? -27.686 -3.237  19.566  1.00 29.46 ? 79  GLN B NE2 1 
ATOM   2788  N  N   . GLY B  1 80  ? -22.951 -1.276  19.614  1.00 17.34 ? 80  GLY B N   1 
ATOM   2789  C  CA  . GLY B  1 80  ? -22.151 -2.132  20.554  1.00 16.29 ? 80  GLY B CA  1 
ATOM   2790  C  C   . GLY B  1 80  ? -20.998 -1.395  21.078  1.00 17.62 ? 80  GLY B C   1 
ATOM   2791  O  O   . GLY B  1 80  ? -20.446 -1.799  22.146  1.00 17.17 ? 80  GLY B O   1 
ATOM   2792  N  N   . LEU B  1 81  ? -20.638 -0.238  20.493  1.00 16.48 ? 81  LEU B N   1 
ATOM   2793  C  CA  . LEU B  1 81  ? -19.684 0.654   21.132  1.00 15.49 ? 81  LEU B CA  1 
ATOM   2794  C  C   . LEU B  1 81  ? -20.362 1.547   22.171  1.00 17.22 ? 81  LEU B C   1 
ATOM   2795  O  O   . LEU B  1 81  ? -21.593 1.435   22.397  1.00 18.07 ? 81  LEU B O   1 
ATOM   2796  C  CB  . LEU B  1 81  ? -18.867 1.473   20.117  1.00 16.41 ? 81  LEU B CB  1 
ATOM   2797  C  CG  . LEU B  1 81  ? -18.157 0.625   19.062  1.00 16.69 ? 81  LEU B CG  1 
ATOM   2798  C  CD1 . LEU B  1 81  ? -17.732 1.512   17.896  1.00 17.07 ? 81  LEU B CD1 1 
ATOM   2799  C  CD2 . LEU B  1 81  ? -16.941 -0.001  19.737  1.00 18.21 ? 81  LEU B CD2 1 
ATOM   2800  N  N   . GLN B  1 82  ? -19.612 2.401   22.833  1.00 17.79 ? 82  GLN B N   1 
ATOM   2801  C  CA  . GLN B  1 82  ? -20.271 3.176   23.919  1.00 22.22 ? 82  GLN B CA  1 
ATOM   2802  C  C   . GLN B  1 82  ? -21.071 4.380   23.447  1.00 22.77 ? 82  GLN B C   1 
ATOM   2803  O  O   . GLN B  1 82  ? -21.739 5.022   24.289  1.00 22.59 ? 82  GLN B O   1 
ATOM   2804  C  CB  . GLN B  1 82  ? -19.239 3.628   24.945  1.00 21.31 ? 82  GLN B CB  1 
ATOM   2805  C  CG  . GLN B  1 82  ? -18.686 2.463   25.768  1.00 26.97 ? 82  GLN B CG  1 
ATOM   2806  C  CD  . GLN B  1 82  ? -17.538 2.916   26.654  1.00 30.75 ? 82  GLN B CD  1 
ATOM   2807  O  OE1 . GLN B  1 82  ? -17.665 3.029   27.918  1.00 28.13 ? 82  GLN B OE1 1 
ATOM   2808  N  NE2 . GLN B  1 82  ? -16.428 3.280   25.997  1.00 23.05 ? 82  GLN B NE2 1 
ATOM   2809  N  N   . SER B  1 83  ? -20.992 4.681   22.137  1.00 19.68 ? 83  SER B N   1 
ATOM   2810  C  CA  . SER B  1 83  ? -21.874 5.631   21.420  1.00 17.17 ? 83  SER B CA  1 
ATOM   2811  C  C   . SER B  1 83  ? -22.274 4.933   20.130  1.00 17.74 ? 83  SER B C   1 
ATOM   2812  O  O   . SER B  1 83  ? -21.622 3.956   19.729  1.00 15.87 ? 83  SER B O   1 
ATOM   2813  C  CB  . SER B  1 83  ? -21.164 6.927   21.088  1.00 19.53 ? 83  SER B CB  1 
ATOM   2814  O  OG  . SER B  1 83  ? -20.872 7.692   22.265  1.00 23.78 ? 83  SER B OG  1 
ATOM   2815  N  N   A ARG B  1 84  ? -23.273 5.529   19.482  0.50 17.21 ? 84  ARG B N   1 
ATOM   2816  N  N   B ARG B  1 84  ? -23.382 5.322   19.501  0.50 16.29 ? 84  ARG B N   1 
ATOM   2817  C  CA  A ARG B  1 84  ? -23.611 5.188   18.138  0.50 17.31 ? 84  ARG B CA  1 
ATOM   2818  C  CA  B ARG B  1 84  ? -23.672 4.808   18.176  0.50 15.22 ? 84  ARG B CA  1 
ATOM   2819  C  C   A ARG B  1 84  ? -22.535 5.755   17.195  0.50 16.36 ? 84  ARG B C   1 
ATOM   2820  C  C   B ARG B  1 84  ? -22.737 5.604   17.212  0.50 16.32 ? 84  ARG B C   1 
ATOM   2821  O  O   A ARG B  1 84  ? -22.075 6.925   17.275  0.50 16.20 ? 84  ARG B O   1 
ATOM   2822  O  O   B ARG B  1 84  ? -22.552 6.790   17.329  0.50 15.71 ? 84  ARG B O   1 
ATOM   2823  C  CB  A ARG B  1 84  ? -25.015 5.714   17.789  0.50 18.31 ? 84  ARG B CB  1 
ATOM   2824  C  CB  B ARG B  1 84  ? -25.163 5.030   17.815  0.50 15.48 ? 84  ARG B CB  1 
ATOM   2825  C  CG  A ARG B  1 84  ? -25.474 5.202   16.417  0.50 23.93 ? 84  ARG B CG  1 
ATOM   2826  C  CG  B ARG B  1 84  ? -25.212 5.677   16.403  0.50 19.10 ? 84  ARG B CG  1 
ATOM   2827  C  CD  A ARG B  1 84  ? -26.713 5.936   15.951  0.50 22.17 ? 84  ARG B CD  1 
ATOM   2828  C  CD  B ARG B  1 84  ? -26.603 5.996   15.896  0.50 18.64 ? 84  ARG B CD  1 
ATOM   2829  N  NE  A ARG B  1 84  ? -26.722 6.014   14.505  0.50 21.51 ? 84  ARG B NE  1 
ATOM   2830  N  NE  B ARG B  1 84  ? -27.618 5.033   16.272  0.50 20.01 ? 84  ARG B NE  1 
ATOM   2831  C  CZ  A ARG B  1 84  ? -27.820 5.925   13.793  0.50 22.02 ? 84  ARG B CZ  1 
ATOM   2832  C  CZ  B ARG B  1 84  ? -28.909 5.256   16.061  0.50 18.60 ? 84  ARG B CZ  1 
ATOM   2833  N  NH1 A ARG B  1 84  ? -28.978 5.756   14.422  0.50 25.39 ? 84  ARG B NH1 1 
ATOM   2834  N  NH1 B ARG B  1 84  ? -29.298 6.421   15.539  0.50 21.16 ? 84  ARG B NH1 1 
ATOM   2835  N  NH2 A ARG B  1 84  ? -27.754 5.968   12.478  0.50 21.36 ? 84  ARG B NH2 1 
ATOM   2836  N  NH2 B ARG B  1 84  ? -29.790 4.308   16.419  0.50 19.20 ? 84  ARG B NH2 1 
ATOM   2837  N  N   . TYR B  1 85  ? -22.164 4.867   16.260  1.00 14.08 ? 85  TYR B N   1 
ATOM   2838  C  CA  . TYR B  1 85  ? -21.200 5.361   15.259  1.00 12.23 ? 85  TYR B CA  1 
ATOM   2839  C  C   . TYR B  1 85  ? -21.963 5.163   13.982  1.00 12.19 ? 85  TYR B C   1 
ATOM   2840  O  O   . TYR B  1 85  ? -22.384 4.054   13.684  1.00 15.18 ? 85  TYR B O   1 
ATOM   2841  C  CB  . TYR B  1 85  ? -19.893 4.666   15.264  1.00 12.93 ? 85  TYR B CB  1 
ATOM   2842  C  CG  . TYR B  1 85  ? -18.991 5.145   16.356  1.00 12.69 ? 85  TYR B CG  1 
ATOM   2843  C  CD1 . TYR B  1 85  ? -19.164 4.698   17.635  1.00 14.70 ? 85  TYR B CD1 1 
ATOM   2844  C  CD2 . TYR B  1 85  ? -17.956 6.051   16.095  1.00 12.59 ? 85  TYR B CD2 1 
ATOM   2845  C  CE1 . TYR B  1 85  ? -18.338 5.120   18.652  1.00 12.77 ? 85  TYR B CE1 1 
ATOM   2846  C  CE2 . TYR B  1 85  ? -17.108 6.475   17.109  1.00 13.68 ? 85  TYR B CE2 1 
ATOM   2847  C  CZ  . TYR B  1 85  ? -17.303 6.000   18.386  1.00 14.51 ? 85  TYR B CZ  1 
ATOM   2848  O  OH  . TYR B  1 85  ? -16.489 6.397   19.428  1.00 17.93 ? 85  TYR B OH  1 
ATOM   2849  N  N   . SER B  1 86  ? -22.077 6.204   13.181  1.00 12.03 ? 86  SER B N   1 
ATOM   2850  C  CA  . SER B  1 86  ? -22.777 6.153   11.901  1.00 12.81 ? 86  SER B CA  1 
ATOM   2851  C  C   . SER B  1 86  ? -21.729 6.165   10.736  1.00 9.63  ? 86  SER B C   1 
ATOM   2852  O  O   . SER B  1 86  ? -20.706 6.874   10.860  1.00 11.24 ? 86  SER B O   1 
ATOM   2853  C  CB  . SER B  1 86  ? -23.670 7.411   11.695  1.00 15.58 ? 86  SER B CB  1 
ATOM   2854  O  OG  . SER B  1 86  ? -24.800 7.321   12.635  1.00 19.56 ? 86  SER B OG  1 
ATOM   2855  N  N   . ALA B  1 87  ? -22.057 5.433   9.731   1.00 10.57 ? 87  ALA B N   1 
ATOM   2856  C  CA  . ALA B  1 87  ? -21.148 5.309   8.554   1.00 9.39  ? 87  ALA B CA  1 
ATOM   2857  C  C   . ALA B  1 87  ? -21.059 6.647   7.843   1.00 11.29 ? 87  ALA B C   1 
ATOM   2858  O  O   . ALA B  1 87  ? -22.046 7.456   7.807   1.00 12.94 ? 87  ALA B O   1 
ATOM   2859  C  CB  . ALA B  1 87  ? -21.654 4.240   7.616   1.00 13.89 ? 87  ALA B CB  1 
ATOM   2860  N  N   . THR B  1 88  ? -19.882 6.898   7.268   1.00 10.81 ? 88  THR B N   1 
ATOM   2861  C  CA  . THR B  1 88  ? -19.729 8.048   6.348   1.00 10.98 ? 88  THR B CA  1 
ATOM   2862  C  C   . THR B  1 88  ? -19.219 7.614   4.990   1.00 9.89  ? 88  THR B C   1 
ATOM   2863  O  O   . THR B  1 88  ? -19.660 8.128   3.982   1.00 10.12 ? 88  THR B O   1 
ATOM   2864  C  CB  . THR B  1 88  ? -18.848 9.124   7.019   1.00 12.01 ? 88  THR B CB  1 
ATOM   2865  O  OG1 . THR B  1 88  ? -18.793 10.225  6.058   1.00 16.27 ? 88  THR B OG1 1 
ATOM   2866  C  CG2 . THR B  1 88  ? -17.448 8.687   7.403   1.00 11.56 ? 88  THR B CG2 1 
ATOM   2867  N  N   . GLN B  1 89  ? -18.264 6.654   4.944   1.00 9.57  ? 89  GLN B N   1 
ATOM   2868  C  CA  . GLN B  1 89  ? -17.715 6.203   3.639   1.00 8.15  ? 89  GLN B CA  1 
ATOM   2869  C  C   . GLN B  1 89  ? -16.933 4.949   3.826   1.00 7.53  ? 89  GLN B C   1 
ATOM   2870  O  O   . GLN B  1 89  ? -16.534 4.660   4.986   1.00 7.57  ? 89  GLN B O   1 
ATOM   2871  C  CB  . GLN B  1 89  ? -16.783 7.329   3.012   1.00 10.20 ? 89  GLN B CB  1 
ATOM   2872  C  CG  . GLN B  1 89  ? -15.666 7.803   3.928   1.00 12.06 ? 89  GLN B CG  1 
ATOM   2873  C  CD  . GLN B  1 89  ? -14.315 7.352   3.459   1.00 10.95 ? 89  GLN B CD  1 
ATOM   2874  O  OE1 . GLN B  1 89  ? -14.147 6.193   3.197   1.00 11.03 ? 89  GLN B OE1 1 
ATOM   2875  N  NE2 . GLN B  1 89  ? -13.379 8.190   3.337   1.00 17.95 ? 89  GLN B NE2 1 
ATOM   2876  N  N   . LEU B  1 90  ? -16.768 4.220   2.745   1.00 7.28  ? 90  LEU B N   1 
ATOM   2877  C  CA  . LEU B  1 90  ? -15.780 3.150   2.742   1.00 6.64  ? 90  LEU B CA  1 
ATOM   2878  C  C   . LEU B  1 90  ? -14.804 3.384   1.636   1.00 7.48  ? 90  LEU B C   1 
ATOM   2879  O  O   . LEU B  1 90  ? -15.104 4.032   0.670   1.00 8.80  ? 90  LEU B O   1 
ATOM   2880  C  CB  . LEU B  1 90  ? -16.423 1.727   2.728   1.00 7.20  ? 90  LEU B CB  1 
ATOM   2881  C  CG  . LEU B  1 90  ? -17.354 1.441   1.592   1.00 7.68  ? 90  LEU B CG  1 
ATOM   2882  C  CD1 . LEU B  1 90  ? -16.601 1.089   0.288   1.00 8.46  ? 90  LEU B CD1 1 
ATOM   2883  C  CD2 . LEU B  1 90  ? -18.244 0.228   1.957   1.00 8.69  ? 90  LEU B CD2 1 
ATOM   2884  N  N   . HIS B  1 91  ? -13.607 2.772   1.748   1.00 6.76  ? 91  HIS B N   1 
ATOM   2885  C  CA  . HIS B  1 91  ? -12.579 2.915   0.665   1.00 6.43  ? 91  HIS B CA  1 
ATOM   2886  C  C   . HIS B  1 91  ? -11.623 1.765   0.865   1.00 6.72  ? 91  HIS B C   1 
ATOM   2887  O  O   . HIS B  1 91  ? -11.705 0.961   1.818   1.00 6.48  ? 91  HIS B O   1 
ATOM   2888  C  CB  . HIS B  1 91  ? -11.889 4.294   0.789   1.00 6.75  ? 91  HIS B CB  1 
ATOM   2889  C  CG  . HIS B  1 91  ? -11.166 4.458   2.089   1.00 5.90  ? 91  HIS B CG  1 
ATOM   2890  N  ND1 . HIS B  1 91  ? -11.710 5.065   3.208   1.00 7.28  ? 91  HIS B ND1 1 
ATOM   2891  C  CD2 . HIS B  1 91  ? -9.922  3.958   2.473   1.00 6.67  ? 91  HIS B CD2 1 
ATOM   2892  C  CE1 . HIS B  1 91  ? -10.854 4.937   4.234   1.00 6.95  ? 91  HIS B CE1 1 
ATOM   2893  N  NE2 . HIS B  1 91  ? -9.752  4.266   3.819   1.00 6.37  ? 91  HIS B NE2 1 
ATOM   2894  N  N   . LEU B  1 92  ? -10.680 1.702   -0.062  1.00 6.46  ? 92  LEU B N   1 
ATOM   2895  C  CA  . LEU B  1 92  ? -9.705  0.582   -0.070  1.00 7.03  ? 92  LEU B CA  1 
ATOM   2896  C  C   . LEU B  1 92  ? -8.264  1.058   -0.204  1.00 6.45  ? 92  LEU B C   1 
ATOM   2897  O  O   . LEU B  1 92  ? -7.964  2.209   -0.545  1.00 7.47  ? 92  LEU B O   1 
ATOM   2898  C  CB  . LEU B  1 92  ? -9.993  -0.376  -1.219  1.00 8.73  ? 92  LEU B CB  1 
ATOM   2899  C  CG  . LEU B  1 92  ? -11.393 -1.074  -1.143  1.00 8.72  ? 92  LEU B CG  1 
ATOM   2900  C  CD1 . LEU B  1 92  ? -12.377 -0.437  -1.942  1.00 13.00 ? 92  LEU B CD1 1 
ATOM   2901  C  CD2 . LEU B  1 92  ? -11.253 -2.563  -1.386  1.00 11.09 ? 92  LEU B CD2 1 
ATOM   2902  N  N   . HIS B  1 93  ? -7.402  0.135   0.165   1.00 6.28  ? 93  HIS B N   1 
ATOM   2903  C  CA  . HIS B  1 93  ? -5.921  0.267   -0.023  1.00 6.62  ? 93  HIS B CA  1 
ATOM   2904  C  C   . HIS B  1 93  ? -5.408  -0.949  -0.683  1.00 7.00  ? 93  HIS B C   1 
ATOM   2905  O  O   . HIS B  1 93  ? -5.895  -2.073  -0.361  1.00 7.23  ? 93  HIS B O   1 
ATOM   2906  C  CB  . HIS B  1 93  ? -5.229  0.415   1.343   1.00 7.86  ? 93  HIS B CB  1 
ATOM   2907  C  CG  . HIS B  1 93  ? -5.731  1.576   2.120   1.00 6.74  ? 93  HIS B CG  1 
ATOM   2908  N  ND1 . HIS B  1 93  ? -5.140  2.837   2.079   1.00 7.01  ? 93  HIS B ND1 1 
ATOM   2909  C  CD2 . HIS B  1 93  ? -6.781  1.709   3.000   1.00 5.93  ? 93  HIS B CD2 1 
ATOM   2910  C  CE1 . HIS B  1 93  ? -5.803  3.693   2.863   1.00 7.70  ? 93  HIS B CE1 1 
ATOM   2911  N  NE2 . HIS B  1 93  ? -6.820  3.043   3.423   1.00 6.48  ? 93  HIS B NE2 1 
ATOM   2912  N  N   . TRP B  1 94  ? -4.449  -0.835  -1.596  1.00 6.62  ? 94  TRP B N   1 
ATOM   2913  C  CA  . TRP B  1 94  ? -3.947  -1.974  -2.402  1.00 6.44  ? 94  TRP B CA  1 
ATOM   2914  C  C   . TRP B  1 94  ? -2.560  -1.702  -2.902  1.00 6.41  ? 94  TRP B C   1 
ATOM   2915  O  O   . TRP B  1 94  ? -1.945  -0.690  -2.629  1.00 6.97  ? 94  TRP B O   1 
ATOM   2916  C  CB  . TRP B  1 94  ? -4.950  -2.243  -3.519  1.00 7.74  ? 94  TRP B CB  1 
ATOM   2917  C  CG  . TRP B  1 94  ? -5.054  -1.043  -4.481  1.00 7.02  ? 94  TRP B CG  1 
ATOM   2918  C  CD1 . TRP B  1 94  ? -4.234  -0.778  -5.532  1.00 7.78  ? 94  TRP B CD1 1 
ATOM   2919  C  CD2 . TRP B  1 94  ? -6.045  -0.027  -4.425  1.00 7.15  ? 94  TRP B CD2 1 
ATOM   2920  N  NE1 . TRP B  1 94  ? -4.687  0.397   -6.195  1.00 8.45  ? 94  TRP B NE1 1 
ATOM   2921  C  CE2 . TRP B  1 94  ? -5.820  0.821   -5.517  1.00 7.39  ? 94  TRP B CE2 1 
ATOM   2922  C  CE3 . TRP B  1 94  ? -7.106  0.247   -3.563  1.00 7.17  ? 94  TRP B CE3 1 
ATOM   2923  C  CZ2 . TRP B  1 94  ? -6.599  1.947   -5.788  1.00 7.34  ? 94  TRP B CZ2 1 
ATOM   2924  C  CZ3 . TRP B  1 94  ? -7.891  1.409   -3.788  1.00 8.08  ? 94  TRP B CZ3 1 
ATOM   2925  C  CH2 . TRP B  1 94  ? -7.661  2.225   -4.960  1.00 7.49  ? 94  TRP B CH2 1 
ATOM   2926  N  N   . GLY B  1 95  ? -2.015  -2.785  -3.502  1.00 6.77  ? 95  GLY B N   1 
ATOM   2927  C  CA  . GLY B  1 95  ? -0.633  -2.769  -3.977  1.00 7.97  ? 95  GLY B CA  1 
ATOM   2928  C  C   . GLY B  1 95  ? -0.557  -2.454  -5.472  1.00 7.59  ? 95  GLY B C   1 
ATOM   2929  O  O   . GLY B  1 95  ? -1.069  -1.455  -5.959  1.00 8.42  ? 95  GLY B O   1 
ATOM   2930  N  N   . ASN B  1 96  ? -0.022  -3.417  -6.253  1.00 9.55  ? 96  ASN B N   1 
ATOM   2931  C  CA  . ASN B  1 96  ? 0.087   -3.162  -7.672  1.00 9.73  ? 96  ASN B CA  1 
ATOM   2932  C  C   . ASN B  1 96  ? 0.113   -4.497  -8.391  1.00 10.79 ? 96  ASN B C   1 
ATOM   2933  O  O   . ASN B  1 96  ? 0.263   -5.536  -7.770  1.00 10.17 ? 96  ASN B O   1 
ATOM   2934  C  CB  . ASN B  1 96  ? 1.342   -2.348  -7.997  1.00 11.57 ? 96  ASN B CB  1 
ATOM   2935  C  CG  . ASN B  1 96  ? 2.687   -3.093  -7.756  1.00 12.10 ? 96  ASN B CG  1 
ATOM   2936  O  OD1 . ASN B  1 96  ? 3.077   -3.920  -8.623  1.00 17.66 ? 96  ASN B OD1 1 
ATOM   2937  N  ND2 . ASN B  1 96  ? 3.354   -2.884  -6.700  1.00 13.46 ? 96  ASN B ND2 1 
ATOM   2938  N  N   . PRO B  1 97  ? 0.005   -4.471  -9.739  1.00 10.98 ? 97  PRO B N   1 
ATOM   2939  C  CA  . PRO B  1 97  ? -0.138  -5.751  -10.405 1.00 11.85 ? 97  PRO B CA  1 
ATOM   2940  C  C   . PRO B  1 97  ? 1.007   -6.722  -10.280 1.00 10.63 ? 97  PRO B C   1 
ATOM   2941  O  O   . PRO B  1 97  ? 0.753   -7.974  -10.312 1.00 13.57 ? 97  PRO B O   1 
ATOM   2942  C  CB  . PRO B  1 97  ? -0.249  -5.332  -11.880 1.00 14.21 ? 97  PRO B CB  1 
ATOM   2943  C  CG  . PRO B  1 97  ? -0.970  -4.014  -11.813 1.00 14.69 ? 97  PRO B CG  1 
ATOM   2944  C  CD  . PRO B  1 97  ? -0.227  -3.353  -10.689 1.00 13.13 ? 97  PRO B CD  1 
ATOM   2945  N  N   . ASN B  1 98  ? 2.225   -6.198  -10.087 1.00 9.79  ? 98  ASN B N   1 
ATOM   2946  C  CA  . ASN B  1 98  ? 3.381   -7.112  -9.960  1.00 12.76 ? 98  ASN B CA  1 
ATOM   2947  C  C   . ASN B  1 98  ? 3.666   -7.412  -8.527  1.00 15.09 ? 98  ASN B C   1 
ATOM   2948  O  O   . ASN B  1 98  ? 4.588   -8.193  -8.219  1.00 18.33 ? 98  ASN B O   1 
ATOM   2949  C  CB  . ASN B  1 98  ? 4.554   -6.407  -10.646 1.00 11.35 ? 98  ASN B CB  1 
ATOM   2950  C  CG  . ASN B  1 98  ? 4.356   -6.195  -12.108 1.00 12.46 ? 98  ASN B CG  1 
ATOM   2951  O  OD1 . ASN B  1 98  ? 4.164   -7.152  -12.857 1.00 12.42 ? 98  ASN B OD1 1 
ATOM   2952  N  ND2 . ASN B  1 98  ? 4.260   -4.936  -12.501 1.00 13.37 ? 98  ASN B ND2 1 
ATOM   2953  N  N   . ASP B  1 99  ? 2.934   -6.819  -7.595  1.00 12.29 ? 99  ASP B N   1 
ATOM   2954  C  CA  . ASP B  1 99  ? 3.160   -7.164  -6.139  1.00 12.93 ? 99  ASP B CA  1 
ATOM   2955  C  C   . ASP B  1 99  ? 1.781   -6.854  -5.472  1.00 10.14 ? 99  ASP B C   1 
ATOM   2956  O  O   . ASP B  1 99  ? 1.582   -5.774  -4.921  1.00 10.49 ? 99  ASP B O   1 
ATOM   2957  C  CB  . ASP B  1 99  ? 4.267   -6.237  -5.550  1.00 16.64 ? 99  ASP B CB  1 
ATOM   2958  C  CG  . ASP B  1 99  ? 4.564   -6.460  -3.983  1.00 20.28 ? 99  ASP B CG  1 
ATOM   2959  O  OD1 . ASP B  1 99  ? 4.163   -7.505  -3.473  1.00 25.03 ? 99  ASP B OD1 1 
ATOM   2960  O  OD2 . ASP B  1 99  ? 5.044   -5.481  -3.347  1.00 28.53 ? 99  ASP B OD2 1 
ATOM   2961  N  N   . PRO B  1 100 ? 0.889   -7.809  -5.502  1.00 9.89  ? 100 PRO B N   1 
ATOM   2962  C  CA  . PRO B  1 100 ? -0.496  -7.585  -4.942  1.00 9.92  ? 100 PRO B CA  1 
ATOM   2963  C  C   . PRO B  1 100 ? -0.474  -7.826  -3.447  1.00 10.01 ? 100 PRO B C   1 
ATOM   2964  O  O   . PRO B  1 100 ? -1.051  -8.795  -2.933  1.00 11.76 ? 100 PRO B O   1 
ATOM   2965  C  CB  . PRO B  1 100 ? -1.345  -8.563  -5.743  1.00 12.09 ? 100 PRO B CB  1 
ATOM   2966  C  CG  . PRO B  1 100 ? -0.323  -9.658  -6.085  1.00 12.40 ? 100 PRO B CG  1 
ATOM   2967  C  CD  . PRO B  1 100 ? 0.978   -9.036  -6.305  1.00 11.32 ? 100 PRO B CD  1 
ATOM   2968  N  N   . HIS B  1 101 ? 0.183   -6.956  -2.688  1.00 9.07  ? 101 HIS B N   1 
ATOM   2969  C  CA  . HIS B  1 101 ? 0.379   -7.118  -1.244  1.00 10.72 ? 101 HIS B CA  1 
ATOM   2970  C  C   . HIS B  1 101 ? 0.309   -5.783  -0.620  1.00 11.10 ? 101 HIS B C   1 
ATOM   2971  O  O   . HIS B  1 101 ? 1.265   -5.370  0.113   1.00 15.92 ? 101 HIS B O   1 
ATOM   2972  C  CB  . HIS B  1 101 ? 1.700   -7.823  -0.869  1.00 12.25 ? 101 HIS B CB  1 
ATOM   2973  C  CG  . HIS B  1 101 ? 1.774   -9.197  -1.406  1.00 16.01 ? 101 HIS B CG  1 
ATOM   2974  N  ND1 . HIS B  1 101 ? 1.045   -10.259 -0.930  1.00 21.49 ? 101 HIS B ND1 1 
ATOM   2975  C  CD2 . HIS B  1 101 ? 2.326   -9.585  -2.561  1.00 13.32 ? 101 HIS B CD2 1 
ATOM   2976  C  CE1 . HIS B  1 101 ? 1.298   -11.308 -1.714  1.00 19.32 ? 101 HIS B CE1 1 
ATOM   2977  N  NE2 . HIS B  1 101 ? 2.026   -10.903 -2.731  1.00 21.63 ? 101 HIS B NE2 1 
ATOM   2978  N  N   . GLY B  1 102 ? -0.875  -5.178  -0.684  1.00 8.27  ? 102 GLY B N   1 
ATOM   2979  C  CA  . GLY B  1 102 ? -1.005  -3.796  -0.256  1.00 8.62  ? 102 GLY B CA  1 
ATOM   2980  C  C   . GLY B  1 102 ? -1.996  -3.541  0.907   1.00 7.47  ? 102 GLY B C   1 
ATOM   2981  O  O   . GLY B  1 102 ? -2.505  -2.430  1.025   1.00 8.49  ? 102 GLY B O   1 
ATOM   2982  N  N   . SER B  1 103 ? -2.227  -4.513  1.769   1.00 7.96  ? 103 SER B N   1 
ATOM   2983  C  CA  . SER B  1 103 ? -2.955  -4.191  2.990   1.00 7.64  ? 103 SER B CA  1 
ATOM   2984  C  C   . SER B  1 103 ? -2.158  -3.169  3.822   1.00 7.58  ? 103 SER B C   1 
ATOM   2985  O  O   . SER B  1 103 ? -0.911  -3.064  3.679   1.00 8.79  ? 103 SER B O   1 
ATOM   2986  C  CB  . SER B  1 103 ? -3.307  -5.441  3.824   1.00 7.43  ? 103 SER B CB  1 
ATOM   2987  O  OG  . SER B  1 103 ? -2.070  -5.975  4.397   1.00 7.92  ? 103 SER B OG  1 
ATOM   2988  N  N   . GLU B  1 104 ? -2.830  -2.457  4.707   1.00 6.96  ? 104 GLU B N   1 
ATOM   2989  C  CA  . GLU B  1 104 ? -2.192  -1.532  5.633   1.00 6.81  ? 104 GLU B CA  1 
ATOM   2990  C  C   . GLU B  1 104 ? -1.774  -2.248  6.921   1.00 7.47  ? 104 GLU B C   1 
ATOM   2991  O  O   . GLU B  1 104 ? -0.629  -2.296  7.249   1.00 7.97  ? 104 GLU B O   1 
ATOM   2992  C  CB  . GLU B  1 104 ? -3.100  -0.345  5.923   1.00 7.13  ? 104 GLU B CB  1 
ATOM   2993  C  CG  . GLU B  1 104 ? -3.504  0.391   4.638   1.00 7.66  ? 104 GLU B CG  1 
ATOM   2994  C  CD  . GLU B  1 104 ? -3.607  1.861   4.957   1.00 6.85  ? 104 GLU B CD  1 
ATOM   2995  O  OE1 . GLU B  1 104 ? -4.619  2.281   5.560   1.00 7.94  ? 104 GLU B OE1 1 
ATOM   2996  O  OE2 . GLU B  1 104 ? -2.661  2.597   4.605   1.00 8.33  ? 104 GLU B OE2 1 
ATOM   2997  N  N   . HIS B  1 105 ? -2.744  -2.875  7.590   1.00 7.72  ? 105 HIS B N   1 
ATOM   2998  C  CA  . HIS B  1 105 ? -2.350  -3.699  8.750   1.00 7.84  ? 105 HIS B CA  1 
ATOM   2999  C  C   . HIS B  1 105 ? -1.713  -4.966  8.184   1.00 8.60  ? 105 HIS B C   1 
ATOM   3000  O  O   . HIS B  1 105 ? -2.043  -5.442  7.096   1.00 8.31  ? 105 HIS B O   1 
ATOM   3001  C  CB  . HIS B  1 105 ? -3.583  -4.048  9.546   1.00 7.63  ? 105 HIS B CB  1 
ATOM   3002  C  CG  . HIS B  1 105 ? -4.141  -2.899  10.257  1.00 7.81  ? 105 HIS B CG  1 
ATOM   3003  N  ND1 . HIS B  1 105 ? -5.081  -2.057  9.677   1.00 7.85  ? 105 HIS B ND1 1 
ATOM   3004  C  CD2 . HIS B  1 105 ? -3.805  -2.353  11.462  1.00 7.66  ? 105 HIS B CD2 1 
ATOM   3005  C  CE1 . HIS B  1 105 ? -5.312  -1.047  10.506  1.00 8.37  ? 105 HIS B CE1 1 
ATOM   3006  N  NE2 . HIS B  1 105 ? -4.563  -1.214  11.615  1.00 8.11  ? 105 HIS B NE2 1 
ATOM   3007  N  N   . THR B  1 106 ? -0.747  -5.509  8.968   1.00 7.96  ? 106 THR B N   1 
ATOM   3008  C  CA  . THR B  1 106 ? -0.101  -6.823  8.712   1.00 8.13  ? 106 THR B CA  1 
ATOM   3009  C  C   . THR B  1 106 ? -0.401  -7.715  9.852   1.00 7.89  ? 106 THR B C   1 
ATOM   3010  O  O   . THR B  1 106 ? -0.738  -7.239  10.919  1.00 8.93  ? 106 THR B O   1 
ATOM   3011  C  CB  . THR B  1 106 ? 1.363   -6.645  8.389   1.00 9.44  ? 106 THR B CB  1 
ATOM   3012  O  OG1 . THR B  1 106 ? 2.048   -6.020  9.496   1.00 9.86  ? 106 THR B OG1 1 
ATOM   3013  C  CG2 . THR B  1 106 ? 1.571   -5.740  7.169   1.00 10.06 ? 106 THR B CG2 1 
ATOM   3014  N  N   . VAL B  1 107 ? -0.294  -9.023  9.584   1.00 9.21  ? 107 VAL B N   1 
ATOM   3015  C  CA  . VAL B  1 107 ? -0.488  -9.978  10.685  1.00 9.74  ? 107 VAL B CA  1 
ATOM   3016  C  C   . VAL B  1 107 ? 0.720   -10.900 10.713  1.00 10.12 ? 107 VAL B C   1 
ATOM   3017  O  O   . VAL B  1 107 ? 1.080   -11.474 9.699   1.00 11.89 ? 107 VAL B O   1 
ATOM   3018  C  CB  . VAL B  1 107 ? -1.758  -10.860 10.413  1.00 10.69 ? 107 VAL B CB  1 
ATOM   3019  C  CG1 . VAL B  1 107 ? -1.897  -11.867 11.596  1.00 12.65 ? 107 VAL B CG1 1 
ATOM   3020  C  CG2 . VAL B  1 107 ? -3.058  -10.024 10.382  1.00 11.62 ? 107 VAL B CG2 1 
ATOM   3021  N  N   . SER B  1 108 ? 1.358   -10.801 11.887  1.00 11.60 ? 108 SER B N   1 
ATOM   3022  C  CA  . SER B  1 108 ? 2.679   -11.562 12.050  1.00 11.57 ? 108 SER B CA  1 
ATOM   3023  C  C   . SER B  1 108 ? 3.575   -11.330 10.864  1.00 12.47 ? 108 SER B C   1 
ATOM   3024  O  O   . SER B  1 108 ? 4.232   -12.192 10.269  1.00 14.50 ? 108 SER B O   1 
ATOM   3025  C  CB  . SER B  1 108 ? 2.380   -13.048 12.294  1.00 12.92 ? 108 SER B CB  1 
ATOM   3026  O  OG  . SER B  1 108 ? 1.520   -13.219 13.365  1.00 15.36 ? 108 SER B OG  1 
ATOM   3027  N  N   . GLY B  1 109 ? 3.688   -10.065 10.521  1.00 11.53 ? 109 GLY B N   1 
ATOM   3028  C  CA  . GLY B  1 109 ? 4.569   -9.570  9.544   1.00 13.47 ? 109 GLY B CA  1 
ATOM   3029  C  C   . GLY B  1 109 ? 4.159   -9.712  8.045   1.00 14.11 ? 109 GLY B C   1 
ATOM   3030  O  O   . GLY B  1 109 ? 4.943   -9.268  7.139   1.00 18.98 ? 109 GLY B O   1 
ATOM   3031  N  N   . GLN B  1 110 ? 2.988   -10.249 7.777   1.00 14.40 ? 110 GLN B N   1 
ATOM   3032  C  CA  . GLN B  1 110 ? 2.613   -10.548 6.407   1.00 15.68 ? 110 GLN B CA  1 
ATOM   3033  C  C   . GLN B  1 110 ? 1.513   -9.555  5.988   1.00 11.62 ? 110 GLN B C   1 
ATOM   3034  O  O   . GLN B  1 110 ? 0.546   -9.291  6.716   1.00 11.13 ? 110 GLN B O   1 
ATOM   3035  C  CB  . GLN B  1 110 ? 1.987   -11.935 6.367   1.00 18.51 ? 110 GLN B CB  1 
ATOM   3036  C  CG  . GLN B  1 110 ? 2.905   -13.107 6.938   1.00 17.89 ? 110 GLN B CG  1 
ATOM   3037  C  CD  . GLN B  1 110 ? 4.323   -13.019 6.417   1.00 26.36 ? 110 GLN B CD  1 
ATOM   3038  O  OE1 . GLN B  1 110 ? 4.578   -13.221 5.215   1.00 29.48 ? 110 GLN B OE1 1 
ATOM   3039  N  NE2 . GLN B  1 110 ? 5.261   -12.672 7.341   1.00 27.10 ? 110 GLN B NE2 1 
ATOM   3040  N  N   . HIS B  1 111 ? 1.745   -8.970  4.824   1.00 12.12 ? 111 HIS B N   1 
ATOM   3041  C  CA  . HIS B  1 111 ? 0.661   -8.242  4.167   1.00 10.92 ? 111 HIS B CA  1 
ATOM   3042  C  C   . HIS B  1 111 ? -0.371  -9.133  3.508   1.00 11.64 ? 111 HIS B C   1 
ATOM   3043  O  O   . HIS B  1 111 ? -0.022  -10.202 2.969   1.00 16.57 ? 111 HIS B O   1 
ATOM   3044  C  CB  . HIS B  1 111 ? 1.158   -7.414  2.947   1.00 13.23 ? 111 HIS B CB  1 
ATOM   3045  C  CG  . HIS B  1 111 ? 1.877   -6.176  3.349   1.00 11.75 ? 111 HIS B CG  1 
ATOM   3046  N  ND1 . HIS B  1 111 ? 1.261   -4.948  3.540   1.00 13.26 ? 111 HIS B ND1 1 
ATOM   3047  C  CD2 . HIS B  1 111 ? 3.180   -6.004  3.717   1.00 13.68 ? 111 HIS B CD2 1 
ATOM   3048  C  CE1 . HIS B  1 111 ? 2.175   -4.058  3.938   1.00 13.32 ? 111 HIS B CE1 1 
ATOM   3049  N  NE2 . HIS B  1 111 ? 3.337   -4.659  4.071   1.00 16.90 ? 111 HIS B NE2 1 
ATOM   3050  N  N   . PHE B  1 112 ? -1.587  -8.667  3.471   1.00 9.73  ? 112 PHE B N   1 
ATOM   3051  C  CA  . PHE B  1 112 ? -2.638  -9.234  2.733   1.00 9.74  ? 112 PHE B CA  1 
ATOM   3052  C  C   . PHE B  1 112 ? -2.657  -8.468  1.363   1.00 7.60  ? 112 PHE B C   1 
ATOM   3053  O  O   . PHE B  1 112 ? -1.928  -7.502  1.217   1.00 8.94  ? 112 PHE B O   1 
ATOM   3054  C  CB  . PHE B  1 112 ? -3.970  -9.195  3.450   1.00 10.97 ? 112 PHE B CB  1 
ATOM   3055  C  CG  . PHE B  1 112 ? -4.031  -10.211 4.525   1.00 11.83 ? 112 PHE B CG  1 
ATOM   3056  C  CD1 . PHE B  1 112 ? -3.426  -10.045 5.778   1.00 14.80 ? 112 PHE B CD1 1 
ATOM   3057  C  CD2 . PHE B  1 112 ? -4.676  -11.396 4.250   1.00 14.31 ? 112 PHE B CD2 1 
ATOM   3058  C  CE1 . PHE B  1 112 ? -3.512  -11.057 6.710   1.00 17.13 ? 112 PHE B CE1 1 
ATOM   3059  C  CE2 . PHE B  1 112 ? -4.752  -12.399 5.159   1.00 19.42 ? 112 PHE B CE2 1 
ATOM   3060  C  CZ  . PHE B  1 112 ? -4.161  -12.250 6.392   1.00 16.50 ? 112 PHE B CZ  1 
ATOM   3061  N  N   . ALA B  1 113 ? -3.490  -8.897  0.447   1.00 7.84  ? 113 ALA B N   1 
ATOM   3062  C  CA  . ALA B  1 113 ? -3.484  -8.289  -0.895  1.00 8.59  ? 113 ALA B CA  1 
ATOM   3063  C  C   . ALA B  1 113 ? -3.985  -6.889  -0.824  1.00 8.23  ? 113 ALA B C   1 
ATOM   3064  O  O   . ALA B  1 113 ? -3.520  -6.006  -1.544  1.00 8.41  ? 113 ALA B O   1 
ATOM   3065  C  CB  . ALA B  1 113 ? -4.380  -9.082  -1.866  1.00 9.52  ? 113 ALA B CB  1 
ATOM   3066  N  N   . ALA B  1 114 ? -5.017  -6.619  0.000   1.00 7.48  ? 114 ALA B N   1 
ATOM   3067  C  CA  . ALA B  1 114 ? -5.631  -5.248  0.035   1.00 6.45  ? 114 ALA B CA  1 
ATOM   3068  C  C   . ALA B  1 114 ? -6.375  -5.170  1.354   1.00 6.41  ? 114 ALA B C   1 
ATOM   3069  O  O   . ALA B  1 114 ? -6.361  -6.089  2.194   1.00 6.86  ? 114 ALA B O   1 
ATOM   3070  C  CB  . ALA B  1 114 ? -6.611  -5.130  -1.165  1.00 6.99  ? 114 ALA B CB  1 
ATOM   3071  N  N   . GLU B  1 115 ? -7.007  -4.003  1.581   1.00 6.36  ? 115 GLU B N   1 
ATOM   3072  C  CA  . GLU B  1 115 ? -7.732  -3.780  2.821   1.00 6.39  ? 115 GLU B CA  1 
ATOM   3073  C  C   . GLU B  1 115 ? -8.863  -2.826  2.602   1.00 6.62  ? 115 GLU B C   1 
ATOM   3074  O  O   . GLU B  1 115 ? -8.722  -1.822  1.839   1.00 7.15  ? 115 GLU B O   1 
ATOM   3075  C  CB  . GLU B  1 115 ? -6.764  -3.216  3.871   1.00 6.87  ? 115 GLU B CB  1 
ATOM   3076  C  CG  . GLU B  1 115 ? -7.339  -3.139  5.290   1.00 8.23  ? 115 GLU B CG  1 
ATOM   3077  C  CD  . GLU B  1 115 ? -6.241  -2.832  6.356   1.00 8.33  ? 115 GLU B CD  1 
ATOM   3078  O  OE1 . GLU B  1 115 ? -5.092  -3.321  6.133   1.00 8.12  ? 115 GLU B OE1 1 
ATOM   3079  O  OE2 . GLU B  1 115 ? -6.532  -2.220  7.392   1.00 7.74  ? 115 GLU B OE2 1 
ATOM   3080  N  N   . LEU B  1 116 ? -10.037 -3.147  3.167   1.00 5.91  ? 116 LEU B N   1 
ATOM   3081  C  CA  . LEU B  1 116 ? -11.221 -2.278  3.102   1.00 6.62  ? 116 LEU B CA  1 
ATOM   3082  C  C   . LEU B  1 116 ? -11.369 -1.593  4.436   1.00 6.84  ? 116 LEU B C   1 
ATOM   3083  O  O   . LEU B  1 116 ? -11.250 -2.246  5.515   1.00 6.76  ? 116 LEU B O   1 
ATOM   3084  C  CB  . LEU B  1 116 ? -12.471 -3.170  2.902   1.00 8.10  ? 116 LEU B CB  1 
ATOM   3085  C  CG  . LEU B  1 116 ? -13.824 -2.417  3.054   1.00 7.57  ? 116 LEU B CG  1 
ATOM   3086  C  CD1 . LEU B  1 116 ? -14.090 -1.585  1.807   1.00 9.20  ? 116 LEU B CD1 1 
ATOM   3087  C  CD2 . LEU B  1 116 ? -14.991 -3.429  3.202   1.00 8.39  ? 116 LEU B CD2 1 
ATOM   3088  N  N   . HIS B  1 117 ? -11.630 -0.306  4.418   1.00 6.37  ? 117 HIS B N   1 
ATOM   3089  C  CA  . HIS B  1 117 ? -11.979 0.489   5.648   1.00 6.33  ? 117 HIS B CA  1 
ATOM   3090  C  C   . HIS B  1 117 ? -13.345 1.062   5.522   1.00 6.58  ? 117 HIS B C   1 
ATOM   3091  O  O   . HIS B  1 117 ? -13.666 1.719   4.546   1.00 6.52  ? 117 HIS B O   1 
ATOM   3092  C  CB  . HIS B  1 117 ? -10.985 1.691   5.751   1.00 5.85  ? 117 HIS B CB  1 
ATOM   3093  C  CG  . HIS B  1 117 ? -9.631  1.204   6.112   1.00 6.12  ? 117 HIS B CG  1 
ATOM   3094  N  ND1 . HIS B  1 117 ? -8.466  1.916   5.834   1.00 6.10  ? 117 HIS B ND1 1 
ATOM   3095  C  CD2 . HIS B  1 117 ? -9.237  0.032   6.660   1.00 6.53  ? 117 HIS B CD2 1 
ATOM   3096  C  CE1 . HIS B  1 117 ? -7.408  1.209   6.247   1.00 7.58  ? 117 HIS B CE1 1 
ATOM   3097  N  NE2 . HIS B  1 117 ? -7.856  0.067   6.749   1.00 6.77  ? 117 HIS B NE2 1 
ATOM   3098  N  N   . ILE B  1 118 ? -14.193 0.765   6.507   1.00 7.18  ? 118 ILE B N   1 
ATOM   3099  C  CA  . ILE B  1 118 ? -15.548 1.424   6.573   1.00 7.39  ? 118 ILE B CA  1 
ATOM   3100  C  C   . ILE B  1 118 ? -15.527 2.416   7.700   1.00 7.54  ? 118 ILE B C   1 
ATOM   3101  O  O   . ILE B  1 118 ? -15.353 2.018   8.887   1.00 7.81  ? 118 ILE B O   1 
ATOM   3102  C  CB  . ILE B  1 118 ? -16.625 0.303   6.790   1.00 7.26  ? 118 ILE B CB  1 
ATOM   3103  C  CG1 . ILE B  1 118 ? -16.485 -0.880  5.851   1.00 8.13  ? 118 ILE B CG1 1 
ATOM   3104  C  CG2 . ILE B  1 118 ? -17.997 1.046   6.686   1.00 8.94  ? 118 ILE B CG2 1 
ATOM   3105  C  CD1 . ILE B  1 118 ? -17.611 -1.963  6.048   1.00 10.44 ? 118 ILE B CD1 1 
ATOM   3106  N  N   . VAL B  1 119 ? -15.487 3.710   7.371   1.00 8.17  ? 119 VAL B N   1 
ATOM   3107  C  CA  . VAL B  1 119 ? -15.281 4.759   8.313   1.00 8.02  ? 119 VAL B CA  1 
ATOM   3108  C  C   . VAL B  1 119 ? -16.621 5.223   8.894   1.00 7.72  ? 119 VAL B C   1 
ATOM   3109  O  O   . VAL B  1 119 ? -17.562 5.455   8.095   1.00 9.03  ? 119 VAL B O   1 
ATOM   3110  C  CB  . VAL B  1 119 ? -14.599 5.974   7.580   1.00 8.65  ? 119 VAL B CB  1 
ATOM   3111  C  CG1 . VAL B  1 119 ? -14.291 7.073   8.567   1.00 10.15 ? 119 VAL B CG1 1 
ATOM   3112  C  CG2 . VAL B  1 119 ? -13.292 5.478   6.820   1.00 8.62  ? 119 VAL B CG2 1 
ATOM   3113  N  N   . HIS B  1 120 ? -16.651 5.296   10.206  1.00 8.79  ? 120 HIS B N   1 
ATOM   3114  C  CA  . HIS B  1 120 ? -17.873 5.752   10.924  1.00 9.48  ? 120 HIS B CA  1 
ATOM   3115  C  C   . HIS B  1 120 ? -17.391 6.870   11.866  1.00 10.05 ? 120 HIS B C   1 
ATOM   3116  O  O   . HIS B  1 120 ? -16.242 7.058   12.283  1.00 9.92  ? 120 HIS B O   1 
ATOM   3117  C  CB  . HIS B  1 120 ? -18.441 4.578   11.814  1.00 8.72  ? 120 HIS B CB  1 
ATOM   3118  C  CG  . HIS B  1 120 ? -18.836 3.373   11.097  1.00 8.83  ? 120 HIS B CG  1 
ATOM   3119  N  ND1 . HIS B  1 120 ? -17.877 2.521   10.522  1.00 8.69  ? 120 HIS B ND1 1 
ATOM   3120  C  CD2 . HIS B  1 120 ? -20.032 2.778   10.898  1.00 9.33  ? 120 HIS B CD2 1 
ATOM   3121  C  CE1 . HIS B  1 120 ? -18.519 1.495   9.999   1.00 10.37 ? 120 HIS B CE1 1 
ATOM   3122  N  NE2 . HIS B  1 120 ? -19.834 1.602   10.218  1.00 10.86 ? 120 HIS B NE2 1 
ATOM   3123  N  N   . TYR B  1 121 ? -18.389 7.701   12.258  1.00 11.49 ? 121 TYR B N   1 
ATOM   3124  C  CA  . TYR B  1 121 ? -18.138 8.753   13.191  1.00 12.68 ? 121 TYR B CA  1 
ATOM   3125  C  C   . TYR B  1 121 ? -19.191 8.745   14.328  1.00 13.43 ? 121 TYR B C   1 
ATOM   3126  O  O   . TYR B  1 121 ? -20.266 8.226   14.154  1.00 13.76 ? 121 TYR B O   1 
ATOM   3127  C  CB  . TYR B  1 121 ? -18.162 10.165  12.494  1.00 14.52 ? 121 TYR B CB  1 
ATOM   3128  C  CG  . TYR B  1 121 ? -19.558 10.577  11.948  1.00 15.71 ? 121 TYR B CG  1 
ATOM   3129  C  CD1 . TYR B  1 121 ? -20.029 10.082  10.776  1.00 17.62 ? 121 TYR B CD1 1 
ATOM   3130  C  CD2 . TYR B  1 121 ? -20.355 11.462  12.718  1.00 19.03 ? 121 TYR B CD2 1 
ATOM   3131  C  CE1 . TYR B  1 121 ? -21.291 10.461  10.271  1.00 16.46 ? 121 TYR B CE1 1 
ATOM   3132  C  CE2 . TYR B  1 121 ? -21.590 11.851  12.222  1.00 19.04 ? 121 TYR B CE2 1 
ATOM   3133  C  CZ  . TYR B  1 121 ? -22.046 11.315  11.011  1.00 21.29 ? 121 TYR B CZ  1 
ATOM   3134  O  OH  . TYR B  1 121 ? -23.299 11.647  10.522  1.00 27.02 ? 121 TYR B OH  1 
ATOM   3135  N  N   . ASN B  1 122 ? -18.796 9.369   15.434  1.00 13.30 ? 122 ASN B N   1 
ATOM   3136  C  CA  . ASN B  1 122 ? -19.717 9.313   16.609  1.00 15.14 ? 122 ASN B CA  1 
ATOM   3137  C  C   . ASN B  1 122 ? -20.873 10.329  16.353  1.00 13.91 ? 122 ASN B C   1 
ATOM   3138  O  O   . ASN B  1 122 ? -20.666 11.506  16.579  1.00 17.47 ? 122 ASN B O   1 
ATOM   3139  C  CB  . ASN B  1 122 ? -18.935 9.618   17.867  1.00 15.60 ? 122 ASN B CB  1 
ATOM   3140  C  CG  . ASN B  1 122 ? -19.797 9.566   19.088  1.00 20.42 ? 122 ASN B CG  1 
ATOM   3141  O  OD1 . ASN B  1 122 ? -21.021 9.659   19.013  1.00 18.24 ? 122 ASN B OD1 1 
ATOM   3142  N  ND2 . ASN B  1 122 ? -19.146 9.336   20.237  1.00 21.82 ? 122 ASN B ND2 1 
ATOM   3143  N  N   . SER B  1 123 ? -22.020 9.830   15.855  1.00 16.39 ? 123 SER B N   1 
ATOM   3144  C  CA  . SER B  1 123 ? -23.116 10.727  15.472  1.00 18.94 ? 123 SER B CA  1 
ATOM   3145  C  C   . SER B  1 123 ? -23.920 11.102  16.722  1.00 24.52 ? 123 SER B C   1 
ATOM   3146  O  O   . SER B  1 123 ? -24.835 11.941  16.611  1.00 21.22 ? 123 SER B O   1 
ATOM   3147  C  CB  . SER B  1 123 ? -23.953 10.060  14.418  1.00 17.39 ? 123 SER B CB  1 
ATOM   3148  O  OG  . SER B  1 123 ? -24.275 8.759   14.784  1.00 19.30 ? 123 SER B OG  1 
ATOM   3149  N  N   . ASP B  1 124 ? -23.668 10.448  17.848  1.00 20.72 ? 124 ASP B N   1 
ATOM   3150  C  CA  . ASP B  1 124 ? -24.397 10.853  19.071  1.00 22.75 ? 124 ASP B CA  1 
ATOM   3151  C  C   . ASP B  1 124 ? -23.827 12.214  19.519  1.00 26.31 ? 124 ASP B C   1 
ATOM   3152  O  O   . ASP B  1 124 ? -24.571 13.072  20.001  1.00 22.63 ? 124 ASP B O   1 
ATOM   3153  C  CB  . ASP B  1 124 ? -24.174 9.790   20.207  1.00 21.37 ? 124 ASP B CB  1 
ATOM   3154  C  CG  . ASP B  1 124 ? -25.077 8.536   20.048  1.00 23.06 ? 124 ASP B CG  1 
ATOM   3155  O  OD1 . ASP B  1 124 ? -26.048 8.535   19.261  1.00 28.79 ? 124 ASP B OD1 1 
ATOM   3156  O  OD2 . ASP B  1 124 ? -24.804 7.546   20.742  1.00 22.95 ? 124 ASP B OD2 1 
ATOM   3157  N  N   . LEU B  1 125 ? -22.559 12.452  19.230  1.00 20.74 ? 125 LEU B N   1 
ATOM   3158  C  CA  . LEU B  1 125 ? -21.812 13.630  19.668  1.00 21.33 ? 125 LEU B CA  1 
ATOM   3159  C  C   . LEU B  1 125 ? -21.579 14.653  18.567  1.00 23.74 ? 125 LEU B C   1 
ATOM   3160  O  O   . LEU B  1 125 ? -21.530 15.881  18.850  1.00 23.72 ? 125 LEU B O   1 
ATOM   3161  C  CB  . LEU B  1 125 ? -20.496 13.301  20.290  1.00 20.67 ? 125 LEU B CB  1 
ATOM   3162  C  CG  . LEU B  1 125 ? -20.579 12.427  21.503  1.00 23.37 ? 125 LEU B CG  1 
ATOM   3163  C  CD1 . LEU B  1 125 ? -19.228 12.251  22.127  1.00 21.27 ? 125 LEU B CD1 1 
ATOM   3164  C  CD2 . LEU B  1 125 ? -21.486 13.056  22.568  1.00 24.28 ? 125 LEU B CD2 1 
ATOM   3165  N  N   . TYR B  1 126 ? -21.498 14.243  17.310  1.00 20.97 ? 126 TYR B N   1 
ATOM   3166  C  CA  . TYR B  1 126 ? -20.990 15.188  16.257  1.00 21.88 ? 126 TYR B CA  1 
ATOM   3167  C  C   . TYR B  1 126 ? -21.870 15.143  15.072  1.00 23.06 ? 126 TYR B C   1 
ATOM   3168  O  O   . TYR B  1 126 ? -22.454 14.103  14.768  1.00 22.13 ? 126 TYR B O   1 
ATOM   3169  C  CB  . TYR B  1 126 ? -19.494 14.862  15.851  1.00 22.61 ? 126 TYR B CB  1 
ATOM   3170  C  CG  . TYR B  1 126 ? -18.620 14.755  17.057  1.00 23.72 ? 126 TYR B CG  1 
ATOM   3171  C  CD1 . TYR B  1 126 ? -18.398 15.881  17.861  1.00 30.55 ? 126 TYR B CD1 1 
ATOM   3172  C  CD2 . TYR B  1 126 ? -18.080 13.511  17.474  1.00 22.85 ? 126 TYR B CD2 1 
ATOM   3173  C  CE1 . TYR B  1 126 ? -17.655 15.790  19.020  1.00 25.40 ? 126 TYR B CE1 1 
ATOM   3174  C  CE2 . TYR B  1 126 ? -17.380 13.405  18.658  1.00 25.37 ? 126 TYR B CE2 1 
ATOM   3175  C  CZ  . TYR B  1 126 ? -17.132 14.560  19.415  1.00 30.66 ? 126 TYR B CZ  1 
ATOM   3176  O  OH  . TYR B  1 126 ? -16.387 14.462  20.591  1.00 31.66 ? 126 TYR B OH  1 
ATOM   3177  N  N   . PRO B  1 127 ? -21.997 16.309  14.384  1.00 28.66 ? 127 PRO B N   1 
ATOM   3178  C  CA  . PRO B  1 127 ? -22.838 16.499  13.240  1.00 31.00 ? 127 PRO B CA  1 
ATOM   3179  C  C   . PRO B  1 127 ? -22.317 15.829  11.971  1.00 28.32 ? 127 PRO B C   1 
ATOM   3180  O  O   . PRO B  1 127 ? -23.107 15.542  11.094  1.00 34.98 ? 127 PRO B O   1 
ATOM   3181  C  CB  . PRO B  1 127 ? -22.843 18.052  13.051  1.00 33.09 ? 127 PRO B CB  1 
ATOM   3182  C  CG  . PRO B  1 127 ? -21.616 18.545  13.727  1.00 33.93 ? 127 PRO B CG  1 
ATOM   3183  C  CD  . PRO B  1 127 ? -21.386 17.572  14.855  1.00 29.69 ? 127 PRO B CD  1 
ATOM   3184  N  N   . ASP B  1 128 ? -21.015 15.490  11.908  1.00 27.04 ? 128 ASP B N   1 
ATOM   3185  C  CA  . ASP B  1 128 ? -20.443 14.941  10.685  1.00 24.58 ? 128 ASP B CA  1 
ATOM   3186  C  C   . ASP B  1 128 ? -19.043 14.405  10.998  1.00 23.85 ? 128 ASP B C   1 
ATOM   3187  O  O   . ASP B  1 128 ? -18.489 14.644  12.071  1.00 24.74 ? 128 ASP B O   1 
ATOM   3188  C  CB  . ASP B  1 128 ? -20.324 16.133  9.687   1.00 27.36 ? 128 ASP B CB  1 
ATOM   3189  C  CG  . ASP B  1 128 ? -19.451 17.206  10.216  1.00 30.63 ? 128 ASP B CG  1 
ATOM   3190  O  OD1 . ASP B  1 128 ? -19.818 17.837  11.248  1.00 41.97 ? 128 ASP B OD1 1 
ATOM   3191  O  OD2 . ASP B  1 128 ? -18.427 17.477  9.595   1.00 38.80 ? 128 ASP B OD2 1 
ATOM   3192  N  N   . ALA B  1 129 ? -18.482 13.647  10.069  1.00 20.63 ? 129 ALA B N   1 
ATOM   3193  C  CA  . ALA B  1 129 ? -17.190 13.032  10.280  1.00 21.37 ? 129 ALA B CA  1 
ATOM   3194  C  C   . ALA B  1 129 ? -16.065 14.034  10.347  1.00 21.11 ? 129 ALA B C   1 
ATOM   3195  O  O   . ALA B  1 129 ? -15.125 13.828  11.065  1.00 20.23 ? 129 ALA B O   1 
ATOM   3196  C  CB  . ALA B  1 129 ? -16.946 12.018  9.119   1.00 23.85 ? 129 ALA B CB  1 
ATOM   3197  N  N   A SER B  1 130 ? -16.167 15.146  9.606   0.50 24.34 ? 130 SER B N   1 
ATOM   3198  N  N   B SER B  1 130 ? -16.152 15.142  9.620   0.50 22.19 ? 130 SER B N   1 
ATOM   3199  C  CA  A SER B  1 130 ? -15.099 16.186  9.665   0.50 26.67 ? 130 SER B CA  1 
ATOM   3200  C  CA  B SER B  1 130 ? -15.045 16.118  9.700   0.50 22.54 ? 130 SER B CA  1 
ATOM   3201  C  C   A SER B  1 130 ? -14.909 16.716  11.089  0.50 26.61 ? 130 SER B C   1 
ATOM   3202  C  C   B SER B  1 130 ? -14.900 16.685  11.136  0.50 23.30 ? 130 SER B C   1 
ATOM   3203  O  O   A SER B  1 130 ? -13.773 16.793  11.578  0.50 30.68 ? 130 SER B O   1 
ATOM   3204  O  O   B SER B  1 130 ? -13.793 16.730  11.707  0.50 24.43 ? 130 SER B O   1 
ATOM   3205  C  CB  A SER B  1 130 ? -15.370 17.375  8.723   0.50 27.44 ? 130 SER B CB  1 
ATOM   3206  C  CB  B SER B  1 130 ? -15.218 17.224  8.651   0.50 20.78 ? 130 SER B CB  1 
ATOM   3207  O  OG  A SER B  1 130 ? -15.308 17.020  7.360   0.50 28.90 ? 130 SER B OG  1 
ATOM   3208  O  OG  B SER B  1 130 ? -14.165 18.152  8.731   0.50 20.22 ? 130 SER B OG  1 
ATOM   3209  N  N   . THR B  1 131 ? -16.011 17.093  11.745  1.00 24.66 ? 131 THR B N   1 
ATOM   3210  C  CA  . THR B  1 131 ? -15.991 17.530  13.135  1.00 24.94 ? 131 THR B CA  1 
ATOM   3211  C  C   . THR B  1 131 ? -15.508 16.478  14.100  1.00 28.01 ? 131 THR B C   1 
ATOM   3212  O  O   . THR B  1 131 ? -14.700 16.796  14.977  1.00 26.22 ? 131 THR B O   1 
ATOM   3213  C  CB  . THR B  1 131 ? -17.434 17.955  13.513  1.00 29.11 ? 131 THR B CB  1 
ATOM   3214  O  OG1 . THR B  1 131 ? -17.788 19.086  12.724  1.00 31.82 ? 131 THR B OG1 1 
ATOM   3215  C  CG2 . THR B  1 131 ? -17.686 18.279  15.071  1.00 29.44 ? 131 THR B CG2 1 
ATOM   3216  N  N   . ALA B  1 132 ? -16.011 15.216  13.959  1.00 22.48 ? 132 ALA B N   1 
ATOM   3217  C  CA  . ALA B  1 132 ? -15.620 14.094  14.791  1.00 21.17 ? 132 ALA B CA  1 
ATOM   3218  C  C   . ALA B  1 132 ? -14.108 13.807  14.707  1.00 20.17 ? 132 ALA B C   1 
ATOM   3219  O  O   . ALA B  1 132 ? -13.571 13.261  15.660  1.00 18.53 ? 132 ALA B O   1 
ATOM   3220  C  CB  . ALA B  1 132 ? -16.403 12.829  14.353  1.00 20.07 ? 132 ALA B CB  1 
ATOM   3221  N  N   . SER B  1 133 ? -13.499 14.134  13.575  1.00 20.76 ? 133 SER B N   1 
ATOM   3222  C  CA  . SER B  1 133 ? -12.151 13.618  13.260  1.00 21.38 ? 133 SER B CA  1 
ATOM   3223  C  C   . SER B  1 133 ? -11.102 14.217  14.186  1.00 23.54 ? 133 SER B C   1 
ATOM   3224  O  O   . SER B  1 133 ? -9.979  13.690  14.247  1.00 21.06 ? 133 SER B O   1 
ATOM   3225  C  CB  . SER B  1 133 ? -11.837 13.827  11.809  1.00 23.43 ? 133 SER B CB  1 
ATOM   3226  O  OG  . SER B  1 133 ? -11.631 15.206  11.442  1.00 24.20 ? 133 SER B OG  1 
ATOM   3227  N  N   . ASN B  1 134 ? -11.451 15.317  14.883  1.00 27.33 ? 134 ASN B N   1 
ATOM   3228  C  CA  . ASN B  1 134 ? -10.570 15.989  15.853  1.00 26.43 ? 134 ASN B CA  1 
ATOM   3229  C  C   . ASN B  1 134 ? -10.834 15.619  17.245  1.00 32.03 ? 134 ASN B C   1 
ATOM   3230  O  O   . ASN B  1 134 ? -10.253 16.204  18.175  1.00 36.59 ? 134 ASN B O   1 
ATOM   3231  C  CB  . ASN B  1 134 ? -10.711 17.526  15.742  1.00 31.76 ? 134 ASN B CB  1 
ATOM   3232  C  CG  . ASN B  1 134 ? -10.228 17.984  14.441  1.00 37.13 ? 134 ASN B CG  1 
ATOM   3233  O  OD1 . ASN B  1 134 ? -9.146  17.575  14.060  1.00 35.49 ? 134 ASN B OD1 1 
ATOM   3234  N  ND2 . ASN B  1 134 ? -11.027 18.722  13.710  1.00 41.13 ? 134 ASN B ND2 1 
ATOM   3235  N  N   . LYS B  1 135 ? -11.729 14.682  17.465  1.00 30.49 ? 135 LYS B N   1 
ATOM   3236  C  CA  . LYS B  1 135 ? -12.115 14.502  18.867  1.00 34.09 ? 135 LYS B CA  1 
ATOM   3237  C  C   . LYS B  1 135 ? -11.856 13.136  19.355  1.00 34.30 ? 135 LYS B C   1 
ATOM   3238  O  O   . LYS B  1 135 ? -11.774 12.207  18.566  1.00 25.79 ? 135 LYS B O   1 
ATOM   3239  C  CB  . LYS B  1 135 ? -13.528 15.001  19.143  1.00 40.31 ? 135 LYS B CB  1 
ATOM   3240  C  CG  . LYS B  1 135 ? -13.487 16.445  19.669  1.00 50.24 ? 135 LYS B CG  1 
ATOM   3241  C  CD  . LYS B  1 135 ? -14.676 17.274  19.209  1.00 52.93 ? 135 LYS B CD  1 
ATOM   3242  C  CE  . LYS B  1 135 ? -14.336 18.743  18.979  1.00 55.23 ? 135 LYS B CE  1 
ATOM   3243  N  NZ  . LYS B  1 135 ? -13.865 18.917  17.572  1.00 58.54 ? 135 LYS B NZ  1 
ATOM   3244  N  N   . SER B  1 136 ? -11.701 13.034  20.666  1.00 33.89 ? 136 SER B N   1 
ATOM   3245  C  CA  . SER B  1 136 ? -11.370 11.816  21.356  1.00 33.61 ? 136 SER B CA  1 
ATOM   3246  C  C   . SER B  1 136 ? -12.296 10.681  20.885  1.00 25.06 ? 136 SER B C   1 
ATOM   3247  O  O   . SER B  1 136 ? -13.447 10.836  20.957  1.00 28.53 ? 136 SER B O   1 
ATOM   3248  C  CB  . SER B  1 136 ? -11.576 12.109  22.854  1.00 37.06 ? 136 SER B CB  1 
ATOM   3249  O  OG  . SER B  1 136 ? -11.671 10.912  23.555  1.00 34.16 ? 136 SER B OG  1 
ATOM   3250  N  N   . GLU B  1 137 ? -11.753 9.582   20.342  1.00 25.53 ? 137 GLU B N   1 
ATOM   3251  C  CA  . GLU B  1 137 ? -12.586 8.448   19.761  1.00 28.96 ? 137 GLU B CA  1 
ATOM   3252  C  C   . GLU B  1 137 ? -13.756 8.928   18.847  1.00 22.22 ? 137 GLU B C   1 
ATOM   3253  O  O   . GLU B  1 137 ? -14.850 8.293   18.802  1.00 21.92 ? 137 GLU B O   1 
ATOM   3254  C  CB  . GLU B  1 137 ? -13.037 7.466   20.883  1.00 36.26 ? 137 GLU B CB  1 
ATOM   3255  C  CG  . GLU B  1 137 ? -14.104 8.020   21.839  1.00 47.36 ? 137 GLU B CG  1 
ATOM   3256  C  CD  . GLU B  1 137 ? -13.996 7.521   23.290  1.00 57.93 ? 137 GLU B CD  1 
ATOM   3257  O  OE1 . GLU B  1 137 ? -13.707 6.297   23.471  1.00 45.65 ? 137 GLU B OE1 1 
ATOM   3258  O  OE2 . GLU B  1 137 ? -14.234 8.370   24.228  1.00 53.56 ? 137 GLU B OE2 1 
ATOM   3259  N  N   . GLY B  1 138 ? -13.582 10.055  18.129  1.00 16.07 ? 138 GLY B N   1 
ATOM   3260  C  CA  . GLY B  1 138 ? -14.550 10.553  17.237  1.00 15.15 ? 138 GLY B CA  1 
ATOM   3261  C  C   . GLY B  1 138 ? -14.864 9.637   16.068  1.00 12.48 ? 138 GLY B C   1 
ATOM   3262  O  O   . GLY B  1 138 ? -15.922 9.744   15.477  1.00 14.18 ? 138 GLY B O   1 
ATOM   3263  N  N   . LEU B  1 139 ? -13.860 8.840   15.629  1.00 10.70 ? 139 LEU B N   1 
ATOM   3264  C  CA  . LEU B  1 139 ? -14.074 7.940   14.469  1.00 10.50 ? 139 LEU B CA  1 
ATOM   3265  C  C   . LEU B  1 139 ? -13.927 6.523   14.892  1.00 9.71  ? 139 LEU B C   1 
ATOM   3266  O  O   . LEU B  1 139 ? -13.199 6.201   15.846  1.00 10.55 ? 139 LEU B O   1 
ATOM   3267  C  CB  . LEU B  1 139 ? -13.032 8.211   13.385  1.00 11.31 ? 139 LEU B CB  1 
ATOM   3268  C  CG  . LEU B  1 139 ? -13.048 9.682   12.881  1.00 11.08 ? 139 LEU B CG  1 
ATOM   3269  C  CD1 . LEU B  1 139 ? -11.863 9.891   11.925  1.00 12.97 ? 139 LEU B CD1 1 
ATOM   3270  C  CD2 . LEU B  1 139 ? -14.369 9.975   12.167  1.00 13.38 ? 139 LEU B CD2 1 
ATOM   3271  N  N   . ALA B  1 140 ? -14.608 5.620   14.207  1.00 10.19 ? 140 ALA B N   1 
ATOM   3272  C  CA  . ALA B  1 140 ? -14.382 4.159   14.408  1.00 9.45  ? 140 ALA B CA  1 
ATOM   3273  C  C   . ALA B  1 140 ? -14.336 3.593   13.004  1.00 9.09  ? 140 ALA B C   1 
ATOM   3274  O  O   . ALA B  1 140 ? -15.203 3.861   12.116  1.00 10.13 ? 140 ALA B O   1 
ATOM   3275  C  CB  . ALA B  1 140 ? -15.579 3.542   15.164  1.00 10.56 ? 140 ALA B CB  1 
ATOM   3276  N  N   . VAL B  1 141 ? -13.302 2.834   12.733  1.00 8.34  ? 141 VAL B N   1 
ATOM   3277  C  CA  . VAL B  1 141 ? -13.150 2.201   11.425  1.00 7.95  ? 141 VAL B CA  1 
ATOM   3278  C  C   . VAL B  1 141 ? -13.249 0.714   11.542  1.00 9.16  ? 141 VAL B C   1 
ATOM   3279  O  O   . VAL B  1 141 ? -12.629 0.133   12.481  1.00 9.42  ? 141 VAL B O   1 
ATOM   3280  C  CB  . VAL B  1 141 ? -11.773 2.588   10.779  1.00 8.47  ? 141 VAL B CB  1 
ATOM   3281  C  CG1 . VAL B  1 141 ? -11.627 1.876   9.424   1.00 10.36 ? 141 VAL B CG1 1 
ATOM   3282  C  CG2 . VAL B  1 141 ? -11.746 4.085   10.601  1.00 9.64  ? 141 VAL B CG2 1 
ATOM   3283  N  N   . LEU B  1 142 ? -13.970 0.092   10.650  1.00 7.26  ? 142 LEU B N   1 
ATOM   3284  C  CA  . LEU B  1 142 ? -13.958 -1.395  10.512  1.00 8.53  ? 142 LEU B CA  1 
ATOM   3285  C  C   . LEU B  1 142 ? -13.018 -1.697  9.403   1.00 8.75  ? 142 LEU B C   1 
ATOM   3286  O  O   . LEU B  1 142 ? -13.155 -1.186  8.274   1.00 8.88  ? 142 LEU B O   1 
ATOM   3287  C  CB  . LEU B  1 142 ? -15.280 -1.975  10.184  1.00 9.68  ? 142 LEU B CB  1 
ATOM   3288  C  CG  . LEU B  1 142 ? -16.435 -1.645  11.126  1.00 9.59  ? 142 LEU B CG  1 
ATOM   3289  C  CD1 . LEU B  1 142 ? -17.687 -2.297  10.575  1.00 12.73 ? 142 LEU B CD1 1 
ATOM   3290  C  CD2 . LEU B  1 142 ? -16.140 -2.070  12.554  1.00 9.90  ? 142 LEU B CD2 1 
ATOM   3291  N  N   . ALA B  1 143 ? -12.022 -2.559  9.654   1.00 7.74  ? 143 ALA B N   1 
ATOM   3292  C  CA  . ALA B  1 143 ? -11.047 -2.955  8.638   1.00 6.88  ? 143 ALA B CA  1 
ATOM   3293  C  C   . ALA B  1 143 ? -11.160 -4.393  8.288   1.00 6.89  ? 143 ALA B C   1 
ATOM   3294  O  O   . ALA B  1 143 ? -11.263 -5.271  9.173   1.00 7.60  ? 143 ALA B O   1 
ATOM   3295  C  CB  . ALA B  1 143 ? -9.624  -2.716  9.159   1.00 8.79  ? 143 ALA B CB  1 
ATOM   3296  N  N   . VAL B  1 144 ? -11.266 -4.695  6.988   1.00 6.87  ? 144 VAL B N   1 
ATOM   3297  C  CA  . VAL B  1 144 ? -11.378 -6.072  6.482   1.00 7.06  ? 144 VAL B CA  1 
ATOM   3298  C  C   . VAL B  1 144 ? -10.076 -6.327  5.677   1.00 7.43  ? 144 VAL B C   1 
ATOM   3299  O  O   . VAL B  1 144 ? -9.776  -5.591  4.708   1.00 7.38  ? 144 VAL B O   1 
ATOM   3300  C  CB  . VAL B  1 144 ? -12.589 -6.268  5.605   1.00 7.54  ? 144 VAL B CB  1 
ATOM   3301  C  CG1 . VAL B  1 144 ? -12.663 -7.728  5.116   1.00 8.61  ? 144 VAL B CG1 1 
ATOM   3302  C  CG2 . VAL B  1 144 ? -13.862 -5.915  6.373   1.00 7.74  ? 144 VAL B CG2 1 
ATOM   3303  N  N   . LEU B  1 145 ? -9.342  -7.369  6.045   1.00 7.03  ? 145 LEU B N   1 
ATOM   3304  C  CA  . LEU B  1 145 ? -8.192  -7.855  5.316   1.00 7.41  ? 145 LEU B CA  1 
ATOM   3305  C  C   . LEU B  1 145 ? -8.645  -8.610  4.124   1.00 7.47  ? 145 LEU B C   1 
ATOM   3306  O  O   . LEU B  1 145 ? -9.585  -9.449  4.197   1.00 7.78  ? 145 LEU B O   1 
ATOM   3307  C  CB  . LEU B  1 145 ? -7.324  -8.723  6.263   1.00 8.24  ? 145 LEU B CB  1 
ATOM   3308  C  CG  . LEU B  1 145 ? -6.861  -7.927  7.471   1.00 9.30  ? 145 LEU B CG  1 
ATOM   3309  C  CD1 . LEU B  1 145 ? -6.234  -8.923  8.521   1.00 10.69 ? 145 LEU B CD1 1 
ATOM   3310  C  CD2 . LEU B  1 145 ? -5.738  -6.947  7.112   1.00 12.34 ? 145 LEU B CD2 1 
ATOM   3311  N  N   . ILE B  1 146 ? -8.053  -8.355  2.935   1.00 7.55  ? 146 ILE B N   1 
ATOM   3312  C  CA  . ILE B  1 146 ? -8.490  -8.974  1.703   1.00 8.06  ? 146 ILE B CA  1 
ATOM   3313  C  C   . ILE B  1 146 ? -7.346  -9.844  1.134   1.00 7.89  ? 146 ILE B C   1 
ATOM   3314  O  O   . ILE B  1 146 ? -6.224  -9.344  0.942   1.00 8.63  ? 146 ILE B O   1 
ATOM   3315  C  CB  . ILE B  1 146 ? -8.892  -7.918  0.683   1.00 7.44  ? 146 ILE B CB  1 
ATOM   3316  C  CG1 . ILE B  1 146 ? -10.065 -7.111  1.216   1.00 8.47  ? 146 ILE B CG1 1 
ATOM   3317  C  CG2 . ILE B  1 146 ? -9.204  -8.574  -0.679  1.00 8.46  ? 146 ILE B CG2 1 
ATOM   3318  C  CD1 . ILE B  1 146 ? -10.327 -5.814  0.413   1.00 8.34  ? 146 ILE B CD1 1 
ATOM   3319  N  N   A GLU B  1 147 ? -7.619  -11.108 0.900   0.50 8.17  ? 147 GLU B N   1 
ATOM   3320  N  N   B GLU B  1 147 ? -7.682  -11.097 0.893   0.50 8.14  ? 147 GLU B N   1 
ATOM   3321  C  CA  A GLU B  1 147 ? -6.582  -11.943 0.353   0.50 9.69  ? 147 GLU B CA  1 
ATOM   3322  C  CA  B GLU B  1 147 ? -6.752  -12.053 0.343   0.50 9.90  ? 147 GLU B CA  1 
ATOM   3323  C  C   A GLU B  1 147 ? -7.023  -12.477 -1.035  0.50 8.26  ? 147 GLU B C   1 
ATOM   3324  C  C   B GLU B  1 147 ? -7.061  -12.395 -1.125  0.50 8.42  ? 147 GLU B C   1 
ATOM   3325  O  O   A GLU B  1 147 ? -8.228  -12.520 -1.332  0.50 8.02  ? 147 GLU B O   1 
ATOM   3326  O  O   B GLU B  1 147 ? -8.198  -12.324 -1.562  0.50 8.88  ? 147 GLU B O   1 
ATOM   3327  C  CB  A GLU B  1 147 ? -6.459  -13.235 1.310   0.50 11.88 ? 147 GLU B CB  1 
ATOM   3328  C  CB  B GLU B  1 147 ? -6.903  -13.377 1.190   0.50 11.25 ? 147 GLU B CB  1 
ATOM   3329  C  CG  A GLU B  1 147 ? -7.500  -14.378 1.149   0.50 14.77 ? 147 GLU B CG  1 
ATOM   3330  C  CG  B GLU B  1 147 ? -5.828  -14.421 0.902   0.50 13.12 ? 147 GLU B CG  1 
ATOM   3331  C  CD  A GLU B  1 147 ? -7.401  -15.483 2.223   0.50 15.35 ? 147 GLU B CD  1 
ATOM   3332  C  CD  B GLU B  1 147 ? -5.516  -15.372 2.041   0.50 16.16 ? 147 GLU B CD  1 
ATOM   3333  O  OE1 A GLU B  1 147 ? -6.369  -15.526 2.927   0.50 14.80 ? 147 GLU B OE1 1 
ATOM   3334  O  OE1 B GLU B  1 147 ? -5.887  -15.064 3.183   0.50 18.24 ? 147 GLU B OE1 1 
ATOM   3335  O  OE2 A GLU B  1 147 ? -8.328  -16.320 2.393   0.50 16.59 ? 147 GLU B OE2 1 
ATOM   3336  O  OE2 B GLU B  1 147 ? -4.826  -16.388 1.814   0.50 21.57 ? 147 GLU B OE2 1 
ATOM   3337  N  N   . MET B  1 148 ? -6.035  -12.692 -1.893  1.00 8.35  ? 148 MET B N   1 
ATOM   3338  C  CA  . MET B  1 148 ? -6.254  -13.231 -3.223  1.00 8.35  ? 148 MET B CA  1 
ATOM   3339  C  C   . MET B  1 148 ? -6.810  -14.657 -3.112  1.00 9.18  ? 148 MET B C   1 
ATOM   3340  O  O   . MET B  1 148 ? -6.223  -15.534 -2.453  1.00 9.85  ? 148 MET B O   1 
ATOM   3341  C  CB  . MET B  1 148 ? -4.946  -13.286 -3.992  1.00 8.97  ? 148 MET B CB  1 
ATOM   3342  C  CG  . MET B  1 148 ? -5.137  -13.660 -5.429  1.00 9.60  ? 148 MET B CG  1 
ATOM   3343  S  SD  . MET B  1 148 ? -3.622  -13.753 -6.397  1.00 11.50 ? 148 MET B SD  1 
ATOM   3344  C  CE  . MET B  1 148 ? -3.196  -12.006 -6.444  1.00 10.76 ? 148 MET B CE  1 
ATOM   3345  N  N   . GLY B  1 149 ? -7.964  -14.797 -3.731  1.00 7.83  ? 149 GLY B N   1 
ATOM   3346  C  CA  . GLY B  1 149 ? -8.716  -16.077 -3.630  1.00 8.66  ? 149 GLY B CA  1 
ATOM   3347  C  C   . GLY B  1 149 ? -9.794  -16.136 -4.681  1.00 8.21  ? 149 GLY B C   1 
ATOM   3348  O  O   . GLY B  1 149 ? -9.616  -15.861 -5.880  1.00 9.04  ? 149 GLY B O   1 
ATOM   3349  N  N   . SER B  1 150 ? -10.954 -16.585 -4.218  1.00 8.34  ? 150 SER B N   1 
ATOM   3350  C  CA  . SER B  1 150 ? -12.178 -16.694 -5.075  1.00 9.23  ? 150 SER B CA  1 
ATOM   3351  C  C   . SER B  1 150 ? -12.710 -15.310 -5.463  1.00 9.40  ? 150 SER B C   1 
ATOM   3352  O  O   . SER B  1 150 ? -12.642 -14.337 -4.703  1.00 10.19 ? 150 SER B O   1 
ATOM   3353  C  CB  . SER B  1 150 ? -13.286 -17.383 -4.360  1.00 8.33  ? 150 SER B CB  1 
ATOM   3354  O  OG  . SER B  1 150 ? -12.891 -18.800 -4.196  1.00 9.92  ? 150 SER B OG  1 
ATOM   3355  N  N   . PHE B  1 151 ? -13.313 -15.289 -6.663  1.00 9.15  ? 151 PHE B N   1 
ATOM   3356  C  CA  . PHE B  1 151 ? -14.118 -14.139 -7.087  1.00 9.08  ? 151 PHE B CA  1 
ATOM   3357  C  C   . PHE B  1 151 ? -15.142 -13.850 -6.085  1.00 9.30  ? 151 PHE B C   1 
ATOM   3358  O  O   . PHE B  1 151 ? -15.790 -14.742 -5.499  1.00 11.01 ? 151 PHE B O   1 
ATOM   3359  C  CB  . PHE B  1 151 ? -14.747 -14.478 -8.436  1.00 9.32  ? 151 PHE B CB  1 
ATOM   3360  C  CG  . PHE B  1 151 ? -15.608 -13.356 -8.989  1.00 10.34 ? 151 PHE B CG  1 
ATOM   3361  C  CD1 . PHE B  1 151 ? -15.015 -12.230 -9.582  1.00 11.67 ? 151 PHE B CD1 1 
ATOM   3362  C  CD2 . PHE B  1 151 ? -16.936 -13.361 -8.821  1.00 10.15 ? 151 PHE B CD2 1 
ATOM   3363  C  CE1 . PHE B  1 151 ? -15.837 -11.177 -10.067 1.00 11.53 ? 151 PHE B CE1 1 
ATOM   3364  C  CE2 . PHE B  1 151 ? -17.801 -12.310 -9.307  1.00 11.93 ? 151 PHE B CE2 1 
ATOM   3365  C  CZ  . PHE B  1 151 ? -17.179 -11.207 -9.892  1.00 10.46 ? 151 PHE B CZ  1 
ATOM   3366  N  N   . ASN B  1 152 ? -15.369 -12.532 -5.786  1.00 8.17  ? 152 ASN B N   1 
ATOM   3367  C  CA  . ASN B  1 152 ? -16.293 -12.101 -4.761  1.00 8.85  ? 152 ASN B CA  1 
ATOM   3368  C  C   . ASN B  1 152 ? -17.346 -11.202 -5.399  1.00 9.89  ? 152 ASN B C   1 
ATOM   3369  O  O   . ASN B  1 152 ? -17.082 -10.017 -5.731  1.00 9.33  ? 152 ASN B O   1 
ATOM   3370  C  CB  . ASN B  1 152 ? -15.495 -11.306 -3.662  1.00 8.18  ? 152 ASN B CB  1 
ATOM   3371  C  CG  . ASN B  1 152 ? -16.327 -11.034 -2.463  1.00 8.84  ? 152 ASN B CG  1 
ATOM   3372  O  OD1 . ASN B  1 152 ? -17.449 -10.530 -2.541  1.00 9.61  ? 152 ASN B OD1 1 
ATOM   3373  N  ND2 . ASN B  1 152 ? -15.778 -11.331 -1.283  1.00 10.28 ? 152 ASN B ND2 1 
ATOM   3374  N  N   . PRO B  1 153 ? -18.553 -11.704 -5.609  1.00 9.56  ? 153 PRO B N   1 
ATOM   3375  C  CA  . PRO B  1 153 ? -19.623 -10.896 -6.284  1.00 9.68  ? 153 PRO B CA  1 
ATOM   3376  C  C   . PRO B  1 153 ? -19.970 -9.673  -5.490  1.00 11.12 ? 153 PRO B C   1 
ATOM   3377  O  O   . PRO B  1 153 ? -20.327 -8.635  -6.119  1.00 12.01 ? 153 PRO B O   1 
ATOM   3378  C  CB  . PRO B  1 153 ? -20.777 -11.888 -6.372  1.00 12.20 ? 153 PRO B CB  1 
ATOM   3379  C  CG  . PRO B  1 153 ? -20.134 -13.269 -6.338  1.00 15.07 ? 153 PRO B CG  1 
ATOM   3380  C  CD  . PRO B  1 153 ? -18.894 -13.147 -5.412  1.00 11.07 ? 153 PRO B CD  1 
ATOM   3381  N  N   . SER B  1 154 ? -19.865 -9.692  -4.156  1.00 9.36  ? 154 SER B N   1 
ATOM   3382  C  CA  . SER B  1 154 ? -20.243 -8.519  -3.380  1.00 8.80  ? 154 SER B CA  1 
ATOM   3383  C  C   . SER B  1 154 ? -19.247 -7.345  -3.584  1.00 10.57 ? 154 SER B C   1 
ATOM   3384  O  O   . SER B  1 154 ? -19.648 -6.196  -3.850  1.00 9.60  ? 154 SER B O   1 
ATOM   3385  C  CB  . SER B  1 154 ? -20.347 -8.837  -1.908  1.00 11.54 ? 154 SER B CB  1 
ATOM   3386  O  OG  . SER B  1 154 ? -21.318 -9.881  -1.744  1.00 15.72 ? 154 SER B OG  1 
ATOM   3387  N  N   . TYR B  1 155 ? -17.931 -7.651  -3.531  1.00 9.10  ? 155 TYR B N   1 
ATOM   3388  C  CA  . TYR B  1 155 ? -16.949 -6.609  -3.830  1.00 8.13  ? 155 TYR B CA  1 
ATOM   3389  C  C   . TYR B  1 155 ? -17.078 -6.177  -5.288  1.00 7.93  ? 155 TYR B C   1 
ATOM   3390  O  O   . TYR B  1 155 ? -16.761 -4.997  -5.617  1.00 8.86  ? 155 TYR B O   1 
ATOM   3391  C  CB  . TYR B  1 155 ? -15.500 -7.084  -3.522  1.00 8.06  ? 155 TYR B CB  1 
ATOM   3392  C  CG  . TYR B  1 155 ? -15.154 -6.951  -2.057  1.00 8.92  ? 155 TYR B CG  1 
ATOM   3393  C  CD1 . TYR B  1 155 ? -15.546 -7.903  -1.103  1.00 8.47  ? 155 TYR B CD1 1 
ATOM   3394  C  CD2 . TYR B  1 155 ? -14.404 -5.851  -1.597  1.00 8.68  ? 155 TYR B CD2 1 
ATOM   3395  C  CE1 . TYR B  1 155 ? -15.268 -7.768  0.233   1.00 9.16  ? 155 TYR B CE1 1 
ATOM   3396  C  CE2 . TYR B  1 155 ? -14.098 -5.718  -0.272  1.00 8.99  ? 155 TYR B CE2 1 
ATOM   3397  C  CZ  . TYR B  1 155 ? -14.592 -6.680  0.643   1.00 8.17  ? 155 TYR B CZ  1 
ATOM   3398  O  OH  . TYR B  1 155 ? -14.271 -6.528  1.982   1.00 9.54  ? 155 TYR B OH  1 
ATOM   3399  N  N   . ASP B  1 156 ? -17.498 -7.061  -6.174  1.00 8.71  ? 156 ASP B N   1 
ATOM   3400  C  CA  . ASP B  1 156 ? -17.644 -6.632  -7.534  1.00 8.19  ? 156 ASP B CA  1 
ATOM   3401  C  C   . ASP B  1 156 ? -18.771 -5.611  -7.692  1.00 8.37  ? 156 ASP B C   1 
ATOM   3402  O  O   . ASP B  1 156 ? -18.764 -4.898  -8.784  1.00 9.82  ? 156 ASP B O   1 
ATOM   3403  C  CB  . ASP B  1 156 ? -17.775 -7.833  -8.553  1.00 10.51 ? 156 ASP B CB  1 
ATOM   3404  C  CG  . ASP B  1 156 ? -16.823 -7.641  -9.706  1.00 10.11 ? 156 ASP B CG  1 
ATOM   3405  O  OD1 . ASP B  1 156 ? -15.661 -7.404  -9.533  1.00 11.39 ? 156 ASP B OD1 1 
ATOM   3406  O  OD2 . ASP B  1 156 ? -17.383 -7.709  -10.871 1.00 16.43 ? 156 ASP B OD2 1 
ATOM   3407  N  N   . LYS B  1 157 ? -19.709 -5.476  -6.748  1.00 8.50  ? 157 LYS B N   1 
ATOM   3408  C  CA  . LYS B  1 157 ? -20.724 -4.418  -6.871  1.00 10.81 ? 157 LYS B CA  1 
ATOM   3409  C  C   . LYS B  1 157 ? -20.009 -3.068  -6.836  1.00 10.57 ? 157 LYS B C   1 
ATOM   3410  O  O   . LYS B  1 157 ? -20.536 -2.091  -7.442  1.00 12.08 ? 157 LYS B O   1 
ATOM   3411  C  CB  . LYS B  1 157 ? -21.762 -4.570  -5.772  1.00 11.99 ? 157 LYS B CB  1 
ATOM   3412  C  CG  . LYS B  1 157 ? -22.585 -5.899  -5.965  1.00 13.54 ? 157 LYS B CG  1 
ATOM   3413  C  CD  . LYS B  1 157 ? -23.553 -6.216  -4.850  1.00 17.77 ? 157 LYS B CD  1 
ATOM   3414  C  CE  . LYS B  1 157 ? -24.333 -7.508  -5.225  1.00 21.94 ? 157 LYS B CE  1 
ATOM   3415  N  NZ  . LYS B  1 157 ? -24.889 -8.085  -3.949  1.00 25.80 ? 157 LYS B NZ  1 
ATOM   3416  N  N   . ILE B  1 158 ? -18.821 -2.971  -6.249  1.00 9.31  ? 158 ILE B N   1 
ATOM   3417  C  CA  . ILE B  1 158 ? -17.993 -1.749  -6.293  1.00 10.93 ? 158 ILE B CA  1 
ATOM   3418  C  C   . ILE B  1 158 ? -17.105 -1.808  -7.493  1.00 10.75 ? 158 ILE B C   1 
ATOM   3419  O  O   . ILE B  1 158 ? -17.022 -0.852  -8.310  1.00 10.10 ? 158 ILE B O   1 
ATOM   3420  C  CB  . ILE B  1 158 ? -17.203 -1.609  -5.018  1.00 10.83 ? 158 ILE B CB  1 
ATOM   3421  C  CG1 . ILE B  1 158 ? -18.192 -1.399  -3.877  1.00 12.58 ? 158 ILE B CG1 1 
ATOM   3422  C  CG2 . ILE B  1 158 ? -16.209 -0.369  -5.120  1.00 11.99 ? 158 ILE B CG2 1 
ATOM   3423  C  CD1 . ILE B  1 158 ? -17.481 -1.489  -2.494  1.00 15.39 ? 158 ILE B CD1 1 
ATOM   3424  N  N   . PHE B  1 159 ? -16.347 -2.897  -7.723  1.00 9.52  ? 159 PHE B N   1 
ATOM   3425  C  CA  . PHE B  1 159 ? -15.303 -2.899  -8.728  1.00 10.03 ? 159 PHE B CA  1 
ATOM   3426  C  C   . PHE B  1 159 ? -15.860 -2.779  -10.136 1.00 10.99 ? 159 PHE B C   1 
ATOM   3427  O  O   . PHE B  1 159 ? -15.126 -2.308  -11.015 1.00 13.50 ? 159 PHE B O   1 
ATOM   3428  C  CB  . PHE B  1 159 ? -14.459 -4.169  -8.622  1.00 10.76 ? 159 PHE B CB  1 
ATOM   3429  C  CG  . PHE B  1 159 ? -13.760 -4.341  -7.303  1.00 11.51 ? 159 PHE B CG  1 
ATOM   3430  C  CD1 . PHE B  1 159 ? -13.337 -3.251  -6.491  1.00 12.11 ? 159 PHE B CD1 1 
ATOM   3431  C  CD2 . PHE B  1 159 ? -13.475 -5.659  -6.871  1.00 11.57 ? 159 PHE B CD2 1 
ATOM   3432  C  CE1 . PHE B  1 159 ? -12.703 -3.507  -5.250  1.00 12.35 ? 159 PHE B CE1 1 
ATOM   3433  C  CE2 . PHE B  1 159 ? -12.794 -5.824  -5.656  1.00 10.80 ? 159 PHE B CE2 1 
ATOM   3434  C  CZ  . PHE B  1 159 ? -12.367 -4.799  -4.877  1.00 11.69 ? 159 PHE B CZ  1 
ATOM   3435  N  N   . SER B  1 160 ? -17.089 -3.188  -10.334 1.00 12.12 ? 160 SER B N   1 
ATOM   3436  C  CA  . SER B  1 160 ? -17.678 -3.073  -11.689 1.00 11.15 ? 160 SER B CA  1 
ATOM   3437  C  C   . SER B  1 160 ? -17.851 -1.653  -12.122 1.00 13.00 ? 160 SER B C   1 
ATOM   3438  O  O   . SER B  1 160 ? -17.979 -1.423  -13.357 1.00 15.17 ? 160 SER B O   1 
ATOM   3439  C  CB  . SER B  1 160 ? -19.009 -3.858  -11.748 1.00 14.61 ? 160 SER B CB  1 
ATOM   3440  O  OG  . SER B  1 160 ? -19.941 -3.308  -10.918 1.00 14.71 ? 160 SER B OG  1 
ATOM   3441  N  N   . HIS B  1 161 ? -17.696 -0.672  -11.217 1.00 11.63 ? 161 HIS B N   1 
ATOM   3442  C  CA  . HIS B  1 161 ? -17.789 0.768   -11.613 1.00 12.06 ? 161 HIS B CA  1 
ATOM   3443  C  C   . HIS B  1 161 ? -16.430 1.436   -11.754 1.00 14.18 ? 161 HIS B C   1 
ATOM   3444  O  O   . HIS B  1 161 ? -16.446 2.679   -12.030 1.00 14.14 ? 161 HIS B O   1 
ATOM   3445  C  CB  . HIS B  1 161 ? -18.582 1.480   -10.586 1.00 11.90 ? 161 HIS B CB  1 
ATOM   3446  C  CG  . HIS B  1 161 ? -20.013 1.021   -10.482 1.00 14.32 ? 161 HIS B CG  1 
ATOM   3447  N  ND1 . HIS B  1 161 ? -20.999 1.593   -11.263 1.00 14.87 ? 161 HIS B ND1 1 
ATOM   3448  C  CD2 . HIS B  1 161 ? -20.610 0.003   -9.808  1.00 14.56 ? 161 HIS B CD2 1 
ATOM   3449  C  CE1 . HIS B  1 161 ? -22.158 0.980   -11.027 1.00 14.06 ? 161 HIS B CE1 1 
ATOM   3450  N  NE2 . HIS B  1 161 ? -21.951 0.008   -10.133 1.00 14.81 ? 161 HIS B NE2 1 
ATOM   3451  N  N   . LEU B  1 162 ? -15.302 0.729   -11.606 1.00 14.29 ? 162 LEU B N   1 
ATOM   3452  C  CA  . LEU B  1 162 ? -13.993 1.421   -11.567 1.00 15.40 ? 162 LEU B CA  1 
ATOM   3453  C  C   . LEU B  1 162 ? -13.663 2.160   -12.804 1.00 16.30 ? 162 LEU B C   1 
ATOM   3454  O  O   . LEU B  1 162 ? -13.054 3.244   -12.706 1.00 14.94 ? 162 LEU B O   1 
ATOM   3455  C  CB  . LEU B  1 162 ? -12.901 0.427   -11.235 1.00 17.52 ? 162 LEU B CB  1 
ATOM   3456  C  CG  . LEU B  1 162 ? -12.932 -0.179  -9.827  1.00 18.32 ? 162 LEU B CG  1 
ATOM   3457  C  CD1 . LEU B  1 162 ? -11.969 -1.381  -9.814  1.00 19.02 ? 162 LEU B CD1 1 
ATOM   3458  C  CD2 . LEU B  1 162 ? -12.724 0.857   -8.718  1.00 21.91 ? 162 LEU B CD2 1 
ATOM   3459  N  N   . GLN B  1 163 ? -14.072 1.680   -13.951 1.00 16.54 ? 163 GLN B N   1 
ATOM   3460  C  CA  . GLN B  1 163 ? -13.715 2.408   -15.169 1.00 15.69 ? 163 GLN B CA  1 
ATOM   3461  C  C   . GLN B  1 163 ? -14.468 3.685   -15.365 1.00 16.57 ? 163 GLN B C   1 
ATOM   3462  O  O   . GLN B  1 163 ? -14.183 4.418   -16.340 1.00 20.13 ? 163 GLN B O   1 
ATOM   3463  C  CB  . GLN B  1 163 ? -13.869 1.485   -16.428 1.00 19.62 ? 163 GLN B CB  1 
ATOM   3464  C  CG  . GLN B  1 163 ? -12.916 0.240   -16.540 1.00 22.54 ? 163 GLN B CG  1 
ATOM   3465  C  CD  . GLN B  1 163 ? -11.385 0.489   -16.426 1.00 25.86 ? 163 GLN B CD  1 
ATOM   3466  O  OE1 . GLN B  1 163 ? -10.928 1.531   -16.709 1.00 28.59 ? 163 GLN B OE1 1 
ATOM   3467  N  NE2 . GLN B  1 163 ? -10.613 -0.536  -16.027 1.00 28.50 ? 163 GLN B NE2 1 
ATOM   3468  N  N   . HIS B  1 164 ? -15.386 4.007   -14.483 1.00 16.03 ? 164 HIS B N   1 
ATOM   3469  C  CA  . HIS B  1 164 ? -16.105 5.263   -14.477 1.00 13.51 ? 164 HIS B CA  1 
ATOM   3470  C  C   . HIS B  1 164 ? -15.625 6.333   -13.471 1.00 12.79 ? 164 HIS B C   1 
ATOM   3471  O  O   . HIS B  1 164 ? -16.141 7.438   -13.327 1.00 14.31 ? 164 HIS B O   1 
ATOM   3472  C  CB  . HIS B  1 164 ? -17.578 4.897   -14.405 1.00 17.86 ? 164 HIS B CB  1 
ATOM   3473  C  CG  . HIS B  1 164 ? -17.845 3.735   -15.352 1.00 18.63 ? 164 HIS B CG  1 
ATOM   3474  N  ND1 . HIS B  1 164 ? -17.503 3.793   -16.702 1.00 25.69 ? 164 HIS B ND1 1 
ATOM   3475  C  CD2 . HIS B  1 164 ? -18.272 2.459   -15.127 1.00 21.96 ? 164 HIS B CD2 1 
ATOM   3476  C  CE1 . HIS B  1 164 ? -17.761 2.619   -17.274 1.00 21.80 ? 164 HIS B CE1 1 
ATOM   3477  N  NE2 . HIS B  1 164 ? -18.233 1.795   -16.349 1.00 23.10 ? 164 HIS B NE2 1 
ATOM   3478  N  N   . VAL B  1 165 ? -14.655 5.897   -12.657 1.00 11.51 ? 165 VAL B N   1 
ATOM   3479  C  CA  . VAL B  1 165 ? -14.063 6.804   -11.677 1.00 10.79 ? 165 VAL B CA  1 
ATOM   3480  C  C   . VAL B  1 165 ? -12.538 6.755   -11.828 1.00 8.96  ? 165 VAL B C   1 
ATOM   3481  O  O   . VAL B  1 165 ? -11.771 6.817   -10.881 1.00 9.63  ? 165 VAL B O   1 
ATOM   3482  C  CB  . VAL B  1 165 ? -14.513 6.537   -10.212 1.00 11.48 ? 165 VAL B CB  1 
ATOM   3483  C  CG1 . VAL B  1 165 ? -15.963 6.974   -10.053 1.00 13.36 ? 165 VAL B CG1 1 
ATOM   3484  C  CG2 . VAL B  1 165 ? -14.261 5.086   -9.754  1.00 12.53 ? 165 VAL B CG2 1 
ATOM   3485  N  N   A LYS B  1 166 ? -12.019 6.600   -13.064 0.50 8.14  ? 166 LYS B N   1 
ATOM   3486  N  N   B LYS B  1 166 ? -12.144 6.658   -13.085 0.50 9.11  ? 166 LYS B N   1 
ATOM   3487  C  CA  A LYS B  1 166 ? -10.545 6.371   -13.265 0.50 8.14  ? 166 LYS B CA  1 
ATOM   3488  C  CA  B LYS B  1 166 ? -10.787 6.403   -13.403 0.50 9.74  ? 166 LYS B CA  1 
ATOM   3489  C  C   A LYS B  1 166 ? -9.706  7.587   -12.770 0.50 7.99  ? 166 LYS B C   1 
ATOM   3490  C  C   B LYS B  1 166 ? -9.846  7.514   -12.911 0.50 9.07  ? 166 LYS B C   1 
ATOM   3491  O  O   A LYS B  1 166 ? -8.561  7.452   -12.302 0.50 8.03  ? 166 LYS B O   1 
ATOM   3492  O  O   B LYS B  1 166 ? -8.757  7.193   -12.576 0.50 8.84  ? 166 LYS B O   1 
ATOM   3493  C  CB  A LYS B  1 166 ? -10.218 6.146   -14.754 0.50 7.75  ? 166 LYS B CB  1 
ATOM   3494  C  CB  B LYS B  1 166 ? -10.706 6.343   -14.909 0.50 10.18 ? 166 LYS B CB  1 
ATOM   3495  C  CG  A LYS B  1 166 ? -10.965 5.008   -15.393 0.50 7.26  ? 166 LYS B CG  1 
ATOM   3496  C  CG  B LYS B  1 166 ? -9.314  6.001   -15.313 0.50 12.44 ? 166 LYS B CG  1 
ATOM   3497  C  CD  A LYS B  1 166 ? -10.486 4.812   -16.806 0.50 8.65  ? 166 LYS B CD  1 
ATOM   3498  C  CD  B LYS B  1 166 ? -9.259  5.686   -16.812 0.50 14.14 ? 166 LYS B CD  1 
ATOM   3499  C  CE  A LYS B  1 166 ? -8.962  4.510   -16.989 0.50 10.04 ? 166 LYS B CE  1 
ATOM   3500  C  CE  B LYS B  1 166 ? -9.680  4.282   -17.254 0.50 17.64 ? 166 LYS B CE  1 
ATOM   3501  N  NZ  A LYS B  1 166 ? -8.488  3.248   -16.296 0.50 10.44 ? 166 LYS B NZ  1 
ATOM   3502  N  NZ  B LYS B  1 166 ? -9.100  3.084   -16.562 0.50 17.15 ? 166 LYS B NZ  1 
ATOM   3503  N  N   . TYR B  1 167 ? -10.285 8.790   -12.910 1.00 8.82  ? 167 TYR B N   1 
ATOM   3504  C  CA  . TYR B  1 167 ? -9.515  9.953   -12.528 1.00 8.30  ? 167 TYR B CA  1 
ATOM   3505  C  C   . TYR B  1 167 ? -9.970  10.754  -11.360 1.00 8.35  ? 167 TYR B C   1 
ATOM   3506  O  O   . TYR B  1 167 ? -11.171 10.717  -11.005 1.00 8.73  ? 167 TYR B O   1 
ATOM   3507  C  CB  . TYR B  1 167 ? -9.443  10.916  -13.831 1.00 9.99  ? 167 TYR B CB  1 
ATOM   3508  C  CG  . TYR B  1 167 ? -9.015  10.164  -15.069 1.00 10.11 ? 167 TYR B CG  1 
ATOM   3509  C  CD1 . TYR B  1 167 ? -7.680  9.778   -15.270 1.00 11.12 ? 167 TYR B CD1 1 
ATOM   3510  C  CD2 . TYR B  1 167 ? -9.968  9.814   -16.030 1.00 10.68 ? 167 TYR B CD2 1 
ATOM   3511  C  CE1 . TYR B  1 167 ? -7.318  9.060   -16.401 1.00 11.82 ? 167 TYR B CE1 1 
ATOM   3512  C  CE2 . TYR B  1 167 ? -9.636  9.101   -17.168 1.00 11.94 ? 167 TYR B CE2 1 
ATOM   3513  C  CZ  . TYR B  1 167 ? -8.308  8.717   -17.342 1.00 13.06 ? 167 TYR B CZ  1 
ATOM   3514  O  OH  . TYR B  1 167 ? -7.936  7.980   -18.446 1.00 16.89 ? 167 TYR B OH  1 
ATOM   3515  N  N   . LYS B  1 168 ? -9.032  11.459  -10.739 1.00 8.28  ? 168 LYS B N   1 
ATOM   3516  C  CA  . LYS B  1 168 ? -9.307  12.286  -9.565  1.00 10.02 ? 168 LYS B CA  1 
ATOM   3517  C  C   . LYS B  1 168 ? -10.527 13.191  -9.830  1.00 10.03 ? 168 LYS B C   1 
ATOM   3518  O  O   . LYS B  1 168 ? -10.620 13.864  -10.871 1.00 10.84 ? 168 LYS B O   1 
ATOM   3519  C  CB  . LYS B  1 168 ? -8.124  13.210  -9.252  1.00 10.59 ? 168 LYS B CB  1 
ATOM   3520  C  CG  . LYS B  1 168 ? -8.427  14.000  -7.987  1.00 10.96 ? 168 LYS B CG  1 
ATOM   3521  C  CD  . LYS B  1 168 ? -7.148  14.703  -7.521  1.00 13.10 ? 168 LYS B CD  1 
ATOM   3522  C  CE  . LYS B  1 168 ? -7.503  15.546  -6.291  1.00 17.49 ? 168 LYS B CE  1 
ATOM   3523  N  NZ  . LYS B  1 168 ? -6.314  16.284  -5.722  1.00 24.66 ? 168 LYS B NZ  1 
ATOM   3524  N  N   . GLY B  1 169 ? -11.466 13.202  -8.901  1.00 9.92  ? 169 GLY B N   1 
ATOM   3525  C  CA  . GLY B  1 169 ? -12.690 14.053  -8.969  1.00 11.41 ? 169 GLY B CA  1 
ATOM   3526  C  C   . GLY B  1 169 ? -13.851 13.436  -9.638  1.00 12.78 ? 169 GLY B C   1 
ATOM   3527  O  O   . GLY B  1 169 ? -14.941 14.005  -9.560  1.00 15.56 ? 169 GLY B O   1 
ATOM   3528  N  N   . GLN B  1 170 ? -13.681 12.324  -10.348 1.00 10.39 ? 170 GLN B N   1 
ATOM   3529  C  CA  . GLN B  1 170 ? -14.777 11.679  -11.049 1.00 10.66 ? 170 GLN B CA  1 
ATOM   3530  C  C   . GLN B  1 170 ? -15.681 10.966  -10.001 1.00 11.09 ? 170 GLN B C   1 
ATOM   3531  O  O   . GLN B  1 170 ? -15.195 10.457  -8.991  1.00 11.43 ? 170 GLN B O   1 
ATOM   3532  C  CB  . GLN B  1 170 ? -14.276 10.743  -12.106 1.00 10.61 ? 170 GLN B CB  1 
ATOM   3533  C  CG  . GLN B  1 170 ? -13.566 11.523  -13.248 1.00 12.60 ? 170 GLN B CG  1 
ATOM   3534  C  CD  . GLN B  1 170 ? -13.311 10.648  -14.395 1.00 12.66 ? 170 GLN B CD  1 
ATOM   3535  O  OE1 . GLN B  1 170 ? -12.815 9.504   -14.306 1.00 12.59 ? 170 GLN B OE1 1 
ATOM   3536  N  NE2 . GLN B  1 170 ? -13.451 11.254  -15.612 1.00 17.67 ? 170 GLN B NE2 1 
ATOM   3537  N  N   . GLU B  1 171 ? -16.940 10.914  -10.335 1.00 12.27 ? 171 GLU B N   1 
ATOM   3538  C  CA  . GLU B  1 171 ? -18.002 10.387  -9.491  1.00 12.37 ? 171 GLU B CA  1 
ATOM   3539  C  C   . GLU B  1 171 ? -18.828 9.411   -10.313 1.00 12.84 ? 171 GLU B C   1 
ATOM   3540  O  O   . GLU B  1 171 ? -19.079 9.589   -11.549 1.00 15.31 ? 171 GLU B O   1 
ATOM   3541  C  CB  . GLU B  1 171 ? -18.863 11.545  -8.994  1.00 15.74 ? 171 GLU B CB  1 
ATOM   3542  C  CG  . GLU B  1 171 ? -18.166 12.485  -8.032  1.00 17.55 ? 171 GLU B CG  1 
ATOM   3543  C  CD  . GLU B  1 171 ? -19.074 13.658  -7.627  1.00 20.15 ? 171 GLU B CD  1 
ATOM   3544  O  OE1 . GLU B  1 171 ? -20.094 13.878  -8.321  1.00 28.28 ? 171 GLU B OE1 1 
ATOM   3545  O  OE2 . GLU B  1 171 ? -18.741 14.260  -6.612  1.00 25.47 ? 171 GLU B OE2 1 
ATOM   3546  N  N   . ALA B  1 172 ? -19.364 8.381   -9.691  1.00 11.57 ? 172 ALA B N   1 
ATOM   3547  C  CA  . ALA B  1 172 ? -20.284 7.432   -10.261 1.00 12.08 ? 172 ALA B CA  1 
ATOM   3548  C  C   . ALA B  1 172 ? -21.285 7.046   -9.205  1.00 12.41 ? 172 ALA B C   1 
ATOM   3549  O  O   . ALA B  1 172 ? -21.073 7.375   -8.013  1.00 15.36 ? 172 ALA B O   1 
ATOM   3550  C  CB  . ALA B  1 172 ? -19.544 6.224   -10.830 1.00 13.47 ? 172 ALA B CB  1 
ATOM   3551  N  N   . PHE B  1 173 ? -22.421 6.502   -9.581  1.00 12.65 ? 173 PHE B N   1 
ATOM   3552  C  CA  . PHE B  1 173 ? -23.374 5.965   -8.657  1.00 11.23 ? 173 PHE B CA  1 
ATOM   3553  C  C   . PHE B  1 173 ? -23.394 4.455   -8.702  1.00 12.55 ? 173 PHE B C   1 
ATOM   3554  O  O   . PHE B  1 173 ? -23.256 3.814   -9.769  1.00 17.02 ? 173 PHE B O   1 
ATOM   3555  C  CB  . PHE B  1 173 ? -24.772 6.471   -9.057  1.00 14.74 ? 173 PHE B CB  1 
ATOM   3556  C  CG  . PHE B  1 173 ? -25.041 7.849   -8.536  1.00 16.16 ? 173 PHE B CG  1 
ATOM   3557  C  CD1 . PHE B  1 173 ? -25.105 8.083   -7.126  1.00 17.96 ? 173 PHE B CD1 1 
ATOM   3558  C  CD2 . PHE B  1 173 ? -25.335 8.932   -9.407  1.00 21.71 ? 173 PHE B CD2 1 
ATOM   3559  C  CE1 . PHE B  1 173 ? -25.391 9.331   -6.588  1.00 20.06 ? 173 PHE B CE1 1 
ATOM   3560  C  CE2 . PHE B  1 173 ? -25.580 10.217  -8.856  1.00 24.08 ? 173 PHE B CE2 1 
ATOM   3561  C  CZ  . PHE B  1 173 ? -25.611 10.423  -7.457  1.00 24.66 ? 173 PHE B CZ  1 
ATOM   3562  N  N   . VAL B  1 174 ? -23.422 3.900   -7.504  1.00 11.77 ? 174 VAL B N   1 
ATOM   3563  C  CA  . VAL B  1 174 ? -23.456 2.440   -7.289  1.00 11.66 ? 174 VAL B CA  1 
ATOM   3564  C  C   . VAL B  1 174 ? -24.798 2.104   -6.615  1.00 10.36 ? 174 VAL B C   1 
ATOM   3565  O  O   . VAL B  1 174 ? -25.114 2.666   -5.595  1.00 11.15 ? 174 VAL B O   1 
ATOM   3566  C  CB  . VAL B  1 174 ? -22.345 2.033   -6.309  1.00 11.17 ? 174 VAL B CB  1 
ATOM   3567  C  CG1 . VAL B  1 174 ? -22.390 0.531   -5.995  1.00 13.01 ? 174 VAL B CG1 1 
ATOM   3568  C  CG2 . VAL B  1 174 ? -20.967 2.343   -6.940  1.00 13.28 ? 174 VAL B CG2 1 
ATOM   3569  N  N   . PRO B  1 175 ? -25.614 1.200   -7.252  1.00 10.00 ? 175 PRO B N   1 
ATOM   3570  C  CA  . PRO B  1 175 ? -26.828 0.818   -6.581  1.00 10.02 ? 175 PRO B CA  1 
ATOM   3571  C  C   . PRO B  1 175 ? -26.548 0.273   -5.181  1.00 10.73 ? 175 PRO B C   1 
ATOM   3572  O  O   . PRO B  1 175 ? -25.549 -0.462  -4.965  1.00 10.98 ? 175 PRO B O   1 
ATOM   3573  C  CB  . PRO B  1 175 ? -27.419 -0.260  -7.477  1.00 10.71 ? 175 PRO B CB  1 
ATOM   3574  C  CG  . PRO B  1 175 ? -26.830 0.026   -8.884  1.00 10.90 ? 175 PRO B CG  1 
ATOM   3575  C  CD  . PRO B  1 175 ? -25.422 0.581   -8.555  1.00 10.75 ? 175 PRO B CD  1 
ATOM   3576  N  N   . GLY B  1 176 ? -27.483 0.411   -4.271  1.00 11.21 ? 176 GLY B N   1 
ATOM   3577  C  CA  . GLY B  1 176 ? -27.256 -0.163  -2.964  1.00 11.88 ? 176 GLY B CA  1 
ATOM   3578  C  C   . GLY B  1 176 ? -27.206 -1.668  -2.968  1.00 12.65 ? 176 GLY B C   1 
ATOM   3579  O  O   . GLY B  1 176 ? -27.801 -2.331  -3.805  1.00 12.56 ? 176 GLY B O   1 
ATOM   3580  N  N   . PHE B  1 177 ? -26.445 -2.117  -1.975  1.00 12.13 ? 177 PHE B N   1 
ATOM   3581  C  CA  . PHE B  1 177 ? -26.328 -3.598  -1.793  1.00 11.33 ? 177 PHE B CA  1 
ATOM   3582  C  C   . PHE B  1 177 ? -26.053 -3.732  -0.302  1.00 12.18 ? 177 PHE B C   1 
ATOM   3583  O  O   . PHE B  1 177 ? -25.883 -2.752  0.436   1.00 11.29 ? 177 PHE B O   1 
ATOM   3584  C  CB  . PHE B  1 177 ? -25.239 -4.234  -2.680  1.00 11.32 ? 177 PHE B CB  1 
ATOM   3585  C  CG  . PHE B  1 177 ? -23.853 -3.765  -2.367  1.00 10.89 ? 177 PHE B CG  1 
ATOM   3586  C  CD1 . PHE B  1 177 ? -23.403 -2.582  -2.948  1.00 12.12 ? 177 PHE B CD1 1 
ATOM   3587  C  CD2 . PHE B  1 177 ? -22.981 -4.610  -1.613  1.00 12.11 ? 177 PHE B CD2 1 
ATOM   3588  C  CE1 . PHE B  1 177 ? -22.094 -2.143  -2.735  1.00 13.37 ? 177 PHE B CE1 1 
ATOM   3589  C  CE2 . PHE B  1 177 ? -21.689 -4.126  -1.374  1.00 11.71 ? 177 PHE B CE2 1 
ATOM   3590  C  CZ  . PHE B  1 177 ? -21.237 -2.963  -1.947  1.00 12.56 ? 177 PHE B CZ  1 
ATOM   3591  N  N   . ASN B  1 178 ? -26.000 -4.983  0.166   1.00 12.24 ? 178 ASN B N   1 
ATOM   3592  C  CA  . ASN B  1 178 ? -25.770 -5.206  1.541   1.00 12.01 ? 178 ASN B CA  1 
ATOM   3593  C  C   . ASN B  1 178 ? -24.290 -5.180  1.867   1.00 11.33 ? 178 ASN B C   1 
ATOM   3594  O  O   . ASN B  1 178 ? -23.534 -6.067  1.573   1.00 11.60 ? 178 ASN B O   1 
ATOM   3595  C  CB  . ASN B  1 178 ? -26.442 -6.577  1.931   1.00 12.09 ? 178 ASN B CB  1 
ATOM   3596  C  CG  . ASN B  1 178 ? -26.305 -6.871  3.359   1.00 14.62 ? 178 ASN B CG  1 
ATOM   3597  O  OD1 . ASN B  1 178 ? -25.912 -6.059  4.214   1.00 13.40 ? 178 ASN B OD1 1 
ATOM   3598  N  ND2 . ASN B  1 178 ? -26.596 -8.177  3.678   1.00 15.71 ? 178 ASN B ND2 1 
ATOM   3599  N  N   . ILE B  1 179 ? -23.956 -4.068  2.486   1.00 10.58 ? 179 ILE B N   1 
ATOM   3600  C  CA  . ILE B  1 179 ? -22.520 -3.815  2.863   1.00 11.06 ? 179 ILE B CA  1 
ATOM   3601  C  C   . ILE B  1 179 ? -22.018 -4.927  3.778   1.00 10.94 ? 179 ILE B C   1 
ATOM   3602  O  O   . ILE B  1 179 ? -20.768 -5.136  3.841   1.00 10.21 ? 179 ILE B O   1 
ATOM   3603  C  CB  . ILE B  1 179 ? -22.399 -2.430  3.477   1.00 9.56  ? 179 ILE B CB  1 
ATOM   3604  C  CG1 . ILE B  1 179 ? -22.898 -1.305  2.505   1.00 10.06 ? 179 ILE B CG1 1 
ATOM   3605  C  CG2 . ILE B  1 179 ? -20.937 -2.158  3.846   1.00 10.35 ? 179 ILE B CG2 1 
ATOM   3606  C  CD1 . ILE B  1 179 ? -22.261 -1.381  1.097   1.00 10.39 ? 179 ILE B CD1 1 
ATOM   3607  N  N   . GLU B  1 180 ? -22.907 -5.540  4.585   1.00 10.93 ? 180 GLU B N   1 
ATOM   3608  C  CA  . GLU B  1 180 ? -22.396 -6.641  5.439   1.00 11.69 ? 180 GLU B CA  1 
ATOM   3609  C  C   . GLU B  1 180 ? -21.803 -7.727  4.619   1.00 10.60 ? 180 GLU B C   1 
ATOM   3610  O  O   . GLU B  1 180 ? -20.984 -8.525  5.167   1.00 12.10 ? 180 GLU B O   1 
ATOM   3611  C  CB  . GLU B  1 180 ? -23.529 -7.195  6.309   1.00 14.82 ? 180 GLU B CB  1 
ATOM   3612  C  CG  . GLU B  1 180 ? -22.967 -7.798  7.607   1.00 16.58 ? 180 GLU B CG  1 
ATOM   3613  C  CD  . GLU B  1 180 ? -24.049 -8.133  8.660   1.00 20.55 ? 180 GLU B CD  1 
ATOM   3614  O  OE1 . GLU B  1 180 ? -25.236 -7.731  8.456   1.00 20.99 ? 180 GLU B OE1 1 
ATOM   3615  O  OE2 . GLU B  1 180 ? -23.674 -8.816  9.649   1.00 23.97 ? 180 GLU B OE2 1 
ATOM   3616  N  N   . GLU B  1 181 ? -22.151 -7.875  3.332   1.00 11.00 ? 181 GLU B N   1 
ATOM   3617  C  CA  . GLU B  1 181 ? -21.533 -8.902  2.484   1.00 10.34 ? 181 GLU B CA  1 
ATOM   3618  C  C   . GLU B  1 181 ? -20.057 -8.662  2.237   1.00 10.78 ? 181 GLU B C   1 
ATOM   3619  O  O   . GLU B  1 181 ? -19.409 -9.593  1.712   1.00 11.75 ? 181 GLU B O   1 
ATOM   3620  C  CB  . GLU B  1 181 ? -22.224 -8.952  1.090   1.00 13.20 ? 181 GLU B CB  1 
ATOM   3621  C  CG  . GLU B  1 181 ? -23.684 -9.335  1.136   1.00 16.25 ? 181 GLU B CG  1 
ATOM   3622  C  CD  . GLU B  1 181 ? -24.364 -9.126  -0.224  1.00 22.23 ? 181 GLU B CD  1 
ATOM   3623  O  OE1 . GLU B  1 181 ? -23.714 -8.713  -1.269  1.00 22.04 ? 181 GLU B OE1 1 
ATOM   3624  O  OE2 . GLU B  1 181 ? -25.646 -9.323  -0.291  1.00 22.59 ? 181 GLU B OE2 1 
ATOM   3625  N  N   . LEU B  1 182 ? -19.571 -7.458  2.593   1.00 9.50  ? 182 LEU B N   1 
ATOM   3626  C  CA  . LEU B  1 182 ? -18.142 -7.153  2.398   1.00 9.22  ? 182 LEU B CA  1 
ATOM   3627  C  C   . LEU B  1 182 ? -17.384 -7.653  3.627   1.00 9.27  ? 182 LEU B C   1 
ATOM   3628  O  O   . LEU B  1 182 ? -16.143 -7.620  3.609   1.00 9.43  ? 182 LEU B O   1 
ATOM   3629  C  CB  . LEU B  1 182 ? -17.923 -5.640  2.254   1.00 9.46  ? 182 LEU B CB  1 
ATOM   3630  C  CG  . LEU B  1 182 ? -18.632 -5.030  1.010   1.00 8.26  ? 182 LEU B CG  1 
ATOM   3631  C  CD1 . LEU B  1 182 ? -18.311 -3.522  0.985   1.00 10.05 ? 182 LEU B CD1 1 
ATOM   3632  C  CD2 . LEU B  1 182 ? -18.234 -5.689  -0.304  1.00 9.44  ? 182 LEU B CD2 1 
ATOM   3633  N  N   . LEU B  1 183 ? -18.050 -7.963  4.754   1.00 9.96  ? 183 LEU B N   1 
ATOM   3634  C  CA  . LEU B  1 183 ? -17.374 -8.415  5.998   1.00 9.63  ? 183 LEU B CA  1 
ATOM   3635  C  C   . LEU B  1 183 ? -17.134 -9.886  5.938   1.00 9.47  ? 183 LEU B C   1 
ATOM   3636  O  O   . LEU B  1 183 ? -17.798 -10.649 5.243   1.00 11.38 ? 183 LEU B O   1 
ATOM   3637  C  CB  . LEU B  1 183 ? -18.306 -8.094  7.191   1.00 10.83 ? 183 LEU B CB  1 
ATOM   3638  C  CG  . LEU B  1 183 ? -18.668 -6.601  7.256   1.00 11.52 ? 183 LEU B CG  1 
ATOM   3639  C  CD1 . LEU B  1 183 ? -19.477 -6.350  8.568   1.00 14.93 ? 183 LEU B CD1 1 
ATOM   3640  C  CD2 . LEU B  1 183 ? -17.518 -5.642  7.193   1.00 13.86 ? 183 LEU B CD2 1 
ATOM   3641  N  N   . PRO B  1 184 ? -16.107 -10.350 6.707   1.00 9.07  ? 184 PRO B N   1 
ATOM   3642  C  CA  . PRO B  1 184 ? -15.730 -11.773 6.694   1.00 10.11 ? 184 PRO B CA  1 
ATOM   3643  C  C   . PRO B  1 184 ? -16.618 -12.543 7.601   1.00 14.18 ? 184 PRO B C   1 
ATOM   3644  O  O   . PRO B  1 184 ? -17.558 -12.066 8.228   1.00 13.92 ? 184 PRO B O   1 
ATOM   3645  C  CB  . PRO B  1 184 ? -14.329 -11.775 7.357   1.00 12.26 ? 184 PRO B CB  1 
ATOM   3646  C  CG  . PRO B  1 184 ? -14.405 -10.567 8.267   1.00 11.34 ? 184 PRO B CG  1 
ATOM   3647  C  CD  . PRO B  1 184 ? -15.220 -9.548  7.518   1.00 9.47  ? 184 PRO B CD  1 
ATOM   3648  N  N   . GLU B  1 185 ? -16.239 -13.825 7.627   1.00 15.22 ? 185 GLU B N   1 
ATOM   3649  C  CA  . GLU B  1 185 ? -16.833 -14.766 8.543   1.00 16.72 ? 185 GLU B CA  1 
ATOM   3650  C  C   . GLU B  1 185 ? -16.423 -14.436 9.974   1.00 16.09 ? 185 GLU B C   1 
ATOM   3651  O  O   . GLU B  1 185 ? -15.306 -13.895 10.253  1.00 15.64 ? 185 GLU B O   1 
ATOM   3652  C  CB  . GLU B  1 185 ? -16.300 -16.169 8.214   1.00 19.28 ? 185 GLU B CB  1 
ATOM   3653  C  CG  . GLU B  1 185 ? -16.911 -16.729 6.930   1.00 24.18 ? 185 GLU B CG  1 
ATOM   3654  C  CD  . GLU B  1 185 ? -16.700 -18.252 6.823   1.00 37.23 ? 185 GLU B CD  1 
ATOM   3655  O  OE1 . GLU B  1 185 ? -15.550 -18.690 6.547   1.00 42.87 ? 185 GLU B OE1 1 
ATOM   3656  O  OE2 . GLU B  1 185 ? -17.691 -19.003 7.042   1.00 45.37 ? 185 GLU B OE2 1 
ATOM   3657  N  N   . ARG B  1 186 ? -17.390 -14.650 10.881  1.00 14.23 ? 186 ARG B N   1 
ATOM   3658  C  CA  . ARG B  1 186 ? -17.115 -14.655 12.341  1.00 14.91 ? 186 ARG B CA  1 
ATOM   3659  C  C   . ARG B  1 186 ? -16.680 -13.232 12.742  1.00 12.09 ? 186 ARG B C   1 
ATOM   3660  O  O   . ARG B  1 186 ? -15.590 -13.019 13.289  1.00 13.96 ? 186 ARG B O   1 
ATOM   3661  C  CB  . ARG B  1 186 ? -16.152 -15.739 12.792  1.00 17.78 ? 186 ARG B CB  1 
ATOM   3662  C  CG  . ARG B  1 186 ? -16.746 -17.160 12.680  1.00 20.76 ? 186 ARG B CG  1 
ATOM   3663  C  CD  . ARG B  1 186 ? -15.750 -18.271 13.176  1.00 21.32 ? 186 ARG B CD  1 
ATOM   3664  N  NE  . ARG B  1 186 ? -14.484 -18.310 12.419  1.00 25.94 ? 186 ARG B NE  1 
ATOM   3665  C  CZ  . ARG B  1 186 ? -14.324 -18.775 11.181  1.00 33.85 ? 186 ARG B CZ  1 
ATOM   3666  N  NH1 . ARG B  1 186 ? -15.340 -19.265 10.494  1.00 39.76 ? 186 ARG B NH1 1 
ATOM   3667  N  NH2 . ARG B  1 186 ? -13.132 -18.740 10.598  1.00 38.40 ? 186 ARG B NH2 1 
ATOM   3668  N  N   . THR B  1 187 ? -17.506 -12.254 12.362  1.00 10.90 ? 187 THR B N   1 
ATOM   3669  C  CA  . THR B  1 187 ? -17.208 -10.911 12.785  1.00 9.88  ? 187 THR B CA  1 
ATOM   3670  C  C   . THR B  1 187 ? -17.067 -10.686 14.274  1.00 10.57 ? 187 THR B C   1 
ATOM   3671  O  O   . THR B  1 187 ? -16.551 -9.670  14.703  1.00 11.13 ? 187 THR B O   1 
ATOM   3672  C  CB  . THR B  1 187 ? -18.184 -9.899  12.175  1.00 10.86 ? 187 THR B CB  1 
ATOM   3673  O  OG1 . THR B  1 187 ? -19.527 -10.323 12.507  1.00 13.78 ? 187 THR B OG1 1 
ATOM   3674  C  CG2 . THR B  1 187 ? -18.002 -9.872  10.642  1.00 11.46 ? 187 THR B CG2 1 
ATOM   3675  N  N   . ALA B  1 188 ? -17.518 -11.643 15.091  1.00 10.86 ? 188 ALA B N   1 
ATOM   3676  C  CA  . ALA B  1 188 ? -17.305 -11.514 16.487  1.00 10.72 ? 188 ALA B CA  1 
ATOM   3677  C  C   . ALA B  1 188 ? -15.831 -11.590 16.903  1.00 9.40  ? 188 ALA B C   1 
ATOM   3678  O  O   . ALA B  1 188 ? -15.540 -11.148 17.970  1.00 10.77 ? 188 ALA B O   1 
ATOM   3679  C  CB  . ALA B  1 188 ? -18.024 -12.692 17.216  1.00 13.14 ? 188 ALA B CB  1 
ATOM   3680  N  N   . GLU B  1 189 ? -14.967 -12.119 16.021  1.00 10.31 ? 189 GLU B N   1 
ATOM   3681  C  CA  . GLU B  1 189 ? -13.557 -12.199 16.315  1.00 9.22  ? 189 GLU B CA  1 
ATOM   3682  C  C   . GLU B  1 189 ? -12.822 -11.040 15.641  1.00 8.86  ? 189 GLU B C   1 
ATOM   3683  O  O   . GLU B  1 189 ? -12.796 -10.919 14.347  1.00 9.27  ? 189 GLU B O   1 
ATOM   3684  C  CB  . GLU B  1 189 ? -13.009 -13.499 15.752  1.00 11.33 ? 189 GLU B CB  1 
ATOM   3685  C  CG  . GLU B  1 189 ? -13.757 -14.705 16.401  1.00 15.90 ? 189 GLU B CG  1 
ATOM   3686  C  CD  . GLU B  1 189 ? -13.328 -16.037 15.943  1.00 20.95 ? 189 GLU B CD  1 
ATOM   3687  O  OE1 . GLU B  1 189 ? -12.164 -16.289 15.667  1.00 21.71 ? 189 GLU B OE1 1 
ATOM   3688  O  OE2 . GLU B  1 189 ? -14.204 -16.972 15.939  1.00 24.16 ? 189 GLU B OE2 1 
ATOM   3689  N  N   . TYR B  1 190 ? -12.286 -10.165 16.433  1.00 7.86  ? 190 TYR B N   1 
ATOM   3690  C  CA  . TYR B  1 190 ? -11.607 -8.942  15.929  1.00 8.23  ? 190 TYR B CA  1 
ATOM   3691  C  C   . TYR B  1 190 ? -10.534 -8.517  16.851  1.00 9.01  ? 190 TYR B C   1 
ATOM   3692  O  O   . TYR B  1 190 ? -10.471 -8.861  18.043  1.00 9.61  ? 190 TYR B O   1 
ATOM   3693  C  CB  . TYR B  1 190 ? -12.666 -7.828  15.685  1.00 8.26  ? 190 TYR B CB  1 
ATOM   3694  C  CG  . TYR B  1 190 ? -13.464 -7.413  16.891  1.00 7.29  ? 190 TYR B CG  1 
ATOM   3695  C  CD1 . TYR B  1 190 ? -12.976 -6.521  17.839  1.00 7.90  ? 190 TYR B CD1 1 
ATOM   3696  C  CD2 . TYR B  1 190 ? -14.785 -7.953  17.051  1.00 8.56  ? 190 TYR B CD2 1 
ATOM   3697  C  CE1 . TYR B  1 190 ? -13.796 -6.134  18.933  1.00 8.03  ? 190 TYR B CE1 1 
ATOM   3698  C  CE2 . TYR B  1 190 ? -15.552 -7.616  18.173  1.00 8.80  ? 190 TYR B CE2 1 
ATOM   3699  C  CZ  . TYR B  1 190 ? -15.079 -6.713  19.061  1.00 8.74  ? 190 TYR B CZ  1 
ATOM   3700  O  OH  . TYR B  1 190 ? -15.803 -6.253  20.200  1.00 11.27 ? 190 TYR B OH  1 
ATOM   3701  N  N   . TYR B  1 191 ? -9.655  -7.660  16.325  1.00 8.61  ? 191 TYR B N   1 
ATOM   3702  C  CA  . TYR B  1 191 ? -8.661  -6.891  17.031  1.00 8.26  ? 191 TYR B CA  1 
ATOM   3703  C  C   . TYR B  1 191 ? -9.163  -5.485  17.240  1.00 8.32  ? 191 TYR B C   1 
ATOM   3704  O  O   . TYR B  1 191 ? -9.778  -4.867  16.347  1.00 8.71  ? 191 TYR B O   1 
ATOM   3705  C  CB  . TYR B  1 191 ? -7.324  -6.794  16.193  1.00 8.96  ? 191 TYR B CB  1 
ATOM   3706  C  CG  . TYR B  1 191 ? -6.734  -8.094  15.638  1.00 8.39  ? 191 TYR B CG  1 
ATOM   3707  C  CD1 . TYR B  1 191 ? -5.707  -8.742  16.335  1.00 9.92  ? 191 TYR B CD1 1 
ATOM   3708  C  CD2 . TYR B  1 191 ? -7.077  -8.559  14.423  1.00 8.98  ? 191 TYR B CD2 1 
ATOM   3709  C  CE1 . TYR B  1 191 ? -5.140  -9.882  15.823  1.00 9.41  ? 191 TYR B CE1 1 
ATOM   3710  C  CE2 . TYR B  1 191 ? -6.505  -9.664  13.830  1.00 9.74  ? 191 TYR B CE2 1 
ATOM   3711  C  CZ  . TYR B  1 191 ? -5.541  -10.316 14.569  1.00 9.85  ? 191 TYR B CZ  1 
ATOM   3712  O  OH  . TYR B  1 191 ? -4.942  -11.431 13.965  1.00 12.67 ? 191 TYR B OH  1 
ATOM   3713  N  N   . ARG B  1 192 ? -8.869  -4.909  18.377  1.00 8.40  ? 192 ARG B N   1 
ATOM   3714  C  CA  . ARG B  1 192 ? -9.286  -3.579  18.727  1.00 8.60  ? 192 ARG B CA  1 
ATOM   3715  C  C   . ARG B  1 192 ? -8.164  -2.784  19.268  1.00 8.93  ? 192 ARG B C   1 
ATOM   3716  O  O   . ARG B  1 192 ? -7.449  -3.236  20.191  1.00 9.60  ? 192 ARG B O   1 
ATOM   3717  C  CB  . ARG B  1 192 ? -10.384 -3.689  19.784  1.00 9.58  ? 192 ARG B CB  1 
ATOM   3718  C  CG  . ARG B  1 192 ? -10.781 -2.424  20.515  1.00 10.94 ? 192 ARG B CG  1 
ATOM   3719  C  CD  . ARG B  1 192 ? -11.430 -1.339  19.652  1.00 11.45 ? 192 ARG B CD  1 
ATOM   3720  N  NE  . ARG B  1 192 ? -12.575 -1.835  18.890  1.00 10.91 ? 192 ARG B NE  1 
ATOM   3721  C  CZ  . ARG B  1 192 ? -13.782 -2.190  19.356  1.00 11.26 ? 192 ARG B CZ  1 
ATOM   3722  N  NH1 . ARG B  1 192 ? -14.043 -2.061  20.703  1.00 13.22 ? 192 ARG B NH1 1 
ATOM   3723  N  NH2 . ARG B  1 192 ? -14.708 -2.705  18.572  1.00 11.76 ? 192 ARG B NH2 1 
ATOM   3724  N  N   . TYR B  1 193 ? -7.923  -1.600  18.790  1.00 8.10  ? 193 TYR B N   1 
ATOM   3725  C  CA  . TYR B  1 193 ? -6.884  -0.722  19.348  1.00 9.00  ? 193 TYR B CA  1 
ATOM   3726  C  C   . TYR B  1 193 ? -7.150  0.718   19.048  1.00 9.91  ? 193 TYR B C   1 
ATOM   3727  O  O   . TYR B  1 193 ? -7.973  1.010   18.151  1.00 9.92  ? 193 TYR B O   1 
ATOM   3728  C  CB  . TYR B  1 193 ? -5.502  -1.160  18.910  1.00 8.72  ? 193 TYR B CB  1 
ATOM   3729  C  CG  . TYR B  1 193 ? -5.132  -0.741  17.457  1.00 8.00  ? 193 TYR B CG  1 
ATOM   3730  C  CD1 . TYR B  1 193 ? -5.534  -1.500  16.360  1.00 9.01  ? 193 TYR B CD1 1 
ATOM   3731  C  CD2 . TYR B  1 193 ? -4.328  0.380   17.241  1.00 9.37  ? 193 TYR B CD2 1 
ATOM   3732  C  CE1 . TYR B  1 193 ? -5.253  -1.069  15.047  1.00 8.02  ? 193 TYR B CE1 1 
ATOM   3733  C  CE2 . TYR B  1 193 ? -4.006  0.799   16.004  1.00 8.25  ? 193 TYR B CE2 1 
ATOM   3734  C  CZ  . TYR B  1 193 ? -4.466  0.097   14.912  1.00 8.25  ? 193 TYR B CZ  1 
ATOM   3735  O  OH  . TYR B  1 193 ? -4.106  0.500   13.654  1.00 8.64  ? 193 TYR B OH  1 
ATOM   3736  N  N   . ARG B  1 194 ? -6.498  1.615   19.806  1.00 11.39 ? 194 ARG B N   1 
ATOM   3737  C  CA  . ARG B  1 194 ? -6.615  3.051   19.592  1.00 11.27 ? 194 ARG B CA  1 
ATOM   3738  C  C   . ARG B  1 194 ? -5.511  3.482   18.671  1.00 10.91 ? 194 ARG B C   1 
ATOM   3739  O  O   . ARG B  1 194 ? -4.346  3.245   18.860  1.00 11.94 ? 194 ARG B O   1 
ATOM   3740  C  CB  . ARG B  1 194 ? -6.455  3.796   20.918  1.00 15.69 ? 194 ARG B CB  1 
ATOM   3741  C  CG  . ARG B  1 194 ? -7.369  3.311   22.018  1.00 25.00 ? 194 ARG B CG  1 
ATOM   3742  C  CD  . ARG B  1 194 ? -8.609  4.194   22.077  1.00 36.29 ? 194 ARG B CD  1 
ATOM   3743  N  NE  . ARG B  1 194 ? -9.244  4.285   23.424  1.00 51.50 ? 194 ARG B NE  1 
ATOM   3744  C  CZ  . ARG B  1 194 ? -10.491 4.720   23.655  1.00 55.99 ? 194 ARG B CZ  1 
ATOM   3745  N  NH1 . ARG B  1 194 ? -11.277 5.144   22.664  1.00 59.55 ? 194 ARG B NH1 1 
ATOM   3746  N  NH2 . ARG B  1 194 ? -10.965 4.731   24.894  1.00 63.02 ? 194 ARG B NH2 1 
ATOM   3747  N  N   . GLY B  1 195 ? -5.929  4.146   17.567  1.00 9.55  ? 195 GLY B N   1 
ATOM   3748  C  CA  . GLY B  1 195 ? -4.925  4.581   16.556  1.00 10.36 ? 195 GLY B CA  1 
ATOM   3749  C  C   . GLY B  1 195 ? -5.408  5.834   15.869  1.00 9.76  ? 195 GLY B C   1 
ATOM   3750  O  O   . GLY B  1 195 ? -6.026  6.726   16.433  1.00 10.30 ? 195 GLY B O   1 
ATOM   3751  N  N   . SER B  1 196 ? -5.078  5.899   14.579  1.00 8.78  ? 196 SER B N   1 
ATOM   3752  C  CA  . SER B  1 196 ? -5.150  7.186   13.880  1.00 8.82  ? 196 SER B CA  1 
ATOM   3753  C  C   . SER B  1 196 ? -5.711  6.931   12.497  1.00 8.05  ? 196 SER B C   1 
ATOM   3754  O  O   . SER B  1 196 ? -5.814  5.797   11.961  1.00 8.18  ? 196 SER B O   1 
ATOM   3755  C  CB  . SER B  1 196 ? -3.747  7.836   13.698  1.00 8.69  ? 196 SER B CB  1 
ATOM   3756  O  OG  . SER B  1 196 ? -2.956  7.133   12.731  1.00 7.60  ? 196 SER B OG  1 
ATOM   3757  N  N   . LEU B  1 197 ? -6.026  8.010   11.808  1.00 8.40  ? 197 LEU B N   1 
ATOM   3758  C  CA  . LEU B  1 197 ? -6.143  7.943   10.318  1.00 8.37  ? 197 LEU B CA  1 
ATOM   3759  C  C   . LEU B  1 197 ? -4.845  7.441   9.745   1.00 7.89  ? 197 LEU B C   1 
ATOM   3760  O  O   . LEU B  1 197 ? -3.764  7.821   10.193  1.00 8.14  ? 197 LEU B O   1 
ATOM   3761  C  CB  . LEU B  1 197 ? -6.432  9.353   9.687   1.00 9.24  ? 197 LEU B CB  1 
ATOM   3762  C  CG  . LEU B  1 197 ? -7.846  9.790   9.566   1.00 11.24 ? 197 LEU B CG  1 
ATOM   3763  C  CD1 . LEU B  1 197 ? -8.422  10.130  10.900  1.00 15.06 ? 197 LEU B CD1 1 
ATOM   3764  C  CD2 . LEU B  1 197 ? -7.861  11.082  8.710   1.00 13.28 ? 197 LEU B CD2 1 
ATOM   3765  N  N   . THR B  1 198 ? -4.935  6.574   8.698   1.00 7.18  ? 198 THR B N   1 
ATOM   3766  C  CA  . THR B  1 198 ? -3.685  6.103   8.080   1.00 7.66  ? 198 THR B CA  1 
ATOM   3767  C  C   . THR B  1 198 ? -3.228  7.002   6.926   1.00 6.79  ? 198 THR B C   1 
ATOM   3768  O  O   . THR B  1 198 ? -2.221  6.727   6.279   1.00 8.17  ? 198 THR B O   1 
ATOM   3769  C  CB  . THR B  1 198 ? -3.790  4.685   7.551   1.00 7.19  ? 198 THR B CB  1 
ATOM   3770  O  OG1 . THR B  1 198 ? -4.757  4.724   6.504   1.00 7.27  ? 198 THR B OG1 1 
ATOM   3771  C  CG2 . THR B  1 198 ? -4.209  3.710   8.605   1.00 8.17  ? 198 THR B CG2 1 
ATOM   3772  N  N   . THR B  1 199 ? -4.035  8.087   6.675   1.00 7.60  ? 199 THR B N   1 
ATOM   3773  C  CA  . THR B  1 199 ? -3.708  9.078   5.673   1.00 7.69  ? 199 THR B CA  1 
ATOM   3774  C  C   . THR B  1 199 ? -3.630  10.401  6.389   1.00 8.06  ? 199 THR B C   1 
ATOM   3775  O  O   . THR B  1 199 ? -4.257  10.603  7.417   1.00 9.13  ? 199 THR B O   1 
ATOM   3776  C  CB  . THR B  1 199 ? -4.860  9.187   4.603   1.00 7.77  ? 199 THR B CB  1 
ATOM   3777  O  OG1 . THR B  1 199 ? -6.073  9.551   5.215   1.00 10.03 ? 199 THR B OG1 1 
ATOM   3778  C  CG2 . THR B  1 199 ? -5.067  7.806   3.980   1.00 8.46  ? 199 THR B CG2 1 
ATOM   3779  N  N   . PRO B  1 200 ? -2.879  11.355  5.777   1.00 7.79  ? 200 PRO B N   1 
ATOM   3780  C  CA  . PRO B  1 200 ? -2.990  12.742  6.271   1.00 8.26  ? 200 PRO B CA  1 
ATOM   3781  C  C   . PRO B  1 200 ? -4.485  13.143  6.420   1.00 8.93  ? 200 PRO B C   1 
ATOM   3782  O  O   . PRO B  1 200 ? -5.271  12.766  5.585   1.00 11.78 ? 200 PRO B O   1 
ATOM   3783  C  CB  . PRO B  1 200 ? -2.295  13.520  5.139   1.00 8.69  ? 200 PRO B CB  1 
ATOM   3784  C  CG  . PRO B  1 200 ? -1.212  12.609  4.687   1.00 8.83  ? 200 PRO B CG  1 
ATOM   3785  C  CD  . PRO B  1 200 ? -1.975  11.231  4.660   1.00 8.49  ? 200 PRO B CD  1 
ATOM   3786  N  N   A PRO B  1 201 ? -4.818  13.874  7.463   0.50 8.74  ? 201 PRO B N   1 
ATOM   3787  N  N   B PRO B  1 201 ? -4.769  13.959  7.442   0.50 10.00 ? 201 PRO B N   1 
ATOM   3788  C  CA  A PRO B  1 201 ? -3.944  14.505  8.451   0.50 7.89  ? 201 PRO B CA  1 
ATOM   3789  C  CA  B PRO B  1 201 ? -3.848  14.528  8.459   0.50 9.14  ? 201 PRO B CA  1 
ATOM   3790  C  C   A PRO B  1 201 ? -3.575  13.620  9.670   0.50 8.06  ? 201 PRO B C   1 
ATOM   3791  C  C   B PRO B  1 201 ? -3.397  13.582  9.554   0.50 8.99  ? 201 PRO B C   1 
ATOM   3792  O  O   A PRO B  1 201 ? -3.038  14.081  10.689  0.50 7.46  ? 201 PRO B O   1 
ATOM   3793  O  O   B PRO B  1 201 ? -2.690  14.000  10.407  0.50 8.68  ? 201 PRO B O   1 
ATOM   3794  C  CB  A PRO B  1 201 ? -4.788  15.727  8.871   0.50 8.21  ? 201 PRO B CB  1 
ATOM   3795  C  CB  B PRO B  1 201 ? -4.680  15.653  9.148   0.50 10.32 ? 201 PRO B CB  1 
ATOM   3796  C  CG  A PRO B  1 201 ? -6.167  15.146  8.849   0.50 7.40  ? 201 PRO B CG  1 
ATOM   3797  C  CG  B PRO B  1 201 ? -5.789  15.861  8.205   0.50 10.66 ? 201 PRO B CG  1 
ATOM   3798  C  CD  A PRO B  1 201 ? -6.228  14.263  7.655   0.50 7.98  ? 201 PRO B CD  1 
ATOM   3799  C  CD  B PRO B  1 201 ? -6.093  14.586  7.511   0.50 9.77  ? 201 PRO B CD  1 
ATOM   3800  N  N   . CYS B  1 202 ? -3.799  12.305  9.571   1.00 8.60  ? 202 CYS B N   1 
ATOM   3801  C  CA  . CYS B  1 202 ? -3.274  11.270  10.561  1.00 8.81  ? 202 CYS B CA  1 
ATOM   3802  C  C   . CYS B  1 202 ? -3.771  11.549  12.003  1.00 9.77  ? 202 CYS B C   1 
ATOM   3803  O  O   . CYS B  1 202 ? -3.068  11.152  12.942  1.00 10.18 ? 202 CYS B O   1 
ATOM   3804  C  CB  . CYS B  1 202 ? -1.737  11.231  10.576  1.00 9.40  ? 202 CYS B CB  1 
ATOM   3805  S  SG  . CYS B  1 202 ? -0.960  10.899  8.975   1.00 9.46  ? 202 CYS B SG  1 
ATOM   3806  N  N   A ASN B  1 203 ? -4.966  12.122  12.134  0.50 11.09 ? 203 ASN B N   1 
ATOM   3807  N  N   B ASN B  1 203 ? -4.965  12.129  12.138  0.50 11.20 ? 203 ASN B N   1 
ATOM   3808  C  CA  A ASN B  1 203 ? -5.524  12.466  13.456  0.50 11.49 ? 203 ASN B CA  1 
ATOM   3809  C  CA  B ASN B  1 203 ? -5.473  12.447  13.479  0.50 11.64 ? 203 ASN B CA  1 
ATOM   3810  C  C   A ASN B  1 203 ? -5.602  11.232  14.322  0.50 12.41 ? 203 ASN B C   1 
ATOM   3811  C  C   B ASN B  1 203 ? -5.467  11.185  14.316  0.50 12.27 ? 203 ASN B C   1 
ATOM   3812  O  O   A ASN B  1 203 ? -6.188  10.248  13.887  0.50 10.05 ? 203 ASN B O   1 
ATOM   3813  O  O   B ASN B  1 203 ? -5.855  10.132  13.871  0.50 9.59  ? 203 ASN B O   1 
ATOM   3814  C  CB  A ASN B  1 203 ? -6.931  12.997  13.341  0.50 13.22 ? 203 ASN B CB  1 
ATOM   3815  C  CB  B ASN B  1 203 ? -6.873  13.040  13.507  0.50 13.63 ? 203 ASN B CB  1 
ATOM   3816  C  CG  A ASN B  1 203 ? -7.010  14.163  12.374  0.50 14.67 ? 203 ASN B CG  1 
ATOM   3817  C  CG  B ASN B  1 203 ? -6.999  14.263  12.600  0.50 15.84 ? 203 ASN B CG  1 
ATOM   3818  O  OD1 A ASN B  1 203 ? -6.873  13.969  11.196  0.50 14.82 ? 203 ASN B OD1 1 
ATOM   3819  O  OD1 B ASN B  1 203 ? -6.019  14.731  12.049  0.50 15.21 ? 203 ASN B OD1 1 
ATOM   3820  N  ND2 A ASN B  1 203 ? -7.200  15.381  12.896  0.50 15.32 ? 203 ASN B ND2 1 
ATOM   3821  N  ND2 B ASN B  1 203 ? -8.226  14.758  12.435  0.50 16.30 ? 203 ASN B ND2 1 
ATOM   3822  N  N   . PRO B  1 204 ? -5.064  11.266  15.591  1.00 11.30 ? 204 PRO B N   1 
ATOM   3823  C  CA  . PRO B  1 204 ? -5.024  10.062  16.470  1.00 12.81 ? 204 PRO B CA  1 
ATOM   3824  C  C   . PRO B  1 204 ? -6.388  9.847   17.163  1.00 13.32 ? 204 PRO B C   1 
ATOM   3825  O  O   . PRO B  1 204 ? -6.460  9.849   18.445  1.00 15.34 ? 204 PRO B O   1 
ATOM   3826  C  CB  . PRO B  1 204 ? -3.844  10.365  17.417  1.00 12.53 ? 204 PRO B CB  1 
ATOM   3827  C  CG  . PRO B  1 204 ? -3.899  11.901  17.561  1.00 13.14 ? 204 PRO B CG  1 
ATOM   3828  C  CD  . PRO B  1 204 ? -4.294  12.421  16.147  1.00 13.09 ? 204 PRO B CD  1 
ATOM   3829  N  N   . THR B  1 205 ? -7.443  9.735   16.378  1.00 10.25 ? 205 THR B N   1 
ATOM   3830  C  CA  . THR B  1 205 ? -8.785  9.818   16.877  1.00 11.59 ? 205 THR B CA  1 
ATOM   3831  C  C   . THR B  1 205 ? -9.653  8.663   16.447  1.00 10.23 ? 205 THR B C   1 
ATOM   3832  O  O   . THR B  1 205 ? -10.860 8.754   16.495  1.00 12.12 ? 205 THR B O   1 
ATOM   3833  C  CB  . THR B  1 205 ? -9.444  11.108  16.361  1.00 12.56 ? 205 THR B CB  1 
ATOM   3834  O  OG1 . THR B  1 205 ? -9.287  11.096  14.954  1.00 12.46 ? 205 THR B OG1 1 
ATOM   3835  C  CG2 . THR B  1 205 ? -8.709  12.333  16.931  1.00 15.12 ? 205 THR B CG2 1 
ATOM   3836  N  N   . VAL B  1 206 ? -9.006  7.544   16.081  1.00 9.79  ? 206 VAL B N   1 
ATOM   3837  C  CA  . VAL B  1 206 ? -9.749  6.380   15.549  1.00 10.83 ? 206 VAL B CA  1 
ATOM   3838  C  C   . VAL B  1 206 ? -9.742  5.173   16.499  1.00 9.52  ? 206 VAL B C   1 
ATOM   3839  O  O   . VAL B  1 206 ? -8.671  4.768   16.944  1.00 10.79 ? 206 VAL B O   1 
ATOM   3840  C  CB  . VAL B  1 206 ? -9.124  5.949   14.164  1.00 8.51  ? 206 VAL B CB  1 
ATOM   3841  C  CG1 . VAL B  1 206 ? -9.838  4.693   13.655  1.00 9.88  ? 206 VAL B CG1 1 
ATOM   3842  C  CG2 . VAL B  1 206 ? -9.209  7.057   13.113  1.00 10.88 ? 206 VAL B CG2 1 
ATOM   3843  N  N   . LEU B  1 207 ? -10.905 4.685   16.782  1.00 8.52  ? 207 LEU B N   1 
ATOM   3844  C  CA  . LEU B  1 207 ? -11.045 3.349   17.404  1.00 9.40  ? 207 LEU B CA  1 
ATOM   3845  C  C   . LEU B  1 207 ? -11.072 2.316   16.221  1.00 8.56  ? 207 LEU B C   1 
ATOM   3846  O  O   . LEU B  1 207 ? -11.998 2.263   15.458  1.00 9.17  ? 207 LEU B O   1 
ATOM   3847  C  CB  . LEU B  1 207 ? -12.385 3.301   18.143  1.00 12.59 ? 207 LEU B CB  1 
ATOM   3848  C  CG  . LEU B  1 207 ? -12.422 2.148   19.124  1.00 17.61 ? 207 LEU B CG  1 
ATOM   3849  C  CD1 . LEU B  1 207 ? -11.441 2.275   20.314  1.00 23.83 ? 207 LEU B CD1 1 
ATOM   3850  C  CD2 . LEU B  1 207 ? -13.831 2.137   19.685  1.00 23.14 ? 207 LEU B CD2 1 
ATOM   3851  N  N   . TRP B  1 208 ? -10.010 1.522   16.150  1.00 8.01  ? 208 TRP B N   1 
ATOM   3852  C  CA  . TRP B  1 208 ? -9.858  0.534   15.071  1.00 8.66  ? 208 TRP B CA  1 
ATOM   3853  C  C   . TRP B  1 208 ? -10.437 -0.789  15.479  1.00 8.33  ? 208 TRP B C   1 
ATOM   3854  O  O   . TRP B  1 208 ? -10.205 -1.261  16.623  1.00 9.51  ? 208 TRP B O   1 
ATOM   3855  C  CB  . TRP B  1 208 ? -8.329  0.311   14.758  1.00 8.81  ? 208 TRP B CB  1 
ATOM   3856  C  CG  . TRP B  1 208 ? -7.830  1.399   13.850  1.00 7.70  ? 208 TRP B CG  1 
ATOM   3857  C  CD1 . TRP B  1 208 ? -7.184  2.539   14.232  1.00 8.64  ? 208 TRP B CD1 1 
ATOM   3858  C  CD2 . TRP B  1 208 ? -7.953  1.427   12.439  1.00 8.12  ? 208 TRP B CD2 1 
ATOM   3859  N  NE1 . TRP B  1 208 ? -6.947  3.348   13.154  1.00 8.57  ? 208 TRP B NE1 1 
ATOM   3860  C  CE2 . TRP B  1 208 ? -7.451  2.695   12.019  1.00 7.42  ? 208 TRP B CE2 1 
ATOM   3861  C  CE3 . TRP B  1 208 ? -8.537  0.576   11.496  1.00 7.63  ? 208 TRP B CE3 1 
ATOM   3862  C  CZ2 . TRP B  1 208 ? -7.446  3.090   10.686  1.00 6.94  ? 208 TRP B CZ2 1 
ATOM   3863  C  CZ3 . TRP B  1 208 ? -8.531  0.927   10.160  1.00 7.48  ? 208 TRP B CZ3 1 
ATOM   3864  C  CH2 . TRP B  1 208 ? -7.978  2.193   9.765   1.00 7.07  ? 208 TRP B CH2 1 
ATOM   3865  N  N   . THR B  1 209 ? -11.191 -1.419  14.589  1.00 7.95  ? 209 THR B N   1 
ATOM   3866  C  CA  . THR B  1 209 ? -11.617 -2.806  14.701  1.00 7.67  ? 209 THR B CA  1 
ATOM   3867  C  C   . THR B  1 209 ? -11.108 -3.485  13.460  1.00 7.98  ? 209 THR B C   1 
ATOM   3868  O  O   . THR B  1 209 ? -11.598 -3.173  12.353  1.00 8.52  ? 209 THR B O   1 
ATOM   3869  C  CB  . THR B  1 209 ? -13.158 -2.869  14.820  1.00 8.42  ? 209 THR B CB  1 
ATOM   3870  O  OG1 . THR B  1 209 ? -13.572 -2.164  16.004  1.00 9.65  ? 209 THR B OG1 1 
ATOM   3871  C  CG2 . THR B  1 209 ? -13.703 -4.331  14.913  1.00 8.70  ? 209 THR B CG2 1 
ATOM   3872  N  N   . VAL B  1 210 ? -10.199 -4.428  13.575  1.00 7.35  ? 210 VAL B N   1 
ATOM   3873  C  CA  . VAL B  1 210 ? -9.716  -5.199  12.398  1.00 7.42  ? 210 VAL B CA  1 
ATOM   3874  C  C   . VAL B  1 210 ? -10.264 -6.587  12.554  1.00 7.76  ? 210 VAL B C   1 
ATOM   3875  O  O   . VAL B  1 210 ? -9.963  -7.293  13.549  1.00 8.46  ? 210 VAL B O   1 
ATOM   3876  C  CB  . VAL B  1 210 ? -8.146  -5.214  12.364  1.00 7.22  ? 210 VAL B CB  1 
ATOM   3877  C  CG1 . VAL B  1 210 ? -7.661  -5.975  11.158  1.00 8.70  ? 210 VAL B CG1 1 
ATOM   3878  C  CG2 . VAL B  1 210 ? -7.556  -3.826  12.337  1.00 8.55  ? 210 VAL B CG2 1 
ATOM   3879  N  N   . PHE B  1 211 ? -11.075 -7.041  11.653  1.00 6.80  ? 211 PHE B N   1 
ATOM   3880  C  CA  . PHE B  1 211 ? -11.586 -8.442  11.795  1.00 7.60  ? 211 PHE B CA  1 
ATOM   3881  C  C   . PHE B  1 211 ? -10.522 -9.469  11.661  1.00 8.12  ? 211 PHE B C   1 
ATOM   3882  O  O   . PHE B  1 211 ? -9.535  -9.296  10.897  1.00 8.66  ? 211 PHE B O   1 
ATOM   3883  C  CB  . PHE B  1 211 ? -12.735 -8.671  10.733  1.00 8.68  ? 211 PHE B CB  1 
ATOM   3884  C  CG  . PHE B  1 211 ? -13.924 -7.783  11.034  1.00 8.61  ? 211 PHE B CG  1 
ATOM   3885  C  CD1 . PHE B  1 211 ? -14.695 -8.016  12.191  1.00 9.07  ? 211 PHE B CD1 1 
ATOM   3886  C  CD2 . PHE B  1 211 ? -14.277 -6.734  10.223  1.00 10.50 ? 211 PHE B CD2 1 
ATOM   3887  C  CE1 . PHE B  1 211 ? -15.756 -7.218  12.522  1.00 10.37 ? 211 PHE B CE1 1 
ATOM   3888  C  CE2 . PHE B  1 211 ? -15.349 -5.893  10.528  1.00 10.99 ? 211 PHE B CE2 1 
ATOM   3889  C  CZ  . PHE B  1 211 ? -16.145 -6.154  11.667  1.00 11.71 ? 211 PHE B CZ  1 
ATOM   3890  N  N   . ARG B  1 212 ? -10.632 -10.538 12.469  1.00 8.19  ? 212 ARG B N   1 
ATOM   3891  C  CA  . ARG B  1 212 ? -9.597  -11.551 12.437  1.00 8.81  ? 212 ARG B CA  1 
ATOM   3892  C  C   . ARG B  1 212 ? -9.503  -12.302 11.111  1.00 8.84  ? 212 ARG B C   1 
ATOM   3893  O  O   . ARG B  1 212 ? -8.410  -12.560 10.675  1.00 9.83  ? 212 ARG B O   1 
ATOM   3894  C  CB  . ARG B  1 212 ? -9.934  -12.580 13.562  1.00 9.24  ? 212 ARG B CB  1 
ATOM   3895  C  CG  . ARG B  1 212 ? -8.861  -13.622 13.695  1.00 10.13 ? 212 ARG B CG  1 
ATOM   3896  C  CD  . ARG B  1 212 ? -9.384  -14.783 14.600  1.00 12.59 ? 212 ARG B CD  1 
ATOM   3897  N  NE  . ARG B  1 212 ? -8.253  -15.609 14.915  1.00 13.80 ? 212 ARG B NE  1 
ATOM   3898  C  CZ  . ARG B  1 212 ? -8.253  -16.567 15.832  1.00 15.64 ? 212 ARG B CZ  1 
ATOM   3899  N  NH1 . ARG B  1 212 ? -9.388  -16.858 16.454  1.00 14.89 ? 212 ARG B NH1 1 
ATOM   3900  N  NH2 . ARG B  1 212 ? -7.144  -17.234 16.100  1.00 18.34 ? 212 ARG B NH2 1 
ATOM   3901  N  N   . ASN B  1 213 ? -10.643 -12.527 10.460  1.00 8.53  ? 213 ASN B N   1 
ATOM   3902  C  CA  . ASN B  1 213 ? -10.633 -13.378 9.283   1.00 9.33  ? 213 ASN B CA  1 
ATOM   3903  C  C   . ASN B  1 213 ? -10.630 -12.505 8.017   1.00 10.97 ? 213 ASN B C   1 
ATOM   3904  O  O   . ASN B  1 213 ? -11.383 -11.506 7.980   1.00 9.92  ? 213 ASN B O   1 
ATOM   3905  C  CB  . ASN B  1 213 ? -11.819 -14.326 9.268   1.00 11.64 ? 213 ASN B CB  1 
ATOM   3906  C  CG  . ASN B  1 213 ? -11.791 -15.255 10.481  1.00 15.43 ? 213 ASN B CG  1 
ATOM   3907  O  OD1 . ASN B  1 213 ? -10.796 -15.907 10.673  1.00 21.33 ? 213 ASN B OD1 1 
ATOM   3908  N  ND2 . ASN B  1 213 ? -12.837 -15.241 11.251  1.00 17.89 ? 213 ASN B ND2 1 
ATOM   3909  N  N   . PRO B  1 214 ? -9.843  -12.829 6.999   1.00 9.88  ? 214 PRO B N   1 
ATOM   3910  C  CA  . PRO B  1 214 ? -9.883  -12.117 5.756   1.00 9.42  ? 214 PRO B CA  1 
ATOM   3911  C  C   . PRO B  1 214 ? -11.069 -12.524 4.898   1.00 9.23  ? 214 PRO B C   1 
ATOM   3912  O  O   . PRO B  1 214 ? -11.680 -13.606 5.091   1.00 10.38 ? 214 PRO B O   1 
ATOM   3913  C  CB  . PRO B  1 214 ? -8.523  -12.492 5.095   1.00 10.66 ? 214 PRO B CB  1 
ATOM   3914  C  CG  . PRO B  1 214 ? -8.313  -13.893 5.511   1.00 13.13 ? 214 PRO B CG  1 
ATOM   3915  C  CD  . PRO B  1 214 ? -8.748  -13.847 6.990   1.00 11.86 ? 214 PRO B CD  1 
ATOM   3916  N  N   . VAL B  1 215 ? -11.372 -11.701 3.931   1.00 8.90  ? 215 VAL B N   1 
ATOM   3917  C  CA  . VAL B  1 215 ? -12.198 -12.110 2.804   1.00 8.10  ? 215 VAL B CA  1 
ATOM   3918  C  C   . VAL B  1 215 ? -11.369 -12.397 1.612   1.00 7.86  ? 215 VAL B C   1 
ATOM   3919  O  O   . VAL B  1 215 ? -10.167 -12.044 1.593   1.00 8.97  ? 215 VAL B O   1 
ATOM   3920  C  CB  . VAL B  1 215 ? -13.256 -11.043 2.454   1.00 7.98  ? 215 VAL B CB  1 
ATOM   3921  C  CG1 . VAL B  1 215 ? -14.185 -10.828 3.617   1.00 9.71  ? 215 VAL B CG1 1 
ATOM   3922  C  CG2 . VAL B  1 215 ? -12.637 -9.748  1.911   1.00 8.67  ? 215 VAL B CG2 1 
ATOM   3923  N  N   . GLN B  1 216 ? -11.919 -13.025 0.595   1.00 7.62  ? 216 GLN B N   1 
ATOM   3924  C  CA  . GLN B  1 216 ? -11.206 -13.248 -0.697  1.00 7.53  ? 216 GLN B CA  1 
ATOM   3925  C  C   . GLN B  1 216 ? -11.811 -12.468 -1.815  1.00 7.29  ? 216 GLN B C   1 
ATOM   3926  O  O   . GLN B  1 216 ? -13.054 -12.353 -1.898  1.00 9.11  ? 216 GLN B O   1 
ATOM   3927  C  CB  . GLN B  1 216 ? -11.258 -14.750 -1.139  1.00 9.01  ? 216 GLN B CB  1 
ATOM   3928  C  CG  . GLN B  1 216 ? -10.493 -15.633 -0.114  1.00 9.28  ? 216 GLN B CG  1 
ATOM   3929  C  CD  . GLN B  1 216 ? -10.533 -17.092 -0.546  1.00 12.88 ? 216 GLN B CD  1 
ATOM   3930  O  OE1 . GLN B  1 216 ? -11.017 -17.542 -1.574  1.00 11.26 ? 216 GLN B OE1 1 
ATOM   3931  N  NE2 . GLN B  1 216 ? -9.977  -17.900 0.345   1.00 17.32 ? 216 GLN B NE2 1 
ATOM   3932  N  N   . ILE B  1 217 ? -10.948 -11.939 -2.686  1.00 6.97  ? 217 ILE B N   1 
ATOM   3933  C  CA  . ILE B  1 217 ? -11.386 -11.471 -3.997  1.00 7.13  ? 217 ILE B CA  1 
ATOM   3934  C  C   . ILE B  1 217 ? -10.404 -12.117 -5.000  1.00 7.50  ? 217 ILE B C   1 
ATOM   3935  O  O   . ILE B  1 217 ? -9.270  -12.503 -4.604  1.00 7.45  ? 217 ILE B O   1 
ATOM   3936  C  CB  . ILE B  1 217 ? -11.359 -9.895  -4.073  1.00 7.19  ? 217 ILE B CB  1 
ATOM   3937  C  CG1 . ILE B  1 217 ? -9.986  -9.340  -4.075  1.00 7.48  ? 217 ILE B CG1 1 
ATOM   3938  C  CG2 . ILE B  1 217 ? -12.304 -9.309  -3.034  1.00 8.60  ? 217 ILE B CG2 1 
ATOM   3939  C  CD1 . ILE B  1 217 ? -9.987  -7.798  -4.253  1.00 10.28 ? 217 ILE B CD1 1 
ATOM   3940  N  N   . SER B  1 218 ? -10.760 -12.160 -6.285  1.00 6.95  ? 218 SER B N   1 
ATOM   3941  C  CA  . SER B  1 218 ? -9.837  -12.878 -7.204  1.00 7.66  ? 218 SER B CA  1 
ATOM   3942  C  C   . SER B  1 218 ? -8.695  -12.092 -7.668  1.00 8.62  ? 218 SER B C   1 
ATOM   3943  O  O   . SER B  1 218 ? -8.669  -10.811 -7.586  1.00 8.46  ? 218 SER B O   1 
ATOM   3944  C  CB  . SER B  1 218 ? -10.609 -13.394 -8.399  1.00 8.14  ? 218 SER B CB  1 
ATOM   3945  O  OG  . SER B  1 218 ? -11.100 -12.294 -9.190  1.00 10.02 ? 218 SER B OG  1 
ATOM   3946  N  N   . GLN B  1 219 ? -7.684  -12.733 -8.274  1.00 9.58  ? 219 GLN B N   1 
ATOM   3947  C  CA  . GLN B  1 219 ? -6.612  -12.079 -8.976  1.00 9.52  ? 219 GLN B CA  1 
ATOM   3948  C  C   . GLN B  1 219 ? -7.130  -11.076 -10.012 1.00 9.53  ? 219 GLN B C   1 
ATOM   3949  O  O   . GLN B  1 219 ? -6.544  -9.980  -10.118 1.00 9.93  ? 219 GLN B O   1 
ATOM   3950  C  CB  . GLN B  1 219 ? -5.728  -13.121 -9.640  1.00 12.55 ? 219 GLN B CB  1 
ATOM   3951  C  CG  . GLN B  1 219 ? -4.381  -12.411 -10.083 1.00 16.26 ? 219 GLN B CG  1 
ATOM   3952  C  CD  . GLN B  1 219 ? -4.393  -11.829 -11.468 1.00 20.15 ? 219 GLN B CD  1 
ATOM   3953  O  OE1 . GLN B  1 219 ? -3.561  -10.963 -11.817 1.00 20.82 ? 219 GLN B OE1 1 
ATOM   3954  N  NE2 . GLN B  1 219 ? -5.263  -12.329 -12.281 1.00 18.51 ? 219 GLN B NE2 1 
ATOM   3955  N  N   . GLU B  1 220 ? -8.177  -11.448 -10.692 1.00 10.40 ? 220 GLU B N   1 
ATOM   3956  C  CA  . GLU B  1 220 ? -8.668  -10.544 -11.792 1.00 9.84  ? 220 GLU B CA  1 
ATOM   3957  C  C   . GLU B  1 220 ? -9.317  -9.308  -11.140 1.00 9.26  ? 220 GLU B C   1 
ATOM   3958  O  O   . GLU B  1 220 ? -9.201  -8.207  -11.696 1.00 9.82  ? 220 GLU B O   1 
ATOM   3959  C  CB  . GLU B  1 220 ? -9.657  -11.274 -12.652 1.00 11.97 ? 220 GLU B CB  1 
ATOM   3960  C  CG  . GLU B  1 220 ? -8.965  -12.420 -13.512 1.00 12.60 ? 220 GLU B CG  1 
ATOM   3961  C  CD  . GLU B  1 220 ? -8.789  -13.747 -12.772 1.00 17.95 ? 220 GLU B CD  1 
ATOM   3962  O  OE1 . GLU B  1 220 ? -9.126  -13.966 -11.620 1.00 16.30 ? 220 GLU B OE1 1 
ATOM   3963  O  OE2 . GLU B  1 220 ? -8.232  -14.650 -13.394 1.00 23.04 ? 220 GLU B OE2 1 
ATOM   3964  N  N   . GLN B  1 221 ? -9.980  -9.475  -10.014 1.00 7.97  ? 221 GLN B N   1 
ATOM   3965  C  CA  . GLN B  1 221 ? -10.566 -8.293  -9.351  1.00 8.34  ? 221 GLN B CA  1 
ATOM   3966  C  C   . GLN B  1 221 ? -9.469  -7.437  -8.783  1.00 8.67  ? 221 GLN B C   1 
ATOM   3967  O  O   . GLN B  1 221 ? -9.529  -6.200  -8.968  1.00 8.84  ? 221 GLN B O   1 
ATOM   3968  C  CB  . GLN B  1 221 ? -11.473 -8.727  -8.207  1.00 8.19  ? 221 GLN B CB  1 
ATOM   3969  C  CG  . GLN B  1 221 ? -12.751 -9.367  -8.717  1.00 8.41  ? 221 GLN B CG  1 
ATOM   3970  C  CD  . GLN B  1 221 ? -13.625 -9.824  -7.569  1.00 8.03  ? 221 GLN B CD  1 
ATOM   3971  O  OE1 . GLN B  1 221 ? -13.300 -10.781 -6.790  1.00 9.52  ? 221 GLN B OE1 1 
ATOM   3972  N  NE2 . GLN B  1 221 ? -14.771 -9.155  -7.393  1.00 9.05  ? 221 GLN B NE2 1 
ATOM   3973  N  N   . LEU B  1 222 ? -8.405  -8.018  -8.222  1.00 8.31  ? 222 LEU B N   1 
ATOM   3974  C  CA  . LEU B  1 222 ? -7.264  -7.220  -7.730  1.00 8.42  ? 222 LEU B CA  1 
ATOM   3975  C  C   . LEU B  1 222 ? -6.641  -6.495  -8.945  1.00 8.73  ? 222 LEU B C   1 
ATOM   3976  O  O   . LEU B  1 222 ? -6.279  -5.317  -8.791  1.00 8.83  ? 222 LEU B O   1 
ATOM   3977  C  CB  . LEU B  1 222 ? -6.268  -8.129  -7.014  1.00 9.95  ? 222 LEU B CB  1 
ATOM   3978  C  CG  . LEU B  1 222 ? -6.651  -8.495  -5.627  1.00 9.23  ? 222 LEU B CG  1 
ATOM   3979  C  CD1 . LEU B  1 222 ? -5.947  -9.766  -5.108  1.00 9.96  ? 222 LEU B CD1 1 
ATOM   3980  C  CD2 . LEU B  1 222 ? -6.353  -7.322  -4.687  1.00 10.77 ? 222 LEU B CD2 1 
ATOM   3981  N  N   . LEU B  1 223 ? -6.473  -7.171  -10.067 1.00 8.79  ? 223 LEU B N   1 
ATOM   3982  C  CA  . LEU B  1 223 ? -5.817  -6.519  -11.209 1.00 8.85  ? 223 LEU B CA  1 
ATOM   3983  C  C   . LEU B  1 223 ? -6.654  -5.383  -11.714 1.00 9.63  ? 223 LEU B C   1 
ATOM   3984  O  O   . LEU B  1 223 ? -6.078  -4.346  -12.055 1.00 10.14 ? 223 LEU B O   1 
ATOM   3985  C  CB  . LEU B  1 223 ? -5.683  -7.599  -12.337 1.00 10.60 ? 223 LEU B CB  1 
ATOM   3986  C  CG  . LEU B  1 223 ? -4.890  -7.037  -13.531 1.00 11.32 ? 223 LEU B CG  1 
ATOM   3987  C  CD1 . LEU B  1 223 ? -3.475  -6.771  -13.157 1.00 14.47 ? 223 LEU B CD1 1 
ATOM   3988  C  CD2 . LEU B  1 223 ? -4.910  -8.095  -14.652 1.00 14.50 ? 223 LEU B CD2 1 
ATOM   3989  N  N   . ALA B  1 224 ? -7.954  -5.535  -11.754 1.00 10.16 ? 224 ALA B N   1 
ATOM   3990  C  CA  . ALA B  1 224 ? -8.814  -4.372  -12.134 1.00 10.81 ? 224 ALA B CA  1 
ATOM   3991  C  C   . ALA B  1 224 ? -8.578  -3.247  -11.137 1.00 10.95 ? 224 ALA B C   1 
ATOM   3992  O  O   . ALA B  1 224 ? -8.355  -2.071  -11.546 1.00 10.86 ? 224 ALA B O   1 
ATOM   3993  C  CB  . ALA B  1 224 ? -10.265 -4.749  -12.187 1.00 12.59 ? 224 ALA B CB  1 
ATOM   3994  N  N   . LEU B  1 225 ? -8.636  -3.473  -9.818  1.00 9.80  ? 225 LEU B N   1 
ATOM   3995  C  CA  . LEU B  1 225 ? -8.455  -2.436  -8.827  1.00 9.65  ? 225 LEU B CA  1 
ATOM   3996  C  C   . LEU B  1 225 ? -7.111  -1.779  -8.974  1.00 9.52  ? 225 LEU B C   1 
ATOM   3997  O  O   . LEU B  1 225 ? -7.011  -0.554  -8.817  1.00 10.81 ? 225 LEU B O   1 
ATOM   3998  C  CB  . LEU B  1 225 ? -8.661  -3.086  -7.444  1.00 10.33 ? 225 LEU B CB  1 
ATOM   3999  C  CG  . LEU B  1 225 ? -8.454  -2.102  -6.289  1.00 9.54  ? 225 LEU B CG  1 
ATOM   4000  C  CD1 . LEU B  1 225 ? -9.481  -1.031  -6.307  1.00 10.31 ? 225 LEU B CD1 1 
ATOM   4001  C  CD2 . LEU B  1 225 ? -8.575  -2.894  -5.005  1.00 10.55 ? 225 LEU B CD2 1 
ATOM   4002  N  N   . GLU B  1 226 ? -6.073  -2.560  -9.293  1.00 9.33  ? 226 GLU B N   1 
ATOM   4003  C  CA  . GLU B  1 226 ? -4.707  -2.041  -9.370  1.00 9.41  ? 226 GLU B CA  1 
ATOM   4004  C  C   . GLU B  1 226 ? -4.393  -1.338  -10.705 1.00 9.68  ? 226 GLU B C   1 
ATOM   4005  O  O   . GLU B  1 226 ? -3.302  -0.767  -10.774 1.00 11.36 ? 226 GLU B O   1 
ATOM   4006  C  CB  . GLU B  1 226 ? -3.718  -3.253  -9.184  1.00 9.46  ? 226 GLU B CB  1 
ATOM   4007  C  CG  . GLU B  1 226 ? -3.730  -3.912  -7.790  1.00 9.11  ? 226 GLU B CG  1 
ATOM   4008  C  CD  . GLU B  1 226 ? -3.452  -5.365  -7.853  1.00 10.37 ? 226 GLU B CD  1 
ATOM   4009  O  OE1 . GLU B  1 226 ? -3.187  -5.974  -8.939  1.00 10.02 ? 226 GLU B OE1 1 
ATOM   4010  O  OE2 . GLU B  1 226 ? -3.494  -5.959  -6.797  1.00 10.35 ? 226 GLU B OE2 1 
ATOM   4011  N  N   . THR B  1 227 ? -5.207  -1.512  -11.706 1.00 9.25  ? 227 THR B N   1 
ATOM   4012  C  CA  . THR B  1 227 ? -4.911  -0.897  -13.042 1.00 9.85  ? 227 THR B CA  1 
ATOM   4013  C  C   . THR B  1 227 ? -5.933  0.141   -13.479 1.00 11.20 ? 227 THR B C   1 
ATOM   4014  O  O   . THR B  1 227 ? -5.594  0.854   -14.431 1.00 12.76 ? 227 THR B O   1 
ATOM   4015  C  CB  . THR B  1 227 ? -4.834  -1.991  -14.134 1.00 10.04 ? 227 THR B CB  1 
ATOM   4016  O  OG1 . THR B  1 227 ? -6.064  -2.683  -14.237 1.00 10.68 ? 227 THR B OG1 1 
ATOM   4017  C  CG2 . THR B  1 227 ? -3.632  -2.985  -13.889 1.00 11.29 ? 227 THR B CG2 1 
ATOM   4018  N  N   . ALA B  1 228 ? -7.071  0.261   -12.797 1.00 9.83  ? 228 ALA B N   1 
ATOM   4019  C  CA  . ALA B  1 228 ? -8.138  1.105   -13.392 1.00 10.19 ? 228 ALA B CA  1 
ATOM   4020  C  C   . ALA B  1 228 ? -7.869  2.575   -13.010 1.00 10.58 ? 228 ALA B C   1 
ATOM   4021  O  O   . ALA B  1 228 ? -8.430  3.444   -13.715 1.00 12.91 ? 228 ALA B O   1 
ATOM   4022  C  CB  . ALA B  1 228 ? -9.438  0.705   -12.886 1.00 11.12 ? 228 ALA B CB  1 
ATOM   4023  N  N   . LEU B  1 229 ? -7.230  2.872   -11.932 1.00 10.48 ? 229 LEU B N   1 
ATOM   4024  C  CA  . LEU B  1 229 ? -7.345  4.179   -11.320 1.00 8.90  ? 229 LEU B CA  1 
ATOM   4025  C  C   . LEU B  1 229 ? -6.076  4.961   -11.323 1.00 8.93  ? 229 LEU B C   1 
ATOM   4026  O  O   . LEU B  1 229 ? -4.982  4.447   -11.272 1.00 9.27  ? 229 LEU B O   1 
ATOM   4027  C  CB  . LEU B  1 229 ? -7.831  4.093   -9.836  1.00 10.39 ? 229 LEU B CB  1 
ATOM   4028  C  CG  . LEU B  1 229 ? -9.122  3.215   -9.686  1.00 10.35 ? 229 LEU B CG  1 
ATOM   4029  C  CD1 . LEU B  1 229 ? -9.440  3.155   -8.163  1.00 11.67 ? 229 LEU B CD1 1 
ATOM   4030  C  CD2 . LEU B  1 229 ? -10.323 3.740   -10.449 1.00 11.90 ? 229 LEU B CD2 1 
ATOM   4031  N  N   . TYR B  1 230 ? -6.259  6.300   -11.426 1.00 9.00  ? 230 TYR B N   1 
ATOM   4032  C  CA  . TYR B  1 230 ? -5.206  7.320   -11.417 1.00 9.03  ? 230 TYR B CA  1 
ATOM   4033  C  C   . TYR B  1 230 ? -5.387  8.280   -10.260 1.00 8.68  ? 230 TYR B C   1 
ATOM   4034  O  O   . TYR B  1 230 ? -6.534  8.680   -9.950  1.00 9.10  ? 230 TYR B O   1 
ATOM   4035  C  CB  . TYR B  1 230 ? -5.241  8.066   -12.808 1.00 9.37  ? 230 TYR B CB  1 
ATOM   4036  C  CG  . TYR B  1 230 ? -4.695  7.147   -13.846 1.00 9.23  ? 230 TYR B CG  1 
ATOM   4037  C  CD1 . TYR B  1 230 ? -5.521  6.210   -14.450 1.00 9.76  ? 230 TYR B CD1 1 
ATOM   4038  C  CD2 . TYR B  1 230 ? -3.319  7.128   -14.086 1.00 10.90 ? 230 TYR B CD2 1 
ATOM   4039  C  CE1 . TYR B  1 230 ? -4.920  5.255   -15.302 1.00 11.32 ? 230 TYR B CE1 1 
ATOM   4040  C  CE2 . TYR B  1 230 ? -2.745  6.171   -14.957 1.00 12.60 ? 230 TYR B CE2 1 
ATOM   4041  C  CZ  . TYR B  1 230 ? -3.570  5.273   -15.515 1.00 11.59 ? 230 TYR B CZ  1 
ATOM   4042  O  OH  . TYR B  1 230 ? -3.103  4.249   -16.384 1.00 16.84 ? 230 TYR B OH  1 
ATOM   4043  N  N   . CYS B  1 231 ? -4.304  8.708   -9.664  1.00 9.64  ? 231 CYS B N   1 
ATOM   4044  C  CA  . CYS B  1 231 ? -4.352  9.728   -8.628  1.00 9.67  ? 231 CYS B CA  1 
ATOM   4045  C  C   . CYS B  1 231 ? -4.651  11.114  -9.188  1.00 9.90  ? 231 CYS B C   1 
ATOM   4046  O  O   . CYS B  1 231 ? -4.999  12.034  -8.463  1.00 11.20 ? 231 CYS B O   1 
ATOM   4047  C  CB  . CYS B  1 231 ? -2.998  9.880   -7.946  1.00 9.46  ? 231 CYS B CB  1 
ATOM   4048  S  SG  . CYS B  1 231 ? -2.488  8.330   -7.076  1.00 11.53 ? 231 CYS B SG  1 
ATOM   4049  N  N   . THR B  1 232 ? -4.423  11.245  -10.484 1.00 9.95  ? 232 THR B N   1 
ATOM   4050  C  CA  . THR B  1 232 ? -4.420  12.578  -11.118 1.00 10.02 ? 232 THR B CA  1 
ATOM   4051  C  C   . THR B  1 232 ? -5.722  12.796  -11.886 1.00 9.36  ? 232 THR B C   1 
ATOM   4052  O  O   . THR B  1 232 ? -6.448  11.850  -12.240 1.00 9.95  ? 232 THR B O   1 
ATOM   4053  C  CB  . THR B  1 232 ? -3.167  12.605  -12.092 1.00 8.74  ? 232 THR B CB  1 
ATOM   4054  O  OG1 . THR B  1 232 ? -3.013  11.323  -12.725 1.00 9.93  ? 232 THR B OG1 1 
ATOM   4055  C  CG2 . THR B  1 232 ? -1.957  12.936  -11.299 1.00 11.04 ? 232 THR B CG2 1 
ATOM   4056  N  N   . HIS B  1 233 ? -5.989  14.065  -12.221 1.00 9.22  ? 233 HIS B N   1 
ATOM   4057  C  CA  . HIS B  1 233 ? -7.117  14.407  -13.061 1.00 10.49 ? 233 HIS B CA  1 
ATOM   4058  C  C   . HIS B  1 233 ? -6.963  13.925  -14.494 1.00 10.00 ? 233 HIS B C   1 
ATOM   4059  O  O   . HIS B  1 233 ? -5.865  13.634  -14.970 1.00 9.91  ? 233 HIS B O   1 
ATOM   4060  C  CB  . HIS B  1 233 ? -7.260  15.955  -13.106 1.00 11.82 ? 233 HIS B CB  1 
ATOM   4061  C  CG  . HIS B  1 233 ? -7.742  16.520  -11.820 1.00 12.89 ? 233 HIS B CG  1 
ATOM   4062  N  ND1 . HIS B  1 233 ? -6.900  17.161  -10.944 1.00 20.34 ? 233 HIS B ND1 1 
ATOM   4063  C  CD2 . HIS B  1 233 ? -8.914  16.398  -11.180 1.00 15.65 ? 233 HIS B CD2 1 
ATOM   4064  C  CE1 . HIS B  1 233 ? -7.585  17.548  -9.880  1.00 20.22 ? 233 HIS B CE1 1 
ATOM   4065  N  NE2 . HIS B  1 233 ? -8.804  17.094  -10.000 1.00 16.56 ? 233 HIS B NE2 1 
ATOM   4066  N  N   . MET B  1 234 ? -8.110  13.758  -15.178 1.00 11.20 ? 234 MET B N   1 
ATOM   4067  C  CA  . MET B  1 234 ? -8.197  13.249  -16.554 1.00 10.78 ? 234 MET B CA  1 
ATOM   4068  C  C   . MET B  1 234 ? -7.246  14.057  -17.481 1.00 11.56 ? 234 MET B C   1 
ATOM   4069  O  O   . MET B  1 234 ? -6.620  13.467  -18.346 1.00 12.08 ? 234 MET B O   1 
ATOM   4070  C  CB  . MET B  1 234 ? -9.638  13.306  -17.019 1.00 11.41 ? 234 MET B CB  1 
ATOM   4071  C  CG  . MET B  1 234 ? -9.781  12.638  -18.383 1.00 13.50 ? 234 MET B CG  1 
ATOM   4072  S  SD  . MET B  1 234 ? -11.566 12.396  -18.645 1.00 19.93 ? 234 MET B SD  1 
ATOM   4073  C  CE  . MET B  1 234 ? -11.487 11.470  -20.167 1.00 19.81 ? 234 MET B CE  1 
ATOM   4074  N  N   . ASP B  1 235 ? -7.095  15.350  -17.225 1.00 11.91 ? 235 ASP B N   1 
ATOM   4075  C  CA  . ASP B  1 235 ? -6.278  16.166  -18.169 1.00 13.64 ? 235 ASP B CA  1 
ATOM   4076  C  C   . ASP B  1 235 ? -4.922  16.402  -17.652 1.00 13.45 ? 235 ASP B C   1 
ATOM   4077  O  O   . ASP B  1 235 ? -4.145  17.231  -18.197 1.00 15.68 ? 235 ASP B O   1 
ATOM   4078  C  CB  . ASP B  1 235 ? -7.021  17.487  -18.450 1.00 16.68 ? 235 ASP B CB  1 
ATOM   4079  C  CG  . ASP B  1 235 ? -7.045  18.381  -17.246 1.00 22.85 ? 235 ASP B CG  1 
ATOM   4080  O  OD1 . ASP B  1 235 ? -6.682  17.983  -16.104 1.00 22.57 ? 235 ASP B OD1 1 
ATOM   4081  O  OD2 . ASP B  1 235 ? -7.551  19.531  -17.423 1.00 27.51 ? 235 ASP B OD2 1 
ATOM   4082  N  N   . ASP B  1 236 ? -4.385  15.664  -16.689 1.00 10.99 ? 236 ASP B N   1 
ATOM   4083  C  CA  . ASP B  1 236 ? -3.113  15.992  -16.109 1.00 10.83 ? 236 ASP B CA  1 
ATOM   4084  C  C   . ASP B  1 236 ? -1.986  15.497  -17.072 1.00 11.84 ? 236 ASP B C   1 
ATOM   4085  O  O   . ASP B  1 236 ? -1.948  14.317  -17.448 1.00 12.23 ? 236 ASP B O   1 
ATOM   4086  C  CB  . ASP B  1 236 ? -2.949  15.309  -14.718 1.00 12.00 ? 236 ASP B CB  1 
ATOM   4087  C  CG  . ASP B  1 236 ? -1.796  15.893  -13.933 1.00 12.61 ? 236 ASP B CG  1 
ATOM   4088  O  OD1 . ASP B  1 236 ? -0.648  16.040  -14.430 1.00 13.60 ? 236 ASP B OD1 1 
ATOM   4089  O  OD2 . ASP B  1 236 ? -1.986  16.239  -12.753 1.00 15.72 ? 236 ASP B OD2 1 
ATOM   4090  N  N   . PRO B  1 237 ? -1.022  16.347  -17.454 1.00 10.72 ? 237 PRO B N   1 
ATOM   4091  C  CA  . PRO B  1 237 ? 0.040   15.891  -18.349 1.00 11.70 ? 237 PRO B CA  1 
ATOM   4092  C  C   . PRO B  1 237 ? 1.135   15.049  -17.655 1.00 10.47 ? 237 PRO B C   1 
ATOM   4093  O  O   . PRO B  1 237 ? 2.055   14.546  -18.312 1.00 11.70 ? 237 PRO B O   1 
ATOM   4094  C  CB  . PRO B  1 237 ? 0.591   17.239  -18.871 1.00 11.63 ? 237 PRO B CB  1 
ATOM   4095  C  CG  . PRO B  1 237 ? 0.387   18.167  -17.677 1.00 12.29 ? 237 PRO B CG  1 
ATOM   4096  C  CD  . PRO B  1 237 ? -1.025  17.805  -17.166 1.00 10.88 ? 237 PRO B CD  1 
ATOM   4097  N  N   A SER B  1 238 ? 1.095   14.850  -16.317 0.50 11.03 ? 238 SER B N   1 
ATOM   4098  N  N   B SER B  1 238 ? 1.022   14.889  -16.320 0.50 10.96 ? 238 SER B N   1 
ATOM   4099  C  CA  A SER B  1 238 ? 2.002   13.881  -15.640 0.50 11.54 ? 238 SER B CA  1 
ATOM   4100  C  CA  B SER B  1 238 ? 1.889   14.027  -15.520 0.50 11.33 ? 238 SER B CA  1 
ATOM   4101  C  C   A SER B  1 238 ? 1.199   12.897  -14.810 0.50 10.85 ? 238 SER B C   1 
ATOM   4102  C  C   B SER B  1 238 ? 1.014   13.001  -14.768 0.50 10.32 ? 238 SER B C   1 
ATOM   4103  O  O   A SER B  1 238 ? 1.251   12.928  -13.567 0.50 11.18 ? 238 SER B O   1 
ATOM   4104  O  O   B SER B  1 238 ? 0.833   13.083  -13.551 0.50 10.21 ? 238 SER B O   1 
ATOM   4105  C  CB  A SER B  1 238 ? 2.906   14.573  -14.646 0.50 13.02 ? 238 SER B CB  1 
ATOM   4106  C  CB  B SER B  1 238 ? 2.636   14.911  -14.534 0.50 12.23 ? 238 SER B CB  1 
ATOM   4107  O  OG  A SER B  1 238 ? 4.049   13.803  -14.303 0.50 17.29 ? 238 SER B OG  1 
ATOM   4108  O  OG  B SER B  1 238 ? 3.612   15.683  -15.281 0.50 14.91 ? 238 SER B OG  1 
ATOM   4109  N  N   . PRO B  1 239 ? 0.485   12.015  -15.499 1.00 10.20 ? 239 PRO B N   1 
ATOM   4110  C  CA  . PRO B  1 239 ? -0.407  11.039  -14.791 1.00 10.72 ? 239 PRO B CA  1 
ATOM   4111  C  C   . PRO B  1 239 ? 0.367   10.192  -13.811 1.00 11.34 ? 239 PRO B C   1 
ATOM   4112  O  O   . PRO B  1 239 ? 1.571   9.851   -13.950 1.00 12.11 ? 239 PRO B O   1 
ATOM   4113  C  CB  . PRO B  1 239 ? -0.896  10.114  -15.905 1.00 11.77 ? 239 PRO B CB  1 
ATOM   4114  C  CG  . PRO B  1 239 ? -0.292  10.623  -17.168 1.00 15.34 ? 239 PRO B CG  1 
ATOM   4115  C  CD  . PRO B  1 239 ? 0.582   11.789  -16.953 1.00 11.55 ? 239 PRO B CD  1 
ATOM   4116  N  N   . ARG B  1 240 ? -0.349  9.853   -12.719 1.00 9.58  ? 240 ARG B N   1 
ATOM   4117  C  CA  . ARG B  1 240 ? 0.247   8.928   -11.706 1.00 9.59  ? 240 ARG B CA  1 
ATOM   4118  C  C   . ARG B  1 240 ? -0.753  7.842   -11.454 1.00 8.48  ? 240 ARG B C   1 
ATOM   4119  O  O   . ARG B  1 240 ? -1.919  8.141   -11.108 1.00 9.84  ? 240 ARG B O   1 
ATOM   4120  C  CB  . ARG B  1 240 ? 0.525   9.693   -10.404 1.00 9.54  ? 240 ARG B CB  1 
ATOM   4121  C  CG  . ARG B  1 240 ? 1.733   10.637  -10.611 1.00 11.24 ? 240 ARG B CG  1 
ATOM   4122  C  CD  . ARG B  1 240 ? 1.968   11.447  -9.322  1.00 10.63 ? 240 ARG B CD  1 
ATOM   4123  N  NE  . ARG B  1 240 ? 0.876   12.385  -9.023  1.00 12.89 ? 240 ARG B NE  1 
ATOM   4124  C  CZ  . ARG B  1 240 ? -0.004  12.273  -8.019  1.00 13.78 ? 240 ARG B CZ  1 
ATOM   4125  N  NH1 . ARG B  1 240 ? 0.005   11.156  -7.249  1.00 12.82 ? 240 ARG B NH1 1 
ATOM   4126  N  NH2 . ARG B  1 240 ? -0.944  13.195  -7.913  1.00 15.13 ? 240 ARG B NH2 1 
ATOM   4127  N  N   . GLU B  1 241 ? -0.384  6.586   -11.603 1.00 10.13 ? 241 GLU B N   1 
ATOM   4128  C  CA  . GLU B  1 241 ? -1.250  5.465   -11.312 1.00 9.68  ? 241 GLU B CA  1 
ATOM   4129  C  C   . GLU B  1 241 ? -1.558  5.390   -9.794  1.00 8.38  ? 241 GLU B C   1 
ATOM   4130  O  O   . GLU B  1 241 ? -0.688  5.604   -8.973  1.00 9.53  ? 241 GLU B O   1 
ATOM   4131  C  CB  . GLU B  1 241 ? -0.502  4.185   -11.665 1.00 12.41 ? 241 GLU B CB  1 
ATOM   4132  C  CG  . GLU B  1 241 ? -0.419  4.010   -13.214 1.00 12.89 ? 241 GLU B CG  1 
ATOM   4133  C  CD  . GLU B  1 241 ? 0.442   2.843   -13.599 1.00 20.49 ? 241 GLU B CD  1 
ATOM   4134  O  OE1 . GLU B  1 241 ? 1.486   2.669   -12.967 1.00 27.66 ? 241 GLU B OE1 1 
ATOM   4135  O  OE2 . GLU B  1 241 ? 0.022   1.997   -14.395 1.00 26.48 ? 241 GLU B OE2 1 
ATOM   4136  N  N   . MET B  1 242 ? -2.819  5.032   -9.479  1.00 7.34  ? 242 MET B N   1 
ATOM   4137  C  CA  . MET B  1 242 ? -3.166  4.849   -8.040  1.00 8.16  ? 242 MET B CA  1 
ATOM   4138  C  C   . MET B  1 242 ? -2.871  3.359   -7.677  1.00 7.75  ? 242 MET B C   1 
ATOM   4139  O  O   . MET B  1 242 ? -3.686  2.458   -7.908  1.00 7.65  ? 242 MET B O   1 
ATOM   4140  C  CB  . MET B  1 242 ? -4.643  5.164   -7.918  1.00 8.42  ? 242 MET B CB  1 
ATOM   4141  C  CG  . MET B  1 242 ? -5.033  5.169   -6.416  1.00 8.35  ? 242 MET B CG  1 
ATOM   4142  S  SD  . MET B  1 242 ? -6.745  5.540   -6.114  1.00 8.79  ? 242 MET B SD  1 
ATOM   4143  C  CE  . MET B  1 242 ? -6.868  7.234   -6.703  1.00 8.86  ? 242 MET B CE  1 
ATOM   4144  N  N   . ILE B  1 243 ? -1.633  3.216   -7.183  1.00 7.68  ? 243 ILE B N   1 
ATOM   4145  C  CA  . ILE B  1 243 ? -1.084  1.927   -6.783  1.00 8.41  ? 243 ILE B CA  1 
ATOM   4146  C  C   . ILE B  1 243 ? -0.349  2.130   -5.512  1.00 8.10  ? 243 ILE B C   1 
ATOM   4147  O  O   . ILE B  1 243 ? 0.084   3.236   -5.159  1.00 8.68  ? 243 ILE B O   1 
ATOM   4148  C  CB  . ILE B  1 243 ? -0.143  1.319   -7.878  1.00 9.11  ? 243 ILE B CB  1 
ATOM   4149  C  CG1 . ILE B  1 243 ? 0.941   2.316   -8.264  1.00 10.54 ? 243 ILE B CG1 1 
ATOM   4150  C  CG2 . ILE B  1 243 ? -0.918  0.811   -9.044  1.00 10.64 ? 243 ILE B CG2 1 
ATOM   4151  C  CD1 . ILE B  1 243 ? 1.989   1.772   -9.224  1.00 12.53 ? 243 ILE B CD1 1 
ATOM   4152  N  N   . ASN B  1 244 ? -0.192  1.014   -4.789  1.00 7.59  ? 244 ASN B N   1 
ATOM   4153  C  CA  . ASN B  1 244 ? 0.626   1.050   -3.551  1.00 8.02  ? 244 ASN B CA  1 
ATOM   4154  C  C   . ASN B  1 244 ? 0.229   2.141   -2.603  1.00 7.31  ? 244 ASN B C   1 
ATOM   4155  O  O   . ASN B  1 244 ? 1.011   2.795   -1.994  1.00 8.03  ? 244 ASN B O   1 
ATOM   4156  C  CB  . ASN B  1 244 ? 2.144   1.152   -3.900  1.00 8.64  ? 244 ASN B CB  1 
ATOM   4157  C  CG  . ASN B  1 244 ? 2.510   0.093   -4.843  1.00 10.56 ? 244 ASN B CG  1 
ATOM   4158  O  OD1 . ASN B  1 244 ? 2.126   -1.074  -4.797  1.00 12.37 ? 244 ASN B OD1 1 
ATOM   4159  N  ND2 . ASN B  1 244 ? 3.372   0.527   -5.792  1.00 13.04 ? 244 ASN B ND2 1 
ATOM   4160  N  N   . ASN B  1 245 ? -1.128  2.275   -2.430  1.00 7.62  ? 245 ASN B N   1 
ATOM   4161  C  CA  . ASN B  1 245 ? -1.676  3.351   -1.632  1.00 7.26  ? 245 ASN B CA  1 
ATOM   4162  C  C   . ASN B  1 245 ? -1.943  2.828   -0.213  1.00 7.74  ? 245 ASN B C   1 
ATOM   4163  O  O   . ASN B  1 245 ? -3.042  2.947   0.333   1.00 8.34  ? 245 ASN B O   1 
ATOM   4164  C  CB  . ASN B  1 245 ? -2.986  3.965   -2.251  1.00 7.26  ? 245 ASN B CB  1 
ATOM   4165  C  CG  . ASN B  1 245 ? -4.088  2.978   -2.441  1.00 8.22  ? 245 ASN B CG  1 
ATOM   4166  O  OD1 . ASN B  1 245 ? -3.859  1.773   -2.461  1.00 8.47  ? 245 ASN B OD1 1 
ATOM   4167  N  ND2 . ASN B  1 245 ? -5.320  3.502   -2.667  1.00 8.22  ? 245 ASN B ND2 1 
ATOM   4168  N  N   . PHE B  1 246 ? -0.909  2.348   0.413   1.00 6.84  ? 246 PHE B N   1 
ATOM   4169  C  CA  . PHE B  1 246 ? -0.938  1.878   1.806   1.00 6.82  ? 246 PHE B CA  1 
ATOM   4170  C  C   . PHE B  1 246 ? 0.257   2.474   2.503   1.00 6.92  ? 246 PHE B C   1 
ATOM   4171  O  O   . PHE B  1 246 ? 1.329   2.665   1.943   1.00 7.65  ? 246 PHE B O   1 
ATOM   4172  C  CB  . PHE B  1 246 ? -0.888  0.324   1.852   1.00 7.79  ? 246 PHE B CB  1 
ATOM   4173  C  CG  . PHE B  1 246 ? 0.365   -0.274  1.226   1.00 7.60  ? 246 PHE B CG  1 
ATOM   4174  C  CD1 . PHE B  1 246 ? 0.433   -0.553  -0.132  1.00 7.90  ? 246 PHE B CD1 1 
ATOM   4175  C  CD2 . PHE B  1 246 ? 1.426   -0.692  2.097   1.00 8.21  ? 246 PHE B CD2 1 
ATOM   4176  C  CE1 . PHE B  1 246 ? 1.584   -1.139  -0.694  1.00 7.99  ? 246 PHE B CE1 1 
ATOM   4177  C  CE2 . PHE B  1 246 ? 2.579   -1.239  1.564   1.00 8.75  ? 246 PHE B CE2 1 
ATOM   4178  C  CZ  . PHE B  1 246 ? 2.705   -1.436  0.163   1.00 8.09  ? 246 PHE B CZ  1 
ATOM   4179  N  N   . ARG B  1 247 ? 0.041   2.741   3.773   1.00 6.93  ? 247 ARG B N   1 
ATOM   4180  C  CA  . ARG B  1 247 ? 1.138   3.298   4.663   1.00 7.29  ? 247 ARG B CA  1 
ATOM   4181  C  C   . ARG B  1 247 ? 1.877   2.104   5.280   1.00 7.61  ? 247 ARG B C   1 
ATOM   4182  O  O   . ARG B  1 247 ? 1.240   1.095   5.595   1.00 7.93  ? 247 ARG B O   1 
ATOM   4183  C  CB  . ARG B  1 247 ? 0.506   4.103   5.783   1.00 7.28  ? 247 ARG B CB  1 
ATOM   4184  C  CG  . ARG B  1 247 ? 1.484   5.037   6.498   1.00 6.62  ? 247 ARG B CG  1 
ATOM   4185  C  CD  . ARG B  1 247 ? 0.790   5.656   7.653   1.00 7.46  ? 247 ARG B CD  1 
ATOM   4186  N  NE  . ARG B  1 247 ? 1.638   6.737   8.248   1.00 7.73  ? 247 ARG B NE  1 
ATOM   4187  C  CZ  . ARG B  1 247 ? 1.356   7.465   9.332   1.00 7.28  ? 247 ARG B CZ  1 
ATOM   4188  N  NH1 . ARG B  1 247 ? 0.247   7.202   10.014  1.00 8.34  ? 247 ARG B NH1 1 
ATOM   4189  N  NH2 . ARG B  1 247 ? 2.093   8.500   9.697   1.00 8.76  ? 247 ARG B NH2 1 
ATOM   4190  N  N   . GLN B  1 248 ? 3.184   2.255   5.502   1.00 6.98  ? 248 GLN B N   1 
ATOM   4191  C  CA  . GLN B  1 248 ? 3.923   1.251   6.291   1.00 7.43  ? 248 GLN B CA  1 
ATOM   4192  C  C   . GLN B  1 248 ? 3.403   1.184   7.703   1.00 7.53  ? 248 GLN B C   1 
ATOM   4193  O  O   . GLN B  1 248 ? 2.897   2.144   8.256   1.00 8.02  ? 248 GLN B O   1 
ATOM   4194  C  CB  . GLN B  1 248 ? 5.411   1.586   6.288   1.00 7.42  ? 248 GLN B CB  1 
ATOM   4195  C  CG  . GLN B  1 248 ? 6.117   1.608   4.935   1.00 7.93  ? 248 GLN B CG  1 
ATOM   4196  C  CD  . GLN B  1 248 ? 6.107   0.259   4.277   1.00 8.57  ? 248 GLN B CD  1 
ATOM   4197  O  OE1 . GLN B  1 248 ? 5.234   -0.099  3.503   1.00 9.30  ? 248 GLN B OE1 1 
ATOM   4198  N  NE2 . GLN B  1 248 ? 7.106   -0.549  4.604   1.00 9.23  ? 248 GLN B NE2 1 
ATOM   4199  N  N   . VAL B  1 249 ? 3.619   0.025   8.325   1.00 7.49  ? 249 VAL B N   1 
ATOM   4200  C  CA  . VAL B  1 249 ? 3.206   -0.104  9.729   1.00 7.76  ? 249 VAL B CA  1 
ATOM   4201  C  C   . VAL B  1 249 ? 4.076   0.806   10.647  1.00 8.14  ? 249 VAL B C   1 
ATOM   4202  O  O   . VAL B  1 249 ? 5.232   1.139   10.284  1.00 8.28  ? 249 VAL B O   1 
ATOM   4203  C  CB  . VAL B  1 249 ? 3.288   -1.564  10.235  1.00 8.42  ? 249 VAL B CB  1 
ATOM   4204  C  CG1 . VAL B  1 249 ? 2.240   -2.415  9.478   1.00 8.06  ? 249 VAL B CG1 1 
ATOM   4205  C  CG2 . VAL B  1 249 ? 4.648   -2.186  10.043  1.00 9.25  ? 249 VAL B CG2 1 
ATOM   4206  N  N   . GLN B  1 250 ? 3.485   1.173   11.732  1.00 8.41  ? 250 GLN B N   1 
ATOM   4207  C  CA  . GLN B  1 250 ? 4.035   2.168   12.692  1.00 8.42  ? 250 GLN B CA  1 
ATOM   4208  C  C   . GLN B  1 250 ? 4.578   1.521   13.912  1.00 8.82  ? 250 GLN B C   1 
ATOM   4209  O  O   . GLN B  1 250 ? 4.130   0.443   14.307  1.00 10.57 ? 250 GLN B O   1 
ATOM   4210  C  CB  . GLN B  1 250 ? 2.908   3.156   13.063  1.00 8.26  ? 250 GLN B CB  1 
ATOM   4211  C  CG  . GLN B  1 250 ? 2.290   3.805   11.811  1.00 8.60  ? 250 GLN B CG  1 
ATOM   4212  C  CD  . GLN B  1 250 ? 3.184   4.710   11.028  1.00 8.65  ? 250 GLN B CD  1 
ATOM   4213  O  OE1 . GLN B  1 250 ? 3.611   5.752   11.607  1.00 10.01 ? 250 GLN B OE1 1 
ATOM   4214  N  NE2 . GLN B  1 250 ? 3.466   4.418   9.771   1.00 8.74  ? 250 GLN B NE2 1 
ATOM   4215  N  N   . LYS B  1 251 ? 5.488   2.246   14.589  1.00 8.56  ? 251 LYS B N   1 
ATOM   4216  C  CA  . LYS B  1 251 ? 5.886   1.749   15.915  1.00 9.51  ? 251 LYS B CA  1 
ATOM   4217  C  C   . LYS B  1 251 ? 4.622   1.672   16.845  1.00 11.00 ? 251 LYS B C   1 
ATOM   4218  O  O   . LYS B  1 251 ? 3.705   2.471   16.749  1.00 11.62 ? 251 LYS B O   1 
ATOM   4219  C  CB  . LYS B  1 251 ? 6.876   2.783   16.514  1.00 11.14 ? 251 LYS B CB  1 
ATOM   4220  C  CG  . LYS B  1 251 ? 8.277   2.830   15.875  1.00 12.33 ? 251 LYS B CG  1 
ATOM   4221  C  CD  . LYS B  1 251 ? 9.105   1.705   16.412  1.00 11.68 ? 251 LYS B CD  1 
ATOM   4222  C  CE  . LYS B  1 251 ? 10.609  1.759   16.016  1.00 10.94 ? 251 LYS B CE  1 
ATOM   4223  N  NZ  . LYS B  1 251 ? 10.772  1.760   14.489  1.00 9.75  ? 251 LYS B NZ  1 
ATOM   4224  N  N   A PHE B  1 252 ? 4.685   0.732   17.812  0.50 12.29 ? 252 PHE B N   1 
ATOM   4225  N  N   B PHE B  1 252 ? 4.794   0.909   17.921  0.50 12.63 ? 252 PHE B N   1 
ATOM   4226  C  CA  A PHE B  1 252 ? 3.569   0.550   18.765  0.50 12.77 ? 252 PHE B CA  1 
ATOM   4227  C  CA  B PHE B  1 252 ? 3.725   0.648   18.885  0.50 13.98 ? 252 PHE B CA  1 
ATOM   4228  C  C   A PHE B  1 252 ? 3.345   1.581   19.908  0.50 19.98 ? 252 PHE B C   1 
ATOM   4229  C  C   B PHE B  1 252 ? 3.526   1.673   20.013  0.50 21.29 ? 252 PHE B C   1 
ATOM   4230  O  O   A PHE B  1 252 ? 2.253   1.646   20.473  0.50 18.50 ? 252 PHE B O   1 
ATOM   4231  O  O   B PHE B  1 252 ? 2.463   1.711   20.632  0.50 20.28 ? 252 PHE B O   1 
ATOM   4232  C  CB  A PHE B  1 252 ? 3.042   -0.851  19.012  0.50 15.00 ? 252 PHE B CB  1 
ATOM   4233  C  CB  B PHE B  1 252 ? 3.858   -0.786  19.423  0.50 13.39 ? 252 PHE B CB  1 
ATOM   4234  C  CG  A PHE B  1 252 ? 1.548   -0.872  19.210  0.50 13.08 ? 252 PHE B CG  1 
ATOM   4235  C  CG  B PHE B  1 252 ? 3.282   -1.820  18.495  0.50 13.46 ? 252 PHE B CG  1 
ATOM   4236  C  CD1 A PHE B  1 252 ? 0.735   0.123   18.661  0.50 12.76 ? 252 PHE B CD1 1 
ATOM   4237  C  CD1 B PHE B  1 252 ? 4.072   -2.476  17.552  0.50 16.92 ? 252 PHE B CD1 1 
ATOM   4238  C  CD2 A PHE B  1 252 ? 0.962   -1.850  19.975  0.50 13.49 ? 252 PHE B CD2 1 
ATOM   4239  C  CD2 B PHE B  1 252 ? 1.938   -2.114  18.543  0.50 14.79 ? 252 PHE B CD2 1 
ATOM   4240  C  CE1 A PHE B  1 252 ? -0.636  0.112   18.864  0.50 14.54 ? 252 PHE B CE1 1 
ATOM   4241  C  CE1 B PHE B  1 252 ? 3.517   -3.421  16.693  0.50 17.15 ? 252 PHE B CE1 1 
ATOM   4242  C  CE2 A PHE B  1 252 ? -0.402  -1.869  20.180  0.50 14.45 ? 252 PHE B CE2 1 
ATOM   4243  C  CE2 B PHE B  1 252 ? 1.400   -3.032  17.677  0.50 15.71 ? 252 PHE B CE2 1 
ATOM   4244  C  CZ  A PHE B  1 252 ? -1.204  -0.889  19.626  0.50 14.97 ? 252 PHE B CZ  1 
ATOM   4245  C  CZ  B PHE B  1 252 ? 2.184   -3.665  16.755  0.50 16.61 ? 252 PHE B CZ  1 
ATOM   4246  N  N   A ASP B  1 253 ? 4.339   2.428   20.176  0.50 19.10 ? 253 ASP B N   1 
ATOM   4247  N  N   B ASP B  1 253 ? 4.536   2.499   20.272  0.50 23.15 ? 253 ASP B N   1 
ATOM   4248  C  CA  A ASP B  1 253 ? 4.248   3.467   21.212  0.50 18.72 ? 253 ASP B CA  1 
ATOM   4249  C  CA  B ASP B  1 253 ? 4.452   3.537   21.307  0.50 26.13 ? 253 ASP B CA  1 
ATOM   4250  C  C   A ASP B  1 253 ? 3.681   2.962   22.540  0.50 22.56 ? 253 ASP B C   1 
ATOM   4251  C  C   B ASP B  1 253 ? 3.922   3.053   22.662  0.50 26.78 ? 253 ASP B C   1 
ATOM   4252  O  O   A ASP B  1 253 ? 2.851   3.620   23.167  0.50 25.39 ? 253 ASP B O   1 
ATOM   4253  O  O   B ASP B  1 253 ? 3.468   3.850   23.482  0.50 26.29 ? 253 ASP B O   1 
ATOM   4254  C  CB  A ASP B  1 253 ? 3.417   4.662   20.728  0.50 18.55 ? 253 ASP B CB  1 
ATOM   4255  C  CB  B ASP B  1 253 ? 3.608   4.714   20.810  0.50 27.47 ? 253 ASP B CB  1 
ATOM   4256  C  CG  A ASP B  1 253 ? 4.047   5.392   19.549  0.50 18.68 ? 253 ASP B CG  1 
ATOM   4257  C  CG  B ASP B  1 253 ? 4.400   5.674   19.944  0.50 29.81 ? 253 ASP B CG  1 
ATOM   4258  O  OD1 A ASP B  1 253 ? 5.290   5.396   19.414  0.50 20.73 ? 253 ASP B OD1 1 
ATOM   4259  O  OD1 B ASP B  1 253 ? 5.522   5.316   19.530  0.50 26.43 ? 253 ASP B OD1 1 
ATOM   4260  O  OD2 A ASP B  1 253 ? 3.285   5.982   18.756  0.50 19.35 ? 253 ASP B OD2 1 
ATOM   4261  O  OD2 B ASP B  1 253 ? 3.899   6.787   19.676  0.50 32.00 ? 253 ASP B OD2 1 
ATOM   4262  N  N   . GLU B  1 254 ? 4.094   1.764   22.926  1.00 22.44 ? 254 GLU B N   1 
ATOM   4263  C  CA  . GLU B  1 254 ? 3.650   1.114   24.207  1.00 27.52 ? 254 GLU B CA  1 
ATOM   4264  C  C   . GLU B  1 254 ? 2.161   0.582   24.168  1.00 28.82 ? 254 GLU B C   1 
ATOM   4265  O  O   . GLU B  1 254 ? 1.725   -0.081  25.126  1.00 28.16 ? 254 GLU B O   1 
ATOM   4266  C  CB  . GLU B  1 254 ? 3.922   1.965   25.507  1.00 29.91 ? 254 GLU B CB  1 
ATOM   4267  C  CG  . GLU B  1 254 ? 5.409   2.053   25.871  1.00 41.15 ? 254 GLU B CG  1 
ATOM   4268  C  CD  . GLU B  1 254 ? 5.821   3.449   26.316  1.00 54.69 ? 254 GLU B CD  1 
ATOM   4269  O  OE1 . GLU B  1 254 ? 6.325   4.241   25.457  1.00 62.76 ? 254 GLU B OE1 1 
ATOM   4270  O  OE2 . GLU B  1 254 ? 5.614   3.764   27.514  1.00 58.79 ? 254 GLU B OE2 1 
ATOM   4271  N  N   . ARG B  1 255 ? 1.435   0.768   23.057  1.00 25.66 ? 255 ARG B N   1 
ATOM   4272  C  CA  . ARG B  1 255 ? 0.098   0.271   23.013  1.00 18.97 ? 255 ARG B CA  1 
ATOM   4273  C  C   . ARG B  1 255 ? 0.053   -1.370  22.968  1.00 20.06 ? 255 ARG B C   1 
ATOM   4274  O  O   . ARG B  1 255 ? 1.037   -2.034  22.604  1.00 23.95 ? 255 ARG B O   1 
ATOM   4275  C  CB  . ARG B  1 255 ? -0.536  0.809   21.629  1.00 20.70 ? 255 ARG B CB  1 
ATOM   4276  C  CG  . ARG B  1 255 ? -0.682  2.340   21.559  1.00 23.64 ? 255 ARG B CG  1 
ATOM   4277  C  CD  . ARG B  1 255 ? -1.258  2.750   20.144  1.00 20.51 ? 255 ARG B CD  1 
ATOM   4278  N  NE  . ARG B  1 255 ? -0.174  2.815   19.145  1.00 21.98 ? 255 ARG B NE  1 
ATOM   4279  C  CZ  . ARG B  1 255 ? -0.332  3.018   17.846  1.00 21.04 ? 255 ARG B CZ  1 
ATOM   4280  N  NH1 . ARG B  1 255 ? -1.586  3.130   17.362  1.00 14.70 ? 255 ARG B NH1 1 
ATOM   4281  N  NH2 . ARG B  1 255 ? 0.782   3.132   17.053  1.00 16.47 ? 255 ARG B NH2 1 
ATOM   4282  N  N   . LEU B  1 256 ? -1.015  -1.937  23.565  1.00 16.95 ? 256 LEU B N   1 
ATOM   4283  C  CA  . LEU B  1 256 ? -1.453  -3.280  23.263  1.00 16.63 ? 256 LEU B CA  1 
ATOM   4284  C  C   . LEU B  1 256 ? -2.641  -3.233  22.252  1.00 14.54 ? 256 LEU B C   1 
ATOM   4285  O  O   . LEU B  1 256 ? -3.330  -2.185  22.079  1.00 16.36 ? 256 LEU B O   1 
ATOM   4286  C  CB  . LEU B  1 256 ? -1.889  -3.971  24.557  1.00 20.24 ? 256 LEU B CB  1 
ATOM   4287  C  CG  . LEU B  1 256 ? -0.752  -4.078  25.540  1.00 22.14 ? 256 LEU B CG  1 
ATOM   4288  C  CD1 . LEU B  1 256 ? -1.205  -4.958  26.686  1.00 26.28 ? 256 LEU B CD1 1 
ATOM   4289  C  CD2 . LEU B  1 256 ? 0.579   -4.520  24.918  1.00 22.41 ? 256 LEU B CD2 1 
ATOM   4290  N  N   . VAL B  1 257 ? -2.843  -4.359  21.601  1.00 13.59 ? 257 VAL B N   1 
ATOM   4291  C  CA  . VAL B  1 257 ? -4.019  -4.611  20.757  1.00 13.09 ? 257 VAL B CA  1 
ATOM   4292  C  C   . VAL B  1 257 ? -4.841  -5.626  21.505  1.00 11.86 ? 257 VAL B C   1 
ATOM   4293  O  O   . VAL B  1 257 ? -4.318  -6.715  21.908  1.00 13.30 ? 257 VAL B O   1 
ATOM   4294  C  CB  . VAL B  1 257 ? -3.568  -5.139  19.415  1.00 12.91 ? 257 VAL B CB  1 
ATOM   4295  C  CG1 . VAL B  1 257 ? -4.744  -5.551  18.575  1.00 12.39 ? 257 VAL B CG1 1 
ATOM   4296  C  CG2 . VAL B  1 257 ? -2.744  -4.090  18.694  1.00 12.75 ? 257 VAL B CG2 1 
ATOM   4297  N  N   . TYR B  1 258 ? -6.105  -5.395  21.730  1.00 11.08 ? 258 TYR B N   1 
ATOM   4298  C  CA  . TYR B  1 258 ? -7.019  -6.270  22.450  1.00 11.03 ? 258 TYR B CA  1 
ATOM   4299  C  C   . TYR B  1 258 ? -7.736  -7.129  21.516  1.00 10.83 ? 258 TYR B C   1 
ATOM   4300  O  O   . TYR B  1 258 ? -8.198  -6.668  20.438  1.00 11.75 ? 258 TYR B O   1 
ATOM   4301  C  CB  . TYR B  1 258 ? -7.899  -5.370  23.304  1.00 12.67 ? 258 TYR B CB  1 
ATOM   4302  C  CG  . TYR B  1 258 ? -7.049  -4.493  24.196  1.00 15.59 ? 258 TYR B CG  1 
ATOM   4303  C  CD1 . TYR B  1 258 ? -6.542  -5.014  25.359  1.00 17.36 ? 258 TYR B CD1 1 
ATOM   4304  C  CD2 . TYR B  1 258 ? -6.721  -3.193  23.842  1.00 15.63 ? 258 TYR B CD2 1 
ATOM   4305  C  CE1 . TYR B  1 258 ? -5.725  -4.265  26.181  1.00 18.64 ? 258 TYR B CE1 1 
ATOM   4306  C  CE2 . TYR B  1 258 ? -5.913  -2.427  24.644  1.00 19.09 ? 258 TYR B CE2 1 
ATOM   4307  C  CZ  . TYR B  1 258 ? -5.414  -2.952  25.814  1.00 18.83 ? 258 TYR B CZ  1 
ATOM   4308  O  OH  . TYR B  1 258 ? -4.612  -2.173  26.597  1.00 22.05 ? 258 TYR B OH  1 
ATOM   4309  N  N   . THR B  1 259 ? -7.912  -8.386  21.842  1.00 10.48 ? 259 THR B N   1 
ATOM   4310  C  CA  . THR B  1 259 ? -8.538  -9.284  20.960  1.00 9.67  ? 259 THR B CA  1 
ATOM   4311  C  C   . THR B  1 259 ? -9.882  -9.808  21.541  1.00 11.08 ? 259 THR B C   1 
ATOM   4312  O  O   . THR B  1 259 ? -9.940  -10.087 22.797  1.00 11.52 ? 259 THR B O   1 
ATOM   4313  C  CB  . THR B  1 259 ? -7.678  -10.462 20.539  1.00 10.38 ? 259 THR B CB  1 
ATOM   4314  O  OG1 . THR B  1 259 ? -7.246  -11.234 21.682  1.00 13.07 ? 259 THR B OG1 1 
ATOM   4315  C  CG2 . THR B  1 259 ? -6.358  -9.933  19.834  1.00 11.46 ? 259 THR B CG2 1 
ATOM   4316  N  N   . SER B  1 260 ? -10.873 -10.046 20.728  1.00 9.45  ? 260 SER B N   1 
ATOM   4317  C  CA  . SER B  1 260 ? -12.151 -10.587 21.230  1.00 9.78  ? 260 SER B CA  1 
ATOM   4318  C  C   . SER B  1 260 ? -12.084 -12.102 21.251  1.00 11.28 ? 260 SER B C   1 
ATOM   4319  O  O   . SER B  1 260 ? -13.094 -12.754 21.601  1.00 13.00 ? 260 SER B O   1 
ATOM   4320  C  CB  . SER B  1 260 ? -13.288 -10.086 20.318  1.00 9.38  ? 260 SER B CB  1 
ATOM   4321  O  OG  . SER B  1 260 ? -13.166 -10.692 19.053  1.00 10.08 ? 260 SER B OG  1 
ATOM   4322  N  N   . PHE B  1 261 ? -11.006 -12.697 20.793  1.00 11.30 ? 261 PHE B N   1 
ATOM   4323  C  CA  . PHE B  1 261 ? -10.829 -14.157 20.693  1.00 11.86 ? 261 PHE B CA  1 
ATOM   4324  C  C   . PHE B  1 261 ? -9.571  -14.465 21.517  1.00 12.63 ? 261 PHE B C   1 
ATOM   4325  O  O   . PHE B  1 261 ? -8.657  -13.674 21.617  1.00 11.95 ? 261 PHE B O   1 
ATOM   4326  C  CB  . PHE B  1 261 ? -10.641 -14.578 19.177  1.00 11.47 ? 261 PHE B CB  1 
ATOM   4327  C  CG  . PHE B  1 261 ? -9.561  -13.826 18.458  1.00 11.59 ? 261 PHE B CG  1 
ATOM   4328  C  CD1 . PHE B  1 261 ? -9.877  -12.596 17.864  1.00 11.71 ? 261 PHE B CD1 1 
ATOM   4329  C  CD2 . PHE B  1 261 ? -8.270  -14.315 18.356  1.00 13.08 ? 261 PHE B CD2 1 
ATOM   4330  C  CE1 . PHE B  1 261 ? -8.895  -11.929 17.166  1.00 12.23 ? 261 PHE B CE1 1 
ATOM   4331  C  CE2 . PHE B  1 261 ? -7.285  -13.641 17.685  1.00 14.26 ? 261 PHE B CE2 1 
ATOM   4332  C  CZ  . PHE B  1 261 ? -7.609  -12.413 17.056  1.00 13.52 ? 261 PHE B CZ  1 
ATOM   4333  N  N   . SER B  1 262 ? -9.641  -15.619 22.216  1.00 14.94 ? 262 SER B N   1 
ATOM   4334  C  CA  . SER B  1 262 ? -8.539  -15.893 23.138  1.00 19.13 ? 262 SER B CA  1 
ATOM   4335  C  C   . SER B  1 262 ? -7.555  -16.848 22.492  1.00 22.45 ? 262 SER B C   1 
ATOM   4336  O  O   . SER B  1 262 ? -6.445  -17.022 23.028  1.00 23.28 ? 262 SER B O   1 
ATOM   4337  C  CB  . SER B  1 262 ? -9.040  -16.470 24.451  1.00 24.51 ? 262 SER B CB  1 
ATOM   4338  O  OG  . SER B  1 262 ? -9.714  -17.679 24.174  1.00 27.09 ? 262 SER B OG  1 
ATOM   4339  N  N   . GLN B  1 263 ? -7.962  -17.543 21.430  1.00 22.89 ? 263 GLN B N   1 
ATOM   4340  C  CA  . GLN B  1 263 ? -7.066  -18.386 20.642  1.00 25.37 ? 263 GLN B CA  1 
ATOM   4341  C  C   . GLN B  1 263 ? -7.666  -18.518 19.263  1.00 24.64 ? 263 GLN B C   1 
ATOM   4342  O  O   . GLN B  1 263 ? -7.000  -19.069 18.336  1.00 23.35 ? 263 GLN B O   1 
ATOM   4343  C  CB  . GLN B  1 263 ? -6.880  -19.799 21.269  1.00 25.29 ? 263 GLN B CB  1 
ATOM   4344  C  CG  . GLN B  1 263 ? -8.195  -20.553 21.568  1.00 31.05 ? 263 GLN B CG  1 
ATOM   4345  C  CD  . GLN B  1 263 ? -7.912  -21.905 22.215  1.00 36.32 ? 263 GLN B CD  1 
ATOM   4346  O  OE1 . GLN B  1 263 ? -7.483  -22.855 21.537  1.00 37.43 ? 263 GLN B OE1 1 
ATOM   4347  N  NE2 . GLN B  1 263 ? -8.170  -22.015 23.506  1.00 32.41 ? 263 GLN B NE2 1 
ATOM   4348  O  OXT . GLN B  1 263 ? -8.784  -18.045 19.120  1.00 20.22 ? 263 GLN B OXT 1 
ATOM   4349  N  N   A SER C  1 2   ? 35.332  21.054  -27.600 0.50 41.97 ? 2   SER C N   1 
ATOM   4350  N  N   B SER C  1 2   ? 36.370  16.959  -26.734 0.50 34.81 ? 2   SER C N   1 
ATOM   4351  C  CA  A SER C  1 2   ? 33.974  20.562  -27.989 0.50 37.56 ? 2   SER C CA  1 
ATOM   4352  C  CA  B SER C  1 2   ? 36.206  16.080  -25.541 0.50 36.63 ? 2   SER C CA  1 
ATOM   4353  C  C   A SER C  1 2   ? 33.589  19.261  -27.275 0.50 34.05 ? 2   SER C C   1 
ATOM   4354  C  C   B SER C  1 2   ? 35.057  16.426  -24.578 0.50 35.91 ? 2   SER C C   1 
ATOM   4355  O  O   A SER C  1 2   ? 33.802  18.160  -27.777 0.50 28.26 ? 2   SER C O   1 
ATOM   4356  O  O   B SER C  1 2   ? 35.021  15.887  -23.482 0.50 33.18 ? 2   SER C O   1 
ATOM   4357  C  CB  A SER C  1 2   ? 33.816  20.407  -29.512 0.50 37.09 ? 2   SER C CB  1 
ATOM   4358  C  CB  B SER C  1 2   ? 37.509  15.958  -24.744 0.50 39.60 ? 2   SER C CB  1 
ATOM   4359  O  OG  A SER C  1 2   ? 34.409  21.486  -30.197 0.50 37.65 ? 2   SER C OG  1 
ATOM   4360  O  OG  B SER C  1 2   ? 37.804  17.150  -24.054 0.50 44.09 ? 2   SER C OG  1 
ATOM   4361  N  N   A LYS C  1 3   ? 32.967  19.416  -26.115 0.50 31.92 ? 3   LYS C N   1 
ATOM   4362  N  N   B LYS C  1 3   ? 34.137  17.326  -24.954 0.50 31.52 ? 3   LYS C N   1 
ATOM   4363  C  CA  A LYS C  1 3   ? 32.395  18.305  -25.379 0.50 27.89 ? 3   LYS C CA  1 
ATOM   4364  C  CA  B LYS C  1 3   ? 32.858  17.422  -24.224 0.50 29.29 ? 3   LYS C CA  1 
ATOM   4365  C  C   A LYS C  1 3   ? 31.604  17.309  -26.256 0.50 24.95 ? 3   LYS C C   1 
ATOM   4366  C  C   B LYS C  1 3   ? 31.716  16.563  -24.814 0.50 26.90 ? 3   LYS C C   1 
ATOM   4367  O  O   A LYS C  1 3   ? 30.733  17.691  -27.076 0.50 23.60 ? 3   LYS C O   1 
ATOM   4368  O  O   B LYS C  1 3   ? 30.681  16.408  -24.167 0.50 25.38 ? 3   LYS C O   1 
ATOM   4369  C  CB  A LYS C  1 3   ? 31.524  18.859  -24.223 0.50 29.13 ? 3   LYS C CB  1 
ATOM   4370  C  CB  B LYS C  1 3   ? 32.396  18.872  -24.085 0.50 33.99 ? 3   LYS C CB  1 
ATOM   4371  C  CG  A LYS C  1 3   ? 30.718  17.814  -23.469 0.50 31.97 ? 3   LYS C CG  1 
ATOM   4372  C  CG  B LYS C  1 3   ? 33.264  19.723  -23.167 0.50 38.51 ? 3   LYS C CG  1 
ATOM   4373  C  CD  A LYS C  1 3   ? 30.707  17.972  -21.952 0.50 35.36 ? 3   LYS C CD  1 
ATOM   4374  C  CD  B LYS C  1 3   ? 33.012  21.207  -23.417 0.50 41.66 ? 3   LYS C CD  1 
ATOM   4375  C  CE  A LYS C  1 3   ? 29.770  19.085  -21.483 0.50 36.00 ? 3   LYS C CE  1 
ATOM   4376  C  CE  B LYS C  1 3   ? 33.938  22.089  -22.591 0.50 41.39 ? 3   LYS C CE  1 
ATOM   4377  N  NZ  A LYS C  1 3   ? 29.984  19.285  -20.029 0.50 35.10 ? 3   LYS C NZ  1 
ATOM   4378  N  NZ  B LYS C  1 3   ? 33.785  23.499  -23.044 0.50 43.66 ? 3   LYS C NZ  1 
ATOM   4379  N  N   . TRP C  1 4   ? 31.897  16.022  -26.036 1.00 21.50 ? 4   TRP C N   1 
ATOM   4380  C  CA  . TRP C  1 4   ? 30.997  14.980  -26.617 1.00 17.16 ? 4   TRP C CA  1 
ATOM   4381  C  C   . TRP C  1 4   ? 30.847  13.824  -25.654 1.00 16.26 ? 4   TRP C C   1 
ATOM   4382  O  O   . TRP C  1 4   ? 31.782  13.494  -24.876 1.00 17.06 ? 4   TRP C O   1 
ATOM   4383  C  CB  . TRP C  1 4   ? 31.511  14.541  -28.030 1.00 14.15 ? 4   TRP C CB  1 
ATOM   4384  C  CG  . TRP C  1 4   ? 32.842  13.936  -28.088 1.00 12.44 ? 4   TRP C CG  1 
ATOM   4385  C  CD1 . TRP C  1 4   ? 34.058  14.524  -28.265 1.00 12.82 ? 4   TRP C CD1 1 
ATOM   4386  C  CD2 . TRP C  1 4   ? 33.110  12.529  -27.937 1.00 10.76 ? 4   TRP C CD2 1 
ATOM   4387  N  NE1 . TRP C  1 4   ? 35.043  13.587  -28.250 1.00 13.65 ? 4   TRP C NE1 1 
ATOM   4388  C  CE2 . TRP C  1 4   ? 34.487  12.334  -28.080 1.00 12.86 ? 4   TRP C CE2 1 
ATOM   4389  C  CE3 . TRP C  1 4   ? 32.273  11.402  -27.805 1.00 11.36 ? 4   TRP C CE3 1 
ATOM   4390  C  CZ2 . TRP C  1 4   ? 35.095  11.085  -28.027 1.00 12.62 ? 4   TRP C CZ2 1 
ATOM   4391  C  CZ3 . TRP C  1 4   ? 32.885  10.137  -27.767 1.00 10.23 ? 4   TRP C CZ3 1 
ATOM   4392  C  CH2 . TRP C  1 4   ? 34.268  9.963   -27.865 1.00 12.27 ? 4   TRP C CH2 1 
ATOM   4393  N  N   . THR C  1 5   ? 29.719  13.152  -25.732 1.00 15.02 ? 5   THR C N   1 
ATOM   4394  C  CA  . THR C  1 5   ? 29.480  12.014  -24.833 1.00 15.24 ? 5   THR C CA  1 
ATOM   4395  C  C   . THR C  1 5   ? 28.761  10.901  -25.610 1.00 14.96 ? 5   THR C C   1 
ATOM   4396  O  O   . THR C  1 5   ? 28.536  10.998  -26.850 1.00 13.67 ? 5   THR C O   1 
ATOM   4397  C  CB  . THR C  1 5   ? 28.486  12.423  -23.715 1.00 17.66 ? 5   THR C CB  1 
ATOM   4398  O  OG1 . THR C  1 5   ? 27.219  12.694  -24.356 1.00 18.62 ? 5   THR C OG1 1 
ATOM   4399  C  CG2 . THR C  1 5   ? 29.065  13.637  -22.954 1.00 18.70 ? 5   THR C CG2 1 
ATOM   4400  N  N   . TYR C  1 6   ? 28.345  9.830   -24.882 1.00 16.01 ? 6   TYR C N   1 
ATOM   4401  C  CA  . TYR C  1 6   ? 27.511  8.749   -25.418 1.00 14.99 ? 6   TYR C CA  1 
ATOM   4402  C  C   . TYR C  1 6   ? 26.005  8.830   -24.947 1.00 16.92 ? 6   TYR C C   1 
ATOM   4403  O  O   . TYR C  1 6   ? 25.277  7.843   -24.997 1.00 17.70 ? 6   TYR C O   1 
ATOM   4404  C  CB  . TYR C  1 6   ? 28.040  7.372   -25.298 1.00 13.57 ? 6   TYR C CB  1 
ATOM   4405  C  CG  . TYR C  1 6   ? 29.360  7.119   -26.029 1.00 12.81 ? 6   TYR C CG  1 
ATOM   4406  C  CD1 . TYR C  1 6   ? 30.611  7.408   -25.439 1.00 13.28 ? 6   TYR C CD1 1 
ATOM   4407  C  CD2 . TYR C  1 6   ? 29.362  6.558   -27.304 1.00 12.87 ? 6   TYR C CD2 1 
ATOM   4408  C  CE1 . TYR C  1 6   ? 31.786  7.160   -26.126 1.00 13.89 ? 6   TYR C CE1 1 
ATOM   4409  C  CE2 . TYR C  1 6   ? 30.536  6.310   -27.987 1.00 11.49 ? 6   TYR C CE2 1 
ATOM   4410  C  CZ  . TYR C  1 6   ? 31.738  6.620   -27.375 1.00 11.49 ? 6   TYR C CZ  1 
ATOM   4411  O  OH  . TYR C  1 6   ? 32.901  6.356   -28.079 1.00 13.15 ? 6   TYR C OH  1 
ATOM   4412  N  N   . PHE C  1 7   ? 25.532  9.986   -24.456 1.00 21.71 ? 7   PHE C N   1 
ATOM   4413  C  CA  . PHE C  1 7   ? 24.066  10.141  -24.114 1.00 27.22 ? 7   PHE C CA  1 
ATOM   4414  C  C   . PHE C  1 7   ? 23.594  11.603  -24.135 1.00 31.57 ? 7   PHE C C   1 
ATOM   4415  O  O   . PHE C  1 7   ? 24.242  12.430  -24.775 1.00 28.07 ? 7   PHE C O   1 
ATOM   4416  C  CB  . PHE C  1 7   ? 23.844  9.766   -22.689 1.00 26.27 ? 7   PHE C CB  1 
ATOM   4417  C  CG  . PHE C  1 7   ? 24.587  10.684  -21.748 1.00 32.89 ? 7   PHE C CG  1 
ATOM   4418  C  CD1 . PHE C  1 7   ? 23.933  11.767  -21.157 1.00 32.99 ? 7   PHE C CD1 1 
ATOM   4419  C  CD2 . PHE C  1 7   ? 25.955  10.522  -21.511 1.00 34.19 ? 7   PHE C CD2 1 
ATOM   4420  C  CE1 . PHE C  1 7   ? 24.625  12.658  -20.315 1.00 28.69 ? 7   PHE C CE1 1 
ATOM   4421  C  CE2 . PHE C  1 7   ? 26.655  11.413  -20.649 1.00 29.53 ? 7   PHE C CE2 1 
ATOM   4422  C  CZ  . PHE C  1 7   ? 26.006  12.495  -20.107 1.00 30.93 ? 7   PHE C CZ  1 
ATOM   4423  N  N   . GLY C  1 8   ? 22.594  11.946  -23.289 1.00 33.65 ? 8   GLY C N   1 
ATOM   4424  C  CA  . GLY C  1 8   ? 22.064  13.353  -23.031 1.00 24.31 ? 8   GLY C CA  1 
ATOM   4425  C  C   . GLY C  1 8   ? 21.980  14.035  -24.347 1.00 26.98 ? 8   GLY C C   1 
ATOM   4426  O  O   . GLY C  1 8   ? 21.498  13.382  -25.374 1.00 30.20 ? 8   GLY C O   1 
ATOM   4427  N  N   . PRO C  1 9   ? 22.335  15.325  -24.381 1.00 21.91 ? 9   PRO C N   1 
ATOM   4428  C  CA  . PRO C  1 9   ? 22.276  16.141  -25.589 1.00 22.08 ? 9   PRO C CA  1 
ATOM   4429  C  C   . PRO C  1 9   ? 23.604  16.200  -26.322 1.00 18.64 ? 9   PRO C C   1 
ATOM   4430  O  O   . PRO C  1 9   ? 23.642  16.721  -27.436 1.00 19.18 ? 9   PRO C O   1 
ATOM   4431  C  CB  . PRO C  1 9   ? 21.930  17.523  -25.039 1.00 23.95 ? 9   PRO C CB  1 
ATOM   4432  C  CG  . PRO C  1 9   ? 22.545  17.546  -23.674 1.00 25.24 ? 9   PRO C CG  1 
ATOM   4433  C  CD  . PRO C  1 9   ? 22.727  16.123  -23.207 1.00 24.04 ? 9   PRO C CD  1 
ATOM   4434  N  N   . ASP C  1 10  ? 24.677  15.685  -25.728 1.00 19.43 ? 10  ASP C N   1 
ATOM   4435  C  CA  . ASP C  1 10  ? 25.967  15.754  -26.443 1.00 19.27 ? 10  ASP C CA  1 
ATOM   4436  C  C   . ASP C  1 10  ? 26.400  14.398  -26.957 1.00 16.50 ? 10  ASP C C   1 
ATOM   4437  O  O   . ASP C  1 10  ? 27.582  14.230  -27.346 1.00 15.68 ? 10  ASP C O   1 
ATOM   4438  C  CB  . ASP C  1 10  ? 27.119  16.388  -25.601 1.00 21.30 ? 10  ASP C CB  1 
ATOM   4439  C  CG  . ASP C  1 10  ? 26.817  17.841  -25.217 1.00 26.58 ? 10  ASP C CG  1 
ATOM   4440  O  OD1 . ASP C  1 10  ? 26.353  18.590  -26.098 1.00 29.87 ? 10  ASP C OD1 1 
ATOM   4441  O  OD2 . ASP C  1 10  ? 26.947  18.173  -23.999 1.00 28.78 ? 10  ASP C OD2 1 
ATOM   4442  N  N   . GLY C  1 11  ? 25.390  13.535  -27.069 1.00 18.51 ? 11  GLY C N   1 
ATOM   4443  C  CA  . GLY C  1 11  ? 25.578  12.100  -27.520 1.00 13.88 ? 11  GLY C CA  1 
ATOM   4444  C  C   . GLY C  1 11  ? 25.647  12.025  -29.044 1.00 11.51 ? 11  GLY C C   1 
ATOM   4445  O  O   . GLY C  1 11  ? 25.722  12.992  -29.826 1.00 11.26 ? 11  GLY C O   1 
ATOM   4446  N  N   . GLU C  1 12  ? 25.725  10.750  -29.476 1.00 10.44 ? 12  GLU C N   1 
ATOM   4447  C  CA  . GLU C  1 12  ? 26.176  10.502  -30.837 1.00 9.99  ? 12  GLU C CA  1 
ATOM   4448  C  C   . GLU C  1 12  ? 25.323  11.150  -31.932 1.00 9.90  ? 12  GLU C C   1 
ATOM   4449  O  O   . GLU C  1 12  ? 25.857  11.471  -32.990 1.00 9.72  ? 12  GLU C O   1 
ATOM   4450  C  CB  . GLU C  1 12  ? 26.342  8.984   -31.082 1.00 9.24  ? 12  GLU C CB  1 
ATOM   4451  C  CG  . GLU C  1 12  ? 25.014  8.241   -31.200 1.00 9.44  ? 12  GLU C CG  1 
ATOM   4452  C  CD  . GLU C  1 12  ? 25.273  6.744   -31.007 1.00 8.73  ? 12  GLU C CD  1 
ATOM   4453  O  OE1 . GLU C  1 12  ? 25.576  6.019   -31.934 1.00 9.80  ? 12  GLU C OE1 1 
ATOM   4454  O  OE2 . GLU C  1 12  ? 25.238  6.337   -29.804 1.00 11.02 ? 12  GLU C OE2 1 
ATOM   4455  N  N   . ASN C  1 13  ? 24.003  11.296  -31.734 1.00 9.27  ? 13  ASN C N   1 
ATOM   4456  C  CA  . ASN C  1 13  ? 23.228  11.930  -32.792 1.00 9.37  ? 13  ASN C CA  1 
ATOM   4457  C  C   . ASN C  1 13  ? 23.551  13.433  -32.954 1.00 9.36  ? 13  ASN C C   1 
ATOM   4458  O  O   . ASN C  1 13  ? 23.189  13.976  -33.978 1.00 10.27 ? 13  ASN C O   1 
ATOM   4459  C  CB  . ASN C  1 13  ? 21.717  11.763  -32.465 1.00 9.31  ? 13  ASN C CB  1 
ATOM   4460  C  CG  . ASN C  1 13  ? 21.251  10.330  -32.633 1.00 9.62  ? 13  ASN C CG  1 
ATOM   4461  O  OD1 . ASN C  1 13  ? 21.944  9.448   -33.186 1.00 10.67 ? 13  ASN C OD1 1 
ATOM   4462  N  ND2 . ASN C  1 13  ? 20.102  10.108  -32.102 1.00 10.21 ? 13  ASN C ND2 1 
ATOM   4463  N  N   A SER C  1 14  ? 24.152  14.012  -31.911 0.50 9.29  ? 14  SER C N   1 
ATOM   4464  N  N   B SER C  1 14  ? 24.175  14.051  -31.960 0.50 10.07 ? 14  SER C N   1 
ATOM   4465  C  CA  A SER C  1 14  ? 24.546  15.432  -31.897 0.50 9.27  ? 14  SER C CA  1 
ATOM   4466  C  CA  B SER C  1 14  ? 24.573  15.469  -32.116 0.50 10.25 ? 14  SER C CA  1 
ATOM   4467  C  C   A SER C  1 14  ? 25.968  15.654  -32.377 0.50 9.75  ? 14  SER C C   1 
ATOM   4468  C  C   B SER C  1 14  ? 26.043  15.661  -32.345 0.50 10.67 ? 14  SER C C   1 
ATOM   4469  O  O   A SER C  1 14  ? 26.301  16.795  -32.723 0.50 9.68  ? 14  SER C O   1 
ATOM   4470  O  O   B SER C  1 14  ? 26.534  16.779  -32.393 0.50 11.20 ? 14  SER C O   1 
ATOM   4471  C  CB  A SER C  1 14  ? 24.299  16.023  -30.483 0.50 9.63  ? 14  SER C CB  1 
ATOM   4472  C  CB  B SER C  1 14  ? 24.277  16.241  -30.856 0.50 11.28 ? 14  SER C CB  1 
ATOM   4473  O  OG  A SER C  1 14  ? 22.910  16.114  -30.303 0.50 10.82 ? 14  SER C OG  1 
ATOM   4474  O  OG  B SER C  1 14  ? 25.087  15.725  -29.822 0.50 15.13 ? 14  SER C OG  1 
ATOM   4475  N  N   . TRP C  1 15  ? 26.794  14.598  -32.511 1.00 10.17 ? 15  TRP C N   1 
ATOM   4476  C  CA  . TRP C  1 15  ? 28.217  14.793  -32.801 1.00 10.32 ? 15  TRP C CA  1 
ATOM   4477  C  C   . TRP C  1 15  ? 28.437  15.590  -34.090 1.00 9.93  ? 15  TRP C C   1 
ATOM   4478  O  O   . TRP C  1 15  ? 29.369  16.396  -34.195 1.00 10.33 ? 15  TRP C O   1 
ATOM   4479  C  CB  . TRP C  1 15  ? 28.918  13.472  -33.002 1.00 9.27  ? 15  TRP C CB  1 
ATOM   4480  C  CG  . TRP C  1 15  ? 29.088  12.646  -31.754 1.00 8.40  ? 15  TRP C CG  1 
ATOM   4481  C  CD1 . TRP C  1 15  ? 28.778  12.973  -30.438 1.00 9.18  ? 15  TRP C CD1 1 
ATOM   4482  C  CD2 . TRP C  1 15  ? 29.527  11.292  -31.723 1.00 8.51  ? 15  TRP C CD2 1 
ATOM   4483  N  NE1 . TRP C  1 15  ? 29.094  11.889  -29.582 1.00 9.91  ? 15  TRP C NE1 1 
ATOM   4484  C  CE2 . TRP C  1 15  ? 29.527  10.848  -30.358 1.00 9.11  ? 15  TRP C CE2 1 
ATOM   4485  C  CE3 . TRP C  1 15  ? 29.941  10.386  -32.748 1.00 8.41  ? 15  TRP C CE3 1 
ATOM   4486  C  CZ2 . TRP C  1 15  ? 29.906  9.563   -30.014 1.00 9.22  ? 15  TRP C CZ2 1 
ATOM   4487  C  CZ3 . TRP C  1 15  ? 30.327  9.100   -32.374 1.00 8.45  ? 15  TRP C CZ3 1 
ATOM   4488  C  CH2 . TRP C  1 15  ? 30.342  8.706   -31.004 1.00 9.04  ? 15  TRP C CH2 1 
ATOM   4489  N  N   . SER C  1 16  ? 27.551  15.447  -35.069 1.00 10.11 ? 16  SER C N   1 
ATOM   4490  C  CA  . SER C  1 16  ? 27.746  16.073  -36.368 1.00 9.40  ? 16  SER C CA  1 
ATOM   4491  C  C   . SER C  1 16  ? 27.638  17.613  -36.253 1.00 10.50 ? 16  SER C C   1 
ATOM   4492  O  O   . SER C  1 16  ? 28.092  18.259  -37.218 1.00 10.96 ? 16  SER C O   1 
ATOM   4493  C  CB  . SER C  1 16  ? 26.696  15.608  -37.378 1.00 10.32 ? 16  SER C CB  1 
ATOM   4494  O  OG  . SER C  1 16  ? 25.362  15.957  -36.923 1.00 11.02 ? 16  SER C OG  1 
ATOM   4495  N  N   A LYS C  1 17  ? 27.073  18.104  -35.135 0.50 10.25 ? 17  LYS C N   1 
ATOM   4496  N  N   B LYS C  1 17  ? 27.074  18.149  -35.193 0.50 10.25 ? 17  LYS C N   1 
ATOM   4497  C  CA  A LYS C  1 17  ? 26.977  19.585  -34.941 0.50 10.85 ? 17  LYS C CA  1 
ATOM   4498  C  CA  B LYS C  1 17  ? 27.073  19.633  -35.175 0.50 10.23 ? 17  LYS C CA  1 
ATOM   4499  C  C   A LYS C  1 17  ? 28.358  20.222  -34.911 0.50 10.68 ? 17  LYS C C   1 
ATOM   4500  C  C   B LYS C  1 17  ? 28.535  20.154  -35.121 0.50 10.01 ? 17  LYS C C   1 
ATOM   4501  O  O   A LYS C  1 17  ? 28.549  21.271  -35.474 0.50 10.21 ? 17  LYS C O   1 
ATOM   4502  O  O   B LYS C  1 17  ? 28.988  20.999  -35.975 0.50 9.12  ? 17  LYS C O   1 
ATOM   4503  C  CB  A LYS C  1 17  ? 26.273  19.895  -33.629 0.50 11.15 ? 17  LYS C CB  1 
ATOM   4504  C  CB  B LYS C  1 17  ? 26.186  20.075  -34.002 0.50 10.72 ? 17  LYS C CB  1 
ATOM   4505  C  CG  A LYS C  1 17  ? 24.774  19.610  -33.589 0.50 12.18 ? 17  LYS C CG  1 
ATOM   4506  C  CG  B LYS C  1 17  ? 24.688  19.844  -34.253 0.50 12.47 ? 17  LYS C CG  1 
ATOM   4507  C  CD  A LYS C  1 17  ? 24.177  19.913  -32.194 0.50 13.11 ? 17  LYS C CD  1 
ATOM   4508  C  CD  B LYS C  1 17  ? 23.811  20.130  -33.037 0.50 14.24 ? 17  LYS C CD  1 
ATOM   4509  C  CE  A LYS C  1 17  ? 22.865  19.193  -31.984 0.50 13.80 ? 17  LYS C CE  1 
ATOM   4510  C  CE  B LYS C  1 17  ? 24.088  21.511  -32.480 0.50 15.46 ? 17  LYS C CE  1 
ATOM   4511  N  NZ  A LYS C  1 17  ? 22.428  19.310  -30.570 0.50 15.28 ? 17  LYS C NZ  1 
ATOM   4512  N  NZ  B LYS C  1 17  ? 22.998  21.881  -31.521 0.50 18.96 ? 17  LYS C NZ  1 
ATOM   4513  N  N   . LYS C  1 18  ? 29.297  19.669  -34.143 1.00 10.66 ? 18  LYS C N   1 
ATOM   4514  C  CA  . LYS C  1 18  ? 30.663  20.150  -34.029 1.00 11.82 ? 18  LYS C CA  1 
ATOM   4515  C  C   . LYS C  1 18  ? 31.650  19.412  -34.862 1.00 12.94 ? 18  LYS C C   1 
ATOM   4516  O  O   . LYS C  1 18  ? 32.697  19.943  -35.212 1.00 15.61 ? 18  LYS C O   1 
ATOM   4517  C  CB  . LYS C  1 18  ? 31.104  20.175  -32.537 1.00 15.57 ? 18  LYS C CB  1 
ATOM   4518  C  CG  . LYS C  1 18  ? 30.442  21.317  -31.716 1.00 23.49 ? 18  LYS C CG  1 
ATOM   4519  C  CD  . LYS C  1 18  ? 30.944  22.761  -31.967 1.00 27.51 ? 18  LYS C CD  1 
ATOM   4520  C  CE  . LYS C  1 18  ? 30.486  23.728  -30.896 1.00 32.80 ? 18  LYS C CE  1 
ATOM   4521  N  NZ  . LYS C  1 18  ? 31.684  24.214  -30.149 1.00 40.50 ? 18  LYS C NZ  1 
ATOM   4522  N  N   . TYR C  1 19  ? 31.329  18.183  -35.313 1.00 11.21 ? 19  TYR C N   1 
ATOM   4523  C  CA  . TYR C  1 19  ? 32.239  17.316  -36.034 1.00 9.81  ? 19  TYR C CA  1 
ATOM   4524  C  C   . TYR C  1 19  ? 31.544  16.897  -37.324 1.00 10.05 ? 19  TYR C C   1 
ATOM   4525  O  O   . TYR C  1 19  ? 30.858  15.797  -37.322 1.00 10.52 ? 19  TYR C O   1 
ATOM   4526  C  CB  . TYR C  1 19  ? 32.595  16.050  -35.175 1.00 9.88  ? 19  TYR C CB  1 
ATOM   4527  C  CG  . TYR C  1 19  ? 33.218  16.475  -33.842 1.00 10.92 ? 19  TYR C CG  1 
ATOM   4528  C  CD1 . TYR C  1 19  ? 34.535  16.805  -33.780 1.00 11.08 ? 19  TYR C CD1 1 
ATOM   4529  C  CD2 . TYR C  1 19  ? 32.437  16.490  -32.693 1.00 10.75 ? 19  TYR C CD2 1 
ATOM   4530  C  CE1 . TYR C  1 19  ? 35.129  17.182  -32.546 1.00 12.27 ? 19  TYR C CE1 1 
ATOM   4531  C  CE2 . TYR C  1 19  ? 33.015  16.809  -31.466 1.00 12.50 ? 19  TYR C CE2 1 
ATOM   4532  C  CZ  . TYR C  1 19  ? 34.351  17.161  -31.424 1.00 12.67 ? 19  TYR C CZ  1 
ATOM   4533  O  OH  . TYR C  1 19  ? 34.945  17.458  -30.144 1.00 18.12 ? 19  TYR C OH  1 
ATOM   4534  N  N   . PRO C  1 20  ? 31.631  17.669  -38.407 1.00 10.00 ? 20  PRO C N   1 
ATOM   4535  C  CA  . PRO C  1 20  ? 30.725  17.434  -39.488 1.00 10.29 ? 20  PRO C CA  1 
ATOM   4536  C  C   . PRO C  1 20  ? 30.946  16.041  -40.122 1.00 10.22 ? 20  PRO C C   1 
ATOM   4537  O  O   . PRO C  1 20  ? 30.001  15.502  -40.743 1.00 11.05 ? 20  PRO C O   1 
ATOM   4538  C  CB  . PRO C  1 20  ? 30.959  18.580  -40.508 1.00 12.27 ? 20  PRO C CB  1 
ATOM   4539  C  CG  . PRO C  1 20  ? 31.836  19.562  -39.690 1.00 16.68 ? 20  PRO C CG  1 
ATOM   4540  C  CD  . PRO C  1 20  ? 32.379  18.928  -38.492 1.00 11.34 ? 20  PRO C CD  1 
ATOM   4541  N  N   . SER C  1 21  ? 32.142  15.473  -40.050 1.00 8.84  ? 21  SER C N   1 
ATOM   4542  C  CA  . SER C  1 21  ? 32.336  14.158  -40.682 1.00 8.92  ? 21  SER C CA  1 
ATOM   4543  C  C   . SER C  1 21  ? 31.478  13.085  -40.021 1.00 9.57  ? 21  SER C C   1 
ATOM   4544  O  O   . SER C  1 21  ? 31.230  12.078  -40.683 1.00 9.63  ? 21  SER C O   1 
ATOM   4545  C  CB  . SER C  1 21  ? 33.840  13.784  -40.589 1.00 9.72  ? 21  SER C CB  1 
ATOM   4546  O  OG  . SER C  1 21  ? 34.575  14.586  -41.509 1.00 11.77 ? 21  SER C OG  1 
ATOM   4547  N  N   . CYS C  1 22  ? 30.964  13.323  -38.814 1.00 9.40  ? 22  CYS C N   1 
ATOM   4548  C  CA  . CYS C  1 22  ? 30.076  12.303  -38.179 1.00 9.60  ? 22  CYS C CA  1 
ATOM   4549  C  C   . CYS C  1 22  ? 28.767  12.151  -38.908 1.00 10.41 ? 22  CYS C C   1 
ATOM   4550  O  O   . CYS C  1 22  ? 28.106  11.111  -38.688 1.00 10.31 ? 22  CYS C O   1 
ATOM   4551  C  CB  . CYS C  1 22  ? 29.883  12.657  -36.682 1.00 9.17  ? 22  CYS C CB  1 
ATOM   4552  S  SG  . CYS C  1 22  ? 31.412  12.710  -35.722 1.00 10.39 ? 22  CYS C SG  1 
ATOM   4553  N  N   . GLY C  1 23  ? 28.366  13.097  -39.767 1.00 10.08 ? 23  GLY C N   1 
ATOM   4554  C  CA  . GLY C  1 23  ? 27.219  12.967  -40.648 1.00 10.21 ? 23  GLY C CA  1 
ATOM   4555  C  C   . GLY C  1 23  ? 27.581  12.723  -42.086 1.00 10.53 ? 23  GLY C C   1 
ATOM   4556  O  O   . GLY C  1 23  ? 26.678  12.812  -42.910 1.00 10.69 ? 23  GLY C O   1 
ATOM   4557  N  N   . GLY C  1 24  ? 28.843  12.385  -42.390 1.00 9.49  ? 24  GLY C N   1 
ATOM   4558  C  CA  . GLY C  1 24  ? 29.304  12.187  -43.731 1.00 10.54 ? 24  GLY C CA  1 
ATOM   4559  C  C   . GLY C  1 24  ? 29.374  10.761  -44.178 1.00 11.51 ? 24  GLY C C   1 
ATOM   4560  O  O   . GLY C  1 24  ? 28.702  9.876   -43.640 1.00 13.04 ? 24  GLY C O   1 
ATOM   4561  N  N   . LEU C  1 25  ? 30.165  10.531  -45.156 1.00 11.50 ? 25  LEU C N   1 
ATOM   4562  C  CA  . LEU C  1 25  ? 30.293  9.206   -45.784 1.00 12.84 ? 25  LEU C CA  1 
ATOM   4563  C  C   . LEU C  1 25  ? 31.190  8.313   -44.923 1.00 13.07 ? 25  LEU C C   1 
ATOM   4564  O  O   . LEU C  1 25  ? 32.005  8.728   -44.043 1.00 10.57 ? 25  LEU C O   1 
ATOM   4565  C  CB  . LEU C  1 25  ? 30.948  9.335   -47.177 1.00 15.31 ? 25  LEU C CB  1 
ATOM   4566  C  CG  . LEU C  1 25  ? 30.205  10.345  -48.103 1.00 17.63 ? 25  LEU C CG  1 
ATOM   4567  C  CD1 . LEU C  1 25  ? 30.893  10.392  -49.487 1.00 21.57 ? 25  LEU C CD1 1 
ATOM   4568  C  CD2 . LEU C  1 25  ? 28.769  9.848   -48.241 1.00 22.56 ? 25  LEU C CD2 1 
ATOM   4569  N  N   . LEU C  1 26  ? 31.091  7.015   -45.238 1.00 12.22 ? 26  LEU C N   1 
ATOM   4570  C  CA  . LEU C  1 26  ? 32.041  5.963   -44.839 1.00 12.10 ? 26  LEU C CA  1 
ATOM   4571  C  C   . LEU C  1 26  ? 32.044  5.800   -43.310 1.00 10.20 ? 26  LEU C C   1 
ATOM   4572  O  O   . LEU C  1 26  ? 33.039  5.390   -42.717 1.00 12.21 ? 26  LEU C O   1 
ATOM   4573  C  CB  . LEU C  1 26  ? 33.481  6.223   -45.333 1.00 13.57 ? 26  LEU C CB  1 
ATOM   4574  C  CG  . LEU C  1 26  ? 33.714  6.246   -46.888 1.00 19.84 ? 26  LEU C CG  1 
ATOM   4575  C  CD1 . LEU C  1 26  ? 35.233  6.236   -47.228 1.00 20.90 ? 26  LEU C CD1 1 
ATOM   4576  C  CD2 . LEU C  1 26  ? 33.050  5.124   -47.664 1.00 20.88 ? 26  LEU C CD2 1 
ATOM   4577  N  N   . GLN C  1 27  ? 30.938  5.997   -42.640 1.00 8.66  ? 27  GLN C N   1 
ATOM   4578  C  CA  . GLN C  1 27  ? 30.880  5.903   -41.190 1.00 8.63  ? 27  GLN C CA  1 
ATOM   4579  C  C   . GLN C  1 27  ? 30.918  4.510   -40.666 1.00 10.04 ? 27  GLN C C   1 
ATOM   4580  O  O   . GLN C  1 27  ? 30.328  3.559   -41.212 1.00 11.56 ? 27  GLN C O   1 
ATOM   4581  C  CB  . GLN C  1 27  ? 29.701  6.647   -40.621 1.00 8.46  ? 27  GLN C CB  1 
ATOM   4582  C  CG  . GLN C  1 27  ? 29.786  8.180   -40.918 1.00 8.42  ? 27  GLN C CG  1 
ATOM   4583  C  CD  . GLN C  1 27  ? 30.930  8.821   -40.220 1.00 7.85  ? 27  GLN C CD  1 
ATOM   4584  O  OE1 . GLN C  1 27  ? 30.888  9.060   -39.014 1.00 8.60  ? 27  GLN C OE1 1 
ATOM   4585  N  NE2 . GLN C  1 27  ? 31.989  9.075   -40.989 1.00 8.81  ? 27  GLN C NE2 1 
ATOM   4586  N  N   . SER C  1 28  ? 31.633  4.355   -39.564 1.00 8.83  ? 28  SER C N   1 
ATOM   4587  C  CA  . SER C  1 28  ? 31.770  3.102   -38.787 1.00 8.53  ? 28  SER C CA  1 
ATOM   4588  C  C   . SER C  1 28  ? 31.154  3.286   -37.439 1.00 8.63  ? 28  SER C C   1 
ATOM   4589  O  O   . SER C  1 28  ? 31.051  4.446   -36.963 1.00 9.21  ? 28  SER C O   1 
ATOM   4590  C  CB  . SER C  1 28  ? 33.268  2.806   -38.620 1.00 8.62  ? 28  SER C CB  1 
ATOM   4591  O  OG  . SER C  1 28  ? 33.829  2.513   -39.908 1.00 8.58  ? 28  SER C OG  1 
ATOM   4592  N  N   . PRO C  1 29  ? 30.797  2.241   -36.721 1.00 7.83  ? 29  PRO C N   1 
ATOM   4593  C  CA  . PRO C  1 29  ? 30.916  0.845   -37.070 1.00 7.07  ? 29  PRO C CA  1 
ATOM   4594  C  C   . PRO C  1 29  ? 29.719  0.391   -37.881 1.00 7.83  ? 29  PRO C C   1 
ATOM   4595  O  O   . PRO C  1 29  ? 28.775  1.118   -38.161 1.00 8.71  ? 29  PRO C O   1 
ATOM   4596  C  CB  . PRO C  1 29  ? 30.938  0.123   -35.684 1.00 7.46  ? 29  PRO C CB  1 
ATOM   4597  C  CG  . PRO C  1 29  ? 29.922  0.953   -34.931 1.00 9.12  ? 29  PRO C CG  1 
ATOM   4598  C  CD  . PRO C  1 29  ? 30.205  2.447   -35.368 1.00 8.79  ? 29  PRO C CD  1 
ATOM   4599  N  N   . ILE C  1 30  ? 29.765  -0.893  -38.292 1.00 8.62  ? 30  ILE C N   1 
ATOM   4600  C  CA  . ILE C  1 30  ? 28.737  -1.489  -39.149 1.00 8.20  ? 30  ILE C CA  1 
ATOM   4601  C  C   . ILE C  1 30  ? 28.451  -2.917  -38.686 1.00 8.78  ? 30  ILE C C   1 
ATOM   4602  O  O   . ILE C  1 30  ? 29.224  -3.529  -37.903 1.00 8.66  ? 30  ILE C O   1 
ATOM   4603  C  CB  . ILE C  1 30  ? 29.209  -1.534  -40.623 1.00 8.36  ? 30  ILE C CB  1 
ATOM   4604  C  CG1 . ILE C  1 30  ? 30.488  -2.402  -40.779 1.00 8.61  ? 30  ILE C CG1 1 
ATOM   4605  C  CG2 . ILE C  1 30  ? 29.383  -0.095  -41.123 1.00 10.11 ? 30  ILE C CG2 1 
ATOM   4606  C  CD1 . ILE C  1 30  ? 30.867  -2.633  -42.261 1.00 10.37 ? 30  ILE C CD1 1 
ATOM   4607  N  N   . ASP C  1 31  ? 27.328  -3.417  -39.138 1.00 9.28  ? 31  ASP C N   1 
ATOM   4608  C  CA  . ASP C  1 31  ? 26.998  -4.833  -38.982 1.00 10.13 ? 31  ASP C CA  1 
ATOM   4609  C  C   . ASP C  1 31  ? 27.633  -5.641  -40.057 1.00 10.04 ? 31  ASP C C   1 
ATOM   4610  O  O   . ASP C  1 31  ? 27.517  -5.359  -41.296 1.00 12.37 ? 31  ASP C O   1 
ATOM   4611  C  CB  . ASP C  1 31  ? 25.489  -5.024  -39.103 1.00 11.08 ? 31  ASP C CB  1 
ATOM   4612  C  CG  . ASP C  1 31  ? 25.099  -6.460  -38.844 1.00 11.35 ? 31  ASP C CG  1 
ATOM   4613  O  OD1 . ASP C  1 31  ? 25.537  -7.097  -37.861 1.00 11.71 ? 31  ASP C OD1 1 
ATOM   4614  O  OD2 . ASP C  1 31  ? 24.259  -6.971  -39.613 1.00 16.01 ? 31  ASP C OD2 1 
ATOM   4615  N  N   . LEU C  1 32  ? 28.269  -6.717  -39.647 1.00 9.90  ? 32  LEU C N   1 
ATOM   4616  C  CA  . LEU C  1 32  ? 28.967  -7.652  -40.567 1.00 11.72 ? 32  LEU C CA  1 
ATOM   4617  C  C   . LEU C  1 32  ? 28.077  -8.861  -40.745 1.00 12.14 ? 32  LEU C C   1 
ATOM   4618  O  O   . LEU C  1 32  ? 27.867  -9.608  -39.816 1.00 13.48 ? 32  LEU C O   1 
ATOM   4619  C  CB  . LEU C  1 32  ? 30.308  -8.096  -39.897 1.00 10.81 ? 32  LEU C CB  1 
ATOM   4620  C  CG  . LEU C  1 32  ? 31.230  -6.915  -39.494 1.00 12.56 ? 32  LEU C CG  1 
ATOM   4621  C  CD1 . LEU C  1 32  ? 32.427  -7.355  -38.707 1.00 12.94 ? 32  LEU C CD1 1 
ATOM   4622  C  CD2 . LEU C  1 32  ? 31.622  -6.094  -40.746 1.00 13.37 ? 32  LEU C CD2 1 
ATOM   4623  N  N   . HIS C  1 33  ? 27.554  -9.044  -41.932 1.00 13.74 ? 33  HIS C N   1 
ATOM   4624  C  CA  . HIS C  1 33  ? 26.572  -10.135 -42.150 1.00 15.37 ? 33  HIS C CA  1 
ATOM   4625  C  C   . HIS C  1 33  ? 26.783  -10.698 -43.520 1.00 15.52 ? 33  HIS C C   1 
ATOM   4626  O  O   . HIS C  1 33  ? 27.298  -10.015 -44.383 1.00 15.11 ? 33  HIS C O   1 
ATOM   4627  C  CB  . HIS C  1 33  ? 25.122  -9.667  -41.911 1.00 16.33 ? 33  HIS C CB  1 
ATOM   4628  C  CG  . HIS C  1 33  ? 24.663  -8.568  -42.797 1.00 17.55 ? 33  HIS C CG  1 
ATOM   4629  N  ND1 . HIS C  1 33  ? 23.968  -8.836  -43.961 1.00 21.14 ? 33  HIS C ND1 1 
ATOM   4630  C  CD2 . HIS C  1 33  ? 24.789  -7.215  -42.719 1.00 18.90 ? 33  HIS C CD2 1 
ATOM   4631  C  CE1 . HIS C  1 33  ? 23.710  -7.699  -44.576 1.00 22.83 ? 33  HIS C CE1 1 
ATOM   4632  N  NE2 . HIS C  1 33  ? 24.210  -6.701  -43.866 1.00 20.14 ? 33  HIS C NE2 1 
ATOM   4633  N  N   . SER C  1 34  ? 26.291  -11.953 -43.741 1.00 16.97 ? 34  SER C N   1 
ATOM   4634  C  CA  . SER C  1 34  ? 26.699  -12.731 -44.951 1.00 18.05 ? 34  SER C CA  1 
ATOM   4635  C  C   . SER C  1 34  ? 26.458  -12.132 -46.238 1.00 18.67 ? 34  SER C C   1 
ATOM   4636  O  O   . SER C  1 34  ? 27.339  -12.241 -47.097 1.00 18.48 ? 34  SER C O   1 
ATOM   4637  C  CB  . SER C  1 34  ? 26.071  -14.168 -44.988 1.00 21.88 ? 34  SER C CB  1 
ATOM   4638  O  OG  . SER C  1 34  ? 26.219  -14.717 -43.716 1.00 31.35 ? 34  SER C OG  1 
ATOM   4639  N  N   . ASP C  1 35  ? 25.342  -11.422 -46.383 1.00 19.91 ? 35  ASP C N   1 
ATOM   4640  C  CA  . ASP C  1 35  ? 24.894  -10.920 -47.711 1.00 24.80 ? 35  ASP C CA  1 
ATOM   4641  C  C   . ASP C  1 35  ? 25.792  -9.848  -48.244 1.00 20.60 ? 35  ASP C C   1 
ATOM   4642  O  O   . ASP C  1 35  ? 25.780  -9.500  -49.444 1.00 22.68 ? 35  ASP C O   1 
ATOM   4643  C  CB  . ASP C  1 35  ? 23.450  -10.352 -47.696 1.00 32.00 ? 35  ASP C CB  1 
ATOM   4644  C  CG  . ASP C  1 35  ? 22.385  -11.403 -47.453 1.00 47.75 ? 35  ASP C CG  1 
ATOM   4645  O  OD1 . ASP C  1 35  ? 22.636  -12.615 -47.670 1.00 50.35 ? 35  ASP C OD1 1 
ATOM   4646  O  OD2 . ASP C  1 35  ? 21.268  -10.996 -47.035 1.00 54.69 ? 35  ASP C OD2 1 
ATOM   4647  N  N   . ILE C  1 36  ? 26.639  -9.273  -47.382 1.00 15.97 ? 36  ILE C N   1 
ATOM   4648  C  CA  . ILE C  1 36  ? 27.519  -8.194  -47.818 1.00 14.96 ? 36  ILE C CA  1 
ATOM   4649  C  C   . ILE C  1 36  ? 28.998  -8.570  -47.779 1.00 13.09 ? 36  ILE C C   1 
ATOM   4650  O  O   . ILE C  1 36  ? 29.842  -7.735  -48.043 1.00 15.99 ? 36  ILE C O   1 
ATOM   4651  C  CB  . ILE C  1 36  ? 27.334  -6.875  -47.058 1.00 15.13 ? 36  ILE C CB  1 
ATOM   4652  C  CG1 . ILE C  1 36  ? 27.496  -7.076  -45.548 1.00 16.55 ? 36  ILE C CG1 1 
ATOM   4653  C  CG2 . ILE C  1 36  ? 25.945  -6.252  -47.417 1.00 16.84 ? 36  ILE C CG2 1 
ATOM   4654  C  CD1 . ILE C  1 36  ? 27.732  -5.749  -44.790 1.00 16.17 ? 36  ILE C CD1 1 
ATOM   4655  N  N   . LEU C  1 37  ? 29.259  -9.810  -47.499 1.00 14.71 ? 37  LEU C N   1 
ATOM   4656  C  CA  . LEU C  1 37  ? 30.673  -10.276 -47.453 1.00 13.52 ? 37  LEU C CA  1 
ATOM   4657  C  C   . LEU C  1 37  ? 31.122  -10.796 -48.792 1.00 15.96 ? 37  LEU C C   1 
ATOM   4658  O  O   . LEU C  1 37  ? 30.314  -11.453 -49.575 1.00 18.14 ? 37  LEU C O   1 
ATOM   4659  C  CB  . LEU C  1 37  ? 30.818  -11.400 -46.446 1.00 14.39 ? 37  LEU C CB  1 
ATOM   4660  C  CG  . LEU C  1 37  ? 30.311  -11.147 -45.063 1.00 14.59 ? 37  LEU C CG  1 
ATOM   4661  C  CD1 . LEU C  1 37  ? 30.619  -12.409 -44.213 1.00 16.86 ? 37  LEU C CD1 1 
ATOM   4662  C  CD2 . LEU C  1 37  ? 31.044  -9.909  -44.477 1.00 15.48 ? 37  LEU C CD2 1 
ATOM   4663  N  N   . GLN C  1 38  ? 32.373  -10.545 -49.139 1.00 13.24 ? 38  GLN C N   1 
ATOM   4664  C  CA  . GLN C  1 38  ? 32.971  -11.111 -50.384 1.00 13.95 ? 38  GLN C CA  1 
ATOM   4665  C  C   . GLN C  1 38  ? 34.387  -11.500 -50.050 1.00 12.47 ? 38  GLN C C   1 
ATOM   4666  O  O   . GLN C  1 38  ? 35.194  -10.649 -49.629 1.00 11.70 ? 38  GLN C O   1 
ATOM   4667  C  CB  . GLN C  1 38  ? 32.954  -10.042 -51.461 1.00 13.75 ? 38  GLN C CB  1 
ATOM   4668  C  CG  . GLN C  1 38  ? 33.359  -10.586 -52.869 1.00 16.35 ? 38  GLN C CG  1 
ATOM   4669  C  CD  . GLN C  1 38  ? 33.110  -9.559  -53.985 1.00 18.64 ? 38  GLN C CD  1 
ATOM   4670  O  OE1 . GLN C  1 38  ? 31.911  -9.424  -54.508 1.00 28.66 ? 38  GLN C OE1 1 
ATOM   4671  N  NE2 . GLN C  1 38  ? 34.046  -8.812  -54.244 1.00 22.00 ? 38  GLN C NE2 1 
ATOM   4672  N  N   . TYR C  1 39  ? 34.774  -12.752 -50.377 1.00 13.27 ? 39  TYR C N   1 
ATOM   4673  C  CA  . TYR C  1 39  ? 36.137  -13.116 -50.285 1.00 11.98 ? 39  TYR C CA  1 
ATOM   4674  C  C   . TYR C  1 39  ? 37.010  -12.308 -51.214 1.00 13.48 ? 39  TYR C C   1 
ATOM   4675  O  O   . TYR C  1 39  ? 36.653  -12.015 -52.366 1.00 14.55 ? 39  TYR C O   1 
ATOM   4676  C  CB  . TYR C  1 39  ? 36.201  -14.668 -50.630 1.00 14.34 ? 39  TYR C CB  1 
ATOM   4677  C  CG  . TYR C  1 39  ? 37.648  -15.101 -50.748 1.00 15.72 ? 39  TYR C CG  1 
ATOM   4678  C  CD1 . TYR C  1 39  ? 38.433  -15.262 -49.615 1.00 16.76 ? 39  TYR C CD1 1 
ATOM   4679  C  CD2 . TYR C  1 39  ? 38.197  -15.387 -52.001 1.00 18.03 ? 39  TYR C CD2 1 
ATOM   4680  C  CE1 . TYR C  1 39  ? 39.754  -15.639 -49.728 1.00 20.54 ? 39  TYR C CE1 1 
ATOM   4681  C  CE2 . TYR C  1 39  ? 39.536  -15.773 -52.125 1.00 21.40 ? 39  TYR C CE2 1 
ATOM   4682  C  CZ  . TYR C  1 39  ? 40.301  -15.907 -50.971 1.00 20.40 ? 39  TYR C CZ  1 
ATOM   4683  O  OH  . TYR C  1 39  ? 41.663  -16.303 -51.105 1.00 21.65 ? 39  TYR C OH  1 
ATOM   4684  N  N   . ASP C  1 40  ? 38.197  -11.922 -50.726 1.00 13.09 ? 40  ASP C N   1 
ATOM   4685  C  CA  . ASP C  1 40  ? 39.178  -11.112 -51.496 1.00 13.69 ? 40  ASP C CA  1 
ATOM   4686  C  C   . ASP C  1 40  ? 40.564  -11.718 -51.249 1.00 14.35 ? 40  ASP C C   1 
ATOM   4687  O  O   . ASP C  1 40  ? 41.133  -11.706 -50.138 1.00 14.49 ? 40  ASP C O   1 
ATOM   4688  C  CB  . ASP C  1 40  ? 39.105  -9.692  -50.935 1.00 15.04 ? 40  ASP C CB  1 
ATOM   4689  C  CG  . ASP C  1 40  ? 40.047  -8.716  -51.599 1.00 17.71 ? 40  ASP C CG  1 
ATOM   4690  O  OD1 . ASP C  1 40  ? 41.011  -9.108  -52.261 1.00 17.25 ? 40  ASP C OD1 1 
ATOM   4691  O  OD2 . ASP C  1 40  ? 39.864  -7.505  -51.289 1.00 19.13 ? 40  ASP C OD2 1 
ATOM   4692  N  N   . ALA C  1 41  ? 41.137  -12.228 -52.341 1.00 14.88 ? 41  ALA C N   1 
ATOM   4693  C  CA  . ALA C  1 41  ? 42.446  -12.920 -52.260 1.00 15.04 ? 41  ALA C CA  1 
ATOM   4694  C  C   . ALA C  1 41  ? 43.574  -12.030 -51.928 1.00 16.16 ? 41  ALA C C   1 
ATOM   4695  O  O   . ALA C  1 41  ? 44.646  -12.489 -51.559 1.00 15.97 ? 41  ALA C O   1 
ATOM   4696  C  CB  . ALA C  1 41  ? 42.690  -13.506 -53.650 1.00 17.82 ? 41  ALA C CB  1 
ATOM   4697  N  N   . SER C  1 42  ? 43.381  -10.714 -51.968 1.00 14.74 ? 42  SER C N   1 
ATOM   4698  C  CA  . SER C  1 42  ? 44.465  -9.766  -51.623 1.00 14.45 ? 42  SER C CA  1 
ATOM   4699  C  C   . SER C  1 42  ? 44.689  -9.743  -50.094 1.00 14.15 ? 42  SER C C   1 
ATOM   4700  O  O   . SER C  1 42  ? 45.682  -9.124  -49.613 1.00 17.05 ? 42  SER C O   1 
ATOM   4701  C  CB  . SER C  1 42  ? 44.160  -8.371  -52.136 1.00 15.86 ? 42  SER C CB  1 
ATOM   4702  O  OG  . SER C  1 42  ? 43.141  -7.719  -51.308 1.00 17.07 ? 42  SER C OG  1 
ATOM   4703  N  N   . LEU C  1 43  ? 43.694  -10.272 -49.329 1.00 13.66 ? 43  LEU C N   1 
ATOM   4704  C  CA  . LEU C  1 43  ? 43.734  -10.144 -47.859 1.00 13.72 ? 43  LEU C CA  1 
ATOM   4705  C  C   . LEU C  1 43  ? 44.607  -11.210 -47.226 1.00 13.91 ? 43  LEU C C   1 
ATOM   4706  O  O   . LEU C  1 43  ? 44.140  -12.168 -46.594 1.00 14.12 ? 43  LEU C O   1 
ATOM   4707  C  CB  . LEU C  1 43  ? 42.298  -10.099 -47.305 1.00 12.17 ? 43  LEU C CB  1 
ATOM   4708  C  CG  . LEU C  1 43  ? 41.479  -8.945  -47.837 1.00 11.71 ? 43  LEU C CG  1 
ATOM   4709  C  CD1 . LEU C  1 43  ? 40.072  -9.066  -47.249 1.00 12.61 ? 43  LEU C CD1 1 
ATOM   4710  C  CD2 . LEU C  1 43  ? 42.088  -7.580  -47.729 1.00 13.30 ? 43  LEU C CD2 1 
ATOM   4711  N  N   . THR C  1 44  ? 45.924  -11.001 -47.429 1.00 15.58 ? 44  THR C N   1 
ATOM   4712  C  CA  . THR C  1 44  ? 46.933  -11.920 -46.921 1.00 16.26 ? 44  THR C CA  1 
ATOM   4713  C  C   . THR C  1 44  ? 47.154  -11.698 -45.412 1.00 18.18 ? 44  THR C C   1 
ATOM   4714  O  O   . THR C  1 44  ? 46.684  -10.693 -44.863 1.00 15.84 ? 44  THR C O   1 
ATOM   4715  C  CB  . THR C  1 44  ? 48.229  -11.707 -47.749 1.00 16.56 ? 44  THR C CB  1 
ATOM   4716  O  OG1 . THR C  1 44  ? 48.516  -10.328 -47.863 1.00 18.98 ? 44  THR C OG1 1 
ATOM   4717  C  CG2 . THR C  1 44  ? 47.979  -12.312 -49.105 1.00 19.41 ? 44  THR C CG2 1 
ATOM   4718  N  N   . PRO C  1 45  ? 47.866  -12.568 -44.705 1.00 16.14 ? 45  PRO C N   1 
ATOM   4719  C  CA  . PRO C  1 45  ? 48.058  -12.393 -43.271 1.00 16.56 ? 45  PRO C CA  1 
ATOM   4720  C  C   . PRO C  1 45  ? 48.872  -11.165 -42.931 1.00 19.57 ? 45  PRO C C   1 
ATOM   4721  O  O   . PRO C  1 45  ? 49.889  -10.918 -43.554 1.00 19.93 ? 45  PRO C O   1 
ATOM   4722  C  CB  . PRO C  1 45  ? 48.815  -13.665 -42.864 1.00 19.01 ? 45  PRO C CB  1 
ATOM   4723  C  CG  . PRO C  1 45  ? 48.404  -14.695 -43.905 1.00 17.29 ? 45  PRO C CG  1 
ATOM   4724  C  CD  . PRO C  1 45  ? 48.296  -13.929 -45.171 1.00 16.93 ? 45  PRO C CD  1 
ATOM   4725  N  N   . LEU C  1 46  ? 48.430  -10.345 -41.948 1.00 14.89 ? 46  LEU C N   1 
ATOM   4726  C  CA  . LEU C  1 46  ? 49.197  -9.213  -41.492 1.00 16.76 ? 46  LEU C CA  1 
ATOM   4727  C  C   . LEU C  1 46  ? 50.332  -9.756  -40.566 1.00 15.97 ? 46  LEU C C   1 
ATOM   4728  O  O   . LEU C  1 46  ? 50.179  -10.798 -39.930 1.00 18.48 ? 46  LEU C O   1 
ATOM   4729  C  CB  . LEU C  1 46  ? 48.290  -8.285  -40.686 1.00 16.22 ? 46  LEU C CB  1 
ATOM   4730  C  CG  . LEU C  1 46  ? 47.202  -7.678  -41.552 1.00 19.25 ? 46  LEU C CG  1 
ATOM   4731  C  CD1 . LEU C  1 46  ? 46.364  -6.731  -40.711 1.00 21.55 ? 46  LEU C CD1 1 
ATOM   4732  C  CD2 . LEU C  1 46  ? 47.729  -6.981  -42.823 1.00 21.44 ? 46  LEU C CD2 1 
ATOM   4733  N  N   . GLU C  1 47  ? 51.382  -8.964  -40.516 1.00 17.49 ? 47  GLU C N   1 
ATOM   4734  C  CA  . GLU C  1 47  ? 52.448  -9.193  -39.501 1.00 20.23 ? 47  GLU C CA  1 
ATOM   4735  C  C   . GLU C  1 47  ? 52.484  -8.059  -38.514 1.00 17.75 ? 47  GLU C C   1 
ATOM   4736  O  O   . GLU C  1 47  ? 52.435  -6.840  -38.903 1.00 17.89 ? 47  GLU C O   1 
ATOM   4737  C  CB  . GLU C  1 47  ? 53.812  -9.337  -40.180 1.00 23.20 ? 47  GLU C CB  1 
ATOM   4738  C  CG  . GLU C  1 47  ? 53.753  -10.335 -41.348 1.00 31.82 ? 47  GLU C CG  1 
ATOM   4739  C  CD  . GLU C  1 47  ? 53.892  -11.801 -40.942 1.00 50.37 ? 47  GLU C CD  1 
ATOM   4740  O  OE1 . GLU C  1 47  ? 54.971  -12.175 -40.384 1.00 62.54 ? 47  GLU C OE1 1 
ATOM   4741  O  OE2 . GLU C  1 47  ? 52.927  -12.591 -41.208 1.00 54.68 ? 47  GLU C OE2 1 
ATOM   4742  N  N   . PHE C  1 48  ? 52.639  -8.432  -37.241 1.00 15.44 ? 48  PHE C N   1 
ATOM   4743  C  CA  . PHE C  1 48  ? 52.616  -7.506  -36.136 1.00 16.50 ? 48  PHE C CA  1 
ATOM   4744  C  C   . PHE C  1 48  ? 54.044  -7.362  -35.651 1.00 16.59 ? 48  PHE C C   1 
ATOM   4745  O  O   . PHE C  1 48  ? 54.565  -8.278  -35.016 1.00 21.64 ? 48  PHE C O   1 
ATOM   4746  C  CB  . PHE C  1 48  ? 51.581  -7.948  -35.036 1.00 15.62 ? 48  PHE C CB  1 
ATOM   4747  C  CG  . PHE C  1 48  ? 50.267  -8.407  -35.668 1.00 15.07 ? 48  PHE C CG  1 
ATOM   4748  C  CD1 . PHE C  1 48  ? 49.446  -7.464  -36.250 1.00 16.27 ? 48  PHE C CD1 1 
ATOM   4749  C  CD2 . PHE C  1 48  ? 49.925  -9.745  -35.760 1.00 15.55 ? 48  PHE C CD2 1 
ATOM   4750  C  CE1 . PHE C  1 48  ? 48.311  -7.854  -36.879 1.00 15.09 ? 48  PHE C CE1 1 
ATOM   4751  C  CE2 . PHE C  1 48  ? 48.761  -10.150 -36.415 1.00 16.59 ? 48  PHE C CE2 1 
ATOM   4752  C  CZ  . PHE C  1 48  ? 47.976  -9.159  -36.965 1.00 15.68 ? 48  PHE C CZ  1 
ATOM   4753  N  N   . GLN C  1 49  ? 54.662  -6.224  -35.932 1.00 15.74 ? 49  GLN C N   1 
ATOM   4754  C  CA  . GLN C  1 49  ? 56.138  -5.983  -35.642 1.00 17.56 ? 49  GLN C CA  1 
ATOM   4755  C  C   . GLN C  1 49  ? 56.315  -5.080  -34.487 1.00 18.67 ? 49  GLN C C   1 
ATOM   4756  O  O   . GLN C  1 49  ? 55.642  -4.076  -34.402 1.00 15.87 ? 49  GLN C O   1 
ATOM   4757  C  CB  . GLN C  1 49  ? 56.786  -5.413  -36.870 1.00 19.34 ? 49  GLN C CB  1 
ATOM   4758  C  CG  . GLN C  1 49  ? 56.694  -6.542  -37.868 1.00 23.49 ? 49  GLN C CG  1 
ATOM   4759  C  CD  . GLN C  1 49  ? 57.410  -6.280  -39.160 1.00 34.31 ? 49  GLN C CD  1 
ATOM   4760  O  OE1 . GLN C  1 49  ? 57.767  -5.136  -39.473 1.00 38.59 ? 49  GLN C OE1 1 
ATOM   4761  N  NE2 . GLN C  1 49  ? 57.638  -7.357  -39.935 1.00 37.00 ? 49  GLN C NE2 1 
ATOM   4762  N  N   . GLY C  1 50  ? 57.268  -5.404  -33.566 1.00 15.33 ? 50  GLY C N   1 
ATOM   4763  C  CA  . GLY C  1 50  ? 57.536  -4.529  -32.478 1.00 17.92 ? 50  GLY C CA  1 
ATOM   4764  C  C   . GLY C  1 50  ? 56.418  -4.537  -31.443 1.00 14.42 ? 50  GLY C C   1 
ATOM   4765  O  O   . GLY C  1 50  ? 56.381  -3.637  -30.570 1.00 17.00 ? 50  GLY C O   1 
ATOM   4766  N  N   . TYR C  1 51  ? 55.557  -5.540  -31.440 1.00 15.38 ? 51  TYR C N   1 
ATOM   4767  C  CA  . TYR C  1 51  ? 54.410  -5.588  -30.499 1.00 16.62 ? 51  TYR C CA  1 
ATOM   4768  C  C   . TYR C  1 51  ? 54.844  -6.101  -29.112 1.00 15.05 ? 51  TYR C C   1 
ATOM   4769  O  O   . TYR C  1 51  ? 54.133  -5.955  -28.138 1.00 15.93 ? 51  TYR C O   1 
ATOM   4770  C  CB  . TYR C  1 51  ? 53.226  -6.520  -30.975 1.00 13.95 ? 51  TYR C CB  1 
ATOM   4771  C  CG  . TYR C  1 51  ? 52.218  -5.835  -31.918 1.00 12.83 ? 51  TYR C CG  1 
ATOM   4772  C  CD1 . TYR C  1 51  ? 52.631  -4.979  -32.958 1.00 12.33 ? 51  TYR C CD1 1 
ATOM   4773  C  CD2 . TYR C  1 51  ? 50.848  -6.096  -31.735 1.00 12.67 ? 51  TYR C CD2 1 
ATOM   4774  C  CE1 . TYR C  1 51  ? 51.713  -4.350  -33.791 1.00 13.61 ? 51  TYR C CE1 1 
ATOM   4775  C  CE2 . TYR C  1 51  ? 49.927  -5.438  -32.554 1.00 13.53 ? 51  TYR C CE2 1 
ATOM   4776  C  CZ  . TYR C  1 51  ? 50.381  -4.649  -33.572 1.00 13.82 ? 51  TYR C CZ  1 
ATOM   4777  O  OH  . TYR C  1 51  ? 49.443  -4.018  -34.333 1.00 15.10 ? 51  TYR C OH  1 
ATOM   4778  N  N   . ASN C  1 52  ? 56.046  -6.732  -29.062 1.00 17.88 ? 52  ASN C N   1 
ATOM   4779  C  CA  . ASN C  1 52  ? 56.466  -7.336  -27.766 1.00 19.09 ? 52  ASN C CA  1 
ATOM   4780  C  C   . ASN C  1 52  ? 57.210  -6.241  -26.998 1.00 21.29 ? 52  ASN C C   1 
ATOM   4781  O  O   . ASN C  1 52  ? 58.407  -6.098  -27.146 1.00 22.98 ? 52  ASN C O   1 
ATOM   4782  C  CB  . ASN C  1 52  ? 57.361  -8.543  -28.078 1.00 19.22 ? 52  ASN C CB  1 
ATOM   4783  C  CG  . ASN C  1 52  ? 57.702  -9.296  -26.828 1.00 24.03 ? 52  ASN C CG  1 
ATOM   4784  O  OD1 . ASN C  1 52  ? 56.959  -9.290  -25.846 1.00 22.91 ? 52  ASN C OD1 1 
ATOM   4785  N  ND2 . ASN C  1 52  ? 58.904  -9.875  -26.814 1.00 29.12 ? 52  ASN C ND2 1 
ATOM   4786  N  N   . LEU C  1 53  ? 56.415  -5.465  -26.250 1.00 19.65 ? 53  LEU C N   1 
ATOM   4787  C  CA  . LEU C  1 53  ? 56.951  -4.319  -25.495 1.00 21.74 ? 53  LEU C CA  1 
ATOM   4788  C  C   . LEU C  1 53  ? 57.547  -4.916  -24.178 1.00 23.61 ? 53  LEU C C   1 
ATOM   4789  O  O   . LEU C  1 53  ? 56.929  -5.743  -23.426 1.00 21.66 ? 53  LEU C O   1 
ATOM   4790  C  CB  . LEU C  1 53  ? 55.873  -3.248  -25.249 1.00 18.91 ? 53  LEU C CB  1 
ATOM   4791  C  CG  . LEU C  1 53  ? 54.897  -2.840  -26.404 1.00 16.75 ? 53  LEU C CG  1 
ATOM   4792  C  CD1 . LEU C  1 53  ? 53.871  -1.909  -25.758 1.00 16.78 ? 53  LEU C CD1 1 
ATOM   4793  C  CD2 . LEU C  1 53  ? 55.575  -2.176  -27.599 1.00 20.10 ? 53  LEU C CD2 1 
ATOM   4794  N  N   . SER C  1 54  ? 58.713  -4.416  -23.866 1.00 25.18 ? 54  SER C N   1 
ATOM   4795  C  CA  . SER C  1 54  ? 59.454  -4.839  -22.626 1.00 29.18 ? 54  SER C CA  1 
ATOM   4796  C  C   . SER C  1 54  ? 58.691  -4.536  -21.356 1.00 31.74 ? 54  SER C C   1 
ATOM   4797  O  O   . SER C  1 54  ? 58.108  -3.445  -21.225 1.00 26.98 ? 54  SER C O   1 
ATOM   4798  C  CB  . SER C  1 54  ? 60.761  -4.115  -22.543 1.00 29.57 ? 54  SER C CB  1 
ATOM   4799  O  OG  . SER C  1 54  ? 61.542  -4.397  -23.714 1.00 39.02 ? 54  SER C OG  1 
ATOM   4800  N  N   . ALA C  1 55  ? 58.759  -5.462  -20.403 1.00 29.64 ? 55  ALA C N   1 
ATOM   4801  C  CA  . ALA C  1 55  ? 58.061  -5.339  -19.063 1.00 30.94 ? 55  ALA C CA  1 
ATOM   4802  C  C   . ALA C  1 55  ? 58.647  -4.206  -18.215 1.00 33.76 ? 55  ALA C C   1 
ATOM   4803  O  O   . ALA C  1 55  ? 57.917  -3.631  -17.326 1.00 29.49 ? 55  ALA C O   1 
ATOM   4804  C  CB  . ALA C  1 55  ? 58.094  -6.657  -18.278 1.00 27.38 ? 55  ALA C CB  1 
ATOM   4805  N  N   . ASN C  1 56  ? 59.910  -3.836  -18.531 1.00 30.83 ? 56  ASN C N   1 
ATOM   4806  C  CA  . ASN C  1 56  ? 60.573  -2.790  -17.745 1.00 33.28 ? 56  ASN C CA  1 
ATOM   4807  C  C   . ASN C  1 56  ? 60.358  -1.394  -18.377 1.00 35.66 ? 56  ASN C C   1 
ATOM   4808  O  O   . ASN C  1 56  ? 60.772  -0.356  -17.805 1.00 29.93 ? 56  ASN C O   1 
ATOM   4809  C  CB  . ASN C  1 56  ? 62.044  -3.197  -17.458 1.00 33.64 ? 56  ASN C CB  1 
ATOM   4810  C  CG  . ASN C  1 56  ? 62.948  -3.093  -18.688 1.00 37.89 ? 56  ASN C CG  1 
ATOM   4811  O  OD1 . ASN C  1 56  ? 62.481  -2.855  -19.854 1.00 37.80 ? 56  ASN C OD1 1 
ATOM   4812  N  ND2 . ASN C  1 56  ? 64.255  -3.224  -18.439 1.00 30.36 ? 56  ASN C ND2 1 
ATOM   4813  N  N   . LYS C  1 57  ? 59.669  -1.365  -19.546 1.00 27.17 ? 57  LYS C N   1 
ATOM   4814  C  CA  . LYS C  1 57  ? 59.135  -0.085  -20.119 1.00 28.56 ? 57  LYS C CA  1 
ATOM   4815  C  C   . LYS C  1 57  ? 57.748  0.123   -19.617 1.00 22.90 ? 57  LYS C C   1 
ATOM   4816  O  O   . LYS C  1 57  ? 57.104  -0.802  -19.020 1.00 22.08 ? 57  LYS C O   1 
ATOM   4817  C  CB  . LYS C  1 57  ? 59.217  -0.044  -21.654 1.00 32.57 ? 57  LYS C CB  1 
ATOM   4818  C  CG  . LYS C  1 57  ? 60.628  0.145   -22.188 1.00 37.84 ? 57  LYS C CG  1 
ATOM   4819  C  CD  . LYS C  1 57  ? 60.623  0.865   -23.542 1.00 43.54 ? 57  LYS C CD  1 
ATOM   4820  C  CE  . LYS C  1 57  ? 60.845  2.391   -23.429 1.00 51.39 ? 57  LYS C CE  1 
ATOM   4821  N  NZ  . LYS C  1 57  ? 61.110  3.162   -24.709 1.00 45.14 ? 57  LYS C NZ  1 
ATOM   4822  N  N   . GLN C  1 58  ? 57.299  1.401   -19.700 1.00 22.94 ? 58  GLN C N   1 
ATOM   4823  C  CA  . GLN C  1 58  ? 55.965  1.705   -19.339 1.00 24.22 ? 58  GLN C CA  1 
ATOM   4824  C  C   . GLN C  1 58  ? 55.373  2.649   -20.390 1.00 18.66 ? 58  GLN C C   1 
ATOM   4825  O  O   . GLN C  1 58  ? 56.048  3.400   -21.092 1.00 20.92 ? 58  GLN C O   1 
ATOM   4826  C  CB  . GLN C  1 58  ? 55.891  2.285   -17.926 1.00 23.65 ? 58  GLN C CB  1 
ATOM   4827  C  CG  . GLN C  1 58  ? 56.581  3.625   -17.825 1.00 23.35 ? 58  GLN C CG  1 
ATOM   4828  C  CD  . GLN C  1 58  ? 56.448  4.246   -16.416 1.00 25.10 ? 58  GLN C CD  1 
ATOM   4829  O  OE1 . GLN C  1 58  ? 55.987  3.557   -15.475 1.00 27.00 ? 58  GLN C OE1 1 
ATOM   4830  N  NE2 . GLN C  1 58  ? 56.695  5.573   -16.302 1.00 23.61 ? 58  GLN C NE2 1 
ATOM   4831  N  N   . PHE C  1 59  ? 54.070  2.566   -20.356 1.00 20.24 ? 59  PHE C N   1 
ATOM   4832  C  CA  . PHE C  1 59  ? 53.207  3.157   -21.369 1.00 18.16 ? 59  PHE C CA  1 
ATOM   4833  C  C   . PHE C  1 59  ? 52.092  3.794   -20.642 1.00 18.20 ? 59  PHE C C   1 
ATOM   4834  O  O   . PHE C  1 59  ? 51.525  3.256   -19.655 1.00 19.03 ? 59  PHE C O   1 
ATOM   4835  C  CB  . PHE C  1 59  ? 52.795  1.982   -22.328 1.00 20.25 ? 59  PHE C CB  1 
ATOM   4836  C  CG  . PHE C  1 59  ? 53.995  1.401   -22.988 1.00 18.69 ? 59  PHE C CG  1 
ATOM   4837  C  CD1 . PHE C  1 59  ? 54.565  2.018   -24.075 1.00 17.35 ? 59  PHE C CD1 1 
ATOM   4838  C  CD2 . PHE C  1 59  ? 54.676  0.295   -22.402 1.00 19.88 ? 59  PHE C CD2 1 
ATOM   4839  C  CE1 . PHE C  1 59  ? 55.751  1.554   -24.622 1.00 19.07 ? 59  PHE C CE1 1 
ATOM   4840  C  CE2 . PHE C  1 59  ? 55.872  -0.142  -22.931 1.00 21.31 ? 59  PHE C CE2 1 
ATOM   4841  C  CZ  . PHE C  1 59  ? 56.397  0.438   -24.039 1.00 18.93 ? 59  PHE C CZ  1 
ATOM   4842  N  N   . LEU C  1 60  ? 51.742  4.999   -21.084 1.00 17.37 ? 60  LEU C N   1 
ATOM   4843  C  CA  . LEU C  1 60  ? 50.821  5.844   -20.380 1.00 16.54 ? 60  LEU C CA  1 
ATOM   4844  C  C   . LEU C  1 60  ? 49.390  5.337   -20.600 1.00 17.80 ? 60  LEU C C   1 
ATOM   4845  O  O   . LEU C  1 60  ? 48.910  5.266   -21.783 1.00 16.76 ? 60  LEU C O   1 
ATOM   4846  C  CB  . LEU C  1 60  ? 50.950  7.258   -20.931 1.00 16.98 ? 60  LEU C CB  1 
ATOM   4847  C  CG  . LEU C  1 60  ? 50.105  8.298   -20.218 1.00 20.11 ? 60  LEU C CG  1 
ATOM   4848  C  CD1 . LEU C  1 60  ? 50.575  8.420   -18.748 1.00 20.66 ? 60  LEU C CD1 1 
ATOM   4849  C  CD2 . LEU C  1 60  ? 50.245  9.612   -20.972 1.00 20.74 ? 60  LEU C CD2 1 
ATOM   4850  N  N   . LEU C  1 61  ? 48.665  5.011   -19.567 1.00 15.70 ? 61  LEU C N   1 
ATOM   4851  C  CA  . LEU C  1 61  ? 47.252  4.743   -19.565 1.00 15.86 ? 61  LEU C CA  1 
ATOM   4852  C  C   . LEU C  1 61  ? 46.478  5.967   -19.175 1.00 17.20 ? 61  LEU C C   1 
ATOM   4853  O  O   . LEU C  1 61  ? 46.831  6.542   -18.137 1.00 20.37 ? 61  LEU C O   1 
ATOM   4854  C  CB  . LEU C  1 61  ? 47.011  3.578   -18.612 1.00 17.69 ? 61  LEU C CB  1 
ATOM   4855  C  CG  . LEU C  1 61  ? 45.637  2.961   -18.584 1.00 18.57 ? 61  LEU C CG  1 
ATOM   4856  C  CD1 . LEU C  1 61  ? 45.569  1.988   -19.763 1.00 21.04 ? 61  LEU C CD1 1 
ATOM   4857  C  CD2 . LEU C  1 61  ? 45.383  2.196   -17.262 1.00 25.12 ? 61  LEU C CD2 1 
ATOM   4858  N  N   . THR C  1 62  ? 45.434  6.373   -19.871 1.00 16.04 ? 62  THR C N   1 
ATOM   4859  C  CA  . THR C  1 62  ? 44.681  7.617   -19.676 1.00 15.39 ? 62  THR C CA  1 
ATOM   4860  C  C   . THR C  1 62  ? 43.217  7.313   -19.683 1.00 20.61 ? 62  THR C C   1 
ATOM   4861  O  O   . THR C  1 62  ? 42.682  6.608   -20.586 1.00 17.87 ? 62  THR C O   1 
ATOM   4862  C  CB  . THR C  1 62  ? 44.828  8.658   -20.836 1.00 19.24 ? 62  THR C CB  1 
ATOM   4863  O  OG1 . THR C  1 62  ? 46.212  8.981   -20.920 1.00 19.26 ? 62  THR C OG1 1 
ATOM   4864  C  CG2 . THR C  1 62  ? 43.973  9.987   -20.547 1.00 20.06 ? 62  THR C CG2 1 
ATOM   4865  N  N   . ASN C  1 63  ? 42.491  7.871   -18.736 1.00 16.88 ? 63  ASN C N   1 
ATOM   4866  C  CA  . ASN C  1 63  ? 41.093  8.014   -18.845 1.00 14.86 ? 63  ASN C CA  1 
ATOM   4867  C  C   . ASN C  1 63  ? 40.850  9.321   -19.477 1.00 19.68 ? 63  ASN C C   1 
ATOM   4868  O  O   . ASN C  1 63  ? 41.010  10.406  -18.850 1.00 20.39 ? 63  ASN C O   1 
ATOM   4869  C  CB  . ASN C  1 63  ? 40.489  7.987   -17.417 1.00 16.45 ? 63  ASN C CB  1 
ATOM   4870  C  CG  . ASN C  1 63  ? 38.958  8.186   -17.396 1.00 18.47 ? 63  ASN C CG  1 
ATOM   4871  O  OD1 . ASN C  1 63  ? 38.389  8.812   -18.310 1.00 16.97 ? 63  ASN C OD1 1 
ATOM   4872  N  ND2 . ASN C  1 63  ? 38.273  7.747   -16.316 1.00 15.65 ? 63  ASN C ND2 1 
ATOM   4873  N  N   . ASN C  1 64  ? 40.464  9.292   -20.753 1.00 20.38 ? 64  ASN C N   1 
ATOM   4874  C  CA  . ASN C  1 64  ? 40.156  10.531  -21.408 1.00 20.45 ? 64  ASN C CA  1 
ATOM   4875  C  C   . ASN C  1 64  ? 38.715  10.980  -21.319 1.00 17.14 ? 64  ASN C C   1 
ATOM   4876  O  O   . ASN C  1 64  ? 38.295  11.889  -22.113 1.00 21.14 ? 64  ASN C O   1 
ATOM   4877  C  CB  . ASN C  1 64  ? 40.671  10.439  -22.870 1.00 18.22 ? 64  ASN C CB  1 
ATOM   4878  C  CG  . ASN C  1 64  ? 39.915  9.435   -23.699 1.00 16.38 ? 64  ASN C CG  1 
ATOM   4879  O  OD1 . ASN C  1 64  ? 38.851  8.951   -23.340 1.00 18.42 ? 64  ASN C OD1 1 
ATOM   4880  N  ND2 . ASN C  1 64  ? 40.491  9.101   -24.842 1.00 20.90 ? 64  ASN C ND2 1 
ATOM   4881  N  N   . GLY C  1 65  ? 37.922  10.392  -20.437 1.00 18.59 ? 65  GLY C N   1 
ATOM   4882  C  CA  . GLY C  1 65  ? 36.517  10.718  -20.351 1.00 19.69 ? 65  GLY C CA  1 
ATOM   4883  C  C   . GLY C  1 65  ? 35.626  10.032  -21.348 1.00 21.48 ? 65  GLY C C   1 
ATOM   4884  O  O   . GLY C  1 65  ? 34.410  10.034  -21.178 1.00 23.24 ? 65  GLY C O   1 
ATOM   4885  N  N   . HIS C  1 66  ? 36.230  9.303   -22.307 1.00 17.79 ? 66  HIS C N   1 
ATOM   4886  C  CA  . HIS C  1 66  ? 35.438  8.587   -23.316 1.00 17.24 ? 66  HIS C CA  1 
ATOM   4887  C  C   . HIS C  1 66  ? 35.776  7.105   -23.309 1.00 14.35 ? 66  HIS C C   1 
ATOM   4888  O  O   . HIS C  1 66  ? 34.948  6.299   -23.734 1.00 18.48 ? 66  HIS C O   1 
ATOM   4889  C  CB  . HIS C  1 66  ? 35.770  9.146   -24.693 1.00 15.12 ? 66  HIS C CB  1 
ATOM   4890  C  CG  . HIS C  1 66  ? 35.490  10.614  -24.779 1.00 15.04 ? 66  HIS C CG  1 
ATOM   4891  N  ND1 . HIS C  1 66  ? 36.485  11.588  -24.941 1.00 16.62 ? 66  HIS C ND1 1 
ATOM   4892  C  CD2 . HIS C  1 66  ? 34.316  11.255  -24.651 1.00 13.78 ? 66  HIS C CD2 1 
ATOM   4893  C  CE1 . HIS C  1 66  ? 35.887  12.759  -24.993 1.00 14.33 ? 66  HIS C CE1 1 
ATOM   4894  N  NE2 . HIS C  1 66  ? 34.577  12.585  -24.791 1.00 17.25 ? 66  HIS C NE2 1 
ATOM   4895  N  N   . SER C  1 67  ? 36.988  6.765   -22.946 1.00 16.33 ? 67  SER C N   1 
ATOM   4896  C  CA  . SER C  1 67  ? 37.449  5.390   -22.896 1.00 13.67 ? 67  SER C CA  1 
ATOM   4897  C  C   . SER C  1 67  ? 38.685  5.386   -21.981 1.00 16.72 ? 67  SER C C   1 
ATOM   4898  O  O   . SER C  1 67  ? 38.987  6.446   -21.382 1.00 18.12 ? 67  SER C O   1 
ATOM   4899  C  CB  . SER C  1 67  ? 37.816  4.874   -24.352 1.00 15.00 ? 67  SER C CB  1 
ATOM   4900  O  OG  . SER C  1 67  ? 38.258  3.545   -24.355 1.00 15.97 ? 67  SER C OG  1 
ATOM   4901  N  N   . VAL C  1 68  ? 39.274  4.224   -21.876 1.00 14.94 ? 68  VAL C N   1 
ATOM   4902  C  CA  . VAL C  1 68  ? 40.585  4.083   -21.302 1.00 14.91 ? 68  VAL C CA  1 
ATOM   4903  C  C   . VAL C  1 68  ? 41.524  3.739   -22.446 1.00 17.42 ? 68  VAL C C   1 
ATOM   4904  O  O   . VAL C  1 68  ? 41.233  2.805   -23.240 1.00 15.92 ? 68  VAL C O   1 
ATOM   4905  C  CB  . VAL C  1 68  ? 40.596  3.054   -20.126 1.00 15.52 ? 68  VAL C CB  1 
ATOM   4906  C  CG1 . VAL C  1 68  ? 40.305  1.619   -20.569 1.00 15.63 ? 68  VAL C CG1 1 
ATOM   4907  C  CG2 . VAL C  1 68  ? 41.976  3.106   -19.469 1.00 17.76 ? 68  VAL C CG2 1 
ATOM   4908  N  N   . LYS C  1 69  ? 42.613  4.505   -22.561 1.00 15.79 ? 69  LYS C N   1 
ATOM   4909  C  CA  . LYS C  1 69  ? 43.528  4.327   -23.707 1.00 15.80 ? 69  LYS C CA  1 
ATOM   4910  C  C   . LYS C  1 69  ? 44.932  4.127   -23.189 1.00 16.27 ? 69  LYS C C   1 
ATOM   4911  O  O   . LYS C  1 69  ? 45.314  4.652   -22.116 1.00 18.50 ? 69  LYS C O   1 
ATOM   4912  C  CB  . LYS C  1 69  ? 43.400  5.507   -24.648 1.00 21.49 ? 69  LYS C CB  1 
ATOM   4913  C  CG  . LYS C  1 69  ? 44.566  6.436   -24.827 1.00 26.22 ? 69  LYS C CG  1 
ATOM   4914  C  CD  . LYS C  1 69  ? 44.136  7.555   -25.740 1.00 23.18 ? 69  LYS C CD  1 
ATOM   4915  C  CE  . LYS C  1 69  ? 44.429  8.868   -25.070 1.00 24.41 ? 69  LYS C CE  1 
ATOM   4916  N  NZ  . LYS C  1 69  ? 44.576  9.961   -26.077 1.00 22.46 ? 69  LYS C NZ  1 
ATOM   4917  N  N   . LEU C  1 70  ? 45.680  3.277   -23.862 1.00 13.40 ? 70  LEU C N   1 
ATOM   4918  C  CA  . LEU C  1 70  ? 47.057  3.044   -23.623 1.00 12.72 ? 70  LEU C CA  1 
ATOM   4919  C  C   . LEU C  1 70  ? 47.873  3.564   -24.764 1.00 14.15 ? 70  LEU C C   1 
ATOM   4920  O  O   . LEU C  1 70  ? 47.701  3.140   -25.959 1.00 14.06 ? 70  LEU C O   1 
ATOM   4921  C  CB  . LEU C  1 70  ? 47.331  1.535   -23.509 1.00 13.51 ? 70  LEU C CB  1 
ATOM   4922  C  CG  . LEU C  1 70  ? 48.728  1.073   -23.110 1.00 14.78 ? 70  LEU C CG  1 
ATOM   4923  C  CD1 . LEU C  1 70  ? 49.061  1.527   -21.666 1.00 15.83 ? 70  LEU C CD1 1 
ATOM   4924  C  CD2 . LEU C  1 70  ? 48.852  -0.461  -23.210 1.00 15.35 ? 70  LEU C CD2 1 
ATOM   4925  N  N   . ASN C  1 71  ? 48.787  4.488   -24.544 1.00 12.30 ? 71  ASN C N   1 
ATOM   4926  C  CA  . ASN C  1 71  ? 49.654  4.989   -25.614 1.00 13.98 ? 71  ASN C CA  1 
ATOM   4927  C  C   . ASN C  1 71  ? 50.623  3.881   -25.999 1.00 14.56 ? 71  ASN C C   1 
ATOM   4928  O  O   . ASN C  1 71  ? 51.064  3.052   -25.168 1.00 15.04 ? 71  ASN C O   1 
ATOM   4929  C  CB  . ASN C  1 71  ? 50.400  6.263   -25.172 1.00 13.46 ? 71  ASN C CB  1 
ATOM   4930  C  CG  . ASN C  1 71  ? 49.494  7.461   -25.069 1.00 17.49 ? 71  ASN C CG  1 
ATOM   4931  O  OD1 . ASN C  1 71  ? 48.286  7.442   -25.397 1.00 19.11 ? 71  ASN C OD1 1 
ATOM   4932  N  ND2 . ASN C  1 71  ? 50.104  8.603   -24.653 1.00 20.96 ? 71  ASN C ND2 1 
ATOM   4933  N  N   . LEU C  1 72  ? 50.909  3.785   -27.314 1.00 12.67 ? 72  LEU C N   1 
ATOM   4934  C  CA  . LEU C  1 72  ? 51.790  2.767   -27.858 1.00 12.82 ? 72  LEU C CA  1 
ATOM   4935  C  C   . LEU C  1 72  ? 52.882  3.411   -28.684 1.00 12.64 ? 72  LEU C C   1 
ATOM   4936  O  O   . LEU C  1 72  ? 52.687  4.543   -29.179 1.00 13.65 ? 72  LEU C O   1 
ATOM   4937  C  CB  . LEU C  1 72  ? 50.955  1.871   -28.855 1.00 12.09 ? 72  LEU C CB  1 
ATOM   4938  C  CG  . LEU C  1 72  ? 49.915  1.035   -28.141 1.00 13.44 ? 72  LEU C CG  1 
ATOM   4939  C  CD1 . LEU C  1 72  ? 48.966  0.352   -29.190 1.00 13.08 ? 72  LEU C CD1 1 
ATOM   4940  C  CD2 . LEU C  1 72  ? 50.479  -0.022  -27.163 1.00 14.26 ? 72  LEU C CD2 1 
ATOM   4941  N  N   . PRO C  1 73  ? 54.057  2.826   -28.745 1.00 14.88 ? 73  PRO C N   1 
ATOM   4942  C  CA  . PRO C  1 73  ? 55.180  3.432   -29.395 1.00 14.09 ? 73  PRO C CA  1 
ATOM   4943  C  C   . PRO C  1 73  ? 55.209  3.264   -30.924 1.00 15.66 ? 73  PRO C C   1 
ATOM   4944  O  O   . PRO C  1 73  ? 54.674  2.274   -31.406 1.00 16.95 ? 73  PRO C O   1 
ATOM   4945  C  CB  . PRO C  1 73  ? 56.380  2.704   -28.754 1.00 15.40 ? 73  PRO C CB  1 
ATOM   4946  C  CG  . PRO C  1 73  ? 55.898  1.262   -28.609 1.00 15.43 ? 73  PRO C CG  1 
ATOM   4947  C  CD  . PRO C  1 73  ? 54.449  1.511   -28.134 1.00 15.36 ? 73  PRO C CD  1 
ATOM   4948  N  N   . SER C  1 74  ? 55.694  4.275   -31.629 1.00 18.24 ? 74  SER C N   1 
ATOM   4949  C  CA  . SER C  1 74  ? 55.627  4.244   -33.101 1.00 18.68 ? 74  SER C CA  1 
ATOM   4950  C  C   . SER C  1 74  ? 56.506  3.203   -33.743 1.00 20.66 ? 74  SER C C   1 
ATOM   4951  O  O   . SER C  1 74  ? 56.380  2.952   -34.977 1.00 22.37 ? 74  SER C O   1 
ATOM   4952  C  CB  . SER C  1 74  ? 55.881  5.640   -33.666 1.00 24.30 ? 74  SER C CB  1 
ATOM   4953  O  OG  . SER C  1 74  ? 57.213  6.027   -33.417 1.00 26.75 ? 74  SER C OG  1 
ATOM   4954  N  N   A ASP C  1 75  ? 57.515  2.703   -33.041 0.50 18.14 ? 75  ASP C N   1 
ATOM   4955  N  N   B ASP C  1 75  ? 57.294  2.470   -32.929 0.50 19.24 ? 75  ASP C N   1 
ATOM   4956  C  CA  A ASP C  1 75  ? 58.255  1.672   -33.686 0.50 16.71 ? 75  ASP C CA  1 
ATOM   4957  C  CA  B ASP C  1 75  ? 58.149  1.340   -33.392 0.50 18.88 ? 75  ASP C CA  1 
ATOM   4958  C  C   A ASP C  1 75  ? 57.353  0.392   -33.867 0.50 17.17 ? 75  ASP C C   1 
ATOM   4959  C  C   B ASP C  1 75  ? 57.373  0.077   -33.602 0.50 17.35 ? 75  ASP C C   1 
ATOM   4960  O  O   A ASP C  1 75  ? 57.715  -0.335  -34.781 0.50 16.70 ? 75  ASP C O   1 
ATOM   4961  O  O   B ASP C  1 75  ? 57.756  -0.976  -34.140 0.50 16.79 ? 75  ASP C O   1 
ATOM   4962  C  CB  A ASP C  1 75  ? 59.638  1.412   -33.023 0.50 16.74 ? 75  ASP C CB  1 
ATOM   4963  C  CB  B ASP C  1 75  ? 59.299  1.112   -32.415 0.50 21.69 ? 75  ASP C CB  1 
ATOM   4964  C  CG  A ASP C  1 75  ? 59.467  0.964   -31.624 0.50 16.32 ? 75  ASP C CG  1 
ATOM   4965  C  CG  B ASP C  1 75  ? 60.324  2.202   -32.522 0.50 22.16 ? 75  ASP C CG  1 
ATOM   4966  O  OD1 A ASP C  1 75  ? 59.110  1.820   -30.807 0.50 19.43 ? 75  ASP C OD1 1 
ATOM   4967  O  OD1 B ASP C  1 75  ? 60.392  2.834   -33.593 0.50 28.30 ? 75  ASP C OD1 1 
ATOM   4968  O  OD2 A ASP C  1 75  ? 59.614  -0.241  -31.400 0.50 19.77 ? 75  ASP C OD2 1 
ATOM   4969  O  OD2 B ASP C  1 75  ? 61.006  2.474   -31.520 0.50 25.54 ? 75  ASP C OD2 1 
ATOM   4970  N  N   . MET C  1 76  ? 56.195  0.201   -33.158 1.00 16.42 ? 76  MET C N   1 
ATOM   4971  C  CA  . MET C  1 76  ? 55.290  -0.923  -33.288 1.00 15.74 ? 76  MET C CA  1 
ATOM   4972  C  C   . MET C  1 76  ? 54.444  -0.749  -34.570 1.00 14.02 ? 76  MET C C   1 
ATOM   4973  O  O   . MET C  1 76  ? 54.007  0.393   -34.799 1.00 16.85 ? 76  MET C O   1 
ATOM   4974  C  CB  . MET C  1 76  ? 54.456  -0.816  -32.055 1.00 20.12 ? 76  MET C CB  1 
ATOM   4975  C  CG  . MET C  1 76  ? 53.367  -1.740  -31.950 1.00 20.51 ? 76  MET C CG  1 
ATOM   4976  S  SD  . MET C  1 76  ? 52.593  -1.652  -30.303 1.00 18.23 ? 76  MET C SD  1 
ATOM   4977  C  CE  . MET C  1 76  ? 51.045  -2.437  -30.754 1.00 16.35 ? 76  MET C CE  1 
ATOM   4978  N  N   . HIS C  1 77  ? 54.406  -1.721  -35.455 1.00 13.81 ? 77  HIS C N   1 
ATOM   4979  C  CA  . HIS C  1 77  ? 53.707  -1.458  -36.755 1.00 15.64 ? 77  HIS C CA  1 
ATOM   4980  C  C   . HIS C  1 77  ? 53.145  -2.671  -37.322 1.00 15.08 ? 77  HIS C C   1 
ATOM   4981  O  O   . HIS C  1 77  ? 53.452  -3.792  -36.953 1.00 14.97 ? 77  HIS C O   1 
ATOM   4982  C  CB  . HIS C  1 77  ? 54.542  -0.625  -37.732 1.00 19.37 ? 77  HIS C CB  1 
ATOM   4983  C  CG  . HIS C  1 77  ? 55.791  -1.316  -38.083 1.00 19.03 ? 77  HIS C CG  1 
ATOM   4984  N  ND1 . HIS C  1 77  ? 57.000  -1.069  -37.477 1.00 23.52 ? 77  HIS C ND1 1 
ATOM   4985  C  CD2 . HIS C  1 77  ? 56.015  -2.272  -38.994 1.00 22.79 ? 77  HIS C CD2 1 
ATOM   4986  C  CE1 . HIS C  1 77  ? 57.919  -1.844  -37.996 1.00 21.32 ? 77  HIS C CE1 1 
ATOM   4987  N  NE2 . HIS C  1 77  ? 57.361  -2.585  -38.941 1.00 27.28 ? 77  HIS C NE2 1 
ATOM   4988  N  N   . ILE C  1 78  ? 52.205  -2.428  -38.227 1.00 14.72 ? 78  ILE C N   1 
ATOM   4989  C  CA  . ILE C  1 78  ? 51.660  -3.497  -39.043 1.00 14.85 ? 78  ILE C CA  1 
ATOM   4990  C  C   . ILE C  1 78  ? 52.402  -3.549  -40.377 1.00 15.18 ? 78  ILE C C   1 
ATOM   4991  O  O   . ILE C  1 78  ? 52.662  -2.511  -40.954 1.00 18.06 ? 78  ILE C O   1 
ATOM   4992  C  CB  . ILE C  1 78  ? 50.126  -3.184  -39.379 1.00 15.42 ? 78  ILE C CB  1 
ATOM   4993  C  CG1 . ILE C  1 78  ? 49.218  -3.157  -38.150 1.00 15.94 ? 78  ILE C CG1 1 
ATOM   4994  C  CG2 . ILE C  1 78  ? 49.542  -4.221  -40.356 1.00 17.68 ? 78  ILE C CG2 1 
ATOM   4995  C  CD1 . ILE C  1 78  ? 47.851  -2.447  -38.409 1.00 15.50 ? 78  ILE C CD1 1 
ATOM   4996  N  N   . GLN C  1 79  ? 52.787  -4.775  -40.763 1.00 16.77 ? 79  GLN C N   1 
ATOM   4997  C  CA  . GLN C  1 79  ? 53.411  -5.051  -42.018 1.00 22.20 ? 79  GLN C CA  1 
ATOM   4998  C  C   . GLN C  1 79  ? 52.380  -5.889  -42.798 1.00 18.85 ? 79  GLN C C   1 
ATOM   4999  O  O   . GLN C  1 79  ? 51.746  -6.813  -42.266 1.00 19.19 ? 79  GLN C O   1 
ATOM   5000  C  CB  . GLN C  1 79  ? 54.720  -5.857  -41.701 1.00 24.00 ? 79  GLN C CB  1 
ATOM   5001  C  CG  . GLN C  1 79  ? 55.340  -6.693  -42.820 1.00 33.95 ? 79  GLN C CG  1 
ATOM   5002  C  CD  . GLN C  1 79  ? 55.614  -5.893  -44.075 1.00 43.78 ? 79  GLN C CD  1 
ATOM   5003  O  OE1 . GLN C  1 79  ? 55.873  -4.673  -44.033 1.00 43.54 ? 79  GLN C OE1 1 
ATOM   5004  N  NE2 . GLN C  1 79  ? 55.507  -6.574  -45.233 1.00 49.83 ? 79  GLN C NE2 1 
ATOM   5005  N  N   . GLY C  1 80  ? 52.243  -5.558  -44.076 1.00 19.06 ? 80  GLY C N   1 
ATOM   5006  C  CA  . GLY C  1 80  ? 51.363  -6.339  -44.964 1.00 20.71 ? 80  GLY C CA  1 
ATOM   5007  C  C   . GLY C  1 80  ? 50.394  -5.460  -45.686 1.00 21.65 ? 80  GLY C C   1 
ATOM   5008  O  O   . GLY C  1 80  ? 49.716  -5.922  -46.617 1.00 24.46 ? 80  GLY C O   1 
ATOM   5009  N  N   . LEU C  1 81  ? 50.236  -4.208  -45.261 1.00 20.14 ? 81  LEU C N   1 
ATOM   5010  C  CA  . LEU C  1 81  ? 49.314  -3.264  -45.879 1.00 19.78 ? 81  LEU C CA  1 
ATOM   5011  C  C   . LEU C  1 81  ? 50.029  -2.457  -46.983 1.00 21.68 ? 81  LEU C C   1 
ATOM   5012  O  O   . LEU C  1 81  ? 51.231  -2.642  -47.134 1.00 25.02 ? 81  LEU C O   1 
ATOM   5013  C  CB  . LEU C  1 81  ? 48.654  -2.309  -44.861 1.00 19.48 ? 81  LEU C CB  1 
ATOM   5014  C  CG  . LEU C  1 81  ? 47.699  -3.026  -43.905 1.00 17.56 ? 81  LEU C CG  1 
ATOM   5015  C  CD1 . LEU C  1 81  ? 47.340  -2.093  -42.771 1.00 17.29 ? 81  LEU C CD1 1 
ATOM   5016  C  CD2 . LEU C  1 81  ? 46.414  -3.517  -44.591 1.00 18.50 ? 81  LEU C CD2 1 
ATOM   5017  N  N   . GLN C  1 82  ? 49.320  -1.555  -47.664 1.00 24.12 ? 82  GLN C N   1 
ATOM   5018  C  CA  . GLN C  1 82  ? 49.972  -0.841  -48.782 1.00 25.46 ? 82  GLN C CA  1 
ATOM   5019  C  C   . GLN C  1 82  ? 51.012  0.177   -48.331 1.00 23.42 ? 82  GLN C C   1 
ATOM   5020  O  O   . GLN C  1 82  ? 51.852  0.587   -49.114 1.00 25.27 ? 82  GLN C O   1 
ATOM   5021  C  CB  . GLN C  1 82  ? 48.956  -0.159  -49.737 1.00 35.76 ? 82  GLN C CB  1 
ATOM   5022  C  CG  . GLN C  1 82  ? 48.528  -0.959  -50.991 1.00 45.55 ? 82  GLN C CG  1 
ATOM   5023  C  CD  . GLN C  1 82  ? 49.568  -0.988  -52.139 1.00 51.66 ? 82  GLN C CD  1 
ATOM   5024  O  OE1 . GLN C  1 82  ? 49.853  0.051   -52.819 1.00 46.19 ? 82  GLN C OE1 1 
ATOM   5025  N  NE2 . GLN C  1 82  ? 50.143  -2.190  -52.369 1.00 41.62 ? 82  GLN C NE2 1 
ATOM   5026  N  N   . SER C  1 83  ? 50.930  0.629   -47.068 1.00 17.95 ? 83  SER C N   1 
ATOM   5027  C  CA  . SER C  1 83  ? 51.857  1.568   -46.413 1.00 16.02 ? 83  SER C CA  1 
ATOM   5028  C  C   . SER C  1 83  ? 52.134  0.919   -45.076 1.00 16.37 ? 83  SER C C   1 
ATOM   5029  O  O   . SER C  1 83  ? 51.368  0.087   -44.587 1.00 14.27 ? 83  SER C O   1 
ATOM   5030  C  CB  . SER C  1 83  ? 51.228  2.925   -46.139 1.00 19.04 ? 83  SER C CB  1 
ATOM   5031  O  OG  . SER C  1 83  ? 50.915  3.654   -47.341 1.00 20.28 ? 83  SER C OG  1 
ATOM   5032  N  N   . ARG C  1 84  ? 53.215  1.344   -44.412 1.00 14.50 ? 84  ARG C N   1 
ATOM   5033  C  CA  . ARG C  1 84  ? 53.397  1.024   -42.977 1.00 13.11 ? 84  ARG C CA  1 
ATOM   5034  C  C   . ARG C  1 84  ? 52.457  1.862   -42.190 1.00 11.41 ? 84  ARG C C   1 
ATOM   5035  O  O   . ARG C  1 84  ? 52.380  3.056   -42.353 1.00 12.74 ? 84  ARG C O   1 
ATOM   5036  C  CB  . ARG C  1 84  ? 54.847  1.406   -42.596 1.00 15.06 ? 84  ARG C CB  1 
ATOM   5037  C  CG  . ARG C  1 84  ? 55.074  1.108   -41.090 1.00 15.71 ? 84  ARG C CG  1 
ATOM   5038  C  CD  . ARG C  1 84  ? 56.514  1.297   -40.637 1.00 15.52 ? 84  ARG C CD  1 
ATOM   5039  N  NE  . ARG C  1 84  ? 57.331  0.223   -41.144 1.00 17.02 ? 84  ARG C NE  1 
ATOM   5040  C  CZ  . ARG C  1 84  ? 58.657  0.158   -40.838 1.00 18.99 ? 84  ARG C CZ  1 
ATOM   5041  N  NH1 . ARG C  1 84  ? 59.179  1.142   -40.132 1.00 20.48 ? 84  ARG C NH1 1 
ATOM   5042  N  NH2 . ARG C  1 84  ? 59.356  -0.880  -41.279 1.00 19.42 ? 84  ARG C NH2 1 
ATOM   5043  N  N   . TYR C  1 85  ? 51.794  1.170   -41.241 1.00 11.43 ? 85  TYR C N   1 
ATOM   5044  C  CA  . TYR C  1 85  ? 50.977  1.824   -40.250 1.00 11.06 ? 85  TYR C CA  1 
ATOM   5045  C  C   . TYR C  1 85  ? 51.596  1.549   -38.901 1.00 11.91 ? 85  TYR C C   1 
ATOM   5046  O  O   . TYR C  1 85  ? 51.805  0.396   -38.543 1.00 12.79 ? 85  TYR C O   1 
ATOM   5047  C  CB  . TYR C  1 85  ? 49.523  1.244   -40.303 1.00 12.74 ? 85  TYR C CB  1 
ATOM   5048  C  CG  . TYR C  1 85  ? 48.778  1.807   -41.492 1.00 11.45 ? 85  TYR C CG  1 
ATOM   5049  C  CD1 . TYR C  1 85  ? 47.996  2.959   -41.337 1.00 10.94 ? 85  TYR C CD1 1 
ATOM   5050  C  CD2 . TYR C  1 85  ? 48.839  1.145   -42.724 1.00 13.83 ? 85  TYR C CD2 1 
ATOM   5051  C  CE1 . TYR C  1 85  ? 47.278  3.439   -42.437 1.00 11.42 ? 85  TYR C CE1 1 
ATOM   5052  C  CE2 . TYR C  1 85  ? 48.129  1.680   -43.820 1.00 12.52 ? 85  TYR C CE2 1 
ATOM   5053  C  CZ  . TYR C  1 85  ? 47.398  2.792   -43.656 1.00 12.35 ? 85  TYR C CZ  1 
ATOM   5054  O  OH  . TYR C  1 85  ? 46.653  3.286   -44.765 1.00 15.56 ? 85  TYR C OH  1 
ATOM   5055  N  N   . SER C  1 86  ? 51.982  2.645   -38.234 1.00 11.87 ? 86  SER C N   1 
ATOM   5056  C  CA  . SER C  1 86  ? 52.625  2.624   -36.923 1.00 11.42 ? 86  SER C CA  1 
ATOM   5057  C  C   . SER C  1 86  ? 51.619  2.858   -35.789 1.00 12.16 ? 86  SER C C   1 
ATOM   5058  O  O   . SER C  1 86  ? 50.694  3.689   -35.866 1.00 13.01 ? 86  SER C O   1 
ATOM   5059  C  CB  . SER C  1 86  ? 53.767  3.652   -36.848 1.00 14.66 ? 86  SER C CB  1 
ATOM   5060  O  OG  . SER C  1 86  ? 54.730  3.358   -37.851 1.00 14.88 ? 86  SER C OG  1 
ATOM   5061  N  N   . ALA C  1 87  ? 51.823  2.132   -34.703 1.00 12.18 ? 87  ALA C N   1 
ATOM   5062  C  CA  . ALA C  1 87  ? 50.895  2.235   -33.591 1.00 11.93 ? 87  ALA C CA  1 
ATOM   5063  C  C   . ALA C  1 87  ? 50.882  3.605   -32.925 1.00 11.58 ? 87  ALA C C   1 
ATOM   5064  O  O   . ALA C  1 87  ? 51.926  4.321   -32.909 1.00 12.37 ? 87  ALA C O   1 
ATOM   5065  C  CB  . ALA C  1 87  ? 51.203  1.195   -32.575 1.00 12.67 ? 87  ALA C CB  1 
ATOM   5066  N  N   . THR C  1 88  ? 49.720  3.985   -32.379 1.00 11.12 ? 88  THR C N   1 
ATOM   5067  C  CA  . THR C  1 88  ? 49.599  5.240   -31.591 1.00 11.26 ? 88  THR C CA  1 
ATOM   5068  C  C   . THR C  1 88  ? 48.963  4.956   -30.245 1.00 12.89 ? 88  THR C C   1 
ATOM   5069  O  O   . THR C  1 88  ? 49.429  5.520   -29.235 1.00 12.73 ? 88  THR C O   1 
ATOM   5070  C  CB  . THR C  1 88  ? 48.987  6.380   -32.385 1.00 10.63 ? 88  THR C CB  1 
ATOM   5071  O  OG1 . THR C  1 88  ? 48.891  7.508   -31.538 1.00 13.33 ? 88  THR C OG1 1 
ATOM   5072  C  CG2 . THR C  1 88  ? 47.636  6.059   -32.937 1.00 11.92 ? 88  THR C CG2 1 
ATOM   5073  N  N   . GLN C  1 89  ? 47.885  4.149   -30.169 1.00 11.07 ? 89  GLN C N   1 
ATOM   5074  C  CA  . GLN C  1 89  ? 47.207  3.907   -28.890 1.00 11.55 ? 89  GLN C CA  1 
ATOM   5075  C  C   . GLN C  1 89  ? 46.278  2.731   -29.077 1.00 11.60 ? 89  GLN C C   1 
ATOM   5076  O  O   . GLN C  1 89  ? 45.881  2.429   -30.241 1.00 10.93 ? 89  GLN C O   1 
ATOM   5077  C  CB  . GLN C  1 89  ? 46.492  5.132   -28.366 1.00 12.50 ? 89  GLN C CB  1 
ATOM   5078  C  CG  . GLN C  1 89  ? 45.555  5.776   -29.363 1.00 14.64 ? 89  GLN C CG  1 
ATOM   5079  C  CD  . GLN C  1 89  ? 44.076  5.483   -29.110 1.00 13.79 ? 89  GLN C CD  1 
ATOM   5080  O  OE1 . GLN C  1 89  ? 43.266  6.380   -29.285 1.00 23.35 ? 89  GLN C OE1 1 
ATOM   5081  N  NE2 . GLN C  1 89  ? 43.731  4.333   -28.780 1.00 12.43 ? 89  GLN C NE2 1 
ATOM   5082  N  N   . LEU C  1 90  ? 45.915  2.103   -27.980 1.00 10.76 ? 90  LEU C N   1 
ATOM   5083  C  CA  . LEU C  1 90  ? 44.797  1.208   -27.980 1.00 10.84 ? 90  LEU C CA  1 
ATOM   5084  C  C   . LEU C  1 90  ? 43.775  1.643   -27.026 1.00 11.64 ? 90  LEU C C   1 
ATOM   5085  O  O   . LEU C  1 90  ? 44.100  2.361   -26.052 1.00 12.60 ? 90  LEU C O   1 
ATOM   5086  C  CB  . LEU C  1 90  ? 45.212  -0.258  -27.872 1.00 11.10 ? 90  LEU C CB  1 
ATOM   5087  C  CG  . LEU C  1 90  ? 45.949  -0.663  -26.533 1.00 12.06 ? 90  LEU C CG  1 
ATOM   5088  C  CD1 . LEU C  1 90  ? 45.020  -0.792  -25.347 1.00 12.55 ? 90  LEU C CD1 1 
ATOM   5089  C  CD2 . LEU C  1 90  ? 46.545  -1.995  -26.841 1.00 13.49 ? 90  LEU C CD2 1 
ATOM   5090  N  N   . HIS C  1 91  ? 42.530  1.179   -27.178 1.00 10.74 ? 91  HIS C N   1 
ATOM   5091  C  CA  . HIS C  1 91  ? 41.464  1.511   -26.246 1.00 10.13 ? 91  HIS C CA  1 
ATOM   5092  C  C   . HIS C  1 91  ? 40.294  0.535   -26.395 1.00 9.79  ? 91  HIS C C   1 
ATOM   5093  O  O   . HIS C  1 91  ? 40.338  -0.332  -27.252 1.00 11.09 ? 91  HIS C O   1 
ATOM   5094  C  CB  . HIS C  1 91  ? 41.044  2.956   -26.420 1.00 10.14 ? 91  HIS C CB  1 
ATOM   5095  C  CG  . HIS C  1 91  ? 40.429  3.155   -27.788 1.00 10.66 ? 91  HIS C CG  1 
ATOM   5096  N  ND1 . HIS C  1 91  ? 41.137  3.583   -28.876 1.00 10.98 ? 91  HIS C ND1 1 
ATOM   5097  C  CD2 . HIS C  1 91  ? 39.168  2.845   -28.210 1.00 10.45 ? 91  HIS C CD2 1 
ATOM   5098  C  CE1 . HIS C  1 91  ? 40.324  3.522   -29.956 1.00 9.62  ? 91  HIS C CE1 1 
ATOM   5099  N  NE2 . HIS C  1 91  ? 39.147  3.060   -29.593 1.00 8.89  ? 91  HIS C NE2 1 
ATOM   5100  N  N   . LEU C  1 92  ? 39.298  0.661   -25.514 1.00 11.21 ? 92  LEU C N   1 
ATOM   5101  C  CA  . LEU C  1 92  ? 38.157  -0.236  -25.532 1.00 11.96 ? 92  LEU C CA  1 
ATOM   5102  C  C   . LEU C  1 92  ? 36.834  0.447   -25.560 1.00 8.97  ? 92  LEU C C   1 
ATOM   5103  O  O   . LEU C  1 92  ? 36.689  1.623   -25.260 1.00 11.54 ? 92  LEU C O   1 
ATOM   5104  C  CB  . LEU C  1 92  ? 38.238  -1.248  -24.270 1.00 13.00 ? 92  LEU C CB  1 
ATOM   5105  C  CG  . LEU C  1 92  ? 39.473  -2.137  -24.326 1.00 13.78 ? 92  LEU C CG  1 
ATOM   5106  C  CD1 . LEU C  1 92  ? 40.519  -1.569  -23.326 1.00 19.70 ? 92  LEU C CD1 1 
ATOM   5107  C  CD2 . LEU C  1 92  ? 39.158  -3.539  -24.026 1.00 15.88 ? 92  LEU C CD2 1 
ATOM   5108  N  N   . HIS C  1 93  ? 35.845  -0.366  -25.944 1.00 10.22 ? 93  HIS C N   1 
ATOM   5109  C  CA  . HIS C  1 93  ? 34.432  0.012   -25.913 1.00 10.49 ? 93  HIS C CA  1 
ATOM   5110  C  C   . HIS C  1 93  ? 33.644  -1.116  -25.233 1.00 10.54 ? 93  HIS C C   1 
ATOM   5111  O  O   . HIS C  1 93  ? 33.894  -2.293  -25.459 1.00 10.71 ? 93  HIS C O   1 
ATOM   5112  C  CB  . HIS C  1 93  ? 33.933  0.182   -27.370 1.00 10.09 ? 93  HIS C CB  1 
ATOM   5113  C  CG  . HIS C  1 93  ? 34.692  1.229   -28.147 1.00 8.57  ? 93  HIS C CG  1 
ATOM   5114  N  ND1 . HIS C  1 93  ? 34.334  2.564   -28.191 1.00 9.82  ? 93  HIS C ND1 1 
ATOM   5115  C  CD2 . HIS C  1 93  ? 35.798  1.095   -28.941 1.00 9.39  ? 93  HIS C CD2 1 
ATOM   5116  C  CE1 . HIS C  1 93  ? 35.221  3.208   -28.957 1.00 8.72  ? 93  HIS C CE1 1 
ATOM   5117  N  NE2 . HIS C  1 93  ? 36.093  2.345   -29.417 1.00 9.20  ? 93  HIS C NE2 1 
ATOM   5118  N  N   . TRP C  1 94  ? 32.652  -0.725  -24.402 1.00 10.88 ? 94  TRP C N   1 
ATOM   5119  C  CA  . TRP C  1 94  ? 31.907  -1.733  -23.635 1.00 11.15 ? 94  TRP C CA  1 
ATOM   5120  C  C   . TRP C  1 94  ? 30.477  -1.198  -23.408 1.00 10.66 ? 94  TRP C C   1 
ATOM   5121  O  O   . TRP C  1 94  ? 30.175  -0.012  -23.633 1.00 11.26 ? 94  TRP C O   1 
ATOM   5122  C  CB  . TRP C  1 94  ? 32.644  -2.114  -22.319 1.00 12.32 ? 94  TRP C CB  1 
ATOM   5123  C  CG  . TRP C  1 94  ? 32.931  -0.922  -21.414 1.00 12.83 ? 94  TRP C CG  1 
ATOM   5124  C  CD1 . TRP C  1 94  ? 32.104  -0.434  -20.496 1.00 12.93 ? 94  TRP C CD1 1 
ATOM   5125  C  CD2 . TRP C  1 94  ? 34.124  -0.138  -21.374 1.00 11.30 ? 94  TRP C CD2 1 
ATOM   5126  N  NE1 . TRP C  1 94  ? 32.675  0.666   -19.837 1.00 12.37 ? 94  TRP C NE1 1 
ATOM   5127  C  CE2 . TRP C  1 94  ? 33.924  0.890   -20.359 1.00 12.74 ? 94  TRP C CE2 1 
ATOM   5128  C  CE3 . TRP C  1 94  ? 35.276  -0.075  -22.180 1.00 11.48 ? 94  TRP C CE3 1 
ATOM   5129  C  CZ2 . TRP C  1 94  ? 34.884  1.888   -20.069 1.00 13.67 ? 94  TRP C CZ2 1 
ATOM   5130  C  CZ3 . TRP C  1 94  ? 36.270  0.893   -21.837 1.00 12.47 ? 94  TRP C CZ3 1 
ATOM   5131  C  CH2 . TRP C  1 94  ? 36.032  1.889   -20.809 1.00 14.08 ? 94  TRP C CH2 1 
ATOM   5132  N  N   . GLY C  1 95  ? 29.707  -2.084  -22.776 1.00 11.49 ? 95  GLY C N   1 
ATOM   5133  C  CA  . GLY C  1 95  ? 28.307  -1.778  -22.427 1.00 13.03 ? 95  GLY C CA  1 
ATOM   5134  C  C   . GLY C  1 95  ? 28.112  -1.428  -20.953 1.00 13.88 ? 95  GLY C C   1 
ATOM   5135  O  O   . GLY C  1 95  ? 28.770  -0.549  -20.428 1.00 13.45 ? 95  GLY C O   1 
ATOM   5136  N  N   . ASN C  1 96  ? 27.221  -2.207  -20.317 1.00 15.76 ? 96  ASN C N   1 
ATOM   5137  C  CA  . ASN C  1 96  ? 27.009  -1.935  -18.870 1.00 15.44 ? 96  ASN C CA  1 
ATOM   5138  C  C   . ASN C  1 96  ? 26.601  -3.249  -18.255 1.00 15.68 ? 96  ASN C C   1 
ATOM   5139  O  O   . ASN C  1 96  ? 26.199  -4.170  -18.917 1.00 16.61 ? 96  ASN C O   1 
ATOM   5140  C  CB  . ASN C  1 96  ? 25.983  -0.857  -18.653 1.00 17.73 ? 96  ASN C CB  1 
ATOM   5141  C  CG  . ASN C  1 96  ? 24.580  -1.287  -18.994 1.00 23.60 ? 96  ASN C CG  1 
ATOM   5142  O  OD1 . ASN C  1 96  ? 23.819  -1.727  -18.089 1.00 23.94 ? 96  ASN C OD1 1 
ATOM   5143  N  ND2 . ASN C  1 96  ? 24.182  -1.075  -20.223 1.00 26.47 ? 96  ASN C ND2 1 
ATOM   5144  N  N   . PRO C  1 97  ? 26.575  -3.333  -16.916 1.00 18.47 ? 97  PRO C N   1 
ATOM   5145  C  CA  . PRO C  1 97  ? 26.292  -4.688  -16.367 1.00 17.82 ? 97  PRO C CA  1 
ATOM   5146  C  C   . PRO C  1 97  ? 24.866  -5.204  -16.539 1.00 18.81 ? 97  PRO C C   1 
ATOM   5147  O  O   . PRO C  1 97  ? 24.662  -6.378  -16.565 1.00 18.53 ? 97  PRO C O   1 
ATOM   5148  C  CB  . PRO C  1 97  ? 26.490  -4.495  -14.848 1.00 18.34 ? 97  PRO C CB  1 
ATOM   5149  C  CG  . PRO C  1 97  ? 27.389  -3.311  -14.753 1.00 19.09 ? 97  PRO C CG  1 
ATOM   5150  C  CD  . PRO C  1 97  ? 27.075  -2.379  -15.895 1.00 19.82 ? 97  PRO C CD  1 
ATOM   5151  N  N   . ASN C  1 98  ? 23.927  -4.328  -16.742 1.00 17.17 ? 98  ASN C N   1 
ATOM   5152  C  CA  . ASN C  1 98  ? 22.553  -4.758  -17.135 1.00 21.91 ? 98  ASN C CA  1 
ATOM   5153  C  C   . ASN C  1 98  ? 22.376  -5.149  -18.598 1.00 21.03 ? 98  ASN C C   1 
ATOM   5154  O  O   . ASN C  1 98  ? 21.345  -5.731  -18.959 1.00 22.70 ? 98  ASN C O   1 
ATOM   5155  C  CB  . ASN C  1 98  ? 21.532  -3.660  -16.850 1.00 21.71 ? 98  ASN C CB  1 
ATOM   5156  C  CG  . ASN C  1 98  ? 21.378  -3.393  -15.370 1.00 31.15 ? 98  ASN C CG  1 
ATOM   5157  O  OD1 . ASN C  1 98  ? 21.268  -4.325  -14.601 1.00 32.24 ? 98  ASN C OD1 1 
ATOM   5158  N  ND2 . ASN C  1 98  ? 21.422  -2.134  -14.981 1.00 33.56 ? 98  ASN C ND2 1 
ATOM   5159  N  N   . ASP C  1 99  ? 23.310  -4.783  -19.482 1.00 18.60 ? 99  ASP C N   1 
ATOM   5160  C  CA  . ASP C  1 99  ? 23.143  -5.075  -20.939 1.00 15.49 ? 99  ASP C CA  1 
ATOM   5161  C  C   . ASP C  1 99  ? 24.618  -5.153  -21.415 1.00 15.35 ? 99  ASP C C   1 
ATOM   5162  O  O   . ASP C  1 99  ? 25.150  -4.189  -21.998 1.00 15.69 ? 99  ASP C O   1 
ATOM   5163  C  CB  . ASP C  1 99  ? 22.349  -3.938  -21.625 1.00 15.87 ? 99  ASP C CB  1 
ATOM   5164  C  CG  . ASP C  1 99  ? 21.823  -4.336  -23.008 1.00 17.02 ? 99  ASP C CG  1 
ATOM   5165  O  OD1 . ASP C  1 99  ? 22.003  -5.509  -23.332 1.00 19.73 ? 99  ASP C OD1 1 
ATOM   5166  O  OD2 . ASP C  1 99  ? 21.475  -3.453  -23.775 1.00 22.24 ? 99  ASP C OD2 1 
ATOM   5167  N  N   . PRO C  1 100 ? 25.258  -6.280  -21.134 1.00 14.40 ? 100 PRO C N   1 
ATOM   5168  C  CA  . PRO C  1 100 ? 26.745  -6.352  -21.264 1.00 13.96 ? 100 PRO C CA  1 
ATOM   5169  C  C   . PRO C  1 100 ? 27.082  -6.758  -22.689 1.00 13.55 ? 100 PRO C C   1 
ATOM   5170  O  O   . PRO C  1 100 ? 27.731  -7.738  -22.965 1.00 14.78 ? 100 PRO C O   1 
ATOM   5171  C  CB  . PRO C  1 100 ? 27.159  -7.432  -20.219 1.00 15.34 ? 100 PRO C CB  1 
ATOM   5172  C  CG  . PRO C  1 100 ? 25.955  -8.353  -20.160 1.00 16.05 ? 100 PRO C CG  1 
ATOM   5173  C  CD  . PRO C  1 100 ? 24.792  -7.425  -20.261 1.00 15.82 ? 100 PRO C CD  1 
ATOM   5174  N  N   . HIS C  1 101 ? 26.681  -5.856  -23.611 1.00 12.98 ? 101 HIS C N   1 
ATOM   5175  C  CA  . HIS C  1 101 ? 26.833  -6.172  -25.066 1.00 13.56 ? 101 HIS C CA  1 
ATOM   5176  C  C   . HIS C  1 101 ? 27.210  -4.870  -25.742 1.00 14.93 ? 101 HIS C C   1 
ATOM   5177  O  O   . HIS C  1 101 ? 26.441  -4.374  -26.553 1.00 17.71 ? 101 HIS C O   1 
ATOM   5178  C  CB  . HIS C  1 101 ? 25.508  -6.713  -25.653 1.00 15.55 ? 101 HIS C CB  1 
ATOM   5179  C  CG  . HIS C  1 101 ? 24.954  -7.844  -24.869 1.00 15.46 ? 101 HIS C CG  1 
ATOM   5180  N  ND1 . HIS C  1 101 ? 25.534  -9.102  -24.869 1.00 16.56 ? 101 HIS C ND1 1 
ATOM   5181  C  CD2 . HIS C  1 101 ? 23.969  -7.869  -23.914 1.00 15.37 ? 101 HIS C CD2 1 
ATOM   5182  C  CE1 . HIS C  1 101 ? 24.873  -9.886  -24.017 1.00 18.71 ? 101 HIS C CE1 1 
ATOM   5183  N  NE2 . HIS C  1 101 ? 23.927  -9.161  -23.439 1.00 17.25 ? 101 HIS C NE2 1 
ATOM   5184  N  N   . GLY C  1 102 ? 28.465  -4.418  -25.555 1.00 12.23 ? 102 GLY C N   1 
ATOM   5185  C  CA  . GLY C  1 102 ? 28.879  -3.113  -26.006 1.00 12.20 ? 102 GLY C CA  1 
ATOM   5186  C  C   . GLY C  1 102 ? 30.062  -3.116  -26.958 1.00 10.12 ? 102 GLY C C   1 
ATOM   5187  O  O   . GLY C  1 102 ? 30.698  -2.058  -27.054 1.00 10.60 ? 102 GLY C O   1 
ATOM   5188  N  N   . SER C  1 103 ? 30.183  -4.153  -27.781 1.00 10.03 ? 103 SER C N   1 
ATOM   5189  C  CA  . SER C  1 103 ? 31.048  -3.974  -28.974 1.00 9.74  ? 103 SER C CA  1 
ATOM   5190  C  C   . SER C  1 103 ? 30.501  -2.916  -29.903 1.00 10.08 ? 103 SER C C   1 
ATOM   5191  O  O   . SER C  1 103 ? 29.297  -2.547  -29.839 1.00 11.49 ? 103 SER C O   1 
ATOM   5192  C  CB  . SER C  1 103 ? 31.192  -5.283  -29.752 1.00 9.45  ? 103 SER C CB  1 
ATOM   5193  O  OG  . SER C  1 103 ? 29.953  -5.737  -30.368 1.00 10.23 ? 103 SER C OG  1 
ATOM   5194  N  N   . GLU C  1 104 ? 31.337  -2.417  -30.811 1.00 9.04  ? 104 GLU C N   1 
ATOM   5195  C  CA  . GLU C  1 104 ? 30.919  -1.456  -31.841 1.00 8.89  ? 104 GLU C CA  1 
ATOM   5196  C  C   . GLU C  1 104 ? 30.442  -2.181  -33.061 1.00 9.04  ? 104 GLU C C   1 
ATOM   5197  O  O   . GLU C  1 104 ? 29.277  -1.988  -33.498 1.00 8.96  ? 104 GLU C O   1 
ATOM   5198  C  CB  . GLU C  1 104 ? 32.038  -0.458  -32.140 1.00 9.23  ? 104 GLU C CB  1 
ATOM   5199  C  CG  . GLU C  1 104 ? 32.538  0.262   -30.841 1.00 9.85  ? 104 GLU C CG  1 
ATOM   5200  C  CD  . GLU C  1 104 ? 32.903  1.684   -31.147 1.00 9.48  ? 104 GLU C CD  1 
ATOM   5201  O  OE1 . GLU C  1 104 ? 33.985  1.836   -31.742 1.00 9.67  ? 104 GLU C OE1 1 
ATOM   5202  O  OE2 . GLU C  1 104 ? 32.100  2.584   -30.912 1.00 10.11 ? 104 GLU C OE2 1 
ATOM   5203  N  N   . HIS C  1 105 ? 31.305  -2.987  -33.670 1.00 8.12  ? 105 HIS C N   1 
ATOM   5204  C  CA  . HIS C  1 105 ? 30.837  -3.841  -34.780 1.00 8.33  ? 105 HIS C CA  1 
ATOM   5205  C  C   . HIS C  1 105 ? 29.905  -4.912  -34.253 1.00 8.34  ? 105 HIS C C   1 
ATOM   5206  O  O   . HIS C  1 105 ? 30.067  -5.388  -33.105 1.00 9.42  ? 105 HIS C O   1 
ATOM   5207  C  CB  . HIS C  1 105 ? 32.051  -4.438  -35.471 1.00 9.11  ? 105 HIS C CB  1 
ATOM   5208  C  CG  . HIS C  1 105 ? 32.827  -3.405  -36.225 1.00 8.97  ? 105 HIS C CG  1 
ATOM   5209  N  ND1 . HIS C  1 105 ? 33.833  -2.689  -35.645 1.00 8.68  ? 105 HIS C ND1 1 
ATOM   5210  C  CD2 . HIS C  1 105 ? 32.622  -2.851  -37.462 1.00 8.35  ? 105 HIS C CD2 1 
ATOM   5211  C  CE1 . HIS C  1 105 ? 34.301  -1.788  -36.523 1.00 9.11  ? 105 HIS C CE1 1 
ATOM   5212  N  NE2 . HIS C  1 105 ? 33.581  -1.878  -37.650 1.00 10.26 ? 105 HIS C NE2 1 
ATOM   5213  N  N   . THR C  1 106 ? 28.974  -5.325  -35.081 1.00 8.57  ? 106 THR C N   1 
ATOM   5214  C  CA  . THR C  1 106 ? 28.141  -6.469  -34.748 1.00 9.19  ? 106 THR C CA  1 
ATOM   5215  C  C   . THR C  1 106 ? 28.337  -7.480  -35.845 1.00 9.37  ? 106 THR C C   1 
ATOM   5216  O  O   . THR C  1 106 ? 28.805  -7.211  -36.954 1.00 9.19  ? 106 THR C O   1 
ATOM   5217  C  CB  . THR C  1 106 ? 26.682  -6.018  -34.607 1.00 9.91  ? 106 THR C CB  1 
ATOM   5218  O  OG1 . THR C  1 106 ? 26.203  -5.447  -35.874 1.00 10.47 ? 106 THR C OG1 1 
ATOM   5219  C  CG2 . THR C  1 106 ? 26.500  -5.035  -33.479 1.00 11.10 ? 106 THR C CG2 1 
ATOM   5220  N  N   . VAL C  1 107 ? 28.020  -8.741  -35.503 1.00 10.15 ? 107 VAL C N   1 
ATOM   5221  C  CA  . VAL C  1 107 ? 28.075  -9.797  -36.491 1.00 10.47 ? 107 VAL C CA  1 
ATOM   5222  C  C   . VAL C  1 107 ? 26.652  -10.474 -36.608 1.00 10.37 ? 107 VAL C C   1 
ATOM   5223  O  O   . VAL C  1 107 ? 26.118  -10.934 -35.570 1.00 10.90 ? 107 VAL C O   1 
ATOM   5224  C  CB  . VAL C  1 107 ? 29.139  -10.840 -36.101 1.00 12.22 ? 107 VAL C CB  1 
ATOM   5225  C  CG1 . VAL C  1 107 ? 29.094  -12.000 -37.107 1.00 14.41 ? 107 VAL C CG1 1 
ATOM   5226  C  CG2 . VAL C  1 107 ? 30.564  -10.232 -35.915 1.00 11.98 ? 107 VAL C CG2 1 
ATOM   5227  N  N   . SER C  1 108 ? 26.030  -10.419 -37.776 1.00 11.59 ? 108 SER C N   1 
ATOM   5228  C  CA  . SER C  1 108 ? 24.678  -10.993 -37.927 1.00 13.69 ? 108 SER C CA  1 
ATOM   5229  C  C   . SER C  1 108 ? 23.736  -10.363 -36.915 1.00 12.17 ? 108 SER C C   1 
ATOM   5230  O  O   . SER C  1 108 ? 22.853  -11.035 -36.370 1.00 13.26 ? 108 SER C O   1 
ATOM   5231  C  CB  . SER C  1 108 ? 24.679  -12.547 -37.799 1.00 13.07 ? 108 SER C CB  1 
ATOM   5232  O  OG  . SER C  1 108 ? 25.562  -13.025 -38.824 1.00 18.05 ? 108 SER C OG  1 
ATOM   5233  N  N   . GLY C  1 109 ? 23.894  -9.051  -36.736 1.00 10.93 ? 109 GLY C N   1 
ATOM   5234  C  CA  . GLY C  1 109 ? 23.042  -8.316  -35.865 1.00 11.46 ? 109 GLY C CA  1 
ATOM   5235  C  C   . GLY C  1 109 ? 23.442  -8.344  -34.386 1.00 12.26 ? 109 GLY C C   1 
ATOM   5236  O  O   . GLY C  1 109 ? 22.800  -7.646  -33.610 1.00 14.88 ? 109 GLY C O   1 
ATOM   5237  N  N   . GLN C  1 110 ? 24.422  -9.146  -33.972 1.00 11.04 ? 110 GLN C N   1 
ATOM   5238  C  CA  . GLN C  1 110 ? 24.684  -9.364  -32.580 1.00 12.87 ? 110 GLN C CA  1 
ATOM   5239  C  C   . GLN C  1 110 ? 25.916  -8.582  -32.093 1.00 10.75 ? 110 GLN C C   1 
ATOM   5240  O  O   . GLN C  1 110 ? 26.976  -8.655  -32.737 1.00 11.19 ? 110 GLN C O   1 
ATOM   5241  C  CB  . GLN C  1 110 ? 24.931  -10.877 -32.324 1.00 13.97 ? 110 GLN C CB  1 
ATOM   5242  C  CG  . GLN C  1 110 ? 23.849  -11.811 -32.974 1.00 15.89 ? 110 GLN C CG  1 
ATOM   5243  C  CD  . GLN C  1 110 ? 22.425  -11.402 -32.548 1.00 15.44 ? 110 GLN C CD  1 
ATOM   5244  O  OE1 . GLN C  1 110 ? 21.605  -11.056 -33.455 1.00 20.23 ? 110 GLN C OE1 1 
ATOM   5245  N  NE2 . GLN C  1 110 ? 22.187  -11.332 -31.306 1.00 15.40 ? 110 GLN C NE2 1 
ATOM   5246  N  N   . HIS C  1 111 ? 25.768  -7.915  -30.940 1.00 12.46 ? 111 HIS C N   1 
ATOM   5247  C  CA  . HIS C  1 111 ? 26.928  -7.327  -30.325 1.00 12.41 ? 111 HIS C CA  1 
ATOM   5248  C  C   . HIS C  1 111 ? 27.742  -8.362  -29.598 1.00 13.31 ? 111 HIS C C   1 
ATOM   5249  O  O   . HIS C  1 111 ? 27.159  -9.379  -29.147 1.00 17.12 ? 111 HIS C O   1 
ATOM   5250  C  CB  . HIS C  1 111 ? 26.511  -6.316  -29.251 1.00 14.10 ? 111 HIS C CB  1 
ATOM   5251  C  CG  . HIS C  1 111 ? 26.004  -5.042  -29.801 1.00 13.15 ? 111 HIS C CG  1 
ATOM   5252  N  ND1 . HIS C  1 111 ? 26.801  -3.914  -29.987 1.00 12.96 ? 111 HIS C ND1 1 
ATOM   5253  C  CD2 . HIS C  1 111 ? 24.785  -4.726  -30.308 1.00 12.97 ? 111 HIS C CD2 1 
ATOM   5254  C  CE1 . HIS C  1 111 ? 26.059  -2.949  -30.514 1.00 12.24 ? 111 HIS C CE1 1 
ATOM   5255  N  NE2 . HIS C  1 111 ? 24.822  -3.405  -30.660 1.00 16.60 ? 111 HIS C NE2 1 
ATOM   5256  N  N   . PHE C  1 112 ? 29.014  -8.173  -29.521 1.00 11.81 ? 112 PHE C N   1 
ATOM   5257  C  CA  . PHE C  1 112 ? 29.855  -8.873  -28.543 1.00 11.56 ? 112 PHE C CA  1 
ATOM   5258  C  C   . PHE C  1 112 ? 29.902  -8.051  -27.264 1.00 12.72 ? 112 PHE C C   1 
ATOM   5259  O  O   . PHE C  1 112 ? 29.365  -6.920  -27.212 1.00 12.37 ? 112 PHE C O   1 
ATOM   5260  C  CB  . PHE C  1 112 ? 31.225  -9.123  -29.138 1.00 12.79 ? 112 PHE C CB  1 
ATOM   5261  C  CG  . PHE C  1 112 ? 31.206  -10.236 -30.131 1.00 14.39 ? 112 PHE C CG  1 
ATOM   5262  C  CD1 . PHE C  1 112 ? 30.646  -10.058 -31.432 1.00 16.21 ? 112 PHE C CD1 1 
ATOM   5263  C  CD2 . PHE C  1 112 ? 31.681  -11.495 -29.771 1.00 15.86 ? 112 PHE C CD2 1 
ATOM   5264  C  CE1 . PHE C  1 112 ? 30.589  -11.131 -32.320 1.00 20.92 ? 112 PHE C CE1 1 
ATOM   5265  C  CE2 . PHE C  1 112 ? 31.644  -12.541 -30.685 1.00 17.21 ? 112 PHE C CE2 1 
ATOM   5266  C  CZ  . PHE C  1 112 ? 31.126  -12.364 -31.934 1.00 19.91 ? 112 PHE C CZ  1 
ATOM   5267  N  N   . ALA C  1 113 ? 30.483  -8.620  -26.150 1.00 12.94 ? 113 ALA C N   1 
ATOM   5268  C  CA  . ALA C  1 113 ? 30.555  -7.913  -24.909 1.00 11.88 ? 113 ALA C CA  1 
ATOM   5269  C  C   . ALA C  1 113 ? 31.261  -6.598  -24.938 1.00 10.67 ? 113 ALA C C   1 
ATOM   5270  O  O   . ALA C  1 113 ? 30.830  -5.625  -24.297 1.00 12.55 ? 113 ALA C O   1 
ATOM   5271  C  CB  . ALA C  1 113 ? 31.137  -8.832  -23.824 1.00 12.56 ? 113 ALA C CB  1 
ATOM   5272  N  N   . ALA C  1 114 ? 32.367  -6.566  -25.707 1.00 10.94 ? 114 ALA C N   1 
ATOM   5273  C  CA  . ALA C  1 114 ? 33.240  -5.402  -25.730 1.00 10.08 ? 114 ALA C CA  1 
ATOM   5274  C  C   . ALA C  1 114 ? 34.114  -5.515  -26.971 1.00 9.61  ? 114 ALA C C   1 
ATOM   5275  O  O   . ALA C  1 114 ? 34.014  -6.483  -27.735 1.00 10.36 ? 114 ALA C O   1 
ATOM   5276  C  CB  . ALA C  1 114 ? 34.096  -5.386  -24.421 1.00 12.69 ? 114 ALA C CB  1 
ATOM   5277  N  N   . GLU C  1 115 ? 34.861  -4.441  -27.277 1.00 9.76  ? 115 GLU C N   1 
ATOM   5278  C  CA  . GLU C  1 115 ? 35.692  -4.477  -28.462 1.00 10.56 ? 115 GLU C CA  1 
ATOM   5279  C  C   . GLU C  1 115 ? 36.956  -3.686  -28.155 1.00 9.35  ? 115 GLU C C   1 
ATOM   5280  O  O   . GLU C  1 115 ? 36.915  -2.544  -27.504 1.00 9.74  ? 115 GLU C O   1 
ATOM   5281  C  CB  . GLU C  1 115 ? 34.909  -3.783  -29.609 1.00 9.62  ? 115 GLU C CB  1 
ATOM   5282  C  CG  . GLU C  1 115 ? 35.609  -3.913  -31.004 1.00 9.52  ? 115 GLU C CG  1 
ATOM   5283  C  CD  . GLU C  1 115 ? 34.622  -3.561  -32.103 1.00 9.18  ? 115 GLU C CD  1 
ATOM   5284  O  OE1 . GLU C  1 115 ? 35.166  -3.048  -33.126 1.00 10.07 ? 115 GLU C OE1 1 
ATOM   5285  O  OE2 . GLU C  1 115 ? 33.425  -3.832  -31.990 1.00 10.17 ? 115 GLU C OE2 1 
ATOM   5286  N  N   . LEU C  1 116 ? 38.117  -4.222  -28.576 1.00 9.69  ? 116 LEU C N   1 
ATOM   5287  C  CA  . LEU C  1 116 ? 39.392  -3.526  -28.425 1.00 9.78  ? 116 LEU C CA  1 
ATOM   5288  C  C   . LEU C  1 116 ? 39.814  -2.959  -29.812 1.00 8.75  ? 116 LEU C C   1 
ATOM   5289  O  O   . LEU C  1 116 ? 39.697  -3.681  -30.821 1.00 9.99  ? 116 LEU C O   1 
ATOM   5290  C  CB  . LEU C  1 116 ? 40.418  -4.616  -27.988 1.00 11.40 ? 116 LEU C CB  1 
ATOM   5291  C  CG  . LEU C  1 116 ? 41.872  -4.144  -28.089 1.00 11.69 ? 116 LEU C CG  1 
ATOM   5292  C  CD1 . LEU C  1 116 ? 42.192  -3.208  -26.936 1.00 14.58 ? 116 LEU C CD1 1 
ATOM   5293  C  CD2 . LEU C  1 116 ? 42.889  -5.262  -28.259 1.00 13.40 ? 116 LEU C CD2 1 
ATOM   5294  N  N   . HIS C  1 117 ? 40.276  -1.700  -29.802 1.00 9.50  ? 117 HIS C N   1 
ATOM   5295  C  CA  . HIS C  1 117 ? 40.777  -1.076  -31.044 1.00 8.27  ? 117 HIS C CA  1 
ATOM   5296  C  C   . HIS C  1 117 ? 42.249  -0.795  -30.844 1.00 9.80  ? 117 HIS C C   1 
ATOM   5297  O  O   . HIS C  1 117 ? 42.598  -0.065  -29.900 1.00 10.39 ? 117 HIS C O   1 
ATOM   5298  C  CB  . HIS C  1 117 ? 40.062  0.202   -31.357 1.00 9.39  ? 117 HIS C CB  1 
ATOM   5299  C  CG  . HIS C  1 117 ? 38.665  -0.073  -31.754 1.00 7.80  ? 117 HIS C CG  1 
ATOM   5300  N  ND1 . HIS C  1 117 ? 37.635  0.851   -31.634 1.00 9.57  ? 117 HIS C ND1 1 
ATOM   5301  C  CD2 . HIS C  1 117 ? 38.184  -1.212  -32.292 1.00 8.79  ? 117 HIS C CD2 1 
ATOM   5302  C  CE1 . HIS C  1 117 ? 36.531  0.246   -32.154 1.00 9.37  ? 117 HIS C CE1 1 
ATOM   5303  N  NE2 . HIS C  1 117 ? 36.824  -0.992  -32.508 1.00 9.38  ? 117 HIS C NE2 1 
ATOM   5304  N  N   . ILE C  1 118 ? 43.073  -1.250  -31.716 1.00 9.06  ? 118 ILE C N   1 
ATOM   5305  C  CA  . ILE C  1 118 ? 44.500  -0.874  -31.722 1.00 10.25 ? 118 ILE C CA  1 
ATOM   5306  C  C   . ILE C  1 118 ? 44.776  0.040   -32.881 1.00 9.46  ? 118 ILE C C   1 
ATOM   5307  O  O   . ILE C  1 118 ? 44.660  -0.382  -34.097 1.00 9.41  ? 118 ILE C O   1 
ATOM   5308  C  CB  . ILE C  1 118 ? 45.413  -2.073  -31.875 1.00 10.54 ? 118 ILE C CB  1 
ATOM   5309  C  CG1 . ILE C  1 118 ? 45.065  -3.198  -30.890 1.00 11.29 ? 118 ILE C CG1 1 
ATOM   5310  C  CG2 . ILE C  1 118 ? 46.884  -1.617  -31.658 1.00 11.53 ? 118 ILE C CG2 1 
ATOM   5311  C  CD1 . ILE C  1 118 ? 45.972  -4.451  -30.900 1.00 13.26 ? 118 ILE C CD1 1 
ATOM   5312  N  N   . VAL C  1 119 ? 44.959  1.324   -32.637 1.00 9.98  ? 119 VAL C N   1 
ATOM   5313  C  CA  . VAL C  1 119 ? 44.912  2.423   -33.643 1.00 9.29  ? 119 VAL C CA  1 
ATOM   5314  C  C   . VAL C  1 119 ? 46.290  2.627   -34.123 1.00 10.40 ? 119 VAL C C   1 
ATOM   5315  O  O   . VAL C  1 119 ? 47.268  2.785   -33.309 1.00 11.24 ? 119 VAL C O   1 
ATOM   5316  C  CB  . VAL C  1 119 ? 44.411  3.733   -33.006 1.00 9.11  ? 119 VAL C CB  1 
ATOM   5317  C  CG1 . VAL C  1 119 ? 44.290  4.818   -34.054 1.00 9.87  ? 119 VAL C CG1 1 
ATOM   5318  C  CG2 . VAL C  1 119 ? 43.049  3.546   -32.367 1.00 12.53 ? 119 VAL C CG2 1 
ATOM   5319  N  N   . HIS C  1 120 ? 46.447  2.654   -35.447 1.00 10.02 ? 120 HIS C N   1 
ATOM   5320  C  CA  . HIS C  1 120 ? 47.750  2.914   -36.117 1.00 10.71 ? 120 HIS C CA  1 
ATOM   5321  C  C   . HIS C  1 120 ? 47.575  4.088   -37.077 1.00 12.15 ? 120 HIS C C   1 
ATOM   5322  O  O   . HIS C  1 120 ? 46.480  4.310   -37.584 1.00 10.27 ? 120 HIS C O   1 
ATOM   5323  C  CB  . HIS C  1 120 ? 48.207  1.686   -36.899 1.00 10.43 ? 120 HIS C CB  1 
ATOM   5324  C  CG  . HIS C  1 120 ? 48.393  0.447   -36.090 1.00 11.47 ? 120 HIS C CG  1 
ATOM   5325  N  ND1 . HIS C  1 120 ? 47.329  -0.247  -35.528 1.00 10.60 ? 120 HIS C ND1 1 
ATOM   5326  C  CD2 . HIS C  1 120 ? 49.508  -0.274  -35.797 1.00 12.58 ? 120 HIS C CD2 1 
ATOM   5327  C  CE1 . HIS C  1 120 ? 47.788  -1.342  -34.942 1.00 11.69 ? 120 HIS C CE1 1 
ATOM   5328  N  NE2 . HIS C  1 120 ? 49.098  -1.410  -35.110 1.00 12.41 ? 120 HIS C NE2 1 
ATOM   5329  N  N   . TYR C  1 121 ? 48.672  4.759   -37.423 1.00 11.31 ? 121 TYR C N   1 
ATOM   5330  C  CA  . TYR C  1 121 ? 48.614  5.872   -38.417 1.00 12.55 ? 121 TYR C CA  1 
ATOM   5331  C  C   . TYR C  1 121 ? 49.612  5.563   -39.518 1.00 11.88 ? 121 TYR C C   1 
ATOM   5332  O  O   . TYR C  1 121 ? 50.582  4.822   -39.330 1.00 11.50 ? 121 TYR C O   1 
ATOM   5333  C  CB  . TYR C  1 121 ? 48.920  7.202   -37.759 1.00 13.01 ? 121 TYR C CB  1 
ATOM   5334  C  CG  . TYR C  1 121 ? 50.318  7.396   -37.305 1.00 12.42 ? 121 TYR C CG  1 
ATOM   5335  C  CD1 . TYR C  1 121 ? 50.777  6.836   -36.067 1.00 12.19 ? 121 TYR C CD1 1 
ATOM   5336  C  CD2 . TYR C  1 121 ? 51.184  8.147   -38.077 1.00 12.51 ? 121 TYR C CD2 1 
ATOM   5337  C  CE1 . TYR C  1 121 ? 52.115  7.049   -35.635 1.00 14.19 ? 121 TYR C CE1 1 
ATOM   5338  C  CE2 . TYR C  1 121 ? 52.554  8.295   -37.673 1.00 13.59 ? 121 TYR C CE2 1 
ATOM   5339  C  CZ  . TYR C  1 121 ? 52.974  7.748   -36.476 1.00 15.41 ? 121 TYR C CZ  1 
ATOM   5340  O  OH  . TYR C  1 121 ? 54.278  7.922   -35.956 1.00 18.00 ? 121 TYR C OH  1 
ATOM   5341  N  N   . ASN C  1 122 ? 49.331  6.154   -40.685 1.00 12.12 ? 122 ASN C N   1 
ATOM   5342  C  CA  . ASN C  1 122 ? 50.219  5.929   -41.822 1.00 11.95 ? 122 ASN C CA  1 
ATOM   5343  C  C   . ASN C  1 122 ? 51.465  6.782   -41.732 1.00 12.27 ? 122 ASN C C   1 
ATOM   5344  O  O   . ASN C  1 122 ? 51.481  7.991   -41.995 1.00 13.92 ? 122 ASN C O   1 
ATOM   5345  C  CB  . ASN C  1 122 ? 49.442  6.351   -43.092 1.00 12.79 ? 122 ASN C CB  1 
ATOM   5346  C  CG  . ASN C  1 122 ? 50.113  5.939   -44.343 1.00 13.01 ? 122 ASN C CG  1 
ATOM   5347  O  OD1 . ASN C  1 122 ? 51.351  5.895   -44.432 1.00 14.83 ? 122 ASN C OD1 1 
ATOM   5348  N  ND2 . ASN C  1 122 ? 49.297  5.590   -45.342 1.00 14.42 ? 122 ASN C ND2 1 
ATOM   5349  N  N   . SER C  1 123 ? 52.491  6.109   -41.285 1.00 12.10 ? 123 SER C N   1 
ATOM   5350  C  CA  . SER C  1 123 ? 53.742  6.836   -41.001 1.00 13.33 ? 123 SER C CA  1 
ATOM   5351  C  C   . SER C  1 123 ? 54.591  6.970   -42.259 1.00 13.90 ? 123 SER C C   1 
ATOM   5352  O  O   . SER C  1 123 ? 55.514  7.764   -42.226 1.00 14.94 ? 123 SER C O   1 
ATOM   5353  C  CB  . SER C  1 123 ? 54.515  6.048   -39.893 1.00 15.33 ? 123 SER C CB  1 
ATOM   5354  O  OG  . SER C  1 123 ? 54.674  4.672   -40.141 1.00 13.81 ? 123 SER C OG  1 
ATOM   5355  N  N   . ASP C  1 124 ? 54.232  6.326   -43.348 1.00 12.94 ? 124 ASP C N   1 
ATOM   5356  C  CA  . ASP C  1 124 ? 54.949  6.560   -44.621 1.00 14.12 ? 124 ASP C CA  1 
ATOM   5357  C  C   . ASP C  1 124 ? 54.460  7.890   -45.156 1.00 16.32 ? 124 ASP C C   1 
ATOM   5358  O  O   . ASP C  1 124 ? 55.267  8.601   -45.751 1.00 20.46 ? 124 ASP C O   1 
ATOM   5359  C  CB  . ASP C  1 124 ? 54.601  5.453   -45.582 1.00 13.26 ? 124 ASP C CB  1 
ATOM   5360  C  CG  . ASP C  1 124 ? 55.325  4.160   -45.309 1.00 16.13 ? 124 ASP C CG  1 
ATOM   5361  O  OD1 . ASP C  1 124 ? 56.347  4.124   -44.532 1.00 15.46 ? 124 ASP C OD1 1 
ATOM   5362  O  OD2 . ASP C  1 124 ? 54.941  3.118   -45.830 1.00 15.24 ? 124 ASP C OD2 1 
ATOM   5363  N  N   . LEU C  1 125 ? 53.230  8.281   -44.923 1.00 12.73 ? 125 LEU C N   1 
ATOM   5364  C  CA  . LEU C  1 125 ? 52.699  9.519   -45.451 1.00 15.49 ? 125 LEU C CA  1 
ATOM   5365  C  C   . LEU C  1 125 ? 52.737  10.644  -44.477 1.00 15.91 ? 125 LEU C C   1 
ATOM   5366  O  O   . LEU C  1 125 ? 52.819  11.856  -44.878 1.00 18.22 ? 125 LEU C O   1 
ATOM   5367  C  CB  . LEU C  1 125 ? 51.243  9.348   -45.918 1.00 14.56 ? 125 LEU C CB  1 
ATOM   5368  C  CG  . LEU C  1 125 ? 51.063  8.402   -47.120 1.00 16.43 ? 125 LEU C CG  1 
ATOM   5369  C  CD1 . LEU C  1 125 ? 49.600  8.269   -47.536 1.00 20.63 ? 125 LEU C CD1 1 
ATOM   5370  C  CD2 . LEU C  1 125 ? 51.905  8.752   -48.329 1.00 18.96 ? 125 LEU C CD2 1 
ATOM   5371  N  N   . TYR C  1 126 ? 52.656  10.362  -43.180 1.00 14.60 ? 126 TYR C N   1 
ATOM   5372  C  CA  . TYR C  1 126 ? 52.383  11.410  -42.195 1.00 15.01 ? 126 TYR C CA  1 
ATOM   5373  C  C   . TYR C  1 126 ? 53.308  11.300  -40.998 1.00 16.03 ? 126 TYR C C   1 
ATOM   5374  O  O   . TYR C  1 126 ? 53.655  10.214  -40.651 1.00 15.16 ? 126 TYR C O   1 
ATOM   5375  C  CB  . TYR C  1 126 ? 50.930  11.348  -41.679 1.00 13.79 ? 126 TYR C CB  1 
ATOM   5376  C  CG  . TYR C  1 126 ? 49.969  11.403  -42.874 1.00 13.63 ? 126 TYR C CG  1 
ATOM   5377  C  CD1 . TYR C  1 126 ? 49.920  12.532  -43.722 1.00 15.39 ? 126 TYR C CD1 1 
ATOM   5378  C  CD2 . TYR C  1 126 ? 49.047  10.378  -43.112 1.00 13.80 ? 126 TYR C CD2 1 
ATOM   5379  C  CE1 . TYR C  1 126 ? 49.086  12.546  -44.820 1.00 14.69 ? 126 TYR C CE1 1 
ATOM   5380  C  CE2 . TYR C  1 126 ? 48.233  10.385  -44.219 1.00 15.05 ? 126 TYR C CE2 1 
ATOM   5381  C  CZ  . TYR C  1 126 ? 48.217  11.474  -45.042 1.00 15.79 ? 126 TYR C CZ  1 
ATOM   5382  O  OH  . TYR C  1 126 ? 47.398  11.447  -46.147 1.00 15.89 ? 126 TYR C OH  1 
ATOM   5383  N  N   . PRO C  1 127 ? 53.614  12.425  -40.285 1.00 16.15 ? 127 PRO C N   1 
ATOM   5384  C  CA  . PRO C  1 127 ? 54.635  12.353  -39.247 1.00 17.12 ? 127 PRO C CA  1 
ATOM   5385  C  C   . PRO C  1 127 ? 54.105  11.892  -37.898 1.00 18.22 ? 127 PRO C C   1 
ATOM   5386  O  O   . PRO C  1 127 ? 54.874  11.479  -37.033 1.00 20.23 ? 127 PRO C O   1 
ATOM   5387  C  CB  . PRO C  1 127 ? 55.085  13.812  -39.118 1.00 18.18 ? 127 PRO C CB  1 
ATOM   5388  C  CG  . PRO C  1 127 ? 53.949  14.640  -39.576 1.00 19.50 ? 127 PRO C CG  1 
ATOM   5389  C  CD  . PRO C  1 127 ? 53.384  13.824  -40.729 1.00 16.63 ? 127 PRO C CD  1 
ATOM   5390  N  N   . ASP C  1 128 ? 52.792  11.889  -37.711 1.00 17.33 ? 128 ASP C N   1 
ATOM   5391  C  CA  . ASP C  1 128 ? 52.228  11.542  -36.410 1.00 16.69 ? 128 ASP C CA  1 
ATOM   5392  C  C   . ASP C  1 128 ? 50.734  11.237  -36.593 1.00 16.65 ? 128 ASP C C   1 
ATOM   5393  O  O   . ASP C  1 128 ? 50.136  11.584  -37.660 1.00 15.68 ? 128 ASP C O   1 
ATOM   5394  C  CB  . ASP C  1 128 ? 52.478  12.685  -35.350 1.00 17.05 ? 128 ASP C CB  1 
ATOM   5395  C  CG  . ASP C  1 128 ? 52.043  13.997  -35.821 1.00 21.34 ? 128 ASP C CG  1 
ATOM   5396  O  OD1 . ASP C  1 128 ? 52.917  14.914  -35.741 1.00 26.86 ? 128 ASP C OD1 1 
ATOM   5397  O  OD2 . ASP C  1 128 ? 50.898  14.190  -36.246 1.00 21.90 ? 128 ASP C OD2 1 
ATOM   5398  N  N   . ALA C  1 129 ? 50.111  10.724  -35.534 1.00 14.01 ? 129 ALA C N   1 
ATOM   5399  C  CA  . ALA C  1 129 ? 48.743  10.277  -35.660 1.00 15.92 ? 129 ALA C CA  1 
ATOM   5400  C  C   . ALA C  1 129 ? 47.763  11.466  -35.773 1.00 16.59 ? 129 ALA C C   1 
ATOM   5401  O  O   . ALA C  1 129 ? 46.800  11.379  -36.532 1.00 17.24 ? 129 ALA C O   1 
ATOM   5402  C  CB  . ALA C  1 129 ? 48.390  9.418   -34.419 1.00 16.06 ? 129 ALA C CB  1 
ATOM   5403  N  N   A SER C  1 130 ? 48.057  12.541  -35.036 0.50 17.64 ? 130 SER C N   1 
ATOM   5404  N  N   B SER C  1 130 ? 47.991  12.553  -35.060 0.50 18.99 ? 130 SER C N   1 
ATOM   5405  C  CA  A SER C  1 130 ? 47.268  13.789  -35.124 0.50 17.76 ? 130 SER C CA  1 
ATOM   5406  C  CA  B SER C  1 130 ? 47.067  13.701  -35.205 0.50 19.96 ? 130 SER C CA  1 
ATOM   5407  C  C   A SER C  1 130 ? 47.106  14.232  -36.554 0.50 16.70 ? 130 SER C C   1 
ATOM   5408  C  C   B SER C  1 130 ? 47.064  14.321  -36.609 0.50 18.13 ? 130 SER C C   1 
ATOM   5409  O  O   A SER C  1 130 ? 45.988  14.334  -37.037 0.50 18.31 ? 130 SER C O   1 
ATOM   5410  O  O   B SER C  1 130 ? 46.003  14.627  -37.162 0.50 19.96 ? 130 SER C O   1 
ATOM   5411  C  CB  A SER C  1 130 ? 47.830  14.896  -34.256 0.50 17.13 ? 130 SER C CB  1 
ATOM   5412  C  CB  B SER C  1 130 ? 47.271  14.680  -34.056 0.50 20.10 ? 130 SER C CB  1 
ATOM   5413  O  OG  A SER C  1 130 ? 46.892  15.992  -34.326 0.50 17.82 ? 130 SER C OG  1 
ATOM   5414  O  OG  B SER C  1 130 ? 48.613  14.724  -33.716 0.50 22.71 ? 130 SER C OG  1 
ATOM   5415  N  N   . THR C  1 131 ? 48.240  14.464  -37.219 1.00 17.64 ? 131 THR C N   1 
ATOM   5416  C  CA  . THR C  1 131 ? 48.324  14.945  -38.579 1.00 15.62 ? 131 THR C CA  1 
ATOM   5417  C  C   . THR C  1 131 ? 47.666  13.917  -39.515 1.00 14.23 ? 131 THR C C   1 
ATOM   5418  O  O   . THR C  1 131 ? 46.965  14.308  -40.434 1.00 14.55 ? 131 THR C O   1 
ATOM   5419  C  CB  . THR C  1 131 ? 49.790  15.086  -39.005 1.00 16.90 ? 131 THR C CB  1 
ATOM   5420  O  OG1 . THR C  1 131 ? 50.440  15.976  -38.083 1.00 19.55 ? 131 THR C OG1 1 
ATOM   5421  C  CG2 . THR C  1 131 ? 49.836  15.677  -40.392 1.00 17.01 ? 131 THR C CG2 1 
ATOM   5422  N  N   . ALA C  1 132 ? 47.906  12.619  -39.276 1.00 14.56 ? 132 ALA C N   1 
ATOM   5423  C  CA  . ALA C  1 132 ? 47.308  11.605  -40.177 1.00 14.56 ? 132 ALA C CA  1 
ATOM   5424  C  C   . ALA C  1 132 ? 45.761  11.512  -40.085 1.00 13.21 ? 132 ALA C C   1 
ATOM   5425  O  O   . ALA C  1 132 ? 45.127  11.121  -41.021 1.00 14.38 ? 132 ALA C O   1 
ATOM   5426  C  CB  . ALA C  1 132 ? 47.854  10.245  -39.797 1.00 12.51 ? 132 ALA C CB  1 
ATOM   5427  N  N   . SER C  1 133 ? 45.202  11.836  -38.916 1.00 13.27 ? 133 SER C N   1 
ATOM   5428  C  CA  . SER C  1 133 ? 43.820  11.384  -38.584 1.00 14.25 ? 133 SER C CA  1 
ATOM   5429  C  C   . SER C  1 133 ? 42.798  11.926  -39.518 1.00 15.69 ? 133 SER C C   1 
ATOM   5430  O  O   . SER C  1 133 ? 41.725  11.299  -39.734 1.00 15.52 ? 133 SER C O   1 
ATOM   5431  C  CB  . SER C  1 133 ? 43.561  11.721  -37.097 1.00 15.91 ? 133 SER C CB  1 
ATOM   5432  O  OG  . SER C  1 133 ? 43.481  13.160  -37.006 1.00 16.56 ? 133 SER C OG  1 
ATOM   5433  N  N   . ASN C  1 134 ? 43.002  13.104  -40.076 1.00 15.11 ? 134 ASN C N   1 
ATOM   5434  C  CA  . ASN C  1 134 ? 42.015  13.692  -40.960 1.00 16.50 ? 134 ASN C CA  1 
ATOM   5435  C  C   . ASN C  1 134 ? 42.448  13.695  -42.400 1.00 15.27 ? 134 ASN C C   1 
ATOM   5436  O  O   . ASN C  1 134 ? 41.893  14.394  -43.248 1.00 18.87 ? 134 ASN C O   1 
ATOM   5437  C  CB  . ASN C  1 134 ? 41.621  15.095  -40.523 1.00 17.98 ? 134 ASN C CB  1 
ATOM   5438  C  CG  . ASN C  1 134 ? 42.761  16.079  -40.572 1.00 21.60 ? 134 ASN C CG  1 
ATOM   5439  O  OD1 . ASN C  1 134 ? 43.913  15.717  -40.733 1.00 20.06 ? 134 ASN C OD1 1 
ATOM   5440  N  ND2 . ASN C  1 134 ? 42.408  17.364  -40.449 1.00 23.18 ? 134 ASN C ND2 1 
ATOM   5441  N  N   . LYS C  1 135 ? 43.373  12.824  -42.769 1.00 16.24 ? 135 LYS C N   1 
ATOM   5442  C  CA  . LYS C  1 135 ? 43.948  12.829  -44.075 1.00 15.52 ? 135 LYS C CA  1 
ATOM   5443  C  C   . LYS C  1 135 ? 43.826  11.519  -44.781 1.00 15.48 ? 135 LYS C C   1 
ATOM   5444  O  O   . LYS C  1 135 ? 43.626  10.455  -44.161 1.00 14.46 ? 135 LYS C O   1 
ATOM   5445  C  CB  . LYS C  1 135 ? 45.433  13.248  -44.004 1.00 17.42 ? 135 LYS C CB  1 
ATOM   5446  C  CG  . LYS C  1 135 ? 45.546  14.741  -43.619 1.00 19.40 ? 135 LYS C CG  1 
ATOM   5447  C  CD  . LYS C  1 135 ? 46.993  15.229  -43.517 1.00 19.98 ? 135 LYS C CD  1 
ATOM   5448  C  CE  . LYS C  1 135 ? 47.082  16.656  -43.045 1.00 21.76 ? 135 LYS C CE  1 
ATOM   5449  N  NZ  . LYS C  1 135 ? 46.573  16.841  -41.641 1.00 23.06 ? 135 LYS C NZ  1 
ATOM   5450  N  N   . SER C  1 136 ? 43.978  11.519  -46.116 1.00 15.53 ? 136 SER C N   1 
ATOM   5451  C  CA  . SER C  1 136 ? 43.775  10.355  -46.934 1.00 15.04 ? 136 SER C CA  1 
ATOM   5452  C  C   . SER C  1 136 ? 44.657  9.219   -46.425 1.00 13.88 ? 136 SER C C   1 
ATOM   5453  O  O   . SER C  1 136 ? 45.886  9.365   -46.215 1.00 15.27 ? 136 SER C O   1 
ATOM   5454  C  CB  . SER C  1 136 ? 44.208  10.705  -48.344 1.00 18.88 ? 136 SER C CB  1 
ATOM   5455  O  OG  . SER C  1 136 ? 44.126  9.585   -49.122 1.00 22.98 ? 136 SER C OG  1 
ATOM   5456  N  N   . GLU C  1 137 ? 44.060  8.045   -46.326 1.00 13.92 ? 137 GLU C N   1 
ATOM   5457  C  CA  . GLU C  1 137 ? 44.734  6.800   -45.943 1.00 13.43 ? 137 GLU C CA  1 
ATOM   5458  C  C   . GLU C  1 137 ? 45.441  6.983   -44.632 1.00 12.55 ? 137 GLU C C   1 
ATOM   5459  O  O   . GLU C  1 137 ? 46.465  6.329   -44.359 1.00 13.36 ? 137 GLU C O   1 
ATOM   5460  C  CB  . GLU C  1 137 ? 45.699  6.291   -46.989 1.00 14.56 ? 137 GLU C CB  1 
ATOM   5461  C  CG  . GLU C  1 137 ? 44.970  6.046   -48.309 1.00 20.54 ? 137 GLU C CG  1 
ATOM   5462  C  CD  . GLU C  1 137 ? 45.910  5.553   -49.432 1.00 29.12 ? 137 GLU C CD  1 
ATOM   5463  O  OE1 . GLU C  1 137 ? 47.165  5.771   -49.396 1.00 35.44 ? 137 GLU C OE1 1 
ATOM   5464  O  OE2 . GLU C  1 137 ? 45.377  4.924   -50.377 1.00 31.76 ? 137 GLU C OE2 1 
ATOM   5465  N  N   . GLY C  1 138 ? 44.908  7.776   -43.715 1.00 11.71 ? 138 GLY C N   1 
ATOM   5466  C  CA  . GLY C  1 138 ? 45.677  8.175   -42.552 1.00 12.34 ? 138 GLY C CA  1 
ATOM   5467  C  C   . GLY C  1 138 ? 45.738  7.137   -41.455 1.00 11.67 ? 138 GLY C C   1 
ATOM   5468  O  O   . GLY C  1 138 ? 46.714  7.087   -40.679 1.00 11.94 ? 138 GLY C O   1 
ATOM   5469  N  N   . LEU C  1 139 ? 44.683  6.277   -41.298 1.00 10.77 ? 139 LEU C N   1 
ATOM   5470  C  CA  . LEU C  1 139 ? 44.636  5.419   -40.100 1.00 9.19  ? 139 LEU C CA  1 
ATOM   5471  C  C   . LEU C  1 139 ? 44.313  3.997   -40.484 1.00 9.07  ? 139 LEU C C   1 
ATOM   5472  O  O   . LEU C  1 139 ? 43.679  3.717   -41.528 1.00 10.20 ? 139 LEU C O   1 
ATOM   5473  C  CB  . LEU C  1 139 ? 43.590  5.922   -39.051 1.00 9.96  ? 139 LEU C CB  1 
ATOM   5474  C  CG  . LEU C  1 139 ? 43.797  7.279   -38.546 1.00 10.68 ? 139 LEU C CG  1 
ATOM   5475  C  CD1 . LEU C  1 139 ? 42.558  7.821   -37.838 1.00 13.61 ? 139 LEU C CD1 1 
ATOM   5476  C  CD2 . LEU C  1 139 ? 45.049  7.302   -37.663 1.00 12.27 ? 139 LEU C CD2 1 
ATOM   5477  N  N   . ALA C  1 140 ? 44.696  3.037   -39.612 1.00 9.74  ? 140 ALA C N   1 
ATOM   5478  C  CA  . ALA C  1 140 ? 44.315  1.645   -39.760 1.00 9.50  ? 140 ALA C CA  1 
ATOM   5479  C  C   . ALA C  1 140 ? 44.074  1.155   -38.332 1.00 10.39 ? 140 ALA C C   1 
ATOM   5480  O  O   . ALA C  1 140 ? 44.894  1.347   -37.434 1.00 11.47 ? 140 ALA C O   1 
ATOM   5481  C  CB  . ALA C  1 140 ? 45.427  0.811   -40.415 1.00 10.87 ? 140 ALA C CB  1 
ATOM   5482  N  N   . VAL C  1 141 ? 42.960  0.438   -38.125 1.00 9.72  ? 141 VAL C N   1 
ATOM   5483  C  CA  . VAL C  1 141 ? 42.605  -0.086  -36.782 1.00 9.88  ? 141 VAL C CA  1 
ATOM   5484  C  C   . VAL C  1 141 ? 42.513  -1.577  -36.882 1.00 9.44  ? 141 VAL C C   1 
ATOM   5485  O  O   . VAL C  1 141 ? 41.987  -2.172  -37.840 1.00 10.60 ? 141 VAL C O   1 
ATOM   5486  C  CB  . VAL C  1 141 ? 41.299  0.537   -36.257 1.00 9.39  ? 141 VAL C CB  1 
ATOM   5487  C  CG1 . VAL C  1 141 ? 40.937  -0.048  -34.877 1.00 13.04 ? 141 VAL C CG1 1 
ATOM   5488  C  CG2 . VAL C  1 141 ? 41.469  2.035   -36.146 1.00 12.18 ? 141 VAL C CG2 1 
ATOM   5489  N  N   . LEU C  1 142 ? 43.049  -2.231  -35.861 1.00 9.35  ? 142 LEU C N   1 
ATOM   5490  C  CA  . LEU C  1 142 ? 42.808  -3.638  -35.664 1.00 9.48  ? 142 LEU C CA  1 
ATOM   5491  C  C   . LEU C  1 142 ? 41.754  -3.739  -34.609 1.00 9.73  ? 142 LEU C C   1 
ATOM   5492  O  O   . LEU C  1 142 ? 41.931  -3.190  -33.482 1.00 10.53 ? 142 LEU C O   1 
ATOM   5493  C  CB  . LEU C  1 142 ? 44.059  -4.377  -35.105 1.00 10.91 ? 142 LEU C CB  1 
ATOM   5494  C  CG  . LEU C  1 142 ? 45.280  -4.221  -36.022 1.00 11.06 ? 142 LEU C CG  1 
ATOM   5495  C  CD1 . LEU C  1 142 ? 46.442  -5.059  -35.386 1.00 14.09 ? 142 LEU C CD1 1 
ATOM   5496  C  CD2 . LEU C  1 142 ? 45.052  -4.767  -37.420 1.00 11.03 ? 142 LEU C CD2 1 
ATOM   5497  N  N   . ALA C  1 143 ? 40.644  -4.437  -34.909 1.00 9.21  ? 143 ALA C N   1 
ATOM   5498  C  CA  . ALA C  1 143 ? 39.582  -4.553  -33.902 1.00 9.13  ? 143 ALA C CA  1 
ATOM   5499  C  C   . ALA C  1 143 ? 39.447  -6.002  -33.513 1.00 9.54  ? 143 ALA C C   1 
ATOM   5500  O  O   . ALA C  1 143 ? 39.407  -6.950  -34.311 1.00 10.49 ? 143 ALA C O   1 
ATOM   5501  C  CB  . ALA C  1 143 ? 38.303  -4.078  -34.555 1.00 11.00 ? 143 ALA C CB  1 
ATOM   5502  N  N   . VAL C  1 144 ? 39.333  -6.161  -32.185 1.00 9.65  ? 144 VAL C N   1 
ATOM   5503  C  CA  . VAL C  1 144 ? 39.162  -7.529  -31.573 1.00 10.76 ? 144 VAL C CA  1 
ATOM   5504  C  C   . VAL C  1 144 ? 37.836  -7.574  -30.833 1.00 10.60 ? 144 VAL C C   1 
ATOM   5505  O  O   . VAL C  1 144 ? 37.571  -6.690  -29.951 1.00 11.39 ? 144 VAL C O   1 
ATOM   5506  C  CB  . VAL C  1 144 ? 40.308  -7.784  -30.607 1.00 10.71 ? 144 VAL C CB  1 
ATOM   5507  C  CG1 . VAL C  1 144 ? 40.159  -9.233  -30.062 1.00 13.18 ? 144 VAL C CG1 1 
ATOM   5508  C  CG2 . VAL C  1 144 ? 41.668  -7.737  -31.338 1.00 11.86 ? 144 VAL C CG2 1 
ATOM   5509  N  N   . LEU C  1 145 ? 37.005  -8.513  -31.239 1.00 11.63 ? 145 LEU C N   1 
ATOM   5510  C  CA  . LEU C  1 145 ? 35.726  -8.718  -30.545 1.00 12.31 ? 145 LEU C CA  1 
ATOM   5511  C  C   . LEU C  1 145 ? 35.978  -9.493  -29.243 1.00 11.64 ? 145 LEU C C   1 
ATOM   5512  O  O   . LEU C  1 145 ? 36.774  -10.444 -29.251 1.00 12.87 ? 145 LEU C O   1 
ATOM   5513  C  CB  . LEU C  1 145 ? 34.741  -9.421  -31.458 1.00 12.21 ? 145 LEU C CB  1 
ATOM   5514  C  CG  . LEU C  1 145 ? 34.541  -8.670  -32.774 1.00 11.89 ? 145 LEU C CG  1 
ATOM   5515  C  CD1 . LEU C  1 145 ? 33.879  -9.608  -33.782 1.00 14.39 ? 145 LEU C CD1 1 
ATOM   5516  C  CD2 . LEU C  1 145 ? 33.624  -7.495  -32.528 1.00 14.74 ? 145 LEU C CD2 1 
ATOM   5517  N  N   . ILE C  1 146 ? 35.309  -9.077  -28.202 1.00 10.99 ? 146 ILE C N   1 
ATOM   5518  C  CA  . ILE C  1 146 ? 35.536  -9.684  -26.812 1.00 11.40 ? 146 ILE C CA  1 
ATOM   5519  C  C   . ILE C  1 146 ? 34.215  -10.274 -26.381 1.00 13.52 ? 146 ILE C C   1 
ATOM   5520  O  O   . ILE C  1 146 ? 33.195  -9.581  -26.316 1.00 13.35 ? 146 ILE C O   1 
ATOM   5521  C  CB  . ILE C  1 146 ? 35.990  -8.581  -25.855 1.00 12.87 ? 146 ILE C CB  1 
ATOM   5522  C  CG1 . ILE C  1 146 ? 37.357  -8.010  -26.298 1.00 12.72 ? 146 ILE C CG1 1 
ATOM   5523  C  CG2 . ILE C  1 146 ? 36.186  -9.197  -24.435 1.00 12.64 ? 146 ILE C CG2 1 
ATOM   5524  C  CD1 . ILE C  1 146 ? 37.743  -6.733  -25.596 1.00 13.83 ? 146 ILE C CD1 1 
ATOM   5525  N  N   . GLU C  1 147 ? 34.277  -11.543 -25.920 1.00 15.31 ? 147 GLU C N   1 
ATOM   5526  C  CA  . GLU C  1 147 ? 33.115  -12.169 -25.252 1.00 16.76 ? 147 GLU C CA  1 
ATOM   5527  C  C   . GLU C  1 147 ? 33.507  -12.717 -23.882 1.00 17.91 ? 147 GLU C C   1 
ATOM   5528  O  O   . GLU C  1 147 ? 34.691  -12.826 -23.524 1.00 16.32 ? 147 GLU C O   1 
ATOM   5529  C  CB  . GLU C  1 147 ? 32.545  -13.272 -26.112 1.00 16.62 ? 147 GLU C CB  1 
ATOM   5530  C  CG  . GLU C  1 147 ? 33.565  -14.379 -26.351 1.00 17.86 ? 147 GLU C CG  1 
ATOM   5531  C  CD  . GLU C  1 147 ? 33.106  -15.451 -27.346 1.00 21.72 ? 147 GLU C CD  1 
ATOM   5532  O  OE1 . GLU C  1 147 ? 32.173  -15.274 -28.185 1.00 22.83 ? 147 GLU C OE1 1 
ATOM   5533  O  OE2 . GLU C  1 147 ? 33.757  -16.519 -27.375 1.00 27.44 ? 147 GLU C OE2 1 
ATOM   5534  N  N   . MET C  1 148 ? 32.461  -12.940 -23.090 1.00 17.86 ? 148 MET C N   1 
ATOM   5535  C  CA  . MET C  1 148 ? 32.669  -13.541 -21.752 1.00 21.10 ? 148 MET C CA  1 
ATOM   5536  C  C   . MET C  1 148 ? 33.099  -15.009 -21.904 1.00 22.62 ? 148 MET C C   1 
ATOM   5537  O  O   . MET C  1 148 ? 32.538  -15.779 -22.716 1.00 26.02 ? 148 MET C O   1 
ATOM   5538  C  CB  . MET C  1 148 ? 31.366  -13.479 -20.965 1.00 27.50 ? 148 MET C CB  1 
ATOM   5539  C  CG  . MET C  1 148 ? 31.302  -12.380 -19.934 1.00 36.04 ? 148 MET C CG  1 
ATOM   5540  S  SD  . MET C  1 148 ? 29.914  -12.555 -18.728 1.00 58.88 ? 148 MET C SD  1 
ATOM   5541  C  CE  . MET C  1 148 ? 28.539  -12.513 -19.896 1.00 43.64 ? 148 MET C CE  1 
ATOM   5542  N  N   . GLY C  1 149 ? 34.140  -15.385 -21.143 1.00 21.00 ? 149 GLY C N   1 
ATOM   5543  C  CA  . GLY C  1 149 ? 34.549  -16.825 -21.115 1.00 22.32 ? 149 GLY C CA  1 
ATOM   5544  C  C   . GLY C  1 149 ? 35.625  -16.985 -20.021 1.00 19.13 ? 149 GLY C C   1 
ATOM   5545  O  O   . GLY C  1 149 ? 35.451  -16.505 -18.904 1.00 21.10 ? 149 GLY C O   1 
ATOM   5546  N  N   . SER C  1 150 ? 36.715  -17.588 -20.422 1.00 22.59 ? 150 SER C N   1 
ATOM   5547  C  CA  . SER C  1 150 ? 37.890  -17.832 -19.590 1.00 23.41 ? 150 SER C CA  1 
ATOM   5548  C  C   . SER C  1 150 ? 38.580  -16.555 -19.188 1.00 24.87 ? 150 SER C C   1 
ATOM   5549  O  O   . SER C  1 150 ? 38.697  -15.611 -20.018 1.00 19.76 ? 150 SER C O   1 
ATOM   5550  C  CB  . SER C  1 150 ? 38.908  -18.644 -20.400 1.00 26.04 ? 150 SER C CB  1 
ATOM   5551  O  OG  . SER C  1 150 ? 38.547  -20.008 -20.447 1.00 37.22 ? 150 SER C OG  1 
ATOM   5552  N  N   . PHE C  1 151 ? 39.097  -16.497 -17.973 1.00 20.82 ? 151 PHE C N   1 
ATOM   5553  C  CA  . PHE C  1 151 ? 39.985  -15.425 -17.539 1.00 20.84 ? 151 PHE C CA  1 
ATOM   5554  C  C   . PHE C  1 151 ? 41.132  -15.223 -18.552 1.00 21.60 ? 151 PHE C C   1 
ATOM   5555  O  O   . PHE C  1 151 ? 41.747  -16.178 -19.016 1.00 22.39 ? 151 PHE C O   1 
ATOM   5556  C  CB  . PHE C  1 151 ? 40.610  -15.773 -16.130 1.00 23.18 ? 151 PHE C CB  1 
ATOM   5557  C  CG  . PHE C  1 151 ? 41.551  -14.731 -15.611 1.00 19.92 ? 151 PHE C CG  1 
ATOM   5558  C  CD1 . PHE C  1 151 ? 41.071  -13.496 -15.137 1.00 19.71 ? 151 PHE C CD1 1 
ATOM   5559  C  CD2 . PHE C  1 151 ? 42.955  -14.961 -15.624 1.00 20.03 ? 151 PHE C CD2 1 
ATOM   5560  C  CE1 . PHE C  1 151 ? 41.997  -12.518 -14.720 1.00 19.00 ? 151 PHE C CE1 1 
ATOM   5561  C  CE2 . PHE C  1 151 ? 43.867  -14.014 -15.202 1.00 19.39 ? 151 PHE C CE2 1 
ATOM   5562  C  CZ  . PHE C  1 151 ? 43.362  -12.773 -14.719 1.00 19.16 ? 151 PHE C CZ  1 
ATOM   5563  N  N   . ASN C  1 152 ? 41.478  -13.974 -18.819 1.00 19.21 ? 152 ASN C N   1 
ATOM   5564  C  CA  . ASN C  1 152 ? 42.522  -13.680 -19.768 1.00 16.60 ? 152 ASN C CA  1 
ATOM   5565  C  C   . ASN C  1 152 ? 43.651  -12.913 -19.103 1.00 17.52 ? 152 ASN C C   1 
ATOM   5566  O  O   . ASN C  1 152 ? 43.489  -11.729 -18.749 1.00 19.14 ? 152 ASN C O   1 
ATOM   5567  C  CB  . ASN C  1 152 ? 41.910  -12.790 -20.954 1.00 16.72 ? 152 ASN C CB  1 
ATOM   5568  C  CG  . ASN C  1 152 ? 42.793  -12.742 -22.134 1.00 17.92 ? 152 ASN C CG  1 
ATOM   5569  O  OD1 . ASN C  1 152 ? 43.972  -12.377 -21.993 1.00 17.92 ? 152 ASN C OD1 1 
ATOM   5570  N  ND2 . ASN C  1 152 ? 42.215  -12.964 -23.390 1.00 15.70 ? 152 ASN C ND2 1 
ATOM   5571  N  N   . PRO C  1 153 ? 44.783  -13.582 -18.788 1.00 18.95 ? 153 PRO C N   1 
ATOM   5572  C  CA  . PRO C  1 153 ? 45.903  -12.921 -18.191 1.00 21.59 ? 153 PRO C CA  1 
ATOM   5573  C  C   . PRO C  1 153 ? 46.452  -11.718 -18.954 1.00 20.73 ? 153 PRO C C   1 
ATOM   5574  O  O   . PRO C  1 153 ? 46.864  -10.738 -18.336 1.00 23.78 ? 153 PRO C O   1 
ATOM   5575  C  CB  . PRO C  1 153 ? 46.952  -14.064 -18.002 1.00 22.66 ? 153 PRO C CB  1 
ATOM   5576  C  CG  . PRO C  1 153 ? 46.262  -15.338 -18.294 1.00 25.18 ? 153 PRO C CG  1 
ATOM   5577  C  CD  . PRO C  1 153 ? 45.013  -15.019 -19.147 1.00 18.85 ? 153 PRO C CD  1 
ATOM   5578  N  N   . SER C  1 154 ? 46.345  -11.743 -20.285 1.00 19.82 ? 154 SER C N   1 
ATOM   5579  C  CA  . SER C  1 154 ? 46.925  -10.690 -21.087 1.00 17.52 ? 154 SER C CA  1 
ATOM   5580  C  C   . SER C  1 154 ? 46.074  -9.421  -20.955 1.00 14.94 ? 154 SER C C   1 
ATOM   5581  O  O   . SER C  1 154 ? 46.594  -8.298  -20.744 1.00 17.21 ? 154 SER C O   1 
ATOM   5582  C  CB  . SER C  1 154 ? 47.096  -11.173 -22.524 1.00 20.83 ? 154 SER C CB  1 
ATOM   5583  O  OG  . SER C  1 154 ? 47.946  -12.332 -22.476 1.00 24.49 ? 154 SER C OG  1 
ATOM   5584  N  N   . TYR C  1 155 ? 44.747  -9.577  -21.040 1.00 17.89 ? 155 TYR C N   1 
ATOM   5585  C  CA  . TYR C  1 155 ? 43.880  -8.435  -20.891 1.00 17.24 ? 155 TYR C CA  1 
ATOM   5586  C  C   . TYR C  1 155 ? 44.035  -7.867  -19.480 1.00 17.13 ? 155 TYR C C   1 
ATOM   5587  O  O   . TYR C  1 155 ? 43.883  -6.641  -19.247 1.00 16.79 ? 155 TYR C O   1 
ATOM   5588  C  CB  . TYR C  1 155 ? 42.420  -8.722  -21.273 1.00 16.40 ? 155 TYR C CB  1 
ATOM   5589  C  CG  . TYR C  1 155 ? 42.214  -8.591  -22.781 1.00 14.75 ? 155 TYR C CG  1 
ATOM   5590  C  CD1 . TYR C  1 155 ? 42.616  -9.599  -23.656 1.00 15.37 ? 155 TYR C CD1 1 
ATOM   5591  C  CD2 . TYR C  1 155 ? 41.654  -7.444  -23.329 1.00 14.56 ? 155 TYR C CD2 1 
ATOM   5592  C  CE1 . TYR C  1 155 ? 42.447  -9.471  -25.026 1.00 15.94 ? 155 TYR C CE1 1 
ATOM   5593  C  CE2 . TYR C  1 155 ? 41.480  -7.309  -24.694 1.00 13.98 ? 155 TYR C CE2 1 
ATOM   5594  C  CZ  . TYR C  1 155 ? 41.874  -8.321  -25.538 1.00 14.39 ? 155 TYR C CZ  1 
ATOM   5595  O  OH  . TYR C  1 155 ? 41.688  -8.166  -26.894 1.00 14.57 ? 155 TYR C OH  1 
ATOM   5596  N  N   . ASP C  1 156 ? 44.300  -8.729  -18.479 1.00 18.49 ? 156 ASP C N   1 
ATOM   5597  C  CA  . ASP C  1 156 ? 44.478  -8.226  -17.124 1.00 20.28 ? 156 ASP C CA  1 
ATOM   5598  C  C   . ASP C  1 156 ? 45.686  -7.336  -16.903 1.00 18.56 ? 156 ASP C C   1 
ATOM   5599  O  O   . ASP C  1 156 ? 45.683  -6.533  -15.934 1.00 19.57 ? 156 ASP C O   1 
ATOM   5600  C  CB  . ASP C  1 156 ? 44.420  -9.398  -16.143 1.00 20.50 ? 156 ASP C CB  1 
ATOM   5601  C  CG  . ASP C  1 156 ? 43.381  -9.140  -15.035 1.00 26.12 ? 156 ASP C CG  1 
ATOM   5602  O  OD1 . ASP C  1 156 ? 42.182  -8.754  -15.318 1.00 23.65 ? 156 ASP C OD1 1 
ATOM   5603  O  OD2 . ASP C  1 156 ? 43.775  -9.348  -13.841 1.00 31.20 ? 156 ASP C OD2 1 
ATOM   5604  N  N   . LYS C  1 157 ? 46.599  -7.300  -17.879 1.00 18.55 ? 157 LYS C N   1 
ATOM   5605  C  CA  . LYS C  1 157 ? 47.781  -6.444  -17.811 1.00 18.96 ? 157 LYS C CA  1 
ATOM   5606  C  C   . LYS C  1 157 ? 47.370  -5.001  -18.023 1.00 23.47 ? 157 LYS C C   1 
ATOM   5607  O  O   . LYS C  1 157 ? 48.111  -4.079  -17.592 1.00 26.69 ? 157 LYS C O   1 
ATOM   5608  C  CB  . LYS C  1 157 ? 48.829  -6.894  -18.827 1.00 22.79 ? 157 LYS C CB  1 
ATOM   5609  C  CG  . LYS C  1 157 ? 49.340  -8.319  -18.577 1.00 23.42 ? 157 LYS C CG  1 
ATOM   5610  C  CD  . LYS C  1 157 ? 50.495  -8.746  -19.430 1.00 26.52 ? 157 LYS C CD  1 
ATOM   5611  C  CE  . LYS C  1 157 ? 50.911  -10.134 -18.988 1.00 30.37 ? 157 LYS C CE  1 
ATOM   5612  N  NZ  . LYS C  1 157 ? 51.335  -10.985 -20.127 1.00 29.49 ? 157 LYS C NZ  1 
ATOM   5613  N  N   . ILE C  1 158 ? 46.194  -4.804  -18.668 1.00 18.28 ? 158 ILE C N   1 
ATOM   5614  C  CA  . ILE C  1 158 ? 45.580  -3.494  -18.629 1.00 19.24 ? 158 ILE C CA  1 
ATOM   5615  C  C   . ILE C  1 158 ? 44.582  -3.367  -17.484 1.00 16.97 ? 158 ILE C C   1 
ATOM   5616  O  O   . ILE C  1 158 ? 44.599  -2.327  -16.752 1.00 17.53 ? 158 ILE C O   1 
ATOM   5617  C  CB  . ILE C  1 158 ? 44.852  -3.297  -19.983 1.00 17.95 ? 158 ILE C CB  1 
ATOM   5618  C  CG1 . ILE C  1 158 ? 45.921  -3.253  -21.053 1.00 20.84 ? 158 ILE C CG1 1 
ATOM   5619  C  CG2 . ILE C  1 158 ? 43.993  -2.038  -19.952 1.00 19.86 ? 158 ILE C CG2 1 
ATOM   5620  C  CD1 . ILE C  1 158 ? 45.451  -3.451  -22.504 1.00 24.08 ? 158 ILE C CD1 1 
ATOM   5621  N  N   . PHE C  1 159 ? 43.642  -4.302  -17.375 1.00 15.86 ? 159 PHE C N   1 
ATOM   5622  C  CA  . PHE C  1 159 ? 42.526  -4.150  -16.401 1.00 17.21 ? 159 PHE C CA  1 
ATOM   5623  C  C   . PHE C  1 159 ? 42.921  -3.990  -14.911 1.00 17.14 ? 159 PHE C C   1 
ATOM   5624  O  O   . PHE C  1 159 ? 42.157  -3.370  -14.156 1.00 18.04 ? 159 PHE C O   1 
ATOM   5625  C  CB  . PHE C  1 159 ? 41.514  -5.307  -16.510 1.00 16.94 ? 159 PHE C CB  1 
ATOM   5626  C  CG  . PHE C  1 159 ? 40.869  -5.478  -17.890 1.00 19.26 ? 159 PHE C CG  1 
ATOM   5627  C  CD1 . PHE C  1 159 ? 40.792  -4.406  -18.825 1.00 21.46 ? 159 PHE C CD1 1 
ATOM   5628  C  CD2 . PHE C  1 159 ? 40.377  -6.728  -18.223 1.00 18.20 ? 159 PHE C CD2 1 
ATOM   5629  C  CE1 . PHE C  1 159 ? 40.151  -4.647  -20.054 1.00 20.76 ? 159 PHE C CE1 1 
ATOM   5630  C  CE2 . PHE C  1 159 ? 39.704  -6.961  -19.454 1.00 20.80 ? 159 PHE C CE2 1 
ATOM   5631  C  CZ  . PHE C  1 159 ? 39.631  -5.909  -20.342 1.00 20.43 ? 159 PHE C CZ  1 
ATOM   5632  N  N   . SER C  1 160 ? 44.095  -4.546  -14.592 1.00 17.84 ? 160 SER C N   1 
ATOM   5633  C  CA  . SER C  1 160 ? 44.616  -4.462  -13.234 1.00 19.40 ? 160 SER C CA  1 
ATOM   5634  C  C   . SER C  1 160 ? 45.081  -3.102  -12.886 1.00 22.09 ? 160 SER C C   1 
ATOM   5635  O  O   . SER C  1 160 ? 45.431  -2.871  -11.720 1.00 21.91 ? 160 SER C O   1 
ATOM   5636  C  CB  . SER C  1 160 ? 45.737  -5.440  -13.032 1.00 20.68 ? 160 SER C CB  1 
ATOM   5637  O  OG  . SER C  1 160 ? 46.898  -5.185  -13.810 1.00 21.22 ? 160 SER C OG  1 
ATOM   5638  N  N   . HIS C  1 161 ? 45.092  -2.151  -13.807 1.00 18.26 ? 161 HIS C N   1 
ATOM   5639  C  CA  . HIS C  1 161 ? 45.361  -0.743  -13.524 1.00 17.67 ? 161 HIS C CA  1 
ATOM   5640  C  C   . HIS C  1 161 ? 44.224  0.195   -13.568 1.00 15.39 ? 161 HIS C C   1 
ATOM   5641  O  O   . HIS C  1 161 ? 44.406  1.429   -13.346 1.00 15.81 ? 161 HIS C O   1 
ATOM   5642  C  CB  . HIS C  1 161 ? 46.483  -0.247  -14.462 1.00 20.40 ? 161 HIS C CB  1 
ATOM   5643  C  CG  . HIS C  1 161 ? 47.734  -1.055  -14.305 1.00 22.61 ? 161 HIS C CG  1 
ATOM   5644  N  ND1 . HIS C  1 161 ? 48.792  -0.644  -13.503 1.00 27.10 ? 161 HIS C ND1 1 
ATOM   5645  C  CD2 . HIS C  1 161 ? 48.026  -2.305  -14.721 1.00 24.67 ? 161 HIS C CD2 1 
ATOM   5646  C  CE1 . HIS C  1 161 ? 49.710  -1.602  -13.500 1.00 27.34 ? 161 HIS C CE1 1 
ATOM   5647  N  NE2 . HIS C  1 161 ? 49.259  -2.624  -14.209 1.00 28.68 ? 161 HIS C NE2 1 
ATOM   5648  N  N   . LEU C  1 162 ? 42.992  -0.317  -13.823 1.00 16.03 ? 162 LEU C N   1 
ATOM   5649  C  CA  . LEU C  1 162 ? 41.912  0.614   -14.062 1.00 17.34 ? 162 LEU C CA  1 
ATOM   5650  C  C   . LEU C  1 162 ? 41.544  1.488   -12.876 1.00 15.47 ? 162 LEU C C   1 
ATOM   5651  O  O   . LEU C  1 162 ? 41.124  2.634   -13.044 1.00 15.82 ? 162 LEU C O   1 
ATOM   5652  C  CB  . LEU C  1 162 ? 40.635  -0.116  -14.521 1.00 19.26 ? 162 LEU C CB  1 
ATOM   5653  C  CG  . LEU C  1 162 ? 40.777  -0.845  -15.826 1.00 19.41 ? 162 LEU C CG  1 
ATOM   5654  C  CD1 . LEU C  1 162 ? 39.530  -1.696  -16.036 1.00 22.09 ? 162 LEU C CD1 1 
ATOM   5655  C  CD2 . LEU C  1 162 ? 41.040  0.184   -16.919 1.00 21.35 ? 162 LEU C CD2 1 
ATOM   5656  N  N   . GLN C  1 163 ? 41.792  0.995   -11.619 1.00 15.84 ? 163 GLN C N   1 
ATOM   5657  C  CA  . GLN C  1 163 ? 41.375  1.801   -10.455 1.00 15.55 ? 163 GLN C CA  1 
ATOM   5658  C  C   . GLN C  1 163 ? 42.354  2.962   -10.218 1.00 14.84 ? 163 GLN C C   1 
ATOM   5659  O  O   . GLN C  1 163 ? 42.051  3.811   -9.356  1.00 20.03 ? 163 GLN C O   1 
ATOM   5660  C  CB  . GLN C  1 163 ? 41.354  0.902   -9.197  1.00 16.67 ? 163 GLN C CB  1 
ATOM   5661  C  CG  . GLN C  1 163 ? 40.303  -0.251  -9.208  1.00 20.87 ? 163 GLN C CG  1 
ATOM   5662  C  CD  . GLN C  1 163 ? 38.873  0.200   -9.323  1.00 22.25 ? 163 GLN C CD  1 
ATOM   5663  O  OE1 . GLN C  1 163 ? 38.393  1.218   -8.787  1.00 23.42 ? 163 GLN C OE1 1 
ATOM   5664  N  NE2 . GLN C  1 163 ? 38.126  -0.584  -10.122 1.00 24.16 ? 163 GLN C NE2 1 
ATOM   5665  N  N   . HIS C  1 164 ? 43.417  3.093   -11.020 1.00 14.94 ? 164 HIS C N   1 
ATOM   5666  C  CA  . HIS C  1 164 ? 44.320  4.235   -10.949 1.00 15.44 ? 164 HIS C CA  1 
ATOM   5667  C  C   . HIS C  1 164 ? 43.925  5.356   -11.859 1.00 18.83 ? 164 HIS C C   1 
ATOM   5668  O  O   . HIS C  1 164 ? 44.462  6.483   -11.787 1.00 19.58 ? 164 HIS C O   1 
ATOM   5669  C  CB  . HIS C  1 164 ? 45.773  3.836   -11.171 1.00 18.77 ? 164 HIS C CB  1 
ATOM   5670  C  CG  . HIS C  1 164 ? 46.223  2.782   -10.244 1.00 15.03 ? 164 HIS C CG  1 
ATOM   5671  N  ND1 . HIS C  1 164 ? 46.405  3.027   -8.889  1.00 15.86 ? 164 HIS C ND1 1 
ATOM   5672  C  CD2 . HIS C  1 164 ? 46.571  1.499   -10.467 1.00 15.22 ? 164 HIS C CD2 1 
ATOM   5673  C  CE1 . HIS C  1 164 ? 46.762  1.898   -8.303  1.00 15.32 ? 164 HIS C CE1 1 
ATOM   5674  N  NE2 . HIS C  1 164 ? 46.837  0.950   -9.220  1.00 15.78 ? 164 HIS C NE2 1 
ATOM   5675  N  N   . VAL C  1 165 ? 42.991  5.055   -12.771 1.00 20.05 ? 165 VAL C N   1 
ATOM   5676  C  CA  . VAL C  1 165 ? 42.474  6.056   -13.715 1.00 18.10 ? 165 VAL C CA  1 
ATOM   5677  C  C   . VAL C  1 165 ? 40.981  6.230   -13.639 1.00 18.86 ? 165 VAL C C   1 
ATOM   5678  O  O   . VAL C  1 165 ? 40.274  6.384   -14.672 1.00 17.52 ? 165 VAL C O   1 
ATOM   5679  C  CB  . VAL C  1 165 ? 43.053  5.818   -15.116 1.00 18.24 ? 165 VAL C CB  1 
ATOM   5680  C  CG1 . VAL C  1 165 ? 44.574  6.069   -15.088 1.00 17.63 ? 165 VAL C CG1 1 
ATOM   5681  C  CG2 . VAL C  1 165 ? 42.666  4.410   -15.577 1.00 18.12 ? 165 VAL C CG2 1 
ATOM   5682  N  N   . LYS C  1 166 ? 40.396  6.139   -12.461 1.00 16.41 ? 166 LYS C N   1 
ATOM   5683  C  CA  . LYS C  1 166 ? 38.968  6.192   -12.390 1.00 16.51 ? 166 LYS C CA  1 
ATOM   5684  C  C   . LYS C  1 166 ? 38.314  7.404   -12.954 1.00 17.71 ? 166 LYS C C   1 
ATOM   5685  O  O   . LYS C  1 166 ? 37.140  7.342   -13.365 1.00 18.72 ? 166 LYS C O   1 
ATOM   5686  C  CB  . LYS C  1 166 ? 38.458  5.965   -10.920 1.00 20.63 ? 166 LYS C CB  1 
ATOM   5687  C  CG  . LYS C  1 166 ? 38.798  4.611   -10.363 1.00 22.98 ? 166 LYS C CG  1 
ATOM   5688  C  CD  . LYS C  1 166 ? 38.185  4.354   -8.953  1.00 22.75 ? 166 LYS C CD  1 
ATOM   5689  C  CE  . LYS C  1 166 ? 36.669  4.229   -8.981  1.00 25.31 ? 166 LYS C CE  1 
ATOM   5690  N  NZ  . LYS C  1 166 ? 36.302  2.886   -9.489  1.00 23.25 ? 166 LYS C NZ  1 
ATOM   5691  N  N   . TYR C  1 167 ? 38.978  8.552   -12.900 1.00 16.09 ? 167 TYR C N   1 
ATOM   5692  C  CA  . TYR C  1 167 ? 38.298  9.753   -13.238 1.00 17.26 ? 167 TYR C CA  1 
ATOM   5693  C  C   . TYR C  1 167 ? 38.874  10.335  -14.515 1.00 17.24 ? 167 TYR C C   1 
ATOM   5694  O  O   . TYR C  1 167 ? 40.084  10.134  -14.749 1.00 18.80 ? 167 TYR C O   1 
ATOM   5695  C  CB  . TYR C  1 167 ? 38.414  10.764  -12.110 1.00 18.65 ? 167 TYR C CB  1 
ATOM   5696  C  CG  . TYR C  1 167 ? 37.751  10.307  -10.829 1.00 19.28 ? 167 TYR C CG  1 
ATOM   5697  C  CD1 . TYR C  1 167 ? 36.380  10.377  -10.665 1.00 21.24 ? 167 TYR C CD1 1 
ATOM   5698  C  CD2 . TYR C  1 167 ? 38.554  9.841   -9.785  1.00 19.93 ? 167 TYR C CD2 1 
ATOM   5699  C  CE1 . TYR C  1 167 ? 35.791  9.993   -9.425  1.00 25.39 ? 167 TYR C CE1 1 
ATOM   5700  C  CE2 . TYR C  1 167 ? 38.006  9.441   -8.551  1.00 23.15 ? 167 TYR C CE2 1 
ATOM   5701  C  CZ  . TYR C  1 167 ? 36.630  9.504   -8.400  1.00 24.37 ? 167 TYR C CZ  1 
ATOM   5702  O  OH  . TYR C  1 167 ? 36.076  9.117   -7.184  1.00 28.83 ? 167 TYR C OH  1 
ATOM   5703  N  N   . LYS C  1 168 ? 38.012  11.151  -15.203 1.00 19.21 ? 168 LYS C N   1 
ATOM   5704  C  CA  . LYS C  1 168 ? 38.445  11.821  -16.433 1.00 22.31 ? 168 LYS C CA  1 
ATOM   5705  C  C   . LYS C  1 168 ? 39.699  12.631  -16.207 1.00 24.94 ? 168 LYS C C   1 
ATOM   5706  O  O   . LYS C  1 168 ? 39.796  13.430  -15.225 1.00 25.46 ? 168 LYS C O   1 
ATOM   5707  C  CB  . LYS C  1 168 ? 37.365  12.786  -16.921 1.00 23.02 ? 168 LYS C CB  1 
ATOM   5708  C  CG  . LYS C  1 168 ? 37.680  13.495  -18.254 1.00 26.74 ? 168 LYS C CG  1 
ATOM   5709  C  CD  . LYS C  1 168 ? 36.439  14.283  -18.652 1.00 30.38 ? 168 LYS C CD  1 
ATOM   5710  C  CE  . LYS C  1 168 ? 36.393  14.646  -20.143 1.00 39.78 ? 168 LYS C CE  1 
ATOM   5711  N  NZ  . LYS C  1 168 ? 37.616  15.288  -20.718 1.00 38.10 ? 168 LYS C NZ  1 
ATOM   5712  N  N   . GLY C  1 169 ? 40.631  12.497  -17.133 1.00 21.27 ? 169 GLY C N   1 
ATOM   5713  C  CA  . GLY C  1 169 ? 41.897  13.157  -17.099 1.00 23.78 ? 169 GLY C CA  1 
ATOM   5714  C  C   . GLY C  1 169 ? 42.938  12.488  -16.332 1.00 22.68 ? 169 GLY C C   1 
ATOM   5715  O  O   . GLY C  1 169 ? 44.104  12.822  -16.469 1.00 26.58 ? 169 GLY C O   1 
ATOM   5716  N  N   . GLN C  1 170 ? 42.605  11.455  -15.550 1.00 19.70 ? 170 GLN C N   1 
ATOM   5717  C  CA  . GLN C  1 170 ? 43.622  10.805  -14.826 1.00 18.35 ? 170 GLN C CA  1 
ATOM   5718  C  C   . GLN C  1 170 ? 44.523  9.896   -15.632 1.00 19.59 ? 170 GLN C C   1 
ATOM   5719  O  O   . GLN C  1 170 ? 44.056  9.302   -16.615 1.00 18.75 ? 170 GLN C O   1 
ATOM   5720  C  CB  . GLN C  1 170 ? 43.076  9.943   -13.615 1.00 19.90 ? 170 GLN C CB  1 
ATOM   5721  C  CG  . GLN C  1 170 ? 42.574  10.853  -12.489 1.00 20.20 ? 170 GLN C CG  1 
ATOM   5722  C  CD  . GLN C  1 170 ? 42.082  10.062  -11.292 1.00 22.27 ? 170 GLN C CD  1 
ATOM   5723  O  OE1 . GLN C  1 170 ? 41.484  8.990   -11.441 1.00 19.27 ? 170 GLN C OE1 1 
ATOM   5724  N  NE2 . GLN C  1 170 ? 42.329  10.594  -10.048 1.00 23.27 ? 170 GLN C NE2 1 
ATOM   5725  N  N   . GLU C  1 171 ? 45.741  9.708   -15.199 1.00 19.33 ? 171 GLU C N   1 
ATOM   5726  C  CA  . GLU C  1 171 ? 46.766  8.976   -15.942 1.00 21.53 ? 171 GLU C CA  1 
ATOM   5727  C  C   . GLU C  1 171 ? 47.516  8.068   -15.064 1.00 19.84 ? 171 GLU C C   1 
ATOM   5728  O  O   . GLU C  1 171 ? 47.706  8.376   -13.855 1.00 22.60 ? 171 GLU C O   1 
ATOM   5729  C  CB  . GLU C  1 171 ? 47.758  9.960   -16.586 1.00 21.65 ? 171 GLU C CB  1 
ATOM   5730  C  CG  . GLU C  1 171 ? 47.267  10.792  -17.756 1.00 28.14 ? 171 GLU C CG  1 
ATOM   5731  C  CD  . GLU C  1 171 ? 48.223  11.927  -18.138 1.00 29.05 ? 171 GLU C CD  1 
ATOM   5732  O  OE1 . GLU C  1 171 ? 49.357  11.966  -17.615 1.00 31.23 ? 171 GLU C OE1 1 
ATOM   5733  O  OE2 . GLU C  1 171 ? 47.774  12.721  -19.005 1.00 37.82 ? 171 GLU C OE2 1 
ATOM   5734  N  N   . ALA C  1 172 ? 48.031  6.995   -15.634 1.00 19.08 ? 172 ALA C N   1 
ATOM   5735  C  CA  . ALA C  1 172 ? 48.907  6.048   -14.963 1.00 18.76 ? 172 ALA C CA  1 
ATOM   5736  C  C   . ALA C  1 172 ? 49.801  5.365   -15.884 1.00 27.22 ? 172 ALA C C   1 
ATOM   5737  O  O   . ALA C  1 172 ? 49.681  5.457   -17.093 1.00 28.93 ? 172 ALA C O   1 
ATOM   5738  C  CB  . ALA C  1 172 ? 48.119  4.988   -14.144 1.00 25.90 ? 172 ALA C CB  1 
ATOM   5739  N  N   . PHE C  1 173 ? 50.777  4.695   -15.366 1.00 25.03 ? 173 PHE C N   1 
ATOM   5740  C  CA  . PHE C  1 173 ? 51.636  3.917   -16.229 1.00 25.18 ? 173 PHE C CA  1 
ATOM   5741  C  C   . PHE C  1 173 ? 51.262  2.426   -16.071 1.00 28.27 ? 173 PHE C C   1 
ATOM   5742  O  O   . PHE C  1 173 ? 50.819  1.973   -14.994 1.00 25.89 ? 173 PHE C O   1 
ATOM   5743  C  CB  . PHE C  1 173 ? 53.106  4.265   -16.132 1.00 22.47 ? 173 PHE C CB  1 
ATOM   5744  C  CG  . PHE C  1 173 ? 53.490  5.645   -16.735 1.00 20.97 ? 173 PHE C CG  1 
ATOM   5745  C  CD1 . PHE C  1 173 ? 53.504  6.849   -15.971 1.00 21.72 ? 173 PHE C CD1 1 
ATOM   5746  C  CD2 . PHE C  1 173 ? 53.853  5.714   -18.095 1.00 23.35 ? 173 PHE C CD2 1 
ATOM   5747  C  CE1 . PHE C  1 173 ? 53.812  8.066   -16.582 1.00 22.99 ? 173 PHE C CE1 1 
ATOM   5748  C  CE2 . PHE C  1 173 ? 54.239  6.942   -18.705 1.00 24.74 ? 173 PHE C CE2 1 
ATOM   5749  C  CZ  . PHE C  1 173 ? 54.174  8.127   -17.935 1.00 22.67 ? 173 PHE C CZ  1 
ATOM   5750  N  N   . VAL C  1 174 ? 51.280  1.721   -17.188 1.00 25.09 ? 174 VAL C N   1 
ATOM   5751  C  CA  . VAL C  1 174 ? 51.061  0.256   -17.235 1.00 24.77 ? 174 VAL C CA  1 
ATOM   5752  C  C   . VAL C  1 174 ? 52.435  -0.277  -17.723 1.00 25.15 ? 174 VAL C C   1 
ATOM   5753  O  O   . VAL C  1 174 ? 52.936  0.203   -18.718 1.00 25.59 ? 174 VAL C O   1 
ATOM   5754  C  CB  . VAL C  1 174 ? 49.969  -0.121  -18.290 1.00 22.93 ? 174 VAL C CB  1 
ATOM   5755  C  CG1 . VAL C  1 174 ? 49.972  -1.629  -18.525 1.00 24.87 ? 174 VAL C CG1 1 
ATOM   5756  C  CG2 . VAL C  1 174 ? 48.611  0.330   -17.755 1.00 29.46 ? 174 VAL C CG2 1 
ATOM   5757  N  N   . PRO C  1 175 ? 53.036  -1.312  -17.043 1.00 24.02 ? 175 PRO C N   1 
ATOM   5758  C  CA  . PRO C  1 175 ? 54.249  -1.883  -17.668 1.00 22.08 ? 175 PRO C CA  1 
ATOM   5759  C  C   . PRO C  1 175 ? 54.010  -2.536  -19.023 1.00 22.60 ? 175 PRO C C   1 
ATOM   5760  O  O   . PRO C  1 175 ? 52.934  -3.013  -19.296 1.00 23.86 ? 175 PRO C O   1 
ATOM   5761  C  CB  . PRO C  1 175 ? 54.707  -2.975  -16.668 1.00 23.16 ? 175 PRO C CB  1 
ATOM   5762  C  CG  . PRO C  1 175 ? 53.800  -2.874  -15.495 1.00 24.68 ? 175 PRO C CG  1 
ATOM   5763  C  CD  . PRO C  1 175 ? 52.595  -2.033  -15.833 1.00 25.59 ? 175 PRO C CD  1 
ATOM   5764  N  N   . GLY C  1 176 ? 55.043  -2.653  -19.799 1.00 17.00 ? 176 GLY C N   1 
ATOM   5765  C  CA  . GLY C  1 176 ? 54.976  -3.195  -21.135 1.00 24.24 ? 176 GLY C CA  1 
ATOM   5766  C  C   . GLY C  1 176 ? 54.699  -4.656  -21.071 1.00 26.14 ? 176 GLY C C   1 
ATOM   5767  O  O   . GLY C  1 176 ? 54.934  -5.335  -20.051 1.00 24.28 ? 176 GLY C O   1 
ATOM   5768  N  N   . PHE C  1 177 ? 54.085  -5.135  -22.147 1.00 22.29 ? 177 PHE C N   1 
ATOM   5769  C  CA  . PHE C  1 177 ? 53.825  -6.596  -22.311 1.00 17.24 ? 177 PHE C CA  1 
ATOM   5770  C  C   . PHE C  1 177 ? 53.695  -6.776  -23.867 1.00 18.14 ? 177 PHE C C   1 
ATOM   5771  O  O   . PHE C  1 177 ? 53.700  -5.810  -24.643 1.00 18.23 ? 177 PHE C O   1 
ATOM   5772  C  CB  . PHE C  1 177 ? 52.592  -7.038  -21.522 1.00 21.47 ? 177 PHE C CB  1 
ATOM   5773  C  CG  . PHE C  1 177 ? 51.286  -6.410  -21.983 1.00 21.79 ? 177 PHE C CG  1 
ATOM   5774  C  CD1 . PHE C  1 177 ? 50.906  -5.121  -21.566 1.00 20.57 ? 177 PHE C CD1 1 
ATOM   5775  C  CD2 . PHE C  1 177 ? 50.425  -7.144  -22.778 1.00 21.57 ? 177 PHE C CD2 1 
ATOM   5776  C  CE1 . PHE C  1 177 ? 49.711  -4.547  -21.984 1.00 24.84 ? 177 PHE C CE1 1 
ATOM   5777  C  CE2 . PHE C  1 177 ? 49.234  -6.570  -23.217 1.00 20.70 ? 177 PHE C CE2 1 
ATOM   5778  C  CZ  . PHE C  1 177 ? 48.853  -5.311  -22.770 1.00 22.66 ? 177 PHE C CZ  1 
ATOM   5779  N  N   . ASN C  1 178 ? 53.593  -8.011  -24.335 1.00 16.59 ? 178 ASN C N   1 
ATOM   5780  C  CA  . ASN C  1 178 ? 53.406  -8.323  -25.734 1.00 15.63 ? 178 ASN C CA  1 
ATOM   5781  C  C   . ASN C  1 178 ? 51.935  -8.123  -26.183 1.00 15.37 ? 178 ASN C C   1 
ATOM   5782  O  O   . ASN C  1 178 ? 51.037  -8.840  -25.833 1.00 17.36 ? 178 ASN C O   1 
ATOM   5783  C  CB  . ASN C  1 178 ? 53.787  -9.785  -25.899 1.00 16.39 ? 178 ASN C CB  1 
ATOM   5784  C  CG  . ASN C  1 178 ? 53.749  -10.183 -27.325 1.00 18.74 ? 178 ASN C CG  1 
ATOM   5785  O  OD1 . ASN C  1 178 ? 53.503  -9.362  -28.267 1.00 19.93 ? 178 ASN C OD1 1 
ATOM   5786  N  ND2 . ASN C  1 178 ? 53.927  -11.469 -27.553 1.00 21.78 ? 178 ASN C ND2 1 
ATOM   5787  N  N   . ILE C  1 179 ? 51.784  -6.992  -26.918 1.00 14.85 ? 179 ILE C N   1 
ATOM   5788  C  CA  . ILE C  1 179 ? 50.428  -6.603  -27.323 1.00 14.96 ? 179 ILE C CA  1 
ATOM   5789  C  C   . ILE C  1 179 ? 49.806  -7.660  -28.198 1.00 15.60 ? 179 ILE C C   1 
ATOM   5790  O  O   . ILE C  1 179 ? 48.565  -7.756  -28.257 1.00 13.70 ? 179 ILE C O   1 
ATOM   5791  C  CB  . ILE C  1 179 ? 50.549  -5.204  -27.994 1.00 14.28 ? 179 ILE C CB  1 
ATOM   5792  C  CG1 . ILE C  1 179 ? 51.154  -4.123  -27.045 1.00 14.02 ? 179 ILE C CG1 1 
ATOM   5793  C  CG2 . ILE C  1 179 ? 49.200  -4.809  -28.501 1.00 15.06 ? 179 ILE C CG2 1 
ATOM   5794  C  CD1 . ILE C  1 179 ? 50.475  -3.889  -25.707 1.00 15.64 ? 179 ILE C CD1 1 
ATOM   5795  N  N   . GLU C  1 180 ? 50.595  -8.434  -28.892 1.00 15.25 ? 180 GLU C N   1 
ATOM   5796  C  CA  . GLU C  1 180 ? 50.063  -9.514  -29.732 1.00 16.53 ? 180 GLU C CA  1 
ATOM   5797  C  C   . GLU C  1 180 ? 49.263  -10.524 -28.921 1.00 19.11 ? 180 GLU C C   1 
ATOM   5798  O  O   . GLU C  1 180 ? 48.399  -11.206 -29.510 1.00 16.54 ? 180 GLU C O   1 
ATOM   5799  C  CB  . GLU C  1 180 ? 51.176  -10.138 -30.490 1.00 17.37 ? 180 GLU C CB  1 
ATOM   5800  C  CG  . GLU C  1 180 ? 50.639  -10.832 -31.740 1.00 20.54 ? 180 GLU C CG  1 
ATOM   5801  C  CD  . GLU C  1 180 ? 51.714  -11.426 -32.623 1.00 22.27 ? 180 GLU C CD  1 
ATOM   5802  O  OE1 . GLU C  1 180 ? 52.927  -11.224 -32.419 1.00 24.15 ? 180 GLU C OE1 1 
ATOM   5803  O  OE2 . GLU C  1 180 ? 51.241  -12.221 -33.482 1.00 25.98 ? 180 GLU C OE2 1 
ATOM   5804  N  N   . GLU C  1 181 ? 49.477  -10.602 -27.611 1.00 14.54 ? 181 GLU C N   1 
ATOM   5805  C  CA  . GLU C  1 181 ? 48.709  -11.510 -26.765 1.00 17.16 ? 181 GLU C CA  1 
ATOM   5806  C  C   . GLU C  1 181 ? 47.250  -11.075 -26.629 1.00 16.67 ? 181 GLU C C   1 
ATOM   5807  O  O   . GLU C  1 181 ? 46.426  -11.850 -26.181 1.00 18.43 ? 181 GLU C O   1 
ATOM   5808  C  CB  . GLU C  1 181 ? 49.267  -11.567 -25.334 1.00 19.43 ? 181 GLU C CB  1 
ATOM   5809  C  CG  . GLU C  1 181 ? 50.629  -12.260 -25.162 1.00 21.94 ? 181 GLU C CG  1 
ATOM   5810  C  CD  . GLU C  1 181 ? 51.243  -11.943 -23.768 1.00 22.74 ? 181 GLU C CD  1 
ATOM   5811  O  OE1 . GLU C  1 181 ? 50.540  -11.477 -22.820 1.00 23.50 ? 181 GLU C OE1 1 
ATOM   5812  O  OE2 . GLU C  1 181 ? 52.499  -12.097 -23.577 1.00 26.38 ? 181 GLU C OE2 1 
ATOM   5813  N  N   . LEU C  1 182 ? 46.940  -9.815  -27.034 1.00 13.06 ? 182 LEU C N   1 
ATOM   5814  C  CA  . LEU C  1 182 ? 45.528  -9.352  -27.046 1.00 13.75 ? 182 LEU C CA  1 
ATOM   5815  C  C   . LEU C  1 182 ? 44.740  -9.760  -28.265 1.00 12.81 ? 182 LEU C C   1 
ATOM   5816  O  O   . LEU C  1 182 ? 43.509  -9.644  -28.320 1.00 13.72 ? 182 LEU C O   1 
ATOM   5817  C  CB  . LEU C  1 182 ? 45.510  -7.814  -26.920 1.00 14.23 ? 182 LEU C CB  1 
ATOM   5818  C  CG  . LEU C  1 182 ? 46.174  -7.239  -25.697 1.00 13.39 ? 182 LEU C CG  1 
ATOM   5819  C  CD1 . LEU C  1 182 ? 46.134  -5.700  -25.692 1.00 13.69 ? 182 LEU C CD1 1 
ATOM   5820  C  CD2 . LEU C  1 182 ? 45.692  -7.743  -24.304 1.00 15.08 ? 182 LEU C CD2 1 
ATOM   5821  N  N   . LEU C  1 183 ? 45.444  -10.289 -29.269 1.00 13.97 ? 183 LEU C N   1 
ATOM   5822  C  CA  . LEU C  1 183 ? 44.836  -10.680 -30.549 1.00 14.28 ? 183 LEU C CA  1 
ATOM   5823  C  C   . LEU C  1 183 ? 44.249  -12.079 -30.409 1.00 14.91 ? 183 LEU C C   1 
ATOM   5824  O  O   . LEU C  1 183 ? 44.750  -12.934 -29.571 1.00 16.52 ? 183 LEU C O   1 
ATOM   5825  C  CB  . LEU C  1 183 ? 45.835  -10.617 -31.708 1.00 15.29 ? 183 LEU C CB  1 
ATOM   5826  C  CG  . LEU C  1 183 ? 46.484  -9.241  -31.854 1.00 15.01 ? 183 LEU C CG  1 
ATOM   5827  C  CD1 . LEU C  1 183 ? 47.334  -9.162  -33.113 1.00 18.25 ? 183 LEU C CD1 1 
ATOM   5828  C  CD2 . LEU C  1 183 ? 45.492  -8.138  -32.005 1.00 16.73 ? 183 LEU C CD2 1 
ATOM   5829  N  N   . PRO C  1 184 ? 43.207  -12.410 -31.167 1.00 13.91 ? 184 PRO C N   1 
ATOM   5830  C  CA  . PRO C  1 184 ? 42.614  -13.709 -31.101 1.00 15.78 ? 184 PRO C CA  1 
ATOM   5831  C  C   . PRO C  1 184 ? 43.402  -14.761 -31.869 1.00 19.40 ? 184 PRO C C   1 
ATOM   5832  O  O   . PRO C  1 184 ? 44.476  -14.508 -32.441 1.00 18.81 ? 184 PRO C O   1 
ATOM   5833  C  CB  . PRO C  1 184 ? 41.288  -13.513 -31.842 1.00 17.77 ? 184 PRO C CB  1 
ATOM   5834  C  CG  . PRO C  1 184 ? 41.610  -12.461 -32.857 1.00 16.61 ? 184 PRO C CG  1 
ATOM   5835  C  CD  . PRO C  1 184 ? 42.519  -11.522 -32.129 1.00 13.61 ? 184 PRO C CD  1 
ATOM   5836  N  N   . GLU C  1 185 ? 42.839  -15.983 -31.780 1.00 20.34 ? 185 GLU C N   1 
ATOM   5837  C  CA  . GLU C  1 185 ? 43.287  -17.077 -32.621 1.00 22.56 ? 185 GLU C CA  1 
ATOM   5838  C  C   . GLU C  1 185 ? 43.018  -16.821 -34.099 1.00 19.01 ? 185 GLU C C   1 
ATOM   5839  O  O   . GLU C  1 185 ? 41.978  -16.148 -34.509 1.00 20.46 ? 185 GLU C O   1 
ATOM   5840  C  CB  . GLU C  1 185 ? 42.577  -18.390 -32.234 1.00 26.29 ? 185 GLU C CB  1 
ATOM   5841  C  CG  . GLU C  1 185 ? 42.852  -18.782 -30.790 1.00 38.31 ? 185 GLU C CG  1 
ATOM   5842  C  CD  . GLU C  1 185 ? 44.246  -19.351 -30.571 1.00 49.85 ? 185 GLU C CD  1 
ATOM   5843  O  OE1 . GLU C  1 185 ? 45.250  -18.723 -31.000 1.00 58.22 ? 185 GLU C OE1 1 
ATOM   5844  O  OE2 . GLU C  1 185 ? 44.329  -20.443 -29.953 1.00 61.86 ? 185 GLU C OE2 1 
ATOM   5845  N  N   A ARG C  1 186 ? 43.830  -17.425 -34.977 0.50 19.18 ? 186 ARG C N   1 
ATOM   5846  N  N   B ARG C  1 186 ? 44.000  -17.263 -34.894 0.50 18.45 ? 186 ARG C N   1 
ATOM   5847  C  CA  A ARG C  1 186 ? 43.680  -17.311 -36.452 0.50 18.09 ? 186 ARG C CA  1 
ATOM   5848  C  CA  B ARG C  1 186 ? 43.920  -17.290 -36.370 0.50 17.57 ? 186 ARG C CA  1 
ATOM   5849  C  C   A ARG C  1 186 ? 43.564  -15.838 -36.915 0.50 17.00 ? 186 ARG C C   1 
ATOM   5850  C  C   B ARG C  1 186 ? 43.645  -15.905 -36.938 0.50 17.18 ? 186 ARG C C   1 
ATOM   5851  O  O   A ARG C  1 186 ? 42.599  -15.454 -37.579 0.50 17.65 ? 186 ARG C O   1 
ATOM   5852  O  O   B ARG C  1 186 ? 42.702  -15.664 -37.678 0.50 17.43 ? 186 ARG C O   1 
ATOM   5853  C  CB  A ARG C  1 186 ? 42.482  -18.123 -36.975 0.50 20.09 ? 186 ARG C CB  1 
ATOM   5854  C  CB  B ARG C  1 186 ? 42.944  -18.342 -36.818 0.50 19.35 ? 186 ARG C CB  1 
ATOM   5855  C  CG  A ARG C  1 186 ? 42.662  -19.646 -36.895 0.50 24.83 ? 186 ARG C CG  1 
ATOM   5856  C  CG  B ARG C  1 186 ? 43.373  -19.711 -36.272 0.50 21.24 ? 186 ARG C CG  1 
ATOM   5857  C  CD  A ARG C  1 186 ? 41.397  -20.473 -37.176 0.50 26.91 ? 186 ARG C CD  1 
ATOM   5858  C  CD  B ARG C  1 186 ? 42.377  -20.820 -36.638 0.50 22.76 ? 186 ARG C CD  1 
ATOM   5859  N  NE  A ARG C  1 186 ? 40.326  -20.293 -36.177 0.50 28.94 ? 186 ARG C NE  1 
ATOM   5860  N  NE  B ARG C  1 186 ? 41.257  -20.723 -35.703 0.50 25.66 ? 186 ARG C NE  1 
ATOM   5861  C  CZ  A ARG C  1 186 ? 39.077  -20.712 -36.323 0.50 29.38 ? 186 ARG C CZ  1 
ATOM   5862  C  CZ  B ARG C  1 186 ? 41.312  -21.083 -34.432 0.50 20.68 ? 186 ARG C CZ  1 
ATOM   5863  N  NH1 A ARG C  1 186 ? 38.747  -21.374 -37.438 0.50 31.87 ? 186 ARG C NH1 1 
ATOM   5864  N  NH1 B ARG C  1 186 ? 42.425  -21.600 -33.929 0.50 25.89 ? 186 ARG C NH1 1 
ATOM   5865  N  NH2 A ARG C  1 186 ? 38.169  -20.543 -35.345 0.50 25.10 ? 186 ARG C NH2 1 
ATOM   5866  N  NH2 B ARG C  1 186 ? 40.237  -20.906 -33.667 0.50 24.62 ? 186 ARG C NH2 1 
ATOM   5867  N  N   . THR C  1 187 ? 44.577  -15.041 -36.612 1.00 16.21 ? 187 THR C N   1 
ATOM   5868  C  CA  . THR C  1 187 ? 44.548  -13.651 -37.072 1.00 15.23 ? 187 THR C CA  1 
ATOM   5869  C  C   . THR C  1 187 ? 44.518  -13.558 -38.594 1.00 15.33 ? 187 THR C C   1 
ATOM   5870  O  O   . THR C  1 187 ? 44.165  -12.527 -39.135 1.00 14.43 ? 187 THR C O   1 
ATOM   5871  C  CB  . THR C  1 187 ? 45.660  -12.775 -36.511 1.00 14.96 ? 187 THR C CB  1 
ATOM   5872  O  OG1 . THR C  1 187 ? 46.890  -13.437 -36.710 1.00 19.20 ? 187 THR C OG1 1 
ATOM   5873  C  CG2 . THR C  1 187 ? 45.406  -12.529 -34.957 1.00 17.69 ? 187 THR C CG2 1 
ATOM   5874  N  N   . ALA C  1 188 ? 44.863  -14.660 -39.302 1.00 15.53 ? 188 ALA C N   1 
ATOM   5875  C  CA  . ALA C  1 188 ? 44.725  -14.633 -40.750 1.00 15.48 ? 188 ALA C CA  1 
ATOM   5876  C  C   . ALA C  1 188 ? 43.259  -14.491 -41.235 1.00 13.26 ? 188 ALA C C   1 
ATOM   5877  O  O   . ALA C  1 188 ? 43.082  -14.069 -42.415 1.00 13.51 ? 188 ALA C O   1 
ATOM   5878  C  CB  . ALA C  1 188 ? 45.397  -15.900 -41.400 1.00 18.35 ? 188 ALA C CB  1 
ATOM   5879  N  N   . GLU C  1 189 ? 42.271  -14.769 -40.391 1.00 14.14 ? 189 GLU C N   1 
ATOM   5880  C  CA  . GLU C  1 189 ? 40.869  -14.648 -40.718 1.00 14.82 ? 189 GLU C CA  1 
ATOM   5881  C  C   . GLU C  1 189 ? 40.319  -13.309 -40.231 1.00 12.24 ? 189 GLU C C   1 
ATOM   5882  O  O   . GLU C  1 189 ? 40.245  -13.076 -39.016 1.00 11.96 ? 189 GLU C O   1 
ATOM   5883  C  CB  . GLU C  1 189 ? 40.058  -15.731 -40.058 1.00 15.92 ? 189 GLU C CB  1 
ATOM   5884  C  CG  . GLU C  1 189 ? 40.533  -17.155 -40.516 1.00 20.80 ? 189 GLU C CG  1 
ATOM   5885  C  CD  . GLU C  1 189 ? 39.958  -18.292 -39.666 1.00 27.79 ? 189 GLU C CD  1 
ATOM   5886  O  OE1 . GLU C  1 189 ? 39.084  -18.145 -38.734 1.00 29.13 ? 189 GLU C OE1 1 
ATOM   5887  O  OE2 . GLU C  1 189 ? 40.467  -19.413 -39.881 1.00 34.69 ? 189 GLU C OE2 1 
ATOM   5888  N  N   . TYR C  1 190 ? 39.956  -12.468 -41.188 1.00 11.06 ? 190 TYR C N   1 
ATOM   5889  C  CA  . TYR C  1 190 ? 39.464  -11.120 -40.781 1.00 11.94 ? 190 TYR C CA  1 
ATOM   5890  C  C   . TYR C  1 190 ? 38.546  -10.573 -41.855 1.00 10.50 ? 190 TYR C C   1 
ATOM   5891  O  O   . TYR C  1 190 ? 38.551  -10.945 -43.014 1.00 12.03 ? 190 TYR C O   1 
ATOM   5892  C  CB  . TYR C  1 190 ? 40.683  -10.147 -40.499 1.00 11.52 ? 190 TYR C CB  1 
ATOM   5893  C  CG  . TYR C  1 190 ? 41.645  -9.991  -41.648 1.00 11.95 ? 190 TYR C CG  1 
ATOM   5894  C  CD1 . TYR C  1 190 ? 41.419  -9.053  -42.684 1.00 11.34 ? 190 TYR C CD1 1 
ATOM   5895  C  CD2 . TYR C  1 190 ? 42.838  -10.761 -41.700 1.00 11.91 ? 190 TYR C CD2 1 
ATOM   5896  C  CE1 . TYR C  1 190 ? 42.352  -8.853  -43.720 1.00 11.01 ? 190 TYR C CE1 1 
ATOM   5897  C  CE2 . TYR C  1 190 ? 43.731  -10.581 -42.774 1.00 11.65 ? 190 TYR C CE2 1 
ATOM   5898  C  CZ  . TYR C  1 190 ? 43.499  -9.638  -43.733 1.00 13.21 ? 190 TYR C CZ  1 
ATOM   5899  O  OH  . TYR C  1 190 ? 44.397  -9.356  -44.744 1.00 12.93 ? 190 TYR C OH  1 
ATOM   5900  N  N   . TYR C  1 191 ? 37.770  -9.561  -41.431 1.00 9.53  ? 191 TYR C N   1 
ATOM   5901  C  CA  . TYR C  1 191 ? 36.993  -8.690  -42.266 1.00 9.39  ? 191 TYR C CA  1 
ATOM   5902  C  C   . TYR C  1 191 ? 37.736  -7.407  -42.532 1.00 9.56  ? 191 TYR C C   1 
ATOM   5903  O  O   . TYR C  1 191 ? 38.429  -6.910  -41.634 1.00 10.14 ? 191 TYR C O   1 
ATOM   5904  C  CB  . TYR C  1 191 ? 35.695  -8.351  -41.504 1.00 10.12 ? 191 TYR C CB  1 
ATOM   5905  C  CG  . TYR C  1 191 ? 34.827  -9.433  -40.967 1.00 10.31 ? 191 TYR C CG  1 
ATOM   5906  C  CD1 . TYR C  1 191 ? 33.778  -9.991  -41.733 1.00 11.42 ? 191 TYR C CD1 1 
ATOM   5907  C  CD2 . TYR C  1 191 ? 35.019  -9.894  -39.619 1.00 10.72 ? 191 TYR C CD2 1 
ATOM   5908  C  CE1 . TYR C  1 191 ? 32.992  -10.981 -41.200 1.00 11.19 ? 191 TYR C CE1 1 
ATOM   5909  C  CE2 . TYR C  1 191 ? 34.162  -10.826 -39.051 1.00 11.68 ? 191 TYR C CE2 1 
ATOM   5910  C  CZ  . TYR C  1 191 ? 33.171  -11.344 -39.855 1.00 12.66 ? 191 TYR C CZ  1 
ATOM   5911  O  OH  . TYR C  1 191 ? 32.348  -12.347 -39.296 1.00 15.73 ? 191 TYR C OH  1 
ATOM   5912  N  N   . ARG C  1 192 ? 37.547  -6.795  -43.716 1.00 9.95  ? 192 ARG C N   1 
ATOM   5913  C  CA  . ARG C  1 192 ? 38.240  -5.561  -44.110 1.00 9.70  ? 192 ARG C CA  1 
ATOM   5914  C  C   . ARG C  1 192 ? 37.276  -4.634  -44.776 1.00 10.44 ? 192 ARG C C   1 
ATOM   5915  O  O   . ARG C  1 192 ? 36.546  -5.046  -45.729 1.00 10.02 ? 192 ARG C O   1 
ATOM   5916  C  CB  . ARG C  1 192 ? 39.325  -5.951  -45.080 1.00 10.60 ? 192 ARG C CB  1 
ATOM   5917  C  CG  . ARG C  1 192 ? 39.972  -4.795  -45.826 1.00 11.32 ? 192 ARG C CG  1 
ATOM   5918  C  CD  . ARG C  1 192 ? 40.792  -3.770  -44.980 1.00 11.27 ? 192 ARG C CD  1 
ATOM   5919  N  NE  . ARG C  1 192 ? 41.739  -4.426  -44.106 1.00 12.37 ? 192 ARG C NE  1 
ATOM   5920  C  CZ  . ARG C  1 192 ? 42.911  -4.974  -44.471 1.00 12.72 ? 192 ARG C CZ  1 
ATOM   5921  N  NH1 . ARG C  1 192 ? 43.305  -4.864  -45.767 1.00 13.79 ? 192 ARG C NH1 1 
ATOM   5922  N  NH2 . ARG C  1 192 ? 43.639  -5.575  -43.588 1.00 13.93 ? 192 ARG C NH2 1 
ATOM   5923  N  N   . TYR C  1 193 ? 37.249  -3.375  -44.367 1.00 8.93  ? 193 TYR C N   1 
ATOM   5924  C  CA  . TYR C  1 193 ? 36.507  -2.370  -45.152 1.00 8.48  ? 193 TYR C CA  1 
ATOM   5925  C  C   . TYR C  1 193 ? 37.086  -1.015  -44.876 1.00 7.57  ? 193 TYR C C   1 
ATOM   5926  O  O   . TYR C  1 193 ? 37.781  -0.813  -43.831 1.00 9.11  ? 193 TYR C O   1 
ATOM   5927  C  CB  . TYR C  1 193 ? 34.979  -2.433  -44.870 1.00 8.38  ? 193 TYR C CB  1 
ATOM   5928  C  CG  . TYR C  1 193 ? 34.580  -1.907  -43.502 1.00 8.30  ? 193 TYR C CG  1 
ATOM   5929  C  CD1 . TYR C  1 193 ? 34.753  -2.652  -42.369 1.00 7.73  ? 193 TYR C CD1 1 
ATOM   5930  C  CD2 . TYR C  1 193 ? 34.049  -0.627  -43.425 1.00 8.28  ? 193 TYR C CD2 1 
ATOM   5931  C  CE1 . TYR C  1 193 ? 34.403  -2.132  -41.094 1.00 7.73  ? 193 TYR C CE1 1 
ATOM   5932  C  CE2 . TYR C  1 193 ? 33.684  -0.099  -42.167 1.00 8.80  ? 193 TYR C CE2 1 
ATOM   5933  C  CZ  . TYR C  1 193 ? 33.888  -0.874  -41.017 1.00 7.49  ? 193 TYR C CZ  1 
ATOM   5934  O  OH  . TYR C  1 193 ? 33.553  -0.293  -39.801 1.00 8.65  ? 193 TYR C OH  1 
ATOM   5935  N  N   . ARG C  1 194 ? 36.738  -0.040  -45.695 1.00 9.58  ? 194 ARG C N   1 
ATOM   5936  C  CA  . ARG C  1 194 ? 37.181  1.344   -45.547 1.00 9.40  ? 194 ARG C CA  1 
ATOM   5937  C  C   . ARG C  1 194 ? 36.058  2.064   -44.747 1.00 10.67 ? 194 ARG C C   1 
ATOM   5938  O  O   . ARG C  1 194 ? 34.849  2.042   -45.155 1.00 10.74 ? 194 ARG C O   1 
ATOM   5939  C  CB  . ARG C  1 194 ? 37.245  2.057   -46.882 1.00 13.32 ? 194 ARG C CB  1 
ATOM   5940  C  CG  . ARG C  1 194 ? 38.442  1.494   -47.644 1.00 16.28 ? 194 ARG C CG  1 
ATOM   5941  C  CD  . ARG C  1 194 ? 39.012  2.316   -48.859 1.00 31.61 ? 194 ARG C CD  1 
ATOM   5942  N  NE  . ARG C  1 194 ? 40.281  1.621   -49.207 1.00 35.54 ? 194 ARG C NE  1 
ATOM   5943  C  CZ  . ARG C  1 194 ? 41.522  1.879   -48.757 1.00 46.97 ? 194 ARG C CZ  1 
ATOM   5944  N  NH1 . ARG C  1 194 ? 41.791  2.898   -47.947 1.00 40.47 ? 194 ARG C NH1 1 
ATOM   5945  N  NH2 . ARG C  1 194 ? 42.530  1.106   -49.159 1.00 45.71 ? 194 ARG C NH2 1 
ATOM   5946  N  N   . GLY C  1 195 ? 36.426  2.662   -43.616 1.00 9.34  ? 195 GLY C N   1 
ATOM   5947  C  CA  . GLY C  1 195 ? 35.422  3.366   -42.808 1.00 8.87  ? 195 GLY C CA  1 
ATOM   5948  C  C   . GLY C  1 195 ? 36.001  4.560   -42.123 1.00 8.87  ? 195 GLY C C   1 
ATOM   5949  O  O   . GLY C  1 195 ? 36.877  5.294   -42.665 1.00 9.32  ? 195 GLY C O   1 
ATOM   5950  N  N   . SER C  1 196 ? 35.518  4.786   -40.886 1.00 8.23  ? 196 SER C N   1 
ATOM   5951  C  CA  . SER C  1 196 ? 35.800  6.034   -40.192 1.00 7.71  ? 196 SER C CA  1 
ATOM   5952  C  C   . SER C  1 196 ? 36.251  5.772   -38.774 1.00 8.32  ? 196 SER C C   1 
ATOM   5953  O  O   . SER C  1 196 ? 36.108  4.652   -38.247 1.00 8.93  ? 196 SER C O   1 
ATOM   5954  C  CB  . SER C  1 196 ? 34.575  6.967   -40.178 1.00 8.08  ? 196 SER C CB  1 
ATOM   5955  O  OG  . SER C  1 196 ? 33.606  6.476   -39.245 1.00 8.49  ? 196 SER C OG  1 
ATOM   5956  N  N   . LEU C  1 197 ? 36.756  6.813   -38.143 1.00 9.02  ? 197 LEU C N   1 
ATOM   5957  C  CA  . LEU C  1 197 ? 36.764  6.769   -36.644 1.00 9.59  ? 197 LEU C CA  1 
ATOM   5958  C  C   . LEU C  1 197 ? 35.323  6.550   -36.163 1.00 8.52  ? 197 LEU C C   1 
ATOM   5959  O  O   . LEU C  1 197 ? 34.385  7.152   -36.696 1.00 9.09  ? 197 LEU C O   1 
ATOM   5960  C  CB  . LEU C  1 197 ? 37.294  8.083   -35.991 1.00 10.55 ? 197 LEU C CB  1 
ATOM   5961  C  CG  . LEU C  1 197 ? 38.801  8.393   -36.091 1.00 11.71 ? 197 LEU C CG  1 
ATOM   5962  C  CD1 . LEU C  1 197 ? 39.161  8.976   -37.431 1.00 12.88 ? 197 LEU C CD1 1 
ATOM   5963  C  CD2 . LEU C  1 197 ? 39.096  9.397   -35.004 1.00 13.21 ? 197 LEU C CD2 1 
ATOM   5964  N  N   . THR C  1 198 ? 35.177  5.801   -35.097 1.00 8.27  ? 198 THR C N   1 
ATOM   5965  C  CA  . THR C  1 198 ? 33.858  5.608   -34.486 1.00 8.07  ? 198 THR C CA  1 
ATOM   5966  C  C   . THR C  1 198 ? 33.529  6.637   -33.394 1.00 8.79  ? 198 THR C C   1 
ATOM   5967  O  O   . THR C  1 198 ? 32.460  6.613   -32.777 1.00 8.33  ? 198 THR C O   1 
ATOM   5968  C  CB  . THR C  1 198 ? 33.676  4.260   -33.892 1.00 8.48  ? 198 THR C CB  1 
ATOM   5969  O  OG1 . THR C  1 198 ? 34.601  4.158   -32.804 1.00 9.13  ? 198 THR C OG1 1 
ATOM   5970  C  CG2 . THR C  1 198 ? 33.908  3.102   -34.856 1.00 8.73  ? 198 THR C CG2 1 
ATOM   5971  N  N   . THR C  1 199 ? 34.472  7.559   -33.198 1.00 9.27  ? 199 THR C N   1 
ATOM   5972  C  CA  . THR C  1 199 ? 34.310  8.677   -32.283 1.00 8.73  ? 199 THR C CA  1 
ATOM   5973  C  C   . THR C  1 199 ? 34.512  9.955   -33.079 1.00 9.22  ? 199 THR C C   1 
ATOM   5974  O  O   . THR C  1 199 ? 35.249  9.927   -34.090 1.00 10.25 ? 199 THR C O   1 
ATOM   5975  C  CB  . THR C  1 199 ? 35.360  8.692   -31.145 1.00 9.29  ? 199 THR C CB  1 
ATOM   5976  O  OG1 . THR C  1 199 ? 36.678  8.803   -31.712 1.00 11.22 ? 199 THR C OG1 1 
ATOM   5977  C  CG2 . THR C  1 199 ? 35.354  7.315   -30.371 1.00 9.52  ? 199 THR C CG2 1 
ATOM   5978  N  N   . PRO C  1 200 ? 34.083  11.095  -32.489 1.00 8.96  ? 200 PRO C N   1 
ATOM   5979  C  CA  . PRO C  1 200 ? 34.495  12.380  -33.097 1.00 10.25 ? 200 PRO C CA  1 
ATOM   5980  C  C   . PRO C  1 200 ? 36.020  12.411  -33.228 1.00 11.32 ? 200 PRO C C   1 
ATOM   5981  O  O   . PRO C  1 200 ? 36.737  11.835  -32.384 1.00 11.79 ? 200 PRO C O   1 
ATOM   5982  C  CB  . PRO C  1 200 ? 34.060  13.389  -32.027 1.00 10.21 ? 200 PRO C CB  1 
ATOM   5983  C  CG  . PRO C  1 200 ? 32.743  12.770  -31.479 1.00 9.90  ? 200 PRO C CG  1 
ATOM   5984  C  CD  . PRO C  1 200 ? 33.126  11.313  -31.372 1.00 10.06 ? 200 PRO C CD  1 
ATOM   5985  N  N   . PRO C  1 201 ? 36.541  12.981  -34.292 1.00 10.11 ? 201 PRO C N   1 
ATOM   5986  C  CA  . PRO C  1 201 ? 35.788  13.700  -35.371 1.00 10.91 ? 201 PRO C CA  1 
ATOM   5987  C  C   . PRO C  1 201 ? 35.207  12.895  -36.523 1.00 9.86  ? 201 PRO C C   1 
ATOM   5988  O  O   . PRO C  1 201 ? 34.719  13.428  -37.470 1.00 10.65 ? 201 PRO C O   1 
ATOM   5989  C  CB  . PRO C  1 201 ? 36.806  14.711  -35.950 1.00 10.68 ? 201 PRO C CB  1 
ATOM   5990  C  CG  . PRO C  1 201 ? 37.968  14.668  -35.009 1.00 12.68 ? 201 PRO C CG  1 
ATOM   5991  C  CD  . PRO C  1 201 ? 37.996  13.215  -34.430 1.00 11.66 ? 201 PRO C CD  1 
ATOM   5992  N  N   . CYS C  1 202 ? 35.233  11.569  -36.384 1.00 9.73  ? 202 CYS C N   1 
ATOM   5993  C  CA  . CYS C  1 202 ? 34.569  10.643  -37.329 1.00 10.21 ? 202 CYS C CA  1 
ATOM   5994  C  C   . CYS C  1 202 ? 35.130  10.706  -38.698 1.00 9.87  ? 202 CYS C C   1 
ATOM   5995  O  O   . CYS C  1 202 ? 34.465  10.357  -39.640 1.00 10.18 ? 202 CYS C O   1 
ATOM   5996  C  CB  . CYS C  1 202 ? 33.033  10.878  -37.427 1.00 10.69 ? 202 CYS C CB  1 
ATOM   5997  S  SG  . CYS C  1 202 ? 32.151  10.799  -35.834 1.00 10.29 ? 202 CYS C SG  1 
ATOM   5998  N  N   . ASN C  1 203 ? 36.424  11.046  -38.820 1.00 10.45 ? 203 ASN C N   1 
ATOM   5999  C  CA  . ASN C  1 203 ? 36.974  11.160  -40.151 1.00 10.56 ? 203 ASN C CA  1 
ATOM   6000  C  C   . ASN C  1 203 ? 36.943  9.848   -40.936 1.00 9.77  ? 203 ASN C C   1 
ATOM   6001  O  O   . ASN C  1 203 ? 37.201  8.803   -40.337 1.00 9.72  ? 203 ASN C O   1 
ATOM   6002  C  CB  . ASN C  1 203 ? 38.455  11.665  -40.074 1.00 12.37 ? 203 ASN C CB  1 
ATOM   6003  C  CG  . ASN C  1 203 ? 38.599  12.855  -39.178 1.00 14.00 ? 203 ASN C CG  1 
ATOM   6004  O  OD1 . ASN C  1 203 ? 38.666  12.716  -37.971 1.00 15.22 ? 203 ASN C OD1 1 
ATOM   6005  N  ND2 . ASN C  1 203 ? 38.513  14.012  -39.768 1.00 16.37 ? 203 ASN C ND2 1 
ATOM   6006  N  N   . PRO C  1 204 ? 36.637  9.924   -42.245 1.00 9.45  ? 204 PRO C N   1 
ATOM   6007  C  CA  . PRO C  1 204 ? 36.481  8.672   -43.049 1.00 10.03 ? 204 PRO C CA  1 
ATOM   6008  C  C   . PRO C  1 204 ? 37.822  8.206   -43.600 1.00 10.34 ? 204 PRO C C   1 
ATOM   6009  O  O   . PRO C  1 204 ? 38.006  8.034   -44.840 1.00 12.11 ? 204 PRO C O   1 
ATOM   6010  C  CB  . PRO C  1 204 ? 35.559  9.128   -44.166 1.00 11.53 ? 204 PRO C CB  1 
ATOM   6011  C  CG  . PRO C  1 204 ? 35.892  10.593  -44.348 1.00 10.41 ? 204 PRO C CG  1 
ATOM   6012  C  CD  . PRO C  1 204 ? 36.145  11.148  -42.958 1.00 10.67 ? 204 PRO C CD  1 
ATOM   6013  N  N   . THR C  1 205 ? 38.735  7.972   -42.649 1.00 9.48  ? 205 THR C N   1 
ATOM   6014  C  CA  . THR C  1 205 ? 40.131  7.816   -42.985 1.00 10.70 ? 205 THR C CA  1 
ATOM   6015  C  C   . THR C  1 205 ? 40.709  6.555   -42.399 1.00 10.91 ? 205 THR C C   1 
ATOM   6016  O  O   . THR C  1 205 ? 41.959  6.340   -42.354 1.00 12.24 ? 205 THR C O   1 
ATOM   6017  C  CB  . THR C  1 205 ? 40.963  8.967   -42.409 1.00 10.13 ? 205 THR C CB  1 
ATOM   6018  O  OG1 . THR C  1 205 ? 40.711  9.011   -41.006 1.00 11.36 ? 205 THR C OG1 1 
ATOM   6019  C  CG2 . THR C  1 205 ? 40.577  10.321  -43.081 1.00 13.03 ? 205 THR C CG2 1 
ATOM   6020  N  N   . VAL C  1 206 ? 39.819  5.631   -41.975 1.00 9.89  ? 206 VAL C N   1 
ATOM   6021  C  CA  . VAL C  1 206 ? 40.290  4.389   -41.322 1.00 9.38  ? 206 VAL C CA  1 
ATOM   6022  C  C   . VAL C  1 206 ? 40.162  3.155   -42.198 1.00 9.47  ? 206 VAL C C   1 
ATOM   6023  O  O   . VAL C  1 206 ? 39.038  2.819   -42.680 1.00 11.34 ? 206 VAL C O   1 
ATOM   6024  C  CB  . VAL C  1 206 ? 39.472  4.137   -40.019 1.00 8.81  ? 206 VAL C CB  1 
ATOM   6025  C  CG1 . VAL C  1 206 ? 39.978  2.797   -39.375 1.00 9.66  ? 206 VAL C CG1 1 
ATOM   6026  C  CG2 . VAL C  1 206 ? 39.678  5.315   -39.042 1.00 9.89  ? 206 VAL C CG2 1 
ATOM   6027  N  N   . LEU C  1 207 ? 41.249  2.400   -42.366 1.00 9.07  ? 207 LEU C N   1 
ATOM   6028  C  CA  . LEU C  1 207 ? 41.184  1.051   -42.933 1.00 9.35  ? 207 LEU C CA  1 
ATOM   6029  C  C   . LEU C  1 207 ? 40.875  0.082   -41.818 1.00 9.12  ? 207 LEU C C   1 
ATOM   6030  O  O   . LEU C  1 207 ? 41.768  -0.098  -40.919 1.00 9.44  ? 207 LEU C O   1 
ATOM   6031  C  CB  . LEU C  1 207 ? 42.529  0.771   -43.667 1.00 11.39 ? 207 LEU C CB  1 
ATOM   6032  C  CG  . LEU C  1 207 ? 42.466  -0.519  -44.477 1.00 14.43 ? 207 LEU C CG  1 
ATOM   6033  C  CD1 . LEU C  1 207 ? 41.549  -0.329  -45.726 1.00 18.01 ? 207 LEU C CD1 1 
ATOM   6034  C  CD2 . LEU C  1 207 ? 43.885  -0.958  -44.902 1.00 21.49 ? 207 LEU C CD2 1 
ATOM   6035  N  N   . TRP C  1 208 ? 39.686  -0.514  -41.784 1.00 8.89  ? 208 TRP C N   1 
ATOM   6036  C  CA  . TRP C  1 208 ? 39.314  -1.405  -40.665 1.00 8.24  ? 208 TRP C CA  1 
ATOM   6037  C  C   . TRP C  1 208 ? 39.707  -2.839  -40.919 1.00 9.03  ? 208 TRP C C   1 
ATOM   6038  O  O   . TRP C  1 208 ? 39.507  -3.329  -42.078 1.00 9.50  ? 208 TRP C O   1 
ATOM   6039  C  CB  . TRP C  1 208 ? 37.771  -1.375  -40.504 1.00 8.27  ? 208 TRP C CB  1 
ATOM   6040  C  CG  . TRP C  1 208 ? 37.373  -0.138  -39.737 1.00 7.71  ? 208 TRP C CG  1 
ATOM   6041  C  CD1 . TRP C  1 208 ? 36.992  1.054   -40.174 1.00 7.69  ? 208 TRP C CD1 1 
ATOM   6042  C  CD2 . TRP C  1 208 ? 37.448  -0.022  -38.295 1.00 7.61  ? 208 TRP C CD2 1 
ATOM   6043  N  NE1 . TRP C  1 208 ? 36.783  1.927   -39.171 1.00 8.88  ? 208 TRP C NE1 1 
ATOM   6044  C  CE2 . TRP C  1 208 ? 37.077  1.296   -37.992 1.00 7.90  ? 208 TRP C CE2 1 
ATOM   6045  C  CE3 . TRP C  1 208 ? 37.778  -0.893  -37.252 1.00 9.44  ? 208 TRP C CE3 1 
ATOM   6046  C  CZ2 . TRP C  1 208 ? 37.052  1.811   -36.657 1.00 8.28  ? 208 TRP C CZ2 1 
ATOM   6047  C  CZ3 . TRP C  1 208 ? 37.727  -0.415  -35.908 1.00 9.58  ? 208 TRP C CZ3 1 
ATOM   6048  C  CH2 . TRP C  1 208 ? 37.376  0.933   -35.621 1.00 9.79  ? 208 TRP C CH2 1 
ATOM   6049  N  N   . THR C  1 209 ? 40.252  -3.505  -39.905 1.00 9.27  ? 209 THR C N   1 
ATOM   6050  C  CA  . THR C  1 209 ? 40.503  -4.927  -39.906 1.00 8.60  ? 209 THR C CA  1 
ATOM   6051  C  C   . THR C  1 209 ? 39.856  -5.444  -38.681 1.00 10.16 ? 209 THR C C   1 
ATOM   6052  O  O   . THR C  1 209 ? 40.297  -5.085  -37.558 1.00 10.80 ? 209 THR C O   1 
ATOM   6053  C  CB  . THR C  1 209 ? 42.016  -5.251  -39.867 1.00 8.87  ? 209 THR C CB  1 
ATOM   6054  O  OG1 . THR C  1 209 ? 42.595  -4.711  -41.075 1.00 10.07 ? 209 THR C OG1 1 
ATOM   6055  C  CG2 . THR C  1 209 ? 42.223  -6.781  -39.807 1.00 10.27 ? 209 THR C CG2 1 
ATOM   6056  N  N   . VAL C  1 210 ? 38.806  -6.236  -38.835 1.00 9.36  ? 210 VAL C N   1 
ATOM   6057  C  CA  . VAL C  1 210 ? 38.059  -6.811  -37.667 1.00 9.05  ? 210 VAL C CA  1 
ATOM   6058  C  C   . VAL C  1 210 ? 38.329  -8.282  -37.714 1.00 9.16  ? 210 VAL C C   1 
ATOM   6059  O  O   . VAL C  1 210 ? 38.010  -8.980  -38.681 1.00 10.13 ? 210 VAL C O   1 
ATOM   6060  C  CB  . VAL C  1 210 ? 36.542  -6.569  -37.751 1.00 8.74  ? 210 VAL C CB  1 
ATOM   6061  C  CG1 . VAL C  1 210 ? 35.833  -7.096  -36.504 1.00 10.27 ? 210 VAL C CG1 1 
ATOM   6062  C  CG2 . VAL C  1 210 ? 36.273  -5.078  -37.952 1.00 11.02 ? 210 VAL C CG2 1 
ATOM   6063  N  N   . PHE C  1 211 ? 38.979  -8.787  -36.658 1.00 9.64  ? 211 PHE C N   1 
ATOM   6064  C  CA  . PHE C  1 211 ? 39.288  -10.224 -36.767 1.00 10.28 ? 211 PHE C CA  1 
ATOM   6065  C  C   . PHE C  1 211 ? 38.012  -11.057 -36.635 1.00 10.59 ? 211 PHE C C   1 
ATOM   6066  O  O   . PHE C  1 211 ? 37.082  -10.700 -35.895 1.00 11.70 ? 211 PHE C O   1 
ATOM   6067  C  CB  . PHE C  1 211 ? 40.309  -10.608 -35.655 1.00 10.95 ? 211 PHE C CB  1 
ATOM   6068  C  CG  . PHE C  1 211 ? 41.670  -9.991  -35.872 1.00 10.22 ? 211 PHE C CG  1 
ATOM   6069  C  CD1 . PHE C  1 211 ? 42.490  -10.425 -36.901 1.00 12.17 ? 211 PHE C CD1 1 
ATOM   6070  C  CD2 . PHE C  1 211 ? 42.134  -8.932  -35.083 1.00 12.78 ? 211 PHE C CD2 1 
ATOM   6071  C  CE1 . PHE C  1 211 ? 43.716  -9.826  -37.154 1.00 12.24 ? 211 PHE C CE1 1 
ATOM   6072  C  CE2 . PHE C  1 211 ? 43.366  -8.321  -35.372 1.00 11.96 ? 211 PHE C CE2 1 
ATOM   6073  C  CZ  . PHE C  1 211 ? 44.145  -8.758  -36.361 1.00 12.43 ? 211 PHE C CZ  1 
ATOM   6074  N  N   A ARG C  1 212 ? 37.980  -12.197 -37.315 0.50 11.47 ? 212 ARG C N   1 
ATOM   6075  N  N   B ARG C  1 212 ? 37.988  -12.196 -37.319 0.50 11.22 ? 212 ARG C N   1 
ATOM   6076  C  CA  A ARG C  1 212 ? 36.824  -13.074 -37.309 0.50 12.58 ? 212 ARG C CA  1 
ATOM   6077  C  CA  B ARG C  1 212 ? 36.814  -13.042 -37.350 0.50 12.18 ? 212 ARG C CA  1 
ATOM   6078  C  C   A ARG C  1 212 ? 36.519  -13.633 -35.941 0.50 12.63 ? 212 ARG C C   1 
ATOM   6079  C  C   B ARG C  1 212 ? 36.521  -13.694 -36.015 0.50 12.53 ? 212 ARG C C   1 
ATOM   6080  O  O   A ARG C  1 212 ? 35.378  -13.703 -35.519 0.50 13.42 ? 212 ARG C O   1 
ATOM   6081  O  O   B ARG C  1 212 ? 35.369  -13.831 -35.672 0.50 13.53 ? 212 ARG C O   1 
ATOM   6082  C  CB  A ARG C  1 212 ? 37.087  -14.221 -38.247 0.50 13.90 ? 212 ARG C CB  1 
ATOM   6083  C  CB  B ARG C  1 212 ? 36.934  -14.055 -38.476 0.50 12.92 ? 212 ARG C CB  1 
ATOM   6084  C  CG  A ARG C  1 212 ? 35.883  -15.163 -38.374 0.50 15.46 ? 212 ARG C CG  1 
ATOM   6085  C  CG  B ARG C  1 212 ? 35.676  -14.925 -38.717 0.50 12.83 ? 212 ARG C CG  1 
ATOM   6086  C  CD  A ARG C  1 212 ? 36.348  -16.462 -39.023 0.50 18.56 ? 212 ARG C CD  1 
ATOM   6087  C  CD  B ARG C  1 212 ? 36.092  -16.121 -39.543 0.50 16.32 ? 212 ARG C CD  1 
ATOM   6088  N  NE  A ARG C  1 212 ? 35.270  -17.442 -39.181 0.50 19.71 ? 212 ARG C NE  1 
ATOM   6089  N  NE  B ARG C  1 212 ? 34.908  -16.780 -40.069 0.50 18.25 ? 212 ARG C NE  1 
ATOM   6090  C  CZ  A ARG C  1 212 ? 35.059  -18.490 -38.379 0.50 23.08 ? 212 ARG C CZ  1 
ATOM   6091  C  CZ  B ARG C  1 212 ? 34.945  -17.896 -40.785 0.50 18.52 ? 212 ARG C CZ  1 
ATOM   6092  N  NH1 A ARG C  1 212 ? 35.865  -18.793 -37.365 0.50 24.24 ? 212 ARG C NH1 1 
ATOM   6093  N  NH1 B ARG C  1 212 ? 36.114  -18.502 -41.020 0.50 21.71 ? 212 ARG C NH1 1 
ATOM   6094  N  NH2 A ARG C  1 212 ? 34.039  -19.295 -38.637 0.50 23.06 ? 212 ARG C NH2 1 
ATOM   6095  N  NH2 B ARG C  1 212 ? 33.801  -18.393 -41.265 0.50 18.01 ? 212 ARG C NH2 1 
ATOM   6096  N  N   . ASN C  1 213 ? 37.566  -14.085 -35.260 1.00 13.17 ? 213 ASN C N   1 
ATOM   6097  C  CA  . ASN C  1 213 ? 37.364  -14.824 -33.992 1.00 14.16 ? 213 ASN C CA  1 
ATOM   6098  C  C   . ASN C  1 213 ? 37.494  -13.891 -32.803 1.00 13.80 ? 213 ASN C C   1 
ATOM   6099  O  O   . ASN C  1 213 ? 38.419  -13.089 -32.742 1.00 14.16 ? 213 ASN C O   1 
ATOM   6100  C  CB  . ASN C  1 213 ? 38.442  -15.935 -33.900 1.00 15.28 ? 213 ASN C CB  1 
ATOM   6101  C  CG  . ASN C  1 213 ? 38.404  -16.853 -35.085 1.00 16.62 ? 213 ASN C CG  1 
ATOM   6102  O  OD1 . ASN C  1 213 ? 39.440  -17.041 -35.750 1.00 21.99 ? 213 ASN C OD1 1 
ATOM   6103  N  ND2 . ASN C  1 213 ? 37.235  -17.371 -35.446 1.00 19.28 ? 213 ASN C ND2 1 
ATOM   6104  N  N   . PRO C  1 214 ? 36.620  -14.054 -31.811 1.00 13.33 ? 214 PRO C N   1 
ATOM   6105  C  CA  . PRO C  1 214 ? 36.674  -13.223 -30.650 1.00 14.08 ? 214 PRO C CA  1 
ATOM   6106  C  C   . PRO C  1 214 ? 37.703  -13.755 -29.649 1.00 14.97 ? 214 PRO C C   1 
ATOM   6107  O  O   . PRO C  1 214 ? 38.162  -14.902 -29.841 1.00 16.74 ? 214 PRO C O   1 
ATOM   6108  C  CB  . PRO C  1 214 ? 35.288  -13.378 -30.029 1.00 16.57 ? 214 PRO C CB  1 
ATOM   6109  C  CG  . PRO C  1 214 ? 34.954  -14.800 -30.378 1.00 17.18 ? 214 PRO C CG  1 
ATOM   6110  C  CD  . PRO C  1 214 ? 35.447  -14.977 -31.799 1.00 17.00 ? 214 PRO C CD  1 
ATOM   6111  N  N   . VAL C  1 215 ? 38.132  -12.916 -28.707 1.00 12.67 ? 215 VAL C N   1 
ATOM   6112  C  CA  . VAL C  1 215 ? 38.857  -13.350 -27.489 1.00 13.62 ? 215 VAL C CA  1 
ATOM   6113  C  C   . VAL C  1 215 ? 37.865  -13.429 -26.367 1.00 15.03 ? 215 VAL C C   1 
ATOM   6114  O  O   . VAL C  1 215 ? 36.718  -12.918 -26.477 1.00 15.16 ? 215 VAL C O   1 
ATOM   6115  C  CB  . VAL C  1 215 ? 39.962  -12.399 -27.106 1.00 16.22 ? 215 VAL C CB  1 
ATOM   6116  C  CG1 . VAL C  1 215 ? 41.060  -12.396 -28.201 1.00 16.16 ? 215 VAL C CG1 1 
ATOM   6117  C  CG2 . VAL C  1 215 ? 39.491  -11.019 -26.701 1.00 14.54 ? 215 VAL C CG2 1 
ATOM   6118  N  N   . GLN C  1 216 ? 38.249  -14.087 -25.269 1.00 16.77 ? 216 GLN C N   1 
ATOM   6119  C  CA  . GLN C  1 216 ? 37.426  -14.241 -24.060 1.00 16.58 ? 216 GLN C CA  1 
ATOM   6120  C  C   . GLN C  1 216 ? 38.094  -13.573 -22.913 1.00 16.75 ? 216 GLN C C   1 
ATOM   6121  O  O   . GLN C  1 216 ? 39.351  -13.581 -22.784 1.00 17.06 ? 216 GLN C O   1 
ATOM   6122  C  CB  . GLN C  1 216 ? 37.271  -15.727 -23.716 1.00 19.31 ? 216 GLN C CB  1 
ATOM   6123  C  CG  . GLN C  1 216 ? 36.581  -16.482 -24.827 1.00 22.22 ? 216 GLN C CG  1 
ATOM   6124  C  CD  . GLN C  1 216 ? 35.938  -17.717 -24.278 1.00 29.48 ? 216 GLN C CD  1 
ATOM   6125  O  OE1 . GLN C  1 216 ? 36.429  -18.307 -23.252 1.00 29.24 ? 216 GLN C OE1 1 
ATOM   6126  N  NE2 . GLN C  1 216 ? 34.793  -18.088 -24.875 1.00 32.15 ? 216 GLN C NE2 1 
ATOM   6127  N  N   . ILE C  1 217 ? 37.289  -12.932 -22.076 1.00 18.19 ? 217 ILE C N   1 
ATOM   6128  C  CA  . ILE C  1 217 ? 37.699  -12.421 -20.792 1.00 17.35 ? 217 ILE C CA  1 
ATOM   6129  C  C   . ILE C  1 217 ? 36.676  -12.974 -19.781 1.00 17.20 ? 217 ILE C C   1 
ATOM   6130  O  O   . ILE C  1 217 ? 35.555  -13.351 -20.154 1.00 17.03 ? 217 ILE C O   1 
ATOM   6131  C  CB  . ILE C  1 217 ? 37.826  -10.866 -20.688 1.00 17.18 ? 217 ILE C CB  1 
ATOM   6132  C  CG1 . ILE C  1 217 ? 36.477  -10.154 -20.940 1.00 15.27 ? 217 ILE C CG1 1 
ATOM   6133  C  CG2 . ILE C  1 217 ? 38.900  -10.413 -21.700 1.00 16.70 ? 217 ILE C CG2 1 
ATOM   6134  C  CD1 . ILE C  1 217 ? 36.437  -8.637  -20.690 1.00 16.83 ? 217 ILE C CD1 1 
ATOM   6135  N  N   . SER C  1 218 ? 37.063  -13.080 -18.502 1.00 19.79 ? 218 SER C N   1 
ATOM   6136  C  CA  . SER C  1 218 ? 36.071  -13.676 -17.558 1.00 21.43 ? 218 SER C CA  1 
ATOM   6137  C  C   . SER C  1 218 ? 34.950  -12.710 -17.250 1.00 22.40 ? 218 SER C C   1 
ATOM   6138  O  O   . SER C  1 218 ? 35.071  -11.458 -17.469 1.00 21.40 ? 218 SER C O   1 
ATOM   6139  C  CB  . SER C  1 218 ? 36.806  -14.048 -16.241 1.00 17.87 ? 218 SER C CB  1 
ATOM   6140  O  OG  . SER C  1 218 ? 37.233  -12.877 -15.554 1.00 20.72 ? 218 SER C OG  1 
ATOM   6141  N  N   . GLN C  1 219 ? 33.842  -13.229 -16.672 1.00 22.62 ? 219 GLN C N   1 
ATOM   6142  C  CA  . GLN C  1 219 ? 32.821  -12.369 -16.137 1.00 23.53 ? 219 GLN C CA  1 
ATOM   6143  C  C   . GLN C  1 219 ? 33.288  -11.310 -15.202 1.00 20.02 ? 219 GLN C C   1 
ATOM   6144  O  O   . GLN C  1 219 ? 32.823  -10.199 -15.233 1.00 20.52 ? 219 GLN C O   1 
ATOM   6145  C  CB  . GLN C  1 219 ? 31.791  -13.159 -15.337 1.00 31.08 ? 219 GLN C CB  1 
ATOM   6146  C  CG  . GLN C  1 219 ? 30.939  -14.108 -16.104 1.00 41.04 ? 219 GLN C CG  1 
ATOM   6147  C  CD  . GLN C  1 219 ? 29.738  -14.575 -15.286 1.00 60.35 ? 219 GLN C CD  1 
ATOM   6148  O  OE1 . GLN C  1 219 ? 29.891  -15.108 -14.159 1.00 67.10 ? 219 GLN C OE1 1 
ATOM   6149  N  NE2 . GLN C  1 219 ? 28.528  -14.370 -15.845 1.00 51.36 ? 219 GLN C NE2 1 
ATOM   6150  N  N   . GLU C  1 220 ? 34.259  -11.671 -14.343 1.00 23.08 ? 220 GLU C N   1 
ATOM   6151  C  CA  . GLU C  1 220 ? 34.832  -10.730 -13.392 1.00 22.39 ? 220 GLU C CA  1 
ATOM   6152  C  C   . GLU C  1 220 ? 35.593  -9.639  -14.075 1.00 17.77 ? 220 GLU C C   1 
ATOM   6153  O  O   . GLU C  1 220 ? 35.471  -8.503  -13.693 1.00 21.10 ? 220 GLU C O   1 
ATOM   6154  C  CB  . GLU C  1 220 ? 35.664  -11.388 -12.260 1.00 28.39 ? 220 GLU C CB  1 
ATOM   6155  C  CG  . GLU C  1 220 ? 35.059  -12.679 -11.662 1.00 34.61 ? 220 GLU C CG  1 
ATOM   6156  C  CD  . GLU C  1 220 ? 35.304  -14.015 -12.447 1.00 42.19 ? 220 GLU C CD  1 
ATOM   6157  O  OE1 . GLU C  1 220 ? 34.688  -14.318 -13.506 1.00 38.63 ? 220 GLU C OE1 1 
ATOM   6158  O  OE2 . GLU C  1 220 ? 36.110  -14.841 -11.952 1.00 55.17 ? 220 GLU C OE2 1 
ATOM   6159  N  N   . GLN C  1 221 ? 36.349  -10.005 -15.115 1.00 20.96 ? 221 GLN C N   1 
ATOM   6160  C  CA  . GLN C  1 221 ? 37.098  -9.003  -15.882 1.00 18.47 ? 221 GLN C CA  1 
ATOM   6161  C  C   . GLN C  1 221 ? 36.163  -8.039  -16.654 1.00 13.65 ? 221 GLN C C   1 
ATOM   6162  O  O   . GLN C  1 221 ? 36.359  -6.805  -16.576 1.00 15.98 ? 221 GLN C O   1 
ATOM   6163  C  CB  . GLN C  1 221 ? 38.106  -9.582  -16.802 1.00 18.78 ? 221 GLN C CB  1 
ATOM   6164  C  CG  . GLN C  1 221 ? 39.232  -10.392 -16.150 1.00 16.80 ? 221 GLN C CG  1 
ATOM   6165  C  CD  . GLN C  1 221 ? 40.103  -10.947 -17.224 1.00 17.61 ? 221 GLN C CD  1 
ATOM   6166  O  OE1 . GLN C  1 221 ? 39.693  -11.877 -17.924 1.00 17.20 ? 221 GLN C OE1 1 
ATOM   6167  N  NE2 . GLN C  1 221 ? 41.289  -10.430 -17.333 1.00 19.05 ? 221 GLN C NE2 1 
ATOM   6168  N  N   . LEU C  1 222 ? 35.117  -8.602  -17.238 1.00 17.64 ? 222 LEU C N   1 
ATOM   6169  C  CA  . LEU C  1 222 ? 34.097  -7.768  -17.886 1.00 16.71 ? 222 LEU C CA  1 
ATOM   6170  C  C   . LEU C  1 222 ? 33.387  -6.814  -16.976 1.00 17.96 ? 222 LEU C C   1 
ATOM   6171  O  O   . LEU C  1 222 ? 33.305  -5.632  -17.251 1.00 15.95 ? 222 LEU C O   1 
ATOM   6172  C  CB  . LEU C  1 222 ? 33.133  -8.647  -18.621 1.00 17.46 ? 222 LEU C CB  1 
ATOM   6173  C  CG  . LEU C  1 222 ? 32.074  -7.908  -19.417 1.00 16.27 ? 222 LEU C CG  1 
ATOM   6174  C  CD1 . LEU C  1 222 ? 32.634  -6.944  -20.483 1.00 17.48 ? 222 LEU C CD1 1 
ATOM   6175  C  CD2 . LEU C  1 222 ? 31.173  -8.972  -20.069 1.00 18.43 ? 222 LEU C CD2 1 
ATOM   6176  N  N   . LEU C  1 223 ? 32.967  -7.301  -15.768 1.00 18.56 ? 223 LEU C N   1 
ATOM   6177  C  CA  . LEU C  1 223 ? 32.361  -6.458  -14.766 1.00 19.01 ? 223 LEU C CA  1 
ATOM   6178  C  C   . LEU C  1 223 ? 33.253  -5.390  -14.307 1.00 16.40 ? 223 LEU C C   1 
ATOM   6179  O  O   . LEU C  1 223 ? 32.847  -4.254  -14.128 1.00 16.85 ? 223 LEU C O   1 
ATOM   6180  C  CB  . LEU C  1 223 ? 31.917  -7.310  -13.581 1.00 22.70 ? 223 LEU C CB  1 
ATOM   6181  C  CG  . LEU C  1 223 ? 31.017  -6.558  -12.623 1.00 24.58 ? 223 LEU C CG  1 
ATOM   6182  C  CD1 . LEU C  1 223 ? 29.757  -5.981  -13.236 1.00 23.53 ? 223 LEU C CD1 1 
ATOM   6183  C  CD2 . LEU C  1 223 ? 30.679  -7.496  -11.429 1.00 24.48 ? 223 LEU C CD2 1 
ATOM   6184  N  N   . ALA C  1 224 ? 34.505  -5.744  -14.042 1.00 18.59 ? 224 ALA C N   1 
ATOM   6185  C  CA  . ALA C  1 224 ? 35.568  -4.744  -13.711 1.00 20.92 ? 224 ALA C CA  1 
ATOM   6186  C  C   . ALA C  1 224 ? 35.657  -3.579  -14.693 1.00 19.20 ? 224 ALA C C   1 
ATOM   6187  O  O   . ALA C  1 224 ? 35.588  -2.376  -14.359 1.00 20.75 ? 224 ALA C O   1 
ATOM   6188  C  CB  . ALA C  1 224 ? 36.974  -5.425  -13.500 1.00 22.66 ? 224 ALA C CB  1 
ATOM   6189  N  N   . LEU C  1 225 ? 35.768  -3.938  -15.994 1.00 20.52 ? 225 LEU C N   1 
ATOM   6190  C  CA  . LEU C  1 225 ? 35.918  -2.903  -17.017 1.00 17.80 ? 225 LEU C CA  1 
ATOM   6191  C  C   . LEU C  1 225 ? 34.639  -2.050  -17.078 1.00 15.05 ? 225 LEU C C   1 
ATOM   6192  O  O   . LEU C  1 225 ? 34.742  -0.855  -17.213 1.00 18.28 ? 225 LEU C O   1 
ATOM   6193  C  CB  . LEU C  1 225 ? 36.056  -3.629  -18.393 1.00 16.21 ? 225 LEU C CB  1 
ATOM   6194  C  CG  . LEU C  1 225 ? 36.100  -2.705  -19.624 1.00 15.36 ? 225 LEU C CG  1 
ATOM   6195  C  CD1 . LEU C  1 225 ? 37.336  -1.819  -19.519 1.00 16.32 ? 225 LEU C CD1 1 
ATOM   6196  C  CD2 . LEU C  1 225 ? 36.112  -3.578  -20.848 1.00 15.70 ? 225 LEU C CD2 1 
ATOM   6197  N  N   . GLU C  1 226 ? 33.464  -2.692  -16.950 1.00 16.55 ? 226 GLU C N   1 
ATOM   6198  C  CA  . GLU C  1 226 ? 32.203  -1.926  -16.966 1.00 16.60 ? 226 GLU C CA  1 
ATOM   6199  C  C   . GLU C  1 226 ? 31.914  -1.044  -15.767 1.00 19.89 ? 226 GLU C C   1 
ATOM   6200  O  O   . GLU C  1 226 ? 31.167  -0.077  -15.886 1.00 21.17 ? 226 GLU C O   1 
ATOM   6201  C  CB  . GLU C  1 226 ? 30.990  -2.857  -17.090 1.00 18.11 ? 226 GLU C CB  1 
ATOM   6202  C  CG  . GLU C  1 226 ? 30.968  -3.671  -18.411 1.00 16.57 ? 226 GLU C CG  1 
ATOM   6203  C  CD  . GLU C  1 226 ? 30.060  -4.892  -18.327 1.00 17.15 ? 226 GLU C CD  1 
ATOM   6204  O  OE1 . GLU C  1 226 ? 29.734  -5.387  -17.230 1.00 19.31 ? 226 GLU C OE1 1 
ATOM   6205  O  OE2 . GLU C  1 226 ? 29.637  -5.381  -19.389 1.00 17.73 ? 226 GLU C OE2 1 
ATOM   6206  N  N   . THR C  1 227 ? 32.611  -1.315  -14.671 1.00 19.53 ? 227 THR C N   1 
ATOM   6207  C  CA  . THR C  1 227 ? 32.285  -0.616  -13.416 1.00 19.06 ? 227 THR C CA  1 
ATOM   6208  C  C   . THR C  1 227 ? 33.430  0.197   -12.862 1.00 20.66 ? 227 THR C C   1 
ATOM   6209  O  O   . THR C  1 227 ? 33.239  0.828   -11.837 1.00 23.44 ? 227 THR C O   1 
ATOM   6210  C  CB  . THR C  1 227 ? 31.752  -1.614  -12.319 1.00 19.59 ? 227 THR C CB  1 
ATOM   6211  O  OG1 . THR C  1 227 ? 32.784  -2.555  -12.043 1.00 22.35 ? 227 THR C OG1 1 
ATOM   6212  C  CG2 . THR C  1 227 ? 30.331  -2.220  -12.737 1.00 22.76 ? 227 THR C CG2 1 
ATOM   6213  N  N   . ALA C  1 228 ? 34.590  0.173   -13.512 1.00 18.11 ? 228 ALA C N   1 
ATOM   6214  C  CA  . ALA C  1 228 ? 35.780  0.799   -12.898 1.00 19.34 ? 228 ALA C CA  1 
ATOM   6215  C  C   . ALA C  1 228 ? 35.843  2.281   -13.086 1.00 20.75 ? 228 ALA C C   1 
ATOM   6216  O  O   . ALA C  1 228 ? 36.445  2.991   -12.276 1.00 20.87 ? 228 ALA C O   1 
ATOM   6217  C  CB  . ALA C  1 228 ? 37.078  0.141   -13.363 1.00 21.22 ? 228 ALA C CB  1 
ATOM   6218  N  N   . LEU C  1 229 ? 35.271  2.828   -14.169 1.00 16.60 ? 229 LEU C N   1 
ATOM   6219  C  CA  . LEU C  1 229 ? 35.583  4.209   -14.574 1.00 16.10 ? 229 LEU C CA  1 
ATOM   6220  C  C   . LEU C  1 229 ? 34.421  5.137   -14.632 1.00 18.94 ? 229 LEU C C   1 
ATOM   6221  O  O   . LEU C  1 229 ? 33.269  4.776   -14.826 1.00 17.28 ? 229 LEU C O   1 
ATOM   6222  C  CB  . LEU C  1 229 ? 36.246  4.230   -15.970 1.00 16.20 ? 229 LEU C CB  1 
ATOM   6223  C  CG  . LEU C  1 229 ? 37.342  3.196   -16.148 1.00 16.31 ? 229 LEU C CG  1 
ATOM   6224  C  CD1 . LEU C  1 229 ? 37.918  3.258   -17.596 1.00 19.83 ? 229 LEU C CD1 1 
ATOM   6225  C  CD2 . LEU C  1 229 ? 38.496  3.437   -15.204 1.00 14.29 ? 229 LEU C CD2 1 
ATOM   6226  N  N   . TYR C  1 230 ? 34.734  6.381   -14.364 1.00 21.80 ? 230 TYR C N   1 
ATOM   6227  C  CA  . TYR C  1 230 ? 33.799  7.443   -14.523 1.00 21.92 ? 230 TYR C CA  1 
ATOM   6228  C  C   . TYR C  1 230 ? 34.197  8.252   -15.734 1.00 21.50 ? 230 TYR C C   1 
ATOM   6229  O  O   . TYR C  1 230 ? 35.357  8.360   -16.092 1.00 23.10 ? 230 TYR C O   1 
ATOM   6230  C  CB  . TYR C  1 230 ? 33.847  8.387   -13.271 1.00 20.51 ? 230 TYR C CB  1 
ATOM   6231  C  CG  . TYR C  1 230 ? 33.300  7.779   -11.973 1.00 25.45 ? 230 TYR C CG  1 
ATOM   6232  C  CD1 . TYR C  1 230 ? 31.906  7.670   -11.698 1.00 27.88 ? 230 TYR C CD1 1 
ATOM   6233  C  CD2 . TYR C  1 230 ? 34.197  7.434   -10.948 1.00 31.58 ? 230 TYR C CD2 1 
ATOM   6234  C  CE1 . TYR C  1 230 ? 31.454  7.168   -10.461 1.00 31.98 ? 230 TYR C CE1 1 
ATOM   6235  C  CE2 . TYR C  1 230 ? 33.747  6.982   -9.685  1.00 30.00 ? 230 TYR C CE2 1 
ATOM   6236  C  CZ  . TYR C  1 230 ? 32.389  6.826   -9.462  1.00 33.39 ? 230 TYR C CZ  1 
ATOM   6237  O  OH  . TYR C  1 230 ? 32.021  6.342   -8.211  1.00 42.72 ? 230 TYR C OH  1 
ATOM   6238  N  N   A CYS C  1 231 ? 33.252  8.943   -16.376 0.50 21.70 ? 231 CYS C N   1 
ATOM   6239  N  N   B CYS C  1 231 ? 33.181  8.871   -16.330 0.50 21.77 ? 231 CYS C N   1 
ATOM   6240  C  CA  A CYS C  1 231 ? 33.638  9.886   -17.429 0.50 24.08 ? 231 CYS C CA  1 
ATOM   6241  C  CA  B CYS C  1 231 ? 33.402  9.770   -17.426 0.50 23.72 ? 231 CYS C CA  1 
ATOM   6242  C  C   A CYS C  1 231 ? 34.051  11.228  -16.887 0.50 26.62 ? 231 CYS C C   1 
ATOM   6243  C  C   B CYS C  1 231 ? 33.471  11.257  -16.979 0.50 24.30 ? 231 CYS C C   1 
ATOM   6244  O  O   A CYS C  1 231 ? 34.683  12.043  -17.586 0.50 25.21 ? 231 CYS C O   1 
ATOM   6245  O  O   B CYS C  1 231 ? 33.504  12.151  -17.791 0.50 21.90 ? 231 CYS C O   1 
ATOM   6246  C  CB  A CYS C  1 231 ? 32.453  10.235  -18.302 0.50 21.42 ? 231 CYS C CB  1 
ATOM   6247  C  CB  B CYS C  1 231 ? 32.359  9.534   -18.527 0.50 23.75 ? 231 CYS C CB  1 
ATOM   6248  S  SG  A CYS C  1 231 ? 32.017  8.967   -19.443 0.50 18.55 ? 231 CYS C SG  1 
ATOM   6249  S  SG  B CYS C  1 231 ? 30.645  9.782   -18.053 0.50 23.50 ? 231 CYS C SG  1 
ATOM   6250  N  N   . THR C  1 232 ? 33.572  11.481  -15.666 1.00 24.86 ? 232 THR C N   1 
ATOM   6251  C  CA  . THR C  1 232 ? 33.624  12.815  -15.055 1.00 24.58 ? 232 THR C CA  1 
ATOM   6252  C  C   . THR C  1 232 ? 34.939  13.003  -14.281 1.00 25.14 ? 232 THR C C   1 
ATOM   6253  O  O   . THR C  1 232 ? 35.606  12.021  -13.905 1.00 22.73 ? 232 THR C O   1 
ATOM   6254  C  CB  . THR C  1 232 ? 32.365  13.023  -14.183 1.00 23.27 ? 232 THR C CB  1 
ATOM   6255  O  OG1 . THR C  1 232 ? 32.120  11.830  -13.401 1.00 23.93 ? 232 THR C OG1 1 
ATOM   6256  C  CG2 . THR C  1 232 ? 31.133  13.273  -15.068 1.00 26.06 ? 232 THR C CG2 1 
ATOM   6257  N  N   . HIS C  1 233 ? 35.321  14.278  -14.038 1.00 25.08 ? 233 HIS C N   1 
ATOM   6258  C  CA  . HIS C  1 233 ? 36.491  14.592  -13.206 1.00 27.68 ? 233 HIS C CA  1 
ATOM   6259  C  C   . HIS C  1 233 ? 36.200  14.254  -11.727 1.00 23.63 ? 233 HIS C C   1 
ATOM   6260  O  O   . HIS C  1 233 ? 35.014  14.195  -11.312 1.00 26.39 ? 233 HIS C O   1 
ATOM   6261  C  CB  . HIS C  1 233 ? 36.802  16.087  -13.300 1.00 30.81 ? 233 HIS C CB  1 
ATOM   6262  C  CG  . HIS C  1 233 ? 37.314  16.480  -14.639 1.00 34.56 ? 233 HIS C CG  1 
ATOM   6263  N  ND1 . HIS C  1 233 ? 36.500  17.032  -15.616 1.00 37.37 ? 233 HIS C ND1 1 
ATOM   6264  C  CD2 . HIS C  1 233 ? 38.544  16.363  -15.184 1.00 33.21 ? 233 HIS C CD2 1 
ATOM   6265  C  CE1 . HIS C  1 233 ? 37.215  17.241  -16.703 1.00 36.31 ? 233 HIS C CE1 1 
ATOM   6266  N  NE2 . HIS C  1 233 ? 38.458  16.862  -16.461 1.00 33.11 ? 233 HIS C NE2 1 
ATOM   6267  N  N   . MET C  1 234 ? 37.281  14.032  -10.986 1.00 30.38 ? 234 MET C N   1 
ATOM   6268  C  CA  . MET C  1 234 ? 37.311  13.673  -9.542  1.00 37.05 ? 234 MET C CA  1 
ATOM   6269  C  C   . MET C  1 234 ? 36.527  14.710  -8.707  1.00 44.17 ? 234 MET C C   1 
ATOM   6270  O  O   . MET C  1 234 ? 35.694  14.349  -7.854  1.00 49.39 ? 234 MET C O   1 
ATOM   6271  C  CB  . MET C  1 234 ? 38.761  13.560  -9.091  1.00 38.51 ? 234 MET C CB  1 
ATOM   6272  C  CG  . MET C  1 234 ? 38.964  12.755  -7.799  1.00 41.26 ? 234 MET C CG  1 
ATOM   6273  S  SD  . MET C  1 234 ? 40.649  12.946  -7.192  1.00 48.91 ? 234 MET C SD  1 
ATOM   6274  C  CE  . MET C  1 234 ? 41.199  11.245  -6.975  1.00 42.12 ? 234 MET C CE  1 
ATOM   6275  N  N   . ASP C  1 235 ? 36.586  15.972  -9.123  1.00 46.49 ? 235 ASP C N   1 
ATOM   6276  C  CA  . ASP C  1 235 ? 35.849  17.042  -8.436  1.00 57.08 ? 235 ASP C CA  1 
ATOM   6277  C  C   . ASP C  1 235 ? 34.363  17.278  -8.838  1.00 53.73 ? 235 ASP C C   1 
ATOM   6278  O  O   . ASP C  1 235 ? 33.789  18.297  -8.454  1.00 52.26 ? 235 ASP C O   1 
ATOM   6279  C  CB  . ASP C  1 235 ? 36.622  18.361  -8.541  1.00 64.57 ? 235 ASP C CB  1 
ATOM   6280  N  N   . ASP C  1 236 ? 33.743  16.365  -9.593  1.00 47.44 ? 236 ASP C N   1 
ATOM   6281  C  CA  . ASP C  1 236 ? 32.337  16.512  -9.996  1.00 51.64 ? 236 ASP C CA  1 
ATOM   6282  C  C   . ASP C  1 236 ? 31.405  15.952  -8.906  1.00 53.18 ? 236 ASP C C   1 
ATOM   6283  O  O   . ASP C  1 236 ? 31.493  14.746  -8.565  1.00 49.29 ? 236 ASP C O   1 
ATOM   6284  C  CB  . ASP C  1 236 ? 32.038  15.882  -11.387 1.00 49.05 ? 236 ASP C CB  1 
ATOM   6285  C  CG  . ASP C  1 236 ? 30.886  16.547  -12.110 1.00 57.86 ? 236 ASP C CG  1 
ATOM   6286  O  OD1 . ASP C  1 236 ? 29.992  17.111  -11.430 1.00 68.97 ? 236 ASP C OD1 1 
ATOM   6287  O  OD2 . ASP C  1 236 ? 30.854  16.495  -13.373 1.00 48.53 ? 236 ASP C OD2 1 
ATOM   6288  N  N   . PRO C  1 237 ? 30.509  16.830  -8.352  1.00 53.35 ? 237 PRO C N   1 
ATOM   6289  C  CA  . PRO C  1 237 ? 29.540  16.366  -7.343  1.00 53.65 ? 237 PRO C CA  1 
ATOM   6290  C  C   . PRO C  1 237 ? 28.383  15.532  -7.958  1.00 48.69 ? 237 PRO C C   1 
ATOM   6291  O  O   . PRO C  1 237 ? 27.612  14.917  -7.186  1.00 41.07 ? 237 PRO C O   1 
ATOM   6292  C  CB  . PRO C  1 237 ? 29.012  17.682  -6.698  1.00 54.41 ? 237 PRO C CB  1 
ATOM   6293  C  CG  . PRO C  1 237 ? 29.836  18.793  -7.291  1.00 54.44 ? 237 PRO C CG  1 
ATOM   6294  C  CD  . PRO C  1 237 ? 30.324  18.273  -8.618  1.00 54.13 ? 237 PRO C CD  1 
ATOM   6295  N  N   . SER C  1 238 ? 28.265  15.528  -9.302  1.00 44.53 ? 238 SER C N   1 
ATOM   6296  C  CA  . SER C  1 238 ? 27.390  14.571  -10.037 1.00 44.40 ? 238 SER C CA  1 
ATOM   6297  C  C   . SER C  1 238 ? 28.211  13.583  -10.883 1.00 35.42 ? 238 SER C C   1 
ATOM   6298  O  O   . SER C  1 238 ? 28.344  13.778  -12.092 1.00 33.29 ? 238 SER C O   1 
ATOM   6299  C  CB  . SER C  1 238 ? 26.339  15.276  -10.901 1.00 48.50 ? 238 SER C CB  1 
ATOM   6300  O  OG  . SER C  1 238 ? 25.567  16.181  -10.122 1.00 58.03 ? 238 SER C OG  1 
ATOM   6301  N  N   . PRO C  1 239 ? 28.769  12.529  -10.250 1.00 36.05 ? 239 PRO C N   1 
ATOM   6302  C  CA  . PRO C  1 239 ? 29.582  11.616  -11.059 1.00 28.66 ? 239 PRO C CA  1 
ATOM   6303  C  C   . PRO C  1 239 ? 28.781  10.749  -12.036 1.00 35.17 ? 239 PRO C C   1 
ATOM   6304  O  O   . PRO C  1 239 ? 27.644  10.307  -11.729 1.00 33.83 ? 239 PRO C O   1 
ATOM   6305  C  CB  . PRO C  1 239 ? 30.231  10.700  -10.024 1.00 32.58 ? 239 PRO C CB  1 
ATOM   6306  C  CG  . PRO C  1 239 ? 29.419  10.851  -8.777  1.00 32.68 ? 239 PRO C CG  1 
ATOM   6307  C  CD  . PRO C  1 239 ? 28.982  12.268  -8.811  1.00 34.14 ? 239 PRO C CD  1 
ATOM   6308  N  N   . ARG C  1 240 ? 29.403  10.448  -13.165 1.00 27.24 ? 240 ARG C N   1 
ATOM   6309  C  CA  . ARG C  1 240 ? 28.725  9.588   -14.136 1.00 30.50 ? 240 ARG C CA  1 
ATOM   6310  C  C   . ARG C  1 240 ? 29.628  8.462   -14.564 1.00 25.70 ? 240 ARG C C   1 
ATOM   6311  O  O   . ARG C  1 240 ? 30.791  8.704   -14.919 1.00 25.29 ? 240 ARG C O   1 
ATOM   6312  C  CB  . ARG C  1 240 ? 28.302  10.383  -15.355 1.00 33.67 ? 240 ARG C CB  1 
ATOM   6313  C  CG  . ARG C  1 240 ? 27.239  9.630   -16.155 1.00 48.09 ? 240 ARG C CG  1 
ATOM   6314  C  CD  . ARG C  1 240 ? 26.635  10.478  -17.269 1.00 53.40 ? 240 ARG C CD  1 
ATOM   6315  N  NE  . ARG C  1 240 ? 25.772  11.579  -16.816 1.00 62.79 ? 240 ARG C NE  1 
ATOM   6316  C  CZ  . ARG C  1 240 ? 24.439  11.561  -16.861 1.00 65.85 ? 240 ARG C CZ  1 
ATOM   6317  N  NH1 . ARG C  1 240 ? 23.792  10.489  -17.313 1.00 67.58 ? 240 ARG C NH1 1 
ATOM   6318  N  NH2 . ARG C  1 240 ? 23.754  12.616  -16.450 1.00 65.31 ? 240 ARG C NH2 1 
ATOM   6319  N  N   . GLU C  1 241 ? 29.038  7.254   -14.592 1.00 25.11 ? 241 GLU C N   1 
ATOM   6320  C  CA  . GLU C  1 241 ? 29.766  6.063   -14.937 1.00 22.30 ? 241 GLU C CA  1 
ATOM   6321  C  C   . GLU C  1 241 ? 30.159  6.078   -16.437 1.00 19.87 ? 241 GLU C C   1 
ATOM   6322  O  O   . GLU C  1 241 ? 29.393  6.552   -17.287 1.00 20.58 ? 241 GLU C O   1 
ATOM   6323  C  CB  . GLU C  1 241 ? 28.934  4.832   -14.706 1.00 27.40 ? 241 GLU C CB  1 
ATOM   6324  C  CG  . GLU C  1 241 ? 28.828  4.481   -13.234 1.00 31.82 ? 241 GLU C CG  1 
ATOM   6325  C  CD  . GLU C  1 241 ? 27.529  3.821   -12.854 1.00 36.86 ? 241 GLU C CD  1 
ATOM   6326  O  OE1 . GLU C  1 241 ? 27.038  2.888   -13.573 1.00 39.34 ? 241 GLU C OE1 1 
ATOM   6327  O  OE2 . GLU C  1 241 ? 27.003  4.229   -11.777 1.00 47.87 ? 241 GLU C OE2 1 
ATOM   6328  N  N   . MET C  1 242 ? 31.369  5.624   -16.683 1.00 17.56 ? 242 MET C N   1 
ATOM   6329  C  CA  . MET C  1 242 ? 31.837  5.350   -18.111 1.00 15.59 ? 242 MET C CA  1 
ATOM   6330  C  C   . MET C  1 242 ? 31.332  3.941   -18.506 1.00 14.72 ? 242 MET C C   1 
ATOM   6331  O  O   . MET C  1 242 ? 31.944  2.903   -18.277 1.00 14.41 ? 242 MET C O   1 
ATOM   6332  C  CB  . MET C  1 242 ? 33.397  5.419   -18.228 1.00 13.31 ? 242 MET C CB  1 
ATOM   6333  C  CG  . MET C  1 242 ? 33.806  5.423   -19.745 1.00 15.57 ? 242 MET C CG  1 
ATOM   6334  S  SD  . MET C  1 242 ? 35.534  5.342   -19.968 1.00 16.03 ? 242 MET C SD  1 
ATOM   6335  C  CE  . MET C  1 242 ? 35.903  7.008   -19.362 1.00 15.72 ? 242 MET C CE  1 
ATOM   6336  N  N   . ILE C  1 243 ? 30.176  3.970   -19.157 1.00 14.23 ? 243 ILE C N   1 
ATOM   6337  C  CA  . ILE C  1 243 ? 29.449  2.804   -19.612 1.00 14.47 ? 243 ILE C CA  1 
ATOM   6338  C  C   . ILE C  1 243 ? 28.914  3.107   -21.027 1.00 12.27 ? 243 ILE C C   1 
ATOM   6339  O  O   . ILE C  1 243 ? 28.671  4.257   -21.388 1.00 13.36 ? 243 ILE C O   1 
ATOM   6340  C  CB  . ILE C  1 243 ? 28.270  2.359   -18.670 1.00 15.02 ? 243 ILE C CB  1 
ATOM   6341  C  CG1 . ILE C  1 243 ? 27.333  3.519   -18.367 1.00 16.51 ? 243 ILE C CG1 1 
ATOM   6342  C  CG2 . ILE C  1 243 ? 28.883  1.714   -17.400 1.00 18.12 ? 243 ILE C CG2 1 
ATOM   6343  C  CD1 . ILE C  1 243 ? 26.124  3.045   -17.504 1.00 18.41 ? 243 ILE C CD1 1 
ATOM   6344  N  N   . ASN C  1 244 ? 28.617  2.018   -21.757 1.00 11.49 ? 244 ASN C N   1 
ATOM   6345  C  CA  . ASN C  1 244 ? 27.928  2.194   -23.069 1.00 13.08 ? 244 ASN C CA  1 
ATOM   6346  C  C   . ASN C  1 244 ? 28.650  3.156   -23.995 1.00 12.54 ? 244 ASN C C   1 
ATOM   6347  O  O   . ASN C  1 244 ? 28.045  3.971   -24.666 1.00 12.85 ? 244 ASN C O   1 
ATOM   6348  C  CB  . ASN C  1 244 ? 26.496  2.601   -22.897 1.00 15.04 ? 244 ASN C CB  1 
ATOM   6349  C  CG  . ASN C  1 244 ? 25.750  1.761   -21.912 1.00 15.74 ? 244 ASN C CG  1 
ATOM   6350  O  OD1 . ASN C  1 244 ? 25.836  0.559   -21.944 1.00 16.60 ? 244 ASN C OD1 1 
ATOM   6351  N  ND2 . ASN C  1 244 ? 24.997  2.481   -20.981 1.00 17.90 ? 244 ASN C ND2 1 
ATOM   6352  N  N   . ASN C  1 245 ? 29.989  3.030   -23.977 1.00 12.04 ? 245 ASN C N   1 
ATOM   6353  C  CA  . ASN C  1 245 ? 30.839  3.941   -24.762 1.00 11.54 ? 245 ASN C CA  1 
ATOM   6354  C  C   . ASN C  1 245 ? 31.139  3.383   -26.134 1.00 9.76  ? 245 ASN C C   1 
ATOM   6355  O  O   . ASN C  1 245 ? 32.266  3.293   -26.574 1.00 11.94 ? 245 ASN C O   1 
ATOM   6356  C  CB  . ASN C  1 245 ? 32.088  4.349   -23.988 1.00 12.05 ? 245 ASN C CB  1 
ATOM   6357  C  CG  . ASN C  1 245 ? 32.980  3.167   -23.697 1.00 14.25 ? 245 ASN C CG  1 
ATOM   6358  O  OD1 . ASN C  1 245 ? 32.555  2.009   -23.648 1.00 14.11 ? 245 ASN C OD1 1 
ATOM   6359  N  ND2 . ASN C  1 245 ? 34.242  3.476   -23.376 1.00 15.71 ? 245 ASN C ND2 1 
ATOM   6360  N  N   . PHE C  1 246 ? 30.076  3.037   -26.842 1.00 10.02 ? 246 PHE C N   1 
ATOM   6361  C  CA  . PHE C  1 246 ? 30.165  2.470   -28.215 1.00 9.86  ? 246 PHE C CA  1 
ATOM   6362  C  C   . PHE C  1 246 ? 29.207  3.252   -29.041 1.00 8.85  ? 246 PHE C C   1 
ATOM   6363  O  O   . PHE C  1 246 ? 28.183  3.727   -28.534 1.00 9.92  ? 246 PHE C O   1 
ATOM   6364  C  CB  . PHE C  1 246 ? 29.850  0.941   -28.230 1.00 10.50 ? 246 PHE C CB  1 
ATOM   6365  C  CG  . PHE C  1 246 ? 28.416  0.596   -27.781 1.00 9.46  ? 246 PHE C CG  1 
ATOM   6366  C  CD1 . PHE C  1 246 ? 28.134  0.449   -26.420 1.00 11.32 ? 246 PHE C CD1 1 
ATOM   6367  C  CD2 . PHE C  1 246 ? 27.347  0.504   -28.686 1.00 11.53 ? 246 PHE C CD2 1 
ATOM   6368  C  CE1 . PHE C  1 246 ? 26.827  0.135   -25.982 1.00 11.85 ? 246 PHE C CE1 1 
ATOM   6369  C  CE2 . PHE C  1 246 ? 26.032  0.241   -28.250 1.00 12.30 ? 246 PHE C CE2 1 
ATOM   6370  C  CZ  . PHE C  1 246 ? 25.761  0.053   -26.884 1.00 11.18 ? 246 PHE C CZ  1 
ATOM   6371  N  N   . ARG C  1 247 ? 29.513  3.361   -30.332 1.00 8.52  ? 247 ARG C N   1 
ATOM   6372  C  CA  . ARG C  1 247 ? 28.587  4.040   -31.234 1.00 9.32  ? 247 ARG C CA  1 
ATOM   6373  C  C   . ARG C  1 247 ? 27.658  3.013   -31.854 1.00 8.25  ? 247 ARG C C   1 
ATOM   6374  O  O   . ARG C  1 247 ? 28.058  1.852   -32.042 1.00 9.46  ? 247 ARG C O   1 
ATOM   6375  C  CB  . ARG C  1 247 ? 29.390  4.693   -32.415 1.00 9.32  ? 247 ARG C CB  1 
ATOM   6376  C  CG  . ARG C  1 247 ? 28.631  5.696   -33.282 1.00 8.73  ? 247 ARG C CG  1 
ATOM   6377  C  CD  . ARG C  1 247 ? 29.449  6.102   -34.483 1.00 7.83  ? 247 ARG C CD  1 
ATOM   6378  N  NE  . ARG C  1 247 ? 28.887  7.282   -35.102 1.00 7.80  ? 247 ARG C NE  1 
ATOM   6379  C  CZ  . ARG C  1 247 ? 29.378  7.846   -36.194 1.00 8.29  ? 247 ARG C CZ  1 
ATOM   6380  N  NH1 . ARG C  1 247 ? 30.426  7.276   -36.795 1.00 9.85  ? 247 ARG C NH1 1 
ATOM   6381  N  NH2 . ARG C  1 247 ? 28.819  8.943   -36.672 1.00 8.68  ? 247 ARG C NH2 1 
ATOM   6382  N  N   . GLN C  1 248 ? 26.388  3.382   -32.057 1.00 8.50  ? 248 GLN C N   1 
ATOM   6383  C  CA  . GLN C  1 248 ? 25.413  2.529   -32.766 1.00 8.30  ? 248 GLN C CA  1 
ATOM   6384  C  C   . GLN C  1 248 ? 25.917  2.230   -34.173 1.00 9.49  ? 248 GLN C C   1 
ATOM   6385  O  O   . GLN C  1 248 ? 26.641  3.035   -34.802 1.00 9.37  ? 248 GLN C O   1 
ATOM   6386  C  CB  . GLN C  1 248 ? 24.021  3.202   -32.897 1.00 9.60  ? 248 GLN C CB  1 
ATOM   6387  C  CG  . GLN C  1 248 ? 23.382  3.518   -31.507 1.00 8.81  ? 248 GLN C CG  1 
ATOM   6388  C  CD  . GLN C  1 248 ? 23.018  2.321   -30.710 1.00 9.90  ? 248 GLN C CD  1 
ATOM   6389  O  OE1 . GLN C  1 248 ? 23.733  1.926   -29.776 1.00 12.18 ? 248 GLN C OE1 1 
ATOM   6390  N  NE2 . GLN C  1 248 ? 21.937  1.630   -31.105 1.00 11.15 ? 248 GLN C NE2 1 
ATOM   6391  N  N   . VAL C  1 249 ? 25.561  1.083   -34.749 1.00 9.12  ? 249 VAL C N   1 
ATOM   6392  C  CA  . VAL C  1 249 ? 25.956  0.754   -36.110 1.00 9.83  ? 249 VAL C CA  1 
ATOM   6393  C  C   . VAL C  1 249 ? 25.344  1.741   -37.119 1.00 10.36 ? 249 VAL C C   1 
ATOM   6394  O  O   . VAL C  1 249 ? 24.214  2.243   -36.919 1.00 9.93  ? 249 VAL C O   1 
ATOM   6395  C  CB  . VAL C  1 249 ? 25.629  -0.705  -36.529 1.00 10.59 ? 249 VAL C CB  1 
ATOM   6396  C  CG1 . VAL C  1 249 ? 26.428  -1.692  -35.716 1.00 11.15 ? 249 VAL C CG1 1 
ATOM   6397  C  CG2 . VAL C  1 249 ? 24.185  -0.989  -36.444 1.00 12.87 ? 249 VAL C CG2 1 
ATOM   6398  N  N   . GLN C  1 250 ? 26.082  1.966   -38.173 1.00 9.02  ? 250 GLN C N   1 
ATOM   6399  C  CA  . GLN C  1 250 ? 25.698  2.914   -39.203 1.00 9.63  ? 250 GLN C CA  1 
ATOM   6400  C  C   . GLN C  1 250 ? 25.118  2.164   -40.400 1.00 10.56 ? 250 GLN C C   1 
ATOM   6401  O  O   . GLN C  1 250 ? 25.475  1.003   -40.664 1.00 12.00 ? 250 GLN C O   1 
ATOM   6402  C  CB  . GLN C  1 250 ? 26.952  3.601   -39.665 1.00 9.47  ? 250 GLN C CB  1 
ATOM   6403  C  CG  . GLN C  1 250 ? 27.795  4.206   -38.487 1.00 8.83  ? 250 GLN C CG  1 
ATOM   6404  C  CD  . GLN C  1 250 ? 27.072  5.366   -37.877 1.00 8.30  ? 250 GLN C CD  1 
ATOM   6405  O  OE1 . GLN C  1 250 ? 26.816  6.421   -38.550 1.00 9.58  ? 250 GLN C OE1 1 
ATOM   6406  N  NE2 . GLN C  1 250 ? 26.724  5.247   -36.626 1.00 9.22  ? 250 GLN C NE2 1 
ATOM   6407  N  N   . LYS C  1 251 ? 24.299  2.917   -41.143 1.00 9.85  ? 251 LYS C N   1 
ATOM   6408  C  CA  . LYS C  1 251 ? 23.845  2.332   -42.438 1.00 10.97 ? 251 LYS C CA  1 
ATOM   6409  C  C   . LYS C  1 251 ? 25.040  2.036   -43.300 1.00 11.18 ? 251 LYS C C   1 
ATOM   6410  O  O   . LYS C  1 251 ? 25.991  2.830   -43.298 1.00 11.35 ? 251 LYS C O   1 
ATOM   6411  C  CB  . LYS C  1 251 ? 22.843  3.260   -43.123 1.00 10.82 ? 251 LYS C CB  1 
ATOM   6412  C  CG  . LYS C  1 251 ? 21.486  3.171   -42.381 1.00 12.15 ? 251 LYS C CG  1 
ATOM   6413  C  CD  . LYS C  1 251 ? 20.563  4.138   -43.029 1.00 12.44 ? 251 LYS C CD  1 
ATOM   6414  C  CE  . LYS C  1 251 ? 19.093  3.789   -42.659 1.00 10.13 ? 251 LYS C CE  1 
ATOM   6415  N  NZ  . LYS C  1 251 ? 18.831  3.891   -41.150 1.00 9.51  ? 251 LYS C NZ  1 
ATOM   6416  N  N   . PHE C  1 252 ? 24.942  0.965   -44.093 1.00 12.38 ? 252 PHE C N   1 
ATOM   6417  C  CA  . PHE C  1 252 ? 26.106  0.557   -45.000 1.00 12.21 ? 252 PHE C CA  1 
ATOM   6418  C  C   . PHE C  1 252 ? 25.353  -0.108  -46.151 1.00 17.47 ? 252 PHE C C   1 
ATOM   6419  O  O   . PHE C  1 252 ? 24.984  -1.274  -46.100 1.00 20.02 ? 252 PHE C O   1 
ATOM   6420  C  CB  . PHE C  1 252 ? 26.850  -0.510  -44.256 1.00 13.14 ? 252 PHE C CB  1 
ATOM   6421  C  CG  . PHE C  1 252 ? 28.123  -0.966  -44.909 1.00 12.42 ? 252 PHE C CG  1 
ATOM   6422  C  CD1 . PHE C  1 252 ? 29.284  -0.192  -44.845 1.00 11.86 ? 252 PHE C CD1 1 
ATOM   6423  C  CD2 . PHE C  1 252 ? 28.188  -2.202  -45.491 1.00 14.25 ? 252 PHE C CD2 1 
ATOM   6424  C  CE1 . PHE C  1 252 ? 30.471  -0.634  -45.415 1.00 10.66 ? 252 PHE C CE1 1 
ATOM   6425  C  CE2 . PHE C  1 252 ? 29.360  -2.655  -46.055 1.00 13.29 ? 252 PHE C CE2 1 
ATOM   6426  C  CZ  . PHE C  1 252 ? 30.503  -1.880  -46.014 1.00 12.39 ? 252 PHE C CZ  1 
ATOM   6427  N  N   . ASP C  1 253 ? 25.122  0.680   -47.130 1.00 20.62 ? 253 ASP C N   1 
ATOM   6428  C  CA  . ASP C  1 253 ? 24.276  0.286   -48.301 1.00 21.41 ? 253 ASP C CA  1 
ATOM   6429  C  C   . ASP C  1 253 ? 25.043  0.270   -49.606 1.00 17.82 ? 253 ASP C C   1 
ATOM   6430  O  O   . ASP C  1 253 ? 25.840  1.146   -49.877 1.00 19.23 ? 253 ASP C O   1 
ATOM   6431  C  CB  . ASP C  1 253 ? 23.153  1.271   -48.293 1.00 28.56 ? 253 ASP C CB  1 
ATOM   6432  C  CG  . ASP C  1 253 ? 21.994  0.785   -49.113 1.00 34.30 ? 253 ASP C CG  1 
ATOM   6433  O  OD1 . ASP C  1 253 ? 21.456  -0.339  -48.864 1.00 35.78 ? 253 ASP C OD1 1 
ATOM   6434  O  OD2 . ASP C  1 253 ? 21.707  1.533   -50.067 1.00 31.79 ? 253 ASP C OD2 1 
ATOM   6435  N  N   A GLU C  1 254 ? 24.758  -0.748  -50.420 0.50 19.80 ? 254 GLU C N   1 
ATOM   6436  N  N   B GLU C  1 254 ? 24.752  -0.765  -50.392 0.50 19.14 ? 254 GLU C N   1 
ATOM   6437  C  CA  A GLU C  1 254 ? 25.424  -0.958  -51.712 0.50 21.00 ? 254 GLU C CA  1 
ATOM   6438  C  CA  B GLU C  1 254 ? 25.407  -0.993  -51.666 0.50 19.85 ? 254 GLU C CA  1 
ATOM   6439  C  C   A GLU C  1 254 ? 26.957  -1.085  -51.560 0.50 20.70 ? 254 GLU C C   1 
ATOM   6440  C  C   B GLU C  1 254 ? 26.929  -0.951  -51.481 0.50 19.90 ? 254 GLU C C   1 
ATOM   6441  O  O   A GLU C  1 254 ? 27.703  -0.710  -52.473 0.50 20.90 ? 254 GLU C O   1 
ATOM   6442  O  O   B GLU C  1 254 ? 27.626  -0.323  -52.277 0.50 21.08 ? 254 GLU C O   1 
ATOM   6443  C  CB  A GLU C  1 254 ? 25.056  0.158   -52.748 0.50 23.31 ? 254 GLU C CB  1 
ATOM   6444  C  CB  B GLU C  1 254 ? 24.961  0.070   -52.705 0.50 21.62 ? 254 GLU C CB  1 
ATOM   6445  C  CG  A GLU C  1 254 ? 23.553  0.233   -53.072 0.50 26.89 ? 254 GLU C CG  1 
ATOM   6446  C  CG  B GLU C  1 254 ? 23.442  0.096   -52.913 0.50 22.76 ? 254 GLU C CG  1 
ATOM   6447  C  CD  A GLU C  1 254 ? 23.241  0.944   -54.394 0.50 29.62 ? 254 GLU C CD  1 
ATOM   6448  C  CD  B GLU C  1 254 ? 22.931  -1.145  -53.599 0.50 25.47 ? 254 GLU C CD  1 
ATOM   6449  O  OE1 A GLU C  1 254 ? 24.054  0.914   -55.343 0.50 31.96 ? 254 GLU C OE1 1 
ATOM   6450  O  OE1 B GLU C  1 254 ? 23.505  -1.558  -54.620 0.50 29.70 ? 254 GLU C OE1 1 
ATOM   6451  O  OE2 A GLU C  1 254 ? 22.146  1.504   -54.503 0.50 34.17 ? 254 GLU C OE2 1 
ATOM   6452  O  OE2 B GLU C  1 254 ? 21.957  -1.709  -53.110 0.50 25.92 ? 254 GLU C OE2 1 
ATOM   6453  N  N   . ARG C  1 255 ? 27.410  -1.592  -50.408 1.00 18.01 ? 255 ARG C N   1 
ATOM   6454  C  CA  . ARG C  1 255 ? 28.848  -1.737  -50.178 1.00 16.57 ? 255 ARG C CA  1 
ATOM   6455  C  C   . ARG C  1 255 ? 29.128  -3.135  -49.693 1.00 14.92 ? 255 ARG C C   1 
ATOM   6456  O  O   . ARG C  1 255 ? 28.248  -3.840  -49.147 1.00 16.86 ? 255 ARG C O   1 
ATOM   6457  C  CB  . ARG C  1 255 ? 29.384  -0.722  -49.149 1.00 15.59 ? 255 ARG C CB  1 
ATOM   6458  C  CG  . ARG C  1 255 ? 29.221  0.744   -49.597 1.00 16.10 ? 255 ARG C CG  1 
ATOM   6459  C  CD  . ARG C  1 255 ? 29.816  1.745   -48.583 1.00 15.85 ? 255 ARG C CD  1 
ATOM   6460  N  NE  . ARG C  1 255 ? 31.217  1.351   -48.385 1.00 17.01 ? 255 ARG C NE  1 
ATOM   6461  C  CZ  . ARG C  1 255 ? 31.943  1.633   -47.271 1.00 17.04 ? 255 ARG C CZ  1 
ATOM   6462  N  NH1 . ARG C  1 255 ? 31.385  2.333   -46.291 1.00 16.60 ? 255 ARG C NH1 1 
ATOM   6463  N  NH2 . ARG C  1 255 ? 33.217  1.194   -47.210 1.00 15.07 ? 255 ARG C NH2 1 
ATOM   6464  N  N   . LEU C  1 256 ? 30.384  -3.546  -49.878 1.00 14.55 ? 256 LEU C N   1 
ATOM   6465  C  CA  . LEU C  1 256 ? 30.817  -4.819  -49.414 1.00 15.07 ? 256 LEU C CA  1 
ATOM   6466  C  C   . LEU C  1 256 ? 31.854  -4.697  -48.255 1.00 13.04 ? 256 LEU C C   1 
ATOM   6467  O  O   . LEU C  1 256 ? 32.576  -3.705  -48.107 1.00 14.49 ? 256 LEU C O   1 
ATOM   6468  C  CB  . LEU C  1 256 ? 31.423  -5.680  -50.535 1.00 18.71 ? 256 LEU C CB  1 
ATOM   6469  C  CG  . LEU C  1 256 ? 30.551  -5.876  -51.768 1.00 21.28 ? 256 LEU C CG  1 
ATOM   6470  C  CD1 . LEU C  1 256 ? 31.415  -6.159  -53.000 1.00 24.21 ? 256 LEU C CD1 1 
ATOM   6471  C  CD2 . LEU C  1 256 ? 29.613  -7.034  -51.418 1.00 23.34 ? 256 LEU C CD2 1 
ATOM   6472  N  N   . VAL C  1 257 ? 31.882  -5.784  -47.480 1.00 14.67 ? 257 VAL C N   1 
ATOM   6473  C  CA  . VAL C  1 257 ? 32.966  -6.038  -46.555 1.00 13.43 ? 257 VAL C CA  1 
ATOM   6474  C  C   . VAL C  1 257 ? 33.750  -7.203  -47.119 1.00 12.83 ? 257 VAL C C   1 
ATOM   6475  O  O   . VAL C  1 257 ? 33.199  -8.285  -47.460 1.00 13.65 ? 257 VAL C O   1 
ATOM   6476  C  CB  . VAL C  1 257 ? 32.403  -6.415  -45.190 1.00 13.42 ? 257 VAL C CB  1 
ATOM   6477  C  CG1 . VAL C  1 257 ? 33.533  -6.833  -44.267 1.00 13.97 ? 257 VAL C CG1 1 
ATOM   6478  C  CG2 . VAL C  1 257 ? 31.726  -5.202  -44.580 1.00 16.58 ? 257 VAL C CG2 1 
ATOM   6479  N  N   . TYR C  1 258 ? 35.060  -7.067  -47.222 1.00 10.85 ? 258 TYR C N   1 
ATOM   6480  C  CA  . TYR C  1 258 ? 35.892  -8.069  -47.880 1.00 12.01 ? 258 TYR C CA  1 
ATOM   6481  C  C   . TYR C  1 258 ? 36.398  -8.994  -46.801 1.00 12.55 ? 258 TYR C C   1 
ATOM   6482  O  O   . TYR C  1 258 ? 36.727  -8.542  -45.674 1.00 13.19 ? 258 TYR C O   1 
ATOM   6483  C  CB  . TYR C  1 258 ? 36.990  -7.380  -48.702 1.00 13.91 ? 258 TYR C CB  1 
ATOM   6484  C  CG  . TYR C  1 258 ? 36.435  -6.472  -49.731 1.00 15.42 ? 258 TYR C CG  1 
ATOM   6485  C  CD1 . TYR C  1 258 ? 35.938  -7.002  -50.926 1.00 16.09 ? 258 TYR C CD1 1 
ATOM   6486  C  CD2 . TYR C  1 258 ? 36.258  -5.125  -49.476 1.00 16.05 ? 258 TYR C CD2 1 
ATOM   6487  C  CE1 . TYR C  1 258 ? 35.340  -6.244  -51.916 1.00 17.82 ? 258 TYR C CE1 1 
ATOM   6488  C  CE2 . TYR C  1 258 ? 35.645  -4.318  -50.421 1.00 18.59 ? 258 TYR C CE2 1 
ATOM   6489  C  CZ  . TYR C  1 258 ? 35.187  -4.871  -51.642 1.00 18.76 ? 258 TYR C CZ  1 
ATOM   6490  O  OH  . TYR C  1 258 ? 34.518  -4.023  -52.578 1.00 22.60 ? 258 TYR C OH  1 
ATOM   6491  N  N   . THR C  1 259 ? 36.499  -10.289 -47.091 1.00 12.45 ? 259 THR C N   1 
ATOM   6492  C  CA  . THR C  1 259 ? 36.899  -11.205 -46.078 1.00 11.83 ? 259 THR C CA  1 
ATOM   6493  C  C   . THR C  1 259 ? 38.148  -12.007 -46.550 1.00 12.78 ? 259 THR C C   1 
ATOM   6494  O  O   . THR C  1 259 ? 38.291  -12.302 -47.730 1.00 12.93 ? 259 THR C O   1 
ATOM   6495  C  CB  . THR C  1 259 ? 35.815  -12.205 -45.683 1.00 12.60 ? 259 THR C CB  1 
ATOM   6496  O  OG1 . THR C  1 259 ? 35.388  -12.892 -46.885 1.00 14.81 ? 259 THR C OG1 1 
ATOM   6497  C  CG2 . THR C  1 259 ? 34.624  -11.515 -45.073 1.00 14.39 ? 259 THR C CG2 1 
ATOM   6498  N  N   . SER C  1 260 ? 39.008  -12.375 -45.614 1.00 13.95 ? 260 SER C N   1 
ATOM   6499  C  CA  . SER C  1 260 ? 40.200  -13.113 -45.977 1.00 13.28 ? 260 SER C CA  1 
ATOM   6500  C  C   . SER C  1 260 ? 39.889  -14.614 -45.963 1.00 15.18 ? 260 SER C C   1 
ATOM   6501  O  O   . SER C  1 260 ? 40.799  -15.405 -46.259 1.00 19.20 ? 260 SER C O   1 
ATOM   6502  C  CB  . SER C  1 260 ? 41.329  -12.799 -45.013 1.00 13.64 ? 260 SER C CB  1 
ATOM   6503  O  OG  . SER C  1 260 ? 40.920  -13.317 -43.757 1.00 13.70 ? 260 SER C OG  1 
ATOM   6504  N  N   . PHE C  1 261 ? 38.670  -14.982 -45.635 1.00 14.77 ? 261 PHE C N   1 
ATOM   6505  C  CA  . PHE C  1 261 ? 38.254  -16.354 -45.517 1.00 16.13 ? 261 PHE C CA  1 
ATOM   6506  C  C   . PHE C  1 261 ? 37.041  -16.487 -46.366 1.00 17.17 ? 261 PHE C C   1 
ATOM   6507  O  O   . PHE C  1 261 ? 36.372  -15.519 -46.759 1.00 20.36 ? 261 PHE C O   1 
ATOM   6508  C  CB  . PHE C  1 261 ? 37.943  -16.638 -44.044 1.00 17.33 ? 261 PHE C CB  1 
ATOM   6509  C  CG  . PHE C  1 261 ? 36.934  -15.670 -43.438 1.00 16.95 ? 261 PHE C CG  1 
ATOM   6510  C  CD1 . PHE C  1 261 ? 37.349  -14.483 -42.867 1.00 16.15 ? 261 PHE C CD1 1 
ATOM   6511  C  CD2 . PHE C  1 261 ? 35.601  -15.947 -43.460 1.00 17.53 ? 261 PHE C CD2 1 
ATOM   6512  C  CE1 . PHE C  1 261 ? 36.397  -13.640 -42.244 1.00 16.27 ? 261 PHE C CE1 1 
ATOM   6513  C  CE2 . PHE C  1 261 ? 34.631  -15.141 -42.880 1.00 19.51 ? 261 PHE C CE2 1 
ATOM   6514  C  CZ  . PHE C  1 261 ? 35.047  -13.927 -42.286 1.00 18.18 ? 261 PHE C CZ  1 
ATOM   6515  N  N   . SER C  1 262 ? 36.664  -17.712 -46.758 1.00 25.42 ? 262 SER C N   1 
ATOM   6516  C  CA  . SER C  1 262 ? 35.311  -17.782 -47.409 1.00 26.94 ? 262 SER C CA  1 
ATOM   6517  C  C   . SER C  1 262 ? 34.379  -18.665 -46.566 1.00 37.82 ? 262 SER C C   1 
ATOM   6518  O  O   . SER C  1 262 ? 33.147  -18.462 -46.478 1.00 41.10 ? 262 SER C O   1 
ATOM   6519  C  CB  . SER C  1 262 ? 35.448  -18.415 -48.800 1.00 35.22 ? 262 SER C CB  1 
ATOM   6520  O  OG  . SER C  1 262 ? 36.153  -19.614 -48.620 1.00 46.78 ? 262 SER C OG  1 
ATOM   6521  N  N   . GLN C  1 263 ? 35.023  -19.665 -45.984 1.00 44.04 ? 263 GLN C N   1 
ATOM   6522  C  CA  . GLN C  1 263 ? 34.387  -20.722 -45.206 1.00 54.67 ? 263 GLN C CA  1 
ATOM   6523  C  C   . GLN C  1 263 ? 34.528  -20.440 -43.686 1.00 54.10 ? 263 GLN C C   1 
ATOM   6524  O  O   . GLN C  1 263 ? 35.629  -20.131 -43.178 1.00 57.04 ? 263 GLN C O   1 
ATOM   6525  C  CB  . GLN C  1 263 ? 34.948  -22.123 -45.634 1.00 44.94 ? 263 GLN C CB  1 
ATOM   6526  C  CG  . GLN C  1 263 ? 36.449  -22.380 -45.363 1.00 41.76 ? 263 GLN C CG  1 
ATOM   6527  C  CD  . GLN C  1 263 ? 36.911  -23.793 -45.724 1.00 33.47 ? 263 GLN C CD  1 
ATOM   6528  O  OE1 . GLN C  1 263 ? 38.086  -24.204 -45.454 1.00 33.44 ? 263 GLN C OE1 1 
ATOM   6529  N  NE2 . GLN C  1 263 ? 35.983  -24.562 -46.346 1.00 18.83 ? 263 GLN C NE2 1 
ATOM   6530  N  N   . LYS D  1 3   ? 14.116  19.695  -45.079 1.00 35.59 ? 3   LYS D N   1 
ATOM   6531  C  CA  . LYS D  1 3   ? 14.573  18.813  -46.173 1.00 24.45 ? 3   LYS D CA  1 
ATOM   6532  C  C   . LYS D  1 3   ? 15.357  17.596  -45.647 1.00 20.04 ? 3   LYS D C   1 
ATOM   6533  O  O   . LYS D  1 3   ? 16.268  17.061  -46.299 1.00 19.01 ? 3   LYS D O   1 
ATOM   6534  C  CB  . LYS D  1 3   ? 15.409  19.547  -47.182 1.00 29.31 ? 3   LYS D CB  1 
ATOM   6535  C  CG  . LYS D  1 3   ? 16.536  20.364  -46.633 1.00 32.66 ? 3   LYS D CG  1 
ATOM   6536  C  CD  . LYS D  1 3   ? 17.123  21.201  -47.783 1.00 34.95 ? 3   LYS D CD  1 
ATOM   6537  C  CE  . LYS D  1 3   ? 18.297  20.428  -48.341 1.00 34.79 ? 3   LYS D CE  1 
ATOM   6538  N  NZ  . LYS D  1 3   ? 19.395  20.551  -47.330 1.00 28.81 ? 3   LYS D NZ  1 
ATOM   6539  N  N   . TRP D  1 4   ? 14.978  17.131  -44.446 1.00 12.95 ? 4   TRP D N   1 
ATOM   6540  C  CA  . TRP D  1 4   ? 15.680  15.980  -43.862 1.00 11.97 ? 4   TRP D CA  1 
ATOM   6541  C  C   . TRP D  1 4   ? 15.421  14.770  -44.762 1.00 11.19 ? 4   TRP D C   1 
ATOM   6542  O  O   . TRP D  1 4   ? 14.424  14.664  -45.448 1.00 11.57 ? 4   TRP D O   1 
ATOM   6543  C  CB  . TRP D  1 4   ? 15.203  15.719  -42.445 1.00 10.99 ? 4   TRP D CB  1 
ATOM   6544  C  CG  . TRP D  1 4   ? 13.737  15.483  -42.258 1.00 9.53  ? 4   TRP D CG  1 
ATOM   6545  C  CD1 . TRP D  1 4   ? 12.707  16.355  -42.036 1.00 10.81 ? 4   TRP D CD1 1 
ATOM   6546  C  CD2 . TRP D  1 4   ? 13.126  14.152  -42.217 1.00 9.44  ? 4   TRP D CD2 1 
ATOM   6547  N  NE1 . TRP D  1 4   ? 11.521  15.701  -41.861 1.00 10.42 ? 4   TRP D NE1 1 
ATOM   6548  C  CE2 . TRP D  1 4   ? 11.743  14.340  -42.013 1.00 8.68  ? 4   TRP D CE2 1 
ATOM   6549  C  CE3 . TRP D  1 4   ? 13.638  12.831  -42.362 1.00 8.95  ? 4   TRP D CE3 1 
ATOM   6550  C  CZ2 . TRP D  1 4   ? 10.864  13.264  -41.862 1.00 9.09  ? 4   TRP D CZ2 1 
ATOM   6551  C  CZ3 . TRP D  1 4   ? 12.740  11.753  -42.211 1.00 9.01  ? 4   TRP D CZ3 1 
ATOM   6552  C  CH2 . TRP D  1 4   ? 11.398  11.986  -41.964 1.00 9.10  ? 4   TRP D CH2 1 
ATOM   6553  N  N   . THR D  1 5   ? 16.366  13.850  -44.707 1.00 10.33 ? 5   THR D N   1 
ATOM   6554  C  CA  . THR D  1 5   ? 16.289  12.616  -45.479 1.00 9.75  ? 5   THR D CA  1 
ATOM   6555  C  C   . THR D  1 5   ? 16.787  11.441  -44.676 1.00 10.61 ? 5   THR D C   1 
ATOM   6556  O  O   . THR D  1 5   ? 17.155  11.577  -43.504 1.00 9.78  ? 5   THR D O   1 
ATOM   6557  C  CB  . THR D  1 5   ? 17.189  12.640  -46.779 1.00 11.55 ? 5   THR D CB  1 
ATOM   6558  O  OG1 . THR D  1 5   ? 18.546  12.632  -46.273 1.00 12.27 ? 5   THR D OG1 1 
ATOM   6559  C  CG2 . THR D  1 5   ? 16.991  13.946  -47.603 1.00 12.09 ? 5   THR D CG2 1 
ATOM   6560  N  N   . TYR D  1 6   ? 16.860  10.236  -45.278 1.00 9.94  ? 6   TYR D N   1 
ATOM   6561  C  CA  . TYR D  1 6   ? 17.512  9.092   -44.679 1.00 9.78  ? 6   TYR D CA  1 
ATOM   6562  C  C   . TYR D  1 6   ? 18.833  8.700   -45.253 1.00 8.84  ? 6   TYR D C   1 
ATOM   6563  O  O   . TYR D  1 6   ? 19.406  7.673   -44.945 1.00 10.48 ? 6   TYR D O   1 
ATOM   6564  C  CB  . TYR D  1 6   ? 16.602  7.870   -44.826 1.00 9.73  ? 6   TYR D CB  1 
ATOM   6565  C  CG  . TYR D  1 6   ? 15.325  7.963   -43.986 1.00 8.99  ? 6   TYR D CG  1 
ATOM   6566  C  CD1 . TYR D  1 6   ? 15.345  7.451   -42.669 1.00 9.54  ? 6   TYR D CD1 1 
ATOM   6567  C  CD2 . TYR D  1 6   ? 14.142  8.552   -44.463 1.00 8.27  ? 6   TYR D CD2 1 
ATOM   6568  C  CE1 . TYR D  1 6   ? 14.187  7.483   -41.878 1.00 9.20  ? 6   TYR D CE1 1 
ATOM   6569  C  CE2 . TYR D  1 6   ? 12.979  8.595   -43.673 1.00 9.09  ? 6   TYR D CE2 1 
ATOM   6570  C  CZ  . TYR D  1 6   ? 13.035  8.071   -42.373 1.00 7.37  ? 6   TYR D CZ  1 
ATOM   6571  O  OH  . TYR D  1 6   ? 11.858  8.075   -41.655 1.00 8.23  ? 6   TYR D OH  1 
ATOM   6572  N  N   . PHE D  1 7   ? 19.346  9.539   -46.161 1.00 11.10 ? 7   PHE D N   1 
ATOM   6573  C  CA  . PHE D  1 7   ? 20.557  9.179   -46.904 1.00 13.19 ? 7   PHE D CA  1 
ATOM   6574  C  C   . PHE D  1 7   ? 21.342  10.446  -47.244 1.00 13.94 ? 7   PHE D C   1 
ATOM   6575  O  O   . PHE D  1 7   ? 20.759  11.317  -47.900 1.00 15.32 ? 7   PHE D O   1 
ATOM   6576  C  CB  . PHE D  1 7   ? 20.206  8.435   -48.220 1.00 14.70 ? 7   PHE D CB  1 
ATOM   6577  C  CG  . PHE D  1 7   ? 21.428  8.006   -48.971 1.00 19.93 ? 7   PHE D CG  1 
ATOM   6578  C  CD1 . PHE D  1 7   ? 22.205  6.966   -48.500 1.00 20.32 ? 7   PHE D CD1 1 
ATOM   6579  C  CD2 . PHE D  1 7   ? 21.883  8.765   -50.071 1.00 26.04 ? 7   PHE D CD2 1 
ATOM   6580  C  CE1 . PHE D  1 7   ? 23.389  6.575   -49.140 1.00 27.36 ? 7   PHE D CE1 1 
ATOM   6581  C  CE2 . PHE D  1 7   ? 23.064  8.406   -50.719 1.00 30.26 ? 7   PHE D CE2 1 
ATOM   6582  C  CZ  . PHE D  1 7   ? 23.802  7.326   -50.257 1.00 26.43 ? 7   PHE D CZ  1 
ATOM   6583  N  N   . GLY D  1 8   ? 22.650  10.431  -46.942 1.00 15.30 ? 8   GLY D N   1 
ATOM   6584  C  CA  . GLY D  1 8   ? 23.487  11.582  -47.420 1.00 15.27 ? 8   GLY D CA  1 
ATOM   6585  C  C   . GLY D  1 8   ? 23.608  12.642  -46.368 1.00 16.64 ? 8   GLY D C   1 
ATOM   6586  O  O   . GLY D  1 8   ? 23.288  12.429  -45.170 1.00 15.77 ? 8   GLY D O   1 
ATOM   6587  N  N   . PRO D  1 9   ? 23.952  13.858  -46.762 1.00 16.05 ? 9   PRO D N   1 
ATOM   6588  C  CA  . PRO D  1 9   ? 24.267  14.893  -45.835 1.00 17.05 ? 9   PRO D CA  1 
ATOM   6589  C  C   . PRO D  1 9   ? 23.215  15.319  -44.874 1.00 16.39 ? 9   PRO D C   1 
ATOM   6590  O  O   . PRO D  1 9   ? 23.540  15.874  -43.828 1.00 18.39 ? 9   PRO D O   1 
ATOM   6591  C  CB  . PRO D  1 9   ? 24.624  16.117  -46.747 1.00 19.19 ? 9   PRO D CB  1 
ATOM   6592  C  CG  . PRO D  1 9   ? 24.921  15.551  -48.026 1.00 21.78 ? 9   PRO D CG  1 
ATOM   6593  C  CD  . PRO D  1 9   ? 24.341  14.165  -48.160 1.00 17.62 ? 9   PRO D CD  1 
ATOM   6594  N  N   . ASP D  1 10  ? 21.928  15.165  -45.256 1.00 14.36 ? 10  ASP D N   1 
ATOM   6595  C  CA  . ASP D  1 10  ? 20.776  15.514  -44.475 1.00 13.16 ? 10  ASP D CA  1 
ATOM   6596  C  C   . ASP D  1 10  ? 20.114  14.300  -43.771 1.00 11.53 ? 10  ASP D C   1 
ATOM   6597  O  O   . ASP D  1 10  ? 18.984  14.430  -43.303 1.00 11.46 ? 10  ASP D O   1 
ATOM   6598  C  CB  . ASP D  1 10  ? 19.738  16.269  -45.298 1.00 14.83 ? 10  ASP D CB  1 
ATOM   6599  C  CG  . ASP D  1 10  ? 20.334  17.577  -45.901 1.00 20.59 ? 10  ASP D CG  1 
ATOM   6600  O  OD1 . ASP D  1 10  ? 21.083  18.276  -45.194 1.00 22.29 ? 10  ASP D OD1 1 
ATOM   6601  O  OD2 . ASP D  1 10  ? 20.147  17.753  -47.104 1.00 25.63 ? 10  ASP D OD2 1 
ATOM   6602  N  N   . GLY D  1 11  ? 20.857  13.205  -43.764 1.00 11.53 ? 11  GLY D N   1 
ATOM   6603  C  CA  . GLY D  1 11  ? 20.395  11.936  -43.160 1.00 9.02  ? 11  GLY D CA  1 
ATOM   6604  C  C   . GLY D  1 11  ? 20.482  11.996  -41.638 1.00 9.69  ? 11  GLY D C   1 
ATOM   6605  O  O   . GLY D  1 11  ? 20.653  13.045  -40.987 1.00 9.21  ? 11  GLY D O   1 
ATOM   6606  N  N   . GLU D  1 12  ? 20.227  10.821  -41.032 1.00 8.16  ? 12  GLU D N   1 
ATOM   6607  C  CA  . GLU D  1 12  ? 19.834  10.783  -39.641 1.00 7.47  ? 12  GLU D CA  1 
ATOM   6608  C  C   . GLU D  1 12  ? 20.851  11.234  -38.649 1.00 8.25  ? 12  GLU D C   1 
ATOM   6609  O  O   . GLU D  1 12  ? 20.451  11.726  -37.619 1.00 8.32  ? 12  GLU D O   1 
ATOM   6610  C  CB  . GLU D  1 12  ? 19.368  9.355   -39.255 1.00 7.81  ? 12  GLU D CB  1 
ATOM   6611  C  CG  . GLU D  1 12  ? 20.439  8.310   -39.162 1.00 8.14  ? 12  GLU D CG  1 
ATOM   6612  C  CD  . GLU D  1 12  ? 19.821  6.915   -39.175 1.00 8.15  ? 12  GLU D CD  1 
ATOM   6613  O  OE1 . GLU D  1 12  ? 19.461  6.454   -38.092 1.00 8.68  ? 12  GLU D OE1 1 
ATOM   6614  O  OE2 . GLU D  1 12  ? 19.736  6.381   -40.286 1.00 9.56  ? 12  GLU D OE2 1 
ATOM   6615  N  N   . ASN D  1 13  ? 22.130  11.148  -38.968 1.00 7.81  ? 13  ASN D N   1 
ATOM   6616  C  CA  . ASN D  1 13  ? 23.146  11.660  -38.048 1.00 8.04  ? 13  ASN D CA  1 
ATOM   6617  C  C   . ASN D  1 13  ? 23.160  13.181  -38.078 1.00 9.46  ? 13  ASN D C   1 
ATOM   6618  O  O   . ASN D  1 13  ? 23.780  13.732  -37.154 1.00 9.33  ? 13  ASN D O   1 
ATOM   6619  C  CB  . ASN D  1 13  ? 24.529  11.120  -38.449 1.00 9.14  ? 13  ASN D CB  1 
ATOM   6620  C  CG  . ASN D  1 13  ? 24.696  9.654   -38.141 1.00 8.44  ? 13  ASN D CG  1 
ATOM   6621  O  OD1 . ASN D  1 13  ? 23.803  9.013   -37.616 1.00 9.78  ? 13  ASN D OD1 1 
ATOM   6622  N  ND2 . ASN D  1 13  ? 25.850  9.156   -38.450 1.00 9.80  ? 13  ASN D ND2 1 
ATOM   6623  N  N   . SER D  1 14  ? 22.509  13.816  -39.032 1.00 9.31  ? 14  SER D N   1 
ATOM   6624  C  CA  . SER D  1 14  ? 22.461  15.299  -39.084 1.00 8.70  ? 14  SER D CA  1 
ATOM   6625  C  C   . SER D  1 14  ? 21.125  15.829  -38.641 1.00 9.06  ? 14  SER D C   1 
ATOM   6626  O  O   . SER D  1 14  ? 21.004  17.047  -38.552 1.00 9.44  ? 14  SER D O   1 
ATOM   6627  C  CB  . SER D  1 14  ? 22.756  15.760  -40.509 1.00 9.16  ? 14  SER D CB  1 
ATOM   6628  O  OG  . SER D  1 14  ? 24.121  15.423  -40.802 1.00 11.44 ? 14  SER D OG  1 
ATOM   6629  N  N   . TRP D  1 15  ? 20.102  15.009  -38.335 1.00 7.96  ? 15  TRP D N   1 
ATOM   6630  C  CA  . TRP D  1 15  ? 18.815  15.606  -38.005 1.00 8.57  ? 15  TRP D CA  1 
ATOM   6631  C  C   . TRP D  1 15  ? 18.896  16.520  -36.812 1.00 8.23  ? 15  TRP D C   1 
ATOM   6632  O  O   . TRP D  1 15  ? 18.117  17.517  -36.792 1.00 8.69  ? 15  TRP D O   1 
ATOM   6633  C  CB  . TRP D  1 15  ? 17.805  14.474  -37.631 1.00 9.04  ? 15  TRP D CB  1 
ATOM   6634  C  CG  . TRP D  1 15  ? 17.421  13.571  -38.803 1.00 9.11  ? 15  TRP D CG  1 
ATOM   6635  C  CD1 . TRP D  1 15  ? 17.673  13.729  -40.112 1.00 8.62  ? 15  TRP D CD1 1 
ATOM   6636  C  CD2 . TRP D  1 15  ? 16.671  12.346  -38.667 1.00 7.97  ? 15  TRP D CD2 1 
ATOM   6637  N  NE1 . TRP D  1 15  ? 17.106  12.689  -40.842 1.00 8.72  ? 15  TRP D NE1 1 
ATOM   6638  C  CE2 . TRP D  1 15  ? 16.479  11.846  -39.962 1.00 7.40  ? 15  TRP D CE2 1 
ATOM   6639  C  CE3 . TRP D  1 15  ? 16.086  11.672  -37.553 1.00 7.36  ? 15  TRP D CE3 1 
ATOM   6640  C  CZ2 . TRP D  1 15  ? 15.795  10.637  -40.232 1.00 8.73  ? 15  TRP D CZ2 1 
ATOM   6641  C  CZ3 . TRP D  1 15  ? 15.372  10.461  -37.799 1.00 8.03  ? 15  TRP D CZ3 1 
ATOM   6642  C  CH2 . TRP D  1 15  ? 15.222  9.990   -39.146 1.00 7.18  ? 15  TRP D CH2 1 
ATOM   6643  N  N   . SER D  1 16  ? 19.729  16.209  -35.841 1.00 9.07  ? 16  SER D N   1 
ATOM   6644  C  CA  . SER D  1 16  ? 19.826  17.024  -34.604 1.00 9.23  ? 16  SER D CA  1 
ATOM   6645  C  C   . SER D  1 16  ? 20.299  18.459  -34.884 1.00 8.70  ? 16  SER D C   1 
ATOM   6646  O  O   . SER D  1 16  ? 20.089  19.266  -33.993 1.00 9.79  ? 16  SER D O   1 
ATOM   6647  C  CB  . SER D  1 16  ? 20.787  16.363  -33.649 1.00 10.63 ? 16  SER D CB  1 
ATOM   6648  O  OG  . SER D  1 16  ? 22.072  16.481  -34.171 1.00 14.06 ? 16  SER D OG  1 
ATOM   6649  N  N   . LYS D  1 17  ? 20.874  18.698  -36.065 1.00 8.68  ? 17  LYS D N   1 
ATOM   6650  C  CA  . LYS D  1 17  ? 21.330  20.074  -36.355 1.00 9.34  ? 17  LYS D CA  1 
ATOM   6651  C  C   . LYS D  1 17  ? 20.166  20.993  -36.463 1.00 10.26 ? 17  LYS D C   1 
ATOM   6652  O  O   . LYS D  1 17  ? 20.269  22.219  -36.146 1.00 11.28 ? 17  LYS D O   1 
ATOM   6653  C  CB  . LYS D  1 17  ? 22.069  20.095  -37.668 1.00 9.07  ? 17  LYS D CB  1 
ATOM   6654  C  CG  . LYS D  1 17  ? 23.371  19.284  -37.672 1.00 11.13 ? 17  LYS D CG  1 
ATOM   6655  C  CD  . LYS D  1 17  ? 23.961  19.241  -39.097 1.00 10.80 ? 17  LYS D CD  1 
ATOM   6656  C  CE  . LYS D  1 17  ? 25.106  18.278  -39.186 1.00 10.34 ? 17  LYS D CE  1 
ATOM   6657  N  NZ  . LYS D  1 17  ? 25.750  18.496  -40.557 1.00 11.90 ? 17  LYS D NZ  1 
ATOM   6658  N  N   . LYS D  1 18  ? 19.029  20.520  -36.935 1.00 9.23  ? 18  LYS D N   1 
ATOM   6659  C  CA  . LYS D  1 18  ? 17.780  21.329  -37.092 1.00 9.74  ? 18  LYS D CA  1 
ATOM   6660  C  C   . LYS D  1 18  ? 16.689  20.950  -36.067 1.00 10.18 ? 18  LYS D C   1 
ATOM   6661  O  O   . LYS D  1 18  ? 15.750  21.700  -35.890 1.00 12.78 ? 18  LYS D O   1 
ATOM   6662  C  CB  . LYS D  1 18  ? 17.205  21.152  -38.484 1.00 12.22 ? 18  LYS D CB  1 
ATOM   6663  C  CG  . LYS D  1 18  ? 18.053  21.924  -39.581 1.00 14.53 ? 18  LYS D CG  1 
ATOM   6664  C  CD  . LYS D  1 18  ? 17.504  21.563  -40.990 1.00 15.96 ? 18  LYS D CD  1 
ATOM   6665  C  CE  . LYS D  1 18  ? 18.237  22.414  -42.061 1.00 21.64 ? 18  LYS D CE  1 
ATOM   6666  N  NZ  . LYS D  1 18  ? 17.968  21.747  -43.404 1.00 27.26 ? 18  LYS D NZ  1 
ATOM   6667  N  N   . TYR D  1 19  ? 16.760  19.745  -35.511 1.00 9.41  ? 19  TYR D N   1 
ATOM   6668  C  CA  . TYR D  1 19  ? 15.628  19.204  -34.685 1.00 9.16  ? 19  TYR D CA  1 
ATOM   6669  C  C   . TYR D  1 19  ? 16.306  18.722  -33.426 1.00 9.38  ? 19  TYR D C   1 
ATOM   6670  O  O   . TYR D  1 19  ? 16.767  17.523  -33.372 1.00 9.79  ? 19  TYR D O   1 
ATOM   6671  C  CB  . TYR D  1 19  ? 14.990  18.020  -35.481 1.00 8.85  ? 19  TYR D CB  1 
ATOM   6672  C  CG  . TYR D  1 19  ? 14.389  18.460  -36.755 1.00 9.41  ? 19  TYR D CG  1 
ATOM   6673  C  CD1 . TYR D  1 19  ? 13.164  19.133  -36.839 1.00 10.80 ? 19  TYR D CD1 1 
ATOM   6674  C  CD2 . TYR D  1 19  ? 15.098  18.212  -37.975 1.00 9.72  ? 19  TYR D CD2 1 
ATOM   6675  C  CE1 . TYR D  1 19  ? 12.634  19.544  -38.041 1.00 11.84 ? 19  TYR D CE1 1 
ATOM   6676  C  CE2 . TYR D  1 19  ? 14.525  18.589  -39.209 1.00 10.16 ? 19  TYR D CE2 1 
ATOM   6677  C  CZ  . TYR D  1 19  ? 13.321  19.223  -39.196 1.00 11.97 ? 19  TYR D CZ  1 
ATOM   6678  O  OH  . TYR D  1 19  ? 12.725  19.626  -40.396 1.00 15.84 ? 19  TYR D OH  1 
ATOM   6679  N  N   . PRO D  1 20  ? 16.450  19.604  -32.407 1.00 9.42  ? 20  PRO D N   1 
ATOM   6680  C  CA  . PRO D  1 20  ? 17.250  19.225  -31.263 1.00 10.13 ? 20  PRO D CA  1 
ATOM   6681  C  C   . PRO D  1 20  ? 16.772  17.923  -30.530 1.00 9.35  ? 20  PRO D C   1 
ATOM   6682  O  O   . PRO D  1 20  ? 17.631  17.250  -29.941 1.00 9.81  ? 20  PRO D O   1 
ATOM   6683  C  CB  . PRO D  1 20  ? 17.202  20.459  -30.302 1.00 11.64 ? 20  PRO D CB  1 
ATOM   6684  C  CG  . PRO D  1 20  ? 16.466  21.427  -31.050 1.00 14.79 ? 20  PRO D CG  1 
ATOM   6685  C  CD  . PRO D  1 20  ? 15.932  20.994  -32.390 1.00 9.41  ? 20  PRO D CD  1 
ATOM   6686  N  N   . SER D  1 21  ? 15.452  17.651  -30.562 1.00 9.62  ? 21  SER D N   1 
ATOM   6687  C  CA  . SER D  1 21  ? 15.014  16.392  -29.834 1.00 9.98  ? 21  SER D CA  1 
ATOM   6688  C  C   . SER D  1 21  ? 15.575  15.157  -30.481 1.00 9.64  ? 21  SER D C   1 
ATOM   6689  O  O   . SER D  1 21  ? 15.676  14.145  -29.816 1.00 10.42 ? 21  SER D O   1 
ATOM   6690  C  CB  . SER D  1 21  ? 13.513  16.283  -29.783 1.00 10.17 ? 21  SER D CB  1 
ATOM   6691  O  OG  . SER D  1 21  ? 12.995  17.370  -28.942 1.00 13.64 ? 21  SER D OG  1 
ATOM   6692  N  N   . CYS D  1 22  ? 16.041  15.177  -31.738 1.00 10.15 ? 22  CYS D N   1 
ATOM   6693  C  CA  . CYS D  1 22  ? 16.611  14.015  -32.377 1.00 8.87  ? 22  CYS D CA  1 
ATOM   6694  C  C   . CYS D  1 22  ? 17.938  13.701  -31.747 1.00 11.10 ? 22  CYS D C   1 
ATOM   6695  O  O   . CYS D  1 22  ? 18.431  12.625  -31.918 1.00 10.94 ? 22  CYS D O   1 
ATOM   6696  C  CB  . CYS D  1 22  ? 16.793  14.275  -33.868 1.00 9.51  ? 22  CYS D CB  1 
ATOM   6697  S  SG  . CYS D  1 22  ? 15.230  14.514  -34.769 1.00 9.55  ? 22  CYS D SG  1 
ATOM   6698  N  N   . GLY D  1 23  ? 18.585  14.671  -31.017 1.00 11.11 ? 23  GLY D N   1 
ATOM   6699  C  CA  . GLY D  1 23  ? 19.838  14.431  -30.211 1.00 11.33 ? 23  GLY D CA  1 
ATOM   6700  C  C   . GLY D  1 23  ? 19.563  14.396  -28.740 1.00 13.42 ? 23  GLY D C   1 
ATOM   6701  O  O   . GLY D  1 23  ? 20.521  14.480  -27.918 1.00 14.99 ? 23  GLY D O   1 
ATOM   6702  N  N   . GLY D  1 24  ? 18.302  14.302  -28.349 1.00 11.23 ? 24  GLY D N   1 
ATOM   6703  C  CA  . GLY D  1 24  ? 17.887  14.234  -26.895 1.00 13.85 ? 24  GLY D CA  1 
ATOM   6704  C  C   . GLY D  1 24  ? 17.710  12.809  -26.426 1.00 15.39 ? 24  GLY D C   1 
ATOM   6705  O  O   . GLY D  1 24  ? 18.203  11.882  -27.021 1.00 17.58 ? 24  GLY D O   1 
ATOM   6706  N  N   . LEU D  1 25  ? 17.144  12.686  -25.256 1.00 15.91 ? 25  LEU D N   1 
ATOM   6707  C  CA  . LEU D  1 25  ? 16.977  11.373  -24.674 1.00 15.01 ? 25  LEU D CA  1 
ATOM   6708  C  C   . LEU D  1 25  ? 15.716  10.679  -25.244 1.00 13.05 ? 25  LEU D C   1 
ATOM   6709  O  O   . LEU D  1 25  ? 14.810  11.290  -25.911 1.00 14.20 ? 25  LEU D O   1 
ATOM   6710  C  CB  . LEU D  1 25  ? 16.785  11.542  -23.114 1.00 18.15 ? 25  LEU D CB  1 
ATOM   6711  C  CG  . LEU D  1 25  ? 18.064  12.195  -22.378 1.00 19.69 ? 25  LEU D CG  1 
ATOM   6712  C  CD1 . LEU D  1 25  ? 17.681  12.484  -20.925 1.00 23.05 ? 25  LEU D CD1 1 
ATOM   6713  C  CD2 . LEU D  1 25  ? 19.256  11.256  -22.469 1.00 23.56 ? 25  LEU D CD2 1 
ATOM   6714  N  N   . LEU D  1 26  ? 15.648  9.362   -24.885 1.00 13.44 ? 26  LEU D N   1 
ATOM   6715  C  CA  . LEU D  1 26  ? 14.406  8.537   -25.040 1.00 13.74 ? 26  LEU D CA  1 
ATOM   6716  C  C   . LEU D  1 26  ? 13.964  8.406   -26.517 1.00 10.08 ? 26  LEU D C   1 
ATOM   6717  O  O   . LEU D  1 26  ? 12.759  8.500   -26.880 1.00 11.19 ? 26  LEU D O   1 
ATOM   6718  C  CB  . LEU D  1 26  ? 13.237  9.057   -24.257 1.00 16.07 ? 26  LEU D CB  1 
ATOM   6719  C  CG  . LEU D  1 26  ? 13.601  9.358   -22.791 1.00 20.69 ? 26  LEU D CG  1 
ATOM   6720  C  CD1 . LEU D  1 26  ? 12.296  9.573   -22.106 1.00 22.71 ? 26  LEU D CD1 1 
ATOM   6721  C  CD2 . LEU D  1 26  ? 14.212  8.092   -22.099 1.00 21.06 ? 26  LEU D CD2 1 
ATOM   6722  N  N   . GLN D  1 27  ? 14.977  8.193   -27.339 1.00 10.49 ? 27  GLN D N   1 
ATOM   6723  C  CA  . GLN D  1 27  ? 14.684  8.119   -28.791 1.00 8.45  ? 27  GLN D CA  1 
ATOM   6724  C  C   . GLN D  1 27  ? 14.286  6.717   -29.215 1.00 8.91  ? 27  GLN D C   1 
ATOM   6725  O  O   . GLN D  1 27  ? 14.680  5.716   -28.627 1.00 10.00 ? 27  GLN D O   1 
ATOM   6726  C  CB  . GLN D  1 27  ? 15.920  8.528   -29.581 1.00 9.27  ? 27  GLN D CB  1 
ATOM   6727  C  CG  . GLN D  1 27  ? 16.282  10.023  -29.325 1.00 9.62  ? 27  GLN D CG  1 
ATOM   6728  C  CD  . GLN D  1 27  ? 15.246  10.897  -29.924 1.00 9.34  ? 27  GLN D CD  1 
ATOM   6729  O  OE1 . GLN D  1 27  ? 15.283  11.068  -31.196 1.00 9.36  ? 27  GLN D OE1 1 
ATOM   6730  N  NE2 . GLN D  1 27  ? 14.323  11.451  -29.176 1.00 10.34 ? 27  GLN D NE2 1 
ATOM   6731  N  N   . SER D  1 28  ? 13.540  6.692   -30.289 1.00 7.87  ? 28  SER D N   1 
ATOM   6732  C  CA  . SER D  1 28  ? 13.106  5.443   -30.957 1.00 8.15  ? 28  SER D CA  1 
ATOM   6733  C  C   . SER D  1 28  ? 13.638  5.395   -32.361 1.00 8.70  ? 28  SER D C   1 
ATOM   6734  O  O   . SER D  1 28  ? 13.954  6.448   -32.944 1.00 8.78  ? 28  SER D O   1 
ATOM   6735  C  CB  . SER D  1 28  ? 11.602  5.438   -30.997 1.00 7.60  ? 28  SER D CB  1 
ATOM   6736  O  OG  . SER D  1 28  ? 11.064  5.390   -29.672 1.00 8.11  ? 28  SER D OG  1 
ATOM   6737  N  N   . PRO D  1 29  ? 13.739  4.254   -33.006 1.00 7.15  ? 29  PRO D N   1 
ATOM   6738  C  CA  . PRO D  1 29  ? 13.417  2.887   -32.466 1.00 7.88  ? 29  PRO D CA  1 
ATOM   6739  C  C   . PRO D  1 29  ? 14.557  2.331   -31.638 1.00 7.63  ? 29  PRO D C   1 
ATOM   6740  O  O   . PRO D  1 29  ? 15.599  2.936   -31.503 1.00 8.66  ? 29  PRO D O   1 
ATOM   6741  C  CB  . PRO D  1 29  ? 13.198  2.122   -33.793 1.00 8.40  ? 29  PRO D CB  1 
ATOM   6742  C  CG  . PRO D  1 29  ? 14.314  2.680   -34.678 1.00 7.97  ? 29  PRO D CG  1 
ATOM   6743  C  CD  . PRO D  1 29  ? 14.311  4.182   -34.370 1.00 8.24  ? 29  PRO D CD  1 
ATOM   6744  N  N   . ILE D  1 30  ? 14.306  1.118   -31.180 1.00 7.49  ? 30  ILE D N   1 
ATOM   6745  C  CA  . ILE D  1 30  ? 15.229  0.353   -30.323 1.00 8.36  ? 30  ILE D CA  1 
ATOM   6746  C  C   . ILE D  1 30  ? 15.228  -1.093  -30.705 1.00 8.23  ? 30  ILE D C   1 
ATOM   6747  O  O   . ILE D  1 30  ? 14.345  -1.553  -31.431 1.00 8.54  ? 30  ILE D O   1 
ATOM   6748  C  CB  . ILE D  1 30  ? 14.952  0.510   -28.825 1.00 9.66  ? 30  ILE D CB  1 
ATOM   6749  C  CG1 . ILE D  1 30  ? 13.516  0.025   -28.538 1.00 10.37 ? 30  ILE D CG1 1 
ATOM   6750  C  CG2 . ILE D  1 30  ? 15.218  1.967   -28.324 1.00 10.15 ? 30  ILE D CG2 1 
ATOM   6751  C  CD1 . ILE D  1 30  ? 13.258  -0.057  -27.035 1.00 13.60 ? 30  ILE D CD1 1 
ATOM   6752  N  N   . ASP D  1 31  ? 16.341  -1.746  -30.305 1.00 8.23  ? 31  ASP D N   1 
ATOM   6753  C  CA  . ASP D  1 31  ? 16.423  -3.217  -30.453 1.00 9.60  ? 31  ASP D CA  1 
ATOM   6754  C  C   . ASP D  1 31  ? 15.772  -3.898  -29.283 1.00 11.19 ? 31  ASP D C   1 
ATOM   6755  O  O   . ASP D  1 31  ? 16.205  -3.761  -28.165 1.00 13.56 ? 31  ASP D O   1 
ATOM   6756  C  CB  . ASP D  1 31  ? 17.921  -3.635  -30.529 1.00 10.68 ? 31  ASP D CB  1 
ATOM   6757  C  CG  . ASP D  1 31  ? 18.023  -5.153  -30.694 1.00 13.30 ? 31  ASP D CG  1 
ATOM   6758  O  OD1 . ASP D  1 31  ? 17.426  -5.748  -31.617 1.00 10.94 ? 31  ASP D OD1 1 
ATOM   6759  O  OD2 . ASP D  1 31  ? 18.649  -5.754  -29.789 1.00 15.61 ? 31  ASP D OD2 1 
ATOM   6760  N  N   . LEU D  1 32  ? 14.842  -4.789  -29.537 1.00 10.10 ? 32  LEU D N   1 
ATOM   6761  C  CA  . LEU D  1 32  ? 14.073  -5.486  -28.472 1.00 10.50 ? 32  LEU D CA  1 
ATOM   6762  C  C   . LEU D  1 32  ? 14.869  -6.793  -28.220 1.00 12.05 ? 32  LEU D C   1 
ATOM   6763  O  O   . LEU D  1 32  ? 14.903  -7.678  -29.071 1.00 12.89 ? 32  LEU D O   1 
ATOM   6764  C  CB  . LEU D  1 32  ? 12.654  -5.766  -28.957 1.00 11.12 ? 32  LEU D CB  1 
ATOM   6765  C  CG  . LEU D  1 32  ? 11.939  -4.472  -29.396 1.00 10.81 ? 32  LEU D CG  1 
ATOM   6766  C  CD1 . LEU D  1 32  ? 10.629  -4.857  -30.062 1.00 11.23 ? 32  LEU D CD1 1 
ATOM   6767  C  CD2 . LEU D  1 32  ? 11.679  -3.608  -28.148 1.00 13.91 ? 32  LEU D CD2 1 
ATOM   6768  N  N   . HIS D  1 33  ? 15.564  -6.855  -27.078 1.00 11.13 ? 33  HIS D N   1 
ATOM   6769  C  CA  . HIS D  1 33  ? 16.357  -8.053  -26.802 1.00 11.55 ? 33  HIS D CA  1 
ATOM   6770  C  C   . HIS D  1 33  ? 16.283  -8.394  -25.304 1.00 11.82 ? 33  HIS D C   1 
ATOM   6771  O  O   . HIS D  1 33  ? 16.029  -7.501  -24.441 1.00 12.58 ? 33  HIS D O   1 
ATOM   6772  C  CB  . HIS D  1 33  ? 17.836  -7.875  -27.274 1.00 13.79 ? 33  HIS D CB  1 
ATOM   6773  C  CG  . HIS D  1 33  ? 18.609  -6.831  -26.557 1.00 12.87 ? 33  HIS D CG  1 
ATOM   6774  N  ND1 . HIS D  1 33  ? 18.470  -5.499  -26.821 1.00 14.31 ? 33  HIS D ND1 1 
ATOM   6775  C  CD2 . HIS D  1 33  ? 19.445  -6.912  -25.492 1.00 14.13 ? 33  HIS D CD2 1 
ATOM   6776  C  CE1 . HIS D  1 33  ? 19.241  -4.809  -25.975 1.00 17.30 ? 33  HIS D CE1 1 
ATOM   6777  N  NE2 . HIS D  1 33  ? 19.875  -5.683  -25.202 1.00 15.62 ? 33  HIS D NE2 1 
ATOM   6778  N  N   . SER D  1 34  ? 16.585  -9.669  -25.040 1.00 13.75 ? 34  SER D N   1 
ATOM   6779  C  CA  . SER D  1 34  ? 16.233  -10.239 -23.698 1.00 12.92 ? 34  SER D CA  1 
ATOM   6780  C  C   . SER D  1 34  ? 16.724  -9.403  -22.509 1.00 14.25 ? 34  SER D C   1 
ATOM   6781  O  O   . SER D  1 34  ? 15.964  -9.257  -21.525 1.00 13.10 ? 34  SER D O   1 
ATOM   6782  C  CB  . SER D  1 34  ? 16.786  -11.673 -23.709 1.00 15.56 ? 34  SER D CB  1 
ATOM   6783  O  OG  . SER D  1 34  ? 18.201  -11.603 -23.659 1.00 21.12 ? 34  SER D OG  1 
ATOM   6784  N  N   . ASP D  1 35  ? 17.917  -8.847  -22.516 1.00 12.57 ? 35  ASP D N   1 
ATOM   6785  C  CA  . ASP D  1 35  ? 18.477  -8.267  -21.318 1.00 13.56 ? 35  ASP D CA  1 
ATOM   6786  C  C   . ASP D  1 35  ? 17.704  -7.099  -20.850 1.00 13.05 ? 35  ASP D C   1 
ATOM   6787  O  O   . ASP D  1 35  ? 17.780  -6.703  -19.703 1.00 16.33 ? 35  ASP D O   1 
ATOM   6788  C  CB  . ASP D  1 35  ? 19.941  -7.736  -21.574 1.00 16.36 ? 35  ASP D CB  1 
ATOM   6789  C  CG  . ASP D  1 35  ? 20.844  -8.729  -22.272 1.00 18.56 ? 35  ASP D CG  1 
ATOM   6790  O  OD1 . ASP D  1 35  ? 21.832  -9.134  -21.570 1.00 16.75 ? 35  ASP D OD1 1 
ATOM   6791  O  OD2 . ASP D  1 35  ? 20.617  -9.144  -23.463 1.00 19.82 ? 35  ASP D OD2 1 
ATOM   6792  N  N   . ILE D  1 36  ? 16.997  -6.405  -21.777 1.00 12.69 ? 36  ILE D N   1 
ATOM   6793  C  CA  . ILE D  1 36  ? 16.195  -5.209  -21.430 1.00 12.22 ? 36  ILE D CA  1 
ATOM   6794  C  C   . ILE D  1 36  ? 14.702  -5.403  -21.348 1.00 13.41 ? 36  ILE D C   1 
ATOM   6795  O  O   . ILE D  1 36  ? 13.986  -4.397  -21.109 1.00 13.64 ? 36  ILE D O   1 
ATOM   6796  C  CB  . ILE D  1 36  ? 16.604  -3.946  -22.211 1.00 14.65 ? 36  ILE D CB  1 
ATOM   6797  C  CG1 . ILE D  1 36  ? 16.518  -4.178  -23.730 1.00 16.93 ? 36  ILE D CG1 1 
ATOM   6798  C  CG2 . ILE D  1 36  ? 18.053  -3.561  -21.834 1.00 18.78 ? 36  ILE D CG2 1 
ATOM   6799  C  CD1 . ILE D  1 36  ? 15.140  -4.423  -24.297 1.00 16.18 ? 36  ILE D CD1 1 
ATOM   6800  N  N   . LEU D  1 37  ? 14.249  -6.655  -21.463 1.00 11.65 ? 37  LEU D N   1 
ATOM   6801  C  CA  . LEU D  1 37  ? 12.827  -6.969  -21.323 1.00 13.07 ? 37  LEU D CA  1 
ATOM   6802  C  C   . LEU D  1 37  ? 12.431  -7.288  -19.917 1.00 14.70 ? 37  LEU D C   1 
ATOM   6803  O  O   . LEU D  1 37  ? 13.203  -7.990  -19.188 1.00 16.05 ? 37  LEU D O   1 
ATOM   6804  C  CB  . LEU D  1 37  ? 12.440  -8.147  -22.207 1.00 13.28 ? 37  LEU D CB  1 
ATOM   6805  C  CG  . LEU D  1 37  ? 12.764  -8.014  -23.724 1.00 13.17 ? 37  LEU D CG  1 
ATOM   6806  C  CD1 . LEU D  1 37  ? 12.302  -9.222  -24.471 1.00 17.04 ? 37  LEU D CD1 1 
ATOM   6807  C  CD2 . LEU D  1 37  ? 12.047  -6.817  -24.315 1.00 13.63 ? 37  LEU D CD2 1 
ATOM   6808  N  N   . GLN D  1 38  ? 11.308  -6.772  -19.522 1.00 12.31 ? 38  GLN D N   1 
ATOM   6809  C  CA  . GLN D  1 38  ? 10.782  -7.174  -18.176 1.00 13.29 ? 38  GLN D CA  1 
ATOM   6810  C  C   . GLN D  1 38  ? 9.280   -7.374  -18.263 1.00 13.07 ? 38  GLN D C   1 
ATOM   6811  O  O   . GLN D  1 38  ? 8.586   -6.441  -18.671 1.00 11.44 ? 38  GLN D O   1 
ATOM   6812  C  CB  . GLN D  1 38  ? 11.123  -6.093  -17.253 1.00 16.12 ? 38  GLN D CB  1 
ATOM   6813  C  CG  . GLN D  1 38  ? 10.785  -6.517  -15.801 1.00 19.25 ? 38  GLN D CG  1 
ATOM   6814  C  CD  . GLN D  1 38  ? 11.269  -5.531  -14.819 1.00 24.14 ? 38  GLN D CD  1 
ATOM   6815  O  OE1 . GLN D  1 38  ? 12.456  -5.498  -14.546 1.00 28.40 ? 38  GLN D OE1 1 
ATOM   6816  N  NE2 . GLN D  1 38  ? 10.405  -4.621  -14.392 1.00 24.49 ? 38  GLN D NE2 1 
ATOM   6817  N  N   . TYR D  1 39  ? 8.768   -8.507  -17.776 1.00 12.22 ? 39  TYR D N   1 
ATOM   6818  C  CA  . TYR D  1 39  ? 7.341   -8.765  -17.801 1.00 9.81  ? 39  TYR D CA  1 
ATOM   6819  C  C   . TYR D  1 39  ? 6.646   -7.792  -16.794 1.00 10.37 ? 39  TYR D C   1 
ATOM   6820  O  O   . TYR D  1 39  ? 7.203   -7.536  -15.722 1.00 12.59 ? 39  TYR D O   1 
ATOM   6821  C  CB  . TYR D  1 39  ? 7.118   -10.207 -17.363 1.00 11.36 ? 39  TYR D CB  1 
ATOM   6822  C  CG  . TYR D  1 39  ? 5.659   -10.476 -17.059 1.00 11.93 ? 39  TYR D CG  1 
ATOM   6823  C  CD1 . TYR D  1 39  ? 4.711   -10.510 -18.077 1.00 13.20 ? 39  TYR D CD1 1 
ATOM   6824  C  CD2 . TYR D  1 39  ? 5.217   -10.656 -15.753 1.00 12.05 ? 39  TYR D CD2 1 
ATOM   6825  C  CE1 . TYR D  1 39  ? 3.380   -10.737 -17.810 1.00 12.17 ? 39  TYR D CE1 1 
ATOM   6826  C  CE2 . TYR D  1 39  ? 3.875   -10.887 -15.477 1.00 12.40 ? 39  TYR D CE2 1 
ATOM   6827  C  CZ  . TYR D  1 39  ? 2.968   -10.926 -16.518 1.00 13.25 ? 39  TYR D CZ  1 
ATOM   6828  O  OH  . TYR D  1 39  ? 1.626   -11.151 -16.297 1.00 16.43 ? 39  TYR D OH  1 
ATOM   6829  N  N   . ASP D  1 40  ? 5.528   -7.194  -17.202 1.00 9.18  ? 40  ASP D N   1 
ATOM   6830  C  CA  . ASP D  1 40  ? 4.748   -6.275  -16.332 1.00 10.72 ? 40  ASP D CA  1 
ATOM   6831  C  C   . ASP D  1 40  ? 3.351   -6.714  -16.472 1.00 11.33 ? 40  ASP D C   1 
ATOM   6832  O  O   . ASP D  1 40  ? 2.657   -6.588  -17.546 1.00 11.49 ? 40  ASP D O   1 
ATOM   6833  C  CB  . ASP D  1 40  ? 4.973   -4.891  -16.949 1.00 12.44 ? 40  ASP D CB  1 
ATOM   6834  C  CG  . ASP D  1 40  ? 4.283   -3.819  -16.170 1.00 17.48 ? 40  ASP D CG  1 
ATOM   6835  O  OD1 . ASP D  1 40  ? 3.476   -4.134  -15.250 1.00 14.49 ? 40  ASP D OD1 1 
ATOM   6836  O  OD2 . ASP D  1 40  ? 4.427   -2.624  -16.527 1.00 20.69 ? 40  ASP D OD2 1 
ATOM   6837  N  N   . ALA D  1 41  ? 2.778   -7.213  -15.295 1.00 9.00  ? 41  ALA D N   1 
ATOM   6838  C  CA  . ALA D  1 41  ? 1.368   -7.671  -15.287 1.00 11.39 ? 41  ALA D CA  1 
ATOM   6839  C  C   . ALA D  1 41  ? 0.368   -6.520  -15.402 1.00 11.85 ? 41  ALA D C   1 
ATOM   6840  O  O   . ALA D  1 41  ? -0.782  -6.785  -15.636 1.00 13.06 ? 41  ALA D O   1 
ATOM   6841  C  CB  . ALA D  1 41  ? 1.140   -8.378  -13.923 1.00 12.27 ? 41  ALA D CB  1 
ATOM   6842  N  N   . SER D  1 42  ? 0.841   -5.268  -15.370 1.00 11.31 ? 42  SER D N   1 
ATOM   6843  C  CA  . SER D  1 42  ? -0.055  -4.115  -15.581 1.00 13.46 ? 42  SER D CA  1 
ATOM   6844  C  C   . SER D  1 42  ? -0.456  -3.951  -17.023 1.00 13.67 ? 42  SER D C   1 
ATOM   6845  O  O   . SER D  1 42  ? -1.347  -3.096  -17.339 1.00 16.57 ? 42  SER D O   1 
ATOM   6846  C  CB  . SER D  1 42  ? 0.512   -2.857  -14.929 1.00 15.61 ? 42  SER D CB  1 
ATOM   6847  O  OG  . SER D  1 42  ? 1.452   -2.326  -15.801 1.00 19.26 ? 42  SER D OG  1 
ATOM   6848  N  N   . LEU D  1 43  ? 0.276   -4.630  -17.934 1.00 12.62 ? 43  LEU D N   1 
ATOM   6849  C  CA  . LEU D  1 43  ? 0.031   -4.490  -19.366 1.00 13.02 ? 43  LEU D CA  1 
ATOM   6850  C  C   . LEU D  1 43  ? -1.100  -5.349  -19.831 1.00 13.14 ? 43  LEU D C   1 
ATOM   6851  O  O   . LEU D  1 43  ? -0.973  -6.456  -20.357 1.00 13.28 ? 43  LEU D O   1 
ATOM   6852  C  CB  . LEU D  1 43  ? 1.344   -4.748  -20.116 1.00 12.47 ? 43  LEU D CB  1 
ATOM   6853  C  CG  . LEU D  1 43  ? 2.446   -3.784  -19.835 1.00 13.19 ? 43  LEU D CG  1 
ATOM   6854  C  CD1 . LEU D  1 43  ? 3.642   -4.265  -20.656 1.00 12.64 ? 43  LEU D CD1 1 
ATOM   6855  C  CD2 . LEU D  1 43  ? 2.162   -2.305  -20.067 1.00 15.50 ? 43  LEU D CD2 1 
ATOM   6856  N  N   . THR D  1 44  ? -2.316  -4.784  -19.725 1.00 14.19 ? 44  THR D N   1 
ATOM   6857  C  CA  . THR D  1 44  ? -3.508  -5.506  -20.026 1.00 14.12 ? 44  THR D CA  1 
ATOM   6858  C  C   . THR D  1 44  ? -3.898  -5.312  -21.519 1.00 13.14 ? 44  THR D C   1 
ATOM   6859  O  O   . THR D  1 44  ? -3.277  -4.472  -22.177 1.00 12.86 ? 44  THR D O   1 
ATOM   6860  C  CB  . THR D  1 44  ? -4.674  -4.921  -19.106 1.00 14.16 ? 44  THR D CB  1 
ATOM   6861  O  OG1 . THR D  1 44  ? -4.686  -3.535  -19.255 1.00 19.29 ? 44  THR D OG1 1 
ATOM   6862  C  CG2 . THR D  1 44  ? -4.389  -5.223  -17.645 1.00 19.55 ? 44  THR D CG2 1 
ATOM   6863  N  N   . PRO D  1 45  ? -4.805  -6.108  -22.028 1.00 14.11 ? 45  PRO D N   1 
ATOM   6864  C  CA  . PRO D  1 45  ? -5.072  -6.063  -23.499 1.00 14.59 ? 45  PRO D CA  1 
ATOM   6865  C  C   . PRO D  1 45  ? -5.657  -4.734  -23.970 1.00 15.40 ? 45  PRO D C   1 
ATOM   6866  O  O   . PRO D  1 45  ? -6.502  -4.200  -23.293 1.00 18.13 ? 45  PRO D O   1 
ATOM   6867  C  CB  . PRO D  1 45  ? -6.054  -7.178  -23.676 1.00 17.21 ? 45  PRO D CB  1 
ATOM   6868  C  CG  . PRO D  1 45  ? -5.824  -8.103  -22.488 1.00 17.11 ? 45  PRO D CG  1 
ATOM   6869  C  CD  . PRO D  1 45  ? -5.532  -7.180  -21.354 1.00 15.79 ? 45  PRO D CD  1 
ATOM   6870  N  N   . LEU D  1 46  ? -5.131  -4.171  -25.075 1.00 12.86 ? 46  LEU D N   1 
ATOM   6871  C  CA  . LEU D  1 46  ? -5.768  -2.994  -25.679 1.00 13.56 ? 46  LEU D CA  1 
ATOM   6872  C  C   . LEU D  1 46  ? -6.998  -3.396  -26.385 1.00 13.45 ? 46  LEU D C   1 
ATOM   6873  O  O   . LEU D  1 46  ? -7.160  -4.514  -26.902 1.00 14.38 ? 46  LEU D O   1 
ATOM   6874  C  CB  . LEU D  1 46  ? -4.810  -2.416  -26.699 1.00 15.83 ? 46  LEU D CB  1 
ATOM   6875  C  CG  . LEU D  1 46  ? -3.546  -1.899  -26.041 1.00 15.32 ? 46  LEU D CG  1 
ATOM   6876  C  CD1 . LEU D  1 46  ? -2.599  -1.455  -27.174 1.00 20.36 ? 46  LEU D CD1 1 
ATOM   6877  C  CD2 . LEU D  1 46  ? -3.826  -0.840  -24.914 1.00 19.09 ? 46  LEU D CD2 1 
ATOM   6878  N  N   . GLU D  1 47  ? -7.933  -2.435  -26.431 1.00 13.81 ? 47  GLU D N   1 
ATOM   6879  C  CA  . GLU D  1 47  ? -9.061  -2.597  -27.254 1.00 14.13 ? 47  GLU D CA  1 
ATOM   6880  C  C   . GLU D  1 47  ? -9.049  -1.567  -28.443 1.00 13.79 ? 47  GLU D C   1 
ATOM   6881  O  O   . GLU D  1 47  ? -8.664  -0.345  -28.235 1.00 13.78 ? 47  GLU D O   1 
ATOM   6882  C  CB  . GLU D  1 47  ? -10.395 -2.459  -26.460 1.00 19.04 ? 47  GLU D CB  1 
ATOM   6883  C  CG  . GLU D  1 47  ? -10.776 -3.783  -25.751 1.00 29.17 ? 47  GLU D CG  1 
ATOM   6884  C  CD  . GLU D  1 47  ? -12.011 -3.647  -24.845 1.00 41.34 ? 47  GLU D CD  1 
ATOM   6885  O  OE1 . GLU D  1 47  ? -12.097 -2.617  -24.112 1.00 52.52 ? 47  GLU D OE1 1 
ATOM   6886  O  OE2 . GLU D  1 47  ? -12.858 -4.565  -24.857 1.00 48.10 ? 47  GLU D OE2 1 
ATOM   6887  N  N   . PHE D  1 48  ? -9.390  -2.073  -29.610 1.00 14.32 ? 48  PHE D N   1 
ATOM   6888  C  CA  . PHE D  1 48  ? -9.339  -1.243  -30.873 1.00 13.85 ? 48  PHE D CA  1 
ATOM   6889  C  C   . PHE D  1 48  ? -10.742 -0.933  -31.214 1.00 16.59 ? 48  PHE D C   1 
ATOM   6890  O  O   . PHE D  1 48  ? -11.449 -1.776  -31.692 1.00 19.11 ? 48  PHE D O   1 
ATOM   6891  C  CB  . PHE D  1 48  ? -8.608  -2.057  -31.988 1.00 14.42 ? 48  PHE D CB  1 
ATOM   6892  C  CG  . PHE D  1 48  ? -7.304  -2.626  -31.488 1.00 13.84 ? 48  PHE D CG  1 
ATOM   6893  C  CD1 . PHE D  1 48  ? -6.270  -1.830  -31.182 1.00 13.09 ? 48  PHE D CD1 1 
ATOM   6894  C  CD2 . PHE D  1 48  ? -7.192  -4.015  -31.234 1.00 15.36 ? 48  PHE D CD2 1 
ATOM   6895  C  CE1 . PHE D  1 48  ? -5.124  -2.335  -30.547 1.00 14.81 ? 48  PHE D CE1 1 
ATOM   6896  C  CE2 . PHE D  1 48  ? -6.036  -4.593  -30.649 1.00 15.46 ? 48  PHE D CE2 1 
ATOM   6897  C  CZ  . PHE D  1 48  ? -4.983  -3.733  -30.343 1.00 14.06 ? 48  PHE D CZ  1 
ATOM   6898  N  N   . GLN D  1 49  ? -11.110 0.341   -31.087 1.00 12.46 ? 49  GLN D N   1 
ATOM   6899  C  CA  . GLN D  1 49  ? -12.476 0.768   -31.231 1.00 15.21 ? 49  GLN D CA  1 
ATOM   6900  C  C   . GLN D  1 49  ? -12.618 1.645   -32.467 1.00 13.18 ? 49  GLN D C   1 
ATOM   6901  O  O   . GLN D  1 49  ? -11.826 2.546   -32.754 1.00 13.06 ? 49  GLN D O   1 
ATOM   6902  C  CB  . GLN D  1 49  ? -12.916 1.600   -30.043 1.00 19.81 ? 49  GLN D CB  1 
ATOM   6903  C  CG  . GLN D  1 49  ? -12.759 0.971   -28.671 1.00 27.34 ? 49  GLN D CG  1 
ATOM   6904  C  CD  . GLN D  1 49  ? -13.740 -0.142  -28.304 1.00 39.06 ? 49  GLN D CD  1 
ATOM   6905  O  OE1 . GLN D  1 49  ? -14.560 -0.605  -29.116 1.00 46.98 ? 49  GLN D OE1 1 
ATOM   6906  N  NE2 . GLN D  1 49  ? -13.671 -0.566  -27.020 1.00 41.37 ? 49  GLN D NE2 1 
ATOM   6907  N  N   . GLY D  1 50  ? -13.632 1.345   -33.281 1.00 12.62 ? 50  GLY D N   1 
ATOM   6908  C  CA  . GLY D  1 50  ? -13.883 2.105   -34.490 1.00 14.27 ? 50  GLY D CA  1 
ATOM   6909  C  C   . GLY D  1 50  ? -12.847 1.930   -35.600 1.00 10.55 ? 50  GLY D C   1 
ATOM   6910  O  O   . GLY D  1 50  ? -12.753 2.771   -36.481 1.00 12.86 ? 50  GLY D O   1 
ATOM   6911  N  N   . TYR D  1 51  ? -12.190 0.795   -35.519 1.00 11.15 ? 51  TYR D N   1 
ATOM   6912  C  CA  . TYR D  1 51  ? -11.164 0.411   -36.559 1.00 10.88 ? 51  TYR D CA  1 
ATOM   6913  C  C   . TYR D  1 51  ? -11.828 -0.116  -37.785 1.00 11.31 ? 51  TYR D C   1 
ATOM   6914  O  O   . TYR D  1 51  ? -11.201 -0.179  -38.848 1.00 10.87 ? 51  TYR D O   1 
ATOM   6915  C  CB  . TYR D  1 51  ? -10.188 -0.658  -36.007 1.00 9.72  ? 51  TYR D CB  1 
ATOM   6916  C  CG  . TYR D  1 51  ? -8.989  -0.074  -35.236 1.00 9.29  ? 51  TYR D CG  1 
ATOM   6917  C  CD1 . TYR D  1 51  ? -9.105  0.951   -34.273 1.00 10.85 ? 51  TYR D CD1 1 
ATOM   6918  C  CD2 . TYR D  1 51  ? -7.716  -0.538  -35.546 1.00 9.68  ? 51  TYR D CD2 1 
ATOM   6919  C  CE1 . TYR D  1 51  ? -8.001  1.457   -33.631 1.00 10.27 ? 51  TYR D CE1 1 
ATOM   6920  C  CE2 . TYR D  1 51  ? -6.598  0.005   -34.865 1.00 10.49 ? 51  TYR D CE2 1 
ATOM   6921  C  CZ  . TYR D  1 51  ? -6.765  0.960   -33.935 1.00 10.89 ? 51  TYR D CZ  1 
ATOM   6922  O  OH  . TYR D  1 51  ? -5.599  1.438   -33.405 1.00 12.21 ? 51  TYR D OH  1 
ATOM   6923  N  N   . ASN D  1 52  ? -13.127 -0.525  -37.723 1.00 12.08 ? 52  ASN D N   1 
ATOM   6924  C  CA  . ASN D  1 52  ? -13.743 -1.065  -38.894 1.00 12.64 ? 52  ASN D CA  1 
ATOM   6925  C  C   . ASN D  1 52  ? -14.343 0.046   -39.710 1.00 15.26 ? 52  ASN D C   1 
ATOM   6926  O  O   . ASN D  1 52  ? -15.509 0.390   -39.566 1.00 16.18 ? 52  ASN D O   1 
ATOM   6927  C  CB  . ASN D  1 52  ? -14.793 -2.081  -38.469 1.00 15.27 ? 52  ASN D CB  1 
ATOM   6928  C  CG  . ASN D  1 52  ? -15.332 -2.869  -39.627 1.00 19.71 ? 52  ASN D CG  1 
ATOM   6929  O  OD1 . ASN D  1 52  ? -15.025 -2.684  -40.749 1.00 21.80 ? 52  ASN D OD1 1 
ATOM   6930  N  ND2 . ASN D  1 52  ? -16.191 -3.770  -39.290 1.00 24.93 ? 52  ASN D ND2 1 
ATOM   6931  N  N   . LEU D  1 53  ? -13.545 0.600   -40.587 1.00 12.44 ? 53  LEU D N   1 
ATOM   6932  C  CA  . LEU D  1 53  ? -13.944 1.804   -41.370 1.00 11.95 ? 53  LEU D CA  1 
ATOM   6933  C  C   . LEU D  1 53  ? -14.931 1.345   -42.493 1.00 14.35 ? 53  LEU D C   1 
ATOM   6934  O  O   . LEU D  1 53  ? -14.726 0.336   -43.184 1.00 13.78 ? 53  LEU D O   1 
ATOM   6935  C  CB  . LEU D  1 53  ? -12.691 2.520   -41.944 1.00 12.82 ? 53  LEU D CB  1 
ATOM   6936  C  CG  . LEU D  1 53  ? -11.653 2.881   -40.853 1.00 13.11 ? 53  LEU D CG  1 
ATOM   6937  C  CD1 . LEU D  1 53  ? -10.560 3.644   -41.589 1.00 14.97 ? 53  LEU D CD1 1 
ATOM   6938  C  CD2 . LEU D  1 53  ? -12.298 3.766   -39.814 1.00 15.47 ? 53  LEU D CD2 1 
ATOM   6939  N  N   . SER D  1 54  ? -15.922 2.162   -42.745 1.00 13.70 ? 54  SER D N   1 
ATOM   6940  C  CA  . SER D  1 54  ? -16.925 1.767   -43.749 1.00 12.99 ? 54  SER D CA  1 
ATOM   6941  C  C   . SER D  1 54  ? -16.332 1.758   -45.172 1.00 12.58 ? 54  SER D C   1 
ATOM   6942  O  O   . SER D  1 54  ? -15.697 2.736   -45.588 1.00 12.31 ? 54  SER D O   1 
ATOM   6943  C  CB  . SER D  1 54  ? -18.115 2.753   -43.680 1.00 14.66 ? 54  SER D CB  1 
ATOM   6944  O  OG  . SER D  1 54  ? -18.984 2.440   -44.761 1.00 15.51 ? 54  SER D OG  1 
ATOM   6945  N  N   . ALA D  1 55  ? -16.626 0.710   -45.900 1.00 14.35 ? 55  ALA D N   1 
ATOM   6946  C  CA  . ALA D  1 55  ? -16.219 0.646   -47.291 1.00 14.75 ? 55  ALA D CA  1 
ATOM   6947  C  C   . ALA D  1 55  ? -16.880 1.657   -48.182 1.00 15.12 ? 55  ALA D C   1 
ATOM   6948  O  O   . ALA D  1 55  ? -16.439 1.928   -49.319 1.00 17.78 ? 55  ALA D O   1 
ATOM   6949  C  CB  . ALA D  1 55  ? -16.530 -0.781  -47.862 1.00 20.61 ? 55  ALA D CB  1 
ATOM   6950  N  N   . ASN D  1 56  ? -17.922 2.343   -47.716 1.00 15.04 ? 56  ASN D N   1 
ATOM   6951  C  CA  . ASN D  1 56  ? -18.522 3.498   -48.432 1.00 15.85 ? 56  ASN D CA  1 
ATOM   6952  C  C   . ASN D  1 56  ? -17.983 4.834   -48.089 1.00 15.54 ? 56  ASN D C   1 
ATOM   6953  O  O   . ASN D  1 56  ? -18.401 5.824   -48.712 1.00 18.81 ? 56  ASN D O   1 
ATOM   6954  C  CB  . ASN D  1 56  ? -20.090 3.565   -48.228 1.00 19.31 ? 56  ASN D CB  1 
ATOM   6955  C  CG  . ASN D  1 56  ? -20.800 2.392   -48.836 1.00 28.68 ? 56  ASN D CG  1 
ATOM   6956  O  OD1 . ASN D  1 56  ? -20.363 1.842   -49.848 1.00 27.03 ? 56  ASN D OD1 1 
ATOM   6957  N  ND2 . ASN D  1 56  ? -21.952 2.033   -48.257 1.00 32.84 ? 56  ASN D ND2 1 
ATOM   6958  N  N   . LYS D  1 57  ? -17.020 4.854   -47.178 1.00 13.80 ? 57  LYS D N   1 
ATOM   6959  C  CA  . LYS D  1 57  ? -16.317 6.097   -46.883 1.00 13.12 ? 57  LYS D CA  1 
ATOM   6960  C  C   . LYS D  1 57  ? -14.886 6.010   -47.486 1.00 13.40 ? 57  LYS D C   1 
ATOM   6961  O  O   . LYS D  1 57  ? -14.505 4.892   -47.979 1.00 13.95 ? 57  LYS D O   1 
ATOM   6962  C  CB  . LYS D  1 57  ? -16.219 6.336   -45.390 1.00 14.20 ? 57  LYS D CB  1 
ATOM   6963  C  CG  . LYS D  1 57  ? -17.604 6.641   -44.735 1.00 17.44 ? 57  LYS D CG  1 
ATOM   6964  C  CD  . LYS D  1 57  ? -17.376 7.112   -43.322 1.00 21.16 ? 57  LYS D CD  1 
ATOM   6965  C  CE  . LYS D  1 57  ? -18.716 7.345   -42.644 1.00 27.17 ? 57  LYS D CE  1 
ATOM   6966  N  NZ  . LYS D  1 57  ? -18.469 7.782   -41.221 1.00 29.35 ? 57  LYS D NZ  1 
ATOM   6967  N  N   . GLN D  1 58  ? -14.251 7.152   -47.575 1.00 13.26 ? 58  GLN D N   1 
ATOM   6968  C  CA  . GLN D  1 58  ? -12.930 7.085   -48.202 1.00 14.04 ? 58  GLN D CA  1 
ATOM   6969  C  C   . GLN D  1 58  ? -11.982 7.957   -47.350 1.00 12.07 ? 58  GLN D C   1 
ATOM   6970  O  O   . GLN D  1 58  ? -12.329 8.882   -46.671 1.00 13.44 ? 58  GLN D O   1 
ATOM   6971  C  CB  . GLN D  1 58  ? -12.963 7.375   -49.683 1.00 20.52 ? 58  GLN D CB  1 
ATOM   6972  C  CG  . GLN D  1 58  ? -13.350 8.731   -49.927 1.00 20.43 ? 58  GLN D CG  1 
ATOM   6973  C  CD  . GLN D  1 58  ? -13.588 9.011   -51.435 1.00 24.79 ? 58  GLN D CD  1 
ATOM   6974  O  OE1 . GLN D  1 58  ? -13.319 8.145   -52.357 1.00 24.10 ? 58  GLN D OE1 1 
ATOM   6975  N  NE2 . GLN D  1 58  ? -13.974 10.285  -51.691 1.00 23.97 ? 58  GLN D NE2 1 
ATOM   6976  N  N   . PHE D  1 59  ? -10.720 7.523   -47.383 1.00 10.83 ? 59  PHE D N   1 
ATOM   6977  C  CA  . PHE D  1 59  ? -9.633  8.034   -46.498 1.00 10.31 ? 59  PHE D CA  1 
ATOM   6978  C  C   . PHE D  1 59  ? -8.492  8.441   -47.362 1.00 9.14  ? 59  PHE D C   1 
ATOM   6979  O  O   . PHE D  1 59  ? -8.141  7.790   -48.356 1.00 10.75 ? 59  PHE D O   1 
ATOM   6980  C  CB  . PHE D  1 59  ? -9.325  6.972   -45.490 1.00 10.92 ? 59  PHE D CB  1 
ATOM   6981  C  CG  . PHE D  1 59  ? -10.517 6.641   -44.676 1.00 10.67 ? 59  PHE D CG  1 
ATOM   6982  C  CD1 . PHE D  1 59  ? -11.462 5.662   -45.113 1.00 11.97 ? 59  PHE D CD1 1 
ATOM   6983  C  CD2 . PHE D  1 59  ? -10.809 7.428   -43.554 1.00 12.49 ? 59  PHE D CD2 1 
ATOM   6984  C  CE1 . PHE D  1 59  ? -12.679 5.453   -44.432 1.00 10.83 ? 59  PHE D CE1 1 
ATOM   6985  C  CE2 . PHE D  1 59  ? -11.995 7.199   -42.867 1.00 11.76 ? 59  PHE D CE2 1 
ATOM   6986  C  CZ  . PHE D  1 59  ? -12.916 6.263   -43.314 1.00 11.31 ? 59  PHE D CZ  1 
ATOM   6987  N  N   . LEU D  1 60  ? -7.872  9.558   -46.995 1.00 9.57  ? 60  LEU D N   1 
ATOM   6988  C  CA  . LEU D  1 60  ? -6.859  10.150  -47.844 1.00 10.88 ? 60  LEU D CA  1 
ATOM   6989  C  C   . LEU D  1 60  ? -5.469  9.545   -47.680 1.00 10.06 ? 60  LEU D C   1 
ATOM   6990  O  O   . LEU D  1 60  ? -4.905  9.546   -46.559 1.00 10.81 ? 60  LEU D O   1 
ATOM   6991  C  CB  . LEU D  1 60  ? -6.808  11.641  -47.465 1.00 13.03 ? 60  LEU D CB  1 
ATOM   6992  C  CG  . LEU D  1 60  ? -5.971  12.453  -48.447 1.00 16.99 ? 60  LEU D CG  1 
ATOM   6993  C  CD1 . LEU D  1 60  ? -6.686  12.508  -49.801 1.00 18.87 ? 60  LEU D CD1 1 
ATOM   6994  C  CD2 . LEU D  1 60  ? -5.810  13.837  -47.825 1.00 21.71 ? 60  LEU D CD2 1 
ATOM   6995  N  N   . LEU D  1 61  ? -4.901  9.036   -48.745 1.00 10.44 ? 61  LEU D N   1 
ATOM   6996  C  CA  . LEU D  1 61  ? -3.516  8.505   -48.799 1.00 9.98  ? 61  LEU D CA  1 
ATOM   6997  C  C   . LEU D  1 61  ? -2.656  9.581   -49.404 1.00 10.37 ? 61  LEU D C   1 
ATOM   6998  O  O   . LEU D  1 61  ? -3.038  10.212  -50.456 1.00 13.03 ? 61  LEU D O   1 
ATOM   6999  C  CB  . LEU D  1 61  ? -3.520  7.262   -49.663 1.00 11.10 ? 61  LEU D CB  1 
ATOM   7000  C  CG  . LEU D  1 61  ? -2.249  6.422   -49.733 1.00 10.42 ? 61  LEU D CG  1 
ATOM   7001  C  CD1 . LEU D  1 61  ? -2.123  5.632   -48.432 1.00 12.28 ? 61  LEU D CD1 1 
ATOM   7002  C  CD2 . LEU D  1 61  ? -2.334  5.445   -50.911 1.00 13.80 ? 61  LEU D CD2 1 
ATOM   7003  N  N   . THR D  1 62  ? -1.499  9.866   -48.811 1.00 10.09 ? 62  THR D N   1 
ATOM   7004  C  CA  . THR D  1 62  ? -0.644  10.961  -49.315 1.00 11.93 ? 62  THR D CA  1 
ATOM   7005  C  C   . THR D  1 62  ? 0.806   10.487  -49.241 1.00 12.10 ? 62  THR D C   1 
ATOM   7006  O  O   . THR D  1 62  ? 1.241   9.787   -48.316 1.00 12.02 ? 62  THR D O   1 
ATOM   7007  C  CB  . THR D  1 62  ? -0.704  12.145  -48.346 1.00 15.13 ? 62  THR D CB  1 
ATOM   7008  O  OG1 . THR D  1 62  ? -2.056  12.642  -48.177 1.00 21.46 ? 62  THR D OG1 1 
ATOM   7009  C  CG2 . THR D  1 62  ? 0.041   13.360  -48.913 1.00 19.06 ? 62  THR D CG2 1 
ATOM   7010  N  N   . ASN D  1 63  ? 1.607   10.905  -50.196 1.00 11.41 ? 63  ASN D N   1 
ATOM   7011  C  CA  . ASN D  1 63  ? 3.091   10.804  -50.148 1.00 10.33 ? 63  ASN D CA  1 
ATOM   7012  C  C   . ASN D  1 63  ? 3.604   12.080  -49.550 1.00 10.23 ? 63  ASN D C   1 
ATOM   7013  O  O   . ASN D  1 63  ? 3.396   13.196  -50.111 1.00 11.09 ? 63  ASN D O   1 
ATOM   7014  C  CB  . ASN D  1 63  ? 3.560   10.612  -51.597 1.00 10.98 ? 63  ASN D CB  1 
ATOM   7015  C  CG  . ASN D  1 63  ? 5.083   10.600  -51.726 1.00 10.17 ? 63  ASN D CG  1 
ATOM   7016  O  OD1 . ASN D  1 63  ? 5.744   11.211  -50.876 1.00 10.33 ? 63  ASN D OD1 1 
ATOM   7017  N  ND2 . ASN D  1 63  ? 5.607   9.957   -52.745 1.00 10.31 ? 63  ASN D ND2 1 
ATOM   7018  N  N   . ASN D  1 64  ? 4.141   12.014  -48.340 1.00 10.73 ? 64  ASN D N   1 
ATOM   7019  C  CA  . ASN D  1 64  ? 4.575   13.260  -47.666 1.00 11.22 ? 64  ASN D CA  1 
ATOM   7020  C  C   . ASN D  1 64  ? 6.060   13.592  -47.855 1.00 11.81 ? 64  ASN D C   1 
ATOM   7021  O  O   . ASN D  1 64  ? 6.608   14.443  -47.108 1.00 13.62 ? 64  ASN D O   1 
ATOM   7022  C  CB  . ASN D  1 64  ? 4.189   13.208  -46.179 1.00 12.80 ? 64  ASN D CB  1 
ATOM   7023  C  CG  . ASN D  1 64  ? 4.925   12.128  -45.429 1.00 13.39 ? 64  ASN D CG  1 
ATOM   7024  O  OD1 . ASN D  1 64  ? 5.854   11.489  -45.945 1.00 11.98 ? 64  ASN D OD1 1 
ATOM   7025  N  ND2 . ASN D  1 64  ? 4.527   11.885  -44.154 1.00 15.60 ? 64  ASN D ND2 1 
ATOM   7026  N  N   . GLY D  1 65  ? 6.655   12.856  -48.792 1.00 11.03 ? 65  GLY D N   1 
ATOM   7027  C  CA  . GLY D  1 65  ? 8.084   13.054  -49.032 1.00 11.24 ? 65  GLY D CA  1 
ATOM   7028  C  C   . GLY D  1 65  ? 9.029   12.128  -48.230 1.00 11.62 ? 65  GLY D C   1 
ATOM   7029  O  O   . GLY D  1 65  ? 10.209  12.005  -48.499 1.00 11.47 ? 65  GLY D O   1 
ATOM   7030  N  N   . HIS D  1 66  ? 8.415   11.433  -47.253 1.00 11.15 ? 66  HIS D N   1 
ATOM   7031  C  CA  . HIS D  1 66  ? 9.216   10.603  -46.314 1.00 9.69  ? 66  HIS D CA  1 
ATOM   7032  C  C   . HIS D  1 66  ? 8.626   9.202   -46.167 1.00 9.34  ? 66  HIS D C   1 
ATOM   7033  O  O   . HIS D  1 66  ? 9.364   8.284   -45.790 1.00 9.68  ? 66  HIS D O   1 
ATOM   7034  C  CB  . HIS D  1 66  ? 9.329   11.287  -44.933 1.00 10.61 ? 66  HIS D CB  1 
ATOM   7035  C  CG  . HIS D  1 66  ? 9.871   12.672  -45.021 1.00 10.08 ? 66  HIS D CG  1 
ATOM   7036  N  ND1 . HIS D  1 66  ? 11.226  12.903  -45.234 1.00 10.74 ? 66  HIS D ND1 1 
ATOM   7037  C  CD2 . HIS D  1 66  ? 9.261   13.860  -44.849 1.00 11.43 ? 66  HIS D CD2 1 
ATOM   7038  C  CE1 . HIS D  1 66  ? 11.383  14.234  -45.219 1.00 10.57 ? 66  HIS D CE1 1 
ATOM   7039  N  NE2 . HIS D  1 66  ? 10.222  14.819  -44.969 1.00 11.64 ? 66  HIS D NE2 1 
ATOM   7040  N  N   . SER D  1 67  ? 7.303   9.042   -46.297 1.00 9.34  ? 67  SER D N   1 
ATOM   7041  C  CA  . SER D  1 67  ? 6.622   7.741   -46.259 1.00 8.98  ? 67  SER D CA  1 
ATOM   7042  C  C   . SER D  1 67  ? 5.321   7.919   -47.053 1.00 9.97  ? 67  SER D C   1 
ATOM   7043  O  O   . SER D  1 67  ? 5.071   8.969   -47.656 1.00 11.71 ? 67  SER D O   1 
ATOM   7044  C  CB  . SER D  1 67  ? 6.265   7.480   -44.785 1.00 9.60  ? 67  SER D CB  1 
ATOM   7045  O  OG  . SER D  1 67  ? 5.702   6.192   -44.642 1.00 9.86  ? 67  SER D OG  1 
ATOM   7046  N  N   . VAL D  1 68  ? 4.525   6.872   -47.052 1.00 9.43  ? 68  VAL D N   1 
ATOM   7047  C  CA  . VAL D  1 68  ? 3.160   6.952   -47.563 1.00 10.45 ? 68  VAL D CA  1 
ATOM   7048  C  C   . VAL D  1 68  ? 2.269   6.855   -46.306 1.00 9.89  ? 68  VAL D C   1 
ATOM   7049  O  O   . VAL D  1 68  ? 2.461   5.974   -45.467 1.00 10.16 ? 68  VAL D O   1 
ATOM   7050  C  CB  . VAL D  1 68  ? 2.907   5.857   -48.593 1.00 10.55 ? 68  VAL D CB  1 
ATOM   7051  C  CG1 . VAL D  1 68  ? 3.128   4.400   -48.141 1.00 12.51 ? 68  VAL D CG1 1 
ATOM   7052  C  CG2 . VAL D  1 68  ? 1.456   5.978   -49.108 1.00 13.89 ? 68  VAL D CG2 1 
ATOM   7053  N  N   . LYS D  1 69  ? 1.324   7.751   -46.257 1.00 10.36 ? 69  LYS D N   1 
ATOM   7054  C  CA  . LYS D  1 69  ? 0.486   7.860   -45.067 1.00 11.07 ? 69  LYS D CA  1 
ATOM   7055  C  C   . LYS D  1 69  ? -0.971  7.819   -45.425 1.00 9.66  ? 69  LYS D C   1 
ATOM   7056  O  O   . LYS D  1 69  ? -1.391  8.364   -46.423 1.00 11.23 ? 69  LYS D O   1 
ATOM   7057  C  CB  . LYS D  1 69  ? 0.951   9.058   -44.278 1.00 14.89 ? 69  LYS D CB  1 
ATOM   7058  C  CG  . LYS D  1 69  ? 0.306   10.304  -44.497 1.00 18.58 ? 69  LYS D CG  1 
ATOM   7059  C  CD  . LYS D  1 69  ? 0.489   11.351  -43.259 1.00 16.34 ? 69  LYS D CD  1 
ATOM   7060  C  CE  . LYS D  1 69  ? 0.097   12.607  -43.945 1.00 19.57 ? 69  LYS D CE  1 
ATOM   7061  N  NZ  . LYS D  1 69  ? 0.418   13.652  -42.921 1.00 20.41 ? 69  LYS D NZ  1 
ATOM   7062  N  N   . LEU D  1 70  ? -1.770  7.160   -44.596 1.00 8.07  ? 70  LEU D N   1 
ATOM   7063  C  CA  . LEU D  1 70  ? -3.210  7.116   -44.723 1.00 8.42  ? 70  LEU D CA  1 
ATOM   7064  C  C   . LEU D  1 70  ? -3.792  7.899   -43.538 1.00 7.89  ? 70  LEU D C   1 
ATOM   7065  O  O   . LEU D  1 70  ? -3.568  7.525   -42.387 1.00 8.83  ? 70  LEU D O   1 
ATOM   7066  C  CB  . LEU D  1 70  ? -3.698  5.631   -44.700 1.00 9.54  ? 70  LEU D CB  1 
ATOM   7067  C  CG  . LEU D  1 70  ? -5.204  5.503   -44.877 1.00 9.11  ? 70  LEU D CG  1 
ATOM   7068  C  CD1 . LEU D  1 70  ? -5.608  5.956   -46.280 1.00 10.62 ? 70  LEU D CD1 1 
ATOM   7069  C  CD2 . LEU D  1 70  ? -5.617  4.037   -44.663 1.00 13.18 ? 70  LEU D CD2 1 
ATOM   7070  N  N   . ASN D  1 71  ? -4.588  8.891   -43.853 1.00 9.24  ? 71  ASN D N   1 
ATOM   7071  C  CA  . ASN D  1 71  ? -5.300  9.598   -42.772 1.00 9.44  ? 71  ASN D CA  1 
ATOM   7072  C  C   . ASN D  1 71  ? -6.404  8.771   -42.176 1.00 10.25 ? 71  ASN D C   1 
ATOM   7073  O  O   . ASN D  1 71  ? -7.071  7.956   -42.890 1.00 12.37 ? 71  ASN D O   1 
ATOM   7074  C  CB  . ASN D  1 71  ? -5.896  10.954  -43.257 1.00 12.22 ? 71  ASN D CB  1 
ATOM   7075  C  CG  . ASN D  1 71  ? -4.860  11.980  -43.468 1.00 14.46 ? 71  ASN D CG  1 
ATOM   7076  O  OD1 . ASN D  1 71  ? -3.699  11.801  -43.197 1.00 18.37 ? 71  ASN D OD1 1 
ATOM   7077  N  ND2 . ASN D  1 71  ? -5.336  13.147  -43.981 1.00 18.59 ? 71  ASN D ND2 1 
ATOM   7078  N  N   . LEU D  1 72  ? -6.544  8.838   -40.871 1.00 8.90  ? 72  LEU D N   1 
ATOM   7079  C  CA  . LEU D  1 72  ? -7.513  8.041   -40.125 1.00 9.89  ? 72  LEU D CA  1 
ATOM   7080  C  C   . LEU D  1 72  ? -8.443  8.995   -39.344 1.00 10.24 ? 72  LEU D C   1 
ATOM   7081  O  O   . LEU D  1 72  ? -8.022  10.086  -38.967 1.00 11.76 ? 72  LEU D O   1 
ATOM   7082  C  CB  . LEU D  1 72  ? -6.774  7.089   -39.158 1.00 9.60  ? 72  LEU D CB  1 
ATOM   7083  C  CG  . LEU D  1 72  ? -5.894  6.067   -39.871 1.00 10.40 ? 72  LEU D CG  1 
ATOM   7084  C  CD1 . LEU D  1 72  ? -5.060  5.370   -38.753 1.00 9.45  ? 72  LEU D CD1 1 
ATOM   7085  C  CD2 . LEU D  1 72  ? -6.706  5.059   -40.671 1.00 11.73 ? 72  LEU D CD2 1 
ATOM   7086  N  N   . PRO D  1 73  ? -9.673  8.567   -39.130 1.00 10.53 ? 73  PRO D N   1 
ATOM   7087  C  CA  . PRO D  1 73  ? -10.676 9.427   -38.400 1.00 11.97 ? 73  PRO D CA  1 
ATOM   7088  C  C   . PRO D  1 73  ? -10.533 9.367   -36.899 1.00 12.70 ? 73  PRO D C   1 
ATOM   7089  O  O   . PRO D  1 73  ? -10.073 8.342   -36.314 1.00 12.05 ? 73  PRO D O   1 
ATOM   7090  C  CB  . PRO D  1 73  ? -11.958 8.816   -38.864 1.00 11.40 ? 73  PRO D CB  1 
ATOM   7091  C  CG  . PRO D  1 73  ? -11.651 7.312   -38.921 1.00 12.59 ? 73  PRO D CG  1 
ATOM   7092  C  CD  . PRO D  1 73  ? -10.267 7.284   -39.564 1.00 12.30 ? 73  PRO D CD  1 
ATOM   7093  N  N   . SER D  1 74  ? -10.764 10.492  -36.238 1.00 14.64 ? 74  SER D N   1 
ATOM   7094  C  CA  . SER D  1 74  ? -10.588 10.540  -34.784 1.00 14.84 ? 74  SER D CA  1 
ATOM   7095  C  C   . SER D  1 74  ? -11.591 9.684   -33.997 1.00 14.46 ? 74  SER D C   1 
ATOM   7096  O  O   . SER D  1 74  ? -11.322 9.436   -32.797 1.00 16.12 ? 74  SER D O   1 
ATOM   7097  C  CB  . SER D  1 74  ? -10.505 11.985  -34.297 1.00 17.31 ? 74  SER D CB  1 
ATOM   7098  O  OG  . SER D  1 74  ? -11.756 12.616  -34.631 1.00 20.25 ? 74  SER D OG  1 
ATOM   7099  N  N   . ASP D  1 75  ? -12.613 9.193   -34.641 1.00 14.84 ? 75  ASP D N   1 
ATOM   7100  C  CA  . ASP D  1 75  ? -13.510 8.268   -33.929 1.00 18.37 ? 75  ASP D CA  1 
ATOM   7101  C  C   . ASP D  1 75  ? -12.856 6.902   -33.705 1.00 18.14 ? 75  ASP D C   1 
ATOM   7102  O  O   . ASP D  1 75  ? -13.336 6.087   -32.941 1.00 20.05 ? 75  ASP D O   1 
ATOM   7103  C  CB  . ASP D  1 75  ? -14.922 8.243   -34.535 1.00 25.41 ? 75  ASP D CB  1 
ATOM   7104  C  CG  . ASP D  1 75  ? -15.121 7.225   -35.544 1.00 41.76 ? 75  ASP D CG  1 
ATOM   7105  O  OD1 . ASP D  1 75  ? -14.748 7.446   -36.747 1.00 45.47 ? 75  ASP D OD1 1 
ATOM   7106  O  OD2 . ASP D  1 75  ? -15.729 6.185   -35.127 1.00 49.55 ? 75  ASP D OD2 1 
ATOM   7107  N  N   . MET D  1 76  ? -11.789 6.645   -34.441 1.00 14.28 ? 76  MET D N   1 
ATOM   7108  C  CA  . MET D  1 76  ? -11.066 5.413   -34.260 1.00 14.14 ? 76  MET D CA  1 
ATOM   7109  C  C   . MET D  1 76  ? -10.146 5.638   -33.021 1.00 12.73 ? 76  MET D C   1 
ATOM   7110  O  O   . MET D  1 76  ? -9.433  6.641   -32.923 1.00 11.84 ? 76  MET D O   1 
ATOM   7111  C  CB  . MET D  1 76  ? -10.412 5.087   -35.621 1.00 16.17 ? 76  MET D CB  1 
ATOM   7112  C  CG  . MET D  1 76  ? -9.420  4.017   -35.552 1.00 15.71 ? 76  MET D CG  1 
ATOM   7113  S  SD  . MET D  1 76  ? -8.776  3.921   -37.307 1.00 15.80 ? 76  MET D SD  1 
ATOM   7114  C  CE  . MET D  1 76  ? -7.377  2.964   -36.908 1.00 14.42 ? 76  MET D CE  1 
ATOM   7115  N  N   . HIS D  1 77  ? -10.167 4.716   -32.013 1.00 12.46 ? 77  HIS D N   1 
ATOM   7116  C  CA  . HIS D  1 77  ? -9.350  4.950   -30.841 1.00 12.83 ? 77  HIS D CA  1 
ATOM   7117  C  C   . HIS D  1 77  ? -8.912  3.738   -30.168 1.00 11.79 ? 77  HIS D C   1 
ATOM   7118  O  O   . HIS D  1 77  ? -9.465  2.675   -30.450 1.00 12.92 ? 77  HIS D O   1 
ATOM   7119  C  CB  . HIS D  1 77  ? -10.039 5.924   -29.877 1.00 19.03 ? 77  HIS D CB  1 
ATOM   7120  C  CG  . HIS D  1 77  ? -11.299 5.406   -29.318 1.00 18.75 ? 77  HIS D CG  1 
ATOM   7121  N  ND1 . HIS D  1 77  ? -12.493 5.433   -30.019 1.00 22.68 ? 77  HIS D ND1 1 
ATOM   7122  C  CD2 . HIS D  1 77  ? -11.593 4.913   -28.081 1.00 21.71 ? 77  HIS D CD2 1 
ATOM   7123  C  CE1 . HIS D  1 77  ? -13.459 4.914   -29.255 1.00 23.50 ? 77  HIS D CE1 1 
ATOM   7124  N  NE2 . HIS D  1 77  ? -12.933 4.595   -28.087 1.00 24.44 ? 77  HIS D NE2 1 
ATOM   7125  N  N   . ILE D  1 78  ? -7.886  3.880   -29.338 1.00 12.57 ? 78  ILE D N   1 
ATOM   7126  C  CA  . ILE D  1 78  ? -7.438  2.799   -28.444 1.00 13.08 ? 78  ILE D CA  1 
ATOM   7127  C  C   . ILE D  1 78  ? -8.004  3.046   -27.056 1.00 15.61 ? 78  ILE D C   1 
ATOM   7128  O  O   . ILE D  1 78  ? -7.849  4.162   -26.538 1.00 16.27 ? 78  ILE D O   1 
ATOM   7129  C  CB  . ILE D  1 78  ? -5.942  2.781   -28.326 1.00 14.89 ? 78  ILE D CB  1 
ATOM   7130  C  CG1 . ILE D  1 78  ? -5.151  2.458   -29.614 1.00 17.99 ? 78  ILE D CG1 1 
ATOM   7131  C  CG2 . ILE D  1 78  ? -5.530  1.726   -27.268 1.00 18.74 ? 78  ILE D CG2 1 
ATOM   7132  C  CD1 . ILE D  1 78  ? -3.705  3.013   -29.437 1.00 16.37 ? 78  ILE D CD1 1 
ATOM   7133  N  N   . GLN D  1 79  ? -8.435  1.956   -26.433 1.00 16.45 ? 79  GLN D N   1 
ATOM   7134  C  CA  . GLN D  1 79  ? -8.773  1.922   -25.020 1.00 20.38 ? 79  GLN D CA  1 
ATOM   7135  C  C   . GLN D  1 79  ? -7.854  1.017   -24.255 1.00 20.34 ? 79  GLN D C   1 
ATOM   7136  O  O   . GLN D  1 79  ? -7.469  -0.074  -24.749 1.00 20.04 ? 79  GLN D O   1 
ATOM   7137  C  CB  . GLN D  1 79  ? -10.224 1.459   -24.806 1.00 26.07 ? 79  GLN D CB  1 
ATOM   7138  C  CG  . GLN D  1 79  ? -11.275 2.593   -24.960 1.00 39.16 ? 79  GLN D CG  1 
ATOM   7139  C  CD  . GLN D  1 79  ? -11.173 3.798   -23.975 1.00 48.00 ? 79  GLN D CD  1 
ATOM   7140  O  OE1 . GLN D  1 79  ? -11.006 3.616   -22.766 1.00 60.76 ? 79  GLN D OE1 1 
ATOM   7141  N  NE2 . GLN D  1 79  ? -11.295 5.027   -24.495 1.00 41.78 ? 79  GLN D NE2 1 
ATOM   7142  N  N   . GLY D  1 80  ? -7.428  1.441   -23.064 1.00 18.68 ? 80  GLY D N   1 
ATOM   7143  C  CA  . GLY D  1 80  ? -6.537  0.601   -22.279 1.00 16.94 ? 80  GLY D CA  1 
ATOM   7144  C  C   . GLY D  1 80  ? -5.342  1.274   -21.780 1.00 22.45 ? 80  GLY D C   1 
ATOM   7145  O  O   . GLY D  1 80  ? -4.732  0.779   -20.891 1.00 25.09 ? 80  GLY D O   1 
ATOM   7146  N  N   . LEU D  1 81  ? -4.988  2.466   -22.296 1.00 15.75 ? 81  LEU D N   1 
ATOM   7147  C  CA  . LEU D  1 81  ? -3.835  3.156   -21.856 1.00 16.18 ? 81  LEU D CA  1 
ATOM   7148  C  C   . LEU D  1 81  ? -4.275  4.159   -20.755 1.00 13.78 ? 81  LEU D C   1 
ATOM   7149  O  O   . LEU D  1 81  ? -5.465  4.163   -20.355 1.00 16.72 ? 81  LEU D O   1 
ATOM   7150  C  CB  . LEU D  1 81  ? -3.257  3.956   -23.057 1.00 14.89 ? 81  LEU D CB  1 
ATOM   7151  C  CG  . LEU D  1 81  ? -2.791  3.008   -24.217 1.00 14.59 ? 81  LEU D CG  1 
ATOM   7152  C  CD1 . LEU D  1 81  ? -2.426  3.841   -25.459 1.00 17.01 ? 81  LEU D CD1 1 
ATOM   7153  C  CD2 . LEU D  1 81  ? -1.596  2.151   -23.705 1.00 14.58 ? 81  LEU D CD2 1 
ATOM   7154  N  N   . GLN D  1 82  ? -3.398  5.061   -20.345 1.00 14.47 ? 82  GLN D N   1 
ATOM   7155  C  CA  . GLN D  1 82  ? -3.753  5.969   -19.207 1.00 13.57 ? 82  GLN D CA  1 
ATOM   7156  C  C   . GLN D  1 82  ? -4.737  7.062   -19.671 1.00 13.46 ? 82  GLN D C   1 
ATOM   7157  O  O   . GLN D  1 82  ? -5.321  7.676   -18.809 1.00 14.04 ? 82  GLN D O   1 
ATOM   7158  C  CB  . GLN D  1 82  ? -2.483  6.615   -18.643 1.00 13.53 ? 82  GLN D CB  1 
ATOM   7159  C  CG  . GLN D  1 82  ? -2.016  7.934   -19.217 1.00 16.56 ? 82  GLN D CG  1 
ATOM   7160  C  CD  . GLN D  1 82  ? -1.514  7.806   -20.645 1.00 18.62 ? 82  GLN D CD  1 
ATOM   7161  O  OE1 . GLN D  1 82  ? -1.275  6.716   -21.169 1.00 18.33 ? 82  GLN D OE1 1 
ATOM   7162  N  NE2 . GLN D  1 82  ? -1.365  8.939   -21.287 1.00 18.35 ? 82  GLN D NE2 1 
ATOM   7163  N  N   . SER D  1 83  ? -4.960  7.234   -20.971 1.00 12.71 ? 83  SER D N   1 
ATOM   7164  C  CA  . SER D  1 83  ? -5.870  8.272   -21.550 1.00 12.88 ? 83  SER D CA  1 
ATOM   7165  C  C   . SER D  1 83  ? -6.443  7.630   -22.809 1.00 12.38 ? 83  SER D C   1 
ATOM   7166  O  O   . SER D  1 83  ? -5.823  6.644   -23.345 1.00 12.37 ? 83  SER D O   1 
ATOM   7167  C  CB  . SER D  1 83  ? -5.085  9.544   -21.994 1.00 12.36 ? 83  SER D CB  1 
ATOM   7168  O  OG  . SER D  1 83  ? -4.501  10.157  -20.836 1.00 12.62 ? 83  SER D OG  1 
ATOM   7169  N  N   A ARG D  1 84  ? -7.542  8.118   -23.364 0.50 10.70 ? 84  ARG D N   1 
ATOM   7170  N  N   B ARG D  1 84  ? -7.523  8.143   -23.379 0.50 12.27 ? 84  ARG D N   1 
ATOM   7171  C  CA  A ARG D  1 84  ? -8.004  7.792   -24.708 0.50 11.09 ? 84  ARG D CA  1 
ATOM   7172  C  CA  B ARG D  1 84  ? -7.954  7.738   -24.707 0.50 13.53 ? 84  ARG D CA  1 
ATOM   7173  C  C   A ARG D  1 84  ? -6.961  8.389   -25.671 0.50 9.85  ? 84  ARG D C   1 
ATOM   7174  C  C   B ARG D  1 84  ? -7.073  8.400   -25.772 0.50 11.56 ? 84  ARG D C   1 
ATOM   7175  O  O   A ARG D  1 84  ? -6.535  9.548   -25.546 0.50 9.58  ? 84  ARG D O   1 
ATOM   7176  O  O   B ARG D  1 84  ? -6.899  9.624   -25.852 0.50 11.35 ? 84  ARG D O   1 
ATOM   7177  C  CB  A ARG D  1 84  ? -9.351  8.464   -24.987 0.50 11.27 ? 84  ARG D CB  1 
ATOM   7178  C  CB  B ARG D  1 84  ? -9.390  8.111   -25.018 0.50 16.27 ? 84  ARG D CB  1 
ATOM   7179  C  CG  A ARG D  1 84  ? -9.855  8.303   -26.397 0.50 12.23 ? 84  ARG D CG  1 
ATOM   7180  C  CG  B ARG D  1 84  ? -9.708  7.598   -26.413 0.50 21.19 ? 84  ARG D CG  1 
ATOM   7181  C  CD  A ARG D  1 84  ? -11.344 8.614   -26.686 0.50 13.19 ? 84  ARG D CD  1 
ATOM   7182  C  CD  B ARG D  1 84  ? -10.999 8.135   -26.963 0.50 21.90 ? 84  ARG D CD  1 
ATOM   7183  N  NE  A ARG D  1 84  ? -11.413 8.663   -28.149 0.50 12.55 ? 84  ARG D NE  1 
ATOM   7184  N  NE  B ARG D  1 84  ? -12.106 7.666   -26.172 0.50 25.98 ? 84  ARG D NE  1 
ATOM   7185  C  CZ  A ARG D  1 84  ? -12.534 8.511   -28.863 0.50 13.26 ? 84  ARG D CZ  1 
ATOM   7186  C  CZ  B ARG D  1 84  ? -13.361 8.075   -26.413 0.50 28.76 ? 84  ARG D CZ  1 
ATOM   7187  N  NH1 A ARG D  1 84  ? -13.725 8.347   -28.233 0.50 14.52 ? 84  ARG D NH1 1 
ATOM   7188  N  NH1 B ARG D  1 84  ? -13.589 8.950   -27.374 0.50 28.73 ? 84  ARG D NH1 1 
ATOM   7189  N  NH2 A ARG D  1 84  ? -12.525 8.538   -30.207 0.50 13.68 ? 84  ARG D NH2 1 
ATOM   7190  N  NH2 B ARG D  1 84  ? -14.360 7.657   -25.681 0.50 25.83 ? 84  ARG D NH2 1 
ATOM   7191  N  N   . TYR D  1 85  ? -6.619  7.528   -26.663 1.00 10.65 ? 85  TYR D N   1 
ATOM   7192  C  CA  . TYR D  1 85  ? -5.732  7.948   -27.767 1.00 10.41 ? 85  TYR D CA  1 
ATOM   7193  C  C   . TYR D  1 85  ? -6.583  7.687   -29.042 1.00 12.14 ? 85  TYR D C   1 
ATOM   7194  O  O   . TYR D  1 85  ? -7.099  6.604   -29.305 1.00 13.76 ? 85  TYR D O   1 
ATOM   7195  C  CB  . TYR D  1 85  ? -4.498  7.198   -27.770 1.00 10.70 ? 85  TYR D CB  1 
ATOM   7196  C  CG  . TYR D  1 85  ? -3.460  7.717   -26.804 1.00 10.33 ? 85  TYR D CG  1 
ATOM   7197  C  CD1 . TYR D  1 85  ? -3.443  7.249   -25.503 1.00 10.94 ? 85  TYR D CD1 1 
ATOM   7198  C  CD2 . TYR D  1 85  ? -2.485  8.642   -27.188 1.00 9.38  ? 85  TYR D CD2 1 
ATOM   7199  C  CE1 . TYR D  1 85  ? -2.510  7.680   -24.595 1.00 10.41 ? 85  TYR D CE1 1 
ATOM   7200  C  CE2 . TYR D  1 85  ? -1.566  9.113   -26.270 1.00 10.52 ? 85  TYR D CE2 1 
ATOM   7201  C  CZ  . TYR D  1 85  ? -1.581  8.635   -24.973 1.00 10.81 ? 85  TYR D CZ  1 
ATOM   7202  O  OH  . TYR D  1 85  ? -0.623  9.085   -24.072 1.00 11.83 ? 85  TYR D OH  1 
ATOM   7203  N  N   . SER D  1 86  ? -6.734  8.745   -29.857 1.00 10.20 ? 86  SER D N   1 
ATOM   7204  C  CA  . SER D  1 86  ? -7.517  8.704   -31.069 1.00 10.52 ? 86  SER D CA  1 
ATOM   7205  C  C   . SER D  1 86  ? -6.607  8.683   -32.311 1.00 8.83  ? 86  SER D C   1 
ATOM   7206  O  O   . SER D  1 86  ? -5.513  9.290   -32.322 1.00 9.68  ? 86  SER D O   1 
ATOM   7207  C  CB  . SER D  1 86  ? -8.343  9.977   -31.197 1.00 10.57 ? 86  SER D CB  1 
ATOM   7208  O  OG  . SER D  1 86  ? -9.356  9.963   -30.131 1.00 13.69 ? 86  SER D OG  1 
ATOM   7209  N  N   . ALA D  1 87  ? -7.010  7.875   -33.264 1.00 9.36  ? 87  ALA D N   1 
ATOM   7210  C  CA  . ALA D  1 87  ? -6.128  7.740   -34.462 1.00 9.83  ? 87  ALA D CA  1 
ATOM   7211  C  C   . ALA D  1 87  ? -5.994  9.035   -35.213 1.00 8.72  ? 87  ALA D C   1 
ATOM   7212  O  O   . ALA D  1 87  ? -6.927  9.892   -35.242 1.00 11.05 ? 87  ALA D O   1 
ATOM   7213  C  CB  . ALA D  1 87  ? -6.716  6.716   -35.393 1.00 11.35 ? 87  ALA D CB  1 
ATOM   7214  N  N   . THR D  1 88  ? -4.837  9.203   -35.860 1.00 9.47  ? 88  THR D N   1 
ATOM   7215  C  CA  . THR D  1 88  ? -4.594  10.327  -36.782 1.00 9.05  ? 88  THR D CA  1 
ATOM   7216  C  C   . THR D  1 88  ? -4.116  9.824   -38.171 1.00 9.02  ? 88  THR D C   1 
ATOM   7217  O  O   . THR D  1 88  ? -4.569  10.332  -39.205 1.00 9.29  ? 88  THR D O   1 
ATOM   7218  C  CB  . THR D  1 88  ? -3.716  11.400  -36.161 1.00 10.31 ? 88  THR D CB  1 
ATOM   7219  O  OG1 . THR D  1 88  ? -3.575  12.459  -37.133 1.00 13.47 ? 88  THR D OG1 1 
ATOM   7220  C  CG2 . THR D  1 88  ? -2.351  10.890  -35.782 1.00 12.16 ? 88  THR D CG2 1 
ATOM   7221  N  N   . GLN D  1 89  ? -3.179  8.852   -38.211 1.00 8.57  ? 89  GLN D N   1 
ATOM   7222  C  CA  . GLN D  1 89  ? -2.731  8.395   -39.530 1.00 8.01  ? 89  GLN D CA  1 
ATOM   7223  C  C   . GLN D  1 89  ? -1.966  7.104   -39.309 1.00 7.23  ? 89  GLN D C   1 
ATOM   7224  O  O   . GLN D  1 89  ? -1.528  6.781   -38.166 1.00 8.10  ? 89  GLN D O   1 
ATOM   7225  C  CB  . GLN D  1 89  ? -1.784  9.432   -40.223 1.00 9.28  ? 89  GLN D CB  1 
ATOM   7226  C  CG  . GLN D  1 89  ? -0.651  9.939   -39.411 1.00 12.27 ? 89  GLN D CG  1 
ATOM   7227  C  CD  . GLN D  1 89  ? 0.682   9.396   -39.748 1.00 11.15 ? 89  GLN D CD  1 
ATOM   7228  O  OE1 . GLN D  1 89  ? 0.802   8.233   -40.018 1.00 12.30 ? 89  GLN D OE1 1 
ATOM   7229  N  NE2 . GLN D  1 89  ? 1.649   10.248  -39.756 1.00 16.23 ? 89  GLN D NE2 1 
ATOM   7230  N  N   . LEU D  1 90  ? -1.838  6.342   -40.399 1.00 7.61  ? 90  LEU D N   1 
ATOM   7231  C  CA  . LEU D  1 90  ? -0.867  5.255   -40.394 1.00 7.22  ? 90  LEU D CA  1 
ATOM   7232  C  C   . LEU D  1 90  ? 0.098   5.424   -41.562 1.00 6.94  ? 90  LEU D C   1 
ATOM   7233  O  O   . LEU D  1 90  ? -0.183  6.085   -42.537 1.00 8.51  ? 90  LEU D O   1 
ATOM   7234  C  CB  . LEU D  1 90  ? -1.533  3.870   -40.423 1.00 7.98  ? 90  LEU D CB  1 
ATOM   7235  C  CG  . LEU D  1 90  ? -2.499  3.502   -41.521 1.00 7.35  ? 90  LEU D CG  1 
ATOM   7236  C  CD1 . LEU D  1 90  ? -1.772  3.136   -42.820 1.00 8.76  ? 90  LEU D CD1 1 
ATOM   7237  C  CD2 . LEU D  1 90  ? -3.355  2.310   -41.132 1.00 8.66  ? 90  LEU D CD2 1 
ATOM   7238  N  N   . HIS D  1 91  ? 1.268   4.784   -41.419 1.00 7.45  ? 91  HIS D N   1 
ATOM   7239  C  CA  . HIS D  1 91  ? 2.302   4.876   -42.494 1.00 7.26  ? 91  HIS D CA  1 
ATOM   7240  C  C   . HIS D  1 91  ? 3.250   3.730   -42.307 1.00 7.37  ? 91  HIS D C   1 
ATOM   7241  O  O   . HIS D  1 91  ? 3.155   2.940   -41.290 1.00 7.03  ? 91  HIS D O   1 
ATOM   7242  C  CB  . HIS D  1 91  ? 3.033   6.263   -42.404 1.00 7.40  ? 91  HIS D CB  1 
ATOM   7243  C  CG  . HIS D  1 91  ? 3.809   6.410   -41.125 1.00 6.55  ? 91  HIS D CG  1 
ATOM   7244  N  ND1 . HIS D  1 91  ? 3.263   7.050   -40.027 1.00 8.19  ? 91  HIS D ND1 1 
ATOM   7245  C  CD2 . HIS D  1 91  ? 5.040   5.926   -40.741 1.00 7.56  ? 91  HIS D CD2 1 
ATOM   7246  C  CE1 . HIS D  1 91  ? 4.131   6.937   -39.010 1.00 7.68  ? 91  HIS D CE1 1 
ATOM   7247  N  NE2 . HIS D  1 91  ? 5.198   6.233   -39.411 1.00 6.98  ? 91  HIS D NE2 1 
ATOM   7248  N  N   . LEU D  1 92  ? 4.216   3.640   -43.228 1.00 8.07  ? 92  LEU D N   1 
ATOM   7249  C  CA  . LEU D  1 92  ? 5.148   2.505   -43.187 1.00 7.92  ? 92  LEU D CA  1 
ATOM   7250  C  C   . LEU D  1 92  ? 6.599   2.949   -43.341 1.00 7.11  ? 92  LEU D C   1 
ATOM   7251  O  O   . LEU D  1 92  ? 6.905   4.064   -43.691 1.00 8.14  ? 92  LEU D O   1 
ATOM   7252  C  CB  . LEU D  1 92  ? 4.798   1.542   -44.341 1.00 9.43  ? 92  LEU D CB  1 
ATOM   7253  C  CG  . LEU D  1 92  ? 3.390   0.887   -44.230 1.00 10.04 ? 92  LEU D CG  1 
ATOM   7254  C  CD1 . LEU D  1 92  ? 2.461   1.568   -45.117 1.00 14.66 ? 92  LEU D CD1 1 
ATOM   7255  C  CD2 . LEU D  1 92  ? 3.520   -0.587  -44.400 1.00 13.32 ? 92  LEU D CD2 1 
ATOM   7256  N  N   . HIS D  1 93  ? 7.444   2.013   -43.003 1.00 7.66  ? 93  HIS D N   1 
ATOM   7257  C  CA  . HIS D  1 93  ? 8.954   2.150   -43.188 1.00 7.43  ? 93  HIS D CA  1 
ATOM   7258  C  C   . HIS D  1 93  ? 9.406   0.885   -43.830 1.00 7.36  ? 93  HIS D C   1 
ATOM   7259  O  O   . HIS D  1 93  ? 8.903   -0.209  -43.487 1.00 7.53  ? 93  HIS D O   1 
ATOM   7260  C  CB  . HIS D  1 93  ? 9.608   2.300   -41.828 1.00 7.53  ? 93  HIS D CB  1 
ATOM   7261  C  CG  . HIS D  1 93  ? 9.135   3.490   -41.056 1.00 8.09  ? 93  HIS D CG  1 
ATOM   7262  N  ND1 . HIS D  1 93  ? 9.748   4.737   -41.128 1.00 7.97  ? 93  HIS D ND1 1 
ATOM   7263  C  CD2 . HIS D  1 93  ? 8.066   3.669   -40.212 1.00 6.47  ? 93  HIS D CD2 1 
ATOM   7264  C  CE1 . HIS D  1 93  ? 9.113   5.607   -40.342 1.00 7.76  ? 93  HIS D CE1 1 
ATOM   7265  N  NE2 . HIS D  1 93  ? 8.087   4.988   -39.756 1.00 6.58  ? 93  HIS D NE2 1 
ATOM   7266  N  N   . TRP D  1 94  ? 10.371  0.999   -44.732 1.00 6.91  ? 94  TRP D N   1 
ATOM   7267  C  CA  . TRP D  1 94  ? 10.862  -0.168  -45.534 1.00 6.72  ? 94  TRP D CA  1 
ATOM   7268  C  C   . TRP D  1 94  ? 12.287  0.094   -45.975 1.00 6.78  ? 94  TRP D C   1 
ATOM   7269  O  O   . TRP D  1 94  ? 12.911  1.142   -45.766 1.00 7.94  ? 94  TRP D O   1 
ATOM   7270  C  CB  . TRP D  1 94  ? 9.886   -0.456  -46.681 1.00 7.81  ? 94  TRP D CB  1 
ATOM   7271  C  CG  . TRP D  1 94  ? 9.790   0.744   -47.622 1.00 7.01  ? 94  TRP D CG  1 
ATOM   7272  C  CD1 . TRP D  1 94  ? 10.606  1.018   -48.698 1.00 8.43  ? 94  TRP D CD1 1 
ATOM   7273  C  CD2 . TRP D  1 94  ? 8.763   1.762   -47.607 1.00 7.49  ? 94  TRP D CD2 1 
ATOM   7274  N  NE1 . TRP D  1 94  ? 10.163  2.188   -49.347 1.00 8.25  ? 94  TRP D NE1 1 
ATOM   7275  C  CE2 . TRP D  1 94  ? 9.020   2.642   -48.691 1.00 7.76  ? 94  TRP D CE2 1 
ATOM   7276  C  CE3 . TRP D  1 94  ? 7.682   2.071   -46.754 1.00 7.81  ? 94  TRP D CE3 1 
ATOM   7277  C  CZ2 . TRP D  1 94  ? 8.241   3.795   -48.965 1.00 7.16  ? 94  TRP D CZ2 1 
ATOM   7278  C  CZ3 . TRP D  1 94  ? 6.933   3.273   -47.032 1.00 7.61  ? 94  TRP D CZ3 1 
ATOM   7279  C  CH2 . TRP D  1 94  ? 7.199   4.083   -48.111 1.00 7.73  ? 94  TRP D CH2 1 
ATOM   7280  N  N   . GLY D  1 95  ? 12.789  -0.983  -46.572 1.00 7.74  ? 95  GLY D N   1 
ATOM   7281  C  CA  . GLY D  1 95  ? 14.204  -0.991  -47.118 1.00 8.29  ? 95  GLY D CA  1 
ATOM   7282  C  C   . GLY D  1 95  ? 14.236  -0.763  -48.617 1.00 8.11  ? 95  GLY D C   1 
ATOM   7283  O  O   . GLY D  1 95  ? 13.791  0.232   -49.116 1.00 7.96  ? 95  GLY D O   1 
ATOM   7284  N  N   . ASN D  1 96  ? 14.849  -1.759  -49.319 1.00 9.46  ? 96  ASN D N   1 
ATOM   7285  C  CA  . ASN D  1 96  ? 14.899  -1.522  -50.782 1.00 11.15 ? 96  ASN D CA  1 
ATOM   7286  C  C   . ASN D  1 96  ? 15.035  -2.915  -51.379 1.00 11.33 ? 96  ASN D C   1 
ATOM   7287  O  O   . ASN D  1 96  ? 15.217  -3.894  -50.651 1.00 12.35 ? 96  ASN D O   1 
ATOM   7288  C  CB  . ASN D  1 96  ? 16.149  -0.611  -51.137 1.00 13.62 ? 96  ASN D CB  1 
ATOM   7289  C  CG  . ASN D  1 96  ? 17.437  -1.309  -50.967 1.00 15.32 ? 96  ASN D CG  1 
ATOM   7290  O  OD1 . ASN D  1 96  ? 17.886  -1.937  -51.974 1.00 21.55 ? 96  ASN D OD1 1 
ATOM   7291  N  ND2 . ASN D  1 96  ? 18.078  -1.206  -49.845 1.00 15.16 ? 96  ASN D ND2 1 
ATOM   7292  N  N   . PRO D  1 97  ? 14.961  -2.986  -52.759 1.00 13.48 ? 97  PRO D N   1 
ATOM   7293  C  CA  . PRO D  1 97  ? 14.952  -4.336  -53.316 1.00 16.80 ? 97  PRO D CA  1 
ATOM   7294  C  C   . PRO D  1 97  ? 16.208  -5.184  -53.008 1.00 15.40 ? 97  PRO D C   1 
ATOM   7295  O  O   . PRO D  1 97  ? 16.092  -6.378  -52.786 1.00 20.21 ? 97  PRO D O   1 
ATOM   7296  C  CB  . PRO D  1 97  ? 14.746  -4.061  -54.785 1.00 18.48 ? 97  PRO D CB  1 
ATOM   7297  C  CG  . PRO D  1 97  ? 14.146  -2.718  -54.921 1.00 19.09 ? 97  PRO D CG  1 
ATOM   7298  C  CD  . PRO D  1 97  ? 14.693  -1.945  -53.729 1.00 13.93 ? 97  PRO D CD  1 
ATOM   7299  N  N   . ASN D  1 98  ? 17.359  -4.561  -52.846 1.00 15.70 ? 98  ASN D N   1 
ATOM   7300  C  CA  . ASN D  1 98  ? 18.588  -5.279  -52.534 1.00 19.35 ? 98  ASN D CA  1 
ATOM   7301  C  C   . ASN D  1 98  ? 18.772  -5.527  -51.057 1.00 22.40 ? 98  ASN D C   1 
ATOM   7302  O  O   . ASN D  1 98  ? 19.748  -6.172  -50.632 1.00 23.72 ? 98  ASN D O   1 
ATOM   7303  C  CB  . ASN D  1 98  ? 19.810  -4.487  -53.048 1.00 22.66 ? 98  ASN D CB  1 
ATOM   7304  C  CG  . ASN D  1 98  ? 19.759  -4.275  -54.577 1.00 31.79 ? 98  ASN D CG  1 
ATOM   7305  O  OD1 . ASN D  1 98  ? 19.286  -5.155  -55.334 1.00 41.55 ? 98  ASN D OD1 1 
ATOM   7306  N  ND2 . ASN D  1 98  ? 20.184  -3.085  -55.027 1.00 38.89 ? 98  ASN D ND2 1 
ATOM   7307  N  N   . ASP D  1 99  ? 17.904  -4.929  -50.234 1.00 15.22 ? 99  ASP D N   1 
ATOM   7308  C  CA  . ASP D  1 99  ? 18.058  -5.176  -48.807 1.00 14.67 ? 99  ASP D CA  1 
ATOM   7309  C  C   . ASP D  1 99  ? 16.624  -4.991  -48.216 1.00 13.30 ? 99  ASP D C   1 
ATOM   7310  O  O   . ASP D  1 99  ? 16.324  -3.884  -47.671 1.00 11.95 ? 99  ASP D O   1 
ATOM   7311  C  CB  . ASP D  1 99  ? 19.074  -4.186  -48.139 1.00 15.91 ? 99  ASP D CB  1 
ATOM   7312  C  CG  . ASP D  1 99  ? 19.220  -4.396  -46.634 1.00 18.23 ? 99  ASP D CG  1 
ATOM   7313  O  OD1 . ASP D  1 99  ? 18.910  -5.503  -46.160 1.00 20.60 ? 99  ASP D OD1 1 
ATOM   7314  O  OD2 . ASP D  1 99  ? 19.495  -3.401  -45.871 1.00 24.57 ? 99  ASP D OD2 1 
ATOM   7315  N  N   . PRO D  1 100 ? 15.783  -5.997  -48.311 1.00 13.41 ? 100 PRO D N   1 
ATOM   7316  C  CA  . PRO D  1 100 ? 14.340  -5.837  -47.879 1.00 11.19 ? 100 PRO D CA  1 
ATOM   7317  C  C   . PRO D  1 100 ? 14.302  -6.082  -46.369 1.00 11.18 ? 100 PRO D C   1 
ATOM   7318  O  O   . PRO D  1 100 ? 13.696  -7.039  -45.879 1.00 11.87 ? 100 PRO D O   1 
ATOM   7319  C  CB  . PRO D  1 100 ? 13.604  -6.917  -48.691 1.00 13.88 ? 100 PRO D CB  1 
ATOM   7320  C  CG  . PRO D  1 100 ? 14.672  -7.960  -48.891 1.00 14.23 ? 100 PRO D CG  1 
ATOM   7321  C  CD  . PRO D  1 100 ? 16.000  -7.282  -49.060 1.00 14.74 ? 100 PRO D CD  1 
ATOM   7322  N  N   . HIS D  1 101 ? 14.996  -5.209  -45.602 1.00 10.62 ? 101 HIS D N   1 
ATOM   7323  C  CA  . HIS D  1 101 ? 15.148  -5.366  -44.132 1.00 11.11 ? 101 HIS D CA  1 
ATOM   7324  C  C   . HIS D  1 101 ? 15.065  -3.986  -43.524 1.00 10.83 ? 101 HIS D C   1 
ATOM   7325  O  O   . HIS D  1 101 ? 15.982  -3.570  -42.807 1.00 13.57 ? 101 HIS D O   1 
ATOM   7326  C  CB  . HIS D  1 101 ? 16.497  -6.097  -43.740 1.00 13.02 ? 101 HIS D CB  1 
ATOM   7327  C  CG  . HIS D  1 101 ? 16.576  -7.472  -44.378 1.00 15.86 ? 101 HIS D CG  1 
ATOM   7328  N  ND1 . HIS D  1 101 ? 15.881  -8.588  -43.926 1.00 20.21 ? 101 HIS D ND1 1 
ATOM   7329  C  CD2 . HIS D  1 101 ? 17.246  -7.866  -45.484 1.00 15.39 ? 101 HIS D CD2 1 
ATOM   7330  C  CE1 . HIS D  1 101 ? 16.122  -9.609  -44.748 1.00 20.49 ? 101 HIS D CE1 1 
ATOM   7331  N  NE2 . HIS D  1 101 ? 16.934  -9.189  -45.703 1.00 19.73 ? 101 HIS D NE2 1 
ATOM   7332  N  N   . GLY D  1 102 ? 13.908  -3.356  -43.692 1.00 8.51  ? 102 GLY D N   1 
ATOM   7333  C  CA  . GLY D  1 102 ? 13.774  -1.993  -43.315 1.00 9.05  ? 102 GLY D CA  1 
ATOM   7334  C  C   . GLY D  1 102 ? 12.810  -1.712  -42.166 1.00 8.06  ? 102 GLY D C   1 
ATOM   7335  O  O   . GLY D  1 102 ? 12.300  -0.598  -42.066 1.00 9.81  ? 102 GLY D O   1 
ATOM   7336  N  N   . SER D  1 103 ? 12.519  -2.708  -41.302 1.00 8.71  ? 103 SER D N   1 
ATOM   7337  C  CA  . SER D  1 103 ? 11.805  -2.314  -40.082 1.00 8.02  ? 103 SER D CA  1 
ATOM   7338  C  C   . SER D  1 103 ? 12.619  -1.323  -39.293 1.00 8.44  ? 103 SER D C   1 
ATOM   7339  O  O   . SER D  1 103 ? 13.850  -1.273  -39.423 1.00 9.10  ? 103 SER D O   1 
ATOM   7340  C  CB  . SER D  1 103 ? 11.477  -3.525  -39.215 1.00 7.91  ? 103 SER D CB  1 
ATOM   7341  O  OG  . SER D  1 103 ? 12.654  -4.122  -38.658 1.00 8.48  ? 103 SER D OG  1 
ATOM   7342  N  N   . GLU D  1 104 ? 11.938  -0.573  -38.422 1.00 8.06  ? 104 GLU D N   1 
ATOM   7343  C  CA  . GLU D  1 104 ? 12.642  0.326   -37.482 1.00 7.56  ? 104 GLU D CA  1 
ATOM   7344  C  C   . GLU D  1 104 ? 13.069  -0.367  -36.241 1.00 6.75  ? 104 GLU D C   1 
ATOM   7345  O  O   . GLU D  1 104 ? 14.229  -0.401  -35.881 1.00 7.56  ? 104 GLU D O   1 
ATOM   7346  C  CB  . GLU D  1 104 ? 11.736  1.562   -37.210 1.00 7.67  ? 104 GLU D CB  1 
ATOM   7347  C  CG  . GLU D  1 104 ? 11.363  2.269   -38.500 1.00 8.25  ? 104 GLU D CG  1 
ATOM   7348  C  CD  . GLU D  1 104 ? 11.297  3.764   -38.248 1.00 8.26  ? 104 GLU D CD  1 
ATOM   7349  O  OE1 . GLU D  1 104 ? 10.321  4.190   -37.681 1.00 8.27  ? 104 GLU D OE1 1 
ATOM   7350  O  OE2 . GLU D  1 104 ? 12.221  4.480   -38.650 1.00 8.54  ? 104 GLU D OE2 1 
ATOM   7351  N  N   . HIS D  1 105 ? 12.082  -0.942  -35.540 1.00 7.32  ? 105 HIS D N   1 
ATOM   7352  C  CA  . HIS D  1 105 ? 12.434  -1.805  -34.407 1.00 7.73  ? 105 HIS D CA  1 
ATOM   7353  C  C   . HIS D  1 105 ? 13.079  -3.077  -34.930 1.00 7.91  ? 105 HIS D C   1 
ATOM   7354  O  O   . HIS D  1 105 ? 12.730  -3.588  -35.989 1.00 8.83  ? 105 HIS D O   1 
ATOM   7355  C  CB  . HIS D  1 105 ? 11.178  -2.092  -33.550 1.00 7.37  ? 105 HIS D CB  1 
ATOM   7356  C  CG  . HIS D  1 105 ? 10.700  -0.873  -32.862 1.00 7.53  ? 105 HIS D CG  1 
ATOM   7357  N  ND1 . HIS D  1 105 ? 9.787   -0.015  -33.453 1.00 8.20  ? 105 HIS D ND1 1 
ATOM   7358  C  CD2 . HIS D  1 105 ? 11.027  -0.344  -31.658 1.00 7.84  ? 105 HIS D CD2 1 
ATOM   7359  C  CE1 . HIS D  1 105 ? 9.586   1.003   -32.621 1.00 8.65  ? 105 HIS D CE1 1 
ATOM   7360  N  NE2 . HIS D  1 105 ? 10.344  0.846   -31.547 1.00 8.76  ? 105 HIS D NE2 1 
ATOM   7361  N  N   . THR D  1 106 ? 14.026  -3.586  -34.147 1.00 7.64  ? 106 THR D N   1 
ATOM   7362  C  CA  . THR D  1 106 ? 14.650  -4.921  -34.431 1.00 8.02  ? 106 THR D CA  1 
ATOM   7363  C  C   . THR D  1 106 ? 14.310  -5.833  -33.248 1.00 8.89  ? 106 THR D C   1 
ATOM   7364  O  O   . THR D  1 106 ? 14.026  -5.376  -32.162 1.00 9.26  ? 106 THR D O   1 
ATOM   7365  C  CB  . THR D  1 106 ? 16.119  -4.760  -34.725 1.00 9.87  ? 106 THR D CB  1 
ATOM   7366  O  OG1 . THR D  1 106 ? 16.788  -4.111  -33.602 1.00 9.95  ? 106 THR D OG1 1 
ATOM   7367  C  CG2 . THR D  1 106 ? 16.384  -3.841  -35.939 1.00 10.21 ? 106 THR D CG2 1 
ATOM   7368  N  N   . VAL D  1 107 ? 14.390  -7.149  -33.481 1.00 10.08 ? 107 VAL D N   1 
ATOM   7369  C  CA  . VAL D  1 107 ? 14.199  -8.124  -32.383 1.00 10.85 ? 107 VAL D CA  1 
ATOM   7370  C  C   . VAL D  1 107 ? 15.471  -8.943  -32.352 1.00 10.69 ? 107 VAL D C   1 
ATOM   7371  O  O   . VAL D  1 107 ? 15.850  -9.540  -33.357 1.00 11.90 ? 107 VAL D O   1 
ATOM   7372  C  CB  . VAL D  1 107 ? 12.948  -8.967  -32.588 1.00 11.18 ? 107 VAL D CB  1 
ATOM   7373  C  CG1 . VAL D  1 107 ? 12.909  -10.004 -31.465 1.00 13.86 ? 107 VAL D CG1 1 
ATOM   7374  C  CG2 . VAL D  1 107 ? 11.683  -8.065  -32.585 1.00 11.27 ? 107 VAL D CG2 1 
ATOM   7375  N  N   . SER D  1 108 ? 16.088  -8.922  -31.192 1.00 11.76 ? 108 SER D N   1 
ATOM   7376  C  CA  . SER D  1 108 ? 17.399  -9.693  -31.030 1.00 12.02 ? 108 SER D CA  1 
ATOM   7377  C  C   . SER D  1 108 ? 18.331  -9.434  -32.173 1.00 12.83 ? 108 SER D C   1 
ATOM   7378  O  O   . SER D  1 108 ? 18.991  -10.332 -32.784 1.00 13.57 ? 108 SER D O   1 
ATOM   7379  C  CB  . SER D  1 108 ? 17.092  -11.198 -30.907 1.00 13.25 ? 108 SER D CB  1 
ATOM   7380  O  OG  . SER D  1 108 ? 16.315  -11.421 -29.774 1.00 15.82 ? 108 SER D OG  1 
ATOM   7381  N  N   . GLY D  1 109 ? 18.417  -8.151  -32.511 1.00 11.05 ? 109 GLY D N   1 
ATOM   7382  C  CA  . GLY D  1 109 ? 19.335  -7.686  -33.568 1.00 13.03 ? 109 GLY D CA  1 
ATOM   7383  C  C   . GLY D  1 109 ? 18.927  -7.825  -35.023 1.00 13.37 ? 109 GLY D C   1 
ATOM   7384  O  O   . GLY D  1 109 ? 19.739  -7.496  -35.905 1.00 17.92 ? 109 GLY D O   1 
ATOM   7385  N  N   A GLN D  1 110 ? 17.720  -8.306  -35.264 0.50 12.72 ? 110 GLN D N   1 
ATOM   7386  N  N   B GLN D  1 110 ? 17.746  -8.360  -35.300 0.50 13.97 ? 110 GLN D N   1 
ATOM   7387  C  CA  A GLN D  1 110 ? 17.282  -8.643  -36.581 0.50 12.78 ? 110 GLN D CA  1 
ATOM   7388  C  CA  B GLN D  1 110 ? 17.360  -8.634  -36.662 0.50 15.13 ? 110 GLN D CA  1 
ATOM   7389  C  C   A GLN D  1 110 ? 16.214  -7.692  -37.068 0.50 10.70 ? 110 GLN D C   1 
ATOM   7390  C  C   B GLN D  1 110 ? 16.257  -7.702  -37.069 0.50 11.85 ? 110 GLN D C   1 
ATOM   7391  O  O   A GLN D  1 110 ? 15.224  -7.482  -36.347 0.50 10.24 ? 110 GLN D O   1 
ATOM   7392  O  O   B GLN D  1 110 ? 15.311  -7.502  -36.293 0.50 11.35 ? 110 GLN D O   1 
ATOM   7393  C  CB  A GLN D  1 110 ? 16.704  -10.041 -36.583 0.50 12.31 ? 110 GLN D CB  1 
ATOM   7394  C  CB  B GLN D  1 110 ? 16.885  -10.076 -36.849 0.50 16.33 ? 110 GLN D CB  1 
ATOM   7395  C  CG  A GLN D  1 110 ? 17.611  -11.192 -36.059 0.50 13.90 ? 110 GLN D CG  1 
ATOM   7396  C  CG  B GLN D  1 110 ? 17.827  -11.175 -36.304 0.50 21.73 ? 110 GLN D CG  1 
ATOM   7397  C  CD  A GLN D  1 110 ? 19.022  -11.082 -36.585 0.50 15.72 ? 110 GLN D CD  1 
ATOM   7398  C  CD  B GLN D  1 110 ? 17.302  -12.583 -36.528 0.50 26.82 ? 110 GLN D CD  1 
ATOM   7399  O  OE1 A GLN D  1 110 ? 19.252  -11.211 -37.772 0.50 19.12 ? 110 GLN D OE1 1 
ATOM   7400  O  OE1 B GLN D  1 110 ? 16.792  -13.229 -35.596 0.50 32.38 ? 110 GLN D OE1 1 
ATOM   7401  N  NE2 A GLN D  1 110 ? 19.959  -10.798 -35.685 0.50 14.77 ? 110 GLN D NE2 1 
ATOM   7402  N  NE2 B GLN D  1 110 ? 17.384  -13.058 -37.766 0.50 31.98 ? 110 GLN D NE2 1 
ATOM   7403  N  N   . HIS D  1 111 ? 16.428  -7.114  -38.242 1.00 11.47 ? 111 HIS D N   1 
ATOM   7404  C  CA  . HIS D  1 111 ? 15.322  -6.375  -38.872 1.00 9.98  ? 111 HIS D CA  1 
ATOM   7405  C  C   . HIS D  1 111 ? 14.276  -7.303  -39.412 1.00 12.18 ? 111 HIS D C   1 
ATOM   7406  O  O   . HIS D  1 111 ? 14.577  -8.446  -39.872 1.00 15.15 ? 111 HIS D O   1 
ATOM   7407  C  CB  . HIS D  1 111 ? 15.806  -5.565  -40.061 1.00 11.54 ? 111 HIS D CB  1 
ATOM   7408  C  CG  . HIS D  1 111 ? 16.573  -4.342  -39.651 1.00 11.01 ? 111 HIS D CG  1 
ATOM   7409  N  ND1 . HIS D  1 111 ? 15.970  -3.114  -39.478 1.00 11.91 ? 111 HIS D ND1 1 
ATOM   7410  C  CD2 . HIS D  1 111 ? 17.886  -4.160  -39.405 1.00 12.64 ? 111 HIS D CD2 1 
ATOM   7411  C  CE1 . HIS D  1 111 ? 16.908  -2.231  -39.128 1.00 11.84 ? 111 HIS D CE1 1 
ATOM   7412  N  NE2 . HIS D  1 111 ? 18.080  -2.839  -39.072 1.00 14.76 ? 111 HIS D NE2 1 
ATOM   7413  N  N   . PHE D  1 112 ? 13.063  -6.797  -39.475 1.00 9.52  ? 112 PHE D N   1 
ATOM   7414  C  CA  . PHE D  1 112 ? 12.027  -7.445  -40.249 1.00 9.45  ? 112 PHE D CA  1 
ATOM   7415  C  C   . PHE D  1 112 ? 12.027  -6.650  -41.655 1.00 8.55  ? 112 PHE D C   1 
ATOM   7416  O  O   . PHE D  1 112 ? 12.765  -5.674  -41.794 1.00 9.02  ? 112 PHE D O   1 
ATOM   7417  C  CB  . PHE D  1 112 ? 10.704  -7.349  -39.527 1.00 11.32 ? 112 PHE D CB  1 
ATOM   7418  C  CG  . PHE D  1 112 ? 10.571  -8.405  -38.482 1.00 11.34 ? 112 PHE D CG  1 
ATOM   7419  C  CD1 . PHE D  1 112 ? 11.144  -8.283  -37.208 1.00 13.36 ? 112 PHE D CD1 1 
ATOM   7420  C  CD2 . PHE D  1 112 ? 9.902   -9.572  -38.803 1.00 15.15 ? 112 PHE D CD2 1 
ATOM   7421  C  CE1 . PHE D  1 112 ? 10.999  -9.305  -36.293 1.00 15.74 ? 112 PHE D CE1 1 
ATOM   7422  C  CE2 . PHE D  1 112 ? 9.746   -10.583 -37.897 1.00 18.40 ? 112 PHE D CE2 1 
ATOM   7423  C  CZ  . PHE D  1 112 ? 10.286  -10.461 -36.633 1.00 15.44 ? 112 PHE D CZ  1 
ATOM   7424  N  N   . ALA D  1 113 ? 11.204  -7.085  -42.577 1.00 8.16  ? 113 ALA D N   1 
ATOM   7425  C  CA  . ALA D  1 113 ? 11.195  -6.480  -43.896 1.00 8.76  ? 113 ALA D CA  1 
ATOM   7426  C  C   . ALA D  1 113 ? 10.731  -5.000  -43.848 1.00 8.37  ? 113 ALA D C   1 
ATOM   7427  O  O   . ALA D  1 113 ? 11.239  -4.187  -44.586 1.00 8.68  ? 113 ALA D O   1 
ATOM   7428  C  CB  . ALA D  1 113 ? 10.342  -7.277  -44.864 1.00 9.38  ? 113 ALA D CB  1 
ATOM   7429  N  N   . ALA D  1 114 ? 9.682   -4.755  -43.071 1.00 7.18  ? 114 ALA D N   1 
ATOM   7430  C  CA  . ALA D  1 114 ? 9.082   -3.426  -43.050 1.00 6.78  ? 114 ALA D CA  1 
ATOM   7431  C  C   . ALA D  1 114 ? 8.354   -3.294  -41.702 1.00 6.88  ? 114 ALA D C   1 
ATOM   7432  O  O   . ALA D  1 114 ? 8.359   -4.197  -40.837 1.00 7.30  ? 114 ALA D O   1 
ATOM   7433  C  CB  . ALA D  1 114 ? 8.149   -3.252  -44.240 1.00 7.59  ? 114 ALA D CB  1 
ATOM   7434  N  N   . GLU D  1 115 ? 7.747   -2.098  -41.517 1.00 7.02  ? 115 GLU D N   1 
ATOM   7435  C  CA  . GLU D  1 115 ? 7.025   -1.855  -40.240 1.00 6.85  ? 115 GLU D CA  1 
ATOM   7436  C  C   . GLU D  1 115 ? 5.901   -0.882  -40.500 1.00 6.98  ? 115 GLU D C   1 
ATOM   7437  O  O   . GLU D  1 115 ? 6.052   0.093   -41.260 1.00 7.48  ? 115 GLU D O   1 
ATOM   7438  C  CB  . GLU D  1 115 ? 8.029   -1.306  -39.190 1.00 7.09  ? 115 GLU D CB  1 
ATOM   7439  C  CG  . GLU D  1 115 ? 7.471   -1.127  -37.786 1.00 8.23  ? 115 GLU D CG  1 
ATOM   7440  C  CD  . GLU D  1 115 ? 8.555   -0.907  -36.792 1.00 8.03  ? 115 GLU D CD  1 
ATOM   7441  O  OE1 . GLU D  1 115 ? 9.690   -1.374  -36.984 1.00 7.84  ? 115 GLU D OE1 1 
ATOM   7442  O  OE2 . GLU D  1 115 ? 8.253   -0.289  -35.722 1.00 8.22  ? 115 GLU D OE2 1 
ATOM   7443  N  N   . LEU D  1 116 ? 4.737   -1.158  -39.897 1.00 6.94  ? 116 LEU D N   1 
ATOM   7444  C  CA  . LEU D  1 116 ? 3.547   -0.255  -39.929 1.00 6.70  ? 116 LEU D CA  1 
ATOM   7445  C  C   . LEU D  1 116 ? 3.432   0.441   -38.598 1.00 7.43  ? 116 LEU D C   1 
ATOM   7446  O  O   . LEU D  1 116 ? 3.576   -0.192  -37.560 1.00 7.67  ? 116 LEU D O   1 
ATOM   7447  C  CB  . LEU D  1 116 ? 2.287   -1.187  -40.080 1.00 7.39  ? 116 LEU D CB  1 
ATOM   7448  C  CG  . LEU D  1 116 ? 0.973   -0.370  -40.006 1.00 7.92  ? 116 LEU D CG  1 
ATOM   7449  C  CD1 . LEU D  1 116 ? 0.713   0.475   -41.238 1.00 9.54  ? 116 LEU D CD1 1 
ATOM   7450  C  CD2 . LEU D  1 116 ? -0.179  -1.343  -39.858 1.00 9.22  ? 116 LEU D CD2 1 
ATOM   7451  N  N   . HIS D  1 117 ? 3.227   1.753   -38.684 1.00 6.89  ? 117 HIS D N   1 
ATOM   7452  C  CA  . HIS D  1 117 ? 2.905   2.537   -37.477 1.00 6.67  ? 117 HIS D CA  1 
ATOM   7453  C  C   . HIS D  1 117 ? 1.518   3.140   -37.617 1.00 7.59  ? 117 HIS D C   1 
ATOM   7454  O  O   . HIS D  1 117 ? 1.205   3.832   -38.592 1.00 8.39  ? 117 HIS D O   1 
ATOM   7455  C  CB  . HIS D  1 117 ? 3.941   3.682   -37.421 1.00 7.35  ? 117 HIS D CB  1 
ATOM   7456  C  CG  . HIS D  1 117 ? 5.294   3.181   -37.090 1.00 6.70  ? 117 HIS D CG  1 
ATOM   7457  N  ND1 . HIS D  1 117 ? 6.467   3.915   -37.374 1.00 6.83  ? 117 HIS D ND1 1 
ATOM   7458  C  CD2 . HIS D  1 117 ? 5.702   2.020   -36.475 1.00 7.73  ? 117 HIS D CD2 1 
ATOM   7459  C  CE1 . HIS D  1 117 ? 7.506   3.200   -36.946 1.00 7.37  ? 117 HIS D CE1 1 
ATOM   7460  N  NE2 . HIS D  1 117 ? 7.075   2.039   -36.423 1.00 7.04  ? 117 HIS D NE2 1 
ATOM   7461  N  N   . ILE D  1 118 ? 0.681   2.823   -36.639 1.00 7.39  ? 118 ILE D N   1 
ATOM   7462  C  CA  . ILE D  1 118 ? -0.648  3.517   -36.515 1.00 7.53  ? 118 ILE D CA  1 
ATOM   7463  C  C   . ILE D  1 118 ? -0.541  4.513   -35.425 1.00 8.01  ? 118 ILE D C   1 
ATOM   7464  O  O   . ILE D  1 118 ? -0.386  4.160   -34.228 1.00 8.11  ? 118 ILE D O   1 
ATOM   7465  C  CB  . ILE D  1 118 ? -1.759  2.469   -36.262 1.00 7.81  ? 118 ILE D CB  1 
ATOM   7466  C  CG1 . ILE D  1 118 ? -1.625  1.240   -37.239 1.00 8.52  ? 118 ILE D CG1 1 
ATOM   7467  C  CG2 . ILE D  1 118 ? -3.120  3.178   -36.399 1.00 7.86  ? 118 ILE D CG2 1 
ATOM   7468  C  CD1 . ILE D  1 118 ? -2.731  0.189   -36.947 1.00 9.95  ? 118 ILE D CD1 1 
ATOM   7469  N  N   . VAL D  1 119 ? -0.503  5.788   -35.853 1.00 7.53  ? 119 VAL D N   1 
ATOM   7470  C  CA  . VAL D  1 119 ? -0.252  6.892   -34.912 1.00 7.84  ? 119 VAL D CA  1 
ATOM   7471  C  C   . VAL D  1 119 ? -1.575  7.403   -34.352 1.00 7.32  ? 119 VAL D C   1 
ATOM   7472  O  O   . VAL D  1 119 ? -2.521  7.626   -35.115 1.00 8.36  ? 119 VAL D O   1 
ATOM   7473  C  CB  . VAL D  1 119 ? 0.451   8.052   -35.677 1.00 7.22  ? 119 VAL D CB  1 
ATOM   7474  C  CG1 . VAL D  1 119 ? 0.797   9.152   -34.680 1.00 8.76  ? 119 VAL D CG1 1 
ATOM   7475  C  CG2 . VAL D  1 119 ? 1.747   7.537   -36.416 1.00 7.62  ? 119 VAL D CG2 1 
ATOM   7476  N  N   . HIS D  1 120 ? -1.580  7.558   -32.996 1.00 7.84  ? 120 HIS D N   1 
ATOM   7477  C  CA  . HIS D  1 120 ? -2.732  8.132   -32.283 1.00 8.11  ? 120 HIS D CA  1 
ATOM   7478  C  C   . HIS D  1 120 ? -2.249  9.266   -31.404 1.00 8.26  ? 120 HIS D C   1 
ATOM   7479  O  O   . HIS D  1 120 ? -1.075  9.332   -31.021 1.00 8.75  ? 120 HIS D O   1 
ATOM   7480  C  CB  . HIS D  1 120 ? -3.301  7.027   -31.348 1.00 8.53  ? 120 HIS D CB  1 
ATOM   7481  C  CG  . HIS D  1 120 ? -3.783  5.775   -32.039 1.00 8.81  ? 120 HIS D CG  1 
ATOM   7482  N  ND1 . HIS D  1 120 ? -2.885  4.827   -32.594 1.00 8.93  ? 120 HIS D ND1 1 
ATOM   7483  C  CD2 . HIS D  1 120 ? -5.011  5.231   -32.149 1.00 9.62  ? 120 HIS D CD2 1 
ATOM   7484  C  CE1 . HIS D  1 120 ? -3.601  3.778   -33.018 1.00 9.93  ? 120 HIS D CE1 1 
ATOM   7485  N  NE2 . HIS D  1 120 ? -4.903  3.996   -32.820 1.00 9.74  ? 120 HIS D NE2 1 
ATOM   7486  N  N   . TYR D  1 121 ? -3.191  10.163  -31.092 1.00 8.75  ? 121 TYR D N   1 
ATOM   7487  C  CA  . TYR D  1 121 ? -2.851  11.287  -30.207 1.00 8.97  ? 121 TYR D CA  1 
ATOM   7488  C  C   . TYR D  1 121 ? -3.768  11.247  -28.994 1.00 9.02  ? 121 TYR D C   1 
ATOM   7489  O  O   . TYR D  1 121 ? -4.892  10.728  -29.021 1.00 8.60  ? 121 TYR D O   1 
ATOM   7490  C  CB  . TYR D  1 121 ? -2.984  12.616  -30.998 1.00 9.90  ? 121 TYR D CB  1 
ATOM   7491  C  CG  . TYR D  1 121 ? -4.342  13.050  -31.345 1.00 10.01 ? 121 TYR D CG  1 
ATOM   7492  C  CD1 . TYR D  1 121 ? -4.970  12.560  -32.480 1.00 11.11 ? 121 TYR D CD1 1 
ATOM   7493  C  CD2 . TYR D  1 121 ? -4.995  13.950  -30.551 1.00 12.06 ? 121 TYR D CD2 1 
ATOM   7494  C  CE1 . TYR D  1 121 ? -6.278  12.882  -32.797 1.00 11.66 ? 121 TYR D CE1 1 
ATOM   7495  C  CE2 . TYR D  1 121 ? -6.318  14.305  -30.844 1.00 11.52 ? 121 TYR D CE2 1 
ATOM   7496  C  CZ  . TYR D  1 121 ? -6.935  13.805  -31.972 1.00 14.14 ? 121 TYR D CZ  1 
ATOM   7497  O  OH  . TYR D  1 121 ? -8.243  14.092  -32.363 1.00 17.95 ? 121 TYR D OH  1 
ATOM   7498  N  N   . ASN D  1 122 ? -3.298  11.916  -27.950 1.00 9.23  ? 122 ASN D N   1 
ATOM   7499  C  CA  . ASN D  1 122 ? -3.994  11.962  -26.635 1.00 10.84 ? 122 ASN D CA  1 
ATOM   7500  C  C   . ASN D  1 122 ? -5.133  12.996  -26.746 1.00 11.38 ? 122 ASN D C   1 
ATOM   7501  O  O   . ASN D  1 122 ? -4.871  14.197  -26.528 1.00 11.29 ? 122 ASN D O   1 
ATOM   7502  C  CB  . ASN D  1 122 ? -3.006  12.281  -25.535 1.00 9.75  ? 122 ASN D CB  1 
ATOM   7503  C  CG  . ASN D  1 122 ? -3.635  12.122  -24.172 1.00 9.69  ? 122 ASN D CG  1 
ATOM   7504  O  OD1 . ASN D  1 122 ? -4.859  12.276  -24.008 1.00 11.14 ? 122 ASN D OD1 1 
ATOM   7505  N  ND2 . ASN D  1 122 ? -2.760  11.852  -23.158 1.00 11.91 ? 122 ASN D ND2 1 
ATOM   7506  N  N   . SER D  1 123 ? -6.321  12.482  -27.073 1.00 10.21 ? 123 SER D N   1 
ATOM   7507  C  CA  . SER D  1 123 ? -7.484  13.333  -27.267 1.00 11.56 ? 123 SER D CA  1 
ATOM   7508  C  C   . SER D  1 123 ? -8.139  13.732  -25.945 1.00 12.68 ? 123 SER D C   1 
ATOM   7509  O  O   . SER D  1 123 ? -8.988  14.635  -25.981 1.00 15.71 ? 123 SER D O   1 
ATOM   7510  C  CB  . SER D  1 123 ? -8.462  12.733  -28.264 1.00 11.29 ? 123 SER D CB  1 
ATOM   7511  O  OG  . SER D  1 123 ? -8.704  11.370  -27.878 1.00 13.31 ? 123 SER D OG  1 
ATOM   7512  N  N   . ASP D  1 124 ? -7.706  13.199  -24.827 1.00 12.29 ? 124 ASP D N   1 
ATOM   7513  C  CA  . ASP D  1 124 ? -8.255  13.667  -23.537 1.00 11.89 ? 124 ASP D CA  1 
ATOM   7514  C  C   . ASP D  1 124 ? -7.495  14.956  -23.181 1.00 15.03 ? 124 ASP D C   1 
ATOM   7515  O  O   . ASP D  1 124 ? -8.054  15.772  -22.412 1.00 16.98 ? 124 ASP D O   1 
ATOM   7516  C  CB  . ASP D  1 124 ? -7.874  12.658  -22.445 1.00 12.83 ? 124 ASP D CB  1 
ATOM   7517  C  CG  . ASP D  1 124 ? -8.781  11.432  -22.493 1.00 11.37 ? 124 ASP D CG  1 
ATOM   7518  O  OD1 . ASP D  1 124 ? -9.795  11.410  -23.239 1.00 12.91 ? 124 ASP D OD1 1 
ATOM   7519  O  OD2 . ASP D  1 124 ? -8.465  10.480  -21.776 1.00 12.64 ? 124 ASP D OD2 1 
ATOM   7520  N  N   . LEU D  1 125 ? -6.302  15.187  -23.678 1.00 12.17 ? 125 LEU D N   1 
ATOM   7521  C  CA  . LEU D  1 125 ? -5.475  16.341  -23.356 1.00 12.33 ? 125 LEU D CA  1 
ATOM   7522  C  C   . LEU D  1 125 ? -5.414  17.361  -24.485 1.00 12.72 ? 125 LEU D C   1 
ATOM   7523  O  O   . LEU D  1 125 ? -5.272  18.581  -24.194 1.00 13.99 ? 125 LEU D O   1 
ATOM   7524  C  CB  . LEU D  1 125 ? -4.028  16.002  -22.950 1.00 13.12 ? 125 LEU D CB  1 
ATOM   7525  C  CG  . LEU D  1 125 ? -3.775  15.523  -21.497 1.00 13.65 ? 125 LEU D CG  1 
ATOM   7526  C  CD1 . LEU D  1 125 ? -4.640  14.343  -21.161 1.00 17.03 ? 125 LEU D CD1 1 
ATOM   7527  C  CD2 . LEU D  1 125 ? -2.334  15.177  -21.358 1.00 15.79 ? 125 LEU D CD2 1 
ATOM   7528  N  N   . TYR D  1 126 ? -5.472  16.942  -25.747 1.00 11.71 ? 126 TYR D N   1 
ATOM   7529  C  CA  . TYR D  1 126 ? -5.111  17.771  -26.847 1.00 11.77 ? 126 TYR D CA  1 
ATOM   7530  C  C   . TYR D  1 126 ? -6.130  17.725  -27.946 1.00 12.21 ? 126 TYR D C   1 
ATOM   7531  O  O   . TYR D  1 126 ? -6.800  16.727  -28.136 1.00 13.23 ? 126 TYR D O   1 
ATOM   7532  C  CB  . TYR D  1 126 ? -3.729  17.323  -27.439 1.00 11.54 ? 126 TYR D CB  1 
ATOM   7533  C  CG  . TYR D  1 126 ? -2.661  17.327  -26.406 1.00 10.18 ? 126 TYR D CG  1 
ATOM   7534  C  CD1 . TYR D  1 126 ? -2.274  18.485  -25.750 1.00 10.97 ? 126 TYR D CD1 1 
ATOM   7535  C  CD2 . TYR D  1 126 ? -2.071  16.098  -25.977 1.00 11.46 ? 126 TYR D CD2 1 
ATOM   7536  C  CE1 . TYR D  1 126 ? -1.379  18.473  -24.700 1.00 11.07 ? 126 TYR D CE1 1 
ATOM   7537  C  CE2 . TYR D  1 126 ? -1.084  16.062  -24.993 1.00 10.84 ? 126 TYR D CE2 1 
ATOM   7538  C  CZ  . TYR D  1 126 ? -0.755  17.248  -24.319 1.00 10.97 ? 126 TYR D CZ  1 
ATOM   7539  O  OH  . TYR D  1 126 ? 0.164   17.224  -23.266 1.00 11.34 ? 126 TYR D OH  1 
ATOM   7540  N  N   . PRO D  1 127 ? -6.265  18.856  -28.692 1.00 14.40 ? 127 PRO D N   1 
ATOM   7541  C  CA  . PRO D  1 127 ? -7.379  18.891  -29.623 1.00 15.22 ? 127 PRO D CA  1 
ATOM   7542  C  C   . PRO D  1 127 ? -7.121  18.244  -30.911 1.00 17.94 ? 127 PRO D C   1 
ATOM   7543  O  O   . PRO D  1 127 ? -8.037  18.016  -31.697 1.00 21.63 ? 127 PRO D O   1 
ATOM   7544  C  CB  . PRO D  1 127 ? -7.541  20.426  -29.862 1.00 17.58 ? 127 PRO D CB  1 
ATOM   7545  C  CG  . PRO D  1 127 ? -6.192  21.022  -29.518 1.00 15.60 ? 127 PRO D CG  1 
ATOM   7546  C  CD  . PRO D  1 127 ? -5.671  20.173  -28.383 1.00 14.40 ? 127 PRO D CD  1 
ATOM   7547  N  N   . ASP D  1 128 ? -5.863  18.000  -31.209 1.00 15.25 ? 128 ASP D N   1 
ATOM   7548  C  CA  . ASP D  1 128 ? -5.416  17.419  -32.462 1.00 14.37 ? 128 ASP D CA  1 
ATOM   7549  C  C   . ASP D  1 128 ? -4.034  16.834  -32.349 1.00 16.35 ? 128 ASP D C   1 
ATOM   7550  O  O   . ASP D  1 128 ? -3.271  17.158  -31.406 1.00 15.10 ? 128 ASP D O   1 
ATOM   7551  C  CB  . ASP D  1 128 ? -5.569  18.504  -33.570 1.00 17.57 ? 128 ASP D CB  1 
ATOM   7552  C  CG  . ASP D  1 128 ? -4.668  19.704  -33.244 1.00 20.25 ? 128 ASP D CG  1 
ATOM   7553  O  OD1 . ASP D  1 128 ? -5.093  20.695  -32.589 1.00 22.82 ? 128 ASP D OD1 1 
ATOM   7554  O  OD2 . ASP D  1 128 ? -3.471  19.583  -33.558 1.00 22.22 ? 128 ASP D OD2 1 
ATOM   7555  N  N   . ALA D  1 129 ? -3.584  16.105  -33.380 1.00 14.02 ? 129 ALA D N   1 
ATOM   7556  C  CA  . ALA D  1 129 ? -2.357  15.471  -33.316 1.00 13.16 ? 129 ALA D CA  1 
ATOM   7557  C  C   . ALA D  1 129 ? -1.150  16.438  -33.376 1.00 11.94 ? 129 ALA D C   1 
ATOM   7558  O  O   . ALA D  1 129 ? -0.097  16.210  -32.773 1.00 12.19 ? 129 ALA D O   1 
ATOM   7559  C  CB  . ALA D  1 129 ? -2.157  14.416  -34.448 1.00 18.14 ? 129 ALA D CB  1 
ATOM   7560  N  N   . SER D  1 130 ? -1.274  17.498  -34.247 1.00 13.18 ? 130 SER D N   1 
ATOM   7561  C  CA  . SER D  1 130 ? -0.131  18.435  -34.343 1.00 13.42 ? 130 SER D CA  1 
ATOM   7562  C  C   . SER D  1 130 ? 0.121   19.078  -32.963 1.00 11.04 ? 130 SER D C   1 
ATOM   7563  O  O   . SER D  1 130 ? 1.305   19.118  -32.491 1.00 12.75 ? 130 SER D O   1 
ATOM   7564  C  CB  . SER D  1 130 ? -0.476  19.499  -35.391 1.00 16.38 ? 130 SER D CB  1 
ATOM   7565  O  OG  . SER D  1 130 ? 0.644   20.400  -35.460 1.00 19.41 ? 130 SER D OG  1 
ATOM   7566  N  N   . THR D  1 131 ? -0.947  19.479  -32.306 1.00 11.82 ? 131 THR D N   1 
ATOM   7567  C  CA  . THR D  1 131 ? -0.796  20.091  -30.970 1.00 11.75 ? 131 THR D CA  1 
ATOM   7568  C  C   . THR D  1 131 ? -0.242  19.072  -29.971 1.00 12.29 ? 131 THR D C   1 
ATOM   7569  O  O   . THR D  1 131 ? 0.659   19.401  -29.137 1.00 13.11 ? 131 THR D O   1 
ATOM   7570  C  CB  . THR D  1 131 ? -2.146  20.594  -30.455 1.00 14.24 ? 131 THR D CB  1 
ATOM   7571  O  OG1 . THR D  1 131 ? -2.658  21.582  -31.413 1.00 15.19 ? 131 THR D OG1 1 
ATOM   7572  C  CG2 . THR D  1 131 ? -2.033  21.281  -29.047 1.00 13.65 ? 131 THR D CG2 1 
ATOM   7573  N  N   . ALA D  1 132 ? -0.688  17.846  -30.072 1.00 11.33 ? 132 ALA D N   1 
ATOM   7574  C  CA  . ALA D  1 132 ? -0.247  16.818  -29.151 1.00 10.86 ? 132 ALA D CA  1 
ATOM   7575  C  C   . ALA D  1 132 ? 1.232   16.394  -29.321 1.00 10.17 ? 132 ALA D C   1 
ATOM   7576  O  O   . ALA D  1 132 ? 1.939   15.928  -28.400 1.00 10.54 ? 132 ALA D O   1 
ATOM   7577  C  CB  . ALA D  1 132 ? -1.089  15.542  -29.384 1.00 10.79 ? 132 ALA D CB  1 
ATOM   7578  N  N   . SER D  1 133 ? 1.680   16.539  -30.583 1.00 10.27 ? 133 SER D N   1 
ATOM   7579  C  CA  . SER D  1 133 ? 2.943   15.900  -30.976 1.00 11.46 ? 133 SER D CA  1 
ATOM   7580  C  C   . SER D  1 133 ? 4.224   16.222  -30.193 1.00 11.60 ? 133 SER D C   1 
ATOM   7581  O  O   . SER D  1 133 ? 5.177   15.476  -30.056 1.00 12.81 ? 133 SER D O   1 
ATOM   7582  C  CB  . SER D  1 133 ? 3.209   16.059  -32.516 1.00 12.30 ? 133 SER D CB  1 
ATOM   7583  O  OG  . SER D  1 133 ? 3.565   17.432  -32.730 1.00 15.52 ? 133 SER D OG  1 
ATOM   7584  N  N   . ASN D  1 134 ? 4.267   17.493  -29.715 1.00 11.42 ? 134 ASN D N   1 
ATOM   7585  C  CA  . ASN D  1 134 ? 5.360   17.964  -28.900 1.00 12.06 ? 134 ASN D CA  1 
ATOM   7586  C  C   . ASN D  1 134 ? 5.098   18.138  -27.440 1.00 13.25 ? 134 ASN D C   1 
ATOM   7587  O  O   . ASN D  1 134 ? 5.872   18.803  -26.741 1.00 14.23 ? 134 ASN D O   1 
ATOM   7588  C  CB  . ASN D  1 134 ? 6.049   19.245  -29.479 1.00 14.82 ? 134 ASN D CB  1 
ATOM   7589  C  CG  . ASN D  1 134 ? 5.167   20.452  -29.352 1.00 18.31 ? 134 ASN D CG  1 
ATOM   7590  O  OD1 . ASN D  1 134 ? 3.921   20.338  -29.256 1.00 16.34 ? 134 ASN D OD1 1 
ATOM   7591  N  ND2 . ASN D  1 134 ? 5.791   21.641  -29.297 1.00 17.16 ? 134 ASN D ND2 1 
ATOM   7592  N  N   . LYS D  1 135 ? 4.013   17.530  -27.006 1.00 11.89 ? 135 LYS D N   1 
ATOM   7593  C  CA  . LYS D  1 135 ? 3.616   17.738  -25.607 1.00 11.42 ? 135 LYS D CA  1 
ATOM   7594  C  C   . LYS D  1 135 ? 3.493   16.451  -24.832 1.00 10.36 ? 135 LYS D C   1 
ATOM   7595  O  O   . LYS D  1 135 ? 3.473   15.317  -25.414 1.00 10.59 ? 135 LYS D O   1 
ATOM   7596  C  CB  . LYS D  1 135 ? 2.274   18.496  -25.598 1.00 12.40 ? 135 LYS D CB  1 
ATOM   7597  C  CG  . LYS D  1 135 ? 2.448   19.939  -26.173 1.00 12.65 ? 135 LYS D CG  1 
ATOM   7598  C  CD  . LYS D  1 135 ? 1.137   20.697  -26.097 1.00 13.91 ? 135 LYS D CD  1 
ATOM   7599  C  CE  . LYS D  1 135 ? 1.238   22.037  -26.874 1.00 14.21 ? 135 LYS D CE  1 
ATOM   7600  N  NZ  . LYS D  1 135 ? 1.677   21.858  -28.346 1.00 16.05 ? 135 LYS D NZ  1 
ATOM   7601  N  N   . SER D  1 136 ? 3.514   16.611  -23.503 1.00 12.22 ? 136 SER D N   1 
ATOM   7602  C  CA  . SER D  1 136 ? 3.597   15.451  -22.582 1.00 12.25 ? 136 SER D CA  1 
ATOM   7603  C  C   . SER D  1 136 ? 2.486   14.452  -22.889 1.00 11.98 ? 136 SER D C   1 
ATOM   7604  O  O   . SER D  1 136 ? 1.328   14.819  -23.024 1.00 11.16 ? 136 SER D O   1 
ATOM   7605  C  CB  . SER D  1 136 ? 3.420   16.016  -21.191 1.00 14.27 ? 136 SER D CB  1 
ATOM   7606  O  OG  . SER D  1 136 ? 3.699   14.940  -20.297 1.00 18.49 ? 136 SER D OG  1 
ATOM   7607  N  N   . GLU D  1 137 ? 2.869   13.167  -22.943 1.00 11.64 ? 137 GLU D N   1 
ATOM   7608  C  CA  . GLU D  1 137 ? 1.901   12.101  -23.167 1.00 11.77 ? 137 GLU D CA  1 
ATOM   7609  C  C   . GLU D  1 137 ? 1.131   12.237  -24.476 1.00 10.15 ? 137 GLU D C   1 
ATOM   7610  O  O   . GLU D  1 137 ? 0.022   11.777  -24.650 1.00 11.44 ? 137 GLU D O   1 
ATOM   7611  C  CB  . GLU D  1 137 ? 0.895   11.918  -22.003 1.00 11.94 ? 137 GLU D CB  1 
ATOM   7612  C  CG  . GLU D  1 137 ? 1.521   11.863  -20.586 1.00 14.89 ? 137 GLU D CG  1 
ATOM   7613  C  CD  . GLU D  1 137 ? 2.406   10.648  -20.345 1.00 21.26 ? 137 GLU D CD  1 
ATOM   7614  O  OE1 . GLU D  1 137 ? 2.290   9.586   -20.999 1.00 26.26 ? 137 GLU D OE1 1 
ATOM   7615  O  OE2 . GLU D  1 137 ? 3.377   10.857  -19.589 1.00 29.92 ? 137 GLU D OE2 1 
ATOM   7616  N  N   . GLY D  1 138 ? 1.725   12.963  -25.453 1.00 9.35  ? 138 GLY D N   1 
ATOM   7617  C  CA  . GLY D  1 138 ? 0.933   13.340  -26.583 1.00 10.77 ? 138 GLY D CA  1 
ATOM   7618  C  C   . GLY D  1 138 ? 0.522   12.211  -27.539 1.00 8.69  ? 138 GLY D C   1 
ATOM   7619  O  O   . GLY D  1 138 ? -0.515  12.345  -28.169 1.00 9.70  ? 138 GLY D O   1 
ATOM   7620  N  N   . LEU D  1 139 ? 1.402   11.229  -27.741 1.00 8.75  ? 139 LEU D N   1 
ATOM   7621  C  CA  . LEU D  1 139 ? 1.144   10.275  -28.901 1.00 8.77  ? 139 LEU D CA  1 
ATOM   7622  C  C   . LEU D  1 139 ? 1.265   8.851   -28.387 1.00 8.60  ? 139 LEU D C   1 
ATOM   7623  O  O   . LEU D  1 139 ? 1.997   8.558   -27.420 1.00 9.14  ? 139 LEU D O   1 
ATOM   7624  C  CB  . LEU D  1 139 ? 2.231   10.535  -30.000 1.00 9.22  ? 139 LEU D CB  1 
ATOM   7625  C  CG  . LEU D  1 139 ? 2.193   11.906  -30.645 1.00 8.86  ? 139 LEU D CG  1 
ATOM   7626  C  CD1 . LEU D  1 139 ? 3.453   12.039  -31.544 1.00 12.22 ? 139 LEU D CD1 1 
ATOM   7627  C  CD2 . LEU D  1 139 ? 0.916   12.125  -31.451 1.00 11.44 ? 139 LEU D CD2 1 
ATOM   7628  N  N   . ALA D  1 140 ? 0.594   7.939   -29.107 1.00 8.88  ? 140 ALA D N   1 
ATOM   7629  C  CA  . ALA D  1 140 ? 0.768   6.492   -28.838 1.00 8.17  ? 140 ALA D CA  1 
ATOM   7630  C  C   . ALA D  1 140 ? 0.786   5.871   -30.234 1.00 8.75  ? 140 ALA D C   1 
ATOM   7631  O  O   . ALA D  1 140 ? -0.061  6.170   -31.094 1.00 9.41  ? 140 ALA D O   1 
ATOM   7632  C  CB  . ALA D  1 140 ? -0.363  5.934   -28.024 1.00 9.33  ? 140 ALA D CB  1 
ATOM   7633  N  N   . VAL D  1 141 ? 1.758   5.026   -30.482 1.00 8.49  ? 141 VAL D N   1 
ATOM   7634  C  CA  . VAL D  1 141 ? 1.829   4.296   -31.718 1.00 8.65  ? 141 VAL D CA  1 
ATOM   7635  C  C   . VAL D  1 141 ? 1.619   2.792   -31.487 1.00 7.86  ? 141 VAL D C   1 
ATOM   7636  O  O   . VAL D  1 141 ? 2.219   2.230   -30.554 1.00 8.49  ? 141 VAL D O   1 
ATOM   7637  C  CB  . VAL D  1 141 ? 3.179   4.572   -32.401 1.00 7.74  ? 141 VAL D CB  1 
ATOM   7638  C  CG1 . VAL D  1 141 ? 3.326   3.794   -33.760 1.00 9.15  ? 141 VAL D CG1 1 
ATOM   7639  C  CG2 . VAL D  1 141 ? 3.361   6.076   -32.676 1.00 9.34  ? 141 VAL D CG2 1 
ATOM   7640  N  N   . LEU D  1 142 ? 0.917   2.187   -32.449 1.00 7.46  ? 142 LEU D N   1 
ATOM   7641  C  CA  . LEU D  1 142 ? 0.893   0.712   -32.546 1.00 7.86  ? 142 LEU D CA  1 
ATOM   7642  C  C   . LEU D  1 142 ? 1.797   0.362   -33.681 1.00 8.05  ? 142 LEU D C   1 
ATOM   7643  O  O   . LEU D  1 142 ? 1.650   0.868   -34.807 1.00 9.69  ? 142 LEU D O   1 
ATOM   7644  C  CB  . LEU D  1 142 ? -0.496  0.216   -32.848 1.00 8.76  ? 142 LEU D CB  1 
ATOM   7645  C  CG  . LEU D  1 142 ? -1.624  0.594   -31.891 1.00 9.81  ? 142 LEU D CG  1 
ATOM   7646  C  CD1 . LEU D  1 142 ? -2.860  -0.067  -32.360 1.00 10.85 ? 142 LEU D CD1 1 
ATOM   7647  C  CD2 . LEU D  1 142 ? -1.270  0.170   -30.413 1.00 10.91 ? 142 LEU D CD2 1 
ATOM   7648  N  N   . ALA D  1 143 ? 2.811   -0.433  -33.390 1.00 8.55  ? 143 ALA D N   1 
ATOM   7649  C  CA  . ALA D  1 143 ? 3.811   -0.881  -34.408 1.00 8.26  ? 143 ALA D CA  1 
ATOM   7650  C  C   . ALA D  1 143 ? 3.611   -2.353  -34.698 1.00 8.31  ? 143 ALA D C   1 
ATOM   7651  O  O   . ALA D  1 143 ? 3.556   -3.207  -33.808 1.00 8.70  ? 143 ALA D O   1 
ATOM   7652  C  CB  . ALA D  1 143 ? 5.194   -0.596  -33.837 1.00 8.73  ? 143 ALA D CB  1 
ATOM   7653  N  N   . VAL D  1 144 ? 3.516   -2.604  -35.987 1.00 7.34  ? 144 VAL D N   1 
ATOM   7654  C  CA  . VAL D  1 144 ? 3.397   -4.004  -36.512 1.00 7.55  ? 144 VAL D CA  1 
ATOM   7655  C  C   . VAL D  1 144 ? 4.650   -4.294  -37.342 1.00 7.45  ? 144 VAL D C   1 
ATOM   7656  O  O   . VAL D  1 144 ? 4.934   -3.615  -38.335 1.00 7.96  ? 144 VAL D O   1 
ATOM   7657  C  CB  . VAL D  1 144 ? 2.160   -4.173  -37.334 1.00 7.68  ? 144 VAL D CB  1 
ATOM   7658  C  CG1 . VAL D  1 144 ? 2.004   -5.637  -37.795 1.00 9.95  ? 144 VAL D CG1 1 
ATOM   7659  C  CG2 . VAL D  1 144 ? 0.906   -3.737  -36.594 1.00 8.74  ? 144 VAL D CG2 1 
ATOM   7660  N  N   . LEU D  1 145 ? 5.374   -5.316  -36.904 1.00 7.76  ? 145 LEU D N   1 
ATOM   7661  C  CA  . LEU D  1 145 ? 6.534   -5.787  -37.649 1.00 8.47  ? 145 LEU D CA  1 
ATOM   7662  C  C   . LEU D  1 145 ? 6.059   -6.603  -38.853 1.00 7.61  ? 145 LEU D C   1 
ATOM   7663  O  O   . LEU D  1 145 ? 5.088   -7.402  -38.721 1.00 8.08  ? 145 LEU D O   1 
ATOM   7664  C  CB  . LEU D  1 145 ? 7.423   -6.663  -36.751 1.00 9.13  ? 145 LEU D CB  1 
ATOM   7665  C  CG  . LEU D  1 145 ? 7.944   -5.931  -35.565 1.00 9.31  ? 145 LEU D CG  1 
ATOM   7666  C  CD1 . LEU D  1 145 ? 8.447   -6.897  -34.488 1.00 11.77 ? 145 LEU D CD1 1 
ATOM   7667  C  CD2 . LEU D  1 145 ? 9.039   -4.946  -35.966 1.00 13.45 ? 145 LEU D CD2 1 
ATOM   7668  N  N   . ILE D  1 146 ? 6.658   -6.373  -40.026 1.00 7.78  ? 146 ILE D N   1 
ATOM   7669  C  CA  . ILE D  1 146 ? 6.221   -7.016  -41.244 1.00 8.22  ? 146 ILE D CA  1 
ATOM   7670  C  C   . ILE D  1 146 ? 7.288   -7.880  -41.831 1.00 8.48  ? 146 ILE D C   1 
ATOM   7671  O  O   . ILE D  1 146 ? 8.410   -7.404  -42.101 1.00 8.44  ? 146 ILE D O   1 
ATOM   7672  C  CB  . ILE D  1 146 ? 5.798   -5.955  -42.281 1.00 7.55  ? 146 ILE D CB  1 
ATOM   7673  C  CG1 . ILE D  1 146 ? 4.638   -5.096  -41.770 1.00 8.99  ? 146 ILE D CG1 1 
ATOM   7674  C  CG2 . ILE D  1 146 ? 5.412   -6.627  -43.634 1.00 8.55  ? 146 ILE D CG2 1 
ATOM   7675  C  CD1 . ILE D  1 146 ? 4.370   -3.879  -42.662 1.00 9.00  ? 146 ILE D CD1 1 
ATOM   7676  N  N   A GLU D  1 147 ? 7.020   -9.205  -41.897 0.50 8.48  ? 147 GLU D N   1 
ATOM   7677  N  N   B GLU D  1 147 ? 6.954   -9.178  -41.986 0.50 7.95  ? 147 GLU D N   1 
ATOM   7678  C  CA  A GLU D  1 147 ? 7.977   -10.119 -42.457 0.50 10.16 ? 147 GLU D CA  1 
ATOM   7679  C  CA  B GLU D  1 147 ? 7.877   -10.145 -42.521 0.50 9.05  ? 147 GLU D CA  1 
ATOM   7680  C  C   A GLU D  1 147 ? 7.599   -10.627 -43.859 0.50 9.09  ? 147 GLU D C   1 
ATOM   7681  C  C   B GLU D  1 147 ? 7.559   -10.496 -43.968 0.50 8.51  ? 147 GLU D C   1 
ATOM   7682  O  O   A GLU D  1 147 ? 6.420   -10.633 -44.161 0.50 9.09  ? 147 GLU D O   1 
ATOM   7683  O  O   B GLU D  1 147 ? 6.407   -10.472 -44.379 0.50 8.63  ? 147 GLU D O   1 
ATOM   7684  C  CB  A GLU D  1 147 ? 8.006   -11.453 -41.495 0.50 11.19 ? 147 GLU D CB  1 
ATOM   7685  C  CB  B GLU D  1 147 ? 7.715   -11.462 -41.682 0.50 9.17  ? 147 GLU D CB  1 
ATOM   7686  C  CG  A GLU D  1 147 ? 7.263   -12.770 -41.907 0.50 15.54 ? 147 GLU D CG  1 
ATOM   7687  C  CG  B GLU D  1 147 ? 8.746   -12.548 -41.968 0.50 9.71  ? 147 GLU D CG  1 
ATOM   7688  C  CD  A GLU D  1 147 ? 7.144   -13.711 -40.656 0.50 14.38 ? 147 GLU D CD  1 
ATOM   7689  C  CD  B GLU D  1 147 ? 8.937   -13.551 -40.814 0.50 11.95 ? 147 GLU D CD  1 
ATOM   7690  O  OE1 A GLU D  1 147 ? 8.086   -13.739 -39.872 0.50 15.09 ? 147 GLU D OE1 1 
ATOM   7691  O  OE1 B GLU D  1 147 ? 8.617   -13.240 -39.635 0.50 16.29 ? 147 GLU D OE1 1 
ATOM   7692  O  OE2 A GLU D  1 147 ? 6.152   -14.503 -40.431 0.50 15.85 ? 147 GLU D OE2 1 
ATOM   7693  O  OE2 B GLU D  1 147 ? 9.425   -14.670 -41.092 0.50 18.14 ? 147 GLU D OE2 1 
ATOM   7694  N  N   . MET D  1 148 ? 8.589   -10.753 -44.767 1.00 9.00  ? 148 MET D N   1 
ATOM   7695  C  CA  . MET D  1 148 ? 8.362   -11.334 -46.105 1.00 9.68  ? 148 MET D CA  1 
ATOM   7696  C  C   . MET D  1 148 ? 7.762   -12.730 -45.990 1.00 8.85  ? 148 MET D C   1 
ATOM   7697  O  O   . MET D  1 148 ? 8.362   -13.603 -45.356 1.00 9.99  ? 148 MET D O   1 
ATOM   7698  C  CB  . MET D  1 148 ? 9.662   -11.346 -46.882 1.00 9.56  ? 148 MET D CB  1 
ATOM   7699  C  CG  . MET D  1 148 ? 9.429   -11.750 -48.292 1.00 10.52 ? 148 MET D CG  1 
ATOM   7700  S  SD  . MET D  1 148 ? 10.994  -11.836 -49.268 1.00 12.04 ? 148 MET D SD  1 
ATOM   7701  C  CE  . MET D  1 148 ? 11.466  -10.113 -49.244 1.00 13.17 ? 148 MET D CE  1 
ATOM   7702  N  N   . GLY D  1 149 ? 6.606   -12.884 -46.576 1.00 8.69  ? 149 GLY D N   1 
ATOM   7703  C  CA  . GLY D  1 149 ? 5.863   -14.145 -46.470 1.00 8.22  ? 149 GLY D CA  1 
ATOM   7704  C  C   . GLY D  1 149 ? 4.757   -14.237 -47.536 1.00 7.62  ? 149 GLY D C   1 
ATOM   7705  O  O   . GLY D  1 149 ? 4.943   -14.011 -48.713 1.00 8.67  ? 149 GLY D O   1 
ATOM   7706  N  N   . SER D  1 150 ? 3.549   -14.591 -47.066 1.00 8.54  ? 150 SER D N   1 
ATOM   7707  C  CA  . SER D  1 150 ? 2.340   -14.688 -47.940 1.00 8.77  ? 150 SER D CA  1 
ATOM   7708  C  C   . SER D  1 150 ? 1.787   -13.341 -48.291 1.00 8.97  ? 150 SER D C   1 
ATOM   7709  O  O   . SER D  1 150 ? 1.848   -12.403 -47.510 1.00 9.92  ? 150 SER D O   1 
ATOM   7710  C  CB  . SER D  1 150 ? 1.290   -15.477 -47.197 1.00 9.05  ? 150 SER D CB  1 
ATOM   7711  O  OG  . SER D  1 150 ? 1.730   -16.873 -47.070 1.00 9.36  ? 150 SER D OG  1 
ATOM   7712  N  N   . PHE D  1 151 ? 1.222   -13.313 -49.486 1.00 9.34  ? 151 PHE D N   1 
ATOM   7713  C  CA  . PHE D  1 151 ? 0.401   -12.171 -49.910 1.00 8.49  ? 151 PHE D CA  1 
ATOM   7714  C  C   . PHE D  1 151 ? -0.627  -11.815 -48.870 1.00 10.52 ? 151 PHE D C   1 
ATOM   7715  O  O   . PHE D  1 151 ? -1.298  -12.713 -48.326 1.00 11.25 ? 151 PHE D O   1 
ATOM   7716  C  CB  . PHE D  1 151 ? -0.221  -12.512 -51.217 1.00 10.44 ? 151 PHE D CB  1 
ATOM   7717  C  CG  . PHE D  1 151 ? -1.072  -11.374 -51.741 1.00 10.65 ? 151 PHE D CG  1 
ATOM   7718  C  CD1 . PHE D  1 151 ? -0.485  -10.322 -52.436 1.00 11.94 ? 151 PHE D CD1 1 
ATOM   7719  C  CD2 . PHE D  1 151 ? -2.446  -11.447 -51.613 1.00 11.39 ? 151 PHE D CD2 1 
ATOM   7720  C  CE1 . PHE D  1 151 ? -1.325  -9.251  -52.901 1.00 11.51 ? 151 PHE D CE1 1 
ATOM   7721  C  CE2 . PHE D  1 151 ? -3.241  -10.428 -52.052 1.00 10.93 ? 151 PHE D CE2 1 
ATOM   7722  C  CZ  . PHE D  1 151 ? -2.674  -9.382  -52.700 1.00 10.88 ? 151 PHE D CZ  1 
ATOM   7723  N  N   . ASN D  1 152 ? -0.773  -10.505 -48.627 1.00 9.19  ? 152 ASN D N   1 
ATOM   7724  C  CA  . ASN D  1 152 ? -1.663  -10.078 -47.622 1.00 9.68  ? 152 ASN D CA  1 
ATOM   7725  C  C   . ASN D  1 152 ? -2.745  -9.172  -48.274 1.00 9.37  ? 152 ASN D C   1 
ATOM   7726  O  O   . ASN D  1 152 ? -2.452  -7.994  -48.652 1.00 9.80  ? 152 ASN D O   1 
ATOM   7727  C  CB  . ASN D  1 152 ? -0.872  -9.268  -46.559 1.00 8.53  ? 152 ASN D CB  1 
ATOM   7728  C  CG  . ASN D  1 152 ? -1.674  -8.980  -45.314 1.00 9.71  ? 152 ASN D CG  1 
ATOM   7729  O  OD1 . ASN D  1 152 ? -2.815  -8.465  -45.465 1.00 9.69  ? 152 ASN D OD1 1 
ATOM   7730  N  ND2 . ASN D  1 152 ? -1.179  -9.292  -44.141 1.00 9.55  ? 152 ASN D ND2 1 
ATOM   7731  N  N   . PRO D  1 153 ? -3.975  -9.680  -48.418 1.00 11.45 ? 153 PRO D N   1 
ATOM   7732  C  CA  . PRO D  1 153 ? -4.984  -8.877  -49.105 1.00 11.21 ? 153 PRO D CA  1 
ATOM   7733  C  C   . PRO D  1 153 ? -5.373  -7.635  -48.352 1.00 11.77 ? 153 PRO D C   1 
ATOM   7734  O  O   . PRO D  1 153 ? -5.772  -6.671  -49.006 1.00 13.38 ? 153 PRO D O   1 
ATOM   7735  C  CB  . PRO D  1 153 ? -6.187  -9.844  -49.232 1.00 12.62 ? 153 PRO D CB  1 
ATOM   7736  C  CG  . PRO D  1 153 ? -5.600  -11.221 -49.137 1.00 16.96 ? 153 PRO D CG  1 
ATOM   7737  C  CD  . PRO D  1 153 ? -4.412  -11.057 -48.175 1.00 12.60 ? 153 PRO D CD  1 
ATOM   7738  N  N   . SER D  1 154 ? -5.191  -7.586  -47.064 1.00 10.50 ? 154 SER D N   1 
ATOM   7739  C  CA  . SER D  1 154 ? -5.610  -6.391  -46.318 1.00 10.01 ? 154 SER D CA  1 
ATOM   7740  C  C   . SER D  1 154 ? -4.566  -5.293  -46.495 1.00 10.39 ? 154 SER D C   1 
ATOM   7741  O  O   . SER D  1 154 ? -4.923  -4.120  -46.771 1.00 11.20 ? 154 SER D O   1 
ATOM   7742  C  CB  . SER D  1 154 ? -5.742  -6.700  -44.837 1.00 12.14 ? 154 SER D CB  1 
ATOM   7743  O  OG  . SER D  1 154 ? -6.714  -7.740  -44.651 1.00 14.76 ? 154 SER D OG  1 
ATOM   7744  N  N   . TYR D  1 155 ? -3.252  -5.582  -46.361 1.00 9.22  ? 155 TYR D N   1 
ATOM   7745  C  CA  . TYR D  1 155 ? -2.253  -4.557  -46.734 1.00 9.73  ? 155 TYR D CA  1 
ATOM   7746  C  C   . TYR D  1 155 ? -2.359  -4.150  -48.196 1.00 9.25  ? 155 TYR D C   1 
ATOM   7747  O  O   . TYR D  1 155 ? -2.097  -2.976  -48.535 1.00 10.35 ? 155 TYR D O   1 
ATOM   7748  C  CB  . TYR D  1 155 ? -0.838  -5.060  -46.395 1.00 8.98  ? 155 TYR D CB  1 
ATOM   7749  C  CG  . TYR D  1 155 ? -0.490  -4.926  -44.949 1.00 8.98  ? 155 TYR D CG  1 
ATOM   7750  C  CD1 . TYR D  1 155 ? -0.927  -5.848  -43.985 1.00 8.67  ? 155 TYR D CD1 1 
ATOM   7751  C  CD2 . TYR D  1 155 ? 0.258   -3.807  -44.510 1.00 9.16  ? 155 TYR D CD2 1 
ATOM   7752  C  CE1 . TYR D  1 155 ? -0.665  -5.722  -42.650 1.00 9.69  ? 155 TYR D CE1 1 
ATOM   7753  C  CE2 . TYR D  1 155 ? 0.595   -3.713  -43.193 1.00 9.30  ? 155 TYR D CE2 1 
ATOM   7754  C  CZ  . TYR D  1 155 ? 0.097   -4.641  -42.238 1.00 9.44  ? 155 TYR D CZ  1 
ATOM   7755  O  OH  . TYR D  1 155 ? 0.404   -4.468  -40.905 1.00 9.91  ? 155 TYR D OH  1 
ATOM   7756  N  N   . ASP D  1 156 ? -2.815  -5.043  -49.090 1.00 9.94  ? 156 ASP D N   1 
ATOM   7757  C  CA  . ASP D  1 156 ? -2.940  -4.677  -50.465 1.00 9.54  ? 156 ASP D CA  1 
ATOM   7758  C  C   . ASP D  1 156 ? -4.033  -3.571  -50.674 1.00 8.79  ? 156 ASP D C   1 
ATOM   7759  O  O   . ASP D  1 156 ? -4.038  -2.953  -51.737 1.00 11.30 ? 156 ASP D O   1 
ATOM   7760  C  CB  . ASP D  1 156 ? -3.120  -5.863  -51.361 1.00 11.67 ? 156 ASP D CB  1 
ATOM   7761  C  CG  . ASP D  1 156 ? -2.310  -5.733  -52.633 1.00 12.66 ? 156 ASP D CG  1 
ATOM   7762  O  OD1 . ASP D  1 156 ? -1.080  -5.548  -52.532 1.00 11.96 ? 156 ASP D OD1 1 
ATOM   7763  O  OD2 . ASP D  1 156 ? -2.940  -5.790  -53.699 1.00 15.52 ? 156 ASP D OD2 1 
ATOM   7764  N  N   . LYS D  1 157 ? -4.979  -3.463  -49.731 1.00 9.94  ? 157 LYS D N   1 
ATOM   7765  C  CA  . LYS D  1 157 ? -6.003  -2.362  -49.865 1.00 10.98 ? 157 LYS D CA  1 
ATOM   7766  C  C   . LYS D  1 157 ? -5.300  -1.018  -49.750 1.00 11.78 ? 157 LYS D C   1 
ATOM   7767  O  O   . LYS D  1 157 ? -5.817  -0.090  -50.398 1.00 13.09 ? 157 LYS D O   1 
ATOM   7768  C  CB  . LYS D  1 157 ? -7.032  -2.519  -48.754 1.00 12.92 ? 157 LYS D CB  1 
ATOM   7769  C  CG  . LYS D  1 157 ? -7.878  -3.749  -48.909 1.00 14.39 ? 157 LYS D CG  1 
ATOM   7770  C  CD  . LYS D  1 157 ? -8.724  -4.019  -47.633 1.00 19.04 ? 157 LYS D CD  1 
ATOM   7771  C  CE  . LYS D  1 157 ? -9.496  -5.364  -47.836 1.00 22.64 ? 157 LYS D CE  1 
ATOM   7772  N  NZ  . LYS D  1 157 ? -10.170 -5.997  -46.616 1.00 26.60 ? 157 LYS D NZ  1 
ATOM   7773  N  N   . ILE D  1 158 ? -4.084  -0.934  -49.202 1.00 10.94 ? 158 ILE D N   1 
ATOM   7774  C  CA  . ILE D  1 158 ? -3.254  0.278   -49.246 1.00 11.75 ? 158 ILE D CA  1 
ATOM   7775  C  C   . ILE D  1 158 ? -2.394  0.238   -50.480 1.00 10.97 ? 158 ILE D C   1 
ATOM   7776  O  O   . ILE D  1 158 ? -2.308  1.174   -51.316 1.00 10.89 ? 158 ILE D O   1 
ATOM   7777  C  CB  . ILE D  1 158 ? -2.398  0.408   -47.985 1.00 11.11 ? 158 ILE D CB  1 
ATOM   7778  C  CG1 . ILE D  1 158 ? -3.314  0.658   -46.804 1.00 13.84 ? 158 ILE D CG1 1 
ATOM   7779  C  CG2 . ILE D  1 158 ? -1.425  1.581   -48.140 1.00 11.68 ? 158 ILE D CG2 1 
ATOM   7780  C  CD1 . ILE D  1 158 ? -2.549  0.422   -45.499 1.00 16.79 ? 158 ILE D CD1 1 
ATOM   7781  N  N   . PHE D  1 159 ? -1.623  -0.893  -50.638 1.00 10.58 ? 159 PHE D N   1 
ATOM   7782  C  CA  . PHE D  1 159 ? -0.667  -0.972  -51.728 1.00 10.99 ? 159 PHE D CA  1 
ATOM   7783  C  C   . PHE D  1 159 ? -1.173  -0.792  -53.153 1.00 10.98 ? 159 PHE D C   1 
ATOM   7784  O  O   . PHE D  1 159 ? -0.410  -0.346  -54.023 1.00 11.98 ? 159 PHE D O   1 
ATOM   7785  C  CB  . PHE D  1 159 ? 0.223   -2.241  -51.588 1.00 10.51 ? 159 PHE D CB  1 
ATOM   7786  C  CG  . PHE D  1 159 ? 0.923   -2.442  -50.260 1.00 10.46 ? 159 PHE D CG  1 
ATOM   7787  C  CD1 . PHE D  1 159 ? 1.369   -1.395  -49.453 1.00 12.26 ? 159 PHE D CD1 1 
ATOM   7788  C  CD2 . PHE D  1 159 ? 1.179   -3.735  -49.856 1.00 11.26 ? 159 PHE D CD2 1 
ATOM   7789  C  CE1 . PHE D  1 159 ? 2.038   -1.659  -48.255 1.00 12.63 ? 159 PHE D CE1 1 
ATOM   7790  C  CE2 . PHE D  1 159 ? 1.840   -4.006  -48.667 1.00 11.66 ? 159 PHE D CE2 1 
ATOM   7791  C  CZ  . PHE D  1 159 ? 2.266   -2.966  -47.874 1.00 10.69 ? 159 PHE D CZ  1 
ATOM   7792  N  N   . SER D  1 160 ? -2.436  -1.215  -53.399 1.00 11.57 ? 160 SER D N   1 
ATOM   7793  C  CA  . SER D  1 160 ? -2.957  -1.040  -54.751 1.00 11.64 ? 160 SER D CA  1 
ATOM   7794  C  C   . SER D  1 160 ? -3.095  0.367   -55.183 1.00 11.86 ? 160 SER D C   1 
ATOM   7795  O  O   . SER D  1 160 ? -3.134  0.609   -56.400 1.00 14.34 ? 160 SER D O   1 
ATOM   7796  C  CB  . SER D  1 160 ? -4.306  -1.732  -54.889 1.00 12.47 ? 160 SER D CB  1 
ATOM   7797  O  OG  . SER D  1 160 ? -5.240  -1.064  -54.051 1.00 13.63 ? 160 SER D OG  1 
ATOM   7798  N  N   . HIS D  1 161 ? -2.959  1.331   -54.273 1.00 10.62 ? 161 HIS D N   1 
ATOM   7799  C  CA  . HIS D  1 161 ? -3.022  2.750   -54.646 1.00 11.88 ? 161 HIS D CA  1 
ATOM   7800  C  C   . HIS D  1 161 ? -1.675  3.466   -54.753 1.00 12.15 ? 161 HIS D C   1 
ATOM   7801  O  O   . HIS D  1 161 ? -1.648  4.661   -55.100 1.00 13.29 ? 161 HIS D O   1 
ATOM   7802  C  CB  . HIS D  1 161 ? -3.869  3.517   -53.571 1.00 11.56 ? 161 HIS D CB  1 
ATOM   7803  C  CG  . HIS D  1 161 ? -5.236  3.033   -53.447 1.00 13.16 ? 161 HIS D CG  1 
ATOM   7804  N  ND1 . HIS D  1 161 ? -6.242  3.638   -54.175 1.00 14.94 ? 161 HIS D ND1 1 
ATOM   7805  C  CD2 . HIS D  1 161 ? -5.814  2.092   -52.664 1.00 13.88 ? 161 HIS D CD2 1 
ATOM   7806  C  CE1 . HIS D  1 161 ? -7.393  3.025   -53.872 1.00 14.49 ? 161 HIS D CE1 1 
ATOM   7807  N  NE2 . HIS D  1 161 ? -7.146  2.035   -52.996 1.00 15.16 ? 161 HIS D NE2 1 
ATOM   7808  N  N   . LEU D  1 162 ? -0.555  2.698   -54.597 1.00 12.45 ? 162 LEU D N   1 
ATOM   7809  C  CA  . LEU D  1 162 ? 0.760   3.397   -54.597 1.00 14.52 ? 162 LEU D CA  1 
ATOM   7810  C  C   . LEU D  1 162 ? 1.124   4.118   -55.884 1.00 15.14 ? 162 LEU D C   1 
ATOM   7811  O  O   . LEU D  1 162 ? 1.789   5.174   -55.833 1.00 15.79 ? 162 LEU D O   1 
ATOM   7812  C  CB  . LEU D  1 162 ? 1.835   2.344   -54.282 1.00 14.44 ? 162 LEU D CB  1 
ATOM   7813  C  CG  . LEU D  1 162 ? 1.857   1.665   -52.911 1.00 15.52 ? 162 LEU D CG  1 
ATOM   7814  C  CD1 . LEU D  1 162 ? 2.843   0.476   -52.917 1.00 17.36 ? 162 LEU D CD1 1 
ATOM   7815  C  CD2 . LEU D  1 162 ? 2.212   2.702   -51.808 1.00 19.09 ? 162 LEU D CD2 1 
ATOM   7816  N  N   . GLN D  1 163 ? 0.668   3.586   -56.999 1.00 18.74 ? 163 GLN D N   1 
ATOM   7817  C  CA  . GLN D  1 163 ? 0.984   4.232   -58.265 1.00 19.51 ? 163 GLN D CA  1 
ATOM   7818  C  C   . GLN D  1 163 ? 0.235   5.507   -58.488 1.00 19.14 ? 163 GLN D C   1 
ATOM   7819  O  O   . GLN D  1 163 ? 0.478   6.095   -59.516 1.00 27.33 ? 163 GLN D O   1 
ATOM   7820  C  CB  . GLN D  1 163 ? 0.747   3.290   -59.469 1.00 23.29 ? 163 GLN D CB  1 
ATOM   7821  C  CG  . GLN D  1 163 ? 1.683   2.039   -59.533 1.00 24.98 ? 163 GLN D CG  1 
ATOM   7822  C  CD  . GLN D  1 163 ? 3.226   2.304   -59.505 1.00 26.77 ? 163 GLN D CD  1 
ATOM   7823  O  OE1 . GLN D  1 163 ? 3.738   3.263   -60.112 1.00 34.37 ? 163 GLN D OE1 1 
ATOM   7824  N  NE2 . GLN D  1 163 ? 3.951   1.406   -58.887 1.00 26.75 ? 163 GLN D NE2 1 
ATOM   7825  N  N   . HIS D  1 164 ? -0.694  5.914   -57.620 1.00 16.30 ? 164 HIS D N   1 
ATOM   7826  C  CA  . HIS D  1 164 ? -1.300  7.234   -57.622 1.00 16.05 ? 164 HIS D CA  1 
ATOM   7827  C  C   . HIS D  1 164 ? -0.733  8.261   -56.671 1.00 16.88 ? 164 HIS D C   1 
ATOM   7828  O  O   . HIS D  1 164 ? -1.218  9.385   -56.563 1.00 17.81 ? 164 HIS D O   1 
ATOM   7829  C  CB  . HIS D  1 164 ? -2.830  7.042   -57.448 1.00 17.77 ? 164 HIS D CB  1 
ATOM   7830  C  CG  . HIS D  1 164 ? -3.432  6.149   -58.504 1.00 22.73 ? 164 HIS D CG  1 
ATOM   7831  N  ND1 . HIS D  1 164 ? -3.840  6.616   -59.737 1.00 29.68 ? 164 HIS D ND1 1 
ATOM   7832  C  CD2 . HIS D  1 164 ? -3.625  4.813   -58.531 1.00 28.51 ? 164 HIS D CD2 1 
ATOM   7833  C  CE1 . HIS D  1 164 ? -4.288  5.604   -60.465 1.00 31.06 ? 164 HIS D CE1 1 
ATOM   7834  N  NE2 . HIS D  1 164 ? -4.148  4.496   -59.766 1.00 36.81 ? 164 HIS D NE2 1 
ATOM   7835  N  N   . VAL D  1 165 ? 0.247   7.830   -55.851 1.00 12.80 ? 165 VAL D N   1 
ATOM   7836  C  CA  . VAL D  1 165 ? 0.889   8.722   -54.900 1.00 12.78 ? 165 VAL D CA  1 
ATOM   7837  C  C   . VAL D  1 165 ? 2.429   8.632   -55.065 1.00 12.07 ? 165 VAL D C   1 
ATOM   7838  O  O   . VAL D  1 165 ? 3.206   8.750   -54.055 1.00 11.84 ? 165 VAL D O   1 
ATOM   7839  C  CB  . VAL D  1 165 ? 0.448   8.466   -53.412 1.00 13.53 ? 165 VAL D CB  1 
ATOM   7840  C  CG1 . VAL D  1 165 ? -1.064  8.768   -53.221 1.00 14.40 ? 165 VAL D CG1 1 
ATOM   7841  C  CG2 . VAL D  1 165 ? 0.679   7.019   -52.950 1.00 13.07 ? 165 VAL D CG2 1 
ATOM   7842  N  N   . LYS D  1 166 ? 2.877   8.490   -56.317 1.00 12.14 ? 166 LYS D N   1 
ATOM   7843  C  CA  . LYS D  1 166 ? 4.271   8.276   -56.588 1.00 12.49 ? 166 LYS D CA  1 
ATOM   7844  C  C   . LYS D  1 166 ? 5.158   9.416   -56.122 1.00 11.66 ? 166 LYS D C   1 
ATOM   7845  O  O   . LYS D  1 166 ? 6.276   9.175   -55.708 1.00 12.21 ? 166 LYS D O   1 
ATOM   7846  C  CB  . LYS D  1 166 ? 4.434   8.143   -58.103 1.00 14.48 ? 166 LYS D CB  1 
ATOM   7847  C  CG  . LYS D  1 166 ? 5.840   7.858   -58.589 1.00 19.83 ? 166 LYS D CG  1 
ATOM   7848  C  CD  . LYS D  1 166 ? 5.842   7.351   -60.060 1.00 25.21 ? 166 LYS D CD  1 
ATOM   7849  C  CE  . LYS D  1 166 ? 5.242   5.945   -60.244 1.00 25.41 ? 166 LYS D CE  1 
ATOM   7850  N  NZ  . LYS D  1 166 ? 6.007   4.715   -59.726 1.00 23.14 ? 166 LYS D NZ  1 
ATOM   7851  N  N   . TYR D  1 167 ? 4.705   10.669  -56.165 1.00 12.66 ? 167 TYR D N   1 
ATOM   7852  C  CA  . TYR D  1 167 ? 5.541   11.837  -55.867 1.00 12.33 ? 167 TYR D CA  1 
ATOM   7853  C  C   . TYR D  1 167 ? 5.043   12.641  -54.672 1.00 10.76 ? 167 TYR D C   1 
ATOM   7854  O  O   . TYR D  1 167 ? 3.860   12.588  -54.341 1.00 11.05 ? 167 TYR D O   1 
ATOM   7855  C  CB  . TYR D  1 167 ? 5.587   12.718  -57.138 1.00 14.00 ? 167 TYR D CB  1 
ATOM   7856  C  CG  . TYR D  1 167 ? 6.312   12.014  -58.249 1.00 15.33 ? 167 TYR D CG  1 
ATOM   7857  C  CD1 . TYR D  1 167 ? 7.714   11.968  -58.218 1.00 17.36 ? 167 TYR D CD1 1 
ATOM   7858  C  CD2 . TYR D  1 167 ? 5.606   11.525  -59.281 1.00 17.71 ? 167 TYR D CD2 1 
ATOM   7859  C  CE1 . TYR D  1 167 ? 8.389   11.352  -59.234 1.00 18.18 ? 167 TYR D CE1 1 
ATOM   7860  C  CE2 . TYR D  1 167 ? 6.254   10.931  -60.379 1.00 20.43 ? 167 TYR D CE2 1 
ATOM   7861  C  CZ  . TYR D  1 167 ? 7.669   10.810  -60.276 1.00 20.78 ? 167 TYR D CZ  1 
ATOM   7862  O  OH  . TYR D  1 167 ? 8.382   10.216  -61.314 1.00 25.46 ? 167 TYR D OH  1 
ATOM   7863  N  N   . LYS D  1 168 ? 5.988   13.357  -54.051 1.00 12.04 ? 168 LYS D N   1 
ATOM   7864  C  CA  . LYS D  1 168 ? 5.648   14.147  -52.878 1.00 12.69 ? 168 LYS D CA  1 
ATOM   7865  C  C   . LYS D  1 168 ? 4.516   15.047  -53.191 1.00 14.21 ? 168 LYS D C   1 
ATOM   7866  O  O   . LYS D  1 168 ? 4.418   15.666  -54.269 1.00 15.45 ? 168 LYS D O   1 
ATOM   7867  C  CB  . LYS D  1 168 ? 6.858   15.009  -52.470 1.00 13.03 ? 168 LYS D CB  1 
ATOM   7868  C  CG  . LYS D  1 168 ? 6.511   15.804  -51.230 1.00 13.62 ? 168 LYS D CG  1 
ATOM   7869  C  CD  . LYS D  1 168 ? 7.791   16.433  -50.758 1.00 15.04 ? 168 LYS D CD  1 
ATOM   7870  C  CE  . LYS D  1 168 ? 7.485   17.378  -49.661 1.00 19.38 ? 168 LYS D CE  1 
ATOM   7871  N  NZ  . LYS D  1 168 ? 8.708   17.956  -48.998 1.00 25.67 ? 168 LYS D NZ  1 
ATOM   7872  N  N   . GLY D  1 169 ? 3.560   15.056  -52.269 1.00 13.02 ? 169 GLY D N   1 
ATOM   7873  C  CA  . GLY D  1 169 ? 2.374   15.899  -52.327 1.00 14.80 ? 169 GLY D CA  1 
ATOM   7874  C  C   . GLY D  1 169 ? 1.174   15.299  -53.032 1.00 16.37 ? 169 GLY D C   1 
ATOM   7875  O  O   . GLY D  1 169 ? 0.041   15.861  -52.949 1.00 18.87 ? 169 GLY D O   1 
ATOM   7876  N  N   . GLN D  1 170 ? 1.330   14.184  -53.757 1.00 14.00 ? 170 GLN D N   1 
ATOM   7877  C  CA  . GLN D  1 170 ? 0.277   13.487  -54.443 1.00 12.54 ? 170 GLN D CA  1 
ATOM   7878  C  C   . GLN D  1 170 ? -0.646  12.758  -53.430 1.00 14.96 ? 170 GLN D C   1 
ATOM   7879  O  O   . GLN D  1 170 ? -0.172  12.314  -52.353 1.00 13.72 ? 170 GLN D O   1 
ATOM   7880  C  CB  . GLN D  1 170 ? 0.820   12.579  -55.506 1.00 12.90 ? 170 GLN D CB  1 
ATOM   7881  C  CG  . GLN D  1 170 ? 1.540   13.393  -56.634 1.00 14.47 ? 170 GLN D CG  1 
ATOM   7882  C  CD  . GLN D  1 170 ? 1.867   12.516  -57.799 1.00 17.58 ? 170 GLN D CD  1 
ATOM   7883  O  OE1 . GLN D  1 170 ? 2.193   11.348  -57.654 1.00 16.95 ? 170 GLN D OE1 1 
ATOM   7884  N  NE2 . GLN D  1 170 ? 1.844   13.095  -59.008 1.00 19.71 ? 170 GLN D NE2 1 
ATOM   7885  N  N   . GLU D  1 171 ? -1.923  12.682  -53.768 1.00 17.41 ? 171 GLU D N   1 
ATOM   7886  C  CA  . GLU D  1 171 ? -2.951  12.185  -52.833 1.00 15.51 ? 171 GLU D CA  1 
ATOM   7887  C  C   . GLU D  1 171 ? -3.876  11.241  -53.617 1.00 15.55 ? 171 GLU D C   1 
ATOM   7888  O  O   . GLU D  1 171 ? -4.062  11.333  -54.870 1.00 16.58 ? 171 GLU D O   1 
ATOM   7889  C  CB  . GLU D  1 171 ? -3.779  13.316  -52.270 1.00 18.97 ? 171 GLU D CB  1 
ATOM   7890  C  CG  . GLU D  1 171 ? -3.110  14.303  -51.371 1.00 21.45 ? 171 GLU D CG  1 
ATOM   7891  C  CD  . GLU D  1 171 ? -4.052  15.441  -51.062 1.00 27.71 ? 171 GLU D CD  1 
ATOM   7892  O  OE1 . GLU D  1 171 ? -5.070  15.585  -51.791 1.00 34.31 ? 171 GLU D OE1 1 
ATOM   7893  O  OE2 . GLU D  1 171 ? -3.786  16.113  -50.082 1.00 29.45 ? 171 GLU D OE2 1 
ATOM   7894  N  N   . ALA D  1 172 ? -4.481  10.324  -52.941 1.00 14.39 ? 172 ALA D N   1 
ATOM   7895  C  CA  . ALA D  1 172 ? -5.431  9.387   -53.528 1.00 13.85 ? 172 ALA D CA  1 
ATOM   7896  C  C   . ALA D  1 172 ? -6.386  9.014   -52.421 1.00 14.26 ? 172 ALA D C   1 
ATOM   7897  O  O   . ALA D  1 172 ? -6.080  9.154   -51.219 1.00 17.44 ? 172 ALA D O   1 
ATOM   7898  C  CB  . ALA D  1 172 ? -4.722  8.172   -54.069 1.00 15.82 ? 172 ALA D CB  1 
ATOM   7899  N  N   . PHE D  1 173 ? -7.530  8.529   -52.791 1.00 13.52 ? 173 PHE D N   1 
ATOM   7900  C  CA  . PHE D  1 173 ? -8.501  8.006   -51.813 1.00 12.61 ? 173 PHE D CA  1 
ATOM   7901  C  C   . PHE D  1 173 ? -8.581  6.555   -51.758 1.00 13.75 ? 173 PHE D C   1 
ATOM   7902  O  O   . PHE D  1 173 ? -8.554  5.879   -52.796 1.00 16.50 ? 173 PHE D O   1 
ATOM   7903  C  CB  . PHE D  1 173 ? -9.941  8.517   -52.141 1.00 15.59 ? 173 PHE D CB  1 
ATOM   7904  C  CG  . PHE D  1 173 ? -10.180 9.948   -51.746 1.00 17.44 ? 173 PHE D CG  1 
ATOM   7905  C  CD1 . PHE D  1 173 ? -10.156 10.318  -50.375 1.00 20.54 ? 173 PHE D CD1 1 
ATOM   7906  C  CD2 . PHE D  1 173 ? -10.510 10.906  -52.713 1.00 22.22 ? 173 PHE D CD2 1 
ATOM   7907  C  CE1 . PHE D  1 173 ? -10.382 11.632  -49.954 1.00 24.16 ? 173 PHE D CE1 1 
ATOM   7908  C  CE2 . PHE D  1 173 ? -10.759 12.256  -52.278 1.00 22.99 ? 173 PHE D CE2 1 
ATOM   7909  C  CZ  . PHE D  1 173 ? -10.686 12.596  -50.921 1.00 23.02 ? 173 PHE D CZ  1 
ATOM   7910  N  N   . VAL D  1 174 ? -8.622  6.078   -50.540 1.00 11.68 ? 174 VAL D N   1 
ATOM   7911  C  CA  . VAL D  1 174 ? -8.650  4.634   -50.227 1.00 12.02 ? 174 VAL D CA  1 
ATOM   7912  C  C   . VAL D  1 174 ? -10.038 4.389   -49.610 1.00 11.74 ? 174 VAL D C   1 
ATOM   7913  O  O   . VAL D  1 174 ? -10.368 4.989   -48.567 1.00 11.73 ? 174 VAL D O   1 
ATOM   7914  C  CB  . VAL D  1 174 ? -7.563  4.241   -49.239 1.00 11.32 ? 174 VAL D CB  1 
ATOM   7915  C  CG1 . VAL D  1 174 ? -7.646  2.728   -48.899 1.00 12.13 ? 174 VAL D CG1 1 
ATOM   7916  C  CG2 . VAL D  1 174 ? -6.209  4.545   -49.952 1.00 12.98 ? 174 VAL D CG2 1 
ATOM   7917  N  N   . PRO D  1 175 ? -10.857 3.455   -50.146 1.00 11.33 ? 175 PRO D N   1 
ATOM   7918  C  CA  . PRO D  1 175 ? -12.089 3.103   -49.445 1.00 10.88 ? 175 PRO D CA  1 
ATOM   7919  C  C   . PRO D  1 175 ? -11.795 2.494   -48.108 1.00 11.81 ? 175 PRO D C   1 
ATOM   7920  O  O   . PRO D  1 175 ? -10.784 1.823   -47.834 1.00 11.68 ? 175 PRO D O   1 
ATOM   7921  C  CB  . PRO D  1 175 ? -12.695 2.005   -50.352 1.00 12.66 ? 175 PRO D CB  1 
ATOM   7922  C  CG  . PRO D  1 175 ? -12.136 2.227   -51.757 1.00 14.46 ? 175 PRO D CG  1 
ATOM   7923  C  CD  . PRO D  1 175 ? -10.717 2.700   -51.405 1.00 13.03 ? 175 PRO D CD  1 
ATOM   7924  N  N   . GLY D  1 176 ? -12.703 2.739   -47.149 1.00 11.82 ? 176 GLY D N   1 
ATOM   7925  C  CA  . GLY D  1 176 ? -12.541 2.186   -45.789 1.00 11.54 ? 176 GLY D CA  1 
ATOM   7926  C  C   . GLY D  1 176 ? -12.464 0.669   -45.808 1.00 10.93 ? 176 GLY D C   1 
ATOM   7927  O  O   . GLY D  1 176 ? -13.112 -0.006  -46.645 1.00 13.59 ? 176 GLY D O   1 
ATOM   7928  N  N   . PHE D  1 177 ? -11.751 0.174   -44.837 1.00 10.82 ? 177 PHE D N   1 
ATOM   7929  C  CA  . PHE D  1 177 ? -11.678 -1.276  -44.588 1.00 11.43 ? 177 PHE D CA  1 
ATOM   7930  C  C   . PHE D  1 177 ? -11.367 -1.411  -43.118 1.00 12.99 ? 177 PHE D C   1 
ATOM   7931  O  O   . PHE D  1 177 ? -11.157 -0.431  -42.412 1.00 12.99 ? 177 PHE D O   1 
ATOM   7932  C  CB  . PHE D  1 177 ? -10.648 -2.011  -45.441 1.00 11.74 ? 177 PHE D CB  1 
ATOM   7933  C  CG  . PHE D  1 177 ? -9.197  -1.587  -45.229 1.00 12.47 ? 177 PHE D CG  1 
ATOM   7934  C  CD1 . PHE D  1 177 ? -8.665  -0.428  -45.840 1.00 12.39 ? 177 PHE D CD1 1 
ATOM   7935  C  CD2 . PHE D  1 177 ? -8.334  -2.440  -44.442 1.00 13.46 ? 177 PHE D CD2 1 
ATOM   7936  C  CE1 . PHE D  1 177 ? -7.317  -0.087  -45.587 1.00 13.30 ? 177 PHE D CE1 1 
ATOM   7937  C  CE2 . PHE D  1 177 ? -6.994  -2.106  -44.260 1.00 13.26 ? 177 PHE D CE2 1 
ATOM   7938  C  CZ  . PHE D  1 177 ? -6.507  -0.938  -44.806 1.00 13.60 ? 177 PHE D CZ  1 
ATOM   7939  N  N   . ASN D  1 178 ? -11.382 -2.624  -42.601 1.00 12.63 ? 178 ASN D N   1 
ATOM   7940  C  CA  . ASN D  1 178 ? -11.206 -2.833  -41.188 1.00 12.30 ? 178 ASN D CA  1 
ATOM   7941  C  C   . ASN D  1 178 ? -9.684  -2.803  -40.937 1.00 11.62 ? 178 ASN D C   1 
ATOM   7942  O  O   . ASN D  1 178 ? -8.971  -3.793  -41.266 1.00 11.76 ? 178 ASN D O   1 
ATOM   7943  C  CB  . ASN D  1 178 ? -11.760 -4.243  -40.822 1.00 13.30 ? 178 ASN D CB  1 
ATOM   7944  C  CG  . ASN D  1 178 ? -11.639 -4.484  -39.395 1.00 13.79 ? 178 ASN D CG  1 
ATOM   7945  O  OD1 . ASN D  1 178 ? -11.193 -3.673  -38.577 1.00 12.95 ? 178 ASN D OD1 1 
ATOM   7946  N  ND2 . ASN D  1 178 ? -12.007 -5.733  -39.030 1.00 19.08 ? 178 ASN D ND2 1 
ATOM   7947  N  N   . ILE D  1 179 ? -9.212  -1.763  -40.274 1.00 11.11 ? 179 ILE D N   1 
ATOM   7948  C  CA  . ILE D  1 179 ? -7.793  -1.615  -39.981 1.00 10.00 ? 179 ILE D CA  1 
ATOM   7949  C  C   . ILE D  1 179 ? -7.285  -2.629  -39.004 1.00 11.87 ? 179 ILE D C   1 
ATOM   7950  O  O   . ILE D  1 179 ? -6.085  -2.902  -38.981 1.00 11.57 ? 179 ILE D O   1 
ATOM   7951  C  CB  . ILE D  1 179 ? -7.600  -0.162  -39.438 1.00 10.17 ? 179 ILE D CB  1 
ATOM   7952  C  CG1 . ILE D  1 179 ? -8.129  0.942   -40.411 1.00 11.00 ? 179 ILE D CG1 1 
ATOM   7953  C  CG2 . ILE D  1 179 ? -6.122  0.090   -39.032 1.00 9.87  ? 179 ILE D CG2 1 
ATOM   7954  C  CD1 . ILE D  1 179 ? -7.491  0.885   -41.789 1.00 13.64 ? 179 ILE D CD1 1 
ATOM   7955  N  N   . GLU D  1 180 ? -8.174  -3.291  -38.251 1.00 11.39 ? 180 GLU D N   1 
ATOM   7956  C  CA  . GLU D  1 180 ? -7.692  -4.365  -37.420 1.00 11.18 ? 180 GLU D CA  1 
ATOM   7957  C  C   . GLU D  1 180 ? -7.151  -5.520  -38.259 1.00 9.88  ? 180 GLU D C   1 
ATOM   7958  O  O   . GLU D  1 180 ? -6.358  -6.301  -37.694 1.00 12.30 ? 180 GLU D O   1 
ATOM   7959  C  CB  . GLU D  1 180 ? -8.816  -4.889  -36.495 1.00 15.34 ? 180 GLU D CB  1 
ATOM   7960  C  CG  . GLU D  1 180 ? -8.299  -5.561  -35.233 1.00 18.06 ? 180 GLU D CG  1 
ATOM   7961  C  CD  . GLU D  1 180 ? -9.376  -5.724  -34.129 1.00 21.88 ? 180 GLU D CD  1 
ATOM   7962  O  OE1 . GLU D  1 180 ? -10.500 -5.233  -34.254 1.00 22.14 ? 180 GLU D OE1 1 
ATOM   7963  O  OE2 . GLU D  1 180 ? -9.021  -6.391  -33.164 1.00 26.54 ? 180 GLU D OE2 1 
ATOM   7964  N  N   . GLU D  1 181 ? -7.533  -5.632  -39.517 1.00 10.88 ? 181 GLU D N   1 
ATOM   7965  C  CA  . GLU D  1 181 ? -6.950  -6.685  -40.372 1.00 10.70 ? 181 GLU D CA  1 
ATOM   7966  C  C   . GLU D  1 181 ? -5.456  -6.434  -40.620 1.00 11.38 ? 181 GLU D C   1 
ATOM   7967  O  O   . GLU D  1 181 ? -4.781  -7.405  -41.065 1.00 12.12 ? 181 GLU D O   1 
ATOM   7968  C  CB  . GLU D  1 181 ? -7.623  -6.697  -41.703 1.00 12.46 ? 181 GLU D CB  1 
ATOM   7969  C  CG  . GLU D  1 181 ? -9.081  -7.109  -41.698 1.00 14.07 ? 181 GLU D CG  1 
ATOM   7970  C  CD  . GLU D  1 181 ? -9.757  -6.911  -43.059 1.00 18.94 ? 181 GLU D CD  1 
ATOM   7971  O  OE1 . GLU D  1 181 ? -9.091  -6.679  -44.130 1.00 21.73 ? 181 GLU D OE1 1 
ATOM   7972  O  OE2 . GLU D  1 181 ? -11.036 -6.997  -43.125 1.00 20.81 ? 181 GLU D OE2 1 
ATOM   7973  N  N   . LEU D  1 182 ? -4.919  -5.256  -40.298 1.00 10.51 ? 182 LEU D N   1 
ATOM   7974  C  CA  . LEU D  1 182 ? -3.466  -5.017  -40.411 1.00 10.08 ? 182 LEU D CA  1 
ATOM   7975  C  C   . LEU D  1 182 ? -2.698  -5.508  -39.206 1.00 10.02 ? 182 LEU D C   1 
ATOM   7976  O  O   . LEU D  1 182 ? -1.469  -5.481  -39.208 1.00 9.60  ? 182 LEU D O   1 
ATOM   7977  C  CB  . LEU D  1 182 ? -3.241  -3.498  -40.618 1.00 9.95  ? 182 LEU D CB  1 
ATOM   7978  C  CG  . LEU D  1 182 ? -3.963  -2.886  -41.811 1.00 9.29  ? 182 LEU D CG  1 
ATOM   7979  C  CD1 . LEU D  1 182 ? -3.544  -1.416  -41.884 1.00 10.13 ? 182 LEU D CD1 1 
ATOM   7980  C  CD2 . LEU D  1 182 ? -3.647  -3.604  -43.118 1.00 10.95 ? 182 LEU D CD2 1 
ATOM   7981  N  N   . LEU D  1 183 ? -3.383  -5.830  -38.081 1.00 11.21 ? 183 LEU D N   1 
ATOM   7982  C  CA  . LEU D  1 183 ? -2.735  -6.252  -36.877 1.00 9.94  ? 183 LEU D CA  1 
ATOM   7983  C  C   . LEU D  1 183 ? -2.470  -7.739  -36.872 1.00 9.13  ? 183 LEU D C   1 
ATOM   7984  O  O   . LEU D  1 183 ? -3.213  -8.508  -37.566 1.00 11.66 ? 183 LEU D O   1 
ATOM   7985  C  CB  . LEU D  1 183 ? -3.675  -5.889  -35.704 1.00 11.24 ? 183 LEU D CB  1 
ATOM   7986  C  CG  . LEU D  1 183 ? -4.047  -4.399  -35.594 1.00 12.10 ? 183 LEU D CG  1 
ATOM   7987  C  CD1 . LEU D  1 183 ? -4.767  -4.146  -34.243 1.00 14.64 ? 183 LEU D CD1 1 
ATOM   7988  C  CD2 . LEU D  1 183 ? -2.826  -3.490  -35.560 1.00 14.22 ? 183 LEU D CD2 1 
ATOM   7989  N  N   . PRO D  1 184 ? -1.460  -8.135  -36.108 1.00 9.43  ? 184 PRO D N   1 
ATOM   7990  C  CA  . PRO D  1 184 ? -1.107  -9.570  -36.063 1.00 11.32 ? 184 PRO D CA  1 
ATOM   7991  C  C   . PRO D  1 184 ? -1.926  -10.362 -35.108 1.00 13.76 ? 184 PRO D C   1 
ATOM   7992  O  O   . PRO D  1 184 ? -2.872  -9.872  -34.460 1.00 14.21 ? 184 PRO D O   1 
ATOM   7993  C  CB  . PRO D  1 184 ? 0.328   -9.523  -35.523 1.00 11.39 ? 184 PRO D CB  1 
ATOM   7994  C  CG  . PRO D  1 184 ? 0.282   -8.320  -34.600 1.00 10.59 ? 184 PRO D CG  1 
ATOM   7995  C  CD  . PRO D  1 184 ? -0.562  -7.323  -35.277 1.00 9.73  ? 184 PRO D CD  1 
ATOM   7996  N  N   A GLU D  1 185 ? -1.624  -11.666 -35.109 0.50 13.47 ? 185 GLU D N   1 
ATOM   7997  N  N   B GLU D  1 185 ? -1.626  -11.662 -35.085 0.50 13.35 ? 185 GLU D N   1 
ATOM   7998  C  CA  A GLU D  1 185 ? -2.182  -12.579 -34.152 0.50 14.90 ? 185 GLU D CA  1 
ATOM   7999  C  CA  B GLU D  1 185 ? -2.248  -12.514 -34.124 0.50 14.62 ? 185 GLU D CA  1 
ATOM   8000  C  C   A GLU D  1 185 ? -1.816  -12.187 -32.722 0.50 13.37 ? 185 GLU D C   1 
ATOM   8001  C  C   B GLU D  1 185 ? -1.834  -12.159 -32.717 0.50 13.31 ? 185 GLU D C   1 
ATOM   8002  O  O   A GLU D  1 185 ? -0.681  -11.664 -32.451 0.50 13.40 ? 185 GLU D O   1 
ATOM   8003  O  O   B GLU D  1 185 ? -0.696  -11.649 -32.457 0.50 13.50 ? 185 GLU D O   1 
ATOM   8004  C  CB  A GLU D  1 185 ? -1.653  -13.988 -34.450 0.50 16.64 ? 185 GLU D CB  1 
ATOM   8005  C  CB  B GLU D  1 185 ? -1.859  -13.953 -34.393 0.50 16.43 ? 185 GLU D CB  1 
ATOM   8006  C  CG  A GLU D  1 185 ? -2.185  -14.564 -35.752 0.50 18.06 ? 185 GLU D CG  1 
ATOM   8007  C  CG  B GLU D  1 185 ? -2.286  -14.377 -35.765 0.50 17.86 ? 185 GLU D CG  1 
ATOM   8008  C  CD  A GLU D  1 185 ? -1.638  -15.976 -36.074 0.50 22.28 ? 185 GLU D CD  1 
ATOM   8009  C  CD  B GLU D  1 185 ? -3.763  -14.639 -35.839 0.50 24.01 ? 185 GLU D CD  1 
ATOM   8010  O  OE1 A GLU D  1 185 ? -1.008  -16.598 -35.216 0.50 26.95 ? 185 GLU D OE1 1 
ATOM   8011  O  OE1 B GLU D  1 185 ? -4.129  -15.804 -36.089 0.50 32.12 ? 185 GLU D OE1 1 
ATOM   8012  O  OE2 A GLU D  1 185 ? -1.830  -16.452 -37.216 0.50 27.06 ? 185 GLU D OE2 1 
ATOM   8013  O  OE2 B GLU D  1 185 ? -4.565  -13.692 -35.678 0.50 24.61 ? 185 GLU D OE2 1 
ATOM   8014  N  N   . ARG D  1 186 ? -2.749  -12.447 -31.789 1.00 13.78 ? 186 ARG D N   1 
ATOM   8015  C  CA  . ARG D  1 186 ? -2.441  -12.383 -30.336 1.00 13.91 ? 186 ARG D CA  1 
ATOM   8016  C  C   . ARG D  1 186 ? -1.946  -10.984 -29.949 1.00 12.51 ? 186 ARG D C   1 
ATOM   8017  O  O   . ARG D  1 186 ? -0.869  -10.786 -29.346 1.00 13.22 ? 186 ARG D O   1 
ATOM   8018  C  CB  . ARG D  1 186 ? -1.503  -13.462 -29.818 1.00 16.15 ? 186 ARG D CB  1 
ATOM   8019  C  CG  . ARG D  1 186 ? -2.164  -14.845 -30.059 1.00 19.58 ? 186 ARG D CG  1 
ATOM   8020  C  CD  . ARG D  1 186 ? -1.247  -16.007 -29.577 1.00 22.04 ? 186 ARG D CD  1 
ATOM   8021  N  NE  . ARG D  1 186 ? -0.140  -16.219 -30.491 1.00 25.24 ? 186 ARG D NE  1 
ATOM   8022  C  CZ  . ARG D  1 186 ? -0.290  -16.786 -31.699 1.00 30.23 ? 186 ARG D CZ  1 
ATOM   8023  N  NH1 . ARG D  1 186 ? -1.526  -17.219 -32.106 1.00 27.87 ? 186 ARG D NH1 1 
ATOM   8024  N  NH2 . ARG D  1 186 ? 0.768   -16.885 -32.507 1.00 35.22 ? 186 ARG D NH2 1 
ATOM   8025  N  N   . THR D  1 187 ? -2.783  -10.014 -30.328 1.00 11.36 ? 187 THR D N   1 
ATOM   8026  C  CA  . THR D  1 187 ? -2.423  -8.647  -29.967 1.00 11.12 ? 187 THR D CA  1 
ATOM   8027  C  C   . THR D  1 187 ? -2.281  -8.355  -28.462 1.00 12.62 ? 187 THR D C   1 
ATOM   8028  O  O   . THR D  1 187 ? -1.708  -7.309  -28.085 1.00 12.68 ? 187 THR D O   1 
ATOM   8029  C  CB  . THR D  1 187 ? -3.459  -7.629  -30.549 1.00 10.75 ? 187 THR D CB  1 
ATOM   8030  O  OG1 . THR D  1 187 ? -4.803  -8.036  -30.187 1.00 13.46 ? 187 THR D OG1 1 
ATOM   8031  C  CG2 . THR D  1 187 ? -3.443  -7.647  -32.088 1.00 12.36 ? 187 THR D CG2 1 
ATOM   8032  N  N   . ALA D  1 188 ? -2.766  -9.271  -27.594 1.00 13.00 ? 188 ALA D N   1 
ATOM   8033  C  CA  . ALA D  1 188 ? -2.551  -9.029  -26.184 1.00 11.88 ? 188 ALA D CA  1 
ATOM   8034  C  C   . ALA D  1 188 ? -1.064  -9.198  -25.809 1.00 10.83 ? 188 ALA D C   1 
ATOM   8035  O  O   . ALA D  1 188 ? -0.710  -8.827  -24.711 1.00 12.03 ? 188 ALA D O   1 
ATOM   8036  C  CB  . ALA D  1 188 ? -3.359  -10.082 -25.369 1.00 13.97 ? 188 ALA D CB  1 
ATOM   8037  N  N   . GLU D  1 189 ? -0.252  -9.776  -26.680 1.00 10.96 ? 189 GLU D N   1 
ATOM   8038  C  CA  . GLU D  1 189 ? 1.168   -9.976  -26.425 1.00 10.70 ? 189 GLU D CA  1 
ATOM   8039  C  C   . GLU D  1 189 ? 1.962   -8.846  -27.192 1.00 8.72  ? 189 GLU D C   1 
ATOM   8040  O  O   . GLU D  1 189 ? 1.937   -8.759  -28.445 1.00 9.42  ? 189 GLU D O   1 
ATOM   8041  C  CB  . GLU D  1 189 ? 1.613   -11.291 -27.051 1.00 12.28 ? 189 GLU D CB  1 
ATOM   8042  C  CG  . GLU D  1 189 ? 0.826   -12.449 -26.331 1.00 14.45 ? 189 GLU D CG  1 
ATOM   8043  C  CD  . GLU D  1 189 ? 1.206   -13.799 -26.818 1.00 18.69 ? 189 GLU D CD  1 
ATOM   8044  O  OE1 . GLU D  1 189 ? 2.308   -14.026 -27.231 1.00 17.60 ? 189 GLU D OE1 1 
ATOM   8045  O  OE2 . GLU D  1 189 ? 0.341   -14.714 -26.625 1.00 23.39 ? 189 GLU D OE2 1 
ATOM   8046  N  N   . TYR D  1 190 ? 2.621   -8.031  -26.369 1.00 9.01  ? 190 TYR D N   1 
ATOM   8047  C  CA  . TYR D  1 190 ? 3.298   -6.820  -26.929 1.00 8.55  ? 190 TYR D CA  1 
ATOM   8048  C  C   . TYR D  1 190 ? 4.340   -6.394  -26.064 1.00 8.91  ? 190 TYR D C   1 
ATOM   8049  O  O   . TYR D  1 190 ? 4.467   -6.752  -24.827 1.00 9.70  ? 190 TYR D O   1 
ATOM   8050  C  CB  . TYR D  1 190 ? 2.284   -5.671  -27.182 1.00 9.68  ? 190 TYR D CB  1 
ATOM   8051  C  CG  . TYR D  1 190 ? 1.458   -5.232  -25.950 1.00 9.49  ? 190 TYR D CG  1 
ATOM   8052  C  CD1 . TYR D  1 190 ? 2.031   -4.381  -25.062 1.00 9.87  ? 190 TYR D CD1 1 
ATOM   8053  C  CD2 . TYR D  1 190 ? 0.150   -5.676  -25.794 1.00 9.61  ? 190 TYR D CD2 1 
ATOM   8054  C  CE1 . TYR D  1 190 ? 1.257   -3.923  -23.964 1.00 10.05 ? 190 TYR D CE1 1 
ATOM   8055  C  CE2 . TYR D  1 190 ? -0.590  -5.281  -24.652 1.00 10.33 ? 190 TYR D CE2 1 
ATOM   8056  C  CZ  . TYR D  1 190 ? -0.027  -4.362  -23.823 1.00 10.59 ? 190 TYR D CZ  1 
ATOM   8057  O  OH  . TYR D  1 190 ? -0.752  -3.956  -22.652 1.00 11.32 ? 190 TYR D OH  1 
ATOM   8058  N  N   . TYR D  1 191 ? 5.235   -5.578  -26.632 1.00 9.25  ? 191 TYR D N   1 
ATOM   8059  C  CA  . TYR D  1 191 ? 6.260   -4.798  -25.978 1.00 8.87  ? 191 TYR D CA  1 
ATOM   8060  C  C   . TYR D  1 191 ? 5.799   -3.336  -25.824 1.00 9.03  ? 191 TYR D C   1 
ATOM   8061  O  O   . TYR D  1 191 ? 5.121   -2.794  -26.716 1.00 9.21  ? 191 TYR D O   1 
ATOM   8062  C  CB  . TYR D  1 191 ? 7.536   -4.742  -26.889 1.00 9.14  ? 191 TYR D CB  1 
ATOM   8063  C  CG  . TYR D  1 191 ? 8.092   -6.061  -27.405 1.00 9.34  ? 191 TYR D CG  1 
ATOM   8064  C  CD1 . TYR D  1 191 ? 9.058   -6.774  -26.681 1.00 10.07 ? 191 TYR D CD1 1 
ATOM   8065  C  CD2 . TYR D  1 191 ? 7.668   -6.547  -28.644 1.00 9.49  ? 191 TYR D CD2 1 
ATOM   8066  C  CE1 . TYR D  1 191 ? 9.597   -7.939  -27.176 1.00 10.25 ? 191 TYR D CE1 1 
ATOM   8067  C  CE2 . TYR D  1 191 ? 8.229   -7.711  -29.147 1.00 9.99  ? 191 TYR D CE2 1 
ATOM   8068  C  CZ  . TYR D  1 191 ? 9.172   -8.369  -28.381 1.00 10.13 ? 191 TYR D CZ  1 
ATOM   8069  O  OH  . TYR D  1 191 ? 9.779   -9.531  -28.923 1.00 13.68 ? 191 TYR D OH  1 
ATOM   8070  N  N   . ARG D  1 192 ? 6.100   -2.747  -24.682 1.00 9.15  ? 192 ARG D N   1 
ATOM   8071  C  CA  . ARG D  1 192 ? 5.734   -1.376  -24.391 1.00 9.14  ? 192 ARG D CA  1 
ATOM   8072  C  C   . ARG D  1 192 ? 6.874   -0.618  -23.805 1.00 8.29  ? 192 ARG D C   1 
ATOM   8073  O  O   . ARG D  1 192 ? 7.617   -1.082  -22.932 1.00 10.48 ? 192 ARG D O   1 
ATOM   8074  C  CB  . ARG D  1 192 ? 4.641   -1.442  -23.325 1.00 10.29 ? 192 ARG D CB  1 
ATOM   8075  C  CG  . ARG D  1 192 ? 4.271   -0.156  -22.587 1.00 14.56 ? 192 ARG D CG  1 
ATOM   8076  C  CD  . ARG D  1 192 ? 3.568   0.843   -23.488 1.00 14.81 ? 192 ARG D CD  1 
ATOM   8077  N  NE  . ARG D  1 192 ? 2.420   0.248   -24.189 1.00 15.14 ? 192 ARG D NE  1 
ATOM   8078  C  CZ  . ARG D  1 192 ? 1.252   -0.100  -23.641 1.00 13.38 ? 192 ARG D CZ  1 
ATOM   8079  N  NH1 . ARG D  1 192 ? 1.030   0.102   -22.351 1.00 17.80 ? 192 ARG D NH1 1 
ATOM   8080  N  NH2 . ARG D  1 192 ? 0.319   -0.649  -24.393 1.00 15.78 ? 192 ARG D NH2 1 
ATOM   8081  N  N   . TYR D  1 193 ? 7.064   0.602   -24.320 1.00 8.57  ? 193 TYR D N   1 
ATOM   8082  C  CA  . TYR D  1 193 ? 8.169   1.426   -23.803 1.00 8.13  ? 193 TYR D CA  1 
ATOM   8083  C  C   . TYR D  1 193 ? 7.920   2.889   -24.148 1.00 8.64  ? 193 TYR D C   1 
ATOM   8084  O  O   . TYR D  1 193 ? 7.073   3.215   -25.011 1.00 9.72  ? 193 TYR D O   1 
ATOM   8085  C  CB  . TYR D  1 193 ? 9.585   1.001   -24.286 1.00 8.87  ? 193 TYR D CB  1 
ATOM   8086  C  CG  . TYR D  1 193 ? 9.898   1.391   -25.717 1.00 7.88  ? 193 TYR D CG  1 
ATOM   8087  C  CD1 . TYR D  1 193 ? 9.454   0.626   -26.795 1.00 9.45  ? 193 TYR D CD1 1 
ATOM   8088  C  CD2 . TYR D  1 193 ? 10.644  2.526   -25.990 1.00 9.21  ? 193 TYR D CD2 1 
ATOM   8089  C  CE1 . TYR D  1 193 ? 9.748   0.990   -28.102 1.00 9.63  ? 193 TYR D CE1 1 
ATOM   8090  C  CE2 . TYR D  1 193 ? 10.941  2.897   -27.285 1.00 8.22  ? 193 TYR D CE2 1 
ATOM   8091  C  CZ  . TYR D  1 193 ? 10.494  2.131   -28.338 1.00 8.91  ? 193 TYR D CZ  1 
ATOM   8092  O  OH  . TYR D  1 193 ? 10.806  2.528   -29.619 1.00 9.42  ? 193 TYR D OH  1 
ATOM   8093  N  N   . ARG D  1 194 ? 8.640   3.726   -23.445 1.00 9.20  ? 194 ARG D N   1 
ATOM   8094  C  CA  . ARG D  1 194 ? 8.528   5.228   -23.666 1.00 9.80  ? 194 ARG D CA  1 
ATOM   8095  C  C   . ARG D  1 194 ? 9.588   5.658   -24.600 1.00 8.72  ? 194 ARG D C   1 
ATOM   8096  O  O   . ARG D  1 194 ? 10.784  5.377   -24.426 1.00 10.02 ? 194 ARG D O   1 
ATOM   8097  C  CB  . ARG D  1 194 ? 8.737   5.946   -22.356 1.00 13.09 ? 194 ARG D CB  1 
ATOM   8098  C  CG  . ARG D  1 194 ? 7.746   5.540   -21.288 1.00 17.71 ? 194 ARG D CG  1 
ATOM   8099  C  CD  . ARG D  1 194 ? 6.572   6.429   -21.489 1.00 25.56 ? 194 ARG D CD  1 
ATOM   8100  N  NE  . ARG D  1 194 ? 5.575   6.092   -20.460 1.00 37.01 ? 194 ARG D NE  1 
ATOM   8101  C  CZ  . ARG D  1 194 ? 4.419   6.728   -20.322 1.00 40.09 ? 194 ARG D CZ  1 
ATOM   8102  N  NH1 . ARG D  1 194 ? 4.135   7.760   -21.131 1.00 36.67 ? 194 ARG D NH1 1 
ATOM   8103  N  NH2 . ARG D  1 194 ? 3.557   6.318   -19.382 1.00 39.68 ? 194 ARG D NH2 1 
ATOM   8104  N  N   . GLY D  1 195 ? 9.148   6.313   -25.679 1.00 8.31  ? 195 GLY D N   1 
ATOM   8105  C  CA  . GLY D  1 195 ? 10.135  6.793   -26.664 1.00 9.38  ? 195 GLY D CA  1 
ATOM   8106  C  C   . GLY D  1 195 ? 9.657   8.009   -27.391 1.00 9.40  ? 195 GLY D C   1 
ATOM   8107  O  O   . GLY D  1 195 ? 9.088   8.927   -26.840 1.00 9.45  ? 195 GLY D O   1 
ATOM   8108  N  N   . SER D  1 196 ? 10.002  8.023   -28.668 1.00 7.89  ? 196 SER D N   1 
ATOM   8109  C  CA  . SER D  1 196 ? 9.900   9.284   -29.409 1.00 8.41  ? 196 SER D CA  1 
ATOM   8110  C  C   . SER D  1 196 ? 9.329   9.030   -30.796 1.00 8.31  ? 196 SER D C   1 
ATOM   8111  O  O   . SER D  1 196 ? 9.191   7.877   -31.279 1.00 8.39  ? 196 SER D O   1 
ATOM   8112  C  CB  . SER D  1 196 ? 11.321  9.924   -29.596 1.00 8.88  ? 196 SER D CB  1 
ATOM   8113  O  OG  . SER D  1 196 ? 12.115  9.185   -30.598 1.00 8.28  ? 196 SER D OG  1 
ATOM   8114  N  N   . LEU D  1 197 ? 9.075   10.097  -31.516 1.00 8.35  ? 197 LEU D N   1 
ATOM   8115  C  CA  . LEU D  1 197 ? 8.887   9.934   -32.943 1.00 8.52  ? 197 LEU D CA  1 
ATOM   8116  C  C   . LEU D  1 197 ? 10.185  9.439   -33.552 1.00 7.62  ? 197 LEU D C   1 
ATOM   8117  O  O   . LEU D  1 197 ? 11.273  9.846   -33.139 1.00 8.40  ? 197 LEU D O   1 
ATOM   8118  C  CB  . LEU D  1 197 ? 8.595   11.333  -33.644 1.00 8.55  ? 197 LEU D CB  1 
ATOM   8119  C  CG  . LEU D  1 197 ? 7.208   11.898  -33.532 1.00 8.86  ? 197 LEU D CG  1 
ATOM   8120  C  CD1 . LEU D  1 197 ? 7.029   12.583  -32.127 1.00 10.44 ? 197 LEU D CD1 1 
ATOM   8121  C  CD2 . LEU D  1 197 ? 7.052   12.955  -34.669 1.00 11.66 ? 197 LEU D CD2 1 
ATOM   8122  N  N   . THR D  1 198 ? 10.109  8.522   -34.530 1.00 7.47  ? 198 THR D N   1 
ATOM   8123  C  CA  . THR D  1 198 ? 11.335  8.102   -35.211 1.00 7.71  ? 198 THR D CA  1 
ATOM   8124  C  C   . THR D  1 198 ? 11.732  8.957   -36.352 1.00 7.30  ? 198 THR D C   1 
ATOM   8125  O  O   . THR D  1 198 ? 12.739  8.645   -37.003 1.00 8.18  ? 198 THR D O   1 
ATOM   8126  C  CB  . THR D  1 198 ? 11.180  6.645   -35.736 1.00 6.88  ? 198 THR D CB  1 
ATOM   8127  O  OG1 . THR D  1 198 ? 10.201  6.682   -36.773 1.00 7.20  ? 198 THR D OG1 1 
ATOM   8128  C  CG2 . THR D  1 198 ? 10.753  5.636   -34.622 1.00 7.86  ? 198 THR D CG2 1 
ATOM   8129  N  N   . THR D  1 199 ? 10.983  10.014  -36.572 1.00 7.30  ? 199 THR D N   1 
ATOM   8130  C  CA  . THR D  1 199 ? 11.332  10.983  -37.623 1.00 7.38  ? 199 THR D CA  1 
ATOM   8131  C  C   . THR D  1 199 ? 11.449  12.351  -36.960 1.00 8.53  ? 199 THR D C   1 
ATOM   8132  O  O   . THR D  1 199 ? 10.835  12.537  -35.922 1.00 8.82  ? 199 THR D O   1 
ATOM   8133  C  CB  . THR D  1 199 ? 10.180  11.136  -38.682 1.00 8.09  ? 199 THR D CB  1 
ATOM   8134  O  OG1 . THR D  1 199 ? 8.993   11.538  -38.055 1.00 9.50  ? 199 THR D OG1 1 
ATOM   8135  C  CG2 . THR D  1 199 ? 9.901   9.754   -39.307 1.00 8.68  ? 199 THR D CG2 1 
ATOM   8136  N  N   . PRO D  1 200 ? 12.154  13.316  -37.579 1.00 7.99  ? 200 PRO D N   1 
ATOM   8137  C  CA  . PRO D  1 200 ? 12.043  14.659  -37.098 1.00 8.58  ? 200 PRO D CA  1 
ATOM   8138  C  C   . PRO D  1 200 ? 10.586  15.055  -36.897 1.00 9.64  ? 200 PRO D C   1 
ATOM   8139  O  O   . PRO D  1 200 ? 9.768   14.701  -37.698 1.00 10.95 ? 200 PRO D O   1 
ATOM   8140  C  CB  . PRO D  1 200 ? 12.723  15.452  -38.254 1.00 8.11  ? 200 PRO D CB  1 
ATOM   8141  C  CG  . PRO D  1 200 ? 13.773  14.493  -38.764 1.00 8.70  ? 200 PRO D CG  1 
ATOM   8142  C  CD  . PRO D  1 200 ? 13.062  13.144  -38.741 1.00 8.28  ? 200 PRO D CD  1 
ATOM   8143  N  N   . PRO D  1 201 ? 10.288  15.841  -35.879 1.00 8.89  ? 201 PRO D N   1 
ATOM   8144  C  CA  . PRO D  1 201 ? 11.272  16.433  -34.928 1.00 9.30  ? 201 PRO D CA  1 
ATOM   8145  C  C   . PRO D  1 201 ? 11.685  15.557  -33.768 1.00 9.49  ? 201 PRO D C   1 
ATOM   8146  O  O   . PRO D  1 201 ? 12.337  16.007  -32.841 1.00 9.76  ? 201 PRO D O   1 
ATOM   8147  C  CB  . PRO D  1 201 ? 10.518  17.664  -34.338 1.00 10.26 ? 201 PRO D CB  1 
ATOM   8148  C  CG  . PRO D  1 201 ? 9.230   17.781  -35.131 1.00 13.33 ? 201 PRO D CG  1 
ATOM   8149  C  CD  . PRO D  1 201 ? 8.945   16.440  -35.687 1.00 9.60  ? 201 PRO D CD  1 
ATOM   8150  N  N   . CYS D  1 202 ? 11.347  14.254  -33.780 1.00 8.51  ? 202 CYS D N   1 
ATOM   8151  C  CA  . CYS D  1 202 ? 11.918  13.287  -32.778 1.00 8.96  ? 202 CYS D CA  1 
ATOM   8152  C  C   . CYS D  1 202 ? 11.460  13.555  -31.313 1.00 9.50  ? 202 CYS D C   1 
ATOM   8153  O  O   . CYS D  1 202 ? 12.113  13.141  -30.411 1.00 9.38  ? 202 CYS D O   1 
ATOM   8154  C  CB  . CYS D  1 202 ? 13.443  13.177  -32.777 1.00 9.31  ? 202 CYS D CB  1 
ATOM   8155  S  SG  . CYS D  1 202 ? 14.166  12.827  -34.433 1.00 9.41  ? 202 CYS D SG  1 
ATOM   8156  N  N   . ASN D  1 203 ? 10.292  14.160  -31.175 1.00 9.52  ? 203 ASN D N   1 
ATOM   8157  C  CA  . ASN D  1 203 ? 9.846   14.577  -29.826 1.00 10.21 ? 203 ASN D CA  1 
ATOM   8158  C  C   . ASN D  1 203 ? 9.754   13.325  -28.993 1.00 10.14 ? 203 ASN D C   1 
ATOM   8159  O  O   . ASN D  1 203 ? 9.179   12.311  -29.471 1.00 9.13  ? 203 ASN D O   1 
ATOM   8160  C  CB  . ASN D  1 203 ? 8.509   15.292  -29.897 1.00 11.15 ? 203 ASN D CB  1 
ATOM   8161  C  CG  . ASN D  1 203 ? 8.561   16.430  -30.915 1.00 13.68 ? 203 ASN D CG  1 
ATOM   8162  O  OD1 . ASN D  1 203 ? 8.448   16.226  -32.099 1.00 17.88 ? 203 ASN D OD1 1 
ATOM   8163  N  ND2 . ASN D  1 203 ? 8.910   17.569  -30.442 1.00 17.03 ? 203 ASN D ND2 1 
ATOM   8164  N  N   . PRO D  1 204 ? 10.166  13.349  -27.745 1.00 9.60  ? 204 PRO D N   1 
ATOM   8165  C  CA  . PRO D  1 204 ? 10.095  12.117  -26.849 1.00 9.61  ? 204 PRO D CA  1 
ATOM   8166  C  C   . PRO D  1 204 ? 8.686   12.028  -26.167 1.00 10.42 ? 204 PRO D C   1 
ATOM   8167  O  O   . PRO D  1 204 ? 8.590   12.139  -24.894 1.00 12.39 ? 204 PRO D O   1 
ATOM   8168  C  CB  . PRO D  1 204 ? 11.258  12.337  -25.800 1.00 10.42 ? 204 PRO D CB  1 
ATOM   8169  C  CG  . PRO D  1 204 ? 11.317  13.845  -25.765 1.00 11.24 ? 204 PRO D CG  1 
ATOM   8170  C  CD  . PRO D  1 204 ? 11.132  14.352  -27.186 1.00 9.37  ? 204 PRO D CD  1 
ATOM   8171  N  N   . THR D  1 205 ? 7.659   11.930  -26.969 1.00 8.97  ? 205 THR D N   1 
ATOM   8172  C  CA  . THR D  1 205 ? 6.307   12.064  -26.562 1.00 8.70  ? 205 THR D CA  1 
ATOM   8173  C  C   . THR D  1 205 ? 5.438   10.857  -26.927 1.00 8.48  ? 205 THR D C   1 
ATOM   8174  O  O   . THR D  1 205 ? 4.210   10.926  -26.923 1.00 9.46  ? 205 THR D O   1 
ATOM   8175  C  CB  . THR D  1 205 ? 5.693   13.335  -27.184 1.00 9.01  ? 205 THR D CB  1 
ATOM   8176  O  OG1 . THR D  1 205 ? 5.865   13.200  -28.621 1.00 10.18 ? 205 THR D OG1 1 
ATOM   8177  C  CG2 . THR D  1 205 ? 6.377   14.625  -26.711 1.00 10.20 ? 205 THR D CG2 1 
ATOM   8178  N  N   . VAL D  1 206 ? 6.110   9.741   -27.250 1.00 8.59  ? 206 VAL D N   1 
ATOM   8179  C  CA  . VAL D  1 206 ? 5.405   8.556   -27.793 1.00 9.60  ? 206 VAL D CA  1 
ATOM   8180  C  C   . VAL D  1 206 ? 5.461   7.363   -26.845 1.00 8.10  ? 206 VAL D C   1 
ATOM   8181  O  O   . VAL D  1 206 ? 6.477   6.951   -26.442 1.00 9.75  ? 206 VAL D O   1 
ATOM   8182  C  CB  . VAL D  1 206 ? 6.003   8.122   -29.179 1.00 8.29  ? 206 VAL D CB  1 
ATOM   8183  C  CG1 . VAL D  1 206 ? 5.190   6.924   -29.695 1.00 8.97  ? 206 VAL D CG1 1 
ATOM   8184  C  CG2 . VAL D  1 206 ? 5.965   9.321   -30.165 1.00 10.37 ? 206 VAL D CG2 1 
ATOM   8185  N  N   . LEU D  1 207 ? 4.275   6.871   -26.539 1.00 8.23  ? 207 LEU D N   1 
ATOM   8186  C  CA  . LEU D  1 207 ? 4.089   5.567   -25.823 1.00 9.63  ? 207 LEU D CA  1 
ATOM   8187  C  C   . LEU D  1 207 ? 4.010   4.514   -26.953 1.00 8.36  ? 207 LEU D C   1 
ATOM   8188  O  O   . LEU D  1 207 ? 3.084   4.511   -27.748 1.00 9.17  ? 207 LEU D O   1 
ATOM   8189  C  CB  . LEU D  1 207 ? 2.801   5.632   -24.997 1.00 12.13 ? 207 LEU D CB  1 
ATOM   8190  C  CG  . LEU D  1 207 ? 2.751   4.374   -24.087 1.00 14.56 ? 207 LEU D CG  1 
ATOM   8191  C  CD1 . LEU D  1 207 ? 4.020   4.235   -23.178 1.00 16.73 ? 207 LEU D CD1 1 
ATOM   8192  C  CD2 . LEU D  1 207 ? 1.438   4.474   -23.349 1.00 20.48 ? 207 LEU D CD2 1 
ATOM   8193  N  N   . TRP D  1 208 ? 5.064   3.715   -27.018 1.00 7.77  ? 208 TRP D N   1 
ATOM   8194  C  CA  . TRP D  1 208 ? 5.161   2.663   -28.031 1.00 8.05  ? 208 TRP D CA  1 
ATOM   8195  C  C   . TRP D  1 208 ? 4.597   1.329   -27.622 1.00 8.36  ? 208 TRP D C   1 
ATOM   8196  O  O   . TRP D  1 208 ? 4.930   0.895   -26.520 1.00 9.94  ? 208 TRP D O   1 
ATOM   8197  C  CB  . TRP D  1 208 ? 6.651   2.448   -28.405 1.00 8.01  ? 208 TRP D CB  1 
ATOM   8198  C  CG  . TRP D  1 208 ? 7.170   3.506   -29.324 1.00 8.30  ? 208 TRP D CG  1 
ATOM   8199  C  CD1 . TRP D  1 208 ? 7.815   4.651   -28.952 1.00 8.81  ? 208 TRP D CD1 1 
ATOM   8200  C  CD2 . TRP D  1 208 ? 7.041   3.530   -30.751 1.00 7.97  ? 208 TRP D CD2 1 
ATOM   8201  N  NE1 . TRP D  1 208 ? 8.042   5.431   -30.083 1.00 8.16  ? 208 TRP D NE1 1 
ATOM   8202  C  CE2 . TRP D  1 208 ? 7.586   4.753   -31.198 1.00 8.49  ? 208 TRP D CE2 1 
ATOM   8203  C  CE3 . TRP D  1 208 ? 6.441   2.675   -31.725 1.00 8.39  ? 208 TRP D CE3 1 
ATOM   8204  C  CZ2 . TRP D  1 208 ? 7.574   5.151   -32.543 1.00 8.30  ? 208 TRP D CZ2 1 
ATOM   8205  C  CZ3 . TRP D  1 208 ? 6.438   3.047   -33.060 1.00 7.95  ? 208 TRP D CZ3 1 
ATOM   8206  C  CH2 . TRP D  1 208 ? 7.033   4.239   -33.476 1.00 9.03  ? 208 TRP D CH2 1 
ATOM   8207  N  N   . THR D  1 209 ? 3.789   0.730   -28.484 1.00 7.20  ? 209 THR D N   1 
ATOM   8208  C  CA  . THR D  1 209 ? 3.341   -0.642  -28.334 1.00 7.52  ? 209 THR D CA  1 
ATOM   8209  C  C   . THR D  1 209 ? 3.763   -1.351  -29.602 1.00 7.76  ? 209 THR D C   1 
ATOM   8210  O  O   . THR D  1 209 ? 3.303   -1.031  -30.694 1.00 8.75  ? 209 THR D O   1 
ATOM   8211  C  CB  . THR D  1 209 ? 1.818   -0.699  -28.202 1.00 8.52  ? 209 THR D CB  1 
ATOM   8212  O  OG1 . THR D  1 209 ? 1.441   0.032   -27.019 1.00 8.67  ? 209 THR D OG1 1 
ATOM   8213  C  CG2 . THR D  1 209 ? 1.324   -2.174  -28.032 1.00 8.73  ? 209 THR D CG2 1 
ATOM   8214  N  N   . VAL D  1 210 ? 4.674   -2.304  -29.475 1.00 8.05  ? 210 VAL D N   1 
ATOM   8215  C  CA  . VAL D  1 210 ? 5.151   -3.139  -30.624 1.00 8.35  ? 210 VAL D CA  1 
ATOM   8216  C  C   . VAL D  1 210 ? 4.597   -4.522  -30.448 1.00 7.92  ? 210 VAL D C   1 
ATOM   8217  O  O   . VAL D  1 210 ? 4.878   -5.126  -29.388 1.00 8.63  ? 210 VAL D O   1 
ATOM   8218  C  CB  . VAL D  1 210 ? 6.673   -3.153  -30.673 1.00 7.46  ? 210 VAL D CB  1 
ATOM   8219  C  CG1 . VAL D  1 210 ? 7.130   -3.961  -31.896 1.00 8.84  ? 210 VAL D CG1 1 
ATOM   8220  C  CG2 . VAL D  1 210 ? 7.308   -1.749  -30.720 1.00 9.48  ? 210 VAL D CG2 1 
ATOM   8221  N  N   . PHE D  1 211 ? 3.714   -4.996  -31.329 1.00 7.82  ? 211 PHE D N   1 
ATOM   8222  C  CA  . PHE D  1 211 ? 3.162   -6.356  -31.112 1.00 8.21  ? 211 PHE D CA  1 
ATOM   8223  C  C   . PHE D  1 211 ? 4.279   -7.389  -31.221 1.00 9.36  ? 211 PHE D C   1 
ATOM   8224  O  O   . PHE D  1 211 ? 5.245   -7.310  -31.999 1.00 9.33  ? 211 PHE D O   1 
ATOM   8225  C  CB  . PHE D  1 211 ? 2.019   -6.604  -32.059 1.00 9.56  ? 211 PHE D CB  1 
ATOM   8226  C  CG  . PHE D  1 211 ? 0.870   -5.650  -31.843 1.00 8.69  ? 211 PHE D CG  1 
ATOM   8227  C  CD1 . PHE D  1 211 ? 0.059   -5.812  -30.696 1.00 9.60  ? 211 PHE D CD1 1 
ATOM   8228  C  CD2 . PHE D  1 211 ? 0.557   -4.632  -32.767 1.00 10.74 ? 211 PHE D CD2 1 
ATOM   8229  C  CE1 . PHE D  1 211 ? -0.936  -4.910  -30.430 1.00 10.62 ? 211 PHE D CE1 1 
ATOM   8230  C  CE2 . PHE D  1 211 ? -0.467  -3.742  -32.440 1.00 11.11 ? 211 PHE D CE2 1 
ATOM   8231  C  CZ  . PHE D  1 211 ? -1.267  -3.915  -31.299 1.00 10.85 ? 211 PHE D CZ  1 
ATOM   8232  N  N   . ARG D  1 212 ? 4.093   -8.458  -30.414 1.00 8.94  ? 212 ARG D N   1 
ATOM   8233  C  CA  . ARG D  1 212 ? 5.119   -9.517  -30.412 1.00 9.09  ? 212 ARG D CA  1 
ATOM   8234  C  C   . ARG D  1 212 ? 5.185   -10.288 -31.732 1.00 9.94  ? 212 ARG D C   1 
ATOM   8235  O  O   . ARG D  1 212 ? 6.288   -10.611 -32.192 1.00 10.91 ? 212 ARG D O   1 
ATOM   8236  C  CB  . ARG D  1 212 ? 4.738   -10.480 -29.245 1.00 10.64 ? 212 ARG D CB  1 
ATOM   8237  C  CG  . ARG D  1 212 ? 5.798   -11.573 -29.088 1.00 10.91 ? 212 ARG D CG  1 
ATOM   8238  C  CD  . ARG D  1 212 ? 5.273   -12.669 -28.158 1.00 13.60 ? 212 ARG D CD  1 
ATOM   8239  N  NE  . ARG D  1 212 ? 6.362   -13.559 -27.833 1.00 14.05 ? 212 ARG D NE  1 
ATOM   8240  C  CZ  . ARG D  1 212 ? 6.232   -14.592 -27.022 1.00 17.81 ? 212 ARG D CZ  1 
ATOM   8241  N  NH1 . ARG D  1 212 ? 5.044   -14.847 -26.493 1.00 19.89 ? 212 ARG D NH1 1 
ATOM   8242  N  NH2 . ARG D  1 212 ? 7.278   -15.354 -26.731 1.00 20.94 ? 212 ARG D NH2 1 
ATOM   8243  N  N   . ASN D  1 213 ? 4.040   -10.471 -32.336 1.00 9.75  ? 213 ASN D N   1 
ATOM   8244  C  CA  . ASN D  1 213 ? 3.993   -11.265 -33.549 1.00 10.69 ? 213 ASN D CA  1 
ATOM   8245  C  C   . ASN D  1 213 ? 4.000   -10.374 -34.799 1.00 10.95 ? 213 ASN D C   1 
ATOM   8246  O  O   . ASN D  1 213 ? 3.266   -9.380  -34.849 1.00 9.53  ? 213 ASN D O   1 
ATOM   8247  C  CB  . ASN D  1 213 ? 2.749   -12.152 -33.554 1.00 12.61 ? 213 ASN D CB  1 
ATOM   8248  C  CG  . ASN D  1 213 ? 2.806   -13.169 -32.422 1.00 16.77 ? 213 ASN D CG  1 
ATOM   8249  O  OD1 . ASN D  1 213 ? 3.820   -13.871 -32.255 1.00 19.35 ? 213 ASN D OD1 1 
ATOM   8250  N  ND2 . ASN D  1 213 ? 1.799   -13.176 -31.619 1.00 18.19 ? 213 ASN D ND2 1 
ATOM   8251  N  N   . PRO D  1 214 ? 4.743   -10.748 -35.839 1.00 9.35  ? 214 PRO D N   1 
ATOM   8252  C  CA  . PRO D  1 214 ? 4.672   -10.076 -37.104 1.00 10.25 ? 214 PRO D CA  1 
ATOM   8253  C  C   . PRO D  1 214 ? 3.512   -10.447 -37.939 1.00 9.54  ? 214 PRO D C   1 
ATOM   8254  O  O   . PRO D  1 214 ? 2.896   -11.496 -37.699 1.00 11.30 ? 214 PRO D O   1 
ATOM   8255  C  CB  . PRO D  1 214 ? 6.024   -10.465 -37.809 1.00 9.94  ? 214 PRO D CB  1 
ATOM   8256  C  CG  . PRO D  1 214 ? 6.169   -11.911 -37.367 1.00 12.30 ? 214 PRO D CG  1 
ATOM   8257  C  CD  . PRO D  1 214 ? 5.746   -11.887 -35.837 1.00 10.82 ? 214 PRO D CD  1 
ATOM   8258  N  N   . VAL D  1 215 ? 3.220   -9.660  -38.946 1.00 9.22  ? 215 VAL D N   1 
ATOM   8259  C  CA  . VAL D  1 215 ? 2.383   -10.082 -40.049 1.00 8.59  ? 215 VAL D CA  1 
ATOM   8260  C  C   . VAL D  1 215 ? 3.243   -10.387 -41.226 1.00 8.27  ? 215 VAL D C   1 
ATOM   8261  O  O   . VAL D  1 215 ? 4.463   -10.075 -41.193 1.00 9.36  ? 215 VAL D O   1 
ATOM   8262  C  CB  . VAL D  1 215 ? 1.344   -9.007  -40.441 1.00 8.02  ? 215 VAL D CB  1 
ATOM   8263  C  CG1 . VAL D  1 215 ? 0.432   -8.703  -39.249 1.00 11.25 ? 215 VAL D CG1 1 
ATOM   8264  C  CG2 . VAL D  1 215 ? 1.962   -7.756  -41.041 1.00 10.03 ? 215 VAL D CG2 1 
ATOM   8265  N  N   . GLN D  1 216 ? 2.692   -10.953 -42.271 1.00 8.07  ? 216 GLN D N   1 
ATOM   8266  C  CA  . GLN D  1 216 ? 3.396   -11.221 -43.520 1.00 8.05  ? 216 GLN D CA  1 
ATOM   8267  C  C   . GLN D  1 216 ? 2.802   -10.450 -44.678 1.00 8.53  ? 216 GLN D C   1 
ATOM   8268  O  O   . GLN D  1 216 ? 1.559   -10.323 -44.765 1.00 9.09  ? 216 GLN D O   1 
ATOM   8269  C  CB  . GLN D  1 216 ? 3.306   -12.715 -43.891 1.00 9.47  ? 216 GLN D CB  1 
ATOM   8270  C  CG  . GLN D  1 216 ? 4.135   -13.625 -42.937 1.00 10.35 ? 216 GLN D CG  1 
ATOM   8271  C  CD  . GLN D  1 216 ? 4.054   -15.089 -43.375 1.00 12.01 ? 216 GLN D CD  1 
ATOM   8272  O  OE1 . GLN D  1 216 ? 3.513   -15.504 -44.378 1.00 12.22 ? 216 GLN D OE1 1 
ATOM   8273  N  NE2 . GLN D  1 216 ? 4.654   -15.909 -42.511 1.00 17.18 ? 216 GLN D NE2 1 
ATOM   8274  N  N   . ILE D  1 217 ? 3.631   -9.946  -45.562 1.00 8.32  ? 217 ILE D N   1 
ATOM   8275  C  CA  . ILE D  1 217 ? 3.225   -9.489  -46.900 1.00 8.03  ? 217 ILE D CA  1 
ATOM   8276  C  C   . ILE D  1 217 ? 4.166   -10.191 -47.896 1.00 8.57  ? 217 ILE D C   1 
ATOM   8277  O  O   . ILE D  1 217 ? 5.298   -10.626 -47.501 1.00 8.36  ? 217 ILE D O   1 
ATOM   8278  C  CB  . ILE D  1 217 ? 3.253   -7.946  -47.054 1.00 7.84  ? 217 ILE D CB  1 
ATOM   8279  C  CG1 . ILE D  1 217 ? 4.678   -7.433  -47.118 1.00 8.80  ? 217 ILE D CG1 1 
ATOM   8280  C  CG2 . ILE D  1 217 ? 2.308   -7.307  -46.035 1.00 10.05 ? 217 ILE D CG2 1 
ATOM   8281  C  CD1 . ILE D  1 217 ? 4.683   -5.836  -47.268 1.00 11.12 ? 217 ILE D CD1 1 
ATOM   8282  N  N   . SER D  1 218 ? 3.755   -10.291 -49.156 1.00 7.98  ? 218 SER D N   1 
ATOM   8283  C  CA  . SER D  1 218 ? 4.691   -11.011 -50.077 1.00 7.64  ? 218 SER D CA  1 
ATOM   8284  C  C   . SER D  1 218 ? 5.855   -10.279 -50.575 1.00 9.40  ? 218 SER D C   1 
ATOM   8285  O  O   . SER D  1 218 ? 5.897   -9.007  -50.484 1.00 9.14  ? 218 SER D O   1 
ATOM   8286  C  CB  . SER D  1 218 ? 3.892   -11.543 -51.252 1.00 8.44  ? 218 SER D CB  1 
ATOM   8287  O  OG  . SER D  1 218 ? 3.455   -10.451 -52.086 1.00 9.31  ? 218 SER D OG  1 
ATOM   8288  N  N   A GLN D  1 219 ? 6.821   -11.020 -51.141 0.50 9.64  ? 219 GLN D N   1 
ATOM   8289  N  N   B GLN D  1 219 ? 6.830   -10.987 -51.138 0.50 8.79  ? 219 GLN D N   1 
ATOM   8290  C  CA  A GLN D  1 219 ? 7.904   -10.435 -51.897 0.50 10.36 ? 219 GLN D CA  1 
ATOM   8291  C  CA  B GLN D  1 219 ? 7.895   -10.279 -51.768 0.50 8.74  ? 219 GLN D CA  1 
ATOM   8292  C  C   A GLN D  1 219 ? 7.401   -9.395  -52.894 0.50 9.23  ? 219 GLN D C   1 
ATOM   8293  C  C   B GLN D  1 219 ? 7.413   -9.379  -52.921 0.50 8.44  ? 219 GLN D C   1 
ATOM   8294  O  O   A GLN D  1 219 ? 7.981   -8.288  -52.969 0.50 10.34 ? 219 GLN D O   1 
ATOM   8295  O  O   B GLN D  1 219 ? 8.036   -8.336  -53.131 0.50 9.63  ? 219 GLN D O   1 
ATOM   8296  C  CB  A GLN D  1 219 ? 8.601   -11.528 -52.731 0.50 11.33 ? 219 GLN D CB  1 
ATOM   8297  C  CB  B GLN D  1 219 ? 8.922   -11.258 -52.294 0.50 8.66  ? 219 GLN D CB  1 
ATOM   8298  C  CG  A GLN D  1 219 ? 9.994   -11.104 -53.332 0.50 14.86 ? 219 GLN D CG  1 
ATOM   8299  C  CG  B GLN D  1 219 ? 10.221  -10.530 -52.811 0.50 9.63  ? 219 GLN D CG  1 
ATOM   8300  C  CD  A GLN D  1 219 ? 10.448  -9.626  -53.053 0.50 17.70 ? 219 GLN D CD  1 
ATOM   8301  C  CD  B GLN D  1 219 ? 10.183  -10.124 -54.312 0.50 10.10 ? 219 GLN D CD  1 
ATOM   8302  O  OE1 A GLN D  1 219 ? 10.477  -9.164  -51.907 0.50 23.28 ? 219 GLN D OE1 1 
ATOM   8303  O  OE1 B GLN D  1 219 ? 9.304   -10.582 -55.021 0.50 13.44 ? 219 GLN D OE1 1 
ATOM   8304  N  NE2 A GLN D  1 219 ? 10.755  -8.869  -54.108 0.50 15.35 ? 219 GLN D NE2 1 
ATOM   8305  N  NE2 B GLN D  1 219 ? 11.152  -9.268  -54.780 0.50 14.58 ? 219 GLN D NE2 1 
ATOM   8306  N  N   . GLU D  1 220 ? 6.370   -9.755  -53.640 1.00 9.50  ? 220 GLU D N   1 
ATOM   8307  C  CA  . GLU D  1 220 ? 5.890   -8.869  -54.702 1.00 10.88 ? 220 GLU D CA  1 
ATOM   8308  C  C   . GLU D  1 220 ? 5.279   -7.605  -54.101 1.00 9.46  ? 220 GLU D C   1 
ATOM   8309  O  O   . GLU D  1 220 ? 5.510   -6.513  -54.646 1.00 10.57 ? 220 GLU D O   1 
ATOM   8310  C  CB  . GLU D  1 220 ? 4.858   -9.595  -55.587 1.00 11.67 ? 220 GLU D CB  1 
ATOM   8311  C  CG  . GLU D  1 220 ? 5.552   -10.733 -56.392 1.00 13.20 ? 220 GLU D CG  1 
ATOM   8312  C  CD  . GLU D  1 220 ? 5.772   -11.996 -55.626 1.00 18.53 ? 220 GLU D CD  1 
ATOM   8313  O  OE1 . GLU D  1 220 ? 5.303   -12.199 -54.531 1.00 17.58 ? 220 GLU D OE1 1 
ATOM   8314  O  OE2 . GLU D  1 220 ? 6.419   -12.856 -56.245 1.00 26.33 ? 220 GLU D OE2 1 
ATOM   8315  N  N   . GLN D  1 221 ? 4.596   -7.728  -52.938 1.00 8.30  ? 221 GLN D N   1 
ATOM   8316  C  CA  . GLN D  1 221 ? 4.112   -6.482  -52.313 1.00 8.80  ? 221 GLN D CA  1 
ATOM   8317  C  C   . GLN D  1 221 ? 5.218   -5.651  -51.766 1.00 9.15  ? 221 GLN D C   1 
ATOM   8318  O  O   . GLN D  1 221 ? 5.171   -4.404  -51.971 1.00 10.26 ? 221 GLN D O   1 
ATOM   8319  C  CB  . GLN D  1 221 ? 3.222   -6.877  -51.151 1.00 8.75  ? 221 GLN D CB  1 
ATOM   8320  C  CG  . GLN D  1 221 ? 1.857   -7.496  -51.635 1.00 8.48  ? 221 GLN D CG  1 
ATOM   8321  C  CD  . GLN D  1 221 ? 0.984   -7.877  -50.507 1.00 8.37  ? 221 GLN D CD  1 
ATOM   8322  O  OE1 . GLN D  1 221 ? 1.287   -8.837  -49.708 1.00 8.89  ? 221 GLN D OE1 1 
ATOM   8323  N  NE2 . GLN D  1 221 ? -0.145  -7.190  -50.352 1.00 9.06  ? 221 GLN D NE2 1 
ATOM   8324  N  N   . LEU D  1 222 ? 6.275   -6.268  -51.200 1.00 9.33  ? 222 LEU D N   1 
ATOM   8325  C  CA  . LEU D  1 222 ? 7.401   -5.462  -50.714 1.00 9.38  ? 222 LEU D CA  1 
ATOM   8326  C  C   . LEU D  1 222 ? 8.078   -4.773  -51.906 1.00 9.53  ? 222 LEU D C   1 
ATOM   8327  O  O   . LEU D  1 222 ? 8.472   -3.616  -51.758 1.00 10.30 ? 222 LEU D O   1 
ATOM   8328  C  CB  . LEU D  1 222 ? 8.339   -6.415  -49.983 1.00 9.86  ? 222 LEU D CB  1 
ATOM   8329  C  CG  . LEU D  1 222 ? 8.038   -6.636  -48.574 1.00 11.38 ? 222 LEU D CG  1 
ATOM   8330  C  CD1 . LEU D  1 222 ? 8.716   -7.928  -48.079 1.00 11.89 ? 222 LEU D CD1 1 
ATOM   8331  C  CD2 . LEU D  1 222 ? 8.403   -5.446  -47.629 1.00 11.49 ? 222 LEU D CD2 1 
ATOM   8332  N  N   . LEU D  1 223 ? 8.238   -5.463  -53.013 1.00 9.83  ? 223 LEU D N   1 
ATOM   8333  C  CA  . LEU D  1 223 ? 8.960   -4.902  -54.150 1.00 10.92 ? 223 LEU D CA  1 
ATOM   8334  C  C   . LEU D  1 223 ? 8.146   -3.719  -54.660 1.00 10.96 ? 223 LEU D C   1 
ATOM   8335  O  O   . LEU D  1 223 ? 8.727   -2.684  -55.063 1.00 10.33 ? 223 LEU D O   1 
ATOM   8336  C  CB  . LEU D  1 223 ? 9.199   -5.989  -55.228 1.00 11.03 ? 223 LEU D CB  1 
ATOM   8337  C  CG  . LEU D  1 223 ? 9.946   -5.424  -56.467 1.00 11.92 ? 223 LEU D CG  1 
ATOM   8338  C  CD1 . LEU D  1 223 ? 11.367  -4.994  -56.113 1.00 14.60 ? 223 LEU D CD1 1 
ATOM   8339  C  CD2 . LEU D  1 223 ? 10.005  -6.531  -57.488 1.00 13.52 ? 223 LEU D CD2 1 
ATOM   8340  N  N   . ALA D  1 224 ? 6.832   -3.849  -54.723 1.00 10.69 ? 224 ALA D N   1 
ATOM   8341  C  CA  . ALA D  1 224 ? 6.002   -2.719  -55.148 1.00 11.25 ? 224 ALA D CA  1 
ATOM   8342  C  C   . ALA D  1 224 ? 6.173   -1.534  -54.187 1.00 10.63 ? 224 ALA D C   1 
ATOM   8343  O  O   . ALA D  1 224 ? 6.404   -0.397  -54.677 1.00 12.49 ? 224 ALA D O   1 
ATOM   8344  C  CB  . ALA D  1 224 ? 4.526   -3.112  -55.232 1.00 11.88 ? 224 ALA D CB  1 
ATOM   8345  N  N   . LEU D  1 225 ? 6.110   -1.770  -52.870 1.00 10.19 ? 225 LEU D N   1 
ATOM   8346  C  CA  . LEU D  1 225 ? 6.349   -0.732  -51.885 1.00 10.89 ? 225 LEU D CA  1 
ATOM   8347  C  C   . LEU D  1 225 ? 7.712   -0.052  -52.079 1.00 11.31 ? 225 LEU D C   1 
ATOM   8348  O  O   . LEU D  1 225 ? 7.813   1.193   -52.015 1.00 12.71 ? 225 LEU D O   1 
ATOM   8349  C  CB  . LEU D  1 225 ? 6.152   -1.322  -50.534 1.00 11.64 ? 225 LEU D CB  1 
ATOM   8350  C  CG  . LEU D  1 225 ? 6.317   -0.324  -49.377 1.00 11.24 ? 225 LEU D CG  1 
ATOM   8351  C  CD1 . LEU D  1 225 ? 5.273   0.830   -49.434 1.00 12.40 ? 225 LEU D CD1 1 
ATOM   8352  C  CD2 . LEU D  1 225 ? 6.126   -1.049  -48.063 1.00 12.33 ? 225 LEU D CD2 1 
ATOM   8353  N  N   . GLU D  1 226 ? 8.725   -0.849  -52.308 1.00 10.84 ? 226 GLU D N   1 
ATOM   8354  C  CA  . GLU D  1 226 ? 10.089  -0.387  -52.372 1.00 11.04 ? 226 GLU D CA  1 
ATOM   8355  C  C   . GLU D  1 226 ? 10.435  0.326   -53.643 1.00 12.54 ? 226 GLU D C   1 
ATOM   8356  O  O   . GLU D  1 226 ? 11.521  0.942   -53.706 1.00 14.59 ? 226 GLU D O   1 
ATOM   8357  C  CB  . GLU D  1 226 ? 11.046  -1.628  -52.246 1.00 10.78 ? 226 GLU D CB  1 
ATOM   8358  C  CG  . GLU D  1 226 ? 11.095  -2.231  -50.852 1.00 8.90  ? 226 GLU D CG  1 
ATOM   8359  C  CD  . GLU D  1 226 ? 11.418  -3.693  -50.888 1.00 11.20 ? 226 GLU D CD  1 
ATOM   8360  O  OE1 . GLU D  1 226 ? 11.671  -4.307  -51.965 1.00 11.54 ? 226 GLU D OE1 1 
ATOM   8361  O  OE2 . GLU D  1 226 ? 11.380  -4.263  -49.790 1.00 12.74 ? 226 GLU D OE2 1 
ATOM   8362  N  N   . THR D  1 227 ? 9.652   0.234   -54.675 1.00 10.92 ? 227 THR D N   1 
ATOM   8363  C  CA  . THR D  1 227 ? 9.938   0.798   -56.008 1.00 11.52 ? 227 THR D CA  1 
ATOM   8364  C  C   . THR D  1 227 ? 8.922   1.791   -56.462 1.00 11.60 ? 227 THR D C   1 
ATOM   8365  O  O   . THR D  1 227 ? 9.224   2.440   -57.470 1.00 14.31 ? 227 THR D O   1 
ATOM   8366  C  CB  . THR D  1 227 ? 10.129  -0.293  -57.076 1.00 13.80 ? 227 THR D CB  1 
ATOM   8367  O  OG1 . THR D  1 227 ? 8.918   -1.025  -57.253 1.00 12.77 ? 227 THR D OG1 1 
ATOM   8368  C  CG2 . THR D  1 227 ? 11.352  -1.204  -56.767 1.00 13.50 ? 227 THR D CG2 1 
ATOM   8369  N  N   . ALA D  1 228 ? 7.802   1.942   -55.805 1.00 10.98 ? 228 ALA D N   1 
ATOM   8370  C  CA  . ALA D  1 228 ? 6.713   2.782   -56.343 1.00 12.31 ? 228 ALA D CA  1 
ATOM   8371  C  C   . ALA D  1 228 ? 6.992   4.248   -56.138 1.00 12.85 ? 228 ALA D C   1 
ATOM   8372  O  O   . ALA D  1 228 ? 6.438   5.031   -56.922 1.00 15.07 ? 228 ALA D O   1 
ATOM   8373  C  CB  . ALA D  1 228 ? 5.346   2.423   -55.751 1.00 14.92 ? 228 ALA D CB  1 
ATOM   8374  N  N   . LEU D  1 229 ? 7.655   4.639   -55.089 1.00 11.42 ? 229 LEU D N   1 
ATOM   8375  C  CA  . LEU D  1 229 ? 7.550   6.009   -54.608 1.00 11.23 ? 229 LEU D CA  1 
ATOM   8376  C  C   . LEU D  1 229 ? 8.861   6.789   -54.643 1.00 10.54 ? 229 LEU D C   1 
ATOM   8377  O  O   . LEU D  1 229 ? 9.919   6.228   -54.528 1.00 10.35 ? 229 LEU D O   1 
ATOM   8378  C  CB  . LEU D  1 229 ? 7.048   6.048   -53.142 1.00 11.89 ? 229 LEU D CB  1 
ATOM   8379  C  CG  . LEU D  1 229 ? 5.776   5.222   -52.839 1.00 12.66 ? 229 LEU D CG  1 
ATOM   8380  C  CD1 . LEU D  1 229 ? 5.402   5.256   -51.357 1.00 14.78 ? 229 LEU D CD1 1 
ATOM   8381  C  CD2 . LEU D  1 229 ? 4.627   5.665   -53.716 1.00 14.49 ? 229 LEU D CD2 1 
ATOM   8382  N  N   . TYR D  1 230 ? 8.696   8.116   -54.789 1.00 10.53 ? 230 TYR D N   1 
ATOM   8383  C  CA  . TYR D  1 230 ? 9.789   9.071   -54.707 1.00 11.33 ? 230 TYR D CA  1 
ATOM   8384  C  C   . TYR D  1 230 ? 9.582   10.027  -53.556 1.00 10.37 ? 230 TYR D C   1 
ATOM   8385  O  O   . TYR D  1 230 ? 8.447   10.409  -53.216 1.00 11.68 ? 230 TYR D O   1 
ATOM   8386  C  CB  . TYR D  1 230 ? 9.828   9.848   -56.040 1.00 11.56 ? 230 TYR D CB  1 
ATOM   8387  C  CG  . TYR D  1 230 ? 10.347  9.045   -57.187 1.00 13.01 ? 230 TYR D CG  1 
ATOM   8388  C  CD1 . TYR D  1 230 ? 9.499   8.161   -57.890 1.00 15.20 ? 230 TYR D CD1 1 
ATOM   8389  C  CD2 . TYR D  1 230 ? 11.674  9.024   -57.461 1.00 14.76 ? 230 TYR D CD2 1 
ATOM   8390  C  CE1 . TYR D  1 230 ? 9.971   7.350   -58.926 1.00 19.04 ? 230 TYR D CE1 1 
ATOM   8391  C  CE2 . TYR D  1 230 ? 12.191  8.167   -58.466 1.00 18.14 ? 230 TYR D CE2 1 
ATOM   8392  C  CZ  . TYR D  1 230 ? 11.305  7.364   -59.200 1.00 19.70 ? 230 TYR D CZ  1 
ATOM   8393  O  OH  . TYR D  1 230 ? 11.735  6.502   -60.196 1.00 24.84 ? 230 TYR D OH  1 
ATOM   8394  N  N   . CYS D  1 231 ? 10.677  10.480  -52.976 1.00 12.02 ? 231 CYS D N   1 
ATOM   8395  C  CA  . CYS D  1 231 ? 10.613  11.467  -51.951 1.00 11.12 ? 231 CYS D CA  1 
ATOM   8396  C  C   . CYS D  1 231 ? 10.371  12.888  -52.466 1.00 11.06 ? 231 CYS D C   1 
ATOM   8397  O  O   . CYS D  1 231 ? 9.981   13.777  -51.713 1.00 14.19 ? 231 CYS D O   1 
ATOM   8398  C  CB  . CYS D  1 231 ? 11.977  11.584  -51.253 1.00 13.40 ? 231 CYS D CB  1 
ATOM   8399  S  SG  . CYS D  1 231 ? 12.489  10.065  -50.351 1.00 12.75 ? 231 CYS D SG  1 
ATOM   8400  N  N   . THR D  1 232 ? 10.631  13.042  -53.754 1.00 11.17 ? 232 THR D N   1 
ATOM   8401  C  CA  . THR D  1 232 ? 10.657  14.358  -54.388 1.00 12.05 ? 232 THR D CA  1 
ATOM   8402  C  C   . THR D  1 232 ? 9.372   14.628  -55.097 1.00 13.56 ? 232 THR D C   1 
ATOM   8403  O  O   . THR D  1 232 ? 8.555   13.764  -55.442 1.00 13.17 ? 232 THR D O   1 
ATOM   8404  C  CB  . THR D  1 232 ? 11.881  14.406  -55.370 1.00 13.39 ? 232 THR D CB  1 
ATOM   8405  O  OG1 . THR D  1 232 ? 11.992  13.134  -56.006 1.00 13.23 ? 232 THR D OG1 1 
ATOM   8406  C  CG2 . THR D  1 232 ? 13.106  14.611  -54.612 1.00 16.02 ? 232 THR D CG2 1 
ATOM   8407  N  N   . HIS D  1 233 ? 9.127   15.942  -55.349 1.00 13.05 ? 233 HIS D N   1 
ATOM   8408  C  CA  . HIS D  1 233 ? 8.040   16.336  -56.200 1.00 13.61 ? 233 HIS D CA  1 
ATOM   8409  C  C   . HIS D  1 233 ? 8.274   15.899  -57.630 1.00 14.34 ? 233 HIS D C   1 
ATOM   8410  O  O   . HIS D  1 233 ? 9.414   15.665  -58.074 1.00 15.40 ? 233 HIS D O   1 
ATOM   8411  C  CB  . HIS D  1 233 ? 7.939   17.892  -56.177 1.00 15.51 ? 233 HIS D CB  1 
ATOM   8412  C  CG  . HIS D  1 233 ? 7.378   18.428  -54.919 1.00 18.47 ? 233 HIS D CG  1 
ATOM   8413  N  ND1 . HIS D  1 233 ? 8.120   19.155  -54.013 1.00 22.32 ? 233 HIS D ND1 1 
ATOM   8414  C  CD2 . HIS D  1 233 ? 6.146   18.267  -54.363 1.00 18.49 ? 233 HIS D CD2 1 
ATOM   8415  C  CE1 . HIS D  1 233 ? 7.344   19.459  -52.974 1.00 22.70 ? 233 HIS D CE1 1 
ATOM   8416  N  NE2 . HIS D  1 233 ? 6.144   18.928  -53.172 1.00 20.56 ? 233 HIS D NE2 1 
ATOM   8417  N  N   . MET D  1 234 ? 7.176   15.771  -58.329 1.00 15.79 ? 234 MET D N   1 
ATOM   8418  C  CA  . MET D  1 234 ? 7.153   15.261  -59.704 1.00 16.48 ? 234 MET D CA  1 
ATOM   8419  C  C   . MET D  1 234 ? 8.137   16.051  -60.609 1.00 19.94 ? 234 MET D C   1 
ATOM   8420  O  O   . MET D  1 234 ? 8.885   15.455  -61.405 1.00 21.11 ? 234 MET D O   1 
ATOM   8421  C  CB  . MET D  1 234 ? 5.708   15.342  -60.173 1.00 19.90 ? 234 MET D CB  1 
ATOM   8422  C  CG  . MET D  1 234 ? 5.632   14.695  -61.546 1.00 24.28 ? 234 MET D CG  1 
ATOM   8423  S  SD  . MET D  1 234 ? 3.869   14.594  -61.945 1.00 30.11 ? 234 MET D SD  1 
ATOM   8424  C  CE  . MET D  1 234 ? 4.040   13.178  -63.021 1.00 34.35 ? 234 MET D CE  1 
ATOM   8425  N  N   . ASP D  1 235 ? 8.235   17.363  -60.379 1.00 19.26 ? 235 ASP D N   1 
ATOM   8426  C  CA  . ASP D  1 235 ? 9.065   18.215  -61.241 1.00 21.26 ? 235 ASP D CA  1 
ATOM   8427  C  C   . ASP D  1 235 ? 10.508  18.427  -60.788 1.00 22.53 ? 235 ASP D C   1 
ATOM   8428  O  O   . ASP D  1 235 ? 11.292  19.157  -61.407 1.00 24.47 ? 235 ASP D O   1 
ATOM   8429  C  CB  . ASP D  1 235 ? 8.290   19.574  -61.464 1.00 22.23 ? 235 ASP D CB  1 
ATOM   8430  C  CG  . ASP D  1 235 ? 8.283   20.467  -60.249 1.00 27.13 ? 235 ASP D CG  1 
ATOM   8431  O  OD1 . ASP D  1 235 ? 8.766   20.052  -59.154 1.00 30.27 ? 235 ASP D OD1 1 
ATOM   8432  O  OD2 . ASP D  1 235 ? 7.741   21.621  -60.313 1.00 28.42 ? 235 ASP D OD2 1 
ATOM   8433  N  N   . ASP D  1 236 ? 10.939  17.765  -59.723 1.00 19.34 ? 236 ASP D N   1 
ATOM   8434  C  CA  . ASP D  1 236 ? 12.294  17.927  -59.237 1.00 21.02 ? 236 ASP D CA  1 
ATOM   8435  C  C   . ASP D  1 236 ? 13.331  17.367  -60.196 1.00 20.68 ? 236 ASP D C   1 
ATOM   8436  O  O   . ASP D  1 236 ? 13.255  16.221  -60.601 1.00 20.95 ? 236 ASP D O   1 
ATOM   8437  C  CB  . ASP D  1 236 ? 12.444  17.216  -57.840 1.00 19.19 ? 236 ASP D CB  1 
ATOM   8438  C  CG  . ASP D  1 236 ? 13.668  17.633  -57.073 1.00 19.76 ? 236 ASP D CG  1 
ATOM   8439  O  OD1 . ASP D  1 236 ? 14.760  17.741  -57.657 1.00 20.37 ? 236 ASP D OD1 1 
ATOM   8440  O  OD2 . ASP D  1 236 ? 13.503  17.842  -55.852 1.00 21.98 ? 236 ASP D OD2 1 
ATOM   8441  N  N   . PRO D  1 237 ? 14.330  18.187  -60.580 1.00 22.95 ? 237 PRO D N   1 
ATOM   8442  C  CA  . PRO D  1 237 ? 15.357  17.690  -61.492 1.00 22.09 ? 237 PRO D CA  1 
ATOM   8443  C  C   . PRO D  1 237 ? 16.325  16.731  -60.858 1.00 22.18 ? 237 PRO D C   1 
ATOM   8444  O  O   . PRO D  1 237 ? 17.099  16.136  -61.593 1.00 21.95 ? 237 PRO D O   1 
ATOM   8445  C  CB  . PRO D  1 237 ? 16.110  18.986  -61.868 1.00 25.73 ? 237 PRO D CB  1 
ATOM   8446  C  CG  . PRO D  1 237 ? 15.965  19.892  -60.695 1.00 26.76 ? 237 PRO D CG  1 
ATOM   8447  C  CD  . PRO D  1 237 ? 14.577  19.584  -60.127 1.00 26.43 ? 237 PRO D CD  1 
ATOM   8448  N  N   A SER D  1 238 ? 16.245  16.517  -59.533 0.50 19.96 ? 238 SER D N   1 
ATOM   8449  N  N   B SER D  1 238 ? 16.235  16.512  -59.528 0.50 19.04 ? 238 SER D N   1 
ATOM   8450  C  CA  A SER D  1 238 ? 17.103  15.559  -58.888 0.50 19.42 ? 238 SER D CA  1 
ATOM   8451  C  CA  B SER D  1 238 ? 17.121  15.612  -58.812 0.50 18.15 ? 238 SER D CA  1 
ATOM   8452  C  C   A SER D  1 238 ? 16.195  14.589  -58.108 0.50 16.02 ? 238 SER D C   1 
ATOM   8453  C  C   B SER D  1 238 ? 16.208  14.584  -58.075 0.50 15.32 ? 238 SER D C   1 
ATOM   8454  O  O   A SER D  1 238 ? 16.057  14.719  -56.908 0.50 16.33 ? 238 SER D O   1 
ATOM   8455  O  O   B SER D  1 238 ? 16.074  14.675  -56.870 0.50 15.88 ? 238 SER D O   1 
ATOM   8456  C  CB  A SER D  1 238 ? 18.035  16.215  -57.914 0.50 22.64 ? 238 SER D CB  1 
ATOM   8457  C  CB  B SER D  1 238 ? 17.955  16.373  -57.788 0.50 20.16 ? 238 SER D CB  1 
ATOM   8458  O  OG  A SER D  1 238 ? 19.103  15.335  -57.679 0.50 24.47 ? 238 SER D OG  1 
ATOM   8459  O  OG  B SER D  1 238 ? 19.012  17.105  -58.438 0.50 19.43 ? 238 SER D OG  1 
ATOM   8460  N  N   . PRO D  1 239 ? 15.571  13.665  -58.839 1.00 16.71 ? 239 PRO D N   1 
ATOM   8461  C  CA  . PRO D  1 239 ? 14.629  12.694  -58.161 1.00 14.87 ? 239 PRO D CA  1 
ATOM   8462  C  C   . PRO D  1 239 ? 15.330  11.840  -57.135 1.00 15.01 ? 239 PRO D C   1 
ATOM   8463  O  O   . PRO D  1 239 ? 16.498  11.473  -57.273 1.00 15.55 ? 239 PRO D O   1 
ATOM   8464  C  CB  . PRO D  1 239 ? 14.093  11.822  -59.270 1.00 17.45 ? 239 PRO D CB  1 
ATOM   8465  C  CG  . PRO D  1 239 ? 14.668  12.297  -60.571 1.00 20.39 ? 239 PRO D CG  1 
ATOM   8466  C  CD  . PRO D  1 239 ? 15.712  13.361  -60.298 1.00 18.65 ? 239 PRO D CD  1 
ATOM   8467  N  N   . ARG D  1 240 ? 14.610  11.540  -56.041 1.00 13.95 ? 240 ARG D N   1 
ATOM   8468  C  CA  . ARG D  1 240 ? 15.205  10.621  -55.076 1.00 13.03 ? 240 ARG D CA  1 
ATOM   8469  C  C   . ARG D  1 240 ? 14.156  9.540   -54.765 1.00 13.30 ? 240 ARG D C   1 
ATOM   8470  O  O   . ARG D  1 240 ? 13.020  9.895   -54.376 1.00 12.61 ? 240 ARG D O   1 
ATOM   8471  C  CB  . ARG D  1 240 ? 15.511  11.364  -53.755 1.00 13.73 ? 240 ARG D CB  1 
ATOM   8472  C  CG  . ARG D  1 240 ? 16.785  12.221  -53.877 1.00 15.80 ? 240 ARG D CG  1 
ATOM   8473  C  CD  . ARG D  1 240 ? 16.971  13.012  -52.615 1.00 16.77 ? 240 ARG D CD  1 
ATOM   8474  N  NE  . ARG D  1 240 ? 15.957  14.051  -52.363 1.00 19.07 ? 240 ARG D NE  1 
ATOM   8475  C  CZ  . ARG D  1 240 ? 15.028  13.971  -51.399 1.00 20.93 ? 240 ARG D CZ  1 
ATOM   8476  N  NH1 . ARG D  1 240 ? 14.997  12.951  -50.519 1.00 16.98 ? 240 ARG D NH1 1 
ATOM   8477  N  NH2 . ARG D  1 240 ? 14.163  14.941  -51.303 1.00 20.63 ? 240 ARG D NH2 1 
ATOM   8478  N  N   . GLU D  1 241 ? 14.531  8.277   -54.919 1.00 12.01 ? 241 GLU D N   1 
ATOM   8479  C  CA  . GLU D  1 241 ? 13.614  7.175   -54.579 1.00 11.28 ? 241 GLU D CA  1 
ATOM   8480  C  C   . GLU D  1 241 ? 13.372  7.084   -53.101 1.00 11.06 ? 241 GLU D C   1 
ATOM   8481  O  O   . GLU D  1 241 ? 14.259  7.287   -52.238 1.00 11.74 ? 241 GLU D O   1 
ATOM   8482  C  CB  . GLU D  1 241 ? 14.265  5.867   -55.006 1.00 12.56 ? 241 GLU D CB  1 
ATOM   8483  C  CG  . GLU D  1 241 ? 14.374  5.770   -56.556 1.00 17.32 ? 241 GLU D CG  1 
ATOM   8484  C  CD  . GLU D  1 241 ? 15.240  4.657   -56.918 1.00 21.47 ? 241 GLU D CD  1 
ATOM   8485  O  OE1 . GLU D  1 241 ? 16.455  4.845   -56.766 1.00 30.25 ? 241 GLU D OE1 1 
ATOM   8486  O  OE2 . GLU D  1 241 ? 14.746  3.602   -57.291 1.00 26.75 ? 241 GLU D OE2 1 
ATOM   8487  N  N   . MET D  1 242 ? 12.101  6.757   -52.742 1.00 9.44  ? 242 MET D N   1 
ATOM   8488  C  CA  . MET D  1 242 ? 11.757  6.596   -51.324 1.00 9.21  ? 242 MET D CA  1 
ATOM   8489  C  C   . MET D  1 242 ? 12.050  5.142   -50.892 1.00 8.30  ? 242 MET D C   1 
ATOM   8490  O  O   . MET D  1 242 ? 11.223  4.233   -51.079 1.00 9.20  ? 242 MET D O   1 
ATOM   8491  C  CB  . MET D  1 242 ? 10.314  6.976   -51.130 1.00 9.50  ? 242 MET D CB  1 
ATOM   8492  C  CG  . MET D  1 242 ? 9.962   6.992   -49.632 1.00 9.29  ? 242 MET D CG  1 
ATOM   8493  S  SD  . MET D  1 242 ? 8.208   7.319   -49.315 1.00 9.96  ? 242 MET D SD  1 
ATOM   8494  C  CE  . MET D  1 242 ? 8.099   9.022   -49.961 1.00 11.29 ? 242 MET D CE  1 
ATOM   8495  N  N   . ILE D  1 243 ? 13.269  4.934   -50.434 1.00 8.21  ? 243 ILE D N   1 
ATOM   8496  C  CA  . ILE D  1 243 ? 13.790  3.652   -50.038 1.00 9.35  ? 243 ILE D CA  1 
ATOM   8497  C  C   . ILE D  1 243 ? 14.546  3.857   -48.714 1.00 8.16  ? 243 ILE D C   1 
ATOM   8498  O  O   . ILE D  1 243 ? 14.998  4.962   -48.396 1.00 8.29  ? 243 ILE D O   1 
ATOM   8499  C  CB  . ILE D  1 243 ? 14.763  3.048   -51.090 1.00 10.35 ? 243 ILE D CB  1 
ATOM   8500  C  CG1 . ILE D  1 243 ? 15.879  4.080   -51.479 1.00 11.49 ? 243 ILE D CG1 1 
ATOM   8501  C  CG2 . ILE D  1 243 ? 14.004  2.561   -52.287 1.00 12.78 ? 243 ILE D CG2 1 
ATOM   8502  C  CD1 . ILE D  1 243 ? 16.943  3.496   -52.412 1.00 15.17 ? 243 ILE D CD1 1 
ATOM   8503  N  N   . ASN D  1 244 ? 14.655  2.764   -47.987 1.00 7.98  ? 244 ASN D N   1 
ATOM   8504  C  CA  . ASN D  1 244 ? 15.460  2.774   -46.760 1.00 8.60  ? 244 ASN D CA  1 
ATOM   8505  C  C   . ASN D  1 244 ? 15.054  3.875   -45.804 1.00 9.01  ? 244 ASN D C   1 
ATOM   8506  O  O   . ASN D  1 244 ? 15.903  4.568   -45.204 1.00 8.97  ? 244 ASN D O   1 
ATOM   8507  C  CB  . ASN D  1 244 ? 16.974  2.894   -47.101 1.00 8.99  ? 244 ASN D CB  1 
ATOM   8508  C  CG  . ASN D  1 244 ? 17.393  1.801   -47.986 1.00 11.28 ? 244 ASN D CG  1 
ATOM   8509  O  OD1 . ASN D  1 244 ? 16.959  0.631   -47.919 1.00 11.21 ? 244 ASN D OD1 1 
ATOM   8510  N  ND2 . ASN D  1 244 ? 18.217  2.243   -48.994 1.00 13.86 ? 244 ASN D ND2 1 
ATOM   8511  N  N   . ASN D  1 245 ? 13.750  4.027   -45.657 1.00 7.61  ? 245 ASN D N   1 
ATOM   8512  C  CA  . ASN D  1 245 ? 13.212  5.128   -44.861 1.00 7.42  ? 245 ASN D CA  1 
ATOM   8513  C  C   . ASN D  1 245 ? 12.945  4.694   -43.420 1.00 7.83  ? 245 ASN D C   1 
ATOM   8514  O  O   . ASN D  1 245 ? 11.820  4.841   -42.896 1.00 8.42  ? 245 ASN D O   1 
ATOM   8515  C  CB  . ASN D  1 245 ? 11.944  5.747   -45.457 1.00 7.42  ? 245 ASN D CB  1 
ATOM   8516  C  CG  . ASN D  1 245 ? 10.816  4.789   -45.684 1.00 7.48  ? 245 ASN D CG  1 
ATOM   8517  O  OD1 . ASN D  1 245 ? 10.985  3.571   -45.652 1.00 8.70  ? 245 ASN D OD1 1 
ATOM   8518  N  ND2 . ASN D  1 245 ? 9.601   5.310   -45.875 1.00 8.76  ? 245 ASN D ND2 1 
ATOM   8519  N  N   . PHE D  1 246 ? 13.981  4.130   -42.798 1.00 7.49  ? 246 PHE D N   1 
ATOM   8520  C  CA  . PHE D  1 246 ? 13.925  3.722   -41.376 1.00 7.07  ? 246 PHE D CA  1 
ATOM   8521  C  C   . PHE D  1 246 ? 15.115  4.325   -40.721 1.00 7.68  ? 246 PHE D C   1 
ATOM   8522  O  O   . PHE D  1 246 ? 16.211  4.497   -41.303 1.00 8.15  ? 246 PHE D O   1 
ATOM   8523  C  CB  . PHE D  1 246 ? 13.977  2.141   -41.319 1.00 7.46  ? 246 PHE D CB  1 
ATOM   8524  C  CG  . PHE D  1 246 ? 15.228  1.511   -41.905 1.00 7.85  ? 246 PHE D CG  1 
ATOM   8525  C  CD1 . PHE D  1 246 ? 15.301  1.183   -43.281 1.00 7.63  ? 246 PHE D CD1 1 
ATOM   8526  C  CD2 . PHE D  1 246 ? 16.326  1.161   -41.055 1.00 8.53  ? 246 PHE D CD2 1 
ATOM   8527  C  CE1 . PHE D  1 246 ? 16.452  0.611   -43.812 1.00 8.75  ? 246 PHE D CE1 1 
ATOM   8528  C  CE2 . PHE D  1 246 ? 17.491  0.614   -41.605 1.00 10.14 ? 246 PHE D CE2 1 
ATOM   8529  C  CZ  . PHE D  1 246 ? 17.539  0.331   -42.970 1.00 9.98  ? 246 PHE D CZ  1 
ATOM   8530  N  N   . ARG D  1 247 ? 14.927  4.634   -39.447 1.00 7.86  ? 247 ARG D N   1 
ATOM   8531  C  CA  . ARG D  1 247 ? 16.022  5.108   -38.601 1.00 7.39  ? 247 ARG D CA  1 
ATOM   8532  C  C   . ARG D  1 247 ? 16.766  3.962   -37.961 1.00 8.48  ? 247 ARG D C   1 
ATOM   8533  O  O   . ARG D  1 247 ? 16.123  2.967   -37.598 1.00 8.04  ? 247 ARG D O   1 
ATOM   8534  C  CB  . ARG D  1 247 ? 15.395  6.027   -37.502 1.00 7.04  ? 247 ARG D CB  1 
ATOM   8535  C  CG  . ARG D  1 247 ? 16.409  6.886   -36.770 1.00 7.30  ? 247 ARG D CG  1 
ATOM   8536  C  CD  . ARG D  1 247 ? 15.751  7.555   -35.619 1.00 7.63  ? 247 ARG D CD  1 
ATOM   8537  N  NE  . ARG D  1 247 ? 16.596  8.677   -35.076 1.00 7.97  ? 247 ARG D NE  1 
ATOM   8538  C  CZ  . ARG D  1 247 ? 16.291  9.395   -33.993 1.00 8.16  ? 247 ARG D CZ  1 
ATOM   8539  N  NH1 . ARG D  1 247 ? 15.164  9.143   -33.254 1.00 8.78  ? 247 ARG D NH1 1 
ATOM   8540  N  NH2 . ARG D  1 247 ? 17.084  10.428  -33.624 1.00 7.82  ? 247 ARG D NH2 1 
ATOM   8541  N  N   . GLN D  1 248 ? 18.063  4.096   -37.778 1.00 7.06  ? 248 GLN D N   1 
ATOM   8542  C  CA  . GLN D  1 248 ? 18.782  3.109   -36.941 1.00 7.62  ? 248 GLN D CA  1 
ATOM   8543  C  C   . GLN D  1 248 ? 18.270  3.063   -35.530 1.00 7.96  ? 248 GLN D C   1 
ATOM   8544  O  O   . GLN D  1 248 ? 17.772  4.070   -34.988 1.00 8.25  ? 248 GLN D O   1 
ATOM   8545  C  CB  . GLN D  1 248 ? 20.292  3.498   -36.928 1.00 7.66  ? 248 GLN D CB  1 
ATOM   8546  C  CG  . GLN D  1 248 ? 21.017  3.449   -38.284 1.00 8.18  ? 248 GLN D CG  1 
ATOM   8547  C  CD  . GLN D  1 248 ? 21.000  2.078   -38.929 1.00 8.82  ? 248 GLN D CD  1 
ATOM   8548  O  OE1 . GLN D  1 248 ? 20.072  1.738   -39.696 1.00 10.13 ? 248 GLN D OE1 1 
ATOM   8549  N  NE2 . GLN D  1 248 ? 21.969  1.273   -38.614 1.00 9.50  ? 248 GLN D NE2 1 
ATOM   8550  N  N   . VAL D  1 249 ? 18.522  1.907   -34.885 1.00 8.08  ? 249 VAL D N   1 
ATOM   8551  C  CA  . VAL D  1 249 ? 18.133  1.804   -33.475 1.00 8.87  ? 249 VAL D CA  1 
ATOM   8552  C  C   . VAL D  1 249 ? 19.021  2.739   -32.583 1.00 8.87  ? 249 VAL D C   1 
ATOM   8553  O  O   . VAL D  1 249 ? 20.161  3.080   -32.958 1.00 8.79  ? 249 VAL D O   1 
ATOM   8554  C  CB  . VAL D  1 249 ? 18.190  0.355   -32.946 1.00 8.42  ? 249 VAL D CB  1 
ATOM   8555  C  CG1 . VAL D  1 249 ? 17.149  -0.522  -33.636 1.00 11.09 ? 249 VAL D CG1 1 
ATOM   8556  C  CG2 . VAL D  1 249 ? 19.571  -0.268  -33.101 1.00 10.05 ? 249 VAL D CG2 1 
ATOM   8557  N  N   . GLN D  1 250 ? 18.445  3.090   -31.457 1.00 7.94  ? 250 GLN D N   1 
ATOM   8558  C  CA  . GLN D  1 250 ? 18.997  4.123   -30.528 1.00 8.53  ? 250 GLN D CA  1 
ATOM   8559  C  C   . GLN D  1 250 ? 19.461  3.565   -29.189 1.00 8.41  ? 250 GLN D C   1 
ATOM   8560  O  O   . GLN D  1 250 ? 19.062  2.470   -28.783 1.00 10.59 ? 250 GLN D O   1 
ATOM   8561  C  CB  . GLN D  1 250 ? 17.850  5.104   -30.216 1.00 8.31  ? 250 GLN D CB  1 
ATOM   8562  C  CG  . GLN D  1 250 ? 17.212  5.744   -31.505 1.00 8.82  ? 250 GLN D CG  1 
ATOM   8563  C  CD  . GLN D  1 250 ? 18.165  6.621   -32.260 1.00 8.77  ? 250 GLN D CD  1 
ATOM   8564  O  OE1 . GLN D  1 250 ? 18.576  7.679   -31.677 1.00 9.63  ? 250 GLN D OE1 1 
ATOM   8565  N  NE2 . GLN D  1 250 ? 18.451  6.345   -33.508 1.00 9.25  ? 250 GLN D NE2 1 
ATOM   8566  N  N   . LYS D  1 251 ? 20.301  4.322   -28.554 1.00 8.89  ? 251 LYS D N   1 
ATOM   8567  C  CA  . LYS D  1 251 ? 20.725  3.944   -27.193 1.00 10.09 ? 251 LYS D CA  1 
ATOM   8568  C  C   . LYS D  1 251 ? 19.504  3.844   -26.295 1.00 9.69  ? 251 LYS D C   1 
ATOM   8569  O  O   . LYS D  1 251 ? 18.521  4.561   -26.374 1.00 10.89 ? 251 LYS D O   1 
ATOM   8570  C  CB  . LYS D  1 251 ? 21.634  5.015   -26.656 1.00 11.35 ? 251 LYS D CB  1 
ATOM   8571  C  CG  . LYS D  1 251 ? 23.041  5.069   -27.275 1.00 11.56 ? 251 LYS D CG  1 
ATOM   8572  C  CD  . LYS D  1 251 ? 23.879  3.895   -26.734 1.00 11.59 ? 251 LYS D CD  1 
ATOM   8573  C  CE  . LYS D  1 251 ? 25.356  3.991   -27.121 1.00 11.36 ? 251 LYS D CE  1 
ATOM   8574  N  NZ  . LYS D  1 251 ? 25.489  3.857   -28.628 1.00 9.78  ? 251 LYS D NZ  1 
ATOM   8575  N  N   . PHE D  1 252 ? 19.554  2.855   -25.406 1.00 12.01 ? 252 PHE D N   1 
ATOM   8576  C  CA  . PHE D  1 252 ? 18.488  2.730   -24.423 1.00 12.36 ? 252 PHE D CA  1 
ATOM   8577  C  C   . PHE D  1 252 ? 18.312  3.854   -23.382 1.00 15.85 ? 252 PHE D C   1 
ATOM   8578  O  O   . PHE D  1 252 ? 17.185  4.109   -22.900 1.00 15.71 ? 252 PHE D O   1 
ATOM   8579  C  CB  . PHE D  1 252 ? 18.651  1.392   -23.687 1.00 14.51 ? 252 PHE D CB  1 
ATOM   8580  C  CG  . PHE D  1 252 ? 18.112  0.299   -24.544 1.00 16.20 ? 252 PHE D CG  1 
ATOM   8581  C  CD1 . PHE D  1 252 ? 16.752  -0.046  -24.395 1.00 19.65 ? 252 PHE D CD1 1 
ATOM   8582  C  CD2 . PHE D  1 252 ? 18.918  -0.311  -25.528 1.00 21.45 ? 252 PHE D CD2 1 
ATOM   8583  C  CE1 . PHE D  1 252 ? 16.198  -0.987  -25.262 1.00 22.09 ? 252 PHE D CE1 1 
ATOM   8584  C  CE2 . PHE D  1 252 ? 18.354  -1.279  -26.400 1.00 22.97 ? 252 PHE D CE2 1 
ATOM   8585  C  CZ  . PHE D  1 252 ? 16.999  -1.556  -26.259 1.00 20.05 ? 252 PHE D CZ  1 
ATOM   8586  N  N   . ASP D  1 253 ? 19.368  4.577   -22.978 1.00 14.40 ? 253 ASP D N   1 
ATOM   8587  C  CA  . ASP D  1 253 ? 19.201  5.685   -22.023 1.00 16.71 ? 253 ASP D CA  1 
ATOM   8588  C  C   . ASP D  1 253 ? 18.567  5.151   -20.705 1.00 16.77 ? 253 ASP D C   1 
ATOM   8589  O  O   . ASP D  1 253 ? 17.705  5.855   -20.142 1.00 19.61 ? 253 ASP D O   1 
ATOM   8590  C  CB  . ASP D  1 253 ? 18.380  6.877   -22.568 1.00 17.37 ? 253 ASP D CB  1 
ATOM   8591  C  CG  . ASP D  1 253 ? 19.099  7.560   -23.750 1.00 20.16 ? 253 ASP D CG  1 
ATOM   8592  O  OD1 . ASP D  1 253 ? 20.344  7.357   -23.943 1.00 22.01 ? 253 ASP D OD1 1 
ATOM   8593  O  OD2 . ASP D  1 253 ? 18.365  8.224   -24.509 1.00 17.60 ? 253 ASP D OD2 1 
ATOM   8594  N  N   . GLU D  1 254 ? 18.952  3.913   -20.310 1.00 16.37 ? 254 GLU D N   1 
ATOM   8595  C  CA  . GLU D  1 254 ? 18.518  3.278   -18.996 1.00 18.39 ? 254 GLU D CA  1 
ATOM   8596  C  C   . GLU D  1 254 ? 17.049  2.748   -19.025 1.00 18.50 ? 254 GLU D C   1 
ATOM   8597  O  O   . GLU D  1 254 ? 16.548  2.197   -18.026 1.00 19.69 ? 254 GLU D O   1 
ATOM   8598  C  CB  . GLU D  1 254 ? 18.744  4.194   -17.778 1.00 20.30 ? 254 GLU D CB  1 
ATOM   8599  C  CG  . GLU D  1 254 ? 20.227  4.337   -17.399 1.00 27.37 ? 254 GLU D CG  1 
ATOM   8600  C  CD  . GLU D  1 254 ? 20.348  5.541   -16.466 1.00 42.95 ? 254 GLU D CD  1 
ATOM   8601  O  OE1 . GLU D  1 254 ? 19.789  5.478   -15.340 1.00 54.85 ? 254 GLU D OE1 1 
ATOM   8602  O  OE2 . GLU D  1 254 ? 20.931  6.578   -16.857 1.00 44.89 ? 254 GLU D OE2 1 
ATOM   8603  N  N   . ARG D  1 255 ? 16.353  2.834   -20.155 1.00 14.82 ? 255 ARG D N   1 
ATOM   8604  C  CA  . ARG D  1 255 ? 15.001  2.329   -20.263 1.00 13.77 ? 255 ARG D CA  1 
ATOM   8605  C  C   . ARG D  1 255 ? 14.975  0.786   -20.319 1.00 14.97 ? 255 ARG D C   1 
ATOM   8606  O  O   . ARG D  1 255 ? 15.951  0.120   -20.832 1.00 16.27 ? 255 ARG D O   1 
ATOM   8607  C  CB  . ARG D  1 255 ? 14.401  2.788   -21.678 1.00 15.03 ? 255 ARG D CB  1 
ATOM   8608  C  CG  . ARG D  1 255 ? 14.058  4.244   -21.668 1.00 14.05 ? 255 ARG D CG  1 
ATOM   8609  C  CD  . ARG D  1 255 ? 13.571  4.571   -23.118 1.00 15.51 ? 255 ARG D CD  1 
ATOM   8610  N  NE  . ARG D  1 255 ? 14.673  4.596   -24.067 1.00 14.98 ? 255 ARG D NE  1 
ATOM   8611  C  CZ  . ARG D  1 255 ? 14.572  4.945   -25.343 1.00 15.28 ? 255 ARG D CZ  1 
ATOM   8612  N  NH1 . ARG D  1 255 ? 13.360  5.242   -25.869 1.00 12.05 ? 255 ARG D NH1 1 
ATOM   8613  N  NH2 . ARG D  1 255 ? 15.688  4.997   -26.095 1.00 13.79 ? 255 ARG D NH2 1 
ATOM   8614  N  N   . LEU D  1 256 ? 13.918  0.222   -19.674 1.00 13.57 ? 256 LEU D N   1 
ATOM   8615  C  CA  . LEU D  1 256 ? 13.533  -1.162  -19.972 1.00 13.80 ? 256 LEU D CA  1 
ATOM   8616  C  C   . LEU D  1 256 ? 12.382  -1.162  -20.944 1.00 14.19 ? 256 LEU D C   1 
ATOM   8617  O  O   . LEU D  1 256 ? 11.702  -0.116  -21.176 1.00 14.55 ? 256 LEU D O   1 
ATOM   8618  C  CB  . LEU D  1 256 ? 13.107  -1.887  -18.677 1.00 15.04 ? 256 LEU D CB  1 
ATOM   8619  C  CG  . LEU D  1 256 ? 14.227  -1.872  -17.633 1.00 14.93 ? 256 LEU D CG  1 
ATOM   8620  C  CD1 . LEU D  1 256 ? 13.627  -2.551  -16.347 1.00 19.24 ? 256 LEU D CD1 1 
ATOM   8621  C  CD2 . LEU D  1 256 ? 15.571  -2.489  -18.119 1.00 18.85 ? 256 LEU D CD2 1 
ATOM   8622  N  N   . VAL D  1 257 ? 12.159  -2.287  -21.552 1.00 12.03 ? 257 VAL D N   1 
ATOM   8623  C  CA  . VAL D  1 257 ? 10.986  -2.544  -22.396 1.00 12.51 ? 257 VAL D CA  1 
ATOM   8624  C  C   . VAL D  1 257 ? 10.153  -3.536  -21.683 1.00 12.38 ? 257 VAL D C   1 
ATOM   8625  O  O   . VAL D  1 257 ? 10.604  -4.604  -21.264 1.00 12.55 ? 257 VAL D O   1 
ATOM   8626  C  CB  . VAL D  1 257 ? 11.352  -3.144  -23.780 1.00 12.57 ? 257 VAL D CB  1 
ATOM   8627  C  CG1 . VAL D  1 257 ? 10.086  -3.528  -24.501 1.00 12.29 ? 257 VAL D CG1 1 
ATOM   8628  C  CG2 . VAL D  1 257 ? 12.159  -2.103  -24.518 1.00 11.88 ? 257 VAL D CG2 1 
ATOM   8629  N  N   . TYR D  1 258 ? 8.958   -3.166  -21.376 1.00 10.29 ? 258 TYR D N   1 
ATOM   8630  C  CA  . TYR D  1 258 ? 7.944   -4.004  -20.580 1.00 10.66 ? 258 TYR D CA  1 
ATOM   8631  C  C   . TYR D  1 258 ? 7.197   -4.876  -21.457 1.00 10.67 ? 258 TYR D C   1 
ATOM   8632  O  O   . TYR D  1 258 ? 6.793   -4.470  -22.578 1.00 11.79 ? 258 TYR D O   1 
ATOM   8633  C  CB  . TYR D  1 258 ? 7.102   -3.082  -19.674 1.00 12.25 ? 258 TYR D CB  1 
ATOM   8634  C  CG  . TYR D  1 258 ? 7.999   -2.208  -18.813 1.00 13.24 ? 258 TYR D CG  1 
ATOM   8635  C  CD1 . TYR D  1 258 ? 8.487   -2.681  -17.606 1.00 14.59 ? 258 TYR D CD1 1 
ATOM   8636  C  CD2 . TYR D  1 258 ? 8.414   -0.956  -19.243 1.00 13.59 ? 258 TYR D CD2 1 
ATOM   8637  C  CE1 . TYR D  1 258 ? 9.336   -1.931  -16.832 1.00 16.25 ? 258 TYR D CE1 1 
ATOM   8638  C  CE2 . TYR D  1 258 ? 9.271   -0.178  -18.478 1.00 17.98 ? 258 TYR D CE2 1 
ATOM   8639  C  CZ  . TYR D  1 258 ? 9.729   -0.667  -17.279 1.00 17.92 ? 258 TYR D CZ  1 
ATOM   8640  O  OH  . TYR D  1 258 ? 10.578  0.097   -16.517 1.00 20.74 ? 258 TYR D OH  1 
ATOM   8641  N  N   . THR D  1 259 ? 6.939   -6.141  -21.083 1.00 10.26 ? 259 THR D N   1 
ATOM   8642  C  CA  . THR D  1 259 ? 6.284   -7.022  -21.977 1.00 9.91  ? 259 THR D CA  1 
ATOM   8643  C  C   . THR D  1 259 ? 4.990   -7.544  -21.306 1.00 9.42  ? 259 THR D C   1 
ATOM   8644  O  O   . THR D  1 259 ? 4.908   -7.691  -20.046 1.00 10.29 ? 259 THR D O   1 
ATOM   8645  C  CB  . THR D  1 259 ? 7.118   -8.236  -22.375 1.00 10.21 ? 259 THR D CB  1 
ATOM   8646  O  OG1 . THR D  1 259 ? 7.580   -8.903  -21.178 1.00 12.21 ? 259 THR D OG1 1 
ATOM   8647  C  CG2 . THR D  1 259 ? 8.398   -7.733  -23.147 1.00 10.83 ? 259 THR D CG2 1 
ATOM   8648  N  N   . SER D  1 260 ? 3.989   -7.864  -22.087 1.00 10.64 ? 260 SER D N   1 
ATOM   8649  C  CA  . SER D  1 260 ? 2.711   -8.418  -21.554 1.00 10.12 ? 260 SER D CA  1 
ATOM   8650  C  C   . SER D  1 260 ? 2.799   -9.960  -21.548 1.00 12.19 ? 260 SER D C   1 
ATOM   8651  O  O   . SER D  1 260 ? 1.787   -10.643 -21.250 1.00 15.73 ? 260 SER D O   1 
ATOM   8652  C  CB  . SER D  1 260 ? 1.539   -7.906  -22.367 1.00 12.28 ? 260 SER D CB  1 
ATOM   8653  O  OG  . SER D  1 260 ? 1.716   -8.436  -23.678 1.00 12.15 ? 260 SER D OG  1 
ATOM   8654  N  N   . PHE D  1 261 ? 3.949   -10.532 -21.858 1.00 11.93 ? 261 PHE D N   1 
ATOM   8655  C  CA  . PHE D  1 261 ? 4.157   -11.993 -21.962 1.00 13.24 ? 261 PHE D CA  1 
ATOM   8656  C  C   . PHE D  1 261 ? 5.488   -12.260 -21.326 1.00 16.24 ? 261 PHE D C   1 
ATOM   8657  O  O   . PHE D  1 261 ? 6.328   -11.427 -21.138 1.00 15.50 ? 261 PHE D O   1 
ATOM   8658  C  CB  . PHE D  1 261 ? 4.121   -12.436 -23.448 1.00 14.50 ? 261 PHE D CB  1 
ATOM   8659  C  CG  . PHE D  1 261 ? 5.162   -11.738 -24.286 1.00 13.97 ? 261 PHE D CG  1 
ATOM   8660  C  CD1 . PHE D  1 261 ? 6.456   -12.270 -24.402 1.00 15.38 ? 261 PHE D CD1 1 
ATOM   8661  C  CD2 . PHE D  1 261 ? 4.886   -10.473 -24.918 1.00 13.55 ? 261 PHE D CD2 1 
ATOM   8662  C  CE1 . PHE D  1 261 ? 7.450   -11.641 -25.172 1.00 16.46 ? 261 PHE D CE1 1 
ATOM   8663  C  CE2 . PHE D  1 261 ? 5.955   -9.830  -25.656 1.00 12.90 ? 261 PHE D CE2 1 
ATOM   8664  C  CZ  . PHE D  1 261 ? 7.189   -10.388 -25.770 1.00 13.62 ? 261 PHE D CZ  1 
ATOM   8665  N  N   . SER D  1 262 ? 5.645   -13.534 -20.904 1.00 20.80 ? 262 SER D N   1 
ATOM   8666  C  CA  . SER D  1 262 ? 6.944   -14.092 -20.497 1.00 27.30 ? 262 SER D CA  1 
ATOM   8667  C  C   . SER D  1 262 ? 7.567   -15.035 -21.527 1.00 31.12 ? 262 SER D C   1 
ATOM   8668  O  O   . SER D  1 262 ? 8.800   -14.997 -21.810 1.00 35.18 ? 262 SER D O   1 
ATOM   8669  C  CB  . SER D  1 262 ? 6.739   -14.880 -19.234 1.00 35.58 ? 262 SER D CB  1 
ATOM   8670  O  OG  . SER D  1 262 ? 6.465   -13.954 -18.247 1.00 35.95 ? 262 SER D OG  1 
ATOM   8671  N  N   . GLN D  1 263 ? 6.670   -15.937 -21.898 1.00 41.72 ? 263 GLN D N   1 
ATOM   8672  C  CA  . GLN D  1 263 ? 6.555   -16.826 -23.056 1.00 58.69 ? 263 GLN D CA  1 
ATOM   8673  C  C   . GLN D  1 263 ? 7.767   -17.579 -23.687 1.00 68.69 ? 263 GLN D C   1 
ATOM   8674  O  O   . GLN D  1 263 ? 8.822   -17.726 -23.048 1.00 76.27 ? 263 GLN D O   1 
ATOM   8675  C  CB  . GLN D  1 263 ? 5.549   -16.232 -24.066 1.00 49.75 ? 263 GLN D CB  1 
ATOM   8676  C  CG  . GLN D  1 263 ? 4.070   -16.661 -23.905 1.00 50.77 ? 263 GLN D CG  1 
ATOM   8677  C  CD  . GLN D  1 263 ? 3.231   -15.829 -22.900 1.00 58.24 ? 263 GLN D CD  1 
ATOM   8678  O  OE1 . GLN D  1 263 ? 3.590   -15.665 -21.706 1.00 46.23 ? 263 GLN D OE1 1 
ATOM   8679  N  NE2 . GLN D  1 263 ? 2.072   -15.323 -23.380 1.00 57.11 ? 263 GLN D NE2 1 
ATOM   8680  O  OXT . GLN D  1 263 ? 7.682   -18.098 -24.817 1.00 72.60 ? 263 GLN D OXT 1 
HETATM 8681  ZN ZN  . ZN  E  2 .   ? 22.873  0.624   12.179  1.00 7.84  ? 301 ZN  A ZN  1 
HETATM 8682  C  C1  . EDO F  3 .   ? 26.280  -8.797  29.779  1.00 24.25 ? 302 EDO A C1  1 
HETATM 8683  O  O1  . EDO F  3 .   ? 25.960  -9.942  28.934  1.00 22.78 ? 302 EDO A O1  1 
HETATM 8684  C  C2  . EDO F  3 .   ? 27.151  -9.224  30.984  1.00 25.37 ? 302 EDO A C2  1 
HETATM 8685  O  O2  . EDO F  3 .   ? 28.537  -9.388  30.562  1.00 26.59 ? 302 EDO A O2  1 
HETATM 8686  C  C6  A EOQ G  4 .   ? 25.661  3.969   9.095   0.50 11.85 ? 303 EOQ A C6  1 
HETATM 8687  C  C6  B EOQ G  4 .   ? 25.663  3.981   9.100   0.50 12.94 ? 303 EOQ A C6  1 
HETATM 8688  C  C7  A EOQ G  4 .   ? 26.600  4.973   9.329   0.50 13.27 ? 303 EOQ A C7  1 
HETATM 8689  C  C7  B EOQ G  4 .   ? 26.593  4.995   9.354   0.50 14.74 ? 303 EOQ A C7  1 
HETATM 8690  C  C8  A EOQ G  4 .   ? 26.545  5.655   10.491  0.50 14.30 ? 303 EOQ A C8  1 
HETATM 8691  C  C8  B EOQ G  4 .   ? 26.546  5.686   10.531  0.50 16.60 ? 303 EOQ A C8  1 
HETATM 8692  C  C9  A EOQ G  4 .   ? 25.575  5.378   11.481  0.50 13.01 ? 303 EOQ A C9  1 
HETATM 8693  C  C9  B EOQ G  4 .   ? 25.559  5.412   11.527  0.50 15.56 ? 303 EOQ A C9  1 
HETATM 8694  C  C10 A EOQ G  4 .   ? 24.590  4.381   11.261  0.50 10.23 ? 303 EOQ A C10 1 
HETATM 8695  C  C10 B EOQ G  4 .   ? 24.610  4.383   11.270  0.50 11.79 ? 303 EOQ A C10 1 
HETATM 8696  C  C12 A EOQ G  4 .   ? 25.501  6.179   12.686  0.50 15.36 ? 303 EOQ A C12 1 
HETATM 8697  C  C12 B EOQ G  4 .   ? 25.413  6.094   12.840  0.50 19.73 ? 303 EOQ A C12 1 
HETATM 8698  C  C2  A EOQ G  4 .   ? 24.677  3.646   10.057  0.50 9.92  ? 303 EOQ A C2  1 
HETATM 8699  C  C2  B EOQ G  4 .   ? 24.684  3.652   10.062  0.50 10.99 ? 303 EOQ A C2  1 
HETATM 8700  N  N5  A EOQ G  4 .   ? 22.568  2.141   10.986  0.50 8.55  ? 303 EOQ A N5  1 
HETATM 8701  N  N5  B EOQ G  4 .   ? 22.563  2.130   10.998  0.50 9.73  ? 303 EOQ A N5  1 
HETATM 8702  C  C15 A EOQ G  4 .   ? 24.269  7.462   14.233  0.50 14.99 ? 303 EOQ A C15 1 
HETATM 8703  C  C15 B EOQ G  4 .   ? 24.039  7.047   14.662  0.50 19.68 ? 303 EOQ A C15 1 
HETATM 8704  C  C16 A EOQ G  4 .   ? 23.411  6.788   15.248  0.50 12.98 ? 303 EOQ A C16 1 
HETATM 8705  C  C16 B EOQ G  4 .   ? 23.333  8.322   14.290  0.50 22.67 ? 303 EOQ A C16 1 
HETATM 8706  O  O13 A EOQ G  4 .   ? 26.538  6.492   13.331  0.50 15.61 ? 303 EOQ A O13 1 
HETATM 8707  O  O13 B EOQ G  4 .   ? 26.437  6.349   13.523  0.50 23.31 ? 303 EOQ A O13 1 
HETATM 8708  N  N14 A EOQ G  4 .   ? 24.326  6.612   13.076  0.50 12.71 ? 303 EOQ A N14 1 
HETATM 8709  N  N14 B EOQ G  4 .   ? 24.214  6.391   13.364  0.50 17.50 ? 303 EOQ A N14 1 
HETATM 8710  O  O17 A EOQ G  4 .   ? 24.201  5.789   15.842  0.50 21.33 ? 303 EOQ A O17 1 
HETATM 8711  O  O17 B EOQ G  4 .   ? 24.207  9.365   14.333  0.50 23.96 ? 303 EOQ A O17 1 
HETATM 8712  S  S1  A EOQ G  4 .   ? 23.606  2.264   9.780   0.50 9.61  ? 303 EOQ A S1  1 
HETATM 8713  S  S1  B EOQ G  4 .   ? 23.606  2.266   9.780   0.50 10.47 ? 303 EOQ A S1  1 
HETATM 8714  O  O4  A EOQ G  4 .   ? 22.853  2.463   8.534   0.50 8.22  ? 303 EOQ A O4  1 
HETATM 8715  O  O4  B EOQ G  4 .   ? 22.853  2.466   8.532   0.50 8.99  ? 303 EOQ A O4  1 
HETATM 8716  O  O3  A EOQ G  4 .   ? 24.510  1.085   9.804   0.50 8.81  ? 303 EOQ A O3  1 
HETATM 8717  O  O3  B EOQ G  4 .   ? 24.511  1.084   9.800   0.50 9.54  ? 303 EOQ A O3  1 
HETATM 8718  CL CL1 A EOQ G  4 .   ? 25.863  3.168   7.603   0.50 12.71 ? 303 EOQ A CL1 1 
HETATM 8719  CL CL1 B EOQ G  4 .   ? 25.861  3.171   7.603   0.50 12.82 ? 303 EOQ A CL1 1 
HETATM 8720  N  N18 A EOQ G  4 .   ? 27.525  6.691   10.646  0.50 18.55 ? 303 EOQ A N18 1 
HETATM 8721  N  N18 B EOQ G  4 .   ? 27.537  6.713   10.658  0.50 20.20 ? 303 EOQ A N18 1 
HETATM 8722  C  C19 A EOQ G  4 .   ? 28.368  7.040   9.499   0.50 22.94 ? 303 EOQ A C19 1 
HETATM 8723  C  C19 B EOQ G  4 .   ? 28.378  7.053   9.505   0.50 23.75 ? 303 EOQ A C19 1 
HETATM 8724  C  C20 A EOQ G  4 .   ? 29.036  8.358   9.710   0.50 28.30 ? 303 EOQ A C20 1 
HETATM 8725  C  C20 B EOQ G  4 .   ? 29.070  8.361   9.714   0.50 28.18 ? 303 EOQ A C20 1 
HETATM 8726  C  C22 A EOQ G  4 .   ? 28.392  9.582   9.421   0.50 33.01 ? 303 EOQ A C22 1 
HETATM 8727  C  C22 B EOQ G  4 .   ? 28.448  9.593   9.415   0.50 32.50 ? 303 EOQ A C22 1 
HETATM 8728  C  C25 A EOQ G  4 .   ? 29.091  10.784  9.670   0.50 35.87 ? 303 EOQ A C25 1 
HETATM 8729  C  C25 B EOQ G  4 .   ? 29.164  10.784  9.661   0.50 34.62 ? 303 EOQ A C25 1 
HETATM 8730  C  C24 A EOQ G  4 .   ? 30.393  10.749  10.212  0.50 31.35 ? 303 EOQ A C24 1 
HETATM 8731  C  C24 B EOQ G  4 .   ? 30.461  10.729  10.211  0.50 29.36 ? 303 EOQ A C24 1 
HETATM 8732  C  C23 A EOQ G  4 .   ? 31.036  9.545   10.496  0.50 29.25 ? 303 EOQ A C23 1 
HETATM 8733  C  C23 B EOQ G  4 .   ? 31.088  9.520   10.504  0.50 27.12 ? 303 EOQ A C23 1 
HETATM 8734  C  C21 A EOQ G  4 .   ? 30.334  8.344   10.254  0.50 29.31 ? 303 EOQ A C21 1 
HETATM 8735  C  C21 B EOQ G  4 .   ? 30.365  8.330   10.266  0.50 28.37 ? 303 EOQ A C21 1 
HETATM 8736  ZN ZN  . ZN  H  2 .   ? -8.147  3.674   4.876   1.00 6.70  ? 301 ZN  B ZN  1 
HETATM 8737  C  C1  . EDO I  3 .   ? -17.251 -3.327  22.855  1.00 25.31 ? 302 EDO B C1  1 
HETATM 8738  O  O1  . EDO I  3 .   ? -16.114 -2.417  22.885  1.00 26.32 ? 302 EDO B O1  1 
HETATM 8739  C  C2  . EDO I  3 .   ? -17.632 -3.628  21.402  1.00 20.88 ? 302 EDO B C2  1 
HETATM 8740  O  O2  . EDO I  3 .   ? -16.511 -3.717  20.415  1.00 17.72 ? 302 EDO B O2  1 
HETATM 8741  C  C1  . EDO J  3 .   ? -13.653 -5.884  -12.173 1.00 24.99 ? 303 EDO B C1  1 
HETATM 8742  O  O1  . EDO J  3 .   ? -13.567 -6.998  -11.250 1.00 18.37 ? 303 EDO B O1  1 
HETATM 8743  C  C2  . EDO J  3 .   ? -14.693 -6.024  -13.277 1.00 26.61 ? 303 EDO B C2  1 
HETATM 8744  O  O2  . EDO J  3 .   ? -16.038 -5.909  -12.707 1.00 24.70 ? 303 EDO B O2  1 
HETATM 8745  C  C1  . EDO K  3 .   ? -30.328 8.586   -4.099  1.00 40.23 ? 304 EDO B C1  1 
HETATM 8746  O  O1  . EDO K  3 .   ? -30.711 7.155   -4.225  1.00 24.11 ? 304 EDO B O1  1 
HETATM 8747  C  C2  . EDO K  3 .   ? -29.085 9.097   -4.909  1.00 40.72 ? 304 EDO B C2  1 
HETATM 8748  O  O2  . EDO K  3 .   ? -29.332 9.578   -6.284  1.00 37.13 ? 304 EDO B O2  1 
HETATM 8749  C  C6  . EOQ L  4 .   ? -10.143 7.608   7.831   1.00 10.69 ? 305 EOQ B C6  1 
HETATM 8750  C  C7  . EOQ L  4 .   ? -10.912 8.727   7.551   1.00 12.01 ? 305 EOQ B C7  1 
HETATM 8751  C  C8  . EOQ L  4 .   ? -10.779 9.292   6.346   1.00 14.55 ? 305 EOQ B C8  1 
HETATM 8752  C  C9  . EOQ L  4 .   ? -9.935  8.808   5.346   1.00 12.36 ? 305 EOQ B C9  1 
HETATM 8753  C  C10 . EOQ L  4 .   ? -9.172  7.669   5.650   1.00 10.27 ? 305 EOQ B C10 1 
HETATM 8754  C  C12 . EOQ L  4 .   ? -9.736  9.424   4.080   1.00 15.98 ? 305 EOQ B C12 1 
HETATM 8755  C  C2  . EOQ L  4 .   ? -9.253  7.069   6.880   1.00 9.16  ? 305 EOQ B C2  1 
HETATM 8756  N  N5  . EOQ L  4 .   ? -7.579  5.125   5.923   1.00 7.69  ? 305 EOQ B N5  1 
HETATM 8757  C  C15 . EOQ L  4 .   ? -8.400  10.447  2.485   1.00 18.93 ? 305 EOQ B C15 1 
HETATM 8758  C  C16 . EOQ L  4 .   ? -7.706  9.701   1.527   1.00 16.18 ? 305 EOQ B C16 1 
HETATM 8759  O  O13 . EOQ L  4 .   ? -10.710 9.856   3.464   1.00 19.66 ? 305 EOQ B O13 1 
HETATM 8760  N  N14 . EOQ L  4 .   ? -8.478  9.617   3.705   1.00 13.25 ? 305 EOQ B N14 1 
HETATM 8761  O  O17 . EOQ L  4 .   ? -8.312  8.540   1.014   1.00 21.61 ? 305 EOQ B O17 1 
HETATM 8762  S  S1  . EOQ L  4 .   ? -8.444  5.498   7.219   1.00 7.89  ? 305 EOQ B S1  1 
HETATM 8763  O  O4  . EOQ L  4 .   ? -7.625  5.679   8.401   1.00 8.00  ? 305 EOQ B O4  1 
HETATM 8764  O  O3  . EOQ L  4 .   ? -9.542  4.546   7.333   1.00 7.80  ? 305 EOQ B O3  1 
HETATM 8765  CL CL1 . EOQ L  4 .   ? -10.376 6.942   9.400   1.00 11.62 ? 305 EOQ B CL1 1 
HETATM 8766  N  N18 . EOQ L  4 .   ? -11.555 10.450  6.054   1.00 19.15 ? 305 EOQ B N18 1 
HETATM 8767  C  C19 . EOQ L  4 .   ? -12.781 10.751  6.804   1.00 25.94 ? 305 EOQ B C19 1 
HETATM 8768  C  C20 . EOQ L  4 .   ? -12.561 12.144  7.141   1.00 25.94 ? 305 EOQ B C20 1 
HETATM 8769  C  C22 . EOQ L  4 .   ? -11.371 12.556  7.758   1.00 33.53 ? 305 EOQ B C22 1 
HETATM 8770  C  C25 . EOQ L  4 .   ? -11.151 13.909  8.028   1.00 33.81 ? 305 EOQ B C25 1 
HETATM 8771  C  C24 . EOQ L  4 .   ? -12.115 14.851  7.578   1.00 33.83 ? 305 EOQ B C24 1 
HETATM 8772  C  C23 . EOQ L  4 .   ? -13.318 14.431  6.925   1.00 36.42 ? 305 EOQ B C23 1 
HETATM 8773  C  C21 . EOQ L  4 .   ? -13.541 13.036  6.688   1.00 32.06 ? 305 EOQ B C21 1 
HETATM 8774  ZN ZN  . ZN  M  2 .   ? 37.570  2.666   -30.809 1.00 9.66  ? 301 ZN  C ZN  1 
HETATM 8775  C  C1  . EDO N  3 .   ? 46.611  -7.140  -46.204 1.00 24.40 ? 302 EDO C C1  1 
HETATM 8776  O  O1  . EDO N  3 .   ? 45.401  -6.916  -45.397 1.00 16.57 ? 302 EDO C O1  1 
HETATM 8777  C  C2  . EDO N  3 .   ? 46.373  -6.751  -47.663 1.00 26.30 ? 302 EDO C C2  1 
HETATM 8778  O  O2  . EDO N  3 .   ? 45.528  -5.586  -47.878 1.00 30.29 ? 302 EDO C O2  1 
HETATM 8779  C  C1  . EDO O  3 .   ? 52.240  -12.923 -36.569 1.00 34.62 ? 303 EDO C C1  1 
HETATM 8780  O  O1  . EDO O  3 .   ? 51.337  -12.866 -37.724 1.00 38.91 ? 303 EDO C O1  1 
HETATM 8781  C  C2  . EDO O  3 .   ? 52.801  -11.512 -36.297 1.00 24.60 ? 303 EDO C C2  1 
HETATM 8782  O  O2  . EDO O  3 .   ? 53.699  -11.036 -37.249 1.00 33.58 ? 303 EDO C O2  1 
HETATM 8783  C  C1  . EDO P  3 .   ? 51.581  9.124   -29.724 1.00 17.24 ? 304 EDO C C1  1 
HETATM 8784  O  O1  . EDO P  3 .   ? 51.456  8.414   -31.052 1.00 17.16 ? 304 EDO C O1  1 
HETATM 8785  C  C2  . EDO P  3 .   ? 50.740  8.553   -28.551 1.00 18.34 ? 304 EDO C C2  1 
HETATM 8786  O  O2  . EDO P  3 .   ? 51.361  7.278   -28.325 1.00 18.23 ? 304 EDO C O2  1 
HETATM 8787  C  C6  . EOQ Q  4 .   ? 40.450  5.980   -33.901 1.00 12.12 ? 305 EOQ C C6  1 
HETATM 8788  C  C7  . EOQ Q  4 .   ? 41.395  7.017   -33.709 1.00 14.06 ? 305 EOQ C C7  1 
HETATM 8789  C  C8  . EOQ Q  4 .   ? 41.285  7.766   -32.591 1.00 14.61 ? 305 EOQ C C8  1 
HETATM 8790  C  C9  . EOQ Q  4 .   ? 40.304  7.485   -31.622 1.00 13.26 ? 305 EOQ C C9  1 
HETATM 8791  C  C10 . EOQ Q  4 .   ? 39.384  6.396   -31.799 1.00 12.11 ? 305 EOQ C C10 1 
HETATM 8792  C  C12 . EOQ Q  4 .   ? 40.200  8.285   -30.374 1.00 15.79 ? 305 EOQ C C12 1 
HETATM 8793  C  C2  . EOQ Q  4 .   ? 39.444  5.641   -33.002 1.00 10.77 ? 305 EOQ C C2  1 
HETATM 8794  N  N5  . EOQ Q  4 .   ? 37.286  4.176   -32.045 1.00 10.10 ? 305 EOQ C N5  1 
HETATM 8795  C  C15 . EOQ Q  4 .   ? 38.838  9.474   -28.772 1.00 17.93 ? 305 EOQ C C15 1 
HETATM 8796  C  C16 . EOQ Q  4 .   ? 37.998  8.876   -27.708 1.00 22.75 ? 305 EOQ C C16 1 
HETATM 8797  O  O13 . EOQ Q  4 .   ? 41.198  8.641   -29.732 1.00 17.06 ? 305 EOQ C O13 1 
HETATM 8798  N  N14 . EOQ Q  4 .   ? 39.000  8.624   -29.958 1.00 14.33 ? 305 EOQ C N14 1 
HETATM 8799  O  O17 . EOQ Q  4 .   ? 38.697  7.818   -27.072 1.00 32.80 ? 305 EOQ C O17 1 
HETATM 8800  S  S1  . EOQ Q  4 .   ? 38.371  4.249   -33.210 1.00 11.32 ? 305 EOQ C S1  1 
HETATM 8801  O  O4  . EOQ Q  4 .   ? 37.637  4.444   -34.451 1.00 10.00 ? 305 EOQ C O4  1 
HETATM 8802  O  O3  . EOQ Q  4 .   ? 39.223  3.113   -33.174 1.00 9.98  ? 305 EOQ C O3  1 
HETATM 8803  CL CL1 . EOQ Q  4 .   ? 40.600  5.102   -35.394 1.00 12.74 ? 305 EOQ C CL1 1 
HETATM 8804  N  N18 . EOQ Q  4 .   ? 42.209  8.812   -32.428 1.00 15.58 ? 305 EOQ C N18 1 
HETATM 8805  C  C19 . EOQ Q  4 .   ? 43.135  9.058   -33.543 1.00 19.30 ? 305 EOQ C C19 1 
HETATM 8806  C  C20 . EOQ Q  4 .   ? 43.743  10.436  -33.234 1.00 20.66 ? 305 EOQ C C20 1 
HETATM 8807  C  C22 . EOQ Q  4 .   ? 43.019  11.639  -33.568 1.00 24.19 ? 305 EOQ C C22 1 
HETATM 8808  C  C25 . EOQ Q  4 .   ? 43.583  12.919  -33.289 1.00 26.32 ? 305 EOQ C C25 1 
HETATM 8809  C  C24 . EOQ Q  4 .   ? 44.837  12.890  -32.690 1.00 23.33 ? 305 EOQ C C24 1 
HETATM 8810  C  C23 . EOQ Q  4 .   ? 45.586  11.751  -32.397 1.00 21.81 ? 305 EOQ C C23 1 
HETATM 8811  C  C21 . EOQ Q  4 .   ? 45.027  10.471  -32.680 1.00 25.00 ? 305 EOQ C C21 1 
HETATM 8812  ZN ZN  . ZN  R  2 .   ? 6.794   5.655   -38.340 1.00 7.20  ? 301 ZN  D ZN  1 
HETATM 8813  C  C1  . EDO S  3 .   ? -2.099  -1.107  -20.146 1.00 25.54 ? 302 EDO D C1  1 
HETATM 8814  O  O1  . EDO S  3 .   ? -1.169  0.040   -20.177 1.00 34.88 ? 302 EDO D O1  1 
HETATM 8815  C  C2  . EDO S  3 .   ? -2.621  -1.429  -21.561 1.00 24.82 ? 302 EDO D C2  1 
HETATM 8816  O  O2  . EDO S  3 .   ? -1.549  -1.414  -22.571 1.00 22.20 ? 302 EDO D O2  1 
HETATM 8817  C  C1  . EDO T  3 .   ? 13.912  -12.556 -37.686 1.00 49.75 ? 303 EDO D C1  1 
HETATM 8818  O  O1  . EDO T  3 .   ? 13.203  -12.648 -36.459 1.00 54.31 ? 303 EDO D O1  1 
HETATM 8819  C  C2  . EDO T  3 .   ? 13.628  -11.184 -38.286 1.00 44.84 ? 303 EDO D C2  1 
HETATM 8820  O  O2  . EDO T  3 .   ? 14.020  -11.171 -39.670 1.00 37.44 ? 303 EDO D O2  1 
HETATM 8821  C  C1  . EDO U  3 .   ? 12.367  -11.741 -41.731 1.00 34.39 ? 304 EDO D C1  1 
HETATM 8822  O  O1  . EDO U  3 .   ? 11.808  -12.276 -40.504 1.00 45.70 ? 304 EDO D O1  1 
HETATM 8823  C  C2  . EDO U  3 .   ? 11.621  -10.439 -42.132 1.00 28.96 ? 304 EDO D C2  1 
HETATM 8824  O  O2  . EDO U  3 .   ? 11.266  -10.415 -43.552 1.00 17.88 ? 304 EDO D O2  1 
HETATM 8825  C  C1  . EDO V  3 .   ? 14.835  -12.693 -47.565 1.00 38.45 ? 305 EDO D C1  1 
HETATM 8826  O  O1  . EDO V  3 .   ? 14.361  -11.324 -47.422 1.00 29.53 ? 305 EDO D O1  1 
HETATM 8827  C  C2  . EDO V  3 .   ? 15.574  -13.092 -46.287 1.00 48.96 ? 305 EDO D C2  1 
HETATM 8828  O  O2  . EDO V  3 .   ? 16.924  -13.416 -46.644 1.00 50.77 ? 305 EDO D O2  1 
HETATM 8829  C  C1  . EDO W  3 .   ? -0.506  -3.970  -56.170 1.00 38.61 ? 306 EDO D C1  1 
HETATM 8830  O  O1  . EDO W  3 .   ? -1.927  -4.059  -55.760 1.00 30.62 ? 306 EDO D O1  1 
HETATM 8831  C  C2  . EDO W  3 .   ? 0.497   -3.840  -54.982 1.00 27.59 ? 306 EDO D C2  1 
HETATM 8832  O  O2  . EDO W  3 .   ? 1.020   -5.079  -54.362 1.00 22.04 ? 306 EDO D O2  1 
HETATM 8833  C  C6  . EOQ X  4 .   ? 4.880   9.606   -35.290 1.00 8.46  ? 307 EOQ D C6  1 
HETATM 8834  C  C7  . EOQ X  4 .   ? 4.149   10.733  -35.525 1.00 10.19 ? 307 EOQ D C7  1 
HETATM 8835  C  C8  . EOQ X  4 .   ? 4.245   11.397  -36.719 1.00 10.76 ? 307 EOQ D C8  1 
HETATM 8836  C  C9  . EOQ X  4 .   ? 5.060   10.931  -37.734 1.00 10.22 ? 307 EOQ D C9  1 
HETATM 8837  C  C10 . EOQ X  4 .   ? 5.778   9.760   -37.492 1.00 9.44  ? 307 EOQ D C10 1 
HETATM 8838  C  C12 . EOQ X  4 .   ? 5.239   11.560  -39.034 1.00 11.53 ? 307 EOQ D C12 1 
HETATM 8839  C  C2  . EOQ X  4 .   ? 5.734   9.098   -36.267 1.00 8.28  ? 307 EOQ D C2  1 
HETATM 8840  N  N5  . EOQ X  4 .   ? 7.391   7.177   -37.320 1.00 7.49  ? 307 EOQ D N5  1 
HETATM 8841  C  C15 . EOQ X  4 .   ? 6.673   12.441  -40.761 1.00 14.30 ? 307 EOQ D C15 1 
HETATM 8842  C  C16 . EOQ X  4 .   ? 7.441   11.669  -41.687 1.00 15.56 ? 307 EOQ D C16 1 
HETATM 8843  O  O13 . EOQ X  4 .   ? 4.233   12.054  -39.586 1.00 13.39 ? 307 EOQ D O13 1 
HETATM 8844  N  N14 . EOQ X  4 .   ? 6.452   11.676  -39.488 1.00 11.23 ? 307 EOQ D N14 1 
HETATM 8845  O  O17 . EOQ X  4 .   ? 6.656   10.612  -42.239 1.00 20.87 ? 307 EOQ D O17 1 
HETATM 8846  S  S1  . EOQ X  4 .   ? 6.528   7.499   -36.007 1.00 8.30  ? 307 EOQ D S1  1 
HETATM 8847  O  O4  . EOQ X  4 .   ? 7.383   7.642   -34.832 1.00 8.07  ? 307 EOQ D O4  1 
HETATM 8848  O  O3  . EOQ X  4 .   ? 5.406   6.569   -35.889 1.00 7.66  ? 307 EOQ D O3  1 
HETATM 8849  CL CL1 . EOQ X  4 .   ? 4.705   8.912   -33.725 1.00 9.75  ? 307 EOQ D CL1 1 
HETATM 8850  N  N18 . EOQ X  4 .   ? 3.529   12.599  -36.947 1.00 12.23 ? 307 EOQ D N18 1 
HETATM 8851  C  C19 . EOQ X  4 .   ? 2.744   13.193  -35.835 1.00 14.57 ? 307 EOQ D C19 1 
HETATM 8852  C  C20 . EOQ X  4 .   ? 2.458   14.617  -36.218 1.00 18.03 ? 307 EOQ D C20 1 
HETATM 8853  C  C22 . EOQ X  4 .   ? 3.418   15.655  -36.022 1.00 19.10 ? 307 EOQ D C22 1 
HETATM 8854  C  C25 . EOQ X  4 .   ? 2.993   16.977  -36.438 1.00 22.09 ? 307 EOQ D C25 1 
HETATM 8855  C  C24 . EOQ X  4 .   ? 1.690   17.066  -37.005 1.00 20.96 ? 307 EOQ D C24 1 
HETATM 8856  C  C23 . EOQ X  4 .   ? 0.700   16.061  -37.081 1.00 22.11 ? 307 EOQ D C23 1 
HETATM 8857  C  C21 . EOQ X  4 .   ? 1.161   14.769  -36.651 1.00 20.24 ? 307 EOQ D C21 1 
HETATM 8858  O  O   . HOH Y  5 .   ? 4.752   -0.411  -8.447  1.00 30.43 ? 401 HOH A O   1 
HETATM 8859  O  O   . HOH Y  5 .   ? 41.055  -4.386  0.452   1.00 31.89 ? 402 HOH A O   1 
HETATM 8860  O  O   . HOH Y  5 .   ? 28.507  8.892   17.393  1.00 34.79 ? 403 HOH A O   1 
HETATM 8861  O  O   . HOH Y  5 .   ? 18.036  12.501  20.809  1.00 27.77 ? 404 HOH A O   1 
HETATM 8862  O  O   . HOH Y  5 .   ? 19.686  12.020  24.078  1.00 27.04 ? 405 HOH A O   1 
HETATM 8863  O  O   . HOH Y  5 .   ? 18.278  -3.194  -5.824  1.00 28.51 ? 406 HOH A O   1 
HETATM 8864  O  O   . HOH Y  5 .   ? 23.999  10.717  12.321  1.00 36.13 ? 407 HOH A O   1 
HETATM 8865  O  O   . HOH Y  5 .   ? 6.094   -4.076  -8.097  1.00 32.41 ? 408 HOH A O   1 
HETATM 8866  O  O   . HOH Y  5 .   ? 42.463  -0.470  5.665   1.00 33.08 ? 409 HOH A O   1 
HETATM 8867  O  O   . HOH Y  5 .   ? 10.840  12.335  20.325  1.00 22.87 ? 410 HOH A O   1 
HETATM 8868  O  O   . HOH Y  5 .   ? 25.149  11.637  19.194  1.00 35.70 ? 411 HOH A O   1 
HETATM 8869  O  O   . HOH Y  5 .   ? 23.102  3.666   15.092  1.00 21.87 ? 412 HOH A O   1 
HETATM 8870  O  O   . HOH Y  5 .   ? 15.304  16.800  30.687  1.00 36.06 ? 413 HOH A O   1 
HETATM 8871  O  O   . HOH Y  5 .   ? 40.184  -3.928  -2.148  1.00 29.70 ? 414 HOH A O   1 
HETATM 8872  O  O   . HOH Y  5 .   ? 42.704  -10.293 18.968  1.00 28.03 ? 415 HOH A O   1 
HETATM 8873  O  O   . HOH Y  5 .   ? 43.786  -4.659  12.841  1.00 22.23 ? 416 HOH A O   1 
HETATM 8874  O  O   . HOH Y  5 .   ? 19.818  14.011  28.405  1.00 21.05 ? 417 HOH A O   1 
HETATM 8875  O  O   . HOH Y  5 .   ? 41.595  5.883   5.320   1.00 28.54 ? 418 HOH A O   1 
HETATM 8876  O  O   . HOH Y  5 .   ? 14.392  -9.919  25.985  1.00 14.22 ? 419 HOH A O   1 
HETATM 8877  O  O   . HOH Y  5 .   ? 8.534   -14.381 13.705  1.00 35.01 ? 420 HOH A O   1 
HETATM 8878  O  O   . HOH Y  5 .   ? 17.832  3.179   12.755  1.00 9.63  ? 421 HOH A O   1 
HETATM 8879  O  O   . HOH Y  5 .   ? 34.402  3.573   31.438  1.00 24.51 ? 422 HOH A O   1 
HETATM 8880  O  O   . HOH Y  5 .   ? 45.125  -4.483  7.678   1.00 27.86 ? 423 HOH A O   1 
HETATM 8881  O  O   . HOH Y  5 .   ? 22.859  15.269  13.026  1.00 35.21 ? 424 HOH A O   1 
HETATM 8882  O  O   . HOH Y  5 .   ? 18.645  20.425  8.294   1.00 27.06 ? 425 HOH A O   1 
HETATM 8883  O  O   . HOH Y  5 .   ? 23.359  11.787  14.788  1.00 34.12 ? 426 HOH A O   1 
HETATM 8884  O  O   . HOH Y  5 .   ? 27.706  -21.673 1.776   1.00 29.89 ? 427 HOH A O   1 
HETATM 8885  O  O   . HOH Y  5 .   ? 36.775  6.192   11.656  1.00 25.72 ? 428 HOH A O   1 
HETATM 8886  O  O   . HOH Y  5 .   ? 4.762   1.253   -10.962 1.00 45.06 ? 429 HOH A O   1 
HETATM 8887  O  O   . HOH Y  5 .   ? 47.176  -3.684  10.206  1.00 24.11 ? 430 HOH A O   1 
HETATM 8888  O  O   . HOH Y  5 .   ? 17.025  0.627   -0.622  1.00 16.61 ? 431 HOH A O   1 
HETATM 8889  O  O   . HOH Y  5 .   ? 30.612  14.350  10.482  1.00 42.69 ? 432 HOH A O   1 
HETATM 8890  O  O   . HOH Y  5 .   ? 6.397   15.798  15.757  1.00 29.93 ? 433 HOH A O   1 
HETATM 8891  O  O   . HOH Y  5 .   ? 7.723   -8.263  11.788  1.00 22.03 ? 434 HOH A O   1 
HETATM 8892  O  O   . HOH Y  5 .   ? 37.220  10.065  23.930  1.00 35.54 ? 435 HOH A O   1 
HETATM 8893  O  O   . HOH Y  5 .   ? 41.672  -8.703  24.308  1.00 41.49 ? 436 HOH A O   1 
HETATM 8894  O  O   . HOH Y  5 .   ? 19.357  9.719   32.117  1.00 19.26 ? 437 HOH A O   1 
HETATM 8895  O  O   . HOH Y  5 .   ? 35.891  -14.904 4.066   1.00 33.74 ? 438 HOH A O   1 
HETATM 8896  O  O   . HOH Y  5 .   ? 33.770  -13.517 26.512  1.00 25.15 ? 439 HOH A O   1 
HETATM 8897  O  O   . HOH Y  5 .   ? 13.630  16.301  11.801  1.00 15.11 ? 440 HOH A O   1 
HETATM 8898  O  O   . HOH Y  5 .   ? 17.979  -15.145 6.097   1.00 17.39 ? 441 HOH A O   1 
HETATM 8899  O  O   . HOH Y  5 .   ? 42.051  2.506   29.075  1.00 23.83 ? 442 HOH A O   1 
HETATM 8900  O  O   . HOH Y  5 .   ? 10.955  3.249   19.065  1.00 22.07 ? 443 HOH A O   1 
HETATM 8901  O  O   . HOH Y  5 .   ? 27.987  3.883   33.398  1.00 25.02 ? 444 HOH A O   1 
HETATM 8902  O  O   . HOH Y  5 .   ? 9.183   11.460  1.043   1.00 14.12 ? 445 HOH A O   1 
HETATM 8903  O  O   . HOH Y  5 .   ? 5.837   -3.493  20.842  1.00 24.03 ? 446 HOH A O   1 
HETATM 8904  O  O   . HOH Y  5 .   ? 24.345  -11.632 30.211  1.00 25.19 ? 447 HOH A O   1 
HETATM 8905  O  O   . HOH Y  5 .   ? 11.578  9.991   23.026  1.00 25.99 ? 448 HOH A O   1 
HETATM 8906  O  O   . HOH Y  5 .   ? 11.007  -4.575  -5.207  1.00 38.82 ? 449 HOH A O   1 
HETATM 8907  O  O   . HOH Y  5 .   ? 27.528  -2.570  -6.589  1.00 41.76 ? 450 HOH A O   1 
HETATM 8908  O  O   . HOH Y  5 .   ? 34.780  -11.278 -3.319  1.00 35.56 ? 451 HOH A O   1 
HETATM 8909  O  O   . HOH Y  5 .   ? 10.376  -3.476  2.657   1.00 13.99 ? 452 HOH A O   1 
HETATM 8910  O  O   . HOH Y  5 .   ? 12.631  -12.322 16.432  1.00 19.38 ? 453 HOH A O   1 
HETATM 8911  O  O   . HOH Y  5 .   ? 31.375  5.580   32.423  1.00 21.66 ? 454 HOH A O   1 
HETATM 8912  O  O   . HOH Y  5 .   ? 39.087  -3.764  -7.714  1.00 33.60 ? 455 HOH A O   1 
HETATM 8913  O  O   . HOH Y  5 .   ? 22.504  7.248   -4.161  1.00 31.74 ? 456 HOH A O   1 
HETATM 8914  O  O   . HOH Y  5 .   ? 36.120  -7.075  26.365  1.00 19.20 ? 457 HOH A O   1 
HETATM 8915  O  O   . HOH Y  5 .   ? 34.820  0.321   -9.172  1.00 32.09 ? 458 HOH A O   1 
HETATM 8916  O  O   . HOH Y  5 .   ? 10.498  6.182   15.339  1.00 11.91 ? 459 HOH A O   1 
HETATM 8917  O  O   . HOH Y  5 .   ? 33.027  -14.999 3.536   1.00 22.17 ? 460 HOH A O   1 
HETATM 8918  O  O   . HOH Y  5 .   ? 42.821  9.528   5.620   1.00 35.60 ? 461 HOH A O   1 
HETATM 8919  O  O   . HOH Y  5 .   ? 10.210  4.696   8.728   1.00 11.05 ? 462 HOH A O   1 
HETATM 8920  O  O   . HOH Y  5 .   ? 26.035  11.132  30.859  1.00 20.03 ? 463 HOH A O   1 
HETATM 8921  O  O   . HOH Y  5 .   ? 13.837  1.629   -0.280  1.00 20.01 ? 464 HOH A O   1 
HETATM 8922  O  O   . HOH Y  5 .   ? 9.834   -14.724 1.606   1.00 27.28 ? 465 HOH A O   1 
HETATM 8923  O  O   . HOH Y  5 .   ? 28.488  2.332   -1.323  1.00 24.84 ? 466 HOH A O   1 
HETATM 8924  O  O   . HOH Y  5 .   ? 25.455  -18.588 12.344  1.00 21.12 ? 467 HOH A O   1 
HETATM 8925  O  O   . HOH Y  5 .   ? 5.202   16.010  13.457  1.00 22.70 ? 468 HOH A O   1 
HETATM 8926  O  O   . HOH Y  5 .   ? 9.407   -5.155  16.621  1.00 25.74 ? 469 HOH A O   1 
HETATM 8927  O  O   . HOH Y  5 .   ? 38.479  6.156   18.886  1.00 32.11 ? 470 HOH A O   1 
HETATM 8928  O  O   . HOH Y  5 .   ? 37.187  7.505   29.984  1.00 24.83 ? 471 HOH A O   1 
HETATM 8929  O  O   . HOH Y  5 .   ? 42.495  5.471   -4.935  1.00 27.98 ? 472 HOH A O   1 
HETATM 8930  O  O   . HOH Y  5 .   ? 15.014  -15.997 14.982  1.00 20.23 ? 473 HOH A O   1 
HETATM 8931  O  O   . HOH Y  5 .   ? 12.533  14.514  2.267   1.00 13.17 ? 474 HOH A O   1 
HETATM 8932  O  O   . HOH Y  5 .   ? 39.509  -12.772 19.813  1.00 22.18 ? 475 HOH A O   1 
HETATM 8933  O  O   . HOH Y  5 .   ? 15.145  -6.860  21.009  1.00 10.19 ? 476 HOH A O   1 
HETATM 8934  O  O   . HOH Y  5 .   ? 28.447  -4.236  2.476   1.00 10.16 ? 477 HOH A O   1 
HETATM 8935  O  O   . HOH Y  5 .   ? 29.056  -16.919 14.791  1.00 26.10 ? 478 HOH A O   1 
HETATM 8936  O  O   . HOH Y  5 .   ? 11.277  5.203   2.162   1.00 11.11 ? 479 HOH A O   1 
HETATM 8937  O  O   . HOH Y  5 .   ? 5.500   -12.091 13.282  1.00 16.35 ? 480 HOH A O   1 
HETATM 8938  O  O   . HOH Y  5 .   ? 11.069  -5.203  0.647   1.00 23.06 ? 481 HOH A O   1 
HETATM 8939  O  O   . HOH Y  5 .   ? 36.683  -4.480  -0.902  1.00 16.95 ? 482 HOH A O   1 
HETATM 8940  O  O   . HOH Y  5 .   ? 30.340  -8.860  -2.640  1.00 17.55 ? 483 HOH A O   1 
HETATM 8941  O  O   . HOH Y  5 .   ? 30.983  -20.971 8.481   1.00 29.73 ? 484 HOH A O   1 
HETATM 8942  O  O   . HOH Y  5 .   ? 26.561  5.324   -3.804  1.00 30.74 ? 485 HOH A O   1 
HETATM 8943  O  O   . HOH Y  5 .   ? 29.666  -15.760 -1.805  1.00 20.33 ? 486 HOH A O   1 
HETATM 8944  O  O   . HOH Y  5 .   ? 39.626  -12.166 23.050  1.00 30.77 ? 487 HOH A O   1 
HETATM 8945  O  O   . HOH Y  5 .   ? 42.028  2.267   0.903   1.00 15.17 ? 488 HOH A O   1 
HETATM 8946  O  O   . HOH Y  5 .   ? 12.013  -10.450 27.324  1.00 15.63 ? 489 HOH A O   1 
HETATM 8947  O  O   . HOH Y  5 .   ? 9.976   -2.625  27.495  1.00 41.73 ? 490 HOH A O   1 
HETATM 8948  O  O   . HOH Y  5 .   ? 38.676  -5.732  -3.171  1.00 25.33 ? 491 HOH A O   1 
HETATM 8949  O  O   . HOH Y  5 .   ? 16.578  -18.465 12.424  1.00 32.04 ? 492 HOH A O   1 
HETATM 8950  O  O   . HOH Y  5 .   ? 19.339  14.100  5.100   1.00 11.23 ? 493 HOH A O   1 
HETATM 8951  O  O   . HOH Y  5 .   ? 39.855  -12.308 11.620  1.00 18.85 ? 494 HOH A O   1 
HETATM 8952  O  O   . HOH Y  5 .   ? 20.636  17.735  7.681   1.00 30.76 ? 495 HOH A O   1 
HETATM 8953  O  O   . HOH Y  5 .   ? 37.984  -7.777  24.395  1.00 20.99 ? 496 HOH A O   1 
HETATM 8954  O  O   . HOH Y  5 .   ? 32.691  6.758   12.896  1.00 26.31 ? 497 HOH A O   1 
HETATM 8955  O  O   . HOH Y  5 .   ? 39.195  -15.920 16.839  1.00 28.68 ? 498 HOH A O   1 
HETATM 8956  O  O   . HOH Y  5 .   ? 32.715  6.843   15.593  1.00 31.21 ? 499 HOH A O   1 
HETATM 8957  O  O   . HOH Y  5 .   ? 27.685  7.732   15.536  1.00 32.78 ? 500 HOH A O   1 
HETATM 8958  O  O   . HOH Y  5 .   ? 34.231  1.214   -6.153  1.00 30.97 ? 501 HOH A O   1 
HETATM 8959  O  O   . HOH Y  5 .   ? 24.666  -23.333 10.458  1.00 35.93 ? 502 HOH A O   1 
HETATM 8960  O  O   . HOH Y  5 .   ? 6.808   -10.086 4.011   1.00 34.50 ? 503 HOH A O   1 
HETATM 8961  O  O   . HOH Y  5 .   ? 24.875  14.016  33.111  1.00 30.19 ? 504 HOH A O   1 
HETATM 8962  O  O   . HOH Y  5 .   ? 34.358  -6.118  30.670  1.00 32.30 ? 505 HOH A O   1 
HETATM 8963  O  O   . HOH Y  5 .   ? 23.002  -12.394 9.659   1.00 10.38 ? 506 HOH A O   1 
HETATM 8964  O  O   . HOH Y  5 .   ? 20.116  -19.921 8.854   1.00 29.21 ? 507 HOH A O   1 
HETATM 8965  O  O   . HOH Y  5 .   ? 12.355  -2.728  10.971  1.00 9.07  ? 508 HOH A O   1 
HETATM 8966  O  O   . HOH Y  5 .   ? 19.557  -0.586  26.551  1.00 13.54 ? 509 HOH A O   1 
HETATM 8967  O  O   . HOH Y  5 .   ? 44.629  -1.616  14.612  1.00 27.31 ? 510 HOH A O   1 
HETATM 8968  O  O   . HOH Y  5 .   ? 31.348  -13.285 2.367   1.00 21.33 ? 511 HOH A O   1 
HETATM 8969  O  O   . HOH Y  5 .   ? 23.802  -16.052 29.631  1.00 19.64 ? 512 HOH A O   1 
HETATM 8970  O  O   . HOH Y  5 .   ? 35.077  -0.997  30.648  1.00 24.20 ? 513 HOH A O   1 
HETATM 8971  O  O   . HOH Y  5 .   ? 7.848   -1.876  15.126  1.00 27.88 ? 514 HOH A O   1 
HETATM 8972  O  O   . HOH Y  5 .   ? 46.642  -9.500  19.798  1.00 36.00 ? 515 HOH A O   1 
HETATM 8973  O  O   . HOH Y  5 .   ? 41.069  -10.526 9.750   1.00 17.60 ? 516 HOH A O   1 
HETATM 8974  O  O   . HOH Y  5 .   ? 13.850  8.202   23.331  1.00 28.41 ? 517 HOH A O   1 
HETATM 8975  O  O   . HOH Y  5 .   ? 27.620  -21.174 24.534  1.00 26.60 ? 518 HOH A O   1 
HETATM 8976  O  O   . HOH Y  5 .   ? 32.076  -16.780 17.180  1.00 28.63 ? 519 HOH A O   1 
HETATM 8977  O  O   . HOH Y  5 .   ? 36.674  5.142   14.366  1.00 31.26 ? 520 HOH A O   1 
HETATM 8978  O  O   . HOH Y  5 .   ? 10.389  -9.191  -8.061  1.00 32.09 ? 521 HOH A O   1 
HETATM 8979  O  O   . HOH Y  5 .   ? 32.650  -16.082 12.527  1.00 40.46 ? 522 HOH A O   1 
HETATM 8980  O  O   . HOH Y  5 .   ? 20.760  -9.808  31.727  1.00 17.47 ? 523 HOH A O   1 
HETATM 8981  O  O   . HOH Y  5 .   ? 17.241  0.351   28.377  1.00 15.06 ? 524 HOH A O   1 
HETATM 8982  O  O   . HOH Y  5 .   ? 8.608   2.876   7.323   1.00 8.06  ? 525 HOH A O   1 
HETATM 8983  O  O   . HOH Y  5 .   ? 19.444  -18.459 26.267  1.00 18.79 ? 526 HOH A O   1 
HETATM 8984  O  O   . HOH Y  5 .   ? 20.680  4.026   16.413  1.00 17.37 ? 527 HOH A O   1 
HETATM 8985  O  O   . HOH Y  5 .   ? 30.260  8.574   20.137  1.00 35.64 ? 528 HOH A O   1 
HETATM 8986  O  O   . HOH Y  5 .   ? 32.342  16.181  9.978   1.00 40.07 ? 529 HOH A O   1 
HETATM 8987  O  O   . HOH Y  5 .   ? 38.861  2.106   -6.114  1.00 19.00 ? 530 HOH A O   1 
HETATM 8988  O  O   . HOH Y  5 .   ? 18.892  11.806  -0.816  1.00 19.05 ? 531 HOH A O   1 
HETATM 8989  O  O   . HOH Y  5 .   ? 17.568  20.053  18.297  1.00 46.59 ? 532 HOH A O   1 
HETATM 8990  O  O   . HOH Y  5 .   ? 15.820  -11.960 26.903  1.00 16.63 ? 533 HOH A O   1 
HETATM 8991  O  O   . HOH Y  5 .   ? 29.007  -14.993 16.878  1.00 16.16 ? 534 HOH A O   1 
HETATM 8992  O  O   . HOH Y  5 .   ? 32.795  4.926   20.030  1.00 22.95 ? 535 HOH A O   1 
HETATM 8993  O  O   . HOH Y  5 .   ? 12.109  -17.112 5.196   1.00 30.28 ? 536 HOH A O   1 
HETATM 8994  O  O   . HOH Y  5 .   ? 41.811  2.562   19.024  1.00 31.04 ? 537 HOH A O   1 
HETATM 8995  O  O   . HOH Y  5 .   ? 4.825   -9.300  25.546  1.00 26.94 ? 538 HOH A O   1 
HETATM 8996  O  O   . HOH Y  5 .   ? 38.409  4.046   11.345  1.00 22.05 ? 539 HOH A O   1 
HETATM 8997  O  O   . HOH Y  5 .   ? 15.311  -15.623 2.411   1.00 32.92 ? 540 HOH A O   1 
HETATM 8998  O  O   . HOH Y  5 .   ? 7.286   4.926   11.188  1.00 9.32  ? 541 HOH A O   1 
HETATM 8999  O  O   . HOH Y  5 .   ? 11.872  7.450   8.615   1.00 10.14 ? 542 HOH A O   1 
HETATM 9000  O  O   . HOH Y  5 .   ? 20.636  -18.868 28.939  1.00 26.47 ? 543 HOH A O   1 
HETATM 9001  O  O   . HOH Y  5 .   ? 26.026  -18.529 20.540  1.00 17.87 ? 544 HOH A O   1 
HETATM 9002  O  O   . HOH Y  5 .   ? 8.867   3.807   2.676   1.00 13.94 ? 545 HOH A O   1 
HETATM 9003  O  O   . HOH Y  5 .   ? 20.980  11.862  21.601  1.00 31.69 ? 546 HOH A O   1 
HETATM 9004  O  O   . HOH Y  5 .   ? 26.082  11.957  6.405   1.00 31.38 ? 547 HOH A O   1 
HETATM 9005  O  O   . HOH Y  5 .   ? 41.923  6.887   2.818   1.00 28.24 ? 548 HOH A O   1 
HETATM 9006  O  O   . HOH Y  5 .   ? 8.689   -6.487  7.358   1.00 18.59 ? 549 HOH A O   1 
HETATM 9007  O  O   . HOH Y  5 .   ? 46.000  -9.406  16.659  1.00 37.05 ? 550 HOH A O   1 
HETATM 9008  O  O   . HOH Y  5 .   ? 10.957  11.093  8.031   1.00 10.08 ? 551 HOH A O   1 
HETATM 9009  O  O   . HOH Y  5 .   ? 8.097   -10.432 26.390  1.00 23.74 ? 552 HOH A O   1 
HETATM 9010  O  O   . HOH Y  5 .   ? 11.929  -15.388 8.435   1.00 21.26 ? 553 HOH A O   1 
HETATM 9011  O  O   . HOH Y  5 .   ? 37.754  10.314  -5.020  1.00 29.25 ? 554 HOH A O   1 
HETATM 9012  O  O   . HOH Y  5 .   ? 11.274  9.681   -1.978  1.00 20.88 ? 555 HOH A O   1 
HETATM 9013  O  O   . HOH Y  5 .   ? 43.443  -9.633  11.433  1.00 23.53 ? 556 HOH A O   1 
HETATM 9014  O  O   . HOH Y  5 .   ? 16.405  -0.196  31.332  1.00 34.76 ? 557 HOH A O   1 
HETATM 9015  O  O   . HOH Y  5 .   ? 31.800  -16.950 20.587  1.00 28.26 ? 558 HOH A O   1 
HETATM 9016  O  O   . HOH Y  5 .   ? 9.634   18.339  18.224  1.00 43.32 ? 559 HOH A O   1 
HETATM 9017  O  O   . HOH Y  5 .   ? 32.307  -16.868 10.291  1.00 29.81 ? 560 HOH A O   1 
HETATM 9018  O  O   . HOH Y  5 .   ? 13.067  5.759   24.483  1.00 31.79 ? 561 HOH A O   1 
HETATM 9019  O  O   . HOH Y  5 .   ? 39.738  -1.710  29.034  1.00 33.38 ? 562 HOH A O   1 
HETATM 9020  O  O   . HOH Y  5 .   ? 13.099  14.053  14.008  1.00 20.73 ? 563 HOH A O   1 
HETATM 9021  O  O   . HOH Y  5 .   ? 12.153  5.177   29.040  1.00 33.56 ? 564 HOH A O   1 
HETATM 9022  O  O   . HOH Y  5 .   ? 16.840  -13.578 30.760  1.00 18.39 ? 565 HOH A O   1 
HETATM 9023  O  O   . HOH Y  5 .   ? 17.633  9.541   0.093   1.00 11.99 ? 566 HOH A O   1 
HETATM 9024  O  O   . HOH Y  5 .   ? 21.103  -4.531  32.290  1.00 30.25 ? 567 HOH A O   1 
HETATM 9025  O  O   . HOH Y  5 .   ? 23.236  3.217   -2.171  1.00 17.28 ? 568 HOH A O   1 
HETATM 9026  O  O   . HOH Y  5 .   ? 15.044  -17.194 19.552  1.00 27.32 ? 569 HOH A O   1 
HETATM 9027  O  O   . HOH Y  5 .   ? 18.127  -23.691 1.416   1.00 38.68 ? 570 HOH A O   1 
HETATM 9028  O  O   . HOH Y  5 .   ? 17.519  7.916   19.773  1.00 25.61 ? 571 HOH A O   1 
HETATM 9029  O  O   . HOH Y  5 .   ? 10.077  -4.110  19.381  1.00 22.08 ? 572 HOH A O   1 
HETATM 9030  O  O   . HOH Y  5 .   ? 16.593  10.912  -3.148  1.00 21.49 ? 573 HOH A O   1 
HETATM 9031  O  O   . HOH Y  5 .   ? 20.823  -2.697  -5.329  1.00 24.20 ? 574 HOH A O   1 
HETATM 9032  O  O   . HOH Y  5 .   ? 14.249  4.343   -4.103  1.00 20.69 ? 575 HOH A O   1 
HETATM 9033  O  O   . HOH Y  5 .   ? 7.423   -6.743  2.407   1.00 24.35 ? 576 HOH A O   1 
HETATM 9034  O  O   . HOH Y  5 .   ? 15.844  4.480   21.648  1.00 16.85 ? 577 HOH A O   1 
HETATM 9035  O  O   . HOH Y  5 .   ? 33.666  -15.489 8.312   1.00 30.80 ? 578 HOH A O   1 
HETATM 9036  O  O   . HOH Y  5 .   ? 9.471   16.879  14.699  1.00 35.82 ? 579 HOH A O   1 
HETATM 9037  O  O   . HOH Y  5 .   ? 13.594  -12.612 20.733  1.00 16.38 ? 580 HOH A O   1 
HETATM 9038  O  O   . HOH Y  5 .   ? 18.254  -15.678 33.945  1.00 23.67 ? 581 HOH A O   1 
HETATM 9039  O  O   . HOH Y  5 .   ? 30.662  14.871  4.314   1.00 36.50 ? 582 HOH A O   1 
HETATM 9040  O  O   . HOH Y  5 .   ? 24.417  -7.236  -7.947  1.00 47.15 ? 583 HOH A O   1 
HETATM 9041  O  O   . HOH Y  5 .   ? 25.938  -17.930 17.360  1.00 19.13 ? 584 HOH A O   1 
HETATM 9042  O  O   . HOH Y  5 .   ? 24.095  -21.026 26.569  1.00 26.22 ? 585 HOH A O   1 
HETATM 9043  O  O   . HOH Y  5 .   ? 25.526  -16.017 6.513   1.00 11.78 ? 586 HOH A O   1 
HETATM 9044  O  O   . HOH Y  5 .   ? 17.890  9.845   21.855  1.00 25.98 ? 587 HOH A O   1 
HETATM 9045  O  O   . HOH Y  5 .   ? 7.969   -13.111 -1.370  1.00 29.72 ? 588 HOH A O   1 
HETATM 9046  O  O   . HOH Y  5 .   ? 24.868  16.048  2.460   1.00 32.36 ? 589 HOH A O   1 
HETATM 9047  O  O   . HOH Y  5 .   ? 14.351  13.270  28.117  1.00 36.09 ? 590 HOH A O   1 
HETATM 9048  O  O   . HOH Y  5 .   ? 17.319  -3.787  -8.394  1.00 33.20 ? 591 HOH A O   1 
HETATM 9049  O  O   . HOH Y  5 .   ? 7.037   0.003   -13.958 1.00 38.64 ? 592 HOH A O   1 
HETATM 9050  O  O   . HOH Y  5 .   ? 11.510  7.967   1.661   1.00 11.80 ? 593 HOH A O   1 
HETATM 9051  O  O   . HOH Y  5 .   ? 39.709  8.600   26.699  1.00 32.93 ? 594 HOH A O   1 
HETATM 9052  O  O   . HOH Y  5 .   ? 27.290  -5.543  -5.305  1.00 20.43 ? 595 HOH A O   1 
HETATM 9053  O  O   . HOH Y  5 .   ? 27.775  -4.784  31.196  1.00 24.21 ? 596 HOH A O   1 
HETATM 9054  O  O   . HOH Y  5 .   ? 9.468   -2.601  10.373  1.00 19.49 ? 597 HOH A O   1 
HETATM 9055  O  O   . HOH Y  5 .   ? 39.168  3.700   19.525  1.00 21.53 ? 598 HOH A O   1 
HETATM 9056  O  O   . HOH Y  5 .   ? 44.122  -9.869  7.904   1.00 26.13 ? 599 HOH A O   1 
HETATM 9057  O  O   . HOH Y  5 .   ? 29.785  9.935   33.729  1.00 26.74 ? 600 HOH A O   1 
HETATM 9058  O  O   . HOH Y  5 .   ? 43.952  1.617   2.876   1.00 28.16 ? 601 HOH A O   1 
HETATM 9059  O  O   . HOH Y  5 .   ? 13.827  1.867   -2.957  1.00 23.70 ? 602 HOH A O   1 
HETATM 9060  O  O   . HOH Y  5 .   ? 42.310  2.824   5.373   1.00 33.51 ? 603 HOH A O   1 
HETATM 9061  O  O   . HOH Y  5 .   ? 7.447   -7.242  31.416  1.00 30.44 ? 604 HOH A O   1 
HETATM 9062  O  O   . HOH Y  5 .   ? 23.960  -22.133 18.394  1.00 34.27 ? 605 HOH A O   1 
HETATM 9063  O  O   . HOH Y  5 .   ? 31.321  -19.030 4.169   1.00 21.47 ? 606 HOH A O   1 
HETATM 9064  O  O   . HOH Y  5 .   ? 10.047  3.142   22.175  1.00 22.33 ? 607 HOH A O   1 
HETATM 9065  O  O   . HOH Y  5 .   ? 32.400  7.632   30.771  1.00 17.33 ? 608 HOH A O   1 
HETATM 9066  O  O   . HOH Y  5 .   ? 42.584  3.831   13.015  1.00 42.63 ? 609 HOH A O   1 
HETATM 9067  O  O   . HOH Y  5 .   ? 11.395  1.539   -4.313  1.00 34.46 ? 610 HOH A O   1 
HETATM 9068  O  O   . HOH Y  5 .   ? 14.625  7.025   21.049  1.00 21.47 ? 611 HOH A O   1 
HETATM 9069  O  O   . HOH Y  5 .   ? 7.613   9.158   14.160  1.00 16.64 ? 612 HOH A O   1 
HETATM 9070  O  O   . HOH Y  5 .   ? 13.859  -16.044 26.839  1.00 27.41 ? 613 HOH A O   1 
HETATM 9071  O  O   . HOH Y  5 .   ? 24.011  12.012  0.407   1.00 29.86 ? 614 HOH A O   1 
HETATM 9072  O  O   . HOH Y  5 .   ? 29.647  11.816  -4.936  1.00 25.47 ? 615 HOH A O   1 
HETATM 9073  O  O   . HOH Y  5 .   ? 7.318   -2.071  -0.784  1.00 19.70 ? 616 HOH A O   1 
HETATM 9074  O  O   . HOH Y  5 .   ? 8.427   -0.266  24.394  1.00 22.42 ? 617 HOH A O   1 
HETATM 9075  O  O   . HOH Y  5 .   ? 38.087  -13.523 5.674   1.00 25.24 ? 618 HOH A O   1 
HETATM 9076  O  O   . HOH Y  5 .   ? 15.087  -14.422 19.165  1.00 16.14 ? 619 HOH A O   1 
HETATM 9077  O  O   . HOH Y  5 .   ? 7.827   -7.099  16.785  1.00 22.52 ? 620 HOH A O   1 
HETATM 9078  O  O   . HOH Y  5 .   ? 45.031  -4.281  15.435  1.00 23.10 ? 621 HOH A O   1 
HETATM 9079  O  O   . HOH Y  5 .   ? 35.127  10.290  9.980   1.00 28.84 ? 622 HOH A O   1 
HETATM 9080  O  O   . HOH Y  5 .   ? 18.122  5.462   20.586  1.00 17.10 ? 623 HOH A O   1 
HETATM 9081  O  O   . HOH Y  5 .   ? 29.177  -6.198  33.154  1.00 41.87 ? 624 HOH A O   1 
HETATM 9082  O  O   . HOH Y  5 .   ? 45.285  -7.460  12.763  1.00 40.32 ? 625 HOH A O   1 
HETATM 9083  O  O   . HOH Y  5 .   ? 30.040  7.003   13.420  1.00 26.26 ? 626 HOH A O   1 
HETATM 9084  O  O   . HOH Y  5 .   ? 7.374   -15.739 7.326   1.00 28.66 ? 627 HOH A O   1 
HETATM 9085  O  O   . HOH Y  5 .   ? 12.421  4.503   22.174  1.00 22.30 ? 628 HOH A O   1 
HETATM 9086  O  O   . HOH Y  5 .   ? 27.286  -15.924 -5.696  1.00 27.56 ? 629 HOH A O   1 
HETATM 9087  O  O   . HOH Y  5 .   ? 28.289  -24.172 8.215   1.00 32.83 ? 630 HOH A O   1 
HETATM 9088  O  O   . HOH Y  5 .   ? 38.434  -15.504 12.178  1.00 27.25 ? 631 HOH A O   1 
HETATM 9089  O  O   . HOH Y  5 .   ? 23.845  14.720  4.596   1.00 27.91 ? 632 HOH A O   1 
HETATM 9090  O  O   . HOH Y  5 .   ? 23.614  -21.658 -3.352  1.00 32.30 ? 633 HOH A O   1 
HETATM 9091  O  O   . HOH Y  5 .   ? 9.263   -11.007 14.283  1.00 27.30 ? 634 HOH A O   1 
HETATM 9092  O  O   . HOH Y  5 .   ? 7.253   -0.800  8.168   1.00 28.62 ? 635 HOH A O   1 
HETATM 9093  O  O   . HOH Y  5 .   ? 24.000  -15.228 -11.919 1.00 32.60 ? 636 HOH A O   1 
HETATM 9094  O  O   . HOH Y  5 .   ? 14.234  -2.037  28.813  1.00 19.80 ? 637 HOH A O   1 
HETATM 9095  O  O   . HOH Y  5 .   ? 13.101  4.982   -0.322  1.00 20.57 ? 638 HOH A O   1 
HETATM 9096  O  O   . HOH Y  5 .   ? 13.296  -14.698 29.215  1.00 29.04 ? 639 HOH A O   1 
HETATM 9097  O  O   . HOH Y  5 .   ? 17.647  -16.655 -8.753  1.00 39.18 ? 640 HOH A O   1 
HETATM 9098  O  O   . HOH Y  5 .   ? 8.400   4.088   19.433  1.00 40.07 ? 641 HOH A O   1 
HETATM 9099  O  O   . HOH Y  5 .   ? 32.162  -18.373 6.931   1.00 30.85 ? 642 HOH A O   1 
HETATM 9100  O  O   . HOH Y  5 .   ? 17.516  -18.160 5.118   1.00 33.24 ? 643 HOH A O   1 
HETATM 9101  O  O   . HOH Y  5 .   ? 32.178  -9.460  -4.149  1.00 52.37 ? 644 HOH A O   1 
HETATM 9102  O  O   . HOH Y  5 .   ? 17.856  -16.765 -3.466  1.00 41.13 ? 645 HOH A O   1 
HETATM 9103  O  O   . HOH Y  5 .   ? 36.364  1.464   30.436  1.00 24.82 ? 646 HOH A O   1 
HETATM 9104  O  O   . HOH Y  5 .   ? 6.115   -2.966  13.297  1.00 21.70 ? 647 HOH A O   1 
HETATM 9105  O  O   . HOH Y  5 .   ? 26.927  13.464  24.629  1.00 35.45 ? 648 HOH A O   1 
HETATM 9106  O  O   . HOH Y  5 .   ? 37.100  7.956   9.559   1.00 27.89 ? 649 HOH A O   1 
HETATM 9107  O  O   . HOH Y  5 .   ? 32.921  -0.516  -4.492  1.00 38.05 ? 650 HOH A O   1 
HETATM 9108  O  O   . HOH Y  5 .   ? 15.000  -13.680 16.573  1.00 14.78 ? 651 HOH A O   1 
HETATM 9109  O  O   . HOH Y  5 .   ? 22.067  -19.073 15.105  1.00 24.33 ? 652 HOH A O   1 
HETATM 9110  O  O   . HOH Y  5 .   ? 31.697  -2.902  -5.150  1.00 33.25 ? 653 HOH A O   1 
HETATM 9111  O  O   . HOH Y  5 .   ? 5.520   -2.832  -10.525 1.00 34.81 ? 654 HOH A O   1 
HETATM 9112  O  O   . HOH Y  5 .   ? 11.430  2.580   -6.906  1.00 40.38 ? 655 HOH A O   1 
HETATM 9113  O  O   . HOH Y  5 .   ? 19.912  12.127  37.765  1.00 26.43 ? 656 HOH A O   1 
HETATM 9114  O  O   . HOH Y  5 .   ? 17.747  -6.423  33.534  1.00 27.74 ? 657 HOH A O   1 
HETATM 9115  O  O   . HOH Y  5 .   ? 15.509  13.926  -0.541  1.00 30.40 ? 658 HOH A O   1 
HETATM 9116  O  O   . HOH Y  5 .   ? 20.112  -7.281  32.224  1.00 21.47 ? 659 HOH A O   1 
HETATM 9117  O  O   . HOH Y  5 .   ? 35.989  14.973  8.145   1.00 46.47 ? 660 HOH A O   1 
HETATM 9118  O  O   . HOH Y  5 .   ? 33.789  -3.846  32.040  1.00 34.37 ? 661 HOH A O   1 
HETATM 9119  O  O   . HOH Y  5 .   ? 41.358  10.255  0.242   1.00 32.50 ? 662 HOH A O   1 
HETATM 9120  O  O   . HOH Y  5 .   ? 23.696  -19.495 16.584  1.00 26.72 ? 663 HOH A O   1 
HETATM 9121  O  O   . HOH Y  5 .   ? 13.054  -14.502 12.924  1.00 30.49 ? 664 HOH A O   1 
HETATM 9122  O  O   . HOH Y  5 .   ? 19.138  -20.113 12.391  1.00 45.30 ? 665 HOH A O   1 
HETATM 9123  O  O   . HOH Y  5 .   ? 25.306  10.915  -3.093  1.00 39.40 ? 666 HOH A O   1 
HETATM 9124  O  O   . HOH Y  5 .   ? 4.264   13.311  19.525  1.00 32.29 ? 667 HOH A O   1 
HETATM 9125  O  O   . HOH Y  5 .   ? 20.204  18.650  33.713  1.00 47.44 ? 668 HOH A O   1 
HETATM 9126  O  O   . HOH Y  5 .   ? 24.733  -28.760 -0.883  1.00 26.16 ? 669 HOH A O   1 
HETATM 9127  O  O   . HOH Y  5 .   ? 28.740  -18.579 20.487  1.00 19.81 ? 670 HOH A O   1 
HETATM 9128  O  O   . HOH Y  5 .   ? 45.599  1.912   8.070   1.00 31.47 ? 671 HOH A O   1 
HETATM 9129  O  O   . HOH Y  5 .   ? 35.673  -16.227 13.642  1.00 42.64 ? 672 HOH A O   1 
HETATM 9130  O  O   . HOH Y  5 .   ? 29.444  10.148  22.534  1.00 32.08 ? 673 HOH A O   1 
HETATM 9131  O  O   . HOH Y  5 .   ? 19.732  -22.273 23.765  1.00 41.77 ? 674 HOH A O   1 
HETATM 9132  O  O   . HOH Y  5 .   ? 27.154  11.304  22.522  1.00 32.55 ? 675 HOH A O   1 
HETATM 9133  O  O   . HOH Y  5 .   ? 16.564  2.191   -7.947  1.00 33.40 ? 676 HOH A O   1 
HETATM 9134  O  O   . HOH Y  5 .   ? 13.112  13.487  -1.923  1.00 30.79 ? 677 HOH A O   1 
HETATM 9135  O  O   . HOH Y  5 .   ? 11.036  -14.753 17.104  1.00 33.87 ? 678 HOH A O   1 
HETATM 9136  O  O   . HOH Y  5 .   ? 7.789   -3.962  11.901  1.00 31.78 ? 679 HOH A O   1 
HETATM 9137  O  O   . HOH Y  5 .   ? 40.307  8.872   -5.742  1.00 32.29 ? 680 HOH A O   1 
HETATM 9138  O  O   . HOH Y  5 .   ? 30.183  -17.770 18.395  1.00 32.72 ? 681 HOH A O   1 
HETATM 9139  O  O   . HOH Y  5 .   ? 33.452  -17.622 2.940   1.00 32.94 ? 682 HOH A O   1 
HETATM 9140  O  O   . HOH Y  5 .   ? 27.207  13.466  30.480  1.00 40.48 ? 683 HOH A O   1 
HETATM 9141  O  O   . HOH Y  5 .   ? 24.513  13.562  37.465  1.00 40.03 ? 684 HOH A O   1 
HETATM 9142  O  O   . HOH Y  5 .   ? 10.217  -4.085  29.878  1.00 30.64 ? 685 HOH A O   1 
HETATM 9143  O  O   . HOH Y  5 .   ? 13.479  25.019  13.027  1.00 24.12 ? 686 HOH A O   1 
HETATM 9144  O  O   . HOH Y  5 .   ? 19.957  14.247  25.731  1.00 32.85 ? 687 HOH A O   1 
HETATM 9145  O  O   . HOH Y  5 .   ? 7.181   -5.755  5.086   1.00 26.45 ? 688 HOH A O   1 
HETATM 9146  O  O   . HOH Y  5 .   ? 41.963  -14.187 12.090  1.00 35.30 ? 689 HOH A O   1 
HETATM 9147  O  O   . HOH Y  5 .   ? 45.400  0.193   5.990   1.00 33.62 ? 690 HOH A O   1 
HETATM 9148  O  O   . HOH Y  5 .   ? 6.006   3.135   -7.775  1.00 36.59 ? 691 HOH A O   1 
HETATM 9149  O  O   . HOH Y  5 .   ? 29.570  -3.764  -5.653  1.00 43.07 ? 692 HOH A O   1 
HETATM 9150  O  O   . HOH Y  5 .   ? 46.105  -6.578  8.523   1.00 43.83 ? 693 HOH A O   1 
HETATM 9151  O  O   . HOH Y  5 .   ? 27.130  -18.448 14.733  1.00 40.46 ? 694 HOH A O   1 
HETATM 9152  O  O   . HOH Y  5 .   ? 14.487  -18.759 17.135  1.00 38.67 ? 695 HOH A O   1 
HETATM 9153  O  O   . HOH Y  5 .   ? 23.180  -4.219  -5.639  1.00 32.96 ? 696 HOH A O   1 
HETATM 9154  O  O   . HOH Y  5 .   ? 36.231  -2.354  36.553  1.00 23.63 ? 697 HOH A O   1 
HETATM 9155  O  O   . HOH Y  5 .   ? 7.723   6.573   15.523  1.00 15.85 ? 698 HOH A O   1 
HETATM 9156  O  O   . HOH Y  5 .   ? 8.534   2.404   -3.405  1.00 40.33 ? 699 HOH A O   1 
HETATM 9157  O  O   . HOH Y  5 .   ? 39.507  -9.769  24.920  1.00 28.95 ? 700 HOH A O   1 
HETATM 9158  O  O   . HOH Y  5 .   ? 26.281  14.034  35.610  1.00 39.28 ? 701 HOH A O   1 
HETATM 9159  O  O   . HOH Y  5 .   ? 23.528  -10.045 32.385  1.00 25.55 ? 702 HOH A O   1 
HETATM 9160  O  O   . HOH Y  5 .   ? 14.587  -12.336 29.396  1.00 14.68 ? 703 HOH A O   1 
HETATM 9161  O  O   . HOH Y  5 .   ? 50.369  -9.268  27.404  1.00 34.53 ? 704 HOH A O   1 
HETATM 9162  O  O   . HOH Y  5 .   ? 23.538  11.128  -1.918  1.00 39.85 ? 705 HOH A O   1 
HETATM 9163  O  O   . HOH Y  5 .   ? 26.702  -23.746 23.231  1.00 36.19 ? 706 HOH A O   1 
HETATM 9164  O  O   . HOH Y  5 .   ? 35.984  -16.247 24.898  1.00 42.45 ? 707 HOH A O   1 
HETATM 9165  O  O   . HOH Y  5 .   ? 16.241  -16.480 7.766   1.00 28.74 ? 708 HOH A O   1 
HETATM 9166  O  O   . HOH Y  5 .   ? 32.458  -14.960 28.159  1.00 32.59 ? 709 HOH A O   1 
HETATM 9167  O  O   . HOH Y  5 .   ? 36.617  13.503  -1.145  1.00 31.52 ? 710 HOH A O   1 
HETATM 9168  O  O   . HOH Y  5 .   ? 29.993  -18.195 -2.817  1.00 29.57 ? 711 HOH A O   1 
HETATM 9169  O  O   . HOH Y  5 .   ? 24.203  -21.085 11.668  1.00 34.58 ? 712 HOH A O   1 
HETATM 9170  O  O   . HOH Y  5 .   ? 23.359  -20.067 28.754  1.00 38.05 ? 713 HOH A O   1 
HETATM 9171  O  O   . HOH Y  5 .   ? 25.013  -5.166  31.471  1.00 31.08 ? 714 HOH A O   1 
HETATM 9172  O  O   . HOH Y  5 .   ? 38.879  -4.361  30.249  1.00 31.49 ? 715 HOH A O   1 
HETATM 9173  O  O   . HOH Y  5 .   ? 25.076  -13.906 30.798  1.00 32.75 ? 716 HOH A O   1 
HETATM 9174  O  O   . HOH Y  5 .   ? 21.345  15.444  39.354  1.00 40.26 ? 717 HOH A O   1 
HETATM 9175  O  O   . HOH Y  5 .   ? 12.643  -3.241  30.738  1.00 29.09 ? 718 HOH A O   1 
HETATM 9176  O  O   . HOH Y  5 .   ? 14.337  -17.810 11.521  1.00 38.82 ? 719 HOH A O   1 
HETATM 9177  O  O   . HOH Y  5 .   ? 8.039   -4.901  9.248   1.00 29.42 ? 720 HOH A O   1 
HETATM 9178  O  O   . HOH Y  5 .   ? 14.872  -13.987 25.422  1.00 22.99 ? 721 HOH A O   1 
HETATM 9179  O  O   . HOH Y  5 .   ? 27.357  12.870  19.998  1.00 41.22 ? 722 HOH A O   1 
HETATM 9180  O  O   . HOH Y  5 .   ? 30.386  -21.191 3.215   1.00 43.96 ? 723 HOH A O   1 
HETATM 9181  O  O   . HOH Y  5 .   ? 36.069  -14.339 26.712  1.00 37.15 ? 724 HOH A O   1 
HETATM 9182  O  O   . HOH Y  5 .   ? 11.056  5.031   -2.361  1.00 31.28 ? 725 HOH A O   1 
HETATM 9183  O  O   . HOH Y  5 .   ? 26.792  -21.924 27.245  1.00 33.56 ? 726 HOH A O   1 
HETATM 9184  O  O   . HOH Y  5 .   ? 21.007  11.869  -2.642  1.00 29.86 ? 727 HOH A O   1 
HETATM 9185  O  O   . HOH Y  5 .   ? 4.387   13.612  22.445  1.00 30.01 ? 728 HOH A O   1 
HETATM 9186  O  O   . HOH Y  5 .   ? 11.505  -12.981 25.894  1.00 25.17 ? 729 HOH A O   1 
HETATM 9187  O  O   . HOH Y  5 .   ? 21.331  16.058  5.151   1.00 24.94 ? 730 HOH A O   1 
HETATM 9188  O  O   . HOH Y  5 .   ? 15.884  4.642   -6.659  1.00 34.25 ? 731 HOH A O   1 
HETATM 9189  O  O   . HOH Y  5 .   ? 24.968  -18.449 30.056  1.00 30.93 ? 732 HOH A O   1 
HETATM 9190  O  O   . HOH Y  5 .   ? 11.922  5.437   -4.344  1.00 35.22 ? 733 HOH A O   1 
HETATM 9191  O  O   . HOH Y  5 .   ? 13.675  -17.086 7.314   1.00 25.89 ? 734 HOH A O   1 
HETATM 9192  O  O   . HOH Y  5 .   ? 19.129  10.225  -4.434  1.00 28.63 ? 735 HOH A O   1 
HETATM 9193  O  O   . HOH Y  5 .   ? 13.633  -13.701 23.111  1.00 30.95 ? 736 HOH A O   1 
HETATM 9194  O  O   . HOH Y  5 .   ? 22.816  16.346  8.335   1.00 39.35 ? 737 HOH A O   1 
HETATM 9195  O  O   . HOH Y  5 .   ? 8.317   -13.290 27.793  1.00 38.43 ? 738 HOH A O   1 
HETATM 9196  O  O   . HOH Y  5 .   ? 21.707  2.548   -6.992  1.00 33.16 ? 739 HOH A O   1 
HETATM 9197  O  O   . HOH Y  5 .   ? 33.356  -18.050 27.791  1.00 34.49 ? 740 HOH A O   1 
HETATM 9198  O  O   . HOH Y  5 .   ? 31.529  -20.011 -1.631  1.00 35.14 ? 741 HOH A O   1 
HETATM 9199  O  O   . HOH Y  5 .   ? 18.629  6.331   -7.055  1.00 38.32 ? 742 HOH A O   1 
HETATM 9200  O  O   . HOH Z  5 .   ? 2.617   6.531   16.639  1.00 26.34 ? 401 HOH B O   1 
HETATM 9201  O  O   . HOH Z  5 .   ? -7.899  -20.724 16.951  1.00 35.70 ? 402 HOH B O   1 
HETATM 9202  O  O   . HOH Z  5 .   ? -7.790  6.420   1.875   1.00 16.45 ? 403 HOH B O   1 
HETATM 9203  O  O   . HOH Z  5 .   ? -33.175 7.249   -4.462  1.00 36.29 ? 404 HOH B O   1 
HETATM 9204  O  O   . HOH Z  5 .   ? 3.453   18.181  -15.471 1.00 32.50 ? 405 HOH B O   1 
HETATM 9205  O  O   . HOH Z  5 .   ? -25.139 3.152   -11.302 1.00 31.32 ? 406 HOH B O   1 
HETATM 9206  O  O   . HOH Z  5 .   ? -17.055 11.138  4.480   1.00 29.37 ? 407 HOH B O   1 
HETATM 9207  O  O   . HOH Z  5 .   ? -0.079  16.627  -11.137 1.00 19.24 ? 408 HOH B O   1 
HETATM 9208  O  O   . HOH Z  5 .   ? -27.102 -3.727  -5.822  1.00 30.82 ? 409 HOH B O   1 
HETATM 9209  O  O   . HOH Z  5 .   ? 7.275   -11.484 24.033  1.00 23.88 ? 410 HOH B O   1 
HETATM 9210  O  O   . HOH Z  5 .   ? -3.685  13.893  -7.244  1.00 19.49 ? 411 HOH B O   1 
HETATM 9211  O  O   . HOH Z  5 .   ? -0.847  18.017  0.588   1.00 30.29 ? 412 HOH B O   1 
HETATM 9212  O  O   . HOH Z  5 .   ? -20.112 -11.903 0.772   1.00 33.43 ? 413 HOH B O   1 
HETATM 9213  O  O   . HOH Z  5 .   ? -9.267  8.845   20.461  1.00 38.71 ? 414 HOH B O   1 
HETATM 9214  O  O   . HOH Z  5 .   ? -21.342 -9.905  9.993   1.00 32.24 ? 415 HOH B O   1 
HETATM 9215  O  O   . HOH Z  5 .   ? 6.162   16.808  0.817   1.00 30.48 ? 416 HOH B O   1 
HETATM 9216  O  O   . HOH Z  5 .   ? -4.033  -17.742 22.374  1.00 21.03 ? 417 HOH B O   1 
HETATM 9217  O  O   . HOH Z  5 .   ? -21.018 -5.017  22.003  1.00 22.84 ? 418 HOH B O   1 
HETATM 9218  O  O   . HOH Z  5 .   ? -2.684  5.151   3.998   1.00 9.14  ? 419 HOH B O   1 
HETATM 9219  O  O   . HOH Z  5 .   ? -27.108 -10.141 1.719   1.00 24.73 ? 420 HOH B O   1 
HETATM 9220  O  O   . HOH Z  5 .   ? 1.018   18.002  -13.930 1.00 25.89 ? 421 HOH B O   1 
HETATM 9221  O  O   . HOH Z  5 .   ? -14.006 -14.940 28.352  1.00 24.34 ? 422 HOH B O   1 
HETATM 9222  O  O   . HOH Z  5 .   ? -16.912 0.017   23.454  1.00 39.12 ? 423 HOH B O   1 
HETATM 9223  O  O   . HOH Z  5 .   ? -13.546 7.400   -15.693 1.00 20.95 ? 424 HOH B O   1 
HETATM 9224  O  O   . HOH Z  5 .   ? 5.800   -9.439  13.506  1.00 14.73 ? 425 HOH B O   1 
HETATM 9225  O  O   . HOH Z  5 .   ? 3.655   -2.219  22.602  1.00 23.98 ? 426 HOH B O   1 
HETATM 9226  O  O   . HOH Z  5 .   ? -8.787  14.505  -2.150  1.00 34.30 ? 427 HOH B O   1 
HETATM 9227  O  O   . HOH Z  5 .   ? 5.167   6.270   0.979   1.00 10.13 ? 428 HOH B O   1 
HETATM 9228  O  O   . HOH Z  5 .   ? -29.315 2.435   5.776   1.00 21.80 ? 429 HOH B O   1 
HETATM 9229  O  O   . HOH Z  5 .   ? -19.943 -7.813  -11.472 1.00 31.87 ? 430 HOH B O   1 
HETATM 9230  O  O   . HOH Z  5 .   ? -29.920 -4.618  -0.719  1.00 19.94 ? 431 HOH B O   1 
HETATM 9231  O  O   . HOH Z  5 .   ? -14.687 -13.436 23.973  1.00 25.40 ? 432 HOH B O   1 
HETATM 9232  O  O   . HOH Z  5 .   ? -16.725 -16.854 16.734  1.00 31.52 ? 433 HOH B O   1 
HETATM 9233  O  O   . HOH Z  5 .   ? 1.307   0.426   -16.097 1.00 27.65 ? 434 HOH B O   1 
HETATM 9234  O  O   . HOH Z  5 .   ? -26.576 8.937   -2.812  1.00 26.86 ? 435 HOH B O   1 
HETATM 9235  O  O   . HOH Z  5 .   ? -17.530 -12.581 3.446   1.00 21.30 ? 436 HOH B O   1 
HETATM 9236  O  O   . HOH Z  5 .   ? -26.652 -7.200  -1.527  1.00 20.53 ? 437 HOH B O   1 
HETATM 9237  O  O   . HOH Z  5 .   ? -5.842  -12.676 11.799  1.00 16.37 ? 438 HOH B O   1 
HETATM 9238  O  O   . HOH Z  5 .   ? -21.882 1.543   18.651  1.00 22.42 ? 439 HOH B O   1 
HETATM 9239  O  O   . HOH Z  5 .   ? -17.607 -16.583 -6.101  1.00 23.80 ? 440 HOH B O   1 
HETATM 9240  O  O   . HOH Z  5 .   ? -7.379  -7.509  28.420  1.00 27.94 ? 441 HOH B O   1 
HETATM 9241  O  O   . HOH Z  5 .   ? -26.266 9.122   16.513  1.00 34.10 ? 442 HOH B O   1 
HETATM 9242  O  O   . HOH Z  5 .   ? -21.142 -11.116 5.757   1.00 36.12 ? 443 HOH B O   1 
HETATM 9243  O  O   . HOH Z  5 .   ? 4.293   -14.853 10.206  1.00 30.12 ? 444 HOH B O   1 
HETATM 9244  O  O   . HOH Z  5 .   ? -4.463  11.182  -14.958 1.00 14.29 ? 445 HOH B O   1 
HETATM 9245  O  O   . HOH Z  5 .   ? -3.464  19.015  -20.065 1.00 21.86 ? 446 HOH B O   1 
HETATM 9246  O  O   . HOH Z  5 .   ? 7.832   11.874  14.700  1.00 20.25 ? 447 HOH B O   1 
HETATM 9247  O  O   . HOH Z  5 .   ? 5.602   -8.258  -1.350  1.00 26.20 ? 448 HOH B O   1 
HETATM 9248  O  O   . HOH Z  5 .   ? -8.109  -1.466  -15.912 1.00 33.99 ? 449 HOH B O   1 
HETATM 9249  O  O   . HOH Z  5 .   ? -32.943 -1.697  -8.404  1.00 22.59 ? 450 HOH B O   1 
HETATM 9250  O  O   . HOH Z  5 .   ? 1.731   6.465   -8.215  1.00 15.84 ? 451 HOH B O   1 
HETATM 9251  O  O   . HOH Z  5 .   ? -27.438 3.393   -10.231 1.00 25.06 ? 452 HOH B O   1 
HETATM 9252  O  O   . HOH Z  5 .   ? -23.136 9.496   6.458   1.00 18.37 ? 453 HOH B O   1 
HETATM 9253  O  O   . HOH Z  5 .   ? 9.100   7.105   8.396   1.00 14.66 ? 454 HOH B O   1 
HETATM 9254  O  O   . HOH Z  5 .   ? 1.423   6.594   20.754  1.00 40.48 ? 455 HOH B O   1 
HETATM 9255  O  O   . HOH Z  5 .   ? -15.580 16.186  -8.142  1.00 26.75 ? 456 HOH B O   1 
HETATM 9256  O  O   . HOH Z  5 .   ? -16.507 5.494   21.951  1.00 31.79 ? 457 HOH B O   1 
HETATM 9257  O  O   . HOH Z  5 .   ? -30.607 1.989   10.824  1.00 37.65 ? 458 HOH B O   1 
HETATM 9258  O  O   . HOH Z  5 .   ? -13.962 0.340   15.112  1.00 10.68 ? 459 HOH B O   1 
HETATM 9259  O  O   . HOH Z  5 .   ? -3.407  2.529   21.275  1.00 27.23 ? 460 HOH B O   1 
HETATM 9260  O  O   . HOH Z  5 .   ? -17.457 13.256  -4.390  1.00 26.66 ? 461 HOH B O   1 
HETATM 9261  O  O   . HOH Z  5 .   ? -0.448  4.029   -16.759 1.00 22.79 ? 462 HOH B O   1 
HETATM 9262  O  O   . HOH Z  5 .   ? -12.030 -17.575 13.243  1.00 27.81 ? 463 HOH B O   1 
HETATM 9263  O  O   . HOH Z  5 .   ? -4.204  16.009  -11.244 1.00 14.42 ? 464 HOH B O   1 
HETATM 9264  O  O   . HOH Z  5 .   ? -9.374  16.120  10.293  1.00 36.79 ? 465 HOH B O   1 
HETATM 9265  O  O   . HOH Z  5 .   ? -23.263 -8.982  14.436  1.00 28.25 ? 466 HOH B O   1 
HETATM 9266  O  O   . HOH Z  5 .   ? -17.797 9.144   -2.673  1.00 16.16 ? 467 HOH B O   1 
HETATM 9267  O  O   . HOH Z  5 .   ? -26.900 -6.270  6.720   1.00 17.80 ? 468 HOH B O   1 
HETATM 9268  O  O   . HOH Z  5 .   ? -29.395 -4.923  15.054  1.00 34.81 ? 469 HOH B O   1 
HETATM 9269  O  O   . HOH Z  5 .   ? 7.707   21.374  7.793   1.00 10.57 ? 470 HOH B O   1 
HETATM 9270  O  O   . HOH Z  5 .   ? -3.529  -8.649  -9.144  1.00 20.55 ? 471 HOH B O   1 
HETATM 9271  O  O   . HOH Z  5 .   ? 5.722   12.333  -4.322  1.00 17.11 ? 472 HOH B O   1 
HETATM 9272  O  O   . HOH Z  5 .   ? 3.645   -2.185  13.855  1.00 14.60 ? 473 HOH B O   1 
HETATM 9273  O  O   . HOH Z  5 .   ? -20.139 -12.240 -2.378  1.00 28.79 ? 474 HOH B O   1 
HETATM 9274  O  O   . HOH Z  5 .   ? 4.133   11.263  -13.348 1.00 30.18 ? 475 HOH B O   1 
HETATM 9275  O  O   . HOH Z  5 .   ? -24.420 -9.355  12.205  1.00 39.75 ? 476 HOH B O   1 
HETATM 9276  O  O   . HOH Z  5 .   ? -5.755  11.168  20.713  1.00 30.45 ? 477 HOH B O   1 
HETATM 9277  O  O   . HOH Z  5 .   ? -21.708 -8.801  -8.453  1.00 18.35 ? 478 HOH B O   1 
HETATM 9278  O  O   . HOH Z  5 .   ? -4.754  14.333  -4.653  1.00 27.77 ? 479 HOH B O   1 
HETATM 9279  O  O   . HOH Z  5 .   ? -24.644 -2.553  -6.447  1.00 13.87 ? 480 HOH B O   1 
HETATM 9280  O  O   . HOH Z  5 .   ? -16.562 -12.230 25.589  1.00 21.84 ? 481 HOH B O   1 
HETATM 9281  O  O   . HOH Z  5 .   ? 3.739   3.405   -2.451  1.00 16.93 ? 482 HOH B O   1 
HETATM 9282  O  O   . HOH Z  5 .   ? -20.409 -9.513  14.950  1.00 19.51 ? 483 HOH B O   1 
HETATM 9283  O  O   . HOH Z  5 .   ? -6.034  -16.574 5.445   1.00 25.87 ? 484 HOH B O   1 
HETATM 9284  O  O   . HOH Z  5 .   ? 4.654   16.930  3.333   1.00 27.36 ? 485 HOH B O   1 
HETATM 9285  O  O   . HOH Z  5 .   ? -4.306  -19.344 18.038  1.00 26.56 ? 486 HOH B O   1 
HETATM 9286  O  O   . HOH Z  5 .   ? -1.614  18.127  14.267  1.00 33.86 ? 487 HOH B O   1 
HETATM 9287  O  O   . HOH Z  5 .   ? -19.251 -0.723  -16.116 1.00 24.35 ? 488 HOH B O   1 
HETATM 9288  O  O   . HOH Z  5 .   ? -12.285 -13.624 -11.254 1.00 15.40 ? 489 HOH B O   1 
HETATM 9289  O  O   . HOH Z  5 .   ? 4.720   -5.912  8.964   1.00 24.48 ? 490 HOH B O   1 
HETATM 9290  O  O   . HOH Z  5 .   ? -27.618 -4.273  8.578   1.00 17.22 ? 491 HOH B O   1 
HETATM 9291  O  O   . HOH Z  5 .   ? 8.854   16.593  0.929   1.00 18.52 ? 492 HOH B O   1 
HETATM 9292  O  O   . HOH Z  5 .   ? 4.309   6.448   14.152  1.00 11.73 ? 493 HOH B O   1 
HETATM 9293  O  O   . HOH Z  5 .   ? -20.274 -11.808 8.131   1.00 26.23 ? 494 HOH B O   1 
HETATM 9294  O  O   . HOH Z  5 .   ? -14.049 -14.711 5.896   1.00 16.20 ? 495 HOH B O   1 
HETATM 9295  O  O   . HOH Z  5 .   ? -3.853  12.498  -18.186 1.00 17.91 ? 496 HOH B O   1 
HETATM 9296  O  O   . HOH Z  5 .   ? -5.541  1.471   -9.923  1.00 10.11 ? 497 HOH B O   1 
HETATM 9297  O  O   . HOH Z  5 .   ? -17.803 -3.829  26.622  1.00 25.63 ? 498 HOH B O   1 
HETATM 9298  O  O   . HOH Z  5 .   ? -15.947 -0.476  -14.930 1.00 18.62 ? 499 HOH B O   1 
HETATM 9299  O  O   . HOH Z  5 .   ? 4.914   -9.678  -12.110 1.00 24.46 ? 500 HOH B O   1 
HETATM 9300  O  O   . HOH Z  5 .   ? -22.970 -2.234  -8.692  1.00 13.80 ? 501 HOH B O   1 
HETATM 9301  O  O   . HOH Z  5 .   ? -3.080  -12.944 15.290  1.00 23.71 ? 502 HOH B O   1 
HETATM 9302  O  O   . HOH Z  5 .   ? -18.451 -8.121  16.023  1.00 17.47 ? 503 HOH B O   1 
HETATM 9303  O  O   . HOH Z  5 .   ? -8.972  -7.966  -14.418 1.00 16.24 ? 504 HOH B O   1 
HETATM 9304  O  O   . HOH Z  5 .   ? -1.790  20.527  8.363   1.00 29.47 ? 505 HOH B O   1 
HETATM 9305  O  O   . HOH Z  5 .   ? -5.961  2.369   -16.901 1.00 30.37 ? 506 HOH B O   1 
HETATM 9306  O  O   . HOH Z  5 .   ? -17.274 9.730   -14.326 1.00 35.50 ? 507 HOH B O   1 
HETATM 9307  O  O   . HOH Z  5 .   ? -10.342 -8.974  8.185   1.00 8.63  ? 508 HOH B O   1 
HETATM 9308  O  O   . HOH Z  5 .   ? -9.535  -20.237 25.155  1.00 31.86 ? 509 HOH B O   1 
HETATM 9309  O  O   . HOH Z  5 .   ? -7.934  12.646  4.926   1.00 38.60 ? 510 HOH B O   1 
HETATM 9310  O  O   . HOH Z  5 .   ? -2.884  -5.376  -4.140  1.00 9.62  ? 511 HOH B O   1 
HETATM 9311  O  O   . HOH Z  5 .   ? 2.732   -13.268 15.830  1.00 17.59 ? 512 HOH B O   1 
HETATM 9312  O  O   . HOH Z  5 .   ? -5.701  -11.796 -14.944 1.00 23.86 ? 513 HOH B O   1 
HETATM 9313  O  O   . HOH Z  5 .   ? -11.446 -17.462 21.255  1.00 37.52 ? 514 HOH B O   1 
HETATM 9314  O  O   . HOH Z  5 .   ? -33.177 7.234   6.748   1.00 41.42 ? 515 HOH B O   1 
HETATM 9315  O  O   . HOH Z  5 .   ? -21.885 -2.284  -12.582 1.00 29.41 ? 516 HOH B O   1 
HETATM 9316  O  O   . HOH Z  5 .   ? 5.304   5.477   7.662   1.00 10.55 ? 517 HOH B O   1 
HETATM 9317  O  O   . HOH Z  5 .   ? -32.006 -6.499  5.876   1.00 26.25 ? 518 HOH B O   1 
HETATM 9318  O  O   . HOH Z  5 .   ? -12.709 -9.265  -12.575 1.00 25.88 ? 519 HOH B O   1 
HETATM 9319  O  O   . HOH Z  5 .   ? 1.673   -1.627  5.805   1.00 9.37  ? 520 HOH B O   1 
HETATM 9320  O  O   . HOH Z  5 .   ? -24.120 0.851   20.937  1.00 25.28 ? 521 HOH B O   1 
HETATM 9321  O  O   . HOH Z  5 .   ? -16.961 -10.800 1.270   1.00 13.54 ? 522 HOH B O   1 
HETATM 9322  O  O   . HOH Z  5 .   ? -6.272  -18.274 -2.076  1.00 28.81 ? 523 HOH B O   1 
HETATM 9323  O  O   . HOH Z  5 .   ? -14.581 -14.304 19.853  1.00 31.96 ? 524 HOH B O   1 
HETATM 9324  O  O   . HOH Z  5 .   ? 4.149   9.958   -6.740  1.00 16.82 ? 525 HOH B O   1 
HETATM 9325  O  O   . HOH Z  5 .   ? 6.915   -11.545 17.266  1.00 20.01 ? 526 HOH B O   1 
HETATM 9326  O  O   . HOH Z  5 .   ? 1.463   14.308  -11.145 1.00 15.54 ? 527 HOH B O   1 
HETATM 9327  O  O   . HOH Z  5 .   ? 9.060   6.867   -2.276  1.00 27.79 ? 528 HOH B O   1 
HETATM 9328  O  O   . HOH Z  5 .   ? -17.088 11.217  1.655   1.00 24.62 ? 529 HOH B O   1 
HETATM 9329  O  O   . HOH Z  5 .   ? -16.857 2.728   22.781  1.00 41.77 ? 530 HOH B O   1 
HETATM 9330  O  O   . HOH Z  5 .   ? 8.072   4.538   5.145   1.00 9.25  ? 531 HOH B O   1 
HETATM 9331  O  O   . HOH Z  5 .   ? -27.378 6.696   -11.753 1.00 21.38 ? 532 HOH B O   1 
HETATM 9332  O  O   . HOH Z  5 .   ? -2.717  1.592   -14.619 1.00 23.34 ? 533 HOH B O   1 
HETATM 9333  O  O   . HOH Z  5 .   ? -1.089  5.750   -4.988  1.00 11.36 ? 534 HOH B O   1 
HETATM 9334  O  O   . HOH Z  5 .   ? 6.554   3.276   9.094   1.00 8.42  ? 535 HOH B O   1 
HETATM 9335  O  O   . HOH Z  5 .   ? 5.980   11.634  7.887   1.00 10.24 ? 536 HOH B O   1 
HETATM 9336  O  O   . HOH Z  5 .   ? -29.097 1.638   16.964  1.00 34.58 ? 537 HOH B O   1 
HETATM 9337  O  O   . HOH Z  5 .   ? 1.023   13.009  19.460  1.00 29.73 ? 538 HOH B O   1 
HETATM 9338  O  O   . HOH Z  5 .   ? -17.084 -10.469 20.186  1.00 14.74 ? 539 HOH B O   1 
HETATM 9339  O  O   . HOH Z  5 .   ? 5.320   14.218  -5.934  1.00 39.90 ? 540 HOH B O   1 
HETATM 9340  O  O   . HOH Z  5 .   ? -31.759 5.271   -7.482  1.00 18.42 ? 541 HOH B O   1 
HETATM 9341  O  O   . HOH Z  5 .   ? -17.915 -10.160 28.518  1.00 22.32 ? 542 HOH B O   1 
HETATM 9342  O  O   . HOH Z  5 .   ? -19.706 -16.084 10.270  1.00 23.58 ? 543 HOH B O   1 
HETATM 9343  O  O   . HOH Z  5 .   ? -27.007 -7.405  10.608  1.00 31.30 ? 544 HOH B O   1 
HETATM 9344  O  O   . HOH Z  5 .   ? -1.510  13.877  -4.473  1.00 23.12 ? 545 HOH B O   1 
HETATM 9345  O  O   . HOH Z  5 .   ? 4.086   -2.409  -3.292  1.00 28.45 ? 546 HOH B O   1 
HETATM 9346  O  O   . HOH Z  5 .   ? -26.346 10.397  5.193   1.00 30.62 ? 547 HOH B O   1 
HETATM 9347  O  O   . HOH Z  5 .   ? -1.914  -11.468 -3.023  1.00 15.17 ? 548 HOH B O   1 
HETATM 9348  O  O   . HOH Z  5 .   ? -4.648  0.291   21.827  1.00 20.37 ? 549 HOH B O   1 
HETATM 9349  O  O   . HOH Z  5 .   ? -6.533  -11.400 29.160  1.00 26.48 ? 550 HOH B O   1 
HETATM 9350  O  O   . HOH Z  5 .   ? 6.559   0.588   22.230  1.00 30.82 ? 551 HOH B O   1 
HETATM 9351  O  O   . HOH Z  5 .   ? -0.883  15.931  -8.588  1.00 23.91 ? 552 HOH B O   1 
HETATM 9352  O  O   . HOH Z  5 .   ? -1.367  -6.756  30.753  1.00 36.98 ? 553 HOH B O   1 
HETATM 9353  O  O   . HOH Z  5 .   ? -14.211 -2.326  -13.685 1.00 26.45 ? 554 HOH B O   1 
HETATM 9354  O  O   . HOH Z  5 .   ? -10.489 14.246  -13.665 1.00 14.62 ? 555 HOH B O   1 
HETATM 9355  O  O   . HOH Z  5 .   ? -14.389 13.860  -16.168 1.00 33.32 ? 556 HOH B O   1 
HETATM 9356  O  O   . HOH Z  5 .   ? 5.326   19.888  10.704  1.00 19.20 ? 557 HOH B O   1 
HETATM 9357  O  O   . HOH Z  5 .   ? -5.558  6.484   0.428   1.00 11.92 ? 558 HOH B O   1 
HETATM 9358  O  O   . HOH Z  5 .   ? -20.028 13.119  7.759   1.00 30.72 ? 559 HOH B O   1 
HETATM 9359  O  O   . HOH Z  5 .   ? -25.293 -7.325  12.969  1.00 26.83 ? 560 HOH B O   1 
HETATM 9360  O  O   . HOH Z  5 .   ? -4.854  -12.731 21.937  1.00 26.82 ? 561 HOH B O   1 
HETATM 9361  O  O   . HOH Z  5 .   ? -3.473  -3.025  29.048  1.00 34.38 ? 562 HOH B O   1 
HETATM 9362  O  O   . HOH Z  5 .   ? -0.042  -13.862 8.655   1.00 30.49 ? 563 HOH B O   1 
HETATM 9363  O  O   . HOH Z  5 .   ? -35.597 -3.801  -7.414  1.00 32.80 ? 564 HOH B O   1 
HETATM 9364  O  O   . HOH Z  5 .   ? -13.069 -17.361 6.962   1.00 36.97 ? 565 HOH B O   1 
HETATM 9365  O  O   . HOH Z  5 .   ? -1.155  -0.697  -12.640 1.00 16.21 ? 566 HOH B O   1 
HETATM 9366  O  O   . HOH Z  5 .   ? 1.647   8.862   -6.858  1.00 14.17 ? 567 HOH B O   1 
HETATM 9367  O  O   . HOH Z  5 .   ? -1.655  16.591  11.003  1.00 11.64 ? 568 HOH B O   1 
HETATM 9368  O  O   . HOH Z  5 .   ? -23.839 -8.010  20.318  1.00 34.14 ? 569 HOH B O   1 
HETATM 9369  O  O   . HOH Z  5 .   ? 2.231   5.040   -5.714  1.00 16.47 ? 570 HOH B O   1 
HETATM 9370  O  O   . HOH Z  5 .   ? -13.596 -18.326 -0.614  1.00 32.11 ? 571 HOH B O   1 
HETATM 9371  O  O   . HOH Z  5 .   ? -1.428  14.479  16.983  1.00 21.25 ? 572 HOH B O   1 
HETATM 9372  O  O   . HOH Z  5 .   ? -21.377 11.451  6.179   1.00 31.72 ? 573 HOH B O   1 
HETATM 9373  O  O   . HOH Z  5 .   ? 4.314   3.227   -6.000  1.00 20.22 ? 574 HOH B O   1 
HETATM 9374  O  O   . HOH Z  5 .   ? -0.702  11.948  16.171  1.00 12.87 ? 575 HOH B O   1 
HETATM 9375  O  O   . HOH Z  5 .   ? 6.475   4.800   13.725  1.00 12.42 ? 576 HOH B O   1 
HETATM 9376  O  O   . HOH Z  5 .   ? -29.764 -3.154  7.126   1.00 22.59 ? 577 HOH B O   1 
HETATM 9377  O  O   . HOH Z  5 .   ? -5.968  -15.343 13.196  1.00 24.48 ? 578 HOH B O   1 
HETATM 9378  O  O   . HOH Z  5 .   ? -1.828  9.503   -3.303  1.00 14.77 ? 579 HOH B O   1 
HETATM 9379  O  O   . HOH Z  5 .   ? -1.437  -9.818  -10.062 1.00 21.67 ? 580 HOH B O   1 
HETATM 9380  O  O   . HOH Z  5 .   ? -11.927 11.264  1.191   1.00 25.98 ? 581 HOH B O   1 
HETATM 9381  O  O   . HOH Z  5 .   ? -3.136  7.139   -3.881  1.00 12.65 ? 582 HOH B O   1 
HETATM 9382  O  O   . HOH Z  5 .   ? -23.279 11.335  -1.121  1.00 20.79 ? 583 HOH B O   1 
HETATM 9383  O  O   . HOH Z  5 .   ? 4.910   9.170   14.299  1.00 12.81 ? 584 HOH B O   1 
HETATM 9384  O  O   . HOH Z  5 .   ? -0.297  -13.201 22.738  1.00 31.13 ? 585 HOH B O   1 
HETATM 9385  O  O   . HOH Z  5 .   ? -14.574 -14.136 0.830   1.00 17.70 ? 586 HOH B O   1 
HETATM 9386  O  O   . HOH Z  5 .   ? -24.609 -10.802 -4.889  1.00 50.76 ? 587 HOH B O   1 
HETATM 9387  O  O   . HOH Z  5 .   ? -12.584 -0.530  22.671  1.00 22.99 ? 588 HOH B O   1 
HETATM 9388  O  O   . HOH Z  5 .   ? -3.513  2.064   -11.987 1.00 12.91 ? 589 HOH B O   1 
HETATM 9389  O  O   . HOH Z  5 .   ? 4.168   8.140   7.676   1.00 9.61  ? 590 HOH B O   1 
HETATM 9390  O  O   . HOH Z  5 .   ? 8.657   8.746   1.900   1.00 15.22 ? 591 HOH B O   1 
HETATM 9391  O  O   . HOH Z  5 .   ? 6.174   -9.980  -9.856  1.00 36.79 ? 592 HOH B O   1 
HETATM 9392  O  O   . HOH Z  5 .   ? -11.237 -15.768 3.215   1.00 27.66 ? 593 HOH B O   1 
HETATM 9393  O  O   . HOH Z  5 .   ? -7.100  6.965   19.113  1.00 21.25 ? 594 HOH B O   1 
HETATM 9394  O  O   . HOH Z  5 .   ? 0.669   7.982   -4.522  1.00 16.09 ? 595 HOH B O   1 
HETATM 9395  O  O   . HOH Z  5 .   ? 2.317   5.965   -12.454 1.00 20.64 ? 596 HOH B O   1 
HETATM 9396  O  O   . HOH Z  5 .   ? -14.385 -10.875 23.831  1.00 27.84 ? 597 HOH B O   1 
HETATM 9397  O  O   . HOH Z  5 .   ? 4.346   -2.078  6.449   1.00 15.21 ? 598 HOH B O   1 
HETATM 9398  O  O   . HOH Z  5 .   ? -5.951  15.024  2.428   1.00 45.45 ? 599 HOH B O   1 
HETATM 9399  O  O   . HOH Z  5 .   ? -26.612 9.551   12.168  1.00 44.43 ? 600 HOH B O   1 
HETATM 9400  O  O   . HOH Z  5 .   ? -14.569 -2.545  25.352  1.00 30.61 ? 601 HOH B O   1 
HETATM 9401  O  O   . HOH Z  5 .   ? -10.637 -10.455 29.690  1.00 21.65 ? 602 HOH B O   1 
HETATM 9402  O  O   . HOH Z  5 .   ? -24.219 8.868   -1.764  1.00 17.29 ? 603 HOH B O   1 
HETATM 9403  O  O   . HOH Z  5 .   ? -0.669  -0.037  26.794  1.00 37.74 ? 604 HOH B O   1 
HETATM 9404  O  O   . HOH Z  5 .   ? -16.745 6.237   -18.106 1.00 33.04 ? 605 HOH B O   1 
HETATM 9405  O  O   . HOH Z  5 .   ? 4.044   -9.341  3.064   1.00 20.99 ? 606 HOH B O   1 
HETATM 9406  O  O   . HOH Z  5 .   ? -10.914 16.967  -7.985  1.00 26.51 ? 607 HOH B O   1 
HETATM 9407  O  O   . HOH Z  5 .   ? -14.122 10.987  3.733   1.00 25.68 ? 608 HOH B O   1 
HETATM 9408  O  O   . HOH Z  5 .   ? -2.203  11.545  -5.198  1.00 16.24 ? 609 HOH B O   1 
HETATM 9409  O  O   . HOH Z  5 .   ? -32.371 -4.097  -1.908  1.00 26.20 ? 610 HOH B O   1 
HETATM 9410  O  O   . HOH Z  5 .   ? 6.933   -1.136  17.722  1.00 22.31 ? 611 HOH B O   1 
HETATM 9411  O  O   . HOH Z  5 .   ? -27.464 12.617  20.166  1.00 35.68 ? 612 HOH B O   1 
HETATM 9412  O  O   . HOH Z  5 .   ? -2.762  -0.268  25.229  1.00 22.11 ? 613 HOH B O   1 
HETATM 9413  O  O   . HOH Z  5 .   ? -22.723 5.971   -12.451 1.00 19.59 ? 614 HOH B O   1 
HETATM 9414  O  O   . HOH Z  5 .   ? -3.323  -12.455 -0.795  1.00 18.45 ? 615 HOH B O   1 
HETATM 9415  O  O   . HOH Z  5 .   ? -7.833  -16.360 -10.513 1.00 29.73 ? 616 HOH B O   1 
HETATM 9416  O  O   . HOH Z  5 .   ? -26.095 -9.738  6.119   1.00 22.82 ? 617 HOH B O   1 
HETATM 9417  O  O   . HOH Z  5 .   ? -17.600 12.458  -12.754 1.00 25.07 ? 618 HOH B O   1 
HETATM 9418  O  O   . HOH Z  5 .   ? -30.964 2.015   1.973   1.00 24.76 ? 619 HOH B O   1 
HETATM 9419  O  O   . HOH Z  5 .   ? -13.376 -11.994 11.636  1.00 11.78 ? 620 HOH B O   1 
HETATM 9420  O  O   . HOH Z  5 .   ? -28.855 -5.621  12.368  1.00 30.31 ? 621 HOH B O   1 
HETATM 9421  O  O   . HOH Z  5 .   ? -16.793 9.682   23.560  1.00 34.01 ? 622 HOH B O   1 
HETATM 9422  O  O   . HOH Z  5 .   ? 3.587   -16.156 18.084  1.00 35.85 ? 623 HOH B O   1 
HETATM 9423  O  O   . HOH Z  5 .   ? 11.306  14.615  -0.020  1.00 26.85 ? 624 HOH B O   1 
HETATM 9424  O  O   . HOH Z  5 .   ? 5.980   -6.073  14.715  1.00 22.27 ? 625 HOH B O   1 
HETATM 9425  O  O   . HOH Z  5 .   ? -8.303  -19.210 3.102   1.00 31.95 ? 626 HOH B O   1 
HETATM 9426  O  O   . HOH Z  5 .   ? 3.394   15.131  1.668   1.00 26.98 ? 627 HOH B O   1 
HETATM 9427  O  O   . HOH Z  5 .   ? 4.387   -13.373 22.321  1.00 32.22 ? 628 HOH B O   1 
HETATM 9428  O  O   . HOH Z  5 .   ? 2.423   7.242   -15.146 1.00 33.38 ? 629 HOH B O   1 
HETATM 9429  O  O   . HOH Z  5 .   ? -34.730 -2.769  -2.124  1.00 29.14 ? 630 HOH B O   1 
HETATM 9430  O  O   . HOH Z  5 .   ? -20.697 -0.304  -13.963 1.00 27.45 ? 631 HOH B O   1 
HETATM 9431  O  O   . HOH Z  5 .   ? -29.282 7.247   -1.586  1.00 29.25 ? 632 HOH B O   1 
HETATM 9432  O  O   . HOH Z  5 .   ? 5.858   -2.485  1.768   1.00 26.01 ? 633 HOH B O   1 
HETATM 9433  O  O   . HOH Z  5 .   ? 4.132   -4.835  0.891   1.00 27.03 ? 634 HOH B O   1 
HETATM 9434  O  O   . HOH Z  5 .   ? -6.531  15.498  15.839  1.00 30.32 ? 635 HOH B O   1 
HETATM 9435  O  O   . HOH Z  5 .   ? -6.372  17.910  11.462  1.00 43.53 ? 636 HOH B O   1 
HETATM 9436  O  O   . HOH Z  5 .   ? -11.893 -19.697 24.750  1.00 34.09 ? 637 HOH B O   1 
HETATM 9437  O  O   . HOH Z  5 .   ? 3.285   21.291  9.456   1.00 19.37 ? 638 HOH B O   1 
HETATM 9438  O  O   . HOH Z  5 .   ? -14.834 -14.705 -2.584  1.00 14.26 ? 639 HOH B O   1 
HETATM 9439  O  O   . HOH Z  5 .   ? -9.463  16.733  -15.919 1.00 23.17 ? 640 HOH B O   1 
HETATM 9440  O  O   . HOH Z  5 .   ? -4.274  -13.071 25.855  1.00 23.80 ? 641 HOH B O   1 
HETATM 9441  O  O   . HOH Z  5 .   ? -10.059 -3.026  24.541  1.00 38.57 ? 642 HOH B O   1 
HETATM 9442  O  O   . HOH Z  5 .   ? -0.863  -12.966 3.999   1.00 37.68 ? 643 HOH B O   1 
HETATM 9443  O  O   . HOH Z  5 .   ? 7.755   -3.335  3.478   1.00 20.93 ? 644 HOH B O   1 
HETATM 9444  O  O   . HOH Z  5 .   ? -0.702  -12.746 15.447  1.00 34.16 ? 645 HOH B O   1 
HETATM 9445  O  O   . HOH Z  5 .   ? -19.649 -13.765 14.417  1.00 21.30 ? 646 HOH B O   1 
HETATM 9446  O  O   . HOH Z  5 .   ? -20.292 -13.454 11.748  1.00 28.56 ? 647 HOH B O   1 
HETATM 9447  O  O   . HOH Z  5 .   ? -2.619  -12.977 23.937  1.00 33.89 ? 648 HOH B O   1 
HETATM 9448  O  O   . HOH Z  5 .   ? -29.543 8.360   6.263   1.00 38.62 ? 649 HOH B O   1 
HETATM 9449  O  O   . HOH Z  5 .   ? -27.320 -6.239  -4.765  1.00 33.74 ? 650 HOH B O   1 
HETATM 9450  O  O   . HOH Z  5 .   ? -9.799  -18.205 12.626  1.00 36.03 ? 651 HOH B O   1 
HETATM 9451  O  O   . HOH Z  5 .   ? -8.740  1.752   -19.434 1.00 34.89 ? 652 HOH B O   1 
HETATM 9452  O  O   . HOH Z  5 .   ? -12.829 18.188  5.733   1.00 46.21 ? 653 HOH B O   1 
HETATM 9453  O  O   . HOH Z  5 .   ? -4.623  17.764  -7.988  1.00 30.79 ? 654 HOH B O   1 
HETATM 9454  O  O   . HOH Z  5 .   ? -20.497 12.098  -12.972 1.00 33.89 ? 655 HOH B O   1 
HETATM 9455  O  O   . HOH Z  5 .   ? -15.201 20.989  9.845   1.00 42.86 ? 656 HOH B O   1 
HETATM 9456  O  O   . HOH Z  5 .   ? -30.149 4.679   2.521   1.00 29.76 ? 657 HOH B O   1 
HETATM 9457  O  O   . HOH Z  5 .   ? -24.576 -1.210  -11.574 1.00 22.68 ? 658 HOH B O   1 
HETATM 9458  O  O   . HOH Z  5 .   ? -2.529  -10.696 -14.873 1.00 29.74 ? 659 HOH B O   1 
HETATM 9459  O  O   . HOH Z  5 .   ? -13.435 9.327   -18.223 1.00 33.07 ? 660 HOH B O   1 
HETATM 9460  O  O   . HOH Z  5 .   ? -0.465  21.508  0.224   1.00 38.98 ? 661 HOH B O   1 
HETATM 9461  O  O   . HOH Z  5 .   ? -20.504 -4.120  26.034  1.00 30.17 ? 662 HOH B O   1 
HETATM 9462  O  O   . HOH Z  5 .   ? -13.306 -16.325 23.675  1.00 37.34 ? 663 HOH B O   1 
HETATM 9463  O  O   . HOH Z  5 .   ? 1.576   -0.632  -12.186 1.00 28.61 ? 664 HOH B O   1 
HETATM 9464  O  O   . HOH Z  5 .   ? -21.451 -6.725  -9.863  1.00 30.66 ? 665 HOH B O   1 
HETATM 9465  O  O   . HOH Z  5 .   ? 7.721   1.360   19.699  1.00 25.59 ? 666 HOH B O   1 
HETATM 9466  O  O   . HOH Z  5 .   ? 12.338  11.417  -3.559  1.00 31.19 ? 667 HOH B O   1 
HETATM 9467  O  O   . HOH Z  5 .   ? -13.532 13.481  -2.478  1.00 40.66 ? 668 HOH B O   1 
HETATM 9468  O  O   . HOH Z  5 .   ? -9.873  20.118  -8.674  1.00 37.01 ? 669 HOH B O   1 
HETATM 9469  O  O   . HOH Z  5 .   ? 3.263   14.177  -7.234  1.00 42.52 ? 670 HOH B O   1 
HETATM 9470  O  O   . HOH Z  5 .   ? -8.735  17.223  -3.374  1.00 38.94 ? 671 HOH B O   1 
HETATM 9471  O  O   . HOH Z  5 .   ? -17.614 -14.162 -2.226  1.00 23.91 ? 672 HOH B O   1 
HETATM 9472  O  O   . HOH Z  5 .   ? -23.185 -4.594  -10.186 1.00 27.10 ? 673 HOH B O   1 
HETATM 9473  O  O   . HOH Z  5 .   ? -32.746 9.707   -7.375  1.00 38.98 ? 674 HOH B O   1 
HETATM 9474  O  O   . HOH Z  5 .   ? -0.209  -13.268 -4.273  1.00 27.01 ? 675 HOH B O   1 
HETATM 9475  O  O   . HOH Z  5 .   ? -14.744 1.497   23.276  1.00 32.31 ? 676 HOH B O   1 
HETATM 9476  O  O   . HOH Z  5 .   ? 5.901   2.190   -3.704  1.00 26.06 ? 677 HOH B O   1 
HETATM 9477  O  O   . HOH Z  5 .   ? 6.329   -5.748  11.171  1.00 29.71 ? 678 HOH B O   1 
HETATM 9478  O  O   . HOH Z  5 .   ? -13.333 -16.434 1.427   1.00 43.13 ? 679 HOH B O   1 
HETATM 9479  O  O   . HOH Z  5 .   ? -18.402 -13.730 0.044   1.00 40.80 ? 680 HOH B O   1 
HETATM 9480  O  O   . HOH Z  5 .   ? -29.637 6.977   1.148   1.00 29.67 ? 681 HOH B O   1 
HETATM 9481  O  O   . HOH Z  5 .   ? -11.019 14.954  -5.541  1.00 36.02 ? 682 HOH B O   1 
HETATM 9482  O  O   . HOH Z  5 .   ? -8.166  -5.642  -15.584 1.00 24.80 ? 683 HOH B O   1 
HETATM 9483  O  O   . HOH Z  5 .   ? -22.358 11.975  -10.791 1.00 43.73 ? 684 HOH B O   1 
HETATM 9484  O  O   . HOH Z  5 .   ? 5.230   11.997  -11.103 1.00 38.48 ? 685 HOH B O   1 
HETATM 9485  O  O   . HOH Z  5 .   ? 1.070   22.593  10.188  1.00 25.22 ? 686 HOH B O   1 
HETATM 9486  O  O   . HOH Z  5 .   ? -29.247 -7.595  6.449   1.00 28.05 ? 687 HOH B O   1 
HETATM 9487  O  O   . HOH Z  5 .   ? 3.967   14.615  -10.507 1.00 32.73 ? 688 HOH B O   1 
HETATM 9488  O  O   . HOH Z  5 .   ? -23.876 -11.113 5.527   1.00 37.72 ? 689 HOH B O   1 
HETATM 9489  O  O   . HOH Z  5 .   ? 7.806   5.815   0.686   1.00 19.53 ? 690 HOH B O   1 
HETATM 9490  O  O   . HOH Z  5 .   ? -21.619 10.209  -14.489 1.00 36.61 ? 691 HOH B O   1 
HETATM 9491  O  O   . HOH Z  5 .   ? 2.375   -11.300 -11.716 1.00 36.67 ? 692 HOH B O   1 
HETATM 9492  O  O   . HOH Z  5 .   ? -16.779 -14.153 27.698  1.00 21.81 ? 693 HOH B O   1 
HETATM 9493  O  O   . HOH Z  5 .   ? 4.347   15.373  17.870  1.00 25.67 ? 694 HOH B O   1 
HETATM 9494  O  O   . HOH Z  5 .   ? -17.531 -16.808 3.611   1.00 44.05 ? 695 HOH B O   1 
HETATM 9495  O  O   . HOH Z  5 .   ? -19.071 -16.301 -3.773  1.00 29.78 ? 696 HOH B O   1 
HETATM 9496  O  O   . HOH Z  5 .   ? 2.000   -15.761 16.447  1.00 27.85 ? 697 HOH B O   1 
HETATM 9497  O  O   . HOH Z  5 .   ? -21.444 -12.185 15.896  1.00 28.38 ? 698 HOH B O   1 
HETATM 9498  O  O   . HOH Z  5 .   ? -11.581 -8.475  -14.955 1.00 23.98 ? 699 HOH B O   1 
HETATM 9499  O  O   . HOH Z  5 .   ? 4.297   -12.023 24.728  1.00 33.38 ? 700 HOH B O   1 
HETATM 9500  O  O   . HOH Z  5 .   ? 8.317   10.317  -7.674  1.00 39.61 ? 701 HOH B O   1 
HETATM 9501  O  O   . HOH Z  5 .   ? -12.079 -1.684  24.975  1.00 31.92 ? 702 HOH B O   1 
HETATM 9502  O  O   . HOH Z  5 .   ? -0.187  -16.521 15.077  1.00 32.46 ? 703 HOH B O   1 
HETATM 9503  O  O   . HOH Z  5 .   ? 7.560   -9.456  15.668  1.00 17.16 ? 704 HOH B O   1 
HETATM 9504  O  O   . HOH Z  5 .   ? -13.243 17.668  -8.692  1.00 30.50 ? 705 HOH B O   1 
HETATM 9505  O  O   . HOH Z  5 .   ? -8.275  -0.122  23.149  1.00 39.09 ? 706 HOH B O   1 
HETATM 9506  O  O   . HOH Z  5 .   ? 5.321   -13.103 15.739  1.00 20.81 ? 707 HOH B O   1 
HETATM 9507  O  O   . HOH Z  5 .   ? 5.824   -0.564  -2.593  1.00 26.28 ? 708 HOH B O   1 
HETATM 9508  O  O   . HOH Z  5 .   ? -22.811 -12.624 1.045   1.00 36.60 ? 709 HOH B O   1 
HETATM 9509  O  O   . HOH Z  5 .   ? -24.372 -9.728  -7.795  1.00 35.76 ? 710 HOH B O   1 
HETATM 9510  O  O   . HOH Z  5 .   ? -17.742 -12.830 21.178  1.00 25.90 ? 711 HOH B O   1 
HETATM 9511  O  O   . HOH Z  5 .   ? -4.450  -13.728 9.706   1.00 32.90 ? 712 HOH B O   1 
HETATM 9512  O  O   . HOH Z  5 .   ? -15.611 -14.538 3.492   1.00 25.55 ? 713 HOH B O   1 
HETATM 9513  O  O   . HOH Z  5 .   ? -1.324  21.674  10.754  1.00 38.62 ? 714 HOH B O   1 
HETATM 9514  O  O   . HOH Z  5 .   ? 4.992   -7.358  1.212   1.00 19.80 ? 715 HOH B O   1 
HETATM 9515  O  O   . HOH Z  5 .   ? -10.863 16.825  -18.590 1.00 32.79 ? 716 HOH B O   1 
HETATM 9516  O  O   . HOH Z  5 .   ? -18.649 -11.809 23.811  1.00 29.72 ? 717 HOH B O   1 
HETATM 9517  O  O   . HOH Z  5 .   ? -3.309  -17.476 19.856  1.00 26.56 ? 718 HOH B O   1 
HETATM 9518  O  O   . HOH Z  5 .   ? 1.499   -15.281 22.872  1.00 27.68 ? 719 HOH B O   1 
HETATM 9519  O  O   . HOH Z  5 .   ? -15.265 -16.979 -0.955  1.00 33.09 ? 720 HOH B O   1 
HETATM 9520  O  O   . HOH Z  5 .   ? -2.344  -15.585 22.880  1.00 31.54 ? 721 HOH B O   1 
HETATM 9521  O  O   . HOH Z  5 .   ? -13.253 -21.419 4.045   1.00 30.92 ? 722 HOH B O   1 
HETATM 9522  O  O   . HOH Z  5 .   ? -0.557  -12.103 -8.823  1.00 21.28 ? 723 HOH B O   1 
HETATM 9523  O  O   . HOH Z  5 .   ? -3.436  15.184  18.566  1.00 30.62 ? 724 HOH B O   1 
HETATM 9524  O  O   . HOH Z  5 .   ? -29.217 -6.372  -2.643  1.00 35.29 ? 725 HOH B O   1 
HETATM 9525  O  O   . HOH Z  5 .   ? 0.929   15.548  17.699  1.00 38.67 ? 726 HOH B O   1 
HETATM 9526  O  O   . HOH Z  5 .   ? -4.164  1.787   24.041  1.00 31.69 ? 727 HOH B O   1 
HETATM 9527  O  O   . HOH Z  5 .   ? 5.527   9.886   -9.040  1.00 32.61 ? 728 HOH B O   1 
HETATM 9528  O  O   . HOH Z  5 .   ? -15.778 14.833  -13.925 1.00 38.90 ? 729 HOH B O   1 
HETATM 9529  O  O   . HOH Z  5 .   ? -20.988 -11.001 -9.947  1.00 25.62 ? 730 HOH B O   1 
HETATM 9530  O  O   . HOH Z  5 .   ? -0.884  24.063  7.019   1.00 38.48 ? 731 HOH B O   1 
HETATM 9531  O  O   . HOH Z  5 .   ? -9.064  15.360  5.152   1.00 34.32 ? 732 HOH B O   1 
HETATM 9532  O  O   . HOH Z  5 .   ? 3.901   6.049   -9.974  1.00 27.12 ? 733 HOH B O   1 
HETATM 9533  O  O   . HOH Z  5 .   ? -3.054  18.915  10.481  1.00 26.92 ? 734 HOH B O   1 
HETATM 9534  O  O   . HOH Z  5 .   ? -2.660  10.881  21.076  1.00 40.18 ? 735 HOH B O   1 
HETATM 9535  O  O   . HOH Z  5 .   ? 2.012   18.622  -11.552 1.00 37.10 ? 736 HOH B O   1 
HETATM 9536  O  O   . HOH Z  5 .   ? -6.008  -15.546 7.855   1.00 36.49 ? 737 HOH B O   1 
HETATM 9537  O  O   . HOH Z  5 .   ? -1.975  -15.476 11.158  1.00 29.87 ? 738 HOH B O   1 
HETATM 9538  O  O   . HOH Z  5 .   ? -12.914 -14.223 30.803  1.00 19.36 ? 739 HOH B O   1 
HETATM 9539  O  O   . HOH Z  5 .   ? -2.449  -14.560 8.907   1.00 41.72 ? 740 HOH B O   1 
HETATM 9540  O  O   . HOH Z  5 .   ? -19.051 -16.164 15.482  1.00 35.93 ? 741 HOH B O   1 
HETATM 9541  O  O   . HOH Z  5 .   ? -2.004  20.360  13.137  1.00 36.01 ? 742 HOH B O   1 
HETATM 9542  O  O   . HOH Z  5 .   ? -10.367 -13.080 30.543  1.00 24.92 ? 743 HOH B O   1 
HETATM 9543  O  O   . HOH Z  5 .   ? -0.876  -14.273 6.273   1.00 34.95 ? 744 HOH B O   1 
HETATM 9544  O  O   . HOH Z  5 .   ? -7.702  -10.023 -15.936 1.00 18.39 ? 745 HOH B O   1 
HETATM 9545  O  O   . HOH Z  5 .   ? 12.797  11.495  -6.264  1.00 29.93 ? 746 HOH B O   1 
HETATM 9546  O  O   . HOH Z  5 .   ? -2.765  3.917   23.845  1.00 39.92 ? 747 HOH B O   1 
HETATM 9547  O  O   . HOH Z  5 .   ? -25.843 -5.933  -8.962  1.00 35.71 ? 748 HOH B O   1 
HETATM 9548  O  O   . HOH Z  5 .   ? -21.679 -13.699 18.265  1.00 32.43 ? 749 HOH B O   1 
HETATM 9549  O  O   . HOH Z  5 .   ? -17.310 -18.241 0.033   1.00 38.19 ? 750 HOH B O   1 
HETATM 9550  O  O   . HOH Z  5 .   ? -19.160 -16.103 1.107   1.00 40.27 ? 751 HOH B O   1 
HETATM 9551  O  O   . HOH AA 5 .   ? 59.468  4.660   -34.546 1.00 41.09 ? 401 HOH C O   1 
HETATM 9552  O  O   . HOH AA 5 .   ? 62.005  4.484   -31.989 1.00 32.15 ? 402 HOH C O   1 
HETATM 9553  O  O   . HOH AA 5 .   ? 37.698  5.881   -28.070 1.00 22.81 ? 403 HOH C O   1 
HETATM 9554  O  O   . HOH AA 5 .   ? 20.805  -1.879  -50.600 1.00 26.30 ? 404 HOH C O   1 
HETATM 9555  O  O   . HOH AA 5 .   ? 51.001  11.179  -16.033 1.00 37.46 ? 405 HOH C O   1 
HETATM 9556  O  O   . HOH AA 5 .   ? 55.753  5.529   -22.347 1.00 33.73 ? 406 HOH C O   1 
HETATM 9557  O  O   . HOH AA 5 .   ? 57.107  -8.221  -23.133 1.00 30.75 ? 407 HOH C O   1 
HETATM 9558  O  O   . HOH AA 5 .   ? 19.727  1.249   -51.599 1.00 23.76 ? 408 HOH C O   1 
HETATM 9559  O  O   . HOH AA 5 .   ? 20.441  17.948  -29.821 1.00 27.53 ? 409 HOH C O   1 
HETATM 9560  O  O   . HOH AA 5 .   ? 33.321  -1.375  -48.780 1.00 18.81 ? 410 HOH C O   1 
HETATM 9561  O  O   . HOH AA 5 .   ? 56.364  8.040   -37.409 1.00 27.67 ? 411 HOH C O   1 
HETATM 9562  O  O   . HOH AA 5 .   ? 37.478  17.144  -30.054 1.00 34.76 ? 412 HOH C O   1 
HETATM 9563  O  O   . HOH AA 5 .   ? 34.366  -4.779  -55.040 1.00 39.71 ? 413 HOH C O   1 
HETATM 9564  O  O   . HOH AA 5 .   ? 47.790  -13.708 -29.740 1.00 38.69 ? 414 HOH C O   1 
HETATM 9565  O  O   . HOH AA 5 .   ? 52.699  4.853   -48.783 1.00 23.20 ? 415 HOH C O   1 
HETATM 9566  O  O   . HOH AA 5 .   ? 24.479  -14.431 -47.742 1.00 42.05 ? 416 HOH C O   1 
HETATM 9567  O  O   . HOH AA 5 .   ? 28.419  18.334  -31.531 1.00 17.49 ? 417 HOH C O   1 
HETATM 9568  O  O   . HOH AA 5 .   ? 46.746  -3.342  -48.323 1.00 40.72 ? 418 HOH C O   1 
HETATM 9569  O  O   . HOH AA 5 .   ? 35.253  -16.736 -14.267 1.00 40.90 ? 419 HOH C O   1 
HETATM 9570  O  O   . HOH AA 5 .   ? 56.257  3.736   -12.894 1.00 17.27 ? 420 HOH C O   1 
HETATM 9571  O  O   . HOH AA 5 .   ? 28.741  -7.785  -17.033 1.00 21.02 ? 421 HOH C O   1 
HETATM 9572  O  O   . HOH AA 5 .   ? 49.684  -5.496  -49.188 1.00 42.27 ? 422 HOH C O   1 
HETATM 9573  O  O   . HOH AA 5 .   ? 59.853  -2.205  -35.090 1.00 33.47 ? 423 HOH C O   1 
HETATM 9574  O  O   . HOH AA 5 .   ? 22.192  -0.930  -23.710 1.00 23.49 ? 424 HOH C O   1 
HETATM 9575  O  O   . HOH AA 5 .   ? 23.471  -12.467 -29.318 1.00 33.52 ? 425 HOH C O   1 
HETATM 9576  O  O   . HOH AA 5 .   ? 40.704  -5.350  -52.542 1.00 27.16 ? 426 HOH C O   1 
HETATM 9577  O  O   . HOH AA 5 .   ? 35.826  -13.521 -54.360 1.00 19.10 ? 427 HOH C O   1 
HETATM 9578  O  O   . HOH AA 5 .   ? 32.557  5.148   -30.393 1.00 10.95 ? 428 HOH C O   1 
HETATM 9579  O  O   . HOH AA 5 .   ? 33.512  22.443  -35.054 1.00 32.96 ? 429 HOH C O   1 
HETATM 9580  O  O   . HOH AA 5 .   ? 47.085  -14.686 -32.119 1.00 29.93 ? 430 HOH C O   1 
HETATM 9581  O  O   . HOH AA 5 .   ? 22.454  -8.894  -39.706 1.00 25.22 ? 431 HOH C O   1 
HETATM 9582  O  O   . HOH AA 5 .   ? 50.288  -4.555  -16.178 1.00 35.40 ? 432 HOH C O   1 
HETATM 9583  O  O   . HOH AA 5 .   ? 53.035  6.303   -31.257 1.00 17.08 ? 433 HOH C O   1 
HETATM 9584  O  O   . HOH AA 5 .   ? 41.990  6.912   -9.879  1.00 29.85 ? 434 HOH C O   1 
HETATM 9585  O  O   . HOH AA 5 .   ? 33.796  -16.279 -16.846 1.00 30.55 ? 435 HOH C O   1 
HETATM 9586  O  O   . HOH AA 5 .   ? 51.943  -5.148  -18.077 1.00 34.12 ? 436 HOH C O   1 
HETATM 9587  O  O   . HOH AA 5 .   ? 44.007  -14.764 -27.803 1.00 27.75 ? 437 HOH C O   1 
HETATM 9588  O  O   . HOH AA 5 .   ? 21.325  17.992  -27.648 1.00 44.02 ? 438 HOH C O   1 
HETATM 9589  O  O   . HOH AA 5 .   ? 53.903  6.974   -27.627 1.00 20.63 ? 439 HOH C O   1 
HETATM 9590  O  O   . HOH AA 5 .   ? 40.204  -7.927  -13.753 1.00 33.48 ? 440 HOH C O   1 
HETATM 9591  O  O   . HOH AA 5 .   ? 43.372  -2.288  -40.310 1.00 11.62 ? 441 HOH C O   1 
HETATM 9592  O  O   . HOH AA 5 .   ? 27.204  -15.052 -38.318 1.00 38.38 ? 442 HOH C O   1 
HETATM 9593  O  O   . HOH AA 5 .   ? 26.115  5.489   -43.355 1.00 22.28 ? 443 HOH C O   1 
HETATM 9594  O  O   . HOH AA 5 .   ? 58.157  -3.550  -41.577 1.00 43.04 ? 444 HOH C O   1 
HETATM 9595  O  O   . HOH AA 5 .   ? 43.883  -5.468  -50.091 1.00 25.01 ? 445 HOH C O   1 
HETATM 9596  O  O   . HOH AA 5 .   ? 54.018  -13.251 -25.441 1.00 28.59 ? 446 HOH C O   1 
HETATM 9597  O  O   . HOH AA 5 .   ? 27.959  16.031  -29.280 1.00 28.27 ? 447 HOH C O   1 
HETATM 9598  O  O   . HOH AA 5 .   ? 25.341  -1.661  -40.518 1.00 12.46 ? 448 HOH C O   1 
HETATM 9599  O  O   . HOH AA 5 .   ? 39.899  13.999  -12.613 1.00 35.50 ? 449 HOH C O   1 
HETATM 9600  O  O   . HOH AA 5 .   ? 47.298  -1.657  -9.605  1.00 24.86 ? 450 HOH C O   1 
HETATM 9601  O  O   . HOH AA 5 .   ? 23.955  9.023   -34.904 1.00 12.47 ? 451 HOH C O   1 
HETATM 9602  O  O   . HOH AA 5 .   ? 33.388  12.044  -11.050 1.00 28.46 ? 452 HOH C O   1 
HETATM 9603  O  O   . HOH AA 5 .   ? 35.404  17.135  -41.466 1.00 25.43 ? 453 HOH C O   1 
HETATM 9604  O  O   . HOH AA 5 .   ? 46.748  -0.860  -47.365 1.00 30.99 ? 454 HOH C O   1 
HETATM 9605  O  O   . HOH AA 5 .   ? 29.712  -4.779  -22.002 1.00 14.62 ? 455 HOH C O   1 
HETATM 9606  O  O   . HOH AA 5 .   ? 53.958  -10.172 -22.406 1.00 27.65 ? 456 HOH C O   1 
HETATM 9607  O  O   . HOH AA 5 .   ? 46.891  11.439  -21.760 1.00 34.82 ? 457 HOH C O   1 
HETATM 9608  O  O   . HOH AA 5 .   ? 26.426  -8.278  -15.866 1.00 24.62 ? 458 HOH C O   1 
HETATM 9609  O  O   . HOH AA 5 .   ? 40.285  -16.503 -30.224 1.00 22.99 ? 459 HOH C O   1 
HETATM 9610  O  O   . HOH AA 5 .   ? 26.394  6.915   -14.240 1.00 36.24 ? 460 HOH C O   1 
HETATM 9611  O  O   . HOH AA 5 .   ? 24.069  13.096  -42.323 1.00 15.94 ? 461 HOH C O   1 
HETATM 9612  O  O   . HOH AA 5 .   ? 25.286  8.284   -27.949 1.00 14.31 ? 462 HOH C O   1 
HETATM 9613  O  O   . HOH AA 5 .   ? 61.143  -9.540  -28.269 1.00 42.69 ? 463 HOH C O   1 
HETATM 9614  O  O   . HOH AA 5 .   ? 52.315  1.045   -12.955 1.00 28.52 ? 464 HOH C O   1 
HETATM 9615  O  O   . HOH AA 5 .   ? 22.400  -6.254  -31.334 1.00 19.79 ? 465 HOH C O   1 
HETATM 9616  O  O   . HOH AA 5 .   ? 27.461  16.318  -41.161 1.00 13.64 ? 466 HOH C O   1 
HETATM 9617  O  O   . HOH AA 5 .   ? 41.745  -8.263  -54.722 1.00 18.07 ? 467 HOH C O   1 
HETATM 9618  O  O   . HOH AA 5 .   ? 30.375  -9.817  -16.317 1.00 27.39 ? 468 HOH C O   1 
HETATM 9619  O  O   . HOH AA 5 .   ? 28.750  3.364   -43.407 1.00 15.02 ? 469 HOH C O   1 
HETATM 9620  O  O   . HOH AA 5 .   ? 54.664  -10.006 -30.729 1.00 22.71 ? 470 HOH C O   1 
HETATM 9621  O  O   . HOH AA 5 .   ? 46.827  2.054   -47.176 1.00 30.79 ? 471 HOH C O   1 
HETATM 9622  O  O   . HOH AA 5 .   ? 25.827  5.362   -23.952 1.00 32.10 ? 472 HOH C O   1 
HETATM 9623  O  O   . HOH AA 5 .   ? 23.635  -4.565  -35.851 1.00 18.54 ? 473 HOH C O   1 
HETATM 9624  O  O   . HOH AA 5 .   ? 56.755  4.578   -41.886 1.00 18.03 ? 474 HOH C O   1 
HETATM 9625  O  O   . HOH AA 5 .   ? 53.533  -3.547  -46.012 1.00 30.75 ? 475 HOH C O   1 
HETATM 9626  O  O   . HOH AA 5 .   ? 24.125  -3.106  -27.191 1.00 34.10 ? 476 HOH C O   1 
HETATM 9627  O  O   . HOH AA 5 .   ? 46.525  8.203   -11.369 1.00 21.49 ? 477 HOH C O   1 
HETATM 9628  O  O   . HOH AA 5 .   ? 44.672  -14.762 -50.067 1.00 29.69 ? 478 HOH C O   1 
HETATM 9629  O  O   . HOH AA 5 .   ? 47.054  7.210   -22.804 1.00 21.92 ? 479 HOH C O   1 
HETATM 9630  O  O   . HOH AA 5 .   ? 22.543  -1.993  -31.119 1.00 30.09 ? 480 HOH C O   1 
HETATM 9631  O  O   . HOH AA 5 .   ? 32.915  -13.307 -36.815 1.00 20.46 ? 481 HOH C O   1 
HETATM 9632  O  O   . HOH AA 5 .   ? 26.180  7.045   -41.120 1.00 11.51 ? 482 HOH C O   1 
HETATM 9633  O  O   . HOH AA 5 .   ? 53.311  14.505  -44.482 1.00 40.68 ? 483 HOH C O   1 
HETATM 9634  O  O   . HOH AA 5 .   ? 50.029  -9.229  -45.882 1.00 26.76 ? 484 HOH C O   1 
HETATM 9635  O  O   . HOH AA 5 .   ? 25.097  6.544   -34.565 1.00 10.42 ? 485 HOH C O   1 
HETATM 9636  O  O   . HOH AA 5 .   ? 37.493  8.986   -47.343 1.00 25.28 ? 486 HOH C O   1 
HETATM 9637  O  O   . HOH AA 5 .   ? 20.263  -10.148 -29.774 1.00 18.20 ? 487 HOH C O   1 
HETATM 9638  O  O   . HOH AA 5 .   ? 51.720  -2.401  -43.517 1.00 20.29 ? 488 HOH C O   1 
HETATM 9639  O  O   . HOH AA 5 .   ? 48.147  -10.905 -15.927 1.00 27.57 ? 489 HOH C O   1 
HETATM 9640  O  O   . HOH AA 5 .   ? 24.767  -12.912 -41.439 1.00 24.24 ? 490 HOH C O   1 
HETATM 9641  O  O   . HOH AA 5 .   ? 26.008  -3.435  -42.524 1.00 17.77 ? 491 HOH C O   1 
HETATM 9642  O  O   . HOH AA 5 .   ? 38.880  -2.875  -11.417 1.00 38.22 ? 492 HOH C O   1 
HETATM 9643  O  O   . HOH AA 5 .   ? 54.454  9.685   -33.868 1.00 29.66 ? 493 HOH C O   1 
HETATM 9644  O  O   . HOH AA 5 .   ? 47.147  9.127   -27.231 1.00 20.16 ? 494 HOH C O   1 
HETATM 9645  O  O   . HOH AA 5 .   ? 57.522  8.019   -47.195 1.00 29.27 ? 495 HOH C O   1 
HETATM 9646  O  O   . HOH AA 5 .   ? 34.216  16.018  -38.216 1.00 10.95 ? 496 HOH C O   1 
HETATM 9647  O  O   . HOH AA 5 .   ? 27.437  -10.187 -26.520 1.00 19.98 ? 497 HOH C O   1 
HETATM 9648  O  O   . HOH AA 5 .   ? 56.487  9.157   -40.072 1.00 27.08 ? 498 HOH C O   1 
HETATM 9649  O  O   . HOH AA 5 .   ? 54.184  -7.062  -18.055 1.00 33.05 ? 499 HOH C O   1 
HETATM 9650  O  O   . HOH AA 5 .   ? 44.902  -13.863 -44.461 1.00 18.87 ? 500 HOH C O   1 
HETATM 9651  O  O   . HOH AA 5 .   ? 54.735  1.251   -14.658 1.00 32.39 ? 501 HOH C O   1 
HETATM 9652  O  O   . HOH AA 5 .   ? 58.754  -2.274  -29.758 1.00 27.00 ? 502 HOH C O   1 
HETATM 9653  O  O   . HOH AA 5 .   ? 43.833  4.194   -44.234 1.00 17.61 ? 503 HOH C O   1 
HETATM 9654  O  O   . HOH AA 5 .   ? 49.110  1.884   -12.460 1.00 32.55 ? 504 HOH C O   1 
HETATM 9655  O  O   . HOH AA 5 .   ? 48.090  -12.864 -39.121 1.00 23.99 ? 505 HOH C O   1 
HETATM 9656  O  O   . HOH AA 5 .   ? 48.636  -13.048 -33.827 1.00 31.02 ? 506 HOH C O   1 
HETATM 9657  O  O   . HOH AA 5 .   ? 46.382  -11.220 -40.325 1.00 20.71 ? 507 HOH C O   1 
HETATM 9658  O  O   . HOH AA 5 .   ? 57.619  11.721  -37.145 1.00 32.25 ? 508 HOH C O   1 
HETATM 9659  O  O   . HOH AA 5 .   ? 55.867  -8.226  -32.585 1.00 19.15 ? 509 HOH C O   1 
HETATM 9660  O  O   . HOH AA 5 .   ? 55.587  14.757  -35.051 1.00 34.48 ? 510 HOH C O   1 
HETATM 9661  O  O   . HOH AA 5 .   ? 40.877  14.053  -36.775 1.00 25.79 ? 511 HOH C O   1 
HETATM 9662  O  O   . HOH AA 5 .   ? 27.319  7.673   -18.734 1.00 34.45 ? 512 HOH C O   1 
HETATM 9663  O  O   . HOH AA 5 .   ? 37.798  -10.319 -33.179 1.00 12.77 ? 513 HOH C O   1 
HETATM 9664  O  O   . HOH AA 5 .   ? 22.513  0.366   -27.842 1.00 23.81 ? 514 HOH C O   1 
HETATM 9665  O  O   . HOH AA 5 .   ? 27.162  -0.772  -32.120 1.00 10.07 ? 515 HOH C O   1 
HETATM 9666  O  O   . HOH AA 5 .   ? 46.808  8.990   -49.514 1.00 29.77 ? 516 HOH C O   1 
HETATM 9667  O  O   . HOH AA 5 .   ? 60.157  -7.803  -20.931 1.00 34.02 ? 517 HOH C O   1 
HETATM 9668  O  O   . HOH AA 5 .   ? 33.931  1.720   -16.560 1.00 16.70 ? 518 HOH C O   1 
HETATM 9669  O  O   . HOH AA 5 .   ? 34.854  -7.659  -11.119 1.00 29.55 ? 519 HOH C O   1 
HETATM 9670  O  O   . HOH AA 5 .   ? 62.021  -1.008  -32.565 1.00 22.75 ? 520 HOH C O   1 
HETATM 9671  O  O   . HOH AA 5 .   ? 32.049  2.551   -43.597 1.00 14.31 ? 521 HOH C O   1 
HETATM 9672  O  O   . HOH AA 5 .   ? 47.185  9.110   -30.031 1.00 21.55 ? 522 HOH C O   1 
HETATM 9673  O  O   . HOH AA 5 .   ? 35.310  6.138   -26.699 1.00 17.84 ? 523 HOH C O   1 
HETATM 9674  O  O   . HOH AA 5 .   ? 24.642  19.052  -28.899 1.00 36.30 ? 524 HOH C O   1 
HETATM 9675  O  O   . HOH AA 5 .   ? 20.926  13.572  -35.553 1.00 9.70  ? 525 HOH C O   1 
HETATM 9676  O  O   . HOH AA 5 .   ? 45.403  16.936  -38.612 1.00 28.04 ? 526 HOH C O   1 
HETATM 9677  O  O   . HOH AA 5 .   ? 51.793  10.214  -33.164 1.00 19.88 ? 527 HOH C O   1 
HETATM 9678  O  O   . HOH AA 5 .   ? 47.094  -12.952 -52.833 1.00 16.75 ? 528 HOH C O   1 
HETATM 9679  O  O   . HOH AA 5 .   ? 22.177  6.885   -32.084 1.00 10.38 ? 529 HOH C O   1 
HETATM 9680  O  O   . HOH AA 5 .   ? 25.755  -3.019  -48.150 1.00 23.15 ? 530 HOH C O   1 
HETATM 9681  O  O   . HOH AA 5 .   ? 48.033  -8.877  -51.121 1.00 30.23 ? 531 HOH C O   1 
HETATM 9682  O  O   . HOH AA 5 .   ? 28.383  -10.345 -51.282 1.00 35.15 ? 532 HOH C O   1 
HETATM 9683  O  O   . HOH AA 5 .   ? 33.863  13.611  -44.042 1.00 16.79 ? 533 HOH C O   1 
HETATM 9684  O  O   . HOH AA 5 .   ? 38.493  -13.908 -13.268 1.00 33.08 ? 534 HOH C O   1 
HETATM 9685  O  O   . HOH AA 5 .   ? 26.761  9.399   -34.657 1.00 10.20 ? 535 HOH C O   1 
HETATM 9686  O  O   . HOH AA 5 .   ? 48.020  19.045  -40.667 1.00 32.16 ? 536 HOH C O   1 
HETATM 9687  O  O   . HOH AA 5 .   ? 23.507  4.772   -35.912 1.00 8.51  ? 537 HOH C O   1 
HETATM 9688  O  O   . HOH AA 5 .   ? 40.588  -15.649 -25.131 1.00 22.48 ? 538 HOH C O   1 
HETATM 9689  O  O   . HOH AA 5 .   ? 24.891  -1.876  -23.584 1.00 21.93 ? 539 HOH C O   1 
HETATM 9690  O  O   . HOH AA 5 .   ? 23.145  -11.473 -44.510 1.00 24.52 ? 540 HOH C O   1 
HETATM 9691  O  O   . HOH AA 5 .   ? 58.224  -7.246  -30.778 1.00 22.69 ? 541 HOH C O   1 
HETATM 9692  O  O   . HOH AA 5 .   ? 52.817  8.569   -23.871 1.00 22.33 ? 542 HOH C O   1 
HETATM 9693  O  O   . HOH AA 5 .   ? 38.993  12.314  -30.738 1.00 32.90 ? 543 HOH C O   1 
HETATM 9694  O  O   . HOH AA 5 .   ? 25.905  13.017  -35.367 1.00 10.18 ? 544 HOH C O   1 
HETATM 9695  O  O   . HOH AA 5 .   ? 43.198  -1.321  -10.779 1.00 30.33 ? 545 HOH C O   1 
HETATM 9696  O  O   . HOH AA 5 .   ? 43.772  -12.802 -25.759 1.00 22.49 ? 546 HOH C O   1 
HETATM 9697  O  O   . HOH AA 5 .   ? 41.322  7.366   -46.681 1.00 23.63 ? 547 HOH C O   1 
HETATM 9698  O  O   . HOH AA 5 .   ? 41.979  9.860   -27.282 1.00 27.92 ? 548 HOH C O   1 
HETATM 9699  O  O   . HOH AA 5 .   ? 26.715  -13.478 -34.440 1.00 19.86 ? 549 HOH C O   1 
HETATM 9700  O  O   . HOH AA 5 .   ? 33.267  16.308  -14.882 1.00 39.12 ? 550 HOH C O   1 
HETATM 9701  O  O   . HOH AA 5 .   ? 51.850  12.981  -47.314 1.00 28.82 ? 551 HOH C O   1 
HETATM 9702  O  O   . HOH AA 5 .   ? 37.740  14.464  -28.563 1.00 37.46 ? 552 HOH C O   1 
HETATM 9703  O  O   . HOH AA 5 .   ? 49.868  12.405  -32.620 1.00 22.41 ? 553 HOH C O   1 
HETATM 9704  O  O   . HOH AA 5 .   ? 35.939  -0.980  -48.271 1.00 18.28 ? 554 HOH C O   1 
HETATM 9705  O  O   . HOH AA 5 .   ? 32.586  11.378  -43.133 1.00 10.30 ? 555 HOH C O   1 
HETATM 9706  O  O   . HOH AA 5 .   ? 38.387  5.084   -45.088 1.00 17.74 ? 556 HOH C O   1 
HETATM 9707  O  O   . HOH AA 5 .   ? 29.102  9.140   -22.207 1.00 22.80 ? 557 HOH C O   1 
HETATM 9708  O  O   . HOH AA 5 .   ? 23.820  5.693   -40.622 1.00 12.10 ? 558 HOH C O   1 
HETATM 9709  O  O   . HOH AA 5 .   ? 58.886  -7.675  -34.235 1.00 28.54 ? 559 HOH C O   1 
HETATM 9710  O  O   . HOH AA 5 .   ? 30.232  6.662   -21.487 1.00 24.40 ? 560 HOH C O   1 
HETATM 9711  O  O   . HOH AA 5 .   ? 31.713  -20.662 -47.641 1.00 34.86 ? 561 HOH C O   1 
HETATM 9712  O  O   . HOH AA 5 .   ? 26.275  11.421  -45.391 1.00 24.08 ? 562 HOH C O   1 
HETATM 9713  O  O   . HOH AA 5 .   ? 40.555  -13.989 -36.185 1.00 15.43 ? 563 HOH C O   1 
HETATM 9714  O  O   . HOH AA 5 .   ? 19.674  0.253   -53.730 1.00 40.10 ? 564 HOH C O   1 
HETATM 9715  O  O   . HOH AA 5 .   ? 22.403  -5.218  -40.939 1.00 26.01 ? 565 HOH C O   1 
HETATM 9716  O  O   . HOH AA 5 .   ? 22.754  -8.481  -17.034 1.00 41.19 ? 566 HOH C O   1 
HETATM 9717  O  O   . HOH AA 5 .   ? 59.291  3.305   -20.541 1.00 30.95 ? 567 HOH C O   1 
HETATM 9718  O  O   . HOH AA 5 .   ? 28.821  3.636   -46.112 1.00 18.06 ? 568 HOH C O   1 
HETATM 9719  O  O   . HOH AA 5 .   ? 22.508  10.977  -29.290 1.00 16.45 ? 569 HOH C O   1 
HETATM 9720  O  O   . HOH AA 5 .   ? 29.735  -12.280 -23.758 1.00 23.29 ? 570 HOH C O   1 
HETATM 9721  O  O   . HOH AA 5 .   ? 35.426  -21.290 -50.852 1.00 23.50 ? 571 HOH C O   1 
HETATM 9722  O  O   . HOH AA 5 .   ? 28.167  -10.526 -22.366 1.00 22.76 ? 572 HOH C O   1 
HETATM 9723  O  O   . HOH AA 5 .   ? 40.960  3.921   -6.686  1.00 21.04 ? 573 HOH C O   1 
HETATM 9724  O  O   . HOH AA 5 .   ? 29.332  6.066   -47.321 1.00 16.13 ? 574 HOH C O   1 
HETATM 9725  O  O   . HOH AA 5 .   ? 31.494  2.508   -14.627 1.00 20.91 ? 575 HOH C O   1 
HETATM 9726  O  O   . HOH AA 5 .   ? 25.428  14.640  -23.140 1.00 24.99 ? 576 HOH C O   1 
HETATM 9727  O  O   . HOH AA 5 .   ? 34.923  -20.232 -21.703 1.00 42.96 ? 577 HOH C O   1 
HETATM 9728  O  O   . HOH AA 5 .   ? 46.850  11.006  -12.857 1.00 35.04 ? 578 HOH C O   1 
HETATM 9729  O  O   . HOH AA 5 .   ? 32.595  0.306   -50.711 1.00 37.31 ? 579 HOH C O   1 
HETATM 9730  O  O   . HOH AA 5 .   ? 42.616  16.945  -44.420 1.00 33.67 ? 580 HOH C O   1 
HETATM 9731  O  O   . HOH AA 5 .   ? 32.648  7.623   -22.561 1.00 22.27 ? 581 HOH C O   1 
HETATM 9732  O  O   . HOH AA 5 .   ? 27.738  2.572   -52.111 1.00 35.28 ? 582 HOH C O   1 
HETATM 9733  O  O   . HOH AA 5 .   ? 32.732  -14.573 -51.353 1.00 20.66 ? 583 HOH C O   1 
HETATM 9734  O  O   . HOH AA 5 .   ? 51.898  5.295   -12.753 1.00 26.84 ? 584 HOH C O   1 
HETATM 9735  O  O   . HOH AA 5 .   ? 42.222  -3.863  -48.271 1.00 21.13 ? 585 HOH C O   1 
HETATM 9736  O  O   . HOH AA 5 .   ? 39.239  -26.571 -44.223 1.00 22.03 ? 586 HOH C O   1 
HETATM 9737  O  O   . HOH AA 5 .   ? 26.516  9.725   -41.726 1.00 12.82 ? 587 HOH C O   1 
HETATM 9738  O  O   . HOH AA 5 .   ? 35.546  19.682  -35.752 1.00 33.58 ? 588 HOH C O   1 
HETATM 9739  O  O   . HOH AA 5 .   ? 27.056  6.655   -21.034 1.00 24.73 ? 589 HOH C O   1 
HETATM 9740  O  O   . HOH AA 5 .   ? 24.434  -3.732  -44.637 1.00 24.26 ? 590 HOH C O   1 
HETATM 9741  O  O   . HOH AA 5 .   ? 24.067  -9.009  -28.842 1.00 30.19 ? 591 HOH C O   1 
HETATM 9742  O  O   . HOH AA 5 .   ? 56.177  0.478   -45.928 1.00 37.41 ? 592 HOH C O   1 
HETATM 9743  O  O   . HOH AA 5 .   ? 52.181  18.070  -39.129 1.00 33.59 ? 593 HOH C O   1 
HETATM 9744  O  O   . HOH AA 5 .   ? 44.095  14.111  -47.460 1.00 29.69 ? 594 HOH C O   1 
HETATM 9745  O  O   . HOH AA 5 .   ? 29.652  -13.795 -28.073 1.00 24.57 ? 595 HOH C O   1 
HETATM 9746  O  O   . HOH AA 5 .   ? 39.938  -11.822 -54.981 1.00 18.67 ? 596 HOH C O   1 
HETATM 9747  O  O   . HOH AA 5 .   ? 41.635  -18.871 -17.865 1.00 38.31 ? 597 HOH C O   1 
HETATM 9748  O  O   . HOH AA 5 .   ? 42.574  -13.760 -48.610 1.00 27.61 ? 598 HOH C O   1 
HETATM 9749  O  O   . HOH AA 5 .   ? 26.378  3.328   -47.354 1.00 27.11 ? 599 HOH C O   1 
HETATM 9750  O  O   . HOH AA 5 .   ? 24.371  -0.704  -32.741 1.00 19.93 ? 600 HOH C O   1 
HETATM 9751  O  O   . HOH AA 5 .   ? 38.782  -19.689 -46.246 1.00 36.75 ? 601 HOH C O   1 
HETATM 9752  O  O   . HOH AA 5 .   ? 31.351  -16.469 -30.746 1.00 32.87 ? 602 HOH C O   1 
HETATM 9753  O  O   . HOH AA 5 .   ? 39.534  17.958  -40.741 1.00 23.04 ? 603 HOH C O   1 
HETATM 9754  O  O   . HOH AA 5 .   ? 58.484  4.002   -39.899 1.00 35.18 ? 604 HOH C O   1 
HETATM 9755  O  O   . HOH AA 5 .   ? 55.874  -2.110  -42.230 1.00 31.40 ? 605 HOH C O   1 
HETATM 9756  O  O   . HOH AA 5 .   ? 31.649  12.775  -46.389 1.00 19.90 ? 606 HOH C O   1 
HETATM 9757  O  O   . HOH AA 5 .   ? 38.601  16.727  -38.573 1.00 19.58 ? 607 HOH C O   1 
HETATM 9758  O  O   . HOH AA 5 .   ? 44.578  7.350   -8.946  1.00 28.02 ? 608 HOH C O   1 
HETATM 9759  O  O   . HOH AA 5 .   ? 50.966  14.849  -31.866 1.00 36.71 ? 609 HOH C O   1 
HETATM 9760  O  O   . HOH AA 5 .   ? 22.263  -0.376  -44.078 1.00 18.11 ? 610 HOH C O   1 
HETATM 9761  O  O   . HOH AA 5 .   ? 53.473  5.907   -23.358 1.00 20.81 ? 611 HOH C O   1 
HETATM 9762  O  O   . HOH AA 5 .   ? 22.266  -13.890 -35.652 1.00 34.06 ? 612 HOH C O   1 
HETATM 9763  O  O   . HOH AA 5 .   ? 48.651  11.145  -23.967 1.00 26.49 ? 613 HOH C O   1 
HETATM 9764  O  O   . HOH AA 5 .   ? 46.534  -16.968 -38.316 1.00 23.42 ? 614 HOH C O   1 
HETATM 9765  O  O   . HOH AA 5 .   ? 19.663  -7.777  -17.518 1.00 33.81 ? 615 HOH C O   1 
HETATM 9766  O  O   . HOH AA 5 .   ? 38.562  -18.908 -16.240 1.00 30.25 ? 616 HOH C O   1 
HETATM 9767  O  O   . HOH AA 5 .   ? 32.174  -1.916  -51.679 1.00 31.54 ? 617 HOH C O   1 
HETATM 9768  O  O   . HOH AA 5 .   ? 60.732  -6.818  -25.357 1.00 43.45 ? 618 HOH C O   1 
HETATM 9769  O  O   . HOH AA 5 .   ? 56.307  7.615   -14.106 1.00 28.27 ? 619 HOH C O   1 
HETATM 9770  O  O   . HOH AA 5 .   ? 41.240  4.519   -45.451 1.00 28.49 ? 620 HOH C O   1 
HETATM 9771  O  O   . HOH AA 5 .   ? 26.640  4.065   -49.941 1.00 32.98 ? 621 HOH C O   1 
HETATM 9772  O  O   . HOH AA 5 .   ? 56.477  10.498  -43.107 1.00 37.69 ? 622 HOH C O   1 
HETATM 9773  O  O   . HOH AA 5 .   ? 28.251  6.762   -43.818 1.00 18.06 ? 623 HOH C O   1 
HETATM 9774  O  O   . HOH AA 5 .   ? 55.890  6.743   -29.871 1.00 26.36 ? 624 HOH C O   1 
HETATM 9775  O  O   . HOH AA 5 .   ? 38.849  13.928  -42.787 1.00 21.70 ? 625 HOH C O   1 
HETATM 9776  O  O   . HOH AA 5 .   ? 44.117  -4.406  -9.447  1.00 31.75 ? 626 HOH C O   1 
HETATM 9777  O  O   . HOH AA 5 .   ? 43.442  -19.743 -40.508 1.00 33.36 ? 627 HOH C O   1 
HETATM 9778  O  O   . HOH AA 5 .   ? 40.799  -16.240 -22.151 1.00 24.14 ? 628 HOH C O   1 
HETATM 9779  O  O   . HOH AA 5 .   ? 46.985  -16.557 -35.469 1.00 30.42 ? 629 HOH C O   1 
HETATM 9780  O  O   . HOH AA 5 .   ? 23.530  3.684   -51.276 1.00 34.56 ? 630 HOH C O   1 
HETATM 9781  O  O   . HOH AA 5 .   ? 24.566  5.522   -21.163 1.00 27.88 ? 631 HOH C O   1 
HETATM 9782  O  O   . HOH AA 5 .   ? 37.795  -21.007 -40.391 1.00 47.11 ? 632 HOH C O   1 
HETATM 9783  O  O   . HOH AA 5 .   ? 29.665  -11.602 -26.445 1.00 17.75 ? 633 HOH C O   1 
HETATM 9784  O  O   . HOH AA 5 .   ? 32.314  12.288  -21.657 1.00 35.05 ? 634 HOH C O   1 
HETATM 9785  O  O   . HOH AA 5 .   ? 44.546  9.185   -29.731 1.00 23.17 ? 635 HOH C O   1 
HETATM 9786  O  O   . HOH AA 5 .   ? 53.360  -13.260 -30.092 1.00 31.23 ? 636 HOH C O   1 
HETATM 9787  O  O   . HOH AA 5 .   ? 26.527  -5.118  -51.427 1.00 30.93 ? 637 HOH C O   1 
HETATM 9788  O  O   . HOH AA 5 .   ? 36.960  -17.053 -27.909 1.00 33.68 ? 638 HOH C O   1 
HETATM 9789  O  O   . HOH AA 5 .   ? 22.773  2.119   -18.800 1.00 27.04 ? 639 HOH C O   1 
HETATM 9790  O  O   . HOH AA 5 .   ? 22.627  -4.700  -26.427 1.00 26.83 ? 640 HOH C O   1 
HETATM 9791  O  O   . HOH AA 5 .   ? 21.052  -1.110  -29.795 1.00 22.93 ? 641 HOH C O   1 
HETATM 9792  O  O   . HOH AA 5 .   ? 31.947  10.103  -23.165 1.00 30.75 ? 642 HOH C O   1 
HETATM 9793  O  O   . HOH AA 5 .   ? 32.825  -14.772 -46.906 1.00 36.95 ? 643 HOH C O   1 
HETATM 9794  O  O   . HOH AA 5 .   ? 61.802  -6.181  -19.558 1.00 33.00 ? 644 HOH C O   1 
HETATM 9795  O  O   . HOH AA 5 .   ? 39.590  -5.094  -49.216 1.00 28.47 ? 645 HOH C O   1 
HETATM 9796  O  O   . HOH AA 5 .   ? 54.774  -1.754  -44.894 1.00 35.27 ? 646 HOH C O   1 
HETATM 9797  O  O   . HOH AA 5 .   ? 29.431  -12.402 -40.735 1.00 34.05 ? 647 HOH C O   1 
HETATM 9798  O  O   . HOH AA 5 .   ? 27.847  -12.479 -29.870 1.00 26.70 ? 648 HOH C O   1 
HETATM 9799  O  O   . HOH AA 5 .   ? 63.079  0.634   -19.899 1.00 31.23 ? 649 HOH C O   1 
HETATM 9800  O  O   . HOH AA 5 .   ? 41.359  -17.672 -43.920 1.00 44.82 ? 650 HOH C O   1 
HETATM 9801  O  O   . HOH AA 5 .   ? 21.203  -0.154  -21.345 1.00 27.25 ? 651 HOH C O   1 
HETATM 9802  O  O   . HOH AA 5 .   ? 33.106  4.077   -11.198 1.00 39.62 ? 652 HOH C O   1 
HETATM 9803  O  O   . HOH AA 5 .   ? 49.668  -6.949  -14.295 1.00 43.37 ? 653 HOH C O   1 
HETATM 9804  O  O   . HOH AA 5 .   ? 31.610  -15.248 -18.860 1.00 24.72 ? 654 HOH C O   1 
HETATM 9805  O  O   . HOH AA 5 .   ? 54.105  -9.276  -18.977 1.00 33.85 ? 655 HOH C O   1 
HETATM 9806  O  O   . HOH AA 5 .   ? 20.938  4.645   -51.443 1.00 44.26 ? 656 HOH C O   1 
HETATM 9807  O  O   . HOH AA 5 .   ? 38.499  -22.194 -49.027 1.00 40.99 ? 657 HOH C O   1 
HETATM 9808  O  O   . HOH AA 5 .   ? 42.884  -5.645  -54.148 1.00 21.29 ? 658 HOH C O   1 
HETATM 9809  O  O   . HOH AA 5 .   ? 43.548  -16.367 -22.100 1.00 33.08 ? 659 HOH C O   1 
HETATM 9810  O  O   . HOH AA 5 .   ? 45.070  -4.901  -52.486 1.00 31.67 ? 660 HOH C O   1 
HETATM 9811  O  O   . HOH AA 5 .   ? 54.104  5.008   -25.841 1.00 23.96 ? 661 HOH C O   1 
HETATM 9812  O  O   . HOH AA 5 .   ? 53.568  -2.984  -53.468 1.00 29.76 ? 662 HOH C O   1 
HETATM 9813  O  O   . HOH AA 5 .   ? 56.602  -11.545 -30.136 1.00 37.72 ? 663 HOH C O   1 
HETATM 9814  O  O   . HOH AA 5 .   ? 27.979  15.361  -45.314 1.00 36.30 ? 664 HOH C O   1 
HETATM 9815  O  O   . HOH AA 5 .   ? 25.657  -12.692 -25.969 1.00 30.77 ? 665 HOH C O   1 
HETATM 9816  O  O   . HOH AA 5 .   ? 20.442  1.261   -45.597 1.00 30.58 ? 666 HOH C O   1 
HETATM 9817  O  O   . HOH AA 5 .   ? 55.042  6.488   -48.987 1.00 21.74 ? 667 HOH C O   1 
HETATM 9818  O  O   . HOH AA 5 .   ? 60.196  -9.148  -30.391 1.00 37.42 ? 668 HOH C O   1 
HETATM 9819  O  O   . HOH AA 5 .   ? 48.597  -15.625 -39.735 1.00 32.15 ? 669 HOH C O   1 
HETATM 9820  O  O   . HOH AA 5 .   ? 22.738  -2.782  -33.883 1.00 28.36 ? 670 HOH C O   1 
HETATM 9821  O  O   . HOH AA 5 .   ? 35.769  1.272   -50.195 1.00 35.91 ? 671 HOH C O   1 
HETATM 9822  O  O   . HOH AA 5 .   ? 61.672  -6.835  -16.694 1.00 30.11 ? 672 HOH C O   1 
HETATM 9823  O  O   . HOH AA 5 .   ? 22.570  8.654   -27.772 1.00 16.42 ? 673 HOH C O   1 
HETATM 9824  O  O   . HOH AA 5 .   ? 21.259  14.257  -20.302 1.00 31.91 ? 674 HOH C O   1 
HETATM 9825  O  O   . HOH AA 5 .   ? 48.214  11.547  -26.658 1.00 29.80 ? 675 HOH C O   1 
HETATM 9826  O  O   . HOH AA 5 .   ? 54.262  9.287   -26.327 1.00 28.12 ? 676 HOH C O   1 
HETATM 9827  O  O   . HOH AA 5 .   ? 21.995  -3.936  -38.000 1.00 23.37 ? 677 HOH C O   1 
HETATM 9828  O  O   . HOH AA 5 .   ? 19.006  -1.679  -18.282 1.00 36.79 ? 678 HOH C O   1 
HETATM 9829  O  O   . HOH AA 5 .   ? 37.896  16.856  -42.756 1.00 39.02 ? 679 HOH C O   1 
HETATM 9830  O  O   . HOH AA 5 .   ? 25.210  6.032   -45.868 1.00 32.57 ? 680 HOH C O   1 
HETATM 9831  O  O   . HOH AA 5 .   ? 46.395  -15.438 -48.002 1.00 31.50 ? 681 HOH C O   1 
HETATM 9832  O  O   . HOH AA 5 .   ? 38.347  -13.448 -55.952 1.00 29.10 ? 682 HOH C O   1 
HETATM 9833  O  O   . HOH AA 5 .   ? 27.541  20.846  -30.485 1.00 33.78 ? 683 HOH C O   1 
HETATM 9834  O  O   . HOH AA 5 .   ? 45.292  -16.108 -45.501 1.00 29.89 ? 684 HOH C O   1 
HETATM 9835  O  O   . HOH AA 5 .   ? 38.515  -2.498  -48.702 1.00 33.68 ? 685 HOH C O   1 
HETATM 9836  O  O   . HOH AA 5 .   ? 41.933  -25.858 -44.610 1.00 29.43 ? 686 HOH C O   1 
HETATM 9837  O  O   . HOH AA 5 .   ? 31.153  -14.631 -35.377 1.00 31.57 ? 687 HOH C O   1 
HETATM 9838  O  O   . HOH AA 5 .   ? 46.894  -12.864 -14.590 1.00 31.23 ? 688 HOH C O   1 
HETATM 9839  O  O   . HOH AA 5 .   ? 48.551  11.618  -30.294 1.00 27.52 ? 689 HOH C O   1 
HETATM 9840  O  O   . HOH AA 5 .   ? 20.821  -15.792 -49.993 1.00 46.23 ? 690 HOH C O   1 
HETATM 9841  O  O   . HOH AA 5 .   ? 28.420  27.056  -30.389 1.00 21.92 ? 691 HOH C O   1 
HETATM 9842  O  O   . HOH AA 5 .   ? 40.345  16.934  -36.658 1.00 32.22 ? 692 HOH C O   1 
HETATM 9843  O  O   . HOH AA 5 .   ? 50.370  -12.779 -16.242 1.00 36.98 ? 693 HOH C O   1 
HETATM 9844  O  O   . HOH AA 5 .   ? 51.398  -6.375  -52.797 1.00 40.19 ? 694 HOH C O   1 
HETATM 9845  O  O   . HOH AA 5 .   ? 42.043  -10.500 -56.314 1.00 16.32 ? 695 HOH C O   1 
HETATM 9846  O  O   . HOH AA 5 .   ? 37.083  4.582   -50.095 1.00 35.33 ? 696 HOH C O   1 
HETATM 9847  O  O   . HOH AA 5 .   ? 52.965  11.400  -27.486 1.00 33.75 ? 697 HOH C O   1 
HETATM 9848  O  O   . HOH AA 5 .   ? 36.190  18.035  -38.177 1.00 22.48 ? 698 HOH C O   1 
HETATM 9849  O  O   . HOH AA 5 .   ? 28.224  -15.244 -35.815 1.00 33.77 ? 699 HOH C O   1 
HETATM 9850  O  O   . HOH AA 5 .   ? 35.997  13.703  -45.849 1.00 27.23 ? 700 HOH C O   1 
HETATM 9851  O  O   . HOH AA 5 .   ? 27.026  7.014   -47.538 1.00 32.43 ? 701 HOH C O   1 
HETATM 9852  O  O   . HOH AA 5 .   ? 19.198  15.918  -20.956 1.00 32.40 ? 702 HOH C O   1 
HETATM 9853  O  O   . HOH AA 5 .   ? 49.064  -11.216 -52.519 1.00 20.60 ? 703 HOH C O   1 
HETATM 9854  O  O   . HOH AA 5 .   ? 50.912  16.052  -43.971 1.00 31.37 ? 704 HOH C O   1 
HETATM 9855  O  O   . HOH AA 5 .   ? 34.680  9.492   -47.873 1.00 33.43 ? 705 HOH C O   1 
HETATM 9856  O  O   . HOH AA 5 .   ? 43.375  16.557  -47.190 1.00 39.29 ? 706 HOH C O   1 
HETATM 9857  O  O   . HOH AA 5 .   ? 35.666  19.342  -40.288 1.00 35.73 ? 707 HOH C O   1 
HETATM 9858  O  O   . HOH AA 5 .   ? 45.856  -19.325 -39.339 1.00 39.58 ? 708 HOH C O   1 
HETATM 9859  O  O   . HOH AA 5 .   ? 40.451  -15.052 -56.151 1.00 27.05 ? 709 HOH C O   1 
HETATM 9860  O  O   . HOH AA 5 .   ? 33.548  18.917  -43.302 1.00 35.23 ? 710 HOH C O   1 
HETATM 9861  O  O   . HOH AA 5 .   ? 30.094  5.936   -49.848 1.00 28.39 ? 711 HOH C O   1 
HETATM 9862  O  O   . HOH AA 5 .   ? 34.140  12.043  -47.540 1.00 24.56 ? 712 HOH C O   1 
HETATM 9863  O  O   . HOH AA 5 .   ? 50.493  12.399  -27.842 1.00 33.30 ? 713 HOH C O   1 
HETATM 9864  O  O   . HOH AA 5 .   ? 30.422  13.887  -48.878 1.00 34.87 ? 714 HOH C O   1 
HETATM 9865  O  O   . HOH AA 5 .   ? 37.584  18.413  -34.652 1.00 38.59 ? 715 HOH C O   1 
HETATM 9866  O  O   . HOH AA 5 .   ? 33.453  8.077   -50.017 1.00 38.18 ? 716 HOH C O   1 
HETATM 9867  O  O   . HOH AA 5 .   ? 46.916  -18.014 -44.208 1.00 35.10 ? 717 HOH C O   1 
HETATM 9868  O  O   . HOH AA 5 .   ? 27.264  6.766   -50.288 1.00 39.44 ? 718 HOH C O   1 
HETATM 9869  O  O   . HOH AA 5 .   ? 29.554  12.311  -52.159 1.00 45.29 ? 719 HOH C O   1 
HETATM 9870  O  O   . HOH BA 5 .   ? 14.099  19.708  -42.810 1.00 27.42 ? 401 HOH D O   1 
HETATM 9871  O  O   . HOH BA 5 .   ? 7.139   8.403   -41.309 1.00 16.66 ? 402 HOH D O   1 
HETATM 9872  O  O   . HOH BA 5 .   ? 4.330   9.768   -17.571 1.00 35.03 ? 403 HOH D O   1 
HETATM 9873  O  O   . HOH BA 5 .   ? 15.298  18.318  -54.175 1.00 38.69 ? 404 HOH D O   1 
HETATM 9874  O  O   . HOH BA 5 .   ? -0.091  -10.395 -17.961 1.00 25.54 ? 405 HOH D O   1 
HETATM 9875  O  O   . HOH BA 5 .   ? -5.820  13.660  -37.291 1.00 23.04 ? 406 HOH D O   1 
HETATM 9876  O  O   . HOH BA 5 .   ? -9.482  5.478   -21.907 1.00 30.28 ? 407 HOH D O   1 
HETATM 9877  O  O   . HOH BA 5 .   ? 1.694   7.851   -18.521 1.00 36.75 ? 408 HOH D O   1 
HETATM 9878  O  O   . HOH BA 5 .   ? -9.999  14.950  -30.697 1.00 26.14 ? 409 HOH D O   1 
HETATM 9879  O  O   . HOH BA 5 .   ? 6.169   16.304  -45.383 1.00 32.53 ? 410 HOH D O   1 
HETATM 9880  O  O   . HOH BA 5 .   ? -0.664  17.867  -51.488 1.00 35.03 ? 411 HOH D O   1 
HETATM 9881  O  O   . HOH BA 5 .   ? -7.818  3.492   -21.190 1.00 26.91 ? 412 HOH D O   1 
HETATM 9882  O  O   . HOH BA 5 .   ? 8.576   -14.612 -37.440 1.00 27.08 ? 413 HOH D O   1 
HETATM 9883  O  O   . HOH BA 5 .   ? 20.474  -6.752  -38.276 1.00 36.76 ? 414 HOH D O   1 
HETATM 9884  O  O   . HOH BA 5 .   ? -6.124  4.265   -24.333 1.00 20.82 ? 415 HOH D O   1 
HETATM 9885  O  O   . HOH BA 5 .   ? 12.225  7.075   -39.285 1.00 8.30  ? 416 HOH D O   1 
HETATM 9886  O  O   . HOH BA 5 .   ? 14.587  -11.900 -34.389 1.00 27.04 ? 417 HOH D O   1 
HETATM 9887  O  O   . HOH BA 5 .   ? 1.508   7.724   -22.644 1.00 33.04 ? 418 HOH D O   1 
HETATM 9888  O  O   . HOH BA 5 .   ? -5.660  -9.816  -41.519 1.00 33.70 ? 419 HOH D O   1 
HETATM 9889  O  O   . HOH BA 5 .   ? 17.300  -6.694  -56.042 1.00 29.90 ? 420 HOH D O   1 
HETATM 9890  O  O   . HOH BA 5 .   ? -9.953  15.191  -20.712 1.00 21.69 ? 421 HOH D O   1 
HETATM 9891  O  O   . HOH BA 5 .   ? 12.589  19.944  -29.211 1.00 27.44 ? 422 HOH D O   1 
HETATM 9892  O  O   . HOH BA 5 .   ? -9.263  -7.046  -30.639 1.00 46.03 ? 423 HOH D O   1 
HETATM 9893  O  O   . HOH BA 5 .   ? 11.438  15.701  -50.690 1.00 28.49 ? 424 HOH D O   1 
HETATM 9894  O  O   . HOH BA 5 .   ? -2.037  11.356  -58.087 1.00 33.97 ? 425 HOH D O   1 
HETATM 9895  O  O   . HOH BA 5 .   ? 11.048  13.528  -58.424 1.00 20.72 ? 426 HOH D O   1 
HETATM 9896  O  O   . HOH BA 5 .   ? -3.019  -14.591 -48.966 1.00 26.48 ? 427 HOH D O   1 
HETATM 9897  O  O   . HOH BA 5 .   ? 10.260  16.063  -48.043 1.00 32.72 ? 428 HOH D O   1 
HETATM 9898  O  O   . HOH BA 5 .   ? 21.746  -9.367  -18.954 1.00 33.68 ? 429 HOH D O   1 
HETATM 9899  O  O   . HOH BA 5 .   ? -15.236 -2.225  -43.479 1.00 21.48 ? 430 HOH D O   1 
HETATM 9900  O  O   . HOH BA 5 .   ? -14.455 4.849   -37.028 1.00 20.77 ? 431 HOH D O   1 
HETATM 9901  O  O   . HOH BA 5 .   ? 11.899  -6.953  -51.967 1.00 19.51 ? 432 HOH D O   1 
HETATM 9902  O  O   . HOH BA 5 .   ? -1.763  13.409  -38.787 1.00 23.17 ? 433 HOH D O   1 
HETATM 9903  O  O   . HOH BA 5 .   ? 22.943  13.726  -28.627 1.00 23.73 ? 434 HOH D O   1 
HETATM 9904  O  O   . HOH BA 5 .   ? 20.619  -7.498  -29.619 1.00 16.41 ? 435 HOH D O   1 
HETATM 9905  O  O   . HOH BA 5 .   ? -12.066 -4.896  -44.346 1.00 21.95 ? 436 HOH D O   1 
HETATM 9906  O  O   . HOH BA 5 .   ? -2.909  -10.452 -39.332 1.00 22.47 ? 437 HOH D O   1 
HETATM 9907  O  O   . HOH BA 5 .   ? -5.461  19.672  -21.789 1.00 24.54 ? 438 HOH D O   1 
HETATM 9908  O  O   . HOH BA 5 .   ? 4.427   -0.935  -14.485 1.00 30.70 ? 439 HOH D O   1 
HETATM 9909  O  O   . HOH BA 5 .   ? 1.331   9.303   -59.106 1.00 24.87 ? 440 HOH D O   1 
HETATM 9910  O  O   . HOH BA 5 .   ? -10.512 11.689  -25.964 1.00 19.02 ? 441 HOH D O   1 
HETATM 9911  O  O   . HOH BA 5 .   ? 20.021  8.074   -42.315 1.00 10.60 ? 442 HOH D O   1 
HETATM 9912  O  O   . HOH BA 5 .   ? 20.458  -6.686  -44.349 1.00 32.08 ? 443 HOH D O   1 
HETATM 9913  O  O   . HOH BA 5 .   ? 11.164  -0.480  -13.983 1.00 31.78 ? 444 HOH D O   1 
HETATM 9914  O  O   . HOH BA 5 .   ? 14.330  5.869   -60.205 1.00 23.97 ? 445 HOH D O   1 
HETATM 9915  O  O   . HOH BA 5 .   ? -14.047 -2.204  -22.332 1.00 41.51 ? 446 HOH D O   1 
HETATM 9916  O  O   . HOH BA 5 .   ? -5.532  -10.106 -45.043 1.00 29.26 ? 447 HOH D O   1 
HETATM 9917  O  O   . HOH BA 5 .   ? 8.790   -10.742 -31.092 1.00 16.48 ? 448 HOH D O   1 
HETATM 9918  O  O   . HOH BA 5 .   ? -6.431  -2.671  -21.088 1.00 27.65 ? 449 HOH D O   1 
HETATM 9919  O  O   . HOH BA 5 .   ? -12.484 -7.783  -41.018 1.00 23.32 ? 450 HOH D O   1 
HETATM 9920  O  O   . HOH BA 5 .   ? -5.534  -9.618  -34.545 1.00 26.50 ? 451 HOH D O   1 
HETATM 9921  O  O   . HOH BA 5 .   ? 13.416  22.543  -34.888 1.00 29.70 ? 452 HOH D O   1 
HETATM 9922  O  O   . HOH BA 5 .   ? -3.903  23.883  -30.844 1.00 33.81 ? 453 HOH D O   1 
HETATM 9923  O  O   . HOH BA 5 .   ? 16.680  8.120   -51.452 1.00 18.49 ? 454 HOH D O   1 
HETATM 9924  O  O   . HOH BA 5 .   ? 2.248   -15.363 -29.622 1.00 22.89 ? 455 HOH D O   1 
HETATM 9925  O  O   . HOH BA 5 .   ? -1.815  -9.035  -16.667 1.00 19.09 ? 456 HOH D O   1 
HETATM 9926  O  O   . HOH BA 5 .   ? 9.187   3.294   -52.960 1.00 12.62 ? 457 HOH D O   1 
HETATM 9927  O  O   . HOH BA 5 .   ? 11.599  -10.979 -27.580 1.00 28.48 ? 458 HOH D O   1 
HETATM 9928  O  O   . HOH BA 5 .   ? 4.699   16.094  -56.906 1.00 20.09 ? 459 HOH D O   1 
HETATM 9929  O  O   . HOH BA 5 .   ? 21.138  18.481  -42.509 1.00 28.50 ? 460 HOH D O   1 
HETATM 9930  O  O   . HOH BA 5 .   ? 10.963  6.836   -62.766 1.00 32.75 ? 461 HOH D O   1 
HETATM 9931  O  O   . HOH BA 5 .   ? 6.187   17.759  -33.311 1.00 28.76 ? 462 HOH D O   1 
HETATM 9932  O  O   . HOH BA 5 .   ? -6.768  10.929  -19.577 1.00 12.21 ? 463 HOH D O   1 
HETATM 9933  O  O   . HOH BA 5 .   ? -6.461  -8.953  -37.166 1.00 29.93 ? 464 HOH D O   1 
HETATM 9934  O  O   . HOH BA 5 .   ? -5.939  5.324   -56.272 1.00 23.12 ? 465 HOH D O   1 
HETATM 9935  O  O   . HOH BA 5 .   ? 17.998  7.366   -27.051 1.00 14.54 ? 466 HOH D O   1 
HETATM 9936  O  O   . HOH BA 5 .   ? -9.188  5.507   -55.403 1.00 33.39 ? 467 HOH D O   1 
HETATM 9937  O  O   . HOH BA 5 .   ? 16.449  19.650  -56.737 1.00 28.37 ? 468 HOH D O   1 
HETATM 9938  O  O   . HOH BA 5 .   ? -12.009 -9.179  -44.404 1.00 32.96 ? 469 HOH D O   1 
HETATM 9939  O  O   . HOH BA 5 .   ? -1.653  2.280   -57.946 1.00 33.49 ? 470 HOH D O   1 
HETATM 9940  O  O   . HOH BA 5 .   ? 14.347  2.460   -16.456 1.00 27.32 ? 471 HOH D O   1 
HETATM 9941  O  O   . HOH BA 5 .   ? 19.307  8.465   -29.181 1.00 12.89 ? 472 HOH D O   1 
HETATM 9942  O  O   . HOH BA 5 .   ? 20.689  14.027  -47.709 1.00 15.57 ? 473 HOH D O   1 
HETATM 9943  O  O   . HOH BA 5 .   ? 2.197   -11.733 -54.127 1.00 16.03 ? 474 HOH D O   1 
HETATM 9944  O  O   . HOH BA 5 .   ? -12.770 -1.736  -34.069 1.00 16.75 ? 475 HOH D O   1 
HETATM 9945  O  O   . HOH BA 5 .   ? 14.223  -8.324  -52.443 1.00 26.13 ? 476 HOH D O   1 
HETATM 9946  O  O   . HOH BA 5 .   ? 8.453   -16.287 -44.925 1.00 25.87 ? 477 HOH D O   1 
HETATM 9947  O  O   . HOH BA 5 .   ? 19.832  11.171  -29.082 1.00 14.54 ? 478 HOH D O   1 
HETATM 9948  O  O   . HOH BA 5 .   ? 20.239  7.419   -35.668 1.00 11.20 ? 479 HOH D O   1 
HETATM 9949  O  O   . HOH BA 5 .   ? -8.277  -0.035  -51.569 1.00 14.92 ? 480 HOH D O   1 
HETATM 9950  O  O   . HOH BA 5 .   ? 5.920   -14.770 -33.744 1.00 36.23 ? 481 HOH D O   1 
HETATM 9951  O  O   . HOH BA 5 .   ? -11.496 11.375  -45.936 1.00 27.80 ? 482 HOH D O   1 
HETATM 9952  O  O   . HOH BA 5 .   ? 18.618  5.160   -45.664 1.00 16.96 ? 483 HOH D O   1 
HETATM 9953  O  O   . HOH BA 5 .   ? -2.289  -14.303 -26.018 1.00 33.65 ? 484 HOH D O   1 
HETATM 9954  O  O   . HOH BA 5 .   ? 1.055   2.552   -27.998 1.00 10.09 ? 485 HOH D O   1 
HETATM 9955  O  O   . HOH BA 5 .   ? 4.393   -6.896  -34.711 1.00 9.30  ? 486 HOH D O   1 
HETATM 9956  O  O   . HOH BA 5 .   ? 11.138  17.807  -54.486 1.00 20.68 ? 487 HOH D O   1 
HETATM 9957  O  O   . HOH BA 5 .   ? -8.549  15.727  -34.532 1.00 34.31 ? 488 HOH D O   1 
HETATM 9958  O  O   . HOH BA 5 .   ? 11.972  -3.607  -47.156 1.00 11.18 ? 489 HOH D O   1 
HETATM 9959  O  O   . HOH BA 5 .   ? 19.112  11.641  -50.061 1.00 18.57 ? 490 HOH D O   1 
HETATM 9960  O  O   . HOH BA 5 .   ? 18.630  -0.136  -20.337 1.00 21.94 ? 491 HOH D O   1 
HETATM 9961  O  O   . HOH BA 5 .   ? 19.456  -3.879  -34.169 1.00 23.30 ? 492 HOH D O   1 
HETATM 9962  O  O   . HOH BA 5 .   ? -4.671  10.065  -57.219 1.00 28.78 ? 493 HOH D O   1 
HETATM 9963  O  O   . HOH BA 5 .   ? -8.486  -6.463  -28.298 1.00 32.10 ? 494 HOH D O   1 
HETATM 9964  O  O   . HOH BA 5 .   ? -2.183  11.466  -20.182 1.00 19.33 ? 495 HOH D O   1 
HETATM 9965  O  O   . HOH BA 5 .   ? -9.892  -0.337  -49.277 1.00 15.22 ? 496 HOH D O   1 
HETATM 9966  O  O   . HOH BA 5 .   ? 7.625   15.583  -39.173 1.00 27.40 ? 497 HOH D O   1 
HETATM 9967  O  O   . HOH BA 5 .   ? 22.967  6.572   -23.698 1.00 21.63 ? 498 HOH D O   1 
HETATM 9968  O  O   . HOH BA 5 .   ? -12.237 10.142  -23.273 1.00 24.22 ? 499 HOH D O   1 
HETATM 9969  O  O   . HOH BA 5 .   ? 9.378   8.340   -42.818 1.00 13.02 ? 500 HOH D O   1 
HETATM 9970  O  O   . HOH BA 5 .   ? -2.068  13.214  -41.489 1.00 23.68 ? 501 HOH D O   1 
HETATM 9971  O  O   . HOH BA 5 .   ? -3.468  -5.654  -26.694 1.00 15.71 ? 502 HOH D O   1 
HETATM 9972  O  O   . HOH BA 5 .   ? 21.450  5.201   -34.153 1.00 9.06  ? 503 HOH D O   1 
HETATM 9973  O  O   . HOH BA 5 .   ? 16.538  0.257   -37.327 1.00 9.72  ? 504 HOH D O   1 
HETATM 9974  O  O   . HOH BA 5 .   ? 20.140  15.995  -49.229 1.00 32.31 ? 505 HOH D O   1 
HETATM 9975  O  O   . HOH BA 5 .   ? -5.682  -5.493  -53.678 1.00 25.28 ? 506 HOH D O   1 
HETATM 9976  O  O   . HOH BA 5 .   ? 11.145  13.901  -61.100 1.00 27.07 ? 507 HOH D O   1 
HETATM 9977  O  O   . HOH BA 5 .   ? 12.715  -9.686  -45.927 1.00 16.11 ? 508 HOH D O   1 
HETATM 9978  O  O   . HOH BA 5 .   ? 22.792  23.152  -35.519 1.00 10.84 ? 509 HOH D O   1 
HETATM 9979  O  O   . HOH BA 5 .   ? 19.254  4.798   -49.178 1.00 18.46 ? 510 HOH D O   1 
HETATM 9980  O  O   . HOH BA 5 .   ? -2.776  11.168  -45.865 1.00 19.11 ? 511 HOH D O   1 
HETATM 9981  O  O   . HOH BA 5 .   ? -6.973  -3.052  -53.220 1.00 23.07 ? 512 HOH D O   1 
HETATM 9982  O  O   . HOH BA 5 .   ? 15.331  6.076   -18.739 1.00 36.71 ? 513 HOH D O   1 
HETATM 9983  O  O   . HOH BA 5 .   ? -7.891  11.945  -36.831 1.00 16.22 ? 514 HOH D O   1 
HETATM 9984  O  O   . HOH BA 5 .   ? 0.507   -12.653 -36.889 1.00 13.74 ? 515 HOH D O   1 
HETATM 9985  O  O   . HOH BA 5 .   ? -2.378  -8.689  -41.605 1.00 14.67 ? 516 HOH D O   1 
HETATM 9986  O  O   . HOH BA 5 .   ? 5.922   -6.361  -57.389 1.00 15.50 ? 517 HOH D O   1 
HETATM 9987  O  O   . HOH BA 5 .   ? 8.369   -9.258  -13.878 1.00 26.65 ? 518 HOH D O   1 
HETATM 9988  O  O   . HOH BA 5 .   ? 13.833  7.484   -48.248 1.00 12.56 ? 519 HOH D O   1 
HETATM 9989  O  O   . HOH BA 5 .   ? -8.636  18.446  -22.916 1.00 42.45 ? 520 HOH D O   1 
HETATM 9990  O  O   . HOH BA 5 .   ? 19.437  18.932  -39.876 1.00 24.53 ? 521 HOH D O   1 
HETATM 9991  O  O   . HOH BA 5 .   ? 21.775  -9.670  -25.943 1.00 24.19 ? 522 HOH D O   1 
HETATM 9992  O  O   . HOH BA 5 .   ? 0.791   -12.071 -13.802 1.00 30.29 ? 523 HOH D O   1 
HETATM 9993  O  O   . HOH BA 5 .   ? -12.166 -3.746  -35.965 1.00 20.54 ? 524 HOH D O   1 
HETATM 9994  O  O   . HOH BA 5 .   ? 20.159  -1.110  -39.754 1.00 29.29 ? 525 HOH D O   1 
HETATM 9995  O  O   . HOH BA 5 .   ? 17.444  -11.383 -27.224 1.00 20.64 ? 526 HOH D O   1 
HETATM 9996  O  O   . HOH BA 5 .   ? 0.141   0.109   -56.720 1.00 26.55 ? 527 HOH D O   1 
HETATM 9997  O  O   . HOH BA 5 .   ? 18.870  -13.116 -32.942 1.00 30.92 ? 528 HOH D O   1 
HETATM 9998  O  O   . HOH BA 5 .   ? 20.172  21.748  -32.719 1.00 24.74 ? 529 HOH D O   1 
HETATM 9999  O  O   . HOH BA 5 .   ? 16.556  16.000  -54.461 1.00 23.00 ? 530 HOH D O   1 
HETATM 10000 O  O   . HOH BA 5 .   ? -2.179  -7.842  -22.462 1.00 14.91 ? 531 HOH D O   1 
HETATM 10001 O  O   . HOH BA 5 .   ? -7.039  -6.739  -51.496 1.00 18.14 ? 532 HOH D O   1 
HETATM 10002 O  O   . HOH BA 5 .   ? -13.744 -1.308  -49.036 1.00 22.46 ? 533 HOH D O   1 
HETATM 10003 O  O   . HOH BA 5 .   ? 9.056   16.741  -41.050 1.00 40.29 ? 534 HOH D O   1 
HETATM 10004 O  O   . HOH BA 5 .   ? 18.494  -0.213  -29.386 1.00 13.35 ? 535 HOH D O   1 
HETATM 10005 O  O   . HOH BA 5 .   ? -6.535  -7.631  -32.828 1.00 30.78 ? 536 HOH D O   1 
HETATM 10006 O  O   . HOH BA 5 .   ? 7.623   -4.909  -14.484 1.00 23.98 ? 537 HOH D O   1 
HETATM 10007 O  O   . HOH BA 5 .   ? -9.719  8.256   -20.628 1.00 21.20 ? 538 HOH D O   1 
HETATM 10008 O  O   . HOH BA 5 .   ? -2.698  15.376  -47.609 1.00 34.93 ? 539 HOH D O   1 
HETATM 10009 O  O   . HOH BA 5 .   ? 22.979  6.383   -38.115 1.00 9.49  ? 540 HOH D O   1 
HETATM 10010 O  O   . HOH BA 5 .   ? 1.991   -7.458  -55.484 1.00 24.89 ? 541 HOH D O   1 
HETATM 10011 O  O   . HOH BA 5 .   ? 5.920   -0.187  -57.683 1.00 27.05 ? 542 HOH D O   1 
HETATM 10012 O  O   . HOH BA 5 .   ? 13.485  15.746  -47.863 1.00 23.01 ? 543 HOH D O   1 
HETATM 10013 O  O   . HOH BA 5 .   ? 3.254   13.212  -41.950 1.00 24.85 ? 544 HOH D O   1 
HETATM 10014 O  O   . HOH BA 5 .   ? 0.745   -8.214  -18.809 1.00 15.79 ? 545 HOH D O   1 
HETATM 10015 O  O   . HOH BA 5 .   ? 3.229   -13.682 -39.440 1.00 29.24 ? 546 HOH D O   1 
HETATM 10016 O  O   . HOH BA 5 .   ? 18.901  -11.669 -20.932 1.00 34.86 ? 547 HOH D O   1 
HETATM 10017 O  O   . HOH BA 5 .   ? 13.438  18.559  -32.385 1.00 11.21 ? 548 HOH D O   1 
HETATM 10018 O  O   . HOH BA 5 .   ? -6.729  0.412   -55.933 1.00 20.76 ? 549 HOH D O   1 
HETATM 10019 O  O   . HOH BA 5 .   ? -12.835 8.642   -55.088 1.00 21.00 ? 550 HOH D O   1 
HETATM 10020 O  O   . HOH BA 5 .   ? 1.326   -17.354 -26.573 1.00 39.52 ? 551 HOH D O   1 
HETATM 10021 O  O   . HOH BA 5 .   ? 21.253  2.461   -21.045 1.00 26.15 ? 552 HOH D O   1 
HETATM 10022 O  O   . HOH BA 5 .   ? 10.350  2.354   -21.349 1.00 15.48 ? 553 HOH D O   1 
HETATM 10023 O  O   . HOH BA 5 .   ? 18.803  -0.664  -46.221 1.00 24.12 ? 554 HOH D O   1 
HETATM 10024 O  O   . HOH BA 5 .   ? -9.605  15.936  -28.412 1.00 24.01 ? 555 HOH D O   1 
HETATM 10025 O  O   . HOH BA 5 .   ? -5.579  -7.021  -27.666 1.00 16.79 ? 556 HOH D O   1 
HETATM 10026 O  O   . HOH BA 5 .   ? -14.399 11.996  -49.479 1.00 37.12 ? 557 HOH D O   1 
HETATM 10027 O  O   . HOH BA 5 .   ? 23.883  18.459  -42.685 1.00 16.85 ? 558 HOH D O   1 
HETATM 10028 O  O   . HOH BA 5 .   ? -8.114  13.595  -44.341 1.00 26.83 ? 559 HOH D O   1 
HETATM 10029 O  O   . HOH BA 5 .   ? 5.917   21.376  -25.546 1.00 19.20 ? 560 HOH D O   1 
HETATM 10030 O  O   . HOH BA 5 .   ? 11.373  19.503  -44.374 1.00 46.19 ? 561 HOH D O   1 
HETATM 10031 O  O   . HOH BA 5 .   ? 18.800  -3.301  -43.024 1.00 22.01 ? 562 HOH D O   1 
HETATM 10032 O  O   . HOH BA 5 .   ? 12.293  1.894   -17.895 1.00 15.69 ? 563 HOH D O   1 
HETATM 10033 O  O   . HOH BA 5 .   ? 2.611   9.384   -24.768 1.00 15.12 ? 564 HOH D O   1 
HETATM 10034 O  O   . HOH BA 5 .   ? -2.611  -0.617  -16.728 1.00 23.35 ? 565 HOH D O   1 
HETATM 10035 O  O   . HOH BA 5 .   ? 26.352  16.163  -43.473 1.00 21.76 ? 566 HOH D O   1 
HETATM 10036 O  O   . HOH BA 5 .   ? 5.569   12.253  -22.918 1.00 19.78 ? 567 HOH D O   1 
HETATM 10037 O  O   . HOH BA 5 .   ? 16.082  2.148   -59.347 1.00 32.88 ? 568 HOH D O   1 
HETATM 10038 O  O   . HOH BA 5 .   ? -10.390 -4.739  -29.755 1.00 28.60 ? 569 HOH D O   1 
HETATM 10039 O  O   . HOH BA 5 .   ? 9.869   -13.364 -55.299 1.00 32.40 ? 570 HOH D O   1 
HETATM 10040 O  O   . HOH BA 5 .   ? 14.001  -11.104 -20.579 1.00 33.05 ? 571 HOH D O   1 
HETATM 10041 O  O   . HOH BA 5 .   ? -12.168 5.597   -52.952 1.00 28.11 ? 572 HOH D O   1 
HETATM 10042 O  O   . HOH BA 5 .   ? -0.848  19.142  -21.402 1.00 23.47 ? 573 HOH D O   1 
HETATM 10043 O  O   . HOH BA 5 .   ? 21.382  6.763   -29.580 1.00 12.45 ? 574 HOH D O   1 
HETATM 10044 O  O   . HOH BA 5 .   ? 18.630  -7.605  -40.005 1.00 21.08 ? 575 HOH D O   1 
HETATM 10045 O  O   . HOH BA 5 .   ? -3.052  17.245  -36.477 1.00 24.79 ? 576 HOH D O   1 
HETATM 10046 O  O   . HOH BA 5 .   ? 23.681  8.233   -45.424 1.00 24.12 ? 577 HOH D O   1 
HETATM 10047 O  O   . HOH BA 5 .   ? 14.370  -13.375 -30.547 1.00 36.73 ? 578 HOH D O   1 
HETATM 10048 O  O   . HOH BA 5 .   ? 17.190  6.717   -48.961 1.00 17.09 ? 579 HOH D O   1 
HETATM 10049 O  O   . HOH BA 5 .   ? 2.691   21.558  -31.539 1.00 33.48 ? 580 HOH D O   1 
HETATM 10050 O  O   . HOH BA 5 .   ? 9.248   20.054  -31.836 1.00 19.93 ? 581 HOH D O   1 
HETATM 10051 O  O   . HOH BA 5 .   ? 11.845  8.905   -47.098 1.00 13.14 ? 582 HOH D O   1 
HETATM 10052 O  O   . HOH BA 5 .   ? 1.013   13.033  -39.454 1.00 19.75 ? 583 HOH D O   1 
HETATM 10053 O  O   . HOH BA 5 .   ? 13.111  11.257  -46.646 1.00 15.08 ? 584 HOH D O   1 
HETATM 10054 O  O   . HOH BA 5 .   ? 9.879   17.668  -44.779 1.00 31.56 ? 585 HOH D O   1 
HETATM 10055 O  O   . HOH BA 5 .   ? 16.625  10.602  -50.182 1.00 15.89 ? 586 HOH D O   1 
HETATM 10056 O  O   . HOH BA 5 .   ? 11.341  3.786   -55.084 1.00 13.79 ? 587 HOH D O   1 
HETATM 10057 O  O   . HOH BA 5 .   ? 17.196  7.532   -55.734 1.00 21.98 ? 588 HOH D O   1 
HETATM 10058 O  O   . HOH BA 5 .   ? 0.632   15.694  -59.360 1.00 27.93 ? 589 HOH D O   1 
HETATM 10059 O  O   . HOH BA 5 .   ? 10.101  19.784  -50.749 1.00 38.21 ? 590 HOH D O   1 
HETATM 10060 O  O   . HOH BA 5 .   ? -16.228 4.402   -40.944 1.00 21.85 ? 591 HOH D O   1 
HETATM 10061 O  O   . HOH BA 5 .   ? 19.161  10.077  -35.625 1.00 9.40  ? 592 HOH D O   1 
HETATM 10062 O  O   . HOH BA 5 .   ? 19.154  -0.258  -36.698 1.00 14.51 ? 593 HOH D O   1 
HETATM 10063 O  O   . HOH BA 5 .   ? 7.966   9.133   -24.178 1.00 19.70 ? 594 HOH D O   1 
HETATM 10064 O  O   . HOH BA 5 .   ? 14.531  13.896  -27.161 1.00 12.62 ? 595 HOH D O   1 
HETATM 10065 O  O   . HOH BA 5 .   ? 15.560  9.730   -47.824 1.00 13.68 ? 596 HOH D O   1 
HETATM 10066 O  O   . HOH BA 5 .   ? -8.323  8.862   -55.565 1.00 22.21 ? 597 HOH D O   1 
HETATM 10067 O  O   . HOH BA 5 .   ? -5.300  -13.666 -32.491 1.00 25.75 ? 598 HOH D O   1 
HETATM 10068 O  O   . HOH BA 5 .   ? 18.776  -4.469  -18.118 1.00 32.63 ? 599 HOH D O   1 
HETATM 10069 O  O   . HOH BA 5 .   ? 19.975  -7.971  -55.671 1.00 40.21 ? 600 HOH D O   1 
HETATM 10070 O  O   . HOH BA 5 .   ? -14.241 9.518   -44.559 1.00 29.61 ? 601 HOH D O   1 
HETATM 10071 O  O   . HOH BA 5 .   ? -15.747 9.606   -47.055 1.00 23.13 ? 602 HOH D O   1 
HETATM 10072 O  O   . HOH BA 5 .   ? 18.449  23.061  -34.022 1.00 21.25 ? 603 HOH D O   1 
HETATM 10073 O  O   . HOH BA 5 .   ? -12.186 -4.600  -31.902 1.00 33.86 ? 604 HOH D O   1 
HETATM 10074 O  O   . HOH BA 5 .   ? 13.638  1.347   -55.686 1.00 19.58 ? 605 HOH D O   1 
HETATM 10075 O  O   . HOH BA 5 .   ? 16.147  15.114  -23.960 1.00 28.23 ? 606 HOH D O   1 
HETATM 10076 O  O   . HOH BA 5 .   ? 8.544   17.780  -27.360 1.00 21.00 ? 607 HOH D O   1 
HETATM 10077 O  O   . HOH BA 5 .   ? -14.255 11.780  -33.347 1.00 31.34 ? 608 HOH D O   1 
HETATM 10078 O  O   . HOH BA 5 .   ? -9.148  11.103  -44.855 1.00 16.73 ? 609 HOH D O   1 
HETATM 10079 O  O   . HOH BA 5 .   ? 21.576  -11.898 -23.152 1.00 34.90 ? 610 HOH D O   1 
HETATM 10080 O  O   . HOH BA 5 .   ? -11.417 12.819  -37.904 1.00 27.21 ? 611 HOH D O   1 
HETATM 10081 O  O   . HOH BA 5 .   ? 12.337  -13.004 -33.672 1.00 32.54 ? 612 HOH D O   1 
HETATM 10082 O  O   . HOH BA 5 .   ? 20.712  9.566   -25.850 1.00 23.41 ? 613 HOH D O   1 
HETATM 10083 O  O   . HOH BA 5 .   ? -17.834 -1.722  -44.761 1.00 31.99 ? 614 HOH D O   1 
HETATM 10084 O  O   . HOH BA 5 .   ? -3.550  15.388  -44.661 1.00 36.70 ? 615 HOH D O   1 
HETATM 10085 O  O   . HOH BA 5 .   ? 23.591  10.477  -41.448 1.00 16.68 ? 616 HOH D O   1 
HETATM 10086 O  O   . HOH BA 5 .   ? -3.932  9.865   -17.387 1.00 17.51 ? 617 HOH D O   1 
HETATM 10087 O  O   . HOH BA 5 .   ? 12.917  13.348  -48.451 1.00 18.34 ? 618 HOH D O   1 
HETATM 10088 O  O   . HOH BA 5 .   ? -0.035  -12.096 -42.128 1.00 15.25 ? 619 HOH D O   1 
HETATM 10089 O  O   . HOH BA 5 .   ? 16.995  18.876  -43.153 1.00 35.33 ? 620 HOH D O   1 
HETATM 10090 O  O   . HOH BA 5 .   ? 4.030   18.728  -51.104 1.00 26.43 ? 621 HOH D O   1 
HETATM 10091 O  O   . HOH BA 5 .   ? 13.946  16.382  -26.309 1.00 20.79 ? 622 HOH D O   1 
HETATM 10092 O  O   . HOH BA 5 .   ? 1.286   -9.838  -31.155 1.00 11.14 ? 623 HOH D O   1 
HETATM 10093 O  O   . HOH BA 5 .   ? 10.706  -10.536 -16.803 1.00 22.74 ? 624 HOH D O   1 
HETATM 10094 O  O   . HOH BA 5 .   ? -0.208  -12.655 -45.274 1.00 15.37 ? 625 HOH D O   1 
HETATM 10095 O  O   . HOH BA 5 .   ? -15.028 -0.694  -35.444 1.00 23.15 ? 626 HOH D O   1 
HETATM 10096 O  O   . HOH BA 5 .   ? 18.483  16.924  -41.764 1.00 28.62 ? 627 HOH D O   1 
HETATM 10097 O  O   . HOH BA 5 .   ? 22.075  1.327   -25.012 1.00 22.26 ? 628 HOH D O   1 
HETATM 10098 O  O   . HOH BA 5 .   ? 8.745   21.680  -29.645 1.00 16.75 ? 629 HOH D O   1 
HETATM 10099 O  O   . HOH BA 5 .   ? 1.490   -15.096 -35.825 1.00 33.71 ? 630 HOH D O   1 
HETATM 10100 O  O   . HOH BA 5 .   ? 0.210   22.439  -37.595 1.00 39.43 ? 631 HOH D O   1 
HETATM 10101 O  O   . HOH BA 5 .   ? 21.276  -5.203  -57.559 1.00 39.62 ? 632 HOH D O   1 
HETATM 10102 O  O   . HOH BA 5 .   ? -4.958  -11.225 -28.136 1.00 19.99 ? 633 HOH D O   1 
HETATM 10103 O  O   . HOH BA 5 .   ? -2.557  13.885  -56.427 1.00 23.95 ? 634 HOH D O   1 
HETATM 10104 O  O   . HOH BA 5 .   ? 22.226  3.778   -23.369 1.00 20.19 ? 635 HOH D O   1 
HETATM 10105 O  O   . HOH BA 5 .   ? 8.948   -10.086 -57.957 1.00 21.59 ? 636 HOH D O   1 
HETATM 10106 O  O   . HOH BA 5 .   ? -9.347  0.633   -54.482 1.00 25.55 ? 637 HOH D O   1 
HETATM 10107 O  O   . HOH BA 5 .   ? 4.222   24.064  -28.465 1.00 27.28 ? 638 HOH D O   1 
HETATM 10108 O  O   . HOH BA 5 .   ? -20.460 5.843   -50.913 1.00 17.21 ? 639 HOH D O   1 
HETATM 10109 O  O   . HOH BA 5 .   ? 0.684   24.266  -29.864 1.00 34.73 ? 640 HOH D O   1 
HETATM 10110 O  O   . HOH BA 5 .   ? -17.239 8.234   -50.137 1.00 29.26 ? 641 HOH D O   1 
HETATM 10111 O  O   . HOH BA 5 .   ? -11.536 12.062  -30.375 1.00 27.92 ? 642 HOH D O   1 
HETATM 10112 O  O   . HOH BA 5 .   ? 16.184  24.149  -34.148 1.00 25.06 ? 643 HOH D O   1 
HETATM 10113 O  O   . HOH BA 5 .   ? 11.537  22.192  -61.479 1.00 31.76 ? 644 HOH D O   1 
HETATM 10114 O  O   . HOH BA 5 .   ? -17.130 -4.092  -36.410 1.00 30.01 ? 645 HOH D O   1 
HETATM 10115 O  O   . HOH BA 5 .   ? 17.013  8.601   -58.165 1.00 49.83 ? 646 HOH D O   1 
HETATM 10116 O  O   . HOH BA 5 .   ? 9.087   -13.141 -16.892 1.00 43.20 ? 647 HOH D O   1 
HETATM 10117 O  O   . HOH BA 5 .   ? -2.636  -14.574 -39.498 1.00 30.69 ? 648 HOH D O   1 
HETATM 10118 O  O   . HOH BA 5 .   ? -5.618  -11.017 -30.941 1.00 25.68 ? 649 HOH D O   1 
HETATM 10119 O  O   . HOH BA 5 .   ? -12.598 -4.334  -47.491 1.00 28.26 ? 650 HOH D O   1 
HETATM 10120 O  O   . HOH BA 5 .   ? 20.794  -4.002  -28.462 1.00 24.54 ? 651 HOH D O   1 
HETATM 10121 O  O   . HOH BA 5 .   ? -10.683 19.369  -30.917 1.00 30.43 ? 652 HOH D O   1 
HETATM 10122 O  O   . HOH BA 5 .   ? 8.784   -13.459 -29.735 1.00 29.44 ? 653 HOH D O   1 
HETATM 10123 O  O   . HOH BA 5 .   ? -11.391 -7.334  -36.460 1.00 27.58 ? 654 HOH D O   1 
HETATM 10124 O  O   . HOH BA 5 .   ? -14.258 10.692  -36.789 1.00 34.82 ? 655 HOH D O   1 
HETATM 10125 O  O   . HOH BA 5 .   ? 22.617  -1.512  -39.798 1.00 25.36 ? 656 HOH D O   1 
HETATM 10126 O  O   . HOH BA 5 .   ? 2.376   11.209  -61.426 1.00 35.07 ? 657 HOH D O   1 
HETATM 10127 O  O   . HOH BA 5 .   ? 6.883   1.368   -59.984 1.00 40.29 ? 658 HOH D O   1 
HETATM 10128 O  O   . HOH BA 5 .   ? 1.347   15.727  -40.757 1.00 38.20 ? 659 HOH D O   1 
HETATM 10129 O  O   . HOH BA 5 .   ? -9.872  -8.918  -47.779 1.00 44.86 ? 660 HOH D O   1 
HETATM 10130 O  O   . HOH BA 5 .   ? 14.056  -10.822 -27.568 1.00 34.45 ? 661 HOH D O   1 
HETATM 10131 O  O   . HOH BA 5 .   ? 7.298   20.074  -47.018 1.00 39.37 ? 662 HOH D O   1 
HETATM 10132 O  O   . HOH BA 5 .   ? -0.874  23.056  -33.694 1.00 39.76 ? 663 HOH D O   1 
HETATM 10133 O  O   . HOH BA 5 .   ? 2.647   -18.483 -42.447 1.00 33.25 ? 664 HOH D O   1 
HETATM 10134 O  O   . HOH BA 5 .   ? 2.697   1.830   -20.124 1.00 30.65 ? 665 HOH D O   1 
HETATM 10135 O  O   . HOH BA 5 .   ? 5.237   9.523   -23.669 1.00 23.77 ? 666 HOH D O   1 
HETATM 10136 O  O   . HOH BA 5 .   ? 10.099  -10.917 -20.545 1.00 33.90 ? 667 HOH D O   1 
HETATM 10137 O  O   . HOH BA 5 .   ? 5.566   2.815   -20.051 1.00 46.51 ? 668 HOH D O   1 
HETATM 10138 O  O   . HOH BA 5 .   ? -0.283  3.718   -20.034 1.00 32.52 ? 669 HOH D O   1 
HETATM 10139 O  O   . HOH BA 5 .   ? 3.123   -17.897 -40.277 1.00 33.42 ? 670 HOH D O   1 
HETATM 10140 O  O   . HOH BA 5 .   ? -8.396  19.291  -26.086 1.00 32.78 ? 671 HOH D O   1 
HETATM 10141 O  O   . HOH BA 5 .   ? 1.437   15.432  -45.671 1.00 42.03 ? 672 HOH D O   1 
HETATM 10142 O  O   . HOH BA 5 .   ? -15.153 7.049   -40.581 1.00 28.61 ? 673 HOH D O   1 
HETATM 10143 O  O   . HOH BA 5 .   ? 14.635  22.760  -43.289 1.00 39.48 ? 674 HOH D O   1 
HETATM 10144 O  O   . HOH BA 5 .   ? 8.287   -12.442 -59.167 1.00 33.29 ? 675 HOH D O   1 
HETATM 10145 O  O   . HOH BA 5 .   ? 7.147   -15.213 -30.823 1.00 45.15 ? 676 HOH D O   1 
HETATM 10146 O  O   . HOH BA 5 .   ? -14.658 -5.139  -36.446 1.00 27.35 ? 677 HOH D O   1 
HETATM 10147 O  O   . HOH BA 5 .   ? -5.609  -10.556 -39.109 1.00 43.53 ? 678 HOH D O   1 
HETATM 10148 O  O   . HOH BA 5 .   ? 7.103   -4.010  -58.221 1.00 25.52 ? 679 HOH D O   1 
HETATM 10149 O  O   . HOH BA 5 .   ? -2.875  -12.212 -45.189 1.00 24.22 ? 680 HOH D O   1 
HETATM 10150 O  O   . HOH BA 5 .   ? 4.584   -16.534 -30.005 1.00 38.63 ? 681 HOH D O   1 
HETATM 10151 O  O   . HOH BA 5 .   ? 18.053  16.238  -50.451 1.00 31.36 ? 682 HOH D O   1 
HETATM 10152 O  O   . HOH BA 5 .   ? 27.431  13.039  -47.035 1.00 27.44 ? 683 HOH D O   1 
HETATM 10153 O  O   . HOH BA 5 .   ? -16.069 10.083  -54.621 1.00 24.00 ? 684 HOH D O   1 
HETATM 10154 O  O   . HOH BA 5 .   ? 20.346  -2.477  -36.240 1.00 37.19 ? 685 HOH D O   1 
HETATM 10155 O  O   . HOH BA 5 .   ? 20.673  3.931   -46.881 1.00 22.64 ? 686 HOH D O   1 
HETATM 10156 O  O   . HOH BA 5 .   ? 12.059  -12.473 -56.549 1.00 25.19 ? 687 HOH D O   1 
HETATM 10157 O  O   . HOH BA 5 .   ? -3.836  -11.498 -42.797 1.00 38.00 ? 688 HOH D O   1 
HETATM 10158 O  O   . HOH BA 5 .   ? 10.068  20.113  -28.008 1.00 28.04 ? 689 HOH D O   1 
HETATM 10159 O  O   . HOH BA 5 .   ? 22.302  -7.415  -27.423 1.00 17.85 ? 690 HOH D O   1 
HETATM 10160 O  O   . HOH BA 5 .   ? -6.459  7.830   -57.356 1.00 21.80 ? 691 HOH D O   1 
HETATM 10161 O  O   . HOH BA 5 .   ? 5.087   22.189  -51.646 1.00 40.41 ? 692 HOH D O   1 
HETATM 10162 O  O   . HOH BA 5 .   ? 16.563  1.024   -55.221 1.00 33.89 ? 693 HOH D O   1 
HETATM 10163 O  O   . HOH BA 5 .   ? 20.898  -1.215  -41.942 1.00 30.21 ? 694 HOH D O   1 
HETATM 10164 O  O   . HOH BA 5 .   ? 3.862   16.877  -48.927 1.00 31.60 ? 695 HOH D O   1 
HETATM 10165 O  O   . HOH BA 5 .   ? 22.619  7.637   -42.474 1.00 20.16 ? 696 HOH D O   1 
HETATM 10166 O  O   . HOH BA 5 .   ? 14.602  -10.647 -51.208 1.00 26.52 ? 697 HOH D O   1 
HETATM 10167 O  O   . HOH BA 5 .   ? -1.906  -11.241 -40.881 1.00 27.17 ? 698 HOH D O   1 
HETATM 10168 O  O   . HOH BA 5 .   ? 21.139  -3.822  -32.065 1.00 26.32 ? 699 HOH D O   1 
HETATM 10169 O  O   . HOH BA 5 .   ? 0.893   -14.670 -41.596 1.00 33.54 ? 700 HOH D O   1 
HETATM 10170 O  O   . HOH BA 5 .   ? 5.080   -2.364  -58.910 1.00 24.66 ? 701 HOH D O   1 
HETATM 10171 O  O   . HOH BA 5 .   ? 23.131  12.047  -50.957 1.00 35.96 ? 702 HOH D O   1 
HETATM 10172 O  O   . HOH BA 5 .   ? 5.600   20.451  -49.568 1.00 44.41 ? 703 HOH D O   1 
HETATM 10173 O  O   . HOH BA 5 .   ? -12.148 14.510  -22.530 1.00 43.82 ? 704 HOH D O   1 
HETATM 10174 O  O   . HOH BA 5 .   ? 3.190   -6.672  -57.908 1.00 23.18 ? 705 HOH D O   1 
HETATM 10175 O  O   . HOH BA 5 .   ? -3.003  -9.901  -21.013 1.00 23.78 ? 706 HOH D O   1 
HETATM 10176 O  O   . HOH BA 5 .   ? -1.162  -12.397 -39.070 1.00 24.19 ? 707 HOH D O   1 
HETATM 10177 O  O   . HOH BA 5 .   ? 11.487  18.012  -51.957 1.00 31.48 ? 708 HOH D O   1 
HETATM 10178 O  O   . HOH BA 5 .   ? -4.400  -14.267 -46.175 1.00 33.92 ? 709 HOH D O   1 
HETATM 10179 O  O   . HOH BA 5 .   ? 4.346   -15.490 -35.977 1.00 36.93 ? 710 HOH D O   1 
HETATM 10180 O  O   . HOH BA 5 .   ? 1.699   -15.464 -39.677 1.00 34.33 ? 711 HOH D O   1 
HETATM 10181 O  O   . HOH BA 5 .   ? -6.835  -9.370  -26.783 1.00 23.32 ? 712 HOH D O   1 
HETATM 10182 O  O   . HOH BA 5 .   ? 10.127  -11.885 -33.136 1.00 27.59 ? 713 HOH D O   1 
HETATM 10183 O  O   . HOH BA 5 .   ? 20.048  -11.169 -27.374 1.00 25.44 ? 714 HOH D O   1 
HETATM 10184 O  O   . HOH BA 5 .   ? -3.894  -8.823  -18.529 1.00 21.73 ? 715 HOH D O   1 
HETATM 10185 O  O   . HOH BA 5 .   ? -8.089  -10.506 -41.766 1.00 38.67 ? 716 HOH D O   1 
HETATM 10186 O  O   . HOH BA 5 .   ? -14.610 9.401   -41.818 1.00 35.31 ? 717 HOH D O   1 
HETATM 10187 O  O   . HOH BA 5 .   ? 19.796  -5.689  -41.683 1.00 21.53 ? 718 HOH D O   1 
HETATM 10188 O  O   . HOH BA 5 .   ? -1.019  -15.240 -44.260 1.00 28.19 ? 719 HOH D O   1 
HETATM 10189 O  O   . HOH BA 5 .   ? -10.702 18.562  -28.288 1.00 39.52 ? 720 HOH D O   1 
HETATM 10190 O  O   . HOH BA 5 .   ? 4.313   15.824  -42.343 1.00 38.00 ? 721 HOH D O   1 
HETATM 10191 O  O   . HOH BA 5 .   ? 20.828  11.813  -52.222 1.00 35.89 ? 722 HOH D O   1 
HETATM 10192 O  O   . HOH BA 5 .   ? -7.826  -6.522  -18.140 1.00 32.88 ? 723 HOH D O   1 
HETATM 10193 O  O   . HOH BA 5 .   ? 10.740  3.866   -19.078 1.00 23.57 ? 724 HOH D O   1 
HETATM 10194 O  O   . HOH BA 5 .   ? -1.008  16.348  -57.399 1.00 39.21 ? 725 HOH D O   1 
HETATM 10195 O  O   . HOH BA 5 .   ? 14.555  -12.368 -54.647 1.00 29.02 ? 726 HOH D O   1 
HETATM 10196 O  O   . HOH BA 5 .   ? 11.993  20.830  -32.404 1.00 20.04 ? 727 HOH D O   1 
HETATM 10197 O  O   . HOH BA 5 .   ? -6.504  -9.157  -52.834 1.00 27.36 ? 728 HOH D O   1 
HETATM 10198 O  O   . HOH BA 5 .   ? 2.270   -19.629 -36.459 1.00 35.18 ? 729 HOH D O   1 
HETATM 10199 O  O   . HOH BA 5 .   ? -2.351  21.922  -25.695 1.00 29.28 ? 730 HOH D O   1 
HETATM 10200 O  O   . HOH BA 5 .   ? 10.893  -12.569 -25.498 1.00 35.19 ? 731 HOH D O   1 
HETATM 10201 O  O   . HOH BA 5 .   ? 7.478   20.696  -33.667 1.00 32.97 ? 732 HOH D O   1 
HETATM 10202 O  O   . HOH BA 5 .   ? 1.358   -19.473 -39.050 1.00 30.99 ? 733 HOH D O   1 
HETATM 10203 O  O   . HOH BA 5 .   ? 27.740  13.221  -49.672 1.00 32.82 ? 734 HOH D O   1 
HETATM 10204 O  O   . HOH BA 5 .   ? 7.030   -8.436  -58.881 1.00 19.64 ? 735 HOH D O   1 
HETATM 10205 O  O   . HOH BA 5 .   ? -4.815  23.413  -27.330 1.00 39.19 ? 736 HOH D O   1 
HETATM 10206 O  O   . HOH BA 5 .   ? -6.636  -8.812  -18.243 1.00 23.66 ? 737 HOH D O   1 
HETATM 10207 O  O   . HOH BA 5 .   ? 11.878  6.182   -19.519 1.00 27.42 ? 738 HOH D O   1 
HETATM 10208 O  O   . HOH BA 5 .   ? 10.168  8.576   -19.517 1.00 30.03 ? 739 HOH D O   1 
HETATM 10209 O  O   . HOH BA 5 .   ? -7.767  -10.149 -20.260 1.00 32.31 ? 740 HOH D O   1 
HETATM 10210 O  O   . HOH BA 5 .   ? 26.632  15.195  -51.203 1.00 32.99 ? 741 HOH D O   1 
HETATM 10211 O  O   . HOH BA 5 .   ? -4.255  -14.110 -41.606 1.00 32.31 ? 742 HOH D O   1 
HETATM 10212 O  O   . HOH BA 5 .   ? -6.878  -11.001 -24.214 1.00 36.63 ? 743 HOH D O   1 
HETATM 10213 O  O   . HOH BA 5 .   ? -3.563  -15.628 -43.477 1.00 34.51 ? 744 HOH D O   1 
# 
