data_8Y4H
# 
_entry.id   8Y4H 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   8Y4H         pdb_00008y4h 10.2210/pdb8y4h/pdb 
WWPDB D_1300044753 ?            ?                   
# 
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 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-01-08 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_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             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
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' citation        
2 2 'Structure model' citation_author 
# 
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' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.journal_volume'          
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 2 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8Y4H 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-30 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              rmsl_2040@163.com 
_pdbx_contact_author.name_first         Jian 
_pdbx_contact_author.name_last          Li 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9511-4219 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Guo, L.'    1 ? 
'Wang, W.W.' 2 ? 
'Zhang, J.'  3 ? 
'Li, J.'     4 ? 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Commun Biol' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2399-3642 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            8 
_citation.language                  ? 
_citation.page_first                493 
_citation.page_last                 493 
_citation.title                     
'Inhibitory efficacy and structural insights of Bofutrelvir against SARS-CoV-2 M pro mutants and MERS-CoV M pro.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s42003-025-07929-9 
_citation.pdbx_database_id_PubMed   40133408 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wang, W.' 1 0009-0007-7332-8217 
primary 'Zhou, X.' 2 ?                   
primary 'Li, W.'   3 ?                   
primary 'Zeng, P.' 4 ?                   
primary 'Guo, L.'  5 ?                   
primary 'Wang, Q.' 6 0000-0002-0614-6903 
primary 'Li, J.'   7 0000-0001-9511-4219 
# 
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 '3C-like proteinase nsp5' 33333.027 2   3.4.22.69 ? ? ? 
2 non-polymer syn 
;~{N}-[(2~{S})-3-cyclohexyl-1-oxidanylidene-1-[[(2~{S})-1-oxidanylidene-3-[(3~{S})-2-oxidanylidenepyrrolidin-3-yl]propan-2-yl]amino]propan-2-yl]-1~{H}-indole-2-carboxamide
;
452.546   2   ?         ? ? ? 
3 water       nat water 18.015    353 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '3CL-PRO,3CLp,Main protease,Mpro,Non-structural protein 5,nsp5,SARS coronavirus main proteinase' 
# 
_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       
;FRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSM
QNCVLKLRVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYM
HHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPL
TQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;FRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSM
QNCVLKLRVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYM
HHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPL
TQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGV
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;~{N}-[(2~{S})-3-cyclohexyl-1-oxidanylidene-1-[[(2~{S})-1-oxidanylidene-3-[(3~{S})-2-oxidanylidenepyrrolidin-3-yl]propan-2-yl]amino]propan-2-yl]-1~{H}-indole-2-carboxamide
;
FHR 
3 water HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   PHE n 
1 2   ARG n 
1 3   LYS n 
1 4   MET n 
1 5   ALA n 
1 6   PHE n 
1 7   PRO n 
1 8   SER n 
1 9   GLY n 
1 10  LYS n 
1 11  VAL n 
1 12  GLU n 
1 13  GLY n 
1 14  CYS n 
1 15  MET n 
1 16  VAL n 
1 17  GLN n 
1 18  VAL n 
1 19  THR n 
1 20  CYS n 
1 21  GLY n 
1 22  THR n 
1 23  THR n 
1 24  THR n 
1 25  LEU n 
1 26  ASN n 
1 27  GLY n 
1 28  LEU n 
1 29  TRP n 
1 30  LEU n 
1 31  ASP n 
1 32  ASP n 
1 33  VAL n 
1 34  VAL n 
1 35  TYR n 
1 36  CYS n 
1 37  PRO n 
1 38  ARG n 
1 39  HIS n 
1 40  VAL n 
1 41  ILE n 
1 42  CYS n 
1 43  THR n 
1 44  SER n 
1 45  GLU n 
1 46  ASP n 
1 47  MET n 
1 48  LEU n 
1 49  ASN n 
1 50  PRO n 
1 51  ASN n 
1 52  TYR n 
1 53  GLU n 
1 54  ASP n 
1 55  LEU n 
1 56  LEU n 
1 57  ILE n 
1 58  ARG n 
1 59  LYS n 
1 60  SER n 
1 61  ASN n 
1 62  HIS n 
1 63  ASN n 
1 64  PHE n 
1 65  LEU n 
1 66  VAL n 
1 67  GLN n 
1 68  ALA n 
1 69  GLY n 
1 70  ASN n 
1 71  VAL n 
1 72  GLN n 
1 73  LEU n 
1 74  ARG n 
1 75  VAL n 
1 76  ILE n 
1 77  GLY n 
1 78  HIS n 
1 79  SER n 
1 80  MET n 
1 81  GLN n 
1 82  ASN n 
1 83  CYS n 
1 84  VAL n 
1 85  LEU n 
1 86  LYS n 
1 87  LEU n 
1 88  ARG n 
1 89  VAL n 
1 90  ASP n 
1 91  THR n 
1 92  ALA n 
1 93  ASN n 
1 94  PRO n 
1 95  LYS n 
1 96  THR n 
1 97  PRO n 
1 98  LYS n 
1 99  TYR n 
1 100 LYS n 
1 101 PHE n 
1 102 VAL n 
1 103 ARG n 
1 104 ILE n 
1 105 GLN n 
1 106 PRO n 
1 107 GLY n 
1 108 GLN n 
1 109 THR n 
1 110 PHE n 
1 111 SER n 
1 112 VAL n 
1 113 LEU n 
1 114 ALA n 
1 115 CYS n 
1 116 TYR n 
1 117 ASN n 
1 118 GLY n 
1 119 SER n 
1 120 PRO n 
1 121 SER n 
1 122 GLY n 
1 123 VAL n 
1 124 TYR n 
1 125 GLN n 
1 126 CYS n 
1 127 ALA n 
1 128 MET n 
1 129 ARG n 
1 130 PRO n 
1 131 ASN n 
1 132 PHE n 
1 133 THR n 
1 134 ILE n 
1 135 LYS n 
1 136 GLY n 
1 137 SER n 
1 138 PHE n 
1 139 LEU n 
1 140 ASN n 
1 141 GLY n 
1 142 SER n 
1 143 CYS n 
1 144 GLY n 
1 145 SER n 
1 146 VAL n 
1 147 GLY n 
1 148 PHE n 
1 149 ASN n 
1 150 ILE n 
1 151 ASP n 
1 152 TYR n 
1 153 ASP n 
1 154 CYS n 
1 155 VAL n 
1 156 SER n 
1 157 PHE n 
1 158 CYS n 
1 159 TYR n 
1 160 MET n 
1 161 HIS n 
1 162 HIS n 
1 163 MET n 
1 164 GLU n 
1 165 LEU n 
1 166 PRO n 
1 167 THR n 
1 168 GLY n 
1 169 VAL n 
1 170 HIS n 
1 171 ALA n 
1 172 GLY n 
1 173 THR n 
1 174 ASP n 
1 175 LEU n 
1 176 GLU n 
1 177 GLY n 
1 178 ASN n 
1 179 PHE n 
1 180 TYR n 
1 181 GLY n 
1 182 PRO n 
1 183 PHE n 
1 184 VAL n 
1 185 ASP n 
1 186 ARG n 
1 187 GLN n 
1 188 THR n 
1 189 ALA n 
1 190 GLN n 
1 191 ALA n 
1 192 ALA n 
1 193 GLY n 
1 194 THR n 
1 195 ASP n 
1 196 THR n 
1 197 THR n 
1 198 ILE n 
1 199 THR n 
1 200 VAL n 
1 201 ASN n 
1 202 VAL n 
1 203 LEU n 
1 204 ALA n 
1 205 TRP n 
1 206 LEU n 
1 207 TYR n 
1 208 ALA n 
1 209 ALA n 
1 210 VAL n 
1 211 ILE n 
1 212 ASN n 
1 213 GLY n 
1 214 ASP n 
1 215 ARG n 
1 216 TRP n 
1 217 PHE n 
1 218 LEU n 
1 219 ASN n 
1 220 ARG n 
1 221 PHE n 
1 222 THR n 
1 223 THR n 
1 224 THR n 
1 225 LEU n 
1 226 ASN n 
1 227 ASP n 
1 228 PHE n 
1 229 ASN n 
1 230 LEU n 
1 231 VAL n 
1 232 ALA n 
1 233 MET n 
1 234 LYS n 
1 235 TYR n 
1 236 ASN n 
1 237 TYR n 
1 238 GLU n 
1 239 PRO n 
1 240 LEU n 
1 241 THR n 
1 242 GLN n 
1 243 ASP n 
1 244 HIS n 
1 245 VAL n 
1 246 ASP n 
1 247 ILE n 
1 248 LEU n 
1 249 GLY n 
1 250 PRO n 
1 251 LEU n 
1 252 SER n 
1 253 ALA n 
1 254 GLN n 
1 255 THR n 
1 256 GLY n 
1 257 ILE n 
1 258 ALA n 
1 259 VAL n 
1 260 LEU n 
1 261 ASP n 
1 262 MET n 
1 263 CYS n 
1 264 ALA n 
1 265 SER n 
1 266 LEU n 
1 267 LYS n 
1 268 GLU n 
1 269 LEU n 
1 270 LEU n 
1 271 GLN n 
1 272 ASN n 
1 273 GLY n 
1 274 MET n 
1 275 ASN n 
1 276 GLY n 
1 277 ARG n 
1 278 THR n 
1 279 ILE n 
1 280 LEU n 
1 281 GLY n 
1 282 SER n 
1 283 ALA n 
1 284 LEU n 
1 285 LEU n 
1 286 GLU n 
1 287 ASP n 
1 288 GLU n 
1 289 PHE n 
1 290 THR n 
1 291 PRO n 
1 292 PHE n 
1 293 ASP n 
1 294 VAL n 
1 295 VAL n 
1 296 ARG n 
1 297 GLN n 
1 298 CYS n 
1 299 SER n 
1 300 GLY n 
1 301 VAL 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                   301 
_entity_src_gen.gene_src_common_name               '2019-nCoV, SARS-CoV-2' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_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      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_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              ? 
_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          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_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 
FHR peptide-like        . 
;~{N}-[(2~{S})-3-cyclohexyl-1-oxidanylidene-1-[[(2~{S})-1-oxidanylidene-3-[(3~{S})-2-oxidanylidenepyrrolidin-3-yl]propan-2-yl]amino]propan-2-yl]-1~{H}-indole-2-carboxamide
;
? 'C25 H32 N4 O4'  452.546 
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 
# 
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   PHE 1   3   ?   ?   ?   A . n 
A 1 2   ARG 2   4   4   ARG ARG A . n 
A 1 3   LYS 3   5   5   LYS LYS A . n 
A 1 4   MET 4   6   6   MET MET A . n 
A 1 5   ALA 5   7   7   ALA ALA A . n 
A 1 6   PHE 6   8   8   PHE PHE A . n 
A 1 7   PRO 7   9   9   PRO PRO A . n 
A 1 8   SER 8   10  10  SER SER A . n 
A 1 9   GLY 9   11  11  GLY GLY A . n 
A 1 10  LYS 10  12  12  LYS LYS A . n 
A 1 11  VAL 11  13  13  VAL VAL A . n 
A 1 12  GLU 12  14  14  GLU GLU A . n 
A 1 13  GLY 13  15  15  GLY GLY A . n 
A 1 14  CYS 14  16  16  CYS CYS A . n 
A 1 15  MET 15  17  17  MET MET A . n 
A 1 16  VAL 16  18  18  VAL VAL A . n 
A 1 17  GLN 17  19  19  GLN GLN A . n 
A 1 18  VAL 18  20  20  VAL VAL A . n 
A 1 19  THR 19  21  21  THR THR A . n 
A 1 20  CYS 20  22  22  CYS CYS A . n 
A 1 21  GLY 21  23  23  GLY GLY A . n 
A 1 22  THR 22  24  24  THR THR A . n 
A 1 23  THR 23  25  25  THR THR A . n 
A 1 24  THR 24  26  26  THR THR A . n 
A 1 25  LEU 25  27  27  LEU LEU A . n 
A 1 26  ASN 26  28  28  ASN ASN A . n 
A 1 27  GLY 27  29  29  GLY GLY A . n 
A 1 28  LEU 28  30  30  LEU LEU A . n 
A 1 29  TRP 29  31  31  TRP TRP A . n 
A 1 30  LEU 30  32  32  LEU LEU A . n 
A 1 31  ASP 31  33  33  ASP ASP A . n 
A 1 32  ASP 32  34  34  ASP ASP A . n 
A 1 33  VAL 33  35  35  VAL VAL A . n 
A 1 34  VAL 34  36  36  VAL VAL A . n 
A 1 35  TYR 35  37  37  TYR TYR A . n 
A 1 36  CYS 36  38  38  CYS CYS A . n 
A 1 37  PRO 37  39  39  PRO PRO A . n 
A 1 38  ARG 38  40  40  ARG ARG A . n 
A 1 39  HIS 39  41  41  HIS HIS A . n 
A 1 40  VAL 40  42  42  VAL VAL A . n 
A 1 41  ILE 41  43  43  ILE ILE A . n 
A 1 42  CYS 42  44  44  CYS CYS A . n 
A 1 43  THR 43  45  45  THR THR A . n 
A 1 44  SER 44  46  46  SER SER A . n 
A 1 45  GLU 45  47  47  GLU GLU A . n 
A 1 46  ASP 46  48  48  ASP ASP A . n 
A 1 47  MET 47  49  49  MET MET A . n 
A 1 48  LEU 48  50  50  LEU LEU A . n 
A 1 49  ASN 49  51  51  ASN ASN A . n 
A 1 50  PRO 50  52  52  PRO PRO A . n 
A 1 51  ASN 51  53  53  ASN ASN A . n 
A 1 52  TYR 52  54  54  TYR TYR A . n 
A 1 53  GLU 53  55  55  GLU GLU A . n 
A 1 54  ASP 54  56  56  ASP ASP A . n 
A 1 55  LEU 55  57  57  LEU LEU A . n 
A 1 56  LEU 56  58  58  LEU LEU A . n 
A 1 57  ILE 57  59  59  ILE ILE A . n 
A 1 58  ARG 58  60  60  ARG ARG A . n 
A 1 59  LYS 59  61  61  LYS LYS A . n 
A 1 60  SER 60  62  62  SER SER A . n 
A 1 61  ASN 61  63  63  ASN ASN A . n 
A 1 62  HIS 62  64  64  HIS HIS A . n 
A 1 63  ASN 63  65  65  ASN ASN A . n 
A 1 64  PHE 64  66  66  PHE PHE A . n 
A 1 65  LEU 65  67  67  LEU LEU A . n 
A 1 66  VAL 66  68  68  VAL VAL A . n 
A 1 67  GLN 67  69  69  GLN GLN A . n 
A 1 68  ALA 68  70  70  ALA ALA A . n 
A 1 69  GLY 69  71  71  GLY GLY A . n 
A 1 70  ASN 70  72  72  ASN ASN A . n 
A 1 71  VAL 71  73  73  VAL VAL A . n 
A 1 72  GLN 72  74  74  GLN GLN A . n 
A 1 73  LEU 73  75  75  LEU LEU A . n 
A 1 74  ARG 74  76  76  ARG ARG A . n 
A 1 75  VAL 75  77  77  VAL VAL A . n 
A 1 76  ILE 76  78  78  ILE ILE A . n 
A 1 77  GLY 77  79  79  GLY GLY A . n 
A 1 78  HIS 78  80  80  HIS HIS A . n 
A 1 79  SER 79  81  81  SER SER A . n 
A 1 80  MET 80  82  82  MET MET A . n 
A 1 81  GLN 81  83  83  GLN GLN A . n 
A 1 82  ASN 82  84  84  ASN ASN A . n 
A 1 83  CYS 83  85  85  CYS CYS A . n 
A 1 84  VAL 84  86  86  VAL VAL A . n 
A 1 85  LEU 85  87  87  LEU LEU A . n 
A 1 86  LYS 86  88  88  LYS LYS A . n 
A 1 87  LEU 87  89  89  LEU LEU A . n 
A 1 88  ARG 88  90  90  ARG ARG A . n 
A 1 89  VAL 89  91  91  VAL VAL A . n 
A 1 90  ASP 90  92  92  ASP ASP A . n 
A 1 91  THR 91  93  93  THR THR A . n 
A 1 92  ALA 92  94  94  ALA ALA A . n 
A 1 93  ASN 93  95  95  ASN ASN A . n 
A 1 94  PRO 94  96  96  PRO PRO A . n 
A 1 95  LYS 95  97  97  LYS LYS A . n 
A 1 96  THR 96  98  98  THR THR A . n 
A 1 97  PRO 97  99  99  PRO PRO A . n 
A 1 98  LYS 98  100 100 LYS LYS A . n 
A 1 99  TYR 99  101 101 TYR TYR A . n 
A 1 100 LYS 100 102 102 LYS LYS A . n 
A 1 101 PHE 101 103 103 PHE PHE A . n 
A 1 102 VAL 102 104 104 VAL VAL A . n 
A 1 103 ARG 103 105 105 ARG ARG A . n 
A 1 104 ILE 104 106 106 ILE ILE A . n 
A 1 105 GLN 105 107 107 GLN GLN A . n 
A 1 106 PRO 106 108 108 PRO PRO A . n 
A 1 107 GLY 107 109 109 GLY GLY A . n 
A 1 108 GLN 108 110 110 GLN GLN A . n 
A 1 109 THR 109 111 111 THR THR A . n 
A 1 110 PHE 110 112 112 PHE PHE A . n 
A 1 111 SER 111 113 113 SER SER A . n 
A 1 112 VAL 112 114 114 VAL VAL A . n 
A 1 113 LEU 113 115 115 LEU LEU A . n 
A 1 114 ALA 114 116 116 ALA ALA A . n 
A 1 115 CYS 115 117 117 CYS CYS A . n 
A 1 116 TYR 116 118 118 TYR TYR A . n 
A 1 117 ASN 117 119 119 ASN ASN A . n 
A 1 118 GLY 118 120 120 GLY GLY A . n 
A 1 119 SER 119 121 121 SER SER A . n 
A 1 120 PRO 120 122 122 PRO PRO A . n 
A 1 121 SER 121 123 123 SER SER A . n 
A 1 122 GLY 122 124 124 GLY GLY A . n 
A 1 123 VAL 123 125 125 VAL VAL A . n 
A 1 124 TYR 124 126 126 TYR TYR A . n 
A 1 125 GLN 125 127 127 GLN GLN A . n 
A 1 126 CYS 126 128 128 CYS CYS A . n 
A 1 127 ALA 127 129 129 ALA ALA A . n 
A 1 128 MET 128 130 130 MET MET A . n 
A 1 129 ARG 129 131 131 ARG ARG A . n 
A 1 130 PRO 130 132 132 PRO PRO A . n 
A 1 131 ASN 131 133 133 ASN ASN A . n 
A 1 132 PHE 132 134 134 PHE PHE A . n 
A 1 133 THR 133 135 135 THR THR A . n 
A 1 134 ILE 134 136 136 ILE ILE A . n 
A 1 135 LYS 135 137 137 LYS LYS A . n 
A 1 136 GLY 136 138 138 GLY GLY A . n 
A 1 137 SER 137 139 139 SER SER A . n 
A 1 138 PHE 138 140 140 PHE PHE A . n 
A 1 139 LEU 139 141 141 LEU LEU A . n 
A 1 140 ASN 140 142 142 ASN ASN A . n 
A 1 141 GLY 141 143 143 GLY GLY A . n 
A 1 142 SER 142 144 144 SER SER A . n 
A 1 143 CYS 143 145 145 CYS CYS A . n 
A 1 144 GLY 144 146 146 GLY GLY A . n 
A 1 145 SER 145 147 147 SER SER A . n 
A 1 146 VAL 146 148 148 VAL VAL A . n 
A 1 147 GLY 147 149 149 GLY GLY A . n 
A 1 148 PHE 148 150 150 PHE PHE A . n 
A 1 149 ASN 149 151 151 ASN ASN A . n 
A 1 150 ILE 150 152 152 ILE ILE A . n 
A 1 151 ASP 151 153 153 ASP ASP A . n 
A 1 152 TYR 152 154 154 TYR TYR A . n 
A 1 153 ASP 153 155 155 ASP ASP A . n 
A 1 154 CYS 154 156 156 CYS CYS A . n 
A 1 155 VAL 155 157 157 VAL VAL A . n 
A 1 156 SER 156 158 158 SER SER A . n 
A 1 157 PHE 157 159 159 PHE PHE A . n 
A 1 158 CYS 158 160 160 CYS CYS A . n 
A 1 159 TYR 159 161 161 TYR TYR A . n 
A 1 160 MET 160 162 162 MET MET A . n 
A 1 161 HIS 161 163 163 HIS HIS A . n 
A 1 162 HIS 162 164 164 HIS HIS A . n 
A 1 163 MET 163 165 165 MET MET A . n 
A 1 164 GLU 164 166 166 GLU GLU A . n 
A 1 165 LEU 165 167 167 LEU LEU A . n 
A 1 166 PRO 166 168 168 PRO PRO A . n 
A 1 167 THR 167 169 169 THR THR A . n 
A 1 168 GLY 168 170 170 GLY GLY A . n 
A 1 169 VAL 169 171 171 VAL VAL A . n 
A 1 170 HIS 170 172 172 HIS HIS A . n 
A 1 171 ALA 171 173 173 ALA ALA A . n 
A 1 172 GLY 172 174 174 GLY GLY A . n 
A 1 173 THR 173 175 175 THR THR A . n 
A 1 174 ASP 174 176 176 ASP ASP A . n 
A 1 175 LEU 175 177 177 LEU LEU A . n 
A 1 176 GLU 176 178 178 GLU GLU A . n 
A 1 177 GLY 177 179 179 GLY GLY A . n 
A 1 178 ASN 178 180 180 ASN ASN A . n 
A 1 179 PHE 179 181 181 PHE PHE A . n 
A 1 180 TYR 180 182 182 TYR TYR A . n 
A 1 181 GLY 181 183 183 GLY GLY A . n 
A 1 182 PRO 182 184 184 PRO PRO A . n 
A 1 183 PHE 183 185 185 PHE PHE A . n 
A 1 184 VAL 184 186 186 VAL VAL A . n 
A 1 185 ASP 185 187 187 ASP ASP A . n 
A 1 186 ARG 186 188 188 ARG ARG A . n 
A 1 187 GLN 187 189 189 GLN GLN A . n 
A 1 188 THR 188 190 190 THR THR A . n 
A 1 189 ALA 189 191 191 ALA ALA A . n 
A 1 190 GLN 190 192 192 GLN GLN A . n 
A 1 191 ALA 191 193 193 ALA ALA A . n 
A 1 192 ALA 192 194 194 ALA ALA A . n 
A 1 193 GLY 193 195 195 GLY GLY A . n 
A 1 194 THR 194 196 196 THR THR A . n 
A 1 195 ASP 195 197 197 ASP ASP A . n 
A 1 196 THR 196 198 198 THR THR A . n 
A 1 197 THR 197 199 199 THR THR A . n 
A 1 198 ILE 198 200 200 ILE ILE A . n 
A 1 199 THR 199 201 201 THR THR A . n 
A 1 200 VAL 200 202 202 VAL VAL A . n 
A 1 201 ASN 201 203 203 ASN ASN A . n 
A 1 202 VAL 202 204 204 VAL VAL A . n 
A 1 203 LEU 203 205 205 LEU LEU A . n 
A 1 204 ALA 204 206 206 ALA ALA A . n 
A 1 205 TRP 205 207 207 TRP TRP A . n 
A 1 206 LEU 206 208 208 LEU LEU A . n 
A 1 207 TYR 207 209 209 TYR TYR A . n 
A 1 208 ALA 208 210 210 ALA ALA A . n 
A 1 209 ALA 209 211 211 ALA ALA A . n 
A 1 210 VAL 210 212 212 VAL VAL A . n 
A 1 211 ILE 211 213 213 ILE ILE A . n 
A 1 212 ASN 212 214 214 ASN ASN A . n 
A 1 213 GLY 213 215 215 GLY GLY A . n 
A 1 214 ASP 214 216 216 ASP ASP A . n 
A 1 215 ARG 215 217 217 ARG ARG A . n 
A 1 216 TRP 216 218 218 TRP TRP A . n 
A 1 217 PHE 217 219 219 PHE PHE A . n 
A 1 218 LEU 218 220 220 LEU LEU A . n 
A 1 219 ASN 219 221 221 ASN ASN A . n 
A 1 220 ARG 220 222 222 ARG ALA A . n 
A 1 221 PHE 221 223 223 PHE ARG A . n 
A 1 222 THR 222 224 224 THR THR A . n 
A 1 223 THR 223 225 225 THR THR A . n 
A 1 224 THR 224 226 226 THR THR A . n 
A 1 225 LEU 225 227 227 LEU LEU A . n 
A 1 226 ASN 226 228 228 ASN ASN A . n 
A 1 227 ASP 227 229 229 ASP ASP A . n 
A 1 228 PHE 228 230 230 PHE PHE A . n 
A 1 229 ASN 229 231 231 ASN ASN A . n 
A 1 230 LEU 230 232 232 LEU LEU A . n 
A 1 231 VAL 231 233 233 VAL VAL A . n 
A 1 232 ALA 232 234 234 ALA ALA A . n 
A 1 233 MET 233 235 235 MET MET A . n 
A 1 234 LYS 234 236 236 LYS LYS A . n 
A 1 235 TYR 235 237 237 TYR TYR A . n 
A 1 236 ASN 236 238 238 ASN ASN A . n 
A 1 237 TYR 237 239 239 TYR TYR A . n 
A 1 238 GLU 238 240 240 GLU GLU A . n 
A 1 239 PRO 239 241 241 PRO PRO A . n 
A 1 240 LEU 240 242 242 LEU LEU A . n 
A 1 241 THR 241 243 243 THR THR A . n 
A 1 242 GLN 242 244 244 GLN GLN A . n 
A 1 243 ASP 243 245 245 ASP ASP A . n 
A 1 244 HIS 244 246 246 HIS HIS A . n 
A 1 245 VAL 245 247 247 VAL VAL A . n 
A 1 246 ASP 246 248 248 ASP ASP A . n 
A 1 247 ILE 247 249 249 ILE ILE A . n 
A 1 248 LEU 248 250 250 LEU LEU A . n 
A 1 249 GLY 249 251 251 GLY GLY A . n 
A 1 250 PRO 250 252 252 PRO PRO A . n 
A 1 251 LEU 251 253 253 LEU LEU A . n 
A 1 252 SER 252 254 254 SER SER A . n 
A 1 253 ALA 253 255 255 ALA ALA A . n 
A 1 254 GLN 254 256 256 GLN GLN A . n 
A 1 255 THR 255 257 257 THR THR A . n 
A 1 256 GLY 256 258 258 GLY GLY A . n 
A 1 257 ILE 257 259 259 ILE ILE A . n 
A 1 258 ALA 258 260 260 ALA ALA A . n 
A 1 259 VAL 259 261 261 VAL VAL A . n 
A 1 260 LEU 260 262 262 LEU LEU A . n 
A 1 261 ASP 261 263 263 ASP ASP A . n 
A 1 262 MET 262 264 264 MET MET A . n 
A 1 263 CYS 263 265 265 CYS CYS A . n 
A 1 264 ALA 264 266 266 ALA ALA A . n 
A 1 265 SER 265 267 267 SER SER A . n 
A 1 266 LEU 266 268 268 LEU LEU A . n 
A 1 267 LYS 267 269 269 LYS LYS A . n 
A 1 268 GLU 268 270 270 GLU GLU A . n 
A 1 269 LEU 269 271 271 LEU LEU A . n 
A 1 270 LEU 270 272 272 LEU LEU A . n 
A 1 271 GLN 271 273 273 GLN GLN A . n 
A 1 272 ASN 272 274 274 ASN ASN A . n 
A 1 273 GLY 273 275 275 GLY GLY A . n 
A 1 274 MET 274 276 276 MET MET A . n 
A 1 275 ASN 275 277 277 ASN ASN A . n 
A 1 276 GLY 276 278 278 GLY GLY A . n 
A 1 277 ARG 277 279 279 ARG ARG A . n 
A 1 278 THR 278 280 280 THR THR A . n 
A 1 279 ILE 279 281 281 ILE ILE A . n 
A 1 280 LEU 280 282 282 LEU LEU A . n 
A 1 281 GLY 281 283 283 GLY GLY A . n 
A 1 282 SER 282 284 284 SER SER A . n 
A 1 283 ALA 283 285 285 ALA ALA A . n 
A 1 284 LEU 284 286 286 LEU LEU A . n 
A 1 285 LEU 285 287 287 LEU LEU A . n 
A 1 286 GLU 286 288 288 GLU GLU A . n 
A 1 287 ASP 287 289 289 ASP ASP A . n 
A 1 288 GLU 288 290 290 GLU GLU A . n 
A 1 289 PHE 289 291 291 PHE PHE A . n 
A 1 290 THR 290 292 292 THR THR A . n 
A 1 291 PRO 291 293 293 PRO PRO A . n 
A 1 292 PHE 292 294 294 PHE PHE A . n 
A 1 293 ASP 293 295 295 ASP ASP A . n 
A 1 294 VAL 294 296 296 VAL VAL A . n 
A 1 295 VAL 295 297 297 VAL VAL A . n 
A 1 296 ARG 296 298 298 ARG ARG A . n 
A 1 297 GLN 297 299 299 GLN GLN A . n 
A 1 298 CYS 298 300 300 CYS CYS A . n 
A 1 299 SER 299 301 301 SER SER A . n 
A 1 300 GLY 300 302 302 GLY GLY A . n 
A 1 301 VAL 301 303 303 VAL VAL A . n 
B 1 1   PHE 1   3   3   PHE PHE B . n 
B 1 2   ARG 2   4   4   ARG ARG B . n 
B 1 3   LYS 3   5   5   LYS LYS B . n 
B 1 4   MET 4   6   6   MET MET B . n 
B 1 5   ALA 5   7   7   ALA ALA B . n 
B 1 6   PHE 6   8   8   PHE PHE B . n 
B 1 7   PRO 7   9   9   PRO PRO B . n 
B 1 8   SER 8   10  10  SER SER B . n 
B 1 9   GLY 9   11  11  GLY GLY B . n 
B 1 10  LYS 10  12  12  LYS LYS B . n 
B 1 11  VAL 11  13  13  VAL VAL B . n 
B 1 12  GLU 12  14  14  GLU GLU B . n 
B 1 13  GLY 13  15  15  GLY GLY B . n 
B 1 14  CYS 14  16  16  CYS CYS B . n 
B 1 15  MET 15  17  17  MET MET B . n 
B 1 16  VAL 16  18  18  VAL VAL B . n 
B 1 17  GLN 17  19  19  GLN GLN B . n 
B 1 18  VAL 18  20  20  VAL VAL B . n 
B 1 19  THR 19  21  21  THR THR B . n 
B 1 20  CYS 20  22  22  CYS CYS B . n 
B 1 21  GLY 21  23  23  GLY GLY B . n 
B 1 22  THR 22  24  24  THR THR B . n 
B 1 23  THR 23  25  25  THR THR B . n 
B 1 24  THR 24  26  26  THR THR B . n 
B 1 25  LEU 25  27  27  LEU LEU B . n 
B 1 26  ASN 26  28  28  ASN ASN B . n 
B 1 27  GLY 27  29  29  GLY GLY B . n 
B 1 28  LEU 28  30  30  LEU LEU B . n 
B 1 29  TRP 29  31  31  TRP TRP B . n 
B 1 30  LEU 30  32  32  LEU LEU B . n 
B 1 31  ASP 31  33  33  ASP ASP B . n 
B 1 32  ASP 32  34  34  ASP ASP B . n 
B 1 33  VAL 33  35  35  VAL VAL B . n 
B 1 34  VAL 34  36  36  VAL VAL B . n 
B 1 35  TYR 35  37  37  TYR TYR B . n 
B 1 36  CYS 36  38  38  CYS CYS B . n 
B 1 37  PRO 37  39  39  PRO PRO B . n 
B 1 38  ARG 38  40  40  ARG ARG B . n 
B 1 39  HIS 39  41  41  HIS HIS B . n 
B 1 40  VAL 40  42  42  VAL VAL B . n 
B 1 41  ILE 41  43  43  ILE ILE B . n 
B 1 42  CYS 42  44  44  CYS CYS B . n 
B 1 43  THR 43  45  45  THR THR B . n 
B 1 44  SER 44  46  46  SER SER B . n 
B 1 45  GLU 45  47  47  GLU GLU B . n 
B 1 46  ASP 46  48  48  ASP ASP B . n 
B 1 47  MET 47  49  49  MET MET B . n 
B 1 48  LEU 48  50  50  LEU LEU B . n 
B 1 49  ASN 49  51  51  ASN ASN B . n 
B 1 50  PRO 50  52  52  PRO PRO B . n 
B 1 51  ASN 51  53  53  ASN ASN B . n 
B 1 52  TYR 52  54  54  TYR TYR B . n 
B 1 53  GLU 53  55  55  GLU GLU B . n 
B 1 54  ASP 54  56  56  ASP ASP B . n 
B 1 55  LEU 55  57  57  LEU LEU B . n 
B 1 56  LEU 56  58  58  LEU LEU B . n 
B 1 57  ILE 57  59  59  ILE ILE B . n 
B 1 58  ARG 58  60  60  ARG ARG B . n 
B 1 59  LYS 59  61  61  LYS LYS B . n 
B 1 60  SER 60  62  62  SER SER B . n 
B 1 61  ASN 61  63  63  ASN ASN B . n 
B 1 62  HIS 62  64  64  HIS HIS B . n 
B 1 63  ASN 63  65  65  ASN ASN B . n 
B 1 64  PHE 64  66  66  PHE PHE B . n 
B 1 65  LEU 65  67  67  LEU LEU B . n 
B 1 66  VAL 66  68  68  VAL VAL B . n 
B 1 67  GLN 67  69  69  GLN GLN B . n 
B 1 68  ALA 68  70  70  ALA ALA B . n 
B 1 69  GLY 69  71  71  GLY GLY B . n 
B 1 70  ASN 70  72  72  ASN ASN B . n 
B 1 71  VAL 71  73  73  VAL VAL B . n 
B 1 72  GLN 72  74  74  GLN GLN B . n 
B 1 73  LEU 73  75  75  LEU LEU B . n 
B 1 74  ARG 74  76  76  ARG ARG B . n 
B 1 75  VAL 75  77  77  VAL VAL B . n 
B 1 76  ILE 76  78  78  ILE ILE B . n 
B 1 77  GLY 77  79  79  GLY GLY B . n 
B 1 78  HIS 78  80  80  HIS HIS B . n 
B 1 79  SER 79  81  81  SER SER B . n 
B 1 80  MET 80  82  82  MET MET B . n 
B 1 81  GLN 81  83  83  GLN GLN B . n 
B 1 82  ASN 82  84  84  ASN ASN B . n 
B 1 83  CYS 83  85  85  CYS CYS B . n 
B 1 84  VAL 84  86  86  VAL VAL B . n 
B 1 85  LEU 85  87  87  LEU LEU B . n 
B 1 86  LYS 86  88  88  LYS LYS B . n 
B 1 87  LEU 87  89  89  LEU LEU B . n 
B 1 88  ARG 88  90  90  ARG ARG B . n 
B 1 89  VAL 89  91  91  VAL VAL B . n 
B 1 90  ASP 90  92  92  ASP ASP B . n 
B 1 91  THR 91  93  93  THR THR B . n 
B 1 92  ALA 92  94  94  ALA ALA B . n 
B 1 93  ASN 93  95  95  ASN ASN B . n 
B 1 94  PRO 94  96  96  PRO PRO B . n 
B 1 95  LYS 95  97  97  LYS LYS B . n 
B 1 96  THR 96  98  98  THR THR B . n 
B 1 97  PRO 97  99  99  PRO PRO B . n 
B 1 98  LYS 98  100 100 LYS LYS B . n 
B 1 99  TYR 99  101 101 TYR TYR B . n 
B 1 100 LYS 100 102 102 LYS LYS B . n 
B 1 101 PHE 101 103 103 PHE PHE B . n 
B 1 102 VAL 102 104 104 VAL VAL B . n 
B 1 103 ARG 103 105 105 ARG ARG B . n 
B 1 104 ILE 104 106 106 ILE ILE B . n 
B 1 105 GLN 105 107 107 GLN GLN B . n 
B 1 106 PRO 106 108 108 PRO PRO B . n 
B 1 107 GLY 107 109 109 GLY GLY B . n 
B 1 108 GLN 108 110 110 GLN GLN B . n 
B 1 109 THR 109 111 111 THR THR B . n 
B 1 110 PHE 110 112 112 PHE PHE B . n 
B 1 111 SER 111 113 113 SER SER B . n 
B 1 112 VAL 112 114 114 VAL VAL B . n 
B 1 113 LEU 113 115 115 LEU LEU B . n 
B 1 114 ALA 114 116 116 ALA ALA B . n 
B 1 115 CYS 115 117 117 CYS CYS B . n 
B 1 116 TYR 116 118 118 TYR TYR B . n 
B 1 117 ASN 117 119 119 ASN ASN B . n 
B 1 118 GLY 118 120 120 GLY GLY B . n 
B 1 119 SER 119 121 121 SER SER B . n 
B 1 120 PRO 120 122 122 PRO PRO B . n 
B 1 121 SER 121 123 123 SER SER B . n 
B 1 122 GLY 122 124 124 GLY GLY B . n 
B 1 123 VAL 123 125 125 VAL VAL B . n 
B 1 124 TYR 124 126 126 TYR TYR B . n 
B 1 125 GLN 125 127 127 GLN GLN B . n 
B 1 126 CYS 126 128 128 CYS CYS B . n 
B 1 127 ALA 127 129 129 ALA ALA B . n 
B 1 128 MET 128 130 130 MET MET B . n 
B 1 129 ARG 129 131 131 ARG ARG B . n 
B 1 130 PRO 130 132 132 PRO PRO B . n 
B 1 131 ASN 131 133 133 ASN ASN B . n 
B 1 132 PHE 132 134 134 PHE PHE B . n 
B 1 133 THR 133 135 135 THR THR B . n 
B 1 134 ILE 134 136 136 ILE ILE B . n 
B 1 135 LYS 135 137 137 LYS LYS B . n 
B 1 136 GLY 136 138 138 GLY GLY B . n 
B 1 137 SER 137 139 139 SER SER B . n 
B 1 138 PHE 138 140 140 PHE PHE B . n 
B 1 139 LEU 139 141 141 LEU LEU B . n 
B 1 140 ASN 140 142 142 ASN ASN B . n 
B 1 141 GLY 141 143 143 GLY GLY B . n 
B 1 142 SER 142 144 144 SER SER B . n 
B 1 143 CYS 143 145 145 CYS CYS B . n 
B 1 144 GLY 144 146 146 GLY GLY B . n 
B 1 145 SER 145 147 147 SER SER B . n 
B 1 146 VAL 146 148 148 VAL VAL B . n 
B 1 147 GLY 147 149 149 GLY GLY B . n 
B 1 148 PHE 148 150 150 PHE PHE B . n 
B 1 149 ASN 149 151 151 ASN ASN B . n 
B 1 150 ILE 150 152 152 ILE ILE B . n 
B 1 151 ASP 151 153 153 ASP ASP B . n 
B 1 152 TYR 152 154 154 TYR TYR B . n 
B 1 153 ASP 153 155 155 ASP ASP B . n 
B 1 154 CYS 154 156 156 CYS CYS B . n 
B 1 155 VAL 155 157 157 VAL VAL B . n 
B 1 156 SER 156 158 158 SER SER B . n 
B 1 157 PHE 157 159 159 PHE PHE B . n 
B 1 158 CYS 158 160 160 CYS CYS B . n 
B 1 159 TYR 159 161 161 TYR TYR B . n 
B 1 160 MET 160 162 162 MET MET B . n 
B 1 161 HIS 161 163 163 HIS HIS B . n 
B 1 162 HIS 162 164 164 HIS HIS B . n 
B 1 163 MET 163 165 165 MET MET B . n 
B 1 164 GLU 164 166 166 GLU GLU B . n 
B 1 165 LEU 165 167 167 LEU LEU B . n 
B 1 166 PRO 166 168 168 PRO PRO B . n 
B 1 167 THR 167 169 169 THR THR B . n 
B 1 168 GLY 168 170 170 GLY GLY B . n 
B 1 169 VAL 169 171 171 VAL VAL B . n 
B 1 170 HIS 170 172 172 HIS HIS B . n 
B 1 171 ALA 171 173 173 ALA ALA B . n 
B 1 172 GLY 172 174 174 GLY GLY B . n 
B 1 173 THR 173 175 175 THR THR B . n 
B 1 174 ASP 174 176 176 ASP ASP B . n 
B 1 175 LEU 175 177 177 LEU LEU B . n 
B 1 176 GLU 176 178 178 GLU GLU B . n 
B 1 177 GLY 177 179 179 GLY GLY B . n 
B 1 178 ASN 178 180 180 ASN ASN B . n 
B 1 179 PHE 179 181 181 PHE PHE B . n 
B 1 180 TYR 180 182 182 TYR TYR B . n 
B 1 181 GLY 181 183 183 GLY GLY B . n 
B 1 182 PRO 182 184 184 PRO PRO B . n 
B 1 183 PHE 183 185 185 PHE PHE B . n 
B 1 184 VAL 184 186 186 VAL VAL B . n 
B 1 185 ASP 185 187 187 ASP ASP B . n 
B 1 186 ARG 186 188 188 ARG ARG B . n 
B 1 187 GLN 187 189 189 GLN GLN B . n 
B 1 188 THR 188 190 190 THR THR B . n 
B 1 189 ALA 189 191 191 ALA ALA B . n 
B 1 190 GLN 190 192 192 GLN GLN B . n 
B 1 191 ALA 191 193 193 ALA ALA B . n 
B 1 192 ALA 192 194 194 ALA ALA B . n 
B 1 193 GLY 193 195 195 GLY GLY B . n 
B 1 194 THR 194 196 196 THR THR B . n 
B 1 195 ASP 195 197 197 ASP ASP B . n 
B 1 196 THR 196 198 198 THR THR B . n 
B 1 197 THR 197 199 199 THR THR B . n 
B 1 198 ILE 198 200 200 ILE ILE B . n 
B 1 199 THR 199 201 201 THR THR B . n 
B 1 200 VAL 200 202 202 VAL VAL B . n 
B 1 201 ASN 201 203 203 ASN ASN B . n 
B 1 202 VAL 202 204 204 VAL VAL B . n 
B 1 203 LEU 203 205 205 LEU LEU B . n 
B 1 204 ALA 204 206 206 ALA ALA B . n 
B 1 205 TRP 205 207 207 TRP TRP B . n 
B 1 206 LEU 206 208 208 LEU LEU B . n 
B 1 207 TYR 207 209 209 TYR TYR B . n 
B 1 208 ALA 208 210 210 ALA ALA B . n 
B 1 209 ALA 209 211 211 ALA ALA B . n 
B 1 210 VAL 210 212 212 VAL VAL B . n 
B 1 211 ILE 211 213 213 ILE ILE B . n 
B 1 212 ASN 212 214 214 ASN ASN B . n 
B 1 213 GLY 213 215 215 GLY GLY B . n 
B 1 214 ASP 214 216 216 ASP ASP B . n 
B 1 215 ARG 215 217 217 ARG ARG B . n 
B 1 216 TRP 216 218 218 TRP TRP B . n 
B 1 217 PHE 217 219 219 PHE PHE B . n 
B 1 218 LEU 218 220 220 LEU LEU B . n 
B 1 219 ASN 219 221 221 ASN ASN B . n 
B 1 220 ARG 220 222 222 ARG ARG B . n 
B 1 221 PHE 221 223 223 PHE PHE B . n 
B 1 222 THR 222 224 224 THR THR B . n 
B 1 223 THR 223 225 225 THR THR B . n 
B 1 224 THR 224 226 226 THR THR B . n 
B 1 225 LEU 225 227 227 LEU LEU B . n 
B 1 226 ASN 226 228 228 ASN ASN B . n 
B 1 227 ASP 227 229 229 ASP ASP B . n 
B 1 228 PHE 228 230 230 PHE PHE B . n 
B 1 229 ASN 229 231 231 ASN ASN B . n 
B 1 230 LEU 230 232 232 LEU LEU B . n 
B 1 231 VAL 231 233 233 VAL VAL B . n 
B 1 232 ALA 232 234 234 ALA ALA B . n 
B 1 233 MET 233 235 235 MET MET B . n 
B 1 234 LYS 234 236 236 LYS LYS B . n 
B 1 235 TYR 235 237 237 TYR TYR B . n 
B 1 236 ASN 236 238 238 ASN ASN B . n 
B 1 237 TYR 237 239 239 TYR TYR B . n 
B 1 238 GLU 238 240 240 GLU GLU B . n 
B 1 239 PRO 239 241 241 PRO PRO B . n 
B 1 240 LEU 240 242 242 LEU LEU B . n 
B 1 241 THR 241 243 243 THR THR B . n 
B 1 242 GLN 242 244 244 GLN GLN B . n 
B 1 243 ASP 243 245 245 ASP ASP B . n 
B 1 244 HIS 244 246 246 HIS HIS B . n 
B 1 245 VAL 245 247 247 VAL VAL B . n 
B 1 246 ASP 246 248 248 ASP ASP B . n 
B 1 247 ILE 247 249 249 ILE ILE B . n 
B 1 248 LEU 248 250 250 LEU LEU B . n 
B 1 249 GLY 249 251 251 GLY GLY B . n 
B 1 250 PRO 250 252 252 PRO PRO B . n 
B 1 251 LEU 251 253 253 LEU LEU B . n 
B 1 252 SER 252 254 254 SER SER B . n 
B 1 253 ALA 253 255 255 ALA ALA B . n 
B 1 254 GLN 254 256 256 GLN GLN B . n 
B 1 255 THR 255 257 257 THR THR B . n 
B 1 256 GLY 256 258 258 GLY GLY B . n 
B 1 257 ILE 257 259 259 ILE ILE B . n 
B 1 258 ALA 258 260 260 ALA ALA B . n 
B 1 259 VAL 259 261 261 VAL VAL B . n 
B 1 260 LEU 260 262 262 LEU LEU B . n 
B 1 261 ASP 261 263 263 ASP ASP B . n 
B 1 262 MET 262 264 264 MET MET B . n 
B 1 263 CYS 263 265 265 CYS CYS B . n 
B 1 264 ALA 264 266 266 ALA ALA B . n 
B 1 265 SER 265 267 267 SER SER B . n 
B 1 266 LEU 266 268 268 LEU LEU B . n 
B 1 267 LYS 267 269 269 LYS LYS B . n 
B 1 268 GLU 268 270 270 GLU GLU B . n 
B 1 269 LEU 269 271 271 LEU LEU B . n 
B 1 270 LEU 270 272 272 LEU LEU B . n 
B 1 271 GLN 271 273 273 GLN GLN B . n 
B 1 272 ASN 272 274 274 ASN ASN B . n 
B 1 273 GLY 273 275 275 GLY GLY B . n 
B 1 274 MET 274 276 276 MET MET B . n 
B 1 275 ASN 275 277 277 ASN ASN B . n 
B 1 276 GLY 276 278 278 GLY GLY B . n 
B 1 277 ARG 277 279 279 ARG ARG B . n 
B 1 278 THR 278 280 280 THR THR B . n 
B 1 279 ILE 279 281 281 ILE ILE B . n 
B 1 280 LEU 280 282 282 LEU LEU B . n 
B 1 281 GLY 281 283 283 GLY GLY B . n 
B 1 282 SER 282 284 284 SER SER B . n 
B 1 283 ALA 283 285 285 ALA ALA B . n 
B 1 284 LEU 284 286 286 LEU LEU B . n 
B 1 285 LEU 285 287 287 LEU LEU B . n 
B 1 286 GLU 286 288 288 GLU GLU B . n 
B 1 287 ASP 287 289 289 ASP ASP B . n 
B 1 288 GLU 288 290 290 GLU GLU B . n 
B 1 289 PHE 289 291 291 PHE PHE B . n 
B 1 290 THR 290 292 292 THR THR B . n 
B 1 291 PRO 291 293 293 PRO PRO B . n 
B 1 292 PHE 292 294 294 PHE PHE B . n 
B 1 293 ASP 293 295 295 ASP ASP B . n 
B 1 294 VAL 294 296 296 VAL VAL B . n 
B 1 295 VAL 295 297 297 VAL VAL B . n 
B 1 296 ARG 296 298 298 ARG ARG B . n 
B 1 297 GLN 297 299 299 GLN GLN B . n 
B 1 298 CYS 298 300 300 CYS CYS B . n 
B 1 299 SER 299 301 ?   ?   ?   B . n 
B 1 300 GLY 300 302 ?   ?   ?   B . n 
B 1 301 VAL 301 303 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        FHR 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   FHR 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 
C 2 FHR 1   401 401 FHR LIG A . 
D 2 FHR 1   401 401 FHR LIG B . 
E 3 HOH 1   501 169 HOH HOH A . 
E 3 HOH 2   502 100 HOH HOH A . 
E 3 HOH 3   503 388 HOH HOH A . 
E 3 HOH 4   504 55  HOH HOH A . 
E 3 HOH 5   505 130 HOH HOH A . 
E 3 HOH 6   506 165 HOH HOH A . 
E 3 HOH 7   507 253 HOH HOH A . 
E 3 HOH 8   508 89  HOH HOH A . 
E 3 HOH 9   509 167 HOH HOH A . 
E 3 HOH 10  510 68  HOH HOH A . 
E 3 HOH 11  511 64  HOH HOH A . 
E 3 HOH 12  512 191 HOH HOH A . 
E 3 HOH 13  513 285 HOH HOH A . 
E 3 HOH 14  514 196 HOH HOH A . 
E 3 HOH 15  515 97  HOH HOH A . 
E 3 HOH 16  516 54  HOH HOH A . 
E 3 HOH 17  517 163 HOH HOH A . 
E 3 HOH 18  518 289 HOH HOH A . 
E 3 HOH 19  519 184 HOH HOH A . 
E 3 HOH 20  520 262 HOH HOH A . 
E 3 HOH 21  521 172 HOH HOH A . 
E 3 HOH 22  522 381 HOH HOH A . 
E 3 HOH 23  523 317 HOH HOH A . 
E 3 HOH 24  524 213 HOH HOH A . 
E 3 HOH 25  525 197 HOH HOH A . 
E 3 HOH 26  526 304 HOH HOH A . 
E 3 HOH 27  527 60  HOH HOH A . 
E 3 HOH 28  528 50  HOH HOH A . 
E 3 HOH 29  529 387 HOH HOH A . 
E 3 HOH 30  530 208 HOH HOH A . 
E 3 HOH 31  531 140 HOH HOH A . 
E 3 HOH 32  532 61  HOH HOH A . 
E 3 HOH 33  533 180 HOH HOH A . 
E 3 HOH 34  534 179 HOH HOH A . 
E 3 HOH 35  535 153 HOH HOH A . 
E 3 HOH 36  536 19  HOH HOH A . 
E 3 HOH 37  537 30  HOH HOH A . 
E 3 HOH 38  538 236 HOH HOH A . 
E 3 HOH 39  539 70  HOH HOH A . 
E 3 HOH 40  540 203 HOH HOH A . 
E 3 HOH 41  541 33  HOH HOH A . 
E 3 HOH 42  542 11  HOH HOH A . 
E 3 HOH 43  543 404 HOH HOH A . 
E 3 HOH 44  544 224 HOH HOH A . 
E 3 HOH 45  545 94  HOH HOH A . 
E 3 HOH 46  546 209 HOH HOH A . 
E 3 HOH 47  547 77  HOH HOH A . 
E 3 HOH 48  548 202 HOH HOH A . 
E 3 HOH 49  549 45  HOH HOH A . 
E 3 HOH 50  550 157 HOH HOH A . 
E 3 HOH 51  551 272 HOH HOH A . 
E 3 HOH 52  552 178 HOH HOH A . 
E 3 HOH 53  553 92  HOH HOH A . 
E 3 HOH 54  554 155 HOH HOH A . 
E 3 HOH 55  555 436 HOH HOH A . 
E 3 HOH 56  556 110 HOH HOH A . 
E 3 HOH 57  557 143 HOH HOH A . 
E 3 HOH 58  558 5   HOH HOH A . 
E 3 HOH 59  559 36  HOH HOH A . 
E 3 HOH 60  560 17  HOH HOH A . 
E 3 HOH 61  561 252 HOH HOH A . 
E 3 HOH 62  562 313 HOH HOH A . 
E 3 HOH 63  563 144 HOH HOH A . 
E 3 HOH 64  564 183 HOH HOH A . 
E 3 HOH 65  565 119 HOH HOH A . 
E 3 HOH 66  566 247 HOH HOH A . 
E 3 HOH 67  567 57  HOH HOH A . 
E 3 HOH 68  568 116 HOH HOH A . 
E 3 HOH 69  569 10  HOH HOH A . 
E 3 HOH 70  570 71  HOH HOH A . 
E 3 HOH 71  571 8   HOH HOH A . 
E 3 HOH 72  572 12  HOH HOH A . 
E 3 HOH 73  573 21  HOH HOH A . 
E 3 HOH 74  574 48  HOH HOH A . 
E 3 HOH 75  575 56  HOH HOH A . 
E 3 HOH 76  576 245 HOH HOH A . 
E 3 HOH 77  577 269 HOH HOH A . 
E 3 HOH 78  578 95  HOH HOH A . 
E 3 HOH 79  579 307 HOH HOH A . 
E 3 HOH 80  580 4   HOH HOH A . 
E 3 HOH 81  581 134 HOH HOH A . 
E 3 HOH 82  582 74  HOH HOH A . 
E 3 HOH 83  583 67  HOH HOH A . 
E 3 HOH 84  584 424 HOH HOH A . 
E 3 HOH 85  585 51  HOH HOH A . 
E 3 HOH 86  586 218 HOH HOH A . 
E 3 HOH 87  587 81  HOH HOH A . 
E 3 HOH 88  588 323 HOH HOH A . 
E 3 HOH 89  589 258 HOH HOH A . 
E 3 HOH 90  590 1   HOH HOH A . 
E 3 HOH 91  591 207 HOH HOH A . 
E 3 HOH 92  592 322 HOH HOH A . 
E 3 HOH 93  593 384 HOH HOH A . 
E 3 HOH 94  594 378 HOH HOH A . 
E 3 HOH 95  595 268 HOH HOH A . 
E 3 HOH 96  596 78  HOH HOH A . 
E 3 HOH 97  597 39  HOH HOH A . 
E 3 HOH 98  598 386 HOH HOH A . 
E 3 HOH 99  599 63  HOH HOH A . 
E 3 HOH 100 600 20  HOH HOH A . 
E 3 HOH 101 601 7   HOH HOH A . 
E 3 HOH 102 602 31  HOH HOH A . 
E 3 HOH 103 603 325 HOH HOH A . 
E 3 HOH 104 604 16  HOH HOH A . 
E 3 HOH 105 605 141 HOH HOH A . 
E 3 HOH 106 606 124 HOH HOH A . 
E 3 HOH 107 607 93  HOH HOH A . 
E 3 HOH 108 608 358 HOH HOH A . 
E 3 HOH 109 609 34  HOH HOH A . 
E 3 HOH 110 610 65  HOH HOH A . 
E 3 HOH 111 611 292 HOH HOH A . 
E 3 HOH 112 612 354 HOH HOH A . 
E 3 HOH 113 613 231 HOH HOH A . 
E 3 HOH 114 614 139 HOH HOH A . 
E 3 HOH 115 615 26  HOH HOH A . 
E 3 HOH 116 616 168 HOH HOH A . 
E 3 HOH 117 617 152 HOH HOH A . 
E 3 HOH 118 618 160 HOH HOH A . 
E 3 HOH 119 619 106 HOH HOH A . 
E 3 HOH 120 620 104 HOH HOH A . 
E 3 HOH 121 621 138 HOH HOH A . 
E 3 HOH 122 622 148 HOH HOH A . 
E 3 HOH 123 623 329 HOH HOH A . 
E 3 HOH 124 624 103 HOH HOH A . 
E 3 HOH 125 625 173 HOH HOH A . 
E 3 HOH 126 626 212 HOH HOH A . 
E 3 HOH 127 627 324 HOH HOH A . 
E 3 HOH 128 628 145 HOH HOH A . 
E 3 HOH 129 629 347 HOH HOH A . 
E 3 HOH 130 630 359 HOH HOH A . 
E 3 HOH 131 631 43  HOH HOH A . 
E 3 HOH 132 632 125 HOH HOH A . 
E 3 HOH 133 633 352 HOH HOH A . 
E 3 HOH 134 634 310 HOH HOH A . 
E 3 HOH 135 635 276 HOH HOH A . 
E 3 HOH 136 636 112 HOH HOH A . 
E 3 HOH 137 637 136 HOH HOH A . 
E 3 HOH 138 638 29  HOH HOH A . 
E 3 HOH 139 639 227 HOH HOH A . 
E 3 HOH 140 640 73  HOH HOH A . 
E 3 HOH 141 641 86  HOH HOH A . 
E 3 HOH 142 642 46  HOH HOH A . 
E 3 HOH 143 643 52  HOH HOH A . 
E 3 HOH 144 644 87  HOH HOH A . 
E 3 HOH 145 645 259 HOH HOH A . 
E 3 HOH 146 646 102 HOH HOH A . 
E 3 HOH 147 647 228 HOH HOH A . 
E 3 HOH 148 648 109 HOH HOH A . 
E 3 HOH 149 649 433 HOH HOH A . 
E 3 HOH 150 650 357 HOH HOH A . 
E 3 HOH 151 651 192 HOH HOH A . 
E 3 HOH 152 652 255 HOH HOH A . 
E 3 HOH 153 653 306 HOH HOH A . 
E 3 HOH 154 654 410 HOH HOH A . 
E 3 HOH 155 655 240 HOH HOH A . 
E 3 HOH 156 656 319 HOH HOH A . 
E 3 HOH 157 657 190 HOH HOH A . 
E 3 HOH 158 658 342 HOH HOH A . 
E 3 HOH 159 659 356 HOH HOH A . 
E 3 HOH 160 660 256 HOH HOH A . 
E 3 HOH 161 661 382 HOH HOH A . 
E 3 HOH 162 662 405 HOH HOH A . 
E 3 HOH 163 663 422 HOH HOH A . 
E 3 HOH 164 664 318 HOH HOH A . 
E 3 HOH 165 665 370 HOH HOH A . 
E 3 HOH 166 666 426 HOH HOH A . 
E 3 HOH 167 667 146 HOH HOH A . 
E 3 HOH 168 668 312 HOH HOH A . 
E 3 HOH 169 669 250 HOH HOH A . 
E 3 HOH 170 670 241 HOH HOH A . 
E 3 HOH 171 671 335 HOH HOH A . 
E 3 HOH 172 672 346 HOH HOH A . 
E 3 HOH 173 673 366 HOH HOH A . 
E 3 HOH 174 674 371 HOH HOH A . 
E 3 HOH 175 675 394 HOH HOH A . 
E 3 HOH 176 676 330 HOH HOH A . 
E 3 HOH 177 677 80  HOH HOH A . 
E 3 HOH 178 678 214 HOH HOH A . 
E 3 HOH 179 679 127 HOH HOH A . 
E 3 HOH 180 680 336 HOH HOH A . 
E 3 HOH 181 681 201 HOH HOH A . 
E 3 HOH 182 682 69  HOH HOH A . 
E 3 HOH 183 683 400 HOH HOH A . 
E 3 HOH 184 684 235 HOH HOH A . 
E 3 HOH 185 685 219 HOH HOH A . 
E 3 HOH 186 686 438 HOH HOH A . 
E 3 HOH 187 687 161 HOH HOH A . 
E 3 HOH 188 688 423 HOH HOH A . 
E 3 HOH 189 689 217 HOH HOH A . 
E 3 HOH 190 690 174 HOH HOH A . 
E 3 HOH 191 691 344 HOH HOH A . 
E 3 HOH 192 692 379 HOH HOH A . 
E 3 HOH 193 693 211 HOH HOH A . 
E 3 HOH 194 694 251 HOH HOH A . 
E 3 HOH 195 695 299 HOH HOH A . 
E 3 HOH 196 696 298 HOH HOH A . 
E 3 HOH 197 697 232 HOH HOH A . 
F 3 HOH 1   501 114 HOH HOH B . 
F 3 HOH 2   502 221 HOH HOH B . 
F 3 HOH 3   503 41  HOH HOH B . 
F 3 HOH 4   504 129 HOH HOH B . 
F 3 HOH 5   505 414 HOH HOH B . 
F 3 HOH 6   506 96  HOH HOH B . 
F 3 HOH 7   507 123 HOH HOH B . 
F 3 HOH 8   508 249 HOH HOH B . 
F 3 HOH 9   509 429 HOH HOH B . 
F 3 HOH 10  510 37  HOH HOH B . 
F 3 HOH 11  511 40  HOH HOH B . 
F 3 HOH 12  512 128 HOH HOH B . 
F 3 HOH 13  513 105 HOH HOH B . 
F 3 HOH 14  514 215 HOH HOH B . 
F 3 HOH 15  515 372 HOH HOH B . 
F 3 HOH 16  516 47  HOH HOH B . 
F 3 HOH 17  517 308 HOH HOH B . 
F 3 HOH 18  518 18  HOH HOH B . 
F 3 HOH 19  519 32  HOH HOH B . 
F 3 HOH 20  520 229 HOH HOH B . 
F 3 HOH 21  521 195 HOH HOH B . 
F 3 HOH 22  522 44  HOH HOH B . 
F 3 HOH 23  523 177 HOH HOH B . 
F 3 HOH 24  524 270 HOH HOH B . 
F 3 HOH 25  525 25  HOH HOH B . 
F 3 HOH 26  526 120 HOH HOH B . 
F 3 HOH 27  527 117 HOH HOH B . 
F 3 HOH 28  528 361 HOH HOH B . 
F 3 HOH 29  529 274 HOH HOH B . 
F 3 HOH 30  530 3   HOH HOH B . 
F 3 HOH 31  531 246 HOH HOH B . 
F 3 HOH 32  532 278 HOH HOH B . 
F 3 HOH 33  533 133 HOH HOH B . 
F 3 HOH 34  534 101 HOH HOH B . 
F 3 HOH 35  535 6   HOH HOH B . 
F 3 HOH 36  536 282 HOH HOH B . 
F 3 HOH 37  537 243 HOH HOH B . 
F 3 HOH 38  538 75  HOH HOH B . 
F 3 HOH 39  539 27  HOH HOH B . 
F 3 HOH 40  540 398 HOH HOH B . 
F 3 HOH 41  541 355 HOH HOH B . 
F 3 HOH 42  542 166 HOH HOH B . 
F 3 HOH 43  543 24  HOH HOH B . 
F 3 HOH 44  544 164 HOH HOH B . 
F 3 HOH 45  545 13  HOH HOH B . 
F 3 HOH 46  546 186 HOH HOH B . 
F 3 HOH 47  547 15  HOH HOH B . 
F 3 HOH 48  548 98  HOH HOH B . 
F 3 HOH 49  549 244 HOH HOH B . 
F 3 HOH 50  550 35  HOH HOH B . 
F 3 HOH 51  551 239 HOH HOH B . 
F 3 HOH 52  552 315 HOH HOH B . 
F 3 HOH 53  553 175 HOH HOH B . 
F 3 HOH 54  554 90  HOH HOH B . 
F 3 HOH 55  555 158 HOH HOH B . 
F 3 HOH 56  556 200 HOH HOH B . 
F 3 HOH 57  557 305 HOH HOH B . 
F 3 HOH 58  558 79  HOH HOH B . 
F 3 HOH 59  559 280 HOH HOH B . 
F 3 HOH 60  560 14  HOH HOH B . 
F 3 HOH 61  561 293 HOH HOH B . 
F 3 HOH 62  562 151 HOH HOH B . 
F 3 HOH 63  563 383 HOH HOH B . 
F 3 HOH 64  564 373 HOH HOH B . 
F 3 HOH 65  565 242 HOH HOH B . 
F 3 HOH 66  566 131 HOH HOH B . 
F 3 HOH 67  567 257 HOH HOH B . 
F 3 HOH 68  568 193 HOH HOH B . 
F 3 HOH 69  569 150 HOH HOH B . 
F 3 HOH 70  570 23  HOH HOH B . 
F 3 HOH 71  571 149 HOH HOH B . 
F 3 HOH 72  572 42  HOH HOH B . 
F 3 HOH 73  573 62  HOH HOH B . 
F 3 HOH 74  574 321 HOH HOH B . 
F 3 HOH 75  575 85  HOH HOH B . 
F 3 HOH 76  576 368 HOH HOH B . 
F 3 HOH 77  577 403 HOH HOH B . 
F 3 HOH 78  578 220 HOH HOH B . 
F 3 HOH 79  579 159 HOH HOH B . 
F 3 HOH 80  580 2   HOH HOH B . 
F 3 HOH 81  581 76  HOH HOH B . 
F 3 HOH 82  582 147 HOH HOH B . 
F 3 HOH 83  583 297 HOH HOH B . 
F 3 HOH 84  584 254 HOH HOH B . 
F 3 HOH 85  585 49  HOH HOH B . 
F 3 HOH 86  586 222 HOH HOH B . 
F 3 HOH 87  587 38  HOH HOH B . 
F 3 HOH 88  588 226 HOH HOH B . 
F 3 HOH 89  589 303 HOH HOH B . 
F 3 HOH 90  590 267 HOH HOH B . 
F 3 HOH 91  591 194 HOH HOH B . 
F 3 HOH 92  592 72  HOH HOH B . 
F 3 HOH 93  593 9   HOH HOH B . 
F 3 HOH 94  594 111 HOH HOH B . 
F 3 HOH 95  595 205 HOH HOH B . 
F 3 HOH 96  596 22  HOH HOH B . 
F 3 HOH 97  597 58  HOH HOH B . 
F 3 HOH 98  598 121 HOH HOH B . 
F 3 HOH 99  599 234 HOH HOH B . 
F 3 HOH 100 600 118 HOH HOH B . 
F 3 HOH 101 601 84  HOH HOH B . 
F 3 HOH 102 602 135 HOH HOH B . 
F 3 HOH 103 603 115 HOH HOH B . 
F 3 HOH 104 604 170 HOH HOH B . 
F 3 HOH 105 605 333 HOH HOH B . 
F 3 HOH 106 606 59  HOH HOH B . 
F 3 HOH 107 607 126 HOH HOH B . 
F 3 HOH 108 608 353 HOH HOH B . 
F 3 HOH 109 609 185 HOH HOH B . 
F 3 HOH 110 610 122 HOH HOH B . 
F 3 HOH 111 611 417 HOH HOH B . 
F 3 HOH 112 612 314 HOH HOH B . 
F 3 HOH 113 613 187 HOH HOH B . 
F 3 HOH 114 614 328 HOH HOH B . 
F 3 HOH 115 615 113 HOH HOH B . 
F 3 HOH 116 616 286 HOH HOH B . 
F 3 HOH 117 617 230 HOH HOH B . 
F 3 HOH 118 618 91  HOH HOH B . 
F 3 HOH 119 619 28  HOH HOH B . 
F 3 HOH 120 620 107 HOH HOH B . 
F 3 HOH 121 621 360 HOH HOH B . 
F 3 HOH 122 622 401 HOH HOH B . 
F 3 HOH 123 623 281 HOH HOH B . 
F 3 HOH 124 624 408 HOH HOH B . 
F 3 HOH 125 625 275 HOH HOH B . 
F 3 HOH 126 626 290 HOH HOH B . 
F 3 HOH 127 627 437 HOH HOH B . 
F 3 HOH 128 628 421 HOH HOH B . 
F 3 HOH 129 629 316 HOH HOH B . 
F 3 HOH 130 630 261 HOH HOH B . 
F 3 HOH 131 631 291 HOH HOH B . 
F 3 HOH 132 632 341 HOH HOH B . 
F 3 HOH 133 633 176 HOH HOH B . 
F 3 HOH 134 634 332 HOH HOH B . 
F 3 HOH 135 635 300 HOH HOH B . 
F 3 HOH 136 636 154 HOH HOH B . 
F 3 HOH 137 637 199 HOH HOH B . 
F 3 HOH 138 638 365 HOH HOH B . 
F 3 HOH 139 639 99  HOH HOH B . 
F 3 HOH 140 640 389 HOH HOH B . 
F 3 HOH 141 641 411 HOH HOH B . 
F 3 HOH 142 642 320 HOH HOH B . 
F 3 HOH 143 643 142 HOH HOH B . 
F 3 HOH 144 644 350 HOH HOH B . 
F 3 HOH 145 645 83  HOH HOH B . 
F 3 HOH 146 646 375 HOH HOH B . 
F 3 HOH 147 647 420 HOH HOH B . 
F 3 HOH 148 648 340 HOH HOH B . 
F 3 HOH 149 649 260 HOH HOH B . 
F 3 HOH 150 650 266 HOH HOH B . 
F 3 HOH 151 651 206 HOH HOH B . 
F 3 HOH 152 652 88  HOH HOH B . 
F 3 HOH 153 653 413 HOH HOH B . 
F 3 HOH 154 654 248 HOH HOH B . 
F 3 HOH 155 655 392 HOH HOH B . 
F 3 HOH 156 656 415 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ARG 76  ? CG  ? A ARG 74  CG  
2  1 Y 1 A ARG 76  ? CD  ? A ARG 74  CD  
3  1 Y 1 A ARG 76  ? NE  ? A ARG 74  NE  
4  1 Y 1 A ARG 76  ? CZ  ? A ARG 74  CZ  
5  1 Y 1 A ARG 76  ? NH1 ? A ARG 74  NH1 
6  1 Y 1 A ARG 76  ? NH2 ? A ARG 74  NH2 
7  1 Y 1 A LYS 100 ? CG  ? A LYS 98  CG  
8  1 Y 1 A LYS 100 ? CD  ? A LYS 98  CD  
9  1 Y 1 A LYS 100 ? CE  ? A LYS 98  CE  
10 1 Y 1 A LYS 100 ? NZ  ? A LYS 98  NZ  
11 1 Y 1 A TYR 154 ? CG  ? A TYR 152 CG  
12 1 Y 1 A TYR 154 ? CD1 ? A TYR 152 CD1 
13 1 Y 1 A TYR 154 ? CD2 ? A TYR 152 CD2 
14 1 Y 1 A TYR 154 ? CE1 ? A TYR 152 CE1 
15 1 Y 1 A TYR 154 ? CE2 ? A TYR 152 CE2 
16 1 Y 1 A TYR 154 ? CZ  ? A TYR 152 CZ  
17 1 Y 1 A TYR 154 ? OH  ? A TYR 152 OH  
18 1 Y 1 A ARG 222 ? CG  ? A ARG 220 CG  
19 1 Y 1 A ARG 222 ? CD  ? A ARG 220 CD  
20 1 Y 1 A ARG 222 ? NE  ? A ARG 220 NE  
21 1 Y 1 A ARG 222 ? CZ  ? A ARG 220 CZ  
22 1 Y 1 A ARG 222 ? NH1 ? A ARG 220 NH1 
23 1 Y 1 A ARG 222 ? NH2 ? A ARG 220 NH2 
24 1 Y 1 A PHE 223 ? CG  ? A PHE 221 CG  
25 1 Y 1 A PHE 223 ? CD1 ? A PHE 221 CD1 
26 1 Y 1 A PHE 223 ? CD2 ? A PHE 221 CD2 
27 1 Y 1 A PHE 223 ? CE1 ? A PHE 221 CE1 
28 1 Y 1 A PHE 223 ? CE2 ? A PHE 221 CE2 
29 1 Y 1 A PHE 223 ? CZ  ? A PHE 221 CZ  
30 1 Y 1 A LEU 286 ? CG  ? A LEU 284 CG  
31 1 Y 1 A LEU 286 ? CD1 ? A LEU 284 CD1 
32 1 Y 1 A LEU 286 ? CD2 ? A LEU 284 CD2 
33 1 Y 1 B GLU 47  ? CG  ? B GLU 45  CG  
34 1 Y 1 B GLU 47  ? CD  ? B GLU 45  CD  
35 1 Y 1 B GLU 47  ? OE1 ? B GLU 45  OE1 
36 1 Y 1 B GLU 47  ? OE2 ? B GLU 45  OE2 
37 1 Y 1 B ASN 72  ? CG  ? B ASN 70  CG  
38 1 Y 1 B ASN 72  ? OD1 ? B ASN 70  OD1 
39 1 Y 1 B ASN 72  ? ND2 ? B ASN 70  ND2 
40 1 Y 1 B ARG 76  ? CG  ? B ARG 74  CG  
41 1 Y 1 B ARG 76  ? CD  ? B ARG 74  CD  
42 1 Y 1 B ARG 76  ? NE  ? B ARG 74  NE  
43 1 Y 1 B ARG 76  ? CZ  ? B ARG 74  CZ  
44 1 Y 1 B ARG 76  ? NH1 ? B ARG 74  NH1 
45 1 Y 1 B ARG 76  ? NH2 ? B ARG 74  NH2 
46 1 Y 1 B LYS 100 ? CG  ? B LYS 98  CG  
47 1 Y 1 B LYS 100 ? CD  ? B LYS 98  CD  
48 1 Y 1 B LYS 100 ? CE  ? B LYS 98  CE  
49 1 Y 1 B LYS 100 ? NZ  ? B LYS 98  NZ  
50 1 Y 1 B LYS 102 ? CG  ? B LYS 100 CG  
51 1 Y 1 B LYS 102 ? CD  ? B LYS 100 CD  
52 1 Y 1 B LYS 102 ? CE  ? B LYS 100 CE  
53 1 Y 1 B LYS 102 ? NZ  ? B LYS 100 NZ  
54 1 Y 1 B LYS 137 ? CG  ? B LYS 135 CG  
55 1 Y 1 B LYS 137 ? CD  ? B LYS 135 CD  
56 1 Y 1 B LYS 137 ? CE  ? B LYS 135 CE  
57 1 Y 1 B LYS 137 ? NZ  ? B LYS 135 NZ  
58 1 Y 1 B TYR 154 ? CG  ? B TYR 152 CG  
59 1 Y 1 B TYR 154 ? CD1 ? B TYR 152 CD1 
60 1 Y 1 B TYR 154 ? CD2 ? B TYR 152 CD2 
61 1 Y 1 B TYR 154 ? CE1 ? B TYR 152 CE1 
62 1 Y 1 B TYR 154 ? CE2 ? B TYR 152 CE2 
63 1 Y 1 B TYR 154 ? CZ  ? B TYR 152 CZ  
64 1 Y 1 B TYR 154 ? OH  ? B TYR 152 OH  
65 1 Y 1 B PHE 223 ? CG  ? B PHE 221 CG  
66 1 Y 1 B PHE 223 ? CD1 ? B PHE 221 CD1 
67 1 Y 1 B PHE 223 ? CD2 ? B PHE 221 CD2 
68 1 Y 1 B PHE 223 ? CE1 ? B PHE 221 CE1 
69 1 Y 1 B PHE 223 ? CE2 ? B PHE 221 CE2 
70 1 Y 1 B PHE 223 ? CZ  ? B PHE 221 CZ  
71 1 Y 1 B ASP 245 ? CG  ? B ASP 243 CG  
72 1 Y 1 B ASP 245 ? OD1 ? B ASP 243 OD1 
73 1 Y 1 B ASP 245 ? OD2 ? B ASP 243 OD2 
74 1 Y 1 B ARG 279 ? CG  ? B ARG 277 CG  
75 1 Y 1 B ARG 279 ? CD  ? B ARG 277 CD  
76 1 Y 1 B ARG 279 ? NE  ? B ARG 277 NE  
77 1 Y 1 B ARG 279 ? CZ  ? B ARG 277 CZ  
78 1 Y 1 B ARG 279 ? NH1 ? B ARG 277 NH1 
79 1 Y 1 B ARG 279 ? NH2 ? B ARG 277 NH2 
80 1 Y 1 B LEU 286 ? CG  ? B LEU 284 CG  
81 1 Y 1 B LEU 286 ? CD1 ? B LEU 284 CD1 
82 1 Y 1 B LEU 286 ? CD2 ? B LEU 284 CD2 
83 1 Y 1 B ARG 298 ? CG  ? B ARG 296 CG  
84 1 Y 1 B ARG 298 ? CD  ? B ARG 296 CD  
85 1 Y 1 B ARG 298 ? NE  ? B ARG 296 NE  
86 1 Y 1 B ARG 298 ? CZ  ? B ARG 296 CZ  
87 1 Y 1 B ARG 298 ? NH1 ? B ARG 296 NH1 
88 1 Y 1 B ARG 298 ? NH2 ? B ARG 296 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.12_2829 1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.12_2829 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .         3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .         4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .         5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   108.353 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Y4H 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     55.508 
_cell.length_a_esd                 ? 
_cell.length_b                     98.691 
_cell.length_b_esd                 ? 
_cell.length_c                     58.955 
_cell.length_c_esd                 ? 
_cell.volume                       306538.212 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8Y4H 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_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                   8Y4H 
_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             2.30 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.53 
_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.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.12~0.21M PEG3350,20%~24%Na2SO4' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_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.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-01-13 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979191 
_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                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979191 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          17.5354707811 
_reflns.entry_id                                       8Y4H 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.93 
_reflns.d_resolution_low                               98.69 
_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                                     44976 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.064 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.93 
_reflns_shell.d_res_low                                     1.98 
_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                             3061 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_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_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                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.133 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               22.4740062794 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_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                                 8Y4H 
_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                            1.93 
_refine.ls_d_res_low                             46.32 
_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                     44902 
_refine.ls_number_reflns_R_free                  2318 
_refine.ls_number_reflns_R_work                  42584 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.1411097127 
_refine.ls_percent_reflns_R_free                 5.16235357 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.180289204374 
_refine.ls_R_factor_R_free                       0.217819340493 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.178257625344 
_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                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_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                          1.38107601152 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9 
_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                 21.4341342688 
_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                            0.205345568408 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_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.details                          ? 
_refine_hist.d_res_high                       1.93 
_refine_hist.d_res_low                        46.32 
_refine_hist.number_atoms_solvent             353 
_refine_hist.number_atoms_total               4967 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4614 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
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' ? 0.0067726272072  ? 4717 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.866297943268   ? 6423 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0519303321303  ? 734  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.00642805285825 ? 833  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 9.20450899153    ? 2746 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_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_error 
_refine_ls_shell.R_factor_R_work 
_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_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.93   1.9694 . . 135 2267 90.4027098231 . . . . 0.199848846298 . . . . . . . . . . . 0.252813901644 
'X-RAY DIFFRACTION' 1.9694 2.0123 . . 140 2404 97.0251716247 . . . . 0.198343854528 . . . . . . . . . . . 0.279447958461 
'X-RAY DIFFRACTION' 2.0123 2.0591 . . 166 2533 100.0         . . . . 0.205780248589 . . . . . . . . . . . 0.239825353183 
'X-RAY DIFFRACTION' 2.0591 2.1106 . . 160 2469 100.0         . . . . 0.190444645518 . . . . . . . . . . . 0.269713096827 
'X-RAY DIFFRACTION' 2.1106 2.1676 . . 157 2514 100.0         . . . . 0.183310024422 . . . . . . . . . . . 0.230394401635 
'X-RAY DIFFRACTION' 2.1676 2.2314 . . 121 2509 100.0         . . . . 0.190227603181 . . . . . . . . . . . 0.2621917998   
'X-RAY DIFFRACTION' 2.2314 2.3034 . . 129 2543 99.9625888515 . . . . 0.183127986802 . . . . . . . . . . . 0.222065553036 
'X-RAY DIFFRACTION' 2.3034 2.3858 . . 130 2517 100.0         . . . . 0.184140992836 . . . . . . . . . . . 0.230281796096 
'X-RAY DIFFRACTION' 2.3858 2.4813 . . 112 2540 100.0         . . . . 0.193564534011 . . . . . . . . . . . 0.243424400264 
'X-RAY DIFFRACTION' 2.4813 2.5942 . . 115 2551 100.0         . . . . 0.186673650912 . . . . . . . . . . . 0.199219324531 
'X-RAY DIFFRACTION' 2.5942 2.731  . . 145 2510 100.0         . . . . 0.193762931634 . . . . . . . . . . . 0.250360204896 
'X-RAY DIFFRACTION' 2.731  2.902  . . 115 2565 100.0         . . . . 0.19808679465  . . . . . . . . . . . 0.201789160325 
'X-RAY DIFFRACTION' 2.902  3.1261 . . 137 2510 100.0         . . . . 0.192785119703 . . . . . . . . . . . 0.211245168918 
'X-RAY DIFFRACTION' 3.1261 3.4406 . . 147 2536 99.9627421759 . . . . 0.187755687332 . . . . . . . . . . . 0.238318282276 
'X-RAY DIFFRACTION' 3.4406 3.9382 . . 150 2531 99.9627143922 . . . . 0.165133643793 . . . . . . . . . . . 0.209160296296 
'X-RAY DIFFRACTION' 3.9382 4.9608 . . 137 2533 99.8877665544 . . . . 0.138544437963 . . . . . . . . . . . 0.181695535817 
'X-RAY DIFFRACTION' 4.9608 46.32  . . 122 2552 98.2365907421 . . . . 0.159398177581 . . . . . . . . . . . 0.166434676299 
# 
_struct.entry_id                     8Y4H 
_struct.title                        'Crystal structure of SARS-Cov-2 main protease K90R mutant in complex with Bofutrelvir' 
_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        8Y4H 
_struct_keywords.text            'VIRAL PROTEIN-INHIBITOR COMPLEX, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
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 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;FRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSM
QNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYM
HHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPL
TQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGV
;
_struct_ref.pdbx_align_begin           0 
# 
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 8Y4H A 1 ? 301 ? P0DTD1 3266 ? 3566 ? 3 303 
2 1 8Y4H B 1 ? 301 ? P0DTD1 3266 ? 3566 ? 3 303 
# 
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 8Y4H ARG A 88 ? UNP P0DTD1 LYS 3353 'engineered mutation' 90 1 
2 8Y4H ARG B 88 ? UNP P0DTD1 LYS 3353 'engineered mutation' 90 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1910  ? 
1 MORE         -9    ? 
1 'SSA (A^2)'  24920 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 8   ? GLY A 13  ? SER A 10  GLY A 15  1 ? 6  
HELX_P HELX_P2  AA2 HIS A 39  ? CYS A 42  ? HIS A 41  CYS A 44  5 ? 4  
HELX_P HELX_P3  AA3 ASN A 51  ? LYS A 59  ? ASN A 53  LYS A 61  1 ? 9  
HELX_P HELX_P4  AA4 SER A 60  ? PHE A 64  ? SER A 62  PHE A 66  5 ? 5  
HELX_P HELX_P5  AA5 ILE A 198 ? ASN A 212 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P6  AA6 THR A 224 ? TYR A 235 ? THR A 226 TYR A 237 1 ? 12 
HELX_P HELX_P7  AA7 THR A 241 ? LEU A 248 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P8  AA8 LEU A 248 ? GLY A 256 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P9  AA9 ALA A 258 ? GLY A 273 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P10 AB1 THR A 290 ? CYS A 298 ? THR A 292 CYS A 300 1 ? 9  
HELX_P HELX_P11 AB2 SER B 8   ? GLY B 13  ? SER B 10  GLY B 15  1 ? 6  
HELX_P HELX_P12 AB3 HIS B 39  ? CYS B 42  ? HIS B 41  CYS B 44  5 ? 4  
HELX_P HELX_P13 AB4 GLU B 45  ? ASN B 49  ? GLU B 47  ASN B 51  5 ? 5  
HELX_P HELX_P14 AB5 ASN B 51  ? ARG B 58  ? ASN B 53  ARG B 60  1 ? 8  
HELX_P HELX_P15 AB6 SER B 60  ? PHE B 64  ? SER B 62  PHE B 66  5 ? 5  
HELX_P HELX_P16 AB7 ILE B 198 ? ASN B 212 ? ILE B 200 ASN B 214 1 ? 15 
HELX_P HELX_P17 AB8 THR B 224 ? TYR B 235 ? THR B 226 TYR B 237 1 ? 12 
HELX_P HELX_P18 AB9 THR B 241 ? LEU B 248 ? THR B 243 LEU B 250 1 ? 8  
HELX_P HELX_P19 AC1 LEU B 248 ? GLY B 256 ? LEU B 250 GLY B 258 1 ? 9  
HELX_P HELX_P20 AC2 ALA B 258 ? GLY B 273 ? ALA B 260 GLY B 275 1 ? 16 
HELX_P HELX_P21 AC3 THR B 290 ? CYS B 298 ? THR B 292 CYS B 300 1 ? 9  
# 
_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 
covale1 covale none ? A CYS 143 SG ? ? ? 1_555 C FHR . C31 ? ? A CYS 145 A FHR 401 1_555 ? ? ? ? ? ? ? 1.770 ? ? 
covale2 covale none ? B CYS 143 SG ? ? ? 1_555 D FHR . C31 ? ? B CYS 145 B FHR 401 1_555 ? ? ? ? ? ? ? 1.770 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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 FHR C . ? CYS A 143 ? FHR A 401 ? 1_555 CYS A 145 ? 1_555 C31 SG CYS 1 FHR None 'Covalent chemical modification' 
2 FHR D . ? CYS B 143 ? FHR B 401 ? 1_555 CYS B 145 ? 1_555 C31 SG CYS 1 FHR None 'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
AA5 ? 5 ? 
AA6 ? 3 ? 
# 
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 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-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 VAL A 71  ? LEU A 73  ? VAL A 73  LEU A 75  
AA1 2 LEU A 65  ? ALA A 68  ? LEU A 67  ALA A 70  
AA1 3 MET A 15  ? CYS A 20  ? MET A 17  CYS A 22  
AA1 4 THR A 23  ? LEU A 30  ? THR A 25  LEU A 32  
AA1 5 VAL A 33  ? PRO A 37  ? VAL A 35  PRO A 39  
AA1 6 VAL A 84  ? VAL A 89  ? VAL A 86  VAL A 91  
AA1 7 VAL A 75  ? GLN A 81  ? VAL A 77  GLN A 83  
AA2 1 LYS A 98  ? PHE A 101 ? LYS A 100 PHE A 103 
AA2 2 CYS A 154 ? GLU A 164 ? CYS A 156 GLU A 166 
AA2 3 VAL A 146 ? ASP A 151 ? VAL A 148 ASP A 153 
AA2 4 THR A 109 ? TYR A 116 ? THR A 111 TYR A 118 
AA2 5 SER A 119 ? ALA A 127 ? SER A 121 ALA A 129 
AA3 1 LYS A 98  ? PHE A 101 ? LYS A 100 PHE A 103 
AA3 2 CYS A 154 ? GLU A 164 ? CYS A 156 GLU A 166 
AA3 3 HIS A 170 ? THR A 173 ? HIS A 172 THR A 175 
AA4 1 VAL B 71  ? LEU B 73  ? VAL B 73  LEU B 75  
AA4 2 LEU B 65  ? ALA B 68  ? LEU B 67  ALA B 70  
AA4 3 MET B 15  ? CYS B 20  ? MET B 17  CYS B 22  
AA4 4 THR B 23  ? LEU B 30  ? THR B 25  LEU B 32  
AA4 5 VAL B 33  ? PRO B 37  ? VAL B 35  PRO B 39  
AA4 6 VAL B 84  ? VAL B 89  ? VAL B 86  VAL B 91  
AA4 7 VAL B 75  ? GLN B 81  ? VAL B 77  GLN B 83  
AA5 1 LYS B 98  ? PHE B 101 ? LYS B 100 PHE B 103 
AA5 2 CYS B 154 ? GLU B 164 ? CYS B 156 GLU B 166 
AA5 3 VAL B 146 ? ASP B 151 ? VAL B 148 ASP B 153 
AA5 4 THR B 109 ? TYR B 116 ? THR B 111 TYR B 118 
AA5 5 SER B 119 ? ALA B 127 ? SER B 121 ALA B 129 
AA6 1 LYS B 98  ? PHE B 101 ? LYS B 100 PHE B 103 
AA6 2 CYS B 154 ? GLU B 164 ? CYS B 156 GLU B 166 
AA6 3 HIS B 170 ? THR B 173 ? HIS B 172 THR B 175 
# 
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 O LEU A 73  ? O LEU A 75  N VAL A 66  ? N VAL A 68  
AA1 2 3 O LEU A 65  ? O LEU A 67  N THR A 19  ? N THR A 21  
AA1 3 4 N VAL A 18  ? N VAL A 20  O LEU A 25  ? O LEU A 27  
AA1 4 5 N LEU A 28  ? N LEU A 30  O TYR A 35  ? O TYR A 37  
AA1 5 6 N VAL A 34  ? N VAL A 36  O LEU A 87  ? O LEU A 89  
AA1 6 7 O LYS A 86  ? O LYS A 88  N SER A 79  ? N SER A 81  
AA2 1 2 N LYS A 98  ? N LYS A 100 O VAL A 155 ? O VAL A 157 
AA2 2 3 O SER A 156 ? O SER A 158 N ASN A 149 ? N ASN A 151 
AA2 3 4 O PHE A 148 ? O PHE A 150 N SER A 111 ? N SER A 113 
AA2 4 5 N ALA A 114 ? N ALA A 116 O SER A 121 ? O SER A 123 
AA3 1 2 N LYS A 98  ? N LYS A 100 O VAL A 155 ? O VAL A 157 
AA3 2 3 N MET A 163 ? N MET A 165 O ALA A 171 ? O ALA A 173 
AA4 1 2 O VAL B 71  ? O VAL B 73  N ALA B 68  ? N ALA B 70  
AA4 2 3 O LEU B 65  ? O LEU B 67  N THR B 19  ? N THR B 21  
AA4 3 4 N VAL B 18  ? N VAL B 20  O LEU B 25  ? O LEU B 27  
AA4 4 5 N LEU B 28  ? N LEU B 30  O TYR B 35  ? O TYR B 37  
AA4 5 6 N VAL B 34  ? N VAL B 36  O LEU B 87  ? O LEU B 89  
AA4 6 7 O LYS B 86  ? O LYS B 88  N SER B 79  ? N SER B 81  
AA5 1 2 N LYS B 98  ? N LYS B 100 O VAL B 155 ? O VAL B 157 
AA5 2 3 O SER B 156 ? O SER B 158 N ASN B 149 ? N ASN B 151 
AA5 3 4 O PHE B 148 ? O PHE B 150 N SER B 111 ? N SER B 113 
AA5 4 5 N VAL B 112 ? N VAL B 114 O TYR B 124 ? O TYR B 126 
AA6 1 2 N LYS B 98  ? N LYS B 100 O VAL B 155 ? O VAL B 157 
AA6 2 3 N MET B 163 ? N MET B 165 O ALA B 171 ? O ALA B 173 
# 
_pdbx_entry_details.entry_id                   8Y4H 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 33  ? ? 53.63  -129.34 
2 1 ASN A 84  ? ? 52.34  -120.55 
3 1 TYR A 154 ? ? 44.58  72.29   
4 1 ASP A 155 ? ? 70.67  -14.00  
5 1 ALA A 191 ? ? -68.75 99.70   
6 1 ASP B 33  ? ? 52.82  -124.67 
7 1 ASN B 84  ? ? 53.07  -123.64 
# 
_pdbx_molecule_features.prd_id    PRD_002347 
_pdbx_molecule_features.name      
;~{N}-[(2~{S})-3-cyclohexyl-1-oxidanylidene-1-[[(2~{S})-1-oxidanylidene-3-[(3~{S})-2-oxidanylidenepyrrolidin-3-yl]propan-2-yl]amino]propan-2-yl]-1~{H}-indole-2-carboxamide
;
_pdbx_molecule_features.type      Peptide-like 
_pdbx_molecule_features.class     Inhibitor 
_pdbx_molecule_features.details   ? 
# 
loop_
_pdbx_molecule.instance_id 
_pdbx_molecule.prd_id 
_pdbx_molecule.asym_id 
1 PRD_002347 C 
2 PRD_002347 D 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
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 655 ? 5.88 . 
2 1 O ? B HOH 656 ? 6.03 . 
# 
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 PHE 3   ? A PHE 1   
2 1 Y 1 B SER 301 ? B SER 299 
3 1 Y 1 B GLY 302 ? B GLY 300 
4 1 Y 1 B VAL 303 ? B VAL 301 
# 
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  
FHR C02  C N N 88  
FHR C07  C Y N 89  
FHR C08  C Y N 90  
FHR C09  C Y N 91  
FHR C10  C Y N 92  
FHR C05  C Y N 93  
FHR C06  C Y N 94  
FHR C04  C Y N 95  
FHR C03  C Y N 96  
FHR N11  N Y N 97  
FHR O01  O N N 98  
FHR N12  N N N 99  
FHR C13  C N S 100 
FHR C21  C N N 101 
FHR O33  O N N 102 
FHR C14  C N N 103 
FHR C15  C N N 104 
FHR C20  C N N 105 
FHR C19  C N N 106 
FHR C18  C N N 107 
FHR C17  C N N 108 
FHR C16  C N N 109 
FHR O30  O N N 110 
FHR C29  C N N 111 
FHR N28  N N N 112 
FHR C27  C N N 113 
FHR C26  C N N 114 
FHR C25  C N S 115 
FHR C24  C N N 116 
FHR C23  C N S 117 
FHR N22  N N N 118 
FHR C31  C N N 119 
FHR O32  O N N 120 
FHR H15  H N N 121 
FHR H16  H N N 122 
FHR H17  H N N 123 
FHR H14  H N N 124 
FHR H13  H N N 125 
FHR H32  H N N 126 
FHR H1   H N N 127 
FHR H2   H N N 128 
FHR H18  H N N 129 
FHR H19  H N N 130 
FHR H3   H N N 131 
FHR H7   H N N 132 
FHR H6   H N N 133 
FHR H25  H N N 134 
FHR H24  H N N 135 
FHR H23  H N N 136 
FHR H22  H N N 137 
FHR H5   H N N 138 
FHR H4   H N N 139 
FHR H20  H N N 140 
FHR H21  H N N 141 
FHR H34  H N N 142 
FHR H28  H N N 143 
FHR H29  H N N 144 
FHR H10  H N N 145 
FHR H11  H N N 146 
FHR H27  H N N 147 
FHR H9   H N N 148 
FHR H8   H N N 149 
FHR H26  H N N 150 
FHR H33  H N N 151 
FHR H31  H N N 152 
GLN N    N N N 153 
GLN CA   C N S 154 
GLN C    C N N 155 
GLN O    O N N 156 
GLN CB   C N N 157 
GLN CG   C N N 158 
GLN CD   C N N 159 
GLN OE1  O N N 160 
GLN NE2  N N N 161 
GLN OXT  O N N 162 
GLN H    H N N 163 
GLN H2   H N N 164 
GLN HA   H N N 165 
GLN HB2  H N N 166 
GLN HB3  H N N 167 
GLN HG2  H N N 168 
GLN HG3  H N N 169 
GLN HE21 H N N 170 
GLN HE22 H N N 171 
GLN HXT  H N N 172 
GLU N    N N N 173 
GLU CA   C N S 174 
GLU C    C N N 175 
GLU O    O N N 176 
GLU CB   C N N 177 
GLU CG   C N N 178 
GLU CD   C N N 179 
GLU OE1  O N N 180 
GLU OE2  O N N 181 
GLU OXT  O N N 182 
GLU H    H N N 183 
GLU H2   H N N 184 
GLU HA   H N N 185 
GLU HB2  H N N 186 
GLU HB3  H N N 187 
GLU HG2  H N N 188 
GLU HG3  H N N 189 
GLU HE2  H N N 190 
GLU HXT  H N N 191 
GLY N    N N N 192 
GLY CA   C N N 193 
GLY C    C N N 194 
GLY O    O N N 195 
GLY OXT  O N N 196 
GLY H    H N N 197 
GLY H2   H N N 198 
GLY HA2  H N N 199 
GLY HA3  H N N 200 
GLY HXT  H N N 201 
HIS N    N N N 202 
HIS CA   C N S 203 
HIS C    C N N 204 
HIS O    O N N 205 
HIS CB   C N N 206 
HIS CG   C Y N 207 
HIS ND1  N Y N 208 
HIS CD2  C Y N 209 
HIS CE1  C Y N 210 
HIS NE2  N Y N 211 
HIS OXT  O N N 212 
HIS H    H N N 213 
HIS H2   H N N 214 
HIS HA   H N N 215 
HIS HB2  H N N 216 
HIS HB3  H N N 217 
HIS HD1  H N N 218 
HIS HD2  H N N 219 
HIS HE1  H N N 220 
HIS HE2  H N N 221 
HIS HXT  H N N 222 
HOH O    O N N 223 
HOH H1   H N N 224 
HOH H2   H N N 225 
ILE N    N N N 226 
ILE CA   C N S 227 
ILE C    C N N 228 
ILE O    O N N 229 
ILE CB   C N S 230 
ILE CG1  C N N 231 
ILE CG2  C N N 232 
ILE CD1  C N N 233 
ILE OXT  O N N 234 
ILE H    H N N 235 
ILE H2   H N N 236 
ILE HA   H N N 237 
ILE HB   H N N 238 
ILE HG12 H N N 239 
ILE HG13 H N N 240 
ILE HG21 H N N 241 
ILE HG22 H N N 242 
ILE HG23 H N N 243 
ILE HD11 H N N 244 
ILE HD12 H N N 245 
ILE HD13 H N N 246 
ILE HXT  H N N 247 
LEU N    N N N 248 
LEU CA   C N S 249 
LEU C    C N N 250 
LEU O    O N N 251 
LEU CB   C N N 252 
LEU CG   C N N 253 
LEU CD1  C N N 254 
LEU CD2  C N N 255 
LEU OXT  O N N 256 
LEU H    H N N 257 
LEU H2   H N N 258 
LEU HA   H N N 259 
LEU HB2  H N N 260 
LEU HB3  H N N 261 
LEU HG   H N N 262 
LEU HD11 H N N 263 
LEU HD12 H N N 264 
LEU HD13 H N N 265 
LEU HD21 H N N 266 
LEU HD22 H N N 267 
LEU HD23 H N N 268 
LEU HXT  H N N 269 
LYS N    N N N 270 
LYS CA   C N S 271 
LYS C    C N N 272 
LYS O    O N N 273 
LYS CB   C N N 274 
LYS CG   C N N 275 
LYS CD   C N N 276 
LYS CE   C N N 277 
LYS NZ   N N N 278 
LYS OXT  O N N 279 
LYS H    H N N 280 
LYS H2   H N N 281 
LYS HA   H N N 282 
LYS HB2  H N N 283 
LYS HB3  H N N 284 
LYS HG2  H N N 285 
LYS HG3  H N N 286 
LYS HD2  H N N 287 
LYS HD3  H N N 288 
LYS HE2  H N N 289 
LYS HE3  H N N 290 
LYS HZ1  H N N 291 
LYS HZ2  H N N 292 
LYS HZ3  H N N 293 
LYS HXT  H N N 294 
MET N    N N N 295 
MET CA   C N S 296 
MET C    C N N 297 
MET O    O N N 298 
MET CB   C N N 299 
MET CG   C N N 300 
MET SD   S N N 301 
MET CE   C N N 302 
MET OXT  O N N 303 
MET H    H N N 304 
MET H2   H N N 305 
MET HA   H N N 306 
MET HB2  H N N 307 
MET HB3  H N N 308 
MET HG2  H N N 309 
MET HG3  H N N 310 
MET HE1  H N N 311 
MET HE2  H N N 312 
MET HE3  H N N 313 
MET HXT  H N N 314 
PHE N    N N N 315 
PHE CA   C N S 316 
PHE C    C N N 317 
PHE O    O N N 318 
PHE CB   C N N 319 
PHE CG   C Y N 320 
PHE CD1  C Y N 321 
PHE CD2  C Y N 322 
PHE CE1  C Y N 323 
PHE CE2  C Y N 324 
PHE CZ   C Y N 325 
PHE OXT  O N N 326 
PHE H    H N N 327 
PHE H2   H N N 328 
PHE HA   H N N 329 
PHE HB2  H N N 330 
PHE HB3  H N N 331 
PHE HD1  H N N 332 
PHE HD2  H N N 333 
PHE HE1  H N N 334 
PHE HE2  H N N 335 
PHE HZ   H N N 336 
PHE HXT  H N N 337 
PRO N    N N N 338 
PRO CA   C N S 339 
PRO C    C N N 340 
PRO O    O N N 341 
PRO CB   C N N 342 
PRO CG   C N N 343 
PRO CD   C N N 344 
PRO OXT  O N N 345 
PRO H    H N N 346 
PRO HA   H N N 347 
PRO HB2  H N N 348 
PRO HB3  H N N 349 
PRO HG2  H N N 350 
PRO HG3  H N N 351 
PRO HD2  H N N 352 
PRO HD3  H N N 353 
PRO HXT  H N N 354 
SER N    N N N 355 
SER CA   C N S 356 
SER C    C N N 357 
SER O    O N N 358 
SER CB   C N N 359 
SER OG   O N N 360 
SER OXT  O N N 361 
SER H    H N N 362 
SER H2   H N N 363 
SER HA   H N N 364 
SER HB2  H N N 365 
SER HB3  H N N 366 
SER HG   H N N 367 
SER HXT  H N N 368 
THR N    N N N 369 
THR CA   C N S 370 
THR C    C N N 371 
THR O    O N N 372 
THR CB   C N R 373 
THR OG1  O N N 374 
THR CG2  C N N 375 
THR OXT  O N N 376 
THR H    H N N 377 
THR H2   H N N 378 
THR HA   H N N 379 
THR HB   H N N 380 
THR HG1  H N N 381 
THR HG21 H N N 382 
THR HG22 H N N 383 
THR HG23 H N N 384 
THR HXT  H N N 385 
TRP N    N N N 386 
TRP CA   C N S 387 
TRP C    C N N 388 
TRP O    O N N 389 
TRP CB   C N N 390 
TRP CG   C Y N 391 
TRP CD1  C Y N 392 
TRP CD2  C Y N 393 
TRP NE1  N Y N 394 
TRP CE2  C Y N 395 
TRP CE3  C Y N 396 
TRP CZ2  C Y N 397 
TRP CZ3  C Y N 398 
TRP CH2  C Y N 399 
TRP OXT  O N N 400 
TRP H    H N N 401 
TRP H2   H N N 402 
TRP HA   H N N 403 
TRP HB2  H N N 404 
TRP HB3  H N N 405 
TRP HD1  H N N 406 
TRP HE1  H N N 407 
TRP HE3  H N N 408 
TRP HZ2  H N N 409 
TRP HZ3  H N N 410 
TRP HH2  H N N 411 
TRP HXT  H N N 412 
TYR N    N N N 413 
TYR CA   C N S 414 
TYR C    C N N 415 
TYR O    O N N 416 
TYR CB   C N N 417 
TYR CG   C Y N 418 
TYR CD1  C Y N 419 
TYR CD2  C Y N 420 
TYR CE1  C Y N 421 
TYR CE2  C Y N 422 
TYR CZ   C Y N 423 
TYR OH   O N N 424 
TYR OXT  O N N 425 
TYR H    H N N 426 
TYR H2   H N N 427 
TYR HA   H N N 428 
TYR HB2  H N N 429 
TYR HB3  H N N 430 
TYR HD1  H N N 431 
TYR HD2  H N N 432 
TYR HE1  H N N 433 
TYR HE2  H N N 434 
TYR HH   H N N 435 
TYR HXT  H N N 436 
VAL N    N N N 437 
VAL CA   C N S 438 
VAL C    C N N 439 
VAL O    O N N 440 
VAL CB   C N N 441 
VAL CG1  C N N 442 
VAL CG2  C N N 443 
VAL OXT  O N N 444 
VAL H    H N N 445 
VAL H2   H N N 446 
VAL HA   H N N 447 
VAL HB   H N N 448 
VAL HG11 H N N 449 
VAL HG12 H N N 450 
VAL HG13 H N N 451 
VAL HG21 H N N 452 
VAL HG22 H N N 453 
VAL HG23 H N N 454 
VAL HXT  H N N 455 
# 
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  
FHR C10 C05  doub Y N 83  
FHR C10 C09  sing Y N 84  
FHR C10 N11  sing Y N 85  
FHR N12 C13  sing N N 86  
FHR N12 C02  sing N N 87  
FHR C13 C21  sing N N 88  
FHR C13 C14  sing N N 89  
FHR C15 C20  sing N N 90  
FHR C15 C14  sing N N 91  
FHR C15 C16  sing N N 92  
FHR C17 C16  sing N N 93  
FHR C17 C18  sing N N 94  
FHR C20 C19  sing N N 95  
FHR C21 N22  sing N N 96  
FHR C21 O33  doub N N 97  
FHR C24 C23  sing N N 98  
FHR C24 C25  sing N N 99  
FHR C26 C25  sing N N 100 
FHR C02 C03  sing N N 101 
FHR C02 O01  doub N N 102 
FHR C03 C04  doub Y N 103 
FHR C03 N11  sing Y N 104 
FHR C04 C05  sing Y N 105 
FHR C05 C06  sing Y N 106 
FHR C06 C07  doub Y N 107 
FHR C07 C08  sing Y N 108 
FHR C08 C09  doub Y N 109 
FHR C18 C19  sing N N 110 
FHR C23 C31  sing N N 111 
FHR C23 N22  sing N N 112 
FHR C25 C29  sing N N 113 
FHR C27 N28  sing N N 114 
FHR C29 N28  sing N N 115 
FHR C29 O30  doub N N 116 
FHR C31 O32  doub N N 117 
FHR N12 H1   sing N N 118 
FHR C13 H2   sing N N 119 
FHR C15 H3   sing N N 120 
FHR C17 H4   sing N N 121 
FHR C17 H5   sing N N 122 
FHR C20 H6   sing N N 123 
FHR C20 H7   sing N N 124 
FHR C24 H8   sing N N 125 
FHR C24 H9   sing N N 126 
FHR C26 H10  sing N N 127 
FHR C26 H11  sing N N 128 
FHR C04 H13  sing N N 129 
FHR C06 H14  sing N N 130 
FHR C07 H15  sing N N 131 
FHR C08 H16  sing N N 132 
FHR C09 H17  sing N N 133 
FHR C14 H18  sing N N 134 
FHR C14 H19  sing N N 135 
FHR C16 H20  sing N N 136 
FHR C16 H21  sing N N 137 
FHR C18 H22  sing N N 138 
FHR C18 H23  sing N N 139 
FHR C19 H24  sing N N 140 
FHR C19 H25  sing N N 141 
FHR C23 H26  sing N N 142 
FHR C25 H27  sing N N 143 
FHR C27 H28  sing N N 144 
FHR C27 H29  sing N N 145 
FHR C31 H31  sing N N 146 
FHR N11 H32  sing N N 147 
FHR N22 H33  sing N N 148 
FHR N28 H34  sing N N 149 
FHR C26 C27  sing N N 150 
GLN N   CA   sing N N 151 
GLN N   H    sing N N 152 
GLN N   H2   sing N N 153 
GLN CA  C    sing N N 154 
GLN CA  CB   sing N N 155 
GLN CA  HA   sing N N 156 
GLN C   O    doub N N 157 
GLN C   OXT  sing N N 158 
GLN CB  CG   sing N N 159 
GLN CB  HB2  sing N N 160 
GLN CB  HB3  sing N N 161 
GLN CG  CD   sing N N 162 
GLN CG  HG2  sing N N 163 
GLN CG  HG3  sing N N 164 
GLN CD  OE1  doub N N 165 
GLN CD  NE2  sing N N 166 
GLN NE2 HE21 sing N N 167 
GLN NE2 HE22 sing N N 168 
GLN OXT HXT  sing N N 169 
GLU N   CA   sing N N 170 
GLU N   H    sing N N 171 
GLU N   H2   sing N N 172 
GLU CA  C    sing N N 173 
GLU CA  CB   sing N N 174 
GLU CA  HA   sing N N 175 
GLU C   O    doub N N 176 
GLU C   OXT  sing N N 177 
GLU CB  CG   sing N N 178 
GLU CB  HB2  sing N N 179 
GLU CB  HB3  sing N N 180 
GLU CG  CD   sing N N 181 
GLU CG  HG2  sing N N 182 
GLU CG  HG3  sing N N 183 
GLU CD  OE1  doub N N 184 
GLU CD  OE2  sing N N 185 
GLU OE2 HE2  sing N N 186 
GLU OXT HXT  sing N N 187 
GLY N   CA   sing N N 188 
GLY N   H    sing N N 189 
GLY N   H2   sing N N 190 
GLY CA  C    sing N N 191 
GLY CA  HA2  sing N N 192 
GLY CA  HA3  sing N N 193 
GLY C   O    doub N N 194 
GLY C   OXT  sing N N 195 
GLY OXT HXT  sing N N 196 
HIS N   CA   sing N N 197 
HIS N   H    sing N N 198 
HIS N   H2   sing N N 199 
HIS CA  C    sing N N 200 
HIS CA  CB   sing N N 201 
HIS CA  HA   sing N N 202 
HIS C   O    doub N N 203 
HIS C   OXT  sing N N 204 
HIS CB  CG   sing N N 205 
HIS CB  HB2  sing N N 206 
HIS CB  HB3  sing N N 207 
HIS CG  ND1  sing Y N 208 
HIS CG  CD2  doub Y N 209 
HIS ND1 CE1  doub Y N 210 
HIS ND1 HD1  sing N N 211 
HIS CD2 NE2  sing Y N 212 
HIS CD2 HD2  sing N N 213 
HIS CE1 NE2  sing Y N 214 
HIS CE1 HE1  sing N N 215 
HIS NE2 HE2  sing N N 216 
HIS OXT HXT  sing N N 217 
HOH O   H1   sing N N 218 
HOH O   H2   sing N N 219 
ILE N   CA   sing N N 220 
ILE N   H    sing N N 221 
ILE N   H2   sing N N 222 
ILE CA  C    sing N N 223 
ILE CA  CB   sing N N 224 
ILE CA  HA   sing N N 225 
ILE C   O    doub N N 226 
ILE C   OXT  sing N N 227 
ILE CB  CG1  sing N N 228 
ILE CB  CG2  sing N N 229 
ILE CB  HB   sing N N 230 
ILE CG1 CD1  sing N N 231 
ILE CG1 HG12 sing N N 232 
ILE CG1 HG13 sing N N 233 
ILE CG2 HG21 sing N N 234 
ILE CG2 HG22 sing N N 235 
ILE CG2 HG23 sing N N 236 
ILE CD1 HD11 sing N N 237 
ILE CD1 HD12 sing N N 238 
ILE CD1 HD13 sing N N 239 
ILE OXT HXT  sing N N 240 
LEU N   CA   sing N N 241 
LEU N   H    sing N N 242 
LEU N   H2   sing N N 243 
LEU CA  C    sing N N 244 
LEU CA  CB   sing N N 245 
LEU CA  HA   sing N N 246 
LEU C   O    doub N N 247 
LEU C   OXT  sing N N 248 
LEU CB  CG   sing N N 249 
LEU CB  HB2  sing N N 250 
LEU CB  HB3  sing N N 251 
LEU CG  CD1  sing N N 252 
LEU CG  CD2  sing N N 253 
LEU CG  HG   sing N N 254 
LEU CD1 HD11 sing N N 255 
LEU CD1 HD12 sing N N 256 
LEU CD1 HD13 sing N N 257 
LEU CD2 HD21 sing N N 258 
LEU CD2 HD22 sing N N 259 
LEU CD2 HD23 sing N N 260 
LEU OXT HXT  sing N N 261 
LYS N   CA   sing N N 262 
LYS N   H    sing N N 263 
LYS N   H2   sing N N 264 
LYS CA  C    sing N N 265 
LYS CA  CB   sing N N 266 
LYS CA  HA   sing N N 267 
LYS C   O    doub N N 268 
LYS C   OXT  sing N N 269 
LYS CB  CG   sing N N 270 
LYS CB  HB2  sing N N 271 
LYS CB  HB3  sing N N 272 
LYS CG  CD   sing N N 273 
LYS CG  HG2  sing N N 274 
LYS CG  HG3  sing N N 275 
LYS CD  CE   sing N N 276 
LYS CD  HD2  sing N N 277 
LYS CD  HD3  sing N N 278 
LYS CE  NZ   sing N N 279 
LYS CE  HE2  sing N N 280 
LYS CE  HE3  sing N N 281 
LYS NZ  HZ1  sing N N 282 
LYS NZ  HZ2  sing N N 283 
LYS NZ  HZ3  sing N N 284 
LYS OXT HXT  sing N N 285 
MET N   CA   sing N N 286 
MET N   H    sing N N 287 
MET N   H2   sing N N 288 
MET CA  C    sing N N 289 
MET CA  CB   sing N N 290 
MET CA  HA   sing N N 291 
MET C   O    doub N N 292 
MET C   OXT  sing N N 293 
MET CB  CG   sing N N 294 
MET CB  HB2  sing N N 295 
MET CB  HB3  sing N N 296 
MET CG  SD   sing N N 297 
MET CG  HG2  sing N N 298 
MET CG  HG3  sing N N 299 
MET SD  CE   sing N N 300 
MET CE  HE1  sing N N 301 
MET CE  HE2  sing N N 302 
MET CE  HE3  sing N N 303 
MET OXT HXT  sing N N 304 
PHE N   CA   sing N N 305 
PHE N   H    sing N N 306 
PHE N   H2   sing N N 307 
PHE CA  C    sing N N 308 
PHE CA  CB   sing N N 309 
PHE CA  HA   sing N N 310 
PHE C   O    doub N N 311 
PHE C   OXT  sing N N 312 
PHE CB  CG   sing N N 313 
PHE CB  HB2  sing N N 314 
PHE CB  HB3  sing N N 315 
PHE CG  CD1  doub Y N 316 
PHE CG  CD2  sing Y N 317 
PHE CD1 CE1  sing Y N 318 
PHE CD1 HD1  sing N N 319 
PHE CD2 CE2  doub Y N 320 
PHE CD2 HD2  sing N N 321 
PHE CE1 CZ   doub Y N 322 
PHE CE1 HE1  sing N N 323 
PHE CE2 CZ   sing Y N 324 
PHE CE2 HE2  sing N N 325 
PHE CZ  HZ   sing N N 326 
PHE OXT HXT  sing N N 327 
PRO N   CA   sing N N 328 
PRO N   CD   sing N N 329 
PRO N   H    sing N N 330 
PRO CA  C    sing N N 331 
PRO CA  CB   sing N N 332 
PRO CA  HA   sing N N 333 
PRO C   O    doub N N 334 
PRO C   OXT  sing N N 335 
PRO CB  CG   sing N N 336 
PRO CB  HB2  sing N N 337 
PRO CB  HB3  sing N N 338 
PRO CG  CD   sing N N 339 
PRO CG  HG2  sing N N 340 
PRO CG  HG3  sing N N 341 
PRO CD  HD2  sing N N 342 
PRO CD  HD3  sing N N 343 
PRO OXT HXT  sing N N 344 
SER N   CA   sing N N 345 
SER N   H    sing N N 346 
SER N   H2   sing N N 347 
SER CA  C    sing N N 348 
SER CA  CB   sing N N 349 
SER CA  HA   sing N N 350 
SER C   O    doub N N 351 
SER C   OXT  sing N N 352 
SER CB  OG   sing N N 353 
SER CB  HB2  sing N N 354 
SER CB  HB3  sing N N 355 
SER OG  HG   sing N N 356 
SER OXT HXT  sing N N 357 
THR N   CA   sing N N 358 
THR N   H    sing N N 359 
THR N   H2   sing N N 360 
THR CA  C    sing N N 361 
THR CA  CB   sing N N 362 
THR CA  HA   sing N N 363 
THR C   O    doub N N 364 
THR C   OXT  sing N N 365 
THR CB  OG1  sing N N 366 
THR CB  CG2  sing N N 367 
THR CB  HB   sing N N 368 
THR OG1 HG1  sing N N 369 
THR CG2 HG21 sing N N 370 
THR CG2 HG22 sing N N 371 
THR CG2 HG23 sing N N 372 
THR OXT HXT  sing N N 373 
TRP N   CA   sing N N 374 
TRP N   H    sing N N 375 
TRP N   H2   sing N N 376 
TRP CA  C    sing N N 377 
TRP CA  CB   sing N N 378 
TRP CA  HA   sing N N 379 
TRP C   O    doub N N 380 
TRP C   OXT  sing N N 381 
TRP CB  CG   sing N N 382 
TRP CB  HB2  sing N N 383 
TRP CB  HB3  sing N N 384 
TRP CG  CD1  doub Y N 385 
TRP CG  CD2  sing Y N 386 
TRP CD1 NE1  sing Y N 387 
TRP CD1 HD1  sing N N 388 
TRP CD2 CE2  doub Y N 389 
TRP CD2 CE3  sing Y N 390 
TRP NE1 CE2  sing Y N 391 
TRP NE1 HE1  sing N N 392 
TRP CE2 CZ2  sing Y N 393 
TRP CE3 CZ3  doub Y N 394 
TRP CE3 HE3  sing N N 395 
TRP CZ2 CH2  doub Y N 396 
TRP CZ2 HZ2  sing N N 397 
TRP CZ3 CH2  sing Y N 398 
TRP CZ3 HZ3  sing N N 399 
TRP CH2 HH2  sing N N 400 
TRP OXT HXT  sing N N 401 
TYR N   CA   sing N N 402 
TYR N   H    sing N N 403 
TYR N   H2   sing N N 404 
TYR CA  C    sing N N 405 
TYR CA  CB   sing N N 406 
TYR CA  HA   sing N N 407 
TYR C   O    doub N N 408 
TYR C   OXT  sing N N 409 
TYR CB  CG   sing N N 410 
TYR CB  HB2  sing N N 411 
TYR CB  HB3  sing N N 412 
TYR CG  CD1  doub Y N 413 
TYR CG  CD2  sing Y N 414 
TYR CD1 CE1  sing Y N 415 
TYR CD1 HD1  sing N N 416 
TYR CD2 CE2  doub Y N 417 
TYR CD2 HD2  sing N N 418 
TYR CE1 CZ   doub Y N 419 
TYR CE1 HE1  sing N N 420 
TYR CE2 CZ   sing Y N 421 
TYR CE2 HE2  sing N N 422 
TYR CZ  OH   sing N N 423 
TYR OH  HH   sing N N 424 
TYR OXT HXT  sing N N 425 
VAL N   CA   sing N N 426 
VAL N   H    sing N N 427 
VAL N   H2   sing N N 428 
VAL CA  C    sing N N 429 
VAL CA  CB   sing N N 430 
VAL CA  HA   sing N N 431 
VAL C   O    doub N N 432 
VAL C   OXT  sing N N 433 
VAL CB  CG1  sing N N 434 
VAL CB  CG2  sing N N 435 
VAL CB  HB   sing N N 436 
VAL CG1 HG11 sing N N 437 
VAL CG1 HG12 sing N N 438 
VAL CG1 HG13 sing N N 439 
VAL CG2 HG21 sing N N 440 
VAL CG2 HG22 sing N N 441 
VAL CG2 HG23 sing N N 442 
VAL OXT HXT  sing N N 443 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_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   7CA8 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8Y4H 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.018015 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005977 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010133 
_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]   0.017871 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 25.62398 1.50364  0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 19.97189 1.75589  0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 15.80542 1.70748  0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 1.23737  29.19336 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . ARG A 1 2   ? -5.10300  13.18700  15.45000  1.000 38.27000 ? 4   ARG A N   1 
ATOM   2    C CA  . ARG A 1 2   ? -4.90200  11.89100  14.79600  1.000 33.98000 ? 4   ARG A CA  1 
ATOM   3    C C   . ARG A 1 2   ? -5.75500  10.77400  15.40400  1.000 28.65000 ? 4   ARG A C   1 
ATOM   4    O O   . ARG A 1 2   ? -6.08100  10.78900  16.59600  1.000 26.99000 ? 4   ARG A O   1 
ATOM   5    C CB  . ARG A 1 2   ? -3.43300  11.48800  14.86900  1.000 37.90000 ? 4   ARG A CB  1 
ATOM   6    C CG  . ARG A 1 2   ? -2.99200  11.11200  16.27200  1.000 35.01000 ? 4   ARG A CG  1 
ATOM   7    C CD  . ARG A 1 2   ? -1.97600  10.01000  16.25500  1.000 34.44000 ? 4   ARG A CD  1 
ATOM   8    N NE  . ARG A 1 2   ? -0.75700  10.38700  15.54100  1.000 36.59000 ? 4   ARG A NE  1 
ATOM   9    C CZ  . ARG A 1 2   ? -0.37000  9.85400   14.38400  1.000 31.39000 ? 4   ARG A CZ  1 
ATOM   10   N NH1 . ARG A 1 2   ? 0.75800   10.26000  13.82200  1.000 34.48000 ? 4   ARG A NH1 1 
ATOM   11   N NH2 . ARG A 1 2   ? -1.10300  8.91600   13.78700  1.000 35.11000 ? 4   ARG A NH2 1 
ATOM   12   N N   . LYS A 1 3   ? -6.09800  9.78500   14.58600  1.000 28.66000 ? 5   LYS A N   1 
ATOM   13   C CA  . LYS A 1 3   ? -6.88100  8.66200   15.07800  1.000 24.85000 ? 5   LYS A CA  1 
ATOM   14   C C   . LYS A 1 3   ? -5.98000  7.71500   15.86900  1.000 21.75000 ? 5   LYS A C   1 
ATOM   15   O O   . LYS A 1 3   ? -4.92300  7.29700   15.38800  1.000 24.24000 ? 5   LYS A O   1 
ATOM   16   C CB  . LYS A 1 3   ? -7.57200  7.95800   13.91600  1.000 26.31000 ? 5   LYS A CB  1 
ATOM   17   C CG  . LYS A 1 3   ? -8.37600  8.94500   13.05800  1.000 32.22000 ? 5   LYS A CG  1 
ATOM   18   C CD  . LYS A 1 3   ? -9.64000  8.33400   12.49700  1.000 34.84000 ? 5   LYS A CD  1 
ATOM   19   C CE  . LYS A 1 3   ? -10.50100 9.39900   11.81400  1.000 39.20000 ? 5   LYS A CE  1 
ATOM   20   N NZ  . LYS A 1 3   ? -10.81700 10.53000  12.74300  1.000 35.58000 ? 5   LYS A NZ  1 
ATOM   21   N N   . MET A 1 4   ? -6.39300  7.41200   17.09500  1.000 18.78000 ? 6   MET A N   1 
ATOM   22   C CA  . MET A 1 4   ? -5.62300  6.61200   18.03600  1.000 22.15000 ? 6   MET A CA  1 
ATOM   23   C C   . MET A 1 4   ? -6.48900  5.45400   18.50800  1.000 21.78000 ? 6   MET A C   1 
ATOM   24   O O   . MET A 1 4   ? -7.54600  5.67600   19.10700  1.000 18.48000 ? 6   MET A O   1 
ATOM   25   C CB  . MET A 1 4   ? -5.19100  7.47300   19.21700  1.000 24.05000 ? 6   MET A CB  1 
ATOM   26   C CG  . MET A 1 4   ? -4.19700  6.86200   20.17100  1.000 27.96000 ? 6   MET A CG  1 
ATOM   27   S SD  . MET A 1 4   ? -3.56200  8.18000   21.23400  1.000 44.78000 ? 6   MET A SD  1 
ATOM   28   C CE  . MET A 1 4   ? -3.43600  9.51600   20.05000  1.000 31.03000 ? 6   MET A CE  1 
ATOM   29   N N   . ALA A 1 5   ? -6.03200  4.22900   18.26100  1.000 14.55000 ? 7   ALA A N   1 
ATOM   30   C CA  . ALA A 1 5   ? -6.74800  3.04200   18.70800  1.000 13.96000 ? 7   ALA A CA  1 
ATOM   31   C C   . ALA A 1 5   ? -6.42500  2.74200   20.17000  1.000 15.44000 ? 7   ALA A C   1 
ATOM   32   O O   . ALA A 1 5   ? -5.41500  3.19700   20.70800  1.000 12.91000 ? 7   ALA A O   1 
ATOM   33   C CB  . ALA A 1 5   ? -6.37700  1.84200   17.83400  1.000 12.48000 ? 7   ALA A CB  1 
ATOM   34   N N   . PHE A 1 6   ? -7.30800  1.98400   20.82300  1.000 11.78000 ? 8   PHE A N   1 
ATOM   35   C CA  . PHE A 1 6   ? -6.97600  1.44900   22.13500  1.000 12.50000 ? 8   PHE A CA  1 
ATOM   36   C C   . PHE A 1 6   ? -5.94100  0.33800   21.99100  1.000 13.32000 ? 8   PHE A C   1 
ATOM   37   O O   . PHE A 1 6   ? -5.91200  -0.36400  20.97400  1.000 11.60000 ? 8   PHE A O   1 
ATOM   38   C CB  . PHE A 1 6   ? -8.21300  0.89700   22.83900  1.000 12.59000 ? 8   PHE A CB  1 
ATOM   39   C CG  . PHE A 1 6   ? -9.15900  1.96000   23.31900  1.000 14.45000 ? 8   PHE A CG  1 
ATOM   40   C CD1 . PHE A 1 6   ? -8.90500  2.64700   24.49500  1.000 23.00000 ? 8   PHE A CD1 1 
ATOM   41   C CD2 . PHE A 1 6   ? -10.28600 2.27400   22.59500  1.000 18.50000 ? 8   PHE A CD2 1 
ATOM   42   C CE1 . PHE A 1 6   ? -9.77300  3.63100   24.94200  1.000 22.65000 ? 8   PHE A CE1 1 
ATOM   43   C CE2 . PHE A 1 6   ? -11.16200 3.25200   23.03600  1.000 23.12000 ? 8   PHE A CE2 1 
ATOM   44   C CZ  . PHE A 1 6   ? -10.89900 3.92800   24.21600  1.000 22.74000 ? 8   PHE A CZ  1 
ATOM   45   N N   . PRO A 1 7   ? -5.07300  0.16100   22.99000  1.000 13.08000 ? 9   PRO A N   1 
ATOM   46   C CA  . PRO A 1 7   ? -4.17600  -0.99700  22.96800  1.000 13.66000 ? 9   PRO A CA  1 
ATOM   47   C C   . PRO A 1 7   ? -5.02900  -2.25100  22.84900  1.000 15.49000 ? 9   PRO A C   1 
ATOM   48   O O   . PRO A 1 7   ? -6.08400  -2.35500  23.47600  1.000 13.90000 ? 9   PRO A O   1 
ATOM   49   C CB  . PRO A 1 7   ? -3.45400  -0.93100  24.31900  1.000 15.71000 ? 9   PRO A CB  1 
ATOM   50   C CG  . PRO A 1 7   ? -3.74100  0.42300   24.89300  1.000 16.88000 ? 9   PRO A CG  1 
ATOM   51   C CD  . PRO A 1 7   ? -5.07800  0.83300   24.29800  1.000 13.81000 ? 9   PRO A CD  1 
ATOM   52   N N   . SER A 1 8   ? -4.58100  -3.18800  22.02700  1.000 13.99000 ? 10  SER A N   1 
ATOM   53   C CA  . SER A 1 8   ? -5.42200  -4.30600  21.61100  1.000 12.53000 ? 10  SER A CA  1 
ATOM   54   C C   . SER A 1 8   ? -5.12100  -5.61100  22.34300  1.000 11.58000 ? 10  SER A C   1 
ATOM   55   O O   . SER A 1 8   ? -5.81100  -6.61200  22.09600  1.000 11.58000 ? 10  SER A O   1 
ATOM   56   C CB  . SER A 1 8   ? -5.27700  -4.53300  20.11100  1.000 13.17000 ? 10  SER A CB  1 
ATOM   57   O OG  . SER A 1 8   ? -3.94800  -4.91300  19.79400  1.000 14.40000 ? 10  SER A OG  1 
ATOM   58   N N   . GLY A 1 9   ? -4.11400  -5.63300  23.22100  1.000 10.68000 ? 11  GLY A N   1 
ATOM   59   C CA  . GLY A 1 9   ? -3.69500  -6.89300  23.82600  1.000 12.36000 ? 11  GLY A CA  1 
ATOM   60   C C   . GLY A 1 9   ? -4.81900  -7.66400  24.50400  1.000 13.40000 ? 11  GLY A C   1 
ATOM   61   O O   . GLY A 1 9   ? -4.89900  -8.89300  24.38600  1.000 13.49000 ? 11  GLY A O   1 
ATOM   62   N N   . LYS A 1 10  ? -5.68900  -6.96100  25.24600  1.000 13.79000 ? 12  LYS A N   1 
ATOM   63   C CA  . LYS A 1 10  ? -6.76700  -7.65100  25.95900  1.000 15.05000 ? 12  LYS A CA  1 
ATOM   64   C C   . LYS A 1 10  ? -7.73700  -8.34200  25.00900  1.000 14.38000 ? 12  LYS A C   1 
ATOM   65   O O   . LYS A 1 10  ? -8.35300  -9.34700  25.38600  1.000 13.94000 ? 12  LYS A O   1 
ATOM   66   C CB  . LYS A 1 10  ? -7.54100  -6.68200  26.85200  1.000 11.85000 ? 12  LYS A CB  1 
ATOM   67   C CG  . LYS A 1 10  ? -6.81000  -6.28000  28.12900  1.000 15.73000 ? 12  LYS A CG  1 
ATOM   68   C CD  . LYS A 1 10  ? -7.60900  -5.20600  28.85200  1.000 21.26000 ? 12  LYS A CD  1 
ATOM   69   C CE  . LYS A 1 10  ? -7.00900  -4.88000  30.21200  1.000 30.10000 ? 12  LYS A CE  1 
ATOM   70   N NZ  . LYS A 1 10  ? -5.76600  -4.09300  30.06000  1.000 37.29000 ? 12  LYS A NZ  1 
ATOM   71   N N   . VAL A 1 11  ? -7.91200  -7.80900  23.79900  1.000 9.61000  ? 13  VAL A N   1 
ATOM   72   C CA  . VAL A 1 11  ? -8.77600  -8.45800  22.81200  1.000 11.03000 ? 13  VAL A CA  1 
ATOM   73   C C   . VAL A 1 11  ? -8.02900  -9.52100  22.01300  1.000 14.36000 ? 13  VAL A C   1 
ATOM   74   O O   . VAL A 1 11  ? -8.62500  -10.54000 21.63400  1.000 9.22000  ? 13  VAL A O   1 
ATOM   75   C CB  . VAL A 1 11  ? -9.40600  -7.41300  21.86800  1.000 8.84000  ? 13  VAL A CB  1 
ATOM   76   C CG1 . VAL A 1 11  ? -10.36000 -8.07500  20.85100  1.000 9.71000  ? 13  VAL A CG1 1 
ATOM   77   C CG2 . VAL A 1 11  ? -10.14500 -6.34400  22.69100  1.000 10.13000 ? 13  VAL A CG2 1 
ATOM   78   N N   . GLU A 1 12  ? -6.73600  -9.30300  21.73900  1.000 8.27000  ? 14  GLU A N   1 
ATOM   79   C CA  . GLU A 1 12  ? -5.95000  -10.30200 21.02200  1.000 10.10000 ? 14  GLU A CA  1 
ATOM   80   C C   . GLU A 1 12  ? -6.03700  -11.66200 21.70400  1.000 10.51000 ? 14  GLU A C   1 
ATOM   81   O O   . GLU A 1 12  ? -6.16400  -12.69700 21.03600  1.000 11.10000 ? 14  GLU A O   1 
ATOM   82   C CB  . GLU A 1 12  ? -4.48600  -9.86200  20.93900  1.000 14.52000 ? 14  GLU A CB  1 
ATOM   83   C CG  . GLU A 1 12  ? -4.18000  -8.72000  19.95600  1.000 13.23000 ? 14  GLU A CG  1 
ATOM   84   C CD  . GLU A 1 12  ? -2.80200  -8.11200  20.23600  1.000 14.53000 ? 14  GLU A CD  1 
ATOM   85   O OE1 . GLU A 1 12  ? -2.71100  -6.89300  20.51600  1.000 14.87000 ? 14  GLU A OE1 1 
ATOM   86   O OE2 . GLU A 1 12  ? -1.80300  -8.87100  20.20300  1.000 20.55000 ? 14  GLU A OE2 1 
ATOM   87   N N   . GLY A 1 13  ? -5.96200  -11.67700 23.03700  1.000 8.91000  ? 15  GLY A N   1 
ATOM   88   C CA  . GLY A 1 13  ? -6.03700  -12.91000 23.80700  1.000 10.55000 ? 15  GLY A CA  1 
ATOM   89   C C   . GLY A 1 13  ? -7.38600  -13.61700 23.73700  1.000 11.68000 ? 15  GLY A C   1 
ATOM   90   O O   . GLY A 1 13  ? -7.50800  -14.73000 24.25900  1.000 10.87000 ? 15  GLY A O   1 
ATOM   91   N N   . CYS A 1 14  ? -8.38800  -13.00000 23.10600  1.000 8.48000  ? 16  CYS A N   1 
ATOM   92   C CA  . CYS A 1 14  ? -9.72700  -13.57100 22.97800  1.000 7.88000  ? 16  CYS A CA  1 
ATOM   93   C C   . CYS A 1 14  ? -10.05300 -14.03900 21.57000  1.000 7.71000  ? 16  CYS A C   1 
ATOM   94   O O   . CYS A 1 14  ? -11.14400 -14.58000 21.35200  1.000 7.53000  ? 16  CYS A O   1 
ATOM   95   C CB  . CYS A 1 14  ? -10.78100 -12.54900 23.40100  1.000 9.88000  ? 16  CYS A CB  1 
ATOM   96   S SG  . CYS A 1 14  ? -10.57900 -12.08600 25.12400  1.000 17.15000 ? 16  CYS A SG  1 
ATOM   97   N N   . MET A 1 15  ? -9.16700  -13.83200 20.61000  1.000 7.46000  ? 17  MET A N   1 
ATOM   98   C CA  . MET A 1 15  ? -9.51300  -14.16000 19.23100  1.000 9.80000  ? 17  MET A CA  1 
ATOM   99   C C   . MET A 1 15  ? -9.22800  -15.62700 18.95600  1.000 10.20000 ? 17  MET A C   1 
ATOM   100  O O   . MET A 1 15  ? -8.15200  -16.14300 19.28400  1.000 11.39000 ? 17  MET A O   1 
ATOM   101  C CB  . MET A 1 15  ? -8.74800  -13.28400 18.24000  1.000 11.03000 ? 17  MET A CB  1 
ATOM   102  C CG  . MET A 1 15  ? -9.06700  -11.78300 18.36100  1.000 13.12000 ? 17  MET A CG  1 
ATOM   103  S SD  . MET A 1 15  ? -10.82900 -11.37900 18.41700  1.000 13.53000 ? 17  MET A SD  1 
ATOM   104  C CE  . MET A 1 15  ? -11.44300 -12.14700 16.89600  1.000 14.81000 ? 17  MET A CE  1 
ATOM   105  N N   . VAL A 1 16  ? -10.19500 -16.29800 18.34300  1.000 9.80000  ? 18  VAL A N   1 
ATOM   106  C CA  . VAL A 1 16  ? -10.01800 -17.67200 17.90100  1.000 8.52000  ? 18  VAL A CA  1 
ATOM   107  C C   . VAL A 1 16  ? -10.52300 -17.75800 16.47000  1.000 10.12000 ? 18  VAL A C   1 
ATOM   108  O O   . VAL A 1 16  ? -11.06100 -16.79800 15.92100  1.000 9.47000  ? 18  VAL A O   1 
ATOM   109  C CB  . VAL A 1 16  ? -10.75100 -18.67600 18.81300  1.000 7.86000  ? 18  VAL A CB  1 
ATOM   110  C CG1 . VAL A 1 16  ? -10.18800 -18.60700 20.23800  1.000 7.44000  ? 18  VAL A CG1 1 
ATOM   111  C CG2 . VAL A 1 16  ? -12.23300 -18.39700 18.81600  1.000 6.66000  ? 18  VAL A CG2 1 
ATOM   112  N N   . GLN A 1 17  ? -10.33000 -18.91300 15.85300  1.000 8.49000  ? 19  GLN A N   1 
ATOM   113  C CA  . GLN A 1 17  ? -10.93000 -19.12900 14.55000  1.000 11.40000 ? 19  GLN A CA  1 
ATOM   114  C C   . GLN A 1 17  ? -12.00600 -20.19700 14.66300  1.000 9.90000  ? 19  GLN A C   1 
ATOM   115  O O   . GLN A 1 17  ? -11.92100 -21.11300 15.49300  1.000 11.11000 ? 19  GLN A O   1 
ATOM   116  C CB  . GLN A 1 17  ? -9.87900  -19.49300 13.48400  1.000 13.37000 ? 19  GLN A CB  1 
ATOM   117  C CG  . GLN A 1 17  ? -8.85900  -20.54500 13.87000  1.000 17.79000 ? 19  GLN A CG  1 
ATOM   118  C CD  . GLN A 1 17  ? -7.91500  -20.88700 12.71500  1.000 22.24000 ? 19  GLN A CD  1 
ATOM   119  O OE1 . GLN A 1 17  ? -8.27800  -20.77800 11.52900  1.000 19.34000 ? 19  GLN A OE1 1 
ATOM   120  N NE2 . GLN A 1 17  ? -6.70600  -21.30800 13.05900  1.000 19.81000 ? 19  GLN A NE2 1 
ATOM   121  N N   . VAL A 1 18  ? -13.05300 -20.03000 13.85700  1.000 10.07000 ? 20  VAL A N   1 
ATOM   122  C CA  . VAL A 1 18  ? -14.19900 -20.92800 13.84000  1.000 8.61000  ? 20  VAL A CA  1 
ATOM   123  C C   . VAL A 1 18  ? -14.40900 -21.38200 12.40500  1.000 12.84000 ? 20  VAL A C   1 
ATOM   124  O O   . VAL A 1 18  ? -14.51500 -20.55400 11.49300  1.000 12.23000 ? 20  VAL A O   1 
ATOM   125  C CB  . VAL A 1 18  ? -15.47500 -20.25800 14.38800  1.000 9.15000  ? 20  VAL A CB  1 
ATOM   126  C CG1 . VAL A 1 18  ? -16.67200 -21.24500 14.34600  1.000 9.32000  ? 20  VAL A CG1 1 
ATOM   127  C CG2 . VAL A 1 18  ? -15.23800 -19.73100 15.82000  1.000 8.87000  ? 20  VAL A CG2 1 
ATOM   128  N N   . THR A 1 19  ? -14.45400 -22.69000 12.20700  1.000 11.97000 ? 21  THR A N   1 
ATOM   129  C CA  . THR A 1 19  ? -14.61800 -23.28000 10.89100  1.000 11.33000 ? 21  THR A CA  1 
ATOM   130  C C   . THR A 1 19  ? -15.84700 -24.17500 10.91900  1.000 15.05000 ? 21  THR A C   1 
ATOM   131  O O   . THR A 1 19  ? -16.02900 -24.98800 11.83900  1.000 14.47000 ? 21  THR A O   1 
ATOM   132  C CB  . THR A 1 19  ? -13.37300 -24.08300 10.46500  1.000 14.93000 ? 21  THR A CB  1 
ATOM   133  O OG1 . THR A 1 19  ? -12.22200 -23.22800 10.45400  1.000 14.27000 ? 21  THR A OG1 1 
ATOM   134  C CG2 . THR A 1 19  ? -13.55200 -24.68200 9.05200   1.000 19.32000 ? 21  THR A CG2 1 
ATOM   135  N N   . CYS A 1 20  ? -16.70100 -23.99500 9.93000   1.000 15.80000 ? 22  CYS A N   1 
ATOM   136  C CA  . CYS A 1 20  ? -17.85800 -24.83700 9.72900   1.000 16.51000 ? 22  CYS A CA  1 
ATOM   137  C C   . CYS A 1 20  ? -17.86600 -25.15300 8.24200   1.000 25.84000 ? 22  CYS A C   1 
ATOM   138  O O   . CYS A 1 20  ? -17.94500 -24.24200 7.40800   1.000 23.03000 ? 22  CYS A O   1 
ATOM   139  C CB  . CYS A 1 20  ? -19.12600 -24.12400 10.21100  1.000 15.04000 ? 22  CYS A CB  1 
ATOM   140  S SG  . CYS A 1 20  ? -20.57500 -25.15700 10.35400  1.000 31.64000 ? 22  CYS A SG  1 
ATOM   141  N N   . GLY A 1 21  ? -17.70000 -26.42800 7.91000   1.000 24.21000 ? 23  GLY A N   1 
ATOM   142  C CA  . GLY A 1 21  ? -17.50900 -26.80900 6.52600   1.000 28.14000 ? 23  GLY A CA  1 
ATOM   143  C C   . GLY A 1 21  ? -16.19900 -26.29500 5.97100   1.000 26.01000 ? 23  GLY A C   1 
ATOM   144  O O   . GLY A 1 21  ? -15.12900 -26.59500 6.50500   1.000 28.20000 ? 23  GLY A O   1 
ATOM   145  N N   . THR A 1 22  ? -16.27500 -25.50800 4.90100   1.000 28.21000 ? 24  THR A N   1 
ATOM   146  C CA  . THR A 1 22  ? -15.10500 -24.90700 4.27600   1.000 31.43000 ? 24  THR A CA  1 
ATOM   147  C C   . THR A 1 22  ? -14.90800 -23.44200 4.67200   1.000 26.59000 ? 24  THR A C   1 
ATOM   148  O O   . THR A 1 22  ? -13.92900 -22.81400 4.24600   1.000 25.75000 ? 24  THR A O   1 
ATOM   149  C CB  . THR A 1 22  ? -15.21700 -25.03400 2.74400   1.000 30.24000 ? 24  THR A CB  1 
ATOM   150  O OG1 . THR A 1 22  ? -14.04800 -24.48600 2.12600   1.000 45.42000 ? 24  THR A OG1 1 
ATOM   151  C CG2 . THR A 1 22  ? -16.45700 -24.31500 2.23000   1.000 25.69000 ? 24  THR A CG2 1 
ATOM   152  N N   . THR A 1 23  ? -15.79800 -22.88900 5.48300   1.000 22.08000 ? 25  THR A N   1 
ATOM   153  C CA  . THR A 1 23  ? -15.75800 -21.47700 5.84100   1.000 23.50000 ? 25  THR A CA  1 
ATOM   154  C C   . THR A 1 23  ? -15.07900 -21.31500 7.19100   1.000 20.15000 ? 25  THR A C   1 
ATOM   155  O O   . THR A 1 23  ? -15.53400 -21.89100 8.18500   1.000 16.07000 ? 25  THR A O   1 
ATOM   156  C CB  . THR A 1 23  ? -17.16500 -20.89600 5.89200   1.000 23.56000 ? 25  THR A CB  1 
ATOM   157  O OG1 . THR A 1 23  ? -17.78700 -21.07100 4.61400   1.000 31.49000 ? 25  THR A OG1 1 
ATOM   158  C CG2 . THR A 1 23  ? -17.10300 -19.41900 6.23300   1.000 24.16000 ? 25  THR A CG2 1 
ATOM   159  N N   . THR A 1 24  ? -13.98800 -20.55400 7.21500   1.000 18.40000 ? 26  THR A N   1 
ATOM   160  C CA  . THR A 1 24  ? -13.29700 -20.18600 8.44200   1.000 15.96000 ? 26  THR A CA  1 
ATOM   161  C C   . THR A 1 24  ? -13.46700 -18.68600 8.64500   1.000 18.35000 ? 26  THR A C   1 
ATOM   162  O O   . THR A 1 24  ? -13.28100 -17.90200 7.70600   1.000 15.67000 ? 26  THR A O   1 
ATOM   163  C CB  . THR A 1 24  ? -11.80800 -20.55100 8.38700   1.000 17.50000 ? 26  THR A CB  1 
ATOM   164  O OG1 . THR A 1 24  ? -11.64800 -21.97800 8.29800   1.000 18.00000 ? 26  THR A OG1 1 
ATOM   165  C CG2 . THR A 1 24  ? -11.08700 -20.05900 9.63400   1.000 19.43000 ? 26  THR A CG2 1 
ATOM   166  N N   . LEU A 1 25  ? -13.85500 -18.29000 9.85000   1.000 11.89000 ? 27  LEU A N   1 
ATOM   167  C CA  . LEU A 1 25  ? -13.85900 -16.87400 10.20800  1.000 13.48000 ? 27  LEU A CA  1 
ATOM   168  C C   . LEU A 1 25  ? -13.40800 -16.77100 11.65800  1.000 11.84000 ? 27  LEU A C   1 
ATOM   169  O O   . LEU A 1 25  ? -12.97300 -17.75600 12.26200  1.000 10.16000 ? 27  LEU A O   1 
ATOM   170  C CB  . LEU A 1 25  ? -15.23000 -16.23300 9.94700   1.000 11.12000 ? 27  LEU A CB  1 
ATOM   171  C CG  . LEU A 1 25  ? -16.51400 -16.96300 10.35300  1.000 13.96000 ? 27  LEU A CG  1 
ATOM   172  C CD1 . LEU A 1 25  ? -16.60200 -17.08800 11.85200  1.000 12.22000 ? 27  LEU A CD1 1 
ATOM   173  C CD2 . LEU A 1 25  ? -17.75300 -16.23000 9.83000   1.000 12.93000 ? 27  LEU A CD2 1 
ATOM   174  N N   . ASN A 1 26  ? -13.52800 -15.57800 12.22100  1.000 9.52000  ? 28  ASN A N   1 
ATOM   175  C CA  . ASN A 1 26  ? -13.02400 -15.30100 13.55300  1.000 10.58000 ? 28  ASN A CA  1 
ATOM   176  C C   . ASN A 1 26  ? -14.13400 -15.40300 14.58600  1.000 8.69000  ? 28  ASN A C   1 
ATOM   177  O O   . ASN A 1 26  ? -15.30000 -15.10100 14.31400  1.000 11.21000 ? 28  ASN A O   1 
ATOM   178  C CB  . ASN A 1 26  ? -12.39600 -13.90200 13.61600  1.000 9.23000  ? 28  ASN A CB  1 
ATOM   179  C CG  . ASN A 1 26  ? -11.32600 -13.72000 12.56700  1.000 13.05000 ? 28  ASN A CG  1 
ATOM   180  O OD1 . ASN A 1 26  ? -10.22700 -14.26700 12.68800  1.000 11.82000 ? 28  ASN A OD1 1 
ATOM   181  N ND2 . ASN A 1 26  ? -11.64700 -12.96600 11.51400  1.000 11.04000 ? 28  ASN A ND2 1 
ATOM   182  N N   . GLY A 1 27  ? -13.73700 -15.78600 15.79900  1.000 8.23000  ? 29  GLY A N   1 
ATOM   183  C CA  . GLY A 1 27  ? -14.65100 -15.81600 16.91700  1.000 8.69000  ? 29  GLY A CA  1 
ATOM   184  C C   . GLY A 1 27  ? -14.02000 -15.16700 18.12700  1.000 8.17000  ? 29  GLY A C   1 
ATOM   185  O O   . GLY A 1 27  ? -12.80100 -15.00800 18.21900  1.000 7.70000  ? 29  GLY A O   1 
ATOM   186  N N   . LEU A 1 28  ? -14.87400 -14.79900 19.07200  1.000 6.60000  ? 30  LEU A N   1 
ATOM   187  C CA  . LEU A 1 28  ? -14.46400 -14.10200 20.28600  1.000 7.91000  ? 30  LEU A CA  1 
ATOM   188  C C   . LEU A 1 28  ? -14.70700 -15.03800 21.45900  1.000 6.48000  ? 30  LEU A C   1 
ATOM   189  O O   . LEU A 1 28  ? -15.85900 -15.38900 21.73500  1.000 9.14000  ? 30  LEU A O   1 
ATOM   190  C CB  . LEU A 1 28  ? -15.27000 -12.81100 20.44700  1.000 7.98000  ? 30  LEU A CB  1 
ATOM   191  C CG  . LEU A 1 28  ? -14.93800 -11.89400 21.61600  1.000 8.63000  ? 30  LEU A CG  1 
ATOM   192  C CD1 . LEU A 1 28  ? -13.57500 -11.26700 21.36600  1.000 10.71000 ? 30  LEU A CD1 1 
ATOM   193  C CD2 . LEU A 1 28  ? -16.00500 -10.80800 21.75200  1.000 7.08000  ? 30  LEU A CD2 1 
ATOM   194  N N   . TRP A 1 29  ? -13.63300 -15.42100 22.14600  1.000 6.50000  ? 31  TRP A N   1 
ATOM   195  C CA  . TRP A 1 29  ? -13.66000 -16.42700 23.20100  1.000 7.46000  ? 31  TRP A CA  1 
ATOM   196  C C   . TRP A 1 29  ? -13.61300 -15.72500 24.55800  1.000 7.62000  ? 31  TRP A C   1 
ATOM   197  O O   . TRP A 1 29  ? -12.57100 -15.19800 24.96100  1.000 8.67000  ? 31  TRP A O   1 
ATOM   198  C CB  . TRP A 1 29  ? -12.47500 -17.37700 23.01500  1.000 6.16000  ? 31  TRP A CB  1 
ATOM   199  C CG  . TRP A 1 29  ? -12.32600 -18.48500 24.00400  1.000 6.57000  ? 31  TRP A CG  1 
ATOM   200  C CD1 . TRP A 1 29  ? -13.30300 -19.05700 24.77500  1.000 7.85000  ? 31  TRP A CD1 1 
ATOM   201  C CD2 . TRP A 1 29  ? -11.11200 -19.18900 24.30200  1.000 8.35000  ? 31  TRP A CD2 1 
ATOM   202  N NE1 . TRP A 1 29  ? -12.75800 -20.06100 25.55800  1.000 6.72000  ? 31  TRP A NE1 1 
ATOM   203  C CE2 . TRP A 1 29  ? -11.42100 -20.17200 25.26600  1.000 8.47000  ? 31  TRP A CE2 1 
ATOM   204  C CE3 . TRP A 1 29  ? -9.79500  -19.08000 23.84400  1.000 9.98000  ? 31  TRP A CE3 1 
ATOM   205  C CZ2 . TRP A 1 29  ? -10.45000 -21.02200 25.80800  1.000 10.89000 ? 31  TRP A CZ2 1 
ATOM   206  C CZ3 . TRP A 1 29  ? -8.83100  -19.93500 24.37800  1.000 13.16000 ? 31  TRP A CZ3 1 
ATOM   207  C CH2 . TRP A 1 29  ? -9.17100  -20.89700 25.33900  1.000 11.06000 ? 31  TRP A CH2 1 
ATOM   208  N N   . LEU A 1 30  ? -14.74100 -15.70600 25.25000  1.000 7.18000  ? 32  LEU A N   1 
ATOM   209  C CA  . LEU A 1 30  ? -14.86400 -15.06100 26.55200  1.000 10.03000 ? 32  LEU A CA  1 
ATOM   210  C C   . LEU A 1 30  ? -15.40500 -16.10500 27.51200  1.000 8.86000  ? 32  LEU A C   1 
ATOM   211  O O   . LEU A 1 30  ? -16.46400 -16.68400 27.25500  1.000 10.03000 ? 32  LEU A O   1 
ATOM   212  C CB  . LEU A 1 30  ? -15.79900 -13.83700 26.47900  1.000 10.70000 ? 32  LEU A CB  1 
ATOM   213  C CG  . LEU A 1 30  ? -15.36000 -12.74800 25.49100  1.000 8.70000  ? 32  LEU A CG  1 
ATOM   214  C CD1 . LEU A 1 30  ? -16.50000 -11.72900 25.20100  1.000 8.97000  ? 32  LEU A CD1 1 
ATOM   215  C CD2 . LEU A 1 30  ? -14.12000 -12.06300 26.04700  1.000 8.16000  ? 32  LEU A CD2 1 
ATOM   216  N N   . ASP A 1 31  ? -14.67700 -16.35800 28.60500  1.000 9.33000  ? 33  ASP A N   1 
ATOM   217  C CA  . ASP A 1 31  ? -15.03900 -17.42600 29.53800  1.000 11.08000 ? 33  ASP A CA  1 
ATOM   218  C C   . ASP A 1 31  ? -15.16900 -18.68800 28.68500  1.000 10.44000 ? 33  ASP A C   1 
ATOM   219  O O   . ASP A 1 31  ? -14.26300 -18.95200 27.88700  1.000 9.03000  ? 33  ASP A O   1 
ATOM   220  C CB  . ASP A 1 31  ? -16.25600 -17.02300 30.34800  1.000 14.68000 ? 33  ASP A CB  1 
ATOM   221  C CG  . ASP A 1 31  ? -15.97400 -15.82300 31.23100  1.000 17.40000 ? 33  ASP A CG  1 
ATOM   222  O OD1 . ASP A 1 31  ? -14.94400 -15.84700 31.92500  1.000 18.65000 ? 33  ASP A OD1 1 
ATOM   223  O OD2 . ASP A 1 31  ? -16.76400 -14.85800 31.23700  1.000 17.41000 ? 33  ASP A OD2 1 
ATOM   224  N N   . ASP A 1 32  ? -16.26000 -19.45100 28.77500  1.000 10.36000 ? 34  ASP A N   1 
ATOM   225  C CA  . ASP A 1 32  ? -16.36000 -20.69900 28.02400  1.000 13.05000 ? 34  ASP A CA  1 
ATOM   226  C C   . ASP A 1 32  ? -17.31500 -20.58600 26.84000  1.000 11.90000 ? 34  ASP A C   1 
ATOM   227  O O   . ASP A 1 32  ? -17.92600 -21.57300 26.43500  1.000 8.97000  ? 34  ASP A O   1 
ATOM   228  C CB  . ASP A 1 32  ? -16.77800 -21.85100 28.93500  1.000 14.52000 ? 34  ASP A CB  1 
ATOM   229  C CG  . ASP A 1 32  ? -18.14700 -21.64100 29.54400  1.000 19.52000 ? 34  ASP A CG  1 
ATOM   230  O OD1 . ASP A 1 32  ? -18.62100 -20.48300 29.53000  1.000 21.83000 ? 34  ASP A OD1 1 
ATOM   231  O OD2 . ASP A 1 32  ? -18.73900 -22.62400 30.04600  1.000 25.56000 ? 34  ASP A OD2 1 
ATOM   232  N N   . VAL A 1 33  ? -17.43300 -19.39600 26.26000  1.000 10.40000 ? 35  VAL A N   1 
ATOM   233  C CA  . VAL A 1 33  ? -18.29800 -19.18500 25.11500  1.000 8.93000  ? 35  VAL A CA  1 
ATOM   234  C C   . VAL A 1 33  ? -17.49500 -18.54600 23.99500  1.000 10.35000 ? 35  VAL A C   1 
ATOM   235  O O   . VAL A 1 33  ? -16.69900 -17.63100 24.22900  1.000 7.70000  ? 35  VAL A O   1 
ATOM   236  C CB  . VAL A 1 33  ? -19.51800 -18.30800 25.47800  1.000 10.26000 ? 35  VAL A CB  1 
ATOM   237  C CG1 . VAL A 1 33  ? -20.35300 -18.03700 24.23500  1.000 9.31000  ? 35  VAL A CG1 1 
ATOM   238  C CG2 . VAL A 1 33  ? -20.36800 -19.02000 26.50600  1.000 15.88000 ? 35  VAL A CG2 1 
ATOM   239  N N   . VAL A 1 34  ? -17.73400 -19.00600 22.76900  1.000 9.08000  ? 36  VAL A N   1 
ATOM   240  C CA  . VAL A 1 34  ? -17.16400 -18.39100 21.58000  1.000 7.92000  ? 36  VAL A CA  1 
ATOM   241  C C   . VAL A 1 34  ? -18.30600 -17.78100 20.77700  1.000 10.75000 ? 36  VAL A C   1 
ATOM   242  O O   . VAL A 1 34  ? -19.31300 -18.45300 20.49200  1.000 9.08000  ? 36  VAL A O   1 
ATOM   243  C CB  . VAL A 1 34  ? -16.34800 -19.41000 20.76300  1.000 7.79000  ? 36  VAL A CB  1 
ATOM   244  C CG1 . VAL A 1 34  ? -15.97800 -18.86200 19.38000  1.000 6.51000  ? 36  VAL A CG1 1 
ATOM   245  C CG2 . VAL A 1 34  ? -15.10300 -19.82300 21.56300  1.000 10.06000 ? 36  VAL A CG2 1 
ATOM   246  N N   . TYR A 1 35  ? -18.16500 -16.49700 20.45600  1.000 7.46000  ? 37  TYR A N   1 
ATOM   247  C CA  . TYR A 1 35  ? -19.14200 -15.73000 19.68800  1.000 7.66000  ? 37  TYR A CA  1 
ATOM   248  C C   . TYR A 1 35  ? -18.63400 -15.52200 18.26800  1.000 9.94000  ? 37  TYR A C   1 
ATOM   249  O O   . TYR A 1 35  ? -17.48000 -15.12600 18.06800  1.000 8.46000  ? 37  TYR A O   1 
ATOM   250  C CB  . TYR A 1 35  ? -19.39900 -14.36200 20.34100  1.000 9.89000  ? 37  TYR A CB  1 
ATOM   251  C CG  . TYR A 1 35  ? -19.78800 -14.45000 21.79100  1.000 10.71000 ? 37  TYR A CG  1 
ATOM   252  C CD1 . TYR A 1 35  ? -18.82000 -14.60300 22.78000  1.000 11.20000 ? 37  TYR A CD1 1 
ATOM   253  C CD2 . TYR A 1 35  ? -21.12600 -14.38000 22.17900  1.000 14.39000 ? 37  TYR A CD2 1 
ATOM   254  C CE1 . TYR A 1 35  ? -19.17100 -14.71300 24.12300  1.000 11.17000 ? 37  TYR A CE1 1 
ATOM   255  C CE2 . TYR A 1 35  ? -21.49000 -14.47600 23.51500  1.000 11.02000 ? 37  TYR A CE2 1 
ATOM   256  C CZ  . TYR A 1 35  ? -20.50800 -14.64400 24.47700  1.000 14.17000 ? 37  TYR A CZ  1 
ATOM   257  O OH  . TYR A 1 35  ? -20.85600 -14.74700 25.80300  1.000 15.68000 ? 37  TYR A OH  1 
ATOM   258  N N   . CYS A 1 36  ? -19.49600 -15.74300 17.28200  1.000 8.97000  ? 38  CYS A N   1 
ATOM   259  C CA  . CYS A 1 36  ? -19.08300 -15.52800 15.89900  1.000 9.76000  ? 38  CYS A CA  1 
ATOM   260  C C   . CYS A 1 36  ? -20.32700 -15.31400 15.04400  1.000 10.42000 ? 38  CYS A C   1 
ATOM   261  O O   . CYS A 1 36  ? -21.45200 -15.58300 15.49700  1.000 8.93000  ? 38  CYS A O   1 
ATOM   262  C CB  . CYS A 1 36  ? -18.24900 -16.70400 15.36400  1.000 8.81000  ? 38  CYS A CB  1 
ATOM   263  S SG  . CYS A 1 36  ? -19.20200 -18.19800 15.01100  1.000 11.80000 ? 38  CYS A SG  1 
ATOM   264  N N   . PRO A 1 37  ? -20.16200 -14.78600 13.82900  1.000 12.11000 ? 39  PRO A N   1 
ATOM   265  C CA  . PRO A 1 37  ? -21.32000 -14.56900 12.95800  1.000 11.05000 ? 39  PRO A CA  1 
ATOM   266  C C   . PRO A 1 37  ? -21.97100 -15.89300 12.59100  1.000 12.18000 ? 39  PRO A C   1 
ATOM   267  O O   . PRO A 1 37  ? -21.29200 -16.85700 12.23000  1.000 8.93000  ? 39  PRO A O   1 
ATOM   268  C CB  . PRO A 1 37  ? -20.71400 -13.88500 11.72700  1.000 11.90000 ? 39  PRO A CB  1 
ATOM   269  C CG  . PRO A 1 37  ? -19.42900 -13.26100 12.23400  1.000 10.43000 ? 39  PRO A CG  1 
ATOM   270  C CD  . PRO A 1 37  ? -18.92100 -14.25900 13.22600  1.000 9.18000  ? 39  PRO A CD  1 
ATOM   271  N N   . ARG A 1 38  ? -23.29900 -15.92800 12.68800  1.000 12.18000 ? 40  ARG A N   1 
ATOM   272  C CA  . ARG A 1 38  ? -24.01700 -17.15900 12.38600  1.000 12.02000 ? 40  ARG A CA  1 
ATOM   273  C C   . ARG A 1 38  ? -23.86100 -17.57500 10.92900  1.000 14.40000 ? 40  ARG A C   1 
ATOM   274  O O   . ARG A 1 38  ? -24.05000 -18.75600 10.61300  1.000 13.51000 ? 40  ARG A O   1 
ATOM   275  C CB  . ARG A 1 38  ? -25.50000 -17.01800 12.74700  1.000 11.83000 ? 40  ARG A CB  1 
ATOM   276  C CG  . ARG A 1 38  ? -26.30400 -16.04000 11.88300  1.000 12.50000 ? 40  ARG A CG  1 
ATOM   277  C CD  . ARG A 1 38  ? -27.79300 -16.15300 12.21200  1.000 14.70000 ? 40  ARG A CD  1 
ATOM   278  N NE  . ARG A 1 38  ? -28.60400 -15.16800 11.49500  1.000 16.13000 ? 40  ARG A NE  1 
ATOM   279  C CZ  . ARG A 1 38  ? -29.92500 -15.03600 11.62900  1.000 19.84000 ? 40  ARG A CZ  1 
ATOM   280  N NH1 . ARG A 1 38  ? -30.59200 -15.81700 12.46400  1.000 18.39000 ? 40  ARG A NH1 1 
ATOM   281  N NH2 . ARG A 1 38  ? -30.57900 -14.10700 10.93000  1.000 17.62000 ? 40  ARG A NH2 1 
ATOM   282  N N   . HIS A 1 39  ? -23.48400 -16.64900 10.03100  1.000 15.74000 ? 41  HIS A N   1 
ATOM   283  C CA  . HIS A 1 39  ? -23.39500 -17.06300 8.63800   1.000 16.58000 ? 41  HIS A CA  1 
ATOM   284  C C   . HIS A 1 39  ? -22.22700 -18.00100 8.37500   1.000 15.10000 ? 41  HIS A C   1 
ATOM   285  O O   . HIS A 1 39  ? -22.13000 -18.52900 7.26400   1.000 15.21000 ? 41  HIS A O   1 
ATOM   286  C CB  . HIS A 1 39  ? -23.37500 -15.84600 7.68500   1.000 15.32000 ? 41  HIS A CB  1 
ATOM   287  C CG  . HIS A 1 39  ? -22.12300 -15.01800 7.70700   1.000 15.05000 ? 41  HIS A CG  1 
ATOM   288  N ND1 . HIS A 1 39  ? -20.88600 -15.50500 7.34700   1.000 15.42000 ? 41  HIS A ND1 1 
ATOM   289  C CD2 . HIS A 1 39  ? -21.94200 -13.69900 7.97500   1.000 13.90000 ? 41  HIS A CD2 1 
ATOM   290  C CE1 . HIS A 1 39  ? -19.99300 -14.53200 7.41100   1.000 14.81000 ? 41  HIS A CE1 1 
ATOM   291  N NE2 . HIS A 1 39  ? -20.61100 -13.42400 7.78500   1.000 13.15000 ? 41  HIS A NE2 1 
ATOM   292  N N   . VAL A 1 40  ? -21.38900 -18.27800 9.37800   1.000 13.21000 ? 42  VAL A N   1 
ATOM   293  C CA  . VAL A 1 40  ? -20.40900 -19.35100 9.26200   1.000 13.37000 ? 42  VAL A CA  1 
ATOM   294  C C   . VAL A 1 40  ? -21.05400 -20.69500 8.91300   1.000 13.30000 ? 42  VAL A C   1 
ATOM   295  O O   . VAL A 1 40  ? -20.37800 -21.56800 8.36300   1.000 15.42000 ? 42  VAL A O   1 
ATOM   296  C CB  . VAL A 1 40  ? -19.59600 -19.45400 10.57000  1.000 13.09000 ? 42  VAL A CB  1 
ATOM   297  C CG1 . VAL A 1 40  ? -20.45900 -19.99100 11.68700  1.000 10.49000 ? 42  VAL A CG1 1 
ATOM   298  C CG2 . VAL A 1 40  ? -18.33200 -20.27500 10.36900  1.000 12.51000 ? 42  VAL A CG2 1 
ATOM   299  N N   . ILE A 1 41  ? -22.34400 -20.89200 9.22400   1.000 13.91000 ? 43  ILE A N   1 
ATOM   300  C CA  . ILE A 1 41  ? -23.00300 -22.16500 8.92100   1.000 15.63000 ? 43  ILE A CA  1 
ATOM   301  C C   . ILE A 1 41  ? -23.59900 -22.20700 7.52200   1.000 22.14000 ? 43  ILE A C   1 
ATOM   302  O O   . ILE A 1 41  ? -24.25200 -23.20100 7.17000   1.000 24.08000 ? 43  ILE A O   1 
ATOM   303  C CB  . ILE A 1 41  ? -24.12000 -22.52200 9.92800   1.000 17.78000 ? 43  ILE A CB  1 
ATOM   304  C CG1 . ILE A 1 41  ? -25.36300 -21.64600 9.73000   1.000 17.52000 ? 43  ILE A CG1 1 
ATOM   305  C CG2 . ILE A 1 41  ? -23.60700 -22.46900 11.37100  1.000 15.23000 ? 43  ILE A CG2 1 
ATOM   306  C CD1 . ILE A 1 41  ? -26.43000 -21.89600 10.77800  1.000 19.28000 ? 43  ILE A CD1 1 
ATOM   307  N N   . CYS A 1 42  ? -23.39300 -21.17400 6.70700   1.000 22.25000 ? 44  CYS A N   1 
ATOM   308  C CA  . CYS A 1 42  ? -23.95700 -21.13800 5.36300   1.000 25.08000 ? 44  CYS A CA  1 
ATOM   309  C C   . CYS A 1 42  ? -23.03700 -21.82200 4.36800   1.000 24.62000 ? 44  CYS A C   1 
ATOM   310  O O   . CYS A 1 42  ? -21.81500 -21.69900 4.45200   1.000 26.97000 ? 44  CYS A O   1 
ATOM   311  C CB  . CYS A 1 42  ? -24.18500 -19.69600 4.90800   1.000 23.82000 ? 44  CYS A CB  1 
ATOM   312  S SG  . CYS A 1 42  ? -25.41300 -18.86200 5.85600   1.000 25.32000 ? 44  CYS A SG  1 
ATOM   313  N N   . THR A 1 43  ? -23.63400 -22.53200 3.41800   1.000 27.79000 ? 45  THR A N   1 
ATOM   314  C CA  . THR A 1 43  ? -22.93100 -22.91200 2.20600   1.000 26.25000 ? 45  THR A CA  1 
ATOM   315  C C   . THR A 1 43  ? -23.06700 -21.79800 1.17100   1.000 30.70000 ? 45  THR A C   1 
ATOM   316  O O   . THR A 1 43  ? -23.85500 -20.86500 1.32900   1.000 34.12000 ? 45  THR A O   1 
ATOM   317  C CB  . THR A 1 43  ? -23.47800 -24.23000 1.66500   1.000 33.59000 ? 45  THR A CB  1 
ATOM   318  O OG1 . THR A 1 43  ? -24.80500 -24.02300 1.17300   1.000 30.53000 ? 45  THR A OG1 1 
ATOM   319  C CG2 . THR A 1 43  ? -23.51600 -25.27200 2.77400   1.000 34.70000 ? 45  THR A CG2 1 
ATOM   320  N N   . SER A 1 44  ? -22.29000 -21.90600 0.09000   1.000 34.88000 ? 46  SER A N   1 
ATOM   321  C CA  . SER A 1 44  ? -22.30300 -20.85300 -0.92300  1.000 40.49000 ? 46  SER A CA  1 
ATOM   322  C C   . SER A 1 44  ? -23.67500 -20.70400 -1.57400  1.000 42.98000 ? 46  SER A C   1 
ATOM   323  O O   . SER A 1 44  ? -24.02600 -19.61000 -2.03300  1.000 43.47000 ? 46  SER A O   1 
ATOM   324  C CB  . SER A 1 44  ? -21.24000 -21.12300 -1.98500  1.000 44.24000 ? 46  SER A CB  1 
ATOM   325  O OG  . SER A 1 44  ? -21.61400 -22.21000 -2.81100  1.000 52.85000 ? 46  SER A OG  1 
ATOM   326  N N   . GLU A 1 45  ? -24.46700 -21.77600 -1.62100  1.000 37.08000 ? 47  GLU A N   1 
ATOM   327  C CA  . GLU A 1 45  ? -25.83000 -21.64900 -2.12200  1.000 43.95000 ? 47  GLU A CA  1 
ATOM   328  C C   . GLU A 1 45  ? -26.82800 -21.30900 -1.02100  1.000 39.00000 ? 47  GLU A C   1 
ATOM   329  O O   . GLU A 1 45  ? -27.96800 -20.94000 -1.32600  1.000 42.09000 ? 47  GLU A O   1 
ATOM   330  C CB  . GLU A 1 45  ? -26.26700 -22.93500 -2.83000  1.000 34.90000 ? 47  GLU A CB  1 
ATOM   331  C CG  . GLU A 1 45  ? -25.48100 -23.23600 -4.09800  1.000 34.89000 ? 47  GLU A CG  1 
ATOM   332  C CD  . GLU A 1 45  ? -25.49300 -22.09900 -5.13500  1.000 43.07000 ? 47  GLU A CD  1 
ATOM   333  O OE1 . GLU A 1 45  ? -26.56600 -21.50200 -5.40700  1.000 32.68000 ? 47  GLU A OE1 1 
ATOM   334  O OE2 . GLU A 1 45  ? -24.40900 -21.80500 -5.69500  1.000 48.46000 ? 47  GLU A OE2 1 
ATOM   335  N N   . ASP A 1 46  ? -26.42500 -21.40400 0.24900   1.000 39.76000 ? 48  ASP A N   1 
ATOM   336  C CA  . ASP A 1 46  ? -27.30700 -21.02200 1.34800   1.000 41.41000 ? 48  ASP A CA  1 
ATOM   337  C C   . ASP A 1 46  ? -27.45300 -19.51700 1.48800   1.000 34.38000 ? 48  ASP A C   1 
ATOM   338  O O   . ASP A 1 46  ? -28.33500 -19.07100 2.22100   1.000 36.04000 ? 48  ASP A O   1 
ATOM   339  C CB  . ASP A 1 46  ? -26.78100 -21.57700 2.67600   1.000 40.23000 ? 48  ASP A CB  1 
ATOM   340  C CG  . ASP A 1 46  ? -27.16800 -23.02000 2.90400   1.000 46.43000 ? 48  ASP A CG  1 
ATOM   341  O OD1 . ASP A 1 46  ? -28.26900 -23.41700 2.46000   1.000 46.75000 ? 48  ASP A OD1 1 
ATOM   342  O OD2 . ASP A 1 46  ? -26.36000 -23.75700 3.52800   1.000 41.14000 ? 48  ASP A OD2 1 
ATOM   343  N N   . MET A 1 47  ? -26.61800 -18.72900 0.80900   1.000 39.73000 ? 49  MET A N   1 
ATOM   344  C CA  . MET A 1 47  ? -26.41200 -17.34000 1.21100   1.000 35.92000 ? 49  MET A CA  1 
ATOM   345  C C   . MET A 1 47  ? -27.47000 -16.38400 0.66700   1.000 35.61000 ? 49  MET A C   1 
ATOM   346  O O   . MET A 1 47  ? -27.67800 -15.31800 1.26000   1.000 28.92000 ? 49  MET A O   1 
ATOM   347  C CB  . MET A 1 47  ? -25.01600 -16.87800 0.78500   1.000 38.33000 ? 49  MET A CB  1 
ATOM   348  C CG  . MET A 1 47  ? -23.88700 -17.49200 1.61400   1.000 37.48000 ? 49  MET A CG  1 
ATOM   349  S SD  . MET A 1 47  ? -22.23300 -17.18100 0.94800   1.000 48.84000 ? 49  MET A SD  1 
ATOM   350  C CE  . MET A 1 47  ? -21.20200 -18.00500 2.16800   1.000 36.21000 ? 49  MET A CE  1 
ATOM   351  N N   . LEU A 1 48  ? -28.14100 -16.72800 -0.44000  1.000 33.54000 ? 50  LEU A N   1 
ATOM   352  C CA  . LEU A 1 48  ? -29.08900 -15.78500 -1.03000  1.000 34.62000 ? 50  LEU A CA  1 
ATOM   353  C C   . LEU A 1 48  ? -30.27900 -15.54500 -0.09800  1.000 35.05000 ? 50  LEU A C   1 
ATOM   354  O O   . LEU A 1 48  ? -30.67400 -14.40200 0.13400   1.000 32.55000 ? 50  LEU A O   1 
ATOM   355  C CB  . LEU A 1 48  ? -29.54500 -16.26000 -2.41600  1.000 38.07000 ? 50  LEU A CB  1 
ATOM   356  C CG  . LEU A 1 48  ? -28.40600 -16.23000 -3.45200  1.000 45.41000 ? 50  LEU A CG  1 
ATOM   357  C CD1 . LEU A 1 48  ? -28.62600 -17.11700 -4.68900  1.000 37.82000 ? 50  LEU A CD1 1 
ATOM   358  C CD2 . LEU A 1 48  ? -28.16100 -14.78800 -3.86300  1.000 35.06000 ? 50  LEU A CD2 1 
ATOM   359  N N   . ASN A 1 49  ? -30.82700 -16.59900 0.49200   1.000 36.23000 ? 51  ASN A N   1 
ATOM   360  C CA  . ASN A 1 49  ? -31.83900 -16.44400 1.54400   1.000 35.12000 ? 51  ASN A CA  1 
ATOM   361  C C   . ASN A 1 49  ? -31.71300 -17.59200 2.51600   1.000 34.08000 ? 51  ASN A C   1 
ATOM   362  O O   . ASN A 1 49  ? -32.38700 -18.62400 2.38100   1.000 35.43000 ? 51  ASN A O   1 
ATOM   363  C CB  . ASN A 1 49  ? -33.24200 -16.35900 0.94300   1.000 43.16000 ? 51  ASN A CB  1 
ATOM   364  C CG  . ASN A 1 49  ? -34.24900 -15.86500 1.93900   1.000 46.96000 ? 51  ASN A CG  1 
ATOM   365  O OD1 . ASN A 1 49  ? -35.44500 -16.14200 1.82700   1.000 56.28000 ? 51  ASN A OD1 1 
ATOM   366  N ND2 . ASN A 1 49  ? -33.75600 -15.17300 2.97400   1.000 41.34000 ? 51  ASN A ND2 1 
ATOM   367  N N   . PRO A 1 50  ? -30.88000 -17.48700 3.54300   1.000 30.57000 ? 52  PRO A N   1 
ATOM   368  C CA  . PRO A 1 50  ? -30.66500 -18.64600 4.40200   1.000 24.80000 ? 52  PRO A CA  1 
ATOM   369  C C   . PRO A 1 50  ? -31.80000 -18.79200 5.40200   1.000 25.98000 ? 52  PRO A C   1 
ATOM   370  O O   . PRO A 1 50  ? -32.31400 -17.79900 5.92400   1.000 26.28000 ? 52  PRO A O   1 
ATOM   371  C CB  . PRO A 1 50  ? -29.33100 -18.35600 5.10100   1.000 26.29000 ? 52  PRO A CB  1 
ATOM   372  C CG  . PRO A 1 50  ? -28.99800 -16.94200 4.79800   1.000 28.83000 ? 52  PRO A CG  1 
ATOM   373  C CD  . PRO A 1 50  ? -30.13700 -16.31700 4.04800   1.000 29.03000 ? 52  PRO A CD  1 
ATOM   374  N N   . ASN A 1 51  ? -32.18300 -20.04000 5.66500   1.000 25.77000 ? 53  ASN A N   1 
ATOM   375  C CA  . ASN A 1 51  ? -33.06200 -20.37300 6.78000   1.000 25.40000 ? 53  ASN A CA  1 
ATOM   376  C C   . ASN A 1 51  ? -32.14300 -20.83600 7.90200   1.000 24.03000 ? 53  ASN A C   1 
ATOM   377  O O   . ASN A 1 51  ? -31.83300 -22.02300 8.03200   1.000 20.18000 ? 53  ASN A O   1 
ATOM   378  C CB  . ASN A 1 51  ? -34.08900 -21.44200 6.41100   1.000 28.48000 ? 53  ASN A CB  1 
ATOM   379  C CG  . ASN A 1 51  ? -35.20200 -21.56300 7.45200   1.000 36.80000 ? 53  ASN A CG  1 
ATOM   380  O OD1 . ASN A 1 51  ? -34.98500 -21.32500 8.64800   1.000 32.22000 ? 53  ASN A OD1 1 
ATOM   381  N ND2 . ASN A 1 51  ? -36.40200 -21.90800 6.99700   1.000 40.60000 ? 53  ASN A ND2 1 
ATOM   382  N N   . TYR A 1 52  ? -31.71000 -19.87500 8.72000   1.000 21.84000 ? 54  TYR A N   1 
ATOM   383  C CA  . TYR A 1 52  ? -30.71300 -20.15900 9.75000   1.000 23.56000 ? 54  TYR A CA  1 
ATOM   384  C C   . TYR A 1 52  ? -31.23100 -21.14000 10.79300  1.000 22.84000 ? 54  TYR A C   1 
ATOM   385  O O   . TYR A 1 52  ? -30.47400 -21.98600 11.28200  1.000 21.65000 ? 54  TYR A O   1 
ATOM   386  C CB  . TYR A 1 52  ? -30.27700 -18.86000 10.41600  1.000 17.96000 ? 54  TYR A CB  1 
ATOM   387  C CG  . TYR A 1 52  ? -29.35900 -18.04000 9.55400   1.000 14.71000 ? 54  TYR A CG  1 
ATOM   388  C CD1 . TYR A 1 52  ? -28.04200 -18.42300 9.35500   1.000 15.56000 ? 54  TYR A CD1 1 
ATOM   389  C CD2 . TYR A 1 52  ? -29.81200 -16.88200 8.93500   1.000 18.60000 ? 54  TYR A CD2 1 
ATOM   390  C CE1 . TYR A 1 52  ? -27.18900 -17.66900 8.58000   1.000 18.48000 ? 54  TYR A CE1 1 
ATOM   391  C CE2 . TYR A 1 52  ? -28.96600 -16.11000 8.16200   1.000 18.18000 ? 54  TYR A CE2 1 
ATOM   392  C CZ  . TYR A 1 52  ? -27.65700 -16.50900 7.97900   1.000 20.36000 ? 54  TYR A CZ  1 
ATOM   393  O OH  . TYR A 1 52  ? -26.81000 -15.74700 7.19500   1.000 18.88000 ? 54  TYR A OH  1 
ATOM   394  N N   . GLU A 1 53  ? -32.50400 -21.01400 11.18300  1.000 25.32000 ? 55  GLU A N   1 
ATOM   395  C CA  . GLU A 1 53  ? -33.09700 -22.00400 12.07900  1.000 31.42000 ? 55  GLU A CA  1 
ATOM   396  C C   . GLU A 1 53  ? -32.99600 -23.40100 11.47500  1.000 29.82000 ? 55  GLU A C   1 
ATOM   397  O O   . GLU A 1 53  ? -32.59900 -24.36000 12.14800  1.000 30.29000 ? 55  GLU A O   1 
ATOM   398  C CB  . GLU A 1 53  ? -34.55500 -21.64700 12.36400  1.000 30.66000 ? 55  GLU A CB  1 
ATOM   399  C CG  . GLU A 1 53  ? -34.73400 -20.38000 13.16800  1.000 34.75000 ? 55  GLU A CG  1 
ATOM   400  C CD  . GLU A 1 53  ? -34.68800 -19.11400 12.30800  1.000 35.63000 ? 55  GLU A CD  1 
ATOM   401  O OE1 . GLU A 1 53  ? -34.74300 -18.01000 12.88900  1.000 40.73000 ? 55  GLU A OE1 1 
ATOM   402  O OE2 . GLU A 1 53  ? -34.59500 -19.21300 11.06100  1.000 36.21000 ? 55  GLU A OE2 1 
ATOM   403  N N   . ASP A 1 54  ? -33.31400 -23.51900 10.18500  1.000 30.38000 ? 56  ASP A N   1 
ATOM   404  C CA  . ASP A 1 54  ? -33.21900 -24.80600 9.50100   1.000 35.91000 ? 56  ASP A CA  1 
ATOM   405  C C   . ASP A 1 54  ? -31.77400 -25.26500 9.35800   1.000 35.62000 ? 56  ASP A C   1 
ATOM   406  O O   . ASP A 1 54  ? -31.47400 -26.45900 9.51900   1.000 33.58000 ? 56  ASP A O   1 
ATOM   407  C CB  . ASP A 1 54  ? -33.87400 -24.70800 8.12300   1.000 38.85000 ? 56  ASP A CB  1 
ATOM   408  C CG  . ASP A 1 54  ? -35.33200 -25.13100 8.13000   1.000 44.93000 ? 56  ASP A CG  1 
ATOM   409  O OD1 . ASP A 1 54  ? -36.04800 -24.82900 9.11100   1.000 44.72000 ? 56  ASP A OD1 1 
ATOM   410  O OD2 . ASP A 1 54  ? -35.75600 -25.77000 7.14100   1.000 48.47000 ? 56  ASP A OD2 1 
ATOM   411  N N   . LEU A 1 55  ? -30.86900 -24.34200 9.02200   1.000 25.40000 ? 57  LEU A N   1 
ATOM   412  C CA  . LEU A 1 55  ? -29.46900 -24.71200 8.84600   1.000 25.65000 ? 57  LEU A CA  1 
ATOM   413  C C   . LEU A 1 55  ? -28.85100 -25.15600 10.16200  1.000 25.12000 ? 57  LEU A C   1 
ATOM   414  O O   . LEU A 1 55  ? -28.00800 -26.06000 10.18500  1.000 31.00000 ? 57  LEU A O   1 
ATOM   415  C CB  . LEU A 1 55  ? -28.68500 -23.53800 8.26000   1.000 24.89000 ? 57  LEU A CB  1 
ATOM   416  C CG  . LEU A 1 55  ? -29.00200 -23.25100 6.79500   1.000 30.01000 ? 57  LEU A CG  1 
ATOM   417  C CD1 . LEU A 1 55  ? -28.30500 -21.98500 6.33200   1.000 25.70000 ? 57  LEU A CD1 1 
ATOM   418  C CD2 . LEU A 1 55  ? -28.62100 -24.43500 5.91800   1.000 28.91000 ? 57  LEU A CD2 1 
ATOM   419  N N   . LEU A 1 56  ? -29.25500 -24.53000 11.26700  1.000 26.27000 ? 58  LEU A N   1 
ATOM   420  C CA  . LEU A 1 56  ? -28.68500 -24.85700 12.56600  1.000 25.80000 ? 58  LEU A CA  1 
ATOM   421  C C   . LEU A 1 56  ? -29.22500 -26.17400 13.11200  1.000 29.40000 ? 58  LEU A C   1 
ATOM   422  O O   . LEU A 1 56  ? -28.51700 -26.86600 13.85500  1.000 24.49000 ? 58  LEU A O   1 
ATOM   423  C CB  . LEU A 1 56  ? -28.96500 -23.73100 13.56300  1.000 24.36000 ? 58  LEU A CB  1 
ATOM   424  C CG  . LEU A 1 56  ? -28.19900 -23.77400 14.89100  1.000 27.91000 ? 58  LEU A CG  1 
ATOM   425  C CD1 . LEU A 1 56  ? -26.73900 -23.44700 14.66400  1.000 24.51000 ? 58  LEU A CD1 1 
ATOM   426  C CD2 . LEU A 1 56  ? -28.80400 -22.81900 15.90000  1.000 31.06000 ? 58  LEU A CD2 1 
ATOM   427  N N   . ILE A 1 57  ? -30.47200 -26.52300 12.78000  1.000 31.23000 ? 59  ILE A N   1 
ATOM   428  C CA  . ILE A 1 57  ? -31.03800 -27.78800 13.24600  1.000 32.41000 ? 59  ILE A CA  1 
ATOM   429  C C   . ILE A 1 57  ? -30.21900 -28.95000 12.72300  1.000 27.49000 ? 59  ILE A C   1 
ATOM   430  O O   . ILE A 1 57  ? -30.01400 -29.94700 13.42500  1.000 34.39000 ? 59  ILE A O   1 
ATOM   431  C CB  . ILE A 1 57  ? -32.51900 -27.91100 12.82800  1.000 32.66000 ? 59  ILE A CB  1 
ATOM   432  C CG1 . ILE A 1 57  ? -33.39900 -27.00400 13.68600  1.000 35.59000 ? 59  ILE A CG1 1 
ATOM   433  C CG2 . ILE A 1 57  ? -33.00000 -29.36000 12.93500  1.000 38.27000 ? 59  ILE A CG2 1 
ATOM   434  C CD1 . ILE A 1 57  ? -33.26600 -27.24600 15.16400  1.000 40.90000 ? 59  ILE A CD1 1 
ATOM   435  N N   . ARG A 1 58  ? -29.71600 -28.83200 11.49700  1.000 25.80000 ? 60  ARG A N   1 
ATOM   436  C CA  . ARG A 1 58  ? -28.92600 -29.89700 10.91000  1.000 29.17000 ? 60  ARG A CA  1 
ATOM   437  C C   . ARG A 1 58  ? -27.52500 -29.98800 11.49900  1.000 28.31000 ? 60  ARG A C   1 
ATOM   438  O O   . ARG A 1 58  ? -26.88400 -31.03200 11.35700  1.000 33.29000 ? 60  ARG A O   1 
ATOM   439  C CB  . ARG A 1 58  ? -28.84400 -29.70800 9.39300   1.000 32.96000 ? 60  ARG A CB  1 
ATOM   440  C CG  . ARG A 1 58  ? -29.84800 -30.55700 8.62100   1.000 42.80000 ? 60  ARG A CG  1 
ATOM   441  C CD  . ARG A 1 58  ? -30.41200 -29.83000 7.40800   1.000 47.12000 ? 60  ARG A CD  1 
ATOM   442  N NE  . ARG A 1 58  ? -31.33900 -28.76600 7.78500   1.000 48.55000 ? 60  ARG A NE  1 
ATOM   443  C CZ  . ARG A 1 58  ? -32.64000 -28.95700 7.99300   1.000 46.88000 ? 60  ARG A CZ  1 
ATOM   444  N NH1 . ARG A 1 58  ? -33.15200 -30.17400 7.87300   1.000 52.54000 ? 60  ARG A NH1 1 
ATOM   445  N NH2 . ARG A 1 58  ? -33.43000 -27.94100 8.32900   1.000 44.34000 ? 60  ARG A NH2 1 
ATOM   446  N N   . LYS A 1 59  ? -27.04300 -28.93700 12.15800  1.000 26.93000 ? 61  LYS A N   1 
ATOM   447  C CA  . LYS A 1 59  ? -25.69300 -28.93200 12.70400  1.000 22.34000 ? 61  LYS A CA  1 
ATOM   448  C C   . LYS A 1 59  ? -25.66200 -29.52300 14.10800  1.000 22.14000 ? 61  LYS A C   1 
ATOM   449  O O   . LYS A 1 59  ? -26.62000 -29.41700 14.87800  1.000 23.38000 ? 61  LYS A O   1 
ATOM   450  C CB  . LYS A 1 59  ? -25.12900 -27.50900 12.74700  1.000 25.44000 ? 61  LYS A CB  1 
ATOM   451  C CG  . LYS A 1 59  ? -24.89200 -26.85400 11.38100  1.000 23.48000 ? 61  LYS A CG  1 
ATOM   452  C CD  . LYS A 1 59  ? -23.56500 -27.28100 10.79100  1.000 26.91000 ? 61  LYS A CD  1 
ATOM   453  C CE  . LYS A 1 59  ? -23.42900 -26.85900 9.32900   1.000 33.14000 ? 61  LYS A CE  1 
ATOM   454  N NZ  . LYS A 1 59  ? -24.35600 -27.59400 8.41200   1.000 37.65000 ? 61  LYS A NZ  1 
ATOM   455  N N   . SER A 1 60  ? -24.52800 -30.12600 14.44300  1.000 18.57000 ? 62  SER A N   1 
ATOM   456  C CA  . SER A 1 60  ? -24.27500 -30.64300 15.77200  1.000 19.51000 ? 62  SER A CA  1 
ATOM   457  C C   . SER A 1 60  ? -22.98500 -30.03000 16.29600  1.000 19.68000 ? 62  SER A C   1 
ATOM   458  O O   . SER A 1 60  ? -22.20100 -29.44000 15.54000  1.000 17.31000 ? 62  SER A O   1 
ATOM   459  C CB  . SER A 1 60  ? -24.17300 -32.17400 15.76800  1.000 27.47000 ? 62  SER A CB  1 
ATOM   460  O OG  . SER A 1 60  ? -25.38900 -32.75600 15.32400  1.000 27.60000 ? 62  SER A OG  1 
ATOM   461  N N   . ASN A 1 61  ? -22.77500 -30.18100 17.60700  1.000 18.35000 ? 63  ASN A N   1 
ATOM   462  C CA  . ASN A 1 61  ? -21.54900 -29.68700 18.22700  1.000 19.56000 ? 63  ASN A CA  1 
ATOM   463  C C   . ASN A 1 61  ? -20.31900 -30.13600 17.44900  1.000 17.71000 ? 63  ASN A C   1 
ATOM   464  O O   . ASN A 1 61  ? -19.36100 -29.37300 17.28500  1.000 15.70000 ? 63  ASN A O   1 
ATOM   465  C CB  . ASN A 1 61  ? -21.46100 -30.18000 19.67300  1.000 20.21000 ? 63  ASN A CB  1 
ATOM   466  C CG  . ASN A 1 61  ? -22.44100 -29.49100 20.58900  1.000 19.39000 ? 63  ASN A CG  1 
ATOM   467  O OD1 . ASN A 1 61  ? -22.83600 -28.35000 20.35900  1.000 18.48000 ? 63  ASN A OD1 1 
ATOM   468  N ND2 . ASN A 1 61  ? -22.83200 -30.18200 21.65100  1.000 21.06000 ? 63  ASN A ND2 1 
ATOM   469  N N   . HIS A 1 62  ? -20.33800 -31.36800 16.93100  1.000 17.92000 ? 64  HIS A N   1 
ATOM   470  C CA  . HIS A 1 62  ? -19.15400 -31.91000 16.27900  1.000 19.60000 ? 64  HIS A CA  1 
ATOM   471  C C   . HIS A 1 62  ? -18.97400 -31.40700 14.84900  1.000 17.34000 ? 64  HIS A C   1 
ATOM   472  O O   . HIS A 1 62  ? -18.00500 -31.79900 14.19200  1.000 19.27000 ? 64  HIS A O   1 
ATOM   473  C CB  . HIS A 1 62  ? -19.19100 -33.44900 16.31100  1.000 24.07000 ? 64  HIS A CB  1 
ATOM   474  C CG  . HIS A 1 62  ? -20.34800 -34.04400 15.56900  1.000 27.87000 ? 64  HIS A CG  1 
ATOM   475  N ND1 . HIS A 1 62  ? -20.33000 -34.25600 14.20700  1.000 32.51000 ? 64  HIS A ND1 1 
ATOM   476  C CD2 . HIS A 1 62  ? -21.56200 -34.46400 16.00000  1.000 26.61000 ? 64  HIS A CD2 1 
ATOM   477  C CE1 . HIS A 1 62  ? -21.48400 -34.78100 13.83100  1.000 31.80000 ? 64  HIS A CE1 1 
ATOM   478  N NE2 . HIS A 1 62  ? -22.24800 -34.91800 14.90000  1.000 31.26000 ? 64  HIS A NE2 1 
ATOM   479  N N   . ASN A 1 63  ? -19.86200 -30.54700 14.35000  1.000 16.61000 ? 65  ASN A N   1 
ATOM   480  C CA  . ASN A 1 63  ? -19.63800 -29.88100 13.07600  1.000 16.47000 ? 65  ASN A CA  1 
ATOM   481  C C   . ASN A 1 63  ? -18.86300 -28.56800 13.19200  1.000 14.08000 ? 65  ASN A C   1 
ATOM   482  O O   . ASN A 1 63  ? -18.59800 -27.94300 12.15900  1.000 15.20000 ? 65  ASN A O   1 
ATOM   483  C CB  . ASN A 1 63  ? -20.96900 -29.59200 12.38800  1.000 18.06000 ? 65  ASN A CB  1 
ATOM   484  C CG  . ASN A 1 63  ? -21.73800 -30.85300 12.06300  1.000 21.16000 ? 65  ASN A CG  1 
ATOM   485  O OD1 . ASN A 1 63  ? -22.89100 -30.99100 12.45200  1.000 22.78000 ? 65  ASN A OD1 1 
ATOM   486  N ND2 . ASN A 1 63  ? -21.10100 -31.77700 11.35300  1.000 21.67000 ? 65  ASN A ND2 1 
ATOM   487  N N   . PHE A 1 64  ? -18.50800 -28.12700 14.39800  1.000 11.97000 ? 66  PHE A N   1 
ATOM   488  C CA  . PHE A 1 64  ? -17.86200 -26.82600 14.60100  1.000 10.65000 ? 66  PHE A CA  1 
ATOM   489  C C   . PHE A 1 64  ? -16.41400 -27.01500 15.03400  1.000 11.48000 ? 66  PHE A C   1 
ATOM   490  O O   . PHE A 1 64  ? -16.15300 -27.63600 16.06600  1.000 11.75000 ? 66  PHE A O   1 
ATOM   491  C CB  . PHE A 1 64  ? -18.61600 -26.01200 15.64600  1.000 10.95000 ? 66  PHE A CB  1 
ATOM   492  C CG  . PHE A 1 64  ? -19.98500 -25.60900 15.21000  1.000 12.87000 ? 66  PHE A CG  1 
ATOM   493  C CD1 . PHE A 1 64  ? -20.16400 -24.53000 14.35900  1.000 13.52000 ? 66  PHE A CD1 1 
ATOM   494  C CD2 . PHE A 1 64  ? -21.09500 -26.32900 15.63200  1.000 16.06000 ? 66  PHE A CD2 1 
ATOM   495  C CE1 . PHE A 1 64  ? -21.43900 -24.16100 13.94200  1.000 15.14000 ? 66  PHE A CE1 1 
ATOM   496  C CE2 . PHE A 1 64  ? -22.36600 -25.97000 15.22500  1.000 17.94000 ? 66  PHE A CE2 1 
ATOM   497  C CZ  . PHE A 1 64  ? -22.54300 -24.88200 14.38100  1.000 16.96000 ? 66  PHE A CZ  1 
ATOM   498  N N   . LEU A 1 65  ? -15.48500 -26.45500 14.26500  1.000 10.23000 ? 67  LEU A N   1 
ATOM   499  C CA  . LEU A 1 65  ? -14.05600 -26.52300 14.56700  1.000 11.07000 ? 67  LEU A CA  1 
ATOM   500  C C   . LEU A 1 65  ? -13.63400 -25.18000 15.13800  1.000 11.29000 ? 67  LEU A C   1 
ATOM   501  O O   . LEU A 1 65  ? -13.50100 -24.20600 14.39400  1.000 13.49000 ? 67  LEU A O   1 
ATOM   502  C CB  . LEU A 1 65  ? -13.24300 -26.84400 13.31300  1.000 10.62000 ? 67  LEU A CB  1 
ATOM   503  C CG  . LEU A 1 65  ? -11.71500 -26.80700 13.46600  1.000 13.81000 ? 67  LEU A CG  1 
ATOM   504  C CD1 . LEU A 1 65  ? -11.26700 -27.72000 14.61100  1.000 16.30000 ? 67  LEU A CD1 1 
ATOM   505  C CD2 . LEU A 1 65  ? -11.04500 -27.20900 12.16600  1.000 17.03000 ? 67  LEU A CD2 1 
ATOM   506  N N   . VAL A 1 66  ? -13.41100 -25.12600 16.44800  1.000 10.99000 ? 68  VAL A N   1 
ATOM   507  C CA  . VAL A 1 66  ? -12.93700 -23.91400 17.11300  1.000 10.08000 ? 68  VAL A CA  1 
ATOM   508  C C   . VAL A 1 66  ? -11.48100 -24.12200 17.49800  1.000 10.97000 ? 68  VAL A C   1 
ATOM   509  O O   . VAL A 1 66  ? -11.15500 -25.10000 18.18200  1.000 11.09000 ? 68  VAL A O   1 
ATOM   510  C CB  . VAL A 1 66  ? -13.78100 -23.58300 18.35500  1.000 9.83000  ? 68  VAL A CB  1 
ATOM   511  C CG1 . VAL A 1 66  ? -13.22300 -22.35600 19.06100  1.000 10.20000 ? 68  VAL A CG1 1 
ATOM   512  C CG2 . VAL A 1 66  ? -15.24000 -23.39200 17.98600  1.000 8.91000  ? 68  VAL A CG2 1 
ATOM   513  N N   . GLN A 1 67  ? -10.61000 -23.20000 17.08100  1.000 8.85000  ? 69  GLN A N   1 
ATOM   514  C CA  . GLN A 1 67  ? -9.17700  -23.31400 17.34200  1.000 12.20000 ? 69  GLN A CA  1 
ATOM   515  C C   . GLN A 1 67  ? -8.60300  -22.01300 17.87200  1.000 11.77000 ? 69  GLN A C   1 
ATOM   516  O O   . GLN A 1 67  ? -8.85100  -20.94400 17.30200  1.000 10.67000 ? 69  GLN A O   1 
ATOM   517  C CB  . GLN A 1 67  ? -8.41300  -23.71300 16.07900  1.000 11.88000 ? 69  GLN A CB  1 
ATOM   518  C CG  . GLN A 1 67  ? -8.85600  -25.04800 15.49300  1.000 15.03000 ? 69  GLN A CG  1 
ATOM   519  C CD  . GLN A 1 67  ? -8.30500  -25.25700 14.10700  1.000 15.32000 ? 69  GLN A CD  1 
ATOM   520  O OE1 . GLN A 1 67  ? -8.67500  -24.55300 13.16700  1.000 15.63000 ? 69  GLN A OE1 1 
ATOM   521  N NE2 . GLN A 1 67  ? -7.38800  -26.20100 13.97700  1.000 18.46000 ? 69  GLN A NE2 1 
ATOM   522  N N   . ALA A 1 68  ? -7.81600  -22.11500 18.95000  1.000 13.22000 ? 70  ALA A N   1 
ATOM   523  C CA  . ALA A 1 68  ? -6.91600  -21.04800 19.38300  1.000 16.04000 ? 70  ALA A CA  1 
ATOM   524  C C   . ALA A 1 68  ? -5.54500  -21.36800 18.79600  1.000 19.51000 ? 70  ALA A C   1 
ATOM   525  O O   . ALA A 1 68  ? -4.91000  -22.35100 19.19100  1.000 15.14000 ? 70  ALA A O   1 
ATOM   526  C CB  . ALA A 1 68  ? -6.85400  -20.94700 20.90600  1.000 16.46000 ? 70  ALA A CB  1 
ATOM   527  N N   . GLY A 1 69  ? -5.09400  -20.55100 17.84800  1.000 19.16000 ? 71  GLY A N   1 
ATOM   528  C CA  . GLY A 1 69  ? -3.99200  -20.99600 17.01100  1.000 20.58000 ? 71  GLY A CA  1 
ATOM   529  C C   . GLY A 1 69  ? -4.40600  -22.29500 16.34700  1.000 21.66000 ? 71  GLY A C   1 
ATOM   530  O O   . GLY A 1 69  ? -5.48600  -22.39100 15.75700  1.000 23.14000 ? 71  GLY A O   1 
ATOM   531  N N   . ASN A 1 70  ? -3.57900  -23.33500 16.48100  1.000 21.15000 ? 72  ASN A N   1 
ATOM   532  C CA  . ASN A 1 70  ? -3.92900  -24.65000 15.96100  1.000 21.45000 ? 72  ASN A CA  1 
ATOM   533  C C   . ASN A 1 70  ? -4.44300  -25.59100 17.04000  1.000 22.41000 ? 72  ASN A C   1 
ATOM   534  O O   . ASN A 1 70  ? -4.60700  -26.78700 16.78400  1.000 22.23000 ? 72  ASN A O   1 
ATOM   535  C CB  . ASN A 1 70  ? -2.73300  -25.27300 15.24400  1.000 27.52000 ? 72  ASN A CB  1 
ATOM   536  C CG  . ASN A 1 70  ? -2.49600  -24.64700 13.88900  1.000 26.87000 ? 72  ASN A CG  1 
ATOM   537  O OD1 . ASN A 1 70  ? -3.44400  -24.24300 13.20500  1.000 29.71000 ? 72  ASN A OD1 1 
ATOM   538  N ND2 . ASN A 1 70  ? -1.23300  -24.52900 13.50600  1.000 32.51000 ? 72  ASN A ND2 1 
ATOM   539  N N   . VAL A 1 71  ? -4.72400  -25.07500 18.22700  1.000 17.27000 ? 73  VAL A N   1 
ATOM   540  C CA  . VAL A 1 71  ? -5.20200  -25.88700 19.33700  1.000 14.52000 ? 73  VAL A CA  1 
ATOM   541  C C   . VAL A 1 71  ? -6.72100  -25.92100 19.29200  1.000 15.66000 ? 73  VAL A C   1 
ATOM   542  O O   . VAL A 1 71  ? -7.36600  -24.87600 19.38800  1.000 13.34000 ? 73  VAL A O   1 
ATOM   543  C CB  . VAL A 1 71  ? -4.71000  -25.31600 20.67100  1.000 17.25000 ? 73  VAL A CB  1 
ATOM   544  C CG1 . VAL A 1 71  ? -5.32500  -26.10000 21.82000  1.000 18.63000 ? 73  VAL A CG1 1 
ATOM   545  C CG2 . VAL A 1 71  ? -3.18600  -25.33500 20.70300  1.000 16.93000 ? 73  VAL A CG2 1 
ATOM   546  N N   . GLN A 1 72  ? -7.30100  -27.11300 19.16600  1.000 12.23000 ? 74  GLN A N   1 
ATOM   547  C CA  . GLN A 1 72  ? -8.75400  -27.21400 19.06900  1.000 14.69000 ? 74  GLN A CA  1 
ATOM   548  C C   . GLN A 1 72  ? -9.42500  -27.05700 20.43000  1.000 14.94000 ? 74  GLN A C   1 
ATOM   549  O O   . GLN A 1 72  ? -8.99200  -27.65300 21.41700  1.000 12.42000 ? 74  GLN A O   1 
ATOM   550  C CB  . GLN A 1 72  ? -9.16200  -28.55700 18.46300  1.000 18.11000 ? 74  GLN A CB  1 
ATOM   551  C CG  . GLN A 1 72  ? -10.68200 -28.74000 18.36200  1.000 15.89000 ? 74  GLN A CG  1 
ATOM   552  C CD  . GLN A 1 72  ? -11.06800 -30.05600 17.71000  1.000 15.62000 ? 74  GLN A CD  1 
ATOM   553  O OE1 . GLN A 1 72  ? -10.21400 -30.91000 17.46500  1.000 18.74000 ? 74  GLN A OE1 1 
ATOM   554  N NE2 . GLN A 1 72  ? -12.35300 -30.23400 17.45100  1.000 17.15000 ? 74  GLN A NE2 1 
ATOM   555  N N   . LEU A 1 73  ? -10.50100 -26.26100 20.47500  1.000 9.46000  ? 75  LEU A N   1 
ATOM   556  C CA  . LEU A 1 73  ? -11.37200 -26.16000 21.64500  1.000 12.71000 ? 75  LEU A CA  1 
ATOM   557  C C   . LEU A 1 73  ? -12.63500 -26.96200 21.37000  1.000 14.64000 ? 75  LEU A C   1 
ATOM   558  O O   . LEU A 1 73  ? -13.39700 -26.62000 20.45600  1.000 15.86000 ? 75  LEU A O   1 
ATOM   559  C CB  . LEU A 1 73  ? -11.75300 -24.70800 21.95300  1.000 10.85000 ? 75  LEU A CB  1 
ATOM   560  C CG  . LEU A 1 73  ? -10.61300 -23.69900 22.10400  1.000 16.14000 ? 75  LEU A CG  1 
ATOM   561  C CD1 . LEU A 1 73  ? -11.18800 -22.29300 22.34900  1.000 12.22000 ? 75  LEU A CD1 1 
ATOM   562  C CD2 . LEU A 1 73  ? -9.72200  -24.12200 23.21500  1.000 18.73000 ? 75  LEU A CD2 1 
ATOM   563  N N   . ARG A 1 74  ? -12.88100 -27.99600 22.17400  1.000 12.46000 ? 76  ARG A N   1 
ATOM   564  C CA  . ARG A 1 74  ? -14.05000 -28.84100 21.93900  1.000 19.24000 ? 76  ARG A CA  1 
ATOM   565  C C   . ARG A 1 74  ? -15.33300 -28.07000 22.22200  1.000 14.00000 ? 76  ARG A C   1 
ATOM   566  O O   . ARG A 1 74  ? -15.49200 -27.48300 23.29400  1.000 15.60000 ? 76  ARG A O   1 
ATOM   567  C CB  . ARG A 1 74  ? -13.99800 -30.09800 22.80600  1.000 19.19000 ? 76  ARG A CB  1 
ATOM   568  N N   . VAL A 1 75  ? -16.24800 -28.08800 21.25500  1.000 13.24000 ? 77  VAL A N   1 
ATOM   569  C CA  . VAL A 1 75  ? -17.55400 -27.45100 21.39100  1.000 12.44000 ? 77  VAL A CA  1 
ATOM   570  C C   . VAL A 1 75  ? -18.50800 -28.41100 22.08900  1.000 14.08000 ? 77  VAL A C   1 
ATOM   571  O O   . VAL A 1 75  ? -18.70700 -29.54400 21.63100  1.000 14.99000 ? 77  VAL A O   1 
ATOM   572  C CB  . VAL A 1 75  ? -18.10000 -27.05300 20.00900  1.000 13.12000 ? 77  VAL A CB  1 
ATOM   573  C CG1 . VAL A 1 75  ? -19.53700 -26.56400 20.11800  1.000 11.92000 ? 77  VAL A CG1 1 
ATOM   574  C CG2 . VAL A 1 75  ? -17.18300 -26.02000 19.34400  1.000 11.39000 ? 77  VAL A CG2 1 
ATOM   575  N N   . ILE A 1 76  ? -19.12800 -27.94800 23.17400  1.000 11.44000 ? 78  ILE A N   1 
ATOM   576  C CA  . ILE A 1 76  ? -20.06400 -28.74500 23.95700  1.000 15.29000 ? 78  ILE A CA  1 
ATOM   577  C C   . ILE A 1 76  ? -21.48200 -28.19900 23.91400  1.000 18.66000 ? 78  ILE A C   1 
ATOM   578  O O   . ILE A 1 76  ? -22.36500 -28.74600 24.58400  1.000 17.92000 ? 78  ILE A O   1 
ATOM   579  C CB  . ILE A 1 76  ? -19.59300 -28.88300 25.41600  1.000 16.77000 ? 78  ILE A CB  1 
ATOM   580  C CG1 . ILE A 1 76  ? -19.59200 -27.50800 26.10700  1.000 16.59000 ? 78  ILE A CG1 1 
ATOM   581  C CG2 . ILE A 1 76  ? -18.21300 -29.49500 25.45400  1.000 16.96000 ? 78  ILE A CG2 1 
ATOM   582  C CD1 . ILE A 1 76  ? -19.29600 -27.56600 27.59500  1.000 20.61000 ? 78  ILE A CD1 1 
ATOM   583  N N   . GLY A 1 77  ? -21.73400 -27.14200 23.15300  1.000 13.87000 ? 79  GLY A N   1 
ATOM   584  C CA  . GLY A 1 77  ? -23.08500 -26.63800 23.04600  1.000 15.31000 ? 79  GLY A CA  1 
ATOM   585  C C   . GLY A 1 77  ? -23.10500 -25.53600 22.01900  1.000 14.98000 ? 79  GLY A C   1 
ATOM   586  O O   . GLY A 1 77  ? -22.06800 -24.92700 21.76400  1.000 13.47000 ? 79  GLY A O   1 
ATOM   587  N N   . HIS A 1 78  ? -24.25000 -25.29800 21.39000  1.000 15.22000 ? 80  HIS A N   1 
ATOM   588  C CA  . HIS A 1 78  ? -24.34200 -24.24800 20.38900  1.000 15.53000 ? 80  HIS A CA  1 
ATOM   589  C C   . HIS A 1 78  ? -25.74800 -23.68100 20.43300  1.000 18.60000 ? 80  HIS A C   1 
ATOM   590  O O   . HIS A 1 78  ? -26.71100 -24.41300 20.68100  1.000 15.45000 ? 80  HIS A O   1 
ATOM   591  C CB  . HIS A 1 78  ? -24.01500 -24.75600 18.97600  1.000 13.41000 ? 80  HIS A CB  1 
ATOM   592  C CG  . HIS A 1 78  ? -24.96200 -25.80500 18.47600  1.000 17.72000 ? 80  HIS A CG  1 
ATOM   593  N ND1 . HIS A 1 78  ? -24.81000 -27.14200 18.77700  1.000 19.71000 ? 80  HIS A ND1 1 
ATOM   594  C CD2 . HIS A 1 78  ? -26.07600 -25.71500 17.70900  1.000 20.18000 ? 80  HIS A CD2 1 
ATOM   595  C CE1 . HIS A 1 78  ? -25.79600 -27.83100 18.22500  1.000 24.24000 ? 80  HIS A CE1 1 
ATOM   596  N NE2 . HIS A 1 78  ? -26.57900 -26.98800 17.57300  1.000 21.25000 ? 80  HIS A NE2 1 
ATOM   597  N N   . SER A 1 79  ? -25.84900 -22.37500 20.20800  1.000 13.87000 ? 81  SER A N   1 
ATOM   598  C CA  . SER A 1 79  ? -27.13800 -21.70600 20.12600  1.000 16.19000 ? 81  SER A CA  1 
ATOM   599  C C   . SER A 1 79  ? -26.96400 -20.46800 19.27100  1.000 19.45000 ? 81  SER A C   1 
ATOM   600  O O   . SER A 1 79  ? -25.84100 -20.03400 18.98400  1.000 10.94000 ? 81  SER A O   1 
ATOM   601  C CB  . SER A 1 79  ? -27.69700 -21.32900 21.50400  1.000 15.30000 ? 81  SER A CB  1 
ATOM   602  O OG  . SER A 1 79  ? -26.80500 -20.48900 22.21400  1.000 21.42000 ? 81  SER A OG  1 
ATOM   603  N N   . MET A 1 80  ? -28.09400 -19.91600 18.85200  1.000 16.66000 ? 82  MET A N   1 
ATOM   604  C CA  . MET A 1 80  ? -28.12900 -18.75000 17.99400  1.000 16.41000 ? 82  MET A CA  1 
ATOM   605  C C   . MET A 1 80  ? -28.85600 -17.64800 18.74300  1.000 18.95000 ? 82  MET A C   1 
ATOM   606  O O   . MET A 1 80  ? -29.95600 -17.87300 19.25900  1.000 18.80000 ? 82  MET A O   1 
ATOM   607  C CB  . MET A 1 80  ? -28.83000 -19.10500 16.68700  1.000 21.42000 ? 82  MET A CB  1 
ATOM   608  C CG  . MET A 1 80  ? -29.08000 -17.97700 15.76600  1.000 21.83000 ? 82  MET A CG  1 
ATOM   609  S SD  . MET A 1 80  ? -29.47900 -18.70900 14.18400  1.000 24.95000 ? 82  MET A SD  1 
ATOM   610  C CE  . MET A 1 80  ? -31.16200 -19.28500 14.46200  1.000 23.90000 ? 82  MET A CE  1 
ATOM   611  N N   . GLN A 1 81  ? -28.21600 -16.48500 18.86800  1.000 20.53000 ? 83  GLN A N   1 
ATOM   612  C CA  . GLN A 1 81  ? -28.83700 -15.30000 19.45800  1.000 18.34000 ? 83  GLN A CA  1 
ATOM   613  C C   . GLN A 1 81  ? -28.82700 -14.23600 18.37000  1.000 16.26000 ? 83  GLN A C   1 
ATOM   614  O O   . GLN A 1 81  ? -27.76400 -13.69900 18.03000  1.000 12.00000 ? 83  GLN A O   1 
ATOM   615  C CB  . GLN A 1 81  ? -28.11300 -14.83200 20.71900  1.000 16.88000 ? 83  GLN A CB  1 
ATOM   616  C CG  . GLN A 1 81  ? -28.74200 -13.59500 21.35400  1.000 19.45000 ? 83  GLN A CG  1 
ATOM   617  C CD  . GLN A 1 81  ? -27.99700 -13.09000 22.57200  1.000 25.53000 ? 83  GLN A CD  1 
ATOM   618  O OE1 . GLN A 1 81  ? -26.81800 -13.38800 22.76800  1.000 22.84000 ? 83  GLN A OE1 1 
ATOM   619  N NE2 . GLN A 1 81  ? -28.68800 -12.31700 23.40500  1.000 26.93000 ? 83  GLN A NE2 1 
ATOM   620  N N   . ASN A 1 82  ? -30.00100 -13.97600 17.79300  1.000 16.55000 ? 84  ASN A N   1 
ATOM   621  C CA  . ASN A 1 82  ? -30.11200 -13.10100 16.63400  1.000 14.18000 ? 84  ASN A CA  1 
ATOM   622  C C   . ASN A 1 82  ? -29.13900 -13.57100 15.56000  1.000 17.66000 ? 84  ASN A C   1 
ATOM   623  O O   . ASN A 1 82  ? -29.22300 -14.72500 15.12700  1.000 15.25000 ? 84  ASN A O   1 
ATOM   624  C CB  . ASN A 1 82  ? -29.87500 -11.65500 17.05600  1.000 14.78000 ? 84  ASN A CB  1 
ATOM   625  C CG  . ASN A 1 82  ? -30.84000 -11.22000 18.13800  1.000 22.14000 ? 84  ASN A CG  1 
ATOM   626  O OD1 . ASN A 1 82  ? -32.06300 -11.34300 17.98300  1.000 20.37000 ? 84  ASN A OD1 1 
ATOM   627  N ND2 . ASN A 1 82  ? -30.30500 -10.73900 19.24900  1.000 20.98000 ? 84  ASN A ND2 1 
ATOM   628  N N   . CYS A 1 83  ? -28.19400 -12.72400 15.13700  1.000 12.20000 ? 85  CYS A N   1 
ATOM   629  C CA  . CYS A 1 83  ? -27.30400 -13.09700 14.04200  1.000 13.51000 ? 85  CYS A CA  1 
ATOM   630  C C   . CYS A 1 83  ? -25.93200 -13.57600 14.51300  1.000 11.27000 ? 85  CYS A C   1 
ATOM   631  O O   . CYS A 1 83  ? -24.98900 -13.61700 13.71500  1.000 10.70000 ? 85  CYS A O   1 
ATOM   632  C CB  . CYS A 1 83  ? -27.13300 -11.93300 13.06800  1.000 17.05000 ? 85  CYS A CB  1 
ATOM   633  S SG  . CYS A 1 83  ? -28.70100 -11.33900 12.37300  1.000 17.17000 ? 85  CYS A SG  1 
ATOM   634  N N   . VAL A 1 84  ? -25.78600 -13.92600 15.77800  1.000 11.58000 ? 86  VAL A N   1 
ATOM   635  C CA  . VAL A 1 84  ? -24.51000 -14.44500 16.24900  1.000 9.67000  ? 86  VAL A CA  1 
ATOM   636  C C   . VAL A 1 84  ? -24.71400 -15.85200 16.78100  1.000 13.59000 ? 86  VAL A C   1 
ATOM   637  O O   . VAL A 1 84  ? -25.73300 -16.16500 17.40900  1.000 13.62000 ? 86  VAL A O   1 
ATOM   638  C CB  . VAL A 1 84  ? -23.83700 -13.55300 17.31200  1.000 14.12000 ? 86  VAL A CB  1 
ATOM   639  C CG1 . VAL A 1 84  ? -23.39500 -12.22100 16.69100  1.000 12.68000 ? 86  VAL A CG1 1 
ATOM   640  C CG2 . VAL A 1 84  ? -24.71500 -13.37600 18.52800  1.000 18.99000 ? 86  VAL A CG2 1 
ATOM   641  N N   . LEU A 1 85  ? -23.75100 -16.69800 16.47600  1.000 11.13000 ? 87  LEU A N   1 
ATOM   642  C CA  . LEU A 1 85  ? -23.67700 -18.04700 16.99100  1.000 11.69000 ? 87  LEU A CA  1 
ATOM   643  C C   . LEU A 1 85  ? -22.89700 -18.01300 18.30100  1.000 14.99000 ? 87  LEU A C   1 
ATOM   644  O O   . LEU A 1 85  ? -21.87400 -17.32600 18.41400  1.000 10.56000 ? 87  LEU A O   1 
ATOM   645  C CB  . LEU A 1 85  ? -22.99200 -18.92600 15.95100  1.000 11.63000 ? 87  LEU A CB  1 
ATOM   646  C CG  . LEU A 1 85  ? -22.87000 -20.43400 16.11400  1.000 19.62000 ? 87  LEU A CG  1 
ATOM   647  C CD1 . LEU A 1 85  ? -24.23100 -21.10200 16.11800  1.000 19.35000 ? 87  LEU A CD1 1 
ATOM   648  C CD2 . LEU A 1 85  ? -22.00000 -20.96200 14.97600  1.000 18.25000 ? 87  LEU A CD2 1 
ATOM   649  N N   . LYS A 1 86  ? -23.41300 -18.69900 19.30800  1.000 11.89000 ? 88  LYS A N   1 
ATOM   650  C CA  . LYS A 1 86  ? -22.71300 -18.85800 20.57000  1.000 13.41000 ? 88  LYS A CA  1 
ATOM   651  C C   . LYS A 1 86  ? -22.32800 -20.31800 20.70000  1.000 13.38000 ? 88  LYS A C   1 
ATOM   652  O O   . LYS A 1 86  ? -23.20700 -21.18600 20.73800  1.000 11.70000 ? 88  LYS A O   1 
ATOM   653  C CB  . LYS A 1 86  ? -23.57900 -18.43000 21.74800  1.000 15.05000 ? 88  LYS A CB  1 
ATOM   654  C CG  . LYS A 1 86  ? -23.85000 -16.94800 21.78600  1.000 16.79000 ? 88  LYS A CG  1 
ATOM   655  C CD  . LYS A 1 86  ? -25.24300 -16.69300 22.31500  1.000 24.23000 ? 88  LYS A CD  1 
ATOM   656  C CE  . LYS A 1 86  ? -25.26000 -16.70500 23.81900  1.000 30.65000 ? 88  LYS A CE  1 
ATOM   657  N NZ  . LYS A 1 86  ? -26.42900 -15.92900 24.32800  1.000 36.33000 ? 88  LYS A NZ  1 
ATOM   658  N N   . LEU A 1 87  ? -21.02800 -20.58000 20.74000  1.000 8.94000  ? 89  LEU A N   1 
ATOM   659  C CA  . LEU A 1 87  ? -20.50600 -21.93100 20.84400  1.000 11.15000 ? 89  LEU A CA  1 
ATOM   660  C C   . LEU A 1 87  ? -19.93300 -22.08700 22.24500  1.000 13.88000 ? 89  LEU A C   1 
ATOM   661  O O   . LEU A 1 87  ? -18.95300 -21.42000 22.60500  1.000 12.29000 ? 89  LEU A O   1 
ATOM   662  C CB  . LEU A 1 87  ? -19.46300 -22.19800 19.76500  1.000 11.27000 ? 89  LEU A CB  1 
ATOM   663  C CG  . LEU A 1 87  ? -19.93300 -22.02700 18.31700  1.000 11.71000 ? 89  LEU A CG  1 
ATOM   664  C CD1 . LEU A 1 87  ? -18.79000 -22.39900 17.37800  1.000 15.94000 ? 89  LEU A CD1 1 
ATOM   665  C CD2 . LEU A 1 87  ? -21.15100 -22.89300 18.05000  1.000 11.19000 ? 89  LEU A CD2 1 
ATOM   666  N N   . ARG A 1 88  ? -20.57500 -22.94900 23.03400  1.000 10.82000 ? 90  ARG A N   1 
ATOM   667  C CA  . ARG A 1 88  ? -20.04100 -23.25500 24.38200  1.000 12.50000 ? 90  ARG A CA  1 
ATOM   668  C C   . ARG A 1 88  ? -18.88400 -24.23300 24.18800  1.000 12.54000 ? 90  ARG A C   1 
ATOM   669  O O   . ARG A 1 88  ? -19.07300 -25.22500 23.47200  1.000 11.99000 ? 90  ARG A O   1 
ATOM   670  C CB  . ARG A 1 88  ? -21.12400 -23.82100 25.30300  1.000 30.00000 ? 90  ARG A CB  1 
ATOM   671  C CG  . ARG A 1 88  ? -20.68400 -23.93700 26.75600  1.000 30.00000 ? 90  ARG A CG  1 
ATOM   672  C CD  . ARG A 1 88  ? -21.83300 -23.91800 27.74400  1.000 30.00000 ? 90  ARG A CD  1 
ATOM   673  N NE  . ARG A 1 88  ? -21.34900 -23.99100 29.11600  1.000 30.00000 ? 90  ARG A NE  1 
ATOM   674  C CZ  . ARG A 1 88  ? -21.36500 -25.08500 29.86700  1.000 30.00000 ? 90  ARG A CZ  1 
ATOM   675  N NH1 . ARG A 1 88  ? -20.89500 -25.04600 31.10200  1.000 30.00000 ? 90  ARG A NH1 1 
ATOM   676  N NH2 . ARG A 1 88  ? -21.86600 -26.21000 29.39000  1.000 30.00000 ? 90  ARG A NH2 1 
ATOM   677  N N   . VAL A 1 89  ? -17.73400 -23.93700 24.77900  1.000 11.93000 ? 91  VAL A N   1 
ATOM   678  C CA  . VAL A 1 89  ? -16.55200 -24.77000 24.63800  1.000 10.95000 ? 91  VAL A CA  1 
ATOM   679  C C   . VAL A 1 89  ? -16.16300 -25.29500 26.01600  1.000 12.01000 ? 91  VAL A C   1 
ATOM   680  O O   . VAL A 1 89  ? -16.62200 -24.80900 27.04400  1.000 12.41000 ? 91  VAL A O   1 
ATOM   681  C CB  . VAL A 1 89  ? -15.38000 -24.02100 23.98000  1.000 12.51000 ? 91  VAL A CB  1 
ATOM   682  C CG1 . VAL A 1 89  ? -15.74500 -23.62800 22.56000  1.000 10.12000 ? 91  VAL A CG1 1 
ATOM   683  C CG2 . VAL A 1 89  ? -15.01400 -22.79700 24.79300  1.000 9.43000  ? 91  VAL A CG2 1 
ATOM   684  N N   . ASP A 1 90  ? -15.28800 -26.29400 26.02300  1.000 15.41000 ? 92  ASP A N   1 
ATOM   685  C CA  . ASP A 1 90  ? -15.00600 -26.97900 27.27500  1.000 16.76000 ? 92  ASP A CA  1 
ATOM   686  C C   . ASP A 1 90  ? -13.93300 -26.28900 28.10700  1.000 15.78000 ? 92  ASP A C   1 
ATOM   687  O O   . ASP A 1 90  ? -13.64700 -26.76100 29.21200  1.000 16.70000 ? 92  ASP A O   1 
ATOM   688  C CB  . ASP A 1 90  ? -14.61000 -28.43100 27.00200  1.000 23.02000 ? 92  ASP A CB  1 
ATOM   689  C CG  . ASP A 1 90  ? -13.32900 -28.55700 26.20200  1.000 24.86000 ? 92  ASP A CG  1 
ATOM   690  O OD1 . ASP A 1 90  ? -12.82700 -27.54600 25.65100  1.000 27.58000 ? 92  ASP A OD1 1 
ATOM   691  O OD2 . ASP A 1 90  ? -12.82000 -29.69900 26.11900  1.000 33.12000 ? 92  ASP A OD2 1 
ATOM   692  N N   . THR A 1 91  ? -13.36300 -25.18400 27.62500  1.000 11.81000 ? 93  THR A N   1 
ATOM   693  C CA  . THR A 1 91  ? -12.28600 -24.47400 28.31300  1.000 11.72000 ? 93  THR A CA  1 
ATOM   694  C C   . THR A 1 91  ? -12.67900 -23.01100 28.48200  1.000 12.35000 ? 93  THR A C   1 
ATOM   695  O O   . THR A 1 91  ? -13.04900 -22.35300 27.50300  1.000 11.38000 ? 93  THR A O   1 
ATOM   696  C CB  . THR A 1 91  ? -10.97300 -24.56200 27.52000  1.000 13.50000 ? 93  THR A CB  1 
ATOM   697  O OG1 . THR A 1 91  ? -10.69800 -25.93000 27.19000  1.000 16.14000 ? 93  THR A OG1 1 
ATOM   698  C CG2 . THR A 1 91  ? -9.80300  -23.97600 28.32600  1.000 10.23000 ? 93  THR A CG2 1 
ATOM   699  N N   . ALA A 1 92  ? -12.61300 -22.51800 29.71500  1.000 13.79000 ? 94  ALA A N   1 
ATOM   700  C CA  . ALA A 1 92  ? -12.77200 -21.09500 29.98200  1.000 12.67000 ? 94  ALA A CA  1 
ATOM   701  C C   . ALA A 1 92  ? -11.48700 -20.37000 29.59300  1.000 10.33000 ? 94  ALA A C   1 
ATOM   702  O O   . ALA A 1 92  ? -10.39300 -20.79500 29.97200  1.000 10.37000 ? 94  ALA A O   1 
ATOM   703  C CB  . ALA A 1 92  ? -13.09700 -20.86500 31.45900  1.000 12.86000 ? 94  ALA A CB  1 
ATOM   704  N N   . ASN A 1 93  ? -11.61000 -19.31700 28.79600  1.000 8.31000  ? 95  ASN A N   1 
ATOM   705  C CA  . ASN A 1 93  ? -10.42000 -18.59900 28.32900  1.000 8.96000  ? 95  ASN A CA  1 
ATOM   706  C C   . ASN A 1 93  ? -9.71000  -17.94100 29.50800  1.000 8.25000  ? 95  ASN A C   1 
ATOM   707  O O   . ASN A 1 93  ? -10.26700 -17.01000 30.10800  1.000 9.23000  ? 95  ASN A O   1 
ATOM   708  C CB  . ASN A 1 93  ? -10.80800 -17.54300 27.27400  1.000 8.43000  ? 95  ASN A CB  1 
ATOM   709  C CG  . ASN A 1 93  ? -9.59300  -16.81900 26.69400  1.000 9.78000  ? 95  ASN A CG  1 
ATOM   710  O OD1 . ASN A 1 93  ? -8.46000  -17.05700 27.10600  1.000 10.33000 ? 95  ASN A OD1 1 
ATOM   711  N ND2 . ASN A 1 93  ? -9.83100  -15.93000 25.72900  1.000 8.60000  ? 95  ASN A ND2 1 
ATOM   712  N N   . PRO A 1 94  ? -8.48800  -18.36500 29.86300  1.000 9.10000  ? 96  PRO A N   1 
ATOM   713  C CA  . PRO A 1 94  ? -7.78500  -17.72500 30.97700  1.000 8.89000  ? 96  PRO A CA  1 
ATOM   714  C C   . PRO A 1 94  ? -7.43700  -16.27100 30.71800  1.000 12.12000 ? 96  PRO A C   1 
ATOM   715  O O   . PRO A 1 94  ? -7.15700  -15.55000 31.67800  1.000 12.51000 ? 96  PRO A O   1 
ATOM   716  C CB  . PRO A 1 94  ? -6.50900  -18.57700 31.12600  1.000 11.77000 ? 96  PRO A CB  1 
ATOM   717  C CG  . PRO A 1 94  ? -6.80300  -19.84900 30.39900  1.000 15.12000 ? 96  PRO A CG  1 
ATOM   718  C CD  . PRO A 1 94  ? -7.67800  -19.43200 29.25500  1.000 8.15000  ? 96  PRO A CD  1 
ATOM   719  N N   . LYS A 1 95  ? -7.42900  -15.82500 29.46500  1.000 7.94000  ? 97  LYS A N   1 
ATOM   720  C CA  . LYS A 1 95  ? -7.12800  -14.43400 29.12800  1.000 10.57000 ? 97  LYS A CA  1 
ATOM   721  C C   . LYS A 1 95  ? -8.37200  -13.54800 29.04900  1.000 12.13000 ? 97  LYS A C   1 
ATOM   722  O O   . LYS A 1 95  ? -8.27200  -12.39800 28.60100  1.000 11.23000 ? 97  LYS A O   1 
ATOM   723  C CB  . LYS A 1 95  ? -6.36400  -14.37200 27.80200  1.000 12.73000 ? 97  LYS A CB  1 
ATOM   724  C CG  . LYS A 1 95  ? -5.02900  -15.11500 27.81900  1.000 16.62000 ? 97  LYS A CG  1 
ATOM   725  C CD  . LYS A 1 95  ? -4.43500  -15.19100 26.41400  1.000 23.58000 ? 97  LYS A CD  1 
ATOM   726  C CE  . LYS A 1 95  ? -2.98800  -15.68400 26.43100  1.000 28.38000 ? 97  LYS A CE  1 
ATOM   727  N NZ  . LYS A 1 95  ? -2.16400  -14.94800 27.44300  1.000 24.84000 ? 97  LYS A NZ  1 
ATOM   728  N N   . THR A 1 96  ? -9.53100  -14.05400 29.45700  1.000 11.07000 ? 98  THR A N   1 
ATOM   729  C CA  . THR A 1 96  ? -10.76600 -13.27900 29.39600  1.000 11.44000 ? 98  THR A CA  1 
ATOM   730  C C   . THR A 1 96  ? -10.60500 -11.99700 30.20400  1.000 13.29000 ? 98  THR A C   1 
ATOM   731  O O   . THR A 1 96  ? -10.32400 -12.07600 31.41000  1.000 11.03000 ? 98  THR A O   1 
ATOM   732  C CB  . THR A 1 96  ? -11.95100 -14.07500 29.95500  1.000 12.80000 ? 98  THR A CB  1 
ATOM   733  O OG1 . THR A 1 96  ? -12.08700 -15.32000 29.26300  1.000 12.22000 ? 98  THR A OG1 1 
ATOM   734  C CG2 . THR A 1 96  ? -13.26400 -13.27000 29.78700  1.000 14.49000 ? 98  THR A CG2 1 
ATOM   735  N N   . PRO A 1 97  ? -10.76200 -10.81800 29.60200  1.000 11.12000 ? 99  PRO A N   1 
ATOM   736  C CA  . PRO A 1 97  ? -10.70500 -9.57300  30.37100  1.000 14.36000 ? 99  PRO A CA  1 
ATOM   737  C C   . PRO A 1 97  ? -12.03500 -9.30500  31.06500  1.000 14.38000 ? 99  PRO A C   1 
ATOM   738  O O   . PRO A 1 97  ? -13.05300 -9.93700  30.78700  1.000 12.34000 ? 99  PRO A O   1 
ATOM   739  C CB  . PRO A 1 97  ? -10.43300 -8.52600  29.29100  1.000 15.16000 ? 99  PRO A CB  1 
ATOM   740  C CG  . PRO A 1 97  ? -11.23800 -9.04800  28.11500  1.000 13.61000 ? 99  PRO A CG  1 
ATOM   741  C CD  . PRO A 1 97  ? -11.12600 -10.56800 28.19400  1.000 12.81000 ? 99  PRO A CD  1 
ATOM   742  N N   . LYS A 1 98  ? -12.01700 -8.34500  31.99800  1.000 13.99000 ? 100 LYS A N   1 
ATOM   743  C CA  . LYS A 1 98  ? -13.28100 -7.77500  32.42700  1.000 13.32000 ? 100 LYS A CA  1 
ATOM   744  C C   . LYS A 1 98  ? -13.93100 -7.17400  31.19300  1.000 12.61000 ? 100 LYS A C   1 
ATOM   745  O O   . LYS A 1 98  ? -13.25900 -6.49800  30.41300  1.000 10.89000 ? 100 LYS A O   1 
ATOM   746  C CB  . LYS A 1 98  ? -13.07600 -6.70200  33.50400  1.000 17.47000 ? 100 LYS A CB  1 
ATOM   747  N N   . TYR A 1 99  ? -15.20800 -7.47100  30.96800  1.000 11.24000 ? 101 TYR A N   1 
ATOM   748  C CA  . TYR A 1 99  ? -15.81400 -7.01300  29.72300  1.000 12.68000 ? 101 TYR A CA  1 
ATOM   749  C C   . TYR A 1 99  ? -17.30500 -6.75600  29.89700  1.000 16.06000 ? 101 TYR A C   1 
ATOM   750  O O   . TYR A 1 99  ? -17.93100 -7.17100  30.87400  1.000 15.26000 ? 101 TYR A O   1 
ATOM   751  C CB  . TYR A 1 99  ? -15.58300 -8.02000  28.58200  1.000 13.97000 ? 101 TYR A CB  1 
ATOM   752  C CG  . TYR A 1 99  ? -16.46300 -9.24700  28.67000  1.000 14.61000 ? 101 TYR A CG  1 
ATOM   753  C CD1 . TYR A 1 99  ? -17.73400 -9.27200  28.09000  1.000 14.42000 ? 101 TYR A CD1 1 
ATOM   754  C CD2 . TYR A 1 99  ? -16.03400 -10.37500 29.35800  1.000 15.61000 ? 101 TYR A CD2 1 
ATOM   755  C CE1 . TYR A 1 99  ? -18.54800 -10.40500 28.18500  1.000 16.49000 ? 101 TYR A CE1 1 
ATOM   756  C CE2 . TYR A 1 99  ? -16.83400 -11.50700 29.45100  1.000 20.51000 ? 101 TYR A CE2 1 
ATOM   757  C CZ  . TYR A 1 99  ? -18.08200 -11.51600 28.86200  1.000 18.48000 ? 101 TYR A CZ  1 
ATOM   758  O OH  . TYR A 1 99  ? -18.86100 -12.64800 28.97200  1.000 25.98000 ? 101 TYR A OH  1 
ATOM   759  N N   . LYS A 1 100 ? -17.86600 -6.06700  28.90600  1.000 12.03000 ? 102 LYS A N   1 
ATOM   760  C CA  . LYS A 1 100 ? -19.30000 -5.93800  28.77300  1.000 15.87000 ? 102 LYS A CA  1 
ATOM   761  C C   . LYS A 1 100 ? -19.62700 -5.82300  27.29200  1.000 13.36000 ? 102 LYS A C   1 
ATOM   762  O O   . LYS A 1 100 ? -18.76100 -5.53600  26.45400  1.000 11.04000 ? 102 LYS A O   1 
ATOM   763  C CB  . LYS A 1 100 ? -19.85100 -4.74200  29.56900  1.000 23.32000 ? 102 LYS A CB  1 
ATOM   764  C CG  . LYS A 1 100 ? -19.36200 -3.38400  29.10700  1.000 25.58000 ? 102 LYS A CG  1 
ATOM   765  C CD  . LYS A 1 100 ? -19.81600 -2.25500  30.05800  1.000 29.34000 ? 102 LYS A CD  1 
ATOM   766  C CE  . LYS A 1 100 ? -19.27400 -2.45900  31.47100  1.000 37.27000 ? 102 LYS A CE  1 
ATOM   767  N NZ  . LYS A 1 100 ? -18.98000 -1.17200  32.18700  1.000 46.42000 ? 102 LYS A NZ  1 
ATOM   768  N N   . PHE A 1 101 ? -20.87800 -6.10300  26.97700  1.000 9.94000  ? 103 PHE A N   1 
ATOM   769  C CA  . PHE A 1 101 ? -21.40300 -5.97700  25.62500  1.000 11.36000 ? 103 PHE A CA  1 
ATOM   770  C C   . PHE A 1 101 ? -22.23300 -4.70300  25.59100  1.000 16.43000 ? 103 PHE A C   1 
ATOM   771  O O   . PHE A 1 101 ? -23.13300 -4.53000  26.41500  1.000 14.44000 ? 103 PHE A O   1 
ATOM   772  C CB  . PHE A 1 101 ? -22.27100 -7.17200  25.24400  1.000 12.37000 ? 103 PHE A CB  1 
ATOM   773  C CG  . PHE A 1 101 ? -21.50200 -8.45100  25.02700  1.000 12.27000 ? 103 PHE A CG  1 
ATOM   774  C CD1 . PHE A 1 101 ? -20.12300 -8.43900  24.89100  1.000 9.31000  ? 103 PHE A CD1 1 
ATOM   775  C CD2 . PHE A 1 101 ? -22.17600 -9.66000  24.93300  1.000 11.94000 ? 103 PHE A CD2 1 
ATOM   776  C CE1 . PHE A 1 101 ? -19.41400 -9.63000  24.67600  1.000 13.56000 ? 103 PHE A CE1 1 
ATOM   777  C CE2 . PHE A 1 101 ? -21.48200 -10.83800 24.72400  1.000 11.01000 ? 103 PHE A CE2 1 
ATOM   778  C CZ  . PHE A 1 101 ? -20.10000 -10.82100 24.59500  1.000 12.52000 ? 103 PHE A CZ  1 
ATOM   779  N N   . VAL A 1 102 ? -21.91900 -3.80600  24.66900  1.000 14.42000 ? 104 VAL A N   1 
ATOM   780  C CA  . VAL A 1 102 ? -22.64000 -2.54200  24.58800  1.000 14.38000 ? 104 VAL A CA  1 
ATOM   781  C C   . VAL A 1 102 ? -23.04000 -2.29700  23.14900  1.000 16.52000 ? 104 VAL A C   1 
ATOM   782  O O   . VAL A 1 102 ? -22.34600 -2.69400  22.20800  1.000 14.52000 ? 104 VAL A O   1 
ATOM   783  C CB  . VAL A 1 102 ? -21.82600 -1.34200  25.10900  1.000 18.20000 ? 104 VAL A CB  1 
ATOM   784  C CG1 . VAL A 1 102 ? -21.24000 -1.62400  26.48900  1.000 18.62000 ? 104 VAL A CG1 1 
ATOM   785  C CG2 . VAL A 1 102 ? -20.74200 -0.97900  24.12000  1.000 22.25000 ? 104 VAL A CG2 1 
ATOM   786  N N   . ARG A 1 103 ? -24.16200 -1.61500  22.98600  1.000 14.43000 ? 105 ARG A N   1 
ATOM   787  C CA  . ARG A 1 103 ? -24.64500 -1.20200  21.68400  1.000 12.48000 ? 105 ARG A CA  1 
ATOM   788  C C   . ARG A 1 103 ? -24.35200 0.28400   21.55100  1.000 16.87000 ? 105 ARG A C   1 
ATOM   789  O O   . ARG A 1 103 ? -24.83700 1.08600   22.35600  1.000 14.61000 ? 105 ARG A O   1 
ATOM   790  C CB  . ARG A 1 103 ? -26.14300 -1.47400  21.54100  1.000 12.55000 ? 105 ARG A CB  1 
ATOM   791  C CG  . ARG A 1 103 ? -26.66200 -1.30100  20.11900  1.000 15.11000 ? 105 ARG A CG  1 
ATOM   792  C CD  . ARG A 1 103 ? -28.07200 -1.84200  19.93700  1.000 18.84000 ? 105 ARG A CD  1 
ATOM   793  N NE  . ARG A 1 103 ? -28.58700 -1.50100  18.61400  1.000 15.25000 ? 105 ARG A NE  1 
ATOM   794  C CZ  . ARG A 1 103 ? -28.31000 -2.18800  17.50800  1.000 15.27000 ? 105 ARG A CZ  1 
ATOM   795  N NH1 . ARG A 1 103 ? -27.53200 -3.26200  17.57200  1.000 15.05000 ? 105 ARG A NH1 1 
ATOM   796  N NH2 . ARG A 1 103 ? -28.80800 -1.81100  16.34000  1.000 17.56000 ? 105 ARG A NH2 1 
ATOM   797  N N   . ILE A 1 104 ? -23.54800 0.65600   20.56000  1.000 13.12000 ? 106 ILE A N   1 
ATOM   798  C CA  . ILE A 1 104 ? -23.16800 2.06500   20.47000  1.000 17.29000 ? 106 ILE A CA  1 
ATOM   799  C C   . ILE A 1 104 ? -24.16600 2.83100   19.61000  1.000 18.20000 ? 106 ILE A C   1 
ATOM   800  O O   . ILE A 1 104 ? -24.96300 2.23700   18.87700  1.000 14.54000 ? 106 ILE A O   1 
ATOM   801  C CB  . ILE A 1 104 ? -21.74600 2.23700   19.92400  1.000 16.77000 ? 106 ILE A CB  1 
ATOM   802  C CG1 . ILE A 1 104 ? -21.61400 1.48900   18.59600  1.000 15.17000 ? 106 ILE A CG1 1 
ATOM   803  C CG2 . ILE A 1 104 ? -20.72300 1.77800   20.97000  1.000 17.92000 ? 106 ILE A CG2 1 
ATOM   804  C CD1 . ILE A 1 104 ? -20.57400 2.05100   17.68200  1.000 17.32000 ? 106 ILE A CD1 1 
ATOM   805  N N   . GLN A 1 105 ? -24.12200 4.16200   19.70100  1.000 20.29000 ? 107 GLN A N   1 
ATOM   806  C CA  . GLN A 1 105 ? -24.90500 5.07800   18.88900  1.000 20.39000 ? 107 GLN A CA  1 
ATOM   807  C C   . GLN A 1 105 ? -24.11100 5.51900   17.66900  1.000 18.43000 ? 107 GLN A C   1 
ATOM   808  O O   . GLN A 1 105 ? -22.87300 5.51700   17.69100  1.000 15.22000 ? 107 GLN A O   1 
ATOM   809  C CB  . GLN A 1 105 ? -25.29000 6.30700   19.71600  1.000 20.21000 ? 107 GLN A CB  1 
ATOM   810  C CG  . GLN A 1 105 ? -26.55200 6.14200   20.54500  1.000 28.88000 ? 107 GLN A CG  1 
ATOM   811  C CD  . GLN A 1 105 ? -27.75100 5.66000   19.71700  1.000 27.84000 ? 107 GLN A CD  1 
ATOM   812  O OE1 . GLN A 1 105 ? -28.05700 4.46800   19.69900  1.000 30.54000 ? 107 GLN A OE1 1 
ATOM   813  N NE2 . GLN A 1 105 ? -28.43900 6.58700   19.05100  1.000 25.79000 ? 107 GLN A NE2 1 
ATOM   814  N N   . PRO A 1 106 ? -24.79400 5.93900   16.59900  1.000 22.09000 ? 108 PRO A N   1 
ATOM   815  C CA  . PRO A 1 106 ? -24.08900 6.57600   15.48200  1.000 17.96000 ? 108 PRO A CA  1 
ATOM   816  C C   . PRO A 1 106 ? -23.23400 7.71800   15.99500  1.000 16.50000 ? 108 PRO A C   1 
ATOM   817  O O   . PRO A 1 106 ? -23.62600 8.44800   16.90500  1.000 17.58000 ? 108 PRO A O   1 
ATOM   818  C CB  . PRO A 1 106 ? -25.22200 7.08900   14.58100  1.000 20.18000 ? 108 PRO A CB  1 
ATOM   819  C CG  . PRO A 1 106 ? -26.39600 6.26500   14.92600  1.000 18.93000 ? 108 PRO A CG  1 
ATOM   820  C CD  . PRO A 1 106 ? -26.25500 5.88900   16.37800  1.000 20.72000 ? 108 PRO A CD  1 
ATOM   821  N N   . GLY A 1 107 ? -22.04900 7.86300   15.41000  1.000 18.33000 ? 109 GLY A N   1 
ATOM   822  C CA  . GLY A 1 107 ? -21.09600 8.86200   15.82600  1.000 12.33000 ? 109 GLY A CA  1 
ATOM   823  C C   . GLY A 1 107 ? -20.06000 8.35000   16.80700  1.000 15.90000 ? 109 GLY A C   1 
ATOM   824  O O   . GLY A 1 107 ? -18.94800 8.88700   16.85200  1.000 15.22000 ? 109 GLY A O   1 
ATOM   825  N N   . GLN A 1 108 ? -20.38900 7.32100   17.58800  1.000 16.55000 ? 110 GLN A N   1 
ATOM   826  C CA  . GLN A 1 108 ? -19.41600 6.79600   18.53500  1.000 13.36000 ? 110 GLN A CA  1 
ATOM   827  C C   . GLN A 1 108 ? -18.30300 6.08600   17.78100  1.000 13.13000 ? 110 GLN A C   1 
ATOM   828  O O   . GLN A 1 108 ? -18.50900 5.52400   16.70200  1.000 14.81000 ? 110 GLN A O   1 
ATOM   829  C CB  . GLN A 1 108 ? -20.06800 5.83900   19.53500  1.000 15.06000 ? 110 GLN A CB  1 
ATOM   830  C CG  . GLN A 1 108 ? -21.13000 6.49500   20.41100  1.000 21.05000 ? 110 GLN A CG  1 
ATOM   831  C CD  . GLN A 1 108 ? -21.51700 5.63500   21.61300  1.000 28.43000 ? 110 GLN A CD  1 
ATOM   832  O OE1 . GLN A 1 108 ? -22.61900 5.09200   21.67300  1.000 23.46000 ? 110 GLN A OE1 1 
ATOM   833  N NE2 . GLN A 1 108 ? -20.60500 5.51300   22.57300  1.000 32.18000 ? 110 GLN A NE2 1 
ATOM   834  N N   . THR A 1 109 ? -17.10400 6.15400   18.33400  1.000 12.45000 ? 111 THR A N   1 
ATOM   835  C CA  . THR A 1 109 ? -15.96500 5.50600   17.71500  1.000 13.64000 ? 111 THR A CA  1 
ATOM   836  C C   . THR A 1 109 ? -15.56700 4.29200   18.53600  1.000 12.79000 ? 111 THR A C   1 
ATOM   837  O O   . THR A 1 109 ? -15.94400 4.14800   19.70000  1.000 13.11000 ? 111 THR A O   1 
ATOM   838  C CB  . THR A 1 109 ? -14.77100 6.45100   17.58400  1.000 17.41000 ? 111 THR A CB  1 
ATOM   839  O OG1 . THR A 1 109 ? -14.40000 6.92800   18.88500  1.000 14.92000 ? 111 THR A OG1 1 
ATOM   840  C CG2 . THR A 1 109 ? -15.11000 7.63100   16.62900  1.000 16.04000 ? 111 THR A CG2 1 
ATOM   841  N N   . PHE A 1 110 ? -14.77700 3.43500   17.90800  1.000 11.64000 ? 112 PHE A N   1 
ATOM   842  C CA  . PHE A 1 110 ? -14.24900 2.25200   18.56900  1.000 11.93000 ? 112 PHE A CA  1 
ATOM   843  C C   . PHE A 1 110 ? -13.02900 1.79500   17.78800  1.000 12.36000 ? 112 PHE A C   1 
ATOM   844  O O   . PHE A 1 110 ? -12.83700 2.17600   16.62800  1.000 13.26000 ? 112 PHE A O   1 
ATOM   845  C CB  . PHE A 1 110 ? -15.30100 1.14300   18.64400  1.000 9.80000  ? 112 PHE A CB  1 
ATOM   846  C CG  . PHE A 1 110 ? -15.98700 0.85900   17.32100  1.000 13.31000 ? 112 PHE A CG  1 
ATOM   847  C CD1 . PHE A 1 110 ? -17.07600 1.61600   16.90900  1.000 14.40000 ? 112 PHE A CD1 1 
ATOM   848  C CD2 . PHE A 1 110 ? -15.55000 -0.17400  16.49700  1.000 12.09000 ? 112 PHE A CD2 1 
ATOM   849  C CE1 . PHE A 1 110 ? -17.71000 1.35200   15.69800  1.000 16.39000 ? 112 PHE A CE1 1 
ATOM   850  C CE2 . PHE A 1 110 ? -16.19100 -0.45000  15.28600  1.000 14.34000 ? 112 PHE A CE2 1 
ATOM   851  C CZ  . PHE A 1 110 ? -17.26900 0.32800   14.88800  1.000 15.76000 ? 112 PHE A CZ  1 
ATOM   852  N N   . SER A 1 111 ? -12.21300 0.97300   18.44000  1.000 10.13000 ? 113 SER A N   1 
ATOM   853  C CA  . SER A 1 111 ? -11.07800 0.31900   17.81000  1.000 7.75000  ? 113 SER A CA  1 
ATOM   854  C C   . SER A 1 111 ? -11.53200 -1.00600  17.21200  1.000 9.97000  ? 113 SER A C   1 
ATOM   855  O O   . SER A 1 111 ? -12.30200 -1.73400  17.82900  1.000 8.53000  ? 113 SER A O   1 
ATOM   856  C CB  . SER A 1 111 ? -9.97500  0.06800   18.83800  1.000 10.68000 ? 113 SER A CB  1 
ATOM   857  O OG  . SER A 1 111 ? -9.47000  1.29600   19.32700  1.000 11.42000 ? 113 SER A OG  1 
ATOM   858  N N   . VAL A 1 112 ? -11.06100 -1.30600  16.01000  1.000 7.74000  ? 114 VAL A N   1 
ATOM   859  C CA  . VAL A 1 112 ? -11.29700 -2.59600  15.36900  1.000 9.66000  ? 114 VAL A CA  1 
ATOM   860  C C   . VAL A 1 112 ? -9.97700  -3.34700  15.36300  1.000 11.25000 ? 114 VAL A C   1 
ATOM   861  O O   . VAL A 1 112 ? -8.94200  -2.79300  14.97300  1.000 9.48000  ? 114 VAL A O   1 
ATOM   862  C CB  . VAL A 1 112 ? -11.83600 -2.43000  13.94200  1.000 12.43000 ? 114 VAL A CB  1 
ATOM   863  C CG1 . VAL A 1 112 ? -11.79200 -3.77400  13.19700  1.000 12.92000 ? 114 VAL A CG1 1 
ATOM   864  C CG2 . VAL A 1 112 ? -13.24500 -1.84400  13.97100  1.000 13.71000 ? 114 VAL A CG2 1 
ATOM   865  N N   . LEU A 1 113 ? -10.00200 -4.58700  15.82800  1.000 10.30000 ? 115 LEU A N   1 
ATOM   866  C CA  . LEU A 1 113 ? -8.86100  -5.48100  15.69400  1.000 8.93000  ? 115 LEU A CA  1 
ATOM   867  C C   . LEU A 1 113 ? -9.14800  -6.37700  14.49200  1.000 11.42000 ? 115 LEU A C   1 
ATOM   868  O O   . LEU A 1 113 ? -9.89500  -7.35500  14.60200  1.000 9.80000  ? 115 LEU A O   1 
ATOM   869  C CB  . LEU A 1 113 ? -8.66200  -6.28300  16.97200  1.000 11.21000 ? 115 LEU A CB  1 
ATOM   870  C CG  . LEU A 1 113 ? -7.48700  -7.25700  16.96900  1.000 12.35000 ? 115 LEU A CG  1 
ATOM   871  C CD1 . LEU A 1 113 ? -6.16200  -6.50700  16.78700  1.000 11.95000 ? 115 LEU A CD1 1 
ATOM   872  C CD2 . LEU A 1 113 ? -7.48200  -8.04000  18.26300  1.000 11.39000 ? 115 LEU A CD2 1 
ATOM   873  N N   . ALA A 1 114 ? -8.57600  -6.03700  13.34000  1.000 9.49000  ? 116 ALA A N   1 
ATOM   874  C CA  . ALA A 1 114 ? -8.80100  -6.85000  12.14900  1.000 11.27000 ? 116 ALA A CA  1 
ATOM   875  C C   . ALA A 1 114 ? -8.06000  -8.17000  12.29700  1.000 14.13000 ? 116 ALA A C   1 
ATOM   876  O O   . ALA A 1 114 ? -6.88100  -8.19300  12.65800  1.000 15.32000 ? 116 ALA A O   1 
ATOM   877  C CB  . ALA A 1 114 ? -8.35300  -6.11400  10.88700  1.000 15.19000 ? 116 ALA A CB  1 
ATOM   878  N N   . CYS A 1 115 ? -8.76900  -9.27100  12.06700  1.000 13.41000 ? 117 CYS A N   1 
ATOM   879  C CA  . CYS A 1 115 ? -8.25000  -10.60400 12.31100  1.000 11.21000 ? 117 CYS A CA  1 
ATOM   880  C C   . CYS A 1 115 ? -8.50900  -11.48400 11.09900  1.000 13.45000 ? 117 CYS A C   1 
ATOM   881  O O   . CYS A 1 115 ? -9.50100  -11.30900 10.38100  1.000 11.82000 ? 117 CYS A O   1 
ATOM   882  C CB  . CYS A 1 115 ? -8.89600  -11.25700 13.53000  1.000 15.21000 ? 117 CYS A CB  1 
ATOM   883  S SG  . CYS A 1 115 ? -8.41200  -10.58800 15.09300  1.000 19.89000 ? 117 CYS A SG  1 
ATOM   884  N N   . TYR A 1 116 ? -7.59700  -12.42900 10.87700  1.000 15.21000 ? 118 TYR A N   1 
ATOM   885  C CA  . TYR A 1 116 ? -7.73500  -13.40500 9.80300   1.000 18.59000 ? 118 TYR A CA  1 
ATOM   886  C C   . TYR A 1 116 ? -7.30200  -14.75900 10.34700  1.000 16.31000 ? 118 TYR A C   1 
ATOM   887  O O   . TYR A 1 116 ? -6.21800  -14.87300 10.92100  1.000 17.97000 ? 118 TYR A O   1 
ATOM   888  C CB  . TYR A 1 116 ? -6.91700  -12.97700 8.57000   1.000 16.86000 ? 118 TYR A CB  1 
ATOM   889  C CG  . TYR A 1 116 ? -7.42600  -11.65600 8.03400   1.000 17.53000 ? 118 TYR A CG  1 
ATOM   890  C CD1 . TYR A 1 116 ? -8.53200  -11.60800 7.19100   1.000 17.06000 ? 118 TYR A CD1 1 
ATOM   891  C CD2 . TYR A 1 116 ? -6.85100  -10.45100 8.43600   1.000 21.31000 ? 118 TYR A CD2 1 
ATOM   892  C CE1 . TYR A 1 116 ? -9.03300  -10.40900 6.73400   1.000 16.49000 ? 118 TYR A CE1 1 
ATOM   893  C CE2 . TYR A 1 116 ? -7.34400  -9.24300  7.99200   1.000 18.36000 ? 118 TYR A CE2 1 
ATOM   894  C CZ  . TYR A 1 116 ? -8.43700  -9.22500  7.13700   1.000 17.72000 ? 118 TYR A CZ  1 
ATOM   895  O OH  . TYR A 1 116 ? -8.93900  -8.02600  6.69000   1.000 20.38000 ? 118 TYR A OH  1 
ATOM   896  N N   . ASN A 1 117 ? -8.16900  -15.76500 10.21100  1.000 17.78000 ? 119 ASN A N   1 
ATOM   897  C CA  . ASN A 1 117 ? -7.92700  -17.09800 10.77800  1.000 20.65000 ? 119 ASN A CA  1 
ATOM   898  C C   . ASN A 1 117 ? -7.58200  -17.02400 12.26600  1.000 18.43000 ? 119 ASN A C   1 
ATOM   899  O O   . ASN A 1 117 ? -6.71100  -17.74400 12.76200  1.000 20.57000 ? 119 ASN A O   1 
ATOM   900  C CB  . ASN A 1 117 ? -6.83000  -17.83400 10.01200  1.000 23.95000 ? 119 ASN A CB  1 
ATOM   901  C CG  . ASN A 1 117 ? -7.00800  -17.73700 8.51400   1.000 25.97000 ? 119 ASN A CG  1 
ATOM   902  O OD1 . ASN A 1 117 ? -7.88100  -18.38200 7.93500   1.000 26.27000 ? 119 ASN A OD1 1 
ATOM   903  N ND2 . ASN A 1 117 ? -6.18300  -16.91400 7.87900   1.000 31.18000 ? 119 ASN A ND2 1 
ATOM   904  N N   . GLY A 1 118 ? -8.29400  -16.16400 12.99200  1.000 14.00000 ? 120 GLY A N   1 
ATOM   905  C CA  . GLY A 1 118 ? -8.09400  -16.01600 14.41900  1.000 15.36000 ? 120 GLY A CA  1 
ATOM   906  C C   . GLY A 1 118 ? -6.82300  -15.29700 14.81100  1.000 20.32000 ? 120 GLY A C   1 
ATOM   907  O O   . GLY A 1 118 ? -6.52200  -15.21600 16.00500  1.000 17.29000 ? 120 GLY A O   1 
ATOM   908  N N   . SER A 1 119 ? -6.06900  -14.77200 13.85000  1.000 18.45000 ? 121 SER A N   1 
ATOM   909  C CA  . SER A 1 119 ? -4.79900  -14.13200 14.14100  1.000 20.03000 ? 121 SER A CA  1 
ATOM   910  C C   . SER A 1 119 ? -4.92800  -12.63600 13.89700  1.000 17.38000 ? 121 SER A C   1 
ATOM   911  O O   . SER A 1 119 ? -5.26600  -12.21700 12.77800  1.000 14.15000 ? 121 SER A O   1 
ATOM   912  C CB  . SER A 1 119 ? -3.68700  -14.72400 13.28000  1.000 22.45000 ? 121 SER A CB  1 
ATOM   913  O OG  . SER A 1 119 ? -2.43100  -14.20700 13.66600  1.000 28.75000 ? 121 SER A OG  1 
ATOM   914  N N   . PRO A 1 120 ? -4.70400  -11.81900 14.92200  1.000 16.72000 ? 122 PRO A N   1 
ATOM   915  C CA  . PRO A 1 120 ? -4.76900  -10.36200 14.75300  1.000 21.03000 ? 122 PRO A CA  1 
ATOM   916  C C   . PRO A 1 120 ? -3.80000  -9.85300  13.69100  1.000 18.03000 ? 122 PRO A C   1 
ATOM   917  O O   . PRO A 1 120 ? -2.62800  -10.22400 13.65700  1.000 17.66000 ? 122 PRO A O   1 
ATOM   918  C CB  . PRO A 1 120 ? -4.41000  -9.84200  16.14900  1.000 18.94000 ? 122 PRO A CB  1 
ATOM   919  C CG  . PRO A 1 120 ? -4.96200  -10.89200 17.06500  1.000 20.87000 ? 122 PRO A CG  1 
ATOM   920  C CD  . PRO A 1 120 ? -4.70500  -12.21100 16.34300  1.000 22.89000 ? 122 PRO A CD  1 
ATOM   921  N N   . SER A 1 121 ? -4.30400  -8.98500  12.82300  1.000 17.67000 ? 123 SER A N   1 
ATOM   922  C CA  . SER A 1 121 ? -3.51200  -8.38300  11.75800  1.000 17.48000 ? 123 SER A CA  1 
ATOM   923  C C   . SER A 1 121 ? -3.26300  -6.89500  11.96700  1.000 16.49000 ? 123 SER A C   1 
ATOM   924  O O   . SER A 1 121 ? -2.18800  -6.40000  11.64200  1.000 21.00000 ? 123 SER A O   1 
ATOM   925  C CB  . SER A 1 121 ? -4.21100  -8.60500  10.41300  1.000 18.85000 ? 123 SER A CB  1 
ATOM   926  O OG  . SER A 1 121 ? -3.92400  -7.58100  9.48800   1.000 32.38000 ? 123 SER A OG  1 
ATOM   927  N N   . GLY A 1 122 ? -4.22800  -6.16200  12.49600  1.000 11.67000 ? 124 GLY A N   1 
ATOM   928  C CA  . GLY A 1 122 ? -3.99000  -4.75300  12.74400  1.000 16.47000 ? 124 GLY A CA  1 
ATOM   929  C C   . GLY A 1 122 ? -5.10300  -4.15000  13.56200  1.000 15.46000 ? 124 GLY A C   1 
ATOM   930  O O   . GLY A 1 122 ? -6.13900  -4.77000  13.80600  1.000 14.14000 ? 124 GLY A O   1 
ATOM   931  N N   . VAL A 1 123 ? -4.87900  -2.91800  13.99400  1.000 12.18000 ? 125 VAL A N   1 
ATOM   932  C CA  . VAL A 1 123 ? -5.85400  -2.25100  14.84000  1.000 11.91000 ? 125 VAL A CA  1 
ATOM   933  C C   . VAL A 1 123 ? -5.98000  -0.81000  14.38400  1.000 14.10000 ? 125 VAL A C   1 
ATOM   934  O O   . VAL A 1 123 ? -4.98000  -0.14200  14.09500  1.000 11.55000 ? 125 VAL A O   1 
ATOM   935  C CB  . VAL A 1 123 ? -5.48200  -2.34400  16.34100  1.000 16.41000 ? 125 VAL A CB  1 
ATOM   936  C CG1 . VAL A 1 123 ? -4.11500  -1.74700  16.60900  1.000 16.18000 ? 125 VAL A CG1 1 
ATOM   937  C CG2 . VAL A 1 123 ? -6.55000  -1.66100  17.20200  1.000 13.51000 ? 125 VAL A CG2 1 
ATOM   938  N N   . TYR A 1 124 ? -7.21300  -0.33700  14.31300  1.000 10.79000 ? 126 TYR A N   1 
ATOM   939  C CA  . TYR A 1 124 ? -7.44100  1.02600   13.86400  1.000 15.75000 ? 126 TYR A CA  1 
ATOM   940  C C   . TYR A 1 124 ? -8.77300  1.49800   14.41300  1.000 15.77000 ? 126 TYR A C   1 
ATOM   941  O O   . TYR A 1 124 ? -9.62900  0.70200   14.81300  1.000 15.39000 ? 126 TYR A O   1 
ATOM   942  C CB  . TYR A 1 124 ? -7.40900  1.11500   12.33600  1.000 14.83000 ? 126 TYR A CB  1 
ATOM   943  C CG  . TYR A 1 124 ? -8.37000  0.15400   11.65500  1.000 16.63000 ? 126 TYR A CG  1 
ATOM   944  C CD1 . TYR A 1 124 ? -9.68500  0.52300   11.39900  1.000 20.35000 ? 126 TYR A CD1 1 
ATOM   945  C CD2 . TYR A 1 124 ? -7.96300  -1.11800  11.27200  1.000 21.99000 ? 126 TYR A CD2 1 
ATOM   946  C CE1 . TYR A 1 124 ? -10.57100 -0.36000  10.77700  1.000 24.91000 ? 126 TYR A CE1 1 
ATOM   947  C CE2 . TYR A 1 124 ? -8.84800  -2.00600  10.65100  1.000 20.42000 ? 126 TYR A CE2 1 
ATOM   948  C CZ  . TYR A 1 124 ? -10.14500 -1.61000  10.40700  1.000 20.92000 ? 126 TYR A CZ  1 
ATOM   949  O OH  . TYR A 1 124 ? -11.02600 -2.47600  9.79200   1.000 24.77000 ? 126 TYR A OH  1 
ATOM   950  N N   . GLN A 1 125 ? -8.94100  2.80700   14.39900  1.000 14.43000 ? 127 GLN A N   1 
ATOM   951  C CA  . GLN A 1 125 ? -10.11500 3.44100   14.95000  1.000 17.44000 ? 127 GLN A CA  1 
ATOM   952  C C   . GLN A 1 125 ? -11.17600 3.62100   13.86700  1.000 18.21000 ? 127 GLN A C   1 
ATOM   953  O O   . GLN A 1 125 ? -10.86300 4.00700   12.74100  1.000 21.90000 ? 127 GLN A O   1 
ATOM   954  C CB  . GLN A 1 125 ? -9.70800  4.78400   15.54900  1.000 19.91000 ? 127 GLN A CB  1 
ATOM   955  C CG  . GLN A 1 125 ? -10.71400 5.33000   16.48500  1.000 25.55000 ? 127 GLN A CG  1 
ATOM   956  C CD  . GLN A 1 125 ? -10.57200 4.77900   17.87300  1.000 20.60000 ? 127 GLN A CD  1 
ATOM   957  O OE1 . GLN A 1 125 ? -10.00200 3.69600   18.08500  1.000 25.37000 ? 127 GLN A OE1 1 
ATOM   958  N NE2 . GLN A 1 125 ? -11.09500 5.52100   18.84700  1.000 28.50000 ? 127 GLN A NE2 1 
ATOM   959  N N   . CYS A 1 126 ? -12.43300 3.33800   14.21300  1.000 14.14000 ? 128 CYS A N   1 
ATOM   960  C CA  . CYS A 1 126 ? -13.55800 3.44600   13.29100  1.000 17.20000 ? 128 CYS A CA  1 
ATOM   961  C C   . CYS A 1 126 ? -14.64600 4.30600   13.90900  1.000 19.98000 ? 128 CYS A C   1 
ATOM   962  O O   . CYS A 1 126 ? -14.77900 4.36800   15.12900  1.000 14.84000 ? 128 CYS A O   1 
ATOM   963  C CB  . CYS A 1 126 ? -14.17100 2.06200   12.96900  1.000 17.90000 ? 128 CYS A CB  1 
ATOM   964  S SG  . CYS A 1 126 ? -13.40200 1.25600   11.59900  1.000 32.09000 ? 128 CYS A SG  1 
ATOM   965  N N   . ALA A 1 127 ? -15.45200 4.94500   13.06600  1.000 18.86000 ? 129 ALA A N   1 
ATOM   966  C CA  . ALA A 1 127 ? -16.65300 5.61300   13.54400  1.000 19.09000 ? 129 ALA A CA  1 
ATOM   967  C C   . ALA A 1 127 ? -17.87500 4.93600   12.94600  1.000 16.96000 ? 129 ALA A C   1 
ATOM   968  O O   . ALA A 1 127 ? -17.89300 4.59600   11.75800  1.000 18.86000 ? 129 ALA A O   1 
ATOM   969  C CB  . ALA A 1 127 ? -16.66400 7.10000   13.20000  1.000 17.88000 ? 129 ALA A CB  1 
ATOM   970  N N   . MET A 1 128 ? -18.88200 4.72900   13.78400  1.000 14.66000 ? 130 MET A N   1 
ATOM   971  C CA  . MET A 1 128 ? -20.18400 4.28400   13.30600  1.000 15.81000 ? 130 MET A CA  1 
ATOM   972  C C   . MET A 1 128 ? -20.86300 5.47200   12.62900  1.000 14.19000 ? 130 MET A C   1 
ATOM   973  O O   . MET A 1 128 ? -21.14500 6.48400   13.27600  1.000 14.44000 ? 130 MET A O   1 
ATOM   974  C CB  . MET A 1 128 ? -21.00200 3.74900   14.48100  1.000 14.67000 ? 130 MET A CB  1 
ATOM   975  C CG  . MET A 1 128 ? -22.44000 3.33400   14.15700  1.000 18.75000 ? 130 MET A CG  1 
ATOM   976  S SD  . MET A 1 128 ? -22.51700 1.87700   13.11700  1.000 24.34000 ? 130 MET A SD  1 
ATOM   977  C CE  . MET A 1 128 ? -21.70400 0.65200   14.15200  1.000 16.62000 ? 130 MET A CE  1 
ATOM   978  N N   . ARG A 1 129 ? -21.08700 5.37500   11.32500  1.000 16.08000 ? 131 ARG A N   1 
ATOM   979  C CA  . ARG A 1 129 ? -21.73100 6.45200   10.59400  1.000 15.30000 ? 131 ARG A CA  1 
ATOM   980  C C   . ARG A 1 129 ? -23.21300 6.54800   10.95600  1.000 15.76000 ? 131 ARG A C   1 
ATOM   981  O O   . ARG A 1 129 ? -23.80100 5.59900   11.48500  1.000 16.27000 ? 131 ARG A O   1 
ATOM   982  C CB  . ARG A 1 129 ? -21.57900 6.23800   9.08800   1.000 16.79000 ? 131 ARG A CB  1 
ATOM   983  C CG  . ARG A 1 129 ? -20.13400 6.17700   8.59200   1.000 15.00000 ? 131 ARG A CG  1 
ATOM   984  C CD  . ARG A 1 129 ? -19.29400 7.36900   9.06600   1.000 17.85000 ? 131 ARG A CD  1 
ATOM   985  N NE  . ARG A 1 129 ? -19.90000 8.65400   8.71300   1.000 17.64000 ? 131 ARG A NE  1 
ATOM   986  C CZ  . ARG A 1 129 ? -19.34000 9.84800   8.92100   1.000 19.08000 ? 131 ARG A CZ  1 
ATOM   987  N NH1 . ARG A 1 129 ? -18.13400 9.94300   9.48300   1.000 15.73000 ? 131 ARG A NH1 1 
ATOM   988  N NH2 . ARG A 1 129 ? -19.99500 10.94900  8.57100   1.000 13.77000 ? 131 ARG A NH2 1 
ATOM   989  N N   . PRO A 1 130 ? -23.84400 7.69500   10.67300  1.000 15.09000 ? 132 PRO A N   1 
ATOM   990  C CA  . PRO A 1 130 ? -25.30100 7.80200   10.87100  1.000 17.46000 ? 132 PRO A CA  1 
ATOM   991  C C   . PRO A 1 130 ? -26.11400 6.80800   10.05900  1.000 16.98000 ? 132 PRO A C   1 
ATOM   992  O O   . PRO A 1 130 ? -27.24200 6.49600   10.45200  1.000 18.14000 ? 132 PRO A O   1 
ATOM   993  C CB  . PRO A 1 130 ? -25.60100 9.24300   10.44200  1.000 13.79000 ? 132 PRO A CB  1 
ATOM   994  C CG  . PRO A 1 130 ? -24.30000 9.97600   10.76300  1.000 15.99000 ? 132 PRO A CG  1 
ATOM   995  C CD  . PRO A 1 130 ? -23.23000 9.00300   10.36700  1.000 13.60000 ? 132 PRO A CD  1 
ATOM   996  N N   . ASN A 1 131 ? -25.59600 6.30000   8.94800   1.000 13.93000 ? 133 ASN A N   1 
ATOM   997  C CA  . ASN A 1 131 ? -26.31600 5.25900   8.22500   1.000 18.05000 ? 133 ASN A CA  1 
ATOM   998  C C   . ASN A 1 131 ? -25.91000 3.85200   8.68200   1.000 21.48000 ? 133 ASN A C   1 
ATOM   999  O O   . ASN A 1 131 ? -26.21700 2.87700   7.98900   1.000 19.59000 ? 133 ASN A O   1 
ATOM   1000 C CB  . ASN A 1 131 ? -26.14700 5.42800   6.70300   1.000 17.20000 ? 133 ASN A CB  1 
ATOM   1001 C CG  . ASN A 1 131 ? -24.73000 5.19700   6.21900   1.000 22.48000 ? 133 ASN A CG  1 
ATOM   1002 O OD1 . ASN A 1 131 ? -23.82800 4.85600   6.98900   1.000 20.81000 ? 133 ASN A OD1 1 
ATOM   1003 N ND2 . ASN A 1 131 ? -24.52900 5.36900   4.92000   1.000 23.65000 ? 133 ASN A ND2 1 
ATOM   1004 N N   . PHE A 1 132 ? -25.22100 3.74400   9.82700   1.000 17.40000 ? 134 PHE A N   1 
ATOM   1005 C CA  . PHE A 1 132 ? -24.95300 2.47800   10.51600  1.000 18.51000 ? 134 PHE A CA  1 
ATOM   1006 C C   . PHE A 1 132 ? -24.01400 1.57500   9.73300   1.000 18.28000 ? 134 PHE A C   1 
ATOM   1007 O O   . PHE A 1 132 ? -24.05000 0.35300   9.87900   1.000 20.58000 ? 134 PHE A O   1 
ATOM   1008 C CB  . PHE A 1 132 ? -26.24400 1.72300   10.84500  1.000 19.20000 ? 134 PHE A CB  1 
ATOM   1009 C CG  . PHE A 1 132 ? -27.15200 2.45300   11.79700  1.000 22.05000 ? 134 PHE A CG  1 
ATOM   1010 C CD1 . PHE A 1 132 ? -26.83500 2.55100   13.13800  1.000 26.30000 ? 134 PHE A CD1 1 
ATOM   1011 C CD2 . PHE A 1 132 ? -28.32500 3.03800   11.34500  1.000 26.98000 ? 134 PHE A CD2 1 
ATOM   1012 C CE1 . PHE A 1 132 ? -27.67200 3.21800   14.02000  1.000 30.72000 ? 134 PHE A CE1 1 
ATOM   1013 C CE2 . PHE A 1 132 ? -29.16500 3.70700   12.22200  1.000 25.37000 ? 134 PHE A CE2 1 
ATOM   1014 C CZ  . PHE A 1 132 ? -28.83100 3.80000   13.56000  1.000 24.98000 ? 134 PHE A CZ  1 
ATOM   1015 N N   . THR A 1 133 ? -23.16900 2.15800   8.90400   1.000 14.21000 ? 135 THR A N   1 
ATOM   1016 C CA  . THR A 1 133 ? -22.03700 1.46000   8.33100   1.000 17.12000 ? 135 THR A CA  1 
ATOM   1017 C C   . THR A 1 133 ? -20.76100 1.99800   8.95000   1.000 19.01000 ? 135 THR A C   1 
ATOM   1018 O O   . THR A 1 133 ? -20.75400 3.05900   9.57700   1.000 19.70000 ? 135 THR A O   1 
ATOM   1019 C CB  . THR A 1 133 ? -21.97900 1.64000   6.81600   1.000 19.91000 ? 135 THR A CB  1 
ATOM   1020 O OG1 . THR A 1 133 ? -21.78300 3.03200   6.52400   1.000 22.05000 ? 135 THR A OG1 1 
ATOM   1021 C CG2 . THR A 1 133 ? -23.27400 1.12200   6.15700   1.000 17.60000 ? 135 THR A CG2 1 
ATOM   1022 N N   . ILE A 1 134 ? -19.67000 1.25900   8.76300   1.000 15.20000 ? 136 ILE A N   1 
ATOM   1023 C CA  . ILE A 1 134 ? -18.36300 1.74900   9.16100   1.000 17.70000 ? 136 ILE A CA  1 
ATOM   1024 C C   . ILE A 1 134 ? -17.43400 1.66300   7.96300   1.000 21.75000 ? 136 ILE A C   1 
ATOM   1025 O O   . ILE A 1 134 ? -17.54700 0.76800   7.11800   1.000 18.11000 ? 136 ILE A O   1 
ATOM   1026 C CB  . ILE A 1 134 ? -17.78100 0.98400   10.38700  1.000 16.82000 ? 136 ILE A CB  1 
ATOM   1027 C CG1 . ILE A 1 134 ? -17.36600 -0.43900  10.03000  1.000 18.03000 ? 136 ILE A CG1 1 
ATOM   1028 C CG2 . ILE A 1 134 ? -18.78700 0.96100   11.54200  1.000 16.39000 ? 136 ILE A CG2 1 
ATOM   1029 C CD1 . ILE A 1 134 ? -16.45700 -1.07500  11.10600  1.000 15.03000 ? 136 ILE A CD1 1 
ATOM   1030 N N   . LYS A 1 135 ? -16.50600 2.61700   7.89200   1.000 21.36000 ? 137 LYS A N   1 
ATOM   1031 C CA  . LYS A 1 135 ? -15.48600 2.61100   6.84800   1.000 23.58000 ? 137 LYS A CA  1 
ATOM   1032 C C   . LYS A 1 135 ? -14.31800 1.79400   7.37400   1.000 24.18000 ? 137 LYS A C   1 
ATOM   1033 O O   . LYS A 1 135 ? -13.30000 2.30900   7.83700   1.000 27.63000 ? 137 LYS A O   1 
ATOM   1034 C CB  . LYS A 1 135 ? -15.08400 4.03100   6.46500   1.000 29.78000 ? 137 LYS A CB  1 
ATOM   1035 C CG  . LYS A 1 135 ? -16.00100 4.66800   5.43200   1.000 33.63000 ? 137 LYS A CG  1 
ATOM   1036 C CD  . LYS A 1 135 ? -15.43700 5.99500   4.91200   1.000 38.54000 ? 137 LYS A CD  1 
ATOM   1037 C CE  . LYS A 1 135 ? -16.45100 6.74700   4.02800   1.000 45.80000 ? 137 LYS A CE  1 
ATOM   1038 N NZ  . LYS A 1 135 ? -16.80800 6.03600   2.76000   1.000 38.86000 ? 137 LYS A NZ  1 
ATOM   1039 N N   . GLY A 1 136 ? -14.49900 0.48000   7.33600   1.000 24.74000 ? 138 GLY A N   1 
ATOM   1040 C CA  . GLY A 1 136 ? -13.49200 -0.43500  7.81200   1.000 24.89000 ? 138 GLY A CA  1 
ATOM   1041 C C   . GLY A 1 136 ? -12.45100 -0.71300  6.75800   1.000 25.56000 ? 138 GLY A C   1 
ATOM   1042 O O   . GLY A 1 136 ? -12.48200 -0.19500  5.64200   1.000 31.90000 ? 138 GLY A O   1 
ATOM   1043 N N   . SER A 1 137 ? -11.50500 -1.54300  7.13500   1.000 21.43000 ? 139 SER A N   1 
ATOM   1044 C CA  . SER A 1 137 ? -10.50300 -2.06100  6.21000   1.000 25.91000 ? 139 SER A CA  1 
ATOM   1045 C C   . SER A 1 137 ? -10.52600 -3.57300  6.39600   1.000 25.62000 ? 139 SER A C   1 
ATOM   1046 O O   . SER A 1 137 ? -9.73600  -4.13300  7.16200   1.000 33.09000 ? 139 SER A O   1 
ATOM   1047 C CB  . SER A 1 137 ? -9.13400  -1.46100  6.47900   1.000 29.91000 ? 139 SER A CB  1 
ATOM   1048 O OG  . SER A 1 137 ? -8.20300  -1.92900  5.52100   1.000 36.40000 ? 139 SER A OG  1 
ATOM   1049 N N   . PHE A 1 138 ? -11.47500 -4.22700  5.72800   1.000 27.44000 ? 140 PHE A N   1 
ATOM   1050 C CA  . PHE A 1 138 ? -11.74800 -5.64700  5.92200   1.000 21.39000 ? 140 PHE A CA  1 
ATOM   1051 C C   . PHE A 1 138 ? -11.53900 -6.38800  4.61300   1.000 23.08000 ? 140 PHE A C   1 
ATOM   1052 O O   . PHE A 1 138 ? -12.03900 -5.95900  3.56700   1.000 24.57000 ? 140 PHE A O   1 
ATOM   1053 C CB  . PHE A 1 138 ? -13.17800 -5.87900  6.41100   1.000 17.72000 ? 140 PHE A CB  1 
ATOM   1054 C CG  . PHE A 1 138 ? -13.43900 -5.39200  7.80700   1.000 18.00000 ? 140 PHE A CG  1 
ATOM   1055 C CD1 . PHE A 1 138 ? -12.73700 -5.91600  8.88100   1.000 17.16000 ? 140 PHE A CD1 1 
ATOM   1056 C CD2 . PHE A 1 138 ? -14.40400 -4.43100  8.05000   1.000 17.74000 ? 140 PHE A CD2 1 
ATOM   1057 C CE1 . PHE A 1 138 ? -12.99900 -5.49000  10.17400  1.000 15.58000 ? 140 PHE A CE1 1 
ATOM   1058 C CE2 . PHE A 1 138 ? -14.65400 -3.99100  9.33400   1.000 21.22000 ? 140 PHE A CE2 1 
ATOM   1059 C CZ  . PHE A 1 138 ? -13.94600 -4.52600  10.40000  1.000 16.11000 ? 140 PHE A CZ  1 
ATOM   1060 N N   . LEU A 1 139 ? -10.81600 -7.49400  4.67600   1.000 21.80000 ? 141 LEU A N   1 
ATOM   1061 C CA  . LEU A 1 139 ? -10.63600 -8.38900  3.54700   1.000 22.47000 ? 141 LEU A CA  1 
ATOM   1062 C C   . LEU A 1 139 ? -11.41700 -9.68400  3.78900   1.000 23.97000 ? 141 LEU A C   1 
ATOM   1063 O O   . LEU A 1 139 ? -12.08300 -9.86100  4.81500   1.000 17.00000 ? 141 LEU A O   1 
ATOM   1064 C CB  . LEU A 1 139 ? -9.15100  -8.67200  3.31700   1.000 23.87000 ? 141 LEU A CB  1 
ATOM   1065 C CG  . LEU A 1 139 ? -8.24400  -7.45800  3.09800   1.000 31.47000 ? 141 LEU A CG  1 
ATOM   1066 C CD1 . LEU A 1 139 ? -6.78100  -7.89400  3.11900   1.000 31.41000 ? 141 LEU A CD1 1 
ATOM   1067 C CD2 . LEU A 1 139 ? -8.58500  -6.74700  1.79500   1.000 28.20000 ? 141 LEU A CD2 1 
ATOM   1068 N N   . ASN A 1 140 ? -11.35600 -10.57500 2.80200   1.000 24.22000 ? 142 ASN A N   1 
ATOM   1069 C CA  . ASN A 1 140 ? -11.91300 -11.91100 2.95300   1.000 24.68000 ? 142 ASN A CA  1 
ATOM   1070 C C   . ASN A 1 140 ? -11.36500 -12.56400 4.21600   1.000 18.40000 ? 142 ASN A C   1 
ATOM   1071 O O   . ASN A 1 140 ? -10.16900 -12.48000 4.51000   1.000 20.51000 ? 142 ASN A O   1 
ATOM   1072 C CB  . ASN A 1 140 ? -11.56700 -12.77300 1.73300   1.000 23.10000 ? 142 ASN A CB  1 
ATOM   1073 C CG  . ASN A 1 140 ? -12.38600 -12.41700 0.51300   1.000 35.88000 ? 142 ASN A CG  1 
ATOM   1074 O OD1 . ASN A 1 140 ? -13.57900 -12.12300 0.61200   1.000 37.64000 ? 142 ASN A OD1 1 
ATOM   1075 N ND2 . ASN A 1 140 ? -11.75000 -12.45500 -0.65600  1.000 35.88000 ? 142 ASN A ND2 1 
ATOM   1076 N N   . GLY A 1 141 ? -12.25200 -13.21100 4.97100   1.000 17.19000 ? 143 GLY A N   1 
ATOM   1077 C CA  . GLY A 1 141 ? -11.86200 -13.87100 6.19700   1.000 15.75000 ? 143 GLY A CA  1 
ATOM   1078 C C   . GLY A 1 141 ? -11.88300 -12.99700 7.43600   1.000 14.29000 ? 143 GLY A C   1 
ATOM   1079 O O   . GLY A 1 141 ? -11.54200 -13.47800 8.52700   1.000 13.57000 ? 143 GLY A O   1 
ATOM   1080 N N   . SER A 1 142 ? -12.27900 -11.73900 7.31700   1.000 15.38000 ? 144 SER A N   1 
ATOM   1081 C CA  . SER A 1 142 ? -12.23800 -10.84200 8.45900   1.000 14.52000 ? 144 SER A CA  1 
ATOM   1082 C C   . SER A 1 142 ? -13.47400 -10.93200 9.34100   1.000 11.82000 ? 144 SER A C   1 
ATOM   1083 O O   . SER A 1 142 ? -13.46200 -10.38000 10.44400  1.000 10.89000 ? 144 SER A O   1 
ATOM   1084 C CB  . SER A 1 142 ? -12.06400 -9.40000  7.98100   1.000 14.17000 ? 144 SER A CB  1 
ATOM   1085 O OG  . SER A 1 142 ? -13.12700 -9.02100  7.12300   1.000 14.79000 ? 144 SER A OG  1 
ATOM   1086 N N   . CYS A 1 143 ? -14.54500 -11.57500 8.87600   1.000 9.54000  ? 145 CYS A N   1 
ATOM   1087 C CA  . CYS A 1 143 ? -15.77500 -11.61900 9.65200   1.000 10.18000 ? 145 CYS A CA  1 
ATOM   1088 C C   . CYS A 1 143 ? -15.51200 -12.18400 11.03500  1.000 10.00000 ? 145 CYS A C   1 
ATOM   1089 O O   . CYS A 1 143 ? -14.64800 -13.05000 11.22600  1.000 10.44000 ? 145 CYS A O   1 
ATOM   1090 C CB  . CYS A 1 143 ? -16.83300 -12.46400 8.95100   1.000 11.74000 ? 145 CYS A CB  1 
ATOM   1091 S SG  . CYS A 1 143 ? -17.44700 -11.66400 7.47800   1.000 13.09000 ? 145 CYS A SG  1 
ATOM   1092 N N   . GLY A 1 144 ? -16.27200 -11.68400 12.00700  1.000 8.69000  ? 146 GLY A N   1 
ATOM   1093 C CA  . GLY A 1 144 ? -16.01000 -12.02400 13.38500  1.000 9.79000  ? 146 GLY A CA  1 
ATOM   1094 C C   . GLY A 1 144 ? -14.95200 -11.17500 14.04900  1.000 9.15000  ? 146 GLY A C   1 
ATOM   1095 O O   . GLY A 1 144 ? -14.80000 -11.25800 15.26900  1.000 9.18000  ? 146 GLY A O   1 
ATOM   1096 N N   . SER A 1 145 ? -14.21300 -10.35800 13.29800  1.000 9.83000  ? 147 SER A N   1 
ATOM   1097 C CA  . SER A 1 145 ? -13.39900 -9.32800  13.93500  1.000 8.45000  ? 147 SER A CA  1 
ATOM   1098 C C   . SER A 1 145 ? -14.30700 -8.40200  14.73600  1.000 11.73000 ? 147 SER A C   1 
ATOM   1099 O O   . SER A 1 145 ? -15.46400 -8.16900  14.36900  1.000 10.63000 ? 147 SER A O   1 
ATOM   1100 C CB  . SER A 1 145 ? -12.62400 -8.51100  12.90200  1.000 8.00000  ? 147 SER A CB  1 
ATOM   1101 O OG  . SER A 1 145 ? -11.68700 -9.30800  12.20000  1.000 10.48000 ? 147 SER A OG  1 
ATOM   1102 N N   . VAL A 1 146 ? -13.79000 -7.86600  15.84500  1.000 7.47000  ? 148 VAL A N   1 
ATOM   1103 C CA  . VAL A 1 146 ? -14.65900 -7.11200  16.73700  1.000 7.47000  ? 148 VAL A CA  1 
ATOM   1104 C C   . VAL A 1 146 ? -14.13700 -5.69100  16.91000  1.000 12.53000 ? 148 VAL A C   1 
ATOM   1105 O O   . VAL A 1 146 ? -12.95600 -5.39500  16.70700  1.000 8.22000  ? 148 VAL A O   1 
ATOM   1106 C CB  . VAL A 1 146 ? -14.84800 -7.78500  18.11800  1.000 7.85000  ? 148 VAL A CB  1 
ATOM   1107 C CG1 . VAL A 1 146 ? -15.54200 -9.17000  17.97300  1.000 8.94000  ? 148 VAL A CG1 1 
ATOM   1108 C CG2 . VAL A 1 146 ? -13.51900 -7.87900  18.88700  1.000 7.90000  ? 148 VAL A CG2 1 
ATOM   1109 N N   . GLY A 1 147 ? -15.06300 -4.80300  17.25800  1.000 11.00000 ? 149 GLY A N   1 
ATOM   1110 C CA  . GLY A 1 147 ? -14.74000 -3.44100  17.63100  1.000 8.36000  ? 149 GLY A CA  1 
ATOM   1111 C C   . GLY A 1 147 ? -15.00700 -3.27800  19.10900  1.000 9.60000  ? 149 GLY A C   1 
ATOM   1112 O O   . GLY A 1 147 ? -15.87900 -3.95000  19.67400  1.000 7.75000  ? 149 GLY A O   1 
ATOM   1113 N N   . PHE A 1 148 ? -14.24100 -2.39400  19.74400  1.000 7.39000  ? 150 PHE A N   1 
ATOM   1114 C CA  . PHE A 1 148 ? -14.28300 -2.32100  21.19300  1.000 8.41000  ? 150 PHE A CA  1 
ATOM   1115 C C   . PHE A 1 148 ? -13.78300 -0.95600  21.65200  1.000 9.59000  ? 150 PHE A C   1 
ATOM   1116 O O   . PHE A 1 148 ? -13.03700 -0.27200  20.94900  1.000 8.51000  ? 150 PHE A O   1 
ATOM   1117 C CB  . PHE A 1 148 ? -13.42200 -3.42100  21.82900  1.000 9.23000  ? 150 PHE A CB  1 
ATOM   1118 C CG  . PHE A 1 148 ? -11.97100 -3.31000  21.47200  1.000 8.67000  ? 150 PHE A CG  1 
ATOM   1119 C CD1 . PHE A 1 148 ? -11.50600 -3.77800  20.24300  1.000 10.96000 ? 150 PHE A CD1 1 
ATOM   1120 C CD2 . PHE A 1 148 ? -11.07100 -2.70500  22.34400  1.000 11.39000 ? 150 PHE A CD2 1 
ATOM   1121 C CE1 . PHE A 1 148 ? -10.15700 -3.64800  19.89200  1.000 12.21000 ? 150 PHE A CE1 1 
ATOM   1122 C CE2 . PHE A 1 148 ? -9.71800  -2.58600  22.00500  1.000 12.00000 ? 150 PHE A CE2 1 
ATOM   1123 C CZ  . PHE A 1 148 ? -9.26700  -3.05200  20.77300  1.000 11.31000 ? 150 PHE A CZ  1 
ATOM   1124 N N   . ASN A 1 149 ? -14.18200 -0.60200  22.86100  1.000 10.40000 ? 151 ASN A N   1 
ATOM   1125 C CA  . ASN A 1 149 ? -13.58800 0.48500   23.62000  1.000 12.30000 ? 151 ASN A CA  1 
ATOM   1126 C C   . ASN A 1 149 ? -13.07700 -0.09300  24.92800  1.000 14.98000 ? 151 ASN A C   1 
ATOM   1127 O O   . ASN A 1 149 ? -13.57600 -1.11100  25.40300  1.000 12.59000 ? 151 ASN A O   1 
ATOM   1128 C CB  . ASN A 1 149 ? -14.60800 1.58600   23.90800  1.000 13.86000 ? 151 ASN A CB  1 
ATOM   1129 C CG  . ASN A 1 149 ? -14.94100 2.40300   22.67800  1.000 18.94000 ? 151 ASN A CG  1 
ATOM   1130 O OD1 . ASN A 1 149 ? -14.21700 3.32900   22.31400  1.000 21.31000 ? 151 ASN A OD1 1 
ATOM   1131 N ND2 . ASN A 1 149 ? -16.03400 2.06300   22.03100  1.000 13.75000 ? 151 ASN A ND2 1 
ATOM   1132 N N   . ILE A 1 150 ? -12.09000 0.56400   25.52900  1.000 13.42000 ? 152 ILE A N   1 
ATOM   1133 C CA  . ILE A 1 150 ? -11.61100 0.16700   26.84600  1.000 15.33000 ? 152 ILE A CA  1 
ATOM   1134 C C   . ILE A 1 150 ? -11.82500 1.33000   27.80300  1.000 25.52000 ? 152 ILE A C   1 
ATOM   1135 O O   . ILE A 1 150 ? -11.50100 2.47700   27.47600  1.000 23.17000 ? 152 ILE A O   1 
ATOM   1136 C CB  . ILE A 1 150 ? -10.13300 -0.26000  26.82300  1.000 17.78000 ? 152 ILE A CB  1 
ATOM   1137 C CG1 . ILE A 1 150 ? -9.88900  -1.27300  25.71100  1.000 16.57000 ? 152 ILE A CG1 1 
ATOM   1138 C CG2 . ILE A 1 150 ? -9.72200  -0.84000  28.19000  1.000 23.51000 ? 152 ILE A CG2 1 
ATOM   1139 C CD1 . ILE A 1 150 ? -8.48300  -1.86600  25.71000  1.000 18.76000 ? 152 ILE A CD1 1 
ATOM   1140 N N   . ASP A 1 151 ? -12.39900 1.03400   28.96600  1.000 23.72000 ? 153 ASP A N   1 
ATOM   1141 C CA  . ASP A 1 151 ? -12.54900 1.98800   30.06200  1.000 28.67000 ? 153 ASP A CA  1 
ATOM   1142 C C   . ASP A 1 151 ? -11.98600 1.32800   31.31600  1.000 31.72000 ? 153 ASP A C   1 
ATOM   1143 O O   . ASP A 1 151 ? -12.60400 0.40700   31.85900  1.000 33.42000 ? 153 ASP A O   1 
ATOM   1144 C CB  . ASP A 1 151 ? -14.01900 2.37300   30.24800  1.000 33.51000 ? 153 ASP A CB  1 
ATOM   1145 C CG  . ASP A 1 151 ? -14.27000 3.19800   31.50900  1.000 49.70000 ? 153 ASP A CG  1 
ATOM   1146 O OD1 . ASP A 1 151 ? -13.31300 3.80100   32.05000  1.000 50.63000 ? 153 ASP A OD1 1 
ATOM   1147 O OD2 . ASP A 1 151 ? -15.44100 3.24000   31.96200  1.000 55.48000 ? 153 ASP A OD2 1 
ATOM   1148 N N   . TYR A 1 152 ? -10.80700 1.78000   31.75800  1.000 32.10000 ? 154 TYR A N   1 
ATOM   1149 C CA  . TYR A 1 152 ? -10.18700 1.31400   32.99700  1.000 31.86000 ? 154 TYR A CA  1 
ATOM   1150 C C   . TYR A 1 152 ? -10.26600 -0.20500  33.13000  1.000 34.45000 ? 154 TYR A C   1 
ATOM   1151 O O   . TYR A 1 152 ? -11.07100 -0.72200  33.91500  1.000 37.90000 ? 154 TYR A O   1 
ATOM   1152 C CB  . TYR A 1 152 ? -10.85000 1.98300   34.20300  1.000 35.23000 ? 154 TYR A CB  1 
ATOM   1153 N N   . ASP A 1 153 ? -9.47500  -0.92100  32.33000  1.000 35.35000 ? 155 ASP A N   1 
ATOM   1154 C CA  . ASP A 1 153 ? -9.38700  -2.38200  32.37500  1.000 37.29000 ? 155 ASP A CA  1 
ATOM   1155 C C   . ASP A 1 153 ? -10.62500 -3.12100  31.85500  1.000 29.65000 ? 155 ASP A C   1 
ATOM   1156 O O   . ASP A 1 153 ? -10.54500 -4.33400  31.62000  1.000 31.92000 ? 155 ASP A O   1 
ATOM   1157 C CB  . ASP A 1 153 ? -9.08300  -2.85400  33.80300  1.000 42.44000 ? 155 ASP A CB  1 
ATOM   1158 C CG  . ASP A 1 153 ? -7.62900  -3.25600  33.99500  1.000 50.65000 ? 155 ASP A CG  1 
ATOM   1159 O OD1 . ASP A 1 153 ? -6.83300  -3.13700  33.03500  1.000 49.54000 ? 155 ASP A OD1 1 
ATOM   1160 O OD2 . ASP A 1 153 ? -7.28200  -3.69400  35.11600  1.000 59.19000 ? 155 ASP A OD2 1 
ATOM   1161 N N   . CYS A 1 154 ? -11.76900 -2.45000  31.67300  1.000 21.93000 ? 156 CYS A N   1 
ATOM   1162 C CA  . CYS A 1 154 ? -12.97600 -3.12400  31.18800  1.000 22.22000 ? 156 CYS A CA  1 
ATOM   1163 C C   . CYS A 1 154 ? -13.11500 -2.91900  29.68300  1.000 19.06000 ? 156 CYS A C   1 
ATOM   1164 O O   . CYS A 1 154 ? -13.18100 -1.77900  29.20600  1.000 17.90000 ? 156 CYS A O   1 
ATOM   1165 C CB  . CYS A 1 154 ? -14.23700 -2.63500  31.90500  1.000 21.36000 ? 156 CYS A CB  1 
ATOM   1166 S SG  . CYS A 1 154 ? -15.78400 -3.46300  31.34900  1.000 21.93000 ? 156 CYS A SG  1 
ATOM   1167 N N   . VAL A 1 155 ? -13.16900 -4.01600  28.93900  1.000 13.78000 ? 157 VAL A N   1 
ATOM   1168 C CA  . VAL A 1 155 ? -13.35100 -3.95700  27.49400  1.000 12.93000 ? 157 VAL A CA  1 
ATOM   1169 C C   . VAL A 1 155 ? -14.84600 -3.93900  27.19100  1.000 13.01000 ? 157 VAL A C   1 
ATOM   1170 O O   . VAL A 1 155 ? -15.57800 -4.84900  27.59100  1.000 12.78000 ? 157 VAL A O   1 
ATOM   1171 C CB  . VAL A 1 155 ? -12.66400 -5.14400  26.80000  1.000 11.75000 ? 157 VAL A CB  1 
ATOM   1172 C CG1 . VAL A 1 155 ? -12.80400 -5.01800  25.28800  1.000 7.51000  ? 157 VAL A CG1 1 
ATOM   1173 C CG2 . VAL A 1 155 ? -11.20700 -5.20600  27.19100  1.000 14.16000 ? 157 VAL A CG2 1 
ATOM   1174 N N   . SER A 1 156 ? -15.31100 -2.91200  26.48100  1.000 12.19000 ? 158 SER A N   1 
ATOM   1175 C CA  . SER A 1 156 ? -16.69500 -2.86400  26.00700  1.000 13.37000 ? 158 SER A CA  1 
ATOM   1176 C C   . SER A 1 156 ? -16.72100 -3.27100  24.53900  1.000 10.36000 ? 158 SER A C   1 
ATOM   1177 O O   . SER A 1 156 ? -16.31600 -2.49600  23.66800  1.000 11.67000 ? 158 SER A O   1 
ATOM   1178 C CB  . SER A 1 156 ? -17.30000 -1.46900  26.19900  1.000 14.72000 ? 158 SER A CB  1 
ATOM   1179 O OG  . SER A 1 156 ? -17.64200 -1.27600  27.55800  1.000 20.72000 ? 158 SER A OG  1 
ATOM   1180 N N   . PHE A 1 157 ? -17.17800 -4.48900  24.26100  1.000 11.04000 ? 159 PHE A N   1 
ATOM   1181 C CA  . PHE A 1 157 ? -17.33200 -4.93500  22.88300  1.000 8.85000  ? 159 PHE A CA  1 
ATOM   1182 C C   . PHE A 1 157 ? -18.60500 -4.34600  22.29200  1.000 10.31000 ? 159 PHE A C   1 
ATOM   1183 O O   . PHE A 1 157 ? -19.69000 -4.49600  22.86800  1.000 11.43000 ? 159 PHE A O   1 
ATOM   1184 C CB  . PHE A 1 157 ? -17.37800 -6.45900  22.81900  1.000 5.81000  ? 159 PHE A CB  1 
ATOM   1185 C CG  . PHE A 1 157 ? -16.09900 -7.11400  23.26100  1.000 10.41000 ? 159 PHE A CG  1 
ATOM   1186 C CD1 . PHE A 1 157 ? -15.01700 -7.20100  22.39400  1.000 7.37000  ? 159 PHE A CD1 1 
ATOM   1187 C CD2 . PHE A 1 157 ? -15.97400 -7.62400  24.54900  1.000 8.97000  ? 159 PHE A CD2 1 
ATOM   1188 C CE1 . PHE A 1 157 ? -13.83700 -7.81500  22.79300  1.000 6.26000  ? 159 PHE A CE1 1 
ATOM   1189 C CE2 . PHE A 1 157 ? -14.79400 -8.23300  24.95800  1.000 7.60000  ? 159 PHE A CE2 1 
ATOM   1190 C CZ  . PHE A 1 157 ? -13.72500 -8.32000  24.07000  1.000 8.00000  ? 159 PHE A CZ  1 
ATOM   1191 N N   . CYS A 1 158 ? -18.47800 -3.69400  21.13400  1.000 9.67000  ? 160 CYS A N   1 
ATOM   1192 C CA  . CYS A 1 158 ? -19.63500 -3.07300  20.49200  1.000 10.87000 ? 160 CYS A CA  1 
ATOM   1193 C C   . CYS A 1 158 ? -19.90700 -3.50400  19.06300  1.000 9.25000  ? 160 CYS A C   1 
ATOM   1194 O O   . CYS A 1 158 ? -20.96400 -3.14100  18.53800  1.000 14.33000 ? 160 CYS A O   1 
ATOM   1195 C CB  . CYS A 1 158 ? -19.49100 -1.54400  20.48800  1.000 12.51000 ? 160 CYS A CB  1 
ATOM   1196 S SG  . CYS A 1 158 ? -17.99000 -0.96300  19.68000  1.000 15.60000 ? 160 CYS A SG  1 
ATOM   1197 N N   . TYR A 1 159 ? -18.99500 -4.20600  18.39600  1.000 7.88000  ? 161 TYR A N   1 
ATOM   1198 C CA  . TYR A 1 159 ? -19.17100 -4.47800  16.97800  1.000 11.37000 ? 161 TYR A CA  1 
ATOM   1199 C C   . TYR A 1 159 ? -18.59600 -5.84300  16.65600  1.000 9.58000  ? 161 TYR A C   1 
ATOM   1200 O O   . TYR A 1 159 ? -17.53400 -6.20100  17.15900  1.000 8.70000  ? 161 TYR A O   1 
ATOM   1201 C CB  . TYR A 1 159 ? -18.48000 -3.41000  16.11200  1.000 9.44000  ? 161 TYR A CB  1 
ATOM   1202 C CG  . TYR A 1 159 ? -18.61100 -3.62700  14.61700  1.000 8.32000  ? 161 TYR A CG  1 
ATOM   1203 C CD1 . TYR A 1 159 ? -19.77800 -3.26500  13.94000  1.000 9.58000  ? 161 TYR A CD1 1 
ATOM   1204 C CD2 . TYR A 1 159 ? -17.56400 -4.16600  13.87700  1.000 10.34000 ? 161 TYR A CD2 1 
ATOM   1205 C CE1 . TYR A 1 159 ? -19.90100 -3.45200  12.57300  1.000 13.06000 ? 161 TYR A CE1 1 
ATOM   1206 C CE2 . TYR A 1 159 ? -17.68700 -4.37000  12.49500  1.000 9.37000  ? 161 TYR A CE2 1 
ATOM   1207 C CZ  . TYR A 1 159 ? -18.85500 -4.00700  11.85800  1.000 9.40000  ? 161 TYR A CZ  1 
ATOM   1208 O OH  . TYR A 1 159 ? -18.98700 -4.19100  10.50200  1.000 11.11000 ? 161 TYR A OH  1 
ATOM   1209 N N   . MET A 1 160 ? -19.28700 -6.59200  15.80500  1.000 8.40000  ? 162 MET A N   1 
ATOM   1210 C CA  . MET A 1 160 ? -18.71400 -7.79200  15.21800  1.000 8.17000  ? 162 MET A CA  1 
ATOM   1211 C C   . MET A 1 160 ? -18.96400 -7.74400  13.71900  1.000 7.27000  ? 162 MET A C   1 
ATOM   1212 O O   . MET A 1 160 ? -20.07900 -7.45400  13.29300  1.000 7.71000  ? 162 MET A O   1 
ATOM   1213 C CB  . MET A 1 160 ? -19.31600 -9.06000  15.81000  1.000 9.70000  ? 162 MET A CB  1 
ATOM   1214 C CG  . MET A 1 160 ? -18.83200 -10.32800 15.07000  1.000 11.26000 ? 162 MET A CG  1 
ATOM   1215 S SD  . MET A 1 160 ? -19.33200 -11.82300 15.96100  1.000 17.78000 ? 162 MET A SD  1 
ATOM   1216 C CE  . MET A 1 160 ? -17.96500 -12.01000 17.10500  1.000 13.43000 ? 162 MET A CE  1 
ATOM   1217 N N   . HIS A 1 161 ? -17.93300 -8.01000  12.93000  1.000 6.99000  ? 163 HIS A N   1 
ATOM   1218 C CA  . HIS A 1 161 ? -18.00400 -7.73300  11.50300  1.000 9.35000  ? 163 HIS A CA  1 
ATOM   1219 C C   . HIS A 1 161 ? -18.71600 -8.85700  10.75100  1.000 11.70000 ? 163 HIS A C   1 
ATOM   1220 O O   . HIS A 1 161 ? -18.41000 -10.03500 10.94700  1.000 7.90000  ? 163 HIS A O   1 
ATOM   1221 C CB  . HIS A 1 161 ? -16.60800 -7.54100  10.93000  1.000 8.05000  ? 163 HIS A CB  1 
ATOM   1222 C CG  . HIS A 1 161 ? -16.61700 -7.21600  9.47400   1.000 12.19000 ? 163 HIS A CG  1 
ATOM   1223 N ND1 . HIS A 1 161 ? -17.38500 -6.19800  8.95400   1.000 13.06000 ? 163 HIS A ND1 1 
ATOM   1224 C CD2 . HIS A 1 161 ? -15.97900 -7.78200  8.42700   1.000 12.48000 ? 163 HIS A CD2 1 
ATOM   1225 C CE1 . HIS A 1 161 ? -17.21400 -6.15000  7.64600   1.000 13.14000 ? 163 HIS A CE1 1 
ATOM   1226 N NE2 . HIS A 1 161 ? -16.36100 -7.09500  7.30100   1.000 12.07000 ? 163 HIS A NE2 1 
ATOM   1227 N N   . HIS A 1 162 ? -19.65600 -8.49600  9.86600   1.000 8.76000  ? 164 HIS A N   1 
ATOM   1228 C CA  . HIS A 1 162 ? -20.36700 -9.53000  9.11400   1.000 10.35000 ? 164 HIS A CA  1 
ATOM   1229 C C   . HIS A 1 162 ? -20.26400 -9.40400  7.60300   1.000 14.95000 ? 164 HIS A C   1 
ATOM   1230 O O   . HIS A 1 162 ? -20.29500 -10.44000 6.91800   1.000 14.68000 ? 164 HIS A O   1 
ATOM   1231 C CB  . HIS A 1 162 ? -21.86700 -9.55400  9.46400   1.000 8.22000  ? 164 HIS A CB  1 
ATOM   1232 C CG  . HIS A 1 162 ? -22.18300 -10.06100 10.83300  1.000 11.17000 ? 164 HIS A CG  1 
ATOM   1233 N ND1 . HIS A 1 162 ? -23.03200 -11.12600 11.05100  1.000 11.13000 ? 164 HIS A ND1 1 
ATOM   1234 C CD2 . HIS A 1 162 ? -21.78700 -9.63500  12.06000  1.000 11.38000 ? 164 HIS A CD2 1 
ATOM   1235 C CE1 . HIS A 1 162 ? -23.13800 -11.34000 12.35200  1.000 11.44000 ? 164 HIS A CE1 1 
ATOM   1236 N NE2 . HIS A 1 162 ? -22.38500 -10.45500 12.98500  1.000 11.37000 ? 164 HIS A NE2 1 
ATOM   1237 N N   . MET A 1 163 ? -20.15900 -8.19100  7.05100   1.000 12.18000 ? 165 MET A N   1 
ATOM   1238 C CA  . MET A 1 163 ? -20.28900 -8.09300  5.60500   1.000 14.95000 ? 165 MET A CA  1 
ATOM   1239 C C   . MET A 1 163 ? -19.86400 -6.72400  5.08900   1.000 18.43000 ? 165 MET A C   1 
ATOM   1240 O O   . MET A 1 163 ? -19.74200 -5.74700  5.84400   1.000 14.35000 ? 165 MET A O   1 
ATOM   1241 C CB  . MET A 1 163 ? -21.72600 -8.38700  5.17100   1.000 20.75000 ? 165 MET A CB  1 
ATOM   1242 C CG  . MET A 1 163 ? -22.75900 -7.46800  5.78300   1.000 21.85000 ? 165 MET A CG  1 
ATOM   1243 S SD  . MET A 1 163 ? -24.43800 -8.13500  5.60600   1.000 26.89000 ? 165 MET A SD  1 
ATOM   1244 C CE  . MET A 1 163 ? -24.37500 -8.75900  3.91800   1.000 32.71000 ? 165 MET A CE  1 
ATOM   1245 N N   . GLU A 1 164 ? -19.65400 -6.68000  3.77300   1.000 17.54000 ? 166 GLU A N   1 
ATOM   1246 C CA  . GLU A 1 164 ? -19.31700 -5.47200  3.03500   1.000 20.45000 ? 166 GLU A CA  1 
ATOM   1247 C C   . GLU A 1 164 ? -20.45200 -5.15400  2.06900   1.000 21.80000 ? 166 GLU A C   1 
ATOM   1248 O O   . GLU A 1 164 ? -20.96100 -6.04600  1.37800   1.000 22.62000 ? 166 GLU A O   1 
ATOM   1249 C CB  . GLU A 1 164 ? -18.00100 -5.64700  2.27800   1.000 19.40000 ? 166 GLU A CB  1 
ATOM   1250 C CG  . GLU A 1 164 ? -17.52900 -4.40200  1.55100   1.000 23.05000 ? 166 GLU A CG  1 
ATOM   1251 C CD  . GLU A 1 164 ? -16.14700 -4.57000  0.94200   1.000 27.93000 ? 166 GLU A CD  1 
ATOM   1252 O OE1 . GLU A 1 164 ? -16.02300 -4.38100  -0.28400  1.000 37.31000 ? 166 GLU A OE1 1 
ATOM   1253 O OE2 . GLU A 1 164 ? -15.18000 -4.88800  1.67900   1.000 31.45000 ? 166 GLU A OE2 1 
ATOM   1254 N N   . LEU A 1 165 ? -20.85200 -3.89600  2.03700   1.000 22.79000 ? 167 LEU A N   1 
ATOM   1255 C CA  . LEU A 1 165 ? -21.86700 -3.43000  1.11000   1.000 24.58000 ? 167 LEU A CA  1 
ATOM   1256 C C   . LEU A 1 165 ? -21.23200 -3.09700  -0.23900  1.000 25.19000 ? 167 LEU A C   1 
ATOM   1257 O O   . LEU A 1 165 ? -20.01900 -2.91000  -0.33200  1.000 22.40000 ? 167 LEU A O   1 
ATOM   1258 C CB  . LEU A 1 165 ? -22.57500 -2.21400  1.69700   1.000 28.40000 ? 167 LEU A CB  1 
ATOM   1259 C CG  . LEU A 1 165 ? -23.23900 -2.44800  3.05500   1.000 26.65000 ? 167 LEU A CG  1 
ATOM   1260 C CD1 . LEU A 1 165 ? -24.18900 -1.31000  3.34000   1.000 29.09000 ? 167 LEU A CD1 1 
ATOM   1261 C CD2 . LEU A 1 165 ? -23.97800 -3.79200  3.09500   1.000 25.48000 ? 167 LEU A CD2 1 
ATOM   1262 N N   . PRO A 1 166 ? -22.02700 -3.06500  -1.31900  1.000 30.39000 ? 168 PRO A N   1 
ATOM   1263 C CA  . PRO A 1 166 ? -21.45100 -2.73100  -2.63800  1.000 30.81000 ? 168 PRO A CA  1 
ATOM   1264 C C   . PRO A 1 166 ? -20.65300 -1.43300  -2.66400  1.000 29.50000 ? 168 PRO A C   1 
ATOM   1265 O O   . PRO A 1 166 ? -19.68400 -1.33900  -3.42800  1.000 35.39000 ? 168 PRO A O   1 
ATOM   1266 C CB  . PRO A 1 166 ? -22.68300 -2.66800  -3.56100  1.000 30.81000 ? 168 PRO A CB  1 
ATOM   1267 C CG  . PRO A 1 166 ? -23.90000 -2.86100  -2.66000  1.000 36.04000 ? 168 PRO A CG  1 
ATOM   1268 C CD  . PRO A 1 166 ? -23.40700 -3.56000  -1.43000  1.000 27.61000 ? 168 PRO A CD  1 
ATOM   1269 N N   . THR A 1 167 ? -20.99500 -0.44100  -1.83700  1.000 28.16000 ? 169 THR A N   1 
ATOM   1270 C CA  . THR A 1 167 ? -20.22100 0.79800   -1.82100  1.000 28.94000 ? 169 THR A CA  1 
ATOM   1271 C C   . THR A 1 167 ? -18.85300 0.63300   -1.17800  1.000 32.03000 ? 169 THR A C   1 
ATOM   1272 O O   . THR A 1 167 ? -18.07100 1.59100   -1.17900  1.000 35.29000 ? 169 THR A O   1 
ATOM   1273 C CB  . THR A 1 167 ? -20.98100 1.90900   -1.08800  1.000 31.98000 ? 169 THR A CB  1 
ATOM   1274 O OG1 . THR A 1 167 ? -21.45800 1.41900   0.17100   1.000 32.01000 ? 169 THR A OG1 1 
ATOM   1275 C CG2 . THR A 1 167 ? -22.17000 2.38400   -1.92300  1.000 29.63000 ? 169 THR A CG2 1 
ATOM   1276 N N   . GLY A 1 168 ? -18.54100 -0.53900  -0.62400  1.000 29.53000 ? 170 GLY A N   1 
ATOM   1277 C CA  . GLY A 1 168 ? -17.26000 -0.74700  0.01600   1.000 26.23000 ? 170 GLY A CA  1 
ATOM   1278 C C   . GLY A 1 168 ? -17.22300 -0.45700  1.50200   1.000 25.93000 ? 170 GLY A C   1 
ATOM   1279 O O   . GLY A 1 168 ? -16.16200 -0.62500  2.11900   1.000 29.24000 ? 170 GLY A O   1 
ATOM   1280 N N   . VAL A 1 169 ? -18.33600 -0.02300  2.09900   1.000 23.60000 ? 171 VAL A N   1 
ATOM   1281 C CA  . VAL A 1 169 ? -18.40400 0.17300   3.54500   1.000 19.10000 ? 171 VAL A CA  1 
ATOM   1282 C C   . VAL A 1 169 ? -18.90700 -1.10800  4.19400   1.000 19.18000 ? 171 VAL A C   1 
ATOM   1283 O O   . VAL A 1 169 ? -19.29100 -2.05900  3.50400   1.000 18.98000 ? 171 VAL A O   1 
ATOM   1284 C CB  . VAL A 1 169 ? -19.30500 1.36100   3.92300   1.000 18.01000 ? 171 VAL A CB  1 
ATOM   1285 C CG1 . VAL A 1 169 ? -18.69200 2.66700   3.42000   1.000 25.92000 ? 171 VAL A CG1 1 
ATOM   1286 C CG2 . VAL A 1 169 ? -20.69800 1.15900   3.36900   1.000 21.17000 ? 171 VAL A CG2 1 
ATOM   1287 N N   . HIS A 1 170 ? -18.94600 -1.13300  5.52300   1.000 16.66000 ? 172 HIS A N   1 
ATOM   1288 C CA  . HIS A 1 170 ? -19.09800 -2.39200  6.22900   1.000 15.49000 ? 172 HIS A CA  1 
ATOM   1289 C C   . HIS A 1 170 ? -20.25600 -2.33800  7.21000   1.000 14.92000 ? 172 HIS A C   1 
ATOM   1290 O O   . HIS A 1 170 ? -20.61400 -1.27800  7.72800   1.000 16.35000 ? 172 HIS A O   1 
ATOM   1291 C CB  . HIS A 1 170 ? -17.78500 -2.73400  6.89800   1.000 14.29000 ? 172 HIS A CB  1 
ATOM   1292 C CG  . HIS A 1 170 ? -16.67100 -2.87000  5.91400   1.000 15.20000 ? 172 HIS A CG  1 
ATOM   1293 N ND1 . HIS A 1 170 ? -15.70400 -1.90500  5.73900   1.000 18.65000 ? 172 HIS A ND1 1 
ATOM   1294 C CD2 . HIS A 1 170 ? -16.40300 -3.84100  5.00900   1.000 17.47000 ? 172 HIS A CD2 1 
ATOM   1295 C CE1 . HIS A 1 170 ? -14.86800 -2.29100  4.79300   1.000 20.93000 ? 172 HIS A CE1 1 
ATOM   1296 N NE2 . HIS A 1 170 ? -15.26900 -3.46300  4.33400   1.000 18.97000 ? 172 HIS A NE2 1 
ATOM   1297 N N   . ALA A 1 171 ? -20.83500 -3.51100  7.45100   1.000 12.06000 ? 173 ALA A N   1 
ATOM   1298 C CA  . ALA A 1 171 ? -21.99800 -3.66900  8.29800   1.000 12.74000 ? 173 ALA A CA  1 
ATOM   1299 C C   . ALA A 1 171 ? -21.79600 -4.86300  9.22000   1.000 11.92000 ? 173 ALA A C   1 
ATOM   1300 O O   . ALA A 1 171 ? -21.14000 -5.84500  8.86200   1.000 11.60000 ? 173 ALA A O   1 
ATOM   1301 C CB  . ALA A 1 171 ? -23.26600 -3.85900  7.47700   1.000 15.90000 ? 173 ALA A CB  1 
ATOM   1302 N N   . GLY A 1 172 ? -22.37300 -4.77100  10.40600  1.000 12.07000 ? 174 GLY A N   1 
ATOM   1303 C CA  . GLY A 1 172 ? -22.17100 -5.82100  11.38200  1.000 10.48000 ? 174 GLY A CA  1 
ATOM   1304 C C   . GLY A 1 172 ? -23.14300 -5.67800  12.52300  1.000 10.86000 ? 174 GLY A C   1 
ATOM   1305 O O   . GLY A 1 172 ? -24.07600 -4.87700  12.47600  1.000 11.26000 ? 174 GLY A O   1 
ATOM   1306 N N   . THR A 1 173 ? -22.89200 -6.44500  13.57800  1.000 9.91000  ? 175 THR A N   1 
ATOM   1307 C CA  . THR A 1 173 ? -23.83100 -6.53700  14.67800  1.000 10.63000 ? 175 THR A CA  1 
ATOM   1308 C C   . THR A 1 173 ? -23.18400 -6.05400  15.96600  1.000 9.50000  ? 175 THR A C   1 
ATOM   1309 O O   . THR A 1 173 ? -21.97600 -5.84900  16.04000  1.000 10.04000 ? 175 THR A O   1 
ATOM   1310 C CB  . THR A 1 173 ? -24.31200 -7.98200  14.85100  1.000 10.21000 ? 175 THR A CB  1 
ATOM   1311 O OG1 . THR A 1 173 ? -23.17400 -8.81200  15.14200  1.000 9.51000  ? 175 THR A OG1 1 
ATOM   1312 C CG2 . THR A 1 173 ? -24.99500 -8.44800  13.55600  1.000 13.13000 ? 175 THR A CG2 1 
ATOM   1313 N N   . ASP A 1 174 ? -23.99800 -5.90600  17.00400  1.000 7.35000  ? 176 ASP A N   1 
ATOM   1314 C CA  . ASP A 1 174 ? -23.41500 -5.83400  18.33300  1.000 11.96000 ? 176 ASP A CA  1 
ATOM   1315 C C   . ASP A 1 174 ? -23.12700 -7.27000  18.77700  1.000 10.54000 ? 176 ASP A C   1 
ATOM   1316 O O   . ASP A 1 174 ? -23.32500 -8.23200  18.02400  1.000 10.92000 ? 176 ASP A O   1 
ATOM   1317 C CB  . ASP A 1 174 ? -24.32500 -5.06100  19.28900  1.000 11.94000 ? 176 ASP A CB  1 
ATOM   1318 C CG  . ASP A 1 174 ? -25.72100 -5.69500  19.44500  1.000 18.15000 ? 176 ASP A CG  1 
ATOM   1319 O OD1 . ASP A 1 174 ? -25.89600 -6.91000  19.18600  1.000 15.15000 ? 176 ASP A OD1 1 
ATOM   1320 O OD2 . ASP A 1 174 ? -26.65400 -4.96600  19.84200  1.000 18.48000 ? 176 ASP A OD2 1 
ATOM   1321 N N   . LEU A 1 175 ? -22.67000 -7.44800  19.99900  1.000 9.11000  ? 177 LEU A N   1 
ATOM   1322 C CA  . LEU A 1 175 ? -22.31600 -8.80300  20.39600  1.000 11.08000 ? 177 LEU A CA  1 
ATOM   1323 C C   . LEU A 1 175 ? -23.51900 -9.60800  20.87100  1.000 16.06000 ? 177 LEU A C   1 
ATOM   1324 O O   . LEU A 1 175 ? -23.34700 -10.75900 21.27400  1.000 14.98000 ? 177 LEU A O   1 
ATOM   1325 C CB  . LEU A 1 175 ? -21.23400 -8.77000  21.47600  1.000 10.94000 ? 177 LEU A CB  1 
ATOM   1326 C CG  . LEU A 1 175 ? -19.79300 -8.88200  20.95400  1.000 13.22000 ? 177 LEU A CG  1 
ATOM   1327 C CD1 . LEU A 1 175 ? -19.55800 -10.22100 20.31500  1.000 15.55000 ? 177 LEU A CD1 1 
ATOM   1328 C CD2 . LEU A 1 175 ? -19.50400 -7.78300  19.95700  1.000 10.70000 ? 177 LEU A CD2 1 
ATOM   1329 N N   . GLU A 1 176 ? -24.72100 -9.03400  20.85700  1.000 15.71000 ? 178 GLU A N   1 
ATOM   1330 C CA  . GLU A 1 176 ? -25.93700 -9.81800  20.99600  1.000 16.63000 ? 178 GLU A CA  1 
ATOM   1331 C C   . GLU A 1 176 ? -26.51500 -10.18800 19.64700  1.000 15.38000 ? 178 GLU A C   1 
ATOM   1332 O O   . GLU A 1 176 ? -27.63900 -10.68800 19.58600  1.000 19.33000 ? 178 GLU A O   1 
ATOM   1333 C CB  . GLU A 1 176 ? -26.98100 -9.07000  21.82400  1.000 18.75000 ? 178 GLU A CB  1 
ATOM   1334 C CG  . GLU A 1 176 ? -26.48900 -8.62900  23.18200  1.000 23.51000 ? 178 GLU A CG  1 
ATOM   1335 C CD  . GLU A 1 176 ? -27.57700 -7.94400  23.98900  1.000 36.17000 ? 178 GLU A CD  1 
ATOM   1336 O OE1 . GLU A 1 176 ? -27.62300 -8.14300  25.22300  1.000 44.03000 ? 178 GLU A OE1 1 
ATOM   1337 O OE2 . GLU A 1 176 ? -28.40100 -7.22100  23.38200  1.000 30.27000 ? 178 GLU A OE2 1 
ATOM   1338 N N   . GLY A 1 177 ? -25.77700 -9.94300  18.56500  1.000 11.65000 ? 179 GLY A N   1 
ATOM   1339 C CA  . GLY A 1 177 ? -26.21000 -10.35000 17.24800  1.000 13.75000 ? 179 GLY A CA  1 
ATOM   1340 C C   . GLY A 1 177 ? -27.21200 -9.44600  16.56600  1.000 15.14000 ? 179 GLY A C   1 
ATOM   1341 O O   . GLY A 1 177 ? -27.73800 -9.82800  15.52100  1.000 14.05000 ? 179 GLY A O   1 
ATOM   1342 N N   . ASN A 1 178 ? -27.49800 -8.26400  17.10700  1.000 15.62000 ? 180 ASN A N   1 
ATOM   1343 C CA  . ASN A 1 178 ? -28.43700 -7.34900  16.45900  1.000 15.93000 ? 180 ASN A CA  1 
ATOM   1344 C C   . ASN A 1 178 ? -27.66600 -6.44200  15.50800  1.000 14.78000 ? 180 ASN A C   1 
ATOM   1345 O O   . ASN A 1 178 ? -26.75400 -5.72900  15.93200  1.000 11.88000 ? 180 ASN A O   1 
ATOM   1346 C CB  . ASN A 1 178 ? -29.20000 -6.52000  17.49500  1.000 18.41000 ? 180 ASN A CB  1 
ATOM   1347 C CG  . ASN A 1 178 ? -30.14600 -7.37400  18.33800  1.000 22.30000 ? 180 ASN A CG  1 
ATOM   1348 O OD1 . ASN A 1 178 ? -30.90700 -8.17400  17.80600  1.000 23.09000 ? 180 ASN A OD1 1 
ATOM   1349 N ND2 . ASN A 1 178 ? -30.07500 -7.22500  19.65500  1.000 23.41000 ? 180 ASN A ND2 1 
ATOM   1350 N N   . PHE A 1 179 ? -28.01500 -6.48800  14.22600  1.000 13.70000 ? 181 PHE A N   1 
ATOM   1351 C CA  . PHE A 1 179 ? -27.34800 -5.63600  13.25700  1.000 14.55000 ? 181 PHE A CA  1 
ATOM   1352 C C   . PHE A 1 179 ? -27.49600 -4.17600  13.65300  1.000 13.12000 ? 181 PHE A C   1 
ATOM   1353 O O   . PHE A 1 179 ? -28.51000 -3.76300  14.22200  1.000 14.85000 ? 181 PHE A O   1 
ATOM   1354 C CB  . PHE A 1 179 ? -27.91400 -5.85600  11.85400  1.000 12.06000 ? 181 PHE A CB  1 
ATOM   1355 C CG  . PHE A 1 179 ? -27.08800 -6.77800  11.00700  1.000 15.56000 ? 181 PHE A CG  1 
ATOM   1356 C CD1 . PHE A 1 179 ? -25.99800 -6.30100  10.29500  1.000 11.67000 ? 181 PHE A CD1 1 
ATOM   1357 C CD2 . PHE A 1 179 ? -27.39000 -8.13900  10.94400  1.000 12.39000 ? 181 PHE A CD2 1 
ATOM   1358 C CE1 . PHE A 1 179 ? -25.22900 -7.15500  9.51700   1.000 13.94000 ? 181 PHE A CE1 1 
ATOM   1359 C CE2 . PHE A 1 179 ? -26.62700 -9.00300  10.17700  1.000 11.62000 ? 181 PHE A CE2 1 
ATOM   1360 C CZ  . PHE A 1 179 ? -25.54800 -8.51700  9.45300   1.000 11.60000 ? 181 PHE A CZ  1 
ATOM   1361 N N   . TYR A 1 180 ? -26.43200 -3.41700  13.43000  1.000 15.88000 ? 182 TYR A N   1 
ATOM   1362 C CA  . TYR A 1 180 ? -26.54500 -1.97100  13.37900  1.000 17.01000 ? 182 TYR A CA  1 
ATOM   1363 C C   . TYR A 1 180 ? -27.22000 -1.59900  12.06900  1.000 14.75000 ? 182 TYR A C   1 
ATOM   1364 O O   . TYR A 1 180 ? -26.79200 -2.04400  11.00000  1.000 15.11000 ? 182 TYR A O   1 
ATOM   1365 C CB  . TYR A 1 180 ? -25.17000 -1.32400  13.47500  1.000 11.98000 ? 182 TYR A CB  1 
ATOM   1366 C CG  . TYR A 1 180 ? -24.58900 -1.42600  14.85500  1.000 11.47000 ? 182 TYR A CG  1 
ATOM   1367 C CD1 . TYR A 1 180 ? -24.98700 -0.54100  15.85500  1.000 12.71000 ? 182 TYR A CD1 1 
ATOM   1368 C CD2 . TYR A 1 180 ? -23.65700 -2.41400  15.17200  1.000 12.22000 ? 182 TYR A CD2 1 
ATOM   1369 C CE1 . TYR A 1 180 ? -24.48000 -0.62200  17.12900  1.000 15.78000 ? 182 TYR A CE1 1 
ATOM   1370 C CE2 . TYR A 1 180 ? -23.13700 -2.51400  16.46800  1.000 12.29000 ? 182 TYR A CE2 1 
ATOM   1371 C CZ  . TYR A 1 180 ? -23.55400 -1.60400  17.43700  1.000 10.27000 ? 182 TYR A CZ  1 
ATOM   1372 O OH  . TYR A 1 180 ? -23.08000 -1.65800  18.71800  1.000 11.23000 ? 182 TYR A OH  1 
ATOM   1373 N N   . GLY A 1 181 ? -28.28400 -0.81000  12.15200  1.000 16.09000 ? 183 GLY A N   1 
ATOM   1374 C CA  . GLY A 1 181 ? -28.95700 -0.34200  10.95900  1.000 19.68000 ? 183 GLY A CA  1 
ATOM   1375 C C   . GLY A 1 181 ? -29.89000 -1.37100  10.36100  1.000 21.88000 ? 183 GLY A C   1 
ATOM   1376 O O   . GLY A 1 181 ? -30.20600 -2.39200  10.98100  1.000 19.32000 ? 183 GLY A O   1 
ATOM   1377 N N   . PRO A 1 182 ? -30.35600 -1.11400  9.12800   1.000 23.63000 ? 184 PRO A N   1 
ATOM   1378 C CA  . PRO A 1 182 ? -31.43600 -1.93300  8.56000   1.000 26.64000 ? 184 PRO A CA  1 
ATOM   1379 C C   . PRO A 1 182 ? -30.94200 -3.12600  7.75600   1.000 28.34000 ? 184 PRO A C   1 
ATOM   1380 O O   . PRO A 1 182 ? -31.61000 -3.55600  6.81400   1.000 37.24000 ? 184 PRO A O   1 
ATOM   1381 C CB  . PRO A 1 182 ? -32.17600 -0.93300  7.66300   1.000 27.24000 ? 184 PRO A CB  1 
ATOM   1382 C CG  . PRO A 1 182 ? -31.06200 -0.02900  7.15400   1.000 25.17000 ? 184 PRO A CG  1 
ATOM   1383 C CD  . PRO A 1 182 ? -30.03800 0.05300   8.28200   1.000 21.07000 ? 184 PRO A CD  1 
ATOM   1384 N N   . PHE A 1 183 ? -29.78400 -3.67200  8.09900   1.000 24.45000 ? 185 PHE A N   1 
ATOM   1385 C CA  . PHE A 1 183 ? -29.20100 -4.73100  7.29700   1.000 21.93000 ? 185 PHE A CA  1 
ATOM   1386 C C   . PHE A 1 183 ? -29.55300 -6.10200  7.87100   1.000 18.89000 ? 185 PHE A C   1 
ATOM   1387 O O   . PHE A 1 183 ? -29.91200 -6.24400  9.04200   1.000 18.27000 ? 185 PHE A O   1 
ATOM   1388 C CB  . PHE A 1 183 ? -27.68700 -4.55400  7.20000   1.000 21.94000 ? 185 PHE A CB  1 
ATOM   1389 C CG  . PHE A 1 183 ? -27.27400 -3.17300  6.79600   1.000 22.95000 ? 185 PHE A CG  1 
ATOM   1390 C CD1 . PHE A 1 183 ? -27.47300 -2.73000  5.49700   1.000 21.49000 ? 185 PHE A CD1 1 
ATOM   1391 C CD2 . PHE A 1 183 ? -26.71500 -2.30400  7.72100   1.000 17.33000 ? 185 PHE A CD2 1 
ATOM   1392 C CE1 . PHE A 1 183 ? -27.11000 -1.44700  5.12200   1.000 27.69000 ? 185 PHE A CE1 1 
ATOM   1393 C CE2 . PHE A 1 183 ? -26.33700 -1.03500  7.35400   1.000 21.42000 ? 185 PHE A CE2 1 
ATOM   1394 C CZ  . PHE A 1 183 ? -26.53700 -0.60000  6.04500   1.000 24.09000 ? 185 PHE A CZ  1 
ATOM   1395 N N   . VAL A 1 184 ? -29.48000 -7.10700  7.00300   1.000 20.69000 ? 186 VAL A N   1 
ATOM   1396 C CA  . VAL A 1 184 ? -29.76200 -8.49400  7.35200   1.000 18.67000 ? 186 VAL A CA  1 
ATOM   1397 C C   . VAL A 1 184 ? -28.62900 -9.34300  6.80100   1.000 17.41000 ? 186 VAL A C   1 
ATOM   1398 O O   . VAL A 1 184 ? -27.96400 -8.96400  5.83200   1.000 16.28000 ? 186 VAL A O   1 
ATOM   1399 C CB  . VAL A 1 184 ? -31.13000 -8.96400  6.79700   1.000 20.38000 ? 186 VAL A CB  1 
ATOM   1400 C CG1 . VAL A 1 184 ? -32.25800 -8.09300  7.34100   1.000 22.09000 ? 186 VAL A CG1 1 
ATOM   1401 C CG2 . VAL A 1 184 ? -31.13100 -8.92700  5.27800   1.000 21.39000 ? 186 VAL A CG2 1 
ATOM   1402 N N   . ASP A 1 185 ? -28.39000 -10.50400 7.42500   1.000 18.18000 ? 187 ASP A N   1 
ATOM   1403 C CA  . ASP A 1 185 ? -27.32100 -11.37300 6.93800   1.000 16.62000 ? 187 ASP A CA  1 
ATOM   1404 C C   . ASP A 1 185 ? -27.88800 -12.29700 5.86000   1.000 22.00000 ? 187 ASP A C   1 
ATOM   1405 O O   . ASP A 1 185 ? -28.12900 -13.48900 6.06500   1.000 21.45000 ? 187 ASP A O   1 
ATOM   1406 C CB  . ASP A 1 185 ? -26.63700 -12.13900 8.07500   1.000 16.22000 ? 187 ASP A CB  1 
ATOM   1407 C CG  . ASP A 1 185 ? -27.60400 -12.81800 9.03600   1.000 14.65000 ? 187 ASP A CG  1 
ATOM   1408 O OD1 . ASP A 1 185 ? -28.83700 -12.67700 8.91600   1.000 17.47000 ? 187 ASP A OD1 1 
ATOM   1409 O OD2 . ASP A 1 185 ? -27.10400 -13.51400 9.94600   1.000 16.60000 ? 187 ASP A OD2 1 
ATOM   1410 N N   . ARG A 1 186 ? -28.09900 -11.71000 4.68300   1.000 18.54000 ? 188 ARG A N   1 
ATOM   1411 C CA  . ARG A 1 186 ? -28.40700 -12.43000 3.45600   1.000 26.51000 ? 188 ARG A CA  1 
ATOM   1412 C C   . ARG A 1 186 ? -27.58900 -11.80100 2.34400   1.000 29.47000 ? 188 ARG A C   1 
ATOM   1413 O O   . ARG A 1 186 ? -27.33900 -10.59200 2.36800   1.000 25.42000 ? 188 ARG A O   1 
ATOM   1414 C CB  . ARG A 1 186 ? -29.89300 -12.36100 3.10600   1.000 27.56000 ? 188 ARG A CB  1 
ATOM   1415 C CG  . ARG A 1 186 ? -30.81500 -12.68300 4.26000   1.000 30.41000 ? 188 ARG A CG  1 
ATOM   1416 C CD  . ARG A 1 186 ? -32.22400 -12.21600 3.96900   1.000 35.52000 ? 188 ARG A CD  1 
ATOM   1417 N NE  . ARG A 1 186 ? -32.51700 -12.33300 2.54600   1.000 40.04000 ? 188 ARG A NE  1 
ATOM   1418 C CZ  . ARG A 1 186 ? -33.63200 -11.89400 1.97100   1.000 48.72000 ? 188 ARG A CZ  1 
ATOM   1419 N NH1 . ARG A 1 186 ? -34.57600 -11.31300 2.70300   1.000 49.50000 ? 188 ARG A NH1 1 
ATOM   1420 N NH2 . ARG A 1 186 ? -33.80300 -12.04100 0.66400   1.000 43.13000 ? 188 ARG A NH2 1 
ATOM   1421 N N   . GLN A 1 187 ? -27.15600 -12.61300 1.38200   1.000 25.77000 ? 189 GLN A N   1 
ATOM   1422 C CA  . GLN A 1 187 ? -26.28900 -12.11600 0.31400   1.000 33.90000 ? 189 GLN A CA  1 
ATOM   1423 C C   . GLN A 1 187 ? -27.16000 -11.57800 -0.82000  1.000 38.78000 ? 189 GLN A C   1 
ATOM   1424 O O   . GLN A 1 187 ? -27.24600 -12.13300 -1.91700  1.000 39.99000 ? 189 GLN A O   1 
ATOM   1425 C CB  . GLN A 1 187 ? -25.33800 -13.20200 -0.16800  1.000 34.24000 ? 189 GLN A CB  1 
ATOM   1426 C CG  . GLN A 1 187 ? -24.24300 -12.67400 -1.08900  1.000 40.06000 ? 189 GLN A CG  1 
ATOM   1427 C CD  . GLN A 1 187 ? -23.03100 -13.57900 -1.12900  1.000 41.51000 ? 189 GLN A CD  1 
ATOM   1428 O OE1 . GLN A 1 187 ? -22.93000 -14.45000 -1.99500  1.000 43.37000 ? 189 GLN A OE1 1 
ATOM   1429 N NE2 . GLN A 1 187 ? -22.09500 -13.37800 -0.19000  1.000 32.37000 ? 189 GLN A NE2 1 
ATOM   1430 N N   . THR A 1 188 ? -27.82400 -10.47000 -0.51400  1.000 38.34000 ? 190 THR A N   1 
ATOM   1431 C CA  . THR A 1 188 ? -28.74000 -9.80400  -1.42000  1.000 38.95000 ? 190 THR A CA  1 
ATOM   1432 C C   . THR A 1 188 ? -28.31300 -8.35200  -1.59600  1.000 45.96000 ? 190 THR A C   1 
ATOM   1433 O O   . THR A 1 188 ? -27.43300 -7.84300  -0.89500  1.000 45.70000 ? 190 THR A O   1 
ATOM   1434 C CB  . THR A 1 188 ? -30.18300 -9.88100  -0.90000  1.000 35.12000 ? 190 THR A CB  1 
ATOM   1435 O OG1 . THR A 1 188 ? -30.34500 -8.97900  0.19800   1.000 43.85000 ? 190 THR A OG1 1 
ATOM   1436 C CG2 . THR A 1 188 ? -30.49900 -11.28300 -0.41700  1.000 38.57000 ? 190 THR A CG2 1 
ATOM   1437 N N   . ALA A 1 189 ? -28.94800 -7.68800  -2.55400  1.000 47.27000 ? 191 ALA A N   1 
ATOM   1438 C CA  . ALA A 1 189 ? -28.65400 -6.28900  -2.84600  1.000 46.24000 ? 191 ALA A CA  1 
ATOM   1439 C C   . ALA A 1 189 ? -29.13300 -5.43900  -1.67900  1.000 46.10000 ? 191 ALA A C   1 
ATOM   1440 O O   . ALA A 1 189 ? -30.32500 -5.15200  -1.54200  1.000 50.55000 ? 191 ALA A O   1 
ATOM   1441 C CB  . ALA A 1 189 ? -29.31400 -5.86000  -4.15100  1.000 47.09000 ? 191 ALA A CB  1 
ATOM   1442 N N   . GLN A 1 190 ? -28.20500 -5.06000  -0.81100  1.000 44.82000 ? 192 GLN A N   1 
ATOM   1443 C CA  . GLN A 1 190 ? -28.46300 -4.09100  0.23800   1.000 40.24000 ? 192 GLN A CA  1 
ATOM   1444 C C   . GLN A 1 190 ? -27.56800 -2.88900  -0.00400  1.000 39.63000 ? 192 GLN A C   1 
ATOM   1445 O O   . GLN A 1 190 ? -26.42200 -3.03300  -0.44200  1.000 40.76000 ? 192 GLN A O   1 
ATOM   1446 C CB  . GLN A 1 190 ? -28.19700 -4.66300  1.63000   1.000 32.55000 ? 192 GLN A CB  1 
ATOM   1447 C CG  . GLN A 1 190 ? -29.09500 -5.80700  2.00900   1.000 34.52000 ? 192 GLN A CG  1 
ATOM   1448 C CD  . GLN A 1 190 ? -28.62600 -6.49800  3.26500   1.000 27.06000 ? 192 GLN A CD  1 
ATOM   1449 O OE1 . GLN A 1 190 ? -28.95300 -6.07400  4.37600   1.000 24.09000 ? 192 GLN A OE1 1 
ATOM   1450 N NE2 . GLN A 1 190 ? -27.85400 -7.56700  3.10000   1.000 27.45000 ? 192 GLN A NE2 1 
ATOM   1451 N N   . ALA A 1 191 ? -28.09800 -1.70800  0.26500   1.000 40.87000 ? 193 ALA A N   1 
ATOM   1452 C CA  . ALA A 1 191 ? -27.35600 -0.47900  0.05200   1.000 43.40000 ? 193 ALA A CA  1 
ATOM   1453 C C   . ALA A 1 191 ? -27.41500 0.36200   1.31200   1.000 30.00000 ? 193 ALA A C   1 
ATOM   1454 O O   . ALA A 1 191 ? -28.45200 0.43000   1.98100   1.000 36.03000 ? 193 ALA A O   1 
ATOM   1455 C CB  . ALA A 1 191 ? -27.91100 0.31200   -1.13700  1.000 42.97000 ? 193 ALA A CB  1 
ATOM   1456 N N   . ALA A 1 192 ? -26.30000 1.00200   1.63300   1.000 36.85000 ? 194 ALA A N   1 
ATOM   1457 C CA  . ALA A 1 192 ? -26.30500 1.96800   2.71600   1.000 35.93000 ? 194 ALA A CA  1 
ATOM   1458 C C   . ALA A 1 192 ? -27.13400 3.17900   2.30500   1.000 39.08000 ? 194 ALA A C   1 
ATOM   1459 O O   . ALA A 1 192 ? -26.94600 3.72200   1.21200   1.000 39.45000 ? 194 ALA A O   1 
ATOM   1460 C CB  . ALA A 1 192 ? -24.87700 2.38300   3.05800   1.000 33.55000 ? 194 ALA A CB  1 
ATOM   1461 N N   . GLY A 1 193 ? -28.07200 3.58000   3.16100   1.000 36.60000 ? 195 GLY A N   1 
ATOM   1462 C CA  . GLY A 1 193 ? -28.77500 4.83200   2.96100   1.000 32.11000 ? 195 GLY A CA  1 
ATOM   1463 C C   . GLY A 1 193 ? -27.81800 6.01400   2.98800   1.000 35.36000 ? 195 GLY A C   1 
ATOM   1464 O O   . GLY A 1 193 ? -26.64700 5.90500   3.34800   1.000 29.34000 ? 195 GLY A O   1 
ATOM   1465 N N   . THR A 1 194 ? -28.33400 7.17500   2.58100   1.000 30.17000 ? 196 THR A N   1 
ATOM   1466 C CA  . THR A 1 194 ? -27.48700 8.35400   2.44500   1.000 30.19000 ? 196 THR A CA  1 
ATOM   1467 C C   . THR A 1 194 ? -26.89400 8.74900   3.79400   1.000 25.83000 ? 196 THR A C   1 
ATOM   1468 O O   . THR A 1 194 ? -27.60800 8.89600   4.79000   1.000 31.55000 ? 196 THR A O   1 
ATOM   1469 C CB  . THR A 1 194 ? -28.28100 9.52200   1.84800   1.000 34.57000 ? 196 THR A CB  1 
ATOM   1470 O OG1 . THR A 1 194 ? -29.40400 9.81900   2.68600   1.000 41.46000 ? 196 THR A OG1 1 
ATOM   1471 C CG2 . THR A 1 194 ? -28.78000 9.15600   0.45200   1.000 32.14000 ? 196 THR A CG2 1 
ATOM   1472 N N   . ASP A 1 195 ? -25.58200 8.91200   3.82300   1.000 24.17000 ? 197 ASP A N   1 
ATOM   1473 C CA  . ASP A 1 195 ? -24.92000 9.26900   5.06600   1.000 22.27000 ? 197 ASP A CA  1 
ATOM   1474 C C   . ASP A 1 195 ? -25.04600 10.76900  5.32700   1.000 28.67000 ? 197 ASP A C   1 
ATOM   1475 O O   . ASP A 1 195 ? -25.36300 11.56100  4.43400   1.000 22.29000 ? 197 ASP A O   1 
ATOM   1476 C CB  . ASP A 1 195 ? -23.44900 8.87400   5.02400   1.000 22.80000 ? 197 ASP A CB  1 
ATOM   1477 C CG  . ASP A 1 195 ? -22.88000 8.63300   6.40600   1.000 22.81000 ? 197 ASP A CG  1 
ATOM   1478 O OD1 . ASP A 1 195 ? -23.68500 8.40800   7.34500   1.000 23.07000 ? 197 ASP A OD1 1 
ATOM   1479 O OD2 . ASP A 1 195 ? -21.64100 8.64900   6.54600   1.000 21.12000 ? 197 ASP A OD2 1 
ATOM   1480 N N   . THR A 1 196 ? -24.80200 11.14700  6.57700   1.000 20.94000 ? 198 THR A N   1 
ATOM   1481 C CA  . THR A 1 196 ? -24.80400 12.53300  7.01600   1.000 17.52000 ? 198 THR A CA  1 
ATOM   1482 C C   . THR A 1 196 ? -23.56200 12.77400  7.86400   1.000 17.09000 ? 198 THR A C   1 
ATOM   1483 O O   . THR A 1 196 ? -22.84900 11.83600  8.23700   1.000 14.72000 ? 198 THR A O   1 
ATOM   1484 C CB  . THR A 1 196 ? -26.07500 12.86100  7.80900   1.000 17.21000 ? 198 THR A CB  1 
ATOM   1485 O OG1 . THR A 1 196 ? -26.31600 11.83700  8.77900   1.000 19.99000 ? 198 THR A OG1 1 
ATOM   1486 C CG2 . THR A 1 196 ? -27.28100 12.96200  6.88500   1.000 25.20000 ? 198 THR A CG2 1 
ATOM   1487 N N   . THR A 1 197 ? -23.30000 14.04400  8.15700   1.000 14.67000 ? 199 THR A N   1 
ATOM   1488 C CA  . THR A 1 197 ? -22.15500 14.41100  8.98100   1.000 10.87000 ? 199 THR A CA  1 
ATOM   1489 C C   . THR A 1 197 ? -22.52700 14.31000  10.45400  1.000 9.43000  ? 199 THR A C   1 
ATOM   1490 O O   . THR A 1 197 ? -23.62500 14.69600  10.85500  1.000 12.61000 ? 199 THR A O   1 
ATOM   1491 C CB  . THR A 1 197 ? -21.68000 15.83000  8.63700   1.000 16.63000 ? 199 THR A CB  1 
ATOM   1492 O OG1 . THR A 1 197 ? -21.36200 15.89400  7.24200   1.000 14.23000 ? 199 THR A OG1 1 
ATOM   1493 C CG2 . THR A 1 197 ? -20.41000 16.20200  9.42800   1.000 10.86000 ? 199 THR A CG2 1 
ATOM   1494 N N   . ILE A 1 198 ? -21.60100 13.77400  11.25500  1.000 12.14000 ? 200 ILE A N   1 
ATOM   1495 C CA  . ILE A 1 198 ? -21.80600 13.56500  12.68600  1.000 9.72000  ? 200 ILE A CA  1 
ATOM   1496 C C   . ILE A 1 198 ? -21.60000 14.87200  13.44200  1.000 10.43000 ? 200 ILE A C   1 
ATOM   1497 O O   . ILE A 1 198 ? -20.47900 15.19900  13.84200  1.000 8.35000  ? 200 ILE A O   1 
ATOM   1498 C CB  . ILE A 1 198 ? -20.86400 12.47900  13.22700  1.000 11.41000 ? 200 ILE A CB  1 
ATOM   1499 C CG1 . ILE A 1 198 ? -20.98700 11.19900  12.38600  1.000 11.52000 ? 200 ILE A CG1 1 
ATOM   1500 C CG2 . ILE A 1 198 ? -21.17000 12.21700  14.68800  1.000 10.08000 ? 200 ILE A CG2 1 
ATOM   1501 C CD1 . ILE A 1 198 ? -19.86200 10.18000  12.63100  1.000 14.02000 ? 200 ILE A CD1 1 
ATOM   1502 N N   . THR A 1 199 ? -22.70000 15.59000  13.67400  1.000 10.31000 ? 201 THR A N   1 
ATOM   1503 C CA  . THR A 1 199 ? -22.65300 16.93500  14.24700  1.000 10.29000 ? 201 THR A CA  1 
ATOM   1504 C C   . THR A 1 199 ? -21.96400 16.96400  15.60600  1.000 10.95000 ? 201 THR A C   1 
ATOM   1505 O O   . THR A 1 199 ? -21.14700 17.85300  15.87200  1.000 9.06000  ? 201 THR A O   1 
ATOM   1506 C CB  . THR A 1 199 ? -24.07400 17.47800  14.36800  1.000 11.76000 ? 201 THR A CB  1 
ATOM   1507 O OG1 . THR A 1 199 ? -24.70500 17.42200  13.08000  1.000 13.75000 ? 201 THR A OG1 1 
ATOM   1508 C CG2 . THR A 1 199 ? -24.05700 18.92600  14.86600  1.000 10.75000 ? 201 THR A CG2 1 
ATOM   1509 N N   . VAL A 1 200 ? -22.30900 16.02600  16.49900  1.000 8.14000  ? 202 VAL A N   1 
ATOM   1510 C CA  . VAL A 1 200 ? -21.71400 16.06000  17.83500  1.000 10.47000 ? 202 VAL A CA  1 
ATOM   1511 C C   . VAL A 1 200 ? -20.19400 15.96900  17.75400  1.000 10.37000 ? 202 VAL A C   1 
ATOM   1512 O O   . VAL A 1 200 ? -19.48500 16.61100  18.53900  1.000 9.70000  ? 202 VAL A O   1 
ATOM   1513 C CB  . VAL A 1 200 ? -22.30300 14.96800  18.75300  1.000 10.54000 ? 202 VAL A CB  1 
ATOM   1514 C CG1 . VAL A 1 200 ? -22.04300 13.55700  18.21100  1.000 11.25000 ? 202 VAL A CG1 1 
ATOM   1515 C CG2 . VAL A 1 200 ? -21.76600 15.13400  20.18900  1.000 12.26000 ? 202 VAL A CG2 1 
ATOM   1516 N N   . ASN A 1 201 ? -19.66800 15.23600  16.77900  1.000 7.65000  ? 203 ASN A N   1 
ATOM   1517 C CA  . ASN A 1 201 ? -18.22200 15.10200  16.65600  1.000 11.26000 ? 203 ASN A CA  1 
ATOM   1518 C C   . ASN A 1 201 ? -17.57500 16.33300  16.03400  1.000 9.69000  ? 203 ASN A C   1 
ATOM   1519 O O   . ASN A 1 201 ? -16.44300 16.68100  16.38800  1.000 9.97000  ? 203 ASN A O   1 
ATOM   1520 C CB  . ASN A 1 201 ? -17.87900 13.87900  15.82000  1.000 8.66000  ? 203 ASN A CB  1 
ATOM   1521 C CG  . ASN A 1 201 ? -18.19800 12.58900  16.53000  1.000 11.14000 ? 203 ASN A CG  1 
ATOM   1522 O OD1 . ASN A 1 201 ? -18.61900 12.58800  17.68200  1.000 11.61000 ? 203 ASN A OD1 1 
ATOM   1523 N ND2 . ASN A 1 201 ? -17.99500 11.48300  15.84500  1.000 9.51000  ? 203 ASN A ND2 1 
ATOM   1524 N N   . VAL A 1 202 ? -18.25800 16.99000  15.10300  1.000 9.33000  ? 204 VAL A N   1 
ATOM   1525 C CA  . VAL A 1 202 ? -17.74700 18.25800  14.58500  1.000 8.16000  ? 204 VAL A CA  1 
ATOM   1526 C C   . VAL A 1 202 ? -17.65300 19.26200  15.71600  1.000 8.69000  ? 204 VAL A C   1 
ATOM   1527 O O   . VAL A 1 202 ? -16.66200 19.99200  15.84300  1.000 8.95000  ? 204 VAL A O   1 
ATOM   1528 C CB  . VAL A 1 202 ? -18.65000 18.76700  13.43900  1.000 11.93000 ? 204 VAL A CB  1 
ATOM   1529 C CG1 . VAL A 1 202 ? -18.23600 20.18300  12.96600  1.000 9.40000  ? 204 VAL A CG1 1 
ATOM   1530 C CG2 . VAL A 1 202 ? -18.64300 17.77600  12.27600  1.000 12.49000 ? 204 VAL A CG2 1 
ATOM   1531 N N   . LEU A 1 203 ? -18.67700 19.30500  16.56600  1.000 8.75000  ? 205 LEU A N   1 
ATOM   1532 C CA  . LEU A 1 203 ? -18.63000 20.19600  17.71600  1.000 9.96000  ? 205 LEU A CA  1 
ATOM   1533 C C   . LEU A 1 203 ? -17.46600 19.83700  18.62500  1.000 9.34000  ? 205 LEU A C   1 
ATOM   1534 O O   . LEU A 1 203 ? -16.74700 20.72700  19.08800  1.000 9.69000  ? 205 LEU A O   1 
ATOM   1535 C CB  . LEU A 1 203 ? -19.95000 20.15300  18.48800  1.000 7.78000  ? 205 LEU A CB  1 
ATOM   1536 C CG  . LEU A 1 203 ? -21.13600 20.71800  17.71000  1.000 9.92000  ? 205 LEU A CG  1 
ATOM   1537 C CD1 . LEU A 1 203 ? -22.44900 20.38900  18.41400  1.000 8.06000  ? 205 LEU A CD1 1 
ATOM   1538 C CD2 . LEU A 1 203 ? -20.96800 22.22900  17.48200  1.000 11.42000 ? 205 LEU A CD2 1 
ATOM   1539 N N   . ALA A 1 204 ? -17.25400 18.53700  18.87400  1.000 9.65000  ? 206 ALA A N   1 
ATOM   1540 C CA  . ALA A 1 204 ? -16.09200 18.10600  19.65700  1.000 10.51000 ? 206 ALA A CA  1 
ATOM   1541 C C   . ALA A 1 204 ? -14.80300 18.63500  19.05600  1.000 10.83000 ? 206 ALA A C   1 
ATOM   1542 O O   . ALA A 1 204 ? -13.91200 19.12400  19.77600  1.000 10.41000 ? 206 ALA A O   1 
ATOM   1543 C CB  . ALA A 1 204 ? -16.04600 16.57400  19.73400  1.000 9.35000  ? 206 ALA A CB  1 
ATOM   1544 N N   . TRP A 1 205 ? -14.69000 18.53300  17.73400  1.000 10.78000 ? 207 TRP A N   1 
ATOM   1545 C CA  . TRP A 1 205 ? -13.51500 19.01200  17.01900  1.000 13.59000 ? 207 TRP A CA  1 
ATOM   1546 C C   . TRP A 1 205 ? -13.35300 20.52300  17.15200  1.000 12.58000 ? 207 TRP A C   1 
ATOM   1547 O O   . TRP A 1 205 ? -12.22800 21.02500  17.29300  1.000 13.33000 ? 207 TRP A O   1 
ATOM   1548 C CB  . TRP A 1 205 ? -13.63100 18.61200  15.55100  1.000 12.91000 ? 207 TRP A CB  1 
ATOM   1549 C CG  . TRP A 1 205 ? -12.34900 18.67800  14.81500  1.000 16.86000 ? 207 TRP A CG  1 
ATOM   1550 C CD1 . TRP A 1 205 ? -11.22500 17.92900  15.03800  1.000 19.54000 ? 207 TRP A CD1 1 
ATOM   1551 C CD2 . TRP A 1 205 ? -12.05100 19.53800  13.72500  1.000 19.55000 ? 207 TRP A CD2 1 
ATOM   1552 N NE1 . TRP A 1 205 ? -10.24700 18.27400  14.13800  1.000 26.10000 ? 207 TRP A NE1 1 
ATOM   1553 C CE2 . TRP A 1 205 ? -10.73400 19.25700  13.31700  1.000 18.98000 ? 207 TRP A CE2 1 
ATOM   1554 C CE3 . TRP A 1 205 ? -12.78200 20.50900  13.03500  1.000 21.50000 ? 207 TRP A CE3 1 
ATOM   1555 C CZ2 . TRP A 1 205 ? -10.13000 19.91700  12.26400  1.000 29.51000 ? 207 TRP A CZ2 1 
ATOM   1556 C CZ3 . TRP A 1 205 ? -12.18200 21.16400  11.98700  1.000 25.92000 ? 207 TRP A CZ3 1 
ATOM   1557 C CH2 . TRP A 1 205 ? -10.86900 20.86800  11.60800  1.000 31.11000 ? 207 TRP A CH2 1 
ATOM   1558 N N   . LEU A 1 206 ? -14.46100 21.26700  17.11800  1.000 12.14000 ? 208 LEU A N   1 
ATOM   1559 C CA  . LEU A 1 206 ? -14.36800 22.71000  17.33600  1.000 11.08000 ? 208 LEU A CA  1 
ATOM   1560 C C   . LEU A 1 206 ? -13.90400 23.02700  18.75200  1.000 10.21000 ? 208 LEU A C   1 
ATOM   1561 O O   . LEU A 1 206 ? -13.11500 23.95500  18.95800  1.000 12.97000 ? 208 LEU A O   1 
ATOM   1562 C CB  . LEU A 1 206 ? -15.71100 23.37400  17.05700  1.000 9.00000  ? 208 LEU A CB  1 
ATOM   1563 C CG  . LEU A 1 206 ? -16.15000 23.38300  15.60000  1.000 15.23000 ? 208 LEU A CG  1 
ATOM   1564 C CD1 . LEU A 1 206 ? -17.52300 24.02900  15.46300  1.000 12.45000 ? 208 LEU A CD1 1 
ATOM   1565 C CD2 . LEU A 1 206 ? -15.10600 24.08800  14.74800  1.000 15.67000 ? 208 LEU A CD2 1 
ATOM   1566 N N   . TYR A 1 207 ? -14.40200 22.28300  19.74600  1.000 10.32000 ? 209 TYR A N   1 
ATOM   1567 C CA  . TYR A 1 207 ? -13.89700 22.43400  21.10700  1.000 10.42000 ? 209 TYR A CA  1 
ATOM   1568 C C   . TYR A 1 207 ? -12.40500 22.15000  21.17400  1.000 14.19000 ? 209 TYR A C   1 
ATOM   1569 O O   . TYR A 1 207 ? -11.65200 22.88400  21.83300  1.000 10.61000 ? 209 TYR A O   1 
ATOM   1570 C CB  . TYR A 1 207 ? -14.66300 21.51500  22.05600  1.000 9.20000  ? 209 TYR A CB  1 
ATOM   1571 C CG  . TYR A 1 207 ? -15.95000 22.13000  22.51900  1.000 10.78000 ? 209 TYR A CG  1 
ATOM   1572 C CD1 . TYR A 1 207 ? -15.94700 23.20800  23.40200  1.000 8.20000  ? 209 TYR A CD1 1 
ATOM   1573 C CD2 . TYR A 1 207 ? -17.17500 21.64700  22.06500  1.000 8.82000  ? 209 TYR A CD2 1 
ATOM   1574 C CE1 . TYR A 1 207 ? -17.11900 23.78400  23.82800  1.000 9.75000  ? 209 TYR A CE1 1 
ATOM   1575 C CE2 . TYR A 1 207 ? -18.35900 22.21700  22.49000  1.000 9.52000  ? 209 TYR A CE2 1 
ATOM   1576 C CZ  . TYR A 1 207 ? -18.32600 23.28300  23.36100  1.000 11.03000 ? 209 TYR A CZ  1 
ATOM   1577 O OH  . TYR A 1 207 ? -19.49400 23.85400  23.78400  1.000 11.03000 ? 209 TYR A OH  1 
ATOM   1578 N N   . ALA A 1 208 ? -11.95600 21.10000  20.47400  1.000 11.97000 ? 210 ALA A N   1 
ATOM   1579 C CA  . ALA A 1 208 ? -10.53000 20.79400  20.43000  1.000 13.99000 ? 210 ALA A CA  1 
ATOM   1580 C C   . ALA A 1 208 ? -9.74800  21.95300  19.83000  1.000 12.97000 ? 210 ALA A C   1 
ATOM   1581 O O   . ALA A 1 208 ? -8.64800  22.27500  20.29300  1.000 12.52000 ? 210 ALA A O   1 
ATOM   1582 C CB  . ALA A 1 208 ? -10.28500 19.51400  19.62200  1.000 14.82000 ? 210 ALA A CB  1 
ATOM   1583 N N   . ALA A 1 209 ? -10.29300 22.57900  18.78500  1.000 13.82000 ? 211 ALA A N   1 
ATOM   1584 C CA  . ALA A 1 209 ? -9.60800  23.71900  18.18400  1.000 15.46000 ? 211 ALA A CA  1 
ATOM   1585 C C   . ALA A 1 209 ? -9.48900  24.86300  19.18300  1.000 14.89000 ? 211 ALA A C   1 
ATOM   1586 O O   . ALA A 1 209 ? -8.42800  25.48700  19.30200  1.000 15.25000 ? 211 ALA A O   1 
ATOM   1587 C CB  . ALA A 1 209 ? -10.34100 24.17500  16.92600  1.000 16.14000 ? 211 ALA A CB  1 
ATOM   1588 N N   . VAL A 1 210 ? -10.56100 25.13100  19.92700  1.000 11.85000 ? 212 VAL A N   1 
ATOM   1589 C CA  . VAL A 1 210 ? -10.54100 26.20100  20.92300  1.000 12.24000 ? 212 VAL A CA  1 
ATOM   1590 C C   . VAL A 1 210 ? -9.52700  25.89700  22.02100  1.000 13.53000 ? 212 VAL A C   1 
ATOM   1591 O O   . VAL A 1 210 ? -8.73100  26.76600  22.40500  1.000 14.12000 ? 212 VAL A O   1 
ATOM   1592 C CB  . VAL A 1 210 ? -11.96100 26.41800  21.48100  1.000 13.65000 ? 212 VAL A CB  1 
ATOM   1593 C CG1 . VAL A 1 210 ? -11.95200 27.36600  22.66000  1.000 10.82000 ? 212 VAL A CG1 1 
ATOM   1594 C CG2 . VAL A 1 210 ? -12.88300 26.95300  20.36700  1.000 10.94000 ? 212 VAL A CG2 1 
ATOM   1595 N N   . ILE A 1 211 ? -9.50600  24.65200  22.51700  1.000 12.87000 ? 213 ILE A N   1 
ATOM   1596 C CA  . ILE A 1 211 ? -8.54300  24.27500  23.55700  1.000 11.02000 ? 213 ILE A CA  1 
ATOM   1597 C C   . ILE A 1 211 ? -7.11700  24.57100  23.10300  1.000 16.13000 ? 213 ILE A C   1 
ATOM   1598 O O   . ILE A 1 211 ? -6.26200  24.98700  23.90500  1.000 10.32000 ? 213 ILE A O   1 
ATOM   1599 C CB  . ILE A 1 211 ? -8.72500  22.78600  23.92300  1.000 13.51000 ? 213 ILE A CB  1 
ATOM   1600 C CG1 . ILE A 1 211 ? -10.01600 22.57900  24.72400  1.000 14.63000 ? 213 ILE A CG1 1 
ATOM   1601 C CG2 . ILE A 1 211 ? -7.51200  22.23700  24.68800  1.000 14.27000 ? 213 ILE A CG2 1 
ATOM   1602 C CD1 . ILE A 1 211 ? -10.52500 21.14100  24.69000  1.000 13.42000 ? 213 ILE A CD1 1 
ATOM   1603 N N   . ASN A 1 212 ? -6.84800  24.40800  21.81100  1.000 13.22000 ? 214 ASN A N   1 
ATOM   1604 C CA  . ASN A 1 212 ? -5.51900  24.61600  21.26100  1.000 18.46000 ? 214 ASN A CA  1 
ATOM   1605 C C   . ASN A 1 212 ? -5.27300  26.04700  20.80800  1.000 18.36000 ? 214 ASN A C   1 
ATOM   1606 O O   . ASN A 1 212 ? -4.21200  26.32400  20.24200  1.000 18.45000 ? 214 ASN A O   1 
ATOM   1607 C CB  . ASN A 1 212 ? -5.29100  23.63900  20.10200  1.000 20.82000 ? 214 ASN A CB  1 
ATOM   1608 C CG  . ASN A 1 212 ? -5.02600  22.21800  20.59600  1.000 26.21000 ? 214 ASN A CG  1 
ATOM   1609 O OD1 . ASN A 1 212 ? -5.81000  21.29800  20.33700  1.000 30.57000 ? 214 ASN A OD1 1 
ATOM   1610 N ND2 . ASN A 1 212 ? -3.92400  22.03900  21.32800  1.000 27.21000 ? 214 ASN A ND2 1 
ATOM   1611 N N   . GLY A 1 213 ? -6.22100  26.95600  21.02900  1.000 15.45000 ? 215 GLY A N   1 
ATOM   1612 C CA  . GLY A 1 213 ? -6.00600  28.36800  20.76800  1.000 15.22000 ? 215 GLY A CA  1 
ATOM   1613 C C   . GLY A 1 213 ? -6.45500  28.83400  19.40500  1.000 19.03000 ? 215 GLY A C   1 
ATOM   1614 O O   . GLY A 1 213 ? -6.17200  29.97300  19.03000  1.000 19.09000 ? 215 GLY A O   1 
ATOM   1615 N N   . ASP A 1 214 ? -7.15200  27.99500  18.66200  1.000 16.68000 ? 216 ASP A N   1 
ATOM   1616 C CA  . ASP A 1 214 ? -7.60300  28.27900  17.30800  1.000 18.25000 ? 216 ASP A CA  1 
ATOM   1617 C C   . ASP A 1 214 ? -9.10300  28.52100  17.42500  1.000 21.15000 ? 216 ASP A C   1 
ATOM   1618 O O   . ASP A 1 214 ? -9.88600  27.56400  17.45600  1.000 20.57000 ? 216 ASP A O   1 
ATOM   1619 C CB  . ASP A 1 214 ? -7.26400  27.09800  16.39900  1.000 18.84000 ? 216 ASP A CB  1 
ATOM   1620 C CG  . ASP A 1 214 ? -7.26300  27.45500  14.92100  1.000 26.76000 ? 216 ASP A CG  1 
ATOM   1621 O OD1 . ASP A 1 214 ? -7.41000  28.64500  14.57800  1.000 30.63000 ? 216 ASP A OD1 1 
ATOM   1622 O OD2 . ASP A 1 214 ? -7.11200  26.52200  14.09800  1.000 28.42000 ? 216 ASP A OD2 1 
ATOM   1623 N N   . ARG A 1 215 ? -9.50000  29.80400  17.52000  1.000 18.34000 ? 217 ARG A N   1 
ATOM   1624 C CA  . ARG A 1 215 ? -10.86100 30.13900  17.92300  1.000 19.25000 ? 217 ARG A CA  1 
ATOM   1625 C C   . ARG A 1 215 ? -11.46400 31.30600  17.13900  1.000 22.11000 ? 217 ARG A C   1 
ATOM   1626 O O   . ARG A 1 215 ? -12.39700 31.95300  17.63500  1.000 18.97000 ? 217 ARG A O   1 
ATOM   1627 C CB  . ARG A 1 215 ? -10.90100 30.45200  19.42100  1.000 20.26000 ? 217 ARG A CB  1 
ATOM   1628 C CG  . ARG A 1 215 ? -9.87500  31.50300  19.85400  1.000 18.53000 ? 217 ARG A CG  1 
ATOM   1629 C CD  . ARG A 1 215 ? -10.08600 31.95600  21.29500  1.000 16.10000 ? 217 ARG A CD  1 
ATOM   1630 N NE  . ARG A 1 215 ? -9.16700  33.05100  21.59500  1.000 18.63000 ? 217 ARG A NE  1 
ATOM   1631 C CZ  . ARG A 1 215 ? -7.96100  32.88400  22.12400  1.000 18.36000 ? 217 ARG A CZ  1 
ATOM   1632 N NH1 . ARG A 1 215 ? -7.17400  33.93700  22.34300  1.000 19.97000 ? 217 ARG A NH1 1 
ATOM   1633 N NH2 . ARG A 1 215 ? -7.54100  31.67100  22.44000  1.000 15.26000 ? 217 ARG A NH2 1 
ATOM   1634 N N   . TRP A 1 216 ? -10.98400 31.57600  15.91900  1.000 18.63000 ? 218 TRP A N   1 
ATOM   1635 C CA  . TRP A 1 216 ? -11.53700 32.67400  15.12700  1.000 21.23000 ? 218 TRP A CA  1 
ATOM   1636 C C   . TRP A 1 216 ? -13.02300 32.49000  14.83100  1.000 23.23000 ? 218 TRP A C   1 
ATOM   1637 O O   . TRP A 1 216 ? -13.74700 33.47800  14.66100  1.000 21.21000 ? 218 TRP A O   1 
ATOM   1638 C CB  . TRP A 1 216 ? -10.75800 32.81700  13.81600  1.000 27.31000 ? 218 TRP A CB  1 
ATOM   1639 C CG  . TRP A 1 216 ? -10.78500 31.58100  12.94800  1.000 23.95000 ? 218 TRP A CG  1 
ATOM   1640 C CD1 . TRP A 1 216 ? -9.84000  30.59500  12.89400  1.000 22.05000 ? 218 TRP A CD1 1 
ATOM   1641 C CD2 . TRP A 1 216 ? -11.80100 31.21300  12.00100  1.000 23.76000 ? 218 TRP A CD2 1 
ATOM   1642 N NE1 . TRP A 1 216 ? -10.20700 29.63300  11.98000  1.000 23.07000 ? 218 TRP A NE1 1 
ATOM   1643 C CE2 . TRP A 1 216 ? -11.40600 29.98900  11.41700  1.000 23.73000 ? 218 TRP A CE2 1 
ATOM   1644 C CE3 . TRP A 1 216 ? -13.00100 31.80100  11.58900  1.000 24.91000 ? 218 TRP A CE3 1 
ATOM   1645 C CZ2 . TRP A 1 216 ? -12.17400 29.33700  10.45000  1.000 25.81000 ? 218 TRP A CZ2 1 
ATOM   1646 C CZ3 . TRP A 1 216 ? -13.76700 31.14800  10.63000  1.000 26.70000 ? 218 TRP A CZ3 1 
ATOM   1647 C CH2 . TRP A 1 216 ? -13.34600 29.92700  10.07400  1.000 25.47000 ? 218 TRP A CH2 1 
ATOM   1648 N N   . PHE A 1 217 ? -13.49600 31.24200  14.76200  1.000 18.79000 ? 219 PHE A N   1 
ATOM   1649 C CA  . PHE A 1 217 ? -14.87500 30.93500  14.40400  1.000 21.13000 ? 219 PHE A CA  1 
ATOM   1650 C C   . PHE A 1 217 ? -15.86200 31.18300  15.52900  1.000 19.00000 ? 219 PHE A C   1 
ATOM   1651 O O   . PHE A 1 217 ? -17.06900 31.10200  15.28800  1.000 16.71000 ? 219 PHE A O   1 
ATOM   1652 C CB  . PHE A 1 217 ? -14.99000 29.47100  13.97300  1.000 17.13000 ? 219 PHE A CB  1 
ATOM   1653 C CG  . PHE A 1 217 ? -14.34300 28.52500  14.93300  1.000 18.15000 ? 219 PHE A CG  1 
ATOM   1654 C CD1 . PHE A 1 217 ? -15.03900 28.05400  16.04200  1.000 15.23000 ? 219 PHE A CD1 1 
ATOM   1655 C CD2 . PHE A 1 217 ? -13.04100 28.12500  14.74200  1.000 15.19000 ? 219 PHE A CD2 1 
ATOM   1656 C CE1 . PHE A 1 217 ? -14.44900 27.19500  16.92800  1.000 15.57000 ? 219 PHE A CE1 1 
ATOM   1657 C CE2 . PHE A 1 217 ? -12.42600 27.26600  15.63500  1.000 15.80000 ? 219 PHE A CE2 1 
ATOM   1658 C CZ  . PHE A 1 217 ? -13.13100 26.80100  16.73300  1.000 19.18000 ? 219 PHE A CZ  1 
ATOM   1659 N N   . LEU A 1 218 ? -15.39800 31.43300  16.74800  1.000 18.74000 ? 220 LEU A N   1 
ATOM   1660 C CA  . LEU A 1 218 ? -16.32600 31.71200  17.83400  1.000 18.18000 ? 220 LEU A CA  1 
ATOM   1661 C C   . LEU A 1 218 ? -17.01600 33.03700  17.55100  1.000 25.61000 ? 220 LEU A C   1 
ATOM   1662 O O   . LEU A 1 218 ? -16.35500 34.05700  17.32500  1.000 23.82000 ? 220 LEU A O   1 
ATOM   1663 C CB  . LEU A 1 218 ? -15.60100 31.77000  19.18000  1.000 16.64000 ? 220 LEU A CB  1 
ATOM   1664 C CG  . LEU A 1 218 ? -14.97400 30.48100  19.72000  1.000 16.46000 ? 220 LEU A CG  1 
ATOM   1665 C CD1 . LEU A 1 218 ? -14.26500 30.77200  21.01800  1.000 15.01000 ? 220 LEU A CD1 1 
ATOM   1666 C CD2 . LEU A 1 218 ? -16.03900 29.39000  19.91200  1.000 15.18000 ? 220 LEU A CD2 1 
ATOM   1667 N N   . ASN A 1 219 ? -18.33800 33.02400  17.54000  1.000 26.33000 ? 221 ASN A N   1 
ATOM   1668 C CA  . ASN A 1 219 ? -19.08900 34.22300  17.20500  1.000 29.39000 ? 221 ASN A CA  1 
ATOM   1669 C C   . ASN A 1 219 ? -19.86100 34.70200  18.42600  1.000 26.03000 ? 221 ASN A C   1 
ATOM   1670 O O   . ASN A 1 219 ? -19.78200 34.11600  19.51600  1.000 25.68000 ? 221 ASN A O   1 
ATOM   1671 C CB  . ASN A 1 219 ? -20.00600 33.98100  15.99400  1.000 27.42000 ? 221 ASN A CB  1 
ATOM   1672 C CG  . ASN A 1 219 ? -21.17900 33.03700  16.28400  1.000 27.57000 ? 221 ASN A CG  1 
ATOM   1673 O OD1 . ASN A 1 219 ? -21.50800 32.73400  17.43100  1.000 31.81000 ? 221 ASN A OD1 1 
ATOM   1674 N ND2 . ASN A 1 219 ? -21.82600 32.57600  15.21100  1.000 27.76000 ? 221 ASN A ND2 1 
ATOM   1675 N N   . ARG A 1 220 ? -20.61600 35.78000  18.22200  1.000 29.36000 ? 222 ARG A N   1 
ATOM   1676 C CA  . ARG A 1 220 ? -21.37600 36.44400  19.27000  1.000 28.13000 ? 222 ARG A CA  1 
ATOM   1677 C C   . ARG A 1 220 ? -22.82100 35.96200  19.36300  1.000 29.78000 ? 222 ARG A C   1 
ATOM   1678 O O   . ARG A 1 220 ? -23.63200 36.61200  20.02800  1.000 30.56000 ? 222 ARG A O   1 
ATOM   1679 C CB  . ARG A 1 220 ? -21.35400 37.96200  19.04600  1.000 37.00000 ? 222 ARG A CB  1 
ATOM   1680 N N   . PHE A 1 221 ? -23.15800 34.83600  18.74000  1.000 27.29000 ? 223 PHE A N   1 
ATOM   1681 C CA  . PHE A 1 221 ? -24.54100 34.39600  18.62900  1.000 24.75000 ? 223 PHE A CA  1 
ATOM   1682 C C   . PHE A 1 221 ? -24.78800 33.14200  19.46000  1.000 27.58000 ? 223 PHE A C   1 
ATOM   1683 O O   . PHE A 1 221 ? -23.86400 32.42500  19.86100  1.000 24.89000 ? 223 PHE A O   1 
ATOM   1684 C CB  . PHE A 1 221 ? -24.90800 34.13200  17.16400  1.000 27.86000 ? 223 PHE A CB  1 
ATOM   1685 N N   . THR A 1 222 ? -26.06300 32.89500  19.73700  1.000 22.11000 ? 224 THR A N   1 
ATOM   1686 C CA  . THR A 1 222 ? -26.48600 31.62600  20.30000  1.000 19.31000 ? 224 THR A CA  1 
ATOM   1687 C C   . THR A 1 222 ? -27.70200 31.16000  19.52100  1.000 18.91000 ? 224 THR A C   1 
ATOM   1688 O O   . THR A 1 222 ? -28.20900 31.86200  18.64200  1.000 20.92000 ? 224 THR A O   1 
ATOM   1689 C CB  . THR A 1 222 ? -26.79700 31.71900  21.79700  1.000 22.14000 ? 224 THR A CB  1 
ATOM   1690 O OG1 . THR A 1 222 ? -26.76100 30.40600  22.36800  1.000 22.59000 ? 224 THR A OG1 1 
ATOM   1691 C CG2 . THR A 1 222 ? -28.17500 32.35800  22.03900  1.000 22.55000 ? 224 THR A CG2 1 
ATOM   1692 N N   . THR A 1 223 ? -28.14500 29.95200  19.83900  1.000 20.75000 ? 225 THR A N   1 
ATOM   1693 C CA  . THR A 1 223 ? -29.25900 29.32900  19.15300  1.000 20.01000 ? 225 THR A CA  1 
ATOM   1694 C C   . THR A 1 223 ? -29.98100 28.43000  20.14200  1.000 20.83000 ? 225 THR A C   1 
ATOM   1695 O O   . THR A 1 223 ? -29.42600 28.03500  21.17500  1.000 20.62000 ? 225 THR A O   1 
ATOM   1696 C CB  . THR A 1 223 ? -28.78700 28.51700  17.93400  1.000 19.60000 ? 225 THR A CB  1 
ATOM   1697 O OG1 . THR A 1 223 ? -29.92100 28.03800  17.20300  1.000 23.49000 ? 225 THR A OG1 1 
ATOM   1698 C CG2 . THR A 1 223 ? -27.92600 27.32400  18.37800  1.000 17.00000 ? 225 THR A CG2 1 
ATOM   1699 N N   . THR A 1 224 ? -31.23900 28.12800  19.82400  1.000 18.73000 ? 226 THR A N   1 
ATOM   1700 C CA  . THR A 1 224 ? -31.90400 27.02400  20.48800  1.000 20.49000 ? 226 THR A CA  1 
ATOM   1701 C C   . THR A 1 224 ? -31.49100 25.72100  19.81900  1.000 17.15000 ? 226 THR A C   1 
ATOM   1702 O O   . THR A 1 224 ? -31.01400 25.69700  18.67900  1.000 14.00000 ? 226 THR A O   1 
ATOM   1703 C CB  . THR A 1 224 ? -33.43100 27.17200  20.43900  1.000 22.36000 ? 226 THR A CB  1 
ATOM   1704 O OG1 . THR A 1 224 ? -33.88200 26.99100  19.09000  1.000 19.40000 ? 226 THR A OG1 1 
ATOM   1705 C CG2 . THR A 1 224 ? -33.87200 28.55500  20.93900  1.000 23.95000 ? 226 THR A CG2 1 
ATOM   1706 N N   . LEU A 1 225 ? -31.67900 24.62500  20.55100  1.000 16.90000 ? 227 LEU A N   1 
ATOM   1707 C CA  . LEU A 1 225 ? -31.35000 23.31600  20.00800  1.000 13.79000 ? 227 LEU A CA  1 
ATOM   1708 C C   . LEU A 1 225 ? -32.25100 22.98500  18.82400  1.000 16.56000 ? 227 LEU A C   1 
ATOM   1709 O O   . LEU A 1 225 ? -31.79000 22.47200  17.79400  1.000 12.89000 ? 227 LEU A O   1 
ATOM   1710 C CB  . LEU A 1 225 ? -31.48300 22.26900  21.11000  1.000 17.28000 ? 227 LEU A CB  1 
ATOM   1711 C CG  . LEU A 1 225 ? -30.91900 20.87600  20.86400  1.000 16.45000 ? 227 LEU A CG  1 
ATOM   1712 C CD1 . LEU A 1 225 ? -29.48400 20.94300  20.35100  1.000 16.21000 ? 227 LEU A CD1 1 
ATOM   1713 C CD2 . LEU A 1 225 ? -31.00600 20.06700  22.15500  1.000 19.84000 ? 227 LEU A CD2 1 
ATOM   1714 N N   . ASN A 1 226 ? -33.54100 23.28800  18.95600  1.000 14.29000 ? 228 ASN A N   1 
ATOM   1715 C CA  . ASN A 1 226 ? -34.47900 23.05300  17.86500  1.000 16.91000 ? 228 ASN A CA  1 
ATOM   1716 C C   . ASN A 1 226 ? -34.09300 23.84400  16.62100  1.000 14.21000 ? 228 ASN A C   1 
ATOM   1717 O O   . ASN A 1 226 ? -34.04000 23.29600  15.51400  1.000 14.78000 ? 228 ASN A O   1 
ATOM   1718 C CB  . ASN A 1 226 ? -35.89300 23.41800  18.30900  1.000 14.89000 ? 228 ASN A CB  1 
ATOM   1719 C CG  . ASN A 1 226 ? -36.91600 23.15400  17.21900  1.000 22.41000 ? 228 ASN A CG  1 
ATOM   1720 O OD1 . ASN A 1 226 ? -37.65000 24.05600  16.79500  1.000 18.55000 ? 228 ASN A OD1 1 
ATOM   1721 N ND2 . ASN A 1 226 ? -36.95300 21.91300  16.74400  1.000 14.36000 ? 228 ASN A ND2 1 
ATOM   1722 N N   . ASP A 1 227 ? -33.83200 25.14500  16.78200  1.000 14.89000 ? 229 ASP A N   1 
ATOM   1723 C CA  . ASP A 1 227 ? -33.44600 25.96500  15.63200  1.000 17.54000 ? 229 ASP A CA  1 
ATOM   1724 C C   . ASP A 1 227 ? -32.20700 25.40500  14.94200  1.000 16.84000 ? 229 ASP A C   1 
ATOM   1725 O O   . ASP A 1 227 ? -32.15700 25.32200  13.70800  1.000 15.31000 ? 229 ASP A O   1 
ATOM   1726 C CB  . ASP A 1 227 ? -33.18900 27.40700  16.06600  1.000 17.82000 ? 229 ASP A CB  1 
ATOM   1727 C CG  . ASP A 1 227 ? -34.45700 28.24200  16.12800  1.000 31.27000 ? 229 ASP A CG  1 
ATOM   1728 O OD1 . ASP A 1 227 ? -35.52800 27.74300  15.71400  1.000 32.81000 ? 229 ASP A OD1 1 
ATOM   1729 O OD2 . ASP A 1 227 ? -34.38400 29.40200  16.59600  1.000 28.97000 ? 229 ASP A OD2 1 
ATOM   1730 N N   . PHE A 1 228 ? -31.20000 25.00600  15.72300  1.000 14.76000 ? 230 PHE A N   1 
ATOM   1731 C CA  . PHE A 1 228 ? -29.97500 24.49400  15.12200  1.000 15.09000 ? 230 PHE A CA  1 
ATOM   1732 C C   . PHE A 1 228 ? -30.23500 23.19100  14.38300  1.000 12.07000 ? 230 PHE A C   1 
ATOM   1733 O O   . PHE A 1 228 ? -29.71200 22.98000  13.28300  1.000 13.28000 ? 230 PHE A O   1 
ATOM   1734 C CB  . PHE A 1 228 ? -28.89900 24.29000  16.19000  1.000 13.46000 ? 230 PHE A CB  1 
ATOM   1735 C CG  . PHE A 1 228 ? -27.68000 23.57600  15.67900  1.000 15.79000 ? 230 PHE A CG  1 
ATOM   1736 C CD1 . PHE A 1 228 ? -26.70600 24.26400  14.96800  1.000 16.14000 ? 230 PHE A CD1 1 
ATOM   1737 C CD2 . PHE A 1 228 ? -27.53000 22.21100  15.86700  1.000 16.86000 ? 230 PHE A CD2 1 
ATOM   1738 C CE1 . PHE A 1 228 ? -25.59000 23.61300  14.48600  1.000 14.30000 ? 230 PHE A CE1 1 
ATOM   1739 C CE2 . PHE A 1 228 ? -26.42500 21.54800  15.37100  1.000 16.37000 ? 230 PHE A CE2 1 
ATOM   1740 C CZ  . PHE A 1 228 ? -25.45300 22.24700  14.68600  1.000 17.52000 ? 230 PHE A CZ  1 
ATOM   1741 N N   . ASN A 1 229 ? -31.03900 22.30500  14.97700  1.000 12.22000 ? 231 ASN A N   1 
ATOM   1742 C CA  . ASN A 1 229 ? -31.31800 21.01700  14.35600  1.000 15.20000 ? 231 ASN A CA  1 
ATOM   1743 C C   . ASN A 1 229 ? -31.98700 21.19800  12.99800  1.000 17.53000 ? 231 ASN A C   1 
ATOM   1744 O O   . ASN A 1 229 ? -31.64600 20.50700  12.03000  1.000 15.75000 ? 231 ASN A O   1 
ATOM   1745 C CB  . ASN A 1 229 ? -32.19100 20.16400  15.28200  1.000 14.98000 ? 231 ASN A CB  1 
ATOM   1746 C CG  . ASN A 1 229 ? -31.38000 19.44400  16.36000  1.000 15.44000 ? 231 ASN A CG  1 
ATOM   1747 O OD1 . ASN A 1 229 ? -30.15300 19.53600  16.38900  1.000 13.80000 ? 231 ASN A OD1 1 
ATOM   1748 N ND2 . ASN A 1 229 ? -32.06600 18.71800  17.24400  1.000 14.53000 ? 231 ASN A ND2 1 
ATOM   1749 N N   . LEU A 1 230 ? -32.93300 22.13300  12.90100  1.000 15.85000 ? 232 LEU A N   1 
ATOM   1750 C CA  . LEU A 1 230 ? -33.63200 22.32900  11.63300  1.000 17.02000 ? 232 LEU A CA  1 
ATOM   1751 C C   . LEU A 1 230 ? -32.68100 22.83800  10.55500  1.000 19.64000 ? 232 LEU A C   1 
ATOM   1752 O O   . LEU A 1 230 ? -32.76300 22.42000  9.39200   1.000 18.80000 ? 232 LEU A O   1 
ATOM   1753 C CB  . LEU A 1 230 ? -34.80600 23.28200  11.83500  1.000 18.82000 ? 232 LEU A CB  1 
ATOM   1754 C CG  . LEU A 1 230 ? -35.86200 22.72500  12.79000  1.000 20.15000 ? 232 LEU A CG  1 
ATOM   1755 C CD1 . LEU A 1 230 ? -36.90400 23.78000  13.16700  1.000 20.71000 ? 232 LEU A CD1 1 
ATOM   1756 C CD2 . LEU A 1 230 ? -36.52400 21.51200  12.15000  1.000 18.55000 ? 232 LEU A CD2 1 
ATOM   1757 N N   . VAL A 1 231 ? -31.74500 23.71200  10.93000  1.000 16.64000 ? 233 VAL A N   1 
ATOM   1758 C CA  . VAL A 1 231 ? -30.77600 24.21600  9.96000   1.000 18.15000 ? 233 VAL A CA  1 
ATOM   1759 C C   . VAL A 1 231 ? -29.77500 23.12900  9.59100   1.000 16.33000 ? 233 VAL A C   1 
ATOM   1760 O O   . VAL A 1 231 ? -29.45000 22.93100  8.41100   1.000 17.24000 ? 233 VAL A O   1 
ATOM   1761 C CB  . VAL A 1 231 ? -30.06800 25.46900  10.50800  1.000 21.58000 ? 233 VAL A CB  1 
ATOM   1762 C CG1 . VAL A 1 231 ? -28.93900 25.88700  9.57800   1.000 27.44000 ? 233 VAL A CG1 1 
ATOM   1763 C CG2 . VAL A 1 231 ? -31.06400 26.60400  10.65800  1.000 22.35000 ? 233 VAL A CG2 1 
ATOM   1764 N N   . ALA A 1 232 ? -29.26100 22.41700  10.59700  1.000 17.95000 ? 234 ALA A N   1 
ATOM   1765 C CA  . ALA A 1 232 ? -28.22800 21.41900  10.34600  1.000 19.20000 ? 234 ALA A CA  1 
ATOM   1766 C C   . ALA A 1 232 ? -28.71900 20.36300  9.36500   1.000 16.67000 ? 234 ALA A C   1 
ATOM   1767 O O   . ALA A 1 232 ? -27.97000 19.92100  8.48600   1.000 17.31000 ? 234 ALA A O   1 
ATOM   1768 C CB  . ALA A 1 232 ? -27.79100 20.78000  11.66600  1.000 20.29000 ? 234 ALA A CB  1 
ATOM   1769 N N   . MET A 1 233 ? -29.98500 19.97300  9.47800   1.000 13.79000 ? 235 MET A N   1 
ATOM   1770 C CA  . MET A 1 233 ? -30.51200 18.96400  8.57200   1.000 19.94000 ? 235 MET A CA  1 
ATOM   1771 C C   . MET A 1 233 ? -30.54000 19.45700  7.12900   1.000 19.37000 ? 235 MET A C   1 
ATOM   1772 O O   . MET A 1 233 ? -30.44800 18.64500  6.20300   1.000 16.73000 ? 235 MET A O   1 
ATOM   1773 C CB  . MET A 1 233 ? -31.89000 18.53600  9.04800   1.000 23.09000 ? 235 MET A CB  1 
ATOM   1774 C CG  . MET A 1 233 ? -31.81400 17.81700  10.41000  1.000 24.16000 ? 235 MET A CG  1 
ATOM   1775 S SD  . MET A 1 233 ? -33.20000 16.71200  10.71300  1.000 43.94000 ? 235 MET A SD  1 
ATOM   1776 C CE  . MET A 1 233 ? -33.21700 15.75200  9.18900   1.000 35.94000 ? 235 MET A CE  1 
ATOM   1777 N N   . LYS A 1 234 ? -30.61500 20.77400  6.91500   1.000 18.04000 ? 236 LYS A N   1 
ATOM   1778 C CA  . LYS A 1 234 ? -30.56200 21.28800  5.54700   1.000 19.24000 ? 236 LYS A CA  1 
ATOM   1779 C C   . LYS A 1 234 ? -29.16200 21.19900  4.96300   1.000 18.23000 ? 236 LYS A C   1 
ATOM   1780 O O   . LYS A 1 234 ? -29.00800 21.24700  3.73900   1.000 19.96000 ? 236 LYS A O   1 
ATOM   1781 C CB  . LYS A 1 234 ? -31.06700 22.72800  5.49800   1.000 19.56000 ? 236 LYS A CB  1 
ATOM   1782 C CG  . LYS A 1 234 ? -32.55500 22.83400  5.72500   1.000 22.89000 ? 236 LYS A CG  1 
ATOM   1783 C CD  . LYS A 1 234 ? -33.00800 24.28000  5.78500   1.000 38.58000 ? 236 LYS A CD  1 
ATOM   1784 C CE  . LYS A 1 234 ? -34.48900 24.38000  6.12700   1.000 40.24000 ? 236 LYS A CE  1 
ATOM   1785 N NZ  . LYS A 1 234 ? -34.98500 25.78100  6.07300   1.000 40.20000 ? 236 LYS A NZ  1 
ATOM   1786 N N   . TYR A 1 235 ? -28.13800 21.05800  5.80400   1.000 13.29000 ? 237 TYR A N   1 
ATOM   1787 C CA  . TYR A 1 235 ? -26.77200 20.86400  5.34000   1.000 14.48000 ? 237 TYR A CA  1 
ATOM   1788 C C   . TYR A 1 235 ? -26.31100 19.41300  5.46100   1.000 14.99000 ? 237 TYR A C   1 
ATOM   1789 O O   . TYR A 1 235 ? -25.10300 19.15300  5.43900   1.000 14.88000 ? 237 TYR A O   1 
ATOM   1790 C CB  . TYR A 1 235 ? -25.82100 21.78500  6.10700   1.000 18.24000 ? 237 TYR A CB  1 
ATOM   1791 C CG  . TYR A 1 235 ? -26.05400 23.24300  5.78400   1.000 17.31000 ? 237 TYR A CG  1 
ATOM   1792 C CD1 . TYR A 1 235 ? -26.95200 23.99800  6.52300   1.000 19.82000 ? 237 TYR A CD1 1 
ATOM   1793 C CD2 . TYR A 1 235 ? -25.38200 23.85700  4.73100   1.000 21.06000 ? 237 TYR A CD2 1 
ATOM   1794 C CE1 . TYR A 1 235 ? -27.17800 25.33600  6.22600   1.000 26.93000 ? 237 TYR A CE1 1 
ATOM   1795 C CE2 . TYR A 1 235 ? -25.60000 25.20100  4.42200   1.000 22.84000 ? 237 TYR A CE2 1 
ATOM   1796 C CZ  . TYR A 1 235 ? -26.50200 25.93000  5.17200   1.000 26.57000 ? 237 TYR A CZ  1 
ATOM   1797 O OH  . TYR A 1 235 ? -26.72200 27.25800  4.88600   1.000 24.07000 ? 237 TYR A OH  1 
ATOM   1798 N N   . ASN A 1 236 ? -27.24400 18.46800  5.57900   1.000 18.64000 ? 238 ASN A N   1 
ATOM   1799 C CA  . ASN A 1 236 ? -26.90600 17.04400  5.67100   1.000 17.05000 ? 238 ASN A CA  1 
ATOM   1800 C C   . ASN A 1 236 ? -26.10300 16.73400  6.93300   1.000 16.63000 ? 238 ASN A C   1 
ATOM   1801 O O   . ASN A 1 236 ? -25.26000 15.83100  6.93400   1.000 16.03000 ? 238 ASN A O   1 
ATOM   1802 C CB  . ASN A 1 236 ? -26.14000 16.57700  4.42400   1.000 22.30000 ? 238 ASN A CB  1 
ATOM   1803 C CG  . ASN A 1 236 ? -26.43500 15.13900  4.06300   1.000 26.73000 ? 238 ASN A CG  1 
ATOM   1804 O OD1 . ASN A 1 236 ? -27.59400 14.75000  3.92300   1.000 38.86000 ? 238 ASN A OD1 1 
ATOM   1805 N ND2 . ASN A 1 236 ? -25.38600 14.34300  3.88800   1.000 27.63000 ? 238 ASN A ND2 1 
ATOM   1806 N N   . TYR A 1 237 ? -26.33900 17.51200  7.99200   1.000 13.35000 ? 239 TYR A N   1 
ATOM   1807 C CA  . TYR A 1 237 ? -25.78800 17.27200  9.31700   1.000 15.82000 ? 239 TYR A CA  1 
ATOM   1808 C C   . TYR A 1 237 ? -26.83000 16.57400  10.17400  1.000 14.97000 ? 239 TYR A C   1 
ATOM   1809 O O   . TYR A 1 237 ? -28.03300 16.81600  10.03700  1.000 15.78000 ? 239 TYR A O   1 
ATOM   1810 C CB  . TYR A 1 237 ? -25.37500 18.58600  10.00000  1.000 11.34000 ? 239 TYR A CB  1 
ATOM   1811 C CG  . TYR A 1 237 ? -23.94900 18.98800  9.75400   1.000 15.67000 ? 239 TYR A CG  1 
ATOM   1812 C CD1 . TYR A 1 237 ? -23.45200 19.12100  8.46300   1.000 14.39000 ? 239 TYR A CD1 1 
ATOM   1813 C CD2 . TYR A 1 237 ? -23.08700 19.23600  10.82200  1.000 15.99000 ? 239 TYR A CD2 1 
ATOM   1814 C CE1 . TYR A 1 237 ? -22.13300 19.48800  8.24400   1.000 17.25000 ? 239 TYR A CE1 1 
ATOM   1815 C CE2 . TYR A 1 237 ? -21.78100 19.60900  10.61100  1.000 15.59000 ? 239 TYR A CE2 1 
ATOM   1816 C CZ  . TYR A 1 237 ? -21.30500 19.73300  9.32500   1.000 19.88000 ? 239 TYR A CZ  1 
ATOM   1817 O OH  . TYR A 1 237 ? -19.98800 20.10200  9.13100   1.000 22.58000 ? 239 TYR A OH  1 
ATOM   1818 N N   . GLU A 1 238 ? -26.35300 15.71000  11.06300  1.000 13.14000 ? 240 GLU A N   1 
ATOM   1819 C CA  . GLU A 1 238 ? -27.23600 15.01600  11.98700  1.000 13.35000 ? 240 GLU A CA  1 
ATOM   1820 C C   . GLU A 1 238 ? -27.82600 15.99200  12.99700  1.000 14.68000 ? 240 GLU A C   1 
ATOM   1821 O O   . GLU A 1 238 ? -27.12900 16.89700  13.46200  1.000 15.47000 ? 240 GLU A O   1 
ATOM   1822 C CB  . GLU A 1 238 ? -26.47100 13.93100  12.74600  1.000 14.96000 ? 240 GLU A CB  1 
ATOM   1823 C CG  . GLU A 1 238 ? -26.29500 12.65800  11.97500  1.000 18.39000 ? 240 GLU A CG  1 
ATOM   1824 C CD  . GLU A 1 238 ? -27.62500 12.02500  11.59100  1.000 24.40000 ? 240 GLU A CD  1 
ATOM   1825 O OE1 . GLU A 1 238 ? -27.89200 11.87200  10.37700  1.000 25.96000 ? 240 GLU A OE1 1 
ATOM   1826 O OE2 . GLU A 1 238 ? -28.41000 11.69000  12.50700  1.000 28.71000 ? 240 GLU A OE2 1 
ATOM   1827 N N   . PRO A 1 239 ? -29.08700 15.81600  13.38400  1.000 15.01000 ? 241 PRO A N   1 
ATOM   1828 C CA  . PRO A 1 239 ? -29.61100 16.58900  14.51000  1.000 13.48000 ? 241 PRO A CA  1 
ATOM   1829 C C   . PRO A 1 239 ? -28.93800 16.17200  15.80800  1.000 15.19000 ? 241 PRO A C   1 
ATOM   1830 O O   . PRO A 1 239 ? -28.48600 15.03300  15.97700  1.000 15.49000 ? 241 PRO A O   1 
ATOM   1831 C CB  . PRO A 1 239 ? -31.10900 16.25300  14.51700  1.000 18.33000 ? 241 PRO A CB  1 
ATOM   1832 C CG  . PRO A 1 239 ? -31.20200 14.91100  13.82600  1.000 19.01000 ? 241 PRO A CG  1 
ATOM   1833 C CD  . PRO A 1 239 ? -30.06900 14.85200  12.84300  1.000 18.77000 ? 241 PRO A CD  1 
ATOM   1834 N N   . LEU A 1 240 ? -28.85400 17.12200  16.72300  1.000 14.36000 ? 242 LEU A N   1 
ATOM   1835 C CA  . LEU A 1 240 ? -28.29800 16.84800  18.03700  1.000 15.74000 ? 242 LEU A CA  1 
ATOM   1836 C C   . LEU A 1 240 ? -29.37500 16.28600  18.95300  1.000 17.44000 ? 242 LEU A C   1 
ATOM   1837 O O   . LEU A 1 240 ? -30.52700 16.72100  18.91700  1.000 18.88000 ? 242 LEU A O   1 
ATOM   1838 C CB  . LEU A 1 240 ? -27.72100 18.12700  18.62600  1.000 15.53000 ? 242 LEU A CB  1 
ATOM   1839 C CG  . LEU A 1 240 ? -26.43300 18.62800  17.99500  1.000 15.98000 ? 242 LEU A CG  1 
ATOM   1840 C CD1 . LEU A 1 240 ? -26.08300 19.98300  18.61400  1.000 14.80000 ? 242 LEU A CD1 1 
ATOM   1841 C CD2 . LEU A 1 240 ? -25.28600 17.62000  18.23900  1.000 14.91000 ? 242 LEU A CD2 1 
ATOM   1842 N N   . THR A 1 241 ? -28.99900 15.30500  19.76300  1.000 13.66000 ? 243 THR A N   1 
ATOM   1843 C CA  . THR A 1 241 ? -29.85400 14.78900  20.81800  1.000 16.40000 ? 243 THR A CA  1 
ATOM   1844 C C   . THR A 1 241 ? -29.46300 15.40900  22.15600  1.000 16.11000 ? 243 THR A C   1 
ATOM   1845 O O   . THR A 1 241 ? -28.42900 16.07100  22.29300  1.000 12.12000 ? 243 THR A O   1 
ATOM   1846 C CB  . THR A 1 241 ? -29.74400 13.26500  20.90900  1.000 16.63000 ? 243 THR A CB  1 
ATOM   1847 O OG1 . THR A 1 241 ? -28.43200 12.92300  21.38500  1.000 13.93000 ? 243 THR A OG1 1 
ATOM   1848 C CG2 . THR A 1 241 ? -29.98700 12.61400  19.53600  1.000 16.58000 ? 243 THR A CG2 1 
ATOM   1849 N N   . GLN A 1 242 ? -30.30600 15.16500  23.16200  1.000 14.24000 ? 244 GLN A N   1 
ATOM   1850 C CA  . GLN A 1 242 ? -29.98400 15.61500  24.51200  1.000 15.77000 ? 244 GLN A CA  1 
ATOM   1851 C C   . GLN A 1 242 ? -28.73000 14.92100  25.03400  1.000 14.79000 ? 244 GLN A C   1 
ATOM   1852 O O   . GLN A 1 242 ? -27.90800 15.53800  25.72400  1.000 16.25000 ? 244 GLN A O   1 
ATOM   1853 C CB  . GLN A 1 242 ? -31.17800 15.37000  25.43200  1.000 16.99000 ? 244 GLN A CB  1 
ATOM   1854 C CG  . GLN A 1 242 ? -30.98000 15.84400  26.88600  1.000 16.89000 ? 244 GLN A CG  1 
ATOM   1855 C CD  . GLN A 1 242 ? -30.64500 17.32900  27.00800  1.000 21.74000 ? 244 GLN A CD  1 
ATOM   1856 O OE1 . GLN A 1 242 ? -31.20100 18.16900  26.29600  1.000 24.10000 ? 244 GLN A OE1 1 
ATOM   1857 N NE2 . GLN A 1 242 ? -29.72000 17.65700  27.92200  1.000 22.50000 ? 244 GLN A NE2 1 
ATOM   1858 N N   . ASP A 1 243 ? -28.55700 13.63900  24.70000  1.000 14.12000 ? 245 ASP A N   1 
ATOM   1859 C CA  . ASP A 1 243 ? -27.33700 12.93000  25.07600  1.000 16.04000 ? 245 ASP A CA  1 
ATOM   1860 C C   . ASP A 1 243 ? -26.10700 13.57300  24.44000  1.000 16.08000 ? 245 ASP A C   1 
ATOM   1861 O O   . ASP A 1 243 ? -25.03700 13.62900  25.05600  1.000 13.03000 ? 245 ASP A O   1 
ATOM   1862 C CB  . ASP A 1 243 ? -27.43500 11.46200  24.66700  1.000 12.94000 ? 245 ASP A CB  1 
ATOM   1863 C CG  . ASP A 1 243 ? -28.38400 10.65900  25.56100  1.000 18.31000 ? 245 ASP A CG  1 
ATOM   1864 O OD1 . ASP A 1 243 ? -28.94000 11.22800  26.53700  1.000 20.38000 ? 245 ASP A OD1 1 
ATOM   1865 O OD2 . ASP A 1 243 ? -28.56100 9.45000   25.28800  1.000 20.84000 ? 245 ASP A OD2 1 
ATOM   1866 N N   . HIS A 1 244 ? -26.23400 14.04500  23.20000  1.000 12.56000 ? 246 HIS A N   1 
ATOM   1867 C CA  . HIS A 1 244 ? -25.11800 14.73800  22.56500  1.000 14.67000 ? 246 HIS A CA  1 
ATOM   1868 C C   . HIS A 1 244 ? -24.75000 15.99900  23.32900  1.000 13.96000 ? 246 HIS A C   1 
ATOM   1869 O O   . HIS A 1 244 ? -23.56500 16.29800  23.52600  1.000 12.68000 ? 246 HIS A O   1 
ATOM   1870 C CB  . HIS A 1 244 ? -25.47200 15.09000  21.12800  1.000 13.24000 ? 246 HIS A CB  1 
ATOM   1871 C CG  . HIS A 1 244 ? -25.56400 13.90400  20.23000  1.000 14.51000 ? 246 HIS A CG  1 
ATOM   1872 N ND1 . HIS A 1 244 ? -26.38000 13.87700  19.11900  1.000 14.92000 ? 246 HIS A ND1 1 
ATOM   1873 C CD2 . HIS A 1 244 ? -24.94700 12.69900  20.28000  1.000 13.46000 ? 246 HIS A CD2 1 
ATOM   1874 C CE1 . HIS A 1 244 ? -26.25700 12.70300  18.52100  1.000 17.00000 ? 246 HIS A CE1 1 
ATOM   1875 N NE2 . HIS A 1 244 ? -25.39600 11.97100  19.20800  1.000 13.93000 ? 246 HIS A NE2 1 
ATOM   1876 N N   . VAL A 1 245 ? -25.75500 16.78400  23.71400  1.000 12.42000 ? 247 VAL A N   1 
ATOM   1877 C CA  . VAL A 1 245 ? -25.48300 17.97900  24.50100  1.000 13.82000 ? 247 VAL A CA  1 
ATOM   1878 C C   . VAL A 1 245 ? -24.76400 17.59200  25.78300  1.000 16.61000 ? 247 VAL A C   1 
ATOM   1879 O O   . VAL A 1 245 ? -23.79900 18.24800  26.19800  1.000 13.93000 ? 247 VAL A O   1 
ATOM   1880 C CB  . VAL A 1 245 ? -26.79200 18.73900  24.78500  1.000 16.50000 ? 247 VAL A CB  1 
ATOM   1881 C CG1 . VAL A 1 245 ? -26.55200 19.86000  25.77800  1.000 14.49000 ? 247 VAL A CG1 1 
ATOM   1882 C CG2 . VAL A 1 245 ? -27.40900 19.27100  23.47400  1.000 12.64000 ? 247 VAL A CG2 1 
ATOM   1883 N N   . ASP A 1 246 ? -25.19400 16.48400  26.39500  1.000 14.00000 ? 248 ASP A N   1 
ATOM   1884 C CA  . ASP A 1 246 ? -24.62100 16.03900  27.66200  1.000 17.33000 ? 248 ASP A CA  1 
ATOM   1885 C C   . ASP A 1 246 ? -23.16100 15.60800  27.51100  1.000 15.65000 ? 248 ASP A C   1 
ATOM   1886 O O   . ASP A 1 246 ? -22.32900 15.95000  28.35800  1.000 14.79000 ? 248 ASP A O   1 
ATOM   1887 C CB  . ASP A 1 246 ? -25.45900 14.89500  28.23900  1.000 18.18000 ? 248 ASP A CB  1 
ATOM   1888 C CG  . ASP A 1 246 ? -26.83600 15.35000  28.70200  1.000 25.28000 ? 248 ASP A CG  1 
ATOM   1889 O OD1 . ASP A 1 246 ? -26.97500 16.52600  29.12100  1.000 27.47000 ? 248 ASP A OD1 1 
ATOM   1890 O OD2 . ASP A 1 246 ? -27.77900 14.52000  28.65100  1.000 32.11000 ? 248 ASP A OD2 1 
ATOM   1891 N N   . ILE A 1 247 ? -22.82100 14.85700  26.45800  1.000 13.59000 ? 249 ILE A N   1 
ATOM   1892 C CA  . ILE A 1 247 ? -21.43800 14.40300  26.32000  1.000 13.27000 ? 249 ILE A CA  1 
ATOM   1893 C C   . ILE A 1 247 ? -20.50300 15.51200  25.86700  1.000 14.15000 ? 249 ILE A C   1 
ATOM   1894 O O   . ILE A 1 247 ? -19.27800 15.35600  25.97000  1.000 12.45000 ? 249 ILE A O   1 
ATOM   1895 C CB  . ILE A 1 247 ? -21.28200 13.19100  25.37700  1.000 15.62000 ? 249 ILE A CB  1 
ATOM   1896 C CG1 . ILE A 1 247 ? -21.62900 13.53900  23.92200  1.000 13.64000 ? 249 ILE A CG1 1 
ATOM   1897 C CG2 . ILE A 1 247 ? -22.11500 11.99800  25.88900  1.000 17.68000 ? 249 ILE A CG2 1 
ATOM   1898 C CD1 . ILE A 1 247 ? -21.23700 12.41800  22.94900  1.000 18.29000 ? 249 ILE A CD1 1 
ATOM   1899 N N   . LEU A 1 248 ? -21.04300 16.64100  25.41200  1.000 11.59000 ? 250 LEU A N   1 
ATOM   1900 C CA  . LEU A 1 248 ? -20.22200 17.82700  25.18800  1.000 12.99000 ? 250 LEU A CA  1 
ATOM   1901 C C   . LEU A 1 248 ? -20.02100 18.63200  26.46400  1.000 15.18000 ? 250 LEU A C   1 
ATOM   1902 O O   . LEU A 1 248 ? -19.26100 19.60700  26.45200  1.000 13.09000 ? 250 LEU A O   1 
ATOM   1903 C CB  . LEU A 1 248 ? -20.84900 18.70200  24.09400  1.000 9.57000  ? 250 LEU A CB  1 
ATOM   1904 C CG  . LEU A 1 248 ? -20.78800 18.12600  22.67100  1.000 13.42000 ? 250 LEU A CG  1 
ATOM   1905 C CD1 . LEU A 1 248 ? -21.67300 18.92500  21.69800  1.000 10.69000 ? 250 LEU A CD1 1 
ATOM   1906 C CD2 . LEU A 1 248 ? -19.35400 18.05300  22.15500  1.000 14.41000 ? 250 LEU A CD2 1 
ATOM   1907 N N   . GLY A 1 249 ? -20.66700 18.23100  27.56200  1.000 13.97000 ? 251 GLY A N   1 
ATOM   1908 C CA  . GLY A 1 249 ? -20.58500 18.94000  28.82300  1.000 14.46000 ? 251 GLY A CA  1 
ATOM   1909 C C   . GLY A 1 249 ? -19.16900 19.24600  29.29900  1.000 15.84000 ? 251 GLY A C   1 
ATOM   1910 O O   . GLY A 1 249 ? -18.82000 20.40100  29.54500  1.000 14.73000 ? 251 GLY A O   1 
ATOM   1911 N N   . PRO A 1 250 ? -18.32900 18.21500  29.44100  1.000 15.29000 ? 252 PRO A N   1 
ATOM   1912 C CA  . PRO A 1 250 ? -16.96500 18.46300  29.93600  1.000 17.58000 ? 252 PRO A CA  1 
ATOM   1913 C C   . PRO A 1 250 ? -16.16200 19.40300  29.05400  1.000 15.31000 ? 252 PRO A C   1 
ATOM   1914 O O   . PRO A 1 250 ? -15.46000 20.27600  29.58300  1.000 12.75000 ? 252 PRO A O   1 
ATOM   1915 C CB  . PRO A 1 250 ? -16.34900 17.05700  29.98900  1.000 16.73000 ? 252 PRO A CB  1 
ATOM   1916 C CG  . PRO A 1 250 ? -17.54100 16.13400  30.14000  1.000 17.60000 ? 252 PRO A CG  1 
ATOM   1917 C CD  . PRO A 1 250 ? -18.61000 16.77600  29.30100  1.000 16.64000 ? 252 PRO A CD  1 
ATOM   1918 N N   . LEU A 1 251 ? -16.26100 19.26800  27.72600  1.000 12.29000 ? 253 LEU A N   1 
ATOM   1919 C CA  . LEU A 1 251 ? -15.53800 20.17100  26.83600  1.000 11.28000 ? 253 LEU A CA  1 
ATOM   1920 C C   . LEU A 1 251 ? -16.08800 21.59000  26.93000  1.000 12.96000 ? 253 LEU A C   1 
ATOM   1921 O O   . LEU A 1 251 ? -15.32700 22.56600  26.87400  1.000 10.67000 ? 253 LEU A O   1 
ATOM   1922 C CB  . LEU A 1 251 ? -15.59800 19.65300  25.39000  1.000 10.90000 ? 253 LEU A CB  1 
ATOM   1923 C CG  . LEU A 1 251 ? -14.68800 18.46300  25.04800  1.000 11.42000 ? 253 LEU A CG  1 
ATOM   1924 C CD1 . LEU A 1 251 ? -14.97000 17.99000  23.61700  1.000 11.84000 ? 253 LEU A CD1 1 
ATOM   1925 C CD2 . LEU A 1 251 ? -13.23000 18.87000  25.18600  1.000 14.58000 ? 253 LEU A CD2 1 
ATOM   1926 N N   . SER A 1 252 ? -17.41300 21.72300  27.05000  1.000 11.40000 ? 254 SER A N   1 
ATOM   1927 C CA  . SER A 1 252 ? -18.01300 23.03500  27.27300  1.000 12.06000 ? 254 SER A CA  1 
ATOM   1928 C C   . SER A 1 252 ? -17.50100 23.65700  28.57100  1.000 12.17000 ? 254 SER A C   1 
ATOM   1929 O O   . SER A 1 252 ? -17.17800 24.84800  28.61900  1.000 12.31000 ? 254 SER A O   1 
ATOM   1930 C CB  . SER A 1 252 ? -19.54000 22.89700  27.29900  1.000 11.22000 ? 254 SER A CB  1 
ATOM   1931 O OG  . SER A 1 252 ? -20.16000 24.14600  27.55300  1.000 18.27000 ? 254 SER A OG  1 
ATOM   1932 N N   . ALA A 1 253 ? -17.40300 22.85800  29.63200  1.000 16.21000 ? 255 ALA A N   1 
ATOM   1933 C CA  . ALA A 1 253 ? -16.90800 23.37400  30.90900  1.000 15.65000 ? 255 ALA A CA  1 
ATOM   1934 C C   . ALA A 1 253 ? -15.44100 23.77700  30.81500  1.000 13.62000 ? 255 ALA A C   1 
ATOM   1935 O O   . ALA A 1 253 ? -15.04500 24.83200  31.32900  1.000 13.94000 ? 255 ALA A O   1 
ATOM   1936 C CB  . ALA A 1 253 ? -17.09900 22.32700  32.00400  1.000 14.31000 ? 255 ALA A CB  1 
ATOM   1937 N N   . GLN A 1 254 ? -14.63100 22.95600  30.14600  1.000 14.41000 ? 256 GLN A N   1 
ATOM   1938 C CA  . GLN A 1 254 ? -13.19400 23.21000  30.04500  1.000 15.96000 ? 256 GLN A CA  1 
ATOM   1939 C C   . GLN A 1 254 ? -12.90900 24.51200  29.31000  1.000 16.45000 ? 256 GLN A C   1 
ATOM   1940 O O   . GLN A 1 254 ? -11.97600 25.24100  29.66100  1.000 16.33000 ? 256 GLN A O   1 
ATOM   1941 C CB  . GLN A 1 254 ? -12.51600 22.03200  29.33400  1.000 16.61000 ? 256 GLN A CB  1 
ATOM   1942 C CG  . GLN A 1 254 ? -10.99700 22.16800  29.11400  1.000 20.46000 ? 256 GLN A CG  1 
ATOM   1943 C CD  . GLN A 1 254 ? -10.40200 20.96800  28.36800  1.000 22.74000 ? 256 GLN A CD  1 
ATOM   1944 O OE1 . GLN A 1 254 ? -11.05900 19.94000  28.19400  1.000 20.18000 ? 256 GLN A OE1 1 
ATOM   1945 N NE2 . GLN A 1 254 ? -9.15600  21.10400  27.92000  1.000 17.15000 ? 256 GLN A NE2 1 
ATOM   1946 N N   . THR A 1 255 ? -13.68100 24.81200  28.27400  1.000 11.02000 ? 257 THR A N   1 
ATOM   1947 C CA  . THR A 1 255 ? -13.45700 26.01500  27.48700  1.000 11.75000 ? 257 THR A CA  1 
ATOM   1948 C C   . THR A 1 255 ? -14.31000 27.19800  27.91700  1.000 12.90000 ? 257 THR A C   1 
ATOM   1949 O O   . THR A 1 255 ? -14.02800 28.31800  27.48900  1.000 13.24000 ? 257 THR A O   1 
ATOM   1950 C CB  . THR A 1 255 ? -13.73900 25.75100  26.01600  1.000 11.04000 ? 257 THR A CB  1 
ATOM   1951 O OG1 . THR A 1 255 ? -15.12100 25.38200  25.86600  1.000 10.85000 ? 257 THR A OG1 1 
ATOM   1952 C CG2 . THR A 1 255 ? -12.85100 24.64200  25.51000  1.000 12.05000 ? 257 THR A CG2 1 
ATOM   1953 N N   . GLY A 1 256 ? -15.34500 26.98000  28.72000  1.000 13.64000 ? 258 GLY A N   1 
ATOM   1954 C CA  . GLY A 1 256 ? -16.26400 28.05200  29.02900  1.000 14.67000 ? 258 GLY A CA  1 
ATOM   1955 C C   . GLY A 1 256 ? -17.17500 28.46000  27.88800  1.000 16.77000 ? 258 GLY A C   1 
ATOM   1956 O O   . GLY A 1 256 ? -17.80200 29.51500  27.96500  1.000 20.75000 ? 258 GLY A O   1 
ATOM   1957 N N   . ILE A 1 257 ? -17.26200 27.66300  26.82200  1.000 15.68000 ? 259 ILE A N   1 
ATOM   1958 C CA  . ILE A 1 257 ? -18.13400 27.95400  25.68700  1.000 15.18000 ? 259 ILE A CA  1 
ATOM   1959 C C   . ILE A 1 257 ? -19.35800 27.05500  25.79900  1.000 16.05000 ? 259 ILE A C   1 
ATOM   1960 O O   . ILE A 1 257 ? -19.23900 25.82900  25.70900  1.000 11.09000 ? 259 ILE A O   1 
ATOM   1961 C CB  . ILE A 1 257 ? -17.41900 27.72100  24.34500  1.000 14.82000 ? 259 ILE A CB  1 
ATOM   1962 C CG1 . ILE A 1 257 ? -16.08800 28.48700  24.27200  1.000 14.69000 ? 259 ILE A CG1 1 
ATOM   1963 C CG2 . ILE A 1 257 ? -18.34000 28.05800  23.17600  1.000 14.70000 ? 259 ILE A CG2 1 
ATOM   1964 C CD1 . ILE A 1 257 ? -16.21500 29.99200  24.44100  1.000 19.85000 ? 259 ILE A CD1 1 
ATOM   1965 N N   . ALA A 1 258 ? -20.53500 27.65700  25.97100  1.000 14.44000 ? 260 ALA A N   1 
ATOM   1966 C CA  . ALA A 1 258 ? -21.76500 26.87600  26.05800  1.000 14.37000 ? 260 ALA A CA  1 
ATOM   1967 C C   . ALA A 1 258 ? -21.96400 26.05500  24.78800  1.000 9.75000  ? 260 ALA A C   1 
ATOM   1968 O O   . ALA A 1 258 ? -21.60400 26.48200  23.68800  1.000 12.53000 ? 260 ALA A O   1 
ATOM   1969 C CB  . ALA A 1 258 ? -22.96700 27.80700  26.27300  1.000 15.92000 ? 260 ALA A CB  1 
ATOM   1970 N N   . VAL A 1 259 ? -22.55800 24.86700  24.93900  1.000 11.55000 ? 261 VAL A N   1 
ATOM   1971 C CA  . VAL A 1 259 ? -22.80100 24.02300  23.76800  1.000 11.30000 ? 261 VAL A CA  1 
ATOM   1972 C C   . VAL A 1 259 ? -23.64000 24.76500  22.72200  1.000 11.15000 ? 261 VAL A C   1 
ATOM   1973 O O   . VAL A 1 259 ? -23.34600 24.70300  21.52500  1.000 13.40000 ? 261 VAL A O   1 
ATOM   1974 C CB  . VAL A 1 259 ? -23.44400 22.68900  24.18200  1.000 14.44000 ? 261 VAL A CB  1 
ATOM   1975 C CG1 . VAL A 1 259 ? -23.97100 21.95300  22.95700  1.000 11.42000 ? 261 VAL A CG1 1 
ATOM   1976 C CG2 . VAL A 1 259 ? -22.40600 21.82800  24.92400  1.000 16.16000 ? 261 VAL A CG2 1 
ATOM   1977 N N   . LEU A 1 260 ? -24.67900 25.49400  23.14800  1.000 12.08000 ? 262 LEU A N   1 
ATOM   1978 C CA  . LEU A 1 260 ? -25.51200 26.18700  22.15800  1.000 13.98000 ? 262 LEU A CA  1 
ATOM   1979 C C   . LEU A 1 260 ? -24.77900 27.36100  21.51900  1.000 16.67000 ? 262 LEU A C   1 
ATOM   1980 O O   . LEU A 1 260 ? -25.08800 27.73500  20.37900  1.000 15.20000 ? 262 LEU A O   1 
ATOM   1981 C CB  . LEU A 1 260 ? -26.83300 26.64800  22.78100  1.000 13.09000 ? 262 LEU A CB  1 
ATOM   1982 C CG  . LEU A 1 260 ? -27.78300 25.46600  23.01200  1.000 17.67000 ? 262 LEU A CG  1 
ATOM   1983 C CD1 . LEU A 1 260 ? -29.02400 25.85000  23.82800  1.000 21.04000 ? 262 LEU A CD1 1 
ATOM   1984 C CD2 . LEU A 1 260 ? -28.19200 24.83500  21.68800  1.000 22.32000 ? 262 LEU A CD2 1 
ATOM   1985 N N   . ASP A 1 261 ? -23.79200 27.93900  22.21400  1.000 13.82000 ? 263 ASP A N   1 
ATOM   1986 C CA  . ASP A 1 261 ? -22.94200 28.93900  21.57100  1.000 16.06000 ? 263 ASP A CA  1 
ATOM   1987 C C   . ASP A 1 261 ? -22.05100 28.30600  20.51000  1.000 15.23000 ? 263 ASP A C   1 
ATOM   1988 O O   . ASP A 1 261 ? -21.81800 28.90300  19.45600  1.000 14.89000 ? 263 ASP A O   1 
ATOM   1989 C CB  . ASP A 1 261 ? -22.08800 29.66800  22.61600  1.000 13.85000 ? 263 ASP A CB  1 
ATOM   1990 C CG  . ASP A 1 261 ? -22.92400 30.53600  23.52900  1.000 21.94000 ? 263 ASP A CG  1 
ATOM   1991 O OD1 . ASP A 1 261 ? -24.11900 30.73600  23.20400  1.000 24.04000 ? 263 ASP A OD1 1 
ATOM   1992 O OD2 . ASP A 1 261 ? -22.40500 31.02100  24.55900  1.000 24.75000 ? 263 ASP A OD2 1 
ATOM   1993 N N   . MET A 1 262 ? -21.52300 27.10900  20.77700  1.000 10.11000 ? 264 MET A N   1 
ATOM   1994 C CA  . MET A 1 262 ? -20.73200 26.42900  19.75900  1.000 12.27000 ? 264 MET A CA  1 
ATOM   1995 C C   . MET A 1 262 ? -21.60800 25.99900  18.58900  1.000 13.13000 ? 264 MET A C   1 
ATOM   1996 O O   . MET A 1 262 ? -21.17300 26.05600  17.43500  1.000 13.90000 ? 264 MET A O   1 
ATOM   1997 C CB  . MET A 1 262 ? -19.99200 25.22700  20.35500  1.000 8.84000  ? 264 MET A CB  1 
ATOM   1998 C CG  . MET A 1 262 ? -18.91300 24.67700  19.44500  1.000 12.28000 ? 264 MET A CG  1 
ATOM   1999 S SD  . MET A 1 262 ? -17.55500 25.85800  19.23600  1.000 15.86000 ? 264 MET A SD  1 
ATOM   2000 C CE  . MET A 1 262 ? -16.49900 25.35100  20.61300  1.000 11.43000 ? 264 MET A CE  1 
ATOM   2001 N N   . CYS A 1 263 ? -22.84600 25.57600  18.86300  1.000 11.74000 ? 265 CYS A N   1 
ATOM   2002 C CA  . CYS A 1 263 ? -23.78000 25.29000  17.77300  1.000 15.13000 ? 265 CYS A CA  1 
ATOM   2003 C C   . CYS A 1 263 ? -23.97400 26.51000  16.87500  1.000 16.81000 ? 265 CYS A C   1 
ATOM   2004 O O   . CYS A 1 263 ? -23.94000 26.39500  15.64600  1.000 13.21000 ? 265 CYS A O   1 
ATOM   2005 C CB  . CYS A 1 263 ? -25.12500 24.82000  18.33300  1.000 14.17000 ? 265 CYS A CB  1 
ATOM   2006 S SG  . CYS A 1 263 ? -25.04700 23.21200  19.15200  1.000 16.09000 ? 265 CYS A SG  1 
ATOM   2007 N N   . ALA A 1 264 ? -24.15500 27.69100  17.47300  1.000 14.67000 ? 266 ALA A N   1 
ATOM   2008 C CA  . ALA A 1 264 ? -24.31000 28.90200  16.67400  1.000 18.93000 ? 266 ALA A CA  1 
ATOM   2009 C C   . ALA A 1 264 ? -23.05100 29.20900  15.87300  1.000 16.02000 ? 266 ALA A C   1 
ATOM   2010 O O   . ALA A 1 264 ? -23.14000 29.71900  14.74700  1.000 17.55000 ? 266 ALA A O   1 
ATOM   2011 C CB  . ALA A 1 264 ? -24.67500 30.08500  17.57600  1.000 17.96000 ? 266 ALA A CB  1 
ATOM   2012 N N   . SER A 1 265 ? -21.87500 28.90600  16.43100  1.000 14.33000 ? 267 SER A N   1 
ATOM   2013 C CA  . SER A 1 265 ? -20.63500 29.05000  15.67500  1.000 15.67000 ? 267 SER A CA  1 
ATOM   2014 C C   . SER A 1 265 ? -20.59100 28.08200  14.50300  1.000 17.60000 ? 267 SER A C   1 
ATOM   2015 O O   . SER A 1 265 ? -20.19200 28.44900  13.39200  1.000 13.94000 ? 267 SER A O   1 
ATOM   2016 C CB  . SER A 1 265 ? -19.42600 28.81300  16.58700  1.000 19.15000 ? 267 SER A CB  1 
ATOM   2017 O OG  . SER A 1 265 ? -19.23700 29.91800  17.44100  1.000 19.71000 ? 267 SER A OG  1 
ATOM   2018 N N   . LEU A 1 266 ? -20.96900 26.83000  14.73900  1.000 14.38000 ? 268 LEU A N   1 
ATOM   2019 C CA  . LEU A 1 266 ? -20.99800 25.88500  13.63300  1.000 16.22000 ? 268 LEU A CA  1 
ATOM   2020 C C   . LEU A 1 266 ? -22.04000 26.29700  12.60000  1.000 13.53000 ? 268 LEU A C   1 
ATOM   2021 O O   . LEU A 1 266 ? -21.82800 26.12800  11.39400  1.000 15.97000 ? 268 LEU A O   1 
ATOM   2022 C CB  . LEU A 1 266 ? -21.27600 24.47800  14.15700  1.000 13.27000 ? 268 LEU A CB  1 
ATOM   2023 C CG  . LEU A 1 266 ? -21.51200 23.44500  13.05700  1.000 11.92000 ? 268 LEU A CG  1 
ATOM   2024 C CD1 . LEU A 1 266 ? -20.29200 23.39700  12.14700  1.000 11.90000 ? 268 LEU A CD1 1 
ATOM   2025 C CD2 . LEU A 1 266 ? -21.79600 22.07600  13.68500  1.000 12.78000 ? 268 LEU A CD2 1 
ATOM   2026 N N   . LYS A 1 267 ? -23.17500 26.82900  13.05400  1.000 15.50000 ? 269 LYS A N   1 
ATOM   2027 C CA  . LYS A 1 267 ? -24.21800 27.22800  12.11600  1.000 16.98000 ? 269 LYS A CA  1 
ATOM   2028 C C   . LYS A 1 267 ? -23.69800 28.29000  11.15800  1.000 21.33000 ? 269 LYS A C   1 
ATOM   2029 O O   . LYS A 1 267 ? -23.96100 28.24300  9.94900   1.000 20.95000 ? 269 LYS A O   1 
ATOM   2030 C CB  . LYS A 1 267 ? -25.43600 27.74100  12.88300  1.000 17.39000 ? 269 LYS A CB  1 
ATOM   2031 C CG  . LYS A 1 267 ? -26.59200 28.14600  11.95900  1.000 23.55000 ? 269 LYS A CG  1 
ATOM   2032 C CD  . LYS A 1 267 ? -27.85600 28.49200  12.73500  1.000 26.86000 ? 269 LYS A CD  1 
ATOM   2033 C CE  . LYS A 1 267 ? -27.83300 29.93400  13.18800  1.000 39.15000 ? 269 LYS A CE  1 
ATOM   2034 N NZ  . LYS A 1 267 ? -29.20200 30.47100  13.44000  1.000 44.76000 ? 269 LYS A NZ  1 
ATOM   2035 N N   . GLU A 1 268 ? -22.92900 29.24500  11.68800  1.000 18.18000 ? 270 GLU A N   1 
ATOM   2036 C CA  . GLU A 1 268 ? -22.30700 30.26700  10.86100  1.000 20.17000 ? 270 GLU A CA  1 
ATOM   2037 C C   . GLU A 1 268 ? -21.35000 29.65700  9.84800   1.000 22.09000 ? 270 GLU A C   1 
ATOM   2038 O O   . GLU A 1 268 ? -21.33900 30.05800  8.67500   1.000 21.31000 ? 270 GLU A O   1 
ATOM   2039 C CB  . GLU A 1 268 ? -21.59100 31.27600  11.76100  1.000 21.20000 ? 270 GLU A CB  1 
ATOM   2040 C CG  . GLU A 1 268 ? -20.70700 32.25800  11.02600  1.000 29.91000 ? 270 GLU A CG  1 
ATOM   2041 C CD  . GLU A 1 268 ? -21.48200 33.21200  10.14000  1.000 42.45000 ? 270 GLU A CD  1 
ATOM   2042 O OE1 . GLU A 1 268 ? -20.85000 33.78600  9.22500   1.000 49.04000 ? 270 GLU A OE1 1 
ATOM   2043 O OE2 . GLU A 1 268 ? -22.70700 33.39800  10.35800  1.000 44.47000 ? 270 GLU A OE2 1 
ATOM   2044 N N   . LEU A 1 269 ? -20.54400 28.67700  10.28100  1.000 16.80000 ? 271 LEU A N   1 
ATOM   2045 C CA  . LEU A 1 269 ? -19.61300 28.02900  9.36400   1.000 19.70000 ? 271 LEU A CA  1 
ATOM   2046 C C   . LEU A 1 269 ? -20.35400 27.30100  8.24800   1.000 22.92000 ? 271 LEU A C   1 
ATOM   2047 O O   . LEU A 1 269 ? -19.90500 27.29100  7.09400   1.000 24.49000 ? 271 LEU A O   1 
ATOM   2048 C CB  . LEU A 1 269 ? -18.70900 27.05300  10.12100  1.000 17.69000 ? 271 LEU A CB  1 
ATOM   2049 C CG  . LEU A 1 269 ? -17.72000 27.66000  11.12700  1.000 19.60000 ? 271 LEU A CG  1 
ATOM   2050 C CD1 . LEU A 1 269 ? -17.01600 26.58500  11.93700  1.000 17.32000 ? 271 LEU A CD1 1 
ATOM   2051 C CD2 . LEU A 1 269 ? -16.69800 28.55900  10.42900  1.000 20.19000 ? 271 LEU A CD2 1 
ATOM   2052 N N   . LEU A 1 270 ? -21.47400 26.65400  8.58000   1.000 18.71000 ? 272 LEU A N   1 
ATOM   2053 C CA  . LEU A 1 270 ? -22.25300 25.96000  7.55900   1.000 21.29000 ? 272 LEU A CA  1 
ATOM   2054 C C   . LEU A 1 270 ? -22.83400 26.94400  6.55000   1.000 26.07000 ? 272 LEU A C   1 
ATOM   2055 O O   . LEU A 1 270 ? -22.79700 26.70300  5.33700   1.000 23.69000 ? 272 LEU A O   1 
ATOM   2056 C CB  . LEU A 1 270 ? -23.37100 25.15700  8.22000   1.000 21.26000 ? 272 LEU A CB  1 
ATOM   2057 C CG  . LEU A 1 270 ? -22.90300 23.97700  9.08300   1.000 21.93000 ? 272 LEU A CG  1 
ATOM   2058 C CD1 . LEU A 1 270 ? -24.08200 23.14100  9.49100   1.000 21.17000 ? 272 LEU A CD1 1 
ATOM   2059 C CD2 . LEU A 1 270 ? -21.87200 23.14100  8.33200   1.000 21.37000 ? 272 LEU A CD2 1 
ATOM   2060 N N   . GLN A 1 271 ? -23.36400 28.05900  7.03400   1.000 24.19000 ? 273 GLN A N   1 
ATOM   2061 C CA  . GLN A 1 271 ? -24.02200 29.01500  6.16100   1.000 26.17000 ? 273 GLN A CA  1 
ATOM   2062 C C   . GLN A 1 271 ? -23.04100 29.85000  5.35200   1.000 30.94000 ? 273 GLN A C   1 
ATOM   2063 O O   . GLN A 1 271 ? -23.39100 30.28200  4.24900   1.000 29.21000 ? 273 GLN A O   1 
ATOM   2064 C CB  . GLN A 1 271 ? -24.93600 29.92000  6.98800   1.000 25.63000 ? 273 GLN A CB  1 
ATOM   2065 C CG  . GLN A 1 271 ? -26.13200 29.17900  7.53600   1.000 26.44000 ? 273 GLN A CG  1 
ATOM   2066 C CD  . GLN A 1 271 ? -26.96600 29.99700  8.49800   1.000 28.69000 ? 273 GLN A CD  1 
ATOM   2067 O OE1 . GLN A 1 271 ? -26.46100 30.89000  9.18400   1.000 30.60000 ? 273 GLN A OE1 1 
ATOM   2068 N NE2 . GLN A 1 271 ? -28.25100 29.67500  8.57500   1.000 27.50000 ? 273 GLN A NE2 1 
ATOM   2069 N N   . ASN A 1 272 ? -21.81100 30.05300  5.84700   1.000 28.15000 ? 274 ASN A N   1 
ATOM   2070 C CA  . ASN A 1 272 ? -20.87700 30.96800  5.21600   1.000 29.90000 ? 274 ASN A CA  1 
ATOM   2071 C C   . ASN A 1 272 ? -19.59600 30.33200  4.70400   1.000 31.84000 ? 274 ASN A C   1 
ATOM   2072 O O   . ASN A 1 272 ? -18.86400 30.99300  3.96000   1.000 35.18000 ? 274 ASN A O   1 
ATOM   2073 C CB  . ASN A 1 272 ? -20.50900 32.09800  6.18800   1.000 32.23000 ? 274 ASN A CB  1 
ATOM   2074 C CG  . ASN A 1 272 ? -21.66800 33.02900  6.44300   1.000 36.50000 ? 274 ASN A CG  1 
ATOM   2075 O OD1 . ASN A 1 272 ? -22.58400 32.71100  7.20500   1.000 37.53000 ? 274 ASN A OD1 1 
ATOM   2076 N ND2 . ASN A 1 272 ? -21.64800 34.18400  5.79000   1.000 43.72000 ? 274 ASN A ND2 1 
ATOM   2077 N N   . GLY A 1 273 ? -19.30000 29.08800  5.06300   1.000 26.95000 ? 275 GLY A N   1 
ATOM   2078 C CA  . GLY A 1 273 ? -18.03100 28.49700  4.69900   1.000 32.00000 ? 275 GLY A CA  1 
ATOM   2079 C C   . GLY A 1 273 ? -16.91900 29.01400  5.58500   1.000 31.62000 ? 275 GLY A C   1 
ATOM   2080 O O   . GLY A 1 273 ? -17.12900 29.77500  6.52800   1.000 36.11000 ? 275 GLY A O   1 
ATOM   2081 N N   . MET A 1 274 ? -15.70100 28.58700  5.27100   1.000 34.99000 ? 276 MET A N   1 
ATOM   2082 C CA  . MET A 1 274 ? -14.55100 28.97200  6.07600   1.000 36.60000 ? 276 MET A CA  1 
ATOM   2083 C C   . MET A 1 274 ? -13.80500 30.18300  5.52800   1.000 44.78000 ? 276 MET A C   1 
ATOM   2084 O O   . MET A 1 274 ? -13.00900 30.78000  6.26300   1.000 45.56000 ? 276 MET A O   1 
ATOM   2085 C CB  . MET A 1 274 ? -13.58900 27.79100  6.21000   1.000 38.72000 ? 276 MET A CB  1 
ATOM   2086 C CG  . MET A 1 274 ? -14.04600 26.77800  7.25500   1.000 38.40000 ? 276 MET A CG  1 
ATOM   2087 S SD  . MET A 1 274 ? -12.72900 25.69500  7.83700   1.000 44.04000 ? 276 MET A SD  1 
ATOM   2088 C CE  . MET A 1 274 ? -13.64300 24.16700  7.96900   1.000 30.45000 ? 276 MET A CE  1 
ATOM   2089 N N   . ASN A 1 275 ? -14.06000 30.57200  4.27300   1.000 48.09000 ? 277 ASN A N   1 
ATOM   2090 C CA  . ASN A 1 275 ? -13.36800 31.69400  3.62800   1.000 46.87000 ? 277 ASN A CA  1 
ATOM   2091 C C   . ASN A 1 275 ? -11.87300 31.42300  3.51200   1.000 45.13000 ? 277 ASN A C   1 
ATOM   2092 O O   . ASN A 1 275 ? -11.03700 32.28300  3.79800   1.000 47.80000 ? 277 ASN A O   1 
ATOM   2093 C CB  . ASN A 1 275 ? -13.61700 33.00800  4.36800   1.000 47.02000 ? 277 ASN A CB  1 
ATOM   2094 C CG  . ASN A 1 275 ? -15.02100 33.51100  4.19900   1.000 50.88000 ? 277 ASN A CG  1 
ATOM   2095 O OD1 . ASN A 1 275 ? -15.81900 32.93500  3.45300   1.000 54.53000 ? 277 ASN A OD1 1 
ATOM   2096 N ND2 . ASN A 1 275 ? -15.33700 34.60600  4.88400   1.000 50.24000 ? 277 ASN A ND2 1 
ATOM   2097 N N   . GLY A 1 276 ? -11.53700 30.20400  3.10500   1.000 44.26000 ? 278 GLY A N   1 
ATOM   2098 C CA  . GLY A 1 276 ? -10.14600 29.82900  2.95800   1.000 49.84000 ? 278 GLY A CA  1 
ATOM   2099 C C   . GLY A 1 276 ? -9.39300  29.72300  4.26900   1.000 48.61000 ? 278 GLY A C   1 
ATOM   2100 O O   . GLY A 1 276 ? -8.22400  29.32200  4.27500   1.000 53.22000 ? 278 GLY A O   1 
ATOM   2101 N N   . ARG A 1 277 ? -10.03500 30.08900  5.38000   1.000 42.96000 ? 279 ARG A N   1 
ATOM   2102 C CA  . ARG A 1 277 ? -9.44200  29.86900  6.69000   1.000 38.79000 ? 279 ARG A CA  1 
ATOM   2103 C C   . ARG A 1 277 ? -9.42500  28.37900  7.00600   1.000 36.75000 ? 279 ARG A C   1 
ATOM   2104 O O   . ARG A 1 277 ? -10.15400 27.58200  6.40800   1.000 40.14000 ? 279 ARG A O   1 
ATOM   2105 C CB  . ARG A 1 277 ? -10.21100 30.62200  7.77900   1.000 38.81000 ? 279 ARG A CB  1 
ATOM   2106 C CG  . ARG A 1 277 ? -10.33800 32.12400  7.56600   1.000 41.58000 ? 279 ARG A CG  1 
ATOM   2107 C CD  . ARG A 1 277 ? -10.29000 32.88700  8.89200   1.000 36.22000 ? 279 ARG A CD  1 
ATOM   2108 N NE  . ARG A 1 277 ? -9.00100  32.70600  9.55900   1.000 41.29000 ? 279 ARG A NE  1 
ATOM   2109 C CZ  . ARG A 1 277 ? -8.56300  33.43300  10.58400  1.000 40.33000 ? 279 ARG A CZ  1 
ATOM   2110 N NH1 . ARG A 1 277 ? -7.37100  33.17800  11.11200  1.000 41.20000 ? 279 ARG A NH1 1 
ATOM   2111 N NH2 . ARG A 1 277 ? -9.31100  34.40700  11.08900  1.000 39.41000 ? 279 ARG A NH2 1 
ATOM   2112 N N   . THR A 1 278 ? -8.57100  28.00200  7.95100   1.000 32.93000 ? 280 THR A N   1 
ATOM   2113 C CA  . THR A 1 278 ? -8.46400  26.62200  8.38900   1.000 32.16000 ? 280 THR A CA  1 
ATOM   2114 C C   . THR A 1 278 ? -8.74900  26.53300  9.88200   1.000 30.12000 ? 280 THR A C   1 
ATOM   2115 O O   . THR A 1 278 ? -8.65700  27.51800  10.61900  1.000 27.53000 ? 280 THR A O   1 
ATOM   2116 C CB  . THR A 1 278 ? -7.07600  26.02000  8.09700   1.000 34.12000 ? 280 THR A CB  1 
ATOM   2117 O OG1 . THR A 1 278 ? -6.06500  26.79400  8.75100   1.000 35.82000 ? 280 THR A OG1 1 
ATOM   2118 C CG2 . THR A 1 278 ? -6.79700  25.97500  6.59100   1.000 32.62000 ? 280 THR A CG2 1 
ATOM   2119 N N   . ILE A 1 279 ? -9.10700  25.32700  10.31000  1.000 27.22000 ? 281 ILE A N   1 
ATOM   2120 C CA  . ILE A 1 279 ? -9.32700  25.00900  11.71300  1.000 23.75000 ? 281 ILE A CA  1 
ATOM   2121 C C   . ILE A 1 279 ? -8.47200  23.79400  12.00900  1.000 28.29000 ? 281 ILE A C   1 
ATOM   2122 O O   . ILE A 1 279 ? -8.61700  22.76200  11.34600  1.000 25.34000 ? 281 ILE A O   1 
ATOM   2123 C CB  . ILE A 1 279 ? -10.80800 24.72600  12.01500  1.000 22.38000 ? 281 ILE A CB  1 
ATOM   2124 C CG1 . ILE A 1 279 ? -11.63500 25.99200  11.82500  1.000 22.12000 ? 281 ILE A CG1 1 
ATOM   2125 C CG2 . ILE A 1 279 ? -10.97300 24.16100  13.42000  1.000 18.72000 ? 281 ILE A CG2 1 
ATOM   2126 C CD1 . ILE A 1 279 ? -13.14700 25.74400  11.86600  1.000 23.79000 ? 281 ILE A CD1 1 
ATOM   2127 N N   . LEU A 1 280 ? -7.57000  23.92000  12.98400  1.000 27.44000 ? 282 LEU A N   1 
ATOM   2128 C CA  . LEU A 1 280 ? -6.57200  22.88800  13.26600  1.000 25.36000 ? 282 LEU A CA  1 
ATOM   2129 C C   . LEU A 1 280 ? -5.82800  22.48300  11.99500  1.000 28.60000 ? 282 LEU A C   1 
ATOM   2130 O O   . LEU A 1 280 ? -5.53100  21.30800  11.77000  1.000 28.11000 ? 282 LEU A O   1 
ATOM   2131 C CB  . LEU A 1 280 ? -7.20200  21.66900  13.94000  1.000 21.91000 ? 282 LEU A CB  1 
ATOM   2132 C CG  . LEU A 1 280 ? -7.64200  21.87600  15.39000  1.000 23.69000 ? 282 LEU A CG  1 
ATOM   2133 C CD1 . LEU A 1 280 ? -8.42900  20.66700  15.88700  1.000 20.87000 ? 282 LEU A CD1 1 
ATOM   2134 C CD2 . LEU A 1 280 ? -6.44100  22.18500  16.29700  1.000 23.46000 ? 282 LEU A CD2 1 
ATOM   2135 N N   . GLY A 1 281 ? -5.52000  23.47500  11.15900  1.000 34.20000 ? 283 GLY A N   1 
ATOM   2136 C CA  . GLY A 1 281 ? -4.75300  23.25900  9.94800   1.000 30.67000 ? 283 GLY A CA  1 
ATOM   2137 C C   . GLY A 1 281 ? -5.48100  22.37700  8.95900   1.000 38.46000 ? 283 GLY A C   1 
ATOM   2138 O O   . GLY A 1 281 ? -4.91900  21.40200  8.45100   1.000 43.36000 ? 283 GLY A O   1 
ATOM   2139 N N   . SER A 1 282 ? -6.74000  22.70600  8.68500   1.000 38.04000 ? 284 SER A N   1 
ATOM   2140 C CA  . SER A 1 282 ? -7.55800  21.87900  7.81400   1.000 35.24000 ? 284 SER A CA  1 
ATOM   2141 C C   . SER A 1 282 ? -8.73000  22.70600  7.31900   1.000 32.29000 ? 284 SER A C   1 
ATOM   2142 O O   . SER A 1 282 ? -9.35400  23.43900  8.09100   1.000 28.53000 ? 284 SER A O   1 
ATOM   2143 C CB  . SER A 1 282 ? -8.05100  20.62100  8.53900   1.000 34.75000 ? 284 SER A CB  1 
ATOM   2144 O OG  . SER A 1 282 ? -8.78600  19.78100  7.66200   1.000 37.54000 ? 284 SER A OG  1 
ATOM   2145 N N   . ALA A 1 283 ? -9.01800  22.59000  6.02400   1.000 32.72000 ? 285 ALA A N   1 
ATOM   2146 C CA  . ALA A 1 283 ? -10.16200 23.27600  5.44500   1.000 30.52000 ? 285 ALA A CA  1 
ATOM   2147 C C   . ALA A 1 283 ? -11.45900 22.50500  5.62300   1.000 31.04000 ? 285 ALA A C   1 
ATOM   2148 O O   . ALA A 1 283 ? -12.52800 23.04700  5.32900   1.000 34.66000 ? 285 ALA A O   1 
ATOM   2149 C CB  . ALA A 1 283 ? -9.92400  23.53800  3.95300   1.000 34.98000 ? 285 ALA A CB  1 
ATOM   2150 N N   . LEU A 1 284 ? -11.39200 21.26400  6.08600   1.000 28.85000 ? 286 LEU A N   1 
ATOM   2151 C CA  . LEU A 1 284 ? -12.56500 20.41700  6.23000   1.000 31.92000 ? 286 LEU A CA  1 
ATOM   2152 C C   . LEU A 1 284 ? -12.88300 20.24900  7.70600   1.000 25.76000 ? 286 LEU A C   1 
ATOM   2153 O O   . LEU A 1 284 ? -11.97400 20.14200  8.53500   1.000 26.77000 ? 286 LEU A O   1 
ATOM   2154 C CB  . LEU A 1 284 ? -12.33800 19.04500  5.58600   1.000 28.25000 ? 286 LEU A CB  1 
ATOM   2155 N N   . LEU A 1 285 ? -14.17100 20.24800  8.03200   1.000 26.02000 ? 287 LEU A N   1 
ATOM   2156 C CA  . LEU A 1 285 ? -14.60000 19.94700  9.39000   1.000 22.51000 ? 287 LEU A CA  1 
ATOM   2157 C C   . LEU A 1 285 ? -14.53300 18.44200  9.59800   1.000 21.80000 ? 287 LEU A C   1 
ATOM   2158 O O   . LEU A 1 285 ? -15.08400 17.67400  8.80700   1.000 26.20000 ? 287 LEU A O   1 
ATOM   2159 C CB  . LEU A 1 285 ? -16.01700 20.46600  9.64100   1.000 24.52000 ? 287 LEU A CB  1 
ATOM   2160 C CG  . LEU A 1 285 ? -16.19000 21.99100  9.65000   1.000 25.75000 ? 287 LEU A CG  1 
ATOM   2161 C CD1 . LEU A 1 285 ? -17.63000 22.36700  9.85300   1.000 25.22000 ? 287 LEU A CD1 1 
ATOM   2162 C CD2 . LEU A 1 285 ? -15.31100 22.63400  10.71400  1.000 25.30000 ? 287 LEU A CD2 1 
ATOM   2163 N N   . GLU A 1 286 ? -13.83500 18.02400  10.64100  1.000 19.46000 ? 288 GLU A N   1 
ATOM   2164 C CA  . GLU A 1 286 ? -13.63100 16.61200  10.92400  1.000 18.87000 ? 288 GLU A CA  1 
ATOM   2165 C C   . GLU A 1 286 ? -14.76700 16.08600  11.79900  1.000 15.59000 ? 288 GLU A C   1 
ATOM   2166 O O   . GLU A 1 286 ? -15.12400 16.72400  12.79600  1.000 16.16000 ? 288 GLU A O   1 
ATOM   2167 C CB  . GLU A 1 286 ? -12.28300 16.44000  11.61300  1.000 21.29000 ? 288 GLU A CB  1 
ATOM   2168 C CG  . GLU A 1 286 ? -12.11800 15.12500  12.29500  1.000 25.07000 ? 288 GLU A CG  1 
ATOM   2169 C CD  . GLU A 1 286 ? -11.82200 14.01200  11.31900  1.000 32.54000 ? 288 GLU A CD  1 
ATOM   2170 O OE1 . GLU A 1 286 ? -12.38700 12.90000  11.49200  1.000 30.53000 ? 288 GLU A OE1 1 
ATOM   2171 O OE2 . GLU A 1 286 ? -11.02700 14.26100  10.38200  1.000 30.60000 ? 288 GLU A OE2 1 
ATOM   2172 N N   . ASP A 1 287 ? -15.32800 14.91700  11.44500  1.000 16.06000 ? 289 ASP A N   1 
ATOM   2173 C CA  . ASP A 1 287 ? -16.47700 14.39400  12.18300  1.000 13.19000 ? 289 ASP A CA  1 
ATOM   2174 C C   . ASP A 1 287 ? -16.27300 12.98400  12.73900  1.000 15.22000 ? 289 ASP A C   1 
ATOM   2175 O O   . ASP A 1 287 ? -17.24700 12.35600  13.16500  1.000 13.34000 ? 289 ASP A O   1 
ATOM   2176 C CB  . ASP A 1 287 ? -17.75800 14.46500  11.33400  1.000 11.47000 ? 289 ASP A CB  1 
ATOM   2177 C CG  . ASP A 1 287 ? -17.92500 13.29600  10.35400  1.000 14.72000 ? 289 ASP A CG  1 
ATOM   2178 O OD1 . ASP A 1 287 ? -16.92700 12.67600  9.94800   1.000 16.70000 ? 289 ASP A OD1 1 
ATOM   2179 O OD2 . ASP A 1 287 ? -19.09100 13.01900  9.97900   1.000 14.78000 ? 289 ASP A OD2 1 
ATOM   2180 N N   . GLU A 1 288 ? -15.03500 12.49500  12.83000  1.000 14.55000 ? 290 GLU A N   1 
ATOM   2181 C CA  . GLU A 1 288 ? -14.80400 11.16700  13.38700  1.000 18.58000 ? 290 GLU A CA  1 
ATOM   2182 C C   . GLU A 1 288 ? -14.03700 11.18600  14.70900  1.000 18.70000 ? 290 GLU A C   1 
ATOM   2183 O O   . GLU A 1 288 ? -13.53400 10.14900  15.14300  1.000 15.31000 ? 290 GLU A O   1 
ATOM   2184 C CB  . GLU A 1 288 ? -14.11000 10.28300  12.34800  1.000 23.75000 ? 290 GLU A CB  1 
ATOM   2185 C CG  . GLU A 1 288 ? -14.99400 10.10100  11.09900  1.000 22.57000 ? 290 GLU A CG  1 
ATOM   2186 C CD  . GLU A 1 288 ? -15.02500 8.67100   10.55900  1.000 33.81000 ? 290 GLU A CD  1 
ATOM   2187 O OE1 . GLU A 1 288 ? -14.09400 7.88800   10.86300  1.000 35.59000 ? 290 GLU A OE1 1 
ATOM   2188 O OE2 . GLU A 1 288 ? -15.99000 8.33300   9.82600   1.000 28.60000 ? 290 GLU A OE2 1 
ATOM   2189 N N   . PHE A 1 289 ? -13.97900 12.33000  15.38500  1.000 15.85000 ? 291 PHE A N   1 
ATOM   2190 C CA  . PHE A 1 289 ? -13.45300 12.41100  16.74500  1.000 13.51000 ? 291 PHE A CA  1 
ATOM   2191 C C   . PHE A 1 289 ? -14.59700 12.70800  17.69400  1.000 15.29000 ? 291 PHE A C   1 
ATOM   2192 O O   . PHE A 1 289 ? -15.25200 13.75100  17.57200  1.000 13.98000 ? 291 PHE A O   1 
ATOM   2193 C CB  . PHE A 1 289 ? -12.39600 13.50400  16.88200  1.000 19.59000 ? 291 PHE A CB  1 
ATOM   2194 C CG  . PHE A 1 289 ? -11.13600 13.20200  16.17800  1.000 23.47000 ? 291 PHE A CG  1 
ATOM   2195 C CD1 . PHE A 1 289 ? -10.21500 12.33200  16.73100  1.000 29.48000 ? 291 PHE A CD1 1 
ATOM   2196 C CD2 . PHE A 1 289 ? -10.86600 13.78100  14.95800  1.000 23.67000 ? 291 PHE A CD2 1 
ATOM   2197 C CE1 . PHE A 1 289 ? -9.03400  12.04200  16.06900  1.000 35.96000 ? 291 PHE A CE1 1 
ATOM   2198 C CE2 . PHE A 1 289 ? -9.69200  13.49500  14.28000  1.000 35.67000 ? 291 PHE A CE2 1 
ATOM   2199 C CZ  . PHE A 1 289 ? -8.77200  12.62400  14.83800  1.000 32.67000 ? 291 PHE A CZ  1 
ATOM   2200 N N   . THR A 1 290 ? -14.81400 11.82600  18.65600  1.000 13.51000 ? 292 THR A N   1 
ATOM   2201 C CA  . THR A 1 290 ? -15.85600 12.05800  19.63900  1.000 14.34000 ? 292 THR A CA  1 
ATOM   2202 C C   . THR A 1 290 ? -15.35100 12.99800  20.72500  1.000 14.73000 ? 292 THR A C   1 
ATOM   2203 O O   . THR A 1 290 ? -14.14400 13.22600  20.86700  1.000 12.68000 ? 292 THR A O   1 
ATOM   2204 C CB  . THR A 1 290 ? -16.29000 10.73700  20.25400  1.000 16.18000 ? 292 THR A CB  1 
ATOM   2205 O OG1 . THR A 1 290 ? -15.23000 10.27500  21.09700  1.000 16.58000 ? 292 THR A OG1 1 
ATOM   2206 C CG2 . THR A 1 290 ? -16.58800 9.70500   19.16000  1.000 14.80000 ? 292 THR A CG2 1 
ATOM   2207 N N   . PRO A 1 291 ? -16.26300 13.54700  21.52700  1.000 14.13000 ? 293 PRO A N   1 
ATOM   2208 C CA  . PRO A 1 291 ? -15.82500 14.28700  22.71400  1.000 15.20000 ? 293 PRO A CA  1 
ATOM   2209 C C   . PRO A 1 291 ? -14.87700 13.48100  23.59000  1.000 19.07000 ? 293 PRO A C   1 
ATOM   2210 O O   . PRO A 1 291 ? -13.90300 14.04500  24.09000  1.000 16.82000 ? 293 PRO A O   1 
ATOM   2211 C CB  . PRO A 1 291 ? -17.14600 14.60900  23.42200  1.000 15.58000 ? 293 PRO A CB  1 
ATOM   2212 C CG  . PRO A 1 291 ? -18.14400 14.68400  22.31300  1.000 15.40000 ? 293 PRO A CG  1 
ATOM   2213 C CD  . PRO A 1 291 ? -17.72100 13.63500  21.32100  1.000 15.14000 ? 293 PRO A CD  1 
ATOM   2214 N N   . PHE A 1 292 ? -15.10100 12.17200  23.75100  1.000 18.29000 ? 294 PHE A N   1 
ATOM   2215 C CA  . PHE A 1 292 ? -14.14900 11.37200  24.52000  1.000 20.67000 ? 294 PHE A CA  1 
ATOM   2216 C C   . PHE A 1 292 ? -12.79400 11.29000  23.82100  1.000 22.19000 ? 294 PHE A C   1 
ATOM   2217 O O   . PHE A 1 292 ? -11.75200 11.40200  24.47100  1.000 23.77000 ? 294 PHE A O   1 
ATOM   2218 C CB  . PHE A 1 292 ? -14.70100 9.96900   24.77800  1.000 23.23000 ? 294 PHE A CB  1 
ATOM   2219 C CG  . PHE A 1 292 ? -13.75000 9.08000   25.54800  1.000 36.62000 ? 294 PHE A CG  1 
ATOM   2220 C CD1 . PHE A 1 292 ? -13.31500 9.44300   26.82200  1.000 35.67000 ? 294 PHE A CD1 1 
ATOM   2221 C CD2 . PHE A 1 292 ? -13.25800 7.90600   24.98800  1.000 36.81000 ? 294 PHE A CD2 1 
ATOM   2222 C CE1 . PHE A 1 292 ? -12.43200 8.64500   27.52700  1.000 38.14000 ? 294 PHE A CE1 1 
ATOM   2223 C CE2 . PHE A 1 292 ? -12.37200 7.09700   25.69500  1.000 37.27000 ? 294 PHE A CE2 1 
ATOM   2224 C CZ  . PHE A 1 292 ? -11.95800 7.46700   26.96300  1.000 39.02000 ? 294 PHE A CZ  1 
ATOM   2225 N N   . ASP A 1 293 ? -12.77900 11.12000  22.49500  1.000 14.77000 ? 295 ASP A N   1 
ATOM   2226 C CA  . ASP A 1 293 ? -11.50800 11.10600  21.76900  1.000 18.19000 ? 295 ASP A CA  1 
ATOM   2227 C C   . ASP A 1 293 ? -10.72800 12.39800  21.98100  1.000 23.22000 ? 295 ASP A C   1 
ATOM   2228 O O   . ASP A 1 293 ? -9.50700  12.37100  22.17100  1.000 21.80000 ? 295 ASP A O   1 
ATOM   2229 C CB  . ASP A 1 293 ? -11.74400 10.88500  20.27600  1.000 19.66000 ? 295 ASP A CB  1 
ATOM   2230 C CG  . ASP A 1 293 ? -12.39800 9.55100   19.98700  1.000 25.49000 ? 295 ASP A CG  1 
ATOM   2231 O OD1 . ASP A 1 293 ? -12.13500 8.58700   20.74600  1.000 30.03000 ? 295 ASP A OD1 1 
ATOM   2232 O OD2 . ASP A 1 293 ? -13.15400 9.46200   18.99700  1.000 20.06000 ? 295 ASP A OD2 1 
ATOM   2233 N N   . VAL A 1 294 ? -11.41000 13.54000  21.92000  1.000 21.03000 ? 296 VAL A N   1 
ATOM   2234 C CA  . VAL A 1 294 ? -10.73800 14.81700  22.14200  1.000 20.40000 ? 296 VAL A CA  1 
ATOM   2235 C C   . VAL A 1 294 ? -10.17600 14.87600  23.55500  1.000 27.32000 ? 296 VAL A C   1 
ATOM   2236 O O   . VAL A 1 294 ? -9.02700  15.28400  23.76900  1.000 31.87000 ? 296 VAL A O   1 
ATOM   2237 C CB  . VAL A 1 294 ? -11.71000 15.98200  21.86900  1.000 19.43000 ? 296 VAL A CB  1 
ATOM   2238 C CG1 . VAL A 1 294 ? -11.07900 17.31600  22.28500  1.000 20.61000 ? 296 VAL A CG1 1 
ATOM   2239 C CG2 . VAL A 1 294 ? -12.12400 16.00000  20.40500  1.000 18.57000 ? 296 VAL A CG2 1 
ATOM   2240 N N   . VAL A 1 295 ? -10.96500 14.44000  24.53800  1.000 23.37000 ? 297 VAL A N   1 
ATOM   2241 C CA  . VAL A 1 295 ? -10.48800 14.43300  25.91800  1.000 31.96000 ? 297 VAL A CA  1 
ATOM   2242 C C   . VAL A 1 295 ? -9.36100  13.41800  26.09400  1.000 32.79000 ? 297 VAL A C   1 
ATOM   2243 O O   . VAL A 1 295 ? -8.31000  13.73600  26.66500  1.000 36.43000 ? 297 VAL A O   1 
ATOM   2244 C CB  . VAL A 1 295 ? -11.65900 14.16900  26.88400  1.000 30.69000 ? 297 VAL A CB  1 
ATOM   2245 C CG1 . VAL A 1 295 ? -11.17200 13.50500  28.15100  1.000 32.82000 ? 297 VAL A CG1 1 
ATOM   2246 C CG2 . VAL A 1 295 ? -12.39200 15.48200  27.20100  1.000 28.87000 ? 297 VAL A CG2 1 
ATOM   2247 N N   . ARG A 1 296 ? -9.55100  12.19300  25.58900  1.000 34.46000 ? 298 ARG A N   1 
ATOM   2248 C CA  . ARG A 1 296 ? -8.52600  11.15900  25.71900  1.000 32.78000 ? 298 ARG A CA  1 
ATOM   2249 C C   . ARG A 1 296 ? -7.21500  11.59000  25.06500  1.000 40.03000 ? 298 ARG A C   1 
ATOM   2250 O O   . ARG A 1 296 ? -6.13300  11.31000  25.58700  1.000 44.51000 ? 298 ARG A O   1 
ATOM   2251 C CB  . ARG A 1 296 ? -9.02800  9.84500   25.11100  1.000 37.68000 ? 298 ARG A CB  1 
ATOM   2252 C CG  . ARG A 1 296 ? -7.93600  8.87700   24.67400  1.000 37.33000 ? 298 ARG A CG  1 
ATOM   2253 C CD  . ARG A 1 296 ? -8.44400  7.43700   24.62400  1.000 41.66000 ? 298 ARG A CD  1 
ATOM   2254 N NE  . ARG A 1 296 ? -8.64800  6.94500   23.24600  1.000 42.14000 ? 298 ARG A NE  1 
ATOM   2255 C CZ  . ARG A 1 296 ? -7.83700  6.09500   22.61000  1.000 35.52000 ? 298 ARG A CZ  1 
ATOM   2256 N NH1 . ARG A 1 296 ? -8.13400  5.71500   21.37300  1.000 32.38000 ? 298 ARG A NH1 1 
ATOM   2257 N NH2 . ARG A 1 296 ? -6.75100  5.60400   23.21500  1.000 26.10000 ? 298 ARG A NH2 1 
ATOM   2258 N N   . GLN A 1 297 ? -7.28800  12.29700  23.93400  1.000 40.70000 ? 299 GLN A N   1 
ATOM   2259 C CA  . GLN A 1 297 ? -6.07800  12.72800  23.23600  1.000 42.68000 ? 299 GLN A CA  1 
ATOM   2260 C C   . GLN A 1 297 ? -5.35300  13.83700  23.98300  1.000 44.00000 ? 299 GLN A C   1 
ATOM   2261 O O   . GLN A 1 297 ? -4.14800  14.01600  23.79000  1.000 48.05000 ? 299 GLN A O   1 
ATOM   2262 C CB  . GLN A 1 297 ? -6.42300  13.18900  21.81500  1.000 41.15000 ? 299 GLN A CB  1 
ATOM   2263 C CG  . GLN A 1 297 ? -5.21900  13.46400  20.93000  1.000 42.55000 ? 299 GLN A CG  1 
ATOM   2264 C CD  . GLN A 1 297 ? -5.25600  12.69300  19.61800  1.000 39.53000 ? 299 GLN A CD  1 
ATOM   2265 O OE1 . GLN A 1 297 ? -6.18300  11.92900  19.35500  1.000 40.84000 ? 299 GLN A OE1 1 
ATOM   2266 N NE2 . GLN A 1 297 ? -4.24400  12.90000  18.78600  1.000 45.58000 ? 299 GLN A NE2 1 
ATOM   2267 N N   . CYS A 1 298 ? -6.06000  14.59200  24.82200  1.000 45.27000 ? 300 CYS A N   1 
ATOM   2268 C CA  . CYS A 1 298 ? -5.46400  15.68600  25.57500  1.000 46.59000 ? 300 CYS A CA  1 
ATOM   2269 C C   . CYS A 1 298 ? -5.23500  15.33700  27.04100  1.000 48.49000 ? 300 CYS A C   1 
ATOM   2270 O O   . CYS A 1 298 ? -4.97000  16.23400  27.84700  1.000 57.30000 ? 300 CYS A O   1 
ATOM   2271 C CB  . CYS A 1 298 ? -6.33200  16.93900  25.46500  1.000 41.25000 ? 300 CYS A CB  1 
ATOM   2272 S SG  . CYS A 1 298 ? -6.72800  17.41100  23.76600  1.000 58.08000 ? 300 CYS A SG  1 
ATOM   2273 N N   . SER A 1 299 ? -5.32800  14.05900  27.40100  1.000 44.16000 ? 301 SER A N   1 
ATOM   2274 C CA  . SER A 1 299 ? -5.06700  13.59500  28.75600  1.000 50.70000 ? 301 SER A CA  1 
ATOM   2275 C C   . SER A 1 299 ? -4.37300  12.24300  28.67800  1.000 48.32000 ? 301 SER A C   1 
ATOM   2276 O O   . SER A 1 299 ? -4.38900  11.57700  27.64200  1.000 52.23000 ? 301 SER A O   1 
ATOM   2277 C CB  . SER A 1 299 ? -6.35700  13.48500  29.57800  1.000 49.17000 ? 301 SER A CB  1 
ATOM   2278 O OG  . SER A 1 299 ? -7.21200  14.58400  29.32500  1.000 48.71000 ? 301 SER A OG  1 
ATOM   2279 N N   . GLY A 1 300 ? -3.75800  11.83700  29.78400  1.000 49.29000 ? 302 GLY A N   1 
ATOM   2280 C CA  . GLY A 1 300 ? -3.02200  10.58500  29.78300  1.000 46.80000 ? 302 GLY A CA  1 
ATOM   2281 C C   . GLY A 1 300 ? -3.76600  9.42100   30.40700  1.000 47.98000 ? 302 GLY A C   1 
ATOM   2282 O O   . GLY A 1 300 ? -3.25300  8.77800   31.32900  1.000 51.37000 ? 302 GLY A O   1 
ATOM   2283 N N   . VAL A 1 301 ? -4.96500  9.13200   29.90300  1.000 49.21000 ? 303 VAL A N   1 
ATOM   2284 C CA  . VAL A 1 301 ? -5.85000  8.13100   30.50200  1.000 48.88000 ? 303 VAL A CA  1 
ATOM   2285 C C   . VAL A 1 301 ? -5.27100  6.71900   30.40800  1.000 48.69000 ? 303 VAL A C   1 
ATOM   2286 O O   . VAL A 1 301 ? -4.74700  6.31800   29.36900  1.000 46.39000 ? 303 VAL A O   1 
ATOM   2287 C CB  . VAL A 1 301 ? -7.25300  8.18100   29.85300  1.000 55.33000 ? 303 VAL A CB  1 
ATOM   2288 C CG1 . VAL A 1 301 ? -8.08900  9.28600   30.48000  1.000 50.97000 ? 303 VAL A CG1 1 
ATOM   2289 C CG2 . VAL A 1 301 ? -7.14000  8.39400   28.35200  1.000 48.79000 ? 303 VAL A CG2 1 
ATOM   2290 N N   . PHE B 1 1   ? -9.56400  1.84600   2.99400   1.000 41.52000 ? 3   PHE B N   1 
ATOM   2291 C CA  . PHE B 1 1   ? -8.13900  1.99900   3.28600   1.000 43.43000 ? 3   PHE B CA  1 
ATOM   2292 C C   . PHE B 1 1   ? -7.86000  2.99400   4.42100   1.000 43.01000 ? 3   PHE B C   1 
ATOM   2293 O O   . PHE B 1 1   ? -8.12300  4.19200   4.28900   1.000 38.37000 ? 3   PHE B O   1 
ATOM   2294 C CB  . PHE B 1 1   ? -7.39600  2.43700   2.03100   1.000 40.01000 ? 3   PHE B CB  1 
ATOM   2295 C CG  . PHE B 1 1   ? -5.91200  2.43500   2.18500   1.000 36.58000 ? 3   PHE B CG  1 
ATOM   2296 C CD1 . PHE B 1 1   ? -5.19900  1.25400   2.08600   1.000 37.34000 ? 3   PHE B CD1 1 
ATOM   2297 C CD2 . PHE B 1 1   ? -5.22800  3.61300   2.42900   1.000 38.05000 ? 3   PHE B CD2 1 
ATOM   2298 C CE1 . PHE B 1 1   ? -3.82600  1.24200   2.22700   1.000 35.75000 ? 3   PHE B CE1 1 
ATOM   2299 C CE2 . PHE B 1 1   ? -3.85300  3.61000   2.56600   1.000 35.21000 ? 3   PHE B CE2 1 
ATOM   2300 C CZ  . PHE B 1 1   ? -3.15200  2.42400   2.46500   1.000 35.26000 ? 3   PHE B CZ  1 
ATOM   2301 N N   . ARG B 1 2   ? -7.29200  2.49300   5.51700   1.000 36.83000 ? 4   ARG B N   1 
ATOM   2302 C CA  . ARG B 1 2   ? -7.12400  3.26400   6.73900   1.000 34.41000 ? 4   ARG B CA  1 
ATOM   2303 C C   . ARG B 1 2   ? -5.69200  3.13000   7.24900   1.000 25.49000 ? 4   ARG B C   1 
ATOM   2304 O O   . ARG B 1 2   ? -4.94100  2.23400   6.84700   1.000 27.62000 ? 4   ARG B O   1 
ATOM   2305 C CB  . ARG B 1 2   ? -8.11300  2.80300   7.83200   1.000 37.87000 ? 4   ARG B CB  1 
ATOM   2306 C CG  . ARG B 1 2   ? -9.57000  3.22600   7.60200   1.000 40.38000 ? 4   ARG B CG  1 
ATOM   2307 C CD  . ARG B 1 2   ? -10.33600 3.31100   8.91800   1.000 32.44000 ? 4   ARG B CD  1 
ATOM   2308 N NE  . ARG B 1 2   ? -9.44800  3.76800   9.97800   1.000 30.97000 ? 4   ARG B NE  1 
ATOM   2309 C CZ  . ARG B 1 2   ? -9.45100  4.98400   10.51200  1.000 36.73000 ? 4   ARG B CZ  1 
ATOM   2310 N NH1 . ARG B 1 2   ? -10.33000 5.90300   10.11000  1.000 37.07000 ? 4   ARG B NH1 1 
ATOM   2311 N NH2 . ARG B 1 2   ? -8.57500  5.27300   11.47300  1.000 35.60000 ? 4   ARG B NH2 1 
ATOM   2312 N N   . LYS B 1 3   ? -5.31700  4.04600   8.13800   1.000 26.54000 ? 5   LYS B N   1 
ATOM   2313 C CA  . LYS B 1 3   ? -4.04700  3.93700   8.84200   1.000 27.68000 ? 5   LYS B CA  1 
ATOM   2314 C C   . LYS B 1 3   ? -4.15700  2.83800   9.89000   1.000 22.30000 ? 5   LYS B C   1 
ATOM   2315 O O   . LYS B 1 3   ? -4.95000  2.94200   10.83100  1.000 24.06000 ? 5   LYS B O   1 
ATOM   2316 C CB  . LYS B 1 3   ? -3.68200  5.26600   9.49700   1.000 30.32000 ? 5   LYS B CB  1 
ATOM   2317 C CG  . LYS B 1 3   ? -2.19800  5.50000   9.57700   1.000 29.39000 ? 5   LYS B CG  1 
ATOM   2318 C CD  . LYS B 1 3   ? -1.89600  6.98200   9.57800   1.000 35.24000 ? 5   LYS B CD  1 
ATOM   2319 C CE  . LYS B 1 3   ? -1.43000  7.44700   8.21200   1.000 32.26000 ? 5   LYS B CE  1 
ATOM   2320 N NZ  . LYS B 1 3   ? -0.99700  8.86300   8.31300   1.000 34.01000 ? 5   LYS B NZ  1 
ATOM   2321 N N   . MET B 1 4   ? -3.37000  1.78900   9.73800   1.000 19.94000 ? 6   MET B N   1 
ATOM   2322 C CA  . MET B 1 4   ? -3.51900  0.60200   10.57100  1.000 20.16000 ? 6   MET B CA  1 
ATOM   2323 C C   . MET B 1 4   ? -2.23000  0.35900   11.33500  1.000 15.90000 ? 6   MET B C   1 
ATOM   2324 O O   . MET B 1 4   ? -1.15300  0.33200   10.73900  1.000 16.78000 ? 6   MET B O   1 
ATOM   2325 C CB  . MET B 1 4   ? -3.86900  -0.60400  9.70300   1.000 16.75000 ? 6   MET B CB  1 
ATOM   2326 C CG  . MET B 1 4   ? -4.09800  -1.88400  10.45700  1.000 25.98000 ? 6   MET B CG  1 
ATOM   2327 S SD  . MET B 1 4   ? -4.64000  -3.16600  9.30300   1.000 35.63000 ? 6   MET B SD  1 
ATOM   2328 C CE  . MET B 1 4   ? -5.89000  -2.27600  8.37900   1.000 24.93000 ? 6   MET B CE  1 
ATOM   2329 N N   . ALA B 1 5   ? -2.34200  0.20000   12.64500  1.000 13.32000 ? 7   ALA B N   1 
ATOM   2330 C CA  . ALA B 1 5   ? -1.20900  -0.13200  13.49300  1.000 12.00000 ? 7   ALA B CA  1 
ATOM   2331 C C   . ALA B 1 5   ? -1.14800  -1.63600  13.70400  1.000 12.75000 ? 7   ALA B C   1 
ATOM   2332 O O   . ALA B 1 5   ? -2.15500  -2.33800  13.57800  1.000 12.29000 ? 7   ALA B O   1 
ATOM   2333 C CB  . ALA B 1 5   ? -1.32400  0.57100   14.84700  1.000 10.99000 ? 7   ALA B CB  1 
ATOM   2334 N N   . PHE B 1 6   ? 0.04500   -2.12700  14.03600  1.000 11.06000 ? 8   PHE B N   1 
ATOM   2335 C CA  . PHE B 1 6   ? 0.17800   -3.51900  14.45000  1.000 13.40000 ? 8   PHE B CA  1 
ATOM   2336 C C   . PHE B 1 6   ? -0.51300  -3.74500  15.79100  1.000 12.09000 ? 8   PHE B C   1 
ATOM   2337 O O   . PHE B 1 6   ? -0.54900  -2.84500  16.64100  1.000 14.38000 ? 8   PHE B O   1 
ATOM   2338 C CB  . PHE B 1 6   ? 1.64700   -3.92700  14.57300  1.000 12.70000 ? 8   PHE B CB  1 
ATOM   2339 C CG  . PHE B 1 6   ? 2.34300   -4.03800  13.25700  1.000 15.46000 ? 8   PHE B CG  1 
ATOM   2340 C CD1 . PHE B 1 6   ? 2.16500   -5.15700  12.46500  1.000 17.99000 ? 8   PHE B CD1 1 
ATOM   2341 C CD2 . PHE B 1 6   ? 3.16200   -3.01300  12.80000  1.000 16.78000 ? 8   PHE B CD2 1 
ATOM   2342 C CE1 . PHE B 1 6   ? 2.79800   -5.25900  11.23500  1.000 23.57000 ? 8   PHE B CE1 1 
ATOM   2343 C CE2 . PHE B 1 6   ? 3.80100   -3.11500  11.56700  1.000 16.64000 ? 8   PHE B CE2 1 
ATOM   2344 C CZ  . PHE B 1 6   ? 3.61900   -4.23800  10.79100  1.000 18.76000 ? 8   PHE B CZ  1 
ATOM   2345 N N   . PRO B 1 7   ? -1.06400  -4.94300  16.00800  1.000 13.05000 ? 9   PRO B N   1 
ATOM   2346 C CA  . PRO B 1 7   ? -1.59500  -5.28100  17.33100  1.000 14.17000 ? 9   PRO B CA  1 
ATOM   2347 C C   . PRO B 1 7   ? -0.50700  -5.10900  18.38200  1.000 15.28000 ? 9   PRO B C   1 
ATOM   2348 O O   . PRO B 1 7   ? 0.62500   -5.56100  18.20500  1.000 15.29000 ? 9   PRO B O   1 
ATOM   2349 C CB  . PRO B 1 7   ? -2.01400  -6.75300  17.18600  1.000 17.31000 ? 9   PRO B CB  1 
ATOM   2350 C CG  . PRO B 1 7   ? -2.14800  -6.98500  15.70900  1.000 18.02000 ? 9   PRO B CG  1 
ATOM   2351 C CD  . PRO B 1 7   ? -1.11100  -6.08400  15.08000  1.000 13.42000 ? 9   PRO B CD  1 
ATOM   2352 N N   . SER B 1 8   ? -0.85800  -4.44900  19.47700  1.000 12.05000 ? 10  SER B N   1 
ATOM   2353 C CA  . SER B 1 8   ? 0.14000   -3.99100  20.42900  1.000 14.73000 ? 10  SER B CA  1 
ATOM   2354 C C   . SER B 1 8   ? 0.39700   -4.97500  21.56900  1.000 12.89000 ? 10  SER B C   1 
ATOM   2355 O O   . SER B 1 8   ? 1.26000   -4.70000  22.40800  1.000 12.71000 ? 10  SER B O   1 
ATOM   2356 C CB  . SER B 1 8   ? -0.28400  -2.63900  21.00100  1.000 14.70000 ? 10  SER B CB  1 
ATOM   2357 O OG  . SER B 1 8   ? -1.52200  -2.74500  21.67600  1.000 15.39000 ? 10  SER B OG  1 
ATOM   2358 N N   . GLY B 1 9   ? -0.29300  -6.12000  21.59500  1.000 14.55000 ? 11  GLY B N   1 
ATOM   2359 C CA  . GLY B 1 9   ? -0.26300  -6.97000  22.78000  1.000 13.90000 ? 11  GLY B CA  1 
ATOM   2360 C C   . GLY B 1 9   ? 1.13300   -7.43000  23.16500  1.000 14.36000 ? 11  GLY B C   1 
ATOM   2361 O O   . GLY B 1 9   ? 1.49200   -7.41300  24.34600  1.000 16.14000 ? 11  GLY B O   1 
ATOM   2362 N N   . LYS B 1 10  ? 1.94500   -7.82600  22.17500  1.000 13.64000 ? 12  LYS B N   1 
ATOM   2363 C CA  . LYS B 1 10  ? 3.30000   -8.29300  22.47400  1.000 14.38000 ? 12  LYS B CA  1 
ATOM   2364 C C   . LYS B 1 10  ? 4.15600   -7.20300  23.11500  1.000 14.76000 ? 12  LYS B C   1 
ATOM   2365 O O   . LYS B 1 10  ? 5.07400   -7.50800  23.88900  1.000 16.93000 ? 12  LYS B O   1 
ATOM   2366 C CB  . LYS B 1 10  ? 3.97400   -8.80900  21.20200  1.000 16.11000 ? 12  LYS B CB  1 
ATOM   2367 C CG  . LYS B 1 10  ? 3.32600   -10.07600 20.62600  1.000 22.22000 ? 12  LYS B CG  1 
ATOM   2368 C CD  . LYS B 1 10  ? 4.02500   -10.53500 19.35400  1.000 22.93000 ? 12  LYS B CD  1 
ATOM   2369 C CE  . LYS B 1 10  ? 3.70200   -11.99800 19.02400  1.000 31.73000 ? 12  LYS B CE  1 
ATOM   2370 N NZ  . LYS B 1 10  ? 2.24000   -12.23400 18.80600  1.000 28.88000 ? 12  LYS B NZ  1 
ATOM   2371 N N   . VAL B 1 11  ? 3.88500   -5.94000  22.80100  1.000 10.53000 ? 13  VAL B N   1 
ATOM   2372 C CA  . VAL B 1 11  ? 4.63400   -4.83100  23.39500  1.000 11.24000 ? 13  VAL B CA  1 
ATOM   2373 C C   . VAL B 1 11  ? 4.05200   -4.43800  24.74200  1.000 11.05000 ? 13  VAL B C   1 
ATOM   2374 O O   . VAL B 1 11  ? 4.79700   -4.12500  25.67700  1.000 10.97000 ? 13  VAL B O   1 
ATOM   2375 C CB  . VAL B 1 11  ? 4.67000   -3.62500  22.42000  1.000 10.50000 ? 13  VAL B CB  1 
ATOM   2376 C CG1 . VAL B 1 11  ? 5.49600   -2.44800  23.00200  1.000 9.50000  ? 13  VAL B CG1 1 
ATOM   2377 C CG2 . VAL B 1 11  ? 5.24300   -4.04700  21.08900  1.000 13.65000 ? 13  VAL B CG2 1 
ATOM   2378 N N   . GLU B 1 12  ? 2.71600   -4.45500  24.87600  1.000 10.40000 ? 14  GLU B N   1 
ATOM   2379 C CA  . GLU B 1 12  ? 2.10700   -4.05700  26.14800  1.000 11.70000 ? 14  GLU B CA  1 
ATOM   2380 C C   . GLU B 1 12  ? 2.67000   -4.86600  27.30800  1.000 12.85000 ? 14  GLU B C   1 
ATOM   2381 O O   . GLU B 1 12  ? 2.84800   -4.33900  28.40800  1.000 14.02000 ? 14  GLU B O   1 
ATOM   2382 C CB  . GLU B 1 12  ? 0.59000   -4.23700  26.11900  1.000 13.15000 ? 14  GLU B CB  1 
ATOM   2383 C CG  . GLU B 1 12  ? -0.16100  -3.37500  25.12300  1.000 12.51000 ? 14  GLU B CG  1 
ATOM   2384 C CD  . GLU B 1 12  ? -1.58200  -3.89200  24.90400  1.000 13.48000 ? 14  GLU B CD  1 
ATOM   2385 O OE1 . GLU B 1 12  ? -2.01800  -3.97400  23.74600  1.000 14.16000 ? 14  GLU B OE1 1 
ATOM   2386 O OE2 . GLU B 1 12  ? -2.25600  -4.21500  25.90100  1.000 17.35000 ? 14  GLU B OE2 1 
ATOM   2387 N N   . GLY B 1 13  ? 2.93200   -6.15100  27.08800  1.000 14.63000 ? 15  GLY B N   1 
ATOM   2388 C CA  . GLY B 1 13  ? 3.46800   -6.98200  28.15000  1.000 18.13000 ? 15  GLY B CA  1 
ATOM   2389 C C   . GLY B 1 13  ? 4.87700   -6.63700  28.56700  1.000 18.14000 ? 15  GLY B C   1 
ATOM   2390 O O   . GLY B 1 13  ? 5.39100   -7.23200  29.51800  1.000 23.39000 ? 15  GLY B O   1 
ATOM   2391 N N   . CYS B 1 14  ? 5.51500   -5.68600  27.88500  1.000 13.54000 ? 16  CYS B N   1 
ATOM   2392 C CA  . CYS B 1 14  ? 6.88700   -5.29500  28.17600  1.000 15.63000 ? 16  CYS B CA  1 
ATOM   2393 C C   . CYS B 1 14  ? 6.98500   -3.91900  28.80100  1.000 13.47000 ? 16  CYS B C   1 
ATOM   2394 O O   . CYS B 1 14  ? 8.08700   -3.50100  29.17000  1.000 14.38000 ? 16  CYS B O   1 
ATOM   2395 C CB  . CYS B 1 14  ? 7.74100   -5.31800  26.90200  1.000 14.11000 ? 16  CYS B CB  1 
ATOM   2396 S SG  . CYS B 1 14  ? 7.81000   -6.86800  26.02000  1.000 19.80000 ? 16  CYS B SG  1 
ATOM   2397 N N   . MET B 1 15  ? 5.87700   -3.19500  28.91600  1.000 13.08000 ? 17  MET B N   1 
ATOM   2398 C CA  . MET B 1 15  ? 5.93700   -1.82200  29.38900  1.000 14.54000 ? 17  MET B CA  1 
ATOM   2399 C C   . MET B 1 15  ? 5.93600   -1.78900  30.90900  1.000 17.11000 ? 17  MET B C   1 
ATOM   2400 O O   . MET B 1 15  ? 5.11800   -2.45400  31.55800  1.000 15.75000 ? 17  MET B O   1 
ATOM   2401 C CB  . MET B 1 15  ? 4.76600   -1.01100  28.84500  1.000 16.17000 ? 17  MET B CB  1 
ATOM   2402 C CG  . MET B 1 15  ? 4.73300   -0.93200  27.33500  1.000 11.27000 ? 17  MET B CG  1 
ATOM   2403 S SD  . MET B 1 15  ? 6.30500   -0.41500  26.62100  1.000 14.73000 ? 17  MET B SD  1 
ATOM   2404 C CE  . MET B 1 15  ? 6.57200   1.16400   27.44200  1.000 9.58000  ? 17  MET B CE  1 
ATOM   2405 N N   . VAL B 1 16  ? 6.85300   -1.01200  31.47700  1.000 13.63000 ? 18  VAL B N   1 
ATOM   2406 C CA  . VAL B 1 16  ? 6.93300   -0.82000  32.91700  1.000 16.48000 ? 18  VAL B CA  1 
ATOM   2407 C C   . VAL B 1 16  ? 7.12800   0.66100   33.19300  1.000 17.13000 ? 18  VAL B C   1 
ATOM   2408 O O   . VAL B 1 16  ? 7.34900   1.46400   32.29100  1.000 14.18000 ? 18  VAL B O   1 
ATOM   2409 C CB  . VAL B 1 16  ? 8.07400   -1.64300  33.56000  1.000 16.15000 ? 18  VAL B CB  1 
ATOM   2410 C CG1 . VAL B 1 16  ? 7.91700   -3.12000  33.22800  1.000 15.90000 ? 18  VAL B CG1 1 
ATOM   2411 C CG2 . VAL B 1 16  ? 9.42000   -1.13700  33.09900  1.000 17.12000 ? 18  VAL B CG2 1 
ATOM   2412 N N   . GLN B 1 17  ? 7.05500   1.01100   34.46600  1.000 19.39000 ? 19  GLN B N   1 
ATOM   2413 C CA  . GLN B 1 17  ? 7.26100   2.36500   34.94100  1.000 18.09000 ? 19  GLN B CA  1 
ATOM   2414 C C   . GLN B 1 17  ? 8.62500   2.43700   35.61800  1.000 20.58000 ? 19  GLN B C   1 
ATOM   2415 O O   . GLN B 1 17  ? 9.02200   1.50700   36.32300  1.000 23.43000 ? 19  GLN B O   1 
ATOM   2416 C CB  . GLN B 1 17  ? 6.13400   2.73500   35.89900  1.000 20.78000 ? 19  GLN B CB  1 
ATOM   2417 C CG  . GLN B 1 17  ? 6.13400   4.11900   36.45600  1.000 24.18000 ? 19  GLN B CG  1 
ATOM   2418 C CD  . GLN B 1 17  ? 4.92500   4.32800   37.34700  1.000 27.61000 ? 19  GLN B CD  1 
ATOM   2419 O OE1 . GLN B 1 17  ? 4.46700   5.44800   37.54100  1.000 32.66000 ? 19  GLN B OE1 1 
ATOM   2420 N NE2 . GLN B 1 17  ? 4.38800   3.22900   37.88200  1.000 33.80000 ? 19  GLN B NE2 1 
ATOM   2421 N N   . VAL B 1 18  ? 9.36900   3.50700   35.34500  1.000 18.76000 ? 20  VAL B N   1 
ATOM   2422 C CA  . VAL B 1 18  ? 10.69200  3.72900   35.92200  1.000 20.60000 ? 20  VAL B CA  1 
ATOM   2423 C C   . VAL B 1 18  ? 10.67200  5.08400   36.60800  1.000 20.58000 ? 20  VAL B C   1 
ATOM   2424 O O   . VAL B 1 18  ? 10.26300  6.08100   36.00500  1.000 19.08000 ? 20  VAL B O   1 
ATOM   2425 C CB  . VAL B 1 18  ? 11.81300  3.68900   34.86500  1.000 17.13000 ? 20  VAL B CB  1 
ATOM   2426 C CG1 . VAL B 1 18  ? 13.16400  3.94000   35.53000  1.000 18.87000 ? 20  VAL B CG1 1 
ATOM   2427 C CG2 . VAL B 1 18  ? 11.82900  2.36700   34.12300  1.000 19.84000 ? 20  VAL B CG2 1 
ATOM   2428 N N   . THR B 1 19  ? 11.12500  5.12300   37.85800  1.000 23.59000 ? 21  THR B N   1 
ATOM   2429 C CA  . THR B 1 19  ? 11.12000  6.35200   38.63600  1.000 24.79000 ? 21  THR B CA  1 
ATOM   2430 C C   . THR B 1 19  ? 12.51300  6.60700   39.18300  1.000 26.28000 ? 21  THR B C   1 
ATOM   2431 O O   . THR B 1 19  ? 13.17400  5.69300   39.69100  1.000 25.75000 ? 21  THR B O   1 
ATOM   2432 C CB  . THR B 1 19  ? 10.11000  6.29600   39.79400  1.000 26.51000 ? 21  THR B CB  1 
ATOM   2433 O OG1 . THR B 1 19  ? 8.80400   6.02700   39.27600  1.000 34.04000 ? 21  THR B OG1 1 
ATOM   2434 C CG2 . THR B 1 19  ? 10.07500  7.63700   40.53400  1.000 30.77000 ? 21  THR B CG2 1 
ATOM   2435 N N   . CYS B 1 20  ? 12.95600  7.85300   39.05500  1.000 29.12000 ? 22  CYS B N   1 
ATOM   2436 C CA  . CYS B 1 20  ? 14.22500  8.29300   39.61300  1.000 30.47000 ? 22  CYS B CA  1 
ATOM   2437 C C   . CYS B 1 20  ? 14.02200  9.70000   40.14500  1.000 35.97000 ? 22  CYS B C   1 
ATOM   2438 O O   . CYS B 1 20  ? 13.73100  10.62400  39.37400  1.000 30.19000 ? 22  CYS B O   1 
ATOM   2439 C CB  . CYS B 1 20  ? 15.33700  8.24600   38.56300  1.000 27.33000 ? 22  CYS B CB  1 
ATOM   2440 S SG  . CYS B 1 20  ? 16.98400  8.47600   39.22600  1.000 41.91000 ? 22  CYS B SG  1 
ATOM   2441 N N   . GLY B 1 21  ? 14.15800  9.85400   41.45900  1.000 35.88000 ? 23  GLY B N   1 
ATOM   2442 C CA  . GLY B 1 21  ? 13.85900  11.13600  42.06800  1.000 32.80000 ? 23  GLY B CA  1 
ATOM   2443 C C   . GLY B 1 21  ? 12.39600  11.47000  41.89400  1.000 30.24000 ? 23  GLY B C   1 
ATOM   2444 O O   . GLY B 1 21  ? 11.50300  10.68200  42.21900  1.000 35.89000 ? 23  GLY B O   1 
ATOM   2445 N N   . THR B 1 22  ? 12.13800  12.65400  41.36100  1.000 30.41000 ? 24  THR B N   1 
ATOM   2446 C CA  . THR B 1 22  ? 10.78600  13.11700  41.11300  1.000 36.35000 ? 24  THR B CA  1 
ATOM   2447 C C   . THR B 1 22  ? 10.34000  12.88100  39.67000  1.000 34.77000 ? 24  THR B C   1 
ATOM   2448 O O   . THR B 1 22  ? 9.31500   13.42800  39.24900  1.000 33.77000 ? 24  THR B O   1 
ATOM   2449 C CB  . THR B 1 22  ? 10.69000  14.60200  41.47100  1.000 36.44000 ? 24  THR B CB  1 
ATOM   2450 O OG1 . THR B 1 22  ? 9.39400   15.10900  41.12900  1.000 43.39000 ? 24  THR B OG1 1 
ATOM   2451 C CG2 . THR B 1 22  ? 11.75600  15.38300  40.72000  1.000 37.13000 ? 24  THR B CG2 1 
ATOM   2452 N N   . THR B 1 23  ? 11.08000  12.08500  38.89900  1.000 30.29000 ? 25  THR B N   1 
ATOM   2453 C CA  . THR B 1 23  ? 10.78700  11.89400  37.48300  1.000 31.79000 ? 25  THR B CA  1 
ATOM   2454 C C   . THR B 1 23  ? 10.30400  10.47400  37.22800  1.000 29.68000 ? 25  THR B C   1 
ATOM   2455 O O   . THR B 1 23  ? 10.96000  9.50600   37.62500  1.000 25.16000 ? 25  THR B O   1 
ATOM   2456 C CB  . THR B 1 23  ? 12.00700  12.19200  36.61400  1.000 33.88000 ? 25  THR B CB  1 
ATOM   2457 O OG1 . THR B 1 23  ? 12.35100  13.57700  36.74200  1.000 35.07000 ? 25  THR B OG1 1 
ATOM   2458 C CG2 . THR B 1 23  ? 11.69600  11.88300  35.15000  1.000 27.16000 ? 25  THR B CG2 1 
ATOM   2459 N N   . THR B 1 24  ? 9.16200   10.36400  36.55600  1.000 28.99000 ? 26  THR B N   1 
ATOM   2460 C CA  . THR B 1 24  ? 8.54700   9.09200   36.21200  1.000 27.12000 ? 26  THR B CA  1 
ATOM   2461 C C   . THR B 1 24  ? 8.35500   9.03300   34.70000  1.000 20.38000 ? 26  THR B C   1 
ATOM   2462 O O   . THR B 1 24  ? 7.93800   10.01700  34.08500  1.000 24.96000 ? 26  THR B O   1 
ATOM   2463 C CB  . THR B 1 24  ? 7.20000   8.93300   36.92400  1.000 26.48000 ? 26  THR B CB  1 
ATOM   2464 O OG1 . THR B 1 24  ? 7.40500   8.93200   38.34400  1.000 38.24000 ? 26  THR B OG1 1 
ATOM   2465 C CG2 . THR B 1 24  ? 6.54100   7.64800   36.52400  1.000 24.29000 ? 26  THR B CG2 1 
ATOM   2466 N N   . LEU B 1 25  ? 8.70100   7.89600   34.10400  1.000 17.93000 ? 27  LEU B N   1 
ATOM   2467 C CA  . LEU B 1 25  ? 8.43900   7.65700   32.68700  1.000 16.76000 ? 27  LEU B CA  1 
ATOM   2468 C C   . LEU B 1 25  ? 8.34200   6.14900   32.47100  1.000 15.12000 ? 27  LEU B C   1 
ATOM   2469 O O   . LEU B 1 25  ? 8.32500   5.36500   33.42600  1.000 17.91000 ? 27  LEU B O   1 
ATOM   2470 C CB  . LEU B 1 25  ? 9.51400   8.31000   31.80200  1.000 15.48000 ? 27  LEU B CB  1 
ATOM   2471 C CG  . LEU B 1 25  ? 10.98500  8.26000   32.23500  1.000 14.10000 ? 27  LEU B CG  1 
ATOM   2472 C CD1 . LEU B 1 25  ? 11.58800  6.83300   32.21500  1.000 15.89000 ? 27  LEU B CD1 1 
ATOM   2473 C CD2 . LEU B 1 25  ? 11.82800  9.19500   31.36600  1.000 17.73000 ? 27  LEU B CD2 1 
ATOM   2474 N N   . ASN B 1 26  ? 8.31900   5.74000   31.20600  1.000 13.01000 ? 28  ASN B N   1 
ATOM   2475 C CA  . ASN B 1 26  ? 8.11700   4.34900   30.83500  1.000 11.16000 ? 28  ASN B CA  1 
ATOM   2476 C C   . ASN B 1 26  ? 9.43400   3.67700   30.49900  1.000 14.09000 ? 28  ASN B C   1 
ATOM   2477 O O   . ASN B 1 26  ? 10.37300  4.32300   30.02700  1.000 14.82000 ? 28  ASN B O   1 
ATOM   2478 C CB  . ASN B 1 26  ? 7.18100   4.25700   29.63300  1.000 12.32000 ? 28  ASN B CB  1 
ATOM   2479 C CG  . ASN B 1 26  ? 5.90400   5.02800   29.85500  1.000 12.95000 ? 28  ASN B CG  1 
ATOM   2480 O OD1 . ASN B 1 26  ? 5.01100   4.55900   30.56500  1.000 15.25000 ? 28  ASN B OD1 1 
ATOM   2481 N ND2 . ASN B 1 26  ? 5.81300   6.22200   29.27500  1.000 11.16000 ? 28  ASN B ND2 1 
ATOM   2482 N N   . GLY B 1 27  ? 9.47600   2.36100   30.72200  1.000 12.25000 ? 29  GLY B N   1 
ATOM   2483 C CA  . GLY B 1 27  ? 10.60100  1.55000   30.31600  1.000 11.09000 ? 29  GLY B CA  1 
ATOM   2484 C C   . GLY B 1 27  ? 10.11700  0.31800   29.58900  1.000 11.55000 ? 29  GLY B C   1 
ATOM   2485 O O   . GLY B 1 27  ? 8.95800   -0.08800  29.69600  1.000 12.80000 ? 29  GLY B O   1 
ATOM   2486 N N   . LEU B 1 28  ? 11.01700  -0.26200  28.80600  1.000 11.61000 ? 30  LEU B N   1 
ATOM   2487 C CA  . LEU B 1 28  ? 10.75700  -1.45800  28.01400  1.000 11.61000 ? 30  LEU B CA  1 
ATOM   2488 C C   . LEU B 1 28  ? 11.51000  -2.61100  28.65900  1.000 13.48000 ? 30  LEU B C   1 
ATOM   2489 O O   . LEU B 1 28  ? 12.74300  -2.56500  28.75700  1.000 14.43000 ? 30  LEU B O   1 
ATOM   2490 C CB  . LEU B 1 28  ? 11.20800  -1.26900  26.56700  1.000 14.24000 ? 30  LEU B CB  1 
ATOM   2491 C CG  . LEU B 1 28  ? 10.97600  -2.42200  25.58800  1.000 13.13000 ? 30  LEU B CG  1 
ATOM   2492 C CD1 . LEU B 1 28  ? 9.48300   -2.55300  25.28800  1.000 12.34000 ? 30  LEU B CD1 1 
ATOM   2493 C CD2 . LEU B 1 28  ? 11.77600  -2.17500  24.30200  1.000 11.48000 ? 30  LEU B CD2 1 
ATOM   2494 N N   . TRP B 1 29  ? 10.76900  -3.63400  29.09500  1.000 12.20000 ? 31  TRP B N   1 
ATOM   2495 C CA  . TRP B 1 29  ? 11.29500  -4.74100  29.89300  1.000 12.96000 ? 31  TRP B CA  1 
ATOM   2496 C C   . TRP B 1 29  ? 11.41900  -5.96600  28.99800  1.000 12.75000 ? 31  TRP B C   1 
ATOM   2497 O O   . TRP B 1 29  ? 10.41100  -6.59100  28.63700  1.000 12.45000 ? 31  TRP B O   1 
ATOM   2498 C CB  . TRP B 1 29  ? 10.38400  -5.00000  31.09500  1.000 13.67000 ? 31  TRP B CB  1 
ATOM   2499 C CG  . TRP B 1 29  ? 10.81600  -6.10800  32.03600  1.000 18.13000 ? 31  TRP B CG  1 
ATOM   2500 C CD1 . TRP B 1 29  ? 12.08300  -6.60200  32.22500  1.000 19.67000 ? 31  TRP B CD1 1 
ATOM   2501 C CD2 . TRP B 1 29  ? 9.96500   -6.84100  32.92900  1.000 19.06000 ? 31  TRP B CD2 1 
ATOM   2502 N NE1 . TRP B 1 29  ? 12.06500  -7.60200  33.18100  1.000 20.94000 ? 31  TRP B NE1 1 
ATOM   2503 C CE2 . TRP B 1 29  ? 10.77900  -7.76500  33.62800  1.000 19.60000 ? 31  TRP B CE2 1 
ATOM   2504 C CE3 . TRP B 1 29  ? 8.59400   -6.80500  33.20500  1.000 17.63000 ? 31  TRP B CE3 1 
ATOM   2505 C CZ2 . TRP B 1 29  ? 10.26300  -8.64600  34.58200  1.000 20.32000 ? 31  TRP B CZ2 1 
ATOM   2506 C CZ3 . TRP B 1 29  ? 8.08100   -7.68500  34.15200  1.000 22.11000 ? 31  TRP B CZ3 1 
ATOM   2507 C CH2 . TRP B 1 29  ? 8.92100   -8.59300  34.83100  1.000 22.78000 ? 31  TRP B CH2 1 
ATOM   2508 N N   . LEU B 1 30  ? 12.65500  -6.29700  28.63000  1.000 12.98000 ? 32  LEU B N   1 
ATOM   2509 C CA  . LEU B 1 30  ? 12.95800  -7.40300  27.73500  1.000 15.11000 ? 32  LEU B CA  1 
ATOM   2510 C C   . LEU B 1 30  ? 13.94000  -8.32600  28.43700  1.000 20.21000 ? 32  LEU B C   1 
ATOM   2511 O O   . LEU B 1 30  ? 15.05500  -7.90600  28.76900  1.000 17.48000 ? 32  LEU B O   1 
ATOM   2512 C CB  . LEU B 1 30  ? 13.55500  -6.90200  26.42200  1.000 17.90000 ? 32  LEU B CB  1 
ATOM   2513 C CG  . LEU B 1 30  ? 12.67600  -5.97700  25.59000  1.000 15.77000 ? 32  LEU B CG  1 
ATOM   2514 C CD1 . LEU B 1 30  ? 13.49300  -5.45200  24.41900  1.000 15.47000 ? 32  LEU B CD1 1 
ATOM   2515 C CD2 . LEU B 1 30  ? 11.42800  -6.72100  25.11000  1.000 12.94000 ? 32  LEU B CD2 1 
ATOM   2516 N N   . ASP B 1 31  ? 13.52900  -9.57300  28.65400  1.000 24.20000 ? 33  ASP B N   1 
ATOM   2517 C CA  . ASP B 1 31  ? 14.32000  -10.49600 29.45900  1.000 26.74000 ? 33  ASP B CA  1 
ATOM   2518 C C   . ASP B 1 31  ? 14.62100  -9.82600  30.79100  1.000 24.63000 ? 33  ASP B C   1 
ATOM   2519 O O   . ASP B 1 31  ? 13.68800  -9.37200  31.45800  1.000 27.09000 ? 33  ASP B O   1 
ATOM   2520 C CB  . ASP B 1 31  ? 15.56900  -10.92400 28.69300  1.000 23.28000 ? 33  ASP B CB  1 
ATOM   2521 C CG  . ASP B 1 31  ? 15.22100  -11.76600 27.46800  1.000 26.71000 ? 33  ASP B CG  1 
ATOM   2522 O OD1 . ASP B 1 31  ? 14.46100  -12.74300 27.62800  1.000 33.57000 ? 33  ASP B OD1 1 
ATOM   2523 O OD2 . ASP B 1 31  ? 15.68300  -11.44800 26.34900  1.000 33.19000 ? 33  ASP B OD2 1 
ATOM   2524 N N   . ASP B 1 32  ? 15.88600  -9.70400  31.19500  1.000 23.41000 ? 34  ASP B N   1 
ATOM   2525 C CA  . ASP B 1 32  ? 16.15500  -9.12600  32.50500  1.000 24.70000 ? 34  ASP B CA  1 
ATOM   2526 C C   . ASP B 1 32  ? 16.70000  -7.69700  32.43600  1.000 25.11000 ? 34  ASP B C   1 
ATOM   2527 O O   . ASP B 1 32  ? 17.35800  -7.24300  33.38000  1.000 23.14000 ? 34  ASP B O   1 
ATOM   2528 C CB  . ASP B 1 32  ? 17.09400  -10.03500 33.30700  1.000 29.38000 ? 34  ASP B CB  1 
ATOM   2529 C CG  . ASP B 1 32  ? 18.49600  -10.11700 32.71800  1.000 32.43000 ? 34  ASP B CG  1 
ATOM   2530 O OD1 . ASP B 1 32  ? 18.70300  -9.73900  31.54300  1.000 32.62000 ? 34  ASP B OD1 1 
ATOM   2531 O OD2 . ASP B 1 32  ? 19.40300  -10.56400 33.45000  1.000 39.09000 ? 34  ASP B OD2 1 
ATOM   2532 N N   . VAL B 1 33  ? 16.41100  -6.95800  31.36100  1.000 18.50000 ? 35  VAL B N   1 
ATOM   2533 C CA  . VAL B 1 33  ? 16.86300  -5.57700  31.22500  1.000 16.96000 ? 35  VAL B CA  1 
ATOM   2534 C C   . VAL B 1 33  ? 15.66400  -4.67600  30.94800  1.000 17.97000 ? 35  VAL B C   1 
ATOM   2535 O O   . VAL B 1 33  ? 14.79900  -5.01500  30.12900  1.000 17.04000 ? 35  VAL B O   1 
ATOM   2536 C CB  . VAL B 1 33  ? 17.92100  -5.44000  30.10700  1.000 20.62000 ? 35  VAL B CB  1 
ATOM   2537 C CG1 . VAL B 1 33  ? 18.28500  -3.99000  29.88400  1.000 18.02000 ? 35  VAL B CG1 1 
ATOM   2538 C CG2 . VAL B 1 33  ? 19.17300  -6.23900  30.46000  1.000 28.64000 ? 35  VAL B CG2 1 
ATOM   2539 N N   . VAL B 1 34  ? 15.62300  -3.52400  31.62200  1.000 13.45000 ? 36  VAL B N   1 
ATOM   2540 C CA  . VAL B 1 34  ? 14.65200  -2.46300  31.35500  1.000 13.53000 ? 36  VAL B CA  1 
ATOM   2541 C C   . VAL B 1 34  ? 15.38900  -1.31700  30.66000  1.000 16.95000 ? 36  VAL B C   1 
ATOM   2542 O O   . VAL B 1 34  ? 16.38300  -0.78900  31.18700  1.000 17.43000 ? 36  VAL B O   1 
ATOM   2543 C CB  . VAL B 1 34  ? 13.96700  -1.99000  32.64700  1.000 13.93000 ? 36  VAL B CB  1 
ATOM   2544 C CG1 . VAL B 1 34  ? 13.04300  -0.81200  32.38000  1.000 18.81000 ? 36  VAL B CG1 1 
ATOM   2545 C CG2 . VAL B 1 34  ? 13.19500  -3.14900  33.30900  1.000 16.32000 ? 36  VAL B CG2 1 
ATOM   2546 N N   . TYR B 1 35  ? 14.90900  -0.94700  29.47500  1.000 13.91000 ? 37  TYR B N   1 
ATOM   2547 C CA  . TYR B 1 35  ? 15.44200  0.15400   28.68500  1.000 14.07000 ? 37  TYR B CA  1 
ATOM   2548 C C   . TYR B 1 35  ? 14.55100  1.37700   28.86100  1.000 15.40000 ? 37  TYR B C   1 
ATOM   2549 O O   . TYR B 1 35  ? 13.32500  1.27500   28.73000  1.000 12.58000 ? 37  TYR B O   1 
ATOM   2550 C CB  . TYR B 1 35  ? 15.50300  -0.22200  27.19700  1.000 11.27000 ? 37  TYR B CB  1 
ATOM   2551 C CG  . TYR B 1 35  ? 16.26700  -1.48700  26.89900  1.000 15.69000 ? 37  TYR B CG  1 
ATOM   2552 C CD1 . TYR B 1 35  ? 15.70700  -2.73900  27.13300  1.000 17.38000 ? 37  TYR B CD1 1 
ATOM   2553 C CD2 . TYR B 1 35  ? 17.54800  -1.43100  26.36900  1.000 16.86000 ? 37  TYR B CD2 1 
ATOM   2554 C CE1 . TYR B 1 35  ? 16.41600  -3.89800  26.86400  1.000 17.44000 ? 37  TYR B CE1 1 
ATOM   2555 C CE2 . TYR B 1 35  ? 18.25300  -2.57400  26.08600  1.000 17.36000 ? 37  TYR B CE2 1 
ATOM   2556 C CZ  . TYR B 1 35  ? 17.69000  -3.80000  26.34200  1.000 18.55000 ? 37  TYR B CZ  1 
ATOM   2557 O OH  . TYR B 1 35  ? 18.40400  -4.92500  26.05500  1.000 25.98000 ? 37  TYR B OH  1 
ATOM   2558 N N   . CYS B 1 36  ? 15.15400  2.53000   29.13800  1.000 12.65000 ? 38  CYS B N   1 
ATOM   2559 C CA  . CYS B 1 36  ? 14.38500  3.76000   29.25600  1.000 14.40000 ? 38  CYS B CA  1 
ATOM   2560 C C   . CYS B 1 36  ? 15.26800  4.93400   28.88300  1.000 13.36000 ? 38  CYS B C   1 
ATOM   2561 O O   . CYS B 1 36  ? 16.49700  4.79300   28.79700  1.000 12.97000 ? 38  CYS B O   1 
ATOM   2562 C CB  . CYS B 1 36  ? 13.80300  3.92500   30.67000  1.000 15.58000 ? 38  CYS B CB  1 
ATOM   2563 S SG  . CYS B 1 36  ? 15.00800  4.35200   31.96000  1.000 17.94000 ? 38  CYS B SG  1 
ATOM   2564 N N   . PRO B 1 37  ? 14.68500  6.10300   28.61800  1.000 12.02000 ? 39  PRO B N   1 
ATOM   2565 C CA  . PRO B 1 37  ? 15.50100  7.28900   28.32700  1.000 12.77000 ? 39  PRO B CA  1 
ATOM   2566 C C   . PRO B 1 37  ? 16.37900  7.65700   29.52100  1.000 14.47000 ? 39  PRO B C   1 
ATOM   2567 O O   . PRO B 1 37  ? 15.92500  7.65500   30.66700  1.000 13.55000 ? 39  PRO B O   1 
ATOM   2568 C CB  . PRO B 1 37  ? 14.45700  8.36900   28.03400  1.000 11.28000 ? 39  PRO B CB  1 
ATOM   2569 C CG  . PRO B 1 37  ? 13.22500  7.56500   27.52400  1.000 10.63000 ? 39  PRO B CG  1 
ATOM   2570 C CD  . PRO B 1 37  ? 13.24100  6.36100   28.41900  1.000 13.46000 ? 39  PRO B CD  1 
ATOM   2571 N N   . ARG B 1 38  ? 17.65300  7.95800   29.24500  1.000 11.50000 ? 40  ARG B N   1 
ATOM   2572 C CA  . ARG B 1 38  ? 18.58200  8.29100   30.32200  1.000 14.70000 ? 40  ARG B CA  1 
ATOM   2573 C C   . ARG B 1 38  ? 18.23300  9.59800   31.01300  1.000 16.84000 ? 40  ARG B C   1 
ATOM   2574 O O   . ARG B 1 38  ? 18.65200  9.79900   32.16200  1.000 21.19000 ? 40  ARG B O   1 
ATOM   2575 C CB  . ARG B 1 38  ? 20.01900  8.34900   29.79800  1.000 12.97000 ? 40  ARG B CB  1 
ATOM   2576 C CG  . ARG B 1 38  ? 20.34000  9.57200   28.96600  1.000 11.08000 ? 40  ARG B CG  1 
ATOM   2577 C CD  . ARG B 1 38  ? 21.77900  9.51000   28.45900  1.000 14.33000 ? 40  ARG B CD  1 
ATOM   2578 N NE  . ARG B 1 38  ? 22.08200  10.60800  27.53500  1.000 12.78000 ? 40  ARG B NE  1 
ATOM   2579 C CZ  . ARG B 1 38  ? 23.28400  10.83100  27.01000  1.000 16.55000 ? 40  ARG B CZ  1 
ATOM   2580 N NH1 . ARG B 1 38  ? 24.29600  10.02600  27.32700  1.000 14.93000 ? 40  ARG B NH1 1 
ATOM   2581 N NH2 . ARG B 1 38  ? 23.47500  11.85500  26.17500  1.000 11.88000 ? 40  ARG B NH2 1 
ATOM   2582 N N   . HIS B 1 39  ? 17.46900  10.48700  30.36300  1.000 15.57000 ? 41  HIS B N   1 
ATOM   2583 C CA  . HIS B 1 39  ? 17.14100  11.73900  31.02800  1.000 15.19000 ? 41  HIS B CA  1 
ATOM   2584 C C   . HIS B 1 39  ? 16.22100  11.55000  32.22700  1.000 20.05000 ? 41  HIS B C   1 
ATOM   2585 O O   . HIS B 1 39  ? 15.94200  12.53600  32.91400  1.000 21.78000 ? 41  HIS B O   1 
ATOM   2586 C CB  . HIS B 1 39  ? 16.56700  12.77500  30.03800  1.000 18.49000 ? 41  HIS B CB  1 
ATOM   2587 C CG  . HIS B 1 39  ? 15.20000  12.46200  29.49100  1.000 20.32000 ? 41  HIS B CG  1 
ATOM   2588 N ND1 . HIS B 1 39  ? 14.06700  12.43200  30.27300  1.000 16.88000 ? 41  HIS B ND1 1 
ATOM   2589 C CD2 . HIS B 1 39  ? 14.78100  12.25100  28.21800  1.000 16.21000 ? 41  HIS B CD2 1 
ATOM   2590 C CE1 . HIS B 1 39  ? 13.01400  12.17600  29.51600  1.000 19.64000 ? 41  HIS B CE1 1 
ATOM   2591 N NE2 . HIS B 1 39  ? 13.41900  12.06700  28.26200  1.000 18.56000 ? 41  HIS B NE2 1 
ATOM   2592 N N   . VAL B 1 40  ? 15.80000  10.31700  32.53300  1.000 16.32000 ? 42  VAL B N   1 
ATOM   2593 C CA  . VAL B 1 40  ? 15.09900  10.07100  33.79200  1.000 19.52000 ? 42  VAL B CA  1 
ATOM   2594 C C   . VAL B 1 40  ? 15.98000  10.42800  34.98700  1.000 27.54000 ? 42  VAL B C   1 
ATOM   2595 O O   . VAL B 1 40  ? 15.46600  10.79200  36.05300  1.000 23.67000 ? 42  VAL B O   1 
ATOM   2596 C CB  . VAL B 1 40  ? 14.62100  8.60600   33.87300  1.000 17.93000 ? 42  VAL B CB  1 
ATOM   2597 C CG1 . VAL B 1 40  ? 15.80200  7.64600   33.94700  1.000 17.41000 ? 42  VAL B CG1 1 
ATOM   2598 C CG2 . VAL B 1 40  ? 13.69300  8.40800   35.06000  1.000 21.37000 ? 42  VAL B CG2 1 
ATOM   2599 N N   . ILE B 1 41  ? 17.30900  10.33500  34.83900  1.000 23.43000 ? 43  ILE B N   1 
ATOM   2600 C CA  . ILE B 1 41  ? 18.21100  10.62100  35.95700  1.000 25.54000 ? 43  ILE B CA  1 
ATOM   2601 C C   . ILE B 1 41  ? 18.48100  12.10200  36.15100  1.000 30.50000 ? 43  ILE B C   1 
ATOM   2602 O O   . ILE B 1 41  ? 19.24700  12.46500  37.05400  1.000 31.72000 ? 43  ILE B O   1 
ATOM   2603 C CB  . ILE B 1 41  ? 19.58200  9.92900   35.80900  1.000 21.55000 ? 43  ILE B CB  1 
ATOM   2604 C CG1 . ILE B 1 41  ? 20.36800  10.52400  34.64000  1.000 19.29000 ? 43  ILE B CG1 1 
ATOM   2605 C CG2 . ILE B 1 41  ? 19.42500  8.44100   35.62400  1.000 21.26000 ? 43  ILE B CG2 1 
ATOM   2606 C CD1 . ILE B 1 41  ? 21.75100  9.96400   34.50800  1.000 21.33000 ? 43  ILE B CD1 1 
ATOM   2607 N N   . CYS B 1 42  ? 17.88900  12.97200  35.34000  1.000 28.48000 ? 44  CYS B N   1 
ATOM   2608 C CA  . CYS B 1 42  ? 18.09800  14.40600  35.48400  1.000 38.01000 ? 44  CYS B CA  1 
ATOM   2609 C C   . CYS B 1 42  ? 17.20500  14.98500  36.56800  1.000 39.97000 ? 44  CYS B C   1 
ATOM   2610 O O   . CYS B 1 42  ? 16.02700  14.63500  36.67100  1.000 35.90000 ? 44  CYS B O   1 
ATOM   2611 C CB  . CYS B 1 42  ? 17.79700  15.12600  34.17400  1.000 34.69000 ? 44  CYS B CB  1 
ATOM   2612 S SG  . CYS B 1 42  ? 18.89900  14.72400  32.85500  1.000 36.02000 ? 44  CYS B SG  1 
ATOM   2613 N N   . THR B 1 43  ? 17.76300  15.88300  37.37200  1.000 46.99000 ? 45  THR B N   1 
ATOM   2614 C CA  . THR B 1 43  ? 16.89100  16.77000  38.12400  1.000 51.66000 ? 45  THR B CA  1 
ATOM   2615 C C   . THR B 1 43  ? 16.52100  17.96100  37.24900  1.000 52.30000 ? 45  THR B C   1 
ATOM   2616 O O   . THR B 1 43  ? 17.14800  18.21300  36.21600  1.000 52.44000 ? 45  THR B O   1 
ATOM   2617 C CB  . THR B 1 43  ? 17.55800  17.26900  39.40400  1.000 47.42000 ? 45  THR B CB  1 
ATOM   2618 O OG1 . THR B 1 43  ? 18.29100  18.46600  39.11000  1.000 48.81000 ? 45  THR B OG1 1 
ATOM   2619 C CG2 . THR B 1 43  ? 18.50400  16.21200  39.96000  1.000 46.95000 ? 45  THR B CG2 1 
ATOM   2620 N N   . SER B 1 44  ? 15.49600  18.70300  37.68100  1.000 54.71000 ? 46  SER B N   1 
ATOM   2621 C CA  . SER B 1 44  ? 15.00600  19.83300  36.89400  1.000 56.64000 ? 46  SER B CA  1 
ATOM   2622 C C   . SER B 1 44  ? 16.13700  20.80200  36.55100  1.000 53.81000 ? 46  SER B C   1 
ATOM   2623 O O   . SER B 1 44  ? 16.21700  21.30400  35.42300  1.000 56.07000 ? 46  SER B O   1 
ATOM   2624 C CB  . SER B 1 44  ? 13.88900  20.55000  37.65900  1.000 58.25000 ? 46  SER B CB  1 
ATOM   2625 O OG  . SER B 1 44  ? 13.25000  21.53300  36.85700  1.000 57.13000 ? 46  SER B OG  1 
ATOM   2626 N N   . GLU B 1 45  ? 17.03900  21.05700  37.50700  1.000 52.28000 ? 47  GLU B N   1 
ATOM   2627 C CA  . GLU B 1 45  ? 18.20000  21.89800  37.23000  1.000 52.17000 ? 47  GLU B CA  1 
ATOM   2628 C C   . GLU B 1 45  ? 19.18300  21.20200  36.29500  1.000 52.25000 ? 47  GLU B C   1 
ATOM   2629 O O   . GLU B 1 45  ? 19.83400  21.86300  35.47800  1.000 56.22000 ? 47  GLU B O   1 
ATOM   2630 C CB  . GLU B 1 45  ? 18.87900  22.28700  38.54200  1.000 55.43000 ? 47  GLU B CB  1 
ATOM   2631 N N   . ASP B 1 46  ? 19.31200  19.87300  36.40500  1.000 56.67000 ? 48  ASP B N   1 
ATOM   2632 C CA  . ASP B 1 46  ? 20.21800  19.12900  35.52800  1.000 53.99000 ? 48  ASP B CA  1 
ATOM   2633 C C   . ASP B 1 46  ? 19.75500  19.18000  34.07700  1.000 46.12000 ? 48  ASP B C   1 
ATOM   2634 O O   . ASP B 1 46  ? 20.57100  19.38300  33.16900  1.000 39.75000 ? 48  ASP B O   1 
ATOM   2635 C CB  . ASP B 1 46  ? 20.33500  17.67200  35.98500  1.000 49.27000 ? 48  ASP B CB  1 
ATOM   2636 C CG  . ASP B 1 46  ? 21.00600  17.53400  37.34000  1.000 52.24000 ? 48  ASP B CG  1 
ATOM   2637 O OD1 . ASP B 1 46  ? 21.50800  18.55300  37.85800  1.000 53.27000 ? 48  ASP B OD1 1 
ATOM   2638 O OD2 . ASP B 1 46  ? 21.03300  16.40400  37.88400  1.000 49.69000 ? 48  ASP B OD2 1 
ATOM   2639 N N   . MET B 1 47  ? 18.44500  19.00600  33.84900  1.000 50.68000 ? 49  MET B N   1 
ATOM   2640 C CA  . MET B 1 47  ? 17.86900  19.01600  32.50700  1.000 43.44000 ? 49  MET B CA  1 
ATOM   2641 C C   . MET B 1 47  ? 18.38000  20.17100  31.65700  1.000 47.10000 ? 49  MET B C   1 
ATOM   2642 O O   . MET B 1 47  ? 18.41600  20.05500  30.42700  1.000 44.29000 ? 49  MET B O   1 
ATOM   2643 C CB  . MET B 1 47  ? 16.33200  19.06400  32.59200  1.000 46.71000 ? 49  MET B CB  1 
ATOM   2644 C CG  . MET B 1 47  ? 15.69200  18.01600  33.52700  1.000 43.62000 ? 49  MET B CG  1 
ATOM   2645 S SD  . MET B 1 47  ? 13.92700  17.73800  33.20200  1.000 60.08000 ? 49  MET B SD  1 
ATOM   2646 C CE  . MET B 1 47  ? 13.19900  17.74300  34.83300  1.000 51.73000 ? 49  MET B CE  1 
ATOM   2647 N N   . LEU B 1 48  ? 18.81500  21.26200  32.28700  1.000 50.96000 ? 50  LEU B N   1 
ATOM   2648 C CA  . LEU B 1 48  ? 19.28200  22.43400  31.55300  1.000 51.77000 ? 50  LEU B CA  1 
ATOM   2649 C C   . LEU B 1 48  ? 20.47600  22.08800  30.66300  1.000 43.81000 ? 50  LEU B C   1 
ATOM   2650 O O   . LEU B 1 48  ? 20.49500  22.41900  29.47400  1.000 44.60000 ? 50  LEU B O   1 
ATOM   2651 C CB  . LEU B 1 48  ? 19.62300  23.55300  32.54400  1.000 55.32000 ? 50  LEU B CB  1 
ATOM   2652 C CG  . LEU B 1 48  ? 18.44800  23.95200  33.45000  1.000 56.36000 ? 50  LEU B CG  1 
ATOM   2653 C CD1 . LEU B 1 48  ? 18.82200  25.08400  34.40300  1.000 54.03000 ? 50  LEU B CD1 1 
ATOM   2654 C CD2 . LEU B 1 48  ? 17.21000  24.31500  32.62400  1.000 56.93000 ? 50  LEU B CD2 1 
ATOM   2655 N N   . ASN B 1 49  ? 21.48800  21.42100  31.22100  1.000 45.77000 ? 51  ASN B N   1 
ATOM   2656 C CA  . ASN B 1 49  ? 22.57300  20.84900  30.42100  1.000 37.84000 ? 51  ASN B CA  1 
ATOM   2657 C C   . ASN B 1 49  ? 23.20900  19.72200  31.22600  1.000 41.74000 ? 51  ASN B C   1 
ATOM   2658 O O   . ASN B 1 49  ? 23.81200  19.97800  32.27700  1.000 43.29000 ? 51  ASN B O   1 
ATOM   2659 C CB  . ASN B 1 49  ? 23.61300  21.90700  30.03100  1.000 42.30000 ? 51  ASN B CB  1 
ATOM   2660 C CG  . ASN B 1 49  ? 24.93000  21.29600  29.58300  1.000 42.42000 ? 51  ASN B CG  1 
ATOM   2661 O OD1 . ASN B 1 49  ? 24.94500  20.21900  28.97200  1.000 46.68000 ? 51  ASN B OD1 1 
ATOM   2662 N ND2 . ASN B 1 49  ? 26.02400  21.97200  29.85200  1.000 45.73000 ? 51  ASN B ND2 1 
ATOM   2663 N N   . PRO B 1 50  ? 23.09300  18.46400  30.77200  1.000 35.79000 ? 52  PRO B N   1 
ATOM   2664 C CA  . PRO B 1 50  ? 23.47200  17.33100  31.62800  1.000 29.15000 ? 52  PRO B CA  1 
ATOM   2665 C C   . PRO B 1 50  ? 24.73600  16.58000  31.23400  1.000 27.93000 ? 52  PRO B C   1 
ATOM   2666 O O   . PRO B 1 50  ? 24.87500  16.11700  30.09500  1.000 26.29000 ? 52  PRO B O   1 
ATOM   2667 C CB  . PRO B 1 50  ? 22.24800  16.41000  31.52500  1.000 26.43000 ? 52  PRO B CB  1 
ATOM   2668 C CG  . PRO B 1 50  ? 21.60000  16.78200  30.16900  1.000 27.93000 ? 52  PRO B CG  1 
ATOM   2669 C CD  . PRO B 1 50  ? 22.25100  18.03500  29.64300  1.000 31.98000 ? 52  PRO B CD  1 
ATOM   2670 N N   . ASN B 1 51  ? 25.65100  16.40600  32.18900  1.000 23.29000 ? 53  ASN B N   1 
ATOM   2671 C CA  . ASN B 1 51  ? 26.80800  15.53300  31.98700  1.000 22.79000 ? 53  ASN B CA  1 
ATOM   2672 C C   . ASN B 1 51  ? 26.41900  14.14400  32.47700  1.000 26.68000 ? 53  ASN B C   1 
ATOM   2673 O O   . ASN B 1 51  ? 26.61600  13.78700  33.63900  1.000 28.27000 ? 53  ASN B O   1 
ATOM   2674 C CB  . ASN B 1 51  ? 28.04900  16.07100  32.69700  1.000 27.24000 ? 53  ASN B CB  1 
ATOM   2675 C CG  . ASN B 1 51  ? 29.31800  15.34200  32.27900  1.000 22.57000 ? 53  ASN B CG  1 
ATOM   2676 O OD1 . ASN B 1 51  ? 29.30800  14.13100  32.07200  1.000 33.04000 ? 53  ASN B OD1 1 
ATOM   2677 N ND2 . ASN B 1 51  ? 30.41000  16.08000  32.12600  1.000 30.13000 ? 53  ASN B ND2 1 
ATOM   2678 N N   . TYR B 1 52  ? 25.89600  13.33600  31.55300  1.000 24.54000 ? 54  TYR B N   1 
ATOM   2679 C CA  . TYR B 1 52  ? 25.18300  12.12200  31.92900  1.000 22.27000 ? 54  TYR B CA  1 
ATOM   2680 C C   . TYR B 1 52  ? 26.10200  11.07500  32.55000  1.000 21.32000 ? 54  TYR B C   1 
ATOM   2681 O O   . TYR B 1 52  ? 25.73800  10.44700  33.54700  1.000 25.57000 ? 54  TYR B O   1 
ATOM   2682 C CB  . TYR B 1 52  ? 24.47900  11.54400  30.71100  1.000 19.10000 ? 54  TYR B CB  1 
ATOM   2683 C CG  . TYR B 1 52  ? 23.19700  12.25000  30.36700  1.000 18.77000 ? 54  TYR B CG  1 
ATOM   2684 C CD1 . TYR B 1 52  ? 22.06200  12.10000  31.15600  1.000 15.14000 ? 54  TYR B CD1 1 
ATOM   2685 C CD2 . TYR B 1 52  ? 23.12100  13.07800  29.24900  1.000 16.84000 ? 54  TYR B CD2 1 
ATOM   2686 C CE1 . TYR B 1 52  ? 20.87900  12.74300  30.83700  1.000 19.35000 ? 54  TYR B CE1 1 
ATOM   2687 C CE2 . TYR B 1 52  ? 21.93400  13.69900  28.90800  1.000 15.06000 ? 54  TYR B CE2 1 
ATOM   2688 C CZ  . TYR B 1 52  ? 20.81600  13.53900  29.70800  1.000 17.29000 ? 54  TYR B CZ  1 
ATOM   2689 O OH  . TYR B 1 52  ? 19.63500  14.18400  29.37000  1.000 19.12000 ? 54  TYR B OH  1 
ATOM   2690 N N   . GLU B 1 53  ? 27.26500  10.81400  31.94500  1.000 22.02000 ? 55  GLU B N   1 
ATOM   2691 C CA  . GLU B 1 53  ? 28.16600  9.83500   32.55000  1.000 30.50000 ? 55  GLU B CA  1 
ATOM   2692 C C   . GLU B 1 53  ? 28.54600  10.24300  33.96400  1.000 26.80000 ? 55  GLU B C   1 
ATOM   2693 O O   . GLU B 1 53  ? 28.74400  9.38200   34.83000  1.000 30.23000 ? 55  GLU B O   1 
ATOM   2694 C CB  . GLU B 1 53  ? 29.42600  9.65100   31.70400  1.000 33.49000 ? 55  GLU B CB  1 
ATOM   2695 C CG  . GLU B 1 53  ? 29.18800  8.89700   30.40500  1.000 36.09000 ? 55  GLU B CG  1 
ATOM   2696 C CD  . GLU B 1 53  ? 30.28700  7.90300   30.08900  1.000 50.17000 ? 55  GLU B CD  1 
ATOM   2697 O OE1 . GLU B 1 53  ? 31.43300  8.34600   29.85100  1.000 55.88000 ? 55  GLU B OE1 1 
ATOM   2698 O OE2 . GLU B 1 53  ? 30.01200  6.68200   30.07600  1.000 63.27000 ? 55  GLU B OE2 1 
ATOM   2699 N N   . ASP B 1 54  ? 28.62600  11.55100  34.21400  1.000 29.02000 ? 56  ASP B N   1 
ATOM   2700 C CA  . ASP B 1 54  ? 28.90200  12.05500  35.55400  1.000 32.41000 ? 56  ASP B CA  1 
ATOM   2701 C C   . ASP B 1 54  ? 27.68500  11.90700  36.45800  1.000 34.85000 ? 56  ASP B C   1 
ATOM   2702 O O   . ASP B 1 54  ? 27.81900  11.50100  37.61900  1.000 28.89000 ? 56  ASP B O   1 
ATOM   2703 C CB  . ASP B 1 54  ? 29.34000  13.52100  35.47700  1.000 29.41000 ? 56  ASP B CB  1 
ATOM   2704 C CG  . ASP B 1 54  ? 30.13500  13.96700  36.70300  1.000 36.72000 ? 56  ASP B CG  1 
ATOM   2705 O OD1 . ASP B 1 54  ? 31.17800  13.34200  36.99800  1.000 30.70000 ? 56  ASP B OD1 1 
ATOM   2706 O OD2 . ASP B 1 54  ? 29.71500  14.94700  37.36200  1.000 36.38000 ? 56  ASP B OD2 1 
ATOM   2707 N N   . LEU B 1 55  ? 26.49100  12.23700  35.94900  1.000 26.11000 ? 57  LEU B N   1 
ATOM   2708 C CA  . LEU B 1 55  ? 25.28000  12.10000  36.75500  1.000 25.62000 ? 57  LEU B CA  1 
ATOM   2709 C C   . LEU B 1 55  ? 24.98100  10.64300  37.05500  1.000 24.36000 ? 57  LEU B C   1 
ATOM   2710 O O   . LEU B 1 55  ? 24.45500  10.33400  38.13000  1.000 28.15000 ? 57  LEU B O   1 
ATOM   2711 C CB  . LEU B 1 55  ? 24.07400  12.73200  36.04900  1.000 25.26000 ? 57  LEU B CB  1 
ATOM   2712 C CG  . LEU B 1 55  ? 24.06400  14.23200  35.76900  1.000 32.95000 ? 57  LEU B CG  1 
ATOM   2713 C CD1 . LEU B 1 55  ? 22.96500  14.58100  34.76800  1.000 31.15000 ? 57  LEU B CD1 1 
ATOM   2714 C CD2 . LEU B 1 55  ? 23.88500  15.02000  37.06700  1.000 40.30000 ? 57  LEU B CD2 1 
ATOM   2715 N N   . LEU B 1 56  ? 25.31900  9.74000   36.13000  1.000 22.07000 ? 58  LEU B N   1 
ATOM   2716 C CA  . LEU B 1 56  ? 24.99300  8.32800   36.30300  1.000 24.27000 ? 58  LEU B CA  1 
ATOM   2717 C C   . LEU B 1 56  ? 25.90400  7.65700   37.32400  1.000 26.85000 ? 58  LEU B C   1 
ATOM   2718 O O   . LEU B 1 56  ? 25.46100  6.77000   38.06400  1.000 23.00000 ? 58  LEU B O   1 
ATOM   2719 C CB  . LEU B 1 56  ? 25.08300  7.58200   34.97200  1.000 19.44000 ? 58  LEU B CB  1 
ATOM   2720 C CG  . LEU B 1 56  ? 24.68200  6.10900   35.08300  1.000 20.96000 ? 58  LEU B CG  1 
ATOM   2721 C CD1 . LEU B 1 56  ? 23.30000  5.99600   35.71800  1.000 25.96000 ? 58  LEU B CD1 1 
ATOM   2722 C CD2 . LEU B 1 56  ? 24.71800  5.37800   33.74000  1.000 26.64000 ? 58  LEU B CD2 1 
ATOM   2723 N N   . ILE B 1 57  ? 27.18600  8.03000   37.34800  1.000 25.88000 ? 59  ILE B N   1 
ATOM   2724 C CA  . ILE B 1 57  ? 28.11300  7.37300   38.27200  1.000 27.29000 ? 59  ILE B CA  1 
ATOM   2725 C C   . ILE B 1 57  ? 27.70200  7.62600   39.71500  1.000 25.25000 ? 59  ILE B C   1 
ATOM   2726 O O   . ILE B 1 57  ? 27.98000  6.80600   40.60300  1.000 31.31000 ? 59  ILE B O   1 
ATOM   2727 C CB  . ILE B 1 57  ? 29.56300  7.83500   38.00000  1.000 28.73000 ? 59  ILE B CB  1 
ATOM   2728 C CG1 . ILE B 1 57  ? 30.58200  6.90400   38.67600  1.000 29.03000 ? 59  ILE B CG1 1 
ATOM   2729 C CG2 . ILE B 1 57  ? 29.77000  9.25800   38.47000  1.000 26.36000 ? 59  ILE B CG2 1 
ATOM   2730 C CD1 . ILE B 1 57  ? 30.86800  5.63100   37.90600  1.000 36.07000 ? 59  ILE B CD1 1 
ATOM   2731 N N   . ARG B 1 58  ? 27.03400  8.75100   39.97100  1.000 24.17000 ? 60  ARG B N   1 
ATOM   2732 C CA  . ARG B 1 58  ? 26.57000  9.15600   41.28900  1.000 27.54000 ? 60  ARG B CA  1 
ATOM   2733 C C   . ARG B 1 58  ? 25.27500  8.47300   41.70600  1.000 31.41000 ? 60  ARG B C   1 
ATOM   2734 O O   . ARG B 1 58  ? 24.83500  8.66700   42.84500  1.000 29.04000 ? 60  ARG B O   1 
ATOM   2735 C CB  . ARG B 1 58  ? 26.38200  10.67700  41.32900  1.000 31.39000 ? 60  ARG B CB  1 
ATOM   2736 C CG  . ARG B 1 58  ? 27.59500  11.47300  40.81900  1.000 26.32000 ? 60  ARG B CG  1 
ATOM   2737 C CD  . ARG B 1 58  ? 27.32700  12.96300  40.80100  1.000 29.91000 ? 60  ARG B CD  1 
ATOM   2738 N NE  . ARG B 1 58  ? 28.42400  13.69900  40.18200  1.000 32.89000 ? 60  ARG B NE  1 
ATOM   2739 C CZ  . ARG B 1 58  ? 29.46900  14.18400  40.84300  1.000 36.30000 ? 60  ARG B CZ  1 
ATOM   2740 N NH1 . ARG B 1 58  ? 29.57100  13.99700  42.15800  1.000 34.09000 ? 60  ARG B NH1 1 
ATOM   2741 N NH2 . ARG B 1 58  ? 30.42000  14.84600  40.19000  1.000 31.99000 ? 60  ARG B NH2 1 
ATOM   2742 N N   . LYS B 1 59  ? 24.65000  7.70200   40.81700  1.000 27.05000 ? 61  LYS B N   1 
ATOM   2743 C CA  . LYS B 1 59  ? 23.40700  7.00700   41.11500  1.000 26.44000 ? 61  LYS B CA  1 
ATOM   2744 C C   . LYS B 1 59  ? 23.69800  5.60600   41.62600  1.000 26.71000 ? 61  LYS B C   1 
ATOM   2745 O O   . LYS B 1 59  ? 24.65500  4.95600   41.20000  1.000 28.78000 ? 61  LYS B O   1 
ATOM   2746 C CB  . LYS B 1 59  ? 22.51300  6.91600   39.86800  1.000 25.79000 ? 61  LYS B CB  1 
ATOM   2747 C CG  . LYS B 1 59  ? 21.77400  8.19300   39.52700  1.000 24.61000 ? 61  LYS B CG  1 
ATOM   2748 C CD  . LYS B 1 59  ? 20.76400  8.53200   40.60500  1.000 30.98000 ? 61  LYS B CD  1 
ATOM   2749 C CE  . LYS B 1 59  ? 20.22100  9.93100   40.42400  1.000 33.51000 ? 61  LYS B CE  1 
ATOM   2750 N NZ  . LYS B 1 59  ? 19.41700  10.02600  39.17100  1.000 37.43000 ? 61  LYS B NZ  1 
ATOM   2751 N N   . SER B 1 60  ? 22.84800  5.13900   42.53100  1.000 29.26000 ? 62  SER B N   1 
ATOM   2752 C CA  . SER B 1 60  ? 22.88500  3.76300   43.00000  1.000 31.06000 ? 62  SER B CA  1 
ATOM   2753 C C   . SER B 1 60  ? 21.74400  2.94400   42.39300  1.000 30.40000 ? 62  SER B C   1 
ATOM   2754 O O   . SER B 1 60  ? 20.74600  3.48200   41.90500  1.000 30.11000 ? 62  SER B O   1 
ATOM   2755 C CB  . SER B 1 60  ? 22.81100  3.71900   44.53000  1.000 36.16000 ? 62  SER B CB  1 
ATOM   2756 O OG  . SER B 1 60  ? 24.03600  4.15800   45.11200  1.000 38.31000 ? 62  SER B OG  1 
ATOM   2757 N N   . ASN B 1 61  ? 21.91400  1.62000   42.42900  1.000 31.87000 ? 63  ASN B N   1 
ATOM   2758 C CA  . ASN B 1 61  ? 20.85600  0.72100   41.98500  1.000 34.09000 ? 63  ASN B CA  1 
ATOM   2759 C C   . ASN B 1 61  ? 19.53600  1.04000   42.67100  1.000 36.25000 ? 63  ASN B C   1 
ATOM   2760 O O   . ASN B 1 61  ? 18.47600  1.02800   42.03400  1.000 32.50000 ? 63  ASN B O   1 
ATOM   2761 C CB  . ASN B 1 61  ? 21.26400  -0.73000  42.24200  1.000 30.78000 ? 63  ASN B CB  1 
ATOM   2762 C CG  . ASN B 1 61  ? 22.28400  -1.22300  41.24300  1.000 34.48000 ? 63  ASN B CG  1 
ATOM   2763 O OD1 . ASN B 1 61  ? 22.54800  -0.55500  40.24500  1.000 37.97000 ? 63  ASN B OD1 1 
ATOM   2764 N ND2 . ASN B 1 61  ? 22.85600  -2.39600  41.49300  1.000 31.45000 ? 63  ASN B ND2 1 
ATOM   2765 N N   . HIS B 1 62  ? 19.57900  1.36500   43.96400  1.000 33.86000 ? 64  HIS B N   1 
ATOM   2766 C CA  . HIS B 1 62  ? 18.34900  1.63300   44.69600  1.000 30.90000 ? 64  HIS B CA  1 
ATOM   2767 C C   . HIS B 1 62  ? 17.75500  2.99400   44.37700  1.000 31.17000 ? 64  HIS B C   1 
ATOM   2768 O O   . HIS B 1 62  ? 16.62500  3.27700   44.79800  1.000 28.21000 ? 64  HIS B O   1 
ATOM   2769 C CB  . HIS B 1 62  ? 18.59200  1.50500   46.20300  1.000 37.57000 ? 64  HIS B CB  1 
ATOM   2770 C CG  . HIS B 1 62  ? 19.50000  2.55400   46.76300  1.000 40.01000 ? 64  HIS B CG  1 
ATOM   2771 N ND1 . HIS B 1 62  ? 19.05200  3.80100   47.14400  1.000 44.79000 ? 64  HIS B ND1 1 
ATOM   2772 C CD2 . HIS B 1 62  ? 20.82900  2.53800   47.01600  1.000 39.65000 ? 64  HIS B CD2 1 
ATOM   2773 C CE1 . HIS B 1 62  ? 20.06700  4.50900   47.60700  1.000 41.08000 ? 64  HIS B CE1 1 
ATOM   2774 N NE2 . HIS B 1 62  ? 21.15800  3.76500   47.53900  1.000 42.06000 ? 64  HIS B NE2 1 
ATOM   2775 N N   . ASN B 1 63  ? 18.46900  3.83800   43.63400  1.000 29.47000 ? 65  ASN B N   1 
ATOM   2776 C CA  . ASN B 1 63  ? 17.88000  5.08900   43.18600  1.000 30.55000 ? 65  ASN B CA  1 
ATOM   2777 C C   . ASN B 1 63  ? 16.81400  4.87300   42.11500  1.000 28.30000 ? 65  ASN B C   1 
ATOM   2778 O O   . ASN B 1 63  ? 16.08700  5.81700   41.78900  1.000 28.48000 ? 65  ASN B O   1 
ATOM   2779 C CB  . ASN B 1 63  ? 18.97000  6.02800   42.64100  1.000 32.64000 ? 65  ASN B CB  1 
ATOM   2780 C CG  . ASN B 1 63  ? 19.85200  6.62400   43.73500  1.000 31.51000 ? 65  ASN B CG  1 
ATOM   2781 O OD1 . ASN B 1 63  ? 21.08100  6.48600   43.71000  1.000 31.34000 ? 65  ASN B OD1 1 
ATOM   2782 N ND2 . ASN B 1 63  ? 19.22800  7.30300   44.69000  1.000 30.84000 ? 65  ASN B ND2 1 
ATOM   2783 N N   . PHE B 1 64  ? 16.71100  3.67300   41.55400  1.000 26.98000 ? 66  PHE B N   1 
ATOM   2784 C CA  . PHE B 1 64  ? 15.80900  3.40700   40.43400  1.000 29.84000 ? 66  PHE B CA  1 
ATOM   2785 C C   . PHE B 1 64  ? 14.65100  2.54200   40.90600  1.000 24.69000 ? 66  PHE B C   1 
ATOM   2786 O O   . PHE B 1 64  ? 14.85000  1.38500   41.28600  1.000 32.81000 ? 66  PHE B O   1 
ATOM   2787 C CB  . PHE B 1 64  ? 16.53900  2.71900   39.28400  1.000 26.57000 ? 66  PHE B CB  1 
ATOM   2788 C CG  . PHE B 1 64  ? 17.62700  3.54900   38.68300  1.000 30.43000 ? 66  PHE B CG  1 
ATOM   2789 C CD1 . PHE B 1 64  ? 17.32500  4.56300   37.79200  1.000 27.10000 ? 66  PHE B CD1 1 
ATOM   2790 C CD2 . PHE B 1 64  ? 18.95400  3.32000   39.01700  1.000 30.47000 ? 66  PHE B CD2 1 
ATOM   2791 C CE1 . PHE B 1 64  ? 18.31800  5.32700   37.24200  1.000 27.80000 ? 66  PHE B CE1 1 
ATOM   2792 C CE2 . PHE B 1 64  ? 19.95900  4.08100   38.46700  1.000 28.21000 ? 66  PHE B CE2 1 
ATOM   2793 C CZ  . PHE B 1 64  ? 19.64100  5.08900   37.57600  1.000 31.56000 ? 66  PHE B CZ  1 
ATOM   2794 N N   . LEU B 1 65  ? 13.45300  3.10200   40.86900  1.000 26.40000 ? 67  LEU B N   1 
ATOM   2795 C CA  . LEU B 1 65  ? 12.22800  2.39400   41.21800  1.000 29.41000 ? 67  LEU B CA  1 
ATOM   2796 C C   . LEU B 1 65  ? 11.54200  1.94300   39.93300  1.000 28.08000 ? 67  LEU B C   1 
ATOM   2797 O O   . LEU B 1 65  ? 11.14900  2.78000   39.11300  1.000 24.61000 ? 67  LEU B O   1 
ATOM   2798 C CB  . LEU B 1 65  ? 11.31200  3.30000   42.03800  1.000 29.28000 ? 67  LEU B CB  1 
ATOM   2799 C CG  . LEU B 1 65  ? 9.91800   2.79400   42.40700  1.000 41.15000 ? 67  LEU B CG  1 
ATOM   2800 C CD1 . LEU B 1 65  ? 10.00100  1.48800   43.20000  1.000 38.59000 ? 67  LEU B CD1 1 
ATOM   2801 C CD2 . LEU B 1 65  ? 9.17600   3.86800   43.19700  1.000 40.29000 ? 67  LEU B CD2 1 
ATOM   2802 N N   . VAL B 1 66  ? 11.40200  0.63100   39.75900  1.000 26.29000 ? 68  VAL B N   1 
ATOM   2803 C CA  . VAL B 1 66  ? 10.82900  0.04000   38.55100  1.000 26.92000 ? 68  VAL B CA  1 
ATOM   2804 C C   . VAL B 1 66  ? 9.60800   -0.77600  38.95300  1.000 27.79000 ? 68  VAL B C   1 
ATOM   2805 O O   . VAL B 1 66  ? 9.71300   -1.69300  39.77600  1.000 27.46000 ? 68  VAL B O   1 
ATOM   2806 C CB  . VAL B 1 66  ? 11.85100  -0.83600  37.81000  1.000 23.55000 ? 68  VAL B CB  1 
ATOM   2807 C CG1 . VAL B 1 66  ? 11.20300  -1.52200  36.62000  1.000 26.10000 ? 68  VAL B CG1 1 
ATOM   2808 C CG2 . VAL B 1 66  ? 13.05300  0.00800   37.37400  1.000 23.90000 ? 68  VAL B CG2 1 
ATOM   2809 N N   . GLN B 1 67  ? 8.45500   -0.45100  38.36800  1.000 22.44000 ? 69  GLN B N   1 
ATOM   2810 C CA  . GLN B 1 67  ? 7.19800   -1.12400  38.67800  1.000 30.27000 ? 69  GLN B CA  1 
ATOM   2811 C C   . GLN B 1 67  ? 6.62500   -1.76100  37.41800  1.000 25.37000 ? 69  GLN B C   1 
ATOM   2812 O O   . GLN B 1 67  ? 6.50800   -1.10100  36.37700  1.000 21.26000 ? 69  GLN B O   1 
ATOM   2813 C CB  . GLN B 1 67  ? 6.16900   -0.15100  39.27800  1.000 26.31000 ? 69  GLN B CB  1 
ATOM   2814 C CG  . GLN B 1 67  ? 6.63200   0.61500   40.52900  1.000 36.51000 ? 69  GLN B CG  1 
ATOM   2815 C CD  . GLN B 1 67  ? 5.57400   1.60700   41.01400  1.000 46.08000 ? 69  GLN B CD  1 
ATOM   2816 O OE1 . GLN B 1 67  ? 4.38500   1.28400   41.06900  1.000 45.37000 ? 69  GLN B OE1 1 
ATOM   2817 N NE2 . GLN B 1 67  ? 5.99900   2.83300   41.32100  1.000 44.44000 ? 69  GLN B NE2 1 
ATOM   2818 N N   . ALA B 1 68  ? 6.27500   -3.04000  37.51700  1.000 27.02000 ? 70  ALA B N   1 
ATOM   2819 C CA  . ALA B 1 68  ? 5.54500   -3.76400  36.47900  1.000 25.89000 ? 70  ALA B CA  1 
ATOM   2820 C C   . ALA B 1 68  ? 4.17400   -4.10000  37.05100  1.000 35.38000 ? 70  ALA B C   1 
ATOM   2821 O O   . ALA B 1 68  ? 4.05400   -4.99400  37.89600  1.000 35.20000 ? 70  ALA B O   1 
ATOM   2822 C CB  . ALA B 1 68  ? 6.28600   -5.02700  36.05000  1.000 25.49000 ? 70  ALA B CB  1 
ATOM   2823 N N   . GLY B 1 69  ? 3.14900   -3.38300  36.60000  1.000 35.49000 ? 71  GLY B N   1 
ATOM   2824 C CA  . GLY B 1 69  ? 1.85100   -3.51400  37.23800  1.000 38.56000 ? 71  GLY B CA  1 
ATOM   2825 C C   . GLY B 1 69  ? 1.95100   -3.06600  38.68200  1.000 45.52000 ? 71  GLY B C   1 
ATOM   2826 O O   . GLY B 1 69  ? 2.40000   -1.95200  38.98100  1.000 43.78000 ? 71  GLY B O   1 
ATOM   2827 N N   . ASN B 1 70  ? 1.53600   -3.94100  39.59800  1.000 47.81000 ? 72  ASN B N   1 
ATOM   2828 C CA  . ASN B 1 70  ? 1.71400   -3.68900  41.02200  1.000 50.35000 ? 72  ASN B CA  1 
ATOM   2829 C C   . ASN B 1 70  ? 3.01900   -4.26200  41.55600  1.000 52.45000 ? 72  ASN B C   1 
ATOM   2830 O O   . ASN B 1 70  ? 3.39900   -3.95200  42.69100  1.000 53.39000 ? 72  ASN B O   1 
ATOM   2831 C CB  . ASN B 1 70  ? 0.53700   -4.26600  41.81900  1.000 45.52000 ? 72  ASN B CB  1 
ATOM   2832 N N   . VAL B 1 71  ? 3.71100   -5.07500  40.76700  1.000 43.78000 ? 73  VAL B N   1 
ATOM   2833 C CA  . VAL B 1 71  ? 4.95200   -5.70000  41.20400  1.000 38.57000 ? 73  VAL B CA  1 
ATOM   2834 C C   . VAL B 1 71  ? 6.09700   -4.70400  41.07200  1.000 40.75000 ? 73  VAL B C   1 
ATOM   2835 O O   . VAL B 1 71  ? 6.15800   -3.92300  40.11500  1.000 36.84000 ? 73  VAL B O   1 
ATOM   2836 C CB  . VAL B 1 71  ? 5.22000   -6.97600  40.38500  1.000 39.88000 ? 73  VAL B CB  1 
ATOM   2837 C CG1 . VAL B 1 71  ? 6.26200   -7.83900  41.07300  1.000 37.91000 ? 73  VAL B CG1 1 
ATOM   2838 C CG2 . VAL B 1 71  ? 3.91700   -7.74700  40.15600  1.000 39.89000 ? 73  VAL B CG2 1 
ATOM   2839 N N   . GLN B 1 72  ? 7.01200   -4.72500  42.03700  1.000 38.64000 ? 74  GLN B N   1 
ATOM   2840 C CA  . GLN B 1 72  ? 8.21000   -3.90000  42.00100  1.000 37.25000 ? 74  GLN B CA  1 
ATOM   2841 C C   . GLN B 1 72  ? 9.39400   -4.79000  41.64800  1.000 36.61000 ? 74  GLN B C   1 
ATOM   2842 O O   . GLN B 1 72  ? 9.55000   -5.87600  42.21500  1.000 37.69000 ? 74  GLN B O   1 
ATOM   2843 C CB  . GLN B 1 72  ? 8.42900   -3.19900  43.34200  1.000 39.77000 ? 74  GLN B CB  1 
ATOM   2844 C CG  . GLN B 1 72  ? 9.46200   -2.08500  43.30400  1.000 43.89000 ? 74  GLN B CG  1 
ATOM   2845 C CD  . GLN B 1 72  ? 10.10600  -1.81900  44.66300  1.000 51.29000 ? 74  GLN B CD  1 
ATOM   2846 O OE1 . GLN B 1 72  ? 9.45400   -1.32800  45.58400  1.000 57.65000 ? 74  GLN B OE1 1 
ATOM   2847 N NE2 . GLN B 1 72  ? 11.39500  -2.14100  44.78700  1.000 49.40000 ? 74  GLN B NE2 1 
ATOM   2848 N N   . LEU B 1 73  ? 10.21200  -4.34400  40.70100  1.000 32.23000 ? 75  LEU B N   1 
ATOM   2849 C CA  . LEU B 1 73  ? 11.36200  -5.10700  40.23200  1.000 34.86000 ? 75  LEU B CA  1 
ATOM   2850 C C   . LEU B 1 73  ? 12.63400  -4.52700  40.84200  1.000 34.55000 ? 75  LEU B C   1 
ATOM   2851 O O   . LEU B 1 73  ? 12.83800  -3.30900  40.81900  1.000 35.51000 ? 75  LEU B O   1 
ATOM   2852 C CB  . LEU B 1 73  ? 11.44400  -5.08800  38.69800  1.000 28.91000 ? 75  LEU B CB  1 
ATOM   2853 C CG  . LEU B 1 73  ? 10.17800  -5.47300  37.91500  1.000 31.92000 ? 75  LEU B CG  1 
ATOM   2854 C CD1 . LEU B 1 73  ? 10.36300  -5.32700  36.38700  1.000 20.90000 ? 75  LEU B CD1 1 
ATOM   2855 C CD2 . LEU B 1 73  ? 9.72600   -6.88900  38.27700  1.000 31.98000 ? 75  LEU B CD2 1 
ATOM   2856 N N   . ARG B 1 74  ? 13.48500  -5.39600  41.38100  1.000 36.10000 ? 76  ARG B N   1 
ATOM   2857 C CA  . ARG B 1 74  ? 14.72200  -4.95100  42.01100  1.000 33.39000 ? 76  ARG B CA  1 
ATOM   2858 C C   . ARG B 1 74  ? 15.79400  -4.73500  40.95100  1.000 25.25000 ? 76  ARG B C   1 
ATOM   2859 O O   . ARG B 1 74  ? 16.12600  -5.65600  40.19700  1.000 27.20000 ? 76  ARG B O   1 
ATOM   2860 C CB  . ARG B 1 74  ? 15.19800  -5.96500  43.05100  1.000 30.77000 ? 76  ARG B CB  1 
ATOM   2861 N N   . VAL B 1 75  ? 16.35700  -3.53200  40.91900  1.000 33.82000 ? 77  VAL B N   1 
ATOM   2862 C CA  . VAL B 1 75  ? 17.45300  -3.22100  40.00800  1.000 26.32000 ? 77  VAL B CA  1 
ATOM   2863 C C   . VAL B 1 75  ? 18.74800  -3.76600  40.59900  1.000 28.93000 ? 77  VAL B C   1 
ATOM   2864 O O   . VAL B 1 75  ? 19.17200  -3.34900  41.68200  1.000 29.64000 ? 77  VAL B O   1 
ATOM   2865 C CB  . VAL B 1 75  ? 17.55500  -1.71200  39.76100  1.000 32.80000 ? 77  VAL B CB  1 
ATOM   2866 C CG1 . VAL B 1 75  ? 18.77700  -1.39900  38.88300  1.000 27.92000 ? 77  VAL B CG1 1 
ATOM   2867 C CG2 . VAL B 1 75  ? 16.26400  -1.18400  39.14000  1.000 29.42000 ? 77  VAL B CG2 1 
ATOM   2868 N N   . ILE B 1 76  ? 19.38400  -4.68400  39.88000  1.000 25.61000 ? 78  ILE B N   1 
ATOM   2869 C CA  . ILE B 1 76  ? 20.64100  -5.29600  40.29200  1.000 32.18000 ? 78  ILE B CA  1 
ATOM   2870 C C   . ILE B 1 76  ? 21.80000  -4.85700  39.40600  1.000 34.93000 ? 78  ILE B C   1 
ATOM   2871 O O   . ILE B 1 76  ? 22.88700  -5.43500  39.48100  1.000 32.18000 ? 78  ILE B O   1 
ATOM   2872 C CB  . ILE B 1 76  ? 20.52800  -6.82700  40.31700  1.000 31.46000 ? 78  ILE B CB  1 
ATOM   2873 C CG1 . ILE B 1 76  ? 20.11300  -7.33700  38.93200  1.000 33.15000 ? 78  ILE B CG1 1 
ATOM   2874 C CG2 . ILE B 1 76  ? 19.53000  -7.25200  41.39300  1.000 28.65000 ? 78  ILE B CG2 1 
ATOM   2875 C CD1 . ILE B 1 76  ? 20.67000  -8.70500  38.57300  1.000 32.69000 ? 78  ILE B CD1 1 
ATOM   2876 N N   . GLY B 1 77  ? 21.59200  -3.84800  38.56300  1.000 31.54000 ? 79  GLY B N   1 
ATOM   2877 C CA  . GLY B 1 77  ? 22.62000  -3.37300  37.66100  1.000 29.37000 ? 79  GLY B CA  1 
ATOM   2878 C C   . GLY B 1 77  ? 22.10600  -2.22400  36.81500  1.000 32.94000 ? 79  GLY B C   1 
ATOM   2879 O O   . GLY B 1 77  ? 20.90500  -2.13900  36.53500  1.000 27.11000 ? 79  GLY B O   1 
ATOM   2880 N N   . HIS B 1 78  ? 22.99000  -1.31000  36.43100  1.000 32.36000 ? 80  HIS B N   1 
ATOM   2881 C CA  . HIS B 1 78  ? 22.59500  -0.24000  35.53000  1.000 30.63000 ? 80  HIS B CA  1 
ATOM   2882 C C   . HIS B 1 78  ? 23.79100  0.16800   34.69100  1.000 34.12000 ? 80  HIS B C   1 
ATOM   2883 O O   . HIS B 1 78  ? 24.92800  0.17900   35.16800  1.000 28.38000 ? 80  HIS B O   1 
ATOM   2884 C CB  . HIS B 1 78  ? 22.02400  0.96800   36.28200  1.000 32.03000 ? 80  HIS B CB  1 
ATOM   2885 C CG  . HIS B 1 78  ? 23.03100  1.71600   37.09500  1.000 37.14000 ? 80  HIS B CG  1 
ATOM   2886 N ND1 . HIS B 1 78  ? 23.32600  1.38800   38.40200  1.000 36.72000 ? 80  HIS B ND1 1 
ATOM   2887 C CD2 . HIS B 1 78  ? 23.79700  2.79200   36.79600  1.000 33.02000 ? 80  HIS B CD2 1 
ATOM   2888 C CE1 . HIS B 1 78  ? 24.23400  2.22500   38.86800  1.000 35.51000 ? 80  HIS B CE1 1 
ATOM   2889 N NE2 . HIS B 1 78  ? 24.53600  3.08800   37.91500  1.000 30.39000 ? 80  HIS B NE2 1 
ATOM   2890 N N   . SER B 1 79  ? 23.51800  0.47700   33.42900  1.000 27.14000 ? 81  SER B N   1 
ATOM   2891 C CA  . SER B 1 79  ? 24.52800  0.94300   32.50400  1.000 26.11000 ? 81  SER B CA  1 
ATOM   2892 C C   . SER B 1 79  ? 23.84300  1.83000   31.47700  1.000 29.12000 ? 81  SER B C   1 
ATOM   2893 O O   . SER B 1 79  ? 22.61500  1.83500   31.34100  1.000 20.98000 ? 81  SER B O   1 
ATOM   2894 C CB  . SER B 1 79  ? 25.26900  -0.21600  31.82800  1.000 26.39000 ? 81  SER B CB  1 
ATOM   2895 O OG  . SER B 1 79  ? 24.42500  -0.98900  30.99500  1.000 28.15000 ? 81  SER B OG  1 
ATOM   2896 N N   . MET B 1 80  ? 24.65700  2.58400   30.76200  1.000 21.55000 ? 82  MET B N   1 
ATOM   2897 C CA  . MET B 1 80  ? 24.17600  3.52600   29.77000  1.000 22.93000 ? 82  MET B CA  1 
ATOM   2898 C C   . MET B 1 80  ? 24.68900  3.09100   28.41100  1.000 23.70000 ? 82  MET B C   1 
ATOM   2899 O O   . MET B 1 80  ? 25.85900  2.71800   28.28000  1.000 21.23000 ? 82  MET B O   1 
ATOM   2900 C CB  . MET B 1 80  ? 24.65500  4.93100   30.11200  1.000 27.81000 ? 82  MET B CB  1 
ATOM   2901 C CG  . MET B 1 80  ? 23.93700  6.01300   29.38400  1.000 21.97000 ? 82  MET B CG  1 
ATOM   2902 S SD  . MET B 1 80  ? 24.29100  7.56600   30.19900  1.000 21.79000 ? 82  MET B SD  1 
ATOM   2903 C CE  . MET B 1 80  ? 26.07600  7.52300   30.27100  1.000 25.88000 ? 82  MET B CE  1 
ATOM   2904 N N   . GLN B 1 81  ? 23.80900  3.09600   27.41500  1.000 22.04000 ? 83  GLN B N   1 
ATOM   2905 C CA  . GLN B 1 81  ? 24.21300  2.93900   26.02300  1.000 20.25000 ? 83  GLN B CA  1 
ATOM   2906 C C   . GLN B 1 81  ? 23.67800  4.16200   25.28600  1.000 19.63000 ? 83  GLN B C   1 
ATOM   2907 O O   . GLN B 1 81  ? 22.47800  4.24900   24.98800  1.000 12.05000 ? 83  GLN B O   1 
ATOM   2908 C CB  . GLN B 1 81  ? 23.70300  1.64700   25.41100  1.000 19.09000 ? 83  GLN B CB  1 
ATOM   2909 C CG  . GLN B 1 81  ? 24.18700  1.43600   23.98300  1.000 22.15000 ? 83  GLN B CG  1 
ATOM   2910 C CD  . GLN B 1 81  ? 23.72900  0.11800   23.40600  1.000 25.16000 ? 83  GLN B CD  1 
ATOM   2911 O OE1 . GLN B 1 81  ? 23.01400  -0.63800  24.06400  1.000 29.46000 ? 83  GLN B OE1 1 
ATOM   2912 N NE2 . GLN B 1 81  ? 24.14300  -0.17500  22.17200  1.000 25.07000 ? 83  GLN B NE2 1 
ATOM   2913 N N   . ASN B 1 82  ? 24.57800  5.10300   25.01300  1.000 16.24000 ? 84  ASN B N   1 
ATOM   2914 C CA  . ASN B 1 82  ? 24.22400  6.37700   24.40600  1.000 16.18000 ? 84  ASN B CA  1 
ATOM   2915 C C   . ASN B 1 82  ? 23.11600  7.02800   25.22000  1.000 15.97000 ? 84  ASN B C   1 
ATOM   2916 O O   . ASN B 1 82  ? 23.29200  7.21500   26.42700  1.000 14.77000 ? 84  ASN B O   1 
ATOM   2917 C CB  . ASN B 1 82  ? 23.84900  6.16100   22.94600  1.000 14.29000 ? 84  ASN B CB  1 
ATOM   2918 C CG  . ASN B 1 82  ? 24.99800  5.57500   22.15200  1.000 20.43000 ? 84  ASN B CG  1 
ATOM   2919 O OD1 . ASN B 1 82  ? 26.10600  6.12000   22.17300  1.000 21.70000 ? 84  ASN B OD1 1 
ATOM   2920 N ND2 . ASN B 1 82  ? 24.75600  4.45400   21.46400  1.000 13.19000 ? 84  ASN B ND2 1 
ATOM   2921 N N   . CYS B 1 83  ? 21.97100  7.36300   24.60800  1.000 9.24000  ? 85  CYS B N   1 
ATOM   2922 C CA  . CYS B 1 83  ? 20.93500  8.07200   25.34900  1.000 9.08000  ? 85  CYS B CA  1 
ATOM   2923 C C   . CYS B 1 83  ? 19.93700  7.14700   26.02800  1.000 12.49000 ? 85  CYS B C   1 
ATOM   2924 O O   . CYS B 1 83  ? 18.91100  7.62100   26.52800  1.000 14.55000 ? 85  CYS B O   1 
ATOM   2925 C CB  . CYS B 1 83  ? 20.19600  9.05400   24.44000  1.000 12.74000 ? 85  CYS B CB  1 
ATOM   2926 S SG  . CYS B 1 83  ? 21.31000  10.24800  23.70800  1.000 13.16000 ? 85  CYS B SG  1 
ATOM   2927 N N   . VAL B 1 84  ? 20.22000  5.85400   26.09400  1.000 12.08000 ? 86  VAL B N   1 
ATOM   2928 C CA  . VAL B 1 84  ? 19.31600  4.89300   26.70200  1.000 12.13000 ? 86  VAL B CA  1 
ATOM   2929 C C   . VAL B 1 84  ? 19.97200  4.31100   27.94300  1.000 17.63000 ? 86  VAL B C   1 
ATOM   2930 O O   . VAL B 1 84  ? 21.14400  3.90400   27.91500  1.000 14.27000 ? 86  VAL B O   1 
ATOM   2931 C CB  . VAL B 1 84  ? 18.90300  3.80900   25.69700  1.000 14.26000 ? 86  VAL B CB  1 
ATOM   2932 C CG1 . VAL B 1 84  ? 18.44000  2.56200   26.39200  1.000 13.92000 ? 86  VAL B CG1 1 
ATOM   2933 C CG2 . VAL B 1 84  ? 17.77600  4.37000   24.82200  1.000 13.46000 ? 86  VAL B CG2 1 
ATOM   2934 N N   . LEU B 1 85  ? 19.22400  4.32500   29.03500  1.000 13.71000 ? 87  LEU B N   1 
ATOM   2935 C CA  . LEU B 1 85  ? 19.60800  3.67900   30.27900  1.000 16.44000 ? 87  LEU B CA  1 
ATOM   2936 C C   . LEU B 1 85  ? 19.15100  2.23000   30.24500  1.000 18.62000 ? 87  LEU B C   1 
ATOM   2937 O O   . LEU B 1 85  ? 18.02700  1.93700   29.81500  1.000 17.67000 ? 87  LEU B O   1 
ATOM   2938 C CB  . LEU B 1 85  ? 18.97500  4.42300   31.45400  1.000 18.82000 ? 87  LEU B CB  1 
ATOM   2939 C CG  . LEU B 1 85  ? 19.34100  4.08700   32.89900  1.000 26.86000 ? 87  LEU B CG  1 
ATOM   2940 C CD1 . LEU B 1 85  ? 20.82800  4.31400   33.17500  1.000 27.59000 ? 87  LEU B CD1 1 
ATOM   2941 C CD2 . LEU B 1 85  ? 18.47600  4.94500   33.81600  1.000 19.79000 ? 87  LEU B CD2 1 
ATOM   2942 N N   . LYS B 1 86  ? 20.03200  1.32200   30.66800  1.000 14.99000 ? 88  LYS B N   1 
ATOM   2943 C CA  . LYS B 1 86  ? 19.72800  -0.10200  30.73600  1.000 17.75000 ? 88  LYS B CA  1 
ATOM   2944 C C   . LYS B 1 86  ? 19.79600  -0.54100  32.19200  1.000 25.24000 ? 88  LYS B C   1 
ATOM   2945 O O   . LYS B 1 86  ? 20.88200  -0.57900  32.78600  1.000 23.04000 ? 88  LYS B O   1 
ATOM   2946 C CB  . LYS B 1 86  ? 20.68500  -0.90400  29.86300  1.000 17.98000 ? 88  LYS B CB  1 
ATOM   2947 C CG  . LYS B 1 86  ? 20.40600  -0.70500  28.39000  1.000 21.54000 ? 88  LYS B CG  1 
ATOM   2948 C CD  . LYS B 1 86  ? 21.64400  -0.76100  27.54200  1.000 24.42000 ? 88  LYS B CD  1 
ATOM   2949 C CE  . LYS B 1 86  ? 22.17800  -2.16900  27.40800  1.000 29.03000 ? 88  LYS B CE  1 
ATOM   2950 N NZ  . LYS B 1 86  ? 23.31900  -2.17700  26.44900  1.000 33.17000 ? 88  LYS B NZ  1 
ATOM   2951 N N   . LEU B 1 87  ? 18.63700  -0.85600  32.76600  1.000 23.68000 ? 89  LEU B N   1 
ATOM   2952 C CA  . LEU B 1 87  ? 18.53300  -1.28700  34.15500  1.000 22.71000 ? 89  LEU B CA  1 
ATOM   2953 C C   . LEU B 1 87  ? 18.41600  -2.80900  34.18200  1.000 28.11000 ? 89  LEU B C   1 
ATOM   2954 O O   . LEU B 1 87  ? 17.43300  -3.37700  33.69200  1.000 21.12000 ? 89  LEU B O   1 
ATOM   2955 C CB  . LEU B 1 87  ? 17.34400  -0.62200  34.84000  1.000 20.80000 ? 89  LEU B CB  1 
ATOM   2956 C CG  . LEU B 1 87  ? 17.30300  0.90500   34.82200  1.000 23.65000 ? 89  LEU B CG  1 
ATOM   2957 C CD1 . LEU B 1 87  ? 16.04600  1.44100   35.50300  1.000 20.66000 ? 89  LEU B CD1 1 
ATOM   2958 C CD2 . LEU B 1 87  ? 18.54100  1.49300   35.47700  1.000 26.05000 ? 89  LEU B CD2 1 
ATOM   2959 N N   . ARG B 1 88  ? 19.44000  -3.45700  34.74000  1.000 25.55000 ? 90  ARG B N   1 
ATOM   2960 C CA  . ARG B 1 88  ? 19.38200  -4.92800  34.91700  1.000 27.33000 ? 90  ARG B CA  1 
ATOM   2961 C C   . ARG B 1 88  ? 18.50900  -5.19100  36.13900  1.000 23.69000 ? 90  ARG B C   1 
ATOM   2962 O O   . ARG B 1 88  ? 18.73800  -4.54200  37.16700  1.000 28.02000 ? 90  ARG B O   1 
ATOM   2963 C CB  . ARG B 1 88  ? 20.78200  -5.51300  35.12000  1.000 30.00000 ? 90  ARG B CB  1 
ATOM   2964 C CG  . ARG B 1 88  ? 21.42400  -6.02700  33.84100  1.000 30.00000 ? 90  ARG B CG  1 
ATOM   2965 C CD  . ARG B 1 88  ? 21.47400  -7.54200  33.83200  1.000 30.00000 ? 90  ARG B CD  1 
ATOM   2966 N NE  . ARG B 1 88  ? 21.25300  -8.09000  32.50300  1.000 30.00000 ? 90  ARG B NE  1 
ATOM   2967 C CZ  . ARG B 1 88  ? 22.19700  -8.25000  31.58500  1.000 30.00000 ? 90  ARG B CZ  1 
ATOM   2968 N NH1 . ARG B 1 88  ? 23.44400  -7.89700  31.84800  1.000 30.00000 ? 90  ARG B NH1 1 
ATOM   2969 N NH2 . ARG B 1 88  ? 21.89100  -8.75900  30.40600  1.000 30.00000 ? 90  ARG B NH2 1 
ATOM   2970 N N   . VAL B 1 89  ? 17.53500  -6.08500  36.00900  1.000 28.02000 ? 91  VAL B N   1 
ATOM   2971 C CA  . VAL B 1 89  ? 16.62300  -6.38800  37.10300  1.000 28.76000 ? 91  VAL B CA  1 
ATOM   2972 C C   . VAL B 1 89  ? 16.76200  -7.86200  37.44800  1.000 25.52000 ? 91  VAL B C   1 
ATOM   2973 O O   . VAL B 1 89  ? 17.24000  -8.67300  36.65000  1.000 28.87000 ? 91  VAL B O   1 
ATOM   2974 C CB  . VAL B 1 89  ? 15.15300  -6.04200  36.77400  1.000 25.53000 ? 91  VAL B CB  1 
ATOM   2975 C CG1 . VAL B 1 89  ? 14.96900  -4.52500  36.67700  1.000 28.57000 ? 91  VAL B CG1 1 
ATOM   2976 C CG2 . VAL B 1 89  ? 14.71900  -6.72500  35.49200  1.000 20.40000 ? 91  VAL B CG2 1 
ATOM   2977 N N   . ASP B 1 90  ? 16.31200  -8.21000  38.64800  1.000 29.54000 ? 92  ASP B N   1 
ATOM   2978 C CA  . ASP B 1 90  ? 16.49200  -9.57800  39.11600  1.000 33.63000 ? 92  ASP B CA  1 
ATOM   2979 C C   . ASP B 1 90  ? 15.44200  -10.54500 38.57900  1.000 34.03000 ? 92  ASP B C   1 
ATOM   2980 O O   . ASP B 1 90  ? 15.52100  -11.73900 38.88400  1.000 34.50000 ? 92  ASP B O   1 
ATOM   2981 C CB  . ASP B 1 90  ? 16.51100  -9.61000  40.64900  1.000 36.41000 ? 92  ASP B CB  1 
ATOM   2982 C CG  . ASP B 1 90  ? 15.15800  -9.32000  41.26700  1.000 36.11000 ? 92  ASP B CG  1 
ATOM   2983 O OD1 . ASP B 1 90  ? 14.30000  -8.67900  40.61600  1.000 38.90000 ? 92  ASP B OD1 1 
ATOM   2984 O OD2 . ASP B 1 90  ? 14.95700  -9.73900  42.42600  1.000 45.00000 ? 92  ASP B OD2 1 
ATOM   2985 N N   . THR B 1 91  ? 14.47800  -10.07900 37.78100  1.000 31.05000 ? 93  THR B N   1 
ATOM   2986 C CA  . THR B 1 91  ? 13.46000  -10.94300 37.19400  1.000 30.45000 ? 93  THR B CA  1 
ATOM   2987 C C   . THR B 1 91  ? 13.45200  -10.77400 35.68200  1.000 30.75000 ? 93  THR B C   1 
ATOM   2988 O O   . THR B 1 91  ? 13.33600  -9.65100  35.18100  1.000 26.09000 ? 93  THR B O   1 
ATOM   2989 C CB  . THR B 1 91  ? 12.06200  -10.62600 37.74000  1.000 27.61000 ? 93  THR B CB  1 
ATOM   2990 O OG1 . THR B 1 91  ? 12.11200  -10.47300 39.16200  1.000 40.21000 ? 93  THR B OG1 1 
ATOM   2991 C CG2 . THR B 1 91  ? 11.09400  -11.74900 37.39300  1.000 34.70000 ? 93  THR B CG2 1 
ATOM   2992 N N   . ALA B 1 92  ? 13.56400  -11.88100 34.96000  1.000 24.88000 ? 94  ALA B N   1 
ATOM   2993 C CA  . ALA B 1 92  ? 13.34300  -11.84000 33.52200  1.000 30.36000 ? 94  ALA B CA  1 
ATOM   2994 C C   . ALA B 1 92  ? 11.85800  -11.65800 33.22600  1.000 25.34000 ? 94  ALA B C   1 
ATOM   2995 O O   . ALA B 1 92  ? 10.99900  -12.21200 33.91800  1.000 23.91000 ? 94  ALA B O   1 
ATOM   2996 C CB  . ALA B 1 92  ? 13.85500  -13.12000 32.86500  1.000 32.01000 ? 94  ALA B CB  1 
ATOM   2997 N N   . ASN B 1 93  ? 11.55200  -10.86900 32.19900  1.000 27.32000 ? 95  ASN B N   1 
ATOM   2998 C CA  . ASN B 1 93  ? 10.15500  -10.68800 31.79500  1.000 22.42000 ? 95  ASN B CA  1 
ATOM   2999 C C   . ASN B 1 93  ? 9.64300   -11.95300 31.12400  1.000 18.82000 ? 95  ASN B C   1 
ATOM   3000 O O   . ASN B 1 93  ? 10.09800  -12.28400 30.01800  1.000 22.86000 ? 95  ASN B O   1 
ATOM   3001 C CB  . ASN B 1 93  ? 10.00500  -9.49300  30.84700  1.000 20.89000 ? 95  ASN B CB  1 
ATOM   3002 C CG  . ASN B 1 93  ? 8.55300   -9.21800  30.48500  1.000 23.80000 ? 95  ASN B CG  1 
ATOM   3003 O OD1 . ASN B 1 93  ? 7.64300   -9.88000  30.98800  1.000 20.86000 ? 95  ASN B OD1 1 
ATOM   3004 N ND2 . ASN B 1 93  ? 8.32800   -8.23600  29.60000  1.000 17.14000 ? 95  ASN B ND2 1 
ATOM   3005 N N   . PRO B 1 94  ? 8.69900   -12.67900 31.72600  1.000 22.48000 ? 96  PRO B N   1 
ATOM   3006 C CA  . PRO B 1 94  ? 8.22300   -13.91200 31.08900  1.000 23.78000 ? 96  PRO B CA  1 
ATOM   3007 C C   . PRO B 1 94  ? 7.40600   -13.65800 29.84200  1.000 26.54000 ? 96  PRO B C   1 
ATOM   3008 O O   . PRO B 1 94  ? 7.23000   -14.58500 29.04200  1.000 29.18000 ? 96  PRO B O   1 
ATOM   3009 C CB  . PRO B 1 94  ? 7.38300   -14.57500 32.18400  1.000 27.25000 ? 96  PRO B CB  1 
ATOM   3010 C CG  . PRO B 1 94  ? 6.88700   -13.44900 32.99100  1.000 29.03000 ? 96  PRO B CG  1 
ATOM   3011 C CD  . PRO B 1 94  ? 7.95800   -12.37400 32.96100  1.000 25.61000 ? 96  PRO B CD  1 
ATOM   3012 N N   . LYS B 1 95  ? 6.90100   -12.43800 29.65100  1.000 23.56000 ? 97  LYS B N   1 
ATOM   3013 C CA  . LYS B 1 95  ? 6.17000   -12.07800 28.44400  1.000 24.43000 ? 97  LYS B CA  1 
ATOM   3014 C C   . LYS B 1 95  ? 7.06900   -11.51200 27.34100  1.000 25.74000 ? 97  LYS B C   1 
ATOM   3015 O O   . LYS B 1 95  ? 6.54400   -10.96400 26.36900  1.000 24.24000 ? 97  LYS B O   1 
ATOM   3016 C CB  . LYS B 1 95  ? 5.07200   -11.05900 28.77600  1.000 27.10000 ? 97  LYS B CB  1 
ATOM   3017 C CG  . LYS B 1 95  ? 4.02500   -11.55300 29.77200  1.000 27.17000 ? 97  LYS B CG  1 
ATOM   3018 C CD  . LYS B 1 95  ? 2.88600   -10.55200 29.90100  1.000 34.17000 ? 97  LYS B CD  1 
ATOM   3019 C CE  . LYS B 1 95  ? 2.07200   -10.77800 31.16700  1.000 44.26000 ? 97  LYS B CE  1 
ATOM   3020 N NZ  . LYS B 1 95  ? 1.27500   -9.56300  31.53400  1.000 42.88000 ? 97  LYS B NZ  1 
ATOM   3021 N N   . THR B 1 96  ? 8.39500   -11.62500 27.46900  1.000 22.82000 ? 98  THR B N   1 
ATOM   3022 C CA  . THR B 1 96  ? 9.31600   -11.13800 26.43800  1.000 21.84000 ? 98  THR B CA  1 
ATOM   3023 C C   . THR B 1 96  ? 9.03000   -11.80600 25.10200  1.000 22.16000 ? 98  THR B C   1 
ATOM   3024 O O   . THR B 1 96  ? 9.11000   -13.03900 25.01000  1.000 22.30000 ? 98  THR B O   1 
ATOM   3025 C CB  . THR B 1 96  ? 10.77100  -11.41100 26.79600  1.000 18.69000 ? 98  THR B CB  1 
ATOM   3026 O OG1 . THR B 1 96  ? 11.09100  -10.79600 28.04400  1.000 21.30000 ? 98  THR B OG1 1 
ATOM   3027 C CG2 . THR B 1 96  ? 11.68700  -10.84600 25.70600  1.000 21.02000 ? 98  THR B CG2 1 
ATOM   3028 N N   . PRO B 1 97  ? 8.74100   -11.05400 24.04800  1.000 18.70000 ? 99  PRO B N   1 
ATOM   3029 C CA  . PRO B 1 97  ? 8.56000   -11.66200 22.73000  1.000 19.66000 ? 99  PRO B CA  1 
ATOM   3030 C C   . PRO B 1 97  ? 9.90700   -11.89600 22.05600  1.000 19.55000 ? 99  PRO B C   1 
ATOM   3031 O O   . PRO B 1 97  ? 10.94800  -11.40800 22.49600  1.000 17.93000 ? 99  PRO B O   1 
ATOM   3032 C CB  . PRO B 1 97  ? 7.74100   -10.60600 21.98700  1.000 17.40000 ? 99  PRO B CB  1 
ATOM   3033 C CG  . PRO B 1 97  ? 8.26700   -9.31200  22.55100  1.000 19.32000 ? 99  PRO B CG  1 
ATOM   3034 C CD  . PRO B 1 97  ? 8.54000   -9.58900  24.00700  1.000 21.44000 ? 99  PRO B CD  1 
ATOM   3035 N N   . LYS B 1 98  ? 9.87300   -12.66700 20.97200  1.000 18.24000 ? 100 LYS B N   1 
ATOM   3036 C CA  . LYS B 1 98  ? 10.96700  -12.61000 20.01200  1.000 19.82000 ? 100 LYS B CA  1 
ATOM   3037 C C   . LYS B 1 98  ? 11.10100  -11.17300 19.52600  1.000 21.68000 ? 100 LYS B C   1 
ATOM   3038 O O   . LYS B 1 98  ? 10.10300  -10.54200 19.16300  1.000 19.19000 ? 100 LYS B O   1 
ATOM   3039 C CB  . LYS B 1 98  ? 10.70300  -13.54300 18.83500  1.000 19.74000 ? 100 LYS B CB  1 
ATOM   3040 N N   . TYR B 1 99  ? 12.32100  -10.63200 19.55900  1.000 21.66000 ? 101 TYR B N   1 
ATOM   3041 C CA  . TYR B 1 99  ? 12.45500  -9.22100  19.22200  1.000 19.29000 ? 101 TYR B CA  1 
ATOM   3042 C C   . TYR B 1 99  ? 13.80100  -8.94100  18.57400  1.000 21.73000 ? 101 TYR B C   1 
ATOM   3043 O O   . TYR B 1 99  ? 14.74200  -9.73700  18.66300  1.000 18.85000 ? 101 TYR B O   1 
ATOM   3044 C CB  . TYR B 1 99  ? 12.25800  -8.32500  20.45400  1.000 17.10000 ? 101 TYR B CB  1 
ATOM   3045 C CG  . TYR B 1 99  ? 13.44200  -8.31500  21.39200  1.000 19.31000 ? 101 TYR B CG  1 
ATOM   3046 C CD1 . TYR B 1 99  ? 13.57000  -9.28200  22.38200  1.000 17.16000 ? 101 TYR B CD1 1 
ATOM   3047 C CD2 . TYR B 1 99  ? 14.43600  -7.35100  21.28000  1.000 16.05000 ? 101 TYR B CD2 1 
ATOM   3048 C CE1 . TYR B 1 99  ? 14.65600  -9.29400  23.23800  1.000 23.12000 ? 101 TYR B CE1 1 
ATOM   3049 C CE2 . TYR B 1 99  ? 15.52900  -7.35500  22.13200  1.000 21.48000 ? 101 TYR B CE2 1 
ATOM   3050 C CZ  . TYR B 1 99  ? 15.63100  -8.33000  23.11000  1.000 23.25000 ? 101 TYR B CZ  1 
ATOM   3051 O OH  . TYR B 1 99  ? 16.70900  -8.33900  23.96100  1.000 27.49000 ? 101 TYR B OH  1 
ATOM   3052 N N   . LYS B 1 100 ? 13.87200  -7.78000  17.91600  1.000 16.59000 ? 102 LYS B N   1 
ATOM   3053 C CA  . LYS B 1 100 ? 15.10600  -7.24300  17.36400  1.000 17.92000 ? 102 LYS B CA  1 
ATOM   3054 C C   . LYS B 1 100 ? 15.09800  -5.73900  17.58900  1.000 18.94000 ? 102 LYS B C   1 
ATOM   3055 O O   . LYS B 1 100 ? 14.03600  -5.12700  17.67200  1.000 16.50000 ? 102 LYS B O   1 
ATOM   3056 C CB  . LYS B 1 100 ? 15.24500  -7.54600  15.85700  1.000 16.56000 ? 102 LYS B CB  1 
ATOM   3057 N N   . PHE B 1 101 ? 16.28600  -5.15300  17.71900  1.000 14.37000 ? 103 PHE B N   1 
ATOM   3058 C CA  . PHE B 1 101 ? 16.44500  -3.70500  17.71000  1.000 15.31000 ? 103 PHE B CA  1 
ATOM   3059 C C   . PHE B 1 101 ? 16.89000  -3.31300  16.30600  1.000 19.06000 ? 103 PHE B C   1 
ATOM   3060 O O   . PHE B 1 101 ? 17.90800  -3.81400  15.81800  1.000 18.47000 ? 103 PHE B O   1 
ATOM   3061 C CB  . PHE B 1 101 ? 17.47000  -3.24000  18.75200  1.000 15.62000 ? 103 PHE B CB  1 
ATOM   3062 C CG  . PHE B 1 101 ? 17.01800  -3.38100  20.19200  1.000 14.76000 ? 103 PHE B CG  1 
ATOM   3063 C CD1 . PHE B 1 101 ? 15.70000  -3.70100  20.51100  1.000 13.50000 ? 103 PHE B CD1 1 
ATOM   3064 C CD2 . PHE B 1 101 ? 17.92800  -3.18900  21.23300  1.000 18.27000 ? 103 PHE B CD2 1 
ATOM   3065 C CE1 . PHE B 1 101 ? 15.28500  -3.81400  21.83000  1.000 15.33000 ? 103 PHE B CE1 1 
ATOM   3066 C CE2 . PHE B 1 101 ? 17.52800  -3.30300  22.56500  1.000 18.97000 ? 103 PHE B CE2 1 
ATOM   3067 C CZ  . PHE B 1 101 ? 16.19700  -3.62100  22.86900  1.000 15.58000 ? 103 PHE B CZ  1 
ATOM   3068 N N   . VAL B 1 102 ? 16.12500  -2.44600  15.64400  1.000 15.71000 ? 104 VAL B N   1 
ATOM   3069 C CA  . VAL B 1 102 ? 16.47700  -1.99100  14.30200  1.000 17.41000 ? 104 VAL B CA  1 
ATOM   3070 C C   . VAL B 1 102 ? 16.47100  -0.46600  14.27500  1.000 15.66000 ? 104 VAL B C   1 
ATOM   3071 O O   . VAL B 1 102 ? 15.77500  0.19200   15.05400  1.000 15.83000 ? 104 VAL B O   1 
ATOM   3072 C CB  . VAL B 1 102 ? 15.54200  -2.57400  13.20300  1.000 18.17000 ? 104 VAL B CB  1 
ATOM   3073 C CG1 . VAL B 1 102 ? 15.48600  -4.09800  13.28800  1.000 21.52000 ? 104 VAL B CG1 1 
ATOM   3074 C CG2 . VAL B 1 102 ? 14.14800  -2.00700  13.29800  1.000 16.50000 ? 104 VAL B CG2 1 
ATOM   3075 N N   . ARG B 1 103 ? 17.28900  0.10200   13.40300  1.000 13.91000 ? 105 ARG B N   1 
ATOM   3076 C CA  . ARG B 1 103 ? 17.27400  1.53800   13.16400  1.000 15.66000 ? 105 ARG B CA  1 
ATOM   3077 C C   . ARG B 1 103 ? 16.58400  1.78100   11.82600  1.000 17.28000 ? 105 ARG B C   1 
ATOM   3078 O O   . ARG B 1 103 ? 17.04800  1.29200   10.79200  1.000 20.11000 ? 105 ARG B O   1 
ATOM   3079 C CB  . ARG B 1 103 ? 18.69100  2.11200   13.16600  1.000 14.73000 ? 105 ARG B CB  1 
ATOM   3080 C CG  . ARG B 1 103 ? 18.70700  3.64100   12.97300  1.000 16.51000 ? 105 ARG B CG  1 
ATOM   3081 C CD  . ARG B 1 103 ? 20.04000  4.28300   13.30500  1.000 18.69000 ? 105 ARG B CD  1 
ATOM   3082 N NE  . ARG B 1 103 ? 20.00200  5.73200   13.08500  1.000 19.83000 ? 105 ARG B NE  1 
ATOM   3083 C CZ  . ARG B 1 103 ? 19.78900  6.63400   14.03800  1.000 17.19000 ? 105 ARG B CZ  1 
ATOM   3084 N NH1 . ARG B 1 103 ? 19.60100  6.25000   15.30000  1.000 15.54000 ? 105 ARG B NH1 1 
ATOM   3085 N NH2 . ARG B 1 103 ? 19.77600  7.92400   13.73500  1.000 14.80000 ? 105 ARG B NH2 1 
ATOM   3086 N N   . ILE B 1 104 ? 15.47400  2.51000   11.83200  1.000 16.62000 ? 106 ILE B N   1 
ATOM   3087 C CA  . ILE B 1 104 ? 14.71900  2.65400   10.59200  1.000 19.48000 ? 106 ILE B CA  1 
ATOM   3088 C C   . ILE B 1 104 ? 15.24100  3.84300   9.79700   1.000 18.89000 ? 106 ILE B C   1 
ATOM   3089 O O   . ILE B 1 104 ? 15.92500  4.72200   10.31300  1.000 16.20000 ? 106 ILE B O   1 
ATOM   3090 C CB  . ILE B 1 104 ? 13.20500  2.78500   10.82300  1.000 20.20000 ? 106 ILE B CB  1 
ATOM   3091 C CG1 . ILE B 1 104 ? 12.90300  3.98500   11.71900  1.000 17.65000 ? 106 ILE B CG1 1 
ATOM   3092 C CG2 . ILE B 1 104 ? 12.61800  1.47200   11.31500  1.000 28.59000 ? 106 ILE B CG2 1 
ATOM   3093 C CD1 . ILE B 1 104 ? 11.51500  4.52300   11.50600  1.000 24.37000 ? 106 ILE B CD1 1 
ATOM   3094 N N   . GLN B 1 105 ? 14.90800  3.85700   8.47900   1.000 19.61000 ? 107 GLN B N   1 
ATOM   3095 C CA  . GLN B 1 105 ? 15.20800  4.87200   7.48400   1.000 21.29000 ? 107 GLN B CA  1 
ATOM   3096 C C   . GLN B 1 105 ? 14.09800  5.91100   7.43100   1.000 21.40000 ? 107 GLN B C   1 
ATOM   3097 O O   . GLN B 1 105 ? 12.92700  5.58400   7.66300   1.000 16.78000 ? 107 GLN B O   1 
ATOM   3098 C CB  . GLN B 1 105 ? 15.34400  4.23500   6.10400   1.000 27.14000 ? 107 GLN B CB  1 
ATOM   3099 C CG  . GLN B 1 105 ? 16.20300  3.00600   6.08100   1.000 28.84000 ? 107 GLN B CG  1 
ATOM   3100 C CD  . GLN B 1 105 ? 17.65700  3.36600   6.14100   1.000 34.88000 ? 107 GLN B CD  1 
ATOM   3101 O OE1 . GLN B 1 105 ? 18.13800  4.17100   5.34500   1.000 39.77000 ? 107 GLN B OE1 1 
ATOM   3102 N NE2 . GLN B 1 105 ? 18.37200  2.78800   7.09900   1.000 41.13000 ? 107 GLN B NE2 1 
ATOM   3103 N N   . PRO B 1 106 ? 14.42500  7.16000   7.09400   1.000 20.57000 ? 108 PRO B N   1 
ATOM   3104 C CA  . PRO B 1 106 ? 13.36800  8.13900   6.83400   1.000 20.56000 ? 108 PRO B CA  1 
ATOM   3105 C C   . PRO B 1 106 ? 12.41800  7.57700   5.78600   1.000 21.54000 ? 108 PRO B C   1 
ATOM   3106 O O   . PRO B 1 106 ? 12.83400  6.87400   4.86400   1.000 22.59000 ? 108 PRO B O   1 
ATOM   3107 C CB  . PRO B 1 106 ? 14.12900  9.36700   6.31500   1.000 20.58000 ? 108 PRO B CB  1 
ATOM   3108 C CG  . PRO B 1 106 ? 15.52700  9.15600   6.72100   1.000 27.41000 ? 108 PRO B CG  1 
ATOM   3109 C CD  . PRO B 1 106 ? 15.75200  7.68300   6.72900   1.000 22.15000 ? 108 PRO B CD  1 
ATOM   3110 N N   . GLY B 1 107 ? 11.12700  7.83600   5.96700   1.000 19.28000 ? 109 GLY B N   1 
ATOM   3111 C CA  . GLY B 1 107 ? 10.11200  7.31500   5.09000   1.000 16.61000 ? 109 GLY B CA  1 
ATOM   3112 C C   . GLY B 1 107 ? 9.44000   6.04200   5.56800   1.000 22.61000 ? 109 GLY B C   1 
ATOM   3113 O O   . GLY B 1 107 ? 8.29500   5.78600   5.18900   1.000 23.82000 ? 109 GLY B O   1 
ATOM   3114 N N   . GLN B 1 108 ? 10.12900  5.23000   6.36400   1.000 20.70000 ? 110 GLN B N   1 
ATOM   3115 C CA  . GLN B 1 108 ? 9.56800   3.99100   6.88100   1.000 18.49000 ? 110 GLN B CA  1 
ATOM   3116 C C   . GLN B 1 108 ? 8.57300   4.29300   8.00500   1.000 16.09000 ? 110 GLN B C   1 
ATOM   3117 O O   . GLN B 1 108 ? 8.67800   5.30300   8.70300   1.000 12.27000 ? 110 GLN B O   1 
ATOM   3118 C CB  . GLN B 1 108 ? 10.68900  3.09100   7.40500   1.000 20.05000 ? 110 GLN B CB  1 
ATOM   3119 C CG  . GLN B 1 108 ? 11.87600  3.00500   6.44000   1.000 31.33000 ? 110 GLN B CG  1 
ATOM   3120 C CD  . GLN B 1 108 ? 12.64600  1.69500   6.53100   1.000 36.76000 ? 110 GLN B CD  1 
ATOM   3121 O OE1 . GLN B 1 108 ? 13.32200  1.42300   7.54000   1.000 27.71000 ? 110 GLN B OE1 1 
ATOM   3122 N NE2 . GLN B 1 108 ? 12.59500  0.90000   5.46400   1.000 41.41000 ? 110 GLN B NE2 1 
ATOM   3123 N N   . THR B 1 109 ? 7.59100   3.41400   8.16700   1.000 16.34000 ? 111 THR B N   1 
ATOM   3124 C CA  . THR B 1 109 ? 6.56000   3.58400   9.17800   1.000 14.00000 ? 111 THR B CA  1 
ATOM   3125 C C   . THR B 1 109 ? 6.73400   2.57300   10.30900  1.000 13.51000 ? 111 THR B C   1 
ATOM   3126 O O   . THR B 1 109 ? 7.40400   1.54300   10.17300  1.000 13.99000 ? 111 THR B O   1 
ATOM   3127 C CB  . THR B 1 109 ? 5.16300   3.44000   8.56900   1.000 16.66000 ? 111 THR B CB  1 
ATOM   3128 O OG1 . THR B 1 109 ? 5.07300   2.18000   7.90700   1.000 16.56000 ? 111 THR B OG1 1 
ATOM   3129 C CG2 . THR B 1 109 ? 4.91600   4.57200   7.56300   1.000 19.33000 ? 111 THR B CG2 1 
ATOM   3130 N N   . PHE B 1 110 ? 6.09400   2.87700   11.42800  1.000 10.93000 ? 112 PHE B N   1 
ATOM   3131 C CA  . PHE B 1 110 ? 6.10600   1.97500   12.56600  1.000 12.12000 ? 112 PHE B CA  1 
ATOM   3132 C C   . PHE B 1 110 ? 4.89300   2.30600   13.41000  1.000 15.90000 ? 112 PHE B C   1 
ATOM   3133 O O   . PHE B 1 110 ? 4.28800   3.37200   13.26200  1.000 12.96000 ? 112 PHE B O   1 
ATOM   3134 C CB  . PHE B 1 110 ? 7.39900   2.09700   13.37800  1.000 9.46000  ? 112 PHE B CB  1 
ATOM   3135 C CG  . PHE B 1 110 ? 7.71900   3.50000   13.83000  1.000 12.45000 ? 112 PHE B CG  1 
ATOM   3136 C CD1 . PHE B 1 110 ? 8.40800   4.37600   13.00600  1.000 14.40000 ? 112 PHE B CD1 1 
ATOM   3137 C CD2 . PHE B 1 110 ? 7.35600   3.92900   15.08900  1.000 11.17000 ? 112 PHE B CD2 1 
ATOM   3138 C CE1 . PHE B 1 110 ? 8.72700   5.66800   13.44000  1.000 19.15000 ? 112 PHE B CE1 1 
ATOM   3139 C CE2 . PHE B 1 110 ? 7.67300   5.22500   15.53800  1.000 15.81000 ? 112 PHE B CE2 1 
ATOM   3140 C CZ  . PHE B 1 110 ? 8.35600   6.09100   14.70800  1.000 17.18000 ? 112 PHE B CZ  1 
ATOM   3141 N N   . SER B 1 111 ? 4.53600   1.37800   14.28800  1.000 9.30000  ? 113 SER B N   1 
ATOM   3142 C CA  . SER B 1 111 ? 3.44400   1.61500   15.22100  1.000 9.35000  ? 113 SER B CA  1 
ATOM   3143 C C   . SER B 1 111 ? 4.01100   2.12300   16.53500  1.000 11.37000 ? 113 SER B C   1 
ATOM   3144 O O   . SER B 1 111 ? 5.03200   1.62700   17.01400  1.000 10.94000 ? 113 SER B O   1 
ATOM   3145 C CB  . SER B 1 111 ? 2.64100   0.33600   15.46700  1.000 10.36000 ? 113 SER B CB  1 
ATOM   3146 O OG  . SER B 1 111 ? 2.10900   -0.15300  14.24800  1.000 11.86000 ? 113 SER B OG  1 
ATOM   3147 N N   . VAL B 1 112 ? 3.32600   3.09100   17.12700  1.000 9.59000  ? 114 VAL B N   1 
ATOM   3148 C CA  . VAL B 1 112 ? 3.69300   3.63800   18.42200  1.000 8.70000  ? 114 VAL B CA  1 
ATOM   3149 C C   . VAL B 1 112 ? 2.68600   3.15300   19.44600  1.000 10.09000 ? 114 VAL B C   1 
ATOM   3150 O O   . VAL B 1 112 ? 1.47300   3.23000   19.21500  1.000 10.46000 ? 114 VAL B O   1 
ATOM   3151 C CB  . VAL B 1 112 ? 3.73400   5.17300   18.37800  1.000 14.06000 ? 114 VAL B CB  1 
ATOM   3152 C CG1 . VAL B 1 112 ? 3.87200   5.72700   19.79100  1.000 9.93000  ? 114 VAL B CG1 1 
ATOM   3153 C CG2 . VAL B 1 112 ? 4.87200   5.59900   17.48500  1.000 11.18000 ? 114 VAL B CG2 1 
ATOM   3154 N N   . LEU B 1 113 ? 3.17900   2.61200   20.55700  1.000 8.75000  ? 115 LEU B N   1 
ATOM   3155 C CA  . LEU B 1 113 ? 2.33800   2.33700   21.71700  1.000 9.23000  ? 115 LEU B CA  1 
ATOM   3156 C C   . LEU B 1 113 ? 2.61300   3.45300   22.71800  1.000 10.42000 ? 115 LEU B C   1 
ATOM   3157 O O   . LEU B 1 113 ? 3.63400   3.43900   23.41400  1.000 10.63000 ? 115 LEU B O   1 
ATOM   3158 C CB  . LEU B 1 113 ? 2.64100   0.96800   22.31800  1.000 10.09000 ? 115 LEU B CB  1 
ATOM   3159 C CG  . LEU B 1 113 ? 1.80000   0.61800   23.54100  1.000 11.23000 ? 115 LEU B CG  1 
ATOM   3160 C CD1 . LEU B 1 113 ? 0.32500   0.52100   23.15400  1.000 12.59000 ? 115 LEU B CD1 1 
ATOM   3161 C CD2 . LEU B 1 113 ? 2.27400   -0.68600  24.16400  1.000 12.20000 ? 115 LEU B CD2 1 
ATOM   3162 N N   . ALA B 1 114 ? 1.71700   4.43500   22.77300  1.000 10.57000 ? 116 ALA B N   1 
ATOM   3163 C CA  . ALA B 1 114 ? 1.85800   5.52200   23.73100  1.000 15.05000 ? 116 ALA B CA  1 
ATOM   3164 C C   . ALA B 1 114 ? 1.45200   5.01900   25.10900  1.000 15.69000 ? 116 ALA B C   1 
ATOM   3165 O O   . ALA B 1 114 ? 0.38000   4.42300   25.27000  1.000 13.26000 ? 116 ALA B O   1 
ATOM   3166 C CB  . ALA B 1 114 ? 1.01000   6.73400   23.31800  1.000 14.21000 ? 116 ALA B CB  1 
ATOM   3167 N N   . CYS B 1 115 ? 2.33500   5.21500   26.09000  1.000 10.71000 ? 117 CYS B N   1 
ATOM   3168 C CA  . CYS B 1 115 ? 2.14400   4.73600   27.45000  1.000 12.63000 ? 117 CYS B CA  1 
ATOM   3169 C C   . CYS B 1 115 ? 2.37200   5.87200   28.43500  1.000 15.52000 ? 117 CYS B C   1 
ATOM   3170 O O   . CYS B 1 115 ? 3.14600   6.79500   28.17000  1.000 13.04000 ? 117 CYS B O   1 
ATOM   3171 C CB  . CYS B 1 115 ? 3.12200   3.60200   27.82800  1.000 14.57000 ? 117 CYS B CB  1 
ATOM   3172 S SG  . CYS B 1 115 ? 3.01600   2.11200   26.82500  1.000 17.05000 ? 117 CYS B SG  1 
ATOM   3173 N N   . TYR B 1 116 ? 1.71600   5.76400   29.58600  1.000 16.60000 ? 118 TYR B N   1 
ATOM   3174 C CA  . TYR B 1 116 ? 1.87100   6.70100   30.69200  1.000 17.01000 ? 118 TYR B CA  1 
ATOM   3175 C C   . TYR B 1 116 ? 1.92200   5.89200   31.97500  1.000 18.38000 ? 118 TYR B C   1 
ATOM   3176 O O   . TYR B 1 116 ? 1.09300   5.00100   32.17400  1.000 17.20000 ? 118 TYR B O   1 
ATOM   3177 C CB  . TYR B 1 116 ? 0.73100   7.73400   30.71100  1.000 17.19000 ? 118 TYR B CB  1 
ATOM   3178 C CG  . TYR B 1 116 ? 0.73500   8.52900   29.43700  1.000 19.03000 ? 118 TYR B CG  1 
ATOM   3179 C CD1 . TYR B 1 116 ? 1.53200   9.66100   29.30300  1.000 16.89000 ? 118 TYR B CD1 1 
ATOM   3180 C CD2 . TYR B 1 116 ? 0.00600   8.10400   28.33400  1.000 21.50000 ? 118 TYR B CD2 1 
ATOM   3181 C CE1 . TYR B 1 116 ? 1.57100   10.37200  28.12000  1.000 19.08000 ? 118 TYR B CE1 1 
ATOM   3182 C CE2 . TYR B 1 116 ? 0.03900   8.79900   27.14100  1.000 18.95000 ? 118 TYR B CE2 1 
ATOM   3183 C CZ  . TYR B 1 116 ? 0.82400   9.93300   27.03700  1.000 17.73000 ? 118 TYR B CZ  1 
ATOM   3184 O OH  . TYR B 1 116 ? 0.85300   10.60900  25.84600  1.000 18.23000 ? 118 TYR B OH  1 
ATOM   3185 N N   . ASN B 1 117 ? 2.93500   6.16600   32.80700  1.000 21.55000 ? 119 ASN B N   1 
ATOM   3186 C CA  . ASN B 1 117 ? 3.13300   5.47200   34.08300  1.000 22.71000 ? 119 ASN B CA  1 
ATOM   3187 C C   . ASN B 1 117 ? 3.22800   3.96100   33.88000  1.000 25.64000 ? 119 ASN B C   1 
ATOM   3188 O O   . ASN B 1 117 ? 2.73800   3.16200   34.68700  1.000 21.08000 ? 119 ASN B O   1 
ATOM   3189 C CB  . ASN B 1 117 ? 2.03000   5.83400   35.08000  1.000 26.72000 ? 119 ASN B CB  1 
ATOM   3190 C CG  . ASN B 1 117 ? 1.97700   7.32600   35.36400  1.000 28.24000 ? 119 ASN B CG  1 
ATOM   3191 O OD1 . ASN B 1 117 ? 1.06200   8.02600   34.92500  1.000 33.74000 ? 119 ASN B OD1 1 
ATOM   3192 N ND2 . ASN B 1 117 ? 2.97500   7.82400   36.08600  1.000 29.63000 ? 119 ASN B ND2 1 
ATOM   3193 N N   . GLY B 1 118 ? 3.88000   3.56000   32.78900  1.000 19.01000 ? 120 GLY B N   1 
ATOM   3194 C CA  . GLY B 1 118 ? 4.04100   2.16100   32.49600  1.000 16.99000 ? 120 GLY B CA  1 
ATOM   3195 C C   . GLY B 1 118 ? 2.80500   1.46800   31.97700  1.000 17.38000 ? 120 GLY B C   1 
ATOM   3196 O O   . GLY B 1 118 ? 2.83600   0.24900   31.79900  1.000 19.59000 ? 120 GLY B O   1 
ATOM   3197 N N   . SER B 1 119 ? 1.72200   2.19200   31.71700  1.000 16.40000 ? 121 SER B N   1 
ATOM   3198 C CA  . SER B 1 119 ? 0.50400   1.54300   31.26300  1.000 17.74000 ? 121 SER B CA  1 
ATOM   3199 C C   . SER B 1 119 ? 0.12700   2.00400   29.86100  1.000 16.08000 ? 121 SER B C   1 
ATOM   3200 O O   . SER B 1 119 ? 0.09100   3.21500   29.59100  1.000 16.34000 ? 121 SER B O   1 
ATOM   3201 C CB  . SER B 1 119 ? -0.64700  1.81400   32.23600  1.000 21.86000 ? 121 SER B CB  1 
ATOM   3202 O OG  . SER B 1 119 ? -0.31900  1.26600   33.51100  1.000 24.86000 ? 121 SER B OG  1 
ATOM   3203 N N   . PRO B 1 120 ? -0.17600  1.07800   28.95600  1.000 18.09000 ? 122 PRO B N   1 
ATOM   3204 C CA  . PRO B 1 120 ? -0.44800  1.45700   27.56500  1.000 16.30000 ? 122 PRO B CA  1 
ATOM   3205 C C   . PRO B 1 120 ? -1.73500  2.25400   27.43800  1.000 18.47000 ? 122 PRO B C   1 
ATOM   3206 O O   . PRO B 1 120 ? -2.74500  1.95200   28.07800  1.000 19.26000 ? 122 PRO B O   1 
ATOM   3207 C CB  . PRO B 1 120 ? -0.55100  0.10600   26.84600  1.000 17.50000 ? 122 PRO B CB  1 
ATOM   3208 C CG  . PRO B 1 120 ? 0.19500   -0.85600  27.73300  1.000 20.23000 ? 122 PRO B CG  1 
ATOM   3209 C CD  . PRO B 1 120 ? -0.10600  -0.38200  29.12700  1.000 19.94000 ? 122 PRO B CD  1 
ATOM   3210 N N   . SER B 1 121 ? -1.68900  3.28200   26.59900  1.000 16.84000 ? 123 SER B N   1 
ATOM   3211 C CA  . SER B 1 121 ? -2.80000  4.21000   26.44600  1.000 17.18000 ? 123 SER B CA  1 
ATOM   3212 C C   . SER B 1 121 ? -3.40800  4.20700   25.05000  1.000 15.58000 ? 123 SER B C   1 
ATOM   3213 O O   . SER B 1 121 ? -4.62200  4.34800   24.91500  1.000 16.80000 ? 123 SER B O   1 
ATOM   3214 C CB  . SER B 1 121 ? -2.33900  5.62900   26.80600  1.000 18.42000 ? 123 SER B CB  1 
ATOM   3215 O OG  . SER B 1 121 ? -3.33900  6.58100   26.50200  1.000 30.17000 ? 123 SER B OG  1 
ATOM   3216 N N   . GLY B 1 122 ? -2.60300  4.05400   24.00700  1.000 11.42000 ? 124 GLY B N   1 
ATOM   3217 C CA  . GLY B 1 122 ? -3.12800  4.07400   22.65200  1.000 13.38000 ? 124 GLY B CA  1 
ATOM   3218 C C   . GLY B 1 122 ? -2.07400  3.59200   21.68600  1.000 14.67000 ? 124 GLY B C   1 
ATOM   3219 O O   . GLY B 1 122 ? -0.88300  3.54700   22.00800  1.000 13.47000 ? 124 GLY B O   1 
ATOM   3220 N N   . VAL B 1 123 ? -2.52100  3.21500   20.49800  1.000 9.97000  ? 125 VAL B N   1 
ATOM   3221 C CA  . VAL B 1 123 ? -1.60700  2.75500   19.47100  1.000 10.63000 ? 125 VAL B CA  1 
ATOM   3222 C C   . VAL B 1 123 ? -1.96500  3.43300   18.16000  1.000 13.94000 ? 125 VAL B C   1 
ATOM   3223 O O   . VAL B 1 123 ? -3.14300  3.62600   17.83700  1.000 13.69000 ? 125 VAL B O   1 
ATOM   3224 C CB  . VAL B 1 123 ? -1.60400  1.21200   19.34700  1.000 14.79000 ? 125 VAL B CB  1 
ATOM   3225 C CG1 . VAL B 1 123 ? -2.92800  0.69700   18.87700  1.000 15.89000 ? 125 VAL B CG1 1 
ATOM   3226 C CG2 . VAL B 1 123 ? -0.46300  0.73400   18.44000  1.000 14.28000 ? 125 VAL B CG2 1 
ATOM   3227 N N   . TYR B 1 124 ? -0.94300  3.81200   17.41000  1.000 11.48000 ? 126 TYR B N   1 
ATOM   3228 C CA  . TYR B 1 124 ? -1.18400  4.51100   16.16300  1.000 12.39000 ? 126 TYR B CA  1 
ATOM   3229 C C   . TYR B 1 124 ? 0.06400   4.39800   15.31300  1.000 13.43000 ? 126 TYR B C   1 
ATOM   3230 O O   . TYR B 1 124 ? 1.15300   4.10400   15.81400  1.000 13.06000 ? 126 TYR B O   1 
ATOM   3231 C CB  . TYR B 1 124 ? -1.54700  5.97700   16.40800  1.000 13.77000 ? 126 TYR B CB  1 
ATOM   3232 C CG  . TYR B 1 124 ? -0.55500  6.74900   17.25700  1.000 17.58000 ? 126 TYR B CG  1 
ATOM   3233 C CD1 . TYR B 1 124 ? 0.51400   7.41300   16.67500  1.000 18.47000 ? 126 TYR B CD1 1 
ATOM   3234 C CD2 . TYR B 1 124 ? -0.71100  6.84700   18.63200  1.000 18.06000 ? 126 TYR B CD2 1 
ATOM   3235 C CE1 . TYR B 1 124 ? 1.41200   8.14200   17.44300  1.000 18.92000 ? 126 TYR B CE1 1 
ATOM   3236 C CE2 . TYR B 1 124 ? 0.18600   7.57000   19.40800  1.000 18.83000 ? 126 TYR B CE2 1 
ATOM   3237 C CZ  . TYR B 1 124 ? 1.24800   8.21400   18.80200  1.000 19.70000 ? 126 TYR B CZ  1 
ATOM   3238 O OH  . TYR B 1 124 ? 2.15500   8.94800   19.54900  1.000 23.11000 ? 126 TYR B OH  1 
ATOM   3239 N N   . GLN B 1 125 ? -0.10900  4.63600   14.02300  1.000 9.88000  ? 127 GLN B N   1 
ATOM   3240 C CA  . GLN B 1 125 ? 0.97500   4.52600   13.06600  1.000 14.57000 ? 127 GLN B CA  1 
ATOM   3241 C C   . GLN B 1 125 ? 1.62400   5.89000   12.85600  1.000 18.14000 ? 127 GLN B C   1 
ATOM   3242 O O   . GLN B 1 125 ? 0.93800   6.91800   12.80300  1.000 14.94000 ? 127 GLN B O   1 
ATOM   3243 C CB  . GLN B 1 125 ? 0.45900   3.96500   11.73800  1.000 19.62000 ? 127 GLN B CB  1 
ATOM   3244 C CG  . GLN B 1 125 ? 1.55900   3.44200   10.87000  1.000 22.31000 ? 127 GLN B CG  1 
ATOM   3245 C CD  . GLN B 1 125 ? 1.76400   1.95700   11.03100  1.000 22.21000 ? 127 GLN B CD  1 
ATOM   3246 O OE1 . GLN B 1 125 ? 1.75500   1.42500   12.15100  1.000 21.52000 ? 127 GLN B OE1 1 
ATOM   3247 N NE2 . GLN B 1 125 ? 1.92700   1.26700   9.90800   1.000 29.71000 ? 127 GLN B NE2 1 
ATOM   3248 N N   . CYS B 1 126 ? 2.95700   5.88100   12.76200  1.000 16.48000 ? 128 CYS B N   1 
ATOM   3249 C CA  . CYS B 1 126 ? 3.79900   7.05200   12.55200  1.000 16.18000 ? 128 CYS B CA  1 
ATOM   3250 C C   . CYS B 1 126 ? 4.77100   6.75400   11.42200  1.000 18.85000 ? 128 CYS B C   1 
ATOM   3251 O O   . CYS B 1 126 ? 4.99700   5.59800   11.06300  1.000 17.60000 ? 128 CYS B O   1 
ATOM   3252 C CB  . CYS B 1 126 ? 4.62100   7.39900   13.81300  1.000 16.51000 ? 128 CYS B CB  1 
ATOM   3253 S SG  . CYS B 1 126 ? 3.70800   8.31900   14.99700  1.000 28.49000 ? 128 CYS B SG  1 
ATOM   3254 N N   . ALA B 1 127 ? 5.37100   7.80100   10.87000  1.000 20.16000 ? 129 ALA B N   1 
ATOM   3255 C CA  . ALA B 1 127 ? 6.47300   7.60800   9.94100   1.000 17.91000 ? 129 ALA B CA  1 
ATOM   3256 C C   . ALA B 1 127 ? 7.65900   8.43400   10.40700  1.000 16.33000 ? 129 ALA B C   1 
ATOM   3257 O O   . ALA B 1 127 ? 7.50300   9.49500   11.00900  1.000 17.38000 ? 129 ALA B O   1 
ATOM   3258 C CB  . ALA B 1 127 ? 6.10100   7.98000   8.50200   1.000 19.24000 ? 129 ALA B CB  1 
ATOM   3259 N N   . MET B 1 128 ? 8.84900   7.91900   10.15100  1.000 15.89000 ? 130 MET B N   1 
ATOM   3260 C CA  . MET B 1 128 ? 10.05100  8.71600   10.36000  1.000 17.87000 ? 130 MET B CA  1 
ATOM   3261 C C   . MET B 1 128 ? 10.11700  9.77100   9.25300   1.000 13.60000 ? 130 MET B C   1 
ATOM   3262 O O   . MET B 1 128 ? 10.28300  9.43100   8.08000   1.000 17.20000 ? 130 MET B O   1 
ATOM   3263 C CB  . MET B 1 128 ? 11.26500  7.79100   10.36100  1.000 14.91000 ? 130 MET B CB  1 
ATOM   3264 C CG  . MET B 1 128 ? 12.60700  8.45700   10.63800  1.000 16.33000 ? 130 MET B CG  1 
ATOM   3265 S SD  . MET B 1 128 ? 12.61400  9.32900   12.21600  1.000 20.69000 ? 130 MET B SD  1 
ATOM   3266 C CE  . MET B 1 128 ? 12.32800  7.96300   13.35400  1.000 15.64000 ? 130 MET B CE  1 
ATOM   3267 N N   . ARG B 1 129 ? 9.94100   11.04500  9.60500   1.000 18.00000 ? 131 ARG B N   1 
ATOM   3268 C CA  . ARG B 1 129 ? 10.00800  12.11200  8.60200   1.000 13.90000 ? 131 ARG B CA  1 
ATOM   3269 C C   . ARG B 1 129 ? 11.41000  12.17100  7.99300   1.000 18.70000 ? 131 ARG B C   1 
ATOM   3270 O O   . ARG B 1 129 ? 12.38500  11.71400  8.60400   1.000 15.61000 ? 131 ARG B O   1 
ATOM   3271 C CB  . ARG B 1 129 ? 9.66300   13.47200  9.21000   1.000 16.76000 ? 131 ARG B CB  1 
ATOM   3272 C CG  . ARG B 1 129 ? 8.34800   13.55000  10.00000  1.000 18.64000 ? 131 ARG B CG  1 
ATOM   3273 C CD  . ARG B 1 129 ? 7.13500   13.26800  9.13000   1.000 18.49000 ? 131 ARG B CD  1 
ATOM   3274 N NE  . ARG B 1 129 ? 7.16100   14.02700  7.88200   1.000 17.09000 ? 131 ARG B NE  1 
ATOM   3275 C CZ  . ARG B 1 129 ? 6.40300   13.74100  6.82700   1.000 24.28000 ? 131 ARG B CZ  1 
ATOM   3276 N NH1 . ARG B 1 129 ? 5.55800   12.72000  6.87800   1.000 16.89000 ? 131 ARG B NH1 1 
ATOM   3277 N NH2 . ARG B 1 129 ? 6.48500   14.47600  5.72300   1.000 19.88000 ? 131 ARG B NH2 1 
ATOM   3278 N N   . PRO B 1 130 ? 11.53900  12.72600  6.78100   1.000 14.70000 ? 132 PRO B N   1 
ATOM   3279 C CA  . PRO B 1 130 ? 12.88600  12.88900  6.20500   1.000 16.74000 ? 132 PRO B CA  1 
ATOM   3280 C C   . PRO B 1 130 ? 13.83400  13.68000  7.09200   1.000 15.88000 ? 132 PRO B C   1 
ATOM   3281 O O   . PRO B 1 130 ? 15.04900  13.42200  7.05900   1.000 15.67000 ? 132 PRO B O   1 
ATOM   3282 C CB  . PRO B 1 130 ? 12.61200  13.60600  4.87800   1.000 16.82000 ? 132 PRO B CB  1 
ATOM   3283 C CG  . PRO B 1 130 ? 11.22400  13.12400  4.49600   1.000 20.65000 ? 132 PRO B CG  1 
ATOM   3284 C CD  . PRO B 1 130 ? 10.47600  13.06000  5.80900   1.000 17.04000 ? 132 PRO B CD  1 
ATOM   3285 N N   . ASN B 1 131 ? 13.32100  14.62500  7.88700   1.000 12.98000 ? 133 ASN B N   1 
ATOM   3286 C CA  . ASN B 1 131 ? 14.13400  15.40100  8.81600   1.000 15.24000 ? 133 ASN B CA  1 
ATOM   3287 C C   . ASN B 1 131 ? 14.25300  14.73700  10.19000  1.000 14.39000 ? 133 ASN B C   1 
ATOM   3288 O O   . ASN B 1 131 ? 14.60000  15.41300  11.16500  1.000 14.23000 ? 133 ASN B O   1 
ATOM   3289 C CB  . ASN B 1 131 ? 13.57400  16.82400  8.95400   1.000 18.32000 ? 133 ASN B CB  1 
ATOM   3290 C CG  . ASN B 1 131 ? 12.24600  16.88800  9.72100   1.000 16.43000 ? 133 ASN B CG  1 
ATOM   3291 O OD1 . ASN B 1 131 ? 11.68600  15.86800  10.14400  1.000 17.97000 ? 133 ASN B OD1 1 
ATOM   3292 N ND2 . ASN B 1 131 ? 11.74000  18.10200  9.90200   1.000 17.90000 ? 133 ASN B ND2 1 
ATOM   3293 N N   . PHE B 1 132 ? 13.90700  13.45000  10.28200  1.000 15.51000 ? 134 PHE B N   1 
ATOM   3294 C CA  . PHE B 1 132 ? 14.11400  12.59500  11.45000  1.000 16.29000 ? 134 PHE B CA  1 
ATOM   3295 C C   . PHE B 1 132 ? 13.28700  13.00200  12.65500  1.000 14.06000 ? 134 PHE B C   1 
ATOM   3296 O O   . PHE B 1 132 ? 13.61800  12.64500  13.79200  1.000 15.31000 ? 134 PHE B O   1 
ATOM   3297 C CB  . PHE B 1 132 ? 15.59400  12.52700  11.82200  1.000 13.66000 ? 134 PHE B CB  1 
ATOM   3298 C CG  . PHE B 1 132 ? 16.42400  11.82700  10.79200  1.000 16.81000 ? 134 PHE B CG  1 
ATOM   3299 C CD1 . PHE B 1 132 ? 16.39500  10.45000  10.68400  1.000 17.58000 ? 134 PHE B CD1 1 
ATOM   3300 C CD2 . PHE B 1 132 ? 17.19000  12.54700  9.89900   1.000 20.45000 ? 134 PHE B CD2 1 
ATOM   3301 C CE1 . PHE B 1 132 ? 17.14500  9.80400   9.73300   1.000 25.29000 ? 134 PHE B CE1 1 
ATOM   3302 C CE2 . PHE B 1 132 ? 17.93800  11.90400  8.94100   1.000 22.21000 ? 134 PHE B CE2 1 
ATOM   3303 C CZ  . PHE B 1 132 ? 17.91600  10.53400  8.85900   1.000 24.39000 ? 134 PHE B CZ  1 
ATOM   3304 N N   . THR B 1 133 ? 12.21000  13.72900  12.44300  1.000 14.81000 ? 135 THR B N   1 
ATOM   3305 C CA  . THR B 1 133 ? 11.19500  13.86900  13.46600  1.000 14.92000 ? 135 THR B CA  1 
ATOM   3306 C C   . THR B 1 133 ? 10.08600  12.86500  13.18600  1.000 15.46000 ? 135 THR B C   1 
ATOM   3307 O O   . THR B 1 133 ? 10.07400  12.18100  12.16100  1.000 16.19000 ? 135 THR B O   1 
ATOM   3308 C CB  . THR B 1 133 ? 10.64900  15.29500  13.50500  1.000 14.04000 ? 135 THR B CB  1 
ATOM   3309 O OG1 . THR B 1 133 ? 9.98800   15.58500  12.26700  1.000 13.04000 ? 135 THR B OG1 1 
ATOM   3310 C CG2 . THR B 1 133 ? 11.78600  16.29100  13.70800  1.000 16.65000 ? 135 THR B CG2 1 
ATOM   3311 N N   . ILE B 1 134 ? 9.16900   12.75300  14.12700  1.000 12.21000 ? 136 ILE B N   1 
ATOM   3312 C CA  . ILE B 1 134 ? 7.94700   11.99500  13.90900  1.000 14.31000 ? 136 ILE B CA  1 
ATOM   3313 C C   . ILE B 1 134 ? 6.79900   12.85400  14.39200  1.000 12.68000 ? 136 ILE B C   1 
ATOM   3314 O O   . ILE B 1 134 ? 6.92500   13.59700  15.37400  1.000 13.55000 ? 136 ILE B O   1 
ATOM   3315 C CB  . ILE B 1 134 ? 7.94400   10.61200  14.60700  1.000 18.31000 ? 136 ILE B CB  1 
ATOM   3316 C CG1 . ILE B 1 134 ? 7.77600   10.73400  16.11800  1.000 17.40000 ? 136 ILE B CG1 1 
ATOM   3317 C CG2 . ILE B 1 134 ? 9.21300   9.79700   14.27800  1.000 18.04000 ? 136 ILE B CG2 1 
ATOM   3318 C CD1 . ILE B 1 134 ? 7.45300   9.39500   16.77800  1.000 16.24000 ? 136 ILE B CD1 1 
ATOM   3319 N N   . LYS B 1 135 ? 5.69100   12.79400  13.67000  1.000 17.00000 ? 137 LYS B N   1 
ATOM   3320 C CA  . LYS B 1 135 ? 4.51000   13.55300  14.04900  1.000 17.58000 ? 137 LYS B CA  1 
ATOM   3321 C C   . LYS B 1 135 ? 3.69200   12.61700  14.92100  1.000 22.13000 ? 137 LYS B C   1 
ATOM   3322 O O   . LYS B 1 135 ? 2.82700   11.87800  14.45100  1.000 23.71000 ? 137 LYS B O   1 
ATOM   3323 C CB  . LYS B 1 135 ? 3.75300   14.03800  12.82100  1.000 20.66000 ? 137 LYS B CB  1 
ATOM   3324 N N   . GLY B 1 136 ? 4.00100   12.62400  16.21400  1.000 21.15000 ? 138 GLY B N   1 
ATOM   3325 C CA  . GLY B 1 136 ? 3.35500   11.75200  17.16200  1.000 20.39000 ? 138 GLY B CA  1 
ATOM   3326 C C   . GLY B 1 136 ? 2.26000   12.46600  17.92600  1.000 19.33000 ? 138 GLY B C   1 
ATOM   3327 O O   . GLY B 1 136 ? 1.91900   13.62300  17.68500  1.000 19.77000 ? 138 GLY B O   1 
ATOM   3328 N N   . SER B 1 137 ? 1.70200   11.73600  18.87700  1.000 20.58000 ? 139 SER B N   1 
ATOM   3329 C CA  . SER B 1 137 ? 0.73700   12.27800  19.82200  1.000 18.29000 ? 139 SER B CA  1 
ATOM   3330 C C   . SER B 1 137 ? 1.25300   11.83100  21.18700  1.000 22.22000 ? 139 SER B C   1 
ATOM   3331 O O   . SER B 1 137 ? 0.99400   10.70900  21.64100  1.000 22.21000 ? 139 SER B O   1 
ATOM   3332 C CB  . SER B 1 137 ? -0.66200  11.77000  19.52300  1.000 27.73000 ? 139 SER B CB  1 
ATOM   3333 O OG  . SER B 1 137 ? -1.55500  12.13600  20.55800  1.000 33.09000 ? 139 SER B OG  1 
ATOM   3334 N N   . PHE B 1 138 ? 2.05200   12.68200  21.81300  1.000 16.55000 ? 140 PHE B N   1 
ATOM   3335 C CA  . PHE B 1 138 ? 2.69200   12.33600  23.06900  1.000 14.37000 ? 140 PHE B CA  1 
ATOM   3336 C C   . PHE B 1 138 ? 2.44900   13.46700  24.05300  1.000 17.03000 ? 140 PHE B C   1 
ATOM   3337 O O   . PHE B 1 138 ? 2.56900   14.63900  23.69200  1.000 18.06000 ? 140 PHE B O   1 
ATOM   3338 C CB  . PHE B 1 138 ? 4.19300   12.14700  22.90000  1.000 14.32000 ? 140 PHE B CB  1 
ATOM   3339 C CG  . PHE B 1 138 ? 4.59500   10.96800  22.05500  1.000 11.66000 ? 140 PHE B CG  1 
ATOM   3340 C CD1 . PHE B 1 138 ? 4.36900   9.66600   22.48500  1.000 14.55000 ? 140 PHE B CD1 1 
ATOM   3341 C CD2 . PHE B 1 138 ? 5.27800   11.16600  20.87500  1.000 14.91000 ? 140 PHE B CD2 1 
ATOM   3342 C CE1 . PHE B 1 138 ? 4.79000   8.59000   21.71900  1.000 17.88000 ? 140 PHE B CE1 1 
ATOM   3343 C CE2 . PHE B 1 138 ? 5.69700   10.09100  20.09900  1.000 18.06000 ? 140 PHE B CE2 1 
ATOM   3344 C CZ  . PHE B 1 138 ? 5.45500   8.80800   20.52200  1.000 14.04000 ? 140 PHE B CZ  1 
ATOM   3345 N N   . LEU B 1 139 ? 2.12600   13.11900  25.28400  1.000 14.29000 ? 141 LEU B N   1 
ATOM   3346 C CA  . LEU B 1 139 ? 1.96300   14.09500  26.34800  1.000 20.79000 ? 141 LEU B CA  1 
ATOM   3347 C C   . LEU B 1 139 ? 3.06700   13.92400  27.38100  1.000 18.01000 ? 141 LEU B C   1 
ATOM   3348 O O   . LEU B 1 139 ? 3.94300   13.06900  27.25100  1.000 16.18000 ? 141 LEU B O   1 
ATOM   3349 C CB  . LEU B 1 139 ? 0.58600   13.95200  26.99100  1.000 23.92000 ? 141 LEU B CB  1 
ATOM   3350 C CG  . LEU B 1 139 ? -0.56300  14.04300  25.99000  1.000 28.94000 ? 141 LEU B CG  1 
ATOM   3351 C CD1 . LEU B 1 139 ? -1.88000  13.71300  26.67700  1.000 36.04000 ? 141 LEU B CD1 1 
ATOM   3352 C CD2 . LEU B 1 139 ? -0.59300  15.43300  25.38100  1.000 31.27000 ? 141 LEU B CD2 1 
ATOM   3353 N N   . ASN B 1 140 ? 3.01100   14.75900  28.42100  1.000 17.76000 ? 142 ASN B N   1 
ATOM   3354 C CA  . ASN B 1 140 ? 3.86100   14.58800  29.58800  1.000 17.03000 ? 142 ASN B CA  1 
ATOM   3355 C C   . ASN B 1 140 ? 3.81800   13.14900  30.08500  1.000 20.85000 ? 142 ASN B C   1 
ATOM   3356 O O   . ASN B 1 140 ? 2.74400   12.55200  30.20300  1.000 17.89000 ? 142 ASN B O   1 
ATOM   3357 C CB  . ASN B 1 140 ? 3.41400   15.53900  30.70800  1.000 21.53000 ? 142 ASN B CB  1 
ATOM   3358 C CG  . ASN B 1 140 ? 3.83200   16.96600  30.44800  1.000 22.72000 ? 142 ASN B CG  1 
ATOM   3359 O OD1 . ASN B 1 140 ? 4.48300   17.24500  29.44900  1.000 26.58000 ? 142 ASN B OD1 1 
ATOM   3360 N ND2 . ASN B 1 140 ? 3.45300   17.87700  31.33200  1.000 20.09000 ? 142 ASN B ND2 1 
ATOM   3361 N N   . GLY B 1 141 ? 4.99300   12.60500  30.39900  1.000 13.81000 ? 143 GLY B N   1 
ATOM   3362 C CA  . GLY B 1 141 ? 5.08400   11.25200  30.90300  1.000 17.75000 ? 143 GLY B CA  1 
ATOM   3363 C C   . GLY B 1 141 ? 5.06400   10.17100  29.84300  1.000 12.74000 ? 143 GLY B C   1 
ATOM   3364 O O   . GLY B 1 141 ? 5.03700   8.98500   30.19100  1.000 16.78000 ? 143 GLY B O   1 
ATOM   3365 N N   . SER B 1 142 ? 5.09500   10.53200  28.56600  1.000 12.99000 ? 144 SER B N   1 
ATOM   3366 C CA  . SER B 1 142 ? 5.08400   9.52000   27.51100  1.000 13.02000 ? 144 SER B CA  1 
ATOM   3367 C C   . SER B 1 142 ? 6.47600   9.00600   27.17400  1.000 11.28000 ? 144 SER B C   1 
ATOM   3368 O O   . SER B 1 142 ? 6.58900   8.04200   26.40900  1.000 8.92000  ? 144 SER B O   1 
ATOM   3369 C CB  . SER B 1 142 ? 4.43400   10.07300  26.23800  1.000 11.08000 ? 144 SER B CB  1 
ATOM   3370 O OG  . SER B 1 142 ? 5.09800   11.24100  25.78700  1.000 13.10000 ? 144 SER B OG  1 
ATOM   3371 N N   . CYS B 1 143 ? 7.52900   9.64100   27.69600  1.000 9.51000  ? 145 CYS B N   1 
ATOM   3372 C CA  . CYS B 1 143 ? 8.88800   9.21500   27.38800  1.000 10.67000 ? 145 CYS B CA  1 
ATOM   3373 C C   . CYS B 1 143 ? 9.10000   7.74900   27.74900  1.000 10.99000 ? 145 CYS B C   1 
ATOM   3374 O O   . CYS B 1 143 ? 8.57200   7.24700   28.75200  1.000 11.89000 ? 145 CYS B O   1 
ATOM   3375 C CB  . CYS B 1 143 ? 9.89700   10.10200  28.12200  1.000 11.81000 ? 145 CYS B CB  1 
ATOM   3376 S SG  . CYS B 1 143 ? 9.93800   11.74400  27.38800  1.000 15.18000 ? 145 CYS B SG  1 
ATOM   3377 N N   . GLY B 1 144 ? 9.87100   7.05200   26.91600  1.000 9.63000  ? 146 GLY B N   1 
ATOM   3378 C CA  . GLY B 1 144 ? 10.01100  5.62300   27.05900  1.000 9.17000  ? 146 GLY B CA  1 
ATOM   3379 C C   . GLY B 1 144 ? 8.99100   4.82400   26.27200  1.000 11.00000 ? 146 GLY B C   1 
ATOM   3380 O O   . GLY B 1 144 ? 9.18600   3.61800   26.09600  1.000 11.91000 ? 146 GLY B O   1 
ATOM   3381 N N   . SER B 1 145 ? 7.92100   5.45800   25.78300  1.000 8.28000  ? 147 SER B N   1 
ATOM   3382 C CA  . SER B 1 145 ? 7.04700   4.80800   24.80800  1.000 10.35000 ? 147 SER B CA  1 
ATOM   3383 C C   . SER B 1 145 ? 7.85800   4.40100   23.57600  1.000 10.85000 ? 147 SER B C   1 
ATOM   3384 O O   . SER B 1 145 ? 8.81200   5.08300   23.18900  1.000 7.75000  ? 147 SER B O   1 
ATOM   3385 C CB  . SER B 1 145 ? 5.91100   5.74800   24.39100  1.000 10.26000 ? 147 SER B CB  1 
ATOM   3386 O OG  . SER B 1 145 ? 5.05600   6.04100   25.48500  1.000 12.92000 ? 147 SER B OG  1 
ATOM   3387 N N   . VAL B 1 146 ? 7.49300   3.26900   22.95700  1.000 7.22000  ? 148 VAL B N   1 
ATOM   3388 C CA  . VAL B 1 146 ? 8.31200   2.74000   21.86800  1.000 8.15000  ? 148 VAL B CA  1 
ATOM   3389 C C   . VAL B 1 146 ? 7.51000   2.61100   20.58600  1.000 10.21000 ? 148 VAL B C   1 
ATOM   3390 O O   . VAL B 1 146 ? 6.28800   2.44300   20.59700  1.000 7.85000  ? 148 VAL B O   1 
ATOM   3391 C CB  . VAL B 1 146 ? 8.96800   1.37900   22.20400  1.000 9.28000  ? 148 VAL B CB  1 
ATOM   3392 C CG1 . VAL B 1 146 ? 9.87000   1.52000   23.43000  1.000 10.67000 ? 148 VAL B CG1 1 
ATOM   3393 C CG2 . VAL B 1 146 ? 7.90900   0.29800   22.38300  1.000 8.73000  ? 148 VAL B CG2 1 
ATOM   3394 N N   . GLY B 1 147 ? 8.23600   2.68600   19.47000  1.000 7.77000  ? 149 GLY B N   1 
ATOM   3395 C CA  . GLY B 1 147 ? 7.70100   2.40800   18.15100  1.000 8.63000  ? 149 GLY B CA  1 
ATOM   3396 C C   . GLY B 1 147 ? 8.25300   1.07500   17.68100  1.000 11.98000 ? 149 GLY B C   1 
ATOM   3397 O O   . GLY B 1 147 ? 9.35500   0.67300   18.07200  1.000 8.98000  ? 149 GLY B O   1 
ATOM   3398 N N   . PHE B 1 148 ? 7.47600   0.37600   16.86100  1.000 9.39000  ? 150 PHE B N   1 
ATOM   3399 C CA  . PHE B 1 148 ? 7.83800   -0.99100  16.52600  1.000 9.28000  ? 150 PHE B CA  1 
ATOM   3400 C C   . PHE B 1 148 ? 7.10100   -1.42700  15.27100  1.000 10.47000 ? 150 PHE B C   1 
ATOM   3401 O O   . PHE B 1 148 ? 6.09700   -0.83100  14.86800  1.000 8.55000  ? 150 PHE B O   1 
ATOM   3402 C CB  . PHE B 1 148 ? 7.50600   -1.94900  17.67200  1.000 10.75000 ? 150 PHE B CB  1 
ATOM   3403 C CG  . PHE B 1 148 ? 6.04900   -2.01600  17.96200  1.000 11.94000 ? 150 PHE B CG  1 
ATOM   3404 C CD1 . PHE B 1 148 ? 5.45900   -1.07500  18.78100  1.000 12.69000 ? 150 PHE B CD1 1 
ATOM   3405 C CD2 . PHE B 1 148 ? 5.25400   -2.99500  17.38000  1.000 11.59000 ? 150 PHE B CD2 1 
ATOM   3406 C CE1 . PHE B 1 148 ? 4.08900   -1.11000  19.02600  1.000 14.79000 ? 150 PHE B CE1 1 
ATOM   3407 C CE2 . PHE B 1 148 ? 3.89300   -3.03300  17.61900  1.000 12.50000 ? 150 PHE B CE2 1 
ATOM   3408 C CZ  . PHE B 1 148 ? 3.31100   -2.09300  18.44300  1.000 12.56000 ? 150 PHE B CZ  1 
ATOM   3409 N N   . ASN B 1 149 ? 7.62100   -2.48400  14.66700  1.000 11.78000 ? 151 ASN B N   1 
ATOM   3410 C CA  . ASN B 1 149 ? 6.94200   -3.21900  13.61100  1.000 12.06000 ? 151 ASN B CA  1 
ATOM   3411 C C   . ASN B 1 149 ? 6.88400   -4.68200  14.03500  1.000 15.13000 ? 151 ASN B C   1 
ATOM   3412 O O   . ASN B 1 149 ? 7.66500   -5.11800  14.88100  1.000 12.24000 ? 151 ASN B O   1 
ATOM   3413 C CB  . ASN B 1 149 ? 7.68300   -3.07900  12.27700  1.000 14.46000 ? 151 ASN B CB  1 
ATOM   3414 C CG  . ASN B 1 149 ? 7.46800   -1.72500  11.62800  1.000 17.96000 ? 151 ASN B CG  1 
ATOM   3415 O OD1 . ASN B 1 149 ? 6.43700   -1.48700  10.98500  1.000 19.71000 ? 151 ASN B OD1 1 
ATOM   3416 N ND2 . ASN B 1 149 ? 8.43400   -0.83200  11.78500  1.000 12.40000 ? 151 ASN B ND2 1 
ATOM   3417 N N   . ILE B 1 150 ? 5.95400   -5.45300  13.45900  1.000 13.35000 ? 152 ILE B N   1 
ATOM   3418 C CA  . ILE B 1 150 ? 5.83000   -6.86600  13.80600  1.000 20.10000 ? 152 ILE B CA  1 
ATOM   3419 C C   . ILE B 1 150 ? 5.84600   -7.68000  12.52700  1.000 24.85000 ? 152 ILE B C   1 
ATOM   3420 O O   . ILE B 1 150 ? 5.04400   -7.43200  11.62400  1.000 28.18000 ? 152 ILE B O   1 
ATOM   3421 C CB  . ILE B 1 150 ? 4.55200   -7.18400  14.60500  1.000 22.79000 ? 152 ILE B CB  1 
ATOM   3422 C CG1 . ILE B 1 150 ? 4.44700   -6.30500  15.85300  1.000 20.27000 ? 152 ILE B CG1 1 
ATOM   3423 C CG2 . ILE B 1 150 ? 4.53100   -8.68000  14.99400  1.000 20.42000 ? 152 ILE B CG2 1 
ATOM   3424 C CD1 . ILE B 1 150 ? 3.35200   -6.74900  16.80800  1.000 22.35000 ? 152 ILE B CD1 1 
ATOM   3425 N N   . ASP B 1 151 ? 6.74500   -8.65200  12.45800  1.000 26.98000 ? 153 ASP B N   1 
ATOM   3426 C CA  . ASP B 1 151 ? 6.84200   -9.56700  11.32600  1.000 31.57000 ? 153 ASP B CA  1 
ATOM   3427 C C   . ASP B 1 151 ? 6.84200   -10.99000 11.87300  1.000 33.51000 ? 153 ASP B C   1 
ATOM   3428 O O   . ASP B 1 151 ? 7.80500   -11.39900 12.53000  1.000 32.46000 ? 153 ASP B O   1 
ATOM   3429 C CB  . ASP B 1 151 ? 8.10500   -9.29500  10.50900  1.000 36.54000 ? 153 ASP B CB  1 
ATOM   3430 C CG  . ASP B 1 151 ? 8.23600   -10.21900 9.30900   1.000 47.44000 ? 153 ASP B CG  1 
ATOM   3431 O OD1 . ASP B 1 151 ? 7.34600   -10.19200 8.42900   1.000 47.20000 ? 153 ASP B OD1 1 
ATOM   3432 O OD2 . ASP B 1 151 ? 9.24400   -10.96200 9.24300   1.000 51.65000 ? 153 ASP B OD2 1 
ATOM   3433 N N   . TYR B 1 152 ? 5.76200   -11.73100 11.61700  1.000 33.53000 ? 154 TYR B N   1 
ATOM   3434 C CA  . TYR B 1 152 ? 5.62400   -13.12700 12.03700  1.000 35.50000 ? 154 TYR B CA  1 
ATOM   3435 C C   . TYR B 1 152 ? 6.05000   -13.30300 13.49400  1.000 38.12000 ? 154 TYR B C   1 
ATOM   3436 O O   . TYR B 1 152 ? 7.00200   -14.01700 13.81900  1.000 39.56000 ? 154 TYR B O   1 
ATOM   3437 C CB  . TYR B 1 152 ? 6.41700   -14.05700 11.11500  1.000 37.49000 ? 154 TYR B CB  1 
ATOM   3438 N N   . ASP B 1 153 ? 5.34800   -12.58800 14.36700  1.000 35.20000 ? 155 ASP B N   1 
ATOM   3439 C CA  . ASP B 1 153 ? 5.51400   -12.65400 15.81700  1.000 40.88000 ? 155 ASP B CA  1 
ATOM   3440 C C   . ASP B 1 153 ? 6.90500   -12.22800 16.30300  1.000 34.87000 ? 155 ASP B C   1 
ATOM   3441 O O   . ASP B 1 153 ? 7.23300   -12.44700 17.47600  1.000 37.66000 ? 155 ASP B O   1 
ATOM   3442 C CB  . ASP B 1 153 ? 5.17800   -14.06000 16.35000  1.000 40.36000 ? 155 ASP B CB  1 
ATOM   3443 C CG  . ASP B 1 153 ? 3.76100   -14.51000 15.98000  1.000 50.31000 ? 155 ASP B CG  1 
ATOM   3444 O OD1 . ASP B 1 153 ? 2.84000   -13.65600 15.92000  1.000 52.34000 ? 155 ASP B OD1 1 
ATOM   3445 O OD2 . ASP B 1 153 ? 3.57000   -15.72100 15.73500  1.000 47.81000 ? 155 ASP B OD2 1 
ATOM   3446 N N   . CYS B 1 154 ? 7.73800   -11.62500 15.44900  1.000 29.60000 ? 156 CYS B N   1 
ATOM   3447 C CA  . CYS B 1 154 ? 8.97700   -10.98800 15.89400  1.000 29.58000 ? 156 CYS B CA  1 
ATOM   3448 C C   . CYS B 1 154 ? 8.78600   -9.47000  15.92900  1.000 22.13000 ? 156 CYS B C   1 
ATOM   3449 O O   . CYS B 1 154 ? 8.47400   -8.86100  14.90200  1.000 21.43000 ? 156 CYS B O   1 
ATOM   3450 C CB  . CYS B 1 154 ? 10.15900  -11.33600 14.99200  1.000 25.00000 ? 156 CYS B CB  1 
ATOM   3451 S SG  . CYS B 1 154 ? 11.68400  -10.48200 15.52700  1.000 29.95000 ? 156 CYS B SG  1 
ATOM   3452 N N   . VAL B 1 155 ? 8.99600   -8.86900  17.09700  1.000 17.41000 ? 157 VAL B N   1 
ATOM   3453 C CA  . VAL B 1 155 ? 8.81500   -7.42900  17.27800  1.000 15.35000 ? 157 VAL B CA  1 
ATOM   3454 C C   . VAL B 1 155 ? 10.13000  -6.71600  16.97800  1.000 14.16000 ? 157 VAL B C   1 
ATOM   3455 O O   . VAL B 1 155 ? 11.13500  -6.93600  17.65600  1.000 14.81000 ? 157 VAL B O   1 
ATOM   3456 C CB  . VAL B 1 155 ? 8.34000   -7.10500  18.70100  1.000 17.19000 ? 157 VAL B CB  1 
ATOM   3457 C CG1 . VAL B 1 155 ? 8.15100   -5.58500  18.87300  1.000 9.92000  ? 157 VAL B CG1 1 
ATOM   3458 C CG2 . VAL B 1 155 ? 7.05100   -7.87600  19.03900  1.000 16.72000 ? 157 VAL B CG2 1 
ATOM   3459 N N   . SER B 1 156 ? 10.12900  -5.84700  15.97800  1.000 14.05000 ? 158 SER B N   1 
ATOM   3460 C CA  . SER B 1 156 ? 11.29600  -5.01700  15.68600  1.000 14.65000 ? 158 SER B CA  1 
ATOM   3461 C C   . SER B 1 156 ? 11.07500  -3.64500  16.31800  1.000 11.30000 ? 158 SER B C   1 
ATOM   3462 O O   . SER B 1 156 ? 10.28400  -2.84200  15.81600  1.000 11.27000 ? 158 SER B O   1 
ATOM   3463 C CB  . SER B 1 156 ? 11.52500  -4.91700  14.18200  1.000 15.87000 ? 158 SER B CB  1 
ATOM   3464 O OG  . SER B 1 156 ? 11.97800  -6.16100  13.66600  1.000 23.14000 ? 158 SER B OG  1 
ATOM   3465 N N   . PHE B 1 157 ? 11.76000  -3.38800  17.43300  1.000 10.93000 ? 159 PHE B N   1 
ATOM   3466 C CA  . PHE B 1 157 ? 11.68400  -2.08300  18.09200  1.000 13.67000 ? 159 PHE B CA  1 
ATOM   3467 C C   . PHE B 1 157 ? 12.56100  -1.09000  17.34600  1.000 11.65000 ? 159 PHE B C   1 
ATOM   3468 O O   . PHE B 1 157 ? 13.73600  -1.36300  17.08900  1.000 14.47000 ? 159 PHE B O   1 
ATOM   3469 C CB  . PHE B 1 157 ? 12.14100  -2.17700  19.55100  1.000 10.01000 ? 159 PHE B CB  1 
ATOM   3470 C CG  . PHE B 1 157 ? 11.24400  -3.01500  20.41300  1.000 12.90000 ? 159 PHE B CG  1 
ATOM   3471 C CD1 . PHE B 1 157 ? 10.02900  -2.51900  20.84400  1.000 11.36000 ? 159 PHE B CD1 1 
ATOM   3472 C CD2 . PHE B 1 157 ? 11.61700  -4.29900  20.79400  1.000 10.67000 ? 159 PHE B CD2 1 
ATOM   3473 C CE1 . PHE B 1 157 ? 9.18200   -3.27600  21.63100  1.000 11.80000 ? 159 PHE B CE1 1 
ATOM   3474 C CE2 . PHE B 1 157 ? 10.77500  -5.06300  21.59200  1.000 12.26000 ? 159 PHE B CE2 1 
ATOM   3475 C CZ  . PHE B 1 157 ? 9.55000   -4.54500  22.01200  1.000 10.74000 ? 159 PHE B CZ  1 
ATOM   3476 N N   . CYS B 1 158 ? 12.00900  0.07000   16.99900  1.000 11.92000 ? 160 CYS B N   1 
ATOM   3477 C CA  . CYS B 1 158 ? 12.81200  1.03700   16.26700  1.000 10.31000 ? 160 CYS B CA  1 
ATOM   3478 C C   . CYS B 1 158 ? 12.86000  2.43200   16.87600  1.000 11.74000 ? 160 CYS B C   1 
ATOM   3479 O O   . CYS B 1 158 ? 13.67700  3.24100   16.42400  1.000 13.85000 ? 160 CYS B O   1 
ATOM   3480 C CB  . CYS B 1 158 ? 12.32100  1.15200   14.82000  1.000 13.55000 ? 160 CYS B CB  1 
ATOM   3481 S SG  . CYS B 1 158 ? 10.60700  1.61600   14.67400  1.000 14.57000 ? 160 CYS B SG  1 
ATOM   3482 N N   . TYR B 1 159 ? 12.03500  2.74600   17.86900  1.000 7.59000  ? 161 TYR B N   1 
ATOM   3483 C CA  . TYR B 1 159 ? 11.94100  4.12000   18.36000  1.000 8.20000  ? 161 TYR B CA  1 
ATOM   3484 C C   . TYR B 1 159 ? 11.68200  4.07800   19.85400  1.000 8.95000  ? 161 TYR B C   1 
ATOM   3485 O O   . TYR B 1 159 ? 10.94700  3.21300   20.33800  1.000 7.97000  ? 161 TYR B O   1 
ATOM   3486 C CB  . TYR B 1 159 ? 10.81200  4.90200   17.65400  1.000 8.80000  ? 161 TYR B CB  1 
ATOM   3487 C CG  . TYR B 1 159 ? 10.60100  6.32700   18.13600  1.000 9.55000  ? 161 TYR B CG  1 
ATOM   3488 C CD1 . TYR B 1 159 ? 11.35700  7.37100   17.61000  1.000 11.15000 ? 161 TYR B CD1 1 
ATOM   3489 C CD2 . TYR B 1 159 ? 9.64500   6.63500   19.10900  1.000 7.78000  ? 161 TYR B CD2 1 
ATOM   3490 C CE1 . TYR B 1 159 ? 11.17600  8.68300   18.03200  1.000 7.83000  ? 161 TYR B CE1 1 
ATOM   3491 C CE2 . TYR B 1 159 ? 9.44600   7.95600   19.52900  1.000 9.50000  ? 161 TYR B CE2 1 
ATOM   3492 C CZ  . TYR B 1 159 ? 10.22700  8.97300   18.98900  1.000 8.21000  ? 161 TYR B CZ  1 
ATOM   3493 O OH  . TYR B 1 159 ? 10.07900  10.28500  19.40700  1.000 9.38000  ? 161 TYR B OH  1 
ATOM   3494 N N   . MET B 1 160 ? 12.31600  4.99400   20.58100  1.000 7.60000  ? 162 MET B N   1 
ATOM   3495 C CA  . MET B 1 160 ? 11.98200  5.23800   21.97000  1.000 7.27000  ? 162 MET B CA  1 
ATOM   3496 C C   . MET B 1 160 ? 11.83500  6.73800   22.13800  1.000 7.63000  ? 162 MET B C   1 
ATOM   3497 O O   . MET B 1 160 ? 12.70200  7.49900   21.69600  1.000 6.93000  ? 162 MET B O   1 
ATOM   3498 C CB  . MET B 1 160 ? 13.04000  4.70000   22.93200  1.000 5.96000  ? 162 MET B CB  1 
ATOM   3499 C CG  . MET B 1 160 ? 12.69500  5.03400   24.37200  1.000 11.17000 ? 162 MET B CG  1 
ATOM   3500 S SD  . MET B 1 160 ? 13.65800  4.13500   25.59900  1.000 14.72000 ? 162 MET B SD  1 
ATOM   3501 C CE  . MET B 1 160 ? 12.67100  2.64000   25.79300  1.000 13.12000 ? 162 MET B CE  1 
ATOM   3502 N N   . HIS B 1 161 ? 10.75600  7.15400   22.78600  1.000 7.17000  ? 163 HIS B N   1 
ATOM   3503 C CA  . HIS B 1 161 ? 10.38000  8.56100   22.77100  1.000 8.24000  ? 163 HIS B CA  1 
ATOM   3504 C C   . HIS B 1 161 ? 11.12500  9.35100   23.84500  1.000 9.03000  ? 163 HIS B C   1 
ATOM   3505 O O   . HIS B 1 161 ? 11.19000  8.92200   24.99600  1.000 8.43000  ? 163 HIS B O   1 
ATOM   3506 C CB  . HIS B 1 161 ? 8.88100   8.70700   22.97100  1.000 10.63000 ? 163 HIS B CB  1 
ATOM   3507 C CG  . HIS B 1 161 ? 8.43800   10.12100  22.91200  1.000 6.55000  ? 163 HIS B CG  1 
ATOM   3508 N ND1 . HIS B 1 161 ? 8.79200   10.95000  21.87400  1.000 8.91000  ? 163 HIS B ND1 1 
ATOM   3509 C CD2 . HIS B 1 161 ? 7.76300   10.88400  23.79900  1.000 9.94000  ? 163 HIS B CD2 1 
ATOM   3510 C CE1 . HIS B 1 161 ? 8.30600   12.16000  22.09900  1.000 9.90000  ? 163 HIS B CE1 1 
ATOM   3511 N NE2 . HIS B 1 161 ? 7.68600   12.14900  23.26400  1.000 10.43000 ? 163 HIS B NE2 1 
ATOM   3512 N N   . HIS B 1 162 ? 11.66400  10.52800  23.47100  1.000 8.37000  ? 164 HIS B N   1 
ATOM   3513 C CA  . HIS B 1 162 ? 12.41500  11.36400  24.41400  1.000 9.53000  ? 164 HIS B CA  1 
ATOM   3514 C C   . HIS B 1 162 ? 11.89800  12.79200  24.55100  1.000 10.07000 ? 164 HIS B C   1 
ATOM   3515 O O   . HIS B 1 162 ? 11.95300  13.34400  25.65200  1.000 12.28000 ? 164 HIS B O   1 
ATOM   3516 C CB  . HIS B 1 162 ? 13.90700  11.44500  24.02800  1.000 10.55000 ? 164 HIS B CB  1 
ATOM   3517 C CG  . HIS B 1 162 ? 14.66600  10.17700  24.23800  1.000 11.63000 ? 164 HIS B CG  1 
ATOM   3518 N ND1 . HIS B 1 162 ? 15.75100  10.08800  25.08500  1.000 11.88000 ? 164 HIS B ND1 1 
ATOM   3519 C CD2 . HIS B 1 162 ? 14.52300  8.95200   23.67500  1.000 9.22000  ? 164 HIS B CD2 1 
ATOM   3520 C CE1 . HIS B 1 162 ? 16.22600  8.85600   25.05500  1.000 14.25000 ? 164 HIS B CE1 1 
ATOM   3521 N NE2 . HIS B 1 162 ? 15.49400  8.14400   24.21300  1.000 12.19000 ? 164 HIS B NE2 1 
ATOM   3522 N N   . MET B 1 163 ? 11.43200  13.44000  23.48300  1.000 10.45000 ? 165 MET B N   1 
ATOM   3523 C CA  . MET B 1 163 ? 11.13200  14.86100  23.64300  1.000 15.93000 ? 165 MET B CA  1 
ATOM   3524 C C   . MET B 1 163 ? 10.17700  15.37500  22.58000  1.000 12.53000 ? 165 MET B C   1 
ATOM   3525 O O   . MET B 1 163 ? 9.94200   14.73800  21.54900  1.000 11.15000 ? 165 MET B O   1 
ATOM   3526 C CB  . MET B 1 163 ? 12.40200  15.70900  23.62200  1.000 17.11000 ? 165 MET B CB  1 
ATOM   3527 C CG  . MET B 1 163 ? 13.32400  15.44200  22.50200  1.000 16.09000 ? 165 MET B CG  1 
ATOM   3528 S SD  . MET B 1 163 ? 14.93400  16.17000  22.99200  1.000 37.12000 ? 165 MET B SD  1 
ATOM   3529 C CE  . MET B 1 163 ? 14.49900  17.90000  22.91800  1.000 25.39000 ? 165 MET B CE  1 
ATOM   3530 N N   . GLU B 1 164 ? 9.64000   16.56600  22.85400  1.000 10.55000 ? 166 GLU B N   1 
ATOM   3531 C CA  . GLU B 1 164 ? 8.74200   17.27700  21.94800  1.000 14.48000 ? 166 GLU B CA  1 
ATOM   3532 C C   . GLU B 1 164 ? 9.40500   18.59100  21.56100  1.000 16.17000 ? 166 GLU B C   1 
ATOM   3533 O O   . GLU B 1 164 ? 9.78500   19.37500  22.43600  1.000 18.87000 ? 166 GLU B O   1 
ATOM   3534 C CB  . GLU B 1 164 ? 7.37500   17.54900  22.59100  1.000 14.84000 ? 166 GLU B CB  1 
ATOM   3535 C CG  . GLU B 1 164 ? 6.39400   18.21900  21.60500  1.000 16.99000 ? 166 GLU B CG  1 
ATOM   3536 C CD  . GLU B 1 164 ? 4.92900   18.16300  22.03900  1.000 25.24000 ? 166 GLU B CD  1 
ATOM   3537 O OE1 . GLU B 1 164 ? 4.21800   19.17800  21.85700  1.000 35.25000 ? 166 GLU B OE1 1 
ATOM   3538 O OE2 . GLU B 1 164 ? 4.47400   17.11500  22.54000  1.000 25.88000 ? 166 GLU B OE2 1 
ATOM   3539 N N   . LEU B 1 165 ? 9.55700   18.82000  20.27100  1.000 13.68000 ? 167 LEU B N   1 
ATOM   3540 C CA  . LEU B 1 165 ? 10.16400  20.05600  19.79700  1.000 16.23000 ? 167 LEU B CA  1 
ATOM   3541 C C   . LEU B 1 165 ? 9.16700   21.20800  19.91800  1.000 20.11000 ? 167 LEU B C   1 
ATOM   3542 O O   . LEU B 1 165 ? 7.95900   20.98200  20.04700  1.000 19.24000 ? 167 LEU B O   1 
ATOM   3543 C CB  . LEU B 1 165 ? 10.60900  19.89900  18.34700  1.000 14.73000 ? 167 LEU B CB  1 
ATOM   3544 C CG  . LEU B 1 165 ? 11.56100  18.74500  18.01000  1.000 15.69000 ? 167 LEU B CG  1 
ATOM   3545 C CD1 . LEU B 1 165 ? 12.15100  18.93900  16.60700  1.000 14.22000 ? 167 LEU B CD1 1 
ATOM   3546 C CD2 . LEU B 1 165 ? 12.65800  18.58700  19.07800  1.000 17.17000 ? 167 LEU B CD2 1 
ATOM   3547 N N   . PRO B 1 166 ? 9.64600   22.45500  19.90500  1.000 21.40000 ? 168 PRO B N   1 
ATOM   3548 C CA  . PRO B 1 166 ? 8.70400   23.59000  20.01300  1.000 22.59000 ? 168 PRO B CA  1 
ATOM   3549 C C   . PRO B 1 166 ? 7.61400   23.58800  18.95600  1.000 22.83000 ? 168 PRO B C   1 
ATOM   3550 O O   . PRO B 1 166 ? 6.52400   24.11200  19.21400  1.000 24.87000 ? 168 PRO B O   1 
ATOM   3551 C CB  . PRO B 1 166 ? 9.61100   24.82900  19.90100  1.000 21.35000 ? 168 PRO B CB  1 
ATOM   3552 C CG  . PRO B 1 166 ? 11.03100  24.31600  19.74000  1.000 27.97000 ? 168 PRO B CG  1 
ATOM   3553 C CD  . PRO B 1 166 ? 11.03700  22.86800  20.15400  1.000 22.31000 ? 168 PRO B CD  1 
ATOM   3554 N N   . THR B 1 167 ? 7.85300   23.00300  17.78300  1.000 21.51000 ? 169 THR B N   1 
ATOM   3555 C CA  . THR B 1 167 ? 6.81600   22.95000  16.75900  1.000 20.93000 ? 169 THR B CA  1 
ATOM   3556 C C   . THR B 1 167 ? 5.77300   21.87500  17.03400  1.000 20.87000 ? 169 THR B C   1 
ATOM   3557 O O   . THR B 1 167 ? 4.81300   21.76400  16.27600  1.000 22.71000 ? 169 THR B O   1 
ATOM   3558 C CB  . THR B 1 167 ? 7.43000   22.70600  15.38200  1.000 24.09000 ? 169 THR B CB  1 
ATOM   3559 O OG1 . THR B 1 167 ? 8.16400   21.47200  15.40500  1.000 25.15000 ? 169 THR B OG1 1 
ATOM   3560 C CG2 . THR B 1 167 ? 8.36900   23.85100  15.00800  1.000 24.43000 ? 169 THR B CG2 1 
ATOM   3561 N N   . GLY B 1 168 ? 5.94300   21.07800  18.08600  1.000 22.05000 ? 170 GLY B N   1 
ATOM   3562 C CA  . GLY B 1 168 ? 5.00200   20.03400  18.40500  1.000 18.86000 ? 170 GLY B CA  1 
ATOM   3563 C C   . GLY B 1 168 ? 5.29100   18.68300  17.78000  1.000 17.09000 ? 170 GLY B C   1 
ATOM   3564 O O   . GLY B 1 168 ? 4.55000   17.73000  18.05200  1.000 20.40000 ? 170 GLY B O   1 
ATOM   3565 N N   . VAL B 1 169 ? 6.32800   18.56500  16.95000  1.000 14.14000 ? 171 VAL B N   1 
ATOM   3566 C CA  . VAL B 1 169 ? 6.76200   17.25600  16.45900  1.000 14.22000 ? 171 VAL B CA  1 
ATOM   3567 C C   . VAL B 1 169 ? 7.66700   16.62200  17.51300  1.000 15.35000 ? 171 VAL B C   1 
ATOM   3568 O O   . VAL B 1 169 ? 8.03300   17.26700  18.50000  1.000 12.56000 ? 171 VAL B O   1 
ATOM   3569 C CB  . VAL B 1 169 ? 7.48500   17.36300  15.11000  1.000 13.96000 ? 171 VAL B CB  1 
ATOM   3570 C CG1 . VAL B 1 169 ? 6.54600   17.96800  14.05300  1.000 20.37000 ? 171 VAL B CG1 1 
ATOM   3571 C CG2 . VAL B 1 169 ? 8.75900   18.20400  15.27300  1.000 12.99000 ? 171 VAL B CG2 1 
ATOM   3572 N N   . HIS B 1 170 ? 8.05900   15.36900  17.30300  1.000 13.73000 ? 172 HIS B N   1 
ATOM   3573 C CA  . HIS B 1 170 ? 8.68400   14.60600  18.37000  1.000 13.40000 ? 172 HIS B CA  1 
ATOM   3574 C C   . HIS B 1 170 ? 10.00400  14.01300  17.90800  1.000 10.73000 ? 172 HIS B C   1 
ATOM   3575 O O   . HIS B 1 170 ? 10.25900  13.83600  16.71500  1.000 12.92000 ? 172 HIS B O   1 
ATOM   3576 C CB  . HIS B 1 170 ? 7.73200   13.52700  18.87600  1.000 13.53000 ? 172 HIS B CB  1 
ATOM   3577 C CG  . HIS B 1 170 ? 6.46000   14.09900  19.41100  1.000 16.45000 ? 172 HIS B CG  1 
ATOM   3578 N ND1 . HIS B 1 170 ? 5.27800   14.08800  18.69800  1.000 16.55000 ? 172 HIS B ND1 1 
ATOM   3579 C CD2 . HIS B 1 170 ? 6.20200   14.75500  20.56600  1.000 13.84000 ? 172 HIS B CD2 1 
ATOM   3580 C CE1 . HIS B 1 170 ? 4.33900   14.69200  19.40800  1.000 17.09000 ? 172 HIS B CE1 1 
ATOM   3581 N NE2 . HIS B 1 170 ? 4.87600   15.11000  20.54200  1.000 17.59000 ? 172 HIS B NE2 1 
ATOM   3582 N N   . ALA B 1 171 ? 10.84900  13.72200  18.88700  1.000 9.72000  ? 173 ALA B N   1 
ATOM   3583 C CA  . ALA B 1 171 ? 12.19800  13.26600  18.62600  1.000 8.71000  ? 173 ALA B CA  1 
ATOM   3584 C C   . ALA B 1 171 ? 12.53900  12.17600  19.62700  1.000 10.57000 ? 173 ALA B C   1 
ATOM   3585 O O   . ALA B 1 171 ? 12.10800  12.22400  20.78100  1.000 8.13000  ? 173 ALA B O   1 
ATOM   3586 C CB  . ALA B 1 171 ? 13.20200  14.42500  18.73300  1.000 13.73000 ? 173 ALA B CB  1 
ATOM   3587 N N   . GLY B 1 172 ? 13.29700  11.20100  19.17600  1.000 7.88000  ? 174 GLY B N   1 
ATOM   3588 C CA  . GLY B 1 172 ? 13.72500  10.14000  20.04900  1.000 10.20000 ? 174 GLY B CA  1 
ATOM   3589 C C   . GLY B 1 172 ? 14.85200  9.36400   19.43600  1.000 9.67000  ? 174 GLY B C   1 
ATOM   3590 O O   . GLY B 1 172 ? 15.49800  9.80600   18.48200  1.000 9.11000  ? 174 GLY B O   1 
ATOM   3591 N N   . THR B 1 173 ? 15.08500  8.19000   20.00000  1.000 8.46000  ? 175 THR B N   1 
ATOM   3592 C CA  . THR B 1 173 ? 16.24900  7.39600   19.67900  1.000 9.07000  ? 175 THR B CA  1 
ATOM   3593 C C   . THR B 1 173 ? 15.82600  6.03300   19.15100  1.000 10.17000 ? 175 THR B C   1 
ATOM   3594 O O   . THR B 1 173 ? 14.67100  5.61100   19.27900  1.000 8.85000  ? 175 THR B O   1 
ATOM   3595 C CB  . THR B 1 173 ? 17.13700  7.21700   20.92000  1.000 10.45000 ? 175 THR B CB  1 
ATOM   3596 O OG1 . THR B 1 173 ? 16.43300  6.42300   21.88300  1.000 10.86000 ? 175 THR B OG1 1 
ATOM   3597 C CG2 . THR B 1 173 ? 17.45700  8.57100   21.51900  1.000 10.20000 ? 175 THR B CG2 1 
ATOM   3598 N N   . ASP B 1 174 ? 16.79800  5.32000   18.59500  1.000 8.10000  ? 176 ASP B N   1 
ATOM   3599 C CA  . ASP B 1 174 ? 16.59200  3.89500   18.44600  1.000 12.68000 ? 176 ASP B CA  1 
ATOM   3600 C C   . ASP B 1 174 ? 16.86000  3.22100   19.79200  1.000 11.52000 ? 176 ASP B C   1 
ATOM   3601 O O   . ASP B 1 174 ? 17.14300  3.87600   20.80800  1.000 11.12000 ? 176 ASP B O   1 
ATOM   3602 C CB  . ASP B 1 174 ? 17.46000  3.33900   17.31300  1.000 12.27000 ? 176 ASP B CB  1 
ATOM   3603 C CG  . ASP B 1 174 ? 18.94900  3.57800   17.52800  1.000 15.74000 ? 176 ASP B CG  1 
ATOM   3604 O OD1 . ASP B 1 174 ? 19.39500  3.69200   18.69200  1.000 15.70000 ? 176 ASP B OD1 1 
ATOM   3605 O OD2 . ASP B 1 174 ? 19.68200  3.64500   16.51900  1.000 17.78000 ? 176 ASP B OD2 1 
ATOM   3606 N N   . LEU B 1 175 ? 16.80800  1.90200   19.81100  1.000 10.20000 ? 177 LEU B N   1 
ATOM   3607 C CA  . LEU B 1 175 ? 16.95600  1.23100   21.09000  1.000 14.32000 ? 177 LEU B CA  1 
ATOM   3608 C C   . LEU B 1 175 ? 18.41800  1.01600   21.45200  1.000 17.13000 ? 177 LEU B C   1 
ATOM   3609 O O   . LEU B 1 175 ? 18.70300  0.49200   22.53200  1.000 16.24000 ? 177 LEU B O   1 
ATOM   3610 C CB  . LEU B 1 175 ? 16.19100  -0.08900  21.09200  1.000 15.69000 ? 177 LEU B CB  1 
ATOM   3611 C CG  . LEU B 1 175 ? 14.76400  0.02100   21.65200  1.000 12.73000 ? 177 LEU B CG  1 
ATOM   3612 C CD1 . LEU B 1 175 ? 14.80700  0.47400   23.10000  1.000 17.74000 ? 177 LEU B CD1 1 
ATOM   3613 C CD2 . LEU B 1 175 ? 13.92300  0.96700   20.79600  1.000 12.45000 ? 177 LEU B CD2 1 
ATOM   3614 N N   . GLU B 1 176 ? 19.34300  1.43100   20.59300  1.000 14.20000 ? 178 GLU B N   1 
ATOM   3615 C CA  . GLU B 1 176 ? 20.73100  1.57400   21.01500  1.000 17.83000 ? 178 GLU B CA  1 
ATOM   3616 C C   . GLU B 1 176 ? 21.00500  2.94900   21.59500  1.000 15.12000 ? 178 GLU B C   1 
ATOM   3617 O O   . GLU B 1 176 ? 22.13700  3.22300   22.00600  1.000 19.71000 ? 178 GLU B O   1 
ATOM   3618 C CB  . GLU B 1 176 ? 21.67800  1.30000   19.84800  1.000 21.45000 ? 178 GLU B CB  1 
ATOM   3619 C CG  . GLU B 1 176 ? 21.48200  -0.04600  19.19200  1.000 24.00000 ? 178 GLU B CG  1 
ATOM   3620 C CD  . GLU B 1 176 ? 22.51900  -0.30300  18.10900  1.000 37.12000 ? 178 GLU B CD  1 
ATOM   3621 O OE1 . GLU B 1 176 ? 22.85000  -1.48300  17.85900  1.000 43.22000 ? 178 GLU B OE1 1 
ATOM   3622 O OE2 . GLU B 1 176 ? 23.02000  0.68500   17.52100  1.000 39.36000 ? 178 GLU B OE2 1 
ATOM   3623 N N   . GLY B 1 177 ? 19.99400  3.80800   21.64600  1.000 10.90000 ? 179 GLY B N   1 
ATOM   3624 C CA  . GLY B 1 177 ? 20.10900  5.09900   22.27200  1.000 11.99000 ? 179 GLY B CA  1 
ATOM   3625 C C   . GLY B 1 177 ? 20.64000  6.20400   21.38900  1.000 12.95000 ? 179 GLY B C   1 
ATOM   3626 O O   . GLY B 1 177 ? 20.99000  7.25900   21.90600  1.000 10.34000 ? 179 GLY B O   1 
ATOM   3627 N N   . ASN B 1 178 ? 20.69500  6.00800   20.07800  1.000 11.74000 ? 180 ASN B N   1 
ATOM   3628 C CA  . ASN B 1 178 ? 21.16400  7.04800   19.18000  1.000 10.77000 ? 180 ASN B CA  1 
ATOM   3629 C C   . ASN B 1 178 ? 19.96500  7.82200   18.65200  1.000 11.90000 ? 180 ASN B C   1 
ATOM   3630 O O   . ASN B 1 178 ? 19.02300  7.22300   18.12600  1.000 10.68000 ? 180 ASN B O   1 
ATOM   3631 C CB  . ASN B 1 178 ? 21.96500  6.44100   18.02800  1.000 12.64000 ? 180 ASN B CB  1 
ATOM   3632 C CG  . ASN B 1 178 ? 23.35600  5.98300   18.46900  1.000 20.83000 ? 180 ASN B CG  1 
ATOM   3633 O OD1 . ASN B 1 178 ? 24.05000  6.70300   19.17600  1.000 18.66000 ? 180 ASN B OD1 1 
ATOM   3634 N ND2 . ASN B 1 178 ? 23.74800  4.77200   18.07000  1.000 22.95000 ? 180 ASN B ND2 1 
ATOM   3635 N N   . PHE B 1 179 ? 19.99100  9.14300   18.80900  1.000 9.09000  ? 181 PHE B N   1 
ATOM   3636 C CA  . PHE B 1 179 ? 18.87500  9.92900   18.30100  1.000 12.41000 ? 181 PHE B CA  1 
ATOM   3637 C C   . PHE B 1 179 ? 18.72800  9.74500   16.79700  1.000 11.35000 ? 181 PHE B C   1 
ATOM   3638 O O   . PHE B 1 179 ? 19.69800  9.54000   16.06700  1.000 13.75000 ? 181 PHE B O   1 
ATOM   3639 C CB  . PHE B 1 179 ? 19.05000  11.40400  18.62000  1.000 12.55000 ? 181 PHE B CB  1 
ATOM   3640 C CG  . PHE B 1 179 ? 18.38000  11.81900  19.89000  1.000 12.03000 ? 181 PHE B CG  1 
ATOM   3641 C CD1 . PHE B 1 179 ? 19.05300  11.73500  21.10400  1.000 11.76000 ? 181 PHE B CD1 1 
ATOM   3642 C CD2 . PHE B 1 179 ? 17.07100  12.26600  19.87600  1.000 11.30000 ? 181 PHE B CD2 1 
ATOM   3643 C CE1 . PHE B 1 179 ? 18.42000  12.11300  22.27400  1.000 13.48000 ? 181 PHE B CE1 1 
ATOM   3644 C CE2 . PHE B 1 179 ? 16.43200  12.63800  21.03000  1.000 11.72000 ? 181 PHE B CE2 1 
ATOM   3645 C CZ  . PHE B 1 179 ? 17.09900  12.56400  22.23800  1.000 13.30000 ? 181 PHE B CZ  1 
ATOM   3646 N N   . TYR B 1 180 ? 17.48900  9.77300   16.34600  1.000 12.84000 ? 182 TYR B N   1 
ATOM   3647 C CA  . TYR B 1 180 ? 17.21500  10.08800  14.95700  1.000 13.66000 ? 182 TYR B CA  1 
ATOM   3648 C C   . TYR B 1 180 ? 17.34700  11.59700  14.80600  1.000 10.66000 ? 182 TYR B C   1 
ATOM   3649 O O   . TYR B 1 180 ? 16.73500  12.35000  15.56100  1.000 11.56000 ? 182 TYR B O   1 
ATOM   3650 C CB  . TYR B 1 180 ? 15.81300  9.62000   14.56900  1.000 10.79000 ? 182 TYR B CB  1 
ATOM   3651 C CG  . TYR B 1 180 ? 15.65700  8.11000   14.54100  1.000 13.01000 ? 182 TYR B CG  1 
ATOM   3652 C CD1 . TYR B 1 180 ? 16.04600  7.37200   13.43100  1.000 12.17000 ? 182 TYR B CD1 1 
ATOM   3653 C CD2 . TYR B 1 180 ? 15.12500  7.42700   15.63000  1.000 12.77000 ? 182 TYR B CD2 1 
ATOM   3654 C CE1 . TYR B 1 180 ? 15.90100  5.98200   13.39600  1.000 15.20000 ? 182 TYR B CE1 1 
ATOM   3655 C CE2 . TYR B 1 180 ? 14.97900  6.03500   15.60900  1.000 13.59000 ? 182 TYR B CE2 1 
ATOM   3656 C CZ  . TYR B 1 180 ? 15.37400  5.32500   14.48800  1.000 13.18000 ? 182 TYR B CZ  1 
ATOM   3657 O OH  . TYR B 1 180 ? 15.23200  3.96200   14.44700  1.000 12.68000 ? 182 TYR B OH  1 
ATOM   3658 N N   . GLY B 1 181 ? 18.16300  12.03900  13.86200  1.000 13.29000 ? 183 GLY B N   1 
ATOM   3659 C CA  . GLY B 1 181 ? 18.28100  13.45400  13.59600  1.000 12.05000 ? 183 GLY B CA  1 
ATOM   3660 C C   . GLY B 1 181 ? 19.32000  14.12900  14.46100  1.000 15.12000 ? 183 GLY B C   1 
ATOM   3661 O O   . GLY B 1 181 ? 19.99600  13.49500  15.28100  1.000 14.25000 ? 183 GLY B O   1 
ATOM   3662 N N   . PRO B 1 182 ? 19.42900  15.44700  14.31700  1.000 12.02000 ? 184 PRO B N   1 
ATOM   3663 C CA  . PRO B 1 182 ? 20.50400  16.19300  14.98900  1.000 16.57000 ? 184 PRO B CA  1 
ATOM   3664 C C   . PRO B 1 182 ? 20.15700  16.60900  16.40700  1.000 14.45000 ? 184 PRO B C   1 
ATOM   3665 O O   . PRO B 1 182 ? 20.65600  17.62800  16.89200  1.000 16.38000 ? 184 PRO B O   1 
ATOM   3666 C CB  . PRO B 1 182 ? 20.66000  17.43000  14.09700  1.000 15.08000 ? 184 PRO B CB  1 
ATOM   3667 C CG  . PRO B 1 182 ? 19.23300  17.69800  13.64200  1.000 15.26000 ? 184 PRO B CG  1 
ATOM   3668 C CD  . PRO B 1 182 ? 18.61500  16.31400  13.44300  1.000 13.05000 ? 184 PRO B CD  1 
ATOM   3669 N N   . PHE B 1 183 ? 19.29000  15.86300  17.07400  1.000 11.26000 ? 185 PHE B N   1 
ATOM   3670 C CA  . PHE B 1 183 ? 18.76500  16.33100  18.34400  1.000 12.44000 ? 185 PHE B CA  1 
ATOM   3671 C C   . PHE B 1 183 ? 19.59700  15.79500  19.49300  1.000 11.61000 ? 185 PHE B C   1 
ATOM   3672 O O   . PHE B 1 183 ? 20.31800  14.80100  19.36200  1.000 13.44000 ? 185 PHE B O   1 
ATOM   3673 C CB  . PHE B 1 183 ? 17.30400  15.92600  18.48800  1.000 10.63000 ? 185 PHE B CB  1 
ATOM   3674 C CG  . PHE B 1 183 ? 16.47800  16.33100  17.30700  1.000 13.43000 ? 185 PHE B CG  1 
ATOM   3675 C CD1 . PHE B 1 183 ? 16.23600  17.67600  17.05100  1.000 12.81000 ? 185 PHE B CD1 1 
ATOM   3676 C CD2 . PHE B 1 183 ? 16.00300  15.37600  16.41800  1.000 12.98000 ? 185 PHE B CD2 1 
ATOM   3677 C CE1 . PHE B 1 183 ? 15.50000  18.05900  15.93700  1.000 14.02000 ? 185 PHE B CE1 1 
ATOM   3678 C CE2 . PHE B 1 183 ? 15.25000  15.75200  15.30800  1.000 13.10000 ? 185 PHE B CE2 1 
ATOM   3679 C CZ  . PHE B 1 183 ? 15.00300  17.09100  15.07100  1.000 15.58000 ? 185 PHE B CZ  1 
ATOM   3680 N N   . VAL B 1 184 ? 19.49300  16.47400  20.62500  1.000 13.52000 ? 186 VAL B N   1 
ATOM   3681 C CA  . VAL B 1 184 ? 20.29400  16.15900  21.80100  1.000 12.67000 ? 186 VAL B CA  1 
ATOM   3682 C C   . VAL B 1 184 ? 19.37600  16.16100  23.00500  1.000 12.41000 ? 186 VAL B C   1 
ATOM   3683 O O   . VAL B 1 184 ? 18.43000  16.95500  23.07500  1.000 13.26000 ? 186 VAL B O   1 
ATOM   3684 C CB  . VAL B 1 184 ? 21.44300  17.17400  21.99800  1.000 15.66000 ? 186 VAL B CB  1 
ATOM   3685 C CG1 . VAL B 1 184 ? 22.40900  17.11000  20.83600  1.000 15.03000 ? 186 VAL B CG1 1 
ATOM   3686 C CG2 . VAL B 1 184 ? 20.89500  18.57000  22.08700  1.000 18.12000 ? 186 VAL B CG2 1 
ATOM   3687 N N   . ASP B 1 185 ? 19.66100  15.28300  23.97500  1.000 12.89000 ? 187 ASP B N   1 
ATOM   3688 C CA  . ASP B 1 185 ? 18.83300  15.24400  25.17900  1.000 13.55000 ? 187 ASP B CA  1 
ATOM   3689 C C   . ASP B 1 185 ? 19.37700  16.23800  26.20300  1.000 16.06000 ? 187 ASP B C   1 
ATOM   3690 O O   . ASP B 1 185 ? 19.91500  15.88900  27.25800  1.000 16.05000 ? 187 ASP B O   1 
ATOM   3691 C CB  . ASP B 1 185 ? 18.70800  13.83000  25.75100  1.000 13.44000 ? 187 ASP B CB  1 
ATOM   3692 C CG  . ASP B 1 185 ? 20.01900  13.08400  25.85700  1.000 12.96000 ? 187 ASP B CG  1 
ATOM   3693 O OD1 . ASP B 1 185 ? 21.05500  13.53600  25.32700  1.000 17.11000 ? 187 ASP B OD1 1 
ATOM   3694 O OD2 . ASP B 1 185 ? 19.99700  11.99000  26.46700  1.000 14.54000 ? 187 ASP B OD2 1 
ATOM   3695 N N   . ARG B 1 186 ? 19.21300  17.50700  25.86100  1.000 18.02000 ? 188 ARG B N   1 
ATOM   3696 C CA  . ARG B 1 186 ? 19.29300  18.58400  26.83500  1.000 22.23000 ? 188 ARG B CA  1 
ATOM   3697 C C   . ARG B 1 186 ? 18.03500  19.42100  26.69000  1.000 22.67000 ? 188 ARG B C   1 
ATOM   3698 O O   . ARG B 1 186 ? 17.47700  19.53200  25.59100  1.000 15.44000 ? 188 ARG B O   1 
ATOM   3699 C CB  . ARG B 1 186 ? 20.55300  19.43800  26.63800  1.000 19.52000 ? 188 ARG B CB  1 
ATOM   3700 C CG  . ARG B 1 186 ? 20.67700  20.03800  25.25000  1.000 22.11000 ? 188 ARG B CG  1 
ATOM   3701 C CD  . ARG B 1 186 ? 21.75400  21.12100  25.18300  1.000 24.66000 ? 188 ARG B CD  1 
ATOM   3702 N NE  . ARG B 1 186 ? 23.06000  20.60800  25.58900  1.000 23.91000 ? 188 ARG B NE  1 
ATOM   3703 C CZ  . ARG B 1 186 ? 24.17800  21.32700  25.59100  1.000 23.24000 ? 188 ARG B CZ  1 
ATOM   3704 N NH1 . ARG B 1 186 ? 25.31600  20.77200  25.98200  1.000 22.88000 ? 188 ARG B NH1 1 
ATOM   3705 N NH2 . ARG B 1 186 ? 24.15200  22.60200  25.20600  1.000 24.36000 ? 188 ARG B NH2 1 
ATOM   3706 N N   . GLN B 1 187 ? 17.57500  19.99800  27.80400  1.000 22.09000 ? 189 GLN B N   1 
ATOM   3707 C CA  . GLN B 1 187 ? 16.32100  20.74900  27.77100  1.000 24.52000 ? 189 GLN B CA  1 
ATOM   3708 C C   . GLN B 1 187 ? 16.60600  22.10600  27.15100  1.000 26.51000 ? 189 GLN B C   1 
ATOM   3709 O O   . GLN B 1 187 ? 16.89900  23.08700  27.83400  1.000 25.82000 ? 189 GLN B O   1 
ATOM   3710 C CB  . GLN B 1 187 ? 15.69600  20.88600  29.15300  1.000 31.74000 ? 189 GLN B CB  1 
ATOM   3711 C CG  . GLN B 1 187 ? 14.27000  21.42400  29.06500  1.000 34.56000 ? 189 GLN B CG  1 
ATOM   3712 C CD  . GLN B 1 187 ? 13.62100  21.66900  30.41000  1.000 38.73000 ? 189 GLN B CD  1 
ATOM   3713 O OE1 . GLN B 1 187 ? 14.07800  21.17000  31.43800  1.000 49.86000 ? 189 GLN B OE1 1 
ATOM   3714 N NE2 . GLN B 1 187 ? 12.54300  22.44500  30.41000  1.000 36.84000 ? 189 GLN B NE2 1 
ATOM   3715 N N   . THR B 1 188 ? 16.52800  22.14400  25.82900  1.000 24.68000 ? 190 THR B N   1 
ATOM   3716 C CA  . THR B 1 188 ? 16.71000  23.34900  25.04800  1.000 24.70000 ? 190 THR B CA  1 
ATOM   3717 C C   . THR B 1 188 ? 15.77400  23.28200  23.85200  1.000 24.79000 ? 190 THR B C   1 
ATOM   3718 O O   . THR B 1 188 ? 15.39100  22.19500  23.40800  1.000 23.13000 ? 190 THR B O   1 
ATOM   3719 C CB  . THR B 1 188 ? 18.15400  23.48900  24.57700  1.000 29.29000 ? 190 THR B CB  1 
ATOM   3720 O OG1 . THR B 1 188 ? 18.31000  24.74000  23.90200  1.000 41.40000 ? 190 THR B OG1 1 
ATOM   3721 C CG2 . THR B 1 188 ? 18.48300  22.36400  23.62500  1.000 18.48000 ? 190 THR B CG2 1 
ATOM   3722 N N   . ALA B 1 189 ? 15.40400  24.45200  23.34000  1.000 22.18000 ? 191 ALA B N   1 
ATOM   3723 C CA  . ALA B 1 189 ? 14.52800  24.52200  22.17700  1.000 21.96000 ? 191 ALA B CA  1 
ATOM   3724 C C   . ALA B 1 189 ? 15.31500  24.14700  20.93300  1.000 23.99000 ? 191 ALA B C   1 
ATOM   3725 O O   . ALA B 1 189 ? 16.29600  24.81100  20.58700  1.000 24.11000 ? 191 ALA B O   1 
ATOM   3726 C CB  . ALA B 1 189 ? 13.93700  25.92200  22.03300  1.000 28.69000 ? 191 ALA B CB  1 
ATOM   3727 N N   . GLN B 1 190 ? 14.89200  23.08400  20.25800  1.000 20.77000 ? 192 GLN B N   1 
ATOM   3728 C CA  . GLN B 1 190 ? 15.62200  22.55500  19.12000  1.000 17.20000 ? 192 GLN B CA  1 
ATOM   3729 C C   . GLN B 1 190 ? 14.73600  22.54300  17.88900  1.000 16.95000 ? 192 GLN B C   1 
ATOM   3730 O O   . GLN B 1 190 ? 13.60000  22.06200  17.94300  1.000 18.93000 ? 192 GLN B O   1 
ATOM   3731 C CB  . GLN B 1 190 ? 16.13800  21.15100  19.42700  1.000 18.71000 ? 192 GLN B CB  1 
ATOM   3732 C CG  . GLN B 1 190 ? 17.14900  21.18300  20.54900  1.000 17.85000 ? 192 GLN B CG  1 
ATOM   3733 C CD  . GLN B 1 190 ? 17.57400  19.81800  21.01500  1.000 16.54000 ? 192 GLN B CD  1 
ATOM   3734 O OE1 . GLN B 1 190 ? 18.03100  18.99500  20.21700  1.000 12.69000 ? 192 GLN B OE1 1 
ATOM   3735 N NE2 . GLN B 1 190 ? 17.45600  19.57200  22.32100  1.000 13.78000 ? 192 GLN B NE2 1 
ATOM   3736 N N   . ALA B 1 191 ? 15.26900  23.05400  16.78500  1.000 16.01000 ? 193 ALA B N   1 
ATOM   3737 C CA  . ALA B 1 191 ? 14.59200  23.05600  15.50000  1.000 19.08000 ? 193 ALA B CA  1 
ATOM   3738 C C   . ALA B 1 191 ? 15.09100  21.89900  14.65100  1.000 19.41000 ? 193 ALA B C   1 
ATOM   3739 O O   . ALA B 1 191 ? 16.26800  21.53200  14.71100  1.000 18.27000 ? 193 ALA B O   1 
ATOM   3740 C CB  . ALA B 1 191 ? 14.81900  24.37300  14.75100  1.000 22.42000 ? 193 ALA B CB  1 
ATOM   3741 N N   . ALA B 1 192 ? 14.18600  21.31800  13.87200  1.000 15.75000 ? 194 ALA B N   1 
ATOM   3742 C CA  . ALA B 1 192 ? 14.56900  20.29400  12.91400  1.000 17.44000 ? 194 ALA B CA  1 
ATOM   3743 C C   . ALA B 1 192 ? 15.01300  20.94100  11.61200  1.000 17.14000 ? 194 ALA B C   1 
ATOM   3744 O O   . ALA B 1 192 ? 14.73000  22.11200  11.34800  1.000 17.63000 ? 194 ALA B O   1 
ATOM   3745 C CB  . ALA B 1 192 ? 13.40400  19.34000  12.64400  1.000 19.66000 ? 194 ALA B CB  1 
ATOM   3746 N N   . GLY B 1 193 ? 15.71500  20.16300  10.79000  1.000 17.17000 ? 195 GLY B N   1 
ATOM   3747 C CA  . GLY B 1 193 ? 15.89600  20.55100  9.40300   1.000 23.19000 ? 195 GLY B CA  1 
ATOM   3748 C C   . GLY B 1 193 ? 14.56500  20.73200  8.69700   1.000 25.97000 ? 195 GLY B C   1 
ATOM   3749 O O   . GLY B 1 193 ? 13.51000  20.31200  9.17600   1.000 19.69000 ? 195 GLY B O   1 
ATOM   3750 N N   . THR B 1 194 ? 14.60000  21.39200  7.54100   1.000 26.28000 ? 196 THR B N   1 
ATOM   3751 C CA  . THR B 1 194 ? 13.35000  21.62100  6.82900   1.000 26.28000 ? 196 THR B CA  1 
ATOM   3752 C C   . THR B 1 194 ? 12.77000  20.28100  6.39600   1.000 20.54000 ? 196 THR B C   1 
ATOM   3753 O O   . THR B 1 194 ? 13.46700  19.43800  5.82500   1.000 23.19000 ? 196 THR B O   1 
ATOM   3754 C CB  . THR B 1 194 ? 13.56000  22.55300  5.63200   1.000 30.73000 ? 196 THR B CB  1 
ATOM   3755 O OG1 . THR B 1 194 ? 14.70900  22.14200  4.88400   1.000 35.06000 ? 196 THR B OG1 1 
ATOM   3756 C CG2 . THR B 1 194 ? 13.76500  23.98300  6.12000   1.000 24.23000 ? 196 THR B CG2 1 
ATOM   3757 N N   . ASP B 1 195 ? 11.50700  20.05400  6.72900   1.000 19.37000 ? 197 ASP B N   1 
ATOM   3758 C CA  . ASP B 1 195 ? 10.95800  18.76500  6.36800   1.000 20.59000 ? 197 ASP B CA  1 
ATOM   3759 C C   . ASP B 1 195 ? 10.60700  18.73800  4.88800   1.000 23.06000 ? 197 ASP B C   1 
ATOM   3760 O O   . ASP B 1 195 ? 10.45400  19.77300  4.23300   1.000 25.58000 ? 197 ASP B O   1 
ATOM   3761 C CB  . ASP B 1 195 ? 9.72500   18.42300  7.20200   1.000 18.03000 ? 197 ASP B CB  1 
ATOM   3762 C CG  . ASP B 1 195 ? 9.49900   16.91300  7.29300   1.000 20.78000 ? 197 ASP B CG  1 
ATOM   3763 O OD1 . ASP B 1 195 ? 10.42000  16.12900  6.91300   1.000 18.03000 ? 197 ASP B OD1 1 
ATOM   3764 O OD2 . ASP B 1 195 ? 8.40700   16.51400  7.74400   1.000 18.05000 ? 197 ASP B OD2 1 
ATOM   3765 N N   . THR B 1 196 ? 10.50000  17.52300  4.36500   1.000 19.73000 ? 198 THR B N   1 
ATOM   3766 C CA  . THR B 1 196 ? 10.14100  17.27900  2.97800   1.000 20.08000 ? 198 THR B CA  1 
ATOM   3767 C C   . THR B 1 196 ? 9.10900   16.16100  2.95800   1.000 20.06000 ? 198 THR B C   1 
ATOM   3768 O O   . THR B 1 196 ? 8.88200   15.47400  3.96100   1.000 19.25000 ? 198 THR B O   1 
ATOM   3769 C CB  . THR B 1 196 ? 11.36800  16.91600  2.13200   1.000 22.34000 ? 198 THR B CB  1 
ATOM   3770 O OG1 . THR B 1 196 ? 12.11700  15.89800  2.80100   1.000 24.55000 ? 198 THR B OG1 1 
ATOM   3771 C CG2 . THR B 1 196 ? 12.27500  18.14200  1.90700   1.000 20.63000 ? 198 THR B CG2 1 
ATOM   3772 N N   . THR B 1 197 ? 8.47600   15.98500  1.80800   1.000 18.50000 ? 199 THR B N   1 
ATOM   3773 C CA  . THR B 1 197 ? 7.41300   15.00200  1.65700   1.000 18.44000 ? 199 THR B CA  1 
ATOM   3774 C C   . THR B 1 197 ? 7.98100   13.69300  1.12000   1.000 16.91000 ? 199 THR B C   1 
ATOM   3775 O O   . THR B 1 197 ? 8.85900   13.69400  0.25200   1.000 16.21000 ? 199 THR B O   1 
ATOM   3776 C CB  . THR B 1 197 ? 6.32300   15.56600  0.74000   1.000 17.75000 ? 199 THR B CB  1 
ATOM   3777 O OG1 . THR B 1 197 ? 5.79900   16.77200  1.32600   1.000 17.18000 ? 199 THR B OG1 1 
ATOM   3778 C CG2 . THR B 1 197 ? 5.20000   14.57500  0.55400   1.000 20.27000 ? 199 THR B CG2 1 
ATOM   3779 N N   . ILE B 1 198 ? 7.50100   12.57100  1.66100   1.000 14.45000 ? 200 ILE B N   1 
ATOM   3780 C CA  . ILE B 1 198 ? 8.04100   11.25900  1.30000   1.000 13.65000 ? 200 ILE B CA  1 
ATOM   3781 C C   . ILE B 1 198 ? 7.36100   10.82000  0.00400   1.000 15.15000 ? 200 ILE B C   1 
ATOM   3782 O O   . ILE B 1 198 ? 6.25900   10.27600  0.03700   1.000 11.20000 ? 200 ILE B O   1 
ATOM   3783 C CB  . ILE B 1 198 ? 7.84200   10.22500  2.40900   1.000 12.42000 ? 200 ILE B CB  1 
ATOM   3784 C CG1 . ILE B 1 198 ? 8.41400   10.73400  3.74300   1.000 15.09000 ? 200 ILE B CG1 1 
ATOM   3785 C CG2 . ILE B 1 198 ? 8.47400   8.89500   1.99000   1.000 12.97000 ? 200 ILE B CG2 1 
ATOM   3786 C CD1 . ILE B 1 198 ? 7.72800   10.11100  4.99200   1.000 15.35000 ? 200 ILE B CD1 1 
ATOM   3787 N N   . THR B 1 199 ? 8.06800   10.98200  -1.12500  1.000 13.99000 ? 201 THR B N   1 
ATOM   3788 C CA  . THR B 1 199 ? 7.47400   10.85200  -2.45300  1.000 14.06000 ? 201 THR B CA  1 
ATOM   3789 C C   . THR B 1 199 ? 7.01900   9.42600   -2.74400  1.000 13.61000 ? 201 THR B C   1 
ATOM   3790 O O   . THR B 1 199 ? 5.90300   9.21300   -3.22700  1.000 14.23000 ? 201 THR B O   1 
ATOM   3791 C CB  . THR B 1 199 ? 8.47600   11.32000  -3.51300  1.000 15.52000 ? 201 THR B CB  1 
ATOM   3792 O OG1 . THR B 1 199 ? 8.90600   12.64900  -3.19800  1.000 14.62000 ? 201 THR B OG1 1 
ATOM   3793 C CG2 . THR B 1 199 ? 7.84000   11.30400  -4.91000  1.000 13.66000 ? 201 THR B CG2 1 
ATOM   3794 N N   . VAL B 1 200 ? 7.88200   8.43500   -2.50300  1.000 11.56000 ? 202 VAL B N   1 
ATOM   3795 C CA  . VAL B 1 200 ? 7.49500   7.05300   -2.79300  1.000 15.15000 ? 202 VAL B CA  1 
ATOM   3796 C C   . VAL B 1 200 ? 6.22500   6.67100   -2.02800  1.000 14.28000 ? 202 VAL B C   1 
ATOM   3797 O O   . VAL B 1 200 ? 5.40900   5.87500   -2.51700  1.000 14.78000 ? 202 VAL B O   1 
ATOM   3798 C CB  . VAL B 1 200 ? 8.67100   6.09700   -2.49000  1.000 18.13000 ? 202 VAL B CB  1 
ATOM   3799 C CG1 . VAL B 1 200 ? 8.95300   6.04700   -0.99800  1.000 14.24000 ? 202 VAL B CG1 1 
ATOM   3800 C CG2 . VAL B 1 200 ? 8.38200   4.69800   -3.03700  1.000 19.87000 ? 202 VAL B CG2 1 
ATOM   3801 N N   . ASN B 1 201 ? 6.01900   7.25700   -0.84000  1.000 14.41000 ? 203 ASN B N   1 
ATOM   3802 C CA  . ASN B 1 201 ? 4.83000   6.96400   -0.04100  1.000 16.18000 ? 203 ASN B CA  1 
ATOM   3803 C C   . ASN B 1 201 ? 3.58900   7.63100   -0.61600  1.000 14.07000 ? 203 ASN B C   1 
ATOM   3804 O O   . ASN B 1 201 ? 2.50200   7.04000   -0.60800  1.000 13.15000 ? 203 ASN B O   1 
ATOM   3805 C CB  . ASN B 1 201 ? 5.02600   7.43000   1.40300   1.000 15.37000 ? 203 ASN B CB  1 
ATOM   3806 C CG  . ASN B 1 201 ? 6.00200   6.55500   2.19100   1.000 14.07000 ? 203 ASN B CG  1 
ATOM   3807 O OD1 . ASN B 1 201 ? 6.60200   5.61100   1.66400   1.000 13.73000 ? 203 ASN B OD1 1 
ATOM   3808 N ND2 . ASN B 1 201 ? 6.16900   6.88600   3.46800   1.000 14.08000 ? 203 ASN B ND2 1 
ATOM   3809 N N   . VAL B 1 202 ? 3.71100   8.88400   -1.06100  1.000 12.00000 ? 204 VAL B N   1 
ATOM   3810 C CA  . VAL B 1 202 ? 2.57200   9.52900   -1.71100  1.000 14.99000 ? 204 VAL B CA  1 
ATOM   3811 C C   . VAL B 1 202 ? 2.11400   8.68800   -2.89700  1.000 15.40000 ? 204 VAL B C   1 
ATOM   3812 O O   . VAL B 1 202 ? 0.91400   8.47700   -3.10000  1.000 15.74000 ? 204 VAL B O   1 
ATOM   3813 C CB  . VAL B 1 202 ? 2.91900   10.97000  -2.13600  1.000 11.89000 ? 204 VAL B CB  1 
ATOM   3814 C CG1 . VAL B 1 202 ? 1.80500   11.55900  -3.00600  1.000 14.64000 ? 204 VAL B CG1 1 
ATOM   3815 C CG2 . VAL B 1 202 ? 3.11800   11.85500  -0.91900  1.000 15.86000 ? 204 VAL B CG2 1 
ATOM   3816 N N   . LEU B 1 203 ? 3.06600   8.15200   -3.66300  1.000 12.78000 ? 205 LEU B N   1 
ATOM   3817 C CA  . LEU B 1 203 ? 2.71100   7.33800   -4.82500  1.000 15.10000 ? 205 LEU B CA  1 
ATOM   3818 C C   . LEU B 1 203 ? 2.03000   6.03900   -4.40800  1.000 20.37000 ? 205 LEU B C   1 
ATOM   3819 O O   . LEU B 1 203 ? 1.05500   5.61300   -5.04100  1.000 17.85000 ? 205 LEU B O   1 
ATOM   3820 C CB  . LEU B 1 203 ? 3.95600   7.03900   -5.65800  1.000 10.39000 ? 205 LEU B CB  1 
ATOM   3821 C CG  . LEU B 1 203 ? 4.54900   8.26300   -6.35300  1.000 14.15000 ? 205 LEU B CG  1 
ATOM   3822 C CD1 . LEU B 1 203 ? 5.93000   7.93800   -6.88500  1.000 13.41000 ? 205 LEU B CD1 1 
ATOM   3823 C CD2 . LEU B 1 203 ? 3.60500   8.77800   -7.48800  1.000 15.59000 ? 205 LEU B CD2 1 
ATOM   3824 N N   . ALA B 1 204 ? 2.54900   5.37700   -3.36900  1.000 13.47000 ? 206 ALA B N   1 
ATOM   3825 C CA  . ALA B 1 204 ? 1.88800   4.17300   -2.86400  1.000 16.65000 ? 206 ALA B CA  1 
ATOM   3826 C C   . ALA B 1 204 ? 0.45400   4.48100   -2.47300  1.000 16.35000 ? 206 ALA B C   1 
ATOM   3827 O O   . ALA B 1 204 ? -0.46500  3.71700   -2.78400  1.000 25.34000 ? 206 ALA B O   1 
ATOM   3828 C CB  . ALA B 1 204 ? 2.66200   3.60300   -1.66900  1.000 19.12000 ? 206 ALA B CB  1 
ATOM   3829 N N   . TRP B 1 205 ? 0.24300   5.62500   -1.83500  1.000 15.19000 ? 207 TRP B N   1 
ATOM   3830 C CA  . TRP B 1 205 ? -1.08900  6.01200   -1.39400  1.000 19.77000 ? 207 TRP B CA  1 
ATOM   3831 C C   . TRP B 1 205 ? -1.99500  6.37100   -2.57700  1.000 25.91000 ? 207 TRP B C   1 
ATOM   3832 O O   . TRP B 1 205 ? -3.19800  6.07400   -2.55500  1.000 21.97000 ? 207 TRP B O   1 
ATOM   3833 C CB  . TRP B 1 205 ? -0.94800  7.15900   -0.41000  1.000 17.96000 ? 207 TRP B CB  1 
ATOM   3834 C CG  . TRP B 1 205 ? -2.18900  7.83300   -0.00200  1.000 23.57000 ? 207 TRP B CG  1 
ATOM   3835 C CD1 . TRP B 1 205 ? -3.10200  7.39600   0.91800   1.000 25.95000 ? 207 TRP B CD1 1 
ATOM   3836 C CD2 . TRP B 1 205 ? -2.63900  9.10800   -0.44300  1.000 22.23000 ? 207 TRP B CD2 1 
ATOM   3837 N NE1 . TRP B 1 205 ? -4.10500  8.31900   1.05600   1.000 26.23000 ? 207 TRP B NE1 1 
ATOM   3838 C CE2 . TRP B 1 205 ? -3.84700  9.38000   0.22900   1.000 27.93000 ? 207 TRP B CE2 1 
ATOM   3839 C CE3 . TRP B 1 205 ? -2.15800  10.03600  -1.36900  1.000 25.52000 ? 207 TRP B CE3 1 
ATOM   3840 C CZ2 . TRP B 1 205 ? -4.57100  10.54500  0.01600   1.000 29.84000 ? 207 TRP B CZ2 1 
ATOM   3841 C CZ3 . TRP B 1 205 ? -2.87000  11.20400  -1.57100  1.000 25.58000 ? 207 TRP B CZ3 1 
ATOM   3842 C CH2 . TRP B 1 205 ? -4.06600  11.44600  -0.88600  1.000 33.36000 ? 207 TRP B CH2 1 
ATOM   3843 N N   . LEU B 1 206 ? -1.43700  6.99000   -3.62700  1.000 21.08000 ? 208 LEU B N   1 
ATOM   3844 C CA  . LEU B 1 206 ? -2.20400  7.18100   -4.85900  1.000 21.53000 ? 208 LEU B CA  1 
ATOM   3845 C C   . LEU B 1 206 ? -2.64500  5.84900   -5.43900  1.000 24.72000 ? 208 LEU B C   1 
ATOM   3846 O O   . LEU B 1 206 ? -3.79500  5.70300   -5.86400  1.000 30.18000 ? 208 LEU B O   1 
ATOM   3847 C CB  . LEU B 1 206 ? -1.38600  7.96100   -5.89000  1.000 21.99000 ? 208 LEU B CB  1 
ATOM   3848 C CG  . LEU B 1 206 ? -1.17000  9.42600   -5.53800  1.000 21.18000 ? 208 LEU B CG  1 
ATOM   3849 C CD1 . LEU B 1 206 ? -0.41300  10.16900  -6.64100  1.000 18.72000 ? 208 LEU B CD1 1 
ATOM   3850 C CD2 . LEU B 1 206 ? -2.51300  10.08800  -5.26200  1.000 22.84000 ? 208 LEU B CD2 1 
ATOM   3851 N N   . TYR B 1 207 ? -1.74300  4.86600   -5.46900  1.000 22.66000 ? 209 TYR B N   1 
ATOM   3852 C CA  . TYR B 1 207 ? -2.10900  3.52800   -5.91600  1.000 26.96000 ? 209 TYR B CA  1 
ATOM   3853 C C   . TYR B 1 207 ? -3.18400  2.92200   -5.02100  1.000 32.99000 ? 209 TYR B C   1 
ATOM   3854 O O   . TYR B 1 207 ? -4.10200  2.24500   -5.50500  1.000 29.87000 ? 209 TYR B O   1 
ATOM   3855 C CB  . TYR B 1 207 ? -0.87900  2.62800   -5.92600  1.000 24.97000 ? 209 TYR B CB  1 
ATOM   3856 C CG  . TYR B 1 207 ? -0.02100  2.71400   -7.16200  1.000 30.04000 ? 209 TYR B CG  1 
ATOM   3857 C CD1 . TYR B 1 207 ? -0.48600  2.26300   -8.39500  1.000 29.77000 ? 209 TYR B CD1 1 
ATOM   3858 C CD2 . TYR B 1 207 ? 1.27200   3.21200   -7.09000  1.000 23.21000 ? 209 TYR B CD2 1 
ATOM   3859 C CE1 . TYR B 1 207 ? 0.31800   2.32300   -9.52000  1.000 27.63000 ? 209 TYR B CE1 1 
ATOM   3860 C CE2 . TYR B 1 207 ? 2.07800   3.28200   -8.20000  1.000 24.03000 ? 209 TYR B CE2 1 
ATOM   3861 C CZ  . TYR B 1 207 ? 1.59800   2.84200   -9.41700  1.000 27.94000 ? 209 TYR B CZ  1 
ATOM   3862 O OH  . TYR B 1 207 ? 2.41100   2.91300   -10.52200 1.000 22.57000 ? 209 TYR B OH  1 
ATOM   3863 N N   . ALA B 1 208 ? -3.07100  3.13300   -3.70800  1.000 26.43000 ? 210 ALA B N   1 
ATOM   3864 C CA  . ALA B 1 208 ? -4.10500  2.67000   -2.79300  1.000 30.32000 ? 210 ALA B CA  1 
ATOM   3865 C C   . ALA B 1 208 ? -5.44700  3.27800   -3.14900  1.000 29.63000 ? 210 ALA B C   1 
ATOM   3866 O O   . ALA B 1 208 ? -6.48300  2.60600   -3.08200  1.000 32.91000 ? 210 ALA B O   1 
ATOM   3867 C CB  . ALA B 1 208 ? -3.73100  3.01800   -1.35400  1.000 29.49000 ? 210 ALA B CB  1 
ATOM   3868 N N   . ALA B 1 209 ? -5.44400  4.55300   -3.53500  1.000 26.58000 ? 211 ALA B N   1 
ATOM   3869 C CA  . ALA B 1 209 ? -6.67200  5.21200   -3.94100  1.000 31.93000 ? 211 ALA B CA  1 
ATOM   3870 C C   . ALA B 1 209 ? -7.25000  4.57500   -5.19800  1.000 36.78000 ? 211 ALA B C   1 
ATOM   3871 O O   . ALA B 1 209 ? -8.47400  4.52400   -5.35800  1.000 38.29000 ? 211 ALA B O   1 
ATOM   3872 C CB  . ALA B 1 209 ? -6.41100  6.70000   -4.15000  1.000 29.15000 ? 211 ALA B CB  1 
ATOM   3873 N N   . VAL B 1 210 ? -6.39200  4.07100   -6.08800  1.000 34.13000 ? 212 VAL B N   1 
ATOM   3874 C CA  . VAL B 1 210 ? -6.87500  3.38600   -7.28500  1.000 35.33000 ? 212 VAL B CA  1 
ATOM   3875 C C   . VAL B 1 210 ? -7.45300  2.02600   -6.91700  1.000 40.12000 ? 212 VAL B C   1 
ATOM   3876 O O   . VAL B 1 210 ? -8.53300  1.64200   -7.38400  1.000 41.79000 ? 212 VAL B O   1 
ATOM   3877 C CB  . VAL B 1 210 ? -5.74400  3.24600   -8.32300  1.000 33.24000 ? 212 VAL B CB  1 
ATOM   3878 C CG1 . VAL B 1 210 ? -6.18000  2.34200   -9.47200  1.000 38.16000 ? 212 VAL B CG1 1 
ATOM   3879 C CG2 . VAL B 1 210 ? -5.32600  4.60400   -8.84300  1.000 26.96000 ? 212 VAL B CG2 1 
ATOM   3880 N N   . ILE B 1 211 ? -6.73300  1.27100   -6.08400  1.000 37.91000 ? 213 ILE B N   1 
ATOM   3881 C CA  . ILE B 1 211 ? -7.19800  -0.04900  -5.67200  1.000 36.79000 ? 213 ILE B CA  1 
ATOM   3882 C C   . ILE B 1 211 ? -8.56800  0.04200   -5.01400  1.000 38.05000 ? 213 ILE B C   1 
ATOM   3883 O O   . ILE B 1 211 ? -9.38500  -0.87800  -5.13600  1.000 41.57000 ? 213 ILE B O   1 
ATOM   3884 C CB  . ILE B 1 211 ? -6.15400  -0.70700  -4.74800  1.000 41.30000 ? 213 ILE B CB  1 
ATOM   3885 C CG1 . ILE B 1 211 ? -4.81000  -0.80500  -5.46800  1.000 36.84000 ? 213 ILE B CG1 1 
ATOM   3886 C CG2 . ILE B 1 211 ? -6.61100  -2.09300  -4.28700  1.000 40.28000 ? 213 ILE B CG2 1 
ATOM   3887 C CD1 . ILE B 1 211 ? -3.72200  -1.42500  -4.64100  1.000 39.65000 ? 213 ILE B CD1 1 
ATOM   3888 N N   . ASN B 1 212 ? -8.86100  1.15800   -4.35000  1.000 35.50000 ? 214 ASN B N   1 
ATOM   3889 C CA  . ASN B 1 212 ? -10.15400 1.36200   -3.71300  1.000 40.80000 ? 214 ASN B CA  1 
ATOM   3890 C C   . ASN B 1 212 ? -11.13000 2.14500   -4.57600  1.000 40.49000 ? 214 ASN B C   1 
ATOM   3891 O O   . ASN B 1 212 ? -12.16500 2.58800   -4.06500  1.000 40.33000 ? 214 ASN B O   1 
ATOM   3892 C CB  . ASN B 1 212 ? -9.98000  2.06000   -2.36500  1.000 37.33000 ? 214 ASN B CB  1 
ATOM   3893 C CG  . ASN B 1 212 ? -9.33900  1.16000   -1.33900  1.000 41.23000 ? 214 ASN B CG  1 
ATOM   3894 O OD1 . ASN B 1 212 ? -9.97900  0.25000   -0.80400  1.000 40.76000 ? 214 ASN B OD1 1 
ATOM   3895 N ND2 . ASN B 1 212 ? -8.06300  1.39800   -1.06200  1.000 40.81000 ? 214 ASN B ND2 1 
ATOM   3896 N N   . GLY B 1 213 ? -10.81700 2.35300   -5.85100  1.000 41.88000 ? 215 GLY B N   1 
ATOM   3897 C CA  . GLY B 1 213 ? -11.81900 2.72000   -6.82800  1.000 40.73000 ? 215 GLY B CA  1 
ATOM   3898 C C   . GLY B 1 213 ? -11.97000 4.18300   -7.18500  1.000 47.10000 ? 215 GLY B C   1 
ATOM   3899 O O   . GLY B 1 213 ? -12.88100 4.51300   -7.95300  1.000 48.80000 ? 215 GLY B O   1 
ATOM   3900 N N   . ASP B 1 214 ? -11.12700 5.07600   -6.67300  1.000 43.28000 ? 216 ASP B N   1 
ATOM   3901 C CA  . ASP B 1 214 ? -11.15400 6.46000   -7.12900  1.000 43.50000 ? 216 ASP B CA  1 
ATOM   3902 C C   . ASP B 1 214 ? -9.96100  6.70500   -8.04600  1.000 45.56000 ? 216 ASP B C   1 
ATOM   3903 O O   . ASP B 1 214 ? -8.82800  6.31800   -7.72800  1.000 39.84000 ? 216 ASP B O   1 
ATOM   3904 C CB  . ASP B 1 214 ? -11.19700 7.46500   -5.96500  1.000 41.55000 ? 216 ASP B CB  1 
ATOM   3905 C CG  . ASP B 1 214 ? -10.13400 7.22000   -4.91600  1.000 49.96000 ? 216 ASP B CG  1 
ATOM   3906 O OD1 . ASP B 1 214 ? -10.36700 6.43400   -3.96400  1.000 51.11000 ? 216 ASP B OD1 1 
ATOM   3907 O OD2 . ASP B 1 214 ? -9.07200  7.86100   -5.01900  1.000 54.94000 ? 216 ASP B OD2 1 
ATOM   3908 N N   . ARG B 1 215 ? -10.23800 7.31100   -9.20600  1.000 41.68000 ? 217 ARG B N   1 
ATOM   3909 C CA  . ARG B 1 215 ? -9.25000  7.50500   -10.25800 1.000 37.12000 ? 217 ARG B CA  1 
ATOM   3910 C C   . ARG B 1 215 ? -9.27500  8.91900   -10.82300 1.000 34.16000 ? 217 ARG B C   1 
ATOM   3911 O O   . ARG B 1 215 ? -8.69600  9.15300   -11.89100 1.000 36.68000 ? 217 ARG B O   1 
ATOM   3912 C CB  . ARG B 1 215 ? -9.47200  6.51100   -11.40300 1.000 35.41000 ? 217 ARG B CB  1 
ATOM   3913 C CG  . ARG B 1 215 ? -9.32600  5.04700   -11.05100 1.000 34.94000 ? 217 ARG B CG  1 
ATOM   3914 C CD  . ARG B 1 215 ? -9.83800  4.17400   -12.18600 1.000 37.68000 ? 217 ARG B CD  1 
ATOM   3915 N NE  . ARG B 1 215 ? -9.17000  4.48700   -13.44500 1.000 39.13000 ? 217 ARG B NE  1 
ATOM   3916 C CZ  . ARG B 1 215 ? -8.22400  3.73500   -13.99700 1.000 38.40000 ? 217 ARG B CZ  1 
ATOM   3917 N NH1 . ARG B 1 215 ? -7.66800  4.10700   -15.14200 1.000 39.71000 ? 217 ARG B NH1 1 
ATOM   3918 N NH2 . ARG B 1 215 ? -7.82900  2.61300   -13.40300 1.000 40.48000 ? 217 ARG B NH2 1 
ATOM   3919 N N   . TRP B 1 216 ? -9.91400  9.86900   -10.13700 1.000 30.29000 ? 218 TRP B N   1 
ATOM   3920 C CA  . TRP B 1 216 ? -10.14500 11.17600  -10.73800 1.000 34.59000 ? 218 TRP B CA  1 
ATOM   3921 C C   . TRP B 1 216 ? -8.85800  11.94800  -10.99400 1.000 35.68000 ? 218 TRP B C   1 
ATOM   3922 O O   . TRP B 1 216 ? -8.87300  12.90200  -11.78100 1.000 34.88000 ? 218 TRP B O   1 
ATOM   3923 C CB  . TRP B 1 216 ? -11.08400 12.00700  -9.86100  1.000 35.06000 ? 218 TRP B CB  1 
ATOM   3924 C CG  . TRP B 1 216 ? -10.50000 12.46800  -8.54300  1.000 37.53000 ? 218 TRP B CG  1 
ATOM   3925 C CD1 . TRP B 1 216 ? -10.67200 11.87900  -7.31800  1.000 36.02000 ? 218 TRP B CD1 1 
ATOM   3926 C CD2 . TRP B 1 216 ? -9.67300  13.62200  -8.31900  1.000 40.60000 ? 218 TRP B CD2 1 
ATOM   3927 N NE1 . TRP B 1 216 ? -10.00600 12.59400  -6.35200  1.000 41.43000 ? 218 TRP B NE1 1 
ATOM   3928 C CE2 . TRP B 1 216 ? -9.38300  13.66600  -6.93800  1.000 39.35000 ? 218 TRP B CE2 1 
ATOM   3929 C CE3 . TRP B 1 216 ? -9.14400  14.61700  -9.15100  1.000 34.55000 ? 218 TRP B CE3 1 
ATOM   3930 C CZ2 . TRP B 1 216 ? -8.59400  14.66500  -6.37300  1.000 36.58000 ? 218 TRP B CZ2 1 
ATOM   3931 C CZ3 . TRP B 1 216 ? -8.35800  15.60600  -8.58600  1.000 35.27000 ? 218 TRP B CZ3 1 
ATOM   3932 C CH2 . TRP B 1 216 ? -8.09200  15.62300  -7.21100  1.000 39.28000 ? 218 TRP B CH2 1 
ATOM   3933 N N   . PHE B 1 217 ? -7.75500  11.57300  -10.34500 1.000 32.87000 ? 219 PHE B N   1 
ATOM   3934 C CA  . PHE B 1 217 ? -6.48300  12.27200  -10.47800 1.000 28.42000 ? 219 PHE B CA  1 
ATOM   3935 C C   . PHE B 1 217 ? -5.58700  11.69600  -11.57200 1.000 25.62000 ? 219 PHE B C   1 
ATOM   3936 O O   . PHE B 1 217 ? -4.57600  12.32200  -11.91000 1.000 29.95000 ? 219 PHE B O   1 
ATOM   3937 C CB  . PHE B 1 217 ? -5.73600  12.23400  -9.12900  1.000 24.68000 ? 219 PHE B CB  1 
ATOM   3938 C CG  . PHE B 1 217 ? -5.76800  10.88600  -8.47800  1.000 27.42000 ? 219 PHE B CG  1 
ATOM   3939 C CD1 . PHE B 1 217 ? -4.86200  9.90700   -8.84100  1.000 23.25000 ? 219 PHE B CD1 1 
ATOM   3940 C CD2 . PHE B 1 217 ? -6.73700  10.57600  -7.53800  1.000 30.27000 ? 219 PHE B CD2 1 
ATOM   3941 C CE1 . PHE B 1 217 ? -4.89700  8.65400   -8.26200  1.000 27.21000 ? 219 PHE B CE1 1 
ATOM   3942 C CE2 . PHE B 1 217 ? -6.77800  9.31600   -6.95900  1.000 31.42000 ? 219 PHE B CE2 1 
ATOM   3943 C CZ  . PHE B 1 217 ? -5.85800  8.35300   -7.32400  1.000 26.36000 ? 219 PHE B CZ  1 
ATOM   3944 N N   . LEU B 1 218 ? -5.90300  10.51500  -12.10400 1.000 27.16000 ? 220 LEU B N   1 
ATOM   3945 C CA  . LEU B 1 218 ? -5.10200  9.91900   -13.16500 1.000 26.35000 ? 220 LEU B CA  1 
ATOM   3946 C C   . LEU B 1 218 ? -5.16300  10.78000  -14.43200 1.000 29.61000 ? 220 LEU B C   1 
ATOM   3947 O O   . LEU B 1 218 ? -6.07800  11.58500  -14.62600 1.000 28.86000 ? 220 LEU B O   1 
ATOM   3948 C CB  . LEU B 1 218 ? -5.58900  8.50100   -13.46800 1.000 27.86000 ? 220 LEU B CB  1 
ATOM   3949 C CG  . LEU B 1 218 ? -5.46000  7.43100   -12.37300 1.000 30.93000 ? 220 LEU B CG  1 
ATOM   3950 C CD1 . LEU B 1 218 ? -5.91100  6.06600   -12.88400 1.000 30.87000 ? 220 LEU B CD1 1 
ATOM   3951 C CD2 . LEU B 1 218 ? -4.02800  7.35100   -11.82600 1.000 28.63000 ? 220 LEU B CD2 1 
ATOM   3952 N N   . ASN B 1 219 ? -4.16100  10.61900  -15.29600 1.000 28.28000 ? 221 ASN B N   1 
ATOM   3953 C CA  . ASN B 1 219 ? -4.18000  11.31100  -16.57900 1.000 29.55000 ? 221 ASN B CA  1 
ATOM   3954 C C   . ASN B 1 219 ? -3.53900  10.43300  -17.64400 1.000 29.58000 ? 221 ASN B C   1 
ATOM   3955 O O   . ASN B 1 219 ? -2.97900  9.37200   -17.35800 1.000 24.38000 ? 221 ASN B O   1 
ATOM   3956 C CB  . ASN B 1 219 ? -3.50200  12.69300  -16.50500 1.000 29.14000 ? 221 ASN B CB  1 
ATOM   3957 C CG  . ASN B 1 219 ? -2.02900  12.62800  -16.09000 1.000 27.53000 ? 221 ASN B CG  1 
ATOM   3958 O OD1 . ASN B 1 219 ? -1.30100  11.69500  -16.42800 1.000 29.80000 ? 221 ASN B OD1 1 
ATOM   3959 N ND2 . ASN B 1 219 ? -1.59000  13.64400  -15.36000 1.000 26.64000 ? 221 ASN B ND2 1 
ATOM   3960 N N   . ARG B 1 220 ? -3.64800  10.88900  -18.89300 1.000 32.71000 ? 222 ARG B N   1 
ATOM   3961 C CA  . ARG B 1 220 ? -3.10500  10.14900  -20.02200 1.000 34.22000 ? 222 ARG B CA  1 
ATOM   3962 C C   . ARG B 1 220 ? -1.60800  10.36300  -20.20300 1.000 34.70000 ? 222 ARG B C   1 
ATOM   3963 O O   . ARG B 1 220 ? -0.98600  9.64500   -20.99600 1.000 32.25000 ? 222 ARG B O   1 
ATOM   3964 C CB  . ARG B 1 220 ? -3.84400  10.54700  -21.30200 1.000 33.95000 ? 222 ARG B CB  1 
ATOM   3965 C CG  . ARG B 1 220 ? -3.61800  11.99000  -21.73400 1.000 29.56000 ? 222 ARG B CG  1 
ATOM   3966 C CD  . ARG B 1 220 ? -4.38000  12.29500  -23.03200 1.000 38.08000 ? 222 ARG B CD  1 
ATOM   3967 N NE  . ARG B 1 220 ? -3.88500  11.49100  -24.15200 1.000 40.18000 ? 222 ARG B NE  1 
ATOM   3968 C CZ  . ARG B 1 220 ? -4.43200  11.46400  -25.36800 1.000 40.46000 ? 222 ARG B CZ  1 
ATOM   3969 N NH1 . ARG B 1 220 ? -5.50900  12.19900  -25.64900 1.000 31.08000 ? 222 ARG B NH1 1 
ATOM   3970 N NH2 . ARG B 1 220 ? -3.89500  10.70200  -26.31100 1.000 36.54000 ? 222 ARG B NH2 1 
ATOM   3971 N N   . PHE B 1 221 ? -1.02000  11.30200  -19.46500 1.000 34.08000 ? 223 PHE B N   1 
ATOM   3972 C CA  . PHE B 1 221 ? 0.35200   11.73200  -19.67200 1.000 33.48000 ? 223 PHE B CA  1 
ATOM   3973 C C   . PHE B 1 221 ? 1.34300   10.78000  -18.99800 1.000 34.24000 ? 223 PHE B C   1 
ATOM   3974 O O   . PHE B 1 221 ? 0.98600   9.90900   -18.19400 1.000 35.28000 ? 223 PHE B O   1 
ATOM   3975 C CB  . PHE B 1 221 ? 0.54300   13.15900  -19.14800 1.000 27.96000 ? 223 PHE B CB  1 
ATOM   3976 N N   . THR B 1 222 ? 2.61300   10.95700  -19.34800 1.000 31.11000 ? 224 THR B N   1 
ATOM   3977 C CA  . THR B 1 222 ? 3.71100   10.23800  -18.72500 1.000 31.40000 ? 224 THR B CA  1 
ATOM   3978 C C   . THR B 1 222 ? 4.86600   11.21500  -18.52200 1.000 33.40000 ? 224 THR B C   1 
ATOM   3979 O O   . THR B 1 222 ? 4.81600   12.37100  -18.95600 1.000 34.16000 ? 224 THR B O   1 
ATOM   3980 C CB  . THR B 1 222 ? 4.13400   9.02500   -19.56200 1.000 35.24000 ? 224 THR B CB  1 
ATOM   3981 O OG1 . THR B 1 222 ? 5.04000   8.20800   -18.80300 1.000 37.90000 ? 224 THR B OG1 1 
ATOM   3982 C CG2 . THR B 1 222 ? 4.79700   9.47600   -20.85900 1.000 35.51000 ? 224 THR B CG2 1 
ATOM   3983 N N   . THR B 1 223 ? 5.90600   10.75200  -17.83500 1.000 25.46000 ? 225 THR B N   1 
ATOM   3984 C CA  . THR B 1 223 ? 7.03400   11.60700  -17.48900 1.000 21.53000 ? 225 THR B CA  1 
ATOM   3985 C C   . THR B 1 223 ? 8.26300   10.72900  -17.34900 1.000 20.14000 ? 225 THR B C   1 
ATOM   3986 O O   . THR B 1 223 ? 8.16200   9.52900   -17.09600 1.000 24.65000 ? 225 THR B O   1 
ATOM   3987 C CB  . THR B 1 223 ? 6.78100   12.40200  -16.19100 1.000 21.16000 ? 225 THR B CB  1 
ATOM   3988 O OG1 . THR B 1 223 ? 7.95500   13.15200  -15.82400 1.000 23.18000 ? 225 THR B OG1 1 
ATOM   3989 C CG2 . THR B 1 223 ? 6.43600   11.46000  -15.05400 1.000 24.82000 ? 225 THR B CG2 1 
ATOM   3990 N N   . THR B 1 224 ? 9.42800   11.33100  -17.54200 1.000 22.34000 ? 226 THR B N   1 
ATOM   3991 C CA  . THR B 1 224 ? 10.65800  10.63400  -17.22400 1.000 20.29000 ? 226 THR B CA  1 
ATOM   3992 C C   . THR B 1 224 ? 10.94400  10.74700  -15.73100 1.000 20.45000 ? 226 THR B C   1 
ATOM   3993 O O   . THR B 1 224 ? 10.40700  11.61000  -15.03000 1.000 19.31000 ? 226 THR B O   1 
ATOM   3994 C CB  . THR B 1 224 ? 11.84000  11.19600  -18.01700 1.000 22.36000 ? 226 THR B CB  1 
ATOM   3995 O OG1 . THR B 1 224 ? 12.16700  12.50200  -17.52500 1.000 20.79000 ? 226 THR B OG1 1 
ATOM   3996 C CG2 . THR B 1 224 ? 11.51300  11.26800  -19.49300 1.000 24.51000 ? 226 THR B CG2 1 
ATOM   3997 N N   . LEU B 1 225 ? 11.81400  9.86100   -15.25000 1.000 16.57000 ? 227 LEU B N   1 
ATOM   3998 C CA  . LEU B 1 225 ? 12.17500  9.88800   -13.83700 1.000 18.08000 ? 227 LEU B CA  1 
ATOM   3999 C C   . LEU B 1 225 ? 12.90100  11.17800  -13.48500 1.000 18.23000 ? 227 LEU B C   1 
ATOM   4000 O O   . LEU B 1 225 ? 12.66700  11.76300  -12.42200 1.000 14.92000 ? 227 LEU B O   1 
ATOM   4001 C CB  . LEU B 1 225 ? 13.05100  8.68900   -13.49700 1.000 17.37000 ? 227 LEU B CB  1 
ATOM   4002 C CG  . LEU B 1 225 ? 13.47600  8.57200   -12.03300 1.000 20.62000 ? 227 LEU B CG  1 
ATOM   4003 C CD1 . LEU B 1 225 ? 12.24200  8.45800   -11.17000 1.000 19.16000 ? 227 LEU B CD1 1 
ATOM   4004 C CD2 . LEU B 1 225 ? 14.38800  7.36800   -11.82900 1.000 22.65000 ? 227 LEU B CD2 1 
ATOM   4005 N N   . ASN B 1 226 ? 13.79100  11.63300  -14.36400 1.000 16.23000 ? 228 ASN B N   1 
ATOM   4006 C CA  . ASN B 1 226 ? 14.54300  12.83800  -14.04800 1.000 18.80000 ? 228 ASN B CA  1 
ATOM   4007 C C   . ASN B 1 226 ? 13.66000  14.07400  -14.09800 1.000 16.88000 ? 228 ASN B C   1 
ATOM   4008 O O   . ASN B 1 226 ? 13.80200  14.97100  -13.26000 1.000 19.58000 ? 228 ASN B O   1 
ATOM   4009 C CB  . ASN B 1 226 ? 15.72700  13.00000  -14.98200 1.000 23.78000 ? 228 ASN B CB  1 
ATOM   4010 C CG  . ASN B 1 226 ? 16.65800  14.07900  -14.50900 1.000 31.39000 ? 228 ASN B CG  1 
ATOM   4011 O OD1 . ASN B 1 226 ? 17.51600  13.84000  -13.65400 1.000 36.40000 ? 228 ASN B OD1 1 
ATOM   4012 N ND2 . ASN B 1 226 ? 16.46100  15.30000  -15.01500 1.000 29.54000 ? 228 ASN B ND2 1 
ATOM   4013 N N   . ASP B 1 227 ? 12.73400  14.14100  -15.05800 1.000 17.05000 ? 229 ASP B N   1 
ATOM   4014 C CA  . ASP B 1 227 ? 11.85200  15.30300  -15.12100 1.000 18.58000 ? 229 ASP B CA  1 
ATOM   4015 C C   . ASP B 1 227 ? 10.89500  15.32400  -13.93800 1.000 17.58000 ? 229 ASP B C   1 
ATOM   4016 O O   . ASP B 1 227 ? 10.59100  16.39200  -13.39300 1.000 15.15000 ? 229 ASP B O   1 
ATOM   4017 C CB  . ASP B 1 227 ? 11.07700  15.32100  -16.44000 1.000 16.24000 ? 229 ASP B CB  1 
ATOM   4018 C CG  . ASP B 1 227 ? 11.95800  15.69400  -17.63300 1.000 23.37000 ? 229 ASP B CG  1 
ATOM   4019 O OD1 . ASP B 1 227 ? 13.07600  16.22400  -17.41200 1.000 24.73000 ? 229 ASP B OD1 1 
ATOM   4020 O OD2 . ASP B 1 227 ? 11.53200  15.45000  -18.78700 1.000 28.16000 ? 229 ASP B OD2 1 
ATOM   4021 N N   . PHE B 1 228 ? 10.41900  14.15500  -13.51300 1.000 14.62000 ? 230 PHE B N   1 
ATOM   4022 C CA  . PHE B 1 228 ? 9.59800   14.12100  -12.30800 1.000 17.62000 ? 230 PHE B CA  1 
ATOM   4023 C C   . PHE B 1 228 ? 10.38700  14.59700  -11.09500 1.000 13.92000 ? 230 PHE B C   1 
ATOM   4024 O O   . PHE B 1 228 ? 9.88300   15.38400  -10.28100 1.000 15.37000 ? 230 PHE B O   1 
ATOM   4025 C CB  . PHE B 1 228 ? 9.06000   12.71500  -12.05200 1.000 15.50000 ? 230 PHE B CB  1 
ATOM   4026 C CG  . PHE B 1 228 ? 8.38500   12.58200  -10.71400 1.000 16.02000 ? 230 PHE B CG  1 
ATOM   4027 C CD1 . PHE B 1 228 ? 7.08400   13.03600  -10.53300 1.000 15.60000 ? 230 PHE B CD1 1 
ATOM   4028 C CD2 . PHE B 1 228 ? 9.05900   12.03800  -9.63400  1.000 14.00000 ? 230 PHE B CD2 1 
ATOM   4029 C CE1 . PHE B 1 228 ? 6.45400   12.92300  -9.29700  1.000 17.38000 ? 230 PHE B CE1 1 
ATOM   4030 C CE2 . PHE B 1 228 ? 8.44500   11.92500  -8.40200  1.000 15.55000 ? 230 PHE B CE2 1 
ATOM   4031 C CZ  . PHE B 1 228 ? 7.14500   12.36800  -8.22800  1.000 18.68000 ? 230 PHE B CZ  1 
ATOM   4032 N N   . ASN B 1 229 ? 11.63200  14.13900  -10.96400 1.000 12.78000 ? 231 ASN B N   1 
ATOM   4033 C CA  . ASN B 1 229 ? 12.42700  14.53300  -9.80700  1.000 14.32000 ? 231 ASN B CA  1 
ATOM   4034 C C   . ASN B 1 229 ? 12.71100  16.02900  -9.78500  1.000 17.16000 ? 231 ASN B C   1 
ATOM   4035 O O   . ASN B 1 229 ? 12.82200  16.61700  -8.70400  1.000 16.72000 ? 231 ASN B O   1 
ATOM   4036 C CB  . ASN B 1 229 ? 13.71400  13.73000  -9.76700  1.000 15.42000 ? 231 ASN B CB  1 
ATOM   4037 C CG  . ASN B 1 229 ? 13.47700  12.36500  -9.17400  1.000 21.87000 ? 231 ASN B CG  1 
ATOM   4038 O OD1 . ASN B 1 229 ? 12.58000  12.21100  -8.34400  1.000 21.32000 ? 231 ASN B OD1 1 
ATOM   4039 N ND2 . ASN B 1 229 ? 14.23500  11.37500  -9.60200  1.000 19.51000 ? 231 ASN B ND2 1 
ATOM   4040 N N   . LEU B 1 230 ? 12.82200  16.66100  -10.94900 1.000 13.38000 ? 232 LEU B N   1 
ATOM   4041 C CA  . LEU B 1 230 ? 12.97600  18.11100  -10.96500 1.000 14.14000 ? 232 LEU B CA  1 
ATOM   4042 C C   . LEU B 1 230 ? 11.75500  18.78400  -10.34600 1.000 13.13000 ? 232 LEU B C   1 
ATOM   4043 O O   . LEU B 1 230 ? 11.88500  19.65500  -9.47700  1.000 17.42000 ? 232 LEU B O   1 
ATOM   4044 C CB  . LEU B 1 230 ? 13.21100  18.58800  -12.39900 1.000 12.67000 ? 232 LEU B CB  1 
ATOM   4045 C CG  . LEU B 1 230 ? 14.61700  18.33600  -12.95700 1.000 13.06000 ? 232 LEU B CG  1 
ATOM   4046 C CD1 . LEU B 1 230 ? 14.67100  18.58500  -14.48000 1.000 16.92000 ? 232 LEU B CD1 1 
ATOM   4047 C CD2 . LEU B 1 230 ? 15.63500  19.19200  -12.23500 1.000 17.25000 ? 232 LEU B CD2 1 
ATOM   4048 N N   . VAL B 1 231 ? 10.55800  18.36900  -10.76000 1.000 14.19000 ? 233 VAL B N   1 
ATOM   4049 C CA  . VAL B 1 231 ? 9.33200   18.96800  -10.23100 1.000 17.22000 ? 233 VAL B CA  1 
ATOM   4050 C C   . VAL B 1 231 ? 9.17500   18.63800  -8.75300  1.000 17.49000 ? 233 VAL B C   1 
ATOM   4051 O O   . VAL B 1 231 ? 8.81700   19.50200  -7.94200  1.000 19.50000 ? 233 VAL B O   1 
ATOM   4052 C CB  . VAL B 1 231 ? 8.10900   18.50400  -11.05000 1.000 18.70000 ? 233 VAL B CB  1 
ATOM   4053 C CG1 . VAL B 1 231 ? 6.81600   19.07300  -10.45700 1.000 22.00000 ? 233 VAL B CG1 1 
ATOM   4054 C CG2 . VAL B 1 231 ? 8.24100   18.93100  -12.51100 1.000 19.42000 ? 233 VAL B CG2 1 
ATOM   4055 N N   . ALA B 1 232 ? 9.45800   17.38900  -8.37400  1.000 15.12000 ? 234 ALA B N   1 
ATOM   4056 C CA  . ALA B 1 232 ? 9.36500   16.99600  -6.96800  1.000 19.96000 ? 234 ALA B CA  1 
ATOM   4057 C C   . ALA B 1 232 ? 10.25700  17.86700  -6.08200  1.000 16.89000 ? 234 ALA B C   1 
ATOM   4058 O O   . ALA B 1 232 ? 9.82100   18.37100  -5.03700  1.000 17.00000 ? 234 ALA B O   1 
ATOM   4059 C CB  . ALA B 1 232 ? 9.73000   15.51400  -6.81900  1.000 16.35000 ? 234 ALA B CB  1 
ATOM   4060 N N   . MET B 1 233 ? 11.51700  18.04800  -6.47700  1.000 16.22000 ? 235 MET B N   1 
ATOM   4061 C CA  . MET B 1 233 ? 12.41500  18.87700  -5.68100  1.000 18.35000 ? 235 MET B CA  1 
ATOM   4062 C C   . MET B 1 233 ? 11.91200  20.31400  -5.60200  1.000 21.25000 ? 235 MET B C   1 
ATOM   4063 O O   . MET B 1 233 ? 12.07000  20.97800  -4.56800  1.000 22.03000 ? 235 MET B O   1 
ATOM   4064 C CB  . MET B 1 233 ? 13.82400  18.83400  -6.27000  1.000 20.63000 ? 235 MET B CB  1 
ATOM   4065 C CG  . MET B 1 233 ? 14.91800  19.23200  -5.28300  1.000 34.30000 ? 235 MET B CG  1 
ATOM   4066 S SD  . MET B 1 233 ? 16.59600  19.07400  -5.95700  1.000 51.87000 ? 235 MET B SD  1 
ATOM   4067 C CE  . MET B 1 233 ? 16.30400  19.42400  -7.68800  1.000 42.24000 ? 235 MET B CE  1 
ATOM   4068 N N   . LYS B 1 234 ? 11.30200  20.80400  -6.67900  1.000 18.20000 ? 236 LYS B N   1 
ATOM   4069 C CA  . LYS B 1 234 ? 10.72100  22.14200  -6.66000  1.000 21.31000 ? 236 LYS B CA  1 
ATOM   4070 C C   . LYS B 1 234 ? 9.63400   22.26700  -5.60000  1.000 21.69000 ? 236 LYS B C   1 
ATOM   4071 O O   . LYS B 1 234 ? 9.45400   23.34000  -5.01800  1.000 22.63000 ? 236 LYS B O   1 
ATOM   4072 C CB  . LYS B 1 234 ? 10.16000  22.47800  -8.04100  1.000 16.81000 ? 236 LYS B CB  1 
ATOM   4073 C CG  . LYS B 1 234 ? 9.79900   23.94300  -8.23100  1.000 19.61000 ? 236 LYS B CG  1 
ATOM   4074 C CD  . LYS B 1 234 ? 8.93900   24.11600  -9.49800  1.000 18.53000 ? 236 LYS B CD  1 
ATOM   4075 C CE  . LYS B 1 234 ? 8.57500   25.58400  -9.72800  1.000 20.28000 ? 236 LYS B CE  1 
ATOM   4076 N NZ  . LYS B 1 234 ? 7.58400   25.71500  -10.85000 1.000 19.94000 ? 236 LYS B NZ  1 
ATOM   4077 N N   . TYR B 1 235 ? 8.91700   21.18300  -5.31300  1.000 19.97000 ? 237 TYR B N   1 
ATOM   4078 C CA  . TYR B 1 235 ? 7.83700   21.21700  -4.33600  1.000 19.56000 ? 237 TYR B CA  1 
ATOM   4079 C C   . TYR B 1 235 ? 8.22600   20.60900  -2.99000  1.000 19.29000 ? 237 TYR B C   1 
ATOM   4080 O O   . TYR B 1 235 ? 7.34000   20.22000  -2.21700  1.000 20.48000 ? 237 TYR B O   1 
ATOM   4081 C CB  . TYR B 1 235 ? 6.61300   20.50700  -4.90300  1.000 16.68000 ? 237 TYR B CB  1 
ATOM   4082 C CG  . TYR B 1 235 ? 5.87700   21.31200  -5.95400  1.000 26.33000 ? 237 TYR B CG  1 
ATOM   4083 C CD1 . TYR B 1 235 ? 4.85700   22.18900  -5.59600  1.000 28.48000 ? 237 TYR B CD1 1 
ATOM   4084 C CD2 . TYR B 1 235 ? 6.19200   21.18800  -7.30800  1.000 22.39000 ? 237 TYR B CD2 1 
ATOM   4085 C CE1 . TYR B 1 235 ? 4.17200   22.93100  -6.55700  1.000 29.19000 ? 237 TYR B CE1 1 
ATOM   4086 C CE2 . TYR B 1 235 ? 5.51100   21.92700  -8.27700  1.000 24.53000 ? 237 TYR B CE2 1 
ATOM   4087 C CZ  . TYR B 1 235 ? 4.50100   22.79400  -7.89400  1.000 29.26000 ? 237 TYR B CZ  1 
ATOM   4088 O OH  . TYR B 1 235 ? 3.80900   23.52100  -8.84800  1.000 26.19000 ? 237 TYR B OH  1 
ATOM   4089 N N   . ASN B 1 236 ? 9.52700   20.50300  -2.70500  1.000 17.87000 ? 238 ASN B N   1 
ATOM   4090 C CA  . ASN B 1 236 ? 10.03700  19.95400  -1.44500  1.000 19.88000 ? 238 ASN B CA  1 
ATOM   4091 C C   . ASN B 1 236 ? 9.57200   18.51800  -1.21600  1.000 21.94000 ? 238 ASN B C   1 
ATOM   4092 O O   . ASN B 1 236 ? 9.23200   18.12600  -0.09400  1.000 18.17000 ? 238 ASN B O   1 
ATOM   4093 C CB  . ASN B 1 236 ? 9.65700   20.83300  -0.25300  1.000 21.65000 ? 238 ASN B CB  1 
ATOM   4094 C CG  . ASN B 1 236 ? 10.85800  21.24100  0.56400   1.000 31.39000 ? 238 ASN B CG  1 
ATOM   4095 O OD1 . ASN B 1 236 ? 12.00000  21.16800  0.09500   1.000 40.52000 ? 238 ASN B OD1 1 
ATOM   4096 N ND2 . ASN B 1 236 ? 10.61400  21.67700  1.79600   1.000 36.15000 ? 238 ASN B ND2 1 
ATOM   4097 N N   . TYR B 1 237 ? 9.55800   17.73500  -2.28400  1.000 15.65000 ? 239 TYR B N   1 
ATOM   4098 C CA  . TYR B 1 237 ? 9.39500   16.29400  -2.21200  1.000 16.04000 ? 239 TYR B CA  1 
ATOM   4099 C C   . TYR B 1 237 ? 10.76500  15.63800  -2.29300  1.000 19.51000 ? 239 TYR B C   1 
ATOM   4100 O O   . TYR B 1 237 ? 11.66200  16.13000  -2.98200  1.000 18.02000 ? 239 TYR B O   1 
ATOM   4101 C CB  . TYR B 1 237 ? 8.51100   15.78500  -3.35500  1.000 14.99000 ? 239 TYR B CB  1 
ATOM   4102 C CG  . TYR B 1 237 ? 7.03500   15.80800  -3.05700  1.000 13.30000 ? 239 TYR B CG  1 
ATOM   4103 C CD1 . TYR B 1 237 ? 6.41000   16.97400  -2.62700  1.000 18.17000 ? 239 TYR B CD1 1 
ATOM   4104 C CD2 . TYR B 1 237 ? 6.26000   14.66400  -3.20900  1.000 13.50000 ? 239 TYR B CD2 1 
ATOM   4105 C CE1 . TYR B 1 237 ? 5.05600   17.00000  -2.35500  1.000 17.88000 ? 239 TYR B CE1 1 
ATOM   4106 C CE2 . TYR B 1 237 ? 4.90900   14.67300  -2.93600  1.000 15.40000 ? 239 TYR B CE2 1 
ATOM   4107 C CZ  . TYR B 1 237 ? 4.31200   15.84600  -2.51500  1.000 19.96000 ? 239 TYR B CZ  1 
ATOM   4108 O OH  . TYR B 1 237 ? 2.96700   15.87300  -2.24400  1.000 26.42000 ? 239 TYR B OH  1 
ATOM   4109 N N   . GLU B 1 238 ? 10.91900  14.51700  -1.59300  1.000 14.66000 ? 240 GLU B N   1 
ATOM   4110 C CA  . GLU B 1 238 ? 12.14900  13.74800  -1.68200  1.000 19.38000 ? 240 GLU B CA  1 
ATOM   4111 C C   . GLU B 1 238 ? 12.33300  13.17700  -3.09100  1.000 19.02000 ? 240 GLU B C   1 
ATOM   4112 O O   . GLU B 1 238 ? 11.36400  12.98200  -3.82800  1.000 15.16000 ? 240 GLU B O   1 
ATOM   4113 C CB  . GLU B 1 238 ? 12.13300  12.60700  -0.66600  1.000 21.57000 ? 240 GLU B CB  1 
ATOM   4114 C CG  . GLU B 1 238 ? 12.27400  13.09000  0.76300   1.000 21.19000 ? 240 GLU B CG  1 
ATOM   4115 C CD  . GLU B 1 238 ? 13.69000  13.53200  1.06200   1.000 29.51000 ? 240 GLU B CD  1 
ATOM   4116 O OE1 . GLU B 1 238 ? 13.89200  14.71900  1.39800   1.000 30.32000 ? 240 GLU B OE1 1 
ATOM   4117 O OE2 . GLU B 1 238 ? 14.60600  12.68900  0.95100   1.000 31.97000 ? 240 GLU B OE2 1 
ATOM   4118 N N   . PRO B 1 239 ? 13.57100  12.88800  -3.48100  1.000 20.52000 ? 241 PRO B N   1 
ATOM   4119 C CA  . PRO B 1 239 ? 13.79300  12.26500  -4.78900  1.000 21.69000 ? 241 PRO B CA  1 
ATOM   4120 C C   . PRO B 1 239 ? 13.18100  10.87500  -4.85400  1.000 18.90000 ? 241 PRO B C   1 
ATOM   4121 O O   . PRO B 1 239 ? 13.09300  10.15600  -3.85600  1.000 17.57000 ? 241 PRO B O   1 
ATOM   4122 C CB  . PRO B 1 239 ? 15.32300  12.20700  -4.91100  1.000 23.87000 ? 241 PRO B CB  1 
ATOM   4123 C CG  . PRO B 1 239 ? 15.84500  12.44100  -3.55500  1.000 29.71000 ? 241 PRO B CG  1 
ATOM   4124 C CD  . PRO B 1 239 ? 14.83100  13.22700  -2.79700  1.000 24.01000 ? 241 PRO B CD  1 
ATOM   4125 N N   . LEU B 1 240 ? 12.73400  10.51000  -6.04600  1.000 16.44000 ? 242 LEU B N   1 
ATOM   4126 C CA  . LEU B 1 240 ? 12.30600  9.14800   -6.33200  1.000 18.60000 ? 242 LEU B CA  1 
ATOM   4127 C C   . LEU B 1 240 ? 13.47000  8.41200   -6.98700  1.000 19.40000 ? 242 LEU B C   1 
ATOM   4128 O O   . LEU B 1 240 ? 13.98300  8.85100   -8.01900  1.000 16.56000 ? 242 LEU B O   1 
ATOM   4129 C CB  . LEU B 1 240 ? 11.08300  9.14200   -7.24300  1.000 17.46000 ? 242 LEU B CB  1 
ATOM   4130 C CG  . LEU B 1 240 ? 10.35000  7.80900   -7.32800  1.000 20.96000 ? 242 LEU B CG  1 
ATOM   4131 C CD1 . LEU B 1 240 ? 9.61500   7.51200   -5.99900  1.000 19.30000 ? 242 LEU B CD1 1 
ATOM   4132 C CD2 . LEU B 1 240 ? 9.39600   7.83000   -8.50600  1.000 19.11000 ? 242 LEU B CD2 1 
ATOM   4133 N N   . THR B 1 241 ? 13.89800  7.31300   -6.38000  1.000 19.16000 ? 243 THR B N   1 
ATOM   4134 C CA  . THR B 1 241 ? 14.99400  6.53700   -6.93300  1.000 21.08000 ? 243 THR B CA  1 
ATOM   4135 C C   . THR B 1 241 ? 14.45400  5.39100   -7.78700  1.000 20.42000 ? 243 THR B C   1 
ATOM   4136 O O   . THR B 1 241 ? 13.26200  5.07500   -7.77400  1.000 19.52000 ? 243 THR B O   1 
ATOM   4137 C CB  . THR B 1 241 ? 15.86400  5.97900   -5.81400  1.000 24.68000 ? 243 THR B CB  1 
ATOM   4138 O OG1 . THR B 1 241 ? 15.09500  5.02100   -5.08500  1.000 18.57000 ? 243 THR B OG1 1 
ATOM   4139 C CG2 . THR B 1 241 ? 16.31400  7.09900   -4.86600  1.000 25.16000 ? 243 THR B CG2 1 
ATOM   4140 N N   . GLN B 1 242 ? 15.35400  4.76000   -8.54300  1.000 22.71000 ? 244 GLN B N   1 
ATOM   4141 C CA  . GLN B 1 242 ? 14.96000  3.55900   -9.26900  1.000 25.94000 ? 244 GLN B CA  1 
ATOM   4142 C C   . GLN B 1 242 ? 14.57600  2.43900   -8.30700  1.000 22.83000 ? 244 GLN B C   1 
ATOM   4143 O O   . GLN B 1 242 ? 13.66400  1.65900   -8.60000  1.000 23.22000 ? 244 GLN B O   1 
ATOM   4144 C CB  . GLN B 1 242 ? 16.07800  3.10600   -10.20700 1.000 29.54000 ? 244 GLN B CB  1 
ATOM   4145 C CG  . GLN B 1 242 ? 15.68400  1.92600   -11.10500 1.000 25.41000 ? 244 GLN B CG  1 
ATOM   4146 C CD  . GLN B 1 242 ? 14.47400  2.23000   -11.96300 1.000 31.20000 ? 244 GLN B CD  1 
ATOM   4147 O OE1 . GLN B 1 242 ? 14.34400  3.33200   -12.49800 1.000 33.40000 ? 244 GLN B OE1 1 
ATOM   4148 N NE2 . GLN B 1 242 ? 13.57200  1.25700   -12.09400 1.000 27.04000 ? 244 GLN B NE2 1 
ATOM   4149 N N   . ASP B 1 243 ? 15.23200  2.36100   -7.14600  1.000 25.21000 ? 245 ASP B N   1 
ATOM   4150 C CA  . ASP B 1 243 ? 14.80200  1.39800   -6.13400  1.000 27.15000 ? 245 ASP B CA  1 
ATOM   4151 C C   . ASP B 1 243 ? 13.35100  1.64500   -5.73600  1.000 25.16000 ? 245 ASP B C   1 
ATOM   4152 O O   . ASP B 1 243 ? 12.55200  0.70900   -5.65000  1.000 24.40000 ? 245 ASP B O   1 
ATOM   4153 C CB  . ASP B 1 243 ? 15.72100  1.45900   -4.91300  1.000 25.90000 ? 245 ASP B CB  1 
ATOM   4154 N N   . HIS B 1 244 ? 12.98900  2.91000   -5.50600  1.000 23.00000 ? 246 HIS B N   1 
ATOM   4155 C CA  . HIS B 1 244 ? 11.59500  3.24700   -5.23200  1.000 19.74000 ? 246 HIS B CA  1 
ATOM   4156 C C   . HIS B 1 244 ? 10.68000  2.78000   -6.35800  1.000 23.29000 ? 246 HIS B C   1 
ATOM   4157 O O   . HIS B 1 244 ? 9.60500   2.22300   -6.11200  1.000 23.29000 ? 246 HIS B O   1 
ATOM   4158 C CB  . HIS B 1 244 ? 11.44900  4.75500   -5.04400  1.000 19.73000 ? 246 HIS B CB  1 
ATOM   4159 C CG  . HIS B 1 244 ? 12.09100  5.28600   -3.80400  1.000 20.49000 ? 246 HIS B CG  1 
ATOM   4160 N ND1 . HIS B 1 244 ? 12.60600  6.56100   -3.72900  1.000 20.88000 ? 246 HIS B ND1 1 
ATOM   4161 C CD2 . HIS B 1 244 ? 12.28900  4.72500   -2.58800  1.000 21.39000 ? 246 HIS B CD2 1 
ATOM   4162 C CE1 . HIS B 1 244 ? 13.10600  6.75900   -2.52000  1.000 24.25000 ? 246 HIS B CE1 1 
ATOM   4163 N NE2 . HIS B 1 244 ? 12.92000  5.66200   -1.80700  1.000 21.95000 ? 246 HIS B NE2 1 
ATOM   4164 N N   . VAL B 1 245 ? 11.07400  3.03900   -7.60800  1.000 23.21000 ? 247 VAL B N   1 
ATOM   4165 C CA  . VAL B 1 245 ? 10.26000  2.62100   -8.74500  1.000 22.07000 ? 247 VAL B CA  1 
ATOM   4166 C C   . VAL B 1 245 ? 10.05200  1.11000   -8.72000  1.000 26.50000 ? 247 VAL B C   1 
ATOM   4167 O O   . VAL B 1 245 ? 8.93900   0.61500   -8.94400  1.000 23.48000 ? 247 VAL B O   1 
ATOM   4168 C CB  . VAL B 1 245 ? 10.90800  3.08700   -10.06500 1.000 24.50000 ? 247 VAL B CB  1 
ATOM   4169 C CG1 . VAL B 1 245 ? 10.29300  2.36500   -11.25100 1.000 23.95000 ? 247 VAL B CG1 1 
ATOM   4170 C CG2 . VAL B 1 245 ? 10.78100  4.60800   -10.22600 1.000 21.05000 ? 247 VAL B CG2 1 
ATOM   4171 N N   . ASP B 1 246 ? 11.11700  0.35900   -8.42500  1.000 24.60000 ? 248 ASP B N   1 
ATOM   4172 C CA  . ASP B 1 246 ? 11.00900  -1.09800  -8.34500  1.000 28.99000 ? 248 ASP B CA  1 
ATOM   4173 C C   . ASP B 1 246 ? 10.11800  -1.52700  -7.18600  1.000 29.43000 ? 248 ASP B C   1 
ATOM   4174 O O   . ASP B 1 246 ? 9.29400   -2.44100  -7.33200  1.000 31.18000 ? 248 ASP B O   1 
ATOM   4175 C CB  . ASP B 1 246 ? 12.39600  -1.71800  -8.20100  1.000 28.97000 ? 248 ASP B CB  1 
ATOM   4176 C CG  . ASP B 1 246 ? 13.27600  -1.47000  -9.41200  1.000 33.43000 ? 248 ASP B CG  1 
ATOM   4177 O OD1 . ASP B 1 246 ? 12.73100  -1.28000  -10.52300 1.000 37.06000 ? 248 ASP B OD1 1 
ATOM   4178 O OD2 . ASP B 1 246 ? 14.51700  -1.47100  -9.25300  1.000 38.57000 ? 248 ASP B OD2 1 
ATOM   4179 N N   . ILE B 1 247 ? 10.27500  -0.88200  -6.02600  1.000 26.77000 ? 249 ILE B N   1 
ATOM   4180 C CA  . ILE B 1 247 ? 9.44400   -1.18900  -4.86600  1.000 28.36000 ? 249 ILE B CA  1 
ATOM   4181 C C   . ILE B 1 247 ? 7.97200   -0.97100  -5.17800  1.000 27.24000 ? 249 ILE B C   1 
ATOM   4182 O O   . ILE B 1 247 ? 7.09800   -1.64100  -4.61100  1.000 28.17000 ? 249 ILE B O   1 
ATOM   4183 C CB  . ILE B 1 247 ? 9.89700   -0.34000  -3.66400  1.000 27.85000 ? 249 ILE B CB  1 
ATOM   4184 C CG1 . ILE B 1 247 ? 11.29500  -0.75300  -3.23100  1.000 28.44000 ? 249 ILE B CG1 1 
ATOM   4185 C CG2 . ILE B 1 247 ? 8.92300   -0.48200  -2.50800  1.000 25.00000 ? 249 ILE B CG2 1 
ATOM   4186 C CD1 . ILE B 1 247 ? 11.99500  0.29100   -2.41800  1.000 33.39000 ? 249 ILE B CD1 1 
ATOM   4187 N N   . LEU B 1 248 ? 7.66600   -0.03700  -6.07300  1.000 23.38000 ? 250 LEU B N   1 
ATOM   4188 C CA  . LEU B 1 248 ? 6.28100   0.18300   -6.45900  1.000 23.53000 ? 250 LEU B CA  1 
ATOM   4189 C C   . LEU B 1 248 ? 5.81200   -0.80900  -7.50900  1.000 27.87000 ? 250 LEU B C   1 
ATOM   4190 O O   . LEU B 1 248 ? 4.63700   -0.76700  -7.88600  1.000 25.57000 ? 250 LEU B O   1 
ATOM   4191 C CB  . LEU B 1 248 ? 6.09500   1.61800   -6.97000  1.000 22.42000 ? 250 LEU B CB  1 
ATOM   4192 C CG  . LEU B 1 248 ? 6.20700   2.71100   -5.90200  1.000 21.46000 ? 250 LEU B CG  1 
ATOM   4193 C CD1 . LEU B 1 248 ? 6.43300   4.07500   -6.54200  1.000 19.88000 ? 250 LEU B CD1 1 
ATOM   4194 C CD2 . LEU B 1 248 ? 4.96800   2.74100   -5.00000  1.000 20.57000 ? 250 LEU B CD2 1 
ATOM   4195 N N   . GLY B 1 249 ? 6.70600   -1.68600  -7.97700  1.000 27.91000 ? 251 GLY B N   1 
ATOM   4196 C CA  . GLY B 1 249 ? 6.41000   -2.67100  -8.99400  1.000 29.98000 ? 251 GLY B CA  1 
ATOM   4197 C C   . GLY B 1 249 ? 5.11200   -3.42400  -8.78400  1.000 31.27000 ? 251 GLY B C   1 
ATOM   4198 O O   . GLY B 1 249 ? 4.23000   -3.41700  -9.64800  1.000 34.39000 ? 251 GLY B O   1 
ATOM   4199 N N   . PRO B 1 250 ? 4.96600   -4.09400  -7.63300  1.000 33.39000 ? 252 PRO B N   1 
ATOM   4200 C CA  . PRO B 1 250 ? 3.73000   -4.86100  -7.39100  1.000 33.82000 ? 252 PRO B CA  1 
ATOM   4201 C C   . PRO B 1 250 ? 2.46300   -4.02900  -7.47300  1.000 34.12000 ? 252 PRO B C   1 
ATOM   4202 O O   . PRO B 1 250 ? 1.45900   -4.49900  -8.02300  1.000 37.33000 ? 252 PRO B O   1 
ATOM   4203 C CB  . PRO B 1 250 ? 3.94700   -5.42200  -5.98100  1.000 33.24000 ? 252 PRO B CB  1 
ATOM   4204 C CG  . PRO B 1 250 ? 5.40800   -5.51900  -5.84300  1.000 37.10000 ? 252 PRO B CG  1 
ATOM   4205 C CD  . PRO B 1 250 ? 5.97000   -4.33700  -6.58100  1.000 35.85000 ? 252 PRO B CD  1 
ATOM   4206 N N   . LEU B 1 251 ? 2.47900   -2.80200  -6.94100  1.000 30.53000 ? 253 LEU B N   1 
ATOM   4207 C CA  . LEU B 1 251 ? 1.29100   -1.95800  -6.99600  1.000 32.27000 ? 253 LEU B CA  1 
ATOM   4208 C C   . LEU B 1 251 ? 0.98900   -1.52900  -8.42600  1.000 30.43000 ? 253 LEU B C   1 
ATOM   4209 O O   . LEU B 1 251 ? -0.18000  -1.43000  -8.81500  1.000 32.05000 ? 253 LEU B O   1 
ATOM   4210 C CB  . LEU B 1 251 ? 1.46000   -0.72900  -6.10000  1.000 30.77000 ? 253 LEU B CB  1 
ATOM   4211 C CG  . LEU B 1 251 ? 1.34100   -0.89700  -4.58300  1.000 33.81000 ? 253 LEU B CG  1 
ATOM   4212 C CD1 . LEU B 1 251 ? 1.52400   0.45600   -3.88800  1.000 23.43000 ? 253 LEU B CD1 1 
ATOM   4213 C CD2 . LEU B 1 251 ? 0.00300   -1.53000  -4.20500  1.000 30.14000 ? 253 LEU B CD2 1 
ATOM   4214 N N   . SER B 1 252 ? 2.02900   -1.27200  -9.22400  1.000 32.82000 ? 254 SER B N   1 
ATOM   4215 C CA  . SER B 1 252 ? 1.80500   -0.92700  -10.62600 1.000 34.10000 ? 254 SER B CA  1 
ATOM   4216 C C   . SER B 1 252 ? 1.25400   -2.11700  -11.39900 1.000 34.34000 ? 254 SER B C   1 
ATOM   4217 O O   . SER B 1 252 ? 0.37600   -1.95600  -12.25200 1.000 32.30000 ? 254 SER B O   1 
ATOM   4218 C CB  . SER B 1 252 ? 3.09900   -0.43300  -11.27300 1.000 30.65000 ? 254 SER B CB  1 
ATOM   4219 O OG  . SER B 1 252 ? 4.14500   -1.37100  -11.12100 1.000 39.00000 ? 254 SER B OG  1 
ATOM   4220 N N   . ALA B 1 253 ? 1.76500   -3.31600  -11.11700 1.000 32.13000 ? 255 ALA B N   1 
ATOM   4221 C CA  . ALA B 1 253 ? 1.21800   -4.51400  -11.74300 1.000 37.48000 ? 255 ALA B CA  1 
ATOM   4222 C C   . ALA B 1 253 ? -0.23400  -4.72600  -11.34200 1.000 37.61000 ? 255 ALA B C   1 
ATOM   4223 O O   . ALA B 1 253 ? -1.07300  -5.07700  -12.17700 1.000 42.16000 ? 255 ALA B O   1 
ATOM   4224 C CB  . ALA B 1 253 ? 2.05500   -5.73600  -11.36600 1.000 37.97000 ? 255 ALA B CB  1 
ATOM   4225 N N   . GLN B 1 254 ? -0.55500  -4.49900  -10.07000 1.000 40.22000 ? 256 GLN B N   1 
ATOM   4226 C CA  . GLN B 1 254 ? -1.91400  -4.74500  -9.60200  1.000 38.08000 ? 256 GLN B CA  1 
ATOM   4227 C C   . GLN B 1 254 ? -2.91900  -3.82600  -10.28300 1.000 41.08000 ? 256 GLN B C   1 
ATOM   4228 O O   . GLN B 1 254 ? -4.04000  -4.24700  -10.59600 1.000 39.31000 ? 256 GLN B O   1 
ATOM   4229 C CB  . GLN B 1 254 ? -1.97600  -4.58900  -8.08400  1.000 43.48000 ? 256 GLN B CB  1 
ATOM   4230 C CG  . GLN B 1 254 ? -2.98100  -5.50500  -7.42400  1.000 51.25000 ? 256 GLN B CG  1 
ATOM   4231 C CD  . GLN B 1 254 ? -3.46900  -4.95000  -6.11200  1.000 49.91000 ? 256 GLN B CD  1 
ATOM   4232 O OE1 . GLN B 1 254 ? -4.67500  -4.83000  -5.89200  1.000 47.52000 ? 256 GLN B OE1 1 
ATOM   4233 N NE2 . GLN B 1 254 ? -2.53300  -4.60100  -5.22800  1.000 43.44000 ? 256 GLN B NE2 1 
ATOM   4234 N N   . THR B 1 255 ? -2.53800  -2.57700  -10.53300 1.000 35.32000 ? 257 THR B N   1 
ATOM   4235 C CA  . THR B 1 255 ? -3.45200  -1.60600  -11.11800 1.000 32.48000 ? 257 THR B CA  1 
ATOM   4236 C C   . THR B 1 255 ? -3.24400  -1.39700  -12.61200 1.000 28.93000 ? 257 THR B C   1 
ATOM   4237 O O   . THR B 1 255 ? -4.04000  -0.68600  -13.23500 1.000 32.25000 ? 257 THR B O   1 
ATOM   4238 C CB  . THR B 1 255 ? -3.30000  -0.25500  -10.41500 1.000 36.71000 ? 257 THR B CB  1 
ATOM   4239 O OG1 . THR B 1 255 ? -1.95000  0.19200   -10.57200 1.000 32.56000 ? 257 THR B OG1 1 
ATOM   4240 C CG2 . THR B 1 255 ? -3.61600  -0.38800  -8.93400  1.000 36.55000 ? 257 THR B CG2 1 
ATOM   4241 N N   . GLY B 1 256 ? -2.19400  -1.97200  -13.19600 1.000 30.45000 ? 258 GLY B N   1 
ATOM   4242 C CA  . GLY B 1 256 ? -1.87500  -1.68900  -14.58200 1.000 36.92000 ? 258 GLY B CA  1 
ATOM   4243 C C   . GLY B 1 256 ? -1.50300  -0.24800  -14.86100 1.000 36.94000 ? 258 GLY B C   1 
ATOM   4244 O O   . GLY B 1 256 ? -1.67100  0.22200   -15.99000 1.000 36.33000 ? 258 GLY B O   1 
ATOM   4245 N N   . ILE B 1 257 ? -1.00600  0.47500   -13.86300 1.000 32.70000 ? 259 ILE B N   1 
ATOM   4246 C CA  . ILE B 1 257 ? -0.59200  1.86300   -14.02500 1.000 29.49000 ? 259 ILE B CA  1 
ATOM   4247 C C   . ILE B 1 257 ? 0.91000   1.90800   -13.79800 1.000 29.03000 ? 259 ILE B C   1 
ATOM   4248 O O   . ILE B 1 257 ? 1.37800   1.71700   -12.67000 1.000 31.10000 ? 259 ILE B O   1 
ATOM   4249 C CB  . ILE B 1 257 ? -1.33300  2.79100   -13.05700 1.000 29.69000 ? 259 ILE B CB  1 
ATOM   4250 C CG1 . ILE B 1 257 ? -2.83900  2.58500   -13.20100 1.000 30.80000 ? 259 ILE B CG1 1 
ATOM   4251 C CG2 . ILE B 1 257 ? -0.94700  4.25000   -13.29800 1.000 27.08000 ? 259 ILE B CG2 1 
ATOM   4252 C CD1 . ILE B 1 257 ? -3.64600  3.41300   -12.25700 1.000 29.48000 ? 259 ILE B CD1 1 
ATOM   4253 N N   . ALA B 1 258 ? 1.66700   2.14000   -14.87200 1.000 24.64000 ? 260 ALA B N   1 
ATOM   4254 C CA  . ALA B 1 258 ? 3.11400   2.26700   -14.76500 1.000 25.68000 ? 260 ALA B CA  1 
ATOM   4255 C C   . ALA B 1 258 ? 3.47700   3.32300   -13.72900 1.000 18.20000 ? 260 ALA B C   1 
ATOM   4256 O O   . ALA B 1 258 ? 2.73600   4.28100   -13.50600 1.000 18.76000 ? 260 ALA B O   1 
ATOM   4257 C CB  . ALA B 1 258 ? 3.71700   2.63900   -16.12300 1.000 22.88000 ? 260 ALA B CB  1 
ATOM   4258 N N   . VAL B 1 259 ? 4.63400   3.14600   -13.09300 1.000 22.89000 ? 261 VAL B N   1 
ATOM   4259 C CA  . VAL B 1 259 ? 5.03300   4.07500   -12.03900 1.000 19.55000 ? 261 VAL B CA  1 
ATOM   4260 C C   . VAL B 1 259 ? 5.19700   5.48400   -12.60000 1.000 20.42000 ? 261 VAL B C   1 
ATOM   4261 O O   . VAL B 1 259 ? 4.73300   6.46700   -12.00900 1.000 21.16000 ? 261 VAL B O   1 
ATOM   4262 C CB  . VAL B 1 259 ? 6.31400   3.58700   -11.34600 1.000 23.50000 ? 261 VAL B CB  1 
ATOM   4263 C CG1 . VAL B 1 259 ? 6.81200   4.64000   -10.35400 1.000 19.90000 ? 261 VAL B CG1 1 
ATOM   4264 C CG2 . VAL B 1 259 ? 6.05000   2.26400   -10.62600 1.000 20.78000 ? 261 VAL B CG2 1 
ATOM   4265 N N   . LEU B 1 260 ? 5.86600   5.60900   -13.74200 1.000 21.87000 ? 262 LEU B N   1 
ATOM   4266 C CA  . LEU B 1 260 ? 6.05400   6.93700   -14.31700 1.000 22.74000 ? 262 LEU B CA  1 
ATOM   4267 C C   . LEU B 1 260 ? 4.74000   7.55000   -14.79000 1.000 22.87000 ? 262 LEU B C   1 
ATOM   4268 O O   . LEU B 1 260 ? 4.63100   8.78000   -14.84200 1.000 21.20000 ? 262 LEU B O   1 
ATOM   4269 C CB  . LEU B 1 260 ? 7.07300   6.87300   -15.45300 1.000 20.38000 ? 262 LEU B CB  1 
ATOM   4270 C CG  . LEU B 1 260 ? 8.47100   6.48100   -14.95800 1.000 21.92000 ? 262 LEU B CG  1 
ATOM   4271 C CD1 . LEU B 1 260 ? 9.43900   6.34200   -16.12200 1.000 29.80000 ? 262 LEU B CD1 1 
ATOM   4272 C CD2 . LEU B 1 260 ? 8.98000   7.50200   -13.94300 1.000 20.60000 ? 262 LEU B CD2 1 
ATOM   4273 N N   . ASP B 1 261 ? 3.73500   6.72900   -15.11200 1.000 25.08000 ? 263 ASP B N   1 
ATOM   4274 C CA  . ASP B 1 261 ? 2.39600   7.26800   -15.33800 1.000 23.88000 ? 263 ASP B CA  1 
ATOM   4275 C C   . ASP B 1 261 ? 1.81900   7.85100   -14.05200 1.000 18.61000 ? 263 ASP B C   1 
ATOM   4276 O O   . ASP B 1 261 ? 1.19600   8.91700   -14.06900 1.000 18.08000 ? 263 ASP B O   1 
ATOM   4277 C CB  . ASP B 1 261 ? 1.46000   6.18200   -15.88000 1.000 26.46000 ? 263 ASP B CB  1 
ATOM   4278 C CG  . ASP B 1 261 ? 1.66200   5.91500   -17.35400 1.000 36.97000 ? 263 ASP B CG  1 
ATOM   4279 O OD1 . ASP B 1 261 ? 2.48400   6.62300   -17.97900 1.000 37.02000 ? 263 ASP B OD1 1 
ATOM   4280 O OD2 . ASP B 1 261 ? 0.99700   4.99300   -17.88500 1.000 35.58000 ? 263 ASP B OD2 1 
ATOM   4281 N N   . MET B 1 262 ? 1.99300   7.15200   -12.92700 1.000 19.89000 ? 264 MET B N   1 
ATOM   4282 C CA  . MET B 1 262 ? 1.50100   7.69300   -11.66400 1.000 18.27000 ? 264 MET B CA  1 
ATOM   4283 C C   . MET B 1 262 ? 2.29400   8.92400   -11.24200 1.000 15.92000 ? 264 MET B C   1 
ATOM   4284 O O   . MET B 1 262 ? 1.72700   9.84100   -10.64500 1.000 18.32000 ? 264 MET B O   1 
ATOM   4285 C CB  . MET B 1 262 ? 1.53800   6.63100   -10.55900 1.000 20.66000 ? 264 MET B CB  1 
ATOM   4286 C CG  . MET B 1 262 ? 0.76700   7.05300   -9.30700  1.000 21.10000 ? 264 MET B CG  1 
ATOM   4287 S SD  . MET B 1 262 ? -1.02000  7.23000   -9.58500  1.000 26.71000 ? 264 MET B SD  1 
ATOM   4288 C CE  . MET B 1 262 ? -1.50800  5.52400   -9.36800  1.000 23.74000 ? 264 MET B CE  1 
ATOM   4289 N N   . CYS B 1 263 ? 3.59200   8.97600   -11.56600 1.000 17.39000 ? 265 CYS B N   1 
ATOM   4290 C CA  . CYS B 1 263 ? 4.36900   10.18200  -11.28100 1.000 18.57000 ? 265 CYS B CA  1 
ATOM   4291 C C   . CYS B 1 263 ? 3.80700   11.38200  -12.01700 1.000 17.91000 ? 265 CYS B C   1 
ATOM   4292 O O   . CYS B 1 263 ? 3.78000   12.50000  -11.48300 1.000 19.20000 ? 265 CYS B O   1 
ATOM   4293 C CB  . CYS B 1 263 ? 5.82700   9.98600   -11.68000 1.000 18.21000 ? 265 CYS B CB  1 
ATOM   4294 S SG  . CYS B 1 263 ? 6.70300   8.88000   -10.59600 1.000 18.71000 ? 265 CYS B SG  1 
ATOM   4295 N N   . ALA B 1 264 ? 3.37900   11.17300  -13.26300 1.000 18.00000 ? 266 ALA B N   1 
ATOM   4296 C CA  . ALA B 1 264 ? 2.79200   12.26500  -14.02300 1.000 19.44000 ? 266 ALA B CA  1 
ATOM   4297 C C   . ALA B 1 264 ? 1.49000   12.72600  -13.38100 1.000 19.41000 ? 266 ALA B C   1 
ATOM   4298 O O   . ALA B 1 264 ? 1.17100   13.91800  -13.39100 1.000 20.61000 ? 266 ALA B O   1 
ATOM   4299 C CB  . ALA B 1 264 ? 2.57500   11.81900  -15.46800 1.000 19.10000 ? 266 ALA B CB  1 
ATOM   4300 N N   . SER B 1 265 ? 0.73000   11.79100  -12.80900 1.000 20.42000 ? 267 SER B N   1 
ATOM   4301 C CA  . SER B 1 265 ? -0.47600  12.16300  -12.08200 1.000 19.53000 ? 267 SER B CA  1 
ATOM   4302 C C   . SER B 1 265 ? -0.13700  13.00200  -10.85600 1.000 16.18000 ? 267 SER B C   1 
ATOM   4303 O O   . SER B 1 265 ? -0.78700  14.01500  -10.58300 1.000 21.27000 ? 267 SER B O   1 
ATOM   4304 C CB  . SER B 1 265 ? -1.24600  10.89600  -11.69700 1.000 26.49000 ? 267 SER B CB  1 
ATOM   4305 O OG  . SER B 1 265 ? -2.30800  11.18800  -10.80500 1.000 35.05000 ? 267 SER B OG  1 
ATOM   4306 N N   . LEU B 1 266 ? 0.90400   12.61300  -10.11600 1.000 20.38000 ? 268 LEU B N   1 
ATOM   4307 C CA  . LEU B 1 266 ? 1.29800   13.39400  -8.94700  1.000 16.34000 ? 268 LEU B CA  1 
ATOM   4308 C C   . LEU B 1 266 ? 1.86000   14.75300  -9.35200  1.000 18.50000 ? 268 LEU B C   1 
ATOM   4309 O O   . LEU B 1 266 ? 1.60800   15.76200  -8.68300  1.000 16.12000 ? 268 LEU B O   1 
ATOM   4310 C CB  . LEU B 1 266 ? 2.31600   12.60000  -8.12100  1.000 14.31000 ? 268 LEU B CB  1 
ATOM   4311 C CG  . LEU B 1 266 ? 3.02000   13.32000  -6.96700  1.000 17.26000 ? 268 LEU B CG  1 
ATOM   4312 C CD1 . LEU B 1 266 ? 2.02200   14.03800  -6.04900  1.000 16.12000 ? 268 LEU B CD1 1 
ATOM   4313 C CD2 . LEU B 1 266 ? 3.87900   12.32000  -6.17500  1.000 17.23000 ? 268 LEU B CD2 1 
ATOM   4314 N N   . LYS B 1 267 ? 2.64200   14.79800  -10.43300 1.000 20.07000 ? 269 LYS B N   1 
ATOM   4315 C CA  . LYS B 1 267 ? 3.05600   16.08400  -10.98700 1.000 17.50000 ? 269 LYS B CA  1 
ATOM   4316 C C   . LYS B 1 267 ? 1.84500   16.98300  -11.24500 1.000 18.09000 ? 269 LYS B C   1 
ATOM   4317 O O   . LYS B 1 267 ? 1.82100   18.14200  -10.82600 1.000 21.98000 ? 269 LYS B O   1 
ATOM   4318 C CB  . LYS B 1 267 ? 3.85600   15.86500  -12.27400 1.000 17.62000 ? 269 LYS B CB  1 
ATOM   4319 C CG  . LYS B 1 267 ? 4.47600   17.13800  -12.84500 1.000 26.10000 ? 269 LYS B CG  1 
ATOM   4320 C CD  . LYS B 1 267 ? 5.13000   16.91000  -14.21000 1.000 21.84000 ? 269 LYS B CD  1 
ATOM   4321 C CE  . LYS B 1 267 ? 6.42500   16.10000  -14.07800 1.000 27.08000 ? 269 LYS B CE  1 
ATOM   4322 N NZ  . LYS B 1 267 ? 6.97600   15.73600  -15.42300 1.000 25.64000 ? 269 LYS B NZ  1 
ATOM   4323 N N   . GLU B 1 268 ? 0.81900   16.45200  -11.92500 1.000 21.75000 ? 270 GLU B N   1 
ATOM   4324 C CA  . GLU B 1 268 ? -0.38700  17.24600  -12.16900 1.000 23.86000 ? 270 GLU B CA  1 
ATOM   4325 C C   . GLU B 1 268 ? -1.02000  17.69500  -10.85400 1.000 25.87000 ? 270 GLU B C   1 
ATOM   4326 O O   . GLU B 1 268 ? -1.40100  18.86200  -10.70800 1.000 29.71000 ? 270 GLU B O   1 
ATOM   4327 C CB  . GLU B 1 268 ? -1.39300  16.45200  -13.01800 1.000 23.90000 ? 270 GLU B CB  1 
ATOM   4328 C CG  . GLU B 1 268 ? -2.74900  17.15700  -13.18200 1.000 31.33000 ? 270 GLU B CG  1 
ATOM   4329 C CD  . GLU B 1 268 ? -3.61300  16.62900  -14.33600 1.000 37.95000 ? 270 GLU B CD  1 
ATOM   4330 O OE1 . GLU B 1 268 ? -3.76800  15.39800  -14.49200 1.000 36.22000 ? 270 GLU B OE1 1 
ATOM   4331 O OE2 . GLU B 1 268 ? -4.15600  17.46900  -15.08600 1.000 42.92000 ? 270 GLU B OE2 1 
ATOM   4332 N N   . LEU B 1 269 ? -1.11000  16.78900  -9.87200  1.000 25.78000 ? 271 LEU B N   1 
ATOM   4333 C CA  . LEU B 1 269 ? -1.67300  17.15300  -8.57400  1.000 24.42000 ? 271 LEU B CA  1 
ATOM   4334 C C   . LEU B 1 269 ? -0.85900  18.25400  -7.91300  1.000 23.90000 ? 271 LEU B C   1 
ATOM   4335 O O   . LEU B 1 269 ? -1.41600  19.17300  -7.30000  1.000 29.47000 ? 271 LEU B O   1 
ATOM   4336 C CB  . LEU B 1 269 ? -1.73600  15.92300  -7.66500  1.000 22.36000 ? 271 LEU B CB  1 
ATOM   4337 C CG  . LEU B 1 269 ? -2.87000  14.95200  -7.97000  1.000 24.17000 ? 271 LEU B CG  1 
ATOM   4338 C CD1 . LEU B 1 269 ? -2.68900  13.65400  -7.18900  1.000 25.66000 ? 271 LEU B CD1 1 
ATOM   4339 C CD2 . LEU B 1 269 ? -4.22300  15.59900  -7.67600  1.000 32.30000 ? 271 LEU B CD2 1 
ATOM   4340 N N   . LEU B 1 270 ? 0.46500   18.18700  -8.03000  1.000 23.09000 ? 272 LEU B N   1 
ATOM   4341 C CA  . LEU B 1 270 ? 1.29900   19.20200  -7.40300  1.000 18.14000 ? 272 LEU B CA  1 
ATOM   4342 C C   . LEU B 1 270 ? 1.16000   20.55100  -8.10300  1.000 28.57000 ? 272 LEU B C   1 
ATOM   4343 O O   . LEU B 1 270 ? 1.13700   21.59800  -7.44600  1.000 27.58000 ? 272 LEU B O   1 
ATOM   4344 C CB  . LEU B 1 270 ? 2.75900   18.74600  -7.39200  1.000 20.49000 ? 272 LEU B CB  1 
ATOM   4345 C CG  . LEU B 1 270 ? 3.11200   17.60700  -6.42900  1.000 18.44000 ? 272 LEU B CG  1 
ATOM   4346 C CD1 . LEU B 1 270 ? 4.55300   17.15900  -6.64500  1.000 13.61000 ? 272 LEU B CD1 1 
ATOM   4347 C CD2 . LEU B 1 270 ? 2.88200   18.06400  -4.98300  1.000 18.40000 ? 272 LEU B CD2 1 
ATOM   4348 N N   . GLN B 1 271 ? 1.06100   20.54900  -9.43700  1.000 29.04000 ? 273 GLN B N   1 
ATOM   4349 C CA  . GLN B 1 271 ? 1.03900   21.80800  -10.17900 1.000 30.57000 ? 273 GLN B CA  1 
ATOM   4350 C C   . GLN B 1 271 ? -0.35300  22.43500  -10.22700 1.000 31.11000 ? 273 GLN B C   1 
ATOM   4351 O O   . GLN B 1 271 ? -0.47200  23.66400  -10.23700 1.000 35.62000 ? 273 GLN B O   1 
ATOM   4352 C CB  . GLN B 1 271 ? 1.57000   21.58300  -11.59900 1.000 25.71000 ? 273 GLN B CB  1 
ATOM   4353 C CG  . GLN B 1 271 ? 3.00200   21.05700  -11.64500 1.000 26.82000 ? 273 GLN B CG  1 
ATOM   4354 C CD  . GLN B 1 271 ? 3.53300   20.86700  -13.06400 1.000 26.76000 ? 273 GLN B CD  1 
ATOM   4355 O OE1 . GLN B 1 271 ? 2.79300   20.50600  -13.98700 1.000 24.79000 ? 273 GLN B OE1 1 
ATOM   4356 N NE2 . GLN B 1 271 ? 4.82400   21.10500  -13.23700 1.000 23.56000 ? 273 GLN B NE2 1 
ATOM   4357 N N   . ASN B 1 272 ? -1.40700  21.62100  -10.25200 1.000 34.08000 ? 274 ASN B N   1 
ATOM   4358 C CA  . ASN B 1 272 ? -2.77800  22.11300  -10.33900 1.000 36.89000 ? 274 ASN B CA  1 
ATOM   4359 C C   . ASN B 1 272 ? -3.51000  22.10500  -9.00400  1.000 42.57000 ? 274 ASN B C   1 
ATOM   4360 O O   . ASN B 1 272 ? -4.60600  22.66800  -8.91800  1.000 42.52000 ? 274 ASN B O   1 
ATOM   4361 C CB  . ASN B 1 272 ? -3.58900  21.27700  -11.34200 1.000 37.93000 ? 274 ASN B CB  1 
ATOM   4362 C CG  . ASN B 1 272 ? -3.06200  21.37900  -12.75800 1.000 37.32000 ? 274 ASN B CG  1 
ATOM   4363 O OD1 . ASN B 1 272 ? -2.38800  22.34400  -13.12100 1.000 44.13000 ? 274 ASN B OD1 1 
ATOM   4364 N ND2 . ASN B 1 272 ? -3.38000  20.38300  -13.57300 1.000 44.69000 ? 274 ASN B ND2 1 
ATOM   4365 N N   . GLY B 1 273 ? -2.94700  21.48100  -7.97100  1.000 34.11000 ? 275 GLY B N   1 
ATOM   4366 C CA  . GLY B 1 273 ? -3.65700  21.31800  -6.71900  1.000 35.62000 ? 275 GLY B CA  1 
ATOM   4367 C C   . GLY B 1 273 ? -4.78500  20.30600  -6.84900  1.000 40.08000 ? 275 GLY B C   1 
ATOM   4368 O O   . GLY B 1 273 ? -4.99400  19.67300  -7.88500  1.000 39.19000 ? 275 GLY B O   1 
ATOM   4369 N N   . MET B 1 274 ? -5.52900  20.15800  -5.75900  1.000 41.40000 ? 276 MET B N   1 
ATOM   4370 C CA  . MET B 1 274 ? -6.60600  19.18100  -5.71300  1.000 43.28000 ? 276 MET B CA  1 
ATOM   4371 C C   . MET B 1 274 ? -7.97100  19.80100  -6.01200  1.000 51.50000 ? 276 MET B C   1 
ATOM   4372 O O   . MET B 1 274 ? -8.98700  19.09600  -5.93600  1.000 54.77000 ? 276 MET B O   1 
ATOM   4373 C CB  . MET B 1 274 ? -6.59600  18.46500  -4.35300  1.000 44.46000 ? 276 MET B CB  1 
ATOM   4374 C CG  . MET B 1 274 ? -5.41000  17.48300  -4.20300  1.000 41.36000 ? 276 MET B CG  1 
ATOM   4375 S SD  . MET B 1 274 ? -5.31900  16.61400  -2.62000  1.000 52.12000 ? 276 MET B SD  1 
ATOM   4376 C CE  . MET B 1 274 ? -6.84900  15.68700  -2.68000  1.000 37.44000 ? 276 MET B CE  1 
ATOM   4377 N N   . ASN B 1 275 ? -7.99700  21.09800  -6.37400  1.000 52.99000 ? 277 ASN B N   1 
ATOM   4378 C CA  . ASN B 1 275 ? -9.19500  21.84400  -6.81200  1.000 56.11000 ? 277 ASN B CA  1 
ATOM   4379 C C   . ASN B 1 275 ? -10.34500 21.75200  -5.80200  1.000 55.73000 ? 277 ASN B C   1 
ATOM   4380 O O   . ASN B 1 275 ? -11.51400 21.99400  -6.13400  1.000 58.47000 ? 277 ASN B O   1 
ATOM   4381 C CB  . ASN B 1 275 ? -9.60900  21.44200  -8.24200  1.000 55.24000 ? 277 ASN B CB  1 
ATOM   4382 C CG  . ASN B 1 275 ? -10.22400 20.06600  -8.33500  1.000 58.27000 ? 277 ASN B CG  1 
ATOM   4383 O OD1 . ASN B 1 275 ? -11.19500 19.74100  -7.63900  1.000 61.27000 ? 277 ASN B OD1 1 
ATOM   4384 N ND2 . ASN B 1 275 ? -9.64900  19.23400  -9.20400  1.000 54.80000 ? 277 ASN B ND2 1 
ATOM   4385 N N   . GLY B 1 276 ? -9.98400  21.48600  -4.53700  1.000 56.69000 ? 278 GLY B N   1 
ATOM   4386 C CA  . GLY B 1 276 ? -10.93900 21.29100  -3.46700  1.000 57.01000 ? 278 GLY B CA  1 
ATOM   4387 C C   . GLY B 1 276 ? -11.49800 19.89400  -3.37000  1.000 55.32000 ? 278 GLY B C   1 
ATOM   4388 O O   . GLY B 1 276 ? -12.34300 19.63600  -2.49700  1.000 55.12000 ? 278 GLY B O   1 
ATOM   4389 N N   . ARG B 1 277 ? -11.08600 18.99900  -4.25900  1.000 53.28000 ? 279 ARG B N   1 
ATOM   4390 C CA  . ARG B 1 277 ? -11.46000 17.60400  -4.21600  1.000 44.51000 ? 279 ARG B CA  1 
ATOM   4391 C C   . ARG B 1 277 ? -10.63400 16.89400  -3.15000  1.000 44.96000 ? 279 ARG B C   1 
ATOM   4392 O O   . ARG B 1 277 ? -9.73800  17.47400  -2.52900  1.000 48.59000 ? 279 ARG B O   1 
ATOM   4393 C CB  . ARG B 1 277 ? -11.26200 16.96300  -5.58800  1.000 43.55000 ? 279 ARG B CB  1 
ATOM   4394 N N   . THR B 1 278 ? -10.95100 15.62200  -2.93100  1.000 39.73000 ? 280 THR B N   1 
ATOM   4395 C CA  . THR B 1 278 ? -10.29400 14.84000  -1.89600  1.000 41.06000 ? 280 THR B CA  1 
ATOM   4396 C C   . THR B 1 278 ? -9.94700  13.46600  -2.44500  1.000 34.15000 ? 280 THR B C   1 
ATOM   4397 O O   . THR B 1 278 ? -10.60400 12.95800  -3.35600  1.000 34.96000 ? 280 THR B O   1 
ATOM   4398 C CB  . THR B 1 278 ? -11.16800 14.67300  -0.63300  1.000 38.46000 ? 280 THR B CB  1 
ATOM   4399 O OG1 . THR B 1 278 ? -12.25700 13.78300  -0.91600  1.000 40.82000 ? 280 THR B OG1 1 
ATOM   4400 C CG2 . THR B 1 278 ? -11.71000 16.01500  -0.14600  1.000 35.90000 ? 280 THR B CG2 1 
ATOM   4401 N N   . ILE B 1 279 ? -8.90000  12.87500  -1.87800  1.000 32.39000 ? 281 ILE B N   1 
ATOM   4402 C CA  . ILE B 1 279 ? -8.46700  11.52500  -2.21000  1.000 32.51000 ? 281 ILE B CA  1 
ATOM   4403 C C   . ILE B 1 279 ? -8.49700  10.69300  -0.93600  1.000 36.39000 ? 281 ILE B C   1 
ATOM   4404 O O   . ILE B 1 279 ? -7.90800  11.08500  0.07900   1.000 34.29000 ? 281 ILE B O   1 
ATOM   4405 C CB  . ILE B 1 279 ? -7.05800  11.50900  -2.83200  1.000 32.23000 ? 281 ILE B CB  1 
ATOM   4406 C CG1 . ILE B 1 279 ? -7.03900  12.23100  -4.17700  1.000 33.96000 ? 281 ILE B CG1 1 
ATOM   4407 C CG2 . ILE B 1 279 ? -6.56700  10.08700  -3.00500  1.000 25.98000 ? 281 ILE B CG2 1 
ATOM   4408 C CD1 . ILE B 1 279 ? -5.63200  12.43500  -4.71300  1.000 32.78000 ? 281 ILE B CD1 1 
ATOM   4409 N N   . LEU B 1 280 ? -9.17200  9.54400   -0.99700  1.000 35.64000 ? 282 LEU B N   1 
ATOM   4410 C CA  . LEU B 1 280 ? -9.32800  8.65300   0.15300   1.000 36.85000 ? 282 LEU B CA  1 
ATOM   4411 C C   . LEU B 1 280 ? -9.74700  9.42000   1.40400   1.000 37.64000 ? 282 LEU B C   1 
ATOM   4412 O O   . LEU B 1 280 ? -9.26900  9.15300   2.50800   1.000 39.14000 ? 282 LEU B O   1 
ATOM   4413 C CB  . LEU B 1 280 ? -8.04700  7.86500   0.40900   1.000 38.32000 ? 282 LEU B CB  1 
ATOM   4414 C CG  . LEU B 1 280 ? -7.79400  6.75400   -0.59800  1.000 35.98000 ? 282 LEU B CG  1 
ATOM   4415 C CD1 . LEU B 1 280 ? -6.47500  6.07500   -0.30000  1.000 33.05000 ? 282 LEU B CD1 1 
ATOM   4416 C CD2 . LEU B 1 280 ? -8.94500  5.75900   -0.58000  1.000 36.83000 ? 282 LEU B CD2 1 
ATOM   4417 N N   . GLY B 1 281 ? -10.63400 10.39900  1.22100   1.000 40.75000 ? 283 GLY B N   1 
ATOM   4418 C CA  . GLY B 1 281 ? -11.13300 11.22000  2.30300   1.000 40.16000 ? 283 GLY B CA  1 
ATOM   4419 C C   . GLY B 1 281 ? -10.22600 12.35000  2.73600   1.000 39.78000 ? 283 GLY B C   1 
ATOM   4420 O O   . GLY B 1 281 ? -10.64200 13.17400  3.56100   1.000 37.16000 ? 283 GLY B O   1 
ATOM   4421 N N   . SER B 1 282 ? -9.00700  12.42900  2.21400   1.000 37.28000 ? 284 SER B N   1 
ATOM   4422 C CA  . SER B 1 282 ? -8.06500  13.46400  2.61500   1.000 33.95000 ? 284 SER B CA  1 
ATOM   4423 C C   . SER B 1 282 ? -8.01400  14.58100  1.58000   1.000 33.28000 ? 284 SER B C   1 
ATOM   4424 O O   . SER B 1 282 ? -8.09500  14.32800  0.37800   1.000 34.49000 ? 284 SER B O   1 
ATOM   4425 C CB  . SER B 1 282 ? -6.66900  12.87100  2.80600   1.000 32.55000 ? 284 SER B CB  1 
ATOM   4426 O OG  . SER B 1 282 ? -5.70200  13.87400  2.60900   1.000 32.42000 ? 284 SER B OG  1 
ATOM   4427 N N   . ALA B 1 283 ? -7.86800  15.81700  2.05800   1.000 36.29000 ? 285 ALA B N   1 
ATOM   4428 C CA  . ALA B 1 283 ? -7.68300  16.97800  1.19800   1.000 35.64000 ? 285 ALA B CA  1 
ATOM   4429 C C   . ALA B 1 283 ? -6.22100  17.27600  0.90200   1.000 34.95000 ? 285 ALA B C   1 
ATOM   4430 O O   . ALA B 1 283 ? -5.93500  18.17400  0.10400   1.000 37.91000 ? 285 ALA B O   1 
ATOM   4431 C CB  . ALA B 1 283 ? -8.32300  18.21700  1.83200   1.000 35.41000 ? 285 ALA B CB  1 
ATOM   4432 N N   . LEU B 1 284 ? -5.29600  16.56700  1.53700   1.000 32.69000 ? 286 LEU B N   1 
ATOM   4433 C CA  . LEU B 1 284 ? -3.87400  16.76300  1.33500   1.000 33.50000 ? 286 LEU B CA  1 
ATOM   4434 C C   . LEU B 1 284 ? -3.25900  15.45600  0.85700   1.000 32.12000 ? 286 LEU B C   1 
ATOM   4435 O O   . LEU B 1 284 ? -3.85400  14.38300  0.98500   1.000 32.49000 ? 286 LEU B O   1 
ATOM   4436 C CB  . LEU B 1 284 ? -3.19500  17.24600  2.62500   1.000 27.90000 ? 286 LEU B CB  1 
ATOM   4437 N N   . LEU B 1 285 ? -2.06200  15.55300  0.28800   1.000 30.38000 ? 287 LEU B N   1 
ATOM   4438 C CA  . LEU B 1 285 ? -1.36300  14.37800  -0.22100  1.000 24.53000 ? 287 LEU B CA  1 
ATOM   4439 C C   . LEU B 1 285 ? -0.71300  13.65000  0.95300   1.000 26.51000 ? 287 LEU B C   1 
ATOM   4440 O O   . LEU B 1 285 ? 0.19500   14.17800  1.59900   1.000 27.27000 ? 287 LEU B O   1 
ATOM   4441 C CB  . LEU B 1 285 ? -0.34000  14.79000  -1.27600  1.000 23.98000 ? 287 LEU B CB  1 
ATOM   4442 C CG  . LEU B 1 285 ? -1.00000  15.47100  -2.48500  1.000 27.04000 ? 287 LEU B CG  1 
ATOM   4443 C CD1 . LEU B 1 285 ? 0.02600   16.00300  -3.48400  1.000 26.33000 ? 287 LEU B CD1 1 
ATOM   4444 C CD2 . LEU B 1 285 ? -1.97800  14.51200  -3.16200  1.000 24.10000 ? 287 LEU B CD2 1 
ATOM   4445 N N   . GLU B 1 286 ? -1.18000  12.43800  1.22100   1.000 23.09000 ? 288 GLU B N   1 
ATOM   4446 C CA  . GLU B 1 286 ? -0.74000  11.65900  2.37200   1.000 23.40000 ? 288 GLU B CA  1 
ATOM   4447 C C   . GLU B 1 286 ? 0.57700   10.94200  2.07800   1.000 18.18000 ? 288 GLU B C   1 
ATOM   4448 O O   . GLU B 1 286 ? 0.70500   10.25700  1.05800   1.000 14.13000 ? 288 GLU B O   1 
ATOM   4449 C CB  . GLU B 1 286 ? -1.83800  10.65400  2.72800   1.000 23.03000 ? 288 GLU B CB  1 
ATOM   4450 C CG  . GLU B 1 286 ? -1.49400  9.65300   3.78800   1.000 28.53000 ? 288 GLU B CG  1 
ATOM   4451 C CD  . GLU B 1 286 ? -1.27400  10.29900  5.15000   1.000 34.61000 ? 288 GLU B CD  1 
ATOM   4452 O OE1 . GLU B 1 286 ? -0.24600  9.99000   5.79300   1.000 31.28000 ? 288 GLU B OE1 1 
ATOM   4453 O OE2 . GLU B 1 286 ? -2.12000  11.12400  5.56600   1.000 37.24000 ? 288 GLU B OE2 1 
ATOM   4454 N N   . ASP B 1 287 ? 1.56400   11.07600  2.98300   1.000 15.18000 ? 289 ASP B N   1 
ATOM   4455 C CA  . ASP B 1 287 ? 2.86400   10.45300  2.74300   1.000 18.71000 ? 289 ASP B CA  1 
ATOM   4456 C C   . ASP B 1 287 ? 3.32900   9.52900   3.87100   1.000 20.08000 ? 289 ASP B C   1 
ATOM   4457 O O   . ASP B 1 287 ? 4.52600   9.22900   3.95300   1.000 14.50000 ? 289 ASP B O   1 
ATOM   4458 C CB  . ASP B 1 287 ? 3.94200   11.51000  2.46100   1.000 16.30000 ? 289 ASP B CB  1 
ATOM   4459 C CG  . ASP B 1 287 ? 4.35000   12.32700  3.69700   1.000 19.28000 ? 289 ASP B CG  1 
ATOM   4460 O OD1 . ASP B 1 287 ? 3.57600   12.41900  4.68200   1.000 21.83000 ? 289 ASP B OD1 1 
ATOM   4461 O OD2 . ASP B 1 287 ? 5.46200   12.91400  3.66500   1.000 17.63000 ? 289 ASP B OD2 1 
ATOM   4462 N N   . GLU B 1 288 ? 2.42800   9.03500   4.72100   1.000 18.42000 ? 290 GLU B N   1 
ATOM   4463 C CA  . GLU B 1 288 ? 2.83100   8.11400   5.77900   1.000 21.02000 ? 290 GLU B CA  1 
ATOM   4464 C C   . GLU B 1 288 ? 2.27800   6.70400   5.56900   1.000 25.33000 ? 290 GLU B C   1 
ATOM   4465 O O   . GLU B 1 288 ? 2.08200   5.96000   6.53400   1.000 23.72000 ? 290 GLU B O   1 
ATOM   4466 C CB  . GLU B 1 288 ? 2.44500   8.68000   7.14500   1.000 22.14000 ? 290 GLU B CB  1 
ATOM   4467 C CG  . GLU B 1 288 ? 3.04900   10.07800  7.36700   1.000 21.30000 ? 290 GLU B CG  1 
ATOM   4468 C CD  . GLU B 1 288 ? 3.39600   10.38300  8.81800   1.000 28.71000 ? 290 GLU B CD  1 
ATOM   4469 O OE1 . GLU B 1 288 ? 2.88800   9.66400   9.71000   1.000 24.15000 ? 290 GLU B OE1 1 
ATOM   4470 O OE2 . GLU B 1 288 ? 4.16600   11.35600  9.06700   1.000 22.98000 ? 290 GLU B OE2 1 
ATOM   4471 N N   . PHE B 1 289 ? 2.04600   6.31600   4.31000   1.000 16.74000 ? 291 PHE B N   1 
ATOM   4472 C CA  . PHE B 1 289 ? 1.82200   4.92600   3.92700   1.000 21.62000 ? 291 PHE B CA  1 
ATOM   4473 C C   . PHE B 1 289 ? 2.96400   4.48100   3.02900   1.000 20.96000 ? 291 PHE B C   1 
ATOM   4474 O O   . PHE B 1 289 ? 3.16900   5.06400   1.95700   1.000 20.31000 ? 291 PHE B O   1 
ATOM   4475 C CB  . PHE B 1 289 ? 0.50900   4.74300   3.16700   1.000 24.83000 ? 291 PHE B CB  1 
ATOM   4476 C CG  . PHE B 1 289 ? -0.71300  4.99100   3.97600   1.000 28.25000 ? 291 PHE B CG  1 
ATOM   4477 C CD1 . PHE B 1 289 ? -1.27900  3.97500   4.73200   1.000 32.50000 ? 291 PHE B CD1 1 
ATOM   4478 C CD2 . PHE B 1 289 ? -1.32100  6.22700   3.95700   1.000 27.27000 ? 291 PHE B CD2 1 
ATOM   4479 C CE1 . PHE B 1 289 ? -2.42900  4.20100   5.47100   1.000 30.61000 ? 291 PHE B CE1 1 
ATOM   4480 C CE2 . PHE B 1 289 ? -2.47100  6.46200   4.69600   1.000 34.87000 ? 291 PHE B CE2 1 
ATOM   4481 C CZ  . PHE B 1 289 ? -3.02600  5.44500   5.45200   1.000 34.25000 ? 291 PHE B CZ  1 
ATOM   4482 N N   . THR B 1 290 ? 3.65600   3.44500   3.42200   1.000 19.53000 ? 292 THR B N   1 
ATOM   4483 C CA  . THR B 1 290 ? 4.70200   2.91900   2.55900   1.000 22.01000 ? 292 THR B CA  1 
ATOM   4484 C C   . THR B 1 290 ? 4.12500   1.92500   1.55900   1.000 21.25000 ? 292 THR B C   1 
ATOM   4485 O O   . THR B 1 290 ? 3.00700   1.43000   1.72700   1.000 21.41000 ? 292 THR B O   1 
ATOM   4486 C CB  . THR B 1 290 ? 5.78500   2.23500   3.38800   1.000 21.67000 ? 292 THR B CB  1 
ATOM   4487 O OG1 . THR B 1 290 ? 5.29900   0.96600   3.85000   1.000 24.29000 ? 292 THR B OG1 1 
ATOM   4488 C CG2 . THR B 1 290 ? 6.20300   3.11600   4.58000   1.000 24.11000 ? 292 THR B CG2 1 
ATOM   4489 N N   . PRO B 1 291 ? 4.86000   1.63400   0.48900   1.000 21.39000 ? 293 PRO B N   1 
ATOM   4490 C CA  . PRO B 1 291 ? 4.41900   0.57300   -0.43400  1.000 23.50000 ? 293 PRO B CA  1 
ATOM   4491 C C   . PRO B 1 291 ? 4.04700   -0.73500  0.25500   1.000 28.39000 ? 293 PRO B C   1 
ATOM   4492 O O   . PRO B 1 291 ? 3.03600   -1.35400  -0.10600  1.000 28.64000 ? 293 PRO B O   1 
ATOM   4493 C CB  . PRO B 1 291 ? 5.63400   0.41700   -1.35400  1.000 22.03000 ? 293 PRO B CB  1 
ATOM   4494 C CG  . PRO B 1 291 ? 6.17000   1.82400   -1.46000  1.000 23.72000 ? 293 PRO B CG  1 
ATOM   4495 C CD  . PRO B 1 291 ? 5.95500   2.44300   -0.08100  1.000 21.55000 ? 293 PRO B CD  1 
ATOM   4496 N N   . PHE B 1 292 ? 4.83600   -1.16400  1.24200   1.000 28.02000 ? 294 PHE B N   1 
ATOM   4497 C CA  . PHE B 1 292 ? 4.49800   -2.35300  2.02700   1.000 30.23000 ? 294 PHE B CA  1 
ATOM   4498 C C   . PHE B 1 292 ? 3.17300   -2.17500  2.76300   1.000 29.90000 ? 294 PHE B C   1 
ATOM   4499 O O   . PHE B 1 292 ? 2.28800   -3.03800  2.68700   1.000 30.59000 ? 294 PHE B O   1 
ATOM   4500 C CB  . PHE B 1 292 ? 5.62800   -2.65500  3.01200   1.000 30.51000 ? 294 PHE B CB  1 
ATOM   4501 C CG  . PHE B 1 292 ? 5.35700   -3.83100  3.92700   1.000 41.59000 ? 294 PHE B CG  1 
ATOM   4502 C CD1 . PHE B 1 292 ? 5.63300   -5.12800  3.51400   1.000 45.66000 ? 294 PHE B CD1 1 
ATOM   4503 C CD2 . PHE B 1 292 ? 4.83800   -3.63400  5.20200   1.000 40.25000 ? 294 PHE B CD2 1 
ATOM   4504 C CE1 . PHE B 1 292 ? 5.39300   -6.20700  4.35000   1.000 45.94000 ? 294 PHE B CE1 1 
ATOM   4505 C CE2 . PHE B 1 292 ? 4.59500   -4.71300  6.04400   1.000 44.48000 ? 294 PHE B CE2 1 
ATOM   4506 C CZ  . PHE B 1 292 ? 4.87300   -5.99800  5.61400   1.000 38.09000 ? 294 PHE B CZ  1 
ATOM   4507 N N   . ASP B 1 293 ? 3.02500   -1.06000  3.49000   1.000 23.50000 ? 295 ASP B N   1 
ATOM   4508 C CA  . ASP B 1 293 ? 1.77800   -0.77600  4.20100   1.000 27.61000 ? 295 ASP B CA  1 
ATOM   4509 C C   . ASP B 1 293 ? 0.56900   -0.90400  3.28500   1.000 34.97000 ? 295 ASP B C   1 
ATOM   4510 O O   . ASP B 1 293 ? -0.45500  -1.48800  3.66200   1.000 33.15000 ? 295 ASP B O   1 
ATOM   4511 C CB  . ASP B 1 293 ? 1.81100   0.62900   4.79900   1.000 25.62000 ? 295 ASP B CB  1 
ATOM   4512 C CG  . ASP B 1 293 ? 2.89500   0.79500   5.83400   1.000 29.76000 ? 295 ASP B CG  1 
ATOM   4513 O OD1 . ASP B 1 293 ? 3.30800   -0.22700  6.43400   1.000 28.36000 ? 295 ASP B OD1 1 
ATOM   4514 O OD2 . ASP B 1 293 ? 3.33400   1.94800   6.03300   1.000 25.13000 ? 295 ASP B OD2 1 
ATOM   4515 N N   . VAL B 1 294 ? 0.66200   -0.33200  2.08300   1.000 28.39000 ? 296 VAL B N   1 
ATOM   4516 C CA  . VAL B 1 294 ? -0.45900  -0.38800  1.15100   1.000 31.69000 ? 296 VAL B CA  1 
ATOM   4517 C C   . VAL B 1 294 ? -0.69500  -1.82100  0.70000   1.000 34.06000 ? 296 VAL B C   1 
ATOM   4518 O O   . VAL B 1 294 ? -1.83900  -2.28800  0.64800   1.000 38.88000 ? 296 VAL B O   1 
ATOM   4519 C CB  . VAL B 1 294 ? -0.20900  0.55300   -0.04200  1.000 24.62000 ? 296 VAL B CB  1 
ATOM   4520 C CG1 . VAL B 1 294 ? -1.21900  0.27700   -1.17100  1.000 32.14000 ? 296 VAL B CG1 1 
ATOM   4521 C CG2 . VAL B 1 294 ? -0.28700  1.99600   0.40600   1.000 25.65000 ? 296 VAL B CG2 1 
ATOM   4522 N N   . VAL B 1 295 ? 0.38100   -2.54500  0.38800   1.000 30.35000 ? 297 VAL B N   1 
ATOM   4523 C CA  . VAL B 1 295 ? 0.24700   -3.93600  -0.03700  1.000 34.40000 ? 297 VAL B CA  1 
ATOM   4524 C C   . VAL B 1 295 ? -0.35700  -4.77600  1.08400   1.000 41.11000 ? 297 VAL B C   1 
ATOM   4525 O O   . VAL B 1 295 ? -1.30700  -5.53900  0.86900   1.000 40.18000 ? 297 VAL B O   1 
ATOM   4526 C CB  . VAL B 1 295 ? 1.60900   -4.49000  -0.49600  1.000 33.65000 ? 297 VAL B CB  1 
ATOM   4527 C CG1 . VAL B 1 295 ? 1.61800   -6.01400  -0.45400  1.000 37.97000 ? 297 VAL B CG1 1 
ATOM   4528 C CG2 . VAL B 1 295 ? 1.93600   -4.00000  -1.90100  1.000 35.04000 ? 297 VAL B CG2 1 
ATOM   4529 N N   . ARG B 1 296 ? 0.17100   -4.62700  2.30400   1.000 39.84000 ? 298 ARG B N   1 
ATOM   4530 C CA  . ARG B 1 296 ? -0.29200  -5.45100  3.41600   1.000 39.61000 ? 298 ARG B CA  1 
ATOM   4531 C C   . ARG B 1 296 ? -1.77600  -5.23300  3.69100   1.000 43.07000 ? 298 ARG B C   1 
ATOM   4532 O O   . ARG B 1 296 ? -2.49000  -6.17200  4.05800   1.000 51.91000 ? 298 ARG B O   1 
ATOM   4533 C CB  . ARG B 1 296 ? 0.54000   -5.16100  4.66800   1.000 36.49000 ? 298 ARG B CB  1 
ATOM   4534 N N   . GLN B 1 297 ? -2.26300  -4.01100  3.49900   1.000 41.85000 ? 299 GLN B N   1 
ATOM   4535 C CA  . GLN B 1 297 ? -3.65700  -3.70300  3.78900   1.000 42.80000 ? 299 GLN B CA  1 
ATOM   4536 C C   . GLN B 1 297 ? -4.59000  -4.00200  2.62100   1.000 48.41000 ? 299 GLN B C   1 
ATOM   4537 O O   . GLN B 1 297 ? -5.76500  -4.31200  2.84300   1.000 50.45000 ? 299 GLN B O   1 
ATOM   4538 C CB  . GLN B 1 297 ? -3.79600  -2.23400  4.19500   1.000 35.10000 ? 299 GLN B CB  1 
ATOM   4539 C CG  . GLN B 1 297 ? -5.22100  -1.81100  4.50300   1.000 36.79000 ? 299 GLN B CG  1 
ATOM   4540 C CD  . GLN B 1 297 ? -5.28700  -0.56400  5.34600   1.000 38.21000 ? 299 GLN B CD  1 
ATOM   4541 O OE1 . GLN B 1 297 ? -6.35000  0.04400   5.49300   1.000 38.99000 ? 299 GLN B OE1 1 
ATOM   4542 N NE2 . GLN B 1 297 ? -4.14300  -0.16500  5.90400   1.000 36.11000 ? 299 GLN B NE2 1 
ATOM   4543 N N   . CYS B 1 298 ? -4.10200  -3.92300  1.38700   1.000 49.08000 ? 300 CYS B N   1 
ATOM   4544 C CA  . CYS B 1 298 ? -4.95100  -4.15800  0.22300   1.000 46.92000 ? 300 CYS B CA  1 
ATOM   4545 C C   . CYS B 1 298 ? -4.87200  -5.61600  -0.22500  1.000 51.19000 ? 300 CYS B C   1 
ATOM   4546 O O   . CYS B 1 298 ? -5.83800  -6.16700  -0.76400  1.000 51.71000 ? 300 CYS B O   1 
ATOM   4547 C CB  . CYS B 1 298 ? -4.55700  -3.22900  -0.92800  1.000 46.06000 ? 300 CYS B CB  1 
ATOM   4548 S SG  . CYS B 1 298 ? -5.13600  -1.51100  -0.76300  1.000 52.42000 ? 300 CYS B SG  1 
HETATM 4549 C C02 . FHR C 2 .   ? -20.57300 -9.92100  1.78600   1.000 22.86000 ? 401 FHR A C02 1 
HETATM 4550 C C07 . FHR C 2 .   ? -23.33200 -8.25200  -3.69500  1.000 42.32000 ? 401 FHR A C07 1 
HETATM 4551 C C08 . FHR C 2 .   ? -22.31000 -7.17700  -3.68600  1.000 34.02000 ? 401 FHR A C08 1 
HETATM 4552 C C09 . FHR C 2 .   ? -21.32100 -7.07100  -2.55100  1.000 33.81000 ? 401 FHR A C09 1 
HETATM 4553 C C10 . FHR C 2 .   ? -21.37500 -8.11500  -1.37700  1.000 29.05000 ? 401 FHR A C10 1 
HETATM 4554 C C05 . FHR C 2 .   ? -22.32700 -9.12800  -1.39000  1.000 33.57000 ? 401 FHR A C05 1 
HETATM 4555 C C06 . FHR C 2 .   ? -23.37700 -9.24800  -2.56600  1.000 40.29000 ? 401 FHR A C06 1 
HETATM 4556 C C04 . FHR C 2 .   ? -22.14200 -9.88800  -0.25900  1.000 35.40000 ? 401 FHR A C04 1 
HETATM 4557 C C03 . FHR C 2 .   ? -21.07800 -9.34700  0.44700   1.000 27.21000 ? 401 FHR A C03 1 
HETATM 4558 N N11 . FHR C 2 .   ? -20.60100 -8.24800  -0.23100  1.000 26.77000 ? 401 FHR A N11 1 
HETATM 4559 O O01 . FHR C 2 .   ? -20.00200 -9.24300  2.56200   1.000 19.84000 ? 401 FHR A O01 1 
HETATM 4560 N N12 . FHR C 2 .   ? -20.83400 -11.32600 2.08900   1.000 17.51000 ? 401 FHR A N12 1 
HETATM 4561 C C13 . FHR C 2 .   ? -20.38000 -11.83900 3.38100   1.000 18.55000 ? 401 FHR A C13 1 
HETATM 4562 C C21 . FHR C 2 .   ? -18.86700 -11.83800 3.47500   1.000 18.13000 ? 401 FHR A C21 1 
HETATM 4563 O O33 . FHR C 2 .   ? -18.19900 -12.10000 2.55900   1.000 18.17000 ? 401 FHR A O33 1 
HETATM 4564 C C14 . FHR C 2 .   ? -20.86900 -13.26500 3.55100   1.000 16.71000 ? 401 FHR A C14 1 
HETATM 4565 C C15 . FHR C 2 .   ? -22.41900 -13.32300 3.48400   1.000 19.85000 ? 401 FHR A C15 1 
HETATM 4566 C C20 . FHR C 2 .   ? -22.85800 -14.74800 3.88500   1.000 19.85000 ? 401 FHR A C20 1 
HETATM 4567 C C19 . FHR C 2 .   ? -24.37400 -14.89600 4.09200   1.000 20.08000 ? 401 FHR A C19 1 
HETATM 4568 C C18 . FHR C 2 .   ? -24.99700 -13.77900 4.93500   1.000 19.85000 ? 401 FHR A C18 1 
HETATM 4569 C C17 . FHR C 2 .   ? -24.54500 -12.38000 4.48100   1.000 22.52000 ? 401 FHR A C17 1 
HETATM 4570 C C16 . FHR C 2 .   ? -23.01200 -12.28300 4.43200   1.000 19.50000 ? 401 FHR A C16 1 
HETATM 4571 O O30 . FHR C 2 .   ? -15.87400 -7.18200  4.75400   1.000 18.50000 ? 401 FHR A O30 1 
HETATM 4572 C C29 . FHR C 2 .   ? -15.65100 -7.94200  3.86500   1.000 16.04000 ? 401 FHR A C29 1 
HETATM 4573 N N28 . FHR C 2 .   ? -14.67500 -7.73300  2.61500   1.000 21.70000 ? 401 FHR A N28 1 
HETATM 4574 C C27 . FHR C 2 .   ? -14.74700 -8.82500  1.89500   1.000 24.67000 ? 401 FHR A C27 1 
HETATM 4575 C C26 . FHR C 2 .   ? -15.57100 -10.00100 2.79900   1.000 24.40000 ? 401 FHR A C26 1 
HETATM 4576 C C25 . FHR C 2 .   ? -16.29400 -9.37600  3.68200   1.000 19.50000 ? 401 FHR A C25 1 
HETATM 4577 C C24 . FHR C 2 .   ? -16.22900 -10.13000 5.09400   1.000 13.31000 ? 401 FHR A C24 1 
HETATM 4578 C C23 . FHR C 2 .   ? -16.81100 -11.53800 4.90600   1.000 16.12000 ? 401 FHR A C23 1 
HETATM 4579 N N22 . FHR C 2 .   ? -18.26800 -11.50000 4.75400   1.000 15.41000 ? 401 FHR A N22 1 
HETATM 4580 C C31 . FHR C 2 .   ? -16.53200 -12.37000 6.13800   1.000 15.26000 ? 401 FHR A C31 1 
HETATM 4581 O O32 . FHR C 2 .   ? -15.42200 -12.73300 6.32900   1.000 17.45000 ? 401 FHR A O32 1 
HETATM 4582 C C02 . FHR D 2 .   ? 11.03700  18.27300  26.06500  1.000 22.79000 ? 401 FHR B C02 1 
HETATM 4583 C C07 . FHR D 2 .   ? 12.32500  24.38000  25.01200  1.000 28.04000 ? 401 FHR B C07 1 
HETATM 4584 C C08 . FHR D 2 .   ? 11.33600  24.21800  23.93100  1.000 27.72000 ? 401 FHR B C08 1 
HETATM 4585 C C09 . FHR D 2 .   ? 10.66800  22.88800  23.71700  1.000 30.85000 ? 401 FHR B C09 1 
HETATM 4586 C C10 . FHR D 2 .   ? 11.04900  21.69500  24.65700  1.000 28.57000 ? 401 FHR B C10 1 
HETATM 4587 C C05 . FHR D 2 .   ? 11.98000  21.84100  25.67500  1.000 29.68000 ? 401 FHR B C05 1 
HETATM 4588 C C06 . FHR D 2 .   ? 12.68400  23.23400  25.91200  1.000 32.67000 ? 401 FHR B C06 1 
HETATM 4589 C C04 . FHR D 2 .   ? 12.09700  20.63500  26.32100  1.000 30.34000 ? 401 FHR B C04 1 
HETATM 4590 C C03 . FHR D 2 .   ? 11.22200  19.75700  25.69600  1.000 24.28000 ? 401 FHR B C03 1 
HETATM 4591 N N11 . FHR D 2 .   ? 10.59100  20.39800  24.67000  1.000 27.55000 ? 401 FHR B N11 1 
HETATM 4592 O O01 . FHR D 2 .   ? 10.36300  17.55400  25.41700  1.000 17.42000 ? 401 FHR B O01 1 
HETATM 4593 N N12 . FHR D 2 .   ? 11.76200  17.80000  27.23000  1.000 19.75000 ? 401 FHR B N12 1 
HETATM 4594 C C13 . FHR D 2 .   ? 11.72200  16.40900  27.65900  1.000 20.08000 ? 401 FHR B C13 1 
HETATM 4595 C C21 . FHR D 2 .   ? 10.32600  15.90300  27.94600  1.000 20.67000 ? 401 FHR B C21 1 
HETATM 4596 O O33 . FHR D 2 .   ? 9.56800   16.58700  28.51900  1.000 20.38000 ? 401 FHR B O33 1 
HETATM 4597 C C14 . FHR D 2 .   ? 12.44700  16.37100  28.98500  1.000 22.56000 ? 401 FHR B C14 1 
HETATM 4598 C C15 . FHR D 2 .   ? 13.96900  16.11800  28.82100  1.000 25.76000 ? 401 FHR B C15 1 
HETATM 4599 C C20 . FHR D 2 .   ? 14.48000  16.36900  27.39600  1.000 23.81000 ? 401 FHR B C20 1 
HETATM 4600 C C19 . FHR D 2 .   ? 15.94100  15.90400  27.30100  1.000 29.80000 ? 401 FHR B C19 1 
HETATM 4601 C C18 . FHR D 2 .   ? 16.84100  16.42700  28.43700  1.000 19.53000 ? 401 FHR B C18 1 
HETATM 4602 C C17 . FHR D 2 .   ? 16.21600  16.52900  29.84100  1.000 25.82000 ? 401 FHR B C17 1 
HETATM 4603 C C16 . FHR D 2 .   ? 14.74400  16.97600  29.81400  1.000 29.34000 ? 401 FHR B C16 1 
HETATM 4604 O O30 . FHR D 2 .   ? 6.50400   14.38900  23.94400  1.000 15.91000 ? 401 FHR B O30 1 
HETATM 4605 C C29 . FHR D 2 .   ? 6.35900   15.13500  24.85100  1.000 15.71000 ? 401 FHR B C29 1 
HETATM 4606 N N28 . FHR D 2 .   ? 5.15100   16.15500  25.06900  1.000 19.96000 ? 401 FHR B N28 1 
HETATM 4607 C C27 . FHR D 2 .   ? 5.38600   16.78300  26.19600  1.000 17.79000 ? 401 FHR B C27 1 
HETATM 4608 C C26 . FHR D 2 .   ? 6.64900   15.98600  27.00500  1.000 17.24000 ? 401 FHR B C26 1 
HETATM 4609 C C25 . FHR D 2 .   ? 7.32300   15.33600  26.08800  1.000 17.30000 ? 401 FHR B C25 1 
HETATM 4610 C C24 . FHR D 2 .   ? 7.74600   13.87100  26.60000  1.000 15.48000 ? 401 FHR B C24 1 
HETATM 4611 C C23 . FHR D 2 .   ? 8.65900   14.00700  27.82800  1.000 16.69000 ? 401 FHR B C23 1 
HETATM 4612 N N22 . FHR D 2 .   ? 9.98900   14.54600  27.51700  1.000 15.37000 ? 401 FHR B N22 1 
HETATM 4613 C C31 . FHR D 2 .   ? 8.83200   12.63700  28.44300  1.000 14.70000 ? 401 FHR B C31 1 
HETATM 4614 O O32 . FHR D 2 .   ? 7.88100   12.18300  28.99000  1.000 15.60000 ? 401 FHR B O32 1 
HETATM 4615 O O   . HOH E 3 .   ? -32.66500 30.16300  17.83000  1.000 26.25000 ? 501 HOH A O   1 
HETATM 4616 O O   . HOH E 3 .   ? -28.51800 -27.73400 16.01600  1.000 25.49000 ? 502 HOH A O   1 
HETATM 4617 O O   . HOH E 3 .   ? -24.99700 -25.22600 6.26200   1.000 33.20000 ? 503 HOH A O   1 
HETATM 4618 O O   . HOH E 3 .   ? 2.34400   10.44400  12.09800  1.000 24.13000 ? 504 HOH A O   1 
HETATM 4619 O O   . HOH E 3 .   ? -10.12800 18.03700  8.50600   1.000 35.31000 ? 505 HOH A O   1 
HETATM 4620 O O   . HOH E 3 .   ? -4.86500  31.66000  20.08500  1.000 25.84000 ? 506 HOH A O   1 
HETATM 4621 O O   . HOH E 3 .   ? -33.32200 -16.09900 12.52300  1.000 31.68000 ? 507 HOH A O   1 
HETATM 4622 O O   . HOH E 3 .   ? -20.52200 30.59400  26.07200  1.000 21.62000 ? 508 HOH A O   1 
HETATM 4623 O O   . HOH E 3 .   ? -18.97200 20.15000  6.88400   1.000 30.26000 ? 509 HOH A O   1 
HETATM 4624 O O   . HOH E 3 .   ? -16.38600 4.54100   9.80600   1.000 25.62000 ? 510 HOH A O   1 
HETATM 4625 O O   . HOH E 3 .   ? -37.49600 26.51600  16.66200  1.000 22.98000 ? 511 HOH A O   1 
HETATM 4626 O O   . HOH E 3 .   ? -17.17500 31.46900  8.34200   1.000 36.02000 ? 512 HOH A O   1 
HETATM 4627 O O   . HOH E 3 .   ? -13.79700 -14.21100 33.40100  1.000 26.23000 ? 513 HOH A O   1 
HETATM 4628 O O   . HOH E 3 .   ? -1.14400  -11.12500 15.43600  1.000 28.42000 ? 514 HOH A O   1 
HETATM 4629 O O   . HOH E 3 .   ? -13.80800 -17.78800 32.99000  1.000 22.70000 ? 515 HOH A O   1 
HETATM 4630 O O   . HOH E 3 .   ? -19.69800 -17.24300 5.97400   1.000 24.55000 ? 516 HOH A O   1 
HETATM 4631 O O   . HOH E 3 .   ? -22.50500 37.57600  22.05800  1.000 32.59000 ? 517 HOH A O   1 
HETATM 4632 O O   . HOH E 3 .   ? -25.24900 -32.53800 12.53200  1.000 29.59000 ? 518 HOH A O   1 
HETATM 4633 O O   . HOH E 3 .   ? -3.75000  6.83800   13.21100  1.000 28.92000 ? 519 HOH A O   1 
HETATM 4634 O O   . HOH E 3 .   ? -6.69600  29.24700  12.24200  1.000 31.80000 ? 520 HOH A O   1 
HETATM 4635 O O   . HOH E 3 .   ? -15.27400 7.95900   22.08600  1.000 23.40000 ? 521 HOH A O   1 
HETATM 4636 O O   . HOH E 3 .   ? -30.166   -21.379   -2.491    1.000 35.05000 ? 522 HOH A O   1 
HETATM 4637 O O   . HOH E 3 .   ? -11.16000 7.21500   22.64300  1.000 32.60000 ? 523 HOH A O   1 
HETATM 4638 O O   . HOH E 3 .   ? -25.41100 -15.45400 26.60400  1.000 41.29000 ? 524 HOH A O   1 
HETATM 4639 O O   . HOH E 3 .   ? -5.46900  -15.76000 33.56400  1.000 25.97000 ? 525 HOH A O   1 
HETATM 4640 O O   . HOH E 3 .   ? -17.69900 31.25100  29.83200  1.000 31.61000 ? 526 HOH A O   1 
HETATM 4641 O O   . HOH E 3 .   ? -20.29000 -19.97000 5.55400   1.000 25.42000 ? 527 HOH A O   1 
HETATM 4642 O O   . HOH E 3 .   ? -7.02600  -10.89600 26.92900  1.000 16.32000 ? 528 HOH A O   1 
HETATM 4643 O O   . HOH E 3 .   ? -30.41300 -30.29100 15.92800  1.000 40.53000 ? 529 HOH A O   1 
HETATM 4644 O O   . HOH E 3 .   ? -28.26100 2.57900   6.47500   1.000 27.48000 ? 530 HOH A O   1 
HETATM 4645 O O   . HOH E 3 .   ? -31.25500 -4.72900  11.12300  1.000 28.76000 ? 531 HOH A O   1 
HETATM 4646 O O   . HOH E 3 .   ? -24.46000 -12.46200 23.24100  1.000 17.84000 ? 532 HOH A O   1 
HETATM 4647 O O   . HOH E 3 .   ? -27.61600 2.51100   18.07800  1.000 28.86000 ? 533 HOH A O   1 
HETATM 4648 O O   . HOH E 3 .   ? -2.08300  -10.90000 18.63200  1.000 24.27000 ? 534 HOH A O   1 
HETATM 4649 O O   . HOH E 3 .   ? -7.71100  -5.89900  7.52900   1.000 27.74000 ? 535 HOH A O   1 
HETATM 4650 O O   . HOH E 3 .   ? -10.57000 -15.86900 8.84400   1.000 18.03000 ? 536 HOH A O   1 
HETATM 4651 O O   . HOH E 3 .   ? -29.41500 7.67600   26.99200  1.000 18.05000 ? 537 HOH A O   1 
HETATM 4652 O O   . HOH E 3 .   ? 0.48600   -25.90500 14.90100  1.000 38.88000 ? 538 HOH A O   1 
HETATM 4653 O O   . HOH E 3 .   ? -29.70200 15.38200  8.63800   1.000 22.47000 ? 539 HOH A O   1 
HETATM 4654 O O   . HOH E 3 .   ? -34.90900 21.19800  8.53700   1.000 26.76000 ? 540 HOH A O   1 
HETATM 4655 O O   . HOH E 3 .   ? -17.17900 16.85700  26.40900  1.000 16.06000 ? 541 HOH A O   1 
HETATM 4656 O O   . HOH E 3 .   ? -14.38100 30.88600  27.86700  1.000 14.91000 ? 542 HOH A O   1 
HETATM 4657 O O   . HOH E 3 .   ? -34.15500 -4.06000  7.18300   1.000 35.31000 ? 543 HOH A O   1 
HETATM 4658 O O   . HOH E 3 .   ? -6.41900  30.70800  5.58100   1.000 40.19000 ? 544 HOH A O   1 
HETATM 4659 O O   . HOH E 3 .   ? -8.21700  -13.14100 32.57400  1.000 20.29000 ? 545 HOH A O   1 
HETATM 4660 O O   . HOH E 3 .   ? -18.45000 13.50500  27.65500  1.000 23.48000 ? 546 HOH A O   1 
HETATM 4661 O O   . HOH E 3 .   ? -13.32400 5.24100   20.60900  1.000 19.51000 ? 547 HOH A O   1 
HETATM 4662 O O   . HOH E 3 .   ? -36.47300 27.43900  18.84100  1.000 28.74000 ? 548 HOH A O   1 
HETATM 4663 O O   . HOH E 3 .   ? -23.78000 19.83500  28.31100  1.000 18.69000 ? 549 HOH A O   1 
HETATM 4664 O O   . HOH E 3 .   ? -2.89000  -21.85300 20.82400  1.000 24.35000 ? 550 HOH A O   1 
HETATM 4665 O O   . HOH E 3 .   ? -29.23000 16.81300  3.65800   1.000 33.21000 ? 551 HOH A O   1 
HETATM 4666 O O   . HOH E 3 .   ? -28.00700 9.16800   18.63800  1.000 27.27000 ? 552 HOH A O   1 
HETATM 4667 O O   . HOH E 3 .   ? -15.39600 -0.37900  28.73700  1.000 25.38000 ? 553 HOH A O   1 
HETATM 4668 O O   . HOH E 3 .   ? -36.15100 -13.71500 2.67500   1.000 60.86000 ? 554 HOH A O   1 
HETATM 4669 O O   . HOH E 3 .   ? -33.84800 27.02600  12.54700  1.000 30.58000 ? 555 HOH A O   1 
HETATM 4670 O O   . HOH E 3 .   ? -5.91800  26.48000  11.70600  1.000 32.52000 ? 556 HOH A O   1 
HETATM 4671 O O   . HOH E 3 .   ? -6.40400  -17.44300 17.72900  1.000 26.27000 ? 557 HOH A O   1 
HETATM 4672 O O   . HOH E 3 .   ? -11.22400 -23.14000 12.93600  1.000 12.62000 ? 558 HOH A O   1 
HETATM 4673 O O   . HOH E 3 .   ? -30.89500 -8.10100  10.71800  1.000 20.15000 ? 559 HOH A O   1 
HETATM 4674 O O   . HOH E 3 .   ? -23.78600 -2.28600  10.34100  1.000 12.87000 ? 560 HOH A O   1 
HETATM 4675 O O   . HOH E 3 .   ? -11.93600 8.03400   14.67200  1.000 28.15000 ? 561 HOH A O   1 
HETATM 4676 O O   . HOH E 3 .   ? -15.37000 -15.42800 6.34500   1.000 23.61000 ? 562 HOH A O   1 
HETATM 4677 O O   . HOH E 3 .   ? -21.79000 24.58200  4.01200   1.000 28.00000 ? 563 HOH A O   1 
HETATM 4678 O O   . HOH E 3 .   ? -27.88600 9.23900   7.45500   1.000 29.27000 ? 564 HOH A O   1 
HETATM 4679 O O   . HOH E 3 .   ? -29.16200 12.43500  15.61900  1.000 19.90000 ? 565 HOH A O   1 
HETATM 4680 O O   . HOH E 3 .   ? -21.92400 33.16500  21.60100  1.000 27.20000 ? 566 HOH A O   1 
HETATM 4681 O O   . HOH E 3 .   ? -30.40100 -21.31100 19.12200  1.000 23.09000 ? 567 HOH A O   1 
HETATM 4682 O O   . HOH E 3 .   ? -25.16000 31.40500  14.05900  1.000 26.68000 ? 568 HOH A O   1 
HETATM 4683 O O   . HOH E 3 .   ? -11.08400 -8.83200  16.55800  1.000 13.09000 ? 569 HOH A O   1 
HETATM 4684 O O   . HOH E 3 .   ? -27.65800 10.35300  20.90100  1.000 19.40000 ? 570 HOH A O   1 
HETATM 4685 O O   . HOH E 3 .   ? -8.88700  29.37000  23.23400  1.000 12.13000 ? 571 HOH A O   1 
HETATM 4686 O O   . HOH E 3 .   ? -18.88500 -15.46900 27.65300  1.000 15.06000 ? 572 HOH A O   1 
HETATM 4687 O O   . HOH E 3 .   ? -17.79600 0.15900   22.90700  1.000 18.83000 ? 573 HOH A O   1 
HETATM 4688 O O   . HOH E 3 .   ? -16.88800 -25.27200 29.73000  1.000 21.07000 ? 574 HOH A O   1 
HETATM 4689 O O   . HOH E 3 .   ? -3.54700  24.88900  24.25400  1.000 20.72000 ? 575 HOH A O   1 
HETATM 4690 O O   . HOH E 3 .   ? -27.85900 31.38200  15.96700  1.000 33.55000 ? 576 HOH A O   1 
HETATM 4691 O O   . HOH E 3 .   ? -31.06400 -4.74600  14.07000  1.000 30.73000 ? 577 HOH A O   1 
HETATM 4692 O O   . HOH E 3 .   ? -20.58100 -23.48500 6.40100   1.000 21.88000 ? 578 HOH A O   1 
HETATM 4693 O O   . HOH E 3 .   ? -2.71400  -16.69500 29.49800  1.000 26.73000 ? 579 HOH A O   1 
HETATM 4694 O O   . HOH E 3 .   ? -13.83700 -27.55500 17.90400  1.000 13.64000 ? 580 HOH A O   1 
HETATM 4695 O O   . HOH E 3 .   ? -20.74600 21.76000  30.97200  1.000 21.82000 ? 581 HOH A O   1 
HETATM 4696 O O   . HOH E 3 .   ? -16.64500 26.58900  32.73400  1.000 23.76000 ? 582 HOH A O   1 
HETATM 4697 O O   . HOH E 3 .   ? -6.64200  4.29100   14.02000  1.000 19.43000 ? 583 HOH A O   1 
HETATM 4698 O O   . HOH E 3 .   ? -14.33400 -28.84200 30.89800  1.000 30.68000 ? 584 HOH A O   1 
HETATM 4699 O O   . HOH E 3 .   ? -14.32300 19.83300  32.06500  1.000 23.72000 ? 585 HOH A O   1 
HETATM 4700 O O   . HOH E 3 .   ? -0.60500  -10.43500 22.14800  1.000 27.11000 ? 586 HOH A O   1 
HETATM 4701 O O   . HOH E 3 .   ? -18.58800 30.86800  12.98200  1.000 19.30000 ? 587 HOH A O   1 
HETATM 4702 O O   . HOH E 3 .   ? -32.41300 -15.03700 6.18900   1.000 31.69000 ? 588 HOH A O   1 
HETATM 4703 O O   . HOH E 3 .   ? -21.95300 4.67400   4.13400   1.000 33.69000 ? 589 HOH A O   1 
HETATM 4704 O O   . HOH E 3 .   ? -14.61000 15.01400  15.00700  1.000 11.66000 ? 590 HOH A O   1 
HETATM 4705 O O   . HOH E 3 .   ? -27.93600 34.89200  19.21800  1.000 27.65000 ? 591 HOH A O   1 
HETATM 4706 O O   . HOH E 3 .   ? -19.02600 1.13300   27.81200  1.000 32.23000 ? 592 HOH A O   1 
HETATM 4707 O O   . HOH E 3 .   ? -5.03600  -14.42400 19.15500  1.000 29.39000 ? 593 HOH A O   1 
HETATM 4708 O O   . HOH E 3 .   ? -5.40400  -2.56400  27.75200  1.000 27.81000 ? 594 HOH A O   1 
HETATM 4709 O O   . HOH E 3 .   ? -30.52800 28.71100  23.65300  1.000 31.56000 ? 595 HOH A O   1 
HETATM 4710 O O   . HOH E 3 .   ? -29.80600 0.20700   14.26500  1.000 29.06000 ? 596 HOH A O   1 
HETATM 4711 O O   . HOH E 3 .   ? -16.12800 -29.48900 18.16500  1.000 22.71000 ? 597 HOH A O   1 
HETATM 4712 O O   . HOH E 3 .   ? -23.09400 20.17000  3.77100   1.000 31.74000 ? 598 HOH A O   1 
HETATM 4713 O O   . HOH E 3 .   ? -31.67000 -15.96800 15.71200  1.000 23.17000 ? 599 HOH A O   1 
HETATM 4714 O O   . HOH E 3 .   ? -22.44800 -5.50000  22.03600  1.000 15.68000 ? 600 HOH A O   1 
HETATM 4715 O O   . HOH E 3 .   ? -24.30200 -13.63200 10.16800  1.000 11.10000 ? 601 HOH A O   1 
HETATM 4716 O O   . HOH E 3 .   ? -9.52800  -6.87000  32.33300  1.000 18.77000 ? 602 HOH A O   1 
HETATM 4717 O O   . HOH E 3 .   ? -31.18500 -11.09200 22.91500  1.000 36.41000 ? 603 HOH A O   1 
HETATM 4718 O O   . HOH E 3 .   ? -5.28800  -4.18100  25.58900  1.000 18.20000 ? 604 HOH A O   1 
HETATM 4719 O O   . HOH E 3 .   ? -31.11300 -13.18800 7.31100   1.000 21.41000 ? 605 HOH A O   1 
HETATM 4720 O O   . HOH E 3 .   ? -22.50700 -7.23300  28.99900  1.000 24.01000 ? 606 HOH A O   1 
HETATM 4721 O O   . HOH E 3 .   ? -24.48900 -21.66700 23.34600  1.000 20.43000 ? 607 HOH A O   1 
HETATM 4722 O O   . HOH E 3 .   ? -20.33600 26.19500  29.50600  1.000 28.61000 ? 608 HOH A O   1 
HETATM 4723 O O   . HOH E 3 .   ? -25.77700 25.52800  25.77500  1.000 19.30000 ? 609 HOH A O   1 
HETATM 4724 O O   . HOH E 3 .   ? -1.13500  -23.18300 17.93500  1.000 19.43000 ? 610 HOH A O   1 
HETATM 4725 O O   . HOH E 3 .   ? -27.60000 1.66800   22.73400  1.000 29.70000 ? 611 HOH A O   1 
HETATM 4726 O O   . HOH E 3 .   ? -31.42500 -22.35000 4.17300   1.000 31.57000 ? 612 HOH A O   1 
HETATM 4727 O O   . HOH E 3 .   ? -13.79100 -1.65200  0.90300   1.000 37.38000 ? 613 HOH A O   1 
HETATM 4728 O O   . HOH E 3 .   ? -30.34900 -7.92600  13.41200  1.000 22.83000 ? 614 HOH A O   1 
HETATM 4729 O O   . HOH E 3 .   ? -6.05500  -18.10200 25.95400  1.000 17.99000 ? 615 HOH A O   1 
HETATM 4730 O O   . HOH E 3 .   ? -10.39700 35.17000  20.11100  1.000 29.66000 ? 616 HOH A O   1 
HETATM 4731 O O   . HOH E 3 .   ? -21.67300 14.90700  30.94600  1.000 27.27000 ? 617 HOH A O   1 
HETATM 4732 O O   . HOH E 3 .   ? -17.57900 13.28600  7.21500   1.000 33.29000 ? 618 HOH A O   1 
HETATM 4733 O O   . HOH E 3 .   ? -20.04600 10.78400  19.41000  1.000 21.07000 ? 619 HOH A O   1 
HETATM 4734 O O   . HOH E 3 .   ? -6.60800  -28.50700 15.51200  1.000 24.28000 ? 620 HOH A O   1 
HETATM 4735 O O   . HOH E 3 .   ? -24.80500 -31.65100 19.02400  1.000 27.43000 ? 621 HOH A O   1 
HETATM 4736 O O   . HOH E 3 .   ? -14.44400 13.59300  8.79600   1.000 25.53000 ? 622 HOH A O   1 
HETATM 4737 O O   . HOH E 3 .   ? -5.850    -25.937   11.543    1.000 31.31000 ? 623 HOH A O   1 
HETATM 4738 O O   . HOH E 3 .   ? -25.69400 -1.05000  25.37200  1.000 18.88000 ? 624 HOH A O   1 
HETATM 4739 O O   . HOH E 3 .   ? -14.34300 15.91500  6.62500   1.000 33.99000 ? 625 HOH A O   1 
HETATM 4740 O O   . HOH E 3 .   ? -3.60200  -12.92500 10.49700  1.000 30.03000 ? 626 HOH A O   1 
HETATM 4741 O O   . HOH E 3 .   ? -14.97900 1.13400   4.15300   1.000 28.89000 ? 627 HOH A O   1 
HETATM 4742 O O   . HOH E 3 .   ? -14.41800 -11.42700 32.92500  1.000 26.26000 ? 628 HOH A O   1 
HETATM 4743 O O   . HOH E 3 .   ? -24.36400 6.33100   1.53500   1.000 31.15000 ? 629 HOH A O   1 
HETATM 4744 O O   . HOH E 3 .   ? -23.17200 -27.03700 26.84600  1.000 29.76000 ? 630 HOH A O   1 
HETATM 4745 O O   . HOH E 3 .   ? -32.75500 24.54400  23.29800  1.000 21.21000 ? 631 HOH A O   1 
HETATM 4746 O O   . HOH E 3 .   ? -27.79000 -11.03600 25.91700  1.000 28.49000 ? 632 HOH A O   1 
HETATM 4747 O O   . HOH E 3 .   ? -3.81500  -15.56300 9.33700   1.000 32.61000 ? 633 HOH A O   1 
HETATM 4748 O O   . HOH E 3 .   ? -11.30300 8.20700   17.05200  1.000 29.82000 ? 634 HOH A O   1 
HETATM 4749 O O   . HOH E 3 .   ? -16.45800 -12.57200 33.10400  1.000 33.20000 ? 635 HOH A O   1 
HETATM 4750 O O   . HOH E 3 .   ? -12.94100 26.78200  32.09000  1.000 20.14000 ? 636 HOH A O   1 
HETATM 4751 O O   . HOH E 3 .   ? -30.63800 -10.50500 9.83800   1.000 23.27000 ? 637 HOH A O   1 
HETATM 4752 O O   . HOH E 3 .   ? -24.81300 14.50700  16.00000  1.000 13.59000 ? 638 HOH A O   1 
HETATM 4753 O O   . HOH E 3 .   ? -31.86700 -9.37000  21.37700  1.000 29.26000 ? 639 HOH A O   1 
HETATM 4754 O O   . HOH E 3 .   ? -22.65000 9.80100   19.36900  1.000 24.30000 ? 640 HOH A O   1 
HETATM 4755 O O   . HOH E 3 .   ? -4.26200  2.66200   14.81100  1.000 20.95000 ? 641 HOH A O   1 
HETATM 4756 O O   . HOH E 3 .   ? -23.61200 24.20600  27.65300  1.000 20.05000 ? 642 HOH A O   1 
HETATM 4757 O O   . HOH E 3 .   ? -16.48400 -9.26300  32.99800  1.000 21.28000 ? 643 HOH A O   1 
HETATM 4758 O O   . HOH E 3 .   ? -1.01300  -3.94800  10.38100  1.000 26.84000 ? 644 HOH A O   1 
HETATM 4759 O O   . HOH E 3 .   ? -26.30800 -27.20900 22.45400  1.000 24.14000 ? 645 HOH A O   1 
HETATM 4760 O O   . HOH E 3 .   ? -11.77600 -3.03000  2.90800   1.000 26.39000 ? 646 HOH A O   1 
HETATM 4761 O O   . HOH E 3 .   ? -32.66100 -14.87200 18.95700  1.000 28.46000 ? 647 HOH A O   1 
HETATM 4762 O O   . HOH E 3 .   ? -19.09600 24.77300  5.58800   1.000 34.26000 ? 648 HOH A O   1 
HETATM 4763 O O   . HOH E 3 .   ? -2.63400  18.18500  27.81700  1.000 39.23000 ? 649 HOH A O   1 
HETATM 4764 O O   . HOH E 3 .   ? -23.36000 4.21000   24.51600  1.000 37.06000 ? 650 HOH A O   1 
HETATM 4765 O O   . HOH E 3 .   ? -21.83900 -33.08900 21.75700  1.000 31.12000 ? 651 HOH A O   1 
HETATM 4766 O O   . HOH E 3 .   ? -16.40000 20.74400  5.87000   1.000 32.25000 ? 652 HOH A O   1 
HETATM 4767 O O   . HOH E 3 .   ? -18.43800 32.22600  26.48700  1.000 22.21000 ? 653 HOH A O   1 
HETATM 4768 O O   . HOH E 3 .   ? -18.69100 -30.96700 9.41500   1.000 29.01000 ? 654 HOH A O   1 
HETATM 4769 O O   . HOH E 3 .   ? -31.68200 -9.46800  14.96600  1.000 32.09000 ? 655 HOH A O   1 
HETATM 4770 O O   . HOH E 3 .   ? -21.09200 3.08200   24.62500  1.000 32.14000 ? 656 HOH A O   1 
HETATM 4771 O O   . HOH E 3 .   ? -25.41700 -29.75600 23.53200  1.000 29.44000 ? 657 HOH A O   1 
HETATM 4772 O O   . HOH E 3 .   ? -15.48200 14.85400  26.79800  1.000 29.45000 ? 658 HOH A O   1 
HETATM 4773 O O   . HOH E 3 .   ? -6.95200  -28.60100 23.78300  1.000 34.91000 ? 659 HOH A O   1 
HETATM 4774 O O   . HOH E 3 .   ? -33.40600 -14.38400 9.27300   1.000 33.80000 ? 660 HOH A O   1 
HETATM 4775 O O   . HOH E 3 .   ? -18.56400 -23.10700 -1.63600  1.000 41.32000 ? 661 HOH A O   1 
HETATM 4776 O O   . HOH E 3 .   ? -5.30500  -17.55200 20.59200  1.000 33.98000 ? 662 HOH A O   1 
HETATM 4777 O O   . HOH E 3 .   ? -15.73400 34.36300  11.97900  1.000 32.85000 ? 663 HOH A O   1 
HETATM 4778 O O   . HOH E 3 .   ? -3.25600  -20.74700 13.64500  1.000 33.24000 ? 664 HOH A O   1 
HETATM 4779 O O   . HOH E 3 .   ? -22.81800 22.30200  28.85500  1.000 29.22000 ? 665 HOH A O   1 
HETATM 4780 O O   . HOH E 3 .   ? -15.83500 1.78700   27.63600  1.000 33.39000 ? 666 HOH A O   1 
HETATM 4781 O O   . HOH E 3 .   ? -25.07600 -5.46600  22.99700  1.000 20.93000 ? 667 HOH A O   1 
HETATM 4782 O O   . HOH E 3 .   ? -2.31800  26.84700  23.25200  1.000 24.84000 ? 668 HOH A O   1 
HETATM 4783 O O   . HOH E 3 .   ? -21.57000 -25.57600 6.49800   1.000 27.63000 ? 669 HOH A O   1 
HETATM 4784 O O   . HOH E 3 .   ? -3.51700  -15.72300 31.86900  1.000 30.61000 ? 670 HOH A O   1 
HETATM 4785 O O   . HOH E 3 .   ? -32.02600 -12.15900 13.68800  1.000 31.25000 ? 671 HOH A O   1 
HETATM 4786 O O   . HOH E 3 .   ? -17.61900 -15.80900 5.57400   1.000 26.37000 ? 672 HOH A O   1 
HETATM 4787 O O   . HOH E 3 .   ? -19.29800 -15.65700 0.76800   1.000 33.58000 ? 673 HOH A O   1 
HETATM 4788 O O   . HOH E 3 .   ? -21.73800 35.53900  23.16800  1.000 30.35000 ? 674 HOH A O   1 
HETATM 4789 O O   . HOH E 3 .   ? -37.079   23.788    8.580     1.000 29.64000 ? 675 HOH A O   1 
HETATM 4790 O O   . HOH E 3 .   ? -18.45500 -10.64700 32.45500  1.000 38.42000 ? 676 HOH A O   1 
HETATM 4791 O O   . HOH E 3 .   ? -25.21100 11.82500  15.35400  1.000 25.12000 ? 677 HOH A O   1 
HETATM 4792 O O   . HOH E 3 .   ? -24.76200 -34.13900 18.91600  1.000 36.70000 ? 678 HOH A O   1 
HETATM 4793 O O   . HOH E 3 .   ? -18.63700 1.75400   24.92700  1.000 24.92000 ? 679 HOH A O   1 
HETATM 4794 O O   . HOH E 3 .   ? -32.91100 -11.50000 9.06300   1.000 30.51000 ? 680 HOH A O   1 
HETATM 4795 O O   . HOH E 3 .   ? -17.27500 -27.51300 30.76300  1.000 29.80000 ? 681 HOH A O   1 
HETATM 4796 O O   . HOH E 3 .   ? -19.15600 9.47800   21.75500  1.000 20.42000 ? 682 HOH A O   1 
HETATM 4797 O O   . HOH E 3 .   ? -15.66900 -19.60300 33.35800  1.000 33.77000 ? 683 HOH A O   1 
HETATM 4798 O O   . HOH E 3 .   ? -13.360   29.231    31.571    1.000 25.13000 ? 684 HOH A O   1 
HETATM 4799 O O   . HOH E 3 .   ? -25.22200 8.74900   21.87200  1.000 32.22000 ? 685 HOH A O   1 
HETATM 4800 O O   . HOH E 3 .   ? -0.56800  -20.58900 15.32800  1.000 37.02000 ? 686 HOH A O   1 
HETATM 4801 O O   . HOH E 3 .   ? -35.09000 18.72300  10.25700  1.000 31.13000 ? 687 HOH A O   1 
HETATM 4802 O O   . HOH E 3 .   ? -14.889   -15.080   36.142    1.000 40.46000 ? 688 HOH A O   1 
HETATM 4803 O O   . HOH E 3 .   ? -23.77500 -20.11100 25.27900  1.000 27.51000 ? 689 HOH A O   1 
HETATM 4804 O O   . HOH E 3 .   ? -22.06900 -9.94600  30.06000  1.000 39.86000 ? 690 HOH A O   1 
HETATM 4805 O O   . HOH E 3 .   ? -29.47700 10.27000  16.94400  1.000 31.99000 ? 691 HOH A O   1 
HETATM 4806 O O   . HOH E 3 .   ? -11.964   1.201     37.859    1.000 38.19000 ? 692 HOH A O   1 
HETATM 4807 O O   . HOH E 3 .   ? -33.49600 -7.75000  11.46100  1.000 39.43000 ? 693 HOH A O   1 
HETATM 4808 O O   . HOH E 3 .   ? -26.88000 27.82400  26.53300  1.000 24.26000 ? 694 HOH A O   1 
HETATM 4809 O O   . HOH E 3 .   ? -13.58100 17.35000  32.81400  1.000 33.63000 ? 695 HOH A O   1 
HETATM 4810 O O   . HOH E 3 .   ? -16.01500 16.48900  33.84400  1.000 36.56000 ? 696 HOH A O   1 
HETATM 4811 O O   . HOH E 3 .   ? -0.649    19.104    25.994    1.000 30.61000 ? 697 HOH A O   1 
HETATM 4812 O O   . HOH F 3 .   ? 1.97200   17.80100  -1.16800  1.000 25.84000 ? 501 HOH B O   1 
HETATM 4813 O O   . HOH F 3 .   ? 15.90300  7.75200   43.25100  1.000 36.53000 ? 502 HOH B O   1 
HETATM 4814 O O   . HOH F 3 .   ? 16.03500  12.53200  5.00100   1.000 24.70000 ? 503 HOH B O   1 
HETATM 4815 O O   . HOH F 3 .   ? 0.94200   8.17600   10.20900  1.000 27.29000 ? 504 HOH B O   1 
HETATM 4816 O O   . HOH F 3 .   ? -5.79600  6.69400   26.03100  1.000 41.05000 ? 505 HOH B O   1 
HETATM 4817 O O   . HOH F 3 .   ? 10.17700  -7.83200  13.15300  1.000 25.94000 ? 506 HOH B O   1 
HETATM 4818 O O   . HOH F 3 .   ? 7.19200   -13.42800 19.79100  1.000 27.66000 ? 507 HOH B O   1 
HETATM 4819 O O   . HOH F 3 .   ? 17.12400  -7.46700  27.39000  1.000 27.42000 ? 508 HOH B O   1 
HETATM 4820 O O   . HOH F 3 .   ? 12.26000  -1.06300  41.82600  1.000 36.30000 ? 509 HOH B O   1 
HETATM 4821 O O   . HOH F 3 .   ? 18.55200  25.80100  21.20100  1.000 26.79000 ? 510 HOH B O   1 
HETATM 4822 O O   . HOH F 3 .   ? 4.86600   -0.06900  9.58100   1.000 19.10000 ? 511 HOH B O   1 
HETATM 4823 O O   . HOH F 3 .   ? 22.20000  3.25600   16.53600  1.000 29.74000 ? 512 HOH B O   1 
HETATM 4824 O O   . HOH F 3 .   ? 16.07900  4.36600   -2.82600  1.000 24.87000 ? 513 HOH B O   1 
HETATM 4825 O O   . HOH F 3 .   ? 16.39700  15.34300  -11.90800 1.000 29.98000 ? 514 HOH B O   1 
HETATM 4826 O O   . HOH F 3 .   ? 16.25200  -0.16000  8.80600   1.000 33.10000 ? 515 HOH B O   1 
HETATM 4827 O O   . HOH F 3 .   ? -0.49800  10.04000  23.71500  1.000 23.03000 ? 516 HOH B O   1 
HETATM 4828 O O   . HOH F 3 .   ? 15.46600  12.27200  38.19300  1.000 29.50000 ? 517 HOH B O   1 
HETATM 4829 O O   . HOH F 3 .   ? 5.45300   11.04100  11.46000  1.000 19.75000 ? 518 HOH B O   1 
HETATM 4830 O O   . HOH F 3 .   ? 0.87000   -7.86300  19.40700  1.000 18.33000 ? 519 HOH B O   1 
HETATM 4831 O O   . HOH F 3 .   ? 9.22400   20.65300  13.16300  1.000 25.73000 ? 520 HOH B O   1 
HETATM 4832 O O   . HOH F 3 .   ? 2.15900   -1.66200  8.29200   1.000 29.55000 ? 521 HOH B O   1 
HETATM 4833 O O   . HOH F 3 .   ? 4.94600   8.22900   32.70300  1.000 18.47000 ? 522 HOH B O   1 
HETATM 4834 O O   . HOH F 3 .   ? 6.88600   19.12700  0.91800   1.000 28.40000 ? 523 HOH B O   1 
HETATM 4835 O O   . HOH F 3 .   ? 1.67800   15.43700  -15.48500 1.000 29.59000 ? 524 HOH B O   1 
HETATM 4836 O O   . HOH F 3 .   ? 16.50800  0.02900   17.59200  1.000 17.37000 ? 525 HOH B O   1 
HETATM 4837 O O   . HOH F 3 .   ? 18.46000  -6.63600  18.05800  1.000 23.56000 ? 526 HOH B O   1 
HETATM 4838 O O   . HOH F 3 .   ? 4.47900   -9.31600  25.74100  1.000 24.75000 ? 527 HOH B O   1 
HETATM 4839 O O   . HOH F 3 .   ? 15.86600  -1.41700  42.46500  1.000 36.52000 ? 528 HOH B O   1 
HETATM 4840 O O   . HOH F 3 .   ? 14.99200  9.85700   -2.00800  1.000 31.10000 ? 529 HOH B O   1 
HETATM 4841 O O   . HOH F 3 .   ? 14.14800  11.98600  16.32700  1.000 11.71000 ? 530 HOH B O   1 
HETATM 4842 O O   . HOH F 3 .   ? 17.94500  6.36100   9.69600   1.000 26.98000 ? 531 HOH B O   1 
HETATM 4843 O O   . HOH F 3 .   ? 23.27600  12.07800  39.78300  1.000 32.78000 ? 532 HOH B O   1 
HETATM 4844 O O   . HOH F 3 .   ? 13.52400  21.03700  21.87500  1.000 21.23000 ? 533 HOH B O   1 
HETATM 4845 O O   . HOH F 3 .   ? 25.648    0.817     16.982    1.000 30.72000 ? 534 HOH B O   1 
HETATM 4846 O O   . HOH F 3 .   ? 22.17100  13.25300  20.57600  1.000 11.32000 ? 535 HOH B O   1 
HETATM 4847 O O   . HOH F 3 .   ? 14.04700  16.64300  4.54400   1.000 30.46000 ? 536 HOH B O   1 
HETATM 4848 O O   . HOH F 3 .   ? 16.33400  4.64800   -13.77900 1.000 36.91000 ? 537 HOH B O   1 
HETATM 4849 O O   . HOH F 3 .   ? 20.54500  -1.46500  23.30800  1.000 22.88000 ? 538 HOH B O   1 
HETATM 4850 O O   . HOH F 3 .   ? 1.49400   7.65700   1.83300   1.000 20.49000 ? 539 HOH B O   1 
HETATM 4851 O O   . HOH F 3 .   ? 16.94500  22.45500  6.66600   1.000 32.50000 ? 540 HOH B O   1 
HETATM 4852 O O   . HOH F 3 .   ? 21.64900  11.59100  14.25500  1.000 30.93000 ? 541 HOH B O   1 
HETATM 4853 O O   . HOH F 3 .   ? 15.94800  26.76200  24.69600  1.000 25.15000 ? 542 HOH B O   1 
HETATM 4854 O O   . HOH F 3 .   ? 16.36600  17.52400  11.11200  1.000 16.11000 ? 543 HOH B O   1 
HETATM 4855 O O   . HOH F 3 .   ? -1.21700  -1.22500  6.28100   1.000 31.27000 ? 544 HOH B O   1 
HETATM 4856 O O   . HOH F 3 .   ? 9.06000   4.50400   2.17900   1.000 20.10000 ? 545 HOH B O   1 
HETATM 4857 O O   . HOH F 3 .   ? 27.19300  2.88900   31.77500  1.000 28.30000 ? 546 HOH B O   1 
HETATM 4858 O O   . HOH F 3 .   ? 19.81100  19.88500  18.21400  1.000 16.76000 ? 547 HOH B O   1 
HETATM 4859 O O   . HOH F 3 .   ? 17.37100  14.88400  7.30900   1.000 29.56000 ? 548 HOH B O   1 
HETATM 4860 O O   . HOH F 3 .   ? 7.74300   18.34300  -15.98300 1.000 25.35000 ? 549 HOH B O   1 
HETATM 4861 O O   . HOH F 3 .   ? 10.80000  -1.36600  13.13600  1.000 18.98000 ? 550 HOH B O   1 
HETATM 4862 O O   . HOH F 3 .   ? 5.82800   21.88800  21.59400  1.000 32.13000 ? 551 HOH B O   1 
HETATM 4863 O O   . HOH F 3 .   ? 14.18300  15.92200  -4.15100  1.000 26.27000 ? 552 HOH B O   1 
HETATM 4864 O O   . HOH F 3 .   ? 0.85200   12.54400  5.28200   1.000 28.39000 ? 553 HOH B O   1 
HETATM 4865 O O   . HOH F 3 .   ? 8.33900   3.27600   39.13900  1.000 28.23000 ? 554 HOH B O   1 
HETATM 4866 O O   . HOH F 3 .   ? 15.81200  24.37800  10.12200  1.000 29.44000 ? 555 HOH B O   1 
HETATM 4867 O O   . HOH F 3 .   ? 14.18800  13.55600  -19.14600 1.000 33.73000 ? 556 HOH B O   1 
HETATM 4868 O O   . HOH F 3 .   ? 24.95300  11.68800  23.80300  1.000 17.42000 ? 557 HOH B O   1 
HETATM 4869 O O   . HOH F 3 .   ? 11.54300  22.19600  14.17200  1.000 26.58000 ? 558 HOH B O   1 
HETATM 4870 O O   . HOH F 3 .   ? 0.06700   13.36600  30.34700  1.000 31.92000 ? 559 HOH B O   1 
HETATM 4871 O O   . HOH F 3 .   ? 22.76200  13.54900  23.10500  1.000 14.42000 ? 560 HOH B O   1 
HETATM 4872 O O   . HOH F 3 .   ? 15.38000  16.41300  -0.27200  1.000 33.16000 ? 561 HOH B O   1 
HETATM 4873 O O   . HOH F 3 .   ? 19.07300  -1.67700  12.15100  1.000 25.86000 ? 562 HOH B O   1 
HETATM 4874 O O   . HOH F 3 .   ? -6.08400  8.29600   3.05600   1.000 37.87000 ? 563 HOH B O   1 
HETATM 4875 O O   . HOH F 3 .   ? 18.41700  -11.20600 36.29800  1.000 33.72000 ? 564 HOH B O   1 
HETATM 4876 O O   . HOH F 3 .   ? 25.51400  17.42300  34.81300  1.000 30.37000 ? 565 HOH B O   1 
HETATM 4877 O O   . HOH F 3 .   ? 18.42900  27.48700  23.27900  1.000 30.69000 ? 566 HOH B O   1 
HETATM 4878 O O   . HOH F 3 .   ? 27.99800  4.50800   23.51000  1.000 27.04000 ? 567 HOH B O   1 
HETATM 4879 O O   . HOH F 3 .   ? 1.07500   21.66300  -4.62000  1.000 34.24000 ? 568 HOH B O   1 
HETATM 4880 O O   . HOH F 3 .   ? 6.50000   -0.29000  6.08800   1.000 27.10000 ? 569 HOH B O   1 
HETATM 4881 O O   . HOH F 3 .   ? 22.32100  10.57800  19.54800  1.000 16.17000 ? 570 HOH B O   1 
HETATM 4882 O O   . HOH F 3 .   ? 1.28900   3.19300   7.92100   1.000 27.00000 ? 571 HOH B O   1 
HETATM 4883 O O   . HOH F 3 .   ? 5.51200   1.54600   24.39400  1.000 15.61000 ? 572 HOH B O   1 
HETATM 4884 O O   . HOH F 3 .   ? 12.90300  7.77200   -16.84900 1.000 23.37000 ? 573 HOH B O   1 
HETATM 4885 O O   . HOH F 3 .   ? 2.62000   -8.91300  11.39800  1.000 33.14000 ? 574 HOH B O   1 
HETATM 4886 O O   . HOH F 3 .   ? 3.38900   15.83700  16.26100  1.000 23.82000 ? 575 HOH B O   1 
HETATM 4887 O O   . HOH F 3 .   ? 16.11700  14.28900  3.14100   1.000 33.41000 ? 576 HOH B O   1 
HETATM 4888 O O   . HOH F 3 .   ? -2.68200  7.00700   -15.76700 1.000 32.61000 ? 577 HOH B O   1 
HETATM 4889 O O   . HOH F 3 .   ? 12.12800  4.44500   -13.94700 1.000 29.51000 ? 578 HOH B O   1 
HETATM 4890 O O   . HOH F 3 .   ? 8.42400   11.68000  31.76600  1.000 24.92000 ? 579 HOH B O   1 
HETATM 4891 O O   . HOH F 3 .   ? 17.47300  10.93000  27.34600  1.000 10.44000 ? 580 HOH B O   1 
HETATM 4892 O O   . HOH F 3 .   ? -2.83900  4.71100   13.12300  1.000 16.90000 ? 581 HOH B O   1 
HETATM 4893 O O   . HOH F 3 .   ? 19.87900  8.03300   10.86000  1.000 31.72000 ? 582 HOH B O   1 
HETATM 4894 O O   . HOH F 3 .   ? 8.17800   0.26900   7.71000   1.000 28.64000 ? 583 HOH B O   1 
HETATM 4895 O O   . HOH F 3 .   ? 3.67700   -1.36000  34.61700  1.000 31.12000 ? 584 HOH B O   1 
HETATM 4896 O O   . HOH F 3 .   ? 11.20000  22.82300  16.52500  1.000 22.03000 ? 585 HOH B O   1 
HETATM 4897 O O   . HOH F 3 .   ? -6.38500  11.32400  -28.26200 1.000 27.31000 ? 586 HOH B O   1 
HETATM 4898 O O   . HOH F 3 .   ? 9.20900   18.27100  11.52200  1.000 24.80000 ? 587 HOH B O   1 
HETATM 4899 O O   . HOH F 3 .   ? 9.06300   13.92600  -18.86700 1.000 26.49000 ? 588 HOH B O   1 
HETATM 4900 O O   . HOH F 3 .   ? 20.99300  -5.42000  27.28900  1.000 30.13000 ? 589 HOH B O   1 
HETATM 4901 O O   . HOH F 3 .   ? 0.57600   -1.98600  10.37600  1.000 29.46000 ? 590 HOH B O   1 
HETATM 4902 O O   . HOH F 3 .   ? 22.88600  -3.00100  32.44100  1.000 33.55000 ? 591 HOH B O   1 
HETATM 4903 O O   . HOH F 3 .   ? 14.29300  -12.51500 20.60300  1.000 25.74000 ? 592 HOH B O   1 
HETATM 4904 O O   . HOH F 3 .   ? 10.67500  9.09600   -1.95600  1.000 15.59000 ? 593 HOH B O   1 
HETATM 4905 O O   . HOH F 3 .   ? 7.66600   -0.46400  1.47700   1.000 23.69000 ? 594 HOH B O   1 
HETATM 4906 O O   . HOH F 3 .   ? 2.28700   17.49200  24.46100  1.000 28.05000 ? 595 HOH B O   1 
HETATM 4907 O O   . HOH F 3 .   ? 19.87200  10.47000  12.03500  1.000 19.71000 ? 596 HOH B O   1 
HETATM 4908 O O   . HOH F 3 .   ? -1.03900  1.52100   7.92900   1.000 23.92000 ? 597 HOH B O   1 
HETATM 4909 O O   . HOH F 3 .   ? 22.58900  9.10900   15.54400  1.000 24.24000 ? 598 HOH B O   1 
HETATM 4910 O O   . HOH F 3 .   ? -1.09100  18.33200  -0.11100  1.000 31.38000 ? 599 HOH B O   1 
HETATM 4911 O O   . HOH F 3 .   ? 18.03800  3.27300   -6.79400  1.000 28.75000 ? 600 HOH B O   1 
HETATM 4912 O O   . HOH F 3 .   ? 27.41600  4.85900   25.89100  1.000 26.79000 ? 601 HOH B O   1 
HETATM 4913 O O   . HOH F 3 .   ? 19.41400  25.17100  29.89700  1.000 50.08000 ? 602 HOH B O   1 
HETATM 4914 O O   . HOH F 3 .   ? 25.97400  9.10800   22.37300  1.000 25.56000 ? 603 HOH B O   1 
HETATM 4915 O O   . HOH F 3 .   ? 5.28500   -9.61200  32.84000  1.000 31.66000 ? 604 HOH B O   1 
HETATM 4916 O O   . HOH F 3 .   ? 14.22200  -1.56300  -4.58500  1.000 37.67000 ? 605 HOH B O   1 
HETATM 4917 O O   . HOH F 3 .   ? 15.06300  9.93900   -16.51300 1.000 22.21000 ? 606 HOH B O   1 
HETATM 4918 O O   . HOH F 3 .   ? 22.76900  15.10000  17.61500  1.000 20.23000 ? 607 HOH B O   1 
HETATM 4919 O O   . HOH F 3 .   ? 6.79500   -3.32600  8.59900   1.000 32.16000 ? 608 HOH B O   1 
HETATM 4920 O O   . HOH F 3 .   ? 26.17800  1.57500   20.75400  1.000 27.31000 ? 609 HOH B O   1 
HETATM 4921 O O   . HOH F 3 .   ? 14.503    21.227    -9.222    1.000 27.66000 ? 610 HOH B O   1 
HETATM 4922 O O   . HOH F 3 .   ? 7.23000   18.21300  10.01400  1.000 32.03000 ? 611 HOH B O   1 
HETATM 4923 O O   . HOH F 3 .   ? 14.32400  14.93500  -6.61600  1.000 23.38000 ? 612 HOH B O   1 
HETATM 4924 O O   . HOH F 3 .   ? 24.13800  9.35600   20.73500  1.000 23.06000 ? 613 HOH B O   1 
HETATM 4925 O O   . HOH F 3 .   ? 16.52800  11.06100  -11.64300 1.000 28.68000 ? 614 HOH B O   1 
HETATM 4926 O O   . HOH F 3 .   ? 25.68200  -0.89900  37.97100  1.000 27.02000 ? 615 HOH B O   1 
HETATM 4927 O O   . HOH F 3 .   ? 15.25100  5.95700   3.14900   1.000 29.39000 ? 616 HOH B O   1 
HETATM 4928 O O   . HOH F 3 .   ? 4.90300   10.70800  34.20300  1.000 32.72000 ? 617 HOH B O   1 
HETATM 4929 O O   . HOH F 3 .   ? 7.47700   3.30100   -15.09400 1.000 25.28000 ? 618 HOH B O   1 
HETATM 4930 O O   . HOH F 3 .   ? 27.26800  23.24000  26.18900  1.000 23.44000 ? 619 HOH B O   1 
HETATM 4931 O O   . HOH F 3 .   ? 22.90700  12.96600  16.57200  1.000 28.05000 ? 620 HOH B O   1 
HETATM 4932 O O   . HOH F 3 .   ? 12.92200  -0.34300  47.02200  1.000 66.71000 ? 621 HOH B O   1 
HETATM 4933 O O   . HOH F 3 .   ? -1.283    12.726    -25.681   1.000 36.47000 ? 622 HOH B O   1 
HETATM 4934 O O   . HOH F 3 .   ? 12.46200  9.59200   3.06300   1.000 29.54000 ? 623 HOH B O   1 
HETATM 4935 O O   . HOH F 3 .   ? -8.46500  -4.14500  -0.82200  1.000 46.53000 ? 624 HOH B O   1 
HETATM 4936 O O   . HOH F 3 .   ? -6.54700  3.00700   27.32500  1.000 30.91000 ? 625 HOH B O   1 
HETATM 4937 O O   . HOH F 3 .   ? 3.71400   -7.04400  32.45500  1.000 34.77000 ? 626 HOH B O   1 
HETATM 4938 O O   . HOH F 3 .   ? -0.06800  16.38700  18.15300  1.000 42.36000 ? 627 HOH B O   1 
HETATM 4939 O O   . HOH F 3 .   ? 22.61900  -5.02500  30.06100  1.000 38.47000 ? 628 HOH B O   1 
HETATM 4940 O O   . HOH F 3 .   ? 11.50900  6.37800   1.67700   1.000 27.96000 ? 629 HOH B O   1 
HETATM 4941 O O   . HOH F 3 .   ? 11.84000  23.95100  12.20600  1.000 33.25000 ? 630 HOH B O   1 
HETATM 4942 O O   . HOH F 3 .   ? 2.20500   -10.75500 25.44100  1.000 32.00000 ? 631 HOH B O   1 
HETATM 4943 O O   . HOH F 3 .   ? 12.32300  2.54100   -0.11000  1.000 35.99000 ? 632 HOH B O   1 
HETATM 4944 O O   . HOH F 3 .   ? 16.36900  6.59800   -1.32100  1.000 34.15000 ? 633 HOH B O   1 
HETATM 4945 O O   . HOH F 3 .   ? 23.29800  4.38900   14.41600  1.000 29.83000 ? 634 HOH B O   1 
HETATM 4946 O O   . HOH F 3 .   ? 18.38500  3.56300   -4.06400  1.000 35.25000 ? 635 HOH B O   1 
HETATM 4947 O O   . HOH F 3 .   ? 19.12600  -0.12400  16.73200  1.000 26.81000 ? 636 HOH B O   1 
HETATM 4948 O O   . HOH F 3 .   ? 11.42000  -3.02800  10.96600  1.000 28.38000 ? 637 HOH B O   1 
HETATM 4949 O O   . HOH F 3 .   ? 10.55800  13.22200  31.57100  1.000 29.03000 ? 638 HOH B O   1 
HETATM 4950 O O   . HOH F 3 .   ? 11.83400  8.69500   0.45000   1.000 24.38000 ? 639 HOH B O   1 
HETATM 4951 O O   . HOH F 3 .   ? 14.59400  6.96200   45.30300  1.000 41.36000 ? 640 HOH B O   1 
HETATM 4952 O O   . HOH F 3 .   ? 24.46900  14.64900  40.84100  1.000 34.48000 ? 641 HOH B O   1 
HETATM 4953 O O   . HOH F 3 .   ? 11.54700  25.29600  16.34200  1.000 28.32000 ? 642 HOH B O   1 
HETATM 4954 O O   . HOH F 3 .   ? 13.19900  26.47700  18.33400  1.000 31.62000 ? 643 HOH B O   1 
HETATM 4955 O O   . HOH F 3 .   ? 27.419    0.009     24.874    1.000 28.04000 ? 644 HOH B O   1 
HETATM 4956 O O   . HOH F 3 .   ? 13.60800  5.77600   -15.90900 1.000 26.52000 ? 645 HOH B O   1 
HETATM 4957 O O   . HOH F 3 .   ? 20.65500  12.22300  10.38700  1.000 28.94000 ? 646 HOH B O   1 
HETATM 4958 O O   . HOH F 3 .   ? 17.36800  17.25400  8.09600   1.000 34.38000 ? 647 HOH B O   1 
HETATM 4959 O O   . HOH F 3 .   ? 16.66500  8.57900   -15.67200 1.000 33.72000 ? 648 HOH B O   1 
HETATM 4960 O O   . HOH F 3 .   ? 9.76100   2.72400   0.21100   1.000 34.63000 ? 649 HOH B O   1 
HETATM 4961 O O   . HOH F 3 .   ? 7.27600   3.62600   -17.81400 1.000 33.61000 ? 650 HOH B O   1 
HETATM 4962 O O   . HOH F 3 .   ? 2.47700   20.72600  -2.56800  1.000 32.50000 ? 651 HOH B O   1 
HETATM 4963 O O   . HOH F 3 .   ? 9.97600   3.09400   -14.98600 1.000 27.96000 ? 652 HOH B O   1 
HETATM 4964 O O   . HOH F 3 .   ? 2.473     17.041    -19.300   1.000 37.17000 ? 653 HOH B O   1 
HETATM 4965 O O   . HOH F 3 .   ? 11.91200  28.05500  19.93300  1.000 34.65000 ? 654 HOH B O   1 
HETATM 4966 O O   . HOH F 3 .   ? 18.78600  14.89600  -5.30500  1.000 44.40000 ? 655 HOH B O   1 
HETATM 4967 O O   . HOH F 3 .   ? 10.05100  3.35300   -17.45700 1.000 37.97000 ? 656 HOH B O   1 
# 
