data_8Y44
# 
_entry.id   8Y44 
# 
_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   8Y44         pdb_00008y44 10.2210/pdb8y44/pdb 
WWPDB D_1300043744 ?            ?                   
# 
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 2025-02-12 ? 
2 'Structure model' 1 1 2025-03-26 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 2 'Structure model' 'Structure summary'   
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 2 'Structure model' struct          
# 
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_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.journal_volume'          
7  2 'Structure model' '_citation.page_first'              
8  2 'Structure model' '_citation.page_last'               
9  2 'Structure model' '_citation.pdbx_database_id_DOI'    
10 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
11 2 'Structure model' '_citation.title'                   
12 2 'Structure model' '_citation.year'                    
13 2 'Structure model' '_struct.title'                     
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8Y44 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              ycxu@simm.ac.cn 
_pdbx_contact_author.name_first         Yechun 
_pdbx_contact_author.name_last          Xu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1581-6155 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Nie, T.Q.' 1 ? 
'Su, H.X.'  2 ? 
'Li, M.J.'  3 ? 
'Xu, Y.C.'  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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            67 
_citation.language                  ? 
_citation.page_first                12760 
_citation.page_last                 12783 
_citation.title                     
'Discovery of Novel Nonpeptidic and Noncovalent Small Molecule 3CL pro Inhibitors as anti-SARS-CoV-2 Drug Candidate.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c00739 
_citation.pdbx_database_id_PubMed   39072488 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Jiang, Z.' 1  ?                   
primary 'Feng, B.'  2  ?                   
primary 'Chen, L.'  3  ?                   
primary 'Nie, T.'   4  ?                   
primary 'Chen, S.'  5  ?                   
primary 'Wang, L.'  6  ?                   
primary 'Liu, H.'   7  ?                   
primary 'Yu, T.'    8  ?                   
primary 'Zhang, Y.' 9  ?                   
primary 'Zheng, M.' 10 ?                   
primary 'Xu, Y.'    11 0000-0002-1581-6155 
primary 'Liu, H.'   12 0000-0003-3685-6268 
primary 'Zang, Y.'  13 ?                   
primary 'Su, H.'    14 ?                   
primary 'Zhang, L.' 15 0000-0002-2593-2571 
primary 'Li, J.'    16 ?                   
primary 'Zhou, Y.'  17 0000-0002-7684-2939 
# 
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' 33825.547 2   3.4.22.69 ? ? ? 
2 non-polymer syn 
;~{N}-[(1~{S},2~{R})-2-[(4-bromanyl-2-morpholin-4-ylcarbonyl-6-nitro-phenyl)amino]cyclohexyl]-2-oxidanylidene-1~{H}-quinoline-4-carboxamide
;
598.445   2   ?         ? ? ? 
3 water       nat water 18.015    122 ?         ? ? ? 
# 
_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       
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_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}-[(1~{S},2~{R})-2-[(4-bromanyl-2-morpholin-4-ylcarbonyl-6-nitro-phenyl)amino]cyclohexyl]-2-oxidanylidene-1~{H}-quinoline-4-carboxamide
;
A1D50 
3 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   PHE n 
1 4   ARG n 
1 5   LYS n 
1 6   MET n 
1 7   ALA n 
1 8   PHE n 
1 9   PRO n 
1 10  SER n 
1 11  GLY n 
1 12  LYS n 
1 13  VAL n 
1 14  GLU n 
1 15  GLY n 
1 16  CYS n 
1 17  MET n 
1 18  VAL n 
1 19  GLN n 
1 20  VAL n 
1 21  THR n 
1 22  CYS n 
1 23  GLY n 
1 24  THR n 
1 25  THR n 
1 26  THR n 
1 27  LEU n 
1 28  ASN n 
1 29  GLY n 
1 30  LEU n 
1 31  TRP n 
1 32  LEU n 
1 33  ASP n 
1 34  ASP n 
1 35  VAL n 
1 36  VAL n 
1 37  TYR n 
1 38  CYS n 
1 39  PRO n 
1 40  ARG n 
1 41  HIS n 
1 42  VAL n 
1 43  ILE n 
1 44  CYS n 
1 45  THR n 
1 46  SER n 
1 47  GLU n 
1 48  ASP n 
1 49  MET n 
1 50  LEU n 
1 51  ASN n 
1 52  PRO n 
1 53  ASN n 
1 54  TYR n 
1 55  GLU n 
1 56  ASP n 
1 57  LEU n 
1 58  LEU n 
1 59  ILE n 
1 60  ARG n 
1 61  LYS n 
1 62  SER n 
1 63  ASN n 
1 64  HIS n 
1 65  ASN n 
1 66  PHE n 
1 67  LEU n 
1 68  VAL n 
1 69  GLN n 
1 70  ALA n 
1 71  GLY n 
1 72  ASN n 
1 73  VAL n 
1 74  GLN n 
1 75  LEU n 
1 76  ARG n 
1 77  VAL n 
1 78  ILE n 
1 79  GLY n 
1 80  HIS n 
1 81  SER n 
1 82  MET n 
1 83  GLN n 
1 84  ASN n 
1 85  CYS n 
1 86  VAL n 
1 87  LEU n 
1 88  LYS n 
1 89  LEU n 
1 90  LYS n 
1 91  VAL n 
1 92  ASP n 
1 93  THR n 
1 94  ALA n 
1 95  ASN n 
1 96  PRO n 
1 97  LYS n 
1 98  THR n 
1 99  PRO n 
1 100 LYS n 
1 101 TYR n 
1 102 LYS n 
1 103 PHE n 
1 104 VAL n 
1 105 ARG n 
1 106 ILE n 
1 107 GLN n 
1 108 PRO n 
1 109 GLY n 
1 110 GLN n 
1 111 THR n 
1 112 PHE n 
1 113 SER n 
1 114 VAL n 
1 115 LEU n 
1 116 ALA n 
1 117 CYS n 
1 118 TYR n 
1 119 ASN n 
1 120 GLY n 
1 121 SER n 
1 122 PRO n 
1 123 SER n 
1 124 GLY n 
1 125 VAL n 
1 126 TYR n 
1 127 GLN n 
1 128 CYS n 
1 129 ALA n 
1 130 MET n 
1 131 ARG n 
1 132 PRO n 
1 133 ASN n 
1 134 PHE n 
1 135 THR n 
1 136 ILE n 
1 137 LYS n 
1 138 GLY n 
1 139 SER n 
1 140 PHE n 
1 141 LEU n 
1 142 ASN n 
1 143 GLY n 
1 144 SER n 
1 145 CYS n 
1 146 GLY n 
1 147 SER n 
1 148 VAL n 
1 149 GLY n 
1 150 PHE n 
1 151 ASN n 
1 152 ILE n 
1 153 ASP n 
1 154 TYR n 
1 155 ASP n 
1 156 CYS n 
1 157 VAL n 
1 158 SER n 
1 159 PHE n 
1 160 CYS n 
1 161 TYR n 
1 162 MET n 
1 163 HIS n 
1 164 HIS n 
1 165 MET n 
1 166 GLU n 
1 167 LEU n 
1 168 PRO n 
1 169 THR n 
1 170 GLY n 
1 171 VAL n 
1 172 HIS n 
1 173 ALA n 
1 174 GLY n 
1 175 THR n 
1 176 ASP n 
1 177 LEU n 
1 178 GLU n 
1 179 GLY n 
1 180 ASN n 
1 181 PHE n 
1 182 TYR n 
1 183 GLY n 
1 184 PRO n 
1 185 PHE n 
1 186 VAL n 
1 187 ASP n 
1 188 ARG n 
1 189 GLN n 
1 190 THR n 
1 191 ALA n 
1 192 GLN n 
1 193 ALA n 
1 194 ALA n 
1 195 GLY n 
1 196 THR n 
1 197 ASP n 
1 198 THR n 
1 199 THR n 
1 200 ILE n 
1 201 THR n 
1 202 VAL n 
1 203 ASN n 
1 204 VAL n 
1 205 LEU n 
1 206 ALA n 
1 207 TRP n 
1 208 LEU n 
1 209 TYR n 
1 210 ALA n 
1 211 ALA n 
1 212 VAL n 
1 213 ILE n 
1 214 ASN n 
1 215 GLY n 
1 216 ASP n 
1 217 ARG n 
1 218 TRP n 
1 219 PHE n 
1 220 LEU n 
1 221 ASN n 
1 222 ARG n 
1 223 PHE n 
1 224 THR n 
1 225 THR n 
1 226 THR n 
1 227 LEU n 
1 228 ASN n 
1 229 ASP n 
1 230 PHE n 
1 231 ASN n 
1 232 LEU n 
1 233 VAL n 
1 234 ALA n 
1 235 MET n 
1 236 LYS n 
1 237 TYR n 
1 238 ASN n 
1 239 TYR n 
1 240 GLU n 
1 241 PRO n 
1 242 LEU n 
1 243 THR n 
1 244 GLN n 
1 245 ASP n 
1 246 HIS n 
1 247 VAL n 
1 248 ASP n 
1 249 ILE n 
1 250 LEU n 
1 251 GLY n 
1 252 PRO n 
1 253 LEU n 
1 254 SER n 
1 255 ALA n 
1 256 GLN n 
1 257 THR n 
1 258 GLY n 
1 259 ILE n 
1 260 ALA n 
1 261 VAL n 
1 262 LEU n 
1 263 ASP n 
1 264 MET n 
1 265 CYS n 
1 266 ALA n 
1 267 SER n 
1 268 LEU n 
1 269 LYS n 
1 270 GLU n 
1 271 LEU n 
1 272 LEU n 
1 273 GLN n 
1 274 ASN n 
1 275 GLY n 
1 276 MET n 
1 277 ASN n 
1 278 GLY n 
1 279 ARG n 
1 280 THR n 
1 281 ILE n 
1 282 LEU n 
1 283 GLY n 
1 284 SER n 
1 285 ALA n 
1 286 LEU n 
1 287 LEU n 
1 288 GLU n 
1 289 ASP n 
1 290 GLU n 
1 291 PHE n 
1 292 THR n 
1 293 PRO n 
1 294 PHE n 
1 295 ASP n 
1 296 VAL n 
1 297 VAL n 
1 298 ARG n 
1 299 GLN n 
1 300 CYS n 
1 301 SER n 
1 302 GLY n 
1 303 VAL n 
1 304 THR n 
1 305 PHE n 
1 306 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   306 
_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                 ? 
_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               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_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 
A1D50 non-polymer         . 
;~{N}-[(1~{S},2~{R})-2-[(4-bromanyl-2-morpholin-4-ylcarbonyl-6-nitro-phenyl)amino]cyclohexyl]-2-oxidanylidene-1~{H}-quinoline-4-carboxamide
;
? 'C27 H28 Br N5 O6' 598.445 
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 
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   SER 1   1   1   SER SER A . n 
A 1 2   GLY 2   2   2   GLY GLY A . n 
A 1 3   PHE 3   3   3   PHE PHE A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   MET 6   6   6   MET MET A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  CYS 16  16  16  CYS CYS A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  ASN 28  28  28  ASN ASN A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  TRP 31  31  31  TRP TRP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  CYS 38  38  38  CYS CYS A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  HIS 41  41  41  HIS HIS A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  CYS 44  44  44  CYS CYS A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  MET 49  49  49  MET MET A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  ASN 51  51  51  ASN ASN A . n 
A 1 52  PRO 52  52  52  PRO PRO A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  GLN 83  83  83  GLN GLN A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  CYS 85  85  85  CYS CYS A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  PRO 99  99  99  PRO PRO A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 CYS 117 117 117 CYS CYS A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 GLN 127 127 127 GLN GLN A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 MET 130 130 130 MET MET A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 CYS 145 145 145 CYS CYS A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 TYR 154 154 154 TYR TYR A . n 
A 1 155 ASP 155 155 155 ASP ASP A . n 
A 1 156 CYS 156 156 156 CYS CYS A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 CYS 160 160 160 CYS CYS A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 MET 162 162 162 MET MET A . n 
A 1 163 HIS 163 163 163 HIS HIS A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 MET 165 165 165 MET MET A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 VAL 171 171 171 VAL VAL A . n 
A 1 172 HIS 172 172 172 HIS HIS A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 GLU 178 178 178 GLU GLU A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 GLN 189 189 189 GLN GLN A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 TRP 207 207 207 TRP TRP A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 TYR 209 209 209 TYR TYR A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 ARG 217 217 217 ARG ARG A . n 
A 1 218 TRP 218 218 218 TRP TRP A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 ASN 221 221 221 ASN ASN A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 ASN 228 228 228 ASN ASN A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 MET 235 235 235 MET MET A . n 
A 1 236 LYS 236 236 236 LYS LYS A . n 
A 1 237 TYR 237 237 237 TYR TYR A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 TYR 239 239 239 TYR TYR A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 THR 243 243 243 THR THR A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 HIS 246 246 246 HIS HIS A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 ASP 248 248 248 ASP ASP A . n 
A 1 249 ILE 249 249 249 ILE ILE A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 MET 264 264 264 MET MET A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 SER 267 267 267 SER SER A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 GLN 273 273 273 GLN GLN A . n 
A 1 274 ASN 274 274 274 ASN ASN A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 MET 276 276 276 MET MET A . n 
A 1 277 ASN 277 277 277 ASN ASN A . n 
A 1 278 GLY 278 278 278 GLY GLY A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 THR 280 280 280 THR THR A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 SER 284 284 284 SER SER A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 GLU 288 288 288 GLU GLU A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 PHE 291 291 291 PHE PHE A . n 
A 1 292 THR 292 292 292 THR THR A . n 
A 1 293 PRO 293 293 293 PRO PRO A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 GLN 299 299 299 GLN GLN A . n 
A 1 300 CYS 300 300 300 CYS CYS A . n 
A 1 301 SER 301 301 301 SER SER A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 THR 304 304 304 THR THR A . n 
A 1 305 PHE 305 305 ?   ?   ?   A . n 
A 1 306 GLN 306 306 ?   ?   ?   A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   GLY 2   2   2   GLY GLY B . n 
B 1 3   PHE 3   3   3   PHE PHE B . n 
B 1 4   ARG 4   4   4   ARG ARG B . n 
B 1 5   LYS 5   5   5   LYS LYS B . n 
B 1 6   MET 6   6   6   MET MET B . n 
B 1 7   ALA 7   7   7   ALA ALA B . n 
B 1 8   PHE 8   8   8   PHE PHE B . n 
B 1 9   PRO 9   9   9   PRO PRO B . n 
B 1 10  SER 10  10  10  SER SER B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  LYS 12  12  12  LYS LYS B . n 
B 1 13  VAL 13  13  13  VAL VAL B . n 
B 1 14  GLU 14  14  14  GLU GLU B . n 
B 1 15  GLY 15  15  15  GLY GLY B . n 
B 1 16  CYS 16  16  16  CYS CYS B . n 
B 1 17  MET 17  17  17  MET MET B . n 
B 1 18  VAL 18  18  18  VAL VAL B . n 
B 1 19  GLN 19  19  19  GLN GLN B . n 
B 1 20  VAL 20  20  20  VAL VAL B . n 
B 1 21  THR 21  21  21  THR THR B . n 
B 1 22  CYS 22  22  22  CYS CYS B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  THR 24  24  24  THR THR B . n 
B 1 25  THR 25  25  25  THR THR B . n 
B 1 26  THR 26  26  26  THR THR B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  ASN 28  28  28  ASN ASN B . n 
B 1 29  GLY 29  29  29  GLY GLY B . n 
B 1 30  LEU 30  30  30  LEU LEU B . n 
B 1 31  TRP 31  31  31  TRP TRP B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  ASP 33  33  33  ASP ASP B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  TYR 37  37  37  TYR TYR B . n 
B 1 38  CYS 38  38  38  CYS CYS B . n 
B 1 39  PRO 39  39  39  PRO PRO B . n 
B 1 40  ARG 40  40  40  ARG ARG B . n 
B 1 41  HIS 41  41  41  HIS HIS B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  ILE 43  43  43  ILE ILE B . n 
B 1 44  CYS 44  44  44  CYS CYS B . n 
B 1 45  THR 45  45  45  THR THR B . n 
B 1 46  SER 46  46  46  SER SER B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  ASP 48  48  48  ASP ASP B . n 
B 1 49  MET 49  49  49  MET MET B . n 
B 1 50  LEU 50  50  50  LEU LEU B . n 
B 1 51  ASN 51  51  51  ASN ASN B . n 
B 1 52  PRO 52  52  52  PRO PRO B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  TYR 54  54  54  TYR TYR B . n 
B 1 55  GLU 55  55  55  GLU GLU B . n 
B 1 56  ASP 56  56  56  ASP ASP B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  LEU 58  58  58  LEU LEU B . n 
B 1 59  ILE 59  59  59  ILE ILE B . n 
B 1 60  ARG 60  60  60  ARG ARG B . n 
B 1 61  LYS 61  61  61  LYS LYS B . n 
B 1 62  SER 62  62  62  SER SER B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  HIS 64  64  64  HIS HIS B . n 
B 1 65  ASN 65  65  65  ASN ASN B . n 
B 1 66  PHE 66  66  66  PHE PHE B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  GLN 69  69  69  GLN GLN B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  GLY 71  71  71  GLY GLY B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  VAL 73  73  73  VAL VAL B . n 
B 1 74  GLN 74  74  74  GLN GLN B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  ARG 76  76  76  ARG ARG B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  HIS 80  80  80  HIS HIS B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  MET 82  82  82  MET MET B . n 
B 1 83  GLN 83  83  83  GLN GLN B . n 
B 1 84  ASN 84  84  84  ASN ASN B . n 
B 1 85  CYS 85  85  85  CYS CYS B . n 
B 1 86  VAL 86  86  86  VAL VAL B . n 
B 1 87  LEU 87  87  87  LEU LEU B . n 
B 1 88  LYS 88  88  88  LYS LYS B . n 
B 1 89  LEU 89  89  89  LEU LEU B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  VAL 91  91  91  VAL VAL B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  THR 93  93  93  THR THR B . n 
B 1 94  ALA 94  94  94  ALA ALA B . n 
B 1 95  ASN 95  95  95  ASN ASN B . n 
B 1 96  PRO 96  96  96  PRO PRO B . n 
B 1 97  LYS 97  97  97  LYS LYS B . n 
B 1 98  THR 98  98  98  THR THR B . n 
B 1 99  PRO 99  99  99  PRO PRO B . n 
B 1 100 LYS 100 100 100 LYS LYS B . n 
B 1 101 TYR 101 101 101 TYR TYR B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 PHE 103 103 103 PHE PHE B . n 
B 1 104 VAL 104 104 104 VAL VAL B . n 
B 1 105 ARG 105 105 105 ARG ARG B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 PRO 108 108 108 PRO PRO B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 THR 111 111 111 THR THR B . n 
B 1 112 PHE 112 112 112 PHE PHE B . n 
B 1 113 SER 113 113 113 SER SER B . n 
B 1 114 VAL 114 114 114 VAL VAL B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 ALA 116 116 116 ALA ALA B . n 
B 1 117 CYS 117 117 117 CYS CYS B . n 
B 1 118 TYR 118 118 118 TYR TYR B . n 
B 1 119 ASN 119 119 119 ASN ASN B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 SER 121 121 121 SER SER B . n 
B 1 122 PRO 122 122 122 PRO PRO B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 GLY 124 124 124 GLY GLY B . n 
B 1 125 VAL 125 125 125 VAL VAL B . n 
B 1 126 TYR 126 126 126 TYR TYR B . n 
B 1 127 GLN 127 127 127 GLN GLN B . n 
B 1 128 CYS 128 128 128 CYS CYS B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 MET 130 130 130 MET MET B . n 
B 1 131 ARG 131 131 131 ARG ARG B . n 
B 1 132 PRO 132 132 132 PRO PRO B . n 
B 1 133 ASN 133 133 133 ASN ASN B . n 
B 1 134 PHE 134 134 134 PHE PHE B . n 
B 1 135 THR 135 135 135 THR THR B . n 
B 1 136 ILE 136 136 136 ILE ILE B . n 
B 1 137 LYS 137 137 137 LYS LYS B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 PHE 140 140 140 PHE PHE B . n 
B 1 141 LEU 141 141 141 LEU LEU B . n 
B 1 142 ASN 142 142 142 ASN ASN B . n 
B 1 143 GLY 143 143 143 GLY GLY B . n 
B 1 144 SER 144 144 144 SER SER B . n 
B 1 145 CYS 145 145 145 CYS CYS B . n 
B 1 146 GLY 146 146 146 GLY GLY B . n 
B 1 147 SER 147 147 147 SER SER B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 PHE 150 150 150 PHE PHE B . n 
B 1 151 ASN 151 151 151 ASN ASN B . n 
B 1 152 ILE 152 152 152 ILE ILE B . n 
B 1 153 ASP 153 153 153 ASP ASP B . n 
B 1 154 TYR 154 154 154 TYR TYR B . n 
B 1 155 ASP 155 155 155 ASP ASP B . n 
B 1 156 CYS 156 156 156 CYS CYS B . n 
B 1 157 VAL 157 157 157 VAL VAL B . n 
B 1 158 SER 158 158 158 SER SER B . n 
B 1 159 PHE 159 159 159 PHE PHE B . n 
B 1 160 CYS 160 160 160 CYS CYS B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 MET 162 162 162 MET MET B . n 
B 1 163 HIS 163 163 163 HIS HIS B . n 
B 1 164 HIS 164 164 164 HIS HIS B . n 
B 1 165 MET 165 165 165 MET MET B . n 
B 1 166 GLU 166 166 166 GLU GLU B . n 
B 1 167 LEU 167 167 167 LEU LEU B . n 
B 1 168 PRO 168 168 168 PRO PRO B . n 
B 1 169 THR 169 169 169 THR THR B . n 
B 1 170 GLY 170 170 170 GLY GLY B . n 
B 1 171 VAL 171 171 171 VAL VAL B . n 
B 1 172 HIS 172 172 172 HIS HIS B . n 
B 1 173 ALA 173 173 173 ALA ALA B . n 
B 1 174 GLY 174 174 174 GLY GLY B . n 
B 1 175 THR 175 175 175 THR THR B . n 
B 1 176 ASP 176 176 176 ASP ASP B . n 
B 1 177 LEU 177 177 177 LEU LEU B . n 
B 1 178 GLU 178 178 178 GLU GLU B . n 
B 1 179 GLY 179 179 179 GLY GLY B . n 
B 1 180 ASN 180 180 180 ASN ASN B . n 
B 1 181 PHE 181 181 181 PHE PHE B . n 
B 1 182 TYR 182 182 182 TYR TYR B . n 
B 1 183 GLY 183 183 183 GLY GLY B . n 
B 1 184 PRO 184 184 184 PRO PRO B . n 
B 1 185 PHE 185 185 185 PHE PHE B . n 
B 1 186 VAL 186 186 186 VAL VAL B . n 
B 1 187 ASP 187 187 187 ASP ASP B . n 
B 1 188 ARG 188 188 188 ARG ARG B . n 
B 1 189 GLN 189 189 189 GLN GLN B . n 
B 1 190 THR 190 190 190 THR THR B . n 
B 1 191 ALA 191 191 191 ALA ALA B . n 
B 1 192 GLN 192 192 192 GLN GLN B . n 
B 1 193 ALA 193 193 193 ALA ALA B . n 
B 1 194 ALA 194 194 194 ALA ALA B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 THR 196 196 196 THR THR B . n 
B 1 197 ASP 197 197 197 ASP ASP B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 ILE 200 200 200 ILE ILE B . n 
B 1 201 THR 201 201 201 THR THR B . n 
B 1 202 VAL 202 202 202 VAL VAL B . n 
B 1 203 ASN 203 203 203 ASN ASN B . n 
B 1 204 VAL 204 204 204 VAL VAL B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 ALA 206 206 206 ALA ALA B . n 
B 1 207 TRP 207 207 207 TRP TRP B . n 
B 1 208 LEU 208 208 208 LEU LEU B . n 
B 1 209 TYR 209 209 209 TYR TYR B . n 
B 1 210 ALA 210 210 210 ALA ALA B . n 
B 1 211 ALA 211 211 211 ALA ALA B . n 
B 1 212 VAL 212 212 212 VAL VAL B . n 
B 1 213 ILE 213 213 213 ILE ILE B . n 
B 1 214 ASN 214 214 214 ASN ASN B . n 
B 1 215 GLY 215 215 215 GLY GLY B . n 
B 1 216 ASP 216 216 216 ASP ASP B . n 
B 1 217 ARG 217 217 217 ARG ARG B . n 
B 1 218 TRP 218 218 218 TRP TRP B . n 
B 1 219 PHE 219 219 219 PHE PHE B . n 
B 1 220 LEU 220 220 220 LEU LEU B . n 
B 1 221 ASN 221 221 221 ASN ASN B . n 
B 1 222 ARG 222 222 222 ARG ARG B . n 
B 1 223 PHE 223 223 223 PHE PHE B . n 
B 1 224 THR 224 224 224 THR THR B . n 
B 1 225 THR 225 225 225 THR THR B . n 
B 1 226 THR 226 226 226 THR THR B . n 
B 1 227 LEU 227 227 227 LEU LEU B . n 
B 1 228 ASN 228 228 228 ASN ASN B . n 
B 1 229 ASP 229 229 229 ASP ASP B . n 
B 1 230 PHE 230 230 230 PHE PHE B . n 
B 1 231 ASN 231 231 231 ASN ASN B . n 
B 1 232 LEU 232 232 232 LEU LEU B . n 
B 1 233 VAL 233 233 233 VAL VAL B . n 
B 1 234 ALA 234 234 234 ALA ALA B . n 
B 1 235 MET 235 235 235 MET MET B . n 
B 1 236 LYS 236 236 236 LYS LYS B . n 
B 1 237 TYR 237 237 237 TYR TYR B . n 
B 1 238 ASN 238 238 238 ASN ASN B . n 
B 1 239 TYR 239 239 239 TYR TYR B . n 
B 1 240 GLU 240 240 240 GLU GLU B . n 
B 1 241 PRO 241 241 241 PRO PRO B . n 
B 1 242 LEU 242 242 242 LEU LEU B . n 
B 1 243 THR 243 243 243 THR THR B . n 
B 1 244 GLN 244 244 244 GLN GLN B . n 
B 1 245 ASP 245 245 245 ASP ASP B . n 
B 1 246 HIS 246 246 246 HIS HIS B . n 
B 1 247 VAL 247 247 247 VAL VAL B . n 
B 1 248 ASP 248 248 248 ASP ASP B . n 
B 1 249 ILE 249 249 249 ILE ILE B . n 
B 1 250 LEU 250 250 250 LEU LEU B . n 
B 1 251 GLY 251 251 251 GLY GLY B . n 
B 1 252 PRO 252 252 252 PRO PRO B . n 
B 1 253 LEU 253 253 253 LEU LEU B . n 
B 1 254 SER 254 254 254 SER SER B . n 
B 1 255 ALA 255 255 255 ALA ALA B . n 
B 1 256 GLN 256 256 256 GLN GLN B . n 
B 1 257 THR 257 257 257 THR THR B . n 
B 1 258 GLY 258 258 258 GLY GLY B . n 
B 1 259 ILE 259 259 259 ILE ILE B . n 
B 1 260 ALA 260 260 260 ALA ALA B . n 
B 1 261 VAL 261 261 261 VAL VAL B . n 
B 1 262 LEU 262 262 262 LEU LEU B . n 
B 1 263 ASP 263 263 263 ASP ASP B . n 
B 1 264 MET 264 264 264 MET MET B . n 
B 1 265 CYS 265 265 265 CYS CYS B . n 
B 1 266 ALA 266 266 266 ALA ALA B . n 
B 1 267 SER 267 267 267 SER SER B . n 
B 1 268 LEU 268 268 268 LEU LEU B . n 
B 1 269 LYS 269 269 269 LYS LYS B . n 
B 1 270 GLU 270 270 270 GLU GLU B . n 
B 1 271 LEU 271 271 271 LEU LEU B . n 
B 1 272 LEU 272 272 272 LEU LEU B . n 
B 1 273 GLN 273 273 273 GLN GLN B . n 
B 1 274 ASN 274 274 274 ASN ASN B . n 
B 1 275 GLY 275 275 275 GLY GLY B . n 
B 1 276 MET 276 276 276 MET MET B . n 
B 1 277 ASN 277 277 277 ASN ASN B . n 
B 1 278 GLY 278 278 278 GLY GLY B . n 
B 1 279 ARG 279 279 279 ARG ARG B . n 
B 1 280 THR 280 280 280 THR THR B . n 
B 1 281 ILE 281 281 281 ILE ILE B . n 
B 1 282 LEU 282 282 282 LEU LEU B . n 
B 1 283 GLY 283 283 283 GLY GLY B . n 
B 1 284 SER 284 284 284 SER SER B . n 
B 1 285 ALA 285 285 285 ALA ALA B . n 
B 1 286 LEU 286 286 286 LEU LEU B . n 
B 1 287 LEU 287 287 287 LEU LEU B . n 
B 1 288 GLU 288 288 288 GLU GLU B . n 
B 1 289 ASP 289 289 289 ASP ASP B . n 
B 1 290 GLU 290 290 290 GLU GLU B . n 
B 1 291 PHE 291 291 291 PHE PHE B . n 
B 1 292 THR 292 292 292 THR THR B . n 
B 1 293 PRO 293 293 293 PRO PRO B . n 
B 1 294 PHE 294 294 294 PHE PHE B . n 
B 1 295 ASP 295 295 295 ASP ASP B . n 
B 1 296 VAL 296 296 296 VAL VAL B . n 
B 1 297 VAL 297 297 297 VAL VAL B . n 
B 1 298 ARG 298 298 298 ARG ARG B . n 
B 1 299 GLN 299 299 299 GLN GLN B . n 
B 1 300 CYS 300 300 300 CYS CYS B . n 
B 1 301 SER 301 301 301 SER SER B . n 
B 1 302 GLY 302 302 302 GLY GLY B . n 
B 1 303 VAL 303 303 ?   ?   ?   B . n 
B 1 304 THR 304 304 ?   ?   ?   B . n 
B 1 305 PHE 305 305 ?   ?   ?   B . n 
B 1 306 GLN 306 306 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1D50 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1D50 
_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 A1D50 1  401 1   A1D50 LIG A . 
D 2 A1D50 1  401 2   A1D50 LIG B . 
E 3 HOH   1  501 95  HOH   HOH A . 
E 3 HOH   2  502 67  HOH   HOH A . 
E 3 HOH   3  503 19  HOH   HOH A . 
E 3 HOH   4  504 42  HOH   HOH A . 
E 3 HOH   5  505 60  HOH   HOH A . 
E 3 HOH   6  506 20  HOH   HOH A . 
E 3 HOH   7  507 68  HOH   HOH A . 
E 3 HOH   8  508 103 HOH   HOH A . 
E 3 HOH   9  509 87  HOH   HOH A . 
E 3 HOH   10 510 11  HOH   HOH A . 
E 3 HOH   11 511 84  HOH   HOH A . 
E 3 HOH   12 512 6   HOH   HOH A . 
E 3 HOH   13 513 43  HOH   HOH A . 
E 3 HOH   14 514 10  HOH   HOH A . 
E 3 HOH   15 515 102 HOH   HOH A . 
E 3 HOH   16 516 26  HOH   HOH A . 
E 3 HOH   17 517 116 HOH   HOH A . 
E 3 HOH   18 518 21  HOH   HOH A . 
E 3 HOH   19 519 4   HOH   HOH A . 
E 3 HOH   20 520 111 HOH   HOH A . 
E 3 HOH   21 521 46  HOH   HOH A . 
E 3 HOH   22 522 104 HOH   HOH A . 
E 3 HOH   23 523 101 HOH   HOH A . 
E 3 HOH   24 524 49  HOH   HOH A . 
E 3 HOH   25 525 120 HOH   HOH A . 
E 3 HOH   26 526 22  HOH   HOH A . 
E 3 HOH   27 527 86  HOH   HOH A . 
E 3 HOH   28 528 23  HOH   HOH A . 
E 3 HOH   29 529 78  HOH   HOH A . 
E 3 HOH   30 530 93  HOH   HOH A . 
E 3 HOH   31 531 81  HOH   HOH A . 
E 3 HOH   32 532 77  HOH   HOH A . 
E 3 HOH   33 533 41  HOH   HOH A . 
E 3 HOH   34 534 12  HOH   HOH A . 
E 3 HOH   35 535 61  HOH   HOH A . 
E 3 HOH   36 536 2   HOH   HOH A . 
E 3 HOH   37 537 58  HOH   HOH A . 
E 3 HOH   38 538 29  HOH   HOH A . 
E 3 HOH   39 539 83  HOH   HOH A . 
E 3 HOH   40 540 32  HOH   HOH A . 
E 3 HOH   41 541 17  HOH   HOH A . 
E 3 HOH   42 542 80  HOH   HOH A . 
E 3 HOH   43 543 62  HOH   HOH A . 
E 3 HOH   44 544 82  HOH   HOH A . 
E 3 HOH   45 545 9   HOH   HOH A . 
E 3 HOH   46 546 1   HOH   HOH A . 
E 3 HOH   47 547 63  HOH   HOH A . 
E 3 HOH   48 548 51  HOH   HOH A . 
E 3 HOH   49 549 98  HOH   HOH A . 
E 3 HOH   50 550 24  HOH   HOH A . 
E 3 HOH   51 551 85  HOH   HOH A . 
E 3 HOH   52 552 57  HOH   HOH A . 
E 3 HOH   53 553 115 HOH   HOH A . 
E 3 HOH   54 554 97  HOH   HOH A . 
E 3 HOH   55 555 108 HOH   HOH A . 
E 3 HOH   56 556 91  HOH   HOH A . 
E 3 HOH   57 557 3   HOH   HOH A . 
E 3 HOH   58 558 113 HOH   HOH A . 
E 3 HOH   59 559 88  HOH   HOH A . 
E 3 HOH   60 560 27  HOH   HOH A . 
E 3 HOH   61 561 76  HOH   HOH A . 
E 3 HOH   62 562 70  HOH   HOH A . 
E 3 HOH   63 563 107 HOH   HOH A . 
E 3 HOH   64 564 36  HOH   HOH A . 
E 3 HOH   65 565 44  HOH   HOH A . 
E 3 HOH   66 566 13  HOH   HOH A . 
E 3 HOH   67 567 99  HOH   HOH A . 
E 3 HOH   68 568 100 HOH   HOH A . 
E 3 HOH   69 569 71  HOH   HOH A . 
E 3 HOH   70 570 55  HOH   HOH A . 
E 3 HOH   71 571 79  HOH   HOH A . 
E 3 HOH   72 572 119 HOH   HOH A . 
E 3 HOH   73 573 114 HOH   HOH A . 
E 3 HOH   74 574 56  HOH   HOH A . 
E 3 HOH   75 575 112 HOH   HOH A . 
E 3 HOH   76 576 106 HOH   HOH A . 
E 3 HOH   77 577 105 HOH   HOH A . 
E 3 HOH   78 578 109 HOH   HOH A . 
E 3 HOH   79 579 121 HOH   HOH A . 
F 3 HOH   1  501 110 HOH   HOH B . 
F 3 HOH   2  502 94  HOH   HOH B . 
F 3 HOH   3  503 45  HOH   HOH B . 
F 3 HOH   4  504 40  HOH   HOH B . 
F 3 HOH   5  505 34  HOH   HOH B . 
F 3 HOH   6  506 28  HOH   HOH B . 
F 3 HOH   7  507 64  HOH   HOH B . 
F 3 HOH   8  508 92  HOH   HOH B . 
F 3 HOH   9  509 7   HOH   HOH B . 
F 3 HOH   10 510 75  HOH   HOH B . 
F 3 HOH   11 511 66  HOH   HOH B . 
F 3 HOH   12 512 118 HOH   HOH B . 
F 3 HOH   13 513 53  HOH   HOH B . 
F 3 HOH   14 514 33  HOH   HOH B . 
F 3 HOH   15 515 39  HOH   HOH B . 
F 3 HOH   16 516 25  HOH   HOH B . 
F 3 HOH   17 517 48  HOH   HOH B . 
F 3 HOH   18 518 38  HOH   HOH B . 
F 3 HOH   19 519 31  HOH   HOH B . 
F 3 HOH   20 520 15  HOH   HOH B . 
F 3 HOH   21 521 89  HOH   HOH B . 
F 3 HOH   22 522 8   HOH   HOH B . 
F 3 HOH   23 523 73  HOH   HOH B . 
F 3 HOH   24 524 18  HOH   HOH B . 
F 3 HOH   25 525 96  HOH   HOH B . 
F 3 HOH   26 526 30  HOH   HOH B . 
F 3 HOH   27 527 14  HOH   HOH B . 
F 3 HOH   28 528 37  HOH   HOH B . 
F 3 HOH   29 529 72  HOH   HOH B . 
F 3 HOH   30 530 74  HOH   HOH B . 
F 3 HOH   31 531 117 HOH   HOH B . 
F 3 HOH   32 532 35  HOH   HOH B . 
F 3 HOH   33 533 5   HOH   HOH B . 
F 3 HOH   34 534 54  HOH   HOH B . 
F 3 HOH   35 535 47  HOH   HOH B . 
F 3 HOH   36 536 50  HOH   HOH B . 
F 3 HOH   37 537 65  HOH   HOH B . 
F 3 HOH   38 538 52  HOH   HOH B . 
F 3 HOH   39 539 69  HOH   HOH B . 
F 3 HOH   40 540 59  HOH   HOH B . 
F 3 HOH   41 541 122 HOH   HOH B . 
F 3 HOH   42 542 16  HOH   HOH B . 
F 3 HOH   43 543 90  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 GLU 47  ? CG  ? A GLU 47  CG  
2   1 Y 1 A GLU 47  ? CD  ? A GLU 47  CD  
3   1 Y 1 A GLU 47  ? OE1 ? A GLU 47  OE1 
4   1 Y 1 A GLU 47  ? OE2 ? A GLU 47  OE2 
5   1 Y 1 A ASN 72  ? CG  ? A ASN 72  CG  
6   1 Y 1 A ASN 72  ? OD1 ? A ASN 72  OD1 
7   1 Y 1 A ASN 72  ? ND2 ? A ASN 72  ND2 
8   1 Y 1 A GLN 74  ? CG  ? A GLN 74  CG  
9   1 Y 1 A GLN 74  ? CD  ? A GLN 74  CD  
10  1 Y 1 A GLN 74  ? OE1 ? A GLN 74  OE1 
11  1 Y 1 A GLN 74  ? NE2 ? A GLN 74  NE2 
12  1 Y 1 A ARG 76  ? CG  ? A ARG 76  CG  
13  1 Y 1 A ARG 76  ? CD  ? A ARG 76  CD  
14  1 Y 1 A ARG 76  ? NE  ? A ARG 76  NE  
15  1 Y 1 A ARG 76  ? CZ  ? A ARG 76  CZ  
16  1 Y 1 A ARG 76  ? NH1 ? A ARG 76  NH1 
17  1 Y 1 A ARG 76  ? NH2 ? A ARG 76  NH2 
18  1 Y 1 A LYS 100 ? CG  ? A LYS 100 CG  
19  1 Y 1 A LYS 100 ? CD  ? A LYS 100 CD  
20  1 Y 1 A LYS 100 ? CE  ? A LYS 100 CE  
21  1 Y 1 A LYS 100 ? NZ  ? A LYS 100 NZ  
22  1 Y 1 A ASP 153 ? CG  ? A ASP 153 CG  
23  1 Y 1 A ASP 153 ? OD1 ? A ASP 153 OD1 
24  1 Y 1 A ASP 153 ? OD2 ? A ASP 153 OD2 
25  1 Y 1 A TYR 154 ? CB  ? A TYR 154 CB  
26  1 Y 1 A TYR 154 ? CG  ? A TYR 154 CG  
27  1 Y 1 A TYR 154 ? CD1 ? A TYR 154 CD1 
28  1 Y 1 A TYR 154 ? CD2 ? A TYR 154 CD2 
29  1 Y 1 A TYR 154 ? CE1 ? A TYR 154 CE1 
30  1 Y 1 A TYR 154 ? CE2 ? A TYR 154 CE2 
31  1 Y 1 A TYR 154 ? CZ  ? A TYR 154 CZ  
32  1 Y 1 A TYR 154 ? OH  ? A TYR 154 OH  
33  1 Y 1 A ASP 155 ? CG  ? A ASP 155 CG  
34  1 Y 1 A ASP 155 ? OD1 ? A ASP 155 OD1 
35  1 Y 1 A ASP 155 ? OD2 ? A ASP 155 OD2 
36  1 Y 1 A GLU 240 ? CG  ? A GLU 240 CG  
37  1 Y 1 A GLU 240 ? CD  ? A GLU 240 CD  
38  1 Y 1 A GLU 240 ? OE1 ? A GLU 240 OE1 
39  1 Y 1 A GLU 240 ? OE2 ? A GLU 240 OE2 
40  1 Y 1 A ASN 277 ? CG  ? A ASN 277 CG  
41  1 Y 1 A ASN 277 ? OD1 ? A ASN 277 OD1 
42  1 Y 1 A ASN 277 ? ND2 ? A ASN 277 ND2 
43  1 Y 1 A ARG 298 ? CG  ? A ARG 298 CG  
44  1 Y 1 A ARG 298 ? CD  ? A ARG 298 CD  
45  1 Y 1 A ARG 298 ? NE  ? A ARG 298 NE  
46  1 Y 1 A ARG 298 ? CZ  ? A ARG 298 CZ  
47  1 Y 1 A ARG 298 ? NH1 ? A ARG 298 NH1 
48  1 Y 1 A ARG 298 ? NH2 ? A ARG 298 NH2 
49  1 Y 1 A SER 301 ? OG  ? A SER 301 OG  
50  1 Y 1 A VAL 303 ? CG1 ? A VAL 303 CG1 
51  1 Y 1 A VAL 303 ? CG2 ? A VAL 303 CG2 
52  1 Y 1 B GLU 47  ? CG  ? B GLU 47  CG  
53  1 Y 1 B GLU 47  ? CD  ? B GLU 47  CD  
54  1 Y 1 B GLU 47  ? OE1 ? B GLU 47  OE1 
55  1 Y 1 B GLU 47  ? OE2 ? B GLU 47  OE2 
56  1 Y 1 B GLU 55  ? CG  ? B GLU 55  CG  
57  1 Y 1 B GLU 55  ? CD  ? B GLU 55  CD  
58  1 Y 1 B GLU 55  ? OE1 ? B GLU 55  OE1 
59  1 Y 1 B GLU 55  ? OE2 ? B GLU 55  OE2 
60  1 Y 1 B HIS 64  ? CG  ? B HIS 64  CG  
61  1 Y 1 B HIS 64  ? ND1 ? B HIS 64  ND1 
62  1 Y 1 B HIS 64  ? CD2 ? B HIS 64  CD2 
63  1 Y 1 B HIS 64  ? CE1 ? B HIS 64  CE1 
64  1 Y 1 B HIS 64  ? NE2 ? B HIS 64  NE2 
65  1 Y 1 B ASN 72  ? CG  ? B ASN 72  CG  
66  1 Y 1 B ASN 72  ? OD1 ? B ASN 72  OD1 
67  1 Y 1 B ASN 72  ? ND2 ? B ASN 72  ND2 
68  1 Y 1 B GLN 74  ? CG  ? B GLN 74  CG  
69  1 Y 1 B GLN 74  ? CD  ? B GLN 74  CD  
70  1 Y 1 B GLN 74  ? OE1 ? B GLN 74  OE1 
71  1 Y 1 B GLN 74  ? NE2 ? B GLN 74  NE2 
72  1 Y 1 B ARG 76  ? CG  ? B ARG 76  CG  
73  1 Y 1 B ARG 76  ? CD  ? B ARG 76  CD  
74  1 Y 1 B ARG 76  ? NE  ? B ARG 76  NE  
75  1 Y 1 B ARG 76  ? CZ  ? B ARG 76  CZ  
76  1 Y 1 B ARG 76  ? NH1 ? B ARG 76  NH1 
77  1 Y 1 B ARG 76  ? NH2 ? B ARG 76  NH2 
78  1 Y 1 B LYS 90  ? CG  ? B LYS 90  CG  
79  1 Y 1 B LYS 90  ? CD  ? B LYS 90  CD  
80  1 Y 1 B LYS 90  ? CE  ? B LYS 90  CE  
81  1 Y 1 B LYS 90  ? NZ  ? B LYS 90  NZ  
82  1 Y 1 B LYS 100 ? CG  ? B LYS 100 CG  
83  1 Y 1 B LYS 100 ? CD  ? B LYS 100 CD  
84  1 Y 1 B LYS 100 ? CE  ? B LYS 100 CE  
85  1 Y 1 B LYS 100 ? NZ  ? B LYS 100 NZ  
86  1 Y 1 B LYS 102 ? CG  ? B LYS 102 CG  
87  1 Y 1 B LYS 102 ? CD  ? B LYS 102 CD  
88  1 Y 1 B LYS 102 ? CE  ? B LYS 102 CE  
89  1 Y 1 B LYS 102 ? NZ  ? B LYS 102 NZ  
90  1 Y 1 B ASP 153 ? CG  ? B ASP 153 CG  
91  1 Y 1 B ASP 153 ? OD1 ? B ASP 153 OD1 
92  1 Y 1 B ASP 153 ? OD2 ? B ASP 153 OD2 
93  1 Y 1 B TYR 154 ? CG  ? B TYR 154 CG  
94  1 Y 1 B TYR 154 ? CD1 ? B TYR 154 CD1 
95  1 Y 1 B TYR 154 ? CD2 ? B TYR 154 CD2 
96  1 Y 1 B TYR 154 ? CE1 ? B TYR 154 CE1 
97  1 Y 1 B TYR 154 ? CE2 ? B TYR 154 CE2 
98  1 Y 1 B TYR 154 ? CZ  ? B TYR 154 CZ  
99  1 Y 1 B TYR 154 ? OH  ? B TYR 154 OH  
100 1 Y 1 B ARG 217 ? CG  ? B ARG 217 CG  
101 1 Y 1 B ARG 217 ? CD  ? B ARG 217 CD  
102 1 Y 1 B ARG 217 ? NE  ? B ARG 217 NE  
103 1 Y 1 B ARG 217 ? CZ  ? B ARG 217 CZ  
104 1 Y 1 B ARG 217 ? NH1 ? B ARG 217 NH1 
105 1 Y 1 B ARG 217 ? NH2 ? B ARG 217 NH2 
106 1 Y 1 B ARG 222 ? CG  ? B ARG 222 CG  
107 1 Y 1 B ARG 222 ? CD  ? B ARG 222 CD  
108 1 Y 1 B ARG 222 ? NE  ? B ARG 222 NE  
109 1 Y 1 B ARG 222 ? CZ  ? B ARG 222 CZ  
110 1 Y 1 B ARG 222 ? NH1 ? B ARG 222 NH1 
111 1 Y 1 B ARG 222 ? NH2 ? B ARG 222 NH2 
112 1 Y 1 B PHE 223 ? CG  ? B PHE 223 CG  
113 1 Y 1 B PHE 223 ? CD1 ? B PHE 223 CD1 
114 1 Y 1 B PHE 223 ? CD2 ? B PHE 223 CD2 
115 1 Y 1 B PHE 223 ? CE1 ? B PHE 223 CE1 
116 1 Y 1 B PHE 223 ? CE2 ? B PHE 223 CE2 
117 1 Y 1 B PHE 223 ? CZ  ? B PHE 223 CZ  
118 1 Y 1 B THR 224 ? OG1 ? B THR 224 OG1 
119 1 Y 1 B THR 224 ? CG2 ? B THR 224 CG2 
120 1 Y 1 B THR 226 ? OG1 ? B THR 226 OG1 
121 1 Y 1 B THR 226 ? CG2 ? B THR 226 CG2 
122 1 Y 1 B ASN 228 ? CG  ? B ASN 228 CG  
123 1 Y 1 B ASN 228 ? OD1 ? B ASN 228 OD1 
124 1 Y 1 B ASN 228 ? ND2 ? B ASN 228 ND2 
125 1 Y 1 B ASP 229 ? CG  ? B ASP 229 CG  
126 1 Y 1 B ASP 229 ? OD1 ? B ASP 229 OD1 
127 1 Y 1 B ASP 229 ? OD2 ? B ASP 229 OD2 
128 1 Y 1 B LEU 232 ? CG  ? B LEU 232 CG  
129 1 Y 1 B LEU 232 ? CD1 ? B LEU 232 CD1 
130 1 Y 1 B LEU 232 ? CD2 ? B LEU 232 CD2 
131 1 Y 1 B MET 235 ? CG  ? B MET 235 CG  
132 1 Y 1 B MET 235 ? SD  ? B MET 235 SD  
133 1 Y 1 B MET 235 ? CE  ? B MET 235 CE  
134 1 Y 1 B LYS 236 ? CG  ? B LYS 236 CG  
135 1 Y 1 B LYS 236 ? CD  ? B LYS 236 CD  
136 1 Y 1 B LYS 236 ? CE  ? B LYS 236 CE  
137 1 Y 1 B LYS 236 ? NZ  ? B LYS 236 NZ  
138 1 Y 1 B ILE 249 ? CG1 ? B ILE 249 CG1 
139 1 Y 1 B ILE 249 ? CG2 ? B ILE 249 CG2 
140 1 Y 1 B ILE 249 ? CD1 ? B ILE 249 CD1 
141 1 Y 1 B ASP 263 ? CG  ? B ASP 263 CG  
142 1 Y 1 B ASP 263 ? OD1 ? B ASP 263 OD1 
143 1 Y 1 B ASP 263 ? OD2 ? B ASP 263 OD2 
144 1 Y 1 B LYS 269 ? CG  ? B LYS 269 CG  
145 1 Y 1 B LYS 269 ? CD  ? B LYS 269 CD  
146 1 Y 1 B LYS 269 ? CE  ? B LYS 269 CE  
147 1 Y 1 B LYS 269 ? NZ  ? B LYS 269 NZ  
148 1 Y 1 B GLU 270 ? CG  ? B GLU 270 CG  
149 1 Y 1 B GLU 270 ? CD  ? B GLU 270 CD  
150 1 Y 1 B GLU 270 ? OE1 ? B GLU 270 OE1 
151 1 Y 1 B GLU 270 ? OE2 ? B GLU 270 OE2 
152 1 Y 1 B MET 276 ? CG  ? B MET 276 CG  
153 1 Y 1 B MET 276 ? SD  ? B MET 276 SD  
154 1 Y 1 B MET 276 ? CE  ? B MET 276 CE  
155 1 Y 1 B ASN 277 ? CG  ? B ASN 277 CG  
156 1 Y 1 B ASN 277 ? OD1 ? B ASN 277 OD1 
157 1 Y 1 B ASN 277 ? ND2 ? B ASN 277 ND2 
158 1 Y 1 B PHE 294 ? CG  ? B PHE 294 CG  
159 1 Y 1 B PHE 294 ? CD1 ? B PHE 294 CD1 
160 1 Y 1 B PHE 294 ? CD2 ? B PHE 294 CD2 
161 1 Y 1 B PHE 294 ? CE1 ? B PHE 294 CE1 
162 1 Y 1 B PHE 294 ? CE2 ? B PHE 294 CE2 
163 1 Y 1 B PHE 294 ? CZ  ? B PHE 294 CZ  
164 1 Y 1 B ARG 298 ? CG  ? B ARG 298 CG  
165 1 Y 1 B ARG 298 ? CD  ? B ARG 298 CD  
166 1 Y 1 B ARG 298 ? NE  ? B ARG 298 NE  
167 1 Y 1 B ARG 298 ? CZ  ? B ARG 298 CZ  
168 1 Y 1 B ARG 298 ? NH1 ? B ARG 298 NH1 
169 1 Y 1 B ARG 298 ? NH2 ? B ARG 298 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  ? ? ? '(1.17.1_3660: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Y44 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     67.970 
_cell.length_a_esd                 ? 
_cell.length_b                     89.440 
_cell.length_b_esd                 ? 
_cell.length_c                     103.090 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8Y44 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   8Y44 
_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             2.32 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.89 
_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    
;100 mM MES, pH5.5-7.0, 5%-25%
PEG6000, 3% DMSO
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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 EIGER 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         2022-12-17 
_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   0.97918 
_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        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8Y44 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.91 
_reflns.d_resolution_low                               41.07 
_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                                     49334 
_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                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.02 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.256 
_reflns.pdbx_Rpim_I_all                                0.070 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       639512 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.246 
_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                                    1.91 
_reflns_shell.d_res_low                                     1.96 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           47947 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3586 
_reflns_shell.percent_possible_obs                          99.6 
_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                               13.4 
_reflns_shell.pdbx_chi_squared                              1.00 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.8 
_reflns_shell.pdbx_Rrim_I_all                               2.462 
_reflns_shell.pdbx_Rpim_I_all                               0.665 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.688 
_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                                  2.369 
_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                               ? 
_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                                 8Y44 
_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                            1.91 
_refine.ls_d_res_low                             31.77 
_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                     49235 
_refine.ls_number_reflns_R_free                  2364 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.58 
_refine.ls_percent_reflns_R_free                 4.80 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2204 
_refine.ls_R_factor_R_free                       0.2623 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2183 
_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                          1.34 
_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       ML 
_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             0.90 
_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                 30.82 
_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                            0.24 
_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.pdbx_number_atoms_protein        4511 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         78 
_refine_hist.number_atoms_solvent             122 
_refine_hist.number_atoms_total               4711 
_refine_hist.d_res_high                       1.91 
_refine_hist.d_res_low                        31.77 
# 
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' ? 0.005  ? 4696 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.749  ? 6409 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.678 ? 1663 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.047  ? 732  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 830  ? f_plane_restr      ? ? 
# 
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' 1.91 1.95  . . 138 2729 99.00  . . . . 0.3457 . . . . . . . . . . . 0.3515 
'X-RAY DIFFRACTION' 1.95 1.99  . . 149 2697 100.00 . . . . 0.3206 . . . . . . . . . . . 0.3256 
'X-RAY DIFFRACTION' 1.99 2.04  . . 145 2694 99.00  . . . . 0.3072 . . . . . . . . . . . 0.3716 
'X-RAY DIFFRACTION' 2.04 2.09  . . 137 2722 99.00  . . . . 0.2943 . . . . . . . . . . . 0.3520 
'X-RAY DIFFRACTION' 2.09 2.15  . . 141 2709 99.00  . . . . 0.2639 . . . . . . . . . . . 0.3320 
'X-RAY DIFFRACTION' 2.15 2.21  . . 139 2742 100.00 . . . . 0.2482 . . . . . . . . . . . 0.3353 
'X-RAY DIFFRACTION' 2.21 2.28  . . 144 2711 100.00 . . . . 0.2412 . . . . . . . . . . . 0.2622 
'X-RAY DIFFRACTION' 2.28 2.36  . . 153 2706 100.00 . . . . 0.2327 . . . . . . . . . . . 0.3215 
'X-RAY DIFFRACTION' 2.36 2.46  . . 126 2759 100.00 . . . . 0.2411 . . . . . . . . . . . 0.3005 
'X-RAY DIFFRACTION' 2.46 2.57  . . 134 2745 100.00 . . . . 0.2359 . . . . . . . . . . . 0.2953 
'X-RAY DIFFRACTION' 2.57 2.70  . . 147 2739 100.00 . . . . 0.2310 . . . . . . . . . . . 0.2606 
'X-RAY DIFFRACTION' 2.70 2.87  . . 121 2795 100.00 . . . . 0.2273 . . . . . . . . . . . 0.2708 
'X-RAY DIFFRACTION' 2.87 3.09  . . 144 2775 100.00 . . . . 0.2317 . . . . . . . . . . . 0.2742 
'X-RAY DIFFRACTION' 3.09 3.40  . . 121 2794 100.00 . . . . 0.2216 . . . . . . . . . . . 0.3057 
'X-RAY DIFFRACTION' 3.40 3.90  . . 138 2802 100.00 . . . . 0.1945 . . . . . . . . . . . 0.2388 
'X-RAY DIFFRACTION' 3.90 4.91  . . 145 2841 100.00 . . . . 0.1643 . . . . . . . . . . . 0.1957 
'X-RAY DIFFRACTION' 4.91 31.77 . . 142 2911 98.00  . . . . 0.1849 . . . . . . . . . . . 0.2020 
# 
_struct.entry_id                     8Y44 
_struct.title                        'Crystal structure of SARS-CoV-2 3CL protease (3CLpro) in complex with compound 44' 
_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        8Y44 
_struct_keywords.text            'Mpro, 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                    R1A_SARS2 
_struct_ref.pdbx_db_accession          P0DTC1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_struct_ref.pdbx_align_begin           3264 
# 
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 8Y44 A 1 ? 306 ? P0DTC1 3264 ? 3569 ? 1 306 
2 1 8Y44 B 1 ? 306 ? P0DTC1 3264 ? 3569 ? 1 306 
# 
_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)' 2860  ? 
1 MORE         -15   ? 
1 'SSA (A^2)'  24470 ? 
# 
_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 10  ? GLY A 15  ? SER A 10  GLY A 15  1 ? 6  
HELX_P HELX_P2  AA2 HIS A 41  ? CYS A 44  ? HIS A 41  CYS A 44  5 ? 4  
HELX_P HELX_P3  AA3 SER A 46  ? LEU A 50  ? SER A 46  LEU A 50  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 53  ? ARG A 60  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P5  AA5 SER A 62  ? HIS A 64  ? SER A 62  HIS A 64  5 ? 3  
HELX_P HELX_P6  AA6 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P7  AA7 THR A 226 ? MET A 235 ? THR A 226 MET A 235 1 ? 10 
HELX_P HELX_P8  AA8 LYS A 236 ? ASN A 238 ? LYS A 236 ASN A 238 5 ? 3  
HELX_P HELX_P9  AA9 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P10 AB1 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P11 AB2 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P12 AB3 THR A 292 ? GLY A 302 ? THR A 292 GLY A 302 1 ? 11 
HELX_P HELX_P13 AB4 SER B 10  ? GLY B 15  ? SER B 10  GLY B 15  1 ? 6  
HELX_P HELX_P14 AB5 HIS B 41  ? CYS B 44  ? HIS B 41  CYS B 44  5 ? 4  
HELX_P HELX_P15 AB6 THR B 45  ? ASN B 51  ? THR B 45  ASN B 51  1 ? 7  
HELX_P HELX_P16 AB7 ASN B 53  ? ARG B 60  ? ASN B 53  ARG B 60  1 ? 8  
HELX_P HELX_P17 AB8 SER B 62  ? HIS B 64  ? SER B 62  HIS B 64  5 ? 3  
HELX_P HELX_P18 AB9 ILE B 200 ? ASN B 214 ? ILE B 200 ASN B 214 1 ? 15 
HELX_P HELX_P19 AC1 THR B 226 ? TYR B 237 ? THR B 226 TYR B 237 1 ? 12 
HELX_P HELX_P20 AC2 THR B 243 ? LEU B 250 ? THR B 243 LEU B 250 1 ? 8  
HELX_P HELX_P21 AC3 LEU B 250 ? GLY B 258 ? LEU B 250 GLY B 258 1 ? 9  
HELX_P HELX_P22 AC4 ALA B 260 ? GLY B 275 ? ALA B 260 GLY B 275 1 ? 16 
HELX_P HELX_P23 AC5 THR B 292 ? CYS B 300 ? THR B 292 CYS B 300 1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
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 73  ? LEU A 75  ? VAL A 73  LEU A 75  
AA1 2 PHE A 66  ? ALA A 70  ? PHE A 66  ALA A 70  
AA1 3 MET A 17  ? CYS A 22  ? MET A 17  CYS A 22  
AA1 4 THR A 25  ? LEU A 32  ? THR A 25  LEU A 32  
AA1 5 VAL A 35  ? PRO A 39  ? VAL A 35  PRO A 39  
AA1 6 VAL A 86  ? VAL A 91  ? VAL A 86  VAL A 91  
AA1 7 VAL A 77  ? GLN A 83  ? VAL A 77  GLN A 83  
AA2 1 TYR A 101 ? PHE A 103 ? TYR A 101 PHE A 103 
AA2 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA2 3 VAL A 148 ? ASP A 153 ? VAL A 148 ASP A 153 
AA2 4 THR A 111 ? TYR A 118 ? THR A 111 TYR A 118 
AA2 5 SER A 121 ? ALA A 129 ? SER A 121 ALA A 129 
AA3 1 TYR A 101 ? PHE A 103 ? TYR A 101 PHE A 103 
AA3 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA3 3 HIS A 172 ? THR A 175 ? HIS A 172 THR A 175 
AA4 1 VAL B 73  ? LEU B 75  ? VAL B 73  LEU B 75  
AA4 2 PHE B 66  ? ALA B 70  ? PHE B 66  ALA B 70  
AA4 3 MET B 17  ? CYS B 22  ? MET B 17  CYS B 22  
AA4 4 THR B 25  ? LEU B 32  ? THR B 25  LEU B 32  
AA4 5 VAL B 35  ? PRO B 39  ? VAL B 35  PRO B 39  
AA4 6 VAL B 86  ? VAL B 91  ? VAL B 86  VAL B 91  
AA4 7 VAL B 77  ? GLN B 83  ? VAL B 77  GLN B 83  
AA5 1 TYR B 101 ? PHE B 103 ? TYR B 101 PHE B 103 
AA5 2 CYS B 156 ? GLU B 166 ? CYS B 156 GLU B 166 
AA5 3 VAL B 148 ? ASP B 153 ? VAL B 148 ASP B 153 
AA5 4 THR B 111 ? TYR B 118 ? THR B 111 TYR B 118 
AA5 5 SER B 121 ? ALA B 129 ? SER B 121 ALA B 129 
AA6 1 TYR B 101 ? PHE B 103 ? TYR B 101 PHE B 103 
AA6 2 CYS B 156 ? GLU B 166 ? CYS B 156 GLU B 166 
AA6 3 HIS B 172 ? THR B 175 ? 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 VAL A 73  ? O VAL A 73  N ALA A 70  ? N ALA A 70  
AA1 2 3 O GLN A 69  ? O GLN A 69  N GLN A 19  ? N GLN A 19  
AA1 3 4 N VAL A 20  ? N VAL A 20  O LEU A 27  ? O LEU A 27  
AA1 4 5 N LEU A 32  ? N LEU A 32  O VAL A 35  ? O VAL A 35  
AA1 5 6 N CYS A 38  ? N CYS A 38  O LEU A 87  ? O LEU A 87  
AA1 6 7 O LYS A 88  ? O LYS A 88  N SER A 81  ? N SER A 81  
AA2 1 2 N LYS A 102 ? N LYS A 102 O VAL A 157 ? O VAL A 157 
AA2 2 3 O SER A 158 ? O SER A 158 N ASN A 151 ? N ASN A 151 
AA2 3 4 O PHE A 150 ? O PHE A 150 N SER A 113 ? N SER A 113 
AA2 4 5 N VAL A 114 ? N VAL A 114 O TYR A 126 ? O TYR A 126 
AA3 1 2 N LYS A 102 ? N LYS A 102 O VAL A 157 ? O VAL A 157 
AA3 2 3 N MET A 162 ? N MET A 162 O THR A 175 ? O THR A 175 
AA4 1 2 O LEU B 75  ? O LEU B 75  N VAL B 68  ? N VAL B 68  
AA4 2 3 O LEU B 67  ? O LEU B 67  N THR B 21  ? N THR B 21  
AA4 3 4 N VAL B 18  ? N VAL B 18  O GLY B 29  ? O GLY B 29  
AA4 4 5 N LEU B 30  ? N LEU B 30  O TYR B 37  ? O TYR B 37  
AA4 5 6 N CYS B 38  ? N CYS B 38  O LEU B 87  ? O LEU B 87  
AA4 6 7 O LYS B 88  ? O LYS B 88  N SER B 81  ? N SER B 81  
AA5 1 2 N LYS B 102 ? N LYS B 102 O VAL B 157 ? O VAL B 157 
AA5 2 3 O SER B 158 ? O SER B 158 N ASN B 151 ? N ASN B 151 
AA5 3 4 O PHE B 150 ? O PHE B 150 N SER B 113 ? N SER B 113 
AA5 4 5 N VAL B 114 ? N VAL B 114 O TYR B 126 ? O TYR B 126 
AA6 1 2 N LYS B 102 ? N LYS B 102 O VAL B 157 ? O VAL B 157 
AA6 2 3 N MET B 165 ? N MET B 165 O ALA B 173 ? O ALA B 173 
# 
_pdbx_entry_details.entry_id                   8Y44 
_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   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 33  ? ? 56.98   -132.83 
2  1 HIS A 41  ? ? -69.97  1.87    
3  1 ASN A 84  ? ? 53.02   -123.06 
4  1 TYR A 154 ? ? 70.87   -124.78 
5  1 ALA A 191 ? ? -55.55  109.66  
6  1 ASP B 33  ? ? 55.92   -126.87 
7  1 ASN B 51  ? ? -158.60 77.98   
8  1 ASN B 84  ? ? 51.47   -127.76 
9  1 TYR B 154 ? ? 53.71   -113.93 
10 1 SER B 301 ? ? -160.11 -8.70   
# 
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 305 ? A PHE 305 
2 1 Y 1 A GLN 306 ? A GLN 306 
3 1 Y 1 B VAL 303 ? B VAL 303 
4 1 Y 1 B THR 304 ? B THR 304 
5 1 Y 1 B PHE 305 ? B PHE 305 
6 1 Y 1 B GLN 306 ? B GLN 306 
# 
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 
A1D50 N1   N  N N 1   
A1D50 N3   N  N N 2   
A1D50 C4   C  N N 3   
A1D50 C5   C  Y N 4   
A1D50 C6   C  Y N 5   
A1D50 C7   C  Y N 6   
A1D50 C8   C  Y N 7   
A1D50 C10  C  N N 8   
A1D50 C13  C  N N 9   
A1D50 C15  C  N N 10  
A1D50 C17  C  Y N 11  
A1D50 C20  C  Y N 12  
A1D50 C21  C  Y N 13  
A1D50 C22  C  Y N 14  
A1D50 C24  C  N N 15  
A1D50 C26  C  N N 16  
A1D50 C1   C  Y N 17  
A1D50 C11  C  N S 18  
A1D50 C12  C  N N 19  
A1D50 C14  C  N N 20  
A1D50 C16  C  N R 21  
A1D50 C18  C  Y N 22  
A1D50 C19  C  Y N 23  
A1D50 C2   C  N N 24  
A1D50 C23  C  N N 25  
A1D50 C25  C  N N 26  
A1D50 C27  C  N N 27  
A1D50 C3   C  N N 28  
A1D50 C9   C  Y N 29  
A1D50 N2   N  N N 30  
A1D50 N4   N  N N 31  
A1D50 N5   N  N N 32  
A1D50 O1   O  N N 33  
A1D50 O2   O  N N 34  
A1D50 O3   O  N N 35  
A1D50 O4   O  N N 36  
A1D50 O5   O  N N 37  
A1D50 O6   O  N N 38  
A1D50 BR1  BR N N 39  
A1D50 H1   H  N N 40  
A1D50 H2   H  N N 41  
A1D50 H3   H  N N 42  
A1D50 H4   H  N N 43  
A1D50 H5   H  N N 44  
A1D50 H6   H  N N 45  
A1D50 H7   H  N N 46  
A1D50 H8   H  N N 47  
A1D50 H9   H  N N 48  
A1D50 H10  H  N N 49  
A1D50 H11  H  N N 50  
A1D50 H12  H  N N 51  
A1D50 H13  H  N N 52  
A1D50 H14  H  N N 53  
A1D50 H15  H  N N 54  
A1D50 H16  H  N N 55  
A1D50 H17  H  N N 56  
A1D50 H18  H  N N 57  
A1D50 H19  H  N N 58  
A1D50 H20  H  N N 59  
A1D50 H21  H  N N 60  
A1D50 H22  H  N N 61  
A1D50 H23  H  N N 62  
A1D50 H24  H  N N 63  
A1D50 H25  H  N N 64  
A1D50 H26  H  N N 65  
A1D50 H27  H  N N 66  
A1D50 H28  H  N N 67  
ALA   N    N  N N 68  
ALA   CA   C  N S 69  
ALA   C    C  N N 70  
ALA   O    O  N N 71  
ALA   CB   C  N N 72  
ALA   OXT  O  N N 73  
ALA   H    H  N N 74  
ALA   H2   H  N N 75  
ALA   HA   H  N N 76  
ALA   HB1  H  N N 77  
ALA   HB2  H  N N 78  
ALA   HB3  H  N N 79  
ALA   HXT  H  N N 80  
ARG   N    N  N N 81  
ARG   CA   C  N S 82  
ARG   C    C  N N 83  
ARG   O    O  N N 84  
ARG   CB   C  N N 85  
ARG   CG   C  N N 86  
ARG   CD   C  N N 87  
ARG   NE   N  N N 88  
ARG   CZ   C  N N 89  
ARG   NH1  N  N N 90  
ARG   NH2  N  N N 91  
ARG   OXT  O  N N 92  
ARG   H    H  N N 93  
ARG   H2   H  N N 94  
ARG   HA   H  N N 95  
ARG   HB2  H  N N 96  
ARG   HB3  H  N N 97  
ARG   HG2  H  N N 98  
ARG   HG3  H  N N 99  
ARG   HD2  H  N N 100 
ARG   HD3  H  N N 101 
ARG   HE   H  N N 102 
ARG   HH11 H  N N 103 
ARG   HH12 H  N N 104 
ARG   HH21 H  N N 105 
ARG   HH22 H  N N 106 
ARG   HXT  H  N N 107 
ASN   N    N  N N 108 
ASN   CA   C  N S 109 
ASN   C    C  N N 110 
ASN   O    O  N N 111 
ASN   CB   C  N N 112 
ASN   CG   C  N N 113 
ASN   OD1  O  N N 114 
ASN   ND2  N  N N 115 
ASN   OXT  O  N N 116 
ASN   H    H  N N 117 
ASN   H2   H  N N 118 
ASN   HA   H  N N 119 
ASN   HB2  H  N N 120 
ASN   HB3  H  N N 121 
ASN   HD21 H  N N 122 
ASN   HD22 H  N N 123 
ASN   HXT  H  N N 124 
ASP   N    N  N N 125 
ASP   CA   C  N S 126 
ASP   C    C  N N 127 
ASP   O    O  N N 128 
ASP   CB   C  N N 129 
ASP   CG   C  N N 130 
ASP   OD1  O  N N 131 
ASP   OD2  O  N N 132 
ASP   OXT  O  N N 133 
ASP   H    H  N N 134 
ASP   H2   H  N N 135 
ASP   HA   H  N N 136 
ASP   HB2  H  N N 137 
ASP   HB3  H  N N 138 
ASP   HD2  H  N N 139 
ASP   HXT  H  N N 140 
CYS   N    N  N N 141 
CYS   CA   C  N R 142 
CYS   C    C  N N 143 
CYS   O    O  N N 144 
CYS   CB   C  N N 145 
CYS   SG   S  N N 146 
CYS   OXT  O  N N 147 
CYS   H    H  N N 148 
CYS   H2   H  N N 149 
CYS   HA   H  N N 150 
CYS   HB2  H  N N 151 
CYS   HB3  H  N N 152 
CYS   HG   H  N N 153 
CYS   HXT  H  N N 154 
GLN   N    N  N N 155 
GLN   CA   C  N S 156 
GLN   C    C  N N 157 
GLN   O    O  N N 158 
GLN   CB   C  N N 159 
GLN   CG   C  N N 160 
GLN   CD   C  N N 161 
GLN   OE1  O  N N 162 
GLN   NE2  N  N N 163 
GLN   OXT  O  N N 164 
GLN   H    H  N N 165 
GLN   H2   H  N N 166 
GLN   HA   H  N N 167 
GLN   HB2  H  N N 168 
GLN   HB3  H  N N 169 
GLN   HG2  H  N N 170 
GLN   HG3  H  N N 171 
GLN   HE21 H  N N 172 
GLN   HE22 H  N N 173 
GLN   HXT  H  N N 174 
GLU   N    N  N N 175 
GLU   CA   C  N S 176 
GLU   C    C  N N 177 
GLU   O    O  N N 178 
GLU   CB   C  N N 179 
GLU   CG   C  N N 180 
GLU   CD   C  N N 181 
GLU   OE1  O  N N 182 
GLU   OE2  O  N N 183 
GLU   OXT  O  N N 184 
GLU   H    H  N N 185 
GLU   H2   H  N N 186 
GLU   HA   H  N N 187 
GLU   HB2  H  N N 188 
GLU   HB3  H  N N 189 
GLU   HG2  H  N N 190 
GLU   HG3  H  N N 191 
GLU   HE2  H  N N 192 
GLU   HXT  H  N N 193 
GLY   N    N  N N 194 
GLY   CA   C  N N 195 
GLY   C    C  N N 196 
GLY   O    O  N N 197 
GLY   OXT  O  N N 198 
GLY   H    H  N N 199 
GLY   H2   H  N N 200 
GLY   HA2  H  N N 201 
GLY   HA3  H  N N 202 
GLY   HXT  H  N N 203 
HIS   N    N  N N 204 
HIS   CA   C  N S 205 
HIS   C    C  N N 206 
HIS   O    O  N N 207 
HIS   CB   C  N N 208 
HIS   CG   C  Y N 209 
HIS   ND1  N  Y N 210 
HIS   CD2  C  Y N 211 
HIS   CE1  C  Y N 212 
HIS   NE2  N  Y N 213 
HIS   OXT  O  N N 214 
HIS   H    H  N N 215 
HIS   H2   H  N N 216 
HIS   HA   H  N N 217 
HIS   HB2  H  N N 218 
HIS   HB3  H  N N 219 
HIS   HD1  H  N N 220 
HIS   HD2  H  N N 221 
HIS   HE1  H  N N 222 
HIS   HE2  H  N N 223 
HIS   HXT  H  N N 224 
HOH   O    O  N N 225 
HOH   H1   H  N N 226 
HOH   H2   H  N N 227 
ILE   N    N  N N 228 
ILE   CA   C  N S 229 
ILE   C    C  N N 230 
ILE   O    O  N N 231 
ILE   CB   C  N S 232 
ILE   CG1  C  N N 233 
ILE   CG2  C  N N 234 
ILE   CD1  C  N N 235 
ILE   OXT  O  N N 236 
ILE   H    H  N N 237 
ILE   H2   H  N N 238 
ILE   HA   H  N N 239 
ILE   HB   H  N N 240 
ILE   HG12 H  N N 241 
ILE   HG13 H  N N 242 
ILE   HG21 H  N N 243 
ILE   HG22 H  N N 244 
ILE   HG23 H  N N 245 
ILE   HD11 H  N N 246 
ILE   HD12 H  N N 247 
ILE   HD13 H  N N 248 
ILE   HXT  H  N N 249 
LEU   N    N  N N 250 
LEU   CA   C  N S 251 
LEU   C    C  N N 252 
LEU   O    O  N N 253 
LEU   CB   C  N N 254 
LEU   CG   C  N N 255 
LEU   CD1  C  N N 256 
LEU   CD2  C  N N 257 
LEU   OXT  O  N N 258 
LEU   H    H  N N 259 
LEU   H2   H  N N 260 
LEU   HA   H  N N 261 
LEU   HB2  H  N N 262 
LEU   HB3  H  N N 263 
LEU   HG   H  N N 264 
LEU   HD11 H  N N 265 
LEU   HD12 H  N N 266 
LEU   HD13 H  N N 267 
LEU   HD21 H  N N 268 
LEU   HD22 H  N N 269 
LEU   HD23 H  N N 270 
LEU   HXT  H  N N 271 
LYS   N    N  N N 272 
LYS   CA   C  N S 273 
LYS   C    C  N N 274 
LYS   O    O  N N 275 
LYS   CB   C  N N 276 
LYS   CG   C  N N 277 
LYS   CD   C  N N 278 
LYS   CE   C  N N 279 
LYS   NZ   N  N N 280 
LYS   OXT  O  N N 281 
LYS   H    H  N N 282 
LYS   H2   H  N N 283 
LYS   HA   H  N N 284 
LYS   HB2  H  N N 285 
LYS   HB3  H  N N 286 
LYS   HG2  H  N N 287 
LYS   HG3  H  N N 288 
LYS   HD2  H  N N 289 
LYS   HD3  H  N N 290 
LYS   HE2  H  N N 291 
LYS   HE3  H  N N 292 
LYS   HZ1  H  N N 293 
LYS   HZ2  H  N N 294 
LYS   HZ3  H  N N 295 
LYS   HXT  H  N N 296 
MET   N    N  N N 297 
MET   CA   C  N S 298 
MET   C    C  N N 299 
MET   O    O  N N 300 
MET   CB   C  N N 301 
MET   CG   C  N N 302 
MET   SD   S  N N 303 
MET   CE   C  N N 304 
MET   OXT  O  N N 305 
MET   H    H  N N 306 
MET   H2   H  N N 307 
MET   HA   H  N N 308 
MET   HB2  H  N N 309 
MET   HB3  H  N N 310 
MET   HG2  H  N N 311 
MET   HG3  H  N N 312 
MET   HE1  H  N N 313 
MET   HE2  H  N N 314 
MET   HE3  H  N N 315 
MET   HXT  H  N N 316 
PHE   N    N  N N 317 
PHE   CA   C  N S 318 
PHE   C    C  N N 319 
PHE   O    O  N N 320 
PHE   CB   C  N N 321 
PHE   CG   C  Y N 322 
PHE   CD1  C  Y N 323 
PHE   CD2  C  Y N 324 
PHE   CE1  C  Y N 325 
PHE   CE2  C  Y N 326 
PHE   CZ   C  Y N 327 
PHE   OXT  O  N N 328 
PHE   H    H  N N 329 
PHE   H2   H  N N 330 
PHE   HA   H  N N 331 
PHE   HB2  H  N N 332 
PHE   HB3  H  N N 333 
PHE   HD1  H  N N 334 
PHE   HD2  H  N N 335 
PHE   HE1  H  N N 336 
PHE   HE2  H  N N 337 
PHE   HZ   H  N N 338 
PHE   HXT  H  N N 339 
PRO   N    N  N N 340 
PRO   CA   C  N S 341 
PRO   C    C  N N 342 
PRO   O    O  N N 343 
PRO   CB   C  N N 344 
PRO   CG   C  N N 345 
PRO   CD   C  N N 346 
PRO   OXT  O  N N 347 
PRO   H    H  N N 348 
PRO   HA   H  N N 349 
PRO   HB2  H  N N 350 
PRO   HB3  H  N N 351 
PRO   HG2  H  N N 352 
PRO   HG3  H  N N 353 
PRO   HD2  H  N N 354 
PRO   HD3  H  N N 355 
PRO   HXT  H  N N 356 
SER   N    N  N N 357 
SER   CA   C  N S 358 
SER   C    C  N N 359 
SER   O    O  N N 360 
SER   CB   C  N N 361 
SER   OG   O  N N 362 
SER   OXT  O  N N 363 
SER   H    H  N N 364 
SER   H2   H  N N 365 
SER   HA   H  N N 366 
SER   HB2  H  N N 367 
SER   HB3  H  N N 368 
SER   HG   H  N N 369 
SER   HXT  H  N N 370 
THR   N    N  N N 371 
THR   CA   C  N S 372 
THR   C    C  N N 373 
THR   O    O  N N 374 
THR   CB   C  N R 375 
THR   OG1  O  N N 376 
THR   CG2  C  N N 377 
THR   OXT  O  N N 378 
THR   H    H  N N 379 
THR   H2   H  N N 380 
THR   HA   H  N N 381 
THR   HB   H  N N 382 
THR   HG1  H  N N 383 
THR   HG21 H  N N 384 
THR   HG22 H  N N 385 
THR   HG23 H  N N 386 
THR   HXT  H  N N 387 
TRP   N    N  N N 388 
TRP   CA   C  N S 389 
TRP   C    C  N N 390 
TRP   O    O  N N 391 
TRP   CB   C  N N 392 
TRP   CG   C  Y N 393 
TRP   CD1  C  Y N 394 
TRP   CD2  C  Y N 395 
TRP   NE1  N  Y N 396 
TRP   CE2  C  Y N 397 
TRP   CE3  C  Y N 398 
TRP   CZ2  C  Y N 399 
TRP   CZ3  C  Y N 400 
TRP   CH2  C  Y N 401 
TRP   OXT  O  N N 402 
TRP   H    H  N N 403 
TRP   H2   H  N N 404 
TRP   HA   H  N N 405 
TRP   HB2  H  N N 406 
TRP   HB3  H  N N 407 
TRP   HD1  H  N N 408 
TRP   HE1  H  N N 409 
TRP   HE3  H  N N 410 
TRP   HZ2  H  N N 411 
TRP   HZ3  H  N N 412 
TRP   HH2  H  N N 413 
TRP   HXT  H  N N 414 
TYR   N    N  N N 415 
TYR   CA   C  N S 416 
TYR   C    C  N N 417 
TYR   O    O  N N 418 
TYR   CB   C  N N 419 
TYR   CG   C  Y N 420 
TYR   CD1  C  Y N 421 
TYR   CD2  C  Y N 422 
TYR   CE1  C  Y N 423 
TYR   CE2  C  Y N 424 
TYR   CZ   C  Y N 425 
TYR   OH   O  N N 426 
TYR   OXT  O  N N 427 
TYR   H    H  N N 428 
TYR   H2   H  N N 429 
TYR   HA   H  N N 430 
TYR   HB2  H  N N 431 
TYR   HB3  H  N N 432 
TYR   HD1  H  N N 433 
TYR   HD2  H  N N 434 
TYR   HE1  H  N N 435 
TYR   HE2  H  N N 436 
TYR   HH   H  N N 437 
TYR   HXT  H  N N 438 
VAL   N    N  N N 439 
VAL   CA   C  N S 440 
VAL   C    C  N N 441 
VAL   O    O  N N 442 
VAL   CB   C  N N 443 
VAL   CG1  C  N N 444 
VAL   CG2  C  N N 445 
VAL   OXT  O  N N 446 
VAL   H    H  N N 447 
VAL   H2   H  N N 448 
VAL   HA   H  N N 449 
VAL   HB   H  N N 450 
VAL   HG11 H  N N 451 
VAL   HG12 H  N N 452 
VAL   HG13 H  N N 453 
VAL   HG21 H  N N 454 
VAL   HG22 H  N N 455 
VAL   HG23 H  N N 456 
VAL   HXT  H  N N 457 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1D50 C8  C7   doub Y N 1   
A1D50 C8  C9   sing Y N 2   
A1D50 O2  C10  doub N N 3   
A1D50 C7  C6   sing Y N 4   
A1D50 C9  C1   doub Y N 5   
A1D50 C6  C5   doub Y N 6   
A1D50 C1  C5   sing Y N 7   
A1D50 C1  N1   sing N N 8   
A1D50 C5  C4   sing N N 9   
A1D50 N1  C2   sing N N 10  
A1D50 C4  C10  sing N N 11  
A1D50 C4  C3   doub N N 12  
A1D50 C2  C3   sing N N 13  
A1D50 C2  O1   doub N N 14  
A1D50 C10 N2   sing N N 15  
A1D50 C12 C13  sing N N 16  
A1D50 C12 C11  sing N N 17  
A1D50 N2  C11  sing N N 18  
A1D50 C13 C14  sing N N 19  
A1D50 C11 C16  sing N N 20  
A1D50 C24 C25  sing N N 21  
A1D50 C24 N5   sing N N 22  
A1D50 C14 C15  sing N N 23  
A1D50 C16 C15  sing N N 24  
A1D50 C16 N3   sing N N 25  
A1D50 C25 O4   sing N N 26  
A1D50 O3  C23  doub N N 27  
A1D50 O4  C26  sing N N 28  
A1D50 N3  C17  sing N N 29  
A1D50 N5  C23  sing N N 30  
A1D50 N5  C27  sing N N 31  
A1D50 C23 C22  sing N N 32  
A1D50 C26 C27  sing N N 33  
A1D50 O6  N4   sing N N 34  
A1D50 C17 C22  doub Y N 35  
A1D50 C17 C18  sing Y N 36  
A1D50 C22 C21  sing Y N 37  
A1D50 N4  C18  sing N N 38  
A1D50 N4  O5   doub N N 39  
A1D50 C18 C19  doub Y N 40  
A1D50 C21 C20  doub Y N 41  
A1D50 C19 C20  sing Y N 42  
A1D50 C20 BR1  sing N N 43  
A1D50 N1  H1   sing N N 44  
A1D50 N3  H2   sing N N 45  
A1D50 C6  H3   sing N N 46  
A1D50 C7  H4   sing N N 47  
A1D50 C8  H5   sing N N 48  
A1D50 C13 H6   sing N N 49  
A1D50 C13 H7   sing N N 50  
A1D50 C15 H8   sing N N 51  
A1D50 C15 H9   sing N N 52  
A1D50 C21 H10  sing N N 53  
A1D50 C24 H11  sing N N 54  
A1D50 C24 H12  sing N N 55  
A1D50 C26 H13  sing N N 56  
A1D50 C26 H14  sing N N 57  
A1D50 C11 H15  sing N N 58  
A1D50 C12 H16  sing N N 59  
A1D50 C12 H17  sing N N 60  
A1D50 C14 H18  sing N N 61  
A1D50 C14 H19  sing N N 62  
A1D50 C16 H20  sing N N 63  
A1D50 C19 H21  sing N N 64  
A1D50 C25 H22  sing N N 65  
A1D50 C25 H23  sing N N 66  
A1D50 C27 H24  sing N N 67  
A1D50 C27 H25  sing N N 68  
A1D50 C3  H26  sing N N 69  
A1D50 C9  H27  sing N N 70  
A1D50 N2  H28  sing N N 71  
ALA   N   CA   sing N N 72  
ALA   N   H    sing N N 73  
ALA   N   H2   sing N N 74  
ALA   CA  C    sing N N 75  
ALA   CA  CB   sing N N 76  
ALA   CA  HA   sing N N 77  
ALA   C   O    doub N N 78  
ALA   C   OXT  sing N N 79  
ALA   CB  HB1  sing N N 80  
ALA   CB  HB2  sing N N 81  
ALA   CB  HB3  sing N N 82  
ALA   OXT HXT  sing N N 83  
ARG   N   CA   sing N N 84  
ARG   N   H    sing N N 85  
ARG   N   H2   sing N N 86  
ARG   CA  C    sing N N 87  
ARG   CA  CB   sing N N 88  
ARG   CA  HA   sing N N 89  
ARG   C   O    doub N N 90  
ARG   C   OXT  sing N N 91  
ARG   CB  CG   sing N N 92  
ARG   CB  HB2  sing N N 93  
ARG   CB  HB3  sing N N 94  
ARG   CG  CD   sing N N 95  
ARG   CG  HG2  sing N N 96  
ARG   CG  HG3  sing N N 97  
ARG   CD  NE   sing N N 98  
ARG   CD  HD2  sing N N 99  
ARG   CD  HD3  sing N N 100 
ARG   NE  CZ   sing N N 101 
ARG   NE  HE   sing N N 102 
ARG   CZ  NH1  sing N N 103 
ARG   CZ  NH2  doub N N 104 
ARG   NH1 HH11 sing N N 105 
ARG   NH1 HH12 sing N N 106 
ARG   NH2 HH21 sing N N 107 
ARG   NH2 HH22 sing N N 108 
ARG   OXT HXT  sing N N 109 
ASN   N   CA   sing N N 110 
ASN   N   H    sing N N 111 
ASN   N   H2   sing N N 112 
ASN   CA  C    sing N N 113 
ASN   CA  CB   sing N N 114 
ASN   CA  HA   sing N N 115 
ASN   C   O    doub N N 116 
ASN   C   OXT  sing N N 117 
ASN   CB  CG   sing N N 118 
ASN   CB  HB2  sing N N 119 
ASN   CB  HB3  sing N N 120 
ASN   CG  OD1  doub N N 121 
ASN   CG  ND2  sing N N 122 
ASN   ND2 HD21 sing N N 123 
ASN   ND2 HD22 sing N N 124 
ASN   OXT HXT  sing N N 125 
ASP   N   CA   sing N N 126 
ASP   N   H    sing N N 127 
ASP   N   H2   sing N N 128 
ASP   CA  C    sing N N 129 
ASP   CA  CB   sing N N 130 
ASP   CA  HA   sing N N 131 
ASP   C   O    doub N N 132 
ASP   C   OXT  sing N N 133 
ASP   CB  CG   sing N N 134 
ASP   CB  HB2  sing N N 135 
ASP   CB  HB3  sing N N 136 
ASP   CG  OD1  doub N N 137 
ASP   CG  OD2  sing N N 138 
ASP   OD2 HD2  sing N N 139 
ASP   OXT HXT  sing N N 140 
CYS   N   CA   sing N N 141 
CYS   N   H    sing N N 142 
CYS   N   H2   sing N N 143 
CYS   CA  C    sing N N 144 
CYS   CA  CB   sing N N 145 
CYS   CA  HA   sing N N 146 
CYS   C   O    doub N N 147 
CYS   C   OXT  sing N N 148 
CYS   CB  SG   sing N N 149 
CYS   CB  HB2  sing N N 150 
CYS   CB  HB3  sing N N 151 
CYS   SG  HG   sing N N 152 
CYS   OXT HXT  sing N N 153 
GLN   N   CA   sing N N 154 
GLN   N   H    sing N N 155 
GLN   N   H2   sing N N 156 
GLN   CA  C    sing N N 157 
GLN   CA  CB   sing N N 158 
GLN   CA  HA   sing N N 159 
GLN   C   O    doub N N 160 
GLN   C   OXT  sing N N 161 
GLN   CB  CG   sing N N 162 
GLN   CB  HB2  sing N N 163 
GLN   CB  HB3  sing N N 164 
GLN   CG  CD   sing N N 165 
GLN   CG  HG2  sing N N 166 
GLN   CG  HG3  sing N N 167 
GLN   CD  OE1  doub N N 168 
GLN   CD  NE2  sing N N 169 
GLN   NE2 HE21 sing N N 170 
GLN   NE2 HE22 sing N N 171 
GLN   OXT HXT  sing N N 172 
GLU   N   CA   sing N N 173 
GLU   N   H    sing N N 174 
GLU   N   H2   sing N N 175 
GLU   CA  C    sing N N 176 
GLU   CA  CB   sing N N 177 
GLU   CA  HA   sing N N 178 
GLU   C   O    doub N N 179 
GLU   C   OXT  sing N N 180 
GLU   CB  CG   sing N N 181 
GLU   CB  HB2  sing N N 182 
GLU   CB  HB3  sing N N 183 
GLU   CG  CD   sing N N 184 
GLU   CG  HG2  sing N N 185 
GLU   CG  HG3  sing N N 186 
GLU   CD  OE1  doub N N 187 
GLU   CD  OE2  sing N N 188 
GLU   OE2 HE2  sing N N 189 
GLU   OXT HXT  sing N N 190 
GLY   N   CA   sing N N 191 
GLY   N   H    sing N N 192 
GLY   N   H2   sing N N 193 
GLY   CA  C    sing N N 194 
GLY   CA  HA2  sing N N 195 
GLY   CA  HA3  sing N N 196 
GLY   C   O    doub N N 197 
GLY   C   OXT  sing N N 198 
GLY   OXT HXT  sing N N 199 
HIS   N   CA   sing N N 200 
HIS   N   H    sing N N 201 
HIS   N   H2   sing N N 202 
HIS   CA  C    sing N N 203 
HIS   CA  CB   sing N N 204 
HIS   CA  HA   sing N N 205 
HIS   C   O    doub N N 206 
HIS   C   OXT  sing N N 207 
HIS   CB  CG   sing N N 208 
HIS   CB  HB2  sing N N 209 
HIS   CB  HB3  sing N N 210 
HIS   CG  ND1  sing Y N 211 
HIS   CG  CD2  doub Y N 212 
HIS   ND1 CE1  doub Y N 213 
HIS   ND1 HD1  sing N N 214 
HIS   CD2 NE2  sing Y N 215 
HIS   CD2 HD2  sing N N 216 
HIS   CE1 NE2  sing Y N 217 
HIS   CE1 HE1  sing N N 218 
HIS   NE2 HE2  sing N N 219 
HIS   OXT HXT  sing N N 220 
HOH   O   H1   sing N N 221 
HOH   O   H2   sing N N 222 
ILE   N   CA   sing N N 223 
ILE   N   H    sing N N 224 
ILE   N   H2   sing N N 225 
ILE   CA  C    sing N N 226 
ILE   CA  CB   sing N N 227 
ILE   CA  HA   sing N N 228 
ILE   C   O    doub N N 229 
ILE   C   OXT  sing N N 230 
ILE   CB  CG1  sing N N 231 
ILE   CB  CG2  sing N N 232 
ILE   CB  HB   sing N N 233 
ILE   CG1 CD1  sing N N 234 
ILE   CG1 HG12 sing N N 235 
ILE   CG1 HG13 sing N N 236 
ILE   CG2 HG21 sing N N 237 
ILE   CG2 HG22 sing N N 238 
ILE   CG2 HG23 sing N N 239 
ILE   CD1 HD11 sing N N 240 
ILE   CD1 HD12 sing N N 241 
ILE   CD1 HD13 sing N N 242 
ILE   OXT HXT  sing N N 243 
LEU   N   CA   sing N N 244 
LEU   N   H    sing N N 245 
LEU   N   H2   sing N N 246 
LEU   CA  C    sing N N 247 
LEU   CA  CB   sing N N 248 
LEU   CA  HA   sing N N 249 
LEU   C   O    doub N N 250 
LEU   C   OXT  sing N N 251 
LEU   CB  CG   sing N N 252 
LEU   CB  HB2  sing N N 253 
LEU   CB  HB3  sing N N 254 
LEU   CG  CD1  sing N N 255 
LEU   CG  CD2  sing N N 256 
LEU   CG  HG   sing N N 257 
LEU   CD1 HD11 sing N N 258 
LEU   CD1 HD12 sing N N 259 
LEU   CD1 HD13 sing N N 260 
LEU   CD2 HD21 sing N N 261 
LEU   CD2 HD22 sing N N 262 
LEU   CD2 HD23 sing N N 263 
LEU   OXT HXT  sing N N 264 
LYS   N   CA   sing N N 265 
LYS   N   H    sing N N 266 
LYS   N   H2   sing N N 267 
LYS   CA  C    sing N N 268 
LYS   CA  CB   sing N N 269 
LYS   CA  HA   sing N N 270 
LYS   C   O    doub N N 271 
LYS   C   OXT  sing N N 272 
LYS   CB  CG   sing N N 273 
LYS   CB  HB2  sing N N 274 
LYS   CB  HB3  sing N N 275 
LYS   CG  CD   sing N N 276 
LYS   CG  HG2  sing N N 277 
LYS   CG  HG3  sing N N 278 
LYS   CD  CE   sing N N 279 
LYS   CD  HD2  sing N N 280 
LYS   CD  HD3  sing N N 281 
LYS   CE  NZ   sing N N 282 
LYS   CE  HE2  sing N N 283 
LYS   CE  HE3  sing N N 284 
LYS   NZ  HZ1  sing N N 285 
LYS   NZ  HZ2  sing N N 286 
LYS   NZ  HZ3  sing N N 287 
LYS   OXT HXT  sing N N 288 
MET   N   CA   sing N N 289 
MET   N   H    sing N N 290 
MET   N   H2   sing N N 291 
MET   CA  C    sing N N 292 
MET   CA  CB   sing N N 293 
MET   CA  HA   sing N N 294 
MET   C   O    doub N N 295 
MET   C   OXT  sing N N 296 
MET   CB  CG   sing N N 297 
MET   CB  HB2  sing N N 298 
MET   CB  HB3  sing N N 299 
MET   CG  SD   sing N N 300 
MET   CG  HG2  sing N N 301 
MET   CG  HG3  sing N N 302 
MET   SD  CE   sing N N 303 
MET   CE  HE1  sing N N 304 
MET   CE  HE2  sing N N 305 
MET   CE  HE3  sing N N 306 
MET   OXT HXT  sing N N 307 
PHE   N   CA   sing N N 308 
PHE   N   H    sing N N 309 
PHE   N   H2   sing N N 310 
PHE   CA  C    sing N N 311 
PHE   CA  CB   sing N N 312 
PHE   CA  HA   sing N N 313 
PHE   C   O    doub N N 314 
PHE   C   OXT  sing N N 315 
PHE   CB  CG   sing N N 316 
PHE   CB  HB2  sing N N 317 
PHE   CB  HB3  sing N N 318 
PHE   CG  CD1  doub Y N 319 
PHE   CG  CD2  sing Y N 320 
PHE   CD1 CE1  sing Y N 321 
PHE   CD1 HD1  sing N N 322 
PHE   CD2 CE2  doub Y N 323 
PHE   CD2 HD2  sing N N 324 
PHE   CE1 CZ   doub Y N 325 
PHE   CE1 HE1  sing N N 326 
PHE   CE2 CZ   sing Y N 327 
PHE   CE2 HE2  sing N N 328 
PHE   CZ  HZ   sing N N 329 
PHE   OXT HXT  sing N N 330 
PRO   N   CA   sing N N 331 
PRO   N   CD   sing N N 332 
PRO   N   H    sing N N 333 
PRO   CA  C    sing N N 334 
PRO   CA  CB   sing N N 335 
PRO   CA  HA   sing N N 336 
PRO   C   O    doub N N 337 
PRO   C   OXT  sing N N 338 
PRO   CB  CG   sing N N 339 
PRO   CB  HB2  sing N N 340 
PRO   CB  HB3  sing N N 341 
PRO   CG  CD   sing N N 342 
PRO   CG  HG2  sing N N 343 
PRO   CG  HG3  sing N N 344 
PRO   CD  HD2  sing N N 345 
PRO   CD  HD3  sing N N 346 
PRO   OXT HXT  sing N N 347 
SER   N   CA   sing N N 348 
SER   N   H    sing N N 349 
SER   N   H2   sing N N 350 
SER   CA  C    sing N N 351 
SER   CA  CB   sing N N 352 
SER   CA  HA   sing N N 353 
SER   C   O    doub N N 354 
SER   C   OXT  sing N N 355 
SER   CB  OG   sing N N 356 
SER   CB  HB2  sing N N 357 
SER   CB  HB3  sing N N 358 
SER   OG  HG   sing N N 359 
SER   OXT HXT  sing N N 360 
THR   N   CA   sing N N 361 
THR   N   H    sing N N 362 
THR   N   H2   sing N N 363 
THR   CA  C    sing N N 364 
THR   CA  CB   sing N N 365 
THR   CA  HA   sing N N 366 
THR   C   O    doub N N 367 
THR   C   OXT  sing N N 368 
THR   CB  OG1  sing N N 369 
THR   CB  CG2  sing N N 370 
THR   CB  HB   sing N N 371 
THR   OG1 HG1  sing N N 372 
THR   CG2 HG21 sing N N 373 
THR   CG2 HG22 sing N N 374 
THR   CG2 HG23 sing N N 375 
THR   OXT HXT  sing N N 376 
TRP   N   CA   sing N N 377 
TRP   N   H    sing N N 378 
TRP   N   H2   sing N N 379 
TRP   CA  C    sing N N 380 
TRP   CA  CB   sing N N 381 
TRP   CA  HA   sing N N 382 
TRP   C   O    doub N N 383 
TRP   C   OXT  sing N N 384 
TRP   CB  CG   sing N N 385 
TRP   CB  HB2  sing N N 386 
TRP   CB  HB3  sing N N 387 
TRP   CG  CD1  doub Y N 388 
TRP   CG  CD2  sing Y N 389 
TRP   CD1 NE1  sing Y N 390 
TRP   CD1 HD1  sing N N 391 
TRP   CD2 CE2  doub Y N 392 
TRP   CD2 CE3  sing Y N 393 
TRP   NE1 CE2  sing Y N 394 
TRP   NE1 HE1  sing N N 395 
TRP   CE2 CZ2  sing Y N 396 
TRP   CE3 CZ3  doub Y N 397 
TRP   CE3 HE3  sing N N 398 
TRP   CZ2 CH2  doub Y N 399 
TRP   CZ2 HZ2  sing N N 400 
TRP   CZ3 CH2  sing Y N 401 
TRP   CZ3 HZ3  sing N N 402 
TRP   CH2 HH2  sing N N 403 
TRP   OXT HXT  sing N N 404 
TYR   N   CA   sing N N 405 
TYR   N   H    sing N N 406 
TYR   N   H2   sing N N 407 
TYR   CA  C    sing N N 408 
TYR   CA  CB   sing N N 409 
TYR   CA  HA   sing N N 410 
TYR   C   O    doub N N 411 
TYR   C   OXT  sing N N 412 
TYR   CB  CG   sing N N 413 
TYR   CB  HB2  sing N N 414 
TYR   CB  HB3  sing N N 415 
TYR   CG  CD1  doub Y N 416 
TYR   CG  CD2  sing Y N 417 
TYR   CD1 CE1  sing Y N 418 
TYR   CD1 HD1  sing N N 419 
TYR   CD2 CE2  doub Y N 420 
TYR   CD2 HD2  sing N N 421 
TYR   CE1 CZ   doub Y N 422 
TYR   CE1 HE1  sing N N 423 
TYR   CE2 CZ   sing Y N 424 
TYR   CE2 HE2  sing N N 425 
TYR   CZ  OH   sing N N 426 
TYR   OH  HH   sing N N 427 
TYR   OXT HXT  sing N N 428 
VAL   N   CA   sing N N 429 
VAL   N   H    sing N N 430 
VAL   N   H2   sing N N 431 
VAL   CA  C    sing N N 432 
VAL   CA  CB   sing N N 433 
VAL   CA  HA   sing N N 434 
VAL   C   O    doub N N 435 
VAL   C   OXT  sing N N 436 
VAL   CB  CG1  sing N N 437 
VAL   CB  CG2  sing N N 438 
VAL   CB  HB   sing N N 439 
VAL   CG1 HG11 sing N N 440 
VAL   CG1 HG12 sing N N 441 
VAL   CG1 HG13 sing N N 442 
VAL   CG2 HG21 sing N N 443 
VAL   CG2 HG22 sing N N 444 
VAL   CG2 HG23 sing N N 445 
VAL   OXT HXT  sing N N 446 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    8Y44 
_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]   0.014712 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011181 
_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]   0.009700 
_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 
BR 
C  
N  
O  
S  
# 
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   . SER   A 1 1   ? -13.811 9.270   -1.214  1.00 30.35 ?  1   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? -14.132 8.228   -0.249  1.00 29.43 ?  1   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? -13.003 7.211   -0.158  1.00 31.42 ?  1   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? -12.099 7.186   -0.994  1.00 27.78 ?  1   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? -15.450 7.536   -0.621  1.00 32.76 ?  1   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? -15.876 6.638   0.391   1.00 40.11 ?  1   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? -13.049 6.376   0.870   1.00 32.60 ?  2   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? -11.973 5.447   1.129   1.00 26.13 ?  2   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? -11.009 5.974   2.177   1.00 27.27 ?  2   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? -10.936 7.173   2.461   1.00 30.72 ?  2   GLY   A O   1 
ATOM   11   N  N   . PHE   A 1 3   ? -10.253 5.054   2.762   1.00 26.00 ?  3   PHE   A N   1 
ATOM   12   C  CA  . PHE   A 1 3   ? -9.260  5.419   3.765   1.00 24.81 ?  3   PHE   A CA  1 
ATOM   13   C  C   . PHE   A 1 3   ? -8.157  4.375   3.730   1.00 28.06 ?  3   PHE   A C   1 
ATOM   14   O  O   . PHE   A 1 3   ? -8.423  3.180   3.882   1.00 27.16 ?  3   PHE   A O   1 
ATOM   15   C  CB  . PHE   A 1 3   ? -9.888  5.526   5.157   1.00 27.49 ?  3   PHE   A CB  1 
ATOM   16   C  CG  . PHE   A 1 3   ? -9.095  6.379   6.108   1.00 29.06 ?  3   PHE   A CG  1 
ATOM   17   C  CD1 . PHE   A 1 3   ? -9.151  7.761   6.027   1.00 29.39 ?  3   PHE   A CD1 1 
ATOM   18   C  CD2 . PHE   A 1 3   ? -8.277  5.801   7.063   1.00 30.92 ?  3   PHE   A CD2 1 
ATOM   19   C  CE1 . PHE   A 1 3   ? -8.414  8.550   6.889   1.00 29.73 ?  3   PHE   A CE1 1 
ATOM   20   C  CE2 . PHE   A 1 3   ? -7.541  6.582   7.936   1.00 28.84 ?  3   PHE   A CE2 1 
ATOM   21   C  CZ  . PHE   A 1 3   ? -7.606  7.961   7.847   1.00 30.18 ?  3   PHE   A CZ  1 
ATOM   22   N  N   . ARG   A 1 4   ? -6.931  4.828   3.492   1.00 28.54 ?  4   ARG   A N   1 
ATOM   23   C  CA  . ARG   A 1 4   ? -5.784  3.955   3.313   1.00 27.52 ?  4   ARG   A CA  1 
ATOM   24   C  C   . ARG   A 1 4   ? -4.650  4.429   4.205   1.00 27.64 ?  4   ARG   A C   1 
ATOM   25   O  O   . ARG   A 1 4   ? -4.555  5.615   4.529   1.00 29.36 ?  4   ARG   A O   1 
ATOM   26   C  CB  . ARG   A 1 4   ? -5.301  3.949   1.846   1.00 30.82 ?  4   ARG   A CB  1 
ATOM   27   C  CG  . ARG   A 1 4   ? -6.105  3.062   0.915   1.00 30.84 ?  4   ARG   A CG  1 
ATOM   28   C  CD  . ARG   A 1 4   ? -5.701  1.608   1.080   1.00 35.29 ?  4   ARG   A CD  1 
ATOM   29   N  NE  . ARG   A 1 4   ? -6.254  0.772   0.023   1.00 37.07 ?  4   ARG   A NE  1 
ATOM   30   C  CZ  . ARG   A 1 4   ? -5.973  -0.517  -0.139  1.00 39.85 ?  4   ARG   A CZ  1 
ATOM   31   N  NH1 . ARG   A 1 4   ? -5.137  -1.122  0.690   1.00 35.46 ?  4   ARG   A NH1 1 
ATOM   32   N  NH2 . ARG   A 1 4   ? -6.526  -1.201  -1.137  1.00 35.48 ?  4   ARG   A NH2 1 
ATOM   33   N  N   . LYS   A 1 5   ? -3.788  3.498   4.596   1.00 29.61 ?  5   LYS   A N   1 
ATOM   34   C  CA  . LYS   A 1 5   ? -2.573  3.884   5.313   1.00 32.41 ?  5   LYS   A CA  1 
ATOM   35   C  C   . LYS   A 1 5   ? -1.610  4.479   4.296   1.00 32.69 ?  5   LYS   A C   1 
ATOM   36   O  O   . LYS   A 1 5   ? -0.920  3.761   3.571   1.00 37.26 ?  5   LYS   A O   1 
ATOM   37   C  CB  . LYS   A 1 5   ? -1.959  2.700   6.047   1.00 34.25 ?  5   LYS   A CB  1 
ATOM   38   C  CG  . LYS   A 1 5   ? -0.903  3.118   7.080   1.00 34.01 ?  5   LYS   A CG  1 
ATOM   39   C  CD  . LYS   A 1 5   ? -0.716  2.053   8.128   1.00 38.23 ?  5   LYS   A CD  1 
ATOM   40   C  CE  . LYS   A 1 5   ? -1.901  2.019   9.066   1.00 37.70 ?  5   LYS   A CE  1 
ATOM   41   N  NZ  . LYS   A 1 5   ? -1.888  0.798   9.914   1.00 43.29 ?  5   LYS   A NZ  1 
ATOM   42   N  N   . MET   A 1 6   ? -1.574  5.802   4.243   1.00 31.61 ?  6   MET   A N   1 
ATOM   43   C  CA  . MET   A 1 6   ? -0.960  6.541   3.155   1.00 29.23 ?  6   MET   A CA  1 
ATOM   44   C  C   . MET   A 1 6   ? 0.387   7.092   3.607   1.00 29.50 ?  6   MET   A C   1 
ATOM   45   O  O   . MET   A 1 6   ? 0.477   7.721   4.668   1.00 29.80 ?  6   MET   A O   1 
ATOM   46   C  CB  . MET   A 1 6   ? -1.894  7.672   2.731   1.00 27.67 ?  6   MET   A CB  1 
ATOM   47   C  CG  . MET   A 1 6   ? -1.689  8.223   1.353   1.00 39.43 ?  6   MET   A CG  1 
ATOM   48   S  SD  . MET   A 1 6   ? -2.969  9.455   1.014   1.00 44.94 ?  6   MET   A SD  1 
ATOM   49   C  CE  . MET   A 1 6   ? -4.349  8.434   0.516   1.00 37.19 ?  6   MET   A CE  1 
ATOM   50   N  N   . ALA   A 1 7   ? 1.427   6.841   2.817   1.00 28.10 ?  7   ALA   A N   1 
ATOM   51   C  CA  . ALA   A 1 7   ? 2.738   7.420   3.076   1.00 28.27 ?  7   ALA   A CA  1 
ATOM   52   C  C   . ALA   A 1 7   ? 2.903   8.705   2.276   1.00 29.87 ?  7   ALA   A C   1 
ATOM   53   O  O   . ALA   A 1 7   ? 2.188   8.957   1.303   1.00 32.54 ?  7   ALA   A O   1 
ATOM   54   C  CB  . ALA   A 1 7   ? 3.857   6.437   2.725   1.00 24.99 ?  7   ALA   A CB  1 
ATOM   55   N  N   . PHE   A 1 8   ? 3.850   9.530   2.706   1.00 28.97 ?  8   PHE   A N   1 
ATOM   56   C  CA  . PHE   A 1 8   ? 4.197   10.716  1.943   1.00 29.46 ?  8   PHE   A CA  1 
ATOM   57   C  C   . PHE   A 1 8   ? 4.920   10.314  0.661   1.00 29.59 ?  8   PHE   A C   1 
ATOM   58   O  O   . PHE   A 1 8   ? 5.628   9.304   0.639   1.00 30.33 ?  8   PHE   A O   1 
ATOM   59   C  CB  . PHE   A 1 8   ? 5.096   11.638  2.761   1.00 27.90 ?  8   PHE   A CB  1 
ATOM   60   C  CG  . PHE   A 1 8   ? 4.375   12.379  3.849   1.00 32.93 ?  8   PHE   A CG  1 
ATOM   61   C  CD1 . PHE   A 1 8   ? 3.649   13.523  3.562   1.00 30.96 ?  8   PHE   A CD1 1 
ATOM   62   C  CD2 . PHE   A 1 8   ? 4.431   11.938  5.162   1.00 28.67 ?  8   PHE   A CD2 1 
ATOM   63   C  CE1 . PHE   A 1 8   ? 2.991   14.212  4.567   1.00 31.50 ?  8   PHE   A CE1 1 
ATOM   64   C  CE2 . PHE   A 1 8   ? 3.769   12.622  6.163   1.00 31.01 ?  8   PHE   A CE2 1 
ATOM   65   C  CZ  . PHE   A 1 8   ? 3.052   13.761  5.863   1.00 32.43 ?  8   PHE   A CZ  1 
ATOM   66   N  N   . PRO   A 1 9   ? 4.754   11.083  -0.419  1.00 28.29 ?  9   PRO   A N   1 
ATOM   67   C  CA  . PRO   A 1 9   ? 5.572   10.850  -1.618  1.00 30.37 ?  9   PRO   A CA  1 
ATOM   68   C  C   . PRO   A 1 9   ? 7.049   10.930  -1.265  1.00 32.41 ?  9   PRO   A C   1 
ATOM   69   O  O   . PRO   A 1 9   ? 7.487   11.868  -0.598  1.00 33.43 ?  9   PRO   A O   1 
ATOM   70   C  CB  . PRO   A 1 9   ? 5.160   11.986  -2.562  1.00 33.21 ?  9   PRO   A CB  1 
ATOM   71   C  CG  . PRO   A 1 9   ? 3.867   12.494  -2.032  1.00 39.11 ?  9   PRO   A CG  1 
ATOM   72   C  CD  . PRO   A 1 9   ? 3.915   12.285  -0.555  1.00 27.99 ?  9   PRO   A CD  1 
ATOM   73   N  N   . SER   A 1 10  ? 7.818   9.948   -1.735  1.00 28.27 ?  10  SER   A N   1 
ATOM   74   C  CA  . SER   A 1 10  ? 9.176   9.718   -1.259  1.00 30.09 ?  10  SER   A CA  1 
ATOM   75   C  C   . SER   A 1 10  ? 10.250  10.365  -2.123  1.00 32.79 ?  10  SER   A C   1 
ATOM   76   O  O   . SER   A 1 10  ? 11.436  10.233  -1.801  1.00 30.17 ?  10  SER   A O   1 
ATOM   77   C  CB  . SER   A 1 10  ? 9.444   8.213   -1.167  1.00 28.65 ?  10  SER   A CB  1 
ATOM   78   O  OG  . SER   A 1 10  ? 9.319   7.592   -2.437  1.00 30.75 ?  10  SER   A OG  1 
ATOM   79   N  N   . GLY   A 1 11  ? 9.866   11.070  -3.192  1.00 29.94 ?  11  GLY   A N   1 
ATOM   80   C  CA  . GLY   A 1 11  ? 10.846  11.522  -4.171  1.00 32.24 ?  11  GLY   A CA  1 
ATOM   81   C  C   . GLY   A 1 11  ? 11.923  12.408  -3.577  1.00 30.51 ?  11  GLY   A C   1 
ATOM   82   O  O   . GLY   A 1 11  ? 13.110  12.241  -3.864  1.00 28.72 ?  11  GLY   A O   1 
ATOM   83   N  N   . LYS   A 1 12  ? 11.526  13.368  -2.739  1.00 32.64 ?  12  LYS   A N   1 
ATOM   84   C  CA  . LYS   A 1 12  ? 12.513  14.291  -2.189  1.00 33.95 ?  12  LYS   A CA  1 
ATOM   85   C  C   . LYS   A 1 12  ? 13.531  13.574  -1.314  1.00 27.53 ?  12  LYS   A C   1 
ATOM   86   O  O   . LYS   A 1 12  ? 14.690  14.003  -1.234  1.00 32.29 ?  12  LYS   A O   1 
ATOM   87   C  CB  . LYS   A 1 12  ? 11.821  15.402  -1.409  1.00 31.67 ?  12  LYS   A CB  1 
ATOM   88   C  CG  . LYS   A 1 12  ? 11.022  16.341  -2.290  1.00 39.33 ?  12  LYS   A CG  1 
ATOM   89   C  CD  . LYS   A 1 12  ? 10.596  17.574  -1.519  1.00 45.07 ?  12  LYS   A CD  1 
ATOM   90   C  CE  . LYS   A 1 12  ? 10.278  18.730  -2.456  1.00 46.67 ?  12  LYS   A CE  1 
ATOM   91   N  NZ  . LYS   A 1 12  ? 10.364  20.029  -1.729  1.00 53.13 ?  12  LYS   A NZ  1 
ATOM   92   N  N   . VAL   A 1 13  ? 13.136  12.473  -0.682  1.00 30.11 ?  13  VAL   A N   1 
ATOM   93   C  CA  . VAL   A 1 13  ? 14.068  11.715  0.147   1.00 30.69 ?  13  VAL   A CA  1 
ATOM   94   C  C   . VAL   A 1 13  ? 14.868  10.709  -0.682  1.00 30.63 ?  13  VAL   A C   1 
ATOM   95   O  O   . VAL   A 1 13  ? 16.036  10.446  -0.375  1.00 27.21 ?  13  VAL   A O   1 
ATOM   96   C  CB  . VAL   A 1 13  ? 13.314  11.016  1.292   1.00 29.34 ?  13  VAL   A CB  1 
ATOM   97   C  CG1 . VAL   A 1 13  ? 14.273  10.200  2.156   1.00 31.52 ?  13  VAL   A CG1 1 
ATOM   98   C  CG2 . VAL   A 1 13  ? 12.572  12.035  2.144   1.00 29.15 ?  13  VAL   A CG2 1 
ATOM   99   N  N   . GLU   A 1 14  ? 14.260  10.138  -1.724  1.00 28.54 ?  14  GLU   A N   1 
ATOM   100  C  CA  . GLU   A 1 14  ? 14.975  9.222   -2.611  1.00 29.40 ?  14  GLU   A CA  1 
ATOM   101  C  C   . GLU   A 1 14  ? 16.263  9.835   -3.152  1.00 31.57 ?  14  GLU   A C   1 
ATOM   102  O  O   . GLU   A 1 14  ? 17.281  9.147   -3.275  1.00 31.61 ?  14  GLU   A O   1 
ATOM   103  C  CB  . GLU   A 1 14  ? 14.084  8.818   -3.786  1.00 26.37 ?  14  GLU   A CB  1 
ATOM   104  C  CG  . GLU   A 1 14  ? 12.955  7.875   -3.432  1.00 30.16 ?  14  GLU   A CG  1 
ATOM   105  C  CD  . GLU   A 1 14  ? 11.962  7.734   -4.568  1.00 31.57 ?  14  GLU   A CD  1 
ATOM   106  O  OE1 . GLU   A 1 14  ? 10.777  8.070   -4.362  1.00 31.53 ?  14  GLU   A OE1 1 
ATOM   107  O  OE2 . GLU   A 1 14  ? 12.377  7.309   -5.666  1.00 30.84 ?  14  GLU   A OE2 1 
ATOM   108  N  N   . GLY   A 1 15  ? 16.224  11.114  -3.522  1.00 28.34 ?  15  GLY   A N   1 
ATOM   109  C  CA  . GLY   A 1 15  ? 17.405  11.773  -4.036  1.00 28.54 ?  15  GLY   A CA  1 
ATOM   110  C  C   . GLY   A 1 15  ? 18.465  12.076  -3.003  1.00 31.84 ?  15  GLY   A C   1 
ATOM   111  O  O   . GLY   A 1 15  ? 19.503  12.646  -3.354  1.00 29.22 ?  15  GLY   A O   1 
ATOM   112  N  N   . CYS   A 1 16  ? 18.237  11.716  -1.737  1.00 28.19 ?  16  CYS   A N   1 
ATOM   113  C  CA  . CYS   A 1 16  ? 19.226  11.930  -0.687  1.00 27.28 ?  16  CYS   A CA  1 
ATOM   114  C  C   . CYS   A 1 16  ? 19.908  10.655  -0.217  1.00 26.79 ?  16  CYS   A C   1 
ATOM   115  O  O   . CYS   A 1 16  ? 20.843  10.740  0.583   1.00 28.42 ?  16  CYS   A O   1 
ATOM   116  C  CB  . CYS   A 1 16  ? 18.583  12.598  0.535   1.00 29.91 ?  16  CYS   A CB  1 
ATOM   117  S  SG  . CYS   A 1 16  ? 17.847  14.199  0.240   1.00 36.16 ?  16  CYS   A SG  1 
ATOM   118  N  N   . MET   A 1 17  ? 19.464  9.486   -0.660  1.00 24.66 ?  17  MET   A N   1 
ATOM   119  C  CA  . MET   A 1 17  ? 19.990  8.246   -0.115  1.00 24.71 ?  17  MET   A CA  1 
ATOM   120  C  C   . MET   A 1 17  ? 21.286  7.857   -0.817  1.00 30.95 ?  17  MET   A C   1 
ATOM   121  O  O   . MET   A 1 17  ? 21.389  7.922   -2.050  1.00 25.98 ?  17  MET   A O   1 
ATOM   122  C  CB  . MET   A 1 17  ? 18.953  7.128   -0.232  1.00 26.89 ?  17  MET   A CB  1 
ATOM   123  C  CG  . MET   A 1 17  ? 17.664  7.392   0.551   1.00 30.18 ?  17  MET   A CG  1 
ATOM   124  S  SD  . MET   A 1 17  ? 17.903  7.859   2.289   1.00 33.98 ?  17  MET   A SD  1 
ATOM   125  C  CE  . MET   A 1 17  ? 18.777  6.440   2.945   1.00 29.65 ?  17  MET   A CE  1 
ATOM   126  N  N   . VAL   A 1 18  ? 22.283  7.470   -0.023  1.00 24.13 ?  18  VAL   A N   1 
ATOM   127  C  CA  . VAL   A 1 18  ? 23.572  7.018   -0.523  1.00 26.82 ?  18  VAL   A CA  1 
ATOM   128  C  C   . VAL   A 1 18  ? 23.965  5.760   0.237   1.00 29.58 ?  18  VAL   A C   1 
ATOM   129  O  O   . VAL   A 1 18  ? 23.333  5.374   1.224   1.00 29.65 ?  18  VAL   A O   1 
ATOM   130  C  CB  . VAL   A 1 18  ? 24.670  8.092   -0.379  1.00 23.98 ?  18  VAL   A CB  1 
ATOM   131  C  CG1 . VAL   A 1 18  ? 24.292  9.340   -1.146  1.00 26.52 ?  18  VAL   A CG1 1 
ATOM   132  C  CG2 . VAL   A 1 18  ? 24.923  8.409   1.118   1.00 21.91 ?  18  VAL   A CG2 1 
ATOM   133  N  N   . GLN   A 1 19  ? 25.043  5.140   -0.229  1.00 26.42 ?  19  GLN   A N   1 
ATOM   134  C  CA  . GLN   A 1 19  ? 25.615  3.957   0.390   1.00 26.84 ?  19  GLN   A CA  1 
ATOM   135  C  C   . GLN   A 1 19  ? 26.912  4.345   1.092   1.00 32.49 ?  19  GLN   A C   1 
ATOM   136  O  O   . GLN   A 1 19  ? 27.756  5.039   0.511   1.00 31.00 ?  19  GLN   A O   1 
ATOM   137  C  CB  . GLN   A 1 19  ? 25.866  2.875   -0.659  1.00 27.92 ?  19  GLN   A CB  1 
ATOM   138  C  CG  . GLN   A 1 19  ? 26.431  1.589   -0.107  1.00 35.11 ?  19  GLN   A CG  1 
ATOM   139  C  CD  . GLN   A 1 19  ? 26.745  0.596   -1.199  1.00 39.66 ?  19  GLN   A CD  1 
ATOM   140  O  OE1 . GLN   A 1 19  ? 26.170  -0.491  -1.248  1.00 39.90 ?  19  GLN   A OE1 1 
ATOM   141  N  NE2 . GLN   A 1 19  ? 27.665  0.964   -2.088  1.00 41.43 ?  19  GLN   A NE2 1 
ATOM   142  N  N   . VAL   A 1 20  ? 27.058  3.920   2.343   1.00 28.94 ?  20  VAL   A N   1 
ATOM   143  C  CA  . VAL   A 1 20  ? 28.239  4.207   3.148   1.00 26.62 ?  20  VAL   A CA  1 
ATOM   144  C  C   . VAL   A 1 20  ? 28.909  2.887   3.483   1.00 33.52 ?  20  VAL   A C   1 
ATOM   145  O  O   . VAL   A 1 20  ? 28.260  1.973   4.004   1.00 32.35 ?  20  VAL   A O   1 
ATOM   146  C  CB  . VAL   A 1 20  ? 27.886  4.965   4.441   1.00 26.66 ?  20  VAL   A CB  1 
ATOM   147  C  CG1 . VAL   A 1 20  ? 29.150  5.246   5.254   1.00 29.58 ?  20  VAL   A CG1 1 
ATOM   148  C  CG2 . VAL   A 1 20  ? 27.134  6.248   4.130   1.00 26.02 ?  20  VAL   A CG2 1 
ATOM   149  N  N   . THR   A 1 21  ? 30.208  2.789   3.205   1.00 30.66 ?  21  THR   A N   1 
ATOM   150  C  CA  . THR   A 1 21  ? 30.953  1.590   3.549   1.00 34.94 ?  21  THR   A CA  1 
ATOM   151  C  C   . THR   A 1 21  ? 32.182  1.939   4.382   1.00 39.97 ?  21  THR   A C   1 
ATOM   152  O  O   . THR   A 1 21  ? 32.852  2.949   4.144   1.00 33.85 ?  21  THR   A O   1 
ATOM   153  C  CB  . THR   A 1 21  ? 31.347  0.817   2.296   1.00 39.00 ?  21  THR   A CB  1 
ATOM   154  O  OG1 . THR   A 1 21  ? 30.156  0.473   1.571   1.00 35.13 ?  21  THR   A OG1 1 
ATOM   155  C  CG2 . THR   A 1 21  ? 32.090  -0.458  2.670   1.00 40.85 ?  21  THR   A CG2 1 
ATOM   156  N  N   . CYS   A 1 22  ? 32.438  1.108   5.388   1.00 36.14 ?  22  CYS   A N   1 
ATOM   157  C  CA  . CYS   A 1 22  ? 33.613  1.209   6.242   1.00 37.44 ?  22  CYS   A CA  1 
ATOM   158  C  C   . CYS   A 1 22  ? 34.063  -0.220  6.500   1.00 40.21 ?  22  CYS   A C   1 
ATOM   159  O  O   . CYS   A 1 22  ? 33.349  -0.987  7.152   1.00 40.93 ?  22  CYS   A O   1 
ATOM   160  C  CB  . CYS   A 1 22  ? 33.295  1.939   7.548   1.00 33.01 ?  22  CYS   A CB  1 
ATOM   161  S  SG  . CYS   A 1 22  ? 34.738  2.218   8.586   1.00 40.15 ?  22  CYS   A SG  1 
ATOM   162  N  N   . GLY   A 1 23  ? 35.218  -0.590  5.967   1.00 41.40 ?  23  GLY   A N   1 
ATOM   163  C  CA  . GLY   A 1 23  ? 35.634  -1.979  6.070   1.00 42.89 ?  23  GLY   A CA  1 
ATOM   164  C  C   . GLY   A 1 23  ? 34.700  -2.860  5.263   1.00 39.25 ?  23  GLY   A C   1 
ATOM   165  O  O   . GLY   A 1 23  ? 34.387  -2.572  4.102   1.00 38.97 ?  23  GLY   A O   1 
ATOM   166  N  N   . THR   A 1 24  ? 34.244  -3.950  5.872   1.00 39.22 ?  24  THR   A N   1 
ATOM   167  C  CA  . THR   A 1 24  ? 33.275  -4.835  5.242   1.00 42.84 ?  24  THR   A CA  1 
ATOM   168  C  C   . THR   A 1 24  ? 31.841  -4.514  5.653   1.00 41.36 ?  24  THR   A C   1 
ATOM   169  O  O   . THR   A 1 24  ? 30.918  -5.246  5.278   1.00 39.65 ?  24  THR   A O   1 
ATOM   170  C  CB  . THR   A 1 24  ? 33.603  -6.292  5.566   1.00 43.97 ?  24  THR   A CB  1 
ATOM   171  O  OG1 . THR   A 1 24  ? 33.681  -6.456  6.985   1.00 49.18 ?  24  THR   A OG1 1 
ATOM   172  C  CG2 . THR   A 1 24  ? 34.933  -6.686  4.949   1.00 46.75 ?  24  THR   A CG2 1 
ATOM   173  N  N   . THR   A 1 25  ? 31.636  -3.434  6.407   1.00 39.12 ?  25  THR   A N   1 
ATOM   174  C  CA  . THR   A 1 25  ? 30.306  -3.016  6.840   1.00 44.27 ?  25  THR   A CA  1 
ATOM   175  C  C   . THR   A 1 25  ? 29.745  -1.991  5.858   1.00 42.25 ?  25  THR   A C   1 
ATOM   176  O  O   . THR   A 1 25  ? 30.391  -0.976  5.574   1.00 45.99 ?  25  THR   A O   1 
ATOM   177  C  CB  . THR   A 1 25  ? 30.358  -2.420  8.247   1.00 40.69 ?  25  THR   A CB  1 
ATOM   178  O  OG1 . THR   A 1 25  ? 31.076  -3.298  9.127   1.00 47.31 ?  25  THR   A OG1 1 
ATOM   179  C  CG2 . THR   A 1 25  ? 28.958  -2.200  8.782   1.00 40.69 ?  25  THR   A CG2 1 
ATOM   180  N  N   . THR   A 1 26  ? 28.546  -2.249  5.346   1.00 38.64 ?  26  THR   A N   1 
ATOM   181  C  CA  . THR   A 1 26  ? 27.847  -1.299  4.495   1.00 39.71 ?  26  THR   A CA  1 
ATOM   182  C  C   . THR   A 1 26  ? 26.450  -1.033  5.050   1.00 38.20 ?  26  THR   A C   1 
ATOM   183  O  O   . THR   A 1 26  ? 25.852  -1.891  5.708   1.00 40.68 ?  26  THR   A O   1 
ATOM   184  C  CB  . THR   A 1 26  ? 27.754  -1.804  3.052   1.00 39.37 ?  26  THR   A CB  1 
ATOM   185  O  OG1 . THR   A 1 26  ? 27.291  -0.747  2.205   1.00 45.48 ?  26  THR   A OG1 1 
ATOM   186  C  CG2 . THR   A 1 26  ? 26.794  -2.985  2.947   1.00 40.30 ?  26  THR   A CG2 1 
ATOM   187  N  N   . LEU   A 1 27  ? 25.947  0.170   4.800   1.00 31.22 ?  27  LEU   A N   1 
ATOM   188  C  CA  . LEU   A 1 27  ? 24.599  0.578   5.206   1.00 27.77 ?  27  LEU   A CA  1 
ATOM   189  C  C   . LEU   A 1 27  ? 24.261  1.862   4.457   1.00 26.77 ?  27  LEU   A C   1 
ATOM   190  O  O   . LEU   A 1 27  ? 25.033  2.323   3.606   1.00 29.86 ?  27  LEU   A O   1 
ATOM   191  C  CB  . LEU   A 1 27  ? 24.485  0.754   6.725   1.00 25.52 ?  27  LEU   A CB  1 
ATOM   192  C  CG  . LEU   A 1 27  ? 25.558  1.506   7.520   1.00 29.27 ?  27  LEU   A CG  1 
ATOM   193  C  CD1 . LEU   A 1 27  ? 25.592  3.000   7.199   1.00 25.24 ?  27  LEU   A CD1 1 
ATOM   194  C  CD2 . LEU   A 1 27  ? 25.346  1.285   9.022   1.00 33.90 ?  27  LEU   A CD2 1 
ATOM   195  N  N   . ASN   A 1 28  ? 23.119  2.454   4.796   1.00 23.24 ?  28  ASN   A N   1 
ATOM   196  C  CA  . ASN   A 1 28  ? 22.592  3.616   4.102   1.00 25.56 ?  28  ASN   A CA  1 
ATOM   197  C  C   . ASN   A 1 28  ? 22.991  4.915   4.794   1.00 27.88 ?  28  ASN   A C   1 
ATOM   198  O  O   . ASN   A 1 28  ? 23.111  4.982   6.023   1.00 24.64 ?  28  ASN   A O   1 
ATOM   199  C  CB  . ASN   A 1 28  ? 21.066  3.531   4.004   1.00 25.78 ?  28  ASN   A CB  1 
ATOM   200  C  CG  . ASN   A 1 28  ? 20.601  2.214   3.415   1.00 25.29 ?  28  ASN   A CG  1 
ATOM   201  O  OD1 . ASN   A 1 28  ? 20.689  2.000   2.205   1.00 26.17 ?  28  ASN   A OD1 1 
ATOM   202  N  ND2 . ASN   A 1 28  ? 20.125  1.315   4.270   1.00 24.76 ?  28  ASN   A ND2 1 
ATOM   203  N  N   . GLY   A 1 29  ? 23.172  5.960   3.980   1.00 26.07 ?  29  GLY   A N   1 
ATOM   204  C  CA  . GLY   A 1 29  ? 23.424  7.289   4.489   1.00 25.20 ?  29  GLY   A CA  1 
ATOM   205  C  C   . GLY   A 1 29  ? 22.466  8.298   3.896   1.00 26.49 ?  29  GLY   A C   1 
ATOM   206  O  O   . GLY   A 1 29  ? 21.834  8.067   2.865   1.00 29.04 ?  29  GLY   A O   1 
ATOM   207  N  N   . LEU   A 1 30  ? 22.366  9.446   4.566   1.00 24.29 ?  30  LEU   A N   1 
ATOM   208  C  CA  . LEU   A 1 30  ? 21.460  10.519  4.166   1.00 25.61 ?  30  LEU   A CA  1 
ATOM   209  C  C   . LEU   A 1 30  ? 22.315  11.720  3.797   1.00 25.65 ?  30  LEU   A C   1 
ATOM   210  O  O   . LEU   A 1 30  ? 22.979  12.300  4.659   1.00 24.60 ?  30  LEU   A O   1 
ATOM   211  C  CB  . LEU   A 1 30  ? 20.470  10.857  5.288   1.00 24.41 ?  30  LEU   A CB  1 
ATOM   212  C  CG  . LEU   A 1 30  ? 19.463  11.989  5.053   1.00 29.61 ?  30  LEU   A CG  1 
ATOM   213  C  CD1 . LEU   A 1 30  ? 18.396  11.591  4.045   1.00 28.52 ?  30  LEU   A CD1 1 
ATOM   214  C  CD2 . LEU   A 1 30  ? 18.809  12.433  6.363   1.00 28.25 ?  30  LEU   A CD2 1 
ATOM   215  N  N   . TRP   A 1 31  ? 22.303  12.086  2.517   1.00 26.73 ?  31  TRP   A N   1 
ATOM   216  C  CA  . TRP   A 1 31  ? 23.203  13.091  1.958   1.00 26.44 ?  31  TRP   A CA  1 
ATOM   217  C  C   . TRP   A 1 31  ? 22.443  14.408  1.814   1.00 29.35 ?  31  TRP   A C   1 
ATOM   218  O  O   . TRP   A 1 31  ? 21.597  14.548  0.927   1.00 29.25 ?  31  TRP   A O   1 
ATOM   219  C  CB  . TRP   A 1 31  ? 23.737  12.601  0.612   1.00 25.63 ?  31  TRP   A CB  1 
ATOM   220  C  CG  . TRP   A 1 31  ? 24.675  13.523  -0.106  1.00 27.62 ?  31  TRP   A CG  1 
ATOM   221  C  CD1 . TRP   A 1 31  ? 25.438  14.523  0.435   1.00 30.28 ?  31  TRP   A CD1 1 
ATOM   222  C  CD2 . TRP   A 1 31  ? 24.951  13.527  -1.513  1.00 27.15 ?  31  TRP   A CD2 1 
ATOM   223  N  NE1 . TRP   A 1 31  ? 26.171  15.145  -0.552  1.00 30.79 ?  31  TRP   A NE1 1 
ATOM   224  C  CE2 . TRP   A 1 31  ? 25.891  14.549  -1.754  1.00 27.87 ?  31  TRP   A CE2 1 
ATOM   225  C  CE3 . TRP   A 1 31  ? 24.495  12.760  -2.591  1.00 32.79 ?  31  TRP   A CE3 1 
ATOM   226  C  CZ2 . TRP   A 1 31  ? 26.378  14.827  -3.030  1.00 31.67 ?  31  TRP   A CZ2 1 
ATOM   227  C  CZ3 . TRP   A 1 31  ? 24.977  13.040  -3.857  1.00 31.93 ?  31  TRP   A CZ3 1 
ATOM   228  C  CH2 . TRP   A 1 31  ? 25.905  14.065  -4.068  1.00 33.13 ?  31  TRP   A CH2 1 
ATOM   229  N  N   . LEU   A 1 32  ? 22.746  15.375  2.678   1.00 27.99 ?  32  LEU   A N   1 
ATOM   230  C  CA  . LEU   A 1 32  ? 22.093  16.680  2.643   1.00 28.86 ?  32  LEU   A CA  1 
ATOM   231  C  C   . LEU   A 1 32  ? 23.165  17.755  2.646   1.00 29.99 ?  32  LEU   A C   1 
ATOM   232  O  O   . LEU   A 1 32  ? 24.002  17.782  3.548   1.00 30.77 ?  32  LEU   A O   1 
ATOM   233  C  CB  . LEU   A 1 32  ? 21.158  16.876  3.842   1.00 27.35 ?  32  LEU   A CB  1 
ATOM   234  C  CG  . LEU   A 1 32  ? 20.034  15.865  4.046   1.00 28.49 ?  32  LEU   A CG  1 
ATOM   235  C  CD1 . LEU   A 1 32  ? 19.495  15.988  5.466   1.00 26.88 ?  32  LEU   A CD1 1 
ATOM   236  C  CD2 . LEU   A 1 32  ? 18.908  16.074  3.028   1.00 24.16 ?  32  LEU   A CD2 1 
ATOM   237  N  N   . ASP   A 1 33  ? 23.131  18.640  1.651   1.00 32.00 ?  33  ASP   A N   1 
ATOM   238  C  CA  . ASP   A 1 33  ? 24.192  19.640  1.434   1.00 33.42 ?  33  ASP   A CA  1 
ATOM   239  C  C   . ASP   A 1 33  ? 25.499  18.865  1.279   1.00 30.04 ?  33  ASP   A C   1 
ATOM   240  O  O   . ASP   A 1 33  ? 25.535  17.862  0.548   1.00 29.59 ?  33  ASP   A O   1 
ATOM   241  C  CB  . ASP   A 1 33  ? 24.173  20.680  2.552   1.00 32.54 ?  33  ASP   A CB  1 
ATOM   242  C  CG  . ASP   A 1 33  ? 22.849  21.398  2.657   1.00 40.87 ?  33  ASP   A CG  1 
ATOM   243  O  OD1 . ASP   A 1 33  ? 22.241  21.660  1.601   1.00 43.82 ?  33  ASP   A OD1 1 
ATOM   244  O  OD2 . ASP   A 1 33  ? 22.416  21.700  3.795   1.00 48.32 ?  33  ASP   A OD2 1 
ATOM   245  N  N   . ASP   A 1 34  ? 26.583  19.249  1.950   1.00 31.85 ?  34  ASP   A N   1 
ATOM   246  C  CA  . ASP   A 1 34  ? 27.837  18.516  1.844   1.00 30.44 ?  34  ASP   A CA  1 
ATOM   247  C  C   . ASP   A 1 34  ? 28.089  17.609  3.047   1.00 32.61 ?  34  ASP   A C   1 
ATOM   248  O  O   . ASP   A 1 34  ? 29.245  17.403  3.434   1.00 30.52 ?  34  ASP   A O   1 
ATOM   249  C  CB  . ASP   A 1 34  ? 29.003  19.485  1.657   1.00 32.70 ?  34  ASP   A CB  1 
ATOM   250  C  CG  . ASP   A 1 34  ? 29.185  20.422  2.843   1.00 35.71 ?  34  ASP   A CG  1 
ATOM   251  O  OD1 . ASP   A 1 34  ? 28.317  20.439  3.741   1.00 31.82 ?  34  ASP   A OD1 1 
ATOM   252  O  OD2 . ASP   A 1 34  ? 30.208  21.140  2.884   1.00 40.35 ?  34  ASP   A OD2 1 
ATOM   253  N  N   . VAL   A 1 35  ? 27.036  17.056  3.646   1.00 26.48 ?  35  VAL   A N   1 
ATOM   254  C  CA  . VAL   A 1 35  ? 27.176  16.179  4.801   1.00 27.77 ?  35  VAL   A CA  1 
ATOM   255  C  C   . VAL   A 1 35  ? 26.362  14.920  4.568   1.00 30.02 ?  35  VAL   A C   1 
ATOM   256  O  O   . VAL   A 1 35  ? 25.225  14.988  4.087   1.00 34.56 ?  35  VAL   A O   1 
ATOM   257  C  CB  . VAL   A 1 35  ? 26.719  16.872  6.099   1.00 29.08 ?  35  VAL   A CB  1 
ATOM   258  C  CG1 . VAL   A 1 35  ? 26.790  15.902  7.260   1.00 29.47 ?  35  VAL   A CG1 1 
ATOM   259  C  CG2 . VAL   A 1 35  ? 27.582  18.091  6.369   1.00 34.88 ?  35  VAL   A CG2 1 
ATOM   260  N  N   . VAL   A 1 36  ? 26.938  13.770  4.911   1.00 24.46 ?  36  VAL   A N   1 
ATOM   261  C  CA  . VAL   A 1 36  ? 26.237  12.493  4.882   1.00 22.78 ?  36  VAL   A CA  1 
ATOM   262  C  C   . VAL   A 1 36  ? 26.074  12.018  6.315   1.00 26.53 ?  36  VAL   A C   1 
ATOM   263  O  O   . VAL   A 1 36  ? 27.057  11.966  7.066   1.00 24.54 ?  36  VAL   A O   1 
ATOM   264  C  CB  . VAL   A 1 36  ? 26.987  11.447  4.044   1.00 30.87 ?  36  VAL   A CB  1 
ATOM   265  C  CG1 . VAL   A 1 36  ? 26.255  10.116  4.115   1.00 29.23 ?  36  VAL   A CG1 1 
ATOM   266  C  CG2 . VAL   A 1 36  ? 27.104  11.925  2.599   1.00 26.64 ?  36  VAL   A CG2 1 
ATOM   267  N  N   . TYR   A 1 37  ? 24.836  11.691  6.694   1.00 24.45 ?  37  TYR   A N   1 
ATOM   268  C  CA  . TYR   A 1 37  ? 24.501  11.223  8.034   1.00 22.01 ?  37  TYR   A CA  1 
ATOM   269  C  C   . TYR   A 1 37  ? 24.279  9.716   8.007   1.00 25.83 ?  37  TYR   A C   1 
ATOM   270  O  O   . TYR   A 1 37  ? 23.662  9.194   7.076   1.00 28.01 ?  37  TYR   A O   1 
ATOM   271  C  CB  . TYR   A 1 37  ? 23.239  11.927  8.546   1.00 24.25 ?  37  TYR   A CB  1 
ATOM   272  C  CG  . TYR   A 1 37  ? 23.340  13.443  8.587   1.00 25.99 ?  37  TYR   A CG  1 
ATOM   273  C  CD1 . TYR   A 1 37  ? 23.132  14.205  7.439   1.00 29.62 ?  37  TYR   A CD1 1 
ATOM   274  C  CD2 . TYR   A 1 37  ? 23.649  14.111  9.773   1.00 25.82 ?  37  TYR   A CD2 1 
ATOM   275  C  CE1 . TYR   A 1 37  ? 23.228  15.588  7.467   1.00 28.28 ?  37  TYR   A CE1 1 
ATOM   276  C  CE2 . TYR   A 1 37  ? 23.737  15.499  9.814   1.00 26.05 ?  37  TYR   A CE2 1 
ATOM   277  C  CZ  . TYR   A 1 37  ? 23.527  16.229  8.654   1.00 29.81 ?  37  TYR   A CZ  1 
ATOM   278  O  OH  . TYR   A 1 37  ? 23.614  17.603  8.678   1.00 32.66 ?  37  TYR   A OH  1 
ATOM   279  N  N   . CYS   A 1 38  ? 24.760  9.009   9.027   1.00 20.94 ?  38  CYS   A N   1 
ATOM   280  C  CA  . CYS   A 1 38  ? 24.549  7.567   9.057   1.00 23.18 ?  38  CYS   A CA  1 
ATOM   281  C  C   . CYS   A 1 38  ? 24.751  7.068   10.480  1.00 28.99 ?  38  CYS   A C   1 
ATOM   282  O  O   . CYS   A 1 38  ? 25.313  7.780   11.328  1.00 26.14 ?  38  CYS   A O   1 
ATOM   283  C  CB  . CYS   A 1 38  ? 25.483  6.840   8.067   1.00 27.42 ?  38  CYS   A CB  1 
ATOM   284  S  SG  . CYS   A 1 38  ? 27.199  6.739   8.549   1.00 29.29 ?  38  CYS   A SG  1 
ATOM   285  N  N   . PRO   A 1 39  ? 24.288  5.854   10.786  1.00 29.49 ?  39  PRO   A N   1 
ATOM   286  C  CA  . PRO   A 1 39  ? 24.522  5.302   12.126  1.00 23.84 ?  39  PRO   A CA  1 
ATOM   287  C  C   . PRO   A 1 39  ? 26.006  5.076   12.389  1.00 25.32 ?  39  PRO   A C   1 
ATOM   288  O  O   . PRO   A 1 39  ? 26.740  4.556   11.547  1.00 24.43 ?  39  PRO   A O   1 
ATOM   289  C  CB  . PRO   A 1 39  ? 23.755  3.978   12.103  1.00 24.91 ?  39  PRO   A CB  1 
ATOM   290  C  CG  . PRO   A 1 39  ? 22.682  4.176   11.042  1.00 23.42 ?  39  PRO   A CG  1 
ATOM   291  C  CD  . PRO   A 1 39  ? 23.391  4.994   9.986   1.00 23.63 ?  39  PRO   A CD  1 
ATOM   292  N  N   . ARG   A 1 40  ? 26.441  5.449   13.590  1.00 22.26 ?  40  ARG   A N   1 
ATOM   293  C  CA  . ARG   A 1 40  ? 27.861  5.351   13.910  1.00 22.87 ?  40  ARG   A CA  1 
ATOM   294  C  C   . ARG   A 1 40  ? 28.354  3.907   13.989  1.00 26.30 ?  40  ARG   A C   1 
ATOM   295  O  O   . ARG   A 1 40  ? 29.567  3.679   13.891  1.00 26.12 ?  40  ARG   A O   1 
ATOM   296  C  CB  . ARG   A 1 40  ? 28.158  6.094   15.212  1.00 22.62 ?  40  ARG   A CB  1 
ATOM   297  C  CG  . ARG   A 1 40  ? 27.630  5.403   16.454  1.00 23.24 ?  40  ARG   A CG  1 
ATOM   298  C  CD  . ARG   A 1 40  ? 27.935  6.228   17.704  1.00 24.61 ?  40  ARG   A CD  1 
ATOM   299  N  NE  . ARG   A 1 40  ? 27.307  5.679   18.907  1.00 25.44 ?  40  ARG   A NE  1 
ATOM   300  C  CZ  . ARG   A 1 40  ? 27.584  6.096   20.144  1.00 30.31 ?  40  ARG   A CZ  1 
ATOM   301  N  NH1 . ARG   A 1 40  ? 28.480  7.060   20.323  1.00 25.90 ?  40  ARG   A NH1 1 
ATOM   302  N  NH2 . ARG   A 1 40  ? 26.977  5.548   21.202  1.00 21.65 ?  40  ARG   A NH2 1 
ATOM   303  N  N   . HIS   A 1 41  ? 27.454  2.923   14.133  1.00 25.84 ?  41  HIS   A N   1 
ATOM   304  C  CA  . HIS   A 1 41  ? 27.923  1.540   14.169  1.00 23.30 ?  41  HIS   A CA  1 
ATOM   305  C  C   . HIS   A 1 41  ? 28.445  1.049   12.811  1.00 26.39 ?  41  HIS   A C   1 
ATOM   306  O  O   . HIS   A 1 41  ? 28.846  -0.119  12.713  1.00 28.02 ?  41  HIS   A O   1 
ATOM   307  C  CB  . HIS   A 1 41  ? 26.834  0.595   14.720  1.00 27.66 ?  41  HIS   A CB  1 
ATOM   308  C  CG  . HIS   A 1 41  ? 25.635  0.435   13.830  1.00 31.14 ?  41  HIS   A CG  1 
ATOM   309  N  ND1 . HIS   A 1 41  ? 24.349  0.620   14.291  1.00 29.21 ?  41  HIS   A ND1 1 
ATOM   310  C  CD2 . HIS   A 1 41  ? 25.517  0.049   12.538  1.00 33.49 ?  41  HIS   A CD2 1 
ATOM   311  C  CE1 . HIS   A 1 41  ? 23.489  0.388   13.314  1.00 31.20 ?  41  HIS   A CE1 1 
ATOM   312  N  NE2 . HIS   A 1 41  ? 24.172  0.039   12.237  1.00 34.51 ?  41  HIS   A NE2 1 
ATOM   313  N  N   . VAL   A 1 42  ? 28.464  1.892   11.773  1.00 22.38 ?  42  VAL   A N   1 
ATOM   314  C  CA  . VAL   A 1 42  ? 29.135  1.520   10.536  1.00 26.27 ?  42  VAL   A CA  1 
ATOM   315  C  C   . VAL   A 1 42  ? 30.632  1.328   10.740  1.00 27.93 ?  42  VAL   A C   1 
ATOM   316  O  O   . VAL   A 1 42  ? 31.287  0.700   9.908   1.00 27.43 ?  42  VAL   A O   1 
ATOM   317  C  CB  . VAL   A 1 42  ? 28.867  2.579   9.456   1.00 25.78 ?  42  VAL   A CB  1 
ATOM   318  C  CG1 . VAL   A 1 42  ? 29.677  3.843   9.731   1.00 23.93 ?  42  VAL   A CG1 1 
ATOM   319  C  CG2 . VAL   A 1 42  ? 29.165  2.013   8.051   1.00 28.14 ?  42  VAL   A CG2 1 
ATOM   320  N  N   . ILE   A 1 43  ? 31.201  1.852   11.834  1.00 25.12 ?  43  ILE   A N   1 
ATOM   321  C  CA  . ILE   A 1 43  ? 32.641  1.721   12.048  1.00 26.19 ?  43  ILE   A CA  1 
ATOM   322  C  C   . ILE   A 1 43  ? 33.005  0.481   12.848  1.00 30.18 ?  43  ILE   A C   1 
ATOM   323  O  O   . ILE   A 1 43  ? 34.199  0.227   13.070  1.00 33.58 ?  43  ILE   A O   1 
ATOM   324  C  CB  . ILE   A 1 43  ? 33.234  2.962   12.744  1.00 25.90 ?  43  ILE   A CB  1 
ATOM   325  C  CG1 . ILE   A 1 43  ? 32.778  3.047   14.202  1.00 28.61 ?  43  ILE   A CG1 1 
ATOM   326  C  CG2 . ILE   A 1 43  ? 32.866  4.225   11.998  1.00 29.46 ?  43  ILE   A CG2 1 
ATOM   327  C  CD1 . ILE   A 1 43  ? 33.350  4.250   14.925  1.00 22.81 ?  43  ILE   A CD1 1 
ATOM   328  N  N   . CYS   A 1 44  ? 32.023  -0.306  13.273  1.00 26.73 ?  44  CYS   A N   1 
ATOM   329  C  CA  . CYS   A 1 44  ? 32.247  -1.469  14.117  1.00 33.12 ?  44  CYS   A CA  1 
ATOM   330  C  C   . CYS   A 1 44  ? 32.283  -2.743  13.291  1.00 33.21 ?  44  CYS   A C   1 
ATOM   331  O  O   . CYS   A 1 44  ? 31.510  -2.906  12.344  1.00 37.31 ?  44  CYS   A O   1 
ATOM   332  C  CB  . CYS   A 1 44  ? 31.145  -1.607  15.176  1.00 32.84 ?  44  CYS   A CB  1 
ATOM   333  S  SG  . CYS   A 1 44  ? 30.949  -0.206  16.259  1.00 33.86 ?  44  CYS   A SG  1 
ATOM   334  N  N   . THR   A 1 45  ? 33.182  -3.645  13.664  1.00 36.83 ?  45  THR   A N   1 
ATOM   335  C  CA  . THR   A 1 45  ? 33.031  -5.051  13.336  1.00 38.78 ?  45  THR   A CA  1 
ATOM   336  C  C   . THR   A 1 45  ? 32.017  -5.679  14.289  1.00 37.89 ?  45  THR   A C   1 
ATOM   337  O  O   . THR   A 1 45  ? 31.565  -5.054  15.250  1.00 41.50 ?  45  THR   A O   1 
ATOM   338  C  CB  . THR   A 1 45  ? 34.369  -5.775  13.446  1.00 38.86 ?  45  THR   A CB  1 
ATOM   339  O  OG1 . THR   A 1 45  ? 34.799  -5.758  14.813  1.00 38.82 ?  45  THR   A OG1 1 
ATOM   340  C  CG2 . THR   A 1 45  ? 35.413  -5.083  12.595  1.00 48.20 ?  45  THR   A CG2 1 
ATOM   341  N  N   . SER   A 1 46  ? 31.655  -6.935  14.023  1.00 41.84 ?  46  SER   A N   1 
ATOM   342  C  CA  . SER   A 1 46  ? 30.719  -7.610  14.917  1.00 43.85 ?  46  SER   A CA  1 
ATOM   343  C  C   . SER   A 1 46  ? 31.338  -7.866  16.287  1.00 45.45 ?  46  SER   A C   1 
ATOM   344  O  O   . SER   A 1 46  ? 30.624  -7.872  17.298  1.00 41.60 ?  46  SER   A O   1 
ATOM   345  C  CB  . SER   A 1 46  ? 30.238  -8.913  14.284  1.00 46.38 ?  46  SER   A CB  1 
ATOM   346  O  OG  . SER   A 1 46  ? 31.273  -9.516  13.530  1.00 55.50 ?  46  SER   A OG  1 
ATOM   347  N  N   . GLU   A 1 47  ? 32.660  -8.057  16.346  1.00 45.32 ?  47  GLU   A N   1 
ATOM   348  C  CA  . GLU   A 1 47  ? 33.325  -8.247  17.630  1.00 44.69 ?  47  GLU   A CA  1 
ATOM   349  C  C   . GLU   A 1 47  ? 33.242  -6.995  18.498  1.00 41.62 ?  47  GLU   A C   1 
ATOM   350  O  O   . GLU   A 1 47  ? 33.197  -7.097  19.729  1.00 50.92 ?  47  GLU   A O   1 
ATOM   351  C  CB  . GLU   A 1 47  ? 34.782  -8.651  17.403  1.00 44.87 ?  47  GLU   A CB  1 
ATOM   352  N  N   . ASP   A 1 48  ? 33.196  -5.813  17.877  1.00 38.12 ?  48  ASP   A N   1 
ATOM   353  C  CA  . ASP   A 1 48  ? 33.145  -4.552  18.608  1.00 36.57 ?  48  ASP   A CA  1 
ATOM   354  C  C   . ASP   A 1 48  ? 31.792  -4.277  19.248  1.00 37.16 ?  48  ASP   A C   1 
ATOM   355  O  O   . ASP   A 1 48  ? 31.702  -3.387  20.098  1.00 36.49 ?  48  ASP   A O   1 
ATOM   356  C  CB  . ASP   A 1 48  ? 33.479  -3.392  17.669  1.00 35.66 ?  48  ASP   A CB  1 
ATOM   357  C  CG  . ASP   A 1 48  ? 34.880  -3.476  17.114  1.00 42.44 ?  48  ASP   A CG  1 
ATOM   358  O  OD1 . ASP   A 1 48  ? 35.798  -3.796  17.897  1.00 40.45 ?  48  ASP   A OD1 1 
ATOM   359  O  OD2 . ASP   A 1 48  ? 35.063  -3.225  15.902  1.00 33.70 ?  48  ASP   A OD2 1 
ATOM   360  N  N   . MET   A 1 49  ? 30.747  -5.011  18.870  1.00 34.72 ?  49  MET   A N   1 
ATOM   361  C  CA  . MET   A 1 49  ? 29.387  -4.571  19.144  1.00 30.81 ?  49  MET   A CA  1 
ATOM   362  C  C   . MET   A 1 49  ? 28.922  -4.820  20.575  1.00 32.93 ?  49  MET   A C   1 
ATOM   363  O  O   . MET   A 1 49  ? 27.940  -4.203  20.999  1.00 34.53 ?  49  MET   A O   1 
ATOM   364  C  CB  . MET   A 1 49  ? 28.434  -5.242  18.158  1.00 41.73 ?  49  MET   A CB  1 
ATOM   365  C  CG  . MET   A 1 49  ? 28.584  -4.693  16.760  1.00 33.88 ?  49  MET   A CG  1 
ATOM   366  S  SD  . MET   A 1 49  ? 27.541  -3.272  16.505  1.00 46.78 ?  49  MET   A SD  1 
ATOM   367  C  CE  . MET   A 1 49  ? 28.307  -1.896  17.275  1.00 28.57 ?  49  MET   A CE  1 
ATOM   368  N  N   . LEU   A 1 50  ? 29.590  -5.686  21.335  1.00 32.77 ?  50  LEU   A N   1 
ATOM   369  C  CA  . LEU   A 1 50  ? 29.131  -5.944  22.699  1.00 34.41 ?  50  LEU   A CA  1 
ATOM   370  C  C   . LEU   A 1 50  ? 29.359  -4.736  23.603  1.00 32.28 ?  50  LEU   A C   1 
ATOM   371  O  O   . LEU   A 1 50  ? 28.443  -4.299  24.310  1.00 35.56 ?  50  LEU   A O   1 
ATOM   372  C  CB  . LEU   A 1 50  ? 29.807  -7.195  23.255  1.00 33.30 ?  50  LEU   A CB  1 
ATOM   373  C  CG  . LEU   A 1 50  ? 29.330  -8.460  22.535  1.00 37.88 ?  50  LEU   A CG  1 
ATOM   374  C  CD1 . LEU   A 1 50  ? 30.333  -9.592  22.668  1.00 46.30 ?  50  LEU   A CD1 1 
ATOM   375  C  CD2 . LEU   A 1 50  ? 27.973  -8.892  23.070  1.00 45.34 ?  50  LEU   A CD2 1 
ATOM   376  N  N   . ASN   A 1 51  ? 30.558  -4.159  23.583  1.00 31.49 ?  51  ASN   A N   1 
ATOM   377  C  CA  . ASN   A 1 51  ? 30.875  -2.999  24.421  1.00 28.79 ?  51  ASN   A CA  1 
ATOM   378  C  C   . ASN   A 1 51  ? 31.779  -2.033  23.672  1.00 28.85 ?  51  ASN   A C   1 
ATOM   379  O  O   . ASN   A 1 51  ? 32.925  -1.806  24.062  1.00 27.52 ?  51  ASN   A O   1 
ATOM   380  C  CB  . ASN   A 1 51  ? 31.526  -3.447  25.733  1.00 29.38 ?  51  ASN   A CB  1 
ATOM   381  C  CG  . ASN   A 1 51  ? 30.538  -4.081  26.675  1.00 28.79 ?  51  ASN   A CG  1 
ATOM   382  O  OD1 . ASN   A 1 51  ? 29.700  -3.396  27.260  1.00 29.07 ?  51  ASN   A OD1 1 
ATOM   383  N  ND2 . ASN   A 1 51  ? 30.622  -5.398  26.824  1.00 30.46 ?  51  ASN   A ND2 1 
ATOM   384  N  N   . PRO   A 1 52  ? 31.278  -1.417  22.596  1.00 28.07 ?  52  PRO   A N   1 
ATOM   385  C  CA  . PRO   A 1 52  ? 32.128  -0.522  21.803  1.00 31.17 ?  52  PRO   A CA  1 
ATOM   386  C  C   . PRO   A 1 52  ? 32.350  0.819   22.484  1.00 31.43 ?  52  PRO   A C   1 
ATOM   387  O  O   . PRO   A 1 52  ? 31.445  1.382   23.105  1.00 29.15 ?  52  PRO   A O   1 
ATOM   388  C  CB  . PRO   A 1 52  ? 31.334  -0.348  20.500  1.00 32.76 ?  52  PRO   A CB  1 
ATOM   389  C  CG  . PRO   A 1 52  ? 29.909  -0.482  20.936  1.00 34.34 ?  52  PRO   A CG  1 
ATOM   390  C  CD  . PRO   A 1 52  ? 29.912  -1.509  22.044  1.00 34.28 ?  52  PRO   A CD  1 
ATOM   391  N  N   . ASN   A 1 53  ? 33.580  1.328   22.367  1.00 26.04 ?  53  ASN   A N   1 
ATOM   392  C  CA  . ASN   A 1 53  ? 33.880  2.718   22.702  1.00 28.28 ?  53  ASN   A CA  1 
ATOM   393  C  C   . ASN   A 1 53  ? 34.009  3.455   21.376  1.00 26.54 ?  53  ASN   A C   1 
ATOM   394  O  O   . ASN   A 1 53  ? 35.051  3.397   20.718  1.00 23.30 ?  53  ASN   A O   1 
ATOM   395  C  CB  . ASN   A 1 53  ? 35.146  2.861   23.545  1.00 29.81 ?  53  ASN   A CB  1 
ATOM   396  C  CG  . ASN   A 1 53  ? 35.341  4.283   24.035  1.00 29.33 ?  53  ASN   A CG  1 
ATOM   397  O  OD1 . ASN   A 1 53  ? 35.693  5.170   23.257  1.00 27.21 ?  53  ASN   A OD1 1 
ATOM   398  N  ND2 . ASN   A 1 53  ? 35.079  4.519   25.320  1.00 31.01 ?  53  ASN   A ND2 1 
ATOM   399  N  N   . TYR   A 1 54  ? 32.933  4.135   20.977  1.00 28.02 ?  54  TYR   A N   1 
ATOM   400  C  CA  . TYR   A 1 54  ? 32.901  4.729   19.648  1.00 29.20 ?  54  TYR   A CA  1 
ATOM   401  C  C   . TYR   A 1 54  ? 33.926  5.847   19.499  1.00 29.05 ?  54  TYR   A C   1 
ATOM   402  O  O   . TYR   A 1 54  ? 34.473  6.036   18.405  1.00 27.66 ?  54  TYR   A O   1 
ATOM   403  C  CB  . TYR   A 1 54  ? 31.495  5.238   19.342  1.00 28.32 ?  54  TYR   A CB  1 
ATOM   404  C  CG  . TYR   A 1 54  ? 30.510  4.135   19.033  1.00 27.20 ?  54  TYR   A CG  1 
ATOM   405  C  CD1 . TYR   A 1 54  ? 30.450  3.576   17.763  1.00 28.05 ?  54  TYR   A CD1 1 
ATOM   406  C  CD2 . TYR   A 1 54  ? 29.643  3.647   20.009  1.00 23.71 ?  54  TYR   A CD2 1 
ATOM   407  C  CE1 . TYR   A 1 54  ? 29.549  2.568   17.467  1.00 26.42 ?  54  TYR   A CE1 1 
ATOM   408  C  CE2 . TYR   A 1 54  ? 28.744  2.639   19.724  1.00 28.20 ?  54  TYR   A CE2 1 
ATOM   409  C  CZ  . TYR   A 1 54  ? 28.695  2.105   18.447  1.00 28.25 ?  54  TYR   A CZ  1 
ATOM   410  O  OH  . TYR   A 1 54  ? 27.799  1.103   18.147  1.00 26.48 ?  54  TYR   A OH  1 
ATOM   411  N  N   . GLU   A 1 55  ? 34.192  6.601   20.572  1.00 25.97 ?  55  GLU   A N   1 
ATOM   412  C  CA  . GLU   A 1 55  ? 35.250  7.605   20.517  1.00 32.75 ?  55  GLU   A CA  1 
ATOM   413  C  C   . GLU   A 1 55  ? 36.577  6.960   20.135  1.00 28.90 ?  55  GLU   A C   1 
ATOM   414  O  O   . GLU   A 1 55  ? 37.282  7.428   19.225  1.00 29.04 ?  55  GLU   A O   1 
ATOM   415  C  CB  . GLU   A 1 55  ? 35.360  8.329   21.863  1.00 32.80 ?  55  GLU   A CB  1 
ATOM   416  C  CG  . GLU   A 1 55  ? 36.267  9.558   21.818  1.00 34.41 ?  55  GLU   A CG  1 
ATOM   417  C  CD  . GLU   A 1 55  ? 36.615  10.106  23.205  1.00 45.92 ?  55  GLU   A CD  1 
ATOM   418  O  OE1 . GLU   A 1 55  ? 36.058  9.613   24.214  1.00 39.40 ?  55  GLU   A OE1 1 
ATOM   419  O  OE2 . GLU   A 1 55  ? 37.458  11.030  23.278  1.00 37.89 ?  55  GLU   A OE2 1 
ATOM   420  N  N   . ASP   A 1 56  ? 36.900  5.837   20.783  1.00 27.97 ?  56  ASP   A N   1 
ATOM   421  C  CA  . ASP   A 1 56  ? 38.149  5.134   20.502  1.00 28.54 ?  56  ASP   A CA  1 
ATOM   422  C  C   . ASP   A 1 56  ? 38.150  4.513   19.108  1.00 29.38 ?  56  ASP   A C   1 
ATOM   423  O  O   . ASP   A 1 56  ? 39.185  4.491   18.432  1.00 29.05 ?  56  ASP   A O   1 
ATOM   424  C  CB  . ASP   A 1 56  ? 38.385  4.057   21.560  1.00 29.40 ?  56  ASP   A CB  1 
ATOM   425  C  CG  . ASP   A 1 56  ? 39.808  3.534   21.546  1.00 35.86 ?  56  ASP   A CG  1 
ATOM   426  O  OD1 . ASP   A 1 56  ? 40.708  4.275   21.992  1.00 33.72 ?  56  ASP   A OD1 1 
ATOM   427  O  OD2 . ASP   A 1 56  ? 40.028  2.392   21.087  1.00 31.48 ?  56  ASP   A OD2 1 
ATOM   428  N  N   . LEU   A 1 57  ? 37.010  3.982   18.664  1.00 25.89 ?  57  LEU   A N   1 
ATOM   429  C  CA  . LEU   A 1 57  ? 36.976  3.354   17.349  1.00 28.47 ?  57  LEU   A CA  1 
ATOM   430  C  C   . LEU   A 1 57  ? 37.108  4.392   16.242  1.00 26.93 ?  57  LEU   A C   1 
ATOM   431  O  O   . LEU   A 1 57  ? 37.790  4.151   15.238  1.00 28.12 ?  57  LEU   A O   1 
ATOM   432  C  CB  . LEU   A 1 57  ? 35.689  2.545   17.185  1.00 31.52 ?  57  LEU   A CB  1 
ATOM   433  C  CG  . LEU   A 1 57  ? 35.608  1.273   18.031  1.00 33.86 ?  57  LEU   A CG  1 
ATOM   434  C  CD1 . LEU   A 1 57  ? 34.184  0.701   18.020  1.00 32.62 ?  57  LEU   A CD1 1 
ATOM   435  C  CD2 . LEU   A 1 57  ? 36.622  0.244   17.530  1.00 34.35 ?  57  LEU   A CD2 1 
ATOM   436  N  N   . LEU   A 1 58  ? 36.482  5.562   16.415  1.00 25.95 ?  58  LEU   A N   1 
ATOM   437  C  CA  . LEU   A 1 58  ? 36.485  6.561   15.348  1.00 28.34 ?  58  LEU   A CA  1 
ATOM   438  C  C   . LEU   A 1 58  ? 37.847  7.230   15.211  1.00 28.64 ?  58  LEU   A C   1 
ATOM   439  O  O   . LEU   A 1 58  ? 38.278  7.554   14.095  1.00 29.13 ?  58  LEU   A O   1 
ATOM   440  C  CB  . LEU   A 1 58  ? 35.403  7.610   15.601  1.00 25.26 ?  58  LEU   A CB  1 
ATOM   441  C  CG  . LEU   A 1 58  ? 35.132  8.592   14.455  1.00 27.31 ?  58  LEU   A CG  1 
ATOM   442  C  CD1 . LEU   A 1 58  ? 34.768  7.852   13.178  1.00 25.65 ?  58  LEU   A CD1 1 
ATOM   443  C  CD2 . LEU   A 1 58  ? 34.022  9.545   14.853  1.00 34.12 ?  58  LEU   A CD2 1 
ATOM   444  N  N   . ILE   A 1 59  ? 38.534  7.452   16.335  1.00 27.08 ?  59  ILE   A N   1 
ATOM   445  C  CA  . ILE   A 1 59  ? 39.840  8.102   16.304  1.00 27.80 ?  59  ILE   A CA  1 
ATOM   446  C  C   . ILE   A 1 59  ? 40.826  7.295   15.469  1.00 24.22 ?  59  ILE   A C   1 
ATOM   447  O  O   . ILE   A 1 59  ? 41.747  7.858   14.860  1.00 26.56 ?  59  ILE   A O   1 
ATOM   448  C  CB  . ILE   A 1 59  ? 40.337  8.320   17.752  1.00 30.95 ?  59  ILE   A CB  1 
ATOM   449  C  CG1 . ILE   A 1 59  ? 41.062  9.660   17.880  1.00 36.59 ?  59  ILE   A CG1 1 
ATOM   450  C  CG2 . ILE   A 1 59  ? 41.242  7.177   18.206  1.00 28.44 ?  59  ILE   A CG2 1 
ATOM   451  C  CD1 . ILE   A 1 59  ? 41.283  10.088  19.332  1.00 37.61 ?  59  ILE   A CD1 1 
ATOM   452  N  N   . ARG   A 1 60  ? 40.640  5.975   15.403  1.00 27.51 ?  60  ARG   A N   1 
ATOM   453  C  CA  . ARG   A 1 60  ? 41.478  5.090   14.601  1.00 27.96 ?  60  ARG   A CA  1 
ATOM   454  C  C   . ARG   A 1 60  ? 41.115  5.103   13.119  1.00 25.83 ?  60  ARG   A C   1 
ATOM   455  O  O   . ARG   A 1 60  ? 41.804  4.449   12.322  1.00 24.12 ?  60  ARG   A O   1 
ATOM   456  C  CB  . ARG   A 1 60  ? 41.383  3.661   15.147  1.00 24.80 ?  60  ARG   A CB  1 
ATOM   457  C  CG  . ARG   A 1 60  ? 41.683  3.561   16.650  1.00 24.22 ?  60  ARG   A CG  1 
ATOM   458  C  CD  . ARG   A 1 60  ? 41.571  2.131   17.144  1.00 21.76 ?  60  ARG   A CD  1 
ATOM   459  N  NE  . ARG   A 1 60  ? 41.658  2.041   18.603  1.00 23.17 ?  60  ARG   A NE  1 
ATOM   460  C  CZ  . ARG   A 1 60  ? 42.771  1.730   19.261  1.00 29.58 ?  60  ARG   A CZ  1 
ATOM   461  N  NH1 . ARG   A 1 60  ? 43.894  1.473   18.592  1.00 28.70 ?  60  ARG   A NH1 1 
ATOM   462  N  NH2 . ARG   A 1 60  ? 42.765  1.669   20.585  1.00 30.17 ?  60  ARG   A NH2 1 
ATOM   463  N  N   . LYS   A 1 61  ? 40.070  5.825   12.727  1.00 27.34 ?  61  LYS   A N   1 
ATOM   464  C  CA  . LYS   A 1 61  ? 39.669  5.911   11.328  1.00 27.64 ?  61  LYS   A CA  1 
ATOM   465  C  C   . LYS   A 1 61  ? 40.187  7.198   10.697  1.00 28.94 ?  61  LYS   A C   1 
ATOM   466  O  O   . LYS   A 1 61  ? 40.381  8.211   11.374  1.00 30.49 ?  61  LYS   A O   1 
ATOM   467  C  CB  . LYS   A 1 61  ? 38.140  5.852   11.176  1.00 28.11 ?  61  LYS   A CB  1 
ATOM   468  C  CG  . LYS   A 1 61  ? 37.514  4.509   11.518  1.00 29.23 ?  61  LYS   A CG  1 
ATOM   469  C  CD  . LYS   A 1 61  ? 38.251  3.394   10.818  1.00 33.82 ?  61  LYS   A CD  1 
ATOM   470  C  CE  . LYS   A 1 61  ? 37.470  2.101   10.828  1.00 33.34 ?  61  LYS   A CE  1 
ATOM   471  N  NZ  . LYS   A 1 61  ? 37.010  1.737   12.179  1.00 37.85 ?  61  LYS   A NZ  1 
ATOM   472  N  N   . SER   A 1 62  ? 40.399  7.140   9.380   1.00 33.03 ?  62  SER   A N   1 
ATOM   473  C  CA  . SER   A 1 62  ? 40.697  8.286   8.534   1.00 33.02 ?  62  SER   A CA  1 
ATOM   474  C  C   . SER   A 1 62  ? 39.546  8.512   7.560   1.00 30.49 ?  62  SER   A C   1 
ATOM   475  O  O   . SER   A 1 62  ? 38.685  7.648   7.368   1.00 29.41 ?  62  SER   A O   1 
ATOM   476  C  CB  . SER   A 1 62  ? 42.000  8.076   7.752   1.00 34.78 ?  62  SER   A CB  1 
ATOM   477  O  OG  . SER   A 1 62  ? 43.094  7.838   8.632   1.00 38.67 ?  62  SER   A OG  1 
ATOM   478  N  N   . ASN   A 1 63  ? 39.558  9.694   6.936   1.00 29.21 ?  63  ASN   A N   1 
ATOM   479  C  CA  . ASN   A 1 63  ? 38.557  10.026  5.925   1.00 31.50 ?  63  ASN   A CA  1 
ATOM   480  C  C   . ASN   A 1 63  ? 38.485  8.961   4.840   1.00 29.57 ?  63  ASN   A C   1 
ATOM   481  O  O   . ASN   A 1 63  ? 37.403  8.653   4.330   1.00 30.41 ?  63  ASN   A O   1 
ATOM   482  C  CB  . ASN   A 1 63  ? 38.876  11.380  5.287   1.00 28.73 ?  63  ASN   A CB  1 
ATOM   483  C  CG  . ASN   A 1 63  ? 38.604  12.543  6.204   1.00 31.40 ?  63  ASN   A CG  1 
ATOM   484  O  OD1 . ASN   A 1 63  ? 37.813  12.445  7.146   1.00 32.32 ?  63  ASN   A OD1 1 
ATOM   485  N  ND2 . ASN   A 1 63  ? 39.241  13.669  5.919   1.00 28.00 ?  63  ASN   A ND2 1 
ATOM   486  N  N   . HIS   A 1 64  ? 39.625  8.390   4.467   1.00 27.08 ?  64  HIS   A N   1 
ATOM   487  C  CA  . HIS   A 1 64  ? 39.656  7.479   3.329   1.00 31.80 ?  64  HIS   A CA  1 
ATOM   488  C  C   . HIS   A 1 64  ? 39.287  6.048   3.696   1.00 34.23 ?  64  HIS   A C   1 
ATOM   489  O  O   . HIS   A 1 64  ? 39.229  5.192   2.806   1.00 28.68 ?  64  HIS   A O   1 
ATOM   490  C  CB  . HIS   A 1 64  ? 41.031  7.520   2.657   1.00 32.74 ?  64  HIS   A CB  1 
ATOM   491  C  CG  . HIS   A 1 64  ? 42.168  7.196   3.573   1.00 38.10 ?  64  HIS   A CG  1 
ATOM   492  N  ND1 . HIS   A 1 64  ? 42.632  5.911   3.758   1.00 40.28 ?  64  HIS   A ND1 1 
ATOM   493  C  CD2 . HIS   A 1 64  ? 42.943  7.992   4.345   1.00 33.41 ?  64  HIS   A CD2 1 
ATOM   494  C  CE1 . HIS   A 1 64  ? 43.643  5.929   4.607   1.00 37.75 ?  64  HIS   A CE1 1 
ATOM   495  N  NE2 . HIS   A 1 64  ? 43.855  7.179   4.975   1.00 40.37 ?  64  HIS   A NE2 1 
ATOM   496  N  N   . ASN   A 1 65  ? 39.028  5.770   4.976   1.00 28.19 ?  65  ASN   A N   1 
ATOM   497  C  CA  . ASN   A 1 65  ? 38.413  4.512   5.382   1.00 29.24 ?  65  ASN   A CA  1 
ATOM   498  C  C   . ASN   A 1 65  ? 36.916  4.455   5.070   1.00 32.28 ?  65  ASN   A C   1 
ATOM   499  O  O   . ASN   A 1 65  ? 36.318  3.379   5.179   1.00 31.82 ?  65  ASN   A O   1 
ATOM   500  C  CB  . ASN   A 1 65  ? 38.609  4.289   6.891   1.00 29.84 ?  65  ASN   A CB  1 
ATOM   501  C  CG  . ASN   A 1 65  ? 40.074  4.131   7.283   1.00 38.48 ?  65  ASN   A CG  1 
ATOM   502  O  OD1 . ASN   A 1 65  ? 40.515  4.644   8.314   1.00 32.54 ?  65  ASN   A OD1 1 
ATOM   503  N  ND2 . ASN   A 1 65  ? 40.830  3.416   6.462   1.00 31.00 ?  65  ASN   A ND2 1 
ATOM   504  N  N   . PHE   A 1 66  ? 36.294  5.577   4.720   1.00 30.30 ?  66  PHE   A N   1 
ATOM   505  C  CA  . PHE   A 1 66  ? 34.875  5.624   4.383   1.00 28.76 ?  66  PHE   A CA  1 
ATOM   506  C  C   . PHE   A 1 66  ? 34.714  5.782   2.879   1.00 33.64 ?  66  PHE   A C   1 
ATOM   507  O  O   . PHE   A 1 66  ? 35.260  6.719   2.287   1.00 30.69 ?  66  PHE   A O   1 
ATOM   508  C  CB  . PHE   A 1 66  ? 34.173  6.784   5.095   1.00 25.03 ?  66  PHE   A CB  1 
ATOM   509  C  CG  . PHE   A 1 66  ? 34.237  6.712   6.594   1.00 28.27 ?  66  PHE   A CG  1 
ATOM   510  C  CD1 . PHE   A 1 66  ? 33.290  6.001   7.304   1.00 26.22 ?  66  PHE   A CD1 1 
ATOM   511  C  CD2 . PHE   A 1 66  ? 35.242  7.367   7.293   1.00 32.91 ?  66  PHE   A CD2 1 
ATOM   512  C  CE1 . PHE   A 1 66  ? 33.341  5.934   8.698   1.00 31.91 ?  66  PHE   A CE1 1 
ATOM   513  C  CE2 . PHE   A 1 66  ? 35.311  7.305   8.676   1.00 30.03 ?  66  PHE   A CE2 1 
ATOM   514  C  CZ  . PHE   A 1 66  ? 34.348  6.589   9.385   1.00 35.54 ?  66  PHE   A CZ  1 
ATOM   515  N  N   . LEU   A 1 67  ? 33.968  4.870   2.266   1.00 32.52 ?  67  LEU   A N   1 
ATOM   516  C  CA  . LEU   A 1 67  ? 33.597  4.964   0.862   1.00 32.13 ?  67  LEU   A CA  1 
ATOM   517  C  C   . LEU   A 1 67  ? 32.113  5.294   0.805   1.00 35.31 ?  67  LEU   A C   1 
ATOM   518  O  O   . LEU   A 1 67  ? 31.287  4.527   1.312   1.00 33.62 ?  67  LEU   A O   1 
ATOM   519  C  CB  . LEU   A 1 67  ? 33.894  3.660   0.123   1.00 34.26 ?  67  LEU   A CB  1 
ATOM   520  C  CG  . LEU   A 1 67  ? 35.245  2.979   0.377   1.00 47.90 ?  67  LEU   A CG  1 
ATOM   521  C  CD1 . LEU   A 1 67  ? 35.409  1.783   -0.554  1.00 46.29 ?  67  LEU   A CD1 1 
ATOM   522  C  CD2 . LEU   A 1 67  ? 36.413  3.957   0.227   1.00 46.61 ?  67  LEU   A CD2 1 
ATOM   523  N  N   . VAL   A 1 68  ? 31.782  6.446   0.230   1.00 30.43 ?  68  VAL   A N   1 
ATOM   524  C  CA  . VAL   A 1 68  ? 30.403  6.889   0.072   1.00 32.26 ?  68  VAL   A CA  1 
ATOM   525  C  C   . VAL   A 1 68  ? 30.069  6.880   -1.412  1.00 31.48 ?  68  VAL   A C   1 
ATOM   526  O  O   . VAL   A 1 68  ? 30.786  7.486   -2.218  1.00 38.02 ?  68  VAL   A O   1 
ATOM   527  C  CB  . VAL   A 1 68  ? 30.184  8.284   0.682   1.00 32.66 ?  68  VAL   A CB  1 
ATOM   528  C  CG1 . VAL   A 1 68  ? 28.788  8.784   0.366   1.00 32.22 ?  68  VAL   A CG1 1 
ATOM   529  C  CG2 . VAL   A 1 68  ? 30.400  8.239   2.184   1.00 31.46 ?  68  VAL   A CG2 1 
ATOM   530  N  N   . GLN   A 1 69  ? 28.987  6.194   -1.772  1.00 32.01 ?  69  GLN   A N   1 
ATOM   531  C  CA  . GLN   A 1 69  ? 28.586  6.015   -3.164  1.00 30.10 ?  69  GLN   A CA  1 
ATOM   532  C  C   . GLN   A 1 69  ? 27.193  6.584   -3.383  1.00 34.69 ?  69  GLN   A C   1 
ATOM   533  O  O   . GLN   A 1 69  ? 26.256  6.246   -2.650  1.00 29.53 ?  69  GLN   A O   1 
ATOM   534  C  CB  . GLN   A 1 69  ? 28.590  4.538   -3.552  1.00 34.33 ?  69  GLN   A CB  1 
ATOM   535  C  CG  . GLN   A 1 69  ? 29.953  3.925   -3.742  1.00 47.44 ?  69  GLN   A CG  1 
ATOM   536  C  CD  . GLN   A 1 69  ? 30.038  3.151   -5.042  1.00 54.11 ?  69  GLN   A CD  1 
ATOM   537  O  OE1 . GLN   A 1 69  ? 29.855  1.932   -5.066  1.00 57.44 ?  69  GLN   A OE1 1 
ATOM   538  N  NE2 . GLN   A 1 69  ? 30.301  3.860   -6.137  1.00 55.89 ?  69  GLN   A NE2 1 
ATOM   539  N  N   . ALA   A 1 70  ? 27.051  7.424   -4.406  1.00 32.33 ?  70  ALA   A N   1 
ATOM   540  C  CA  . ALA   A 1 70  ? 25.763  7.981   -4.809  1.00 28.79 ?  70  ALA   A CA  1 
ATOM   541  C  C   . ALA   A 1 70  ? 25.551  7.573   -6.259  1.00 38.67 ?  70  ALA   A C   1 
ATOM   542  O  O   . ALA   A 1 70  ? 26.149  8.165   -7.162  1.00 35.04 ?  70  ALA   A O   1 
ATOM   543  C  CB  . ALA   A 1 70  ? 25.731  9.499   -4.647  1.00 27.35 ?  70  ALA   A CB  1 
ATOM   544  N  N   . GLY   A 1 71  ? 24.712  6.568   -6.477  1.00 38.19 ?  71  GLY   A N   1 
ATOM   545  C  CA  . GLY   A 1 71  ? 24.563  6.021   -7.816  1.00 46.48 ?  71  GLY   A CA  1 
ATOM   546  C  C   . GLY   A 1 71  ? 25.863  5.375   -8.250  1.00 49.30 ?  71  GLY   A C   1 
ATOM   547  O  O   . GLY   A 1 71  ? 26.402  4.491   -7.573  1.00 52.25 ?  71  GLY   A O   1 
ATOM   548  N  N   . ASN   A 1 72  ? 26.395  5.823   -9.384  1.00 50.43 ?  72  ASN   A N   1 
ATOM   549  C  CA  . ASN   A 1 72  ? 27.673  5.341   -9.884  1.00 47.81 ?  72  ASN   A CA  1 
ATOM   550  C  C   . ASN   A 1 72  ? 28.830  6.242   -9.481  1.00 52.12 ?  72  ASN   A C   1 
ATOM   551  O  O   . ASN   A 1 72  ? 29.961  6.011   -9.919  1.00 55.25 ?  72  ASN   A O   1 
ATOM   552  C  CB  . ASN   A 1 72  ? 27.625  5.206   -11.408 1.00 51.20 ?  72  ASN   A CB  1 
ATOM   553  N  N   . VAL   A 1 73  ? 28.581  7.252   -8.650  1.00 48.33 ?  73  VAL   A N   1 
ATOM   554  C  CA  . VAL   A 1 73  ? 29.574  8.268   -8.317  1.00 42.80 ?  73  VAL   A CA  1 
ATOM   555  C  C   . VAL   A 1 73  ? 30.058  8.049   -6.891  1.00 48.55 ?  73  VAL   A C   1 
ATOM   556  O  O   . VAL   A 1 73  ? 29.249  7.855   -5.973  1.00 38.81 ?  73  VAL   A O   1 
ATOM   557  C  CB  . VAL   A 1 73  ? 29.000  9.684   -8.486  1.00 44.24 ?  73  VAL   A CB  1 
ATOM   558  C  CG1 . VAL   A 1 73  ? 30.080  10.717  -8.259  1.00 46.28 ?  73  VAL   A CG1 1 
ATOM   559  C  CG2 . VAL   A 1 73  ? 28.394  9.840   -9.868  1.00 45.09 ?  73  VAL   A CG2 1 
ATOM   560  N  N   . GLN   A 1 74  ? 31.380  8.086   -6.710  1.00 42.35 ?  74  GLN   A N   1 
ATOM   561  C  CA  . GLN   A 1 74  ? 32.001  8.067   -5.394  1.00 42.21 ?  74  GLN   A CA  1 
ATOM   562  C  C   . GLN   A 1 74  ? 32.185  9.502   -4.916  1.00 41.40 ?  74  GLN   A C   1 
ATOM   563  O  O   . GLN   A 1 74  ? 32.642  10.360  -5.679  1.00 41.55 ?  74  GLN   A O   1 
ATOM   564  C  CB  . GLN   A 1 74  ? 33.348  7.341   -5.439  1.00 34.97 ?  74  GLN   A CB  1 
ATOM   565  N  N   . LEU   A 1 75  ? 31.805  9.761   -3.666  1.00 34.29 ?  75  LEU   A N   1 
ATOM   566  C  CA  . LEU   A 1 75  ? 31.961  11.068  -3.038  1.00 33.22 ?  75  LEU   A CA  1 
ATOM   567  C  C   . LEU   A 1 75  ? 33.179  11.048  -2.127  1.00 36.45 ?  75  LEU   A C   1 
ATOM   568  O  O   . LEU   A 1 75  ? 33.290  10.181  -1.251  1.00 38.05 ?  75  LEU   A O   1 
ATOM   569  C  CB  . LEU   A 1 75  ? 30.716  11.448  -2.233  1.00 29.36 ?  75  LEU   A CB  1 
ATOM   570  C  CG  . LEU   A 1 75  ? 29.435  11.599  -3.053  1.00 39.79 ?  75  LEU   A CG  1 
ATOM   571  C  CD1 . LEU   A 1 75  ? 28.204  11.442  -2.166  1.00 37.74 ?  75  LEU   A CD1 1 
ATOM   572  C  CD2 . LEU   A 1 75  ? 29.415  12.946  -3.774  1.00 40.31 ?  75  LEU   A CD2 1 
ATOM   573  N  N   . ARG   A 1 76  ? 34.084  12.002  -2.326  1.00 30.73 ?  76  ARG   A N   1 
ATOM   574  C  CA  . ARG   A 1 76  ? 35.284  12.069  -1.504  1.00 27.89 ?  76  ARG   A CA  1 
ATOM   575  C  C   . ARG   A 1 76  ? 34.924  12.565  -0.110  1.00 27.72 ?  76  ARG   A C   1 
ATOM   576  O  O   . ARG   A 1 76  ? 34.391  13.669  0.046   1.00 28.02 ?  76  ARG   A O   1 
ATOM   577  C  CB  . ARG   A 1 76  ? 36.323  12.986  -2.141  1.00 27.42 ?  76  ARG   A CB  1 
ATOM   578  N  N   . VAL   A 1 77  ? 35.221  11.751  0.899   1.00 28.60 ?  77  VAL   A N   1 
ATOM   579  C  CA  . VAL   A 1 77  ? 35.025  12.142  2.291   1.00 29.70 ?  77  VAL   A CA  1 
ATOM   580  C  C   . VAL   A 1 77  ? 36.192  13.024  2.717   1.00 31.13 ?  77  VAL   A C   1 
ATOM   581  O  O   . VAL   A 1 77  ? 37.359  12.621  2.632   1.00 28.42 ?  77  VAL   A O   1 
ATOM   582  C  CB  . VAL   A 1 77  ? 34.889  10.910  3.198   1.00 31.26 ?  77  VAL   A CB  1 
ATOM   583  C  CG1 . VAL   A 1 77  ? 34.900  11.317  4.658   1.00 28.75 ?  77  VAL   A CG1 1 
ATOM   584  C  CG2 . VAL   A 1 77  ? 33.592  10.155  2.863   1.00 28.69 ?  77  VAL   A CG2 1 
ATOM   585  N  N   . ILE   A 1 78  ? 35.884  14.242  3.155   1.00 29.99 ?  78  ILE   A N   1 
ATOM   586  C  CA  . ILE   A 1 78  ? 36.911  15.192  3.556   1.00 30.98 ?  78  ILE   A CA  1 
ATOM   587  C  C   . ILE   A 1 78  ? 36.878  15.493  5.046   1.00 32.56 ?  78  ILE   A C   1 
ATOM   588  O  O   . ILE   A 1 78  ? 37.710  16.277  5.523   1.00 31.58 ?  78  ILE   A O   1 
ATOM   589  C  CB  . ILE   A 1 78  ? 36.818  16.495  2.736   1.00 30.81 ?  78  ILE   A CB  1 
ATOM   590  C  CG1 . ILE   A 1 78  ? 35.452  17.151  2.920   1.00 31.48 ?  78  ILE   A CG1 1 
ATOM   591  C  CG2 . ILE   A 1 78  ? 37.087  16.215  1.251   1.00 30.67 ?  78  ILE   A CG2 1 
ATOM   592  C  CD1 . ILE   A 1 78  ? 35.340  18.521  2.285   1.00 33.94 ?  78  ILE   A CD1 1 
ATOM   593  N  N   . GLY   A 1 79  ? 35.956  14.894  5.800   1.00 29.25 ?  79  GLY   A N   1 
ATOM   594  C  CA  . GLY   A 1 79  ? 35.911  15.112  7.237   1.00 29.91 ?  79  GLY   A CA  1 
ATOM   595  C  C   . GLY   A 1 79  ? 34.905  14.189  7.886   1.00 28.54 ?  79  GLY   A C   1 
ATOM   596  O  O   . GLY   A 1 79  ? 33.983  13.690  7.237   1.00 29.13 ?  79  GLY   A O   1 
ATOM   597  N  N   . HIS   A 1 80  ? 35.098  13.955  9.180   1.00 30.94 ?  80  HIS   A N   1 
ATOM   598  C  CA  . HIS   A 1 80  ? 34.199  13.059  9.893   1.00 28.24 ?  80  HIS   A CA  1 
ATOM   599  C  C   . HIS   A 1 80  ? 34.168  13.438  11.362  1.00 34.07 ?  80  HIS   A C   1 
ATOM   600  O  O   . HIS   A 1 80  ? 35.195  13.797  11.941  1.00 29.93 ?  80  HIS   A O   1 
ATOM   601  C  CB  . HIS   A 1 80  ? 34.614  11.591  9.743   1.00 26.91 ?  80  HIS   A CB  1 
ATOM   602  C  CG  . HIS   A 1 80  ? 35.986  11.295  10.267  1.00 35.37 ?  80  HIS   A CG  1 
ATOM   603  N  ND1 . HIS   A 1 80  ? 37.102  11.268  9.457   1.00 31.13 ?  80  HIS   A ND1 1 
ATOM   604  C  CD2 . HIS   A 1 80  ? 36.422  11.025  11.520  1.00 30.68 ?  80  HIS   A CD2 1 
ATOM   605  C  CE1 . HIS   A 1 80  ? 38.167  10.992  10.190  1.00 34.56 ?  80  HIS   A CE1 1 
ATOM   606  N  NE2 . HIS   A 1 80  ? 37.781  10.841  11.445  1.00 32.06 ?  80  HIS   A NE2 1 
ATOM   607  N  N   . SER   A 1 81  ? 32.980  13.353  11.949  1.00 30.74 ?  81  SER   A N   1 
ATOM   608  C  CA  . SER   A 1 81  ? 32.793  13.596  13.367  1.00 33.85 ?  81  SER   A CA  1 
ATOM   609  C  C   . SER   A 1 81  ? 31.562  12.827  13.809  1.00 33.41 ?  81  SER   A C   1 
ATOM   610  O  O   . SER   A 1 81  ? 30.744  12.394  12.989  1.00 27.97 ?  81  SER   A O   1 
ATOM   611  C  CB  . SER   A 1 81  ? 32.640  15.089  13.680  1.00 36.37 ?  81  SER   A CB  1 
ATOM   612  O  OG  . SER   A 1 81  ? 31.452  15.613  13.104  1.00 32.36 ?  81  SER   A OG  1 
ATOM   613  N  N   . MET   A 1 82  ? 31.443  12.665  15.116  1.00 30.82 ?  82  MET   A N   1 
ATOM   614  C  CA  . MET   A 1 82  ? 30.332  11.958  15.725  1.00 31.23 ?  82  MET   A CA  1 
ATOM   615  C  C   . MET   A 1 82  ? 29.437  12.965  16.439  1.00 30.05 ?  82  MET   A C   1 
ATOM   616  O  O   . MET   A 1 82  ? 29.923  13.936  17.024  1.00 30.10 ?  82  MET   A O   1 
ATOM   617  C  CB  . MET   A 1 82  ? 30.871  10.902  16.693  1.00 38.38 ?  82  MET   A CB  1 
ATOM   618  C  CG  . MET   A 1 82  ? 29.876  9.910   17.249  1.00 36.26 ?  82  MET   A CG  1 
ATOM   619  S  SD  . MET   A 1 82  ? 30.752  8.474   17.926  1.00 36.52 ?  82  MET   A SD  1 
ATOM   620  C  CE  . MET   A 1 82  ? 31.924  9.263   19.027  1.00 36.37 ?  82  MET   A CE  1 
ATOM   621  N  N   . GLN   A 1 83  ? 28.127  12.763  16.357  1.00 30.51 ?  83  GLN   A N   1 
ATOM   622  C  CA  . GLN   A 1 83  ? 27.189  13.486  17.206  1.00 29.01 ?  83  GLN   A CA  1 
ATOM   623  C  C   . GLN   A 1 83  ? 26.243  12.453  17.787  1.00 32.21 ?  83  GLN   A C   1 
ATOM   624  O  O   . GLN   A 1 83  ? 25.386  11.925  17.069  1.00 26.91 ?  83  GLN   A O   1 
ATOM   625  C  CB  . GLN   A 1 83  ? 26.416  14.566  16.454  1.00 30.71 ?  83  GLN   A CB  1 
ATOM   626  C  CG  . GLN   A 1 83  ? 25.410  15.258  17.372  1.00 31.04 ?  83  GLN   A CG  1 
ATOM   627  C  CD  . GLN   A 1 83  ? 24.667  16.402  16.712  1.00 44.06 ?  83  GLN   A CD  1 
ATOM   628  O  OE1 . GLN   A 1 83  ? 24.657  16.532  15.490  1.00 37.01 ?  83  GLN   A OE1 1 
ATOM   629  N  NE2 . GLN   A 1 83  ? 24.036  17.244  17.530  1.00 44.97 ?  83  GLN   A NE2 1 
ATOM   630  N  N   . ASN   A 1 84  ? 26.410  12.165  19.079  1.00 25.84 ?  84  ASN   A N   1 
ATOM   631  C  CA  . ASN   A 1 84  ? 25.649  11.113  19.734  1.00 28.81 ?  84  ASN   A CA  1 
ATOM   632  C  C   . ASN   A 1 84  ? 25.806  9.830   18.927  1.00 25.61 ?  84  ASN   A C   1 
ATOM   633  O  O   . ASN   A 1 84  ? 26.937  9.405   18.672  1.00 26.16 ?  84  ASN   A O   1 
ATOM   634  C  CB  . ASN   A 1 84  ? 24.191  11.551  19.899  1.00 28.30 ?  84  ASN   A CB  1 
ATOM   635  C  CG  . ASN   A 1 84  ? 24.074  12.852  20.674  1.00 29.83 ?  84  ASN   A CG  1 
ATOM   636  O  OD1 . ASN   A 1 84  ? 24.622  12.978  21.765  1.00 30.43 ?  84  ASN   A OD1 1 
ATOM   637  N  ND2 . ASN   A 1 84  ? 23.399  13.836  20.097  1.00 30.46 ?  84  ASN   A ND2 1 
ATOM   638  N  N   . CYS   A 1 85  ? 24.712  9.223   18.472  1.00 23.94 ?  85  CYS   A N   1 
ATOM   639  C  CA  . CYS   A 1 85  ? 24.814  7.932   17.809  1.00 22.63 ?  85  CYS   A CA  1 
ATOM   640  C  C   . CYS   A 1 85  ? 24.840  8.030   16.291  1.00 22.49 ?  85  CYS   A C   1 
ATOM   641  O  O   . CYS   A 1 85  ? 24.735  6.998   15.617  1.00 21.25 ?  85  CYS   A O   1 
ATOM   642  C  CB  . CYS   A 1 85  ? 23.679  7.020   18.245  1.00 23.18 ?  85  CYS   A CB  1 
ATOM   643  S  SG  . CYS   A 1 85  ? 23.700  6.737   20.022  1.00 27.45 ?  85  CYS   A SG  1 
ATOM   644  N  N   . VAL   A 1 86  ? 24.975  9.228   15.731  1.00 23.85 ?  86  VAL   A N   1 
ATOM   645  C  CA  . VAL   A 1 86  ? 25.083  9.375   14.285  1.00 22.57 ?  86  VAL   A CA  1 
ATOM   646  C  C   . VAL   A 1 86  ? 26.483  9.857   13.931  1.00 24.19 ?  86  VAL   A C   1 
ATOM   647  O  O   . VAL   A 1 86  ? 27.132  10.595  14.690  1.00 26.10 ?  86  VAL   A O   1 
ATOM   648  C  CB  . VAL   A 1 86  ? 24.007  10.308  13.685  1.00 27.91 ?  86  VAL   A CB  1 
ATOM   649  C  CG1 . VAL   A 1 86  ? 22.614  9.668   13.780  1.00 26.10 ?  86  VAL   A CG1 1 
ATOM   650  C  CG2 . VAL   A 1 86  ? 24.020  11.663  14.352  1.00 30.77 ?  86  VAL   A CG2 1 
ATOM   651  N  N   . LEU   A 1 87  ? 26.962  9.383   12.798  1.00 24.68 ?  87  LEU   A N   1 
ATOM   652  C  CA  . LEU   A 1 87  ? 28.230  9.801   12.231  1.00 24.06 ?  87  LEU   A CA  1 
ATOM   653  C  C   . LEU   A 1 87  ? 27.949  10.810  11.128  1.00 29.11 ?  87  LEU   A C   1 
ATOM   654  O  O   . LEU   A 1 87  ? 27.020  10.626  10.332  1.00 26.50 ?  87  LEU   A O   1 
ATOM   655  C  CB  . LEU   A 1 87  ? 28.972  8.585   11.685  1.00 28.80 ?  87  LEU   A CB  1 
ATOM   656  C  CG  . LEU   A 1 87  ? 30.351  8.744   11.067  1.00 29.97 ?  87  LEU   A CG  1 
ATOM   657  C  CD1 . LEU   A 1 87  ? 31.374  9.143   12.119  1.00 36.36 ?  87  LEU   A CD1 1 
ATOM   658  C  CD2 . LEU   A 1 87  ? 30.727  7.435   10.407  1.00 32.42 ?  87  LEU   A CD2 1 
ATOM   659  N  N   . LYS   A 1 88  ? 28.716  11.896  11.115  1.00 26.63 ?  88  LYS   A N   1 
ATOM   660  C  CA  . LYS   A 1 88  ? 28.596  12.934  10.097  1.00 25.97 ?  88  LYS   A CA  1 
ATOM   661  C  C   . LYS   A 1 88  ? 29.855  12.911  9.234   1.00 29.90 ?  88  LYS   A C   1 
ATOM   662  O  O   . LYS   A 1 88  ? 30.954  13.213  9.717   1.00 28.70 ?  88  LYS   A O   1 
ATOM   663  C  CB  . LYS   A 1 88  ? 28.378  14.301  10.740  1.00 26.90 ?  88  LYS   A CB  1 
ATOM   664  C  CG  . LYS   A 1 88  ? 27.072  14.398  11.516  1.00 26.11 ?  88  LYS   A CG  1 
ATOM   665  C  CD  . LYS   A 1 88  ? 26.862  15.785  12.091  1.00 33.18 ?  88  LYS   A CD  1 
ATOM   666  C  CE  . LYS   A 1 88  ? 28.019  16.161  13.003  1.00 36.85 ?  88  LYS   A CE  1 
ATOM   667  N  NZ  . LYS   A 1 88  ? 27.624  17.108  14.089  1.00 38.64 ?  88  LYS   A NZ  1 
ATOM   668  N  N   . LEU   A 1 89  ? 29.691  12.539  7.967   1.00 27.07 ?  89  LEU   A N   1 
ATOM   669  C  CA  . LEU   A 1 89  ? 30.783  12.496  6.998   1.00 25.60 ?  89  LEU   A CA  1 
ATOM   670  C  C   . LEU   A 1 89  ? 30.671  13.722  6.104   1.00 28.13 ?  89  LEU   A C   1 
ATOM   671  O  O   . LEU   A 1 89  ? 29.727  13.840  5.318   1.00 27.27 ?  89  LEU   A O   1 
ATOM   672  C  CB  . LEU   A 1 89  ? 30.726  11.221  6.162   1.00 24.22 ?  89  LEU   A CB  1 
ATOM   673  C  CG  . LEU   A 1 89  ? 30.741  9.889   6.900   1.00 26.64 ?  89  LEU   A CG  1 
ATOM   674  C  CD1 . LEU   A 1 89  ? 30.665  8.744   5.907   1.00 26.43 ?  89  LEU   A CD1 1 
ATOM   675  C  CD2 . LEU   A 1 89  ? 31.987  9.777   7.774   1.00 29.28 ?  89  LEU   A CD2 1 
ATOM   676  N  N   . LYS   A 1 90  ? 31.630  14.631  6.218   1.00 27.94 ?  90  LYS   A N   1 
ATOM   677  C  CA  . LYS   A 1 90  ? 31.689  15.751  5.295   1.00 28.94 ?  90  LYS   A CA  1 
ATOM   678  C  C   . LYS   A 1 90  ? 32.286  15.286  3.975   1.00 30.31 ?  90  LYS   A C   1 
ATOM   679  O  O   . LYS   A 1 90  ? 33.279  14.555  3.950   1.00 29.70 ?  90  LYS   A O   1 
ATOM   680  C  CB  . LYS   A 1 90  ? 32.516  16.893  5.884   1.00 30.51 ?  90  LYS   A CB  1 
ATOM   681  C  CG  . LYS   A 1 90  ? 32.495  18.167  5.059   1.00 32.80 ?  90  LYS   A CG  1 
ATOM   682  C  CD  . LYS   A 1 90  ? 32.807  19.374  5.932   1.00 38.93 ?  90  LYS   A CD  1 
ATOM   683  C  CE  . LYS   A 1 90  ? 33.179  20.595  5.105   1.00 40.90 ?  90  LYS   A CE  1 
ATOM   684  N  NZ  . LYS   A 1 90  ? 34.552  21.063  5.443   1.00 47.80 ?  90  LYS   A NZ  1 
ATOM   685  N  N   . VAL   A 1 91  ? 31.654  15.685  2.872   1.00 29.22 ?  91  VAL   A N   1 
ATOM   686  C  CA  . VAL   A 1 91  ? 32.132  15.332  1.545   1.00 27.12 ?  91  VAL   A CA  1 
ATOM   687  C  C   . VAL   A 1 91  ? 32.359  16.614  0.752   1.00 28.42 ?  91  VAL   A C   1 
ATOM   688  O  O   . VAL   A 1 91  ? 31.878  17.692  1.114   1.00 28.21 ?  91  VAL   A O   1 
ATOM   689  C  CB  . VAL   A 1 91  ? 31.165  14.383  0.813   1.00 34.11 ?  91  VAL   A CB  1 
ATOM   690  C  CG1 . VAL   A 1 91  ? 31.165  13.024  1.509   1.00 30.87 ?  91  VAL   A CG1 1 
ATOM   691  C  CG2 . VAL   A 1 91  ? 29.754  14.981  0.755   1.00 30.47 ?  91  VAL   A CG2 1 
ATOM   692  N  N   . ASP   A 1 92  ? 33.134  16.495  -0.328  1.00 33.92 ?  92  ASP   A N   1 
ATOM   693  C  CA  . ASP   A 1 92  ? 33.540  17.684  -1.066  1.00 36.04 ?  92  ASP   A CA  1 
ATOM   694  C  C   . ASP   A 1 92  ? 32.472  18.192  -2.020  1.00 35.22 ?  92  ASP   A C   1 
ATOM   695  O  O   . ASP   A 1 92  ? 32.700  19.209  -2.680  1.00 35.03 ?  92  ASP   A O   1 
ATOM   696  C  CB  . ASP   A 1 92  ? 34.850  17.434  -1.836  1.00 35.37 ?  92  ASP   A CB  1 
ATOM   697  C  CG  . ASP   A 1 92  ? 34.721  16.372  -2.937  1.00 35.10 ?  92  ASP   A CG  1 
ATOM   698  O  OD1 . ASP   A 1 92  ? 33.620  15.835  -3.173  1.00 36.92 ?  92  ASP   A OD1 1 
ATOM   699  O  OD2 . ASP   A 1 92  ? 35.752  16.060  -3.567  1.00 40.43 ?  92  ASP   A OD2 1 
ATOM   700  N  N   . THR   A 1 93  ? 31.319  17.529  -2.101  1.00 36.21 ?  93  THR   A N   1 
ATOM   701  C  CA  . THR   A 1 93  ? 30.255  17.915  -3.022  1.00 36.94 ?  93  THR   A CA  1 
ATOM   702  C  C   . THR   A 1 93  ? 28.948  18.065  -2.257  1.00 36.05 ?  93  THR   A C   1 
ATOM   703  O  O   . THR   A 1 93  ? 28.564  17.179  -1.484  1.00 31.60 ?  93  THR   A O   1 
ATOM   704  C  CB  . THR   A 1 93  ? 30.104  16.887  -4.152  1.00 37.06 ?  93  THR   A CB  1 
ATOM   705  O  OG1 . THR   A 1 93  ? 31.359  16.741  -4.825  1.00 40.59 ?  93  THR   A OG1 1 
ATOM   706  C  CG2 . THR   A 1 93  ? 29.042  17.331  -5.172  1.00 32.87 ?  93  THR   A CG2 1 
ATOM   707  N  N   . ALA   A 1 94  ? 28.281  19.197  -2.455  1.00 31.50 ?  94  ALA   A N   1 
ATOM   708  C  CA  . ALA   A 1 94  ? 26.947  19.390  -1.915  1.00 30.58 ?  94  ALA   A CA  1 
ATOM   709  C  C   . ALA   A 1 94  ? 25.923  18.706  -2.812  1.00 33.64 ?  94  ALA   A C   1 
ATOM   710  O  O   . ALA   A 1 94  ? 26.012  18.770  -4.042  1.00 30.33 ?  94  ALA   A O   1 
ATOM   711  C  CB  . ALA   A 1 94  ? 26.633  20.878  -1.790  1.00 34.51 ?  94  ALA   A CB  1 
ATOM   712  N  N   . ASN   A 1 95  ? 24.965  18.036  -2.191  1.00 32.38 ?  95  ASN   A N   1 
ATOM   713  C  CA  . ASN   A 1 95  ? 23.942  17.290  -2.914  1.00 31.82 ?  95  ASN   A CA  1 
ATOM   714  C  C   . ASN   A 1 95  ? 23.078  18.251  -3.714  1.00 30.90 ?  95  ASN   A C   1 
ATOM   715  O  O   . ASN   A 1 95  ? 22.351  19.053  -3.115  1.00 31.39 ?  95  ASN   A O   1 
ATOM   716  C  CB  . ASN   A 1 95  ? 23.083  16.488  -1.937  1.00 31.39 ?  95  ASN   A CB  1 
ATOM   717  C  CG  . ASN   A 1 95  ? 22.120  15.543  -2.635  1.00 31.82 ?  95  ASN   A CG  1 
ATOM   718  O  OD1 . ASN   A 1 95  ? 21.985  15.558  -3.860  1.00 32.15 ?  95  ASN   A OD1 1 
ATOM   719  N  ND2 . ASN   A 1 95  ? 21.438  14.715  -1.849  1.00 31.06 ?  95  ASN   A ND2 1 
ATOM   720  N  N   . PRO   A 1 96  ? 23.122  18.218  -5.046  1.00 30.75 ?  96  PRO   A N   1 
ATOM   721  C  CA  . PRO   A 1 96  ? 22.292  19.150  -5.820  1.00 29.44 ?  96  PRO   A CA  1 
ATOM   722  C  C   . PRO   A 1 96  ? 20.802  18.906  -5.637  1.00 33.37 ?  96  PRO   A C   1 
ATOM   723  O  O   . PRO   A 1 96  ? 20.010  19.838  -5.834  1.00 34.99 ?  96  PRO   A O   1 
ATOM   724  C  CB  . PRO   A 1 96  ? 22.742  18.900  -7.267  1.00 31.44 ?  96  PRO   A CB  1 
ATOM   725  C  CG  . PRO   A 1 96  ? 23.213  17.479  -7.263  1.00 34.68 ?  96  PRO   A CG  1 
ATOM   726  C  CD  . PRO   A 1 96  ? 23.839  17.258  -5.903  1.00 31.93 ?  96  PRO   A CD  1 
ATOM   727  N  N   . LYS   A 1 97  ? 20.400  17.699  -5.237  1.00 29.02 ?  97  LYS   A N   1 
ATOM   728  C  CA  . LYS   A 1 97  ? 18.997  17.368  -5.014  1.00 33.03 ?  97  LYS   A CA  1 
ATOM   729  C  C   . LYS   A 1 97  ? 18.553  17.594  -3.571  1.00 36.63 ?  97  LYS   A C   1 
ATOM   730  O  O   . LYS   A 1 97  ? 17.481  17.112  -3.183  1.00 32.82 ?  97  LYS   A O   1 
ATOM   731  C  CB  . LYS   A 1 97  ? 18.729  15.912  -5.402  1.00 33.25 ?  97  LYS   A CB  1 
ATOM   732  C  CG  . LYS   A 1 97  ? 19.101  15.538  -6.835  1.00 39.97 ?  97  LYS   A CG  1 
ATOM   733  C  CD  . LYS   A 1 97  ? 18.738  14.077  -7.105  1.00 39.78 ?  97  LYS   A CD  1 
ATOM   734  C  CE  . LYS   A 1 97  ? 19.186  13.619  -8.480  1.00 50.99 ?  97  LYS   A CE  1 
ATOM   735  N  NZ  . LYS   A 1 97  ? 19.046  12.140  -8.635  1.00 53.78 ?  97  LYS   A NZ  1 
ATOM   736  N  N   . THR   A 1 98  ? 19.342  18.304  -2.769  1.00 33.40 ?  98  THR   A N   1 
ATOM   737  C  CA  . THR   A 1 98  ? 18.939  18.562  -1.389  1.00 36.73 ?  98  THR   A CA  1 
ATOM   738  C  C   . THR   A 1 98  ? 17.602  19.298  -1.352  1.00 33.69 ?  98  THR   A C   1 
ATOM   739  O  O   . THR   A 1 98  ? 17.495  20.405  -1.902  1.00 33.23 ?  98  THR   A O   1 
ATOM   740  C  CB  . THR   A 1 98  ? 19.991  19.381  -0.642  1.00 31.13 ?  98  THR   A CB  1 
ATOM   741  O  OG1 . THR   A 1 98  ? 21.252  18.690  -0.657  1.00 28.76 ?  98  THR   A OG1 1 
ATOM   742  C  CG2 . THR   A 1 98  ? 19.548  19.608  0.799   1.00 34.58 ?  98  THR   A CG2 1 
ATOM   743  N  N   . PRO   A 1 99  ? 16.573  18.738  -0.726  1.00 33.60 ?  99  PRO   A N   1 
ATOM   744  C  CA  . PRO   A 1 99  ? 15.317  19.469  -0.554  1.00 37.85 ?  99  PRO   A CA  1 
ATOM   745  C  C   . PRO   A 1 99  ? 15.442  20.466  0.585   1.00 33.69 ?  99  PRO   A C   1 
ATOM   746  O  O   . PRO   A 1 99  ? 16.395  20.446  1.361   1.00 33.73 ?  99  PRO   A O   1 
ATOM   747  C  CB  . PRO   A 1 99  ? 14.315  18.365  -0.207  1.00 32.18 ?  99  PRO   A CB  1 
ATOM   748  C  CG  . PRO   A 1 99  ? 15.144  17.376  0.554   1.00 31.56 ?  99  PRO   A CG  1 
ATOM   749  C  CD  . PRO   A 1 99  ? 16.524  17.407  -0.096  1.00 34.60 ?  99  PRO   A CD  1 
ATOM   750  N  N   . LYS   A 1 100 ? 14.463  21.359  0.671   1.00 30.98 ?  100 LYS   A N   1 
ATOM   751  C  CA  . LYS   A 1 100 ? 14.312  22.117  1.901   1.00 36.76 ?  100 LYS   A CA  1 
ATOM   752  C  C   . LYS   A 1 100 ? 13.964  21.130  3.002   1.00 35.10 ?  100 LYS   A C   1 
ATOM   753  O  O   . LYS   A 1 100 ? 13.092  20.277  2.817   1.00 34.57 ?  100 LYS   A O   1 
ATOM   754  C  CB  . LYS   A 1 100 ? 13.223  23.180  1.753   1.00 38.06 ?  100 LYS   A CB  1 
ATOM   755  N  N   . TYR   A 1 101 ? 14.666  21.206  4.132   1.00 34.06 ?  101 TYR   A N   1 
ATOM   756  C  CA  . TYR   A 1 101 ? 14.494  20.167  5.140   1.00 33.35 ?  101 TYR   A CA  1 
ATOM   757  C  C   . TYR   A 1 101 ? 14.677  20.711  6.552   1.00 31.41 ?  101 TYR   A C   1 
ATOM   758  O  O   . TYR   A 1 101 ? 15.196  21.811  6.764   1.00 32.76 ?  101 TYR   A O   1 
ATOM   759  C  CB  . TYR   A 1 101 ? 15.463  19.003  4.910   1.00 32.70 ?  101 TYR   A CB  1 
ATOM   760  C  CG  . TYR   A 1 101 ? 16.896  19.346  5.247   1.00 35.06 ?  101 TYR   A CG  1 
ATOM   761  C  CD1 . TYR   A 1 101 ? 17.729  19.943  4.308   1.00 31.28 ?  101 TYR   A CD1 1 
ATOM   762  C  CD2 . TYR   A 1 101 ? 17.415  19.076  6.509   1.00 29.33 ?  101 TYR   A CD2 1 
ATOM   763  C  CE1 . TYR   A 1 101 ? 19.051  20.263  4.622   1.00 35.30 ?  101 TYR   A CE1 1 
ATOM   764  C  CE2 . TYR   A 1 101 ? 18.721  19.391  6.829   1.00 33.13 ?  101 TYR   A CE2 1 
ATOM   765  C  CZ  . TYR   A 1 101 ? 19.534  19.983  5.886   1.00 36.43 ?  101 TYR   A CZ  1 
ATOM   766  O  OH  . TYR   A 1 101 ? 20.837  20.292  6.217   1.00 31.40 ?  101 TYR   A OH  1 
ATOM   767  N  N   . LYS   A 1 102 ? 14.241  19.899  7.516   1.00 30.98 ?  102 LYS   A N   1 
ATOM   768  C  CA  . LYS   A 1 102 ? 14.347  20.174  8.941   1.00 30.37 ?  102 LYS   A CA  1 
ATOM   769  C  C   . LYS   A 1 102 ? 14.620  18.867  9.667   1.00 30.45 ?  102 LYS   A C   1 
ATOM   770  O  O   . LYS   A 1 102 ? 14.189  17.797  9.230   1.00 31.71 ?  102 LYS   A O   1 
ATOM   771  C  CB  . LYS   A 1 102 ? 13.059  20.798  9.514   1.00 35.52 ?  102 LYS   A CB  1 
ATOM   772  C  CG  . LYS   A 1 102 ? 12.862  22.264  9.207   1.00 40.65 ?  102 LYS   A CG  1 
ATOM   773  C  CD  . LYS   A 1 102 ? 11.411  22.675  9.424   1.00 46.93 ?  102 LYS   A CD  1 
ATOM   774  C  CE  . LYS   A 1 102 ? 10.990  22.456  10.863  1.00 49.40 ?  102 LYS   A CE  1 
ATOM   775  N  NZ  . LYS   A 1 102 ? 11.909  23.157  11.809  1.00 52.29 ?  102 LYS   A NZ  1 
ATOM   776  N  N   . PHE   A 1 103 ? 15.330  18.960  10.786  1.00 27.49 ?  103 PHE   A N   1 
ATOM   777  C  CA  . PHE   A 1 103 ? 15.475  17.847  11.714  1.00 29.35 ?  103 PHE   A CA  1 
ATOM   778  C  C   . PHE   A 1 103 ? 14.547  18.087  12.893  1.00 30.85 ?  103 PHE   A C   1 
ATOM   779  O  O   . PHE   A 1 103 ? 14.585  19.159  13.504  1.00 27.91 ?  103 PHE   A O   1 
ATOM   780  C  CB  . PHE   A 1 103 ? 16.916  17.702  12.210  1.00 31.69 ?  103 PHE   A CB  1 
ATOM   781  C  CG  . PHE   A 1 103 ? 17.893  17.287  11.146  1.00 30.68 ?  103 PHE   A CG  1 
ATOM   782  C  CD1 . PHE   A 1 103 ? 17.453  16.748  9.941   1.00 28.32 ?  103 PHE   A CD1 1 
ATOM   783  C  CD2 . PHE   A 1 103 ? 19.257  17.425  11.359  1.00 32.32 ?  103 PHE   A CD2 1 
ATOM   784  C  CE1 . PHE   A 1 103 ? 18.358  16.370  8.966   1.00 29.27 ?  103 PHE   A CE1 1 
ATOM   785  C  CE2 . PHE   A 1 103 ? 20.169  17.045  10.385  1.00 30.16 ?  103 PHE   A CE2 1 
ATOM   786  C  CZ  . PHE   A 1 103 ? 19.722  16.517  9.194   1.00 29.75 ?  103 PHE   A CZ  1 
ATOM   787  N  N   . VAL   A 1 104 ? 13.710  17.097  13.203  1.00 30.05 ?  104 VAL   A N   1 
ATOM   788  C  CA  . VAL   A 1 104 ? 12.760  17.205  14.299  1.00 28.55 ?  104 VAL   A CA  1 
ATOM   789  C  C   . VAL   A 1 104 ? 12.805  15.933  15.133  1.00 30.06 ?  104 VAL   A C   1 
ATOM   790  O  O   . VAL   A 1 104 ? 13.225  14.868  14.680  1.00 32.18 ?  104 VAL   A O   1 
ATOM   791  C  CB  . VAL   A 1 104 ? 11.317  17.465  13.812  1.00 31.75 ?  104 VAL   A CB  1 
ATOM   792  C  CG1 . VAL   A 1 104 ? 11.232  18.765  13.028  1.00 35.58 ?  104 VAL   A CG1 1 
ATOM   793  C  CG2 . VAL   A 1 104 ? 10.821  16.305  12.976  1.00 32.99 ?  104 VAL   A CG2 1 
ATOM   794  N  N   . ARG   A 1 105 ? 12.372  16.056  16.377  1.00 27.84 ?  105 ARG   A N   1 
ATOM   795  C  CA  . ARG   A 1 105 ? 12.179  14.900  17.236  1.00 27.68 ?  105 ARG   A CA  1 
ATOM   796  C  C   . ARG   A 1 105 ? 10.692  14.811  17.535  1.00 30.96 ?  105 ARG   A C   1 
ATOM   797  O  O   . ARG   A 1 105 ? 10.101  15.779  18.020  1.00 33.63 ?  105 ARG   A O   1 
ATOM   798  C  CB  . ARG   A 1 105 ? 13.001  15.015  18.515  1.00 29.84 ?  105 ARG   A CB  1 
ATOM   799  C  CG  . ARG   A 1 105 ? 13.011  13.742  19.346  1.00 30.62 ?  105 ARG   A CG  1 
ATOM   800  C  CD  . ARG   A 1 105 ? 13.736  13.942  20.660  1.00 34.19 ?  105 ARG   A CD  1 
ATOM   801  N  NE  . ARG   A 1 105 ? 13.673  12.744  21.493  1.00 31.29 ?  105 ARG   A NE  1 
ATOM   802  C  CZ  . ARG   A 1 105 ? 14.489  11.701  21.372  1.00 34.01 ?  105 ARG   A CZ  1 
ATOM   803  N  NH1 . ARG   A 1 105 ? 15.448  11.693  20.444  1.00 29.77 ?  105 ARG   A NH1 1 
ATOM   804  N  NH2 . ARG   A 1 105 ? 14.343  10.658  22.181  1.00 29.36 ?  105 ARG   A NH2 1 
ATOM   805  N  N   . ILE   A 1 106 ? 10.087  13.673  17.211  1.00 24.13 ?  106 ILE   A N   1 
ATOM   806  C  CA  . ILE   A 1 106 ? 8.645   13.512  17.360  1.00 33.04 ?  106 ILE   A CA  1 
ATOM   807  C  C   . ILE   A 1 106 ? 8.312   12.907  18.717  1.00 31.72 ?  106 ILE   A C   1 
ATOM   808  O  O   . ILE   A 1 106 ? 9.194   12.427  19.438  1.00 30.30 ?  106 ILE   A O   1 
ATOM   809  C  CB  . ILE   A 1 106 ? 8.061   12.649  16.233  1.00 34.40 ?  106 ILE   A CB  1 
ATOM   810  C  CG1 . ILE   A 1 106 ? 8.681   11.249  16.267  1.00 32.64 ?  106 ILE   A CG1 1 
ATOM   811  C  CG2 . ILE   A 1 106 ? 8.242   13.336  14.871  1.00 32.50 ?  106 ILE   A CG2 1 
ATOM   812  C  CD1 . ILE   A 1 106 ? 7.986   10.272  15.335  1.00 37.08 ?  106 ILE   A CD1 1 
ATOM   813  N  N   . GLN   A 1 107 ? 7.033   12.919  19.060  1.00 31.94 ?  107 GLN   A N   1 
ATOM   814  C  CA  . GLN   A 1 107 ? 6.466   12.407  20.292  1.00 36.27 ?  107 GLN   A CA  1 
ATOM   815  C  C   . GLN   A 1 107 ? 5.964   10.988  20.093  1.00 33.21 ?  107 GLN   A C   1 
ATOM   816  O  O   . GLN   A 1 107 ? 5.648   10.581  18.972  1.00 30.27 ?  107 GLN   A O   1 
ATOM   817  C  CB  . GLN   A 1 107 ? 5.300   13.294  20.748  1.00 37.02 ?  107 GLN   A CB  1 
ATOM   818  C  CG  . GLN   A 1 107 ? 5.640   14.763  20.855  1.00 43.45 ?  107 GLN   A CG  1 
ATOM   819  C  CD  . GLN   A 1 107 ? 6.688   15.032  21.914  1.00 48.84 ?  107 GLN   A CD  1 
ATOM   820  O  OE1 . GLN   A 1 107 ? 6.657   14.444  22.999  1.00 51.57 ?  107 GLN   A OE1 1 
ATOM   821  N  NE2 . GLN   A 1 107 ? 7.631   15.916  21.603  1.00 52.60 ?  107 GLN   A NE2 1 
ATOM   822  N  N   . PRO   A 1 108 ? 5.873   10.202  21.164  1.00 32.06 ?  108 PRO   A N   1 
ATOM   823  C  CA  . PRO   A 1 108 ? 5.170   8.921   21.066  1.00 33.64 ?  108 PRO   A CA  1 
ATOM   824  C  C   . PRO   A 1 108 ? 3.775   9.159   20.512  1.00 30.57 ?  108 PRO   A C   1 
ATOM   825  O  O   . PRO   A 1 108 ? 3.128   10.158  20.831  1.00 27.98 ?  108 PRO   A O   1 
ATOM   826  C  CB  . PRO   A 1 108 ? 5.123   8.420   22.516  1.00 33.55 ?  108 PRO   A CB  1 
ATOM   827  C  CG  . PRO   A 1 108 ? 6.143   9.200   23.234  1.00 33.48 ?  108 PRO   A CG  1 
ATOM   828  C  CD  . PRO   A 1 108 ? 6.271   10.513  22.546  1.00 32.32 ?  108 PRO   A CD  1 
ATOM   829  N  N   . GLY   A 1 109 ? 3.331   8.258   19.643  1.00 28.63 ?  109 GLY   A N   1 
ATOM   830  C  CA  . GLY   A 1 109 ? 2.039   8.380   19.000  1.00 28.61 ?  109 GLY   A CA  1 
ATOM   831  C  C   . GLY   A 1 109 ? 2.035   9.085   17.656  1.00 30.82 ?  109 GLY   A C   1 
ATOM   832  O  O   . GLY   A 1 109 ? 1.060   8.945   16.906  1.00 31.60 ?  109 GLY   A O   1 
ATOM   833  N  N   . GLN   A 1 110 ? 3.085   9.837   17.320  1.00 31.55 ?  110 GLN   A N   1 
ATOM   834  C  CA  . GLN   A 1 110 ? 3.086   10.524  16.038  1.00 32.89 ?  110 GLN   A CA  1 
ATOM   835  C  C   . GLN   A 1 110 ? 3.515   9.571   14.931  1.00 27.58 ?  110 GLN   A C   1 
ATOM   836  O  O   . GLN   A 1 110 ? 4.176   8.560   15.165  1.00 28.15 ?  110 GLN   A O   1 
ATOM   837  C  CB  . GLN   A 1 110 ? 3.997   11.750  16.066  1.00 31.58 ?  110 GLN   A CB  1 
ATOM   838  C  CG  . GLN   A 1 110 ? 3.542   12.801  17.066  1.00 37.99 ?  110 GLN   A CG  1 
ATOM   839  C  CD  . GLN   A 1 110 ? 4.307   14.095  16.937  1.00 40.52 ?  110 GLN   A CD  1 
ATOM   840  O  OE1 . GLN   A 1 110 ? 5.324   14.296  17.597  1.00 44.99 ?  110 GLN   A OE1 1 
ATOM   841  N  NE2 . GLN   A 1 110 ? 3.823   14.985  16.076  1.00 54.42 ?  110 GLN   A NE2 1 
ATOM   842  N  N   . THR   A 1 111 ? 3.110   9.893   13.716  1.00 27.89 ?  111 THR   A N   1 
ATOM   843  C  CA  . THR   A 1 111 ? 3.370   9.030   12.576  1.00 27.57 ?  111 THR   A CA  1 
ATOM   844  C  C   . THR   A 1 111 ? 4.404   9.659   11.654  1.00 26.16 ?  111 THR   A C   1 
ATOM   845  O  O   . THR   A 1 111 ? 4.679   10.859  11.710  1.00 28.96 ?  111 THR   A O   1 
ATOM   846  C  CB  . THR   A 1 111 ? 2.081   8.752   11.800  1.00 29.65 ?  111 THR   A CB  1 
ATOM   847  O  OG1 . THR   A 1 111 ? 1.433   9.996   11.513  1.00 29.91 ?  111 THR   A OG1 1 
ATOM   848  C  CG2 . THR   A 1 111 ? 1.151   7.867   12.625  1.00 29.55 ?  111 THR   A CG2 1 
ATOM   849  N  N   . PHE   A 1 112 ? 4.966   8.819   10.791  1.00 27.09 ?  112 PHE   A N   1 
ATOM   850  C  CA  . PHE   A 1 112 ? 5.889   9.262   9.756   1.00 29.21 ?  112 PHE   A CA  1 
ATOM   851  C  C   . PHE   A 1 112 ? 6.004   8.166   8.711   1.00 25.59 ?  112 PHE   A C   1 
ATOM   852  O  O   . PHE   A 1 112 ? 5.621   7.017   8.945   1.00 26.91 ?  112 PHE   A O   1 
ATOM   853  C  CB  . PHE   A 1 112 ? 7.266   9.597   10.337  1.00 26.28 ?  112 PHE   A CB  1 
ATOM   854  C  CG  . PHE   A 1 112 ? 7.884   8.476   11.125  1.00 27.75 ?  112 PHE   A CG  1 
ATOM   855  C  CD1 . PHE   A 1 112 ? 7.639   8.348   12.484  1.00 30.40 ?  112 PHE   A CD1 1 
ATOM   856  C  CD2 . PHE   A 1 112 ? 8.735   7.567   10.516  1.00 28.68 ?  112 PHE   A CD2 1 
ATOM   857  C  CE1 . PHE   A 1 112 ? 8.225   7.327   13.220  1.00 30.80 ?  112 PHE   A CE1 1 
ATOM   858  C  CE2 . PHE   A 1 112 ? 9.320   6.540   11.239  1.00 28.04 ?  112 PHE   A CE2 1 
ATOM   859  C  CZ  . PHE   A 1 112 ? 9.068   6.421   12.599  1.00 31.05 ?  112 PHE   A CZ  1 
ATOM   860  N  N   . SER   A 1 113 ? 6.538   8.535   7.551   1.00 27.04 ?  113 SER   A N   1 
ATOM   861  C  CA  . SER   A 1 113 ? 6.778   7.579   6.484   1.00 25.33 ?  113 SER   A CA  1 
ATOM   862  C  C   . SER   A 1 113 ? 8.206   7.057   6.559   1.00 25.91 ?  113 SER   A C   1 
ATOM   863  O  O   . SER   A 1 113 ? 9.133   7.806   6.864   1.00 26.90 ?  113 SER   A O   1 
ATOM   864  C  CB  . SER   A 1 113 ? 6.520   8.229   5.122   1.00 25.75 ?  113 SER   A CB  1 
ATOM   865  O  OG  . SER   A 1 113 ? 5.177   8.676   5.059   1.00 25.23 ?  113 SER   A OG  1 
ATOM   866  N  N   . VAL   A 1 114 ? 8.376   5.769   6.279   1.00 25.51 ?  114 VAL   A N   1 
ATOM   867  C  CA  . VAL   A 1 114 ? 9.687   5.133   6.217   1.00 26.22 ?  114 VAL   A CA  1 
ATOM   868  C  C   . VAL   A 1 114 ? 10.019  4.844   4.758   1.00 31.02 ?  114 VAL   A C   1 
ATOM   869  O  O   . VAL   A 1 114 ? 9.241   4.187   4.060   1.00 28.03 ?  114 VAL   A O   1 
ATOM   870  C  CB  . VAL   A 1 114 ? 9.718   3.831   7.035   1.00 28.78 ?  114 VAL   A CB  1 
ATOM   871  C  CG1 . VAL   A 1 114 ? 10.978  3.062   6.720   1.00 26.21 ?  114 VAL   A CG1 1 
ATOM   872  C  CG2 . VAL   A 1 114 ? 9.595   4.116   8.542   1.00 30.61 ?  114 VAL   A CG2 1 
ATOM   873  N  N   . LEU   A 1 115 ? 11.179  5.313   4.302   1.00 26.98 ?  115 LEU   A N   1 
ATOM   874  C  CA  . LEU   A 1 115 ? 11.731  4.900   3.010   1.00 27.62 ?  115 LEU   A CA  1 
ATOM   875  C  C   . LEU   A 1 115 ? 12.753  3.805   3.294   1.00 29.17 ?  115 LEU   A C   1 
ATOM   876  O  O   . LEU   A 1 115 ? 13.888  4.087   3.679   1.00 28.06 ?  115 LEU   A O   1 
ATOM   877  C  CB  . LEU   A 1 115 ? 12.360  6.078   2.273   1.00 24.25 ?  115 LEU   A CB  1 
ATOM   878  C  CG  . LEU   A 1 115 ? 12.901  5.746   0.880   1.00 27.06 ?  115 LEU   A CG  1 
ATOM   879  C  CD1 . LEU   A 1 115 ? 11.776  5.263   -0.022  1.00 27.81 ?  115 LEU   A CD1 1 
ATOM   880  C  CD2 . LEU   A 1 115 ? 13.586  6.951   0.258   1.00 28.35 ?  115 LEU   A CD2 1 
ATOM   881  N  N   . ALA   A 1 116 ? 12.345  2.550   3.144   1.00 26.44 ?  116 ALA   A N   1 
ATOM   882  C  CA  . ALA   A 1 116 ? 13.245  1.445   3.441   1.00 24.61 ?  116 ALA   A CA  1 
ATOM   883  C  C   . ALA   A 1 116 ? 14.270  1.316   2.322   1.00 30.21 ?  116 ALA   A C   1 
ATOM   884  O  O   . ALA   A 1 116 ? 13.906  1.251   1.140   1.00 29.25 ?  116 ALA   A O   1 
ATOM   885  C  CB  . ALA   A 1 116 ? 12.463  0.143   3.607   1.00 32.08 ?  116 ALA   A CB  1 
ATOM   886  N  N   . CYS   A 1 117 ? 15.548  1.284   2.689   1.00 27.48 ?  117 CYS   A N   1 
ATOM   887  C  CA  . CYS   A 1 117 ? 16.632  1.264   1.717   1.00 29.71 ?  117 CYS   A CA  1 
ATOM   888  C  C   . CYS   A 1 117 ? 17.623  0.159   2.044   1.00 28.76 ?  117 CYS   A C   1 
ATOM   889  O  O   . CYS   A 1 117 ? 17.739  -0.285  3.189   1.00 23.94 ?  117 CYS   A O   1 
ATOM   890  C  CB  . CYS   A 1 117 ? 17.387  2.594   1.660   1.00 29.95 ?  117 CYS   A CB  1 
ATOM   891  S  SG  . CYS   A 1 117 ? 16.402  3.991   1.126   1.00 35.87 ?  117 CYS   A SG  1 
ATOM   892  N  N   . TYR   A 1 118 ? 18.330  -0.279  1.011   1.00 28.49 ?  118 TYR   A N   1 
ATOM   893  C  CA  . TYR   A 1 118 ? 19.403  -1.254  1.127   1.00 27.56 ?  118 TYR   A CA  1 
ATOM   894  C  C   . TYR   A 1 118 ? 20.460  -0.869  0.113   1.00 27.83 ?  118 TYR   A C   1 
ATOM   895  O  O   . TYR   A 1 118 ? 20.125  -0.563  -1.035  1.00 26.69 ?  118 TYR   A O   1 
ATOM   896  C  CB  . TYR   A 1 118 ? 18.897  -2.676  0.866   1.00 33.99 ?  118 TYR   A CB  1 
ATOM   897  C  CG  . TYR   A 1 118 ? 17.834  -3.076  1.842   1.00 32.22 ?  118 TYR   A CG  1 
ATOM   898  C  CD1 . TYR   A 1 118 ? 18.184  -3.555  3.092   1.00 31.02 ?  118 TYR   A CD1 1 
ATOM   899  C  CD2 . TYR   A 1 118 ? 16.475  -2.940  1.535   1.00 31.84 ?  118 TYR   A CD2 1 
ATOM   900  C  CE1 . TYR   A 1 118 ? 17.236  -3.911  4.013   1.00 29.24 ?  118 TYR   A CE1 1 
ATOM   901  C  CE2 . TYR   A 1 118 ? 15.498  -3.292  2.469   1.00 28.22 ?  118 TYR   A CE2 1 
ATOM   902  C  CZ  . TYR   A 1 118 ? 15.903  -3.779  3.711   1.00 29.66 ?  118 TYR   A CZ  1 
ATOM   903  O  OH  . TYR   A 1 118 ? 14.996  -4.144  4.667   1.00 26.59 ?  118 TYR   A OH  1 
ATOM   904  N  N   . ASN   A 1 119 ? 21.720  -0.841  0.552   1.00 31.41 ?  119 ASN   A N   1 
ATOM   905  C  CA  . ASN   A 1 119 ? 22.849  -0.493  -0.305  1.00 30.87 ?  119 ASN   A CA  1 
ATOM   906  C  C   . ASN   A 1 119 ? 22.677  0.879   -0.941  1.00 27.70 ?  119 ASN   A C   1 
ATOM   907  O  O   . ASN   A 1 119 ? 23.165  1.123   -2.043  1.00 30.60 ?  119 ASN   A O   1 
ATOM   908  C  CB  . ASN   A 1 119 ? 23.068  -1.557  -1.384  1.00 29.73 ?  119 ASN   A CB  1 
ATOM   909  C  CG  . ASN   A 1 119 ? 23.390  -2.918  -0.799  1.00 36.17 ?  119 ASN   A CG  1 
ATOM   910  O  OD1 . ASN   A 1 119 ? 24.302  -3.055  0.016   1.00 40.87 ?  119 ASN   A OD1 1 
ATOM   911  N  ND2 . ASN   A 1 119 ? 22.637  -3.931  -1.205  1.00 41.73 ?  119 ASN   A ND2 1 
ATOM   912  N  N   . GLY   A 1 120 ? 21.979  1.784   -0.258  1.00 27.86 ?  120 GLY   A N   1 
ATOM   913  C  CA  . GLY   A 1 120 ? 21.752  3.118   -0.776  1.00 27.01 ?  120 GLY   A CA  1 
ATOM   914  C  C   . GLY   A 1 120 ? 20.605  3.259   -1.760  1.00 30.88 ?  120 GLY   A C   1 
ATOM   915  O  O   . GLY   A 1 120 ? 20.403  4.357   -2.291  1.00 33.05 ?  120 GLY   A O   1 
ATOM   916  N  N   . SER   A 1 121 ? 19.852  2.198   -2.027  1.00 28.40 ?  121 SER   A N   1 
ATOM   917  C  CA  . SER   A 1 121 ? 18.763  2.277   -2.988  1.00 29.71 ?  121 SER   A CA  1 
ATOM   918  C  C   . SER   A 1 121 ? 17.422  2.074   -2.295  1.00 29.73 ?  121 SER   A C   1 
ATOM   919  O  O   . SER   A 1 121 ? 17.237  1.070   -1.594  1.00 30.59 ?  121 SER   A O   1 
ATOM   920  C  CB  . SER   A 1 121 ? 18.932  1.232   -4.098  1.00 28.21 ?  121 SER   A CB  1 
ATOM   921  O  OG  . SER   A 1 121 ? 20.207  1.351   -4.701  1.00 37.31 ?  121 SER   A OG  1 
ATOM   922  N  N   . PRO   A 1 122 ? 16.452  2.963   -2.504  1.00 34.69 ?  122 PRO   A N   1 
ATOM   923  C  CA  . PRO   A 1 122 ? 15.143  2.797   -1.859  1.00 34.63 ?  122 PRO   A CA  1 
ATOM   924  C  C   . PRO   A 1 122 ? 14.396  1.614   -2.457  1.00 33.65 ?  122 PRO   A C   1 
ATOM   925  O  O   . PRO   A 1 122 ? 14.346  1.452   -3.678  1.00 35.35 ?  122 PRO   A O   1 
ATOM   926  C  CB  . PRO   A 1 122 ? 14.437  4.119   -2.167  1.00 34.04 ?  122 PRO   A CB  1 
ATOM   927  C  CG  . PRO   A 1 122 ? 14.989  4.504   -3.513  1.00 40.22 ?  122 PRO   A CG  1 
ATOM   928  C  CD  . PRO   A 1 122 ? 16.447  4.061   -3.488  1.00 35.33 ?  122 PRO   A CD  1 
ATOM   929  N  N   . SER   A 1 123 ? 13.815  0.779   -1.592  1.00 33.25 ?  123 SER   A N   1 
ATOM   930  C  CA  . SER   A 1 123 ? 13.067  -0.366  -2.079  1.00 35.56 ?  123 SER   A CA  1 
ATOM   931  C  C   . SER   A 1 123 ? 11.590  -0.341  -1.718  1.00 33.75 ?  123 SER   A C   1 
ATOM   932  O  O   . SER   A 1 123 ? 10.829  -1.138  -2.276  1.00 36.92 ?  123 SER   A O   1 
ATOM   933  C  CB  . SER   A 1 123 ? 13.696  -1.677  -1.585  1.00 33.60 ?  123 SER   A CB  1 
ATOM   934  O  OG  . SER   A 1 123 ? 13.482  -1.884  -0.209  1.00 34.83 ?  123 SER   A OG  1 
ATOM   935  N  N   . GLY   A 1 124 ? 11.157  0.550   -0.834  1.00 29.67 ?  124 GLY   A N   1 
ATOM   936  C  CA  . GLY   A 1 124 ? 9.741   0.656   -0.518  1.00 33.87 ?  124 GLY   A CA  1 
ATOM   937  C  C   . GLY   A 1 124 ? 9.515   1.762   0.489   1.00 30.28 ?  124 GLY   A C   1 
ATOM   938  O  O   . GLY   A 1 124 ? 10.440  2.206   1.180   1.00 26.46 ?  124 GLY   A O   1 
ATOM   939  N  N   . VAL   A 1 125 ? 8.262   2.205   0.566   1.00 28.82 ?  125 VAL   A N   1 
ATOM   940  C  CA  . VAL   A 1 125 ? 7.866   3.266   1.489   1.00 24.46 ?  125 VAL   A CA  1 
ATOM   941  C  C   . VAL   A 1 125 ? 6.602   2.847   2.236   1.00 31.11 ?  125 VAL   A C   1 
ATOM   942  O  O   . VAL   A 1 125 ? 5.676   2.285   1.644   1.00 28.41 ?  125 VAL   A O   1 
ATOM   943  C  CB  . VAL   A 1 125 ? 7.666   4.608   0.745   1.00 29.38 ?  125 VAL   A CB  1 
ATOM   944  C  CG1 . VAL   A 1 125 ? 6.547   4.515   -0.266  1.00 31.06 ?  125 VAL   A CG1 1 
ATOM   945  C  CG2 . VAL   A 1 125 ? 7.408   5.737   1.718   1.00 30.57 ?  125 VAL   A CG2 1 
ATOM   946  N  N   . TYR   A 1 126 ? 6.568   3.103   3.544   1.00 22.76 ?  126 TYR   A N   1 
ATOM   947  C  CA  . TYR   A 1 126 ? 5.378   2.785   4.321   1.00 29.28 ?  126 TYR   A CA  1 
ATOM   948  C  C   . TYR   A 1 126 ? 5.229   3.771   5.468   1.00 27.06 ?  126 TYR   A C   1 
ATOM   949  O  O   . TYR   A 1 126 ? 6.139   4.541   5.787   1.00 28.36 ?  126 TYR   A O   1 
ATOM   950  C  CB  . TYR   A 1 126 ? 5.399   1.343   4.839   1.00 27.03 ?  126 TYR   A CB  1 
ATOM   951  C  CG  . TYR   A 1 126 ? 6.620   0.954   5.648   1.00 32.16 ?  126 TYR   A CG  1 
ATOM   952  C  CD1 . TYR   A 1 126 ? 6.658   1.141   7.026   1.00 33.59 ?  126 TYR   A CD1 1 
ATOM   953  C  CD2 . TYR   A 1 126 ? 7.723   0.369   5.037   1.00 32.05 ?  126 TYR   A CD2 1 
ATOM   954  C  CE1 . TYR   A 1 126 ? 7.771   0.771   7.765   1.00 32.48 ?  126 TYR   A CE1 1 
ATOM   955  C  CE2 . TYR   A 1 126 ? 8.838   -0.003  5.769   1.00 31.56 ?  126 TYR   A CE2 1 
ATOM   956  C  CZ  . TYR   A 1 126 ? 8.854   0.200   7.133   1.00 32.10 ?  126 TYR   A CZ  1 
ATOM   957  O  OH  . TYR   A 1 126 ? 9.963   -0.172  7.869   1.00 37.79 ?  126 TYR   A OH  1 
ATOM   958  N  N   . GLN   A 1 127 ? 4.057   3.731   6.090   1.00 29.41 ?  127 GLN   A N   1 
ATOM   959  C  CA  . GLN   A 1 127 ? 3.693   4.645   7.159   1.00 29.89 ?  127 GLN   A CA  1 
ATOM   960  C  C   . GLN   A 1 127 ? 3.836   3.924   8.495   1.00 35.37 ?  127 GLN   A C   1 
ATOM   961  O  O   . GLN   A 1 127 ? 3.465   2.754   8.615   1.00 33.33 ?  127 GLN   A O   1 
ATOM   962  C  CB  . GLN   A 1 127 ? 2.258   5.149   6.945   1.00 37.68 ?  127 GLN   A CB  1 
ATOM   963  C  CG  . GLN   A 1 127 ? 1.843   6.358   7.773   1.00 32.88 ?  127 GLN   A CG  1 
ATOM   964  C  CD  . GLN   A 1 127 ? 2.594   7.628   7.401   1.00 33.35 ?  127 GLN   A CD  1 
ATOM   965  O  OE1 . GLN   A 1 127 ? 3.458   7.623   6.526   1.00 30.40 ?  127 GLN   A OE1 1 
ATOM   966  N  NE2 . GLN   A 1 127 ? 2.267   8.726   8.077   1.00 35.63 ?  127 GLN   A NE2 1 
ATOM   967  N  N   . CYS   A 1 128 ? 4.411   4.617   9.482   1.00 31.44 ?  128 CYS   A N   1 
ATOM   968  C  CA  . CYS   A 1 128 ? 4.727   4.060   10.794  1.00 32.96 ?  128 CYS   A CA  1 
ATOM   969  C  C   . CYS   A 1 128 ? 4.252   5.007   11.881  1.00 32.88 ?  128 CYS   A C   1 
ATOM   970  O  O   . CYS   A 1 128 ? 4.109   6.207   11.653  1.00 35.33 ?  128 CYS   A O   1 
ATOM   971  C  CB  . CYS   A 1 128 ? 6.243   3.859   10.996  1.00 28.64 ?  128 CYS   A CB  1 
ATOM   972  S  SG  . CYS   A 1 128 ? 6.845   2.229   10.611  1.00 48.16 ?  128 CYS   A SG  1 
ATOM   973  N  N   . ALA   A 1 129 ? 4.040   4.461   13.079  1.00 38.09 ?  129 ALA   A N   1 
ATOM   974  C  CA  . ALA   A 1 129 ? 3.849   5.257   14.286  1.00 31.83 ?  129 ALA   A CA  1 
ATOM   975  C  C   . ALA   A 1 129 ? 4.962   4.951   15.276  1.00 30.56 ?  129 ALA   A C   1 
ATOM   976  O  O   . ALA   A 1 129 ? 5.383   3.797   15.414  1.00 32.07 ?  129 ALA   A O   1 
ATOM   977  C  CB  . ALA   A 1 129 ? 2.498   4.988   14.955  1.00 31.48 ?  129 ALA   A CB  1 
ATOM   978  N  N   . MET   A 1 130 ? 5.459   5.994   15.930  1.00 29.00 ?  130 MET   A N   1 
ATOM   979  C  CA  . MET   A 1 130 ? 6.275   5.829   17.126  1.00 30.42 ?  130 MET   A CA  1 
ATOM   980  C  C   . MET   A 1 130 ? 5.380   5.275   18.228  1.00 29.11 ?  130 MET   A C   1 
ATOM   981  O  O   . MET   A 1 130 ? 4.479   5.972   18.708  1.00 29.57 ?  130 MET   A O   1 
ATOM   982  C  CB  . MET   A 1 130 ? 6.891   7.168   17.530  1.00 27.00 ?  130 MET   A CB  1 
ATOM   983  C  CG  . MET   A 1 130 ? 7.766   7.131   18.787  1.00 28.84 ?  130 MET   A CG  1 
ATOM   984  S  SD  . MET   A 1 130 ? 9.142   5.989   18.598  1.00 34.61 ?  130 MET   A SD  1 
ATOM   985  C  CE  . MET   A 1 130 ? 10.003  6.701   17.181  1.00 30.46 ?  130 MET   A CE  1 
ATOM   986  N  N   . ARG   A 1 131 ? 5.591   4.013   18.605  1.00 32.16 ?  131 ARG   A N   1 
ATOM   987  C  CA  . ARG   A 1 131 ? 4.787   3.415   19.664  1.00 27.86 ?  131 ARG   A CA  1 
ATOM   988  C  C   . ARG   A 1 131 ? 5.043   4.133   20.989  1.00 29.06 ?  131 ARG   A C   1 
ATOM   989  O  O   . ARG   A 1 131 ? 6.070   4.796   21.162  1.00 28.88 ?  131 ARG   A O   1 
ATOM   990  C  CB  . ARG   A 1 131 ? 5.099   1.923   19.799  1.00 25.66 ?  131 ARG   A CB  1 
ATOM   991  C  CG  . ARG   A 1 131 ? 4.956   1.116   18.501  1.00 30.84 ?  131 ARG   A CG  1 
ATOM   992  C  CD  . ARG   A 1 131 ? 3.552   1.262   17.882  1.00 25.22 ?  131 ARG   A CD  1 
ATOM   993  N  NE  . ARG   A 1 131 ? 2.507   1.163   18.905  1.00 29.79 ?  131 ARG   A NE  1 
ATOM   994  C  CZ  . ARG   A 1 131 ? 1.208   1.268   18.650  1.00 30.25 ?  131 ARG   A CZ  1 
ATOM   995  N  NH1 . ARG   A 1 131 ? 0.793   1.464   17.403  1.00 25.69 ?  131 ARG   A NH1 1 
ATOM   996  N  NH2 . ARG   A 1 131 ? 0.323   1.176   19.632  1.00 29.44 ?  131 ARG   A NH2 1 
ATOM   997  N  N   . PRO   A 1 132 ? 4.107   4.032   21.940  1.00 28.75 ?  132 PRO   A N   1 
ATOM   998  C  CA  . PRO   A 1 132 ? 4.361   4.604   23.273  1.00 27.18 ?  132 PRO   A CA  1 
ATOM   999  C  C   . PRO   A 1 132 ? 5.629   4.084   23.927  1.00 28.19 ?  132 PRO   A C   1 
ATOM   1000 O  O   . PRO   A 1 132 ? 6.256   4.820   24.700  1.00 31.42 ?  132 PRO   A O   1 
ATOM   1001 C  CB  . PRO   A 1 132 ? 3.115   4.200   24.073  1.00 28.01 ?  132 PRO   A CB  1 
ATOM   1002 C  CG  . PRO   A 1 132 ? 2.049   4.061   23.053  1.00 24.71 ?  132 PRO   A CG  1 
ATOM   1003 C  CD  . PRO   A 1 132 ? 2.732   3.529   21.806  1.00 27.21 ?  132 PRO   A CD  1 
ATOM   1004 N  N   . ASN   A 1 133 ? 6.032   2.842   23.651  1.00 25.68 ?  133 ASN   A N   1 
ATOM   1005 C  CA  . ASN   A 1 133 ? 7.258   2.316   24.240  1.00 27.44 ?  133 ASN   A CA  1 
ATOM   1006 C  C   . ASN   A 1 133 ? 8.497   2.654   23.412  1.00 34.91 ?  133 ASN   A C   1 
ATOM   1007 O  O   . ASN   A 1 133 ? 9.553   2.047   23.627  1.00 29.36 ?  133 ASN   A O   1 
ATOM   1008 C  CB  . ASN   A 1 133 ? 7.154   0.799   24.447  1.00 29.88 ?  133 ASN   A CB  1 
ATOM   1009 C  CG  . ASN   A 1 133 ? 7.056   0.026   23.145  1.00 32.15 ?  133 ASN   A CG  1 
ATOM   1010 O  OD1 . ASN   A 1 133 ? 7.067   0.604   22.060  1.00 28.52 ?  133 ASN   A OD1 1 
ATOM   1011 N  ND2 . ASN   A 1 133 ? 6.991   -1.296  23.248  1.00 30.84 ?  133 ASN   A ND2 1 
ATOM   1012 N  N   . PHE   A 1 134 ? 8.368   3.585   22.462  1.00 30.39 ?  134 PHE   A N   1 
ATOM   1013 C  CA  . PHE   A 1 134 ? 9.493   4.148   21.716  1.00 32.18 ?  134 PHE   A CA  1 
ATOM   1014 C  C   . PHE   A 1 134 ? 10.139  3.137   20.782  1.00 32.70 ?  134 PHE   A C   1 
ATOM   1015 O  O   . PHE   A 1 134 ? 11.344  3.193   20.530  1.00 35.16 ?  134 PHE   A O   1 
ATOM   1016 C  CB  . PHE   A 1 134 ? 10.548  4.748   22.649  1.00 28.91 ?  134 PHE   A CB  1 
ATOM   1017 C  CG  . PHE   A 1 134 ? 10.067  5.949   23.396  1.00 31.49 ?  134 PHE   A CG  1 
ATOM   1018 C  CD1 . PHE   A 1 134 ? 9.918   7.162   22.745  1.00 30.41 ?  134 PHE   A CD1 1 
ATOM   1019 C  CD2 . PHE   A 1 134 ? 9.758   5.867   24.749  1.00 30.83 ?  134 PHE   A CD2 1 
ATOM   1020 C  CE1 . PHE   A 1 134 ? 9.468   8.279   23.421  1.00 38.45 ?  134 PHE   A CE1 1 
ATOM   1021 C  CE2 . PHE   A 1 134 ? 9.302   6.983   25.437  1.00 34.78 ?  134 PHE   A CE2 1 
ATOM   1022 C  CZ  . PHE   A 1 134 ? 9.156   8.192   24.769  1.00 33.70 ?  134 PHE   A CZ  1 
ATOM   1023 N  N   . THR   A 1 135 ? 9.352   2.208   20.262  1.00 30.43 ?  135 THR   A N   1 
ATOM   1024 C  CA  . THR   A 1 135 ? 9.775   1.377   19.152  1.00 30.66 ?  135 THR   A CA  1 
ATOM   1025 C  C   . THR   A 1 135 ? 8.856   1.673   17.979  1.00 30.89 ?  135 THR   A C   1 
ATOM   1026 O  O   . THR   A 1 135 ? 7.829   2.343   18.121  1.00 26.50 ?  135 THR   A O   1 
ATOM   1027 C  CB  . THR   A 1 135 ? 9.731   -0.113  19.509  1.00 29.85 ?  135 THR   A CB  1 
ATOM   1028 O  OG1 . THR   A 1 135 ? 8.365   -0.515  19.687  1.00 28.09 ?  135 THR   A OG1 1 
ATOM   1029 C  CG2 . THR   A 1 135 ? 10.494  -0.377  20.798  1.00 29.29 ?  135 THR   A CG2 1 
ATOM   1030 N  N   . ILE   A 1 136 ? 9.244   1.199   16.806  1.00 25.08 ?  136 ILE   A N   1 
ATOM   1031 C  CA  . ILE   A 1 136 ? 8.349   1.252   15.665  1.00 25.16 ?  136 ILE   A CA  1 
ATOM   1032 C  C   . ILE   A 1 136 ? 8.162   -0.171  15.166  1.00 27.14 ?  136 ILE   A C   1 
ATOM   1033 O  O   . ILE   A 1 136 ? 9.057   -1.013  15.274  1.00 27.64 ?  136 ILE   A O   1 
ATOM   1034 C  CB  . ILE   A 1 136 ? 8.864   2.186   14.547  1.00 32.35 ?  136 ILE   A CB  1 
ATOM   1035 C  CG1 . ILE   A 1 136 ? 10.097  1.600   13.862  1.00 28.36 ?  136 ILE   A CG1 1 
ATOM   1036 C  CG2 . ILE   A 1 136 ? 9.179   3.563   15.126  1.00 29.24 ?  136 ILE   A CG2 1 
ATOM   1037 C  CD1 . ILE   A 1 136 ? 10.577  2.438   12.685  1.00 31.64 ?  136 ILE   A CD1 1 
ATOM   1038 N  N   . LYS   A 1 137 ? 6.968   -0.453  14.666  1.00 29.32 ?  137 LYS   A N   1 
ATOM   1039 C  CA  . LYS   A 1 137 ? 6.680   -1.765  14.097  1.00 30.34 ?  137 LYS   A CA  1 
ATOM   1040 C  C   . LYS   A 1 137 ? 6.984   -1.652  12.612  1.00 31.88 ?  137 LYS   A C   1 
ATOM   1041 O  O   . LYS   A 1 137 ? 6.117   -1.343  11.799  1.00 30.59 ?  137 LYS   A O   1 
ATOM   1042 C  CB  . LYS   A 1 137 ? 5.238   -2.177  14.375  1.00 30.03 ?  137 LYS   A CB  1 
ATOM   1043 C  CG  . LYS   A 1 137 ? 4.903   -2.257  15.870  1.00 36.67 ?  137 LYS   A CG  1 
ATOM   1044 C  CD  . LYS   A 1 137 ? 3.867   -3.349  16.130  1.00 45.49 ?  137 LYS   A CD  1 
ATOM   1045 C  CE  . LYS   A 1 137 ? 3.010   -3.074  17.361  1.00 48.05 ?  137 LYS   A CE  1 
ATOM   1046 N  NZ  . LYS   A 1 137 ? 3.731   -3.213  18.665  1.00 47.44 ?  137 LYS   A NZ  1 
ATOM   1047 N  N   . GLY   A 1 138 ? 8.247   -1.864  12.258  1.00 27.86 ?  138 GLY   A N   1 
ATOM   1048 C  CA  . GLY   A 1 138 ? 8.711   -1.658  10.906  1.00 27.52 ?  138 GLY   A CA  1 
ATOM   1049 C  C   . GLY   A 1 138 ? 8.813   -2.951  10.121  1.00 27.41 ?  138 GLY   A C   1 
ATOM   1050 O  O   . GLY   A 1 138 ? 8.383   -4.022  10.555  1.00 27.82 ?  138 GLY   A O   1 
ATOM   1051 N  N   . SER   A 1 139 ? 9.386   -2.825  8.927   1.00 23.55 ?  139 SER   A N   1 
ATOM   1052 C  CA  . SER   A 1 139 ? 9.748   -3.953  8.079   1.00 24.98 ?  139 SER   A CA  1 
ATOM   1053 C  C   . SER   A 1 139 ? 11.175  -3.693  7.625   1.00 25.35 ?  139 SER   A C   1 
ATOM   1054 O  O   . SER   A 1 139 ? 11.405  -2.843  6.763   1.00 25.79 ?  139 SER   A O   1 
ATOM   1055 C  CB  . SER   A 1 139 ? 8.790   -4.087  6.889   1.00 25.40 ?  139 SER   A CB  1 
ATOM   1056 O  OG  . SER   A 1 139 ? 9.123   -5.214  6.096   1.00 29.58 ?  139 SER   A OG  1 
ATOM   1057 N  N   . PHE   A 1 140 ? 12.134  -4.384  8.239   1.00 30.53 ?  140 PHE   A N   1 
ATOM   1058 C  CA  . PHE   A 1 140 ? 13.548  -4.096  8.034   1.00 26.84 ?  140 PHE   A CA  1 
ATOM   1059 C  C   . PHE   A 1 140 ? 14.334  -5.393  8.069   1.00 28.21 ?  140 PHE   A C   1 
ATOM   1060 O  O   . PHE   A 1 140 ? 14.069  -6.260  8.906   1.00 33.45 ?  140 PHE   A O   1 
ATOM   1061 C  CB  . PHE   A 1 140 ? 14.104  -3.153  9.102   1.00 30.11 ?  140 PHE   A CB  1 
ATOM   1062 C  CG  . PHE   A 1 140 ? 13.656  -1.732  8.962   1.00 28.90 ?  140 PHE   A CG  1 
ATOM   1063 C  CD1 . PHE   A 1 140 ? 13.892  -1.034  7.789   1.00 27.94 ?  140 PHE   A CD1 1 
ATOM   1064 C  CD2 . PHE   A 1 140 ? 13.044  -1.077  10.025  1.00 29.66 ?  140 PHE   A CD2 1 
ATOM   1065 C  CE1 . PHE   A 1 140 ? 13.497  0.282   7.667   1.00 30.50 ?  140 PHE   A CE1 1 
ATOM   1066 C  CE2 . PHE   A 1 140 ? 12.644  0.242   9.912   1.00 30.16 ?  140 PHE   A CE2 1 
ATOM   1067 C  CZ  . PHE   A 1 140 ? 12.877  0.924   8.736   1.00 32.78 ?  140 PHE   A CZ  1 
ATOM   1068 N  N   . LEU   A 1 141 ? 15.312  -5.506  7.178   1.00 27.63 ?  141 LEU   A N   1 
ATOM   1069 C  CA  . LEU   A 1 141 ? 16.180  -6.669  7.077   1.00 29.63 ?  141 LEU   A CA  1 
ATOM   1070 C  C   . LEU   A 1 141 ? 17.626  -6.243  7.333   1.00 29.45 ?  141 LEU   A C   1 
ATOM   1071 O  O   . LEU   A 1 141 ? 17.919  -5.072  7.579   1.00 29.15 ?  141 LEU   A O   1 
ATOM   1072 C  CB  . LEU   A 1 141 ? 16.042  -7.331  5.702   1.00 30.33 ?  141 LEU   A CB  1 
ATOM   1073 C  CG  . LEU   A 1 141 ? 14.624  -7.697  5.247   1.00 33.26 ?  141 LEU   A CG  1 
ATOM   1074 C  CD1 . LEU   A 1 141 ? 14.605  -8.062  3.770   1.00 33.34 ?  141 LEU   A CD1 1 
ATOM   1075 C  CD2 . LEU   A 1 141 ? 14.073  -8.841  6.071   1.00 34.31 ?  141 LEU   A CD2 1 
ATOM   1076 N  N   . ASN   A 1 142 ? 18.542  -7.205  7.272   1.00 28.36 ?  142 ASN   A N   1 
ATOM   1077 C  CA  . ASN   A 1 142 ? 19.952  -6.854  7.340   1.00 29.67 ?  142 ASN   A CA  1 
ATOM   1078 C  C   . ASN   A 1 142 ? 20.295  -5.905  6.197   1.00 32.32 ?  142 ASN   A C   1 
ATOM   1079 O  O   . ASN   A 1 142 ? 19.934  -6.149  5.042   1.00 32.46 ?  142 ASN   A O   1 
ATOM   1080 C  CB  . ASN   A 1 142 ? 20.818  -8.110  7.280   1.00 34.34 ?  142 ASN   A CB  1 
ATOM   1081 C  CG  . ASN   A 1 142 ? 22.300  -7.797  7.378   1.00 34.83 ?  142 ASN   A CG  1 
ATOM   1082 O  OD1 . ASN   A 1 142 ? 23.096  -8.244  6.555   1.00 47.01 ?  142 ASN   A OD1 1 
ATOM   1083 N  ND2 . ASN   A 1 142 ? 22.672  -7.002  8.369   1.00 39.47 ?  142 ASN   A ND2 1 
ATOM   1084 N  N   . GLY   A 1 143 ? 20.951  -4.796  6.527   1.00 31.00 ?  143 GLY   A N   1 
ATOM   1085 C  CA  . GLY   A 1 143 ? 21.349  -3.817  5.537   1.00 30.02 ?  143 GLY   A CA  1 
ATOM   1086 C  C   . GLY   A 1 143 ? 20.492  -2.574  5.495   1.00 28.96 ?  143 GLY   A C   1 
ATOM   1087 O  O   . GLY   A 1 143 ? 20.804  -1.649  4.730   1.00 23.61 ?  143 GLY   A O   1 
ATOM   1088 N  N   . SER   A 1 144 ? 19.429  -2.520  6.299   1.00 23.53 ?  144 SER   A N   1 
ATOM   1089 C  CA  . SER   A 1 144 ? 18.480  -1.418  6.265   1.00 26.22 ?  144 SER   A CA  1 
ATOM   1090 C  C   . SER   A 1 144 ? 18.875  -0.253  7.155   1.00 26.89 ?  144 SER   A C   1 
ATOM   1091 O  O   . SER   A 1 144 ? 18.210  0.788   7.110   1.00 21.33 ?  144 SER   A O   1 
ATOM   1092 C  CB  . SER   A 1 144 ? 17.093  -1.906  6.682   1.00 27.16 ?  144 SER   A CB  1 
ATOM   1093 O  OG  . SER   A 1 144 ? 17.139  -2.480  7.976   1.00 29.68 ?  144 SER   A OG  1 
ATOM   1094 N  N   . CYS   A 1 145 ? 19.923  -0.396  7.967   1.00 25.64 ?  145 CYS   A N   1 
ATOM   1095 C  CA  . CYS   A 1 145 ? 20.263  0.665   8.901   1.00 25.45 ?  145 CYS   A CA  1 
ATOM   1096 C  C   . CYS   A 1 145 ? 20.620  1.927   8.132   1.00 24.71 ?  145 CYS   A C   1 
ATOM   1097 O  O   . CYS   A 1 145 ? 21.193  1.864   7.044   1.00 24.41 ?  145 CYS   A O   1 
ATOM   1098 C  CB  . CYS   A 1 145 ? 21.413  0.226   9.799   1.00 30.77 ?  145 CYS   A CB  1 
ATOM   1099 S  SG  . CYS   A 1 145 ? 20.964  -1.173  10.873  1.00 33.15 ?  145 CYS   A SG  1 
ATOM   1100 N  N   . GLY   A 1 146 ? 20.236  3.079   8.680   1.00 23.57 ?  146 GLY   A N   1 
ATOM   1101 C  CA  . GLY   A 1 146 ? 20.382  4.328   7.970   1.00 24.40 ?  146 GLY   A CA  1 
ATOM   1102 C  C   . GLY   A 1 146 ? 19.187  4.745   7.125   1.00 24.26 ?  146 GLY   A C   1 
ATOM   1103 O  O   . GLY   A 1 146 ? 19.157  5.891   6.661   1.00 21.19 ?  146 GLY   A O   1 
ATOM   1104 N  N   . SER   A 1 147 ? 18.210  3.861   6.903   1.00 24.11 ?  147 SER   A N   1 
ATOM   1105 C  CA  . SER   A 1 147 ? 16.933  4.297   6.338   1.00 24.80 ?  147 SER   A CA  1 
ATOM   1106 C  C   . SER   A 1 147 ? 16.301  5.347   7.244   1.00 27.20 ?  147 SER   A C   1 
ATOM   1107 O  O   . SER   A 1 147 ? 16.481  5.329   8.464   1.00 22.23 ?  147 SER   A O   1 
ATOM   1108 C  CB  . SER   A 1 147 ? 15.967  3.120   6.189   1.00 23.97 ?  147 SER   A CB  1 
ATOM   1109 O  OG  . SER   A 1 147 ? 16.505  2.088   5.393   1.00 26.90 ?  147 SER   A OG  1 
ATOM   1110 N  N   . VAL   A 1 148 ? 15.549  6.274   6.650   1.00 23.01 ?  148 VAL   A N   1 
ATOM   1111 C  CA  . VAL   A 1 148 ? 15.039  7.393   7.431   1.00 24.24 ?  148 VAL   A CA  1 
ATOM   1112 C  C   . VAL   A 1 148 ? 13.519  7.401   7.413   1.00 25.29 ?  148 VAL   A C   1 
ATOM   1113 O  O   . VAL   A 1 148 ? 12.878  6.837   6.530   1.00 22.60 ?  148 VAL   A O   1 
ATOM   1114 C  CB  . VAL   A 1 148 ? 15.585  8.752   6.950   1.00 26.09 ?  148 VAL   A CB  1 
ATOM   1115 C  CG1 . VAL   A 1 148 ? 17.105  8.838   7.191   1.00 28.58 ?  148 VAL   A CG1 1 
ATOM   1116 C  CG2 . VAL   A 1 148 ? 15.242  8.980   5.513   1.00 23.81 ?  148 VAL   A CG2 1 
ATOM   1117 N  N   . GLY   A 1 149 ? 12.952  8.030   8.443   1.00 26.73 ?  149 GLY   A N   1 
ATOM   1118 C  CA  . GLY   A 1 149 ? 11.536  8.327   8.503   1.00 23.18 ?  149 GLY   A CA  1 
ATOM   1119 C  C   . GLY   A 1 149 ? 11.345  9.829   8.426   1.00 24.86 ?  149 GLY   A C   1 
ATOM   1120 O  O   . GLY   A 1 149 ? 12.221  10.595  8.828   1.00 24.47 ?  149 GLY   A O   1 
ATOM   1121 N  N   . PHE   A 1 150 ? 10.208  10.260  7.887   1.00 25.73 ?  150 PHE   A N   1 
ATOM   1122 C  CA  . PHE   A 1 150 ? 10.074  11.679  7.591   1.00 22.42 ?  150 PHE   A CA  1 
ATOM   1123 C  C   . PHE   A 1 150 ? 8.603   12.048  7.501   1.00 25.70 ?  150 PHE   A C   1 
ATOM   1124 O  O   . PHE   A 1 150 ? 7.738   11.188  7.342   1.00 24.48 ?  150 PHE   A O   1 
ATOM   1125 C  CB  . PHE   A 1 150 ? 10.801  12.041  6.286   1.00 25.25 ?  150 PHE   A CB  1 
ATOM   1126 C  CG  . PHE   A 1 150 ? 10.270  11.321  5.077   1.00 26.36 ?  150 PHE   A CG  1 
ATOM   1127 C  CD1 . PHE   A 1 150 ? 10.630  10.007  4.815   1.00 29.21 ?  150 PHE   A CD1 1 
ATOM   1128 C  CD2 . PHE   A 1 150 ? 9.412   11.961  4.201   1.00 25.65 ?  150 PHE   A CD2 1 
ATOM   1129 C  CE1 . PHE   A 1 150 ? 10.134  9.345   3.696   1.00 26.70 ?  150 PHE   A CE1 1 
ATOM   1130 C  CE2 . PHE   A 1 150 ? 8.908   11.306  3.085   1.00 26.43 ?  150 PHE   A CE2 1 
ATOM   1131 C  CZ  . PHE   A 1 150 ? 9.270   9.997   2.833   1.00 28.57 ?  150 PHE   A CZ  1 
ATOM   1132 N  N   . ASN   A 1 151 ? 8.343   13.347  7.625   1.00 27.40 ?  151 ASN   A N   1 
ATOM   1133 C  CA  . ASN   A 1 151 ? 7.068   13.959  7.279   1.00 30.31 ?  151 ASN   A CA  1 
ATOM   1134 C  C   . ASN   A 1 151 ? 7.338   15.112  6.320   1.00 35.32 ?  151 ASN   A C   1 
ATOM   1135 O  O   . ASN   A 1 151 ? 8.472   15.581  6.188   1.00 29.81 ?  151 ASN   A O   1 
ATOM   1136 C  CB  . ASN   A 1 151 ? 6.317   14.484  8.520   1.00 28.11 ?  151 ASN   A CB  1 
ATOM   1137 C  CG  . ASN   A 1 151 ? 5.761   13.369  9.397   1.00 33.66 ?  151 ASN   A CG  1 
ATOM   1138 O  OD1 . ASN   A 1 151 ? 4.738   12.764  9.076   1.00 32.27 ?  151 ASN   A OD1 1 
ATOM   1139 N  ND2 . ASN   A 1 151 ? 6.415   13.116  10.524  1.00 29.20 ?  151 ASN   A ND2 1 
ATOM   1140 N  N   . ILE   A 1 152 ? 6.288   15.583  5.650   1.00 33.20 ?  152 ILE   A N   1 
ATOM   1141 C  CA  . ILE   A 1 152 ? 6.378   16.777  4.817   1.00 36.03 ?  152 ILE   A CA  1 
ATOM   1142 C  C   . ILE   A 1 152 ? 5.329   17.771  5.288   1.00 44.48 ?  152 ILE   A C   1 
ATOM   1143 O  O   . ILE   A 1 152 ? 4.160   17.410  5.467   1.00 44.56 ?  152 ILE   A O   1 
ATOM   1144 C  CB  . ILE   A 1 152 ? 6.202   16.455  3.324   1.00 36.77 ?  152 ILE   A CB  1 
ATOM   1145 C  CG1 . ILE   A 1 152 ? 7.277   15.465  2.873   1.00 33.02 ?  152 ILE   A CG1 1 
ATOM   1146 C  CG2 . ILE   A 1 152 ? 6.312   17.723  2.505   1.00 43.75 ?  152 ILE   A CG2 1 
ATOM   1147 C  CD1 . ILE   A 1 152 ? 6.870   14.637  1.700   1.00 34.83 ?  152 ILE   A CD1 1 
ATOM   1148 N  N   . ASP   A 1 153 ? 5.754   19.013  5.517   1.00 48.66 ?  153 ASP   A N   1 
ATOM   1149 C  CA  . ASP   A 1 153 ? 4.867   20.093  5.941   1.00 48.20 ?  153 ASP   A CA  1 
ATOM   1150 C  C   . ASP   A 1 153 ? 5.173   21.304  5.073   1.00 53.11 ?  153 ASP   A C   1 
ATOM   1151 O  O   . ASP   A 1 153 ? 6.243   21.909  5.202   1.00 53.93 ?  153 ASP   A O   1 
ATOM   1152 C  CB  . ASP   A 1 153 ? 5.050   20.414  7.426   1.00 46.97 ?  153 ASP   A CB  1 
ATOM   1153 N  N   . TYR   A 1 154 ? 4.245   21.651  4.182   1.00 52.00 ?  154 TYR   A N   1 
ATOM   1154 C  CA  . TYR   A 1 154 ? 4.508   22.686  3.191   1.00 50.13 ?  154 TYR   A CA  1 
ATOM   1155 C  C   . TYR   A 1 154 ? 5.503   22.177  2.157   1.00 53.81 ?  154 TYR   A C   1 
ATOM   1156 O  O   . TYR   A 1 154 ? 5.282   21.134  1.536   1.00 53.75 ?  154 TYR   A O   1 
ATOM   1157 N  N   . ASP   A 1 155 ? 6.603   22.904  1.969   1.00 50.94 ?  155 ASP   A N   1 
ATOM   1158 C  CA  . ASP   A 1 155 ? 7.638   22.547  1.006   1.00 52.86 ?  155 ASP   A CA  1 
ATOM   1159 C  C   . ASP   A 1 155 ? 8.787   21.766  1.632   1.00 44.36 ?  155 ASP   A C   1 
ATOM   1160 O  O   . ASP   A 1 155 ? 9.711   21.359  0.915   1.00 50.10 ?  155 ASP   A O   1 
ATOM   1161 C  CB  . ASP   A 1 155 ? 8.195   23.812  0.338   1.00 51.11 ?  155 ASP   A CB  1 
ATOM   1162 N  N   . CYS   A 1 156 ? 8.733   21.522  2.935   1.00 46.23 ?  156 CYS   A N   1 
ATOM   1163 C  CA  . CYS   A 1 156 ? 9.894   21.131  3.716   1.00 38.22 ?  156 CYS   A CA  1 
ATOM   1164 C  C   . CYS   A 1 156 ? 9.787   19.687  4.186   1.00 38.17 ?  156 CYS   A C   1 
ATOM   1165 O  O   . CYS   A 1 156 ? 8.736   19.258  4.668   1.00 36.23 ?  156 CYS   A O   1 
ATOM   1166 C  CB  . CYS   A 1 156 ? 10.036  22.069  4.910   1.00 42.51 ?  156 CYS   A CB  1 
ATOM   1167 S  SG  . CYS   A 1 156 ? 11.296  21.626  6.091   1.00 48.24 ?  156 CYS   A SG  1 
ATOM   1168 N  N   . VAL   A 1 157 ? 10.883  18.944  4.048   1.00 36.05 ?  157 VAL   A N   1 
ATOM   1169 C  CA  . VAL   A 1 157 ? 10.977  17.577  4.552   1.00 33.85 ?  157 VAL   A CA  1 
ATOM   1170 C  C   . VAL   A 1 157 ? 11.422  17.623  6.010   1.00 31.65 ?  157 VAL   A C   1 
ATOM   1171 O  O   . VAL   A 1 157 ? 12.492  18.150  6.324   1.00 31.18 ?  157 VAL   A O   1 
ATOM   1172 C  CB  . VAL   A 1 157 ? 11.956  16.739  3.719   1.00 32.48 ?  157 VAL   A CB  1 
ATOM   1173 C  CG1 . VAL   A 1 157 ? 12.109  15.350  4.335   1.00 31.80 ?  157 VAL   A CG1 1 
ATOM   1174 C  CG2 . VAL   A 1 157 ? 11.498  16.645  2.291   1.00 31.63 ?  157 VAL   A CG2 1 
ATOM   1175 N  N   . SER   A 1 158 ? 10.626  17.050  6.900   1.00 27.79 ?  158 SER   A N   1 
ATOM   1176 C  CA  . SER   A 1 158 ? 10.993  16.957  8.310   1.00 30.73 ?  158 SER   A CA  1 
ATOM   1177 C  C   . SER   A 1 158 ? 11.480  15.542  8.592   1.00 27.63 ?  158 SER   A C   1 
ATOM   1178 O  O   . SER   A 1 158 ? 10.679  14.616  8.735   1.00 27.16 ?  158 SER   A O   1 
ATOM   1179 C  CB  . SER   A 1 158 ? 9.815   17.329  9.203   1.00 33.91 ?  158 SER   A CB  1 
ATOM   1180 O  OG  . SER   A 1 158 ? 9.740   18.735  9.368   1.00 40.32 ?  158 SER   A OG  1 
ATOM   1181 N  N   . PHE   A 1 159 ? 12.798  15.375  8.679   1.00 29.38 ?  159 PHE   A N   1 
ATOM   1182 C  CA  . PHE   A 1 159 ? 13.373  14.085  9.032   1.00 25.61 ?  159 PHE   A CA  1 
ATOM   1183 C  C   . PHE   A 1 159 ? 13.267  13.888  10.536  1.00 27.00 ?  159 PHE   A C   1 
ATOM   1184 O  O   . PHE   A 1 159 ? 13.663  14.765  11.309  1.00 27.63 ?  159 PHE   A O   1 
ATOM   1185 C  CB  . PHE   A 1 159 ? 14.840  13.998  8.605   1.00 26.58 ?  159 PHE   A CB  1 
ATOM   1186 C  CG  . PHE   A 1 159 ? 15.054  14.034  7.119   1.00 26.41 ?  159 PHE   A CG  1 
ATOM   1187 C  CD1 . PHE   A 1 159 ? 14.870  12.897  6.354   1.00 24.81 ?  159 PHE   A CD1 1 
ATOM   1188 C  CD2 . PHE   A 1 159 ? 15.470  15.198  6.495   1.00 28.49 ?  159 PHE   A CD2 1 
ATOM   1189 C  CE1 . PHE   A 1 159 ? 15.083  12.927  4.990   1.00 26.67 ?  159 PHE   A CE1 1 
ATOM   1190 C  CE2 . PHE   A 1 159 ? 15.693  15.228  5.125   1.00 27.82 ?  159 PHE   A CE2 1 
ATOM   1191 C  CZ  . PHE   A 1 159 ? 15.501  14.093  4.377   1.00 26.51 ?  159 PHE   A CZ  1 
ATOM   1192 N  N   . CYS   A 1 160 ? 12.747  12.732  10.952  1.00 28.41 ?  160 CYS   A N   1 
ATOM   1193 C  CA  . CYS   A 1 160 ? 12.527  12.465  12.367  1.00 24.35 ?  160 CYS   A CA  1 
ATOM   1194 C  C   . CYS   A 1 160 ? 13.078  11.138  12.857  1.00 26.13 ?  160 CYS   A C   1 
ATOM   1195 O  O   . CYS   A 1 160 ? 13.072  10.908  14.075  1.00 27.63 ?  160 CYS   A O   1 
ATOM   1196 C  CB  . CYS   A 1 160 ? 11.024  12.502  12.694  1.00 27.29 ?  160 CYS   A CB  1 
ATOM   1197 S  SG  . CYS   A 1 160 ? 10.042  11.331  11.738  1.00 30.13 ?  160 CYS   A SG  1 
ATOM   1198 N  N   . TYR   A 1 161 ? 13.517  10.250  11.974  1.00 26.26 ?  161 TYR   A N   1 
ATOM   1199 C  CA  . TYR   A 1 161 ? 13.935  8.923   12.398  1.00 24.37 ?  161 TYR   A CA  1 
ATOM   1200 C  C   . TYR   A 1 161 ? 15.047  8.434   11.490  1.00 26.56 ?  161 TYR   A C   1 
ATOM   1201 O  O   . TYR   A 1 161 ? 14.978  8.603   10.268  1.00 24.59 ?  161 TYR   A O   1 
ATOM   1202 C  CB  . TYR   A 1 161 ? 12.763  7.935   12.372  1.00 23.09 ?  161 TYR   A CB  1 
ATOM   1203 C  CG  . TYR   A 1 161 ? 13.115  6.516   12.772  1.00 23.75 ?  161 TYR   A CG  1 
ATOM   1204 C  CD1 . TYR   A 1 161 ? 13.211  6.156   14.116  1.00 25.03 ?  161 TYR   A CD1 1 
ATOM   1205 C  CD2 . TYR   A 1 161 ? 13.339  5.532   11.812  1.00 22.19 ?  161 TYR   A CD2 1 
ATOM   1206 C  CE1 . TYR   A 1 161 ? 13.522  4.863   14.489  1.00 23.09 ?  161 TYR   A CE1 1 
ATOM   1207 C  CE2 . TYR   A 1 161 ? 13.650  4.234   12.172  1.00 19.74 ?  161 TYR   A CE2 1 
ATOM   1208 C  CZ  . TYR   A 1 161 ? 13.737  3.905   13.518  1.00 23.06 ?  161 TYR   A CZ  1 
ATOM   1209 O  OH  . TYR   A 1 161 ? 14.046  2.615   13.898  1.00 24.45 ?  161 TYR   A OH  1 
ATOM   1210 N  N   . MET   A 1 162 ? 16.084  7.857   12.097  1.00 23.15 ?  162 MET   A N   1 
ATOM   1211 C  CA  . MET   A 1 162 ? 17.088  7.071   11.393  1.00 22.98 ?  162 MET   A CA  1 
ATOM   1212 C  C   . MET   A 1 162 ? 17.128  5.694   12.037  1.00 21.09 ?  162 MET   A C   1 
ATOM   1213 O  O   . MET   A 1 162 ? 17.134  5.582   13.264  1.00 24.51 ?  162 MET   A O   1 
ATOM   1214 C  CB  . MET   A 1 162 ? 18.477  7.738   11.432  1.00 25.13 ?  162 MET   A CB  1 
ATOM   1215 C  CG  . MET   A 1 162 ? 19.584  6.913   10.784  1.00 27.81 ?  162 MET   A CG  1 
ATOM   1216 S  SD  . MET   A 1 162 ? 21.108  7.855   10.442  1.00 33.31 ?  162 MET   A SD  1 
ATOM   1217 C  CE  . MET   A 1 162 ? 20.738  8.450   8.787   1.00 29.63 ?  162 MET   A CE  1 
ATOM   1218 N  N   . HIS   A 1 163 ? 17.148  4.652   11.213  1.00 21.84 ?  163 HIS   A N   1 
ATOM   1219 C  CA  . HIS   A 1 163 ? 17.008  3.285   11.700  1.00 23.10 ?  163 HIS   A CA  1 
ATOM   1220 C  C   . HIS   A 1 163 ? 18.355  2.739   12.164  1.00 25.30 ?  163 HIS   A C   1 
ATOM   1221 O  O   . HIS   A 1 163 ? 19.363  2.907   11.476  1.00 24.03 ?  163 HIS   A O   1 
ATOM   1222 C  CB  . HIS   A 1 163 ? 16.426  2.393   10.597  1.00 22.74 ?  163 HIS   A CB  1 
ATOM   1223 C  CG  . HIS   A 1 163 ? 16.221  0.975   11.027  1.00 23.36 ?  163 HIS   A CG  1 
ATOM   1224 N  ND1 . HIS   A 1 163 ? 15.591  0.647   12.206  1.00 23.28 ?  163 HIS   A ND1 1 
ATOM   1225 C  CD2 . HIS   A 1 163 ? 16.590  -0.197  10.459  1.00 23.69 ?  163 HIS   A CD2 1 
ATOM   1226 C  CE1 . HIS   A 1 163 ? 15.560  -0.666  12.338  1.00 23.37 ?  163 HIS   A CE1 1 
ATOM   1227 N  NE2 . HIS   A 1 163 ? 16.163  -1.203  11.295  1.00 24.39 ?  163 HIS   A NE2 1 
ATOM   1228 N  N   . HIS   A 1 164 ? 18.375  2.084   13.335  1.00 27.30 ?  164 HIS   A N   1 
ATOM   1229 C  CA  . HIS   A 1 164 ? 19.601  1.495   13.864  1.00 25.32 ?  164 HIS   A CA  1 
ATOM   1230 C  C   . HIS   A 1 164 ? 19.522  0.001   14.152  1.00 28.23 ?  164 HIS   A C   1 
ATOM   1231 O  O   . HIS   A 1 164 ? 20.535  -0.680  13.992  1.00 32.19 ?  164 HIS   A O   1 
ATOM   1232 C  CB  . HIS   A 1 164 ? 20.043  2.194   15.162  1.00 24.43 ?  164 HIS   A CB  1 
ATOM   1233 C  CG  . HIS   A 1 164 ? 20.548  3.589   14.967  1.00 23.92 ?  164 HIS   A CG  1 
ATOM   1234 N  ND1 . HIS   A 1 164 ? 21.835  3.964   15.290  1.00 26.13 ?  164 HIS   A ND1 1 
ATOM   1235 C  CD2 . HIS   A 1 164 ? 19.935  4.704   14.507  1.00 25.55 ?  164 HIS   A CD2 1 
ATOM   1236 C  CE1 . HIS   A 1 164 ? 21.996  5.249   15.022  1.00 26.69 ?  164 HIS   A CE1 1 
ATOM   1237 N  NE2 . HIS   A 1 164 ? 20.859  5.720   14.542  1.00 25.76 ?  164 HIS   A NE2 1 
ATOM   1238 N  N   . MET   A 1 165 ? 18.380  -0.539  14.584  1.00 24.25 ?  165 MET   A N   1 
ATOM   1239 C  CA  . MET   A 1 165 ? 18.428  -1.928  15.032  1.00 28.46 ?  165 MET   A CA  1 
ATOM   1240 C  C   . MET   A 1 165 ? 17.049  -2.560  15.124  1.00 25.22 ?  165 MET   A C   1 
ATOM   1241 O  O   . MET   A 1 165 ? 16.024  -1.878  15.195  1.00 23.67 ?  165 MET   A O   1 
ATOM   1242 C  CB  . MET   A 1 165 ? 19.099  -2.038  16.399  1.00 29.41 ?  165 MET   A CB  1 
ATOM   1243 C  CG  . MET   A 1 165 ? 18.197  -1.586  17.505  1.00 30.19 ?  165 MET   A CG  1 
ATOM   1244 S  SD  . MET   A 1 165 ? 19.110  -1.508  19.061  1.00 42.99 ?  165 MET   A SD  1 
ATOM   1245 C  CE  . MET   A 1 165 ? 18.436  -0.018  19.719  1.00 34.73 ?  165 MET   A CE  1 
ATOM   1246 N  N   . GLU   A 1 166 ? 17.061  -3.889  15.198  1.00 26.11 ?  166 GLU   A N   1 
ATOM   1247 C  CA  . GLU   A 1 166 ? 15.877  -4.698  15.431  1.00 27.92 ?  166 GLU   A CA  1 
ATOM   1248 C  C   . GLU   A 1 166 ? 15.999  -5.412  16.769  1.00 29.60 ?  166 GLU   A C   1 
ATOM   1249 O  O   . GLU   A 1 166 ? 17.011  -6.068  17.033  1.00 30.95 ?  166 GLU   A O   1 
ATOM   1250 C  CB  . GLU   A 1 166 ? 15.693  -5.728  14.319  1.00 29.09 ?  166 GLU   A CB  1 
ATOM   1251 C  CG  . GLU   A 1 166 ? 14.388  -6.513  14.416  1.00 27.74 ?  166 GLU   A CG  1 
ATOM   1252 C  CD  . GLU   A 1 166 ? 14.172  -7.377  13.188  1.00 32.42 ?  166 GLU   A CD  1 
ATOM   1253 O  OE1 . GLU   A 1 166 ? 14.229  -8.619  13.307  1.00 32.80 ?  166 GLU   A OE1 1 
ATOM   1254 O  OE2 . GLU   A 1 166 ? 13.979  -6.806  12.094  1.00 30.55 ?  166 GLU   A OE2 1 
ATOM   1255 N  N   . LEU   A 1 167 ? 14.959  -5.304  17.593  1.00 29.21 ?  167 LEU   A N   1 
ATOM   1256 C  CA  . LEU   A 1 167 ? 14.917  -5.923  18.907  1.00 29.55 ?  167 LEU   A CA  1 
ATOM   1257 C  C   . LEU   A 1 167 ? 14.456  -7.376  18.797  1.00 36.40 ?  167 LEU   A C   1 
ATOM   1258 O  O   . LEU   A 1 167 ? 13.947  -7.793  17.756  1.00 33.08 ?  167 LEU   A O   1 
ATOM   1259 C  CB  . LEU   A 1 167 ? 13.991  -5.118  19.815  1.00 26.76 ?  167 LEU   A CB  1 
ATOM   1260 C  CG  . LEU   A 1 167 ? 14.523  -3.716  20.122  1.00 33.73 ?  167 LEU   A CG  1 
ATOM   1261 C  CD1 . LEU   A 1 167 ? 13.417  -2.798  20.618  1.00 31.53 ?  167 LEU   A CD1 1 
ATOM   1262 C  CD2 . LEU   A 1 167 ? 15.694  -3.760  21.127  1.00 35.30 ?  167 LEU   A CD2 1 
ATOM   1263 N  N   . PRO   A 1 168 ? 14.639  -8.175  19.856  1.00 35.36 ?  168 PRO   A N   1 
ATOM   1264 C  CA  . PRO   A 1 168 ? 14.314  -9.611  19.755  1.00 37.95 ?  168 PRO   A CA  1 
ATOM   1265 C  C   . PRO   A 1 168 ? 12.883  -9.909  19.348  1.00 36.61 ?  168 PRO   A C   1 
ATOM   1266 O  O   . PRO   A 1 168 ? 12.647  -10.907 18.657  1.00 38.85 ?  168 PRO   A O   1 
ATOM   1267 C  CB  . PRO   A 1 168 ? 14.601  -10.127 21.173  1.00 35.27 ?  168 PRO   A CB  1 
ATOM   1268 C  CG  . PRO   A 1 168 ? 15.660  -9.241  21.663  1.00 32.29 ?  168 PRO   A CG  1 
ATOM   1269 C  CD  . PRO   A 1 168 ? 15.364  -7.877  21.106  1.00 38.00 ?  168 PRO   A CD  1 
ATOM   1270 N  N   . THR   A 1 169 ? 11.917  -9.087  19.763  1.00 37.51 ?  169 THR   A N   1 
ATOM   1271 C  CA  . THR   A 1 169 ? 10.526  -9.287  19.368  1.00 40.52 ?  169 THR   A CA  1 
ATOM   1272 C  C   . THR   A 1 169 ? 10.247  -8.881  17.927  1.00 37.58 ?  169 THR   A C   1 
ATOM   1273 O  O   . THR   A 1 169 ? 9.103   -9.008  17.476  1.00 38.56 ?  169 THR   A O   1 
ATOM   1274 C  CB  . THR   A 1 169 ? 9.604   -8.510  20.304  1.00 38.62 ?  169 THR   A CB  1 
ATOM   1275 O  OG1 . THR   A 1 169 ? 10.068  -7.159  20.395  1.00 41.83 ?  169 THR   A OG1 1 
ATOM   1276 C  CG2 . THR   A 1 169 ? 9.588   -9.143  21.703  1.00 42.32 ?  169 THR   A CG2 1 
ATOM   1277 N  N   . GLY   A 1 170 ? 11.246  -8.404  17.192  1.00 35.58 ?  170 GLY   A N   1 
ATOM   1278 C  CA  . GLY   A 1 170 ? 11.058  -8.070  15.799  1.00 33.44 ?  170 GLY   A CA  1 
ATOM   1279 C  C   . GLY   A 1 170 ? 10.664  -6.635  15.545  1.00 34.84 ?  170 GLY   A C   1 
ATOM   1280 O  O   . GLY   A 1 170 ? 10.498  -6.253  14.381  1.00 34.61 ?  170 GLY   A O   1 
ATOM   1281 N  N   . VAL   A 1 171 ? 10.487  -5.829  16.592  1.00 30.82 ?  171 VAL   A N   1 
ATOM   1282 C  CA  . VAL   A 1 171 ? 10.233  -4.401  16.421  1.00 29.23 ?  171 VAL   A CA  1 
ATOM   1283 C  C   . VAL   A 1 171 ? 11.563  -3.669  16.317  1.00 29.71 ?  171 VAL   A C   1 
ATOM   1284 O  O   . VAL   A 1 171 ? 12.632  -4.288  16.395  1.00 29.03 ?  171 VAL   A O   1 
ATOM   1285 C  CB  . VAL   A 1 171 ? 9.371   -3.838  17.564  1.00 30.17 ?  171 VAL   A CB  1 
ATOM   1286 C  CG1 . VAL   A 1 171 ? 7.991   -4.475  17.560  1.00 33.58 ?  171 VAL   A CG1 1 
ATOM   1287 C  CG2 . VAL   A 1 171 ? 10.078  -4.061  18.902  1.00 29.26 ?  171 VAL   A CG2 1 
ATOM   1288 N  N   . HIS   A 1 172 ? 11.511  -2.349  16.165  1.00 28.55 ?  172 HIS   A N   1 
ATOM   1289 C  CA  . HIS   A 1 172 ? 12.666  -1.612  15.680  1.00 28.05 ?  172 HIS   A CA  1 
ATOM   1290 C  C   . HIS   A 1 172 ? 12.885  -0.354  16.502  1.00 27.34 ?  172 HIS   A C   1 
ATOM   1291 O  O   . HIS   A 1 172 ? 11.951  0.188   17.095  1.00 24.35 ?  172 HIS   A O   1 
ATOM   1292 C  CB  . HIS   A 1 172 ? 12.497  -1.280  14.179  1.00 26.90 ?  172 HIS   A CB  1 
ATOM   1293 C  CG  . HIS   A 1 172 ? 12.348  -2.501  13.325  1.00 27.79 ?  172 HIS   A CG  1 
ATOM   1294 N  ND1 . HIS   A 1 172 ? 11.135  -2.910  12.816  1.00 25.54 ?  172 HIS   A ND1 1 
ATOM   1295 C  CD2 . HIS   A 1 172 ? 13.252  -3.434  12.943  1.00 26.24 ?  172 HIS   A CD2 1 
ATOM   1296 C  CE1 . HIS   A 1 172 ? 11.301  -4.036  12.148  1.00 27.98 ?  172 HIS   A CE1 1 
ATOM   1297 N  NE2 . HIS   A 1 172 ? 12.576  -4.374  12.206  1.00 28.34 ?  172 HIS   A NE2 1 
ATOM   1298 N  N   . ALA   A 1 173 ? 14.142  0.096   16.539  1.00 26.97 ?  173 ALA   A N   1 
ATOM   1299 C  CA  . ALA   A 1 173 ? 14.545  1.237   17.349  1.00 20.55 ?  173 ALA   A CA  1 
ATOM   1300 C  C   . ALA   A 1 173 ? 15.581  2.050   16.588  1.00 21.93 ?  173 ALA   A C   1 
ATOM   1301 O  O   . ALA   A 1 173 ? 16.360  1.511   15.802  1.00 24.63 ?  173 ALA   A O   1 
ATOM   1302 C  CB  . ALA   A 1 173 ? 15.109  0.797   18.713  1.00 25.82 ?  173 ALA   A CB  1 
ATOM   1303 N  N   . GLY   A 1 174 ? 15.554  3.355   16.808  1.00 21.80 ?  174 GLY   A N   1 
ATOM   1304 C  CA  . GLY   A 1 174 ? 16.493  4.241   16.165  1.00 19.40 ?  174 GLY   A CA  1 
ATOM   1305 C  C   . GLY   A 1 174 ? 16.514  5.595   16.833  1.00 23.69 ?  174 GLY   A C   1 
ATOM   1306 O  O   . GLY   A 1 174 ? 16.029  5.760   17.952  1.00 26.61 ?  174 GLY   A O   1 
ATOM   1307 N  N   . THR   A 1 175 ? 17.064  6.568   16.122  1.00 21.21 ?  175 THR   A N   1 
ATOM   1308 C  CA  . THR   A 1 175 ? 17.402  7.868   16.673  1.00 21.08 ?  175 THR   A CA  1 
ATOM   1309 C  C   . THR   A 1 175 ? 16.716  8.962   15.879  1.00 22.14 ?  175 THR   A C   1 
ATOM   1310 O  O   . THR   A 1 175 ? 16.218  8.738   14.773  1.00 23.40 ?  175 THR   A O   1 
ATOM   1311 C  CB  . THR   A 1 175 ? 18.925  8.095   16.638  1.00 21.10 ?  175 THR   A CB  1 
ATOM   1312 O  OG1 . THR   A 1 175 ? 19.376  8.148   15.272  1.00 25.03 ?  175 THR   A OG1 1 
ATOM   1313 C  CG2 . THR   A 1 175 ? 19.632  6.974   17.350  1.00 24.19 ?  175 THR   A CG2 1 
ATOM   1314 N  N   . ASP   A 1 176 ? 16.711  10.167  16.443  1.00 21.08 ?  176 ASP   A N   1 
ATOM   1315 C  CA  . ASP   A 1 176 ? 16.456  11.327  15.611  1.00 26.40 ?  176 ASP   A CA  1 
ATOM   1316 C  C   . ASP   A 1 176 ? 17.714  11.654  14.811  1.00 26.80 ?  176 ASP   A C   1 
ATOM   1317 O  O   . ASP   A 1 176 ? 18.729  10.954  14.879  1.00 26.10 ?  176 ASP   A O   1 
ATOM   1318 C  CB  . ASP   A 1 176 ? 15.975  12.515  16.446  1.00 25.91 ?  176 ASP   A CB  1 
ATOM   1319 C  CG  . ASP   A 1 176 ? 16.917  12.873  17.574  1.00 28.92 ?  176 ASP   A CG  1 
ATOM   1320 O  OD1 . ASP   A 1 176 ? 18.103  12.509  17.493  1.00 31.97 ?  176 ASP   A OD1 1 
ATOM   1321 O  OD2 . ASP   A 1 176 ? 16.451  13.512  18.552  1.00 30.68 ?  176 ASP   A OD2 1 
ATOM   1322 N  N   . LEU   A 1 177 ? 17.657  12.725  14.033  1.00 28.22 ?  177 LEU   A N   1 
ATOM   1323 C  CA  . LEU   A 1 177 ? 18.811  13.048  13.207  1.00 31.25 ?  177 LEU   A CA  1 
ATOM   1324 C  C   . LEU   A 1 177 ? 19.892  13.763  13.998  1.00 30.77 ?  177 LEU   A C   1 
ATOM   1325 O  O   . LEU   A 1 177 ? 20.946  14.074  13.435  1.00 30.39 ?  177 LEU   A O   1 
ATOM   1326 C  CB  . LEU   A 1 177 ? 18.383  13.872  11.991  1.00 28.78 ?  177 LEU   A CB  1 
ATOM   1327 C  CG  . LEU   A 1 177 ? 18.045  13.033  10.752  1.00 26.17 ?  177 LEU   A CG  1 
ATOM   1328 C  CD1 . LEU   A 1 177 ? 19.299  12.360  10.225  1.00 26.87 ?  177 LEU   A CD1 1 
ATOM   1329 C  CD2 . LEU   A 1 177 ? 16.960  11.993  11.072  1.00 28.77 ?  177 LEU   A CD2 1 
ATOM   1330 N  N   . GLU   A 1 178 ? 19.642  14.026  15.284  1.00 33.25 ?  178 GLU   A N   1 
ATOM   1331 C  CA  . GLU   A 1 178 ? 20.662  14.414  16.249  1.00 28.78 ?  178 GLU   A CA  1 
ATOM   1332 C  C   . GLU   A 1 178 ? 21.448  13.232  16.779  1.00 28.65 ?  178 GLU   A C   1 
ATOM   1333 O  O   . GLU   A 1 178 ? 22.425  13.437  17.504  1.00 30.73 ?  178 GLU   A O   1 
ATOM   1334 C  CB  . GLU   A 1 178 ? 20.027  15.106  17.455  1.00 39.21 ?  178 GLU   A CB  1 
ATOM   1335 C  CG  . GLU   A 1 178 ? 20.027  16.603  17.445  1.00 42.21 ?  178 GLU   A CG  1 
ATOM   1336 C  CD  . GLU   A 1 178 ? 19.354  17.151  18.681  1.00 40.56 ?  178 GLU   A CD  1 
ATOM   1337 O  OE1 . GLU   A 1 178 ? 19.965  17.086  19.775  1.00 48.92 ?  178 GLU   A OE1 1 
ATOM   1338 O  OE2 . GLU   A 1 178 ? 18.203  17.623  18.563  1.00 49.32 ?  178 GLU   A OE2 1 
ATOM   1339 N  N   . GLY   A 1 179 ? 21.021  12.009  16.488  1.00 24.90 ?  179 GLY   A N   1 
ATOM   1340 C  CA  . GLY   A 1 179 ? 21.671  10.840  17.037  1.00 25.19 ?  179 GLY   A CA  1 
ATOM   1341 C  C   . GLY   A 1 179 ? 21.195  10.398  18.406  1.00 25.41 ?  179 GLY   A C   1 
ATOM   1342 O  O   . GLY   A 1 179 ? 21.771  9.455   18.964  1.00 27.79 ?  179 GLY   A O   1 
ATOM   1343 N  N   . ASN   A 1 180 ? 20.168  11.030  18.970  1.00 28.47 ?  180 ASN   A N   1 
ATOM   1344 C  CA  . ASN   A 1 180 ? 19.632  10.611  20.262  1.00 26.87 ?  180 ASN   A CA  1 
ATOM   1345 C  C   . ASN   A 1 180 ? 18.552  9.563   20.035  1.00 25.09 ?  180 ASN   A C   1 
ATOM   1346 O  O   . ASN   A 1 180 ? 17.588  9.800   19.301  1.00 27.03 ?  180 ASN   A O   1 
ATOM   1347 C  CB  . ASN   A 1 180 ? 19.080  11.800  21.049  1.00 27.88 ?  180 ASN   A CB  1 
ATOM   1348 C  CG  . ASN   A 1 180 ? 20.177  12.681  21.612  1.00 32.20 ?  180 ASN   A CG  1 
ATOM   1349 O  OD1 . ASN   A 1 180 ? 21.213  12.187  22.055  1.00 29.67 ?  180 ASN   A OD1 1 
ATOM   1350 N  ND2 . ASN   A 1 180 ? 19.955  13.993  21.598  1.00 32.12 ?  180 ASN   A ND2 1 
ATOM   1351 N  N   . PHE   A 1 181 ? 18.725  8.401   20.650  1.00 25.74 ?  181 PHE   A N   1 
ATOM   1352 C  CA  . PHE   A 1 181 ? 17.748  7.333   20.508  1.00 25.14 ?  181 PHE   A CA  1 
ATOM   1353 C  C   . PHE   A 1 181 ? 16.372  7.763   21.005  1.00 25.83 ?  181 PHE   A C   1 
ATOM   1354 O  O   . PHE   A 1 181 ? 16.250  8.551   21.947  1.00 24.30 ?  181 PHE   A O   1 
ATOM   1355 C  CB  . PHE   A 1 181 ? 18.219  6.105   21.286  1.00 24.26 ?  181 PHE   A CB  1 
ATOM   1356 C  CG  . PHE   A 1 181 ? 18.866  5.076   20.430  1.00 26.57 ?  181 PHE   A CG  1 
ATOM   1357 C  CD1 . PHE   A 1 181 ? 18.099  4.147   19.757  1.00 26.48 ?  181 PHE   A CD1 1 
ATOM   1358 C  CD2 . PHE   A 1 181 ? 20.247  5.048   20.274  1.00 25.28 ?  181 PHE   A CD2 1 
ATOM   1359 C  CE1 . PHE   A 1 181 ? 18.700  3.199   18.934  1.00 27.53 ?  181 PHE   A CE1 1 
ATOM   1360 C  CE2 . PHE   A 1 181 ? 20.844  4.104   19.473  1.00 25.36 ?  181 PHE   A CE2 1 
ATOM   1361 C  CZ  . PHE   A 1 181 ? 20.062  3.174   18.802  1.00 26.43 ?  181 PHE   A CZ  1 
ATOM   1362 N  N   . TYR   A 1 182 ? 15.329  7.254   20.346  1.00 26.43 ?  182 TYR   A N   1 
ATOM   1363 C  CA  . TYR   A 1 182 ? 14.013  7.226   20.969  1.00 25.93 ?  182 TYR   A CA  1 
ATOM   1364 C  C   . TYR   A 1 182 ? 13.982  6.091   21.988  1.00 26.25 ?  182 TYR   A C   1 
ATOM   1365 O  O   . TYR   A 1 182 ? 14.357  4.956   21.682  1.00 28.15 ?  182 TYR   A O   1 
ATOM   1366 C  CB  . TYR   A 1 182 ? 12.915  7.044   19.914  1.00 24.78 ?  182 TYR   A CB  1 
ATOM   1367 C  CG  . TYR   A 1 182 ? 12.739  8.239   18.994  1.00 25.86 ?  182 TYR   A CG  1 
ATOM   1368 C  CD1 . TYR   A 1 182 ? 11.940  9.309   19.366  1.00 27.39 ?  182 TYR   A CD1 1 
ATOM   1369 C  CD2 . TYR   A 1 182 ? 13.380  8.296   17.756  1.00 23.18 ?  182 TYR   A CD2 1 
ATOM   1370 C  CE1 . TYR   A 1 182 ? 11.777  10.406  18.538  1.00 27.78 ?  182 TYR   A CE1 1 
ATOM   1371 C  CE2 . TYR   A 1 182 ? 13.221  9.395   16.911  1.00 23.11 ?  182 TYR   A CE2 1 
ATOM   1372 C  CZ  . TYR   A 1 182 ? 12.420  10.444  17.314  1.00 27.07 ?  182 TYR   A CZ  1 
ATOM   1373 O  OH  . TYR   A 1 182 ? 12.248  11.538  16.505  1.00 27.73 ?  182 TYR   A OH  1 
ATOM   1374 N  N   . GLY   A 1 183 ? 13.551  6.389   23.208  1.00 27.47 ?  183 GLY   A N   1 
ATOM   1375 C  CA  . GLY   A 1 183 ? 13.490  5.374   24.229  1.00 26.28 ?  183 GLY   A CA  1 
ATOM   1376 C  C   . GLY   A 1 183 ? 14.834  5.133   24.885  1.00 32.74 ?  183 GLY   A C   1 
ATOM   1377 O  O   . GLY   A 1 183 ? 15.800  5.867   24.667  1.00 30.85 ?  183 GLY   A O   1 
ATOM   1378 N  N   . PRO   A 1 184 ? 14.922  4.079   25.686  1.00 32.67 ?  184 PRO   A N   1 
ATOM   1379 C  CA  . PRO   A 1 184 ? 16.127  3.859   26.493  1.00 27.34 ?  184 PRO   A CA  1 
ATOM   1380 C  C   . PRO   A 1 184 ? 17.150  2.971   25.799  1.00 34.99 ?  184 PRO   A C   1 
ATOM   1381 O  O   . PRO   A 1 184 ? 18.071  2.455   26.439  1.00 33.19 ?  184 PRO   A O   1 
ATOM   1382 C  CB  . PRO   A 1 184 ? 15.563  3.199   27.757  1.00 30.68 ?  184 PRO   A CB  1 
ATOM   1383 C  CG  . PRO   A 1 184 ? 14.381  2.407   27.243  1.00 33.97 ?  184 PRO   A CG  1 
ATOM   1384 C  CD  . PRO   A 1 184 ? 13.863  3.104   25.998  1.00 34.27 ?  184 PRO   A CD  1 
ATOM   1385 N  N   . PHE   A 1 185 ? 17.025  2.812   24.487  1.00 30.28 ?  185 PHE   A N   1 
ATOM   1386 C  CA  . PHE   A 1 185 ? 17.855  1.855   23.775  1.00 31.85 ?  185 PHE   A CA  1 
ATOM   1387 C  C   . PHE   A 1 185 ? 19.214  2.454   23.424  1.00 27.53 ?  185 PHE   A C   1 
ATOM   1388 O  O   . PHE   A 1 185 ? 19.378  3.674   23.350  1.00 29.36 ?  185 PHE   A O   1 
ATOM   1389 C  CB  . PHE   A 1 185 ? 17.130  1.378   22.519  1.00 28.63 ?  185 PHE   A CB  1 
ATOM   1390 C  CG  . PHE   A 1 185 ? 15.734  0.912   22.787  1.00 32.44 ?  185 PHE   A CG  1 
ATOM   1391 C  CD1 . PHE   A 1 185 ? 15.503  -0.305  23.410  1.00 31.89 ?  185 PHE   A CD1 1 
ATOM   1392 C  CD2 . PHE   A 1 185 ? 14.654  1.700   22.440  1.00 33.76 ?  185 PHE   A CD2 1 
ATOM   1393 C  CE1 . PHE   A 1 185 ? 14.216  -0.731  23.685  1.00 29.25 ?  185 PHE   A CE1 1 
ATOM   1394 C  CE2 . PHE   A 1 185 ? 13.363  1.281   22.706  1.00 34.07 ?  185 PHE   A CE2 1 
ATOM   1395 C  CZ  . PHE   A 1 185 ? 13.145  0.062   23.332  1.00 35.49 ?  185 PHE   A CZ  1 
ATOM   1396 N  N   . VAL   A 1 186 ? 20.199  1.576   23.232  1.00 28.42 ?  186 VAL   A N   1 
ATOM   1397 C  CA  . VAL   A 1 186 ? 21.563  1.976   22.908  1.00 29.32 ?  186 VAL   A CA  1 
ATOM   1398 C  C   . VAL   A 1 186 ? 22.047  1.157   21.718  1.00 29.26 ?  186 VAL   A C   1 
ATOM   1399 O  O   . VAL   A 1 186 ? 21.544  0.067   21.438  1.00 28.74 ?  186 VAL   A O   1 
ATOM   1400 C  CB  . VAL   A 1 186 ? 22.521  1.800   24.110  1.00 31.60 ?  186 VAL   A CB  1 
ATOM   1401 C  CG1 . VAL   A 1 186 ? 22.170  2.771   25.222  1.00 27.75 ?  186 VAL   A CG1 1 
ATOM   1402 C  CG2 . VAL   A 1 186 ? 22.464  0.375   24.620  1.00 32.82 ?  186 VAL   A CG2 1 
ATOM   1403 N  N   . ASP   A 1 187 ? 23.054  1.682   21.016  1.00 26.85 ?  187 ASP   A N   1 
ATOM   1404 C  CA  . ASP   A 1 187 ? 23.624  0.941   19.889  1.00 28.49 ?  187 ASP   A CA  1 
ATOM   1405 C  C   . ASP   A 1 187 ? 24.771  0.037   20.364  1.00 32.82 ?  187 ASP   A C   1 
ATOM   1406 O  O   . ASP   A 1 187 ? 25.938  0.157   19.969  1.00 29.48 ?  187 ASP   A O   1 
ATOM   1407 C  CB  . ASP   A 1 187 ? 24.036  1.893   18.765  1.00 26.66 ?  187 ASP   A CB  1 
ATOM   1408 C  CG  . ASP   A 1 187 ? 25.004  2.991   19.214  1.00 29.66 ?  187 ASP   A CG  1 
ATOM   1409 O  OD1 . ASP   A 1 187 ? 25.264  3.117   20.424  1.00 27.89 ?  187 ASP   A OD1 1 
ATOM   1410 O  OD2 . ASP   A 1 187 ? 25.509  3.739   18.337  1.00 27.26 ?  187 ASP   A OD2 1 
ATOM   1411 N  N   . ARG   A 1 188 ? 24.396  -0.879  21.265  1.00 34.21 ?  188 ARG   A N   1 
ATOM   1412 C  CA  . ARG   A 1 188 ? 25.205  -2.012  21.698  1.00 34.64 ?  188 ARG   A CA  1 
ATOM   1413 C  C   . ARG   A 1 188 ? 24.403  -3.283  21.472  1.00 31.14 ?  188 ARG   A C   1 
ATOM   1414 O  O   . ARG   A 1 188 ? 23.174  -3.283  21.586  1.00 34.04 ?  188 ARG   A O   1 
ATOM   1415 C  CB  . ARG   A 1 188 ? 25.573  -1.972  23.206  1.00 34.54 ?  188 ARG   A CB  1 
ATOM   1416 C  CG  . ARG   A 1 188 ? 26.474  -0.861  23.685  1.00 37.10 ?  188 ARG   A CG  1 
ATOM   1417 C  CD  . ARG   A 1 188 ? 26.334  -0.708  25.209  1.00 33.41 ?  188 ARG   A CD  1 
ATOM   1418 N  NE  . ARG   A 1 188 ? 26.687  -1.920  25.950  1.00 37.78 ?  188 ARG   A NE  1 
ATOM   1419 C  CZ  . ARG   A 1 188 ? 26.337  -2.150  27.216  1.00 40.73 ?  188 ARG   A CZ  1 
ATOM   1420 N  NH1 . ARG   A 1 188 ? 25.603  -1.265  27.876  1.00 37.22 ?  188 ARG   A NH1 1 
ATOM   1421 N  NH2 . ARG   A 1 188 ? 26.712  -3.269  27.823  1.00 36.25 ?  188 ARG   A NH2 1 
ATOM   1422 N  N   . GLN   A 1 189 ? 25.101  -4.375  21.163  1.00 31.85 ?  189 GLN   A N   1 
ATOM   1423 C  CA  . GLN   A 1 189 ? 24.466  -5.691  21.155  1.00 33.68 ?  189 GLN   A CA  1 
ATOM   1424 C  C   . GLN   A 1 189 ? 24.495  -6.256  22.573  1.00 37.71 ?  189 GLN   A C   1 
ATOM   1425 O  O   . GLN   A 1 189 ? 25.247  -7.169  22.914  1.00 43.36 ?  189 GLN   A O   1 
ATOM   1426 C  CB  . GLN   A 1 189 ? 25.134  -6.621  20.156  1.00 35.59 ?  189 GLN   A CB  1 
ATOM   1427 C  CG  . GLN   A 1 189 ? 24.667  -6.361  18.724  1.00 44.76 ?  189 GLN   A CG  1 
ATOM   1428 C  CD  . GLN   A 1 189 ? 24.914  -7.532  17.792  1.00 47.02 ?  189 GLN   A CD  1 
ATOM   1429 O  OE1 . GLN   A 1 189 ? 25.840  -7.512  16.984  1.00 45.19 ?  189 GLN   A OE1 1 
ATOM   1430 N  NE2 . GLN   A 1 189 ? 24.068  -8.555  17.889  1.00 50.81 ?  189 GLN   A NE2 1 
ATOM   1431 N  N   . THR   A 1 190 ? 23.668  -5.661  23.419  1.00 40.94 ?  190 THR   A N   1 
ATOM   1432 C  CA  . THR   A 1 190 ? 23.477  -6.115  24.783  1.00 35.79 ?  190 THR   A CA  1 
ATOM   1433 C  C   . THR   A 1 190 ? 21.993  -6.413  24.960  1.00 42.98 ?  190 THR   A C   1 
ATOM   1434 O  O   . THR   A 1 190 ? 21.168  -6.035  24.124  1.00 40.42 ?  190 THR   A O   1 
ATOM   1435 C  CB  . THR   A 1 190 ? 23.969  -5.056  25.787  1.00 38.86 ?  190 THR   A CB  1 
ATOM   1436 O  OG1 . THR   A 1 190 ? 24.052  -5.613  27.113  1.00 46.74 ?  190 THR   A OG1 1 
ATOM   1437 C  CG2 . THR   A 1 190 ? 23.031  -3.861  25.794  1.00 39.45 ?  190 THR   A CG2 1 
ATOM   1438 N  N   . ALA   A 1 191 ? 21.663  -7.127  26.036  1.00 38.95 ?  191 ALA   A N   1 
ATOM   1439 C  CA  . ALA   A 1 191 ? 20.278  -7.501  26.303  1.00 37.48 ?  191 ALA   A CA  1 
ATOM   1440 C  C   . ALA   A 1 191 ? 19.379  -6.272  26.343  1.00 40.61 ?  191 ALA   A C   1 
ATOM   1441 O  O   . ALA   A 1 191 ? 19.480  -5.445  27.252  1.00 35.56 ?  191 ALA   A O   1 
ATOM   1442 C  CB  . ALA   A 1 191 ? 20.173  -8.283  27.618  1.00 43.15 ?  191 ALA   A CB  1 
ATOM   1443 N  N   . GLN   A 1 192 ? 18.524  -6.119  25.336  1.00 37.66 ?  192 GLN   A N   1 
ATOM   1444 C  CA  . GLN   A 1 192 ? 17.565  -5.030  25.299  1.00 37.21 ?  192 GLN   A CA  1 
ATOM   1445 C  C   . GLN   A 1 192 ? 16.216  -5.606  24.905  1.00 37.61 ?  192 GLN   A C   1 
ATOM   1446 O  O   . GLN   A 1 192 ? 16.139  -6.568  24.136  1.00 42.69 ?  192 GLN   A O   1 
ATOM   1447 C  CB  . GLN   A 1 192 ? 17.962  -3.928  24.305  1.00 39.25 ?  192 GLN   A CB  1 
ATOM   1448 C  CG  . GLN   A 1 192 ? 19.394  -3.443  24.420  1.00 35.80 ?  192 GLN   A CG  1 
ATOM   1449 C  CD  . GLN   A 1 192 ? 19.658  -2.222  23.566  1.00 31.81 ?  192 GLN   A CD  1 
ATOM   1450 O  OE1 . GLN   A 1 192 ? 19.027  -1.180  23.740  1.00 31.72 ?  192 GLN   A OE1 1 
ATOM   1451 N  NE2 . GLN   A 1 192 ? 20.593  -2.346  22.631  1.00 31.70 ?  192 GLN   A NE2 1 
ATOM   1452 N  N   . ALA   A 1 193 ? 15.156  -5.003  25.426  1.00 37.54 ?  193 ALA   A N   1 
ATOM   1453 C  CA  . ALA   A 1 193 ? 13.817  -5.517  25.182  1.00 41.08 ?  193 ALA   A CA  1 
ATOM   1454 C  C   . ALA   A 1 193 ? 12.828  -4.366  25.200  1.00 39.22 ?  193 ALA   A C   1 
ATOM   1455 O  O   . ALA   A 1 193 ? 12.895  -3.501  26.079  1.00 41.90 ?  193 ALA   A O   1 
ATOM   1456 C  CB  . ALA   A 1 193 ? 13.432  -6.569  26.230  1.00 38.59 ?  193 ALA   A CB  1 
ATOM   1457 N  N   . ALA   A 1 194 ? 11.921  -4.359  24.227  1.00 42.26 ?  194 ALA   A N   1 
ATOM   1458 C  CA  . ALA   A 1 194 ? 10.805  -3.426  24.263  1.00 42.79 ?  194 ALA   A CA  1 
ATOM   1459 C  C   . ALA   A 1 194 ? 9.979   -3.657  25.525  1.00 41.05 ?  194 ALA   A C   1 
ATOM   1460 O  O   . ALA   A 1 194 ? 9.644   -4.797  25.857  1.00 43.91 ?  194 ALA   A O   1 
ATOM   1461 C  CB  . ALA   A 1 194 ? 9.938   -3.597  23.012  1.00 35.22 ?  194 ALA   A CB  1 
ATOM   1462 N  N   . GLY   A 1 195 ? 9.683   -2.581  26.249  1.00 41.89 ?  195 GLY   A N   1 
ATOM   1463 C  CA  . GLY   A 1 195 ? 8.725   -2.642  27.333  1.00 38.49 ?  195 GLY   A CA  1 
ATOM   1464 C  C   . GLY   A 1 195 ? 7.320   -2.912  26.809  1.00 40.90 ?  195 GLY   A C   1 
ATOM   1465 O  O   . GLY   A 1 195 ? 7.062   -2.965  25.604  1.00 36.56 ?  195 GLY   A O   1 
ATOM   1466 N  N   . THR   A 1 196 ? 6.388   -3.093  27.742  1.00 42.80 ?  196 THR   A N   1 
ATOM   1467 C  CA  . THR   A 1 196 ? 5.012   -3.347  27.332  1.00 35.94 ?  196 THR   A CA  1 
ATOM   1468 C  C   . THR   A 1 196 ? 4.418   -2.105  26.676  1.00 34.64 ?  196 THR   A C   1 
ATOM   1469 O  O   . THR   A 1 196 ? 4.570   -0.983  27.170  1.00 37.54 ?  196 THR   A O   1 
ATOM   1470 C  CB  . THR   A 1 196 ? 4.155   -3.786  28.520  1.00 44.27 ?  196 THR   A CB  1 
ATOM   1471 O  OG1 . THR   A 1 196 ? 4.460   -2.976  29.661  1.00 41.08 ?  196 THR   A OG1 1 
ATOM   1472 C  CG2 . THR   A 1 196 ? 4.409   -5.256  28.848  1.00 42.76 ?  196 THR   A CG2 1 
ATOM   1473 N  N   . ASP   A 1 197 ? 3.738   -2.311  25.556  1.00 29.96 ?  197 ASP   A N   1 
ATOM   1474 C  CA  . ASP   A 1 197 ? 3.213   -1.217  24.756  1.00 36.25 ?  197 ASP   A CA  1 
ATOM   1475 C  C   . ASP   A 1 197 ? 1.752   -0.930  25.104  1.00 36.98 ?  197 ASP   A C   1 
ATOM   1476 O  O   . ASP   A 1 197 ? 1.058   -1.743  25.723  1.00 36.28 ?  197 ASP   A O   1 
ATOM   1477 C  CB  . ASP   A 1 197 ? 3.351   -1.541  23.265  1.00 30.99 ?  197 ASP   A CB  1 
ATOM   1478 C  CG  . ASP   A 1 197 ? 3.331   -0.307  22.403  1.00 32.87 ?  197 ASP   A CG  1 
ATOM   1479 O  OD1 . ASP   A 1 197 ? 3.701   0.768   22.915  1.00 32.44 ?  197 ASP   A OD1 1 
ATOM   1480 O  OD2 . ASP   A 1 197 ? 2.938   -0.406  21.223  1.00 33.05 ?  197 ASP   A OD2 1 
ATOM   1481 N  N   . THR   A 1 198 ? 1.297   0.260   24.709  1.00 32.00 ?  198 THR   A N   1 
ATOM   1482 C  CA  . THR   A 1 198 ? -0.082  0.683   24.897  1.00 28.77 ?  198 THR   A CA  1 
ATOM   1483 C  C   . THR   A 1 198 ? -0.653  1.172   23.571  1.00 31.62 ?  198 THR   A C   1 
ATOM   1484 O  O   . THR   A 1 198 ? 0.073   1.443   22.610  1.00 25.19 ?  198 THR   A O   1 
ATOM   1485 C  CB  . THR   A 1 198 ? -0.203  1.786   25.954  1.00 35.76 ?  198 THR   A CB  1 
ATOM   1486 O  OG1 . THR   A 1 198 ? 0.669   2.869   25.621  1.00 37.82 ?  198 THR   A OG1 1 
ATOM   1487 C  CG2 . THR   A 1 198 ? 0.179   1.252   27.332  1.00 34.93 ?  198 THR   A CG2 1 
ATOM   1488 N  N   . THR   A 1 199 ? -1.974  1.274   23.525  1.00 23.77 ?  199 THR   A N   1 
ATOM   1489 C  CA  . THR   A 1 199 ? -2.642  1.773   22.334  1.00 25.72 ?  199 THR   A CA  1 
ATOM   1490 C  C   . THR   A 1 199 ? -2.693  3.295   22.375  1.00 26.95 ?  199 THR   A C   1 
ATOM   1491 O  O   . THR   A 1 199 ? -2.849  3.894   23.442  1.00 25.59 ?  199 THR   A O   1 
ATOM   1492 C  CB  . THR   A 1 199 ? -4.042  1.174   22.237  1.00 26.28 ?  199 THR   A CB  1 
ATOM   1493 O  OG1 . THR   A 1 199 ? -3.925  -0.249  22.110  1.00 27.16 ?  199 THR   A OG1 1 
ATOM   1494 C  CG2 . THR   A 1 199 ? -4.792  1.727   21.036  1.00 23.96 ?  199 THR   A CG2 1 
ATOM   1495 N  N   . ILE   A 1 200 ? -2.511  3.919   21.214  1.00 23.29 ?  200 ILE   A N   1 
ATOM   1496 C  CA  . ILE   A 1 200 ? -2.484  5.376   21.098  1.00 25.01 ?  200 ILE   A CA  1 
ATOM   1497 C  C   . ILE   A 1 200 ? -3.924  5.871   20.973  1.00 27.83 ?  200 ILE   A C   1 
ATOM   1498 O  O   . ILE   A 1 200 ? -4.495  5.909   19.878  1.00 26.09 ?  200 ILE   A O   1 
ATOM   1499 C  CB  . ILE   A 1 200 ? -1.625  5.827   19.917  1.00 25.70 ?  200 ILE   A CB  1 
ATOM   1500 C  CG1 . ILE   A 1 200 ? -0.208  5.246   20.045  1.00 22.68 ?  200 ILE   A CG1 1 
ATOM   1501 C  CG2 . ILE   A 1 200 ? -1.584  7.338   19.855  1.00 24.59 ?  200 ILE   A CG2 1 
ATOM   1502 C  CD1 . ILE   A 1 200 ? 0.506   5.077   18.685  1.00 23.71 ?  200 ILE   A CD1 1 
ATOM   1503 N  N   . THR   A 1 201 ? -4.490  6.317   22.101  1.00 25.97 ?  201 THR   A N   1 
ATOM   1504 C  CA  . THR   A 1 201 ? -5.928  6.569   22.187  1.00 25.27 ?  201 THR   A CA  1 
ATOM   1505 C  C   . THR   A 1 201 ? -6.370  7.720   21.295  1.00 23.86 ?  201 THR   A C   1 
ATOM   1506 O  O   . THR   A 1 201 ? -7.397  7.627   20.610  1.00 26.69 ?  201 THR   A O   1 
ATOM   1507 C  CB  . THR   A 1 201 ? -6.313  6.854   23.636  1.00 24.85 ?  201 THR   A CB  1 
ATOM   1508 O  OG1 . THR   A 1 201 ? -5.813  5.796   24.448  1.00 23.80 ?  201 THR   A OG1 1 
ATOM   1509 C  CG2 . THR   A 1 201 ? -7.828  6.932   23.775  1.00 25.55 ?  201 THR   A CG2 1 
ATOM   1510 N  N   . VAL   A 1 202 ? -5.635  8.833   21.317  1.00 22.67 ?  202 VAL   A N   1 
ATOM   1511 C  CA  . VAL   A 1 202 ? -6.035  9.971   20.499  1.00 25.77 ?  202 VAL   A CA  1 
ATOM   1512 C  C   . VAL   A 1 202 ? -6.064  9.596   19.016  1.00 27.76 ?  202 VAL   A C   1 
ATOM   1513 O  O   . VAL   A 1 202 ? -6.882  10.121  18.252  1.00 25.61 ?  202 VAL   A O   1 
ATOM   1514 C  CB  . VAL   A 1 202 ? -5.115  11.175  20.777  1.00 23.49 ?  202 VAL   A CB  1 
ATOM   1515 C  CG1 . VAL   A 1 202 ? -3.663  10.893  20.312  1.00 30.36 ?  202 VAL   A CG1 1 
ATOM   1516 C  CG2 . VAL   A 1 202 ? -5.680  12.428  20.111  1.00 29.10 ?  202 VAL   A CG2 1 
ATOM   1517 N  N   . ASN   A 1 203 ? -5.213  8.655   18.592  1.00 25.32 ?  203 ASN   A N   1 
ATOM   1518 C  CA  . ASN   A 1 203 ? -5.229  8.223   17.196  1.00 27.29 ?  203 ASN   A CA  1 
ATOM   1519 C  C   . ASN   A 1 203 ? -6.459  7.385   16.882  1.00 26.24 ?  203 ASN   A C   1 
ATOM   1520 O  O   . ASN   A 1 203 ? -7.037  7.509   15.793  1.00 24.75 ?  203 ASN   A O   1 
ATOM   1521 C  CB  . ASN   A 1 203 ? -3.962  7.445   16.871  1.00 25.09 ?  203 ASN   A CB  1 
ATOM   1522 C  CG  . ASN   A 1 203 ? -2.746  8.337   16.802  1.00 27.04 ?  203 ASN   A CG  1 
ATOM   1523 O  OD1 . ASN   A 1 203 ? -2.841  9.538   17.050  1.00 25.46 ?  203 ASN   A OD1 1 
ATOM   1524 N  ND2 . ASN   A 1 203 ? -1.598  7.762   16.460  1.00 26.64 ?  203 ASN   A ND2 1 
ATOM   1525 N  N   . VAL   A 1 204 ? -6.872  6.520   17.814  1.00 26.29 ?  204 VAL   A N   1 
ATOM   1526 C  CA  . VAL   A 1 204 ? -8.087  5.734   17.606  1.00 27.55 ?  204 VAL   A CA  1 
ATOM   1527 C  C   . VAL   A 1 204 ? -9.292  6.650   17.446  1.00 26.94 ?  204 VAL   A C   1 
ATOM   1528 O  O   . VAL   A 1 204 ? -10.162 6.422   16.594  1.00 26.59 ?  204 VAL   A O   1 
ATOM   1529 C  CB  . VAL   A 1 204 ? -8.289  4.732   18.759  1.00 25.98 ?  204 VAL   A CB  1 
ATOM   1530 C  CG1 . VAL   A 1 204 ? -9.575  3.914   18.535  1.00 22.95 ?  204 VAL   A CG1 1 
ATOM   1531 C  CG2 . VAL   A 1 204 ? -7.093  3.823   18.869  1.00 24.33 ?  204 VAL   A CG2 1 
ATOM   1532 N  N   . LEU   A 1 205 ? -9.356  7.712   18.248  1.00 26.54 ?  205 LEU   A N   1 
ATOM   1533 C  CA  . LEU   A 1 205 ? -10.483 8.631   18.149  1.00 26.64 ?  205 LEU   A CA  1 
ATOM   1534 C  C   . LEU   A 1 205 ? -10.483 9.354   16.810  1.00 25.63 ?  205 LEU   A C   1 
ATOM   1535 O  O   . LEU   A 1 205 ? -11.536 9.518   16.186  1.00 26.70 ?  205 LEU   A O   1 
ATOM   1536 C  CB  . LEU   A 1 205 ? -10.437 9.627   19.306  1.00 24.77 ?  205 LEU   A CB  1 
ATOM   1537 C  CG  . LEU   A 1 205 ? -10.704 9.009   20.676  1.00 24.44 ?  205 LEU   A CG  1 
ATOM   1538 C  CD1 . LEU   A 1 205 ? -10.380 10.017  21.765  1.00 23.49 ?  205 LEU   A CD1 1 
ATOM   1539 C  CD2 . LEU   A 1 205 ? -12.171 8.586   20.741  1.00 24.52 ?  205 LEU   A CD2 1 
ATOM   1540 N  N   . ALA   A 1 206 ? -9.309  9.801   16.358  1.00 23.64 ?  206 ALA   A N   1 
ATOM   1541 C  CA  . ALA   A 1 206 ? -9.217  10.455  15.057  1.00 23.23 ?  206 ALA   A CA  1 
ATOM   1542 C  C   . ALA   A 1 206 ? -9.699  9.530   13.949  1.00 23.29 ?  206 ALA   A C   1 
ATOM   1543 O  O   . ALA   A 1 206 ? -10.389 9.962   13.023  1.00 27.36 ?  206 ALA   A O   1 
ATOM   1544 C  CB  . ALA   A 1 206 ? -7.775  10.894  14.799  1.00 26.59 ?  206 ALA   A CB  1 
ATOM   1545 N  N   . TRP   A 1 207 ? -9.354  8.248   14.050  1.00 22.55 ?  207 TRP   A N   1 
ATOM   1546 C  CA  . TRP   A 1 207 ? -9.747  7.249   13.068  1.00 22.23 ?  207 TRP   A CA  1 
ATOM   1547 C  C   . TRP   A 1 207 ? -11.251 6.997   13.089  1.00 27.42 ?  207 TRP   A C   1 
ATOM   1548 O  O   . TRP   A 1 207 ? -11.877 6.823   12.030  1.00 25.55 ?  207 TRP   A O   1 
ATOM   1549 C  CB  . TRP   A 1 207 ? -8.965  5.974   13.354  1.00 23.81 ?  207 TRP   A CB  1 
ATOM   1550 C  CG  . TRP   A 1 207 ? -9.247  4.803   12.498  1.00 28.23 ?  207 TRP   A CG  1 
ATOM   1551 C  CD1 . TRP   A 1 207 ? -8.874  4.616   11.195  1.00 27.80 ?  207 TRP   A CD1 1 
ATOM   1552 C  CD2 . TRP   A 1 207 ? -9.909  3.609   12.903  1.00 27.29 ?  207 TRP   A CD2 1 
ATOM   1553 N  NE1 . TRP   A 1 207 ? -9.287  3.379   10.764  1.00 27.19 ?  207 TRP   A NE1 1 
ATOM   1554 C  CE2 . TRP   A 1 207 ? -9.926  2.744   11.798  1.00 30.00 ?  207 TRP   A CE2 1 
ATOM   1555 C  CE3 . TRP   A 1 207 ? -10.507 3.194   14.097  1.00 30.05 ?  207 TRP   A CE3 1 
ATOM   1556 C  CZ2 . TRP   A 1 207 ? -10.519 1.489   11.849  1.00 33.83 ?  207 TRP   A CZ2 1 
ATOM   1557 C  CZ3 . TRP   A 1 207 ? -11.085 1.951   14.149  1.00 29.06 ?  207 TRP   A CZ3 1 
ATOM   1558 C  CH2 . TRP   A 1 207 ? -11.088 1.110   13.034  1.00 29.23 ?  207 TRP   A CH2 1 
ATOM   1559 N  N   . LEU   A 1 208 ? -11.850 6.966   14.279  1.00 21.94 ?  208 LEU   A N   1 
ATOM   1560 C  CA  . LEU   A 1 208 ? -13.307 6.894   14.351  1.00 22.36 ?  208 LEU   A CA  1 
ATOM   1561 C  C   . LEU   A 1 208 ? -13.939 8.095   13.661  1.00 23.53 ?  208 LEU   A C   1 
ATOM   1562 O  O   . LEU   A 1 208 ? -14.974 7.967   12.994  1.00 25.37 ?  208 LEU   A O   1 
ATOM   1563 C  CB  . LEU   A 1 208 ? -13.757 6.793   15.812  1.00 24.07 ?  208 LEU   A CB  1 
ATOM   1564 C  CG  . LEU   A 1 208 ? -13.357 5.465   16.462  1.00 25.62 ?  208 LEU   A CG  1 
ATOM   1565 C  CD1 . LEU   A 1 208 ? -13.798 5.407   17.920  1.00 24.23 ?  208 LEU   A CD1 1 
ATOM   1566 C  CD2 . LEU   A 1 208 ? -13.942 4.291   15.682  1.00 27.97 ?  208 LEU   A CD2 1 
ATOM   1567 N  N   . TYR   A 1 209 ? -13.311 9.268   13.781  1.00 25.83 ?  209 TYR   A N   1 
ATOM   1568 C  CA  . TYR   A 1 209 ? -13.804 10.435  13.058  1.00 27.84 ?  209 TYR   A CA  1 
ATOM   1569 C  C   . TYR   A 1 209 ? -13.696 10.236  11.550  1.00 30.50 ?  209 TYR   A C   1 
ATOM   1570 O  O   . TYR   A 1 209 ? -14.590 10.645  10.800  1.00 28.82 ?  209 TYR   A O   1 
ATOM   1571 C  CB  . TYR   A 1 209 ? -13.049 11.688  13.494  1.00 23.77 ?  209 TYR   A CB  1 
ATOM   1572 C  CG  . TYR   A 1 209 ? -13.593 12.309  14.765  1.00 28.55 ?  209 TYR   A CG  1 
ATOM   1573 C  CD1 . TYR   A 1 209 ? -14.848 12.914  14.787  1.00 30.09 ?  209 TYR   A CD1 1 
ATOM   1574 C  CD2 . TYR   A 1 209 ? -12.850 12.302  15.940  1.00 31.00 ?  209 TYR   A CD2 1 
ATOM   1575 C  CE1 . TYR   A 1 209 ? -15.354 13.489  15.942  1.00 27.95 ?  209 TYR   A CE1 1 
ATOM   1576 C  CE2 . TYR   A 1 209 ? -13.348 12.876  17.107  1.00 29.24 ?  209 TYR   A CE2 1 
ATOM   1577 C  CZ  . TYR   A 1 209 ? -14.602 13.465  17.100  1.00 31.27 ?  209 TYR   A CZ  1 
ATOM   1578 O  OH  . TYR   A 1 209 ? -15.099 14.037  18.249  1.00 30.54 ?  209 TYR   A OH  1 
ATOM   1579 N  N   . ALA   A 1 210 ? -12.614 9.599   11.087  1.00 26.54 ?  210 ALA   A N   1 
ATOM   1580 C  CA  . ALA   A 1 210 ? -12.505 9.302   9.660   1.00 28.79 ?  210 ALA   A CA  1 
ATOM   1581 C  C   . ALA   A 1 210 ? -13.625 8.377   9.214   1.00 29.15 ?  210 ALA   A C   1 
ATOM   1582 O  O   . ALA   A 1 210 ? -14.180 8.542   8.120   1.00 28.89 ?  210 ALA   A O   1 
ATOM   1583 C  CB  . ALA   A 1 210 ? -11.145 8.681   9.345   1.00 28.62 ?  210 ALA   A CB  1 
ATOM   1584 N  N   . ALA   A 1 211 ? -13.972 7.397   10.052  1.00 27.35 ?  211 ALA   A N   1 
ATOM   1585 C  CA  . ALA   A 1 211 ? -15.087 6.514   9.732   1.00 29.09 ?  211 ALA   A CA  1 
ATOM   1586 C  C   . ALA   A 1 211 ? -16.388 7.299   9.600   1.00 29.95 ?  211 ALA   A C   1 
ATOM   1587 O  O   . ALA   A 1 211 ? -17.179 7.059   8.678   1.00 26.00 ?  211 ALA   A O   1 
ATOM   1588 C  CB  . ALA   A 1 211 ? -15.212 5.427   10.797  1.00 31.11 ?  211 ALA   A CB  1 
ATOM   1589 N  N   . VAL   A 1 212 ? -16.613 8.259   10.497  1.00 27.22 ?  212 VAL   A N   1 
ATOM   1590 C  CA  . VAL   A 1 212 ? -17.809 9.092   10.411  1.00 28.91 ?  212 VAL   A CA  1 
ATOM   1591 C  C   . VAL   A 1 212 ? -17.764 9.953   9.158   1.00 28.70 ?  212 VAL   A C   1 
ATOM   1592 O  O   . VAL   A 1 212 ? -18.754 10.059  8.423   1.00 27.48 ?  212 VAL   A O   1 
ATOM   1593 C  CB  . VAL   A 1 212 ? -17.959 9.947   11.682  1.00 30.59 ?  212 VAL   A CB  1 
ATOM   1594 C  CG1 . VAL   A 1 212 ? -19.093 10.951  11.529  1.00 29.46 ?  212 VAL   A CG1 1 
ATOM   1595 C  CG2 . VAL   A 1 212 ? -18.209 9.054   12.885  1.00 25.61 ?  212 VAL   A CG2 1 
ATOM   1596 N  N   . ILE   A 1 213 ? -16.611 10.573  8.890   1.00 28.65 ?  213 ILE   A N   1 
ATOM   1597 C  CA  . ILE   A 1 213 ? -16.462 11.380  7.678   1.00 30.54 ?  213 ILE   A CA  1 
ATOM   1598 C  C   . ILE   A 1 213 ? -16.798 10.555  6.441   1.00 28.41 ?  213 ILE   A C   1 
ATOM   1599 O  O   . ILE   A 1 213 ? -17.455 11.039  5.512   1.00 34.78 ?  213 ILE   A O   1 
ATOM   1600 C  CB  . ILE   A 1 213 ? -15.044 11.981  7.609   1.00 29.45 ?  213 ILE   A CB  1 
ATOM   1601 C  CG1 . ILE   A 1 213 ? -14.928 13.163  8.571   1.00 26.69 ?  213 ILE   A CG1 1 
ATOM   1602 C  CG2 . ILE   A 1 213 ? -14.704 12.434  6.185   1.00 33.47 ?  213 ILE   A CG2 1 
ATOM   1603 C  CD1 . ILE   A 1 213 ? -13.553 13.336  9.193   1.00 31.80 ?  213 ILE   A CD1 1 
ATOM   1604 N  N   . ASN   A 1 214 ? -16.394 9.287   6.426   1.00 29.32 ?  214 ASN   A N   1 
ATOM   1605 C  CA  . ASN   A 1 214 ? -16.661 8.404   5.299   1.00 32.08 ?  214 ASN   A CA  1 
ATOM   1606 C  C   . ASN   A 1 214 ? -18.078 7.833   5.299   1.00 31.27 ?  214 ASN   A C   1 
ATOM   1607 O  O   . ASN   A 1 214 ? -18.390 6.991   4.451   1.00 31.84 ?  214 ASN   A O   1 
ATOM   1608 C  CB  . ASN   A 1 214 ? -15.645 7.266   5.275   1.00 27.88 ?  214 ASN   A CB  1 
ATOM   1609 C  CG  . ASN   A 1 214 ? -14.492 7.537   4.318   1.00 38.50 ?  214 ASN   A CG  1 
ATOM   1610 O  OD1 . ASN   A 1 214 ? -14.336 6.847   3.308   1.00 38.36 ?  214 ASN   A OD1 1 
ATOM   1611 N  ND2 . ASN   A 1 214 ? -13.686 8.552   4.628   1.00 36.76 ?  214 ASN   A ND2 1 
ATOM   1612 N  N   . GLY   A 1 215 ? -18.930 8.250   6.226   1.00 28.97 ?  215 GLY   A N   1 
ATOM   1613 C  CA  . GLY   A 1 215 ? -20.338 7.936   6.154   1.00 30.11 ?  215 GLY   A CA  1 
ATOM   1614 C  C   . GLY   A 1 215 ? -20.828 6.812   7.040   1.00 38.02 ?  215 GLY   A C   1 
ATOM   1615 O  O   . GLY   A 1 215 ? -21.947 6.333   6.824   1.00 38.72 ?  215 GLY   A O   1 
ATOM   1616 N  N   . ASP   A 1 216 ? -20.042 6.379   8.028   1.00 33.49 ?  216 ASP   A N   1 
ATOM   1617 C  CA  . ASP   A 1 216 ? -20.429 5.295   8.927   1.00 31.40 ?  216 ASP   A CA  1 
ATOM   1618 C  C   . ASP   A 1 216 ? -20.778 5.862   10.295  1.00 30.08 ?  216 ASP   A C   1 
ATOM   1619 O  O   . ASP   A 1 216 ? -20.015 6.660   10.851  1.00 32.75 ?  216 ASP   A O   1 
ATOM   1620 C  CB  . ASP   A 1 216 ? -19.312 4.256   9.057   1.00 38.81 ?  216 ASP   A CB  1 
ATOM   1621 C  CG  . ASP   A 1 216 ? -19.249 3.310   7.864   1.00 45.90 ?  216 ASP   A CG  1 
ATOM   1622 O  OD1 . ASP   A 1 216 ? -19.330 3.789   6.710   1.00 50.93 ?  216 ASP   A OD1 1 
ATOM   1623 O  OD2 . ASP   A 1 216 ? -19.110 2.086   8.082   1.00 57.93 ?  216 ASP   A OD2 1 
ATOM   1624 N  N   . ARG   A 1 217 ? -21.927 5.443   10.836  1.00 24.38 ?  217 ARG   A N   1 
ATOM   1625 C  CA  . ARG   A 1 217 ? -22.352 5.879   12.160  1.00 25.78 ?  217 ARG   A CA  1 
ATOM   1626 C  C   . ARG   A 1 217 ? -22.774 4.745   13.083  1.00 28.40 ?  217 ARG   A C   1 
ATOM   1627 O  O   . ARG   A 1 217 ? -23.198 5.024   14.211  1.00 26.50 ?  217 ARG   A O   1 
ATOM   1628 C  CB  . ARG   A 1 217 ? -23.509 6.886   12.057  1.00 29.16 ?  217 ARG   A CB  1 
ATOM   1629 C  CG  . ARG   A 1 217 ? -23.097 8.247   11.508  1.00 30.27 ?  217 ARG   A CG  1 
ATOM   1630 C  CD  . ARG   A 1 217 ? -24.292 9.165   11.358  1.00 33.15 ?  217 ARG   A CD  1 
ATOM   1631 N  NE  . ARG   A 1 217 ? -24.928 9.452   12.636  1.00 36.49 ?  217 ARG   A NE  1 
ATOM   1632 C  CZ  . ARG   A 1 217 ? -24.699 10.547  13.352  1.00 36.92 ?  217 ARG   A CZ  1 
ATOM   1633 N  NH1 . ARG   A 1 217 ? -23.844 11.467  12.904  1.00 35.52 ?  217 ARG   A NH1 1 
ATOM   1634 N  NH2 . ARG   A 1 217 ? -25.329 10.725  14.510  1.00 31.40 ?  217 ARG   A NH2 1 
ATOM   1635 N  N   . TRP   A 1 218 ? -22.642 3.483   12.663  1.00 25.20 ?  218 TRP   A N   1 
ATOM   1636 C  CA  . TRP   A 1 218 ? -23.244 2.387   13.417  1.00 24.41 ?  218 TRP   A CA  1 
ATOM   1637 C  C   . TRP   A 1 218 ? -22.685 2.242   14.834  1.00 25.01 ?  218 TRP   A C   1 
ATOM   1638 O  O   . TRP   A 1 218 ? -23.354 1.640   15.681  1.00 23.49 ?  218 TRP   A O   1 
ATOM   1639 C  CB  . TRP   A 1 218 ? -23.082 1.068   12.657  1.00 23.25 ?  218 TRP   A CB  1 
ATOM   1640 C  CG  . TRP   A 1 218 ? -21.667 0.603   12.447  1.00 28.05 ?  218 TRP   A CG  1 
ATOM   1641 C  CD1 . TRP   A 1 218 ? -20.908 0.748   11.308  1.00 28.57 ?  218 TRP   A CD1 1 
ATOM   1642 C  CD2 . TRP   A 1 218 ? -20.846 -0.110  13.387  1.00 24.91 ?  218 TRP   A CD2 1 
ATOM   1643 N  NE1 . TRP   A 1 218 ? -19.668 0.175   11.496  1.00 28.12 ?  218 TRP   A NE1 1 
ATOM   1644 C  CE2 . TRP   A 1 218 ? -19.605 -0.357  12.760  1.00 31.63 ?  218 TRP   A CE2 1 
ATOM   1645 C  CE3 . TRP   A 1 218 ? -21.039 -0.562  14.695  1.00 27.02 ?  218 TRP   A CE3 1 
ATOM   1646 C  CZ2 . TRP   A 1 218 ? -18.567 -1.032  13.401  1.00 28.58 ?  218 TRP   A CZ2 1 
ATOM   1647 C  CZ3 . TRP   A 1 218 ? -20.005 -1.234  15.329  1.00 30.83 ?  218 TRP   A CZ3 1 
ATOM   1648 C  CH2 . TRP   A 1 218 ? -18.783 -1.460  14.680  1.00 35.23 ?  218 TRP   A CH2 1 
ATOM   1649 N  N   . PHE   A 1 219 ? -21.486 2.772   15.111  1.00 27.02 ?  219 PHE   A N   1 
ATOM   1650 C  CA  . PHE   A 1 219 ? -20.808 2.618   16.396  1.00 24.43 ?  219 PHE   A CA  1 
ATOM   1651 C  C   . PHE   A 1 219 ? -21.042 3.781   17.352  1.00 27.62 ?  219 PHE   A C   1 
ATOM   1652 O  O   . PHE   A 1 219 ? -20.551 3.733   18.485  1.00 26.98 ?  219 PHE   A O   1 
ATOM   1653 C  CB  . PHE   A 1 219 ? -19.287 2.447   16.185  1.00 23.63 ?  219 PHE   A CB  1 
ATOM   1654 C  CG  . PHE   A 1 219 ? -18.695 3.475   15.267  1.00 26.23 ?  219 PHE   A CG  1 
ATOM   1655 C  CD1 . PHE   A 1 219 ? -18.345 4.723   15.742  1.00 24.70 ?  219 PHE   A CD1 1 
ATOM   1656 C  CD2 . PHE   A 1 219 ? -18.536 3.205   13.907  1.00 26.85 ?  219 PHE   A CD2 1 
ATOM   1657 C  CE1 . PHE   A 1 219 ? -17.830 5.687   14.887  1.00 27.25 ?  219 PHE   A CE1 1 
ATOM   1658 C  CE2 . PHE   A 1 219 ? -18.021 4.161   13.044  1.00 27.80 ?  219 PHE   A CE2 1 
ATOM   1659 C  CZ  . PHE   A 1 219 ? -17.665 5.403   13.530  1.00 27.00 ?  219 PHE   A CZ  1 
ATOM   1660 N  N   . LEU   A 1 220 ? -21.739 4.834   16.927  1.00 25.64 ?  220 LEU   A N   1 
ATOM   1661 C  CA  . LEU   A 1 220 ? -22.095 5.909   17.846  1.00 28.83 ?  220 LEU   A CA  1 
ATOM   1662 C  C   . LEU   A 1 220 ? -23.164 5.428   18.826  1.00 28.77 ?  220 LEU   A C   1 
ATOM   1663 O  O   . LEU   A 1 220 ? -23.823 4.412   18.602  1.00 25.57 ?  220 LEU   A O   1 
ATOM   1664 C  CB  . LEU   A 1 220 ? -22.603 7.129   17.077  1.00 26.70 ?  220 LEU   A CB  1 
ATOM   1665 C  CG  . LEU   A 1 220 ? -21.639 7.702   16.036  1.00 28.38 ?  220 LEU   A CG  1 
ATOM   1666 C  CD1 . LEU   A 1 220 ? -22.256 8.893   15.323  1.00 27.56 ?  220 LEU   A CD1 1 
ATOM   1667 C  CD2 . LEU   A 1 220 ? -20.310 8.091   16.698  1.00 28.87 ?  220 LEU   A CD2 1 
ATOM   1668 N  N   . ASN   A 1 221 ? -23.325 6.163   19.932  1.00 27.88 ?  221 ASN   A N   1 
ATOM   1669 C  CA  . ASN   A 1 221 ? -24.391 5.867   20.883  1.00 21.62 ?  221 ASN   A CA  1 
ATOM   1670 C  C   . ASN   A 1 221 ? -24.896 7.161   21.513  1.00 26.94 ?  221 ASN   A C   1 
ATOM   1671 O  O   . ASN   A 1 221 ? -24.377 8.252   21.261  1.00 25.41 ?  221 ASN   A O   1 
ATOM   1672 C  CB  . ASN   A 1 221 ? -23.950 4.850   21.945  1.00 26.09 ?  221 ASN   A CB  1 
ATOM   1673 C  CG  . ASN   A 1 221 ? -22.864 5.385   22.904  1.00 25.86 ?  221 ASN   A CG  1 
ATOM   1674 O  OD1 . ASN   A 1 221 ? -22.597 6.581   22.987  1.00 28.31 ?  221 ASN   A OD1 1 
ATOM   1675 N  ND2 . ASN   A 1 221 ? -22.255 4.476   23.641  1.00 28.08 ?  221 ASN   A ND2 1 
ATOM   1676 N  N   . ARG   A 1 222 ? -25.932 7.028   22.344  1.00 28.26 ?  222 ARG   A N   1 
ATOM   1677 C  CA  . ARG   A 1 222 ? -26.584 8.185   22.932  1.00 28.54 ?  222 ARG   A CA  1 
ATOM   1678 C  C   . ARG   A 1 222 ? -25.863 8.704   24.164  1.00 29.07 ?  222 ARG   A C   1 
ATOM   1679 O  O   . ARG   A 1 222 ? -26.285 9.722   24.719  1.00 27.56 ?  222 ARG   A O   1 
ATOM   1680 C  CB  . ARG   A 1 222 ? -28.037 7.841   23.285  1.00 31.33 ?  222 ARG   A CB  1 
ATOM   1681 C  CG  . ARG   A 1 222 ? -28.200 6.894   24.483  1.00 32.67 ?  222 ARG   A CG  1 
ATOM   1682 C  CD  . ARG   A 1 222 ? -29.690 6.725   24.852  1.00 36.97 ?  222 ARG   A CD  1 
ATOM   1683 N  NE  . ARG   A 1 222 ? -29.882 5.885   26.036  1.00 31.77 ?  222 ARG   A NE  1 
ATOM   1684 C  CZ  . ARG   A 1 222 ? -29.960 6.355   27.276  1.00 33.08 ?  222 ARG   A CZ  1 
ATOM   1685 N  NH1 . ARG   A 1 222 ? -29.857 7.660   27.496  1.00 35.13 ?  222 ARG   A NH1 1 
ATOM   1686 N  NH2 . ARG   A 1 222 ? -30.129 5.525   28.299  1.00 37.38 ?  222 ARG   A NH2 1 
ATOM   1687 N  N   . PHE   A 1 223 ? -24.787 8.050   24.586  1.00 27.47 ?  223 PHE   A N   1 
ATOM   1688 C  CA  . PHE   A 1 223 ? -24.110 8.389   25.826  1.00 30.58 ?  223 PHE   A CA  1 
ATOM   1689 C  C   . PHE   A 1 223 ? -23.029 9.436   25.608  1.00 31.40 ?  223 PHE   A C   1 
ATOM   1690 O  O   . PHE   A 1 223 ? -22.534 9.649   24.497  1.00 29.90 ?  223 PHE   A O   1 
ATOM   1691 C  CB  . PHE   A 1 223 ? -23.480 7.147   26.455  1.00 29.65 ?  223 PHE   A CB  1 
ATOM   1692 C  CG  . PHE   A 1 223 ? -24.477 6.183   27.026  1.00 31.89 ?  223 PHE   A CG  1 
ATOM   1693 C  CD1 . PHE   A 1 223 ? -25.660 6.641   27.578  1.00 32.23 ?  223 PHE   A CD1 1 
ATOM   1694 C  CD2 . PHE   A 1 223 ? -24.229 4.820   27.009  1.00 33.45 ?  223 PHE   A CD2 1 
ATOM   1695 C  CE1 . PHE   A 1 223 ? -26.585 5.758   28.105  1.00 34.33 ?  223 PHE   A CE1 1 
ATOM   1696 C  CE2 . PHE   A 1 223 ? -25.145 3.929   27.538  1.00 34.72 ?  223 PHE   A CE2 1 
ATOM   1697 C  CZ  . PHE   A 1 223 ? -26.326 4.398   28.088  1.00 36.22 ?  223 PHE   A CZ  1 
ATOM   1698 N  N   . THR   A 1 224 ? -22.666 10.094  26.705  1.00 29.57 ?  224 THR   A N   1 
ATOM   1699 C  CA  . THR   A 1 224 ? -21.450 10.886  26.752  1.00 29.57 ?  224 THR   A CA  1 
ATOM   1700 C  C   . THR   A 1 224 ? -20.614 10.388  27.926  1.00 33.76 ?  224 THR   A C   1 
ATOM   1701 O  O   . THR   A 1 224 ? -20.949 9.378   28.554  1.00 30.48 ?  224 THR   A O   1 
ATOM   1702 C  CB  . THR   A 1 224 ? -21.763 12.379  26.875  1.00 30.41 ?  224 THR   A CB  1 
ATOM   1703 O  OG1 . THR   A 1 224 ? -20.573 13.141  26.622  1.00 36.10 ?  224 THR   A OG1 1 
ATOM   1704 C  CG2 . THR   A 1 224 ? -22.310 12.710  28.272  1.00 36.64 ?  224 THR   A CG2 1 
ATOM   1705 N  N   . THR   A 1 225 ? -19.516 11.068  28.223  1.00 28.65 ?  225 THR   A N   1 
ATOM   1706 C  CA  . THR   A 1 225 ? -18.661 10.642  29.313  1.00 28.80 ?  225 THR   A CA  1 
ATOM   1707 C  C   . THR   A 1 225 ? -17.898 11.850  29.819  1.00 29.04 ?  225 THR   A C   1 
ATOM   1708 O  O   . THR   A 1 225 ? -17.728 12.842  29.106  1.00 29.84 ?  225 THR   A O   1 
ATOM   1709 C  CB  . THR   A 1 225 ? -17.688 9.538   28.875  1.00 30.36 ?  225 THR   A CB  1 
ATOM   1710 O  OG1 . THR   A 1 225 ? -16.967 9.052   30.017  1.00 29.92 ?  225 THR   A OG1 1 
ATOM   1711 C  CG2 . THR   A 1 225 ? -16.689 10.080  27.846  1.00 26.92 ?  225 THR   A CG2 1 
ATOM   1712 N  N   . THR   A 1 226 ? -17.461 11.770  31.069  1.00 29.69 ?  226 THR   A N   1 
ATOM   1713 C  CA  . THR   A 1 226 ? -16.437 12.702  31.496  1.00 28.39 ?  226 THR   A CA  1 
ATOM   1714 C  C   . THR   A 1 226 ? -15.083 12.194  31.019  1.00 28.11 ?  226 THR   A C   1 
ATOM   1715 O  O   . THR   A 1 226 ? -14.895 11.002  30.751  1.00 25.61 ?  226 THR   A O   1 
ATOM   1716 C  CB  . THR   A 1 226 ? -16.430 12.886  33.019  1.00 29.46 ?  226 THR   A CB  1 
ATOM   1717 O  OG1 . THR   A 1 226 ? -15.932 11.702  33.652  1.00 29.74 ?  226 THR   A OG1 1 
ATOM   1718 C  CG2 . THR   A 1 226 ? -17.826 13.188  33.526  1.00 24.67 ?  226 THR   A CG2 1 
ATOM   1719 N  N   . LEU   A 1 227 ? -14.135 13.121  30.902  1.00 30.28 ?  227 LEU   A N   1 
ATOM   1720 C  CA  . LEU   A 1 227 ? -12.798 12.730  30.474  1.00 30.61 ?  227 LEU   A CA  1 
ATOM   1721 C  C   . LEU   A 1 227 ? -12.171 11.759  31.467  1.00 28.66 ?  227 LEU   A C   1 
ATOM   1722 O  O   . LEU   A 1 227 ? -11.513 10.791  31.073  1.00 29.04 ?  227 LEU   A O   1 
ATOM   1723 C  CB  . LEU   A 1 227 ? -11.927 13.972  30.292  1.00 33.79 ?  227 LEU   A CB  1 
ATOM   1724 C  CG  . LEU   A 1 227 ? -10.474 13.751  29.882  1.00 32.41 ?  227 LEU   A CG  1 
ATOM   1725 C  CD1 . LEU   A 1 227 ? -10.412 13.079  28.512  1.00 34.54 ?  227 LEU   A CD1 1 
ATOM   1726 C  CD2 . LEU   A 1 227 ? -9.724  15.079  29.887  1.00 33.75 ?  227 LEU   A CD2 1 
ATOM   1727 N  N   . ASN   A 1 228 ? -12.388 11.979  32.766  1.00 32.49 ?  228 ASN   A N   1 
ATOM   1728 C  CA  . ASN   A 1 228 ? -11.748 11.107  33.746  1.00 29.35 ?  228 ASN   A CA  1 
ATOM   1729 C  C   . ASN   A 1 228 ? -12.369 9.715   33.752  1.00 29.54 ?  228 ASN   A C   1 
ATOM   1730 O  O   . ASN   A 1 228 ? -11.649 8.718   33.893  1.00 26.77 ?  228 ASN   A O   1 
ATOM   1731 C  CB  . ASN   A 1 228 ? -11.804 11.722  35.138  1.00 33.64 ?  228 ASN   A CB  1 
ATOM   1732 C  CG  . ASN   A 1 228 ? -10.833 11.059  36.080  1.00 37.27 ?  228 ASN   A CG  1 
ATOM   1733 O  OD1 . ASN   A 1 228 ? -9.618  11.185  35.913  1.00 38.88 ?  228 ASN   A OD1 1 
ATOM   1734 N  ND2 . ASN   A 1 228 ? -11.355 10.332  37.068  1.00 39.16 ?  228 ASN   A ND2 1 
ATOM   1735 N  N   . ASP   A 1 229 ? -13.700 9.618   33.596  1.00 27.67 ?  229 ASP   A N   1 
ATOM   1736 C  CA  . ASP   A 1 229 ? -14.321 8.301   33.482  1.00 26.58 ?  229 ASP   A CA  1 
ATOM   1737 C  C   . ASP   A 1 229 ? -13.854 7.587   32.217  1.00 25.79 ?  229 ASP   A C   1 
ATOM   1738 O  O   . ASP   A 1 229 ? -13.626 6.371   32.232  1.00 24.57 ?  229 ASP   A O   1 
ATOM   1739 C  CB  . ASP   A 1 229 ? -15.853 8.416   33.498  1.00 25.51 ?  229 ASP   A CB  1 
ATOM   1740 C  CG  . ASP   A 1 229 ? -16.428 8.570   34.914  1.00 33.21 ?  229 ASP   A CG  1 
ATOM   1741 O  OD1 . ASP   A 1 229 ? -15.657 8.498   35.904  1.00 31.65 ?  229 ASP   A OD1 1 
ATOM   1742 O  OD2 . ASP   A 1 229 ? -17.664 8.755   35.026  1.00 33.98 ?  229 ASP   A OD2 1 
ATOM   1743 N  N   . PHE   A 1 230 ? -13.724 8.317   31.109  1.00 28.12 ?  230 PHE   A N   1 
ATOM   1744 C  CA  . PHE   A 1 230 ? -13.190 7.696   29.899  1.00 26.44 ?  230 PHE   A CA  1 
ATOM   1745 C  C   . PHE   A 1 230 ? -11.814 7.094   30.160  1.00 27.52 ?  230 PHE   A C   1 
ATOM   1746 O  O   . PHE   A 1 230 ? -11.541 5.946   29.786  1.00 26.66 ?  230 PHE   A O   1 
ATOM   1747 C  CB  . PHE   A 1 230 ? -13.113 8.703   28.755  1.00 23.21 ?  230 PHE   A CB  1 
ATOM   1748 C  CG  . PHE   A 1 230 ? -12.384 8.163   27.562  1.00 25.99 ?  230 PHE   A CG  1 
ATOM   1749 C  CD1 . PHE   A 1 230 ? -13.000 7.243   26.729  1.00 25.18 ?  230 PHE   A CD1 1 
ATOM   1750 C  CD2 . PHE   A 1 230 ? -11.062 8.517   27.313  1.00 27.98 ?  230 PHE   A CD2 1 
ATOM   1751 C  CE1 . PHE   A 1 230 ? -12.329 6.723   25.637  1.00 27.48 ?  230 PHE   A CE1 1 
ATOM   1752 C  CE2 . PHE   A 1 230 ? -10.380 7.991   26.233  1.00 27.52 ?  230 PHE   A CE2 1 
ATOM   1753 C  CZ  . PHE   A 1 230 ? -11.017 7.095   25.390  1.00 27.09 ?  230 PHE   A CZ  1 
ATOM   1754 N  N   . ASN   A 1 231 ? -10.941 7.844   30.839  1.00 26.40 ?  231 ASN   A N   1 
ATOM   1755 C  CA  . ASN   A 1 231 ? -9.584  7.356   31.054  1.00 26.90 ?  231 ASN   A CA  1 
ATOM   1756 C  C   . ASN   A 1 231 ? -9.558  6.177   32.015  1.00 29.64 ?  231 ASN   A C   1 
ATOM   1757 O  O   . ASN   A 1 231 ? -8.761  5.253   31.833  1.00 27.83 ?  231 ASN   A O   1 
ATOM   1758 C  CB  . ASN   A 1 231 ? -8.680  8.483   31.554  1.00 29.71 ?  231 ASN   A CB  1 
ATOM   1759 C  CG  . ASN   A 1 231 ? -8.252  9.413   30.443  1.00 30.52 ?  231 ASN   A CG  1 
ATOM   1760 O  OD1 . ASN   A 1 231 ? -8.068  8.986   29.301  1.00 31.34 ?  231 ASN   A OD1 1 
ATOM   1761 N  ND2 . ASN   A 1 231 ? -8.097  10.690  30.762  1.00 32.40 ?  231 ASN   A ND2 1 
ATOM   1762 N  N   . LEU   A 1 232 ? -10.412 6.187   33.049  1.00 26.06 ?  232 LEU   A N   1 
ATOM   1763 C  CA  . LEU   A 1 232 ? -10.447 5.049   33.963  1.00 24.35 ?  232 LEU   A CA  1 
ATOM   1764 C  C   . LEU   A 1 232 ? -10.812 3.766   33.226  1.00 26.19 ?  232 LEU   A C   1 
ATOM   1765 O  O   . LEU   A 1 232 ? -10.247 2.702   33.501  1.00 26.10 ?  232 LEU   A O   1 
ATOM   1766 C  CB  . LEU   A 1 232 ? -11.433 5.311   35.112  1.00 24.54 ?  232 LEU   A CB  1 
ATOM   1767 C  CG  . LEU   A 1 232 ? -11.007 6.329   36.177  1.00 29.02 ?  232 LEU   A CG  1 
ATOM   1768 C  CD1 . LEU   A 1 232 ? -12.178 6.646   37.114  1.00 26.77 ?  232 LEU   A CD1 1 
ATOM   1769 C  CD2 . LEU   A 1 232 ? -9.789  5.825   36.976  1.00 27.87 ?  232 LEU   A CD2 1 
ATOM   1770 N  N   . VAL   A 1 233 ? -11.763 3.846   32.289  1.00 24.10 ?  233 VAL   A N   1 
ATOM   1771 C  CA  . VAL   A 1 233 ? -12.151 2.668   31.517  1.00 22.93 ?  233 VAL   A CA  1 
ATOM   1772 C  C   . VAL   A 1 233 ? -11.063 2.310   30.505  1.00 24.87 ?  233 VAL   A C   1 
ATOM   1773 O  O   . VAL   A 1 233 ? -10.624 1.157   30.418  1.00 26.45 ?  233 VAL   A O   1 
ATOM   1774 C  CB  . VAL   A 1 233 ? -13.500 2.904   30.815  1.00 24.14 ?  233 VAL   A CB  1 
ATOM   1775 C  CG1 . VAL   A 1 233 ? -13.805 1.754   29.842  1.00 23.47 ?  233 VAL   A CG1 1 
ATOM   1776 C  CG2 . VAL   A 1 233 ? -14.607 3.057   31.819  1.00 26.75 ?  233 VAL   A CG2 1 
ATOM   1777 N  N   . ALA   A 1 234 ? -10.625 3.293   29.719  1.00 24.59 ?  234 ALA   A N   1 
ATOM   1778 C  CA  . ALA   A 1 234 ? -9.723  3.001   28.602  1.00 27.26 ?  234 ALA   A CA  1 
ATOM   1779 C  C   . ALA   A 1 234 ? -8.415  2.391   29.094  1.00 26.43 ?  234 ALA   A C   1 
ATOM   1780 O  O   . ALA   A 1 234 ? -7.878  1.469   28.473  1.00 26.67 ?  234 ALA   A O   1 
ATOM   1781 C  CB  . ALA   A 1 234 ? -9.469  4.271   27.790  1.00 26.69 ?  234 ALA   A CB  1 
ATOM   1782 N  N   . MET   A 1 235 ? -7.924  2.836   30.250  1.00 30.86 ?  235 MET   A N   1 
ATOM   1783 C  CA  . MET   A 1 235 ? -6.669  2.288   30.753  1.00 32.12 ?  235 MET   A CA  1 
ATOM   1784 C  C   . MET   A 1 235 ? -6.779  0.821   31.158  1.00 28.81 ?  235 MET   A C   1 
ATOM   1785 O  O   . MET   A 1 235 ? -5.758  0.129   31.207  1.00 30.01 ?  235 MET   A O   1 
ATOM   1786 C  CB  . MET   A 1 235 ? -6.165  3.148   31.907  1.00 32.56 ?  235 MET   A CB  1 
ATOM   1787 C  CG  . MET   A 1 235 ? -5.723  4.534   31.437  1.00 36.16 ?  235 MET   A CG  1 
ATOM   1788 S  SD  . MET   A 1 235 ? -5.079  5.587   32.744  1.00 49.45 ?  235 MET   A SD  1 
ATOM   1789 C  CE  . MET   A 1 235 ? -3.521  4.775   33.132  1.00 36.52 ?  235 MET   A CE  1 
ATOM   1790 N  N   . LYS   A 1 236 ? -7.984  0.312   31.410  1.00 28.38 ?  236 LYS   A N   1 
ATOM   1791 C  CA  . LYS   A 1 236 ? -8.126  -1.114  31.676  1.00 25.91 ?  236 LYS   A CA  1 
ATOM   1792 C  C   . LYS   A 1 236 ? -8.003  -1.959  30.413  1.00 27.23 ?  236 LYS   A C   1 
ATOM   1793 O  O   . LYS   A 1 236 ? -7.887  -3.187  30.509  1.00 26.15 ?  236 LYS   A O   1 
ATOM   1794 C  CB  . LYS   A 1 236 ? -9.459  -1.382  32.385  1.00 30.66 ?  236 LYS   A CB  1 
ATOM   1795 C  CG  . LYS   A 1 236 ? -9.627  -0.566  33.660  1.00 29.30 ?  236 LYS   A CG  1 
ATOM   1796 C  CD  . LYS   A 1 236 ? -10.974 -0.810  34.336  1.00 24.74 ?  236 LYS   A CD  1 
ATOM   1797 C  CE  . LYS   A 1 236 ? -11.192 0.161   35.496  1.00 29.09 ?  236 LYS   A CE  1 
ATOM   1798 N  NZ  . LYS   A 1 236 ? -12.551 0.018   36.142  1.00 24.77 ?  236 LYS   A NZ  1 
ATOM   1799 N  N   . TYR   A 1 237 ? -8.028  -1.337  29.233  1.00 25.81 ?  237 TYR   A N   1 
ATOM   1800 C  CA  . TYR   A 1 237 ? -7.723  -2.022  27.988  1.00 24.05 ?  237 TYR   A CA  1 
ATOM   1801 C  C   . TYR   A 1 237 ? -6.319  -1.706  27.495  1.00 29.81 ?  237 TYR   A C   1 
ATOM   1802 O  O   . TYR   A 1 237 ? -6.015  -1.938  26.319  1.00 25.69 ?  237 TYR   A O   1 
ATOM   1803 C  CB  . TYR   A 1 237 ? -8.751  -1.658  26.913  1.00 25.06 ?  237 TYR   A CB  1 
ATOM   1804 C  CG  . TYR   A 1 237 ? -10.186 -2.016  27.259  1.00 30.02 ?  237 TYR   A CG  1 
ATOM   1805 C  CD1 . TYR   A 1 237 ? -10.712 -3.258  26.921  1.00 26.97 ?  237 TYR   A CD1 1 
ATOM   1806 C  CD2 . TYR   A 1 237 ? -11.022 -1.103  27.896  1.00 27.86 ?  237 TYR   A CD2 1 
ATOM   1807 C  CE1 . TYR   A 1 237 ? -12.021 -3.592  27.216  1.00 28.78 ?  237 TYR   A CE1 1 
ATOM   1808 C  CE2 . TYR   A 1 237 ? -12.347 -1.429  28.194  1.00 27.41 ?  237 TYR   A CE2 1 
ATOM   1809 C  CZ  . TYR   A 1 237 ? -12.835 -2.675  27.848  1.00 26.85 ?  237 TYR   A CZ  1 
ATOM   1810 O  OH  . TYR   A 1 237 ? -14.131 -3.018  28.121  1.00 29.04 ?  237 TYR   A OH  1 
ATOM   1811 N  N   . ASN   A 1 238 ? -5.461  -1.165  28.368  1.00 26.81 ?  238 ASN   A N   1 
ATOM   1812 C  CA  . ASN   A 1 238 ? -4.086  -0.827  28.010  1.00 29.83 ?  238 ASN   A CA  1 
ATOM   1813 C  C   . ASN   A 1 238 ? -4.049  0.256   26.927  1.00 31.65 ?  238 ASN   A C   1 
ATOM   1814 O  O   . ASN   A 1 238 ? -3.188  0.255   26.045  1.00 32.24 ?  238 ASN   A O   1 
ATOM   1815 C  CB  . ASN   A 1 238 ? -3.322  -2.085  27.586  1.00 31.39 ?  238 ASN   A CB  1 
ATOM   1816 C  CG  . ASN   A 1 238 ? -1.827  -1.895  27.594  1.00 44.15 ?  238 ASN   A CG  1 
ATOM   1817 O  OD1 . ASN   A 1 238 ? -1.208  -1.826  28.651  1.00 51.94 ?  238 ASN   A OD1 1 
ATOM   1818 N  ND2 . ASN   A 1 238 ? -1.232  -1.830  26.407  1.00 44.82 ?  238 ASN   A ND2 1 
ATOM   1819 N  N   . TYR   A 1 239 ? -5.002  1.182   26.996  1.00 30.55 ?  239 TYR   A N   1 
ATOM   1820 C  CA  . TYR   A 1 239 ? -5.009  2.383   26.172  1.00 26.13 ?  239 TYR   A CA  1 
ATOM   1821 C  C   . TYR   A 1 239 ? -4.299  3.518   26.902  1.00 32.40 ?  239 TYR   A C   1 
ATOM   1822 O  O   . TYR   A 1 239 ? -4.434  3.665   28.120  1.00 27.25 ?  239 TYR   A O   1 
ATOM   1823 C  CB  . TYR   A 1 239 ? -6.448  2.796   25.841  1.00 25.84 ?  239 TYR   A CB  1 
ATOM   1824 C  CG  . TYR   A 1 239 ? -7.006  2.184   24.568  1.00 24.16 ?  239 TYR   A CG  1 
ATOM   1825 C  CD1 . TYR   A 1 239 ? -7.095  0.806   24.409  1.00 24.27 ?  239 TYR   A CD1 1 
ATOM   1826 C  CD2 . TYR   A 1 239 ? -7.442  2.989   23.522  1.00 30.23 ?  239 TYR   A CD2 1 
ATOM   1827 C  CE1 . TYR   A 1 239 ? -7.590  0.248   23.226  1.00 23.30 ?  239 TYR   A CE1 1 
ATOM   1828 C  CE2 . TYR   A 1 239 ? -7.947  2.440   22.345  1.00 26.60 ?  239 TYR   A CE2 1 
ATOM   1829 C  CZ  . TYR   A 1 239 ? -8.022  1.070   22.210  1.00 24.68 ?  239 TYR   A CZ  1 
ATOM   1830 O  OH  . TYR   A 1 239 ? -8.513  0.515   21.047  1.00 27.21 ?  239 TYR   A OH  1 
ATOM   1831 N  N   . GLU   A 1 240 ? -3.541  4.320   26.155  1.00 29.41 ?  240 GLU   A N   1 
ATOM   1832 C  CA  . GLU   A 1 240 ? -2.878  5.470   26.750  1.00 30.95 ?  240 GLU   A CA  1 
ATOM   1833 C  C   . GLU   A 1 240 ? -3.928  6.478   27.225  1.00 33.42 ?  240 GLU   A C   1 
ATOM   1834 O  O   . GLU   A 1 240 ? -4.994  6.612   26.618  1.00 30.86 ?  240 GLU   A O   1 
ATOM   1835 C  CB  . GLU   A 1 240 ? -1.922  6.121   25.741  1.00 28.55 ?  240 GLU   A CB  1 
ATOM   1836 N  N   . PRO   A 1 241 ? -3.679  7.165   28.334  1.00 35.94 ?  241 PRO   A N   1 
ATOM   1837 C  CA  . PRO   A 1 241 ? -4.679  8.116   28.829  1.00 36.04 ?  241 PRO   A CA  1 
ATOM   1838 C  C   . PRO   A 1 241 ? -4.804  9.305   27.889  1.00 35.83 ?  241 PRO   A C   1 
ATOM   1839 O  O   . PRO   A 1 241 ? -3.839  9.724   27.244  1.00 35.12 ?  241 PRO   A O   1 
ATOM   1840 C  CB  . PRO   A 1 241 ? -4.144  8.527   30.209  1.00 36.73 ?  241 PRO   A CB  1 
ATOM   1841 C  CG  . PRO   A 1 241 ? -2.683  8.169   30.188  1.00 33.71 ?  241 PRO   A CG  1 
ATOM   1842 C  CD  . PRO   A 1 241 ? -2.537  7.007   29.258  1.00 38.78 ?  241 PRO   A CD  1 
ATOM   1843 N  N   . LEU   A 1 242 ? -6.032  9.813   27.783  1.00 30.81 ?  242 LEU   A N   1 
ATOM   1844 C  CA  . LEU   A 1 242 ? -6.349  10.948  26.924  1.00 31.76 ?  242 LEU   A CA  1 
ATOM   1845 C  C   . LEU   A 1 242 ? -6.245  12.238  27.731  1.00 36.99 ?  242 LEU   A C   1 
ATOM   1846 O  O   . LEU   A 1 242 ? -6.803  12.338  28.828  1.00 34.34 ?  242 LEU   A O   1 
ATOM   1847 C  CB  . LEU   A 1 242 ? -7.757  10.793  26.334  1.00 27.42 ?  242 LEU   A CB  1 
ATOM   1848 C  CG  . LEU   A 1 242 ? -8.165  11.720  25.189  1.00 32.78 ?  242 LEU   A CG  1 
ATOM   1849 C  CD1 . LEU   A 1 242 ? -7.460  11.330  23.890  1.00 25.32 ?  242 LEU   A CD1 1 
ATOM   1850 C  CD2 . LEU   A 1 242 ? -9.681  11.727  24.996  1.00 30.87 ?  242 LEU   A CD2 1 
ATOM   1851 N  N   . THR   A 1 243 ? -5.532  13.222  27.192  1.00 37.23 ?  243 THR   A N   1 
ATOM   1852 C  CA  . THR   A 1 243 ? -5.302  14.482  27.887  1.00 37.15 ?  243 THR   A CA  1 
ATOM   1853 C  C   . THR   A 1 243 ? -6.142  15.586  27.263  1.00 36.73 ?  243 THR   A C   1 
ATOM   1854 O  O   . THR   A 1 243 ? -6.754  15.417  26.205  1.00 37.55 ?  243 THR   A O   1 
ATOM   1855 C  CB  . THR   A 1 243 ? -3.820  14.870  27.847  1.00 39.79 ?  243 THR   A CB  1 
ATOM   1856 O  OG1 . THR   A 1 243 ? -3.435  15.130  26.492  1.00 39.28 ?  243 THR   A OG1 1 
ATOM   1857 C  CG2 . THR   A 1 243 ? -2.963  13.752  28.398  1.00 35.05 ?  243 THR   A CG2 1 
ATOM   1858 N  N   . GLN   A 1 244 ? -6.159  16.739  27.934  1.00 33.88 ?  244 GLN   A N   1 
ATOM   1859 C  CA  . GLN   A 1 244 ? -6.911  17.870  27.401  1.00 39.45 ?  244 GLN   A CA  1 
ATOM   1860 C  C   . GLN   A 1 244 ? -6.269  18.429  26.137  1.00 44.59 ?  244 GLN   A C   1 
ATOM   1861 O  O   . GLN   A 1 244 ? -6.979  18.924  25.253  1.00 42.88 ?  244 GLN   A O   1 
ATOM   1862 C  CB  . GLN   A 1 244 ? -7.051  18.962  28.459  1.00 38.48 ?  244 GLN   A CB  1 
ATOM   1863 C  CG  . GLN   A 1 244 ? -7.916  20.135  28.022  1.00 39.23 ?  244 GLN   A CG  1 
ATOM   1864 C  CD  . GLN   A 1 244 ? -9.317  19.714  27.602  1.00 43.05 ?  244 GLN   A CD  1 
ATOM   1865 O  OE1 . GLN   A 1 244 ? -9.938  18.852  28.228  1.00 42.93 ?  244 GLN   A OE1 1 
ATOM   1866 N  NE2 . GLN   A 1 244 ? -9.815  20.319  26.531  1.00 40.14 ?  244 GLN   A NE2 1 
ATOM   1867 N  N   . ASP   A 1 245 ? -4.936  18.374  26.032  1.00 44.19 ?  245 ASP   A N   1 
ATOM   1868 C  CA  . ASP   A 1 245 ? -4.296  18.723  24.767  1.00 41.75 ?  245 ASP   A CA  1 
ATOM   1869 C  C   . ASP   A 1 245 ? -4.807  17.838  23.642  1.00 43.03 ?  245 ASP   A C   1 
ATOM   1870 O  O   . ASP   A 1 245 ? -5.101  18.325  22.546  1.00 42.36 ?  245 ASP   A O   1 
ATOM   1871 C  CB  . ASP   A 1 245 ? -2.776  18.605  24.874  1.00 43.10 ?  245 ASP   A CB  1 
ATOM   1872 C  CG  . ASP   A 1 245 ? -2.158  19.717  25.702  1.00 50.71 ?  245 ASP   A CG  1 
ATOM   1873 O  OD1 . ASP   A 1 245 ? -2.811  20.772  25.864  1.00 54.12 ?  245 ASP   A OD1 1 
ATOM   1874 O  OD2 . ASP   A 1 245 ? -1.015  19.535  26.183  1.00 54.02 ?  245 ASP   A OD2 1 
ATOM   1875 N  N   . HIS   A 1 246 ? -4.918  16.532  23.896  1.00 41.47 ?  246 HIS   A N   1 
ATOM   1876 C  CA  . HIS   A 1 246 ? -5.492  15.625  22.908  1.00 40.08 ?  246 HIS   A CA  1 
ATOM   1877 C  C   . HIS   A 1 246 ? -6.916  16.029  22.537  1.00 37.32 ?  246 HIS   A C   1 
ATOM   1878 O  O   . HIS   A 1 246 ? -7.281  16.035  21.353  1.00 34.81 ?  246 HIS   A O   1 
ATOM   1879 C  CB  . HIS   A 1 246 ? -5.465  14.194  23.442  1.00 37.15 ?  246 HIS   A CB  1 
ATOM   1880 C  CG  . HIS   A 1 246 ? -4.088  13.632  23.600  1.00 33.95 ?  246 HIS   A CG  1 
ATOM   1881 N  ND1 . HIS   A 1 246 ? -3.802  12.599  24.465  1.00 36.22 ?  246 HIS   A ND1 1 
ATOM   1882 C  CD2 . HIS   A 1 246 ? -2.920  13.946  22.989  1.00 34.48 ?  246 HIS   A CD2 1 
ATOM   1883 C  CE1 . HIS   A 1 246 ? -2.515  12.308  24.390  1.00 38.66 ?  246 HIS   A CE1 1 
ATOM   1884 N  NE2 . HIS   A 1 246 ? -1.957  13.111  23.501  1.00 34.99 ?  246 HIS   A NE2 1 
ATOM   1885 N  N   . VAL   A 1 247 ? -7.735  16.370  23.533  1.00 34.19 ?  247 VAL   A N   1 
ATOM   1886 C  CA  . VAL   A 1 247 ? -9.111  16.771  23.253  1.00 36.57 ?  247 VAL   A CA  1 
ATOM   1887 C  C   . VAL   A 1 247 ? -9.139  18.002  22.353  1.00 37.39 ?  247 VAL   A C   1 
ATOM   1888 O  O   . VAL   A 1 247 ? -9.949  18.088  21.419  1.00 40.19 ?  247 VAL   A O   1 
ATOM   1889 C  CB  . VAL   A 1 247 ? -9.876  17.012  24.566  1.00 36.10 ?  247 VAL   A CB  1 
ATOM   1890 C  CG1 . VAL   A 1 247 ? -11.203 17.674  24.276  1.00 31.48 ?  247 VAL   A CG1 1 
ATOM   1891 C  CG2 . VAL   A 1 247 ? -10.074 15.698  25.314  1.00 33.98 ?  247 VAL   A CG2 1 
ATOM   1892 N  N   . ASP   A 1 248 ? -8.261  18.976  22.618  1.00 38.91 ?  248 ASP   A N   1 
ATOM   1893 C  CA  . ASP   A 1 248 ? -8.189  20.153  21.759  1.00 39.59 ?  248 ASP   A CA  1 
ATOM   1894 C  C   . ASP   A 1 248 ? -7.693  19.792  20.368  1.00 37.10 ?  248 ASP   A C   1 
ATOM   1895 O  O   . ASP   A 1 248 ? -8.119  20.402  19.382  1.00 43.76 ?  248 ASP   A O   1 
ATOM   1896 C  CB  . ASP   A 1 248 ? -7.274  21.219  22.369  1.00 40.49 ?  248 ASP   A CB  1 
ATOM   1897 C  CG  . ASP   A 1 248 ? -7.582  21.504  23.829  1.00 43.29 ?  248 ASP   A CG  1 
ATOM   1898 O  OD1 . ASP   A 1 248 ? -8.744  21.337  24.241  1.00 43.70 ?  248 ASP   A OD1 1 
ATOM   1899 O  OD2 . ASP   A 1 248 ? -6.651  21.894  24.568  1.00 43.00 ?  248 ASP   A OD2 1 
ATOM   1900 N  N   . ILE   A 1 249 ? -6.794  18.809  20.268  1.00 40.70 ?  249 ILE   A N   1 
ATOM   1901 C  CA  . ILE   A 1 249 ? -6.249  18.432  18.964  1.00 41.02 ?  249 ILE   A CA  1 
ATOM   1902 C  C   . ILE   A 1 249 ? -7.323  17.791  18.092  1.00 39.88 ?  249 ILE   A C   1 
ATOM   1903 O  O   . ILE   A 1 249 ? -7.276  17.893  16.859  1.00 37.95 ?  249 ILE   A O   1 
ATOM   1904 C  CB  . ILE   A 1 249 ? -5.024  17.518  19.162  1.00 43.32 ?  249 ILE   A CB  1 
ATOM   1905 C  CG1 . ILE   A 1 249 ? -3.850  18.341  19.678  1.00 42.12 ?  249 ILE   A CG1 1 
ATOM   1906 C  CG2 . ILE   A 1 249 ? -4.622  16.817  17.881  1.00 38.09 ?  249 ILE   A CG2 1 
ATOM   1907 C  CD1 . ILE   A 1 249 ? -3.735  19.700  19.017  1.00 44.08 ?  249 ILE   A CD1 1 
ATOM   1908 N  N   . LEU   A 1 250 ? -8.321  17.155  18.709  1.00 37.64 ?  250 LEU   A N   1 
ATOM   1909 C  CA  . LEU   A 1 250 ? -9.451  16.581  17.988  1.00 36.46 ?  250 LEU   A CA  1 
ATOM   1910 C  C   . LEU   A 1 250 ? -10.539 17.598  17.675  1.00 36.57 ?  250 LEU   A C   1 
ATOM   1911 O  O   . LEU   A 1 250 ? -11.527 17.241  17.021  1.00 38.71 ?  250 LEU   A O   1 
ATOM   1912 C  CB  . LEU   A 1 250 ? -10.042 15.421  18.790  1.00 31.91 ?  250 LEU   A CB  1 
ATOM   1913 C  CG  . LEU   A 1 250 ? -9.081  14.238  18.933  1.00 33.60 ?  250 LEU   A CG  1 
ATOM   1914 C  CD1 . LEU   A 1 250 ? -9.531  13.277  20.015  1.00 33.51 ?  250 LEU   A CD1 1 
ATOM   1915 C  CD2 . LEU   A 1 250 ? -8.928  13.506  17.600  1.00 30.58 ?  250 LEU   A CD2 1 
ATOM   1916 N  N   . GLY   A 1 251 ? -10.375 18.845  18.111  1.00 35.65 ?  251 GLY   A N   1 
ATOM   1917 C  CA  . GLY   A 1 251 ? -11.332 19.896  17.852  1.00 36.73 ?  251 GLY   A CA  1 
ATOM   1918 C  C   . GLY   A 1 251 ? -11.783 19.991  16.405  1.00 38.76 ?  251 GLY   A C   1 
ATOM   1919 O  O   . GLY   A 1 251 ? -12.975 19.885  16.106  1.00 38.88 ?  251 GLY   A O   1 
ATOM   1920 N  N   . PRO   A 1 252 ? -10.842 20.210  15.478  1.00 39.82 ?  252 PRO   A N   1 
ATOM   1921 C  CA  . PRO   A 1 252 ? -11.225 20.314  14.056  1.00 41.94 ?  252 PRO   A CA  1 
ATOM   1922 C  C   . PRO   A 1 252 ? -12.036 19.137  13.536  1.00 39.77 ?  252 PRO   A C   1 
ATOM   1923 O  O   . PRO   A 1 252 ? -13.000 19.339  12.790  1.00 39.08 ?  252 PRO   A O   1 
ATOM   1924 C  CB  . PRO   A 1 252 ? -9.869  20.417  13.349  1.00 35.86 ?  252 PRO   A CB  1 
ATOM   1925 C  CG  . PRO   A 1 252 ? -8.997  21.086  14.346  1.00 39.98 ?  252 PRO   A CG  1 
ATOM   1926 C  CD  . PRO   A 1 252 ? -9.430  20.572  15.692  1.00 37.94 ?  252 PRO   A CD  1 
ATOM   1927 N  N   . LEU   A 1 253 ? -11.670 17.909  13.904  1.00 38.96 ?  253 LEU   A N   1 
ATOM   1928 C  CA  . LEU   A 1 253 ? -12.463 16.758  13.486  1.00 36.08 ?  253 LEU   A CA  1 
ATOM   1929 C  C   . LEU   A 1 253 ? -13.839 16.770  14.139  1.00 37.33 ?  253 LEU   A C   1 
ATOM   1930 O  O   . LEU   A 1 253 ? -14.845 16.446  13.491  1.00 38.04 ?  253 LEU   A O   1 
ATOM   1931 C  CB  . LEU   A 1 253 ? -11.717 15.469  13.814  1.00 32.08 ?  253 LEU   A CB  1 
ATOM   1932 C  CG  . LEU   A 1 253 ? -10.543 15.187  12.883  1.00 34.90 ?  253 LEU   A CG  1 
ATOM   1933 C  CD1 . LEU   A 1 253 ? -9.767  13.982  13.365  1.00 30.46 ?  253 LEU   A CD1 1 
ATOM   1934 C  CD2 . LEU   A 1 253 ? -11.064 14.964  11.464  1.00 31.25 ?  253 LEU   A CD2 1 
ATOM   1935 N  N   . SER   A 1 254 ? -13.898 17.138  15.424  1.00 34.66 ?  254 SER   A N   1 
ATOM   1936 C  CA  . SER   A 1 254 ? -15.174 17.228  16.125  1.00 35.36 ?  254 SER   A CA  1 
ATOM   1937 C  C   . SER   A 1 254 ? -16.069 18.287  15.501  1.00 36.06 ?  254 SER   A C   1 
ATOM   1938 O  O   . SER   A 1 254 ? -17.282 18.087  15.371  1.00 34.40 ?  254 SER   A O   1 
ATOM   1939 C  CB  . SER   A 1 254 ? -14.935 17.533  17.607  1.00 34.67 ?  254 SER   A CB  1 
ATOM   1940 O  OG  . SER   A 1 254 ? -16.160 17.688  18.306  1.00 37.69 ?  254 SER   A OG  1 
ATOM   1941 N  N   . ALA   A 1 255 ? -15.487 19.423  15.107  1.00 36.18 ?  255 ALA   A N   1 
ATOM   1942 C  CA  . ALA   A 1 255 ? -16.274 20.490  14.497  1.00 40.15 ?  255 ALA   A CA  1 
ATOM   1943 C  C   . ALA   A 1 255 ? -16.781 20.103  13.113  1.00 39.19 ?  255 ALA   A C   1 
ATOM   1944 O  O   . ALA   A 1 255 ? -17.861 20.546  12.706  1.00 45.45 ?  255 ALA   A O   1 
ATOM   1945 C  CB  . ALA   A 1 255 ? -15.450 21.775  14.417  1.00 36.46 ?  255 ALA   A CB  1 
ATOM   1946 N  N   . GLN   A 1 256 ? -16.033 19.277  12.382  1.00 39.42 ?  256 GLN   A N   1 
ATOM   1947 C  CA  . GLN   A 1 256 ? -16.459 18.903  11.034  1.00 44.18 ?  256 GLN   A CA  1 
ATOM   1948 C  C   . GLN   A 1 256 ? -17.620 17.912  11.060  1.00 38.60 ?  256 GLN   A C   1 
ATOM   1949 O  O   . GLN   A 1 256 ? -18.521 17.985  10.217  1.00 44.38 ?  256 GLN   A O   1 
ATOM   1950 C  CB  . GLN   A 1 256 ? -15.276 18.320  10.258  1.00 41.13 ?  256 GLN   A CB  1 
ATOM   1951 C  CG  . GLN   A 1 256 ? -15.609 17.906  8.837   1.00 44.66 ?  256 GLN   A CG  1 
ATOM   1952 C  CD  . GLN   A 1 256 ? -14.416 17.330  8.094   1.00 48.70 ?  256 GLN   A CD  1 
ATOM   1953 O  OE1 . GLN   A 1 256 ? -13.268 17.475  8.522   1.00 51.42 ?  256 GLN   A OE1 1 
ATOM   1954 N  NE2 . GLN   A 1 256 ? -14.686 16.668  6.973   1.00 44.50 ?  256 GLN   A NE2 1 
ATOM   1955 N  N   . THR   A 1 257 ? -17.616 16.984  12.015  1.00 37.71 ?  257 THR   A N   1 
ATOM   1956 C  CA  . THR   A 1 257 ? -18.631 15.944  12.097  1.00 35.44 ?  257 THR   A CA  1 
ATOM   1957 C  C   . THR   A 1 257 ? -19.788 16.299  13.023  1.00 36.66 ?  257 THR   A C   1 
ATOM   1958 O  O   . THR   A 1 257 ? -20.804 15.596  13.018  1.00 32.01 ?  257 THR   A O   1 
ATOM   1959 C  CB  . THR   A 1 257 ? -18.006 14.632  12.578  1.00 35.95 ?  257 THR   A CB  1 
ATOM   1960 O  OG1 . THR   A 1 257 ? -17.502 14.807  13.907  1.00 33.57 ?  257 THR   A OG1 1 
ATOM   1961 C  CG2 . THR   A 1 257 ? -16.867 14.218  11.671  1.00 29.96 ?  257 THR   A CG2 1 
ATOM   1962 N  N   . GLY   A 1 258 ? -19.664 17.358  13.817  1.00 34.59 ?  258 GLY   A N   1 
ATOM   1963 C  CA  . GLY   A 1 258 ? -20.707 17.656  14.774  1.00 40.39 ?  258 GLY   A CA  1 
ATOM   1964 C  C   . GLY   A 1 258 ? -20.788 16.712  15.952  1.00 35.91 ?  258 GLY   A C   1 
ATOM   1965 O  O   . GLY   A 1 258 ? -21.746 16.796  16.727  1.00 40.30 ?  258 GLY   A O   1 
ATOM   1966 N  N   . ILE   A 1 259 ? -19.821 15.814  16.112  1.00 37.52 ?  259 ILE   A N   1 
ATOM   1967 C  CA  . ILE   A 1 259 ? -19.772 14.883  17.235  1.00 32.48 ?  259 ILE   A CA  1 
ATOM   1968 C  C   . ILE   A 1 259 ? -18.756 15.406  18.240  1.00 33.20 ?  259 ILE   A C   1 
ATOM   1969 O  O   . ILE   A 1 259 ? -17.567 15.535  17.922  1.00 32.84 ?  259 ILE   A O   1 
ATOM   1970 C  CB  . ILE   A 1 259 ? -19.400 13.468  16.772  1.00 33.59 ?  259 ILE   A CB  1 
ATOM   1971 C  CG1 . ILE   A 1 259 ? -20.401 12.964  15.733  1.00 31.39 ?  259 ILE   A CG1 1 
ATOM   1972 C  CG2 . ILE   A 1 259 ? -19.323 12.515  17.971  1.00 32.64 ?  259 ILE   A CG2 1 
ATOM   1973 C  CD1 . ILE   A 1 259 ? -19.964 11.686  15.078  1.00 28.86 ?  259 ILE   A CD1 1 
ATOM   1974 N  N   . ALA   A 1 260 ? -19.216 15.715  19.448  1.00 28.69 ?  260 ALA   A N   1 
ATOM   1975 C  CA  . ALA   A 1 260 ? -18.305 16.202  20.473  1.00 28.77 ?  260 ALA   A CA  1 
ATOM   1976 C  C   . ALA   A 1 260 ? -17.294 15.121  20.837  1.00 28.39 ?  260 ALA   A C   1 
ATOM   1977 O  O   . ALA   A 1 260 ? -17.572 13.922  20.744  1.00 28.42 ?  260 ALA   A O   1 
ATOM   1978 C  CB  . ALA   A 1 260 ? -19.083 16.644  21.712  1.00 32.96 ?  260 ALA   A CB  1 
ATOM   1979 N  N   . VAL   A 1 261 ? -16.110 15.560  21.269  1.00 32.85 ?  261 VAL   A N   1 
ATOM   1980 C  CA  . VAL   A 1 261 ? -15.024 14.627  21.567  1.00 31.71 ?  261 VAL   A CA  1 
ATOM   1981 C  C   . VAL   A 1 261 ? -15.448 13.624  22.634  1.00 28.28 ?  261 VAL   A C   1 
ATOM   1982 O  O   . VAL   A 1 261 ? -15.271 12.409  22.475  1.00 27.31 ?  261 VAL   A O   1 
ATOM   1983 C  CB  . VAL   A 1 261 ? -13.757 15.400  21.979  1.00 29.43 ?  261 VAL   A CB  1 
ATOM   1984 C  CG1 . VAL   A 1 261 ? -12.705 14.456  22.539  1.00 28.69 ?  261 VAL   A CG1 1 
ATOM   1985 C  CG2 . VAL   A 1 261 ? -13.205 16.170  20.779  1.00 32.31 ?  261 VAL   A CG2 1 
ATOM   1986 N  N   . LEU   A 1 262 ? -16.017 14.112  23.737  1.00 27.01 ?  262 LEU   A N   1 
ATOM   1987 C  CA  . LEU   A 1 262 ? -16.445 13.201  24.795  1.00 29.27 ?  262 LEU   A CA  1 
ATOM   1988 C  C   . LEU   A 1 262 ? -17.588 12.284  24.357  1.00 28.97 ?  262 LEU   A C   1 
ATOM   1989 O  O   . LEU   A 1 262 ? -17.769 11.219  24.958  1.00 27.49 ?  262 LEU   A O   1 
ATOM   1990 C  CB  . LEU   A 1 262 ? -16.838 13.995  26.041  1.00 29.84 ?  262 LEU   A CB  1 
ATOM   1991 C  CG  . LEU   A 1 262 ? -15.616 14.648  26.696  1.00 32.15 ?  262 LEU   A CG  1 
ATOM   1992 C  CD1 . LEU   A 1 262 ? -16.025 15.545  27.847  1.00 27.64 ?  262 LEU   A CD1 1 
ATOM   1993 C  CD2 . LEU   A 1 262 ? -14.620 13.590  27.164  1.00 30.16 ?  262 LEU   A CD2 1 
ATOM   1994 N  N   . ASP   A 1 263 ? -18.353 12.654  23.322  1.00 28.31 ?  263 ASP   A N   1 
ATOM   1995 C  CA  . ASP   A 1 263 ? -19.324 11.711  22.765  1.00 26.99 ?  263 ASP   A CA  1 
ATOM   1996 C  C   . ASP   A 1 263 ? -18.636 10.631  21.928  1.00 27.95 ?  263 ASP   A C   1 
ATOM   1997 O  O   . ASP   A 1 263 ? -19.037 9.462   21.965  1.00 26.82 ?  263 ASP   A O   1 
ATOM   1998 C  CB  . ASP   A 1 263 ? -20.376 12.456  21.937  1.00 30.13 ?  263 ASP   A CB  1 
ATOM   1999 C  CG  . ASP   A 1 263 ? -21.242 13.371  22.788  1.00 35.82 ?  263 ASP   A CG  1 
ATOM   2000 O  OD1 . ASP   A 1 263 ? -21.042 13.392  24.020  1.00 36.97 ?  263 ASP   A OD1 1 
ATOM   2001 O  OD2 . ASP   A 1 263 ? -22.116 14.071  22.239  1.00 36.90 ?  263 ASP   A OD2 1 
ATOM   2002 N  N   . MET   A 1 264 ? -17.590 10.991  21.174  1.00 27.78 ?  264 MET   A N   1 
ATOM   2003 C  CA  . MET   A 1 264 ? -16.798 9.962   20.505  1.00 24.94 ?  264 MET   A CA  1 
ATOM   2004 C  C   . MET   A 1 264 ? -16.093 9.063   21.515  1.00 26.86 ?  264 MET   A C   1 
ATOM   2005 O  O   . MET   A 1 264 ? -15.923 7.861   21.273  1.00 24.80 ?  264 MET   A O   1 
ATOM   2006 C  CB  . MET   A 1 264 ? -15.780 10.593  19.551  1.00 27.60 ?  264 MET   A CB  1 
ATOM   2007 C  CG  . MET   A 1 264 ? -15.173 9.591   18.567  1.00 28.11 ?  264 MET   A CG  1 
ATOM   2008 S  SD  . MET   A 1 264 ? -16.423 8.860   17.455  1.00 32.03 ?  264 MET   A SD  1 
ATOM   2009 C  CE  . MET   A 1 264 ? -16.455 10.084  16.147  1.00 31.89 ?  264 MET   A CE  1 
ATOM   2010 N  N   . CYS   A 1 265 ? -15.665 9.627   22.653  1.00 26.11 ?  265 CYS   A N   1 
ATOM   2011 C  CA  . CYS   A 1 265 ? -15.066 8.807   23.703  1.00 25.97 ?  265 CYS   A CA  1 
ATOM   2012 C  C   . CYS   A 1 265 ? -16.057 7.778   24.234  1.00 27.27 ?  265 CYS   A C   1 
ATOM   2013 O  O   . CYS   A 1 265 ? -15.681 6.630   24.508  1.00 23.79 ?  265 CYS   A O   1 
ATOM   2014 C  CB  . CYS   A 1 265 ? -14.545 9.692   24.840  1.00 27.95 ?  265 CYS   A CB  1 
ATOM   2015 S  SG  . CYS   A 1 265 ? -13.066 10.667  24.415  1.00 28.83 ?  265 CYS   A SG  1 
ATOM   2016 N  N   . ALA   A 1 266 ? -17.331 8.171   24.376  1.00 27.82 ?  266 ALA   A N   1 
ATOM   2017 C  CA  . ALA   A 1 266 ? -18.378 7.225   24.759  1.00 23.03 ?  266 ALA   A CA  1 
ATOM   2018 C  C   . ALA   A 1 266 ? -18.481 6.080   23.758  1.00 26.90 ?  266 ALA   A C   1 
ATOM   2019 O  O   . ALA   A 1 266 ? -18.591 4.910   24.143  1.00 23.76 ?  266 ALA   A O   1 
ATOM   2020 C  CB  . ALA   A 1 266 ? -19.722 7.947   24.881  1.00 28.68 ?  266 ALA   A CB  1 
ATOM   2021 N  N   . SER   A 1 267 ? -18.441 6.398   22.460  1.00 25.72 ?  267 SER   A N   1 
ATOM   2022 C  CA  . SER   A 1 267 ? -18.486 5.345   21.449  1.00 26.80 ?  267 SER   A CA  1 
ATOM   2023 C  C   . SER   A 1 267 ? -17.298 4.399   21.573  1.00 24.39 ?  267 SER   A C   1 
ATOM   2024 O  O   . SER   A 1 267 ? -17.464 3.172   21.530  1.00 24.25 ?  267 SER   A O   1 
ATOM   2025 C  CB  . SER   A 1 267 ? -18.536 5.960   20.051  1.00 29.92 ?  267 SER   A CB  1 
ATOM   2026 O  OG  . SER   A 1 267 ? -18.310 4.962   19.073  1.00 33.76 ?  267 SER   A OG  1 
ATOM   2027 N  N   . LEU   A 1 268 ? -16.088 4.948   21.733  1.00 23.83 ?  268 LEU   A N   1 
ATOM   2028 C  CA  . LEU   A 1 268 ? -14.912 4.100   21.916  1.00 24.40 ?  268 LEU   A CA  1 
ATOM   2029 C  C   . LEU   A 1 268 ? -15.092 3.155   23.100  1.00 24.31 ?  268 LEU   A C   1 
ATOM   2030 O  O   . LEU   A 1 268 ? -14.791 1.960   22.995  1.00 24.70 ?  268 LEU   A O   1 
ATOM   2031 C  CB  . LEU   A 1 268 ? -13.662 4.961   22.098  1.00 22.86 ?  268 LEU   A CB  1 
ATOM   2032 C  CG  . LEU   A 1 268 ? -12.339 4.221   22.341  1.00 26.88 ?  268 LEU   A CG  1 
ATOM   2033 C  CD1 . LEU   A 1 268 ? -12.124 3.090   21.339  1.00 23.47 ?  268 LEU   A CD1 1 
ATOM   2034 C  CD2 . LEU   A 1 268 ? -11.164 5.185   22.290  1.00 26.29 ?  268 LEU   A CD2 1 
ATOM   2035 N  N   . LYS   A 1 269 ? -15.602 3.665   24.224  1.00 24.23 ?  269 LYS   A N   1 
ATOM   2036 C  CA  . LYS   A 1 269 ? -15.809 2.805   25.389  1.00 24.64 ?  269 LYS   A CA  1 
ATOM   2037 C  C   . LYS   A 1 269 ? -16.704 1.627   25.043  1.00 24.48 ?  269 LYS   A C   1 
ATOM   2038 O  O   . LYS   A 1 269 ? -16.438 0.491   25.455  1.00 24.46 ?  269 LYS   A O   1 
ATOM   2039 C  CB  . LYS   A 1 269 ? -16.418 3.594   26.551  1.00 27.20 ?  269 LYS   A CB  1 
ATOM   2040 C  CG  . LYS   A 1 269 ? -15.507 4.614   27.203  1.00 30.54 ?  269 LYS   A CG  1 
ATOM   2041 C  CD  . LYS   A 1 269 ? -16.327 5.610   28.017  1.00 30.26 ?  269 LYS   A CD  1 
ATOM   2042 C  CE  . LYS   A 1 269 ? -16.676 5.096   29.403  1.00 26.04 ?  269 LYS   A CE  1 
ATOM   2043 N  NZ  . LYS   A 1 269 ? -17.497 6.117   30.125  1.00 29.31 ?  269 LYS   A NZ  1 
ATOM   2044 N  N   . GLU   A 1 270 ? -17.773 1.878   24.278  1.00 23.92 ?  270 GLU   A N   1 
ATOM   2045 C  CA  . GLU   A 1 270 ? -18.677 0.793   23.916  1.00 24.03 ?  270 GLU   A CA  1 
ATOM   2046 C  C   . GLU   A 1 270 ? -18.008 -0.177  22.953  1.00 22.59 ?  270 GLU   A C   1 
ATOM   2047 O  O   . GLU   A 1 270 ? -18.194 -1.394  23.068  1.00 22.90 ?  270 GLU   A O   1 
ATOM   2048 C  CB  . GLU   A 1 270 ? -19.973 1.354   23.328  1.00 25.89 ?  270 GLU   A CB  1 
ATOM   2049 C  CG  . GLU   A 1 270 ? -21.064 0.310   23.149  1.00 25.47 ?  270 GLU   A CG  1 
ATOM   2050 C  CD  . GLU   A 1 270 ? -22.397 0.922   22.732  1.00 32.07 ?  270 GLU   A CD  1 
ATOM   2051 O  OE1 . GLU   A 1 270 ? -22.529 1.291   21.545  1.00 28.45 ?  270 GLU   A OE1 1 
ATOM   2052 O  OE2 . GLU   A 1 270 ? -23.306 1.048   23.594  1.00 27.92 ?  270 GLU   A OE2 1 
ATOM   2053 N  N   . LEU   A 1 271 ? -17.215 0.340   22.004  1.00 23.05 ?  271 LEU   A N   1 
ATOM   2054 C  CA  . LEU   A 1 271 ? -16.488 -0.539  21.092  1.00 24.99 ?  271 LEU   A CA  1 
ATOM   2055 C  C   . LEU   A 1 271 ? -15.546 -1.472  21.845  1.00 24.39 ?  271 LEU   A C   1 
ATOM   2056 O  O   . LEU   A 1 271 ? -15.453 -2.660  21.518  1.00 22.73 ?  271 LEU   A O   1 
ATOM   2057 C  CB  . LEU   A 1 271 ? -15.712 0.289   20.063  1.00 26.05 ?  271 LEU   A CB  1 
ATOM   2058 C  CG  . LEU   A 1 271 ? -16.611 0.941   19.012  1.00 27.80 ?  271 LEU   A CG  1 
ATOM   2059 C  CD1 . LEU   A 1 271 ? -15.849 1.941   18.168  1.00 26.18 ?  271 LEU   A CD1 1 
ATOM   2060 C  CD2 . LEU   A 1 271 ? -17.252 -0.131  18.147  1.00 29.75 ?  271 LEU   A CD2 1 
ATOM   2061 N  N   . LEU   A 1 272 ? -14.830 -0.952  22.849  1.00 22.92 ?  272 LEU   A N   1 
ATOM   2062 C  CA  . LEU   A 1 272 ? -13.955 -1.804  23.652  1.00 25.59 ?  272 LEU   A CA  1 
ATOM   2063 C  C   . LEU   A 1 272 ? -14.757 -2.857  24.398  1.00 24.28 ?  272 LEU   A C   1 
ATOM   2064 O  O   . LEU   A 1 272 ? -14.313 -3.999  24.571  1.00 22.39 ?  272 LEU   A O   1 
ATOM   2065 C  CB  . LEU   A 1 272 ? -13.156 -0.947  24.637  1.00 24.12 ?  272 LEU   A CB  1 
ATOM   2066 C  CG  . LEU   A 1 272 ? -12.198 0.042   23.968  1.00 26.12 ?  272 LEU   A CG  1 
ATOM   2067 C  CD1 . LEU   A 1 272 ? -11.671 1.075   24.958  1.00 25.32 ?  272 LEU   A CD1 1 
ATOM   2068 C  CD2 . LEU   A 1 272 ? -11.059 -0.733  23.369  1.00 26.01 ?  272 LEU   A CD2 1 
ATOM   2069 N  N   . GLN   A 1 273 ? -15.946 -2.480  24.848  1.00 24.74 ?  273 GLN   A N   1 
ATOM   2070 C  CA  . GLN   A 1 273 ? -16.809 -3.391  25.581  1.00 23.25 ?  273 GLN   A CA  1 
ATOM   2071 C  C   . GLN   A 1 273 ? -17.413 -4.459  24.674  1.00 24.18 ?  273 GLN   A C   1 
ATOM   2072 O  O   . GLN   A 1 273 ? -17.513 -5.627  25.070  1.00 24.79 ?  273 GLN   A O   1 
ATOM   2073 C  CB  . GLN   A 1 273 ? -17.888 -2.565  26.266  1.00 24.33 ?  273 GLN   A CB  1 
ATOM   2074 C  CG  . GLN   A 1 273 ? -19.014 -3.320  26.901  1.00 27.00 ?  273 GLN   A CG  1 
ATOM   2075 C  CD  . GLN   A 1 273 ? -20.133 -2.372  27.220  1.00 25.71 ?  273 GLN   A CD  1 
ATOM   2076 O  OE1 . GLN   A 1 273 ? -20.111 -1.700  28.244  1.00 28.18 ?  273 GLN   A OE1 1 
ATOM   2077 N  NE2 . GLN   A 1 273 ? -21.093 -2.261  26.311  1.00 24.37 ?  273 GLN   A NE2 1 
ATOM   2078 N  N   . ASN   A 1 274 ? -17.803 -4.090  23.449  1.00 26.85 ?  274 ASN   A N   1 
ATOM   2079 C  CA  . ASN   A 1 274 ? -18.542 -4.989  22.569  1.00 24.50 ?  274 ASN   A CA  1 
ATOM   2080 C  C   . ASN   A 1 274 ? -17.730 -5.563  21.413  1.00 31.44 ?  274 ASN   A C   1 
ATOM   2081 O  O   . ASN   A 1 274 ? -18.122 -6.599  20.861  1.00 29.90 ?  274 ASN   A O   1 
ATOM   2082 C  CB  . ASN   A 1 274 ? -19.745 -4.269  21.957  1.00 26.30 ?  274 ASN   A CB  1 
ATOM   2083 C  CG  . ASN   A 1 274 ? -20.754 -3.847  22.987  1.00 27.41 ?  274 ASN   A CG  1 
ATOM   2084 O  OD1 . ASN   A 1 274 ? -20.731 -4.314  24.126  1.00 25.87 ?  274 ASN   A OD1 1 
ATOM   2085 N  ND2 . ASN   A 1 274 ? -21.657 -2.959  22.592  1.00 29.21 ?  274 ASN   A ND2 1 
ATOM   2086 N  N   . GLY   A 1 275 ? -16.644 -4.918  21.009  1.00 32.81 ?  275 GLY   A N   1 
ATOM   2087 C  CA  . GLY   A 1 275 ? -16.078 -5.322  19.731  1.00 31.38 ?  275 GLY   A CA  1 
ATOM   2088 C  C   . GLY   A 1 275 ? -16.959 -4.840  18.587  1.00 31.97 ?  275 GLY   A C   1 
ATOM   2089 O  O   . GLY   A 1 275 ? -17.850 -3.994  18.747  1.00 33.88 ?  275 GLY   A O   1 
ATOM   2090 N  N   . MET   A 1 276 ? -16.714 -5.408  17.410  1.00 31.59 ?  276 MET   A N   1 
ATOM   2091 C  CA  . MET   A 1 276 ? -17.396 -4.960  16.209  1.00 34.10 ?  276 MET   A CA  1 
ATOM   2092 C  C   . MET   A 1 276 ? -18.563 -5.851  15.811  1.00 32.33 ?  276 MET   A C   1 
ATOM   2093 O  O   . MET   A 1 276 ? -19.320 -5.477  14.910  1.00 36.29 ?  276 MET   A O   1 
ATOM   2094 C  CB  . MET   A 1 276 ? -16.396 -4.861  15.046  1.00 29.51 ?  276 MET   A CB  1 
ATOM   2095 C  CG  . MET   A 1 276 ? -15.281 -3.861  15.304  1.00 27.46 ?  276 MET   A CG  1 
ATOM   2096 S  SD  . MET   A 1 276 ? -14.349 -3.481  13.817  1.00 44.52 ?  276 MET   A SD  1 
ATOM   2097 C  CE  . MET   A 1 276 ? -13.015 -2.489  14.505  1.00 35.45 ?  276 MET   A CE  1 
ATOM   2098 N  N   . ASN   A 1 277 ? -18.718 -7.015  16.442  1.00 34.35 ?  277 ASN   A N   1 
ATOM   2099 C  CA  . ASN   A 1 277 ? -19.826 -7.929  16.161  1.00 38.73 ?  277 ASN   A CA  1 
ATOM   2100 C  C   . ASN   A 1 277 ? -19.916 -8.255  14.668  1.00 40.73 ?  277 ASN   A C   1 
ATOM   2101 O  O   . ASN   A 1 277 ? -20.964 -8.109  14.036  1.00 39.20 ?  277 ASN   A O   1 
ATOM   2102 C  CB  . ASN   A 1 277 ? -21.150 -7.358  16.676  1.00 42.98 ?  277 ASN   A CB  1 
ATOM   2103 N  N   . GLY   A 1 278 ? -18.794 -8.697  14.099  1.00 35.01 ?  278 GLY   A N   1 
ATOM   2104 C  CA  . GLY   A 1 278 ? -18.749 -9.120  12.709  1.00 39.84 ?  278 GLY   A CA  1 
ATOM   2105 C  C   . GLY   A 1 278 ? -18.711 -8.009  11.680  1.00 37.40 ?  278 GLY   A C   1 
ATOM   2106 O  O   . GLY   A 1 278 ? -18.719 -8.299  10.474  1.00 41.02 ?  278 GLY   A O   1 
ATOM   2107 N  N   . ARG   A 1 279 ? -18.677 -6.754  12.104  1.00 33.28 ?  279 ARG   A N   1 
ATOM   2108 C  CA  . ARG   A 1 279 ? -18.554 -5.625  11.199  1.00 36.32 ?  279 ARG   A CA  1 
ATOM   2109 C  C   . ARG   A 1 279 ? -17.093 -5.199  11.078  1.00 34.37 ?  279 ARG   A C   1 
ATOM   2110 O  O   . ARG   A 1 279 ? -16.215 -5.688  11.787  1.00 28.57 ?  279 ARG   A O   1 
ATOM   2111 C  CB  . ARG   A 1 279 ? -19.425 -4.470  11.692  1.00 28.46 ?  279 ARG   A CB  1 
ATOM   2112 C  CG  . ARG   A 1 279 ? -20.907 -4.816  11.667  1.00 34.59 ?  279 ARG   A CG  1 
ATOM   2113 C  CD  . ARG   A 1 279 ? -21.763 -3.751  12.306  1.00 33.16 ?  279 ARG   A CD  1 
ATOM   2114 N  NE  . ARG   A 1 279 ? -21.670 -3.774  13.761  1.00 41.71 ?  279 ARG   A NE  1 
ATOM   2115 C  CZ  . ARG   A 1 279 ? -22.664 -3.434  14.580  1.00 43.01 ?  279 ARG   A CZ  1 
ATOM   2116 N  NH1 . ARG   A 1 279 ? -23.832 -3.051  14.080  1.00 45.80 ?  279 ARG   A NH1 1 
ATOM   2117 N  NH2 . ARG   A 1 279 ? -22.490 -3.480  15.898  1.00 38.35 ?  279 ARG   A NH2 1 
ATOM   2118 N  N   . THR   A 1 280 ? -16.831 -4.293  10.139  1.00 34.98 ?  280 THR   A N   1 
ATOM   2119 C  CA  . THR   A 1 280 ? -15.531 -3.649  10.054  1.00 30.42 ?  280 THR   A CA  1 
ATOM   2120 C  C   . THR   A 1 280 ? -15.722 -2.142  10.035  1.00 29.19 ?  280 THR   A C   1 
ATOM   2121 O  O   . THR   A 1 280 ? -16.826 -1.632  9.834   1.00 34.55 ?  280 THR   A O   1 
ATOM   2122 C  CB  . THR   A 1 280 ? -14.720 -4.085  8.819   1.00 35.61 ?  280 THR   A CB  1 
ATOM   2123 O  OG1 . THR   A 1 280 ? -15.400 -3.694  7.619   1.00 40.08 ?  280 THR   A OG1 1 
ATOM   2124 C  CG2 . THR   A 1 280 ? -14.505 -5.588  8.825   1.00 34.01 ?  280 THR   A CG2 1 
ATOM   2125 N  N   . ILE   A 1 281 ? -14.627 -1.439  10.289  1.00 31.45 ?  281 ILE   A N   1 
ATOM   2126 C  CA  . ILE   A 1 281 ? -14.577 0.015   10.248  1.00 28.99 ?  281 ILE   A CA  1 
ATOM   2127 C  C   . ILE   A 1 281 ? -13.427 0.386   9.331   1.00 29.05 ?  281 ILE   A C   1 
ATOM   2128 O  O   . ILE   A 1 281 ? -12.272 0.065   9.632   1.00 29.42 ?  281 ILE   A O   1 
ATOM   2129 C  CB  . ILE   A 1 281 ? -14.372 0.625   11.645  1.00 28.63 ?  281 ILE   A CB  1 
ATOM   2130 C  CG1 . ILE   A 1 281 ? -15.565 0.311   12.554  1.00 27.55 ?  281 ILE   A CG1 1 
ATOM   2131 C  CG2 . ILE   A 1 281 ? -14.153 2.125   11.550  1.00 26.42 ?  281 ILE   A CG2 1 
ATOM   2132 C  CD1 . ILE   A 1 281 ? -15.505 1.004   13.885  1.00 24.97 ?  281 ILE   A CD1 1 
ATOM   2133 N  N   . LEU   A 1 282 ? -13.738 1.026   8.203   1.00 32.31 ?  282 LEU   A N   1 
ATOM   2134 C  CA  . LEU   A 1 282 ? -12.719 1.401   7.214   1.00 31.64 ?  282 LEU   A CA  1 
ATOM   2135 C  C   . LEU   A 1 282 ? -11.816 0.217   6.874   1.00 26.61 ?  282 LEU   A C   1 
ATOM   2136 O  O   . LEU   A 1 282 ? -10.592 0.332   6.823   1.00 27.51 ?  282 LEU   A O   1 
ATOM   2137 C  CB  . LEU   A 1 282 ? -11.898 2.596   7.704   1.00 29.36 ?  282 LEU   A CB  1 
ATOM   2138 C  CG  . LEU   A 1 282 ? -12.731 3.866   7.897   1.00 26.67 ?  282 LEU   A CG  1 
ATOM   2139 C  CD1 . LEU   A 1 282 ? -11.950 4.951   8.628   1.00 26.32 ?  282 LEU   A CD1 1 
ATOM   2140 C  CD2 . LEU   A 1 282 ? -13.249 4.368   6.552   1.00 32.21 ?  282 LEU   A CD2 1 
ATOM   2141 N  N   . GLY   A 1 283 ? -12.429 -0.950  6.685   1.00 32.74 ?  283 GLY   A N   1 
ATOM   2142 C  CA  . GLY   A 1 283 ? -11.711 -2.129  6.251   1.00 32.69 ?  283 GLY   A CA  1 
ATOM   2143 C  C   . GLY   A 1 283 ? -10.971 -2.893  7.327   1.00 36.24 ?  283 GLY   A C   1 
ATOM   2144 O  O   . GLY   A 1 283 ? -10.359 -3.925  7.020   1.00 40.23 ?  283 GLY   A O   1 
ATOM   2145 N  N   . SER   A 1 284 ? -11.005 -2.438  8.572   1.00 31.95 ?  284 SER   A N   1 
ATOM   2146 C  CA  . SER   A 1 284 ? -10.258 -3.070  9.648   1.00 31.99 ?  284 SER   A CA  1 
ATOM   2147 C  C   . SER   A 1 284 ? -11.221 -3.701  10.645  1.00 33.13 ?  284 SER   A C   1 
ATOM   2148 O  O   . SER   A 1 284 ? -12.294 -3.153  10.919  1.00 26.44 ?  284 SER   A O   1 
ATOM   2149 C  CB  . SER   A 1 284 ? -9.359  -2.057  10.352  1.00 28.72 ?  284 SER   A CB  1 
ATOM   2150 O  OG  . SER   A 1 284 ? -8.666  -2.670  11.425  1.00 36.43 ?  284 SER   A OG  1 
ATOM   2151 N  N   . ALA   A 1 285 ? -10.850 -4.873  11.151  1.00 32.12 ?  285 ALA   A N   1 
ATOM   2152 C  CA  . ALA   A 1 285 ? -11.602 -5.531  12.210  1.00 35.11 ?  285 ALA   A CA  1 
ATOM   2153 C  C   . ALA   A 1 285 ? -11.047 -5.229  13.596  1.00 36.44 ?  285 ALA   A C   1 
ATOM   2154 O  O   . ALA   A 1 285 ? -11.584 -5.733  14.588  1.00 33.07 ?  285 ALA   A O   1 
ATOM   2155 C  CB  . ALA   A 1 285 ? -11.626 -7.044  11.982  1.00 31.16 ?  285 ALA   A CB  1 
ATOM   2156 N  N   . LEU   A 1 286 ? -9.988  -4.429  13.688  1.00 33.07 ?  286 LEU   A N   1 
ATOM   2157 C  CA  . LEU   A 1 286 ? -9.451  -3.957  14.957  1.00 31.89 ?  286 LEU   A CA  1 
ATOM   2158 C  C   . LEU   A 1 286 ? -9.505  -2.435  14.980  1.00 32.65 ?  286 LEU   A C   1 
ATOM   2159 O  O   . LEU   A 1 286 ? -9.696  -1.784  13.951  1.00 33.06 ?  286 LEU   A O   1 
ATOM   2160 C  CB  . LEU   A 1 286 ? -8.012  -4.450  15.171  1.00 33.95 ?  286 LEU   A CB  1 
ATOM   2161 C  CG  . LEU   A 1 286 ? -7.849  -5.967  15.264  1.00 34.47 ?  286 LEU   A CG  1 
ATOM   2162 C  CD1 . LEU   A 1 286 ? -6.401  -6.376  15.042  1.00 34.37 ?  286 LEU   A CD1 1 
ATOM   2163 C  CD2 . LEU   A 1 286 ? -8.363  -6.477  16.612  1.00 32.65 ?  286 LEU   A CD2 1 
ATOM   2164 N  N   . LEU   A 1 287 ? -9.327  -1.862  16.167  1.00 25.12 ?  287 LEU   A N   1 
ATOM   2165 C  CA  . LEU   A 1 287 ? -9.310  -0.409  16.320  1.00 27.29 ?  287 LEU   A CA  1 
ATOM   2166 C  C   . LEU   A 1 287 ? -7.920  0.115   15.957  1.00 28.33 ?  287 LEU   A C   1 
ATOM   2167 O  O   . LEU   A 1 287 ? -6.960  -0.105  16.695  1.00 28.40 ?  287 LEU   A O   1 
ATOM   2168 C  CB  . LEU   A 1 287 ? -9.696  -0.025  17.744  1.00 28.66 ?  287 LEU   A CB  1 
ATOM   2169 C  CG  . LEU   A 1 287 ? -11.120 -0.443  18.142  1.00 27.30 ?  287 LEU   A CG  1 
ATOM   2170 C  CD1 . LEU   A 1 287 ? -11.347 -0.263  19.636  1.00 26.85 ?  287 LEU   A CD1 1 
ATOM   2171 C  CD2 . LEU   A 1 287 ? -12.149 0.339   17.340  1.00 27.82 ?  287 LEU   A CD2 1 
ATOM   2172 N  N   . GLU   A 1 288 ? -7.825  0.833   14.835  1.00 32.88 ?  288 GLU   A N   1 
ATOM   2173 C  CA  . GLU   A 1 288 ? -6.552  1.312   14.295  1.00 29.92 ?  288 GLU   A CA  1 
ATOM   2174 C  C   . GLU   A 1 288 ? -6.025  2.523   15.059  1.00 28.11 ?  288 GLU   A C   1 
ATOM   2175 O  O   . GLU   A 1 288 ? -6.759  3.488   15.277  1.00 25.97 ?  288 GLU   A O   1 
ATOM   2176 C  CB  . GLU   A 1 288 ? -6.744  1.695   12.826  1.00 31.85 ?  288 GLU   A CB  1 
ATOM   2177 C  CG  . GLU   A 1 288 ? -6.442  0.590   11.848  1.00 42.07 ?  288 GLU   A CG  1 
ATOM   2178 C  CD  . GLU   A 1 288 ? -4.957  0.295   11.792  1.00 40.07 ?  288 GLU   A CD  1 
ATOM   2179 O  OE1 . GLU   A 1 288 ? -4.150  1.211   12.085  1.00 48.42 ?  288 GLU   A OE1 1 
ATOM   2180 O  OE2 . GLU   A 1 288 ? -4.602  -0.854  11.468  1.00 49.84 ?  288 GLU   A OE2 1 
ATOM   2181 N  N   . ASP   A 1 289 ? -4.730  2.516   15.414  1.00 28.16 ?  289 ASP   A N   1 
ATOM   2182 C  CA  . ASP   A 1 289 ? -4.155  3.639   16.152  1.00 24.45 ?  289 ASP   A CA  1 
ATOM   2183 C  C   . ASP   A 1 289 ? -2.907  4.231   15.493  1.00 29.71 ?  289 ASP   A C   1 
ATOM   2184 O  O   . ASP   A 1 289 ? -2.125  4.911   16.167  1.00 27.18 ?  289 ASP   A O   1 
ATOM   2185 C  CB  . ASP   A 1 289 ? -3.852  3.242   17.604  1.00 28.36 ?  289 ASP   A CB  1 
ATOM   2186 C  CG  . ASP   A 1 289 ? -2.606  2.372   17.754  1.00 31.29 ?  289 ASP   A CG  1 
ATOM   2187 O  OD1 . ASP   A 1 289 ? -2.094  1.831   16.749  1.00 29.67 ?  289 ASP   A OD1 1 
ATOM   2188 O  OD2 . ASP   A 1 289 ? -2.137  2.229   18.908  1.00 25.40 ?  289 ASP   A OD2 1 
ATOM   2189 N  N   . GLU   A 1 290 ? -2.706  4.031   14.189  1.00 29.15 ?  290 GLU   A N   1 
ATOM   2190 C  CA  . GLU   A 1 290 ? -1.535  4.601   13.529  1.00 31.73 ?  290 GLU   A CA  1 
ATOM   2191 C  C   . GLU   A 1 290 ? -1.914  5.712   12.552  1.00 32.11 ?  290 GLU   A C   1 
ATOM   2192 O  O   . GLU   A 1 290 ? -1.195  5.960   11.583  1.00 32.60 ?  290 GLU   A O   1 
ATOM   2193 C  CB  . GLU   A 1 290 ? -0.703  3.502   12.861  1.00 27.11 ?  290 GLU   A CB  1 
ATOM   2194 C  CG  . GLU   A 1 290 ? -0.154  2.482   13.918  1.00 35.01 ?  290 GLU   A CG  1 
ATOM   2195 C  CD  . GLU   A 1 290 ? 1.323   2.074   13.735  1.00 38.47 ?  290 GLU   A CD  1 
ATOM   2196 O  OE1 . GLU   A 1 290 ? 1.810   2.119   12.596  1.00 31.11 ?  290 GLU   A OE1 1 
ATOM   2197 O  OE2 . GLU   A 1 290 ? 2.005   1.700   14.739  1.00 31.57 ?  290 GLU   A OE2 1 
ATOM   2198 N  N   . PHE   A 1 291 ? -3.035  6.400   12.812  1.00 26.76 ?  291 PHE   A N   1 
ATOM   2199 C  CA  . PHE   A 1 291 ? -3.410  7.637   12.126  1.00 26.25 ?  291 PHE   A CA  1 
ATOM   2200 C  C   . PHE   A 1 291 ? -3.606  8.739   13.162  1.00 28.23 ?  291 PHE   A C   1 
ATOM   2201 O  O   . PHE   A 1 291 ? -4.466  8.613   14.038  1.00 26.80 ?  291 PHE   A O   1 
ATOM   2202 C  CB  . PHE   A 1 291 ? -4.712  7.488   11.331  1.00 24.13 ?  291 PHE   A CB  1 
ATOM   2203 C  CG  . PHE   A 1 291 ? -4.676  6.446   10.259  1.00 24.40 ?  291 PHE   A CG  1 
ATOM   2204 C  CD1 . PHE   A 1 291 ? -4.150  6.736   9.011   1.00 29.61 ?  291 PHE   A CD1 1 
ATOM   2205 C  CD2 . PHE   A 1 291 ? -5.201  5.185   10.485  1.00 29.29 ?  291 PHE   A CD2 1 
ATOM   2206 C  CE1 . PHE   A 1 291 ? -4.130  5.774   8.012   1.00 30.07 ?  291 PHE   A CE1 1 
ATOM   2207 C  CE2 . PHE   A 1 291 ? -5.186  4.220   9.496   1.00 29.54 ?  291 PHE   A CE2 1 
ATOM   2208 C  CZ  . PHE   A 1 291 ? -4.646  4.516   8.254   1.00 29.76 ?  291 PHE   A CZ  1 
ATOM   2209 N  N   . THR   A 1 292 ? -2.860  9.833   13.031  1.00 30.49 ?  292 THR   A N   1 
ATOM   2210 C  CA  . THR   A 1 292 ? -3.045  11.000  13.891  1.00 30.94 ?  292 THR   A CA  1 
ATOM   2211 C  C   . THR   A 1 292 ? -4.235  11.833  13.429  1.00 31.05 ?  292 THR   A C   1 
ATOM   2212 O  O   . THR   A 1 292 ? -4.745  11.657  12.320  1.00 29.37 ?  292 THR   A O   1 
ATOM   2213 C  CB  . THR   A 1 292 ? -1.788  11.863  13.879  1.00 29.74 ?  292 THR   A CB  1 
ATOM   2214 O  OG1 . THR   A 1 292 ? -1.632  12.438  12.572  1.00 29.12 ?  292 THR   A OG1 1 
ATOM   2215 C  CG2 . THR   A 1 292 ? -0.575  11.034  14.239  1.00 27.44 ?  292 THR   A CG2 1 
ATOM   2216 N  N   . PRO   A 1 293 ? -4.698  12.772  14.265  1.00 29.96 ?  293 PRO   A N   1 
ATOM   2217 C  CA  . PRO   A 1 293 ? -5.722  13.715  13.788  1.00 32.68 ?  293 PRO   A CA  1 
ATOM   2218 C  C   . PRO   A 1 293 ? -5.296  14.487  12.553  1.00 32.10 ?  293 PRO   A C   1 
ATOM   2219 O  O   . PRO   A 1 293 ? -6.121  14.760  11.675  1.00 28.60 ?  293 PRO   A O   1 
ATOM   2220 C  CB  . PRO   A 1 293 ? -5.930  14.638  14.995  1.00 31.63 ?  293 PRO   A CB  1 
ATOM   2221 C  CG  . PRO   A 1 293 ? -5.610  13.782  16.157  1.00 31.96 ?  293 PRO   A CG  1 
ATOM   2222 C  CD  . PRO   A 1 293 ? -4.455  12.924  15.710  1.00 31.48 ?  293 PRO   A CD  1 
ATOM   2223 N  N   . PHE   A 1 294 ? -4.023  14.849  12.454  1.00 35.62 ?  294 PHE   A N   1 
ATOM   2224 C  CA  . PHE   A 1 294 ? -3.578  15.581  11.274  1.00 32.92 ?  294 PHE   A CA  1 
ATOM   2225 C  C   . PHE   A 1 294 ? -3.561  14.684  10.043  1.00 31.76 ?  294 PHE   A C   1 
ATOM   2226 O  O   . PHE   A 1 294 ? -3.913  15.129  8.942   1.00 31.81 ?  294 PHE   A O   1 
ATOM   2227 C  CB  . PHE   A 1 294 ? -2.216  16.202  11.555  1.00 37.16 ?  294 PHE   A CB  1 
ATOM   2228 C  CG  . PHE   A 1 294 ? -2.189  16.984  12.835  1.00 46.36 ?  294 PHE   A CG  1 
ATOM   2229 C  CD1 . PHE   A 1 294 ? -2.607  18.308  12.858  1.00 48.39 ?  294 PHE   A CD1 1 
ATOM   2230 C  CD2 . PHE   A 1 294 ? -1.798  16.383  14.029  1.00 47.04 ?  294 PHE   A CD2 1 
ATOM   2231 C  CE1 . PHE   A 1 294 ? -2.606  19.032  14.041  1.00 51.15 ?  294 PHE   A CE1 1 
ATOM   2232 C  CE2 . PHE   A 1 294 ? -1.800  17.100  15.216  1.00 43.28 ?  294 PHE   A CE2 1 
ATOM   2233 C  CZ  . PHE   A 1 294 ? -2.204  18.428  15.221  1.00 47.12 ?  294 PHE   A CZ  1 
ATOM   2234 N  N   . ASP   A 1 295 ? -3.186  13.411  10.214  1.00 28.52 ?  295 ASP   A N   1 
ATOM   2235 C  CA  . ASP   A 1 295 ? -3.281  12.449  9.117   1.00 32.04 ?  295 ASP   A CA  1 
ATOM   2236 C  C   . ASP   A 1 295 ? -4.704  12.341  8.595   1.00 32.23 ?  295 ASP   A C   1 
ATOM   2237 O  O   . ASP   A 1 295 ? -4.925  12.284  7.379   1.00 29.09 ?  295 ASP   A O   1 
ATOM   2238 C  CB  . ASP   A 1 295 ? -2.810  11.067  9.566   1.00 31.55 ?  295 ASP   A CB  1 
ATOM   2239 C  CG  . ASP   A 1 295 ? -1.349  11.033  9.958   1.00 32.22 ?  295 ASP   A CG  1 
ATOM   2240 O  OD1 . ASP   A 1 295 ? -0.555  11.878  9.475   1.00 32.98 ?  295 ASP   A OD1 1 
ATOM   2241 O  OD2 . ASP   A 1 295 ? -1.001  10.133  10.754  1.00 35.50 ?  295 ASP   A OD2 1 
ATOM   2242 N  N   . VAL   A 1 296 ? -5.682  12.277  9.504   1.00 29.92 ?  296 VAL   A N   1 
ATOM   2243 C  CA  . VAL   A 1 296 ? -7.075  12.119  9.096   1.00 29.72 ?  296 VAL   A CA  1 
ATOM   2244 C  C   . VAL   A 1 296 ? -7.533  13.338  8.309   1.00 34.08 ?  296 VAL   A C   1 
ATOM   2245 O  O   . VAL   A 1 296 ? -8.065  13.218  7.199   1.00 33.55 ?  296 VAL   A O   1 
ATOM   2246 C  CB  . VAL   A 1 296 ? -7.969  11.868  10.325  1.00 26.43 ?  296 VAL   A CB  1 
ATOM   2247 C  CG1 . VAL   A 1 296 ? -9.446  11.965  9.937   1.00 28.31 ?  296 VAL   A CG1 1 
ATOM   2248 C  CG2 . VAL   A 1 296 ? -7.674  10.509  10.917  1.00 24.40 ?  296 VAL   A CG2 1 
ATOM   2249 N  N   . VAL   A 1 297 ? -7.308  14.533  8.862   1.00 33.01 ?  297 VAL   A N   1 
ATOM   2250 C  CA  . VAL   A 1 297 ? -7.696  15.750  8.159   1.00 32.25 ?  297 VAL   A CA  1 
ATOM   2251 C  C   . VAL   A 1 297 ? -7.004  15.835  6.805   1.00 37.29 ?  297 VAL   A C   1 
ATOM   2252 O  O   . VAL   A 1 297 ? -7.609  16.273  5.821   1.00 42.89 ?  297 VAL   A O   1 
ATOM   2253 C  CB  . VAL   A 1 297 ? -7.396  16.989  9.023   1.00 37.19 ?  297 VAL   A CB  1 
ATOM   2254 C  CG1 . VAL   A 1 297 ? -7.822  18.254  8.292   1.00 41.16 ?  297 VAL   A CG1 1 
ATOM   2255 C  CG2 . VAL   A 1 297 ? -8.101  16.883  10.372  1.00 34.41 ?  297 VAL   A CG2 1 
ATOM   2256 N  N   . ARG   A 1 298 ? -5.747  15.389  6.717   1.00 38.06 ?  298 ARG   A N   1 
ATOM   2257 C  CA  . ARG   A 1 298 ? -5.014  15.488  5.454   1.00 35.88 ?  298 ARG   A CA  1 
ATOM   2258 C  C   . ARG   A 1 298 ? -5.593  14.549  4.404   1.00 41.50 ?  298 ARG   A C   1 
ATOM   2259 O  O   . ARG   A 1 298 ? -5.880  14.964  3.276   1.00 40.83 ?  298 ARG   A O   1 
ATOM   2260 C  CB  . ARG   A 1 298 ? -3.528  15.197  5.675   1.00 38.92 ?  298 ARG   A CB  1 
ATOM   2261 N  N   . GLN   A 1 299 ? -5.762  13.272  4.749   1.00 39.16 ?  299 GLN   A N   1 
ATOM   2262 C  CA  . GLN   A 1 299 ? -6.276  12.327  3.766   1.00 34.80 ?  299 GLN   A CA  1 
ATOM   2263 C  C   . GLN   A 1 299 ? -7.730  12.611  3.423   1.00 37.59 ?  299 GLN   A C   1 
ATOM   2264 O  O   . GLN   A 1 299 ? -8.153  12.358  2.290   1.00 41.19 ?  299 GLN   A O   1 
ATOM   2265 C  CB  . GLN   A 1 299 ? -6.123  10.893  4.272   1.00 33.97 ?  299 GLN   A CB  1 
ATOM   2266 C  CG  . GLN   A 1 299 ? -6.566  9.851   3.250   1.00 29.49 ?  299 GLN   A CG  1 
ATOM   2267 C  CD  . GLN   A 1 299 ? -6.263  8.431   3.675   1.00 28.85 ?  299 GLN   A CD  1 
ATOM   2268 O  OE1 . GLN   A 1 299 ? -6.754  7.479   3.070   1.00 28.12 ?  299 GLN   A OE1 1 
ATOM   2269 N  NE2 . GLN   A 1 299 ? -5.450  8.277   4.721   1.00 28.79 ?  299 GLN   A NE2 1 
ATOM   2270 N  N   . CYS   A 1 300 ? -8.512  13.125  4.376   1.00 39.16 ?  300 CYS   A N   1 
ATOM   2271 C  CA  . CYS   A 1 300 ? -9.910  13.455  4.108   1.00 40.54 ?  300 CYS   A CA  1 
ATOM   2272 C  C   . CYS   A 1 300 ? -10.092 14.844  3.498   1.00 42.97 ?  300 CYS   A C   1 
ATOM   2273 O  O   . CYS   A 1 300 ? -11.226 15.200  3.174   1.00 43.03 ?  300 CYS   A O   1 
ATOM   2274 C  CB  . CYS   A 1 300 ? -10.751 13.334  5.388   1.00 42.67 ?  300 CYS   A CB  1 
ATOM   2275 S  SG  . CYS   A 1 300 ? -10.932 11.638  6.027   1.00 40.11 ?  300 CYS   A SG  1 
ATOM   2276 N  N   . SER   A 1 301 ? -9.015  15.625  3.307   1.00 49.56 ?  301 SER   A N   1 
ATOM   2277 C  CA  . SER   A 1 301 ? -9.117  16.937  2.675   1.00 45.21 ?  301 SER   A CA  1 
ATOM   2278 C  C   . SER   A 1 301 ? -8.223  17.122  1.453   1.00 43.99 ?  301 SER   A C   1 
ATOM   2279 O  O   . SER   A 1 301 ? -8.273  18.195  0.837   1.00 36.64 ?  301 SER   A O   1 
ATOM   2280 C  CB  . SER   A 1 301 ? -8.797  18.063  3.676   1.00 46.86 ?  301 SER   A CB  1 
ATOM   2281 N  N   . GLY   A 1 302 ? -7.397  16.143  1.098   1.00 43.92 ?  302 GLY   A N   1 
ATOM   2282 C  CA  . GLY   A 1 302 ? -6.678  16.241  -0.160  1.00 43.52 ?  302 GLY   A CA  1 
ATOM   2283 C  C   . GLY   A 1 302 ? -5.480  17.167  -0.112  1.00 45.16 ?  302 GLY   A C   1 
ATOM   2284 O  O   . GLY   A 1 302 ? -5.169  17.824  -1.109  1.00 52.60 ?  302 GLY   A O   1 
ATOM   2285 N  N   . VAL   A 1 303 ? -4.803  17.234  1.036   1.00 49.66 ?  303 VAL   A N   1 
ATOM   2286 C  CA  . VAL   A 1 303 ? -3.628  18.094  1.166   1.00 45.11 ?  303 VAL   A CA  1 
ATOM   2287 C  C   . VAL   A 1 303 ? -2.508  17.598  0.261   1.00 42.88 ?  303 VAL   A C   1 
ATOM   2288 O  O   . VAL   A 1 303 ? -2.194  16.405  0.235   1.00 41.70 ?  303 VAL   A O   1 
ATOM   2289 C  CB  . VAL   A 1 303 ? -3.172  18.156  2.636   1.00 40.42 ?  303 VAL   A CB  1 
ATOM   2290 N  N   . THR   A 1 304 ? -1.883  18.516  -0.477  1.00 40.41 ?  304 THR   A N   1 
ATOM   2291 C  CA  . THR   A 1 304 ? -0.820  18.138  -1.419  1.00 41.16 ?  304 THR   A CA  1 
ATOM   2292 C  C   . THR   A 1 304 ? 0.496   18.846  -1.117  1.00 40.45 ?  304 THR   A C   1 
ATOM   2293 O  O   . THR   A 1 304 ? 0.547   19.683  -0.210  1.00 46.87 ?  304 THR   A O   1 
ATOM   2294 C  CB  . THR   A 1 304 ? -1.223  18.451  -2.869  1.00 36.20 ?  304 THR   A CB  1 
ATOM   2295 O  OG1 . THR   A 1 304 ? -1.554  19.844  -2.985  1.00 38.91 ?  304 THR   A OG1 1 
ATOM   2296 C  CG2 . THR   A 1 304 ? -2.410  17.591  -3.288  1.00 34.24 ?  304 THR   A CG2 1 
ATOM   2297 N  N   . SER   B 1 1   ? 12.824  -8.477  10.033  1.00 28.63 ?  1   SER   B N   1 
ATOM   2298 C  CA  . SER   B 1 1   ? 11.502  -8.889  10.486  1.00 27.17 ?  1   SER   B CA  1 
ATOM   2299 C  C   . SER   B 1 1   ? 10.526  -7.744  10.349  1.00 29.86 ?  1   SER   B C   1 
ATOM   2300 O  O   . SER   B 1 1   ? 10.927  -6.591  10.202  1.00 29.73 ?  1   SER   B O   1 
ATOM   2301 C  CB  . SER   B 1 1   ? 11.530  -9.363  11.947  1.00 33.75 ?  1   SER   B CB  1 
ATOM   2302 O  OG  . SER   B 1 1   ? 12.281  -10.557 12.087  1.00 42.62 ?  1   SER   B OG  1 
ATOM   2303 N  N   . GLY   B 1 2   ? 9.249   -8.073  10.433  1.00 30.64 ?  2   GLY   B N   1 
ATOM   2304 C  CA  . GLY   B 1 2   ? 8.173   -7.132  10.220  1.00 32.54 ?  2   GLY   B CA  1 
ATOM   2305 C  C   . GLY   B 1 2   ? 7.626   -7.244  8.809   1.00 32.58 ?  2   GLY   B C   1 
ATOM   2306 O  O   . GLY   B 1 2   ? 8.326   -7.636  7.868   1.00 31.48 ?  2   GLY   B O   1 
ATOM   2307 N  N   . PHE   B 1 3   ? 6.349   -6.914  8.660   1.00 28.29 ?  3   PHE   B N   1 
ATOM   2308 C  CA  . PHE   B 1 3   ? 5.670   -7.012  7.372   1.00 31.28 ?  3   PHE   B CA  1 
ATOM   2309 C  C   . PHE   B 1 3   ? 4.681   -5.861  7.289   1.00 33.31 ?  3   PHE   B C   1 
ATOM   2310 O  O   . PHE   B 1 3   ? 3.711   -5.813  8.054   1.00 30.08 ?  3   PHE   B O   1 
ATOM   2311 C  CB  . PHE   B 1 3   ? 4.970   -8.358  7.211   1.00 32.47 ?  3   PHE   B CB  1 
ATOM   2312 C  CG  . PHE   B 1 3   ? 4.729   -8.740  5.780   1.00 35.20 ?  3   PHE   B CG  1 
ATOM   2313 C  CD1 . PHE   B 1 3   ? 5.786   -9.103  4.963   1.00 34.63 ?  3   PHE   B CD1 1 
ATOM   2314 C  CD2 . PHE   B 1 3   ? 3.448   -8.722  5.251   1.00 33.84 ?  3   PHE   B CD2 1 
ATOM   2315 C  CE1 . PHE   B 1 3   ? 5.572   -9.446  3.632   1.00 36.61 ?  3   PHE   B CE1 1 
ATOM   2316 C  CE2 . PHE   B 1 3   ? 3.226   -9.064  3.930   1.00 33.76 ?  3   PHE   B CE2 1 
ATOM   2317 C  CZ  . PHE   B 1 3   ? 4.289   -9.425  3.118   1.00 31.99 ?  3   PHE   B CZ  1 
ATOM   2318 N  N   . ARG   B 1 4   ? 4.949   -4.917  6.395   1.00 28.08 ?  4   ARG   B N   1 
ATOM   2319 C  CA  . ARG   B 1 4   ? 4.102   -3.752  6.207   1.00 29.44 ?  4   ARG   B CA  1 
ATOM   2320 C  C   . ARG   B 1 4   ? 3.515   -3.773  4.803   1.00 29.16 ?  4   ARG   B C   1 
ATOM   2321 O  O   . ARG   B 1 4   ? 4.047   -4.424  3.903   1.00 30.17 ?  4   ARG   B O   1 
ATOM   2322 C  CB  . ARG   B 1 4   ? 4.893   -2.458  6.409   1.00 31.13 ?  4   ARG   B CB  1 
ATOM   2323 C  CG  . ARG   B 1 4   ? 5.210   -2.142  7.850   1.00 33.17 ?  4   ARG   B CG  1 
ATOM   2324 C  CD  . ARG   B 1 4   ? 3.945   -1.756  8.578   1.00 37.49 ?  4   ARG   B CD  1 
ATOM   2325 N  NE  . ARG   B 1 4   ? 4.221   -1.068  9.835   1.00 28.87 ?  4   ARG   B NE  1 
ATOM   2326 C  CZ  . ARG   B 1 4   ? 3.318   -0.354  10.497  1.00 33.15 ?  4   ARG   B CZ  1 
ATOM   2327 N  NH1 . ARG   B 1 4   ? 2.087   -0.233  10.019  1.00 32.05 ?  4   ARG   B NH1 1 
ATOM   2328 N  NH2 . ARG   B 1 4   ? 3.644   0.247   11.628  1.00 31.73 ?  4   ARG   B NH2 1 
ATOM   2329 N  N   . LYS   B 1 5   ? 2.419   -3.042  4.621   1.00 28.94 ?  5   LYS   B N   1 
ATOM   2330 C  CA  . LYS   B 1 5   ? 1.860   -2.826  3.288   1.00 37.41 ?  5   LYS   B CA  1 
ATOM   2331 C  C   . LYS   B 1 5   ? 2.692   -1.730  2.641   1.00 35.17 ?  5   LYS   B C   1 
ATOM   2332 O  O   . LYS   B 1 5   ? 2.494   -0.539  2.893   1.00 33.75 ?  5   LYS   B O   1 
ATOM   2333 C  CB  . LYS   B 1 5   ? 0.379   -2.465  3.351   1.00 34.91 ?  5   LYS   B CB  1 
ATOM   2334 C  CG  . LYS   B 1 5   ? -0.294  -2.446  1.963   1.00 35.87 ?  5   LYS   B CG  1 
ATOM   2335 C  CD  . LYS   B 1 5   ? -1.821  -2.491  2.059   1.00 38.37 ?  5   LYS   B CD  1 
ATOM   2336 C  CE  . LYS   B 1 5   ? -2.312  -3.855  2.530   1.00 35.12 ?  5   LYS   B CE  1 
ATOM   2337 N  NZ  . LYS   B 1 5   ? -3.762  -3.831  2.924   1.00 35.50 ?  5   LYS   B NZ  1 
ATOM   2338 N  N   . MET   B 1 6   ? 3.648   -2.145  1.824   1.00 30.51 ?  6   MET   B N   1 
ATOM   2339 C  CA  . MET   B 1 6   ? 4.694   -1.275  1.320   1.00 30.81 ?  6   MET   B CA  1 
ATOM   2340 C  C   . MET   B 1 6   ? 4.401   -0.875  -0.118  1.00 27.43 ?  6   MET   B C   1 
ATOM   2341 O  O   . MET   B 1 6   ? 4.074   -1.726  -0.950  1.00 29.77 ?  6   MET   B O   1 
ATOM   2342 C  CB  . MET   B 1 6   ? 6.033   -1.998  1.405   1.00 33.33 ?  6   MET   B CB  1 
ATOM   2343 C  CG  . MET   B 1 6   ? 7.239   -1.114  1.382   1.00 41.08 ?  6   MET   B CG  1 
ATOM   2344 S  SD  . MET   B 1 6   ? 8.672   -2.174  1.618   1.00 43.68 ?  6   MET   B SD  1 
ATOM   2345 C  CE  . MET   B 1 6   ? 8.391   -2.837  3.249   1.00 39.62 ?  6   MET   B CE  1 
ATOM   2346 N  N   . ALA   B 1 7   ? 4.518   0.414   -0.404  1.00 26.93 ?  7   ALA   B N   1 
ATOM   2347 C  CA  . ALA   B 1 7   ? 4.378   0.918   -1.759  1.00 26.74 ?  7   ALA   B CA  1 
ATOM   2348 C  C   . ALA   B 1 7   ? 5.759   1.101   -2.364  1.00 30.71 ?  7   ALA   B C   1 
ATOM   2349 O  O   . ALA   B 1 7   ? 6.761   1.214   -1.650  1.00 27.91 ?  7   ALA   B O   1 
ATOM   2350 C  CB  . ALA   B 1 7   ? 3.613   2.242   -1.777  1.00 27.22 ?  7   ALA   B CB  1 
ATOM   2351 N  N   . PHE   B 1 8   ? 5.809   1.106   -3.697  1.00 25.81 ?  8   PHE   B N   1 
ATOM   2352 C  CA  . PHE   B 1 8   ? 7.047   1.439   -4.379  1.00 25.99 ?  8   PHE   B CA  1 
ATOM   2353 C  C   . PHE   B 1 8   ? 7.407   2.895   -4.115  1.00 25.77 ?  8   PHE   B C   1 
ATOM   2354 O  O   . PHE   B 1 8   ? 6.522   3.739   -3.954  1.00 24.79 ?  8   PHE   B O   1 
ATOM   2355 C  CB  . PHE   B 1 8   ? 6.920   1.230   -5.894  1.00 26.74 ?  8   PHE   B CB  1 
ATOM   2356 C  CG  . PHE   B 1 8   ? 6.900   -0.205  -6.311  1.00 28.63 ?  8   PHE   B CG  1 
ATOM   2357 C  CD1 . PHE   B 1 8   ? 8.081   -0.896  -6.495  1.00 29.19 ?  8   PHE   B CD1 1 
ATOM   2358 C  CD2 . PHE   B 1 8   ? 5.703   -0.864  -6.525  1.00 27.29 ?  8   PHE   B CD2 1 
ATOM   2359 C  CE1 . PHE   B 1 8   ? 8.068   -2.224  -6.877  1.00 30.58 ?  8   PHE   B CE1 1 
ATOM   2360 C  CE2 . PHE   B 1 8   ? 5.685   -2.192  -6.905  1.00 27.67 ?  8   PHE   B CE2 1 
ATOM   2361 C  CZ  . PHE   B 1 8   ? 6.870   -2.870  -7.084  1.00 27.39 ?  8   PHE   B CZ  1 
ATOM   2362 N  N   . PRO   B 1 9   ? 8.697   3.223   -4.110  1.00 26.18 ?  9   PRO   B N   1 
ATOM   2363 C  CA  . PRO   B 1 9   ? 9.093   4.636   -4.061  1.00 27.82 ?  9   PRO   B CA  1 
ATOM   2364 C  C   . PRO   B 1 9   ? 8.530   5.384   -5.264  1.00 28.87 ?  9   PRO   B C   1 
ATOM   2365 O  O   . PRO   B 1 9   ? 8.595   4.911   -6.400  1.00 30.03 ?  9   PRO   B O   1 
ATOM   2366 C  CB  . PRO   B 1 9   ? 10.627  4.582   -4.089  1.00 30.46 ?  9   PRO   B CB  1 
ATOM   2367 C  CG  . PRO   B 1 9   ? 10.989  3.163   -3.724  1.00 34.26 ?  9   PRO   B CG  1 
ATOM   2368 C  CD  . PRO   B 1 9   ? 9.850   2.320   -4.239  1.00 24.70 ?  9   PRO   B CD  1 
ATOM   2369 N  N   . SER   B 1 10  ? 7.982   6.569   -5.004  1.00 32.35 ?  10  SER   B N   1 
ATOM   2370 C  CA  . SER   B 1 10  ? 7.148   7.266   -5.974  1.00 31.68 ?  10  SER   B CA  1 
ATOM   2371 C  C   . SER   B 1 10  ? 7.877   8.364   -6.741  1.00 31.20 ?  10  SER   B C   1 
ATOM   2372 O  O   . SER   B 1 10  ? 7.247   9.046   -7.559  1.00 30.75 ?  10  SER   B O   1 
ATOM   2373 C  CB  . SER   B 1 10  ? 5.921   7.856   -5.269  1.00 31.70 ?  10  SER   B CB  1 
ATOM   2374 O  OG  . SER   B 1 10  ? 6.298   8.737   -4.222  1.00 31.89 ?  10  SER   B OG  1 
ATOM   2375 N  N   . GLY   B 1 11  ? 9.185   8.534   -6.519  1.00 29.40 ?  11  GLY   B N   1 
ATOM   2376 C  CA  . GLY   B 1 11  ? 9.889   9.667   -7.104  1.00 25.37 ?  11  GLY   B CA  1 
ATOM   2377 C  C   . GLY   B 1 11  ? 9.834   9.687   -8.621  1.00 27.89 ?  11  GLY   B C   1 
ATOM   2378 O  O   . GLY   B 1 11  ? 9.606   10.734  -9.230  1.00 27.68 ?  11  GLY   B O   1 
ATOM   2379 N  N   . LYS   B 1 12  ? 10.051  8.530   -9.253  1.00 26.30 ?  12  LYS   B N   1 
ATOM   2380 C  CA  . LYS   B 1 12  ? 10.030  8.470   -10.716 1.00 26.97 ?  12  LYS   B CA  1 
ATOM   2381 C  C   . LYS   B 1 12  ? 8.687   8.912   -11.290 1.00 31.65 ?  12  LYS   B C   1 
ATOM   2382 O  O   . LYS   B 1 12  ? 8.630   9.409   -12.420 1.00 32.65 ?  12  LYS   B O   1 
ATOM   2383 C  CB  . LYS   B 1 12  ? 10.344  7.053   -11.195 1.00 30.04 ?  12  LYS   B CB  1 
ATOM   2384 C  CG  . LYS   B 1 12  ? 11.787  6.623   -11.032 1.00 29.95 ?  12  LYS   B CG  1 
ATOM   2385 C  CD  . LYS   B 1 12  ? 12.001  5.218   -11.589 1.00 32.50 ?  12  LYS   B CD  1 
ATOM   2386 C  CE  . LYS   B 1 12  ? 13.372  4.655   -11.217 1.00 39.56 ?  12  LYS   B CE  1 
ATOM   2387 N  NZ  . LYS   B 1 12  ? 14.489  5.475   -11.748 1.00 51.18 ?  12  LYS   B NZ  1 
ATOM   2388 N  N   . VAL   B 1 13  ? 7.602   8.729   -10.538 1.00 29.76 ?  13  VAL   B N   1 
ATOM   2389 C  CA  . VAL   B 1 13  ? 6.260   9.088   -10.998 1.00 27.80 ?  13  VAL   B CA  1 
ATOM   2390 C  C   . VAL   B 1 13  ? 5.907   10.529  -10.636 1.00 31.28 ?  13  VAL   B C   1 
ATOM   2391 O  O   . VAL   B 1 13  ? 5.231   11.214  -11.408 1.00 29.54 ?  13  VAL   B O   1 
ATOM   2392 C  CB  . VAL   B 1 13  ? 5.231   8.093   -10.426 1.00 24.02 ?  13  VAL   B CB  1 
ATOM   2393 C  CG1 . VAL   B 1 13  ? 3.801   8.429   -10.913 1.00 29.32 ?  13  VAL   B CG1 1 
ATOM   2394 C  CG2 . VAL   B 1 13  ? 5.611   6.676   -10.813 1.00 26.88 ?  13  VAL   B CG2 1 
ATOM   2395 N  N   . GLU   B 1 14  ? 6.350   11.017  -9.466  1.00 31.68 ?  14  GLU   B N   1 
ATOM   2396 C  CA  . GLU   B 1 14  ? 6.154   12.425  -9.119  1.00 28.01 ?  14  GLU   B CA  1 
ATOM   2397 C  C   . GLU   B 1 14  ? 6.667   13.352  -10.222 1.00 29.41 ?  14  GLU   B C   1 
ATOM   2398 O  O   . GLU   B 1 14  ? 6.072   14.402  -10.492 1.00 30.84 ?  14  GLU   B O   1 
ATOM   2399 C  CB  . GLU   B 1 14  ? 6.862   12.744  -7.801  1.00 29.26 ?  14  GLU   B CB  1 
ATOM   2400 C  CG  . GLU   B 1 14  ? 6.332   11.986  -6.613  1.00 30.49 ?  14  GLU   B CG  1 
ATOM   2401 C  CD  . GLU   B 1 14  ? 7.232   12.147  -5.392  1.00 35.89 ?  14  GLU   B CD  1 
ATOM   2402 O  OE1 . GLU   B 1 14  ? 7.619   11.126  -4.785  1.00 30.75 ?  14  GLU   B OE1 1 
ATOM   2403 O  OE2 . GLU   B 1 14  ? 7.570   13.302  -5.061  1.00 31.87 ?  14  GLU   B OE2 1 
ATOM   2404 N  N   . GLY   B 1 15  ? 7.776   12.984  -10.857 1.00 26.46 ?  15  GLY   B N   1 
ATOM   2405 C  CA  . GLY   B 1 15  ? 8.350   13.798  -11.911 1.00 31.45 ?  15  GLY   B CA  1 
ATOM   2406 C  C   . GLY   B 1 15  ? 7.497   13.901  -13.163 1.00 28.25 ?  15  GLY   B C   1 
ATOM   2407 O  O   . GLY   B 1 15  ? 7.796   14.741  -14.016 1.00 32.60 ?  15  GLY   B O   1 
ATOM   2408 N  N   . CYS   B 1 16  ? 6.447   13.083  -13.286 1.00 27.36 ?  16  CYS   B N   1 
ATOM   2409 C  CA  . CYS   B 1 16  ? 5.580   13.099  -14.459 1.00 30.05 ?  16  CYS   B CA  1 
ATOM   2410 C  C   . CYS   B 1 16  ? 4.221   13.737  -14.222 1.00 27.78 ?  16  CYS   B C   1 
ATOM   2411 O  O   . CYS   B 1 16  ? 3.465   13.916  -15.183 1.00 28.49 ?  16  CYS   B O   1 
ATOM   2412 C  CB  . CYS   B 1 16  ? 5.365   11.672  -14.974 1.00 25.07 ?  16  CYS   B CB  1 
ATOM   2413 S  SG  . CYS   B 1 16  ? 6.910   10.795  -15.218 1.00 32.63 ?  16  CYS   B SG  1 
ATOM   2414 N  N   . MET   B 1 17  ? 3.873   14.075  -12.987 1.00 28.20 ?  17  MET   B N   1 
ATOM   2415 C  CA  . MET   B 1 17  ? 2.525   14.554  -12.729 1.00 26.82 ?  17  MET   B CA  1 
ATOM   2416 C  C   . MET   B 1 17  ? 2.397   16.022  -13.109 1.00 24.16 ?  17  MET   B C   1 
ATOM   2417 O  O   . MET   B 1 17  ? 3.285   16.831  -12.837 1.00 29.72 ?  17  MET   B O   1 
ATOM   2418 C  CB  . MET   B 1 17  ? 2.154   14.345  -11.259 1.00 27.88 ?  17  MET   B CB  1 
ATOM   2419 C  CG  . MET   B 1 17  ? 2.144   12.881  -10.843 1.00 28.15 ?  17  MET   B CG  1 
ATOM   2420 S  SD  . MET   B 1 17  ? 1.201   11.797  -11.949 1.00 30.79 ?  17  MET   B SD  1 
ATOM   2421 C  CE  . MET   B 1 17  ? -0.437  12.521  -11.838 1.00 29.88 ?  17  MET   B CE  1 
ATOM   2422 N  N   . VAL   B 1 18  ? 1.286   16.358  -13.754 1.00 27.98 ?  18  VAL   B N   1 
ATOM   2423 C  CA  . VAL   B 1 18  ? 0.986   17.721  -14.168 1.00 27.60 ?  18  VAL   B CA  1 
ATOM   2424 C  C   . VAL   B 1 18  ? -0.499  17.965  -13.945 1.00 26.26 ?  18  VAL   B C   1 
ATOM   2425 O  O   . VAL   B 1 18  ? -1.276  17.039  -13.714 1.00 31.22 ?  18  VAL   B O   1 
ATOM   2426 C  CB  . VAL   B 1 18  ? 1.350   17.982  -15.650 1.00 30.15 ?  18  VAL   B CB  1 
ATOM   2427 C  CG1 . VAL   B 1 18  ? 2.838   17.805  -15.870 1.00 29.37 ?  18  VAL   B CG1 1 
ATOM   2428 C  CG2 . VAL   B 1 18  ? 0.560   17.051  -16.551 1.00 29.02 ?  18  VAL   B CG2 1 
ATOM   2429 N  N   . GLN   B 1 19  ? -0.889  19.230  -14.043 1.00 30.85 ?  19  GLN   B N   1 
ATOM   2430 C  CA  . GLN   B 1 19  ? -2.276  19.642  -13.911 1.00 30.14 ?  19  GLN   B CA  1 
ATOM   2431 C  C   . GLN   B 1 19  ? -2.856  19.954  -15.288 1.00 33.45 ?  19  GLN   B C   1 
ATOM   2432 O  O   . GLN   B 1 19  ? -2.264  20.718  -16.055 1.00 37.32 ?  19  GLN   B O   1 
ATOM   2433 C  CB  . GLN   B 1 19  ? -2.374  20.861  -12.994 1.00 33.48 ?  19  GLN   B CB  1 
ATOM   2434 C  CG  . GLN   B 1 19  ? -3.678  21.609  -13.099 1.00 40.91 ?  19  GLN   B CG  1 
ATOM   2435 C  CD  . GLN   B 1 19  ? -3.734  22.817  -12.186 1.00 43.27 ?  19  GLN   B CD  1 
ATOM   2436 O  OE1 . GLN   B 1 19  ? -4.260  22.745  -11.078 1.00 49.75 ?  19  GLN   B OE1 1 
ATOM   2437 N  NE2 . GLN   B 1 19  ? -3.201  23.938  -12.652 1.00 48.09 ?  19  GLN   B NE2 1 
ATOM   2438 N  N   . VAL   B 1 20  ? -4.008  19.365  -15.599 1.00 32.76 ?  20  VAL   B N   1 
ATOM   2439 C  CA  . VAL   B 1 20  ? -4.678  19.570  -16.880 1.00 38.82 ?  20  VAL   B CA  1 
ATOM   2440 C  C   . VAL   B 1 20  ? -6.010  20.256  -16.620 1.00 36.33 ?  20  VAL   B C   1 
ATOM   2441 O  O   . VAL   B 1 20  ? -6.870  19.704  -15.922 1.00 36.65 ?  20  VAL   B O   1 
ATOM   2442 C  CB  . VAL   B 1 20  ? -4.893  18.248  -17.634 1.00 32.85 ?  20  VAL   B CB  1 
ATOM   2443 C  CG1 . VAL   B 1 20  ? -5.663  18.497  -18.916 1.00 34.35 ?  20  VAL   B CG1 1 
ATOM   2444 C  CG2 . VAL   B 1 20  ? -3.560  17.578  -17.910 1.00 28.03 ?  20  VAL   B CG2 1 
ATOM   2445 N  N   . THR   B 1 21  ? -6.191  21.443  -17.190 1.00 37.72 ?  21  THR   B N   1 
ATOM   2446 C  CA  . THR   B 1 21  ? -7.456  22.155  -17.092 1.00 40.23 ?  21  THR   B CA  1 
ATOM   2447 C  C   . THR   B 1 21  ? -8.101  22.261  -18.466 1.00 39.38 ?  21  THR   B C   1 
ATOM   2448 O  O   . THR   B 1 21  ? -7.427  22.536  -19.465 1.00 34.45 ?  21  THR   B O   1 
ATOM   2449 C  CB  . THR   B 1 21  ? -7.274  23.557  -16.501 1.00 41.30 ?  21  THR   B CB  1 
ATOM   2450 O  OG1 . THR   B 1 21  ? -6.487  23.479  -15.308 1.00 42.64 ?  21  THR   B OG1 1 
ATOM   2451 C  CG2 . THR   B 1 21  ? -8.624  24.162  -16.152 1.00 40.51 ?  21  THR   B CG2 1 
ATOM   2452 N  N   . CYS   B 1 22  ? -9.408  22.020  -18.510 1.00 35.01 ?  22  CYS   B N   1 
ATOM   2453 C  CA  . CYS   B 1 22  ? -10.210 22.230  -19.706 1.00 36.91 ?  22  CYS   B CA  1 
ATOM   2454 C  C   . CYS   B 1 22  ? -11.556 22.774  -19.260 1.00 42.24 ?  22  CYS   B C   1 
ATOM   2455 O  O   . CYS   B 1 22  ? -12.338 22.054  -18.629 1.00 41.10 ?  22  CYS   B O   1 
ATOM   2456 C  CB  . CYS   B 1 22  ? -10.391 20.937  -20.504 1.00 34.71 ?  22  CYS   B CB  1 
ATOM   2457 S  SG  . CYS   B 1 22  ? -11.376 21.154  -22.002 1.00 40.45 ?  22  CYS   B SG  1 
ATOM   2458 N  N   . GLY   B 1 23  ? -11.823 24.034  -19.581 1.00 43.29 ?  23  GLY   B N   1 
ATOM   2459 C  CA  . GLY   B 1 23  ? -13.031 24.660  -19.074 1.00 42.57 ?  23  GLY   B CA  1 
ATOM   2460 C  C   . GLY   B 1 23  ? -12.957 24.833  -17.565 1.00 40.33 ?  23  GLY   B C   1 
ATOM   2461 O  O   . GLY   B 1 23  ? -11.995 25.386  -17.019 1.00 42.52 ?  23  GLY   B O   1 
ATOM   2462 N  N   . THR   B 1 24  ? -13.987 24.356  -16.873 1.00 36.61 ?  24  THR   B N   1 
ATOM   2463 C  CA  . THR   B 1 24  ? -14.047 24.429  -15.420 1.00 41.85 ?  24  THR   B CA  1 
ATOM   2464 C  C   . THR   B 1 24  ? -13.469 23.194  -14.745 1.00 44.91 ?  24  THR   B C   1 
ATOM   2465 O  O   . THR   B 1 24  ? -13.411 23.153  -13.512 1.00 42.99 ?  24  THR   B O   1 
ATOM   2466 C  CB  . THR   B 1 24  ? -15.493 24.620  -14.951 1.00 35.05 ?  24  THR   B CB  1 
ATOM   2467 O  OG1 . THR   B 1 24  ? -16.276 23.500  -15.379 1.00 40.77 ?  24  THR   B OG1 1 
ATOM   2468 C  CG2 . THR   B 1 24  ? -16.093 25.896  -15.538 1.00 34.87 ?  24  THR   B CG2 1 
ATOM   2469 N  N   . THR   B 1 25  ? -13.050 22.188  -15.506 1.00 39.97 ?  25  THR   B N   1 
ATOM   2470 C  CA  . THR   B 1 25  ? -12.543 20.948  -14.935 1.00 37.40 ?  25  THR   B CA  1 
ATOM   2471 C  C   . THR   B 1 25  ? -11.025 20.994  -14.854 1.00 42.34 ?  25  THR   B C   1 
ATOM   2472 O  O   . THR   B 1 25  ? -10.350 21.291  -15.846 1.00 38.42 ?  25  THR   B O   1 
ATOM   2473 C  CB  . THR   B 1 25  ? -12.977 19.735  -15.757 1.00 40.24 ?  25  THR   B CB  1 
ATOM   2474 O  OG1 . THR   B 1 25  ? -14.405 19.697  -15.845 1.00 46.08 ?  25  THR   B OG1 1 
ATOM   2475 C  CG2 . THR   B 1 25  ? -12.478 18.453  -15.098 1.00 45.01 ?  25  THR   B CG2 1 
ATOM   2476 N  N   . THR   B 1 26  ? -10.496 20.701  -13.671 1.00 35.82 ?  26  THR   B N   1 
ATOM   2477 C  CA  . THR   B 1 26  ? -9.070  20.532  -13.460 1.00 34.23 ?  26  THR   B CA  1 
ATOM   2478 C  C   . THR   B 1 26  ? -8.836  19.133  -12.912 1.00 39.29 ?  26  THR   B C   1 
ATOM   2479 O  O   . THR   B 1 26  ? -9.554  18.691  -12.009 1.00 41.08 ?  26  THR   B O   1 
ATOM   2480 C  CB  . THR   B 1 26  ? -8.534  21.589  -12.496 1.00 46.25 ?  26  THR   B CB  1 
ATOM   2481 O  OG1 . THR   B 1 26  ? -8.925  22.888  -12.958 1.00 50.00 ?  26  THR   B OG1 1 
ATOM   2482 C  CG2 . THR   B 1 26  ? -7.027  21.520  -12.413 1.00 47.20 ?  26  THR   B CG2 1 
ATOM   2483 N  N   . LEU   B 1 27  ? -7.857  18.430  -13.465 1.00 31.48 ?  27  LEU   B N   1 
ATOM   2484 C  CA  . LEU   B 1 27  ? -7.486  17.136  -12.911 1.00 29.62 ?  27  LEU   B CA  1 
ATOM   2485 C  C   . LEU   B 1 27  ? -5.996  16.917  -13.160 1.00 29.65 ?  27  LEU   B C   1 
ATOM   2486 O  O   . LEU   B 1 27  ? -5.254  17.862  -13.441 1.00 31.77 ?  27  LEU   B O   1 
ATOM   2487 C  CB  . LEU   B 1 27  ? -8.390  16.023  -13.470 1.00 24.89 ?  27  LEU   B CB  1 
ATOM   2488 C  CG  . LEU   B 1 27  ? -8.774  15.953  -14.952 1.00 29.73 ?  27  LEU   B CG  1 
ATOM   2489 C  CD1 . LEU   B 1 27  ? -7.538  15.825  -15.851 1.00 25.38 ?  27  LEU   B CD1 1 
ATOM   2490 C  CD2 . LEU   B 1 27  ? -9.720  14.780  -15.168 1.00 30.97 ?  27  LEU   B CD2 1 
ATOM   2491 N  N   . ASN   B 1 28  ? -5.552  15.678  -13.023 1.00 25.30 ?  28  ASN   B N   1 
ATOM   2492 C  CA  . ASN   B 1 28  ? -4.144  15.340  -13.126 1.00 24.47 ?  28  ASN   B CA  1 
ATOM   2493 C  C   . ASN   B 1 28  ? -3.850  14.729  -14.490 1.00 25.94 ?  28  ASN   B C   1 
ATOM   2494 O  O   . ASN   B 1 28  ? -4.664  13.974  -15.025 1.00 25.60 ?  28  ASN   B O   1 
ATOM   2495 C  CB  . ASN   B 1 28  ? -3.757  14.364  -12.019 1.00 25.99 ?  28  ASN   B CB  1 
ATOM   2496 C  CG  . ASN   B 1 28  ? -4.149  14.872  -10.645 1.00 27.44 ?  28  ASN   B CG  1 
ATOM   2497 O  OD1 . ASN   B 1 28  ? -3.479  15.738  -10.088 1.00 31.35 ?  28  ASN   B OD1 1 
ATOM   2498 N  ND2 . ASN   B 1 28  ? -5.253  14.354  -10.104 1.00 26.07 ?  28  ASN   B ND2 1 
ATOM   2499 N  N   . GLY   B 1 29  ? -2.683  15.064  -15.042 1.00 26.28 ?  29  GLY   B N   1 
ATOM   2500 C  CA  . GLY   B 1 29  ? -2.194  14.439  -16.256 1.00 27.88 ?  29  GLY   B CA  1 
ATOM   2501 C  C   . GLY   B 1 29  ? -0.857  13.763  -16.029 1.00 29.44 ?  29  GLY   B C   1 
ATOM   2502 O  O   . GLY   B 1 29  ? -0.116  14.110  -15.102 1.00 28.32 ?  29  GLY   B O   1 
ATOM   2503 N  N   . LEU   B 1 30  ? -0.548  12.772  -16.853 1.00 28.32 ?  30  LEU   B N   1 
ATOM   2504 C  CA  . LEU   B 1 30  ? 0.716   12.055  -16.795 1.00 26.03 ?  30  LEU   B CA  1 
ATOM   2505 C  C   . LEU   B 1 30  ? 1.557   12.505  -17.980 1.00 29.56 ?  30  LEU   B C   1 
ATOM   2506 O  O   . LEU   B 1 30  ? 1.161   12.288  -19.129 1.00 28.20 ?  30  LEU   B O   1 
ATOM   2507 C  CB  . LEU   B 1 30  ? 0.488   10.544  -16.840 1.00 23.91 ?  30  LEU   B CB  1 
ATOM   2508 C  CG  . LEU   B 1 30  ? 1.736   9.685   -16.614 1.00 27.17 ?  30  LEU   B CG  1 
ATOM   2509 C  CD1 . LEU   B 1 30  ? 2.217   9.844   -15.175 1.00 26.63 ?  30  LEU   B CD1 1 
ATOM   2510 C  CD2 . LEU   B 1 30  ? 1.458   8.218   -16.935 1.00 27.10 ?  30  LEU   B CD2 1 
ATOM   2511 N  N   . TRP   B 1 31  ? 2.714   13.121  -17.704 1.00 29.32 ?  31  TRP   B N   1 
ATOM   2512 C  CA  . TRP   B 1 31  ? 3.544   13.755  -18.731 1.00 28.50 ?  31  TRP   B CA  1 
ATOM   2513 C  C   . TRP   B 1 31  ? 4.730   12.852  -19.060 1.00 30.69 ?  31  TRP   B C   1 
ATOM   2514 O  O   . TRP   B 1 31  ? 5.664   12.724  -18.259 1.00 28.15 ?  31  TRP   B O   1 
ATOM   2515 C  CB  . TRP   B 1 31  ? 4.022   15.125  -18.254 1.00 29.61 ?  31  TRP   B CB  1 
ATOM   2516 C  CG  . TRP   B 1 31  ? 4.833   15.902  -19.250 1.00 30.86 ?  31  TRP   B CG  1 
ATOM   2517 C  CD1 . TRP   B 1 31  ? 4.878   15.713  -20.608 1.00 32.11 ?  31  TRP   B CD1 1 
ATOM   2518 C  CD2 . TRP   B 1 31  ? 5.712   17.003  -18.972 1.00 33.48 ?  31  TRP   B CD2 1 
ATOM   2519 N  NE1 . TRP   B 1 31  ? 5.731   16.625  -21.183 1.00 33.56 ?  31  TRP   B NE1 1 
ATOM   2520 C  CE2 . TRP   B 1 31  ? 6.254   17.428  -20.205 1.00 35.85 ?  31  TRP   B CE2 1 
ATOM   2521 C  CE3 . TRP   B 1 31  ? 6.097   17.666  -17.802 1.00 35.59 ?  31  TRP   B CE3 1 
ATOM   2522 C  CZ2 . TRP   B 1 31  ? 7.158   18.485  -20.299 1.00 35.25 ?  31  TRP   B CZ2 1 
ATOM   2523 C  CZ3 . TRP   B 1 31  ? 6.994   18.714  -17.898 1.00 34.81 ?  31  TRP   B CZ3 1 
ATOM   2524 C  CH2 . TRP   B 1 31  ? 7.514   19.114  -19.140 1.00 36.16 ?  31  TRP   B CH2 1 
ATOM   2525 N  N   . LEU   B 1 32  ? 4.709   12.252  -20.252 1.00 29.33 ?  32  LEU   B N   1 
ATOM   2526 C  CA  . LEU   B 1 32  ? 5.734   11.307  -20.679 1.00 27.18 ?  32  LEU   B CA  1 
ATOM   2527 C  C   . LEU   B 1 32  ? 6.196   11.687  -22.076 1.00 31.66 ?  32  LEU   B C   1 
ATOM   2528 O  O   . LEU   B 1 32  ? 5.391   11.709  -23.018 1.00 30.47 ?  32  LEU   B O   1 
ATOM   2529 C  CB  . LEU   B 1 32  ? 5.214   9.868   -20.657 1.00 27.08 ?  32  LEU   B CB  1 
ATOM   2530 C  CG  . LEU   B 1 32  ? 4.803   9.331   -19.283 1.00 28.85 ?  32  LEU   B CG  1 
ATOM   2531 C  CD1 . LEU   B 1 32  ? 4.201   7.943   -19.400 1.00 26.55 ?  32  LEU   B CD1 1 
ATOM   2532 C  CD2 . LEU   B 1 32  ? 6.002   9.313   -18.358 1.00 31.78 ?  32  LEU   B CD2 1 
ATOM   2533 N  N   . ASP   B 1 33  ? 7.488   11.973  -22.205 1.00 33.54 ?  33  ASP   B N   1 
ATOM   2534 C  CA  . ASP   B 1 33  ? 8.061   12.508  -23.439 1.00 33.56 ?  33  ASP   B CA  1 
ATOM   2535 C  C   . ASP   B 1 33  ? 7.273   13.777  -23.756 1.00 31.13 ?  33  ASP   B C   1 
ATOM   2536 O  O   . ASP   B 1 33  ? 7.132   14.641  -22.876 1.00 32.09 ?  33  ASP   B O   1 
ATOM   2537 C  CB  . ASP   B 1 33  ? 8.063   11.417  -24.496 1.00 33.70 ?  33  ASP   B CB  1 
ATOM   2538 C  CG  . ASP   B 1 33  ? 9.004   10.264  -24.138 1.00 37.58 ?  33  ASP   B CG  1 
ATOM   2539 O  OD1 . ASP   B 1 33  ? 10.107  10.538  -23.615 1.00 46.05 ?  33  ASP   B OD1 1 
ATOM   2540 O  OD2 . ASP   B 1 33  ? 8.644   9.087   -24.372 1.00 43.02 ?  33  ASP   B OD2 1 
ATOM   2541 N  N   . ASP   B 1 34  ? 6.716   13.933  -24.948 1.00 29.11 ?  34  ASP   B N   1 
ATOM   2542 C  CA  . ASP   B 1 34  ? 5.987   15.153  -25.273 1.00 32.94 ?  34  ASP   B CA  1 
ATOM   2543 C  C   . ASP   B 1 34  ? 4.475   14.939  -25.309 1.00 31.30 ?  34  ASP   B C   1 
ATOM   2544 O  O   . ASP   B 1 34  ? 3.765   15.635  -26.041 1.00 34.22 ?  34  ASP   B O   1 
ATOM   2545 C  CB  . ASP   B 1 34  ? 6.475   15.732  -26.602 1.00 34.02 ?  34  ASP   B CB  1 
ATOM   2546 C  CG  . ASP   B 1 34  ? 6.341   14.752  -27.754 1.00 40.64 ?  34  ASP   B CG  1 
ATOM   2547 O  OD1 . ASP   B 1 34  ? 6.065   13.561  -27.495 1.00 37.74 ?  34  ASP   B OD1 1 
ATOM   2548 O  OD2 . ASP   B 1 34  ? 6.515   15.176  -28.921 1.00 44.18 ?  34  ASP   B OD2 1 
ATOM   2549 N  N   . VAL   B 1 35  ? 3.963   13.990  -24.523 1.00 32.46 ?  35  VAL   B N   1 
ATOM   2550 C  CA  . VAL   B 1 35  ? 2.533   13.713  -24.461 1.00 26.74 ?  35  VAL   B CA  1 
ATOM   2551 C  C   . VAL   B 1 35  ? 2.068   13.734  -23.010 1.00 26.59 ?  35  VAL   B C   1 
ATOM   2552 O  O   . VAL   B 1 35  ? 2.760   13.228  -22.117 1.00 26.45 ?  35  VAL   B O   1 
ATOM   2553 C  CB  . VAL   B 1 35  ? 2.177   12.361  -25.112 1.00 29.91 ?  35  VAL   B CB  1 
ATOM   2554 C  CG1 . VAL   B 1 35  ? 0.664   12.144  -25.061 1.00 27.89 ?  35  VAL   B CG1 1 
ATOM   2555 C  CG2 . VAL   B 1 35  ? 2.686   12.311  -26.546 1.00 30.74 ?  35  VAL   B CG2 1 
ATOM   2556 N  N   . VAL   B 1 36  ? 0.897   14.327  -22.779 1.00 26.12 ?  36  VAL   B N   1 
ATOM   2557 C  CA  . VAL   B 1 36  ? 0.219   14.283  -21.487 1.00 24.79 ?  36  VAL   B CA  1 
ATOM   2558 C  C   . VAL   B 1 36  ? -1.004  13.392  -21.630 1.00 28.20 ?  36  VAL   B C   1 
ATOM   2559 O  O   . VAL   B 1 36  ? -1.809  13.573  -22.553 1.00 28.24 ?  36  VAL   B O   1 
ATOM   2560 C  CB  . VAL   B 1 36  ? -0.174  15.687  -20.996 1.00 27.06 ?  36  VAL   B CB  1 
ATOM   2561 C  CG1 . VAL   B 1 36  ? -0.826  15.603  -19.616 1.00 23.09 ?  36  VAL   B CG1 1 
ATOM   2562 C  CG2 . VAL   B 1 36  ? 1.055   16.589  -20.938 1.00 26.64 ?  36  VAL   B CG2 1 
ATOM   2563 N  N   . TYR   B 1 37  ? -1.127  12.418  -20.736 1.00 27.12 ?  37  TYR   B N   1 
ATOM   2564 C  CA  . TYR   B 1 37  ? -2.244  11.489  -20.714 1.00 23.96 ?  37  TYR   B CA  1 
ATOM   2565 C  C   . TYR   B 1 37  ? -3.144  11.831  -19.537 1.00 29.06 ?  37  TYR   B C   1 
ATOM   2566 O  O   . TYR   B 1 37  ? -2.658  12.115  -18.438 1.00 24.60 ?  37  TYR   B O   1 
ATOM   2567 C  CB  . TYR   B 1 37  ? -1.760  10.043  -20.584 1.00 26.96 ?  37  TYR   B CB  1 
ATOM   2568 C  CG  . TYR   B 1 37  ? -0.737  9.646   -21.623 1.00 25.68 ?  37  TYR   B CG  1 
ATOM   2569 C  CD1 . TYR   B 1 37  ? 0.613   9.976   -21.480 1.00 30.08 ?  37  TYR   B CD1 1 
ATOM   2570 C  CD2 . TYR   B 1 37  ? -1.119  8.940   -22.747 1.00 27.90 ?  37  TYR   B CD2 1 
ATOM   2571 C  CE1 . TYR   B 1 37  ? 1.549   9.614   -22.452 1.00 29.33 ?  37  TYR   B CE1 1 
ATOM   2572 C  CE2 . TYR   B 1 37  ? -0.202  8.573   -23.709 1.00 26.92 ?  37  TYR   B CE2 1 
ATOM   2573 C  CZ  . TYR   B 1 37  ? 1.126   8.910   -23.566 1.00 28.72 ?  37  TYR   B CZ  1 
ATOM   2574 O  OH  . TYR   B 1 37  ? 2.013   8.523   -24.557 1.00 28.94 ?  37  TYR   B OH  1 
ATOM   2575 N  N   . CYS   B 1 38  ? -4.450  11.799  -19.767 1.00 25.28 ?  38  CYS   B N   1 
ATOM   2576 C  CA  . CYS   B 1 38  ? -5.411  12.121  -18.721 1.00 25.09 ?  38  CYS   B CA  1 
ATOM   2577 C  C   . CYS   B 1 38  ? -6.768  11.568  -19.142 1.00 26.45 ?  38  CYS   B C   1 
ATOM   2578 O  O   . CYS   B 1 38  ? -6.948  11.167  -20.300 1.00 25.10 ?  38  CYS   B O   1 
ATOM   2579 C  CB  . CYS   B 1 38  ? -5.464  13.638  -18.471 1.00 24.24 ?  38  CYS   B CB  1 
ATOM   2580 S  SG  . CYS   B 1 38  ? -6.490  14.535  -19.632 1.00 28.51 ?  38  CYS   B SG  1 
ATOM   2581 N  N   . PRO   B 1 39  ? -7.734  11.482  -18.215 1.00 24.15 ?  39  PRO   B N   1 
ATOM   2582 C  CA  . PRO   B 1 39  ? -9.053  10.949  -18.588 1.00 23.13 ?  39  PRO   B CA  1 
ATOM   2583 C  C   . PRO   B 1 39  ? -9.770  11.846  -19.591 1.00 24.27 ?  39  PRO   B C   1 
ATOM   2584 O  O   . PRO   B 1 39  ? -9.720  13.076  -19.506 1.00 25.86 ?  39  PRO   B O   1 
ATOM   2585 C  CB  . PRO   B 1 39  ? -9.806  10.895  -17.252 1.00 27.26 ?  39  PRO   B CB  1 
ATOM   2586 C  CG  . PRO   B 1 39  ? -8.724  10.825  -16.205 1.00 22.90 ?  39  PRO   B CG  1 
ATOM   2587 C  CD  . PRO   B 1 39  ? -7.613  11.675  -16.757 1.00 25.60 ?  39  PRO   B CD  1 
ATOM   2588 N  N   . ARG   B 1 40  ? -10.455 11.218  -20.549 1.00 24.62 ?  40  ARG   B N   1 
ATOM   2589 C  CA  . ARG   B 1 40  ? -11.155 12.018  -21.547 1.00 28.01 ?  40  ARG   B CA  1 
ATOM   2590 C  C   . ARG   B 1 40  ? -12.319 12.803  -20.946 1.00 28.83 ?  40  ARG   B C   1 
ATOM   2591 O  O   . ARG   B 1 40  ? -12.734 13.806  -21.532 1.00 29.96 ?  40  ARG   B O   1 
ATOM   2592 C  CB  . ARG   B 1 40  ? -11.630 11.140  -22.714 1.00 26.18 ?  40  ARG   B CB  1 
ATOM   2593 C  CG  . ARG   B 1 40  ? -12.590 10.028  -22.347 1.00 28.42 ?  40  ARG   B CG  1 
ATOM   2594 C  CD  . ARG   B 1 40  ? -13.238 9.429   -23.594 1.00 27.27 ?  40  ARG   B CD  1 
ATOM   2595 N  NE  . ARG   B 1 40  ? -14.115 8.303   -23.281 1.00 26.11 ?  40  ARG   B NE  1 
ATOM   2596 C  CZ  . ARG   B 1 40  ? -14.772 7.594   -24.194 1.00 31.94 ?  40  ARG   B CZ  1 
ATOM   2597 N  NH1 . ARG   B 1 40  ? -14.652 7.888   -25.485 1.00 28.50 ?  40  ARG   B NH1 1 
ATOM   2598 N  NH2 . ARG   B 1 40  ? -15.547 6.587   -23.818 1.00 30.12 ?  40  ARG   B NH2 1 
ATOM   2599 N  N   . HIS   B 1 41  ? -12.811 12.430  -19.761 1.00 27.80 ?  41  HIS   B N   1 
ATOM   2600 C  CA  . HIS   B 1 41  ? -13.946 13.176  -19.224 1.00 29.61 ?  41  HIS   B CA  1 
ATOM   2601 C  C   . HIS   B 1 41  ? -13.567 14.584  -18.777 1.00 27.84 ?  41  HIS   B C   1 
ATOM   2602 O  O   . HIS   B 1 41  ? -14.457 15.367  -18.444 1.00 32.32 ?  41  HIS   B O   1 
ATOM   2603 C  CB  . HIS   B 1 41  ? -14.636 12.393  -18.098 1.00 30.78 ?  41  HIS   B CB  1 
ATOM   2604 C  CG  . HIS   B 1 41  ? -13.830 12.235  -16.841 1.00 26.10 ?  41  HIS   B CG  1 
ATOM   2605 N  ND1 . HIS   B 1 41  ? -13.813 11.055  -16.129 1.00 32.67 ?  41  HIS   B ND1 1 
ATOM   2606 C  CD2 . HIS   B 1 41  ? -13.082 13.113  -16.130 1.00 27.03 ?  41  HIS   B CD2 1 
ATOM   2607 C  CE1 . HIS   B 1 41  ? -13.061 11.202  -15.051 1.00 29.18 ?  41  HIS   B CE1 1 
ATOM   2608 N  NE2 . HIS   B 1 41  ? -12.606 12.442  -15.028 1.00 34.57 ?  41  HIS   B NE2 1 
ATOM   2609 N  N   . VAL   B 1 42  ? -12.282 14.942  -18.824 1.00 25.38 ?  42  VAL   B N   1 
ATOM   2610 C  CA  . VAL   B 1 42  ? -11.859 16.325  -18.607 1.00 27.85 ?  42  VAL   B CA  1 
ATOM   2611 C  C   . VAL   B 1 42  ? -12.545 17.311  -19.560 1.00 34.24 ?  42  VAL   B C   1 
ATOM   2612 O  O   . VAL   B 1 42  ? -12.651 18.504  -19.248 1.00 36.59 ?  42  VAL   B O   1 
ATOM   2613 C  CB  . VAL   B 1 42  ? -10.322 16.420  -18.727 1.00 29.27 ?  42  VAL   B CB  1 
ATOM   2614 C  CG1 . VAL   B 1 42  ? -9.870  16.326  -20.193 1.00 32.27 ?  42  VAL   B CG1 1 
ATOM   2615 C  CG2 . VAL   B 1 42  ? -9.817  17.697  -18.085 1.00 33.41 ?  42  VAL   B CG2 1 
ATOM   2616 N  N   . ILE   B 1 43  ? -13.002 16.854  -20.736 1.00 35.20 ?  43  ILE   B N   1 
ATOM   2617 C  CA  . ILE   B 1 43  ? -13.617 17.773  -21.698 1.00 30.90 ?  43  ILE   B CA  1 
ATOM   2618 C  C   . ILE   B 1 43  ? -15.121 17.930  -21.488 1.00 36.06 ?  43  ILE   B C   1 
ATOM   2619 O  O   . ILE   B 1 43  ? -15.769 18.672  -22.237 1.00 41.07 ?  43  ILE   B O   1 
ATOM   2620 C  CB  . ILE   B 1 43  ? -13.370 17.353  -23.166 1.00 34.78 ?  43  ILE   B CB  1 
ATOM   2621 C  CG1 . ILE   B 1 43  ? -14.157 16.090  -23.534 1.00 30.03 ?  43  ILE   B CG1 1 
ATOM   2622 C  CG2 . ILE   B 1 43  ? -11.879 17.165  -23.451 1.00 32.36 ?  43  ILE   B CG2 1 
ATOM   2623 C  CD1 . ILE   B 1 43  ? -13.936 15.652  -24.986 1.00 31.68 ?  43  ILE   B CD1 1 
ATOM   2624 N  N   . CYS   B 1 44  ? -15.695 17.275  -20.491 1.00 35.31 ?  44  CYS   B N   1 
ATOM   2625 C  CA  . CYS   B 1 44  ? -17.132 17.313  -20.279 1.00 34.48 ?  44  CYS   B CA  1 
ATOM   2626 C  C   . CYS   B 1 44  ? -17.517 18.295  -19.185 1.00 37.54 ?  44  CYS   B C   1 
ATOM   2627 O  O   . CYS   B 1 44  ? -16.860 18.373  -18.144 1.00 38.84 ?  44  CYS   B O   1 
ATOM   2628 C  CB  . CYS   B 1 44  ? -17.652 15.934  -19.901 1.00 34.82 ?  44  CYS   B CB  1 
ATOM   2629 S  SG  . CYS   B 1 44  ? -17.447 14.720  -21.174 1.00 38.91 ?  44  CYS   B SG  1 
ATOM   2630 N  N   . THR   B 1 45  ? -18.602 19.028  -19.428 1.00 43.84 ?  45  THR   B N   1 
ATOM   2631 C  CA  . THR   B 1 45  ? -19.332 19.679  -18.352 1.00 39.56 ?  45  THR   B CA  1 
ATOM   2632 C  C   . THR   B 1 45  ? -20.129 18.630  -17.581 1.00 38.43 ?  45  THR   B C   1 
ATOM   2633 O  O   . THR   B 1 45  ? -20.247 17.474  -17.995 1.00 37.48 ?  45  THR   B O   1 
ATOM   2634 C  CB  . THR   B 1 45  ? -20.273 20.753  -18.905 1.00 46.01 ?  45  THR   B CB  1 
ATOM   2635 O  OG1 . THR   B 1 45  ? -21.404 20.127  -19.528 1.00 42.76 ?  45  THR   B OG1 1 
ATOM   2636 C  CG2 . THR   B 1 45  ? -19.556 21.628  -19.943 1.00 39.26 ?  45  THR   B CG2 1 
ATOM   2637 N  N   . SER   B 1 46  ? -20.689 19.036  -16.441 1.00 43.25 ?  46  SER   B N   1 
ATOM   2638 C  CA  . SER   B 1 46  ? -21.497 18.091  -15.678 1.00 41.05 ?  46  SER   B CA  1 
ATOM   2639 C  C   . SER   B 1 46  ? -22.740 17.664  -16.458 1.00 39.25 ?  46  SER   B C   1 
ATOM   2640 O  O   . SER   B 1 46  ? -23.168 16.507  -16.362 1.00 42.26 ?  46  SER   B O   1 
ATOM   2641 C  CB  . SER   B 1 46  ? -21.866 18.695  -14.321 1.00 45.83 ?  46  SER   B CB  1 
ATOM   2642 O  OG  . SER   B 1 46  ? -22.586 19.904  -14.485 1.00 50.31 ?  46  SER   B OG  1 
ATOM   2643 N  N   . GLU   B 1 47  ? -23.322 18.566  -17.252 1.00 39.58 ?  47  GLU   B N   1 
ATOM   2644 C  CA  . GLU   B 1 47  ? -24.438 18.171  -18.109 1.00 43.71 ?  47  GLU   B CA  1 
ATOM   2645 C  C   . GLU   B 1 47  ? -23.986 17.188  -19.184 1.00 42.41 ?  47  GLU   B C   1 
ATOM   2646 O  O   . GLU   B 1 47  ? -24.719 16.251  -19.524 1.00 35.27 ?  47  GLU   B O   1 
ATOM   2647 C  CB  . GLU   B 1 47  ? -25.081 19.402  -18.751 1.00 44.19 ?  47  GLU   B CB  1 
ATOM   2648 N  N   . ASP   B 1 48  ? -22.775 17.380  -19.718 1.00 36.68 ?  48  ASP   B N   1 
ATOM   2649 C  CA  . ASP   B 1 48  ? -22.241 16.447  -20.707 1.00 38.24 ?  48  ASP   B CA  1 
ATOM   2650 C  C   . ASP   B 1 48  ? -22.157 15.026  -20.155 1.00 36.19 ?  48  ASP   B C   1 
ATOM   2651 O  O   . ASP   B 1 48  ? -22.440 14.062  -20.875 1.00 34.56 ?  48  ASP   B O   1 
ATOM   2652 C  CB  . ASP   B 1 48  ? -20.858 16.906  -21.174 1.00 37.84 ?  48  ASP   B CB  1 
ATOM   2653 C  CG  . ASP   B 1 48  ? -20.898 18.212  -21.943 1.00 43.02 ?  48  ASP   B CG  1 
ATOM   2654 O  OD1 . ASP   B 1 48  ? -21.863 18.426  -22.716 1.00 41.02 ?  48  ASP   B OD1 1 
ATOM   2655 O  OD2 . ASP   B 1 48  ? -19.955 19.019  -21.773 1.00 42.51 ?  48  ASP   B OD2 1 
ATOM   2656 N  N   . MET   B 1 49  ? -21.764 14.879  -18.880 1.00 34.98 ?  49  MET   B N   1 
ATOM   2657 C  CA  . MET   B 1 49  ? -21.519 13.561  -18.290 1.00 32.97 ?  49  MET   B CA  1 
ATOM   2658 C  C   . MET   B 1 49  ? -22.753 12.672  -18.288 1.00 35.12 ?  49  MET   B C   1 
ATOM   2659 O  O   . MET   B 1 49  ? -22.616 11.443  -18.283 1.00 34.13 ?  49  MET   B O   1 
ATOM   2660 C  CB  . MET   B 1 49  ? -21.010 13.691  -16.848 1.00 37.87 ?  49  MET   B CB  1 
ATOM   2661 C  CG  . MET   B 1 49  ? -19.569 14.132  -16.686 1.00 33.90 ?  49  MET   B CG  1 
ATOM   2662 S  SD  . MET   B 1 49  ? -18.367 13.210  -17.681 1.00 34.44 ?  49  MET   B SD  1 
ATOM   2663 C  CE  . MET   B 1 49  ? -18.644 11.502  -17.213 1.00 31.51 ?  49  MET   B CE  1 
ATOM   2664 N  N   . LEU   B 1 50  ? -23.953 13.260  -18.271 1.00 36.56 ?  50  LEU   B N   1 
ATOM   2665 C  CA  . LEU   B 1 50  ? -25.176 12.465  -18.268 1.00 34.08 ?  50  LEU   B CA  1 
ATOM   2666 C  C   . LEU   B 1 50  ? -25.295 11.609  -19.524 1.00 36.37 ?  50  LEU   B C   1 
ATOM   2667 O  O   . LEU   B 1 50  ? -25.788 10.477  -19.462 1.00 35.53 ?  50  LEU   B O   1 
ATOM   2668 C  CB  . LEU   B 1 50  ? -26.385 13.391  -18.131 1.00 36.58 ?  50  LEU   B CB  1 
ATOM   2669 C  CG  . LEU   B 1 50  ? -26.407 14.234  -16.854 1.00 39.93 ?  50  LEU   B CG  1 
ATOM   2670 C  CD1 . LEU   B 1 50  ? -27.374 15.406  -16.983 1.00 43.21 ?  50  LEU   B CD1 1 
ATOM   2671 C  CD2 . LEU   B 1 50  ? -26.757 13.364  -15.653 1.00 36.58 ?  50  LEU   B CD2 1 
ATOM   2672 N  N   . ASN   B 1 51  ? -24.835 12.117  -20.657 1.00 37.33 ?  51  ASN   B N   1 
ATOM   2673 C  CA  . ASN   B 1 51  ? -24.853 11.345  -21.893 1.00 36.86 ?  51  ASN   B CA  1 
ATOM   2674 C  C   . ASN   B 1 51  ? -23.827 11.917  -22.870 1.00 39.06 ?  51  ASN   B C   1 
ATOM   2675 O  O   . ASN   B 1 51  ? -24.196 12.633  -23.808 1.00 33.02 ?  51  ASN   B O   1 
ATOM   2676 C  CB  . ASN   B 1 51  ? -26.260 11.349  -22.498 1.00 36.57 ?  51  ASN   B CB  1 
ATOM   2677 C  CG  . ASN   B 1 51  ? -26.404 10.374  -23.650 1.00 46.87 ?  51  ASN   B CG  1 
ATOM   2678 O  OD1 . ASN   B 1 51  ? -25.712 9.356   -23.709 1.00 49.04 ?  51  ASN   B OD1 1 
ATOM   2679 N  ND2 . ASN   B 1 51  ? -27.307 10.681  -24.575 1.00 46.22 ?  51  ASN   B ND2 1 
ATOM   2680 N  N   . PRO   B 1 52  ? -22.539 11.624  -22.688 1.00 34.44 ?  52  PRO   B N   1 
ATOM   2681 C  CA  . PRO   B 1 52  ? -21.505 12.316  -23.467 1.00 31.80 ?  52  PRO   B CA  1 
ATOM   2682 C  C   . PRO   B 1 52  ? -21.278 11.698  -24.838 1.00 32.60 ?  52  PRO   B C   1 
ATOM   2683 O  O   . PRO   B 1 52  ? -21.325 10.478  -25.016 1.00 31.76 ?  52  PRO   B O   1 
ATOM   2684 C  CB  . PRO   B 1 52  ? -20.254 12.168  -22.588 1.00 36.08 ?  52  PRO   B CB  1 
ATOM   2685 C  CG  . PRO   B 1 52  ? -20.459 10.859  -21.892 1.00 33.01 ?  52  PRO   B CG  1 
ATOM   2686 C  CD  . PRO   B 1 52  ? -21.960 10.727  -21.672 1.00 33.07 ?  52  PRO   B CD  1 
ATOM   2687 N  N   . ASN   B 1 53  ? -21.029 12.562  -25.814 1.00 33.04 ?  53  ASN   B N   1 
ATOM   2688 C  CA  . ASN   B 1 53  ? -20.529 12.155  -27.126 1.00 30.62 ?  53  ASN   B CA  1 
ATOM   2689 C  C   . ASN   B 1 53  ? -19.123 12.738  -27.217 1.00 30.17 ?  53  ASN   B C   1 
ATOM   2690 O  O   . ASN   B 1 53  ? -18.932 13.893  -27.604 1.00 32.07 ?  53  ASN   B O   1 
ATOM   2691 C  CB  . ASN   B 1 53  ? -21.434 12.632  -28.264 1.00 31.67 ?  53  ASN   B CB  1 
ATOM   2692 C  CG  . ASN   B 1 53  ? -20.985 12.112  -29.619 1.00 38.33 ?  53  ASN   B CG  1 
ATOM   2693 O  OD1 . ASN   B 1 53  ? -19.791 12.088  -29.930 1.00 35.43 ?  53  ASN   B OD1 1 
ATOM   2694 N  ND2 . ASN   B 1 53  ? -21.946 11.685  -30.434 1.00 44.74 ?  53  ASN   B ND2 1 
ATOM   2695 N  N   . TYR   B 1 54  ? -18.133 11.929  -26.832 1.00 31.75 ?  54  TYR   B N   1 
ATOM   2696 C  CA  . TYR   B 1 54  ? -16.774 12.445  -26.704 1.00 31.67 ?  54  TYR   B CA  1 
ATOM   2697 C  C   . TYR   B 1 54  ? -16.212 12.886  -28.048 1.00 31.24 ?  54  TYR   B C   1 
ATOM   2698 O  O   . TYR   B 1 54  ? -15.582 13.945  -28.148 1.00 31.14 ?  54  TYR   B O   1 
ATOM   2699 C  CB  . TYR   B 1 54  ? -15.877 11.392  -26.061 1.00 30.07 ?  54  TYR   B CB  1 
ATOM   2700 C  CG  . TYR   B 1 54  ? -16.163 11.222  -24.591 1.00 28.36 ?  54  TYR   B CG  1 
ATOM   2701 C  CD1 . TYR   B 1 54  ? -15.637 12.108  -23.665 1.00 31.03 ?  54  TYR   B CD1 1 
ATOM   2702 C  CD2 . TYR   B 1 54  ? -16.967 10.187  -24.129 1.00 27.01 ?  54  TYR   B CD2 1 
ATOM   2703 C  CE1 . TYR   B 1 54  ? -15.890 11.964  -22.316 1.00 29.18 ?  54  TYR   B CE1 1 
ATOM   2704 C  CE2 . TYR   B 1 54  ? -17.224 10.033  -22.771 1.00 29.59 ?  54  TYR   B CE2 1 
ATOM   2705 C  CZ  . TYR   B 1 54  ? -16.687 10.931  -21.873 1.00 31.06 ?  54  TYR   B CZ  1 
ATOM   2706 O  OH  . TYR   B 1 54  ? -16.931 10.800  -20.515 1.00 29.41 ?  54  TYR   B OH  1 
ATOM   2707 N  N   . GLU   B 1 55  ? -16.426 12.090  -29.094 1.00 32.88 ?  55  GLU   B N   1 
ATOM   2708 C  CA  . GLU   B 1 55  ? -15.979 12.502  -30.424 1.00 32.25 ?  55  GLU   B CA  1 
ATOM   2709 C  C   . GLU   B 1 55  ? -16.496 13.898  -30.760 1.00 33.40 ?  55  GLU   B C   1 
ATOM   2710 O  O   . GLU   B 1 55  ? -15.724 14.793  -31.125 1.00 35.61 ?  55  GLU   B O   1 
ATOM   2711 C  CB  . GLU   B 1 55  ? -16.441 11.484  -31.470 1.00 32.61 ?  55  GLU   B CB  1 
ATOM   2712 N  N   . ASP   B 1 56  ? -17.803 14.112  -30.593 1.00 35.96 ?  56  ASP   B N   1 
ATOM   2713 C  CA  . ASP   B 1 56  ? -18.394 15.413  -30.894 1.00 35.58 ?  56  ASP   B CA  1 
ATOM   2714 C  C   . ASP   B 1 56  ? -17.884 16.493  -29.947 1.00 37.07 ?  56  ASP   B C   1 
ATOM   2715 O  O   . ASP   B 1 56  ? -17.632 17.627  -30.366 1.00 38.31 ?  56  ASP   B O   1 
ATOM   2716 C  CB  . ASP   B 1 56  ? -19.920 15.318  -30.825 1.00 39.81 ?  56  ASP   B CB  1 
ATOM   2717 C  CG  . ASP   B 1 56  ? -20.604 16.573  -31.327 1.00 46.63 ?  56  ASP   B CG  1 
ATOM   2718 O  OD1 . ASP   B 1 56  ? -20.389 16.932  -32.505 1.00 46.47 ?  56  ASP   B OD1 1 
ATOM   2719 O  OD2 . ASP   B 1 56  ? -21.357 17.196  -30.548 1.00 51.03 ?  56  ASP   B OD2 1 
ATOM   2720 N  N   . LEU   B 1 57  ? -17.745 16.172  -28.661 1.00 38.61 ?  57  LEU   B N   1 
ATOM   2721 C  CA  . LEU   B 1 57  ? -17.237 17.168  -27.727 1.00 34.57 ?  57  LEU   B CA  1 
ATOM   2722 C  C   . LEU   B 1 57  ? -15.796 17.549  -28.047 1.00 35.63 ?  57  LEU   B C   1 
ATOM   2723 O  O   . LEU   B 1 57  ? -15.425 18.725  -27.955 1.00 40.19 ?  57  LEU   B O   1 
ATOM   2724 C  CB  . LEU   B 1 57  ? -17.354 16.647  -26.293 1.00 40.86 ?  57  LEU   B CB  1 
ATOM   2725 C  CG  . LEU   B 1 57  ? -18.774 16.640  -25.718 1.00 38.48 ?  57  LEU   B CG  1 
ATOM   2726 C  CD1 . LEU   B 1 57  ? -18.824 15.894  -24.393 1.00 37.09 ?  57  LEU   B CD1 1 
ATOM   2727 C  CD2 . LEU   B 1 57  ? -19.286 18.067  -25.555 1.00 39.46 ?  57  LEU   B CD2 1 
ATOM   2728 N  N   . LEU   B 1 58  ? -14.966 16.571  -28.418 1.00 34.72 ?  58  LEU   B N   1 
ATOM   2729 C  CA  . LEU   B 1 58  ? -13.556 16.865  -28.681 1.00 38.50 ?  58  LEU   B CA  1 
ATOM   2730 C  C   . LEU   B 1 58  ? -13.369 17.718  -29.936 1.00 38.41 ?  58  LEU   B C   1 
ATOM   2731 O  O   . LEU   B 1 58  ? -12.454 18.548  -29.979 1.00 35.87 ?  58  LEU   B O   1 
ATOM   2732 C  CB  . LEU   B 1 58  ? -12.755 15.568  -28.801 1.00 36.41 ?  58  LEU   B CB  1 
ATOM   2733 C  CG  . LEU   B 1 58  ? -11.228 15.714  -28.867 1.00 38.85 ?  58  LEU   B CG  1 
ATOM   2734 C  CD1 . LEU   B 1 58  ? -10.732 16.574  -27.717 1.00 35.24 ?  58  LEU   B CD1 1 
ATOM   2735 C  CD2 . LEU   B 1 58  ? -10.533 14.359  -28.853 1.00 31.91 ?  58  LEU   B CD2 1 
ATOM   2736 N  N   . ILE   B 1 59  ? -14.223 17.548  -30.953 1.00 42.44 ?  59  ILE   B N   1 
ATOM   2737 C  CA  . ILE   B 1 59  ? -14.074 18.336  -32.180 1.00 40.89 ?  59  ILE   B CA  1 
ATOM   2738 C  C   . ILE   B 1 59  ? -14.311 19.819  -31.909 1.00 40.96 ?  59  ILE   B C   1 
ATOM   2739 O  O   . ILE   B 1 59  ? -13.708 20.681  -32.561 1.00 50.27 ?  59  ILE   B O   1 
ATOM   2740 C  CB  . ILE   B 1 59  ? -15.007 17.804  -33.290 1.00 42.74 ?  59  ILE   B CB  1 
ATOM   2741 C  CG1 . ILE   B 1 59  ? -14.626 16.371  -33.663 1.00 40.35 ?  59  ILE   B CG1 1 
ATOM   2742 C  CG2 . ILE   B 1 59  ? -14.935 18.680  -34.538 1.00 47.49 ?  59  ILE   B CG2 1 
ATOM   2743 C  CD1 . ILE   B 1 59  ? -15.288 15.863  -34.915 1.00 43.91 ?  59  ILE   B CD1 1 
ATOM   2744 N  N   . ARG   B 1 60  ? -15.164 20.146  -30.933 1.00 44.69 ?  60  ARG   B N   1 
ATOM   2745 C  CA  . ARG   B 1 60  ? -15.418 21.542  -30.588 1.00 44.26 ?  60  ARG   B CA  1 
ATOM   2746 C  C   . ARG   B 1 60  ? -14.249 22.201  -29.864 1.00 45.32 ?  60  ARG   B C   1 
ATOM   2747 O  O   . ARG   B 1 60  ? -14.241 23.429  -29.732 1.00 49.08 ?  60  ARG   B O   1 
ATOM   2748 C  CB  . ARG   B 1 60  ? -16.681 21.657  -29.725 1.00 45.17 ?  60  ARG   B CB  1 
ATOM   2749 C  CG  . ARG   B 1 60  ? -17.977 21.255  -30.423 1.00 52.31 ?  60  ARG   B CG  1 
ATOM   2750 C  CD  . ARG   B 1 60  ? -19.159 21.235  -29.441 1.00 51.27 ?  60  ARG   B CD  1 
ATOM   2751 N  NE  . ARG   B 1 60  ? -20.209 20.303  -29.858 1.00 51.84 ?  60  ARG   B NE  1 
ATOM   2752 C  CZ  . ARG   B 1 60  ? -21.443 20.659  -30.212 1.00 59.70 ?  60  ARG   B CZ  1 
ATOM   2753 N  NH1 . ARG   B 1 60  ? -21.805 21.936  -30.191 1.00 57.48 ?  60  ARG   B NH1 1 
ATOM   2754 N  NH2 . ARG   B 1 60  ? -22.325 19.734  -30.580 1.00 56.93 ?  60  ARG   B NH2 1 
ATOM   2755 N  N   . LYS   B 1 61  ? -13.272 21.433  -29.388 1.00 45.23 ?  61  LYS   B N   1 
ATOM   2756 C  CA  . LYS   B 1 61  ? -12.128 21.985  -28.677 1.00 42.68 ?  61  LYS   B CA  1 
ATOM   2757 C  C   . LYS   B 1 61  ? -10.950 22.170  -29.627 1.00 44.22 ?  61  LYS   B C   1 
ATOM   2758 O  O   . LYS   B 1 61  ? -10.713 21.340  -30.510 1.00 43.81 ?  61  LYS   B O   1 
ATOM   2759 C  CB  . LYS   B 1 61  ? -11.706 21.077  -27.516 1.00 41.46 ?  61  LYS   B CB  1 
ATOM   2760 C  CG  . LYS   B 1 61  ? -12.816 20.689  -26.541 1.00 44.00 ?  61  LYS   B CG  1 
ATOM   2761 C  CD  . LYS   B 1 61  ? -13.229 21.848  -25.654 1.00 43.93 ?  61  LYS   B CD  1 
ATOM   2762 C  CE  . LYS   B 1 61  ? -13.914 21.360  -24.378 1.00 40.24 ?  61  LYS   B CE  1 
ATOM   2763 N  NZ  . LYS   B 1 61  ? -15.105 20.508  -24.652 1.00 47.27 ?  61  LYS   B NZ  1 
ATOM   2764 N  N   . SER   B 1 62  ? -10.218 23.265  -29.438 1.00 41.78 ?  62  SER   B N   1 
ATOM   2765 C  CA  . SER   B 1 62  ? -8.921  23.490  -30.060 1.00 43.19 ?  62  SER   B CA  1 
ATOM   2766 C  C   . SER   B 1 62  ? -7.826  23.308  -29.019 1.00 44.92 ?  62  SER   B C   1 
ATOM   2767 O  O   . SER   B 1 62  ? -8.095  23.187  -27.820 1.00 45.07 ?  62  SER   B O   1 
ATOM   2768 C  CB  . SER   B 1 62  ? -8.843  24.891  -30.670 1.00 45.75 ?  62  SER   B CB  1 
ATOM   2769 O  OG  . SER   B 1 62  ? -10.022 25.175  -31.396 1.00 50.69 ?  62  SER   B OG  1 
ATOM   2770 N  N   . ASN   B 1 63  ? -6.574  23.305  -29.489 1.00 41.30 ?  63  ASN   B N   1 
ATOM   2771 C  CA  . ASN   B 1 63  ? -5.442  23.098  -28.584 1.00 42.18 ?  63  ASN   B CA  1 
ATOM   2772 C  C   . ASN   B 1 63  ? -5.408  24.134  -27.469 1.00 44.55 ?  63  ASN   B C   1 
ATOM   2773 O  O   . ASN   B 1 63  ? -4.923  23.846  -26.369 1.00 40.37 ?  63  ASN   B O   1 
ATOM   2774 C  CB  . ASN   B 1 63  ? -4.126  23.123  -29.361 1.00 34.68 ?  63  ASN   B CB  1 
ATOM   2775 C  CG  . ASN   B 1 63  ? -3.978  21.934  -30.288 1.00 41.36 ?  63  ASN   B CG  1 
ATOM   2776 O  OD1 . ASN   B 1 63  ? -4.390  20.825  -29.949 1.00 37.94 ?  63  ASN   B OD1 1 
ATOM   2777 N  ND2 . ASN   B 1 63  ? -3.400  22.160  -31.474 1.00 41.38 ?  63  ASN   B ND2 1 
ATOM   2778 N  N   . HIS   B 1 64  ? -5.918  25.338  -27.725 1.00 45.12 ?  64  HIS   B N   1 
ATOM   2779 C  CA  . HIS   B 1 64  ? -5.894  26.392  -26.720 1.00 44.61 ?  64  HIS   B CA  1 
ATOM   2780 C  C   . HIS   B 1 64  ? -6.949  26.206  -25.638 1.00 44.50 ?  64  HIS   B C   1 
ATOM   2781 O  O   . HIS   B 1 64  ? -6.880  26.893  -24.616 1.00 47.17 ?  64  HIS   B O   1 
ATOM   2782 C  CB  . HIS   B 1 64  ? -6.081  27.759  -27.381 1.00 47.27 ?  64  HIS   B CB  1 
ATOM   2783 N  N   . ASN   B 1 65  ? -7.924  25.316  -25.839 1.00 44.14 ?  65  ASN   B N   1 
ATOM   2784 C  CA  . ASN   B 1 65  ? -8.897  25.017  -24.794 1.00 45.48 ?  65  ASN   B CA  1 
ATOM   2785 C  C   . ASN   B 1 65  ? -8.317  24.161  -23.673 1.00 43.41 ?  65  ASN   B C   1 
ATOM   2786 O  O   . ASN   B 1 65  ? -9.016  23.917  -22.686 1.00 44.29 ?  65  ASN   B O   1 
ATOM   2787 C  CB  . ASN   B 1 65  ? -10.118 24.312  -25.387 1.00 42.71 ?  65  ASN   B CB  1 
ATOM   2788 C  CG  . ASN   B 1 65  ? -10.899 25.197  -26.332 1.00 45.50 ?  65  ASN   B CG  1 
ATOM   2789 O  OD1 . ASN   B 1 65  ? -11.112 24.850  -27.493 1.00 47.67 ?  65  ASN   B OD1 1 
ATOM   2790 N  ND2 . ASN   B 1 65  ? -11.328 26.350  -25.842 1.00 44.73 ?  65  ASN   B ND2 1 
ATOM   2791 N  N   . PHE   B 1 66  ? -7.076  23.697  -23.804 1.00 41.96 ?  66  PHE   B N   1 
ATOM   2792 C  CA  . PHE   B 1 66  ? -6.415  22.880  -22.796 1.00 36.82 ?  66  PHE   B CA  1 
ATOM   2793 C  C   . PHE   B 1 66  ? -5.238  23.650  -22.221 1.00 42.98 ?  66  PHE   B C   1 
ATOM   2794 O  O   . PHE   B 1 66  ? -4.364  24.103  -22.971 1.00 43.00 ?  66  PHE   B O   1 
ATOM   2795 C  CB  . PHE   B 1 66  ? -5.913  21.559  -23.381 1.00 34.00 ?  66  PHE   B CB  1 
ATOM   2796 C  CG  . PHE   B 1 66  ? -6.985  20.723  -23.997 1.00 36.05 ?  66  PHE   B CG  1 
ATOM   2797 C  CD1 . PHE   B 1 66  ? -7.732  19.855  -23.226 1.00 33.80 ?  66  PHE   B CD1 1 
ATOM   2798 C  CD2 . PHE   B 1 66  ? -7.240  20.797  -25.356 1.00 36.22 ?  66  PHE   B CD2 1 
ATOM   2799 C  CE1 . PHE   B 1 66  ? -8.726  19.082  -23.797 1.00 36.24 ?  66  PHE   B CE1 1 
ATOM   2800 C  CE2 . PHE   B 1 66  ? -8.229  20.026  -25.930 1.00 33.78 ?  66  PHE   B CE2 1 
ATOM   2801 C  CZ  . PHE   B 1 66  ? -8.974  19.169  -25.151 1.00 34.12 ?  66  PHE   B CZ  1 
ATOM   2802 N  N   . LEU   B 1 67  ? -5.219  23.791  -20.899 1.00 33.25 ?  67  LEU   B N   1 
ATOM   2803 C  CA  . LEU   B 1 67  ? -4.095  24.356  -20.166 1.00 39.35 ?  67  LEU   B CA  1 
ATOM   2804 C  C   . LEU   B 1 67  ? -3.416  23.243  -19.383 1.00 38.07 ?  67  LEU   B C   1 
ATOM   2805 O  O   . LEU   B 1 67  ? -4.079  22.499  -18.654 1.00 39.62 ?  67  LEU   B O   1 
ATOM   2806 C  CB  . LEU   B 1 67  ? -4.556  25.463  -19.216 1.00 38.93 ?  67  LEU   B CB  1 
ATOM   2807 C  CG  . LEU   B 1 67  ? -5.437  26.558  -19.813 1.00 39.57 ?  67  LEU   B CG  1 
ATOM   2808 C  CD1 . LEU   B 1 67  ? -5.945  27.446  -18.694 1.00 43.89 ?  67  LEU   B CD1 1 
ATOM   2809 C  CD2 . LEU   B 1 67  ? -4.666  27.370  -20.843 1.00 41.03 ?  67  LEU   B CD2 1 
ATOM   2810 N  N   . VAL   B 1 68  ? -2.102  23.120  -19.545 1.00 39.92 ?  68  VAL   B N   1 
ATOM   2811 C  CA  . VAL   B 1 68  ? -1.301  22.120  -18.849 1.00 41.67 ?  68  VAL   B CA  1 
ATOM   2812 C  C   . VAL   B 1 68  ? -0.220  22.843  -18.059 1.00 42.13 ?  68  VAL   B C   1 
ATOM   2813 O  O   . VAL   B 1 68  ? 0.544   23.634  -18.625 1.00 44.32 ?  68  VAL   B O   1 
ATOM   2814 C  CB  . VAL   B 1 68  ? -0.685  21.109  -19.834 1.00 35.44 ?  68  VAL   B CB  1 
ATOM   2815 C  CG1 . VAL   B 1 68  ? 0.166   20.084  -19.094 1.00 36.61 ?  68  VAL   B CG1 1 
ATOM   2816 C  CG2 . VAL   B 1 68  ? -1.788  20.424  -20.638 1.00 33.08 ?  68  VAL   B CG2 1 
ATOM   2817 N  N   . GLN   B 1 69  ? -0.153  22.573  -16.756 1.00 43.08 ?  69  GLN   B N   1 
ATOM   2818 C  CA  . GLN   B 1 69  ? 0.804   23.221  -15.867 1.00 42.18 ?  69  GLN   B CA  1 
ATOM   2819 C  C   . GLN   B 1 69  ? 1.680   22.176  -15.193 1.00 40.70 ?  69  GLN   B C   1 
ATOM   2820 O  O   . GLN   B 1 69  ? 1.172   21.274  -14.521 1.00 38.38 ?  69  GLN   B O   1 
ATOM   2821 C  CB  . GLN   B 1 69  ? 0.093   24.056  -14.796 1.00 48.34 ?  69  GLN   B CB  1 
ATOM   2822 C  CG  . GLN   B 1 69  ? -0.984  24.994  -15.329 1.00 51.42 ?  69  GLN   B CG  1 
ATOM   2823 C  CD  . GLN   B 1 69  ? -0.486  26.415  -15.506 1.00 55.53 ?  69  GLN   B CD  1 
ATOM   2824 O  OE1 . GLN   B 1 69  ? 0.589   26.773  -15.019 1.00 55.29 ?  69  GLN   B OE1 1 
ATOM   2825 N  NE2 . GLN   B 1 69  ? -1.267  27.234  -16.207 1.00 57.11 ?  69  GLN   B NE2 1 
ATOM   2826 N  N   . ALA   B 1 70  ? 2.989   22.298  -15.374 1.00 43.66 ?  70  ALA   B N   1 
ATOM   2827 C  CA  . ALA   B 1 70  ? 3.973   21.550  -14.602 1.00 45.40 ?  70  ALA   B CA  1 
ATOM   2828 C  C   . ALA   B 1 70  ? 4.728   22.556  -13.748 1.00 49.23 ?  70  ALA   B C   1 
ATOM   2829 O  O   . ALA   B 1 70  ? 5.451   23.399  -14.284 1.00 46.27 ?  70  ALA   B O   1 
ATOM   2830 C  CB  . ALA   B 1 70  ? 4.929   20.779  -15.513 1.00 42.30 ?  70  ALA   B CB  1 
ATOM   2831 N  N   . GLY   B 1 71  ? 4.546   22.488  -12.432 1.00 55.97 ?  71  GLY   B N   1 
ATOM   2832 C  CA  . GLY   B 1 71  ? 5.108   23.531  -11.586 1.00 47.63 ?  71  GLY   B CA  1 
ATOM   2833 C  C   . GLY   B 1 71  ? 4.577   24.884  -12.022 1.00 54.21 ?  71  GLY   B C   1 
ATOM   2834 O  O   . GLY   B 1 71  ? 3.371   25.065  -12.233 1.00 46.49 ?  71  GLY   B O   1 
ATOM   2835 N  N   . ASN   B 1 72  ? 5.485   25.839  -12.216 1.00 51.72 ?  72  ASN   B N   1 
ATOM   2836 C  CA  . ASN   B 1 72  ? 5.102   27.199  -12.573 1.00 53.98 ?  72  ASN   B CA  1 
ATOM   2837 C  C   . ASN   B 1 72  ? 5.115   27.460  -14.077 1.00 55.03 ?  72  ASN   B C   1 
ATOM   2838 O  O   . ASN   B 1 72  ? 4.862   28.595  -14.492 1.00 57.30 ?  72  ASN   B O   1 
ATOM   2839 C  CB  . ASN   B 1 72  ? 6.015   28.207  -11.869 1.00 55.49 ?  72  ASN   B CB  1 
ATOM   2840 N  N   . VAL   B 1 73  ? 5.386   26.452  -14.906 1.00 55.80 ?  73  VAL   B N   1 
ATOM   2841 C  CA  . VAL   B 1 73  ? 5.463   26.638  -16.354 1.00 50.88 ?  73  VAL   B CA  1 
ATOM   2842 C  C   . VAL   B 1 73  ? 4.215   26.053  -17.004 1.00 50.89 ?  73  VAL   B C   1 
ATOM   2843 O  O   . VAL   B 1 73  ? 3.813   24.923  -16.698 1.00 51.44 ?  73  VAL   B O   1 
ATOM   2844 C  CB  . VAL   B 1 73  ? 6.749   26.029  -16.951 1.00 54.92 ?  73  VAL   B CB  1 
ATOM   2845 C  CG1 . VAL   B 1 73  ? 7.039   24.647  -16.400 1.00 53.38 ?  73  VAL   B CG1 1 
ATOM   2846 C  CG2 . VAL   B 1 73  ? 6.653   25.973  -18.465 1.00 49.86 ?  73  VAL   B CG2 1 
ATOM   2847 N  N   . GLN   B 1 74  ? 3.597   26.832  -17.889 1.00 43.95 ?  74  GLN   B N   1 
ATOM   2848 C  CA  . GLN   B 1 74  ? 2.450   26.385  -18.668 1.00 45.08 ?  74  GLN   B CA  1 
ATOM   2849 C  C   . GLN   B 1 74  ? 2.934   25.760  -19.973 1.00 49.05 ?  74  GLN   B C   1 
ATOM   2850 O  O   . GLN   B 1 74  ? 3.588   26.428  -20.779 1.00 51.85 ?  74  GLN   B O   1 
ATOM   2851 C  CB  . GLN   B 1 74  ? 1.508   27.553  -18.953 1.00 51.43 ?  74  GLN   B CB  1 
ATOM   2852 N  N   . LEU   B 1 75  ? 2.616   24.483  -20.179 1.00 46.78 ?  75  LEU   B N   1 
ATOM   2853 C  CA  . LEU   B 1 75  ? 3.043   23.785  -21.384 1.00 40.99 ?  75  LEU   B CA  1 
ATOM   2854 C  C   . LEU   B 1 75  ? 2.096   24.114  -22.527 1.00 43.71 ?  75  LEU   B C   1 
ATOM   2855 O  O   . LEU   B 1 75  ? 0.874   24.074  -22.360 1.00 47.04 ?  75  LEU   B O   1 
ATOM   2856 C  CB  . LEU   B 1 75  ? 3.078   22.274  -21.160 1.00 38.81 ?  75  LEU   B CB  1 
ATOM   2857 C  CG  . LEU   B 1 75  ? 4.011   21.729  -20.082 1.00 41.59 ?  75  LEU   B CG  1 
ATOM   2858 C  CD1 . LEU   B 1 75  ? 3.863   20.218  -19.965 1.00 38.19 ?  75  LEU   B CD1 1 
ATOM   2859 C  CD2 . LEU   B 1 75  ? 5.445   22.105  -20.384 1.00 45.63 ?  75  LEU   B CD2 1 
ATOM   2860 N  N   . ARG   B 1 76  ? 2.662   24.433  -23.691 1.00 45.41 ?  76  ARG   B N   1 
ATOM   2861 C  CA  . ARG   B 1 76  ? 1.859   24.714  -24.871 1.00 45.87 ?  76  ARG   B CA  1 
ATOM   2862 C  C   . ARG   B 1 76  ? 1.393   23.406  -25.499 1.00 38.65 ?  76  ARG   B C   1 
ATOM   2863 O  O   . ARG   B 1 76  ? 2.203   22.511  -25.763 1.00 39.07 ?  76  ARG   B O   1 
ATOM   2864 C  CB  . ARG   B 1 76  ? 2.658   25.536  -25.882 1.00 48.29 ?  76  ARG   B CB  1 
ATOM   2865 N  N   . VAL   B 1 77  ? 0.090   23.295  -25.724 1.00 38.58 ?  77  VAL   B N   1 
ATOM   2866 C  CA  . VAL   B 1 77  ? -0.495  22.114  -26.342 1.00 31.95 ?  77  VAL   B CA  1 
ATOM   2867 C  C   . VAL   B 1 77  ? -0.525  22.319  -27.850 1.00 40.63 ?  77  VAL   B C   1 
ATOM   2868 O  O   . VAL   B 1 77  ? -1.072  23.313  -28.343 1.00 39.31 ?  77  VAL   B O   1 
ATOM   2869 C  CB  . VAL   B 1 77  ? -1.904  21.846  -25.797 1.00 34.27 ?  77  VAL   B CB  1 
ATOM   2870 C  CG1 . VAL   B 1 77  ? -2.451  20.571  -26.401 1.00 36.14 ?  77  VAL   B CG1 1 
ATOM   2871 C  CG2 . VAL   B 1 77  ? -1.887  21.766  -24.263 1.00 33.72 ?  77  VAL   B CG2 1 
ATOM   2872 N  N   . ILE   B 1 78  ? 0.062   21.375  -28.584 1.00 39.56 ?  78  ILE   B N   1 
ATOM   2873 C  CA  . ILE   B 1 78  ? 0.176   21.467  -30.032 1.00 39.13 ?  78  ILE   B CA  1 
ATOM   2874 C  C   . ILE   B 1 78  ? -0.609  20.381  -30.751 1.00 38.54 ?  78  ILE   B C   1 
ATOM   2875 O  O   . ILE   B 1 78  ? -0.532  20.291  -31.980 1.00 42.33 ?  78  ILE   B O   1 
ATOM   2876 C  CB  . ILE   B 1 78  ? 1.653   21.449  -30.475 1.00 37.20 ?  78  ILE   B CB  1 
ATOM   2877 C  CG1 . ILE   B 1 78  ? 2.321   20.139  -30.066 1.00 34.48 ?  78  ILE   B CG1 1 
ATOM   2878 C  CG2 . ILE   B 1 78  ? 2.393   22.629  -29.873 1.00 39.71 ?  78  ILE   B CG2 1 
ATOM   2879 C  CD1 . ILE   B 1 78  ? 3.746   20.010  -30.567 1.00 41.51 ?  78  ILE   B CD1 1 
ATOM   2880 N  N   . GLY   B 1 79  ? -1.366  19.562  -30.029 1.00 37.40 ?  79  GLY   B N   1 
ATOM   2881 C  CA  . GLY   B 1 79  ? -2.193  18.544  -30.656 1.00 35.35 ?  79  GLY   B CA  1 
ATOM   2882 C  C   . GLY   B 1 79  ? -2.962  17.777  -29.600 1.00 37.62 ?  79  GLY   B C   1 
ATOM   2883 O  O   . GLY   B 1 79  ? -2.543  17.679  -28.441 1.00 34.80 ?  79  GLY   B O   1 
ATOM   2884 N  N   . HIS   B 1 80  ? -4.103  17.233  -30.022 1.00 34.73 ?  80  HIS   B N   1 
ATOM   2885 C  CA  . HIS   B 1 80  ? -4.917  16.444  -29.111 1.00 33.88 ?  80  HIS   B CA  1 
ATOM   2886 C  C   . HIS   B 1 80  ? -5.627  15.334  -29.870 1.00 38.67 ?  80  HIS   B C   1 
ATOM   2887 O  O   . HIS   B 1 80  ? -5.994  15.491  -31.038 1.00 39.28 ?  80  HIS   B O   1 
ATOM   2888 C  CB  . HIS   B 1 80  ? -5.935  17.315  -28.355 1.00 34.39 ?  80  HIS   B CB  1 
ATOM   2889 C  CG  . HIS   B 1 80  ? -6.878  18.068  -29.241 1.00 39.15 ?  80  HIS   B CG  1 
ATOM   2890 N  ND1 . HIS   B 1 80  ? -6.657  19.374  -29.626 1.00 41.74 ?  80  HIS   B ND1 1 
ATOM   2891 C  CD2 . HIS   B 1 80  ? -8.060  17.709  -29.794 1.00 39.40 ?  80  HIS   B CD2 1 
ATOM   2892 C  CE1 . HIS   B 1 80  ? -7.655  19.780  -30.391 1.00 38.71 ?  80  HIS   B CE1 1 
ATOM   2893 N  NE2 . HIS   B 1 80  ? -8.518  18.788  -30.511 1.00 43.62 ?  80  HIS   B NE2 1 
ATOM   2894 N  N   . SER   B 1 81  ? -5.816  14.208  -29.183 1.00 34.29 ?  81  SER   B N   1 
ATOM   2895 C  CA  . SER   B 1 81  ? -6.532  13.060  -29.724 1.00 33.64 ?  81  SER   B CA  1 
ATOM   2896 C  C   . SER   B 1 81  ? -6.909  12.146  -28.563 1.00 32.46 ?  81  SER   B C   1 
ATOM   2897 O  O   . SER   B 1 81  ? -6.409  12.291  -27.445 1.00 32.21 ?  81  SER   B O   1 
ATOM   2898 C  CB  . SER   B 1 81  ? -5.689  12.314  -30.762 1.00 29.18 ?  81  SER   B CB  1 
ATOM   2899 O  OG  . SER   B 1 81  ? -4.704  11.525  -30.133 1.00 31.56 ?  81  SER   B OG  1 
ATOM   2900 N  N   . MET   B 1 82  ? -7.801  11.200  -28.842 1.00 29.79 ?  82  MET   B N   1 
ATOM   2901 C  CA  . MET   B 1 82  ? -8.227  10.204  -27.871 1.00 31.19 ?  82  MET   B CA  1 
ATOM   2902 C  C   . MET   B 1 82  ? -7.706  8.831   -28.261 1.00 31.85 ?  82  MET   B C   1 
ATOM   2903 O  O   . MET   B 1 82  ? -7.585  8.511   -29.447 1.00 27.91 ?  82  MET   B O   1 
ATOM   2904 C  CB  . MET   B 1 82  ? -9.752  10.119  -27.781 1.00 28.67 ?  82  MET   B CB  1 
ATOM   2905 C  CG  . MET   B 1 82  ? -10.416 11.136  -26.893 1.00 28.72 ?  82  MET   B CG  1 
ATOM   2906 S  SD  . MET   B 1 82  ? -12.188 10.816  -26.846 1.00 31.54 ?  82  MET   B SD  1 
ATOM   2907 C  CE  . MET   B 1 82  ? -12.726 11.403  -28.460 1.00 36.72 ?  82  MET   B CE  1 
ATOM   2908 N  N   . GLN   B 1 83  ? -7.403  8.025   -27.249 1.00 25.31 ?  83  GLN   B N   1 
ATOM   2909 C  CA  . GLN   B 1 83  ? -7.273  6.577   -27.387 1.00 29.42 ?  83  GLN   B CA  1 
ATOM   2910 C  C   . GLN   B 1 83  ? -8.193  5.966   -26.344 1.00 29.95 ?  83  GLN   B C   1 
ATOM   2911 O  O   . GLN   B 1 83  ? -7.919  6.065   -25.147 1.00 27.17 ?  83  GLN   B O   1 
ATOM   2912 C  CB  . GLN   B 1 83  ? -5.836  6.088   -27.183 1.00 28.58 ?  83  GLN   B CB  1 
ATOM   2913 C  CG  . GLN   B 1 83  ? -5.734  4.555   -27.192 1.00 27.06 ?  83  GLN   B CG  1 
ATOM   2914 C  CD  . GLN   B 1 83  ? -4.314  4.029   -27.070 1.00 37.92 ?  83  GLN   B CD  1 
ATOM   2915 O  OE1 . GLN   B 1 83  ? -3.439  4.684   -26.499 1.00 30.12 ?  83  GLN   B OE1 1 
ATOM   2916 N  NE2 . GLN   B 1 83  ? -4.081  2.828   -27.600 1.00 34.20 ?  83  GLN   B NE2 1 
ATOM   2917 N  N   . ASN   B 1 84  ? -9.293  5.360   -26.787 1.00 26.76 ?  84  ASN   B N   1 
ATOM   2918 C  CA  . ASN   B 1 84  ? -10.299 4.801   -25.878 1.00 26.23 ?  84  ASN   B CA  1 
ATOM   2919 C  C   . ASN   B 1 84  ? -10.670 5.898   -24.877 1.00 25.19 ?  84  ASN   B C   1 
ATOM   2920 O  O   . ASN   B 1 84  ? -10.979 7.024   -25.291 1.00 25.11 ?  84  ASN   B O   1 
ATOM   2921 C  CB  . ASN   B 1 84  ? -9.771  3.505   -25.283 1.00 23.30 ?  84  ASN   B CB  1 
ATOM   2922 C  CG  . ASN   B 1 84  ? -9.451  2.454   -26.338 1.00 32.81 ?  84  ASN   B CG  1 
ATOM   2923 O  OD1 . ASN   B 1 84  ? -10.234 2.225   -27.263 1.00 27.44 ?  84  ASN   B OD1 1 
ATOM   2924 N  ND2 . ASN   B 1 84  ? -8.287  1.815   -26.209 1.00 27.90 ?  84  ASN   B ND2 1 
ATOM   2925 N  N   . CYS   B 1 85  ? -10.622 5.647   -23.572 1.00 25.92 ?  85  CYS   B N   1 
ATOM   2926 C  CA  . CYS   B 1 85  ? -11.077 6.629   -22.600 1.00 26.91 ?  85  CYS   B CA  1 
ATOM   2927 C  C   . CYS   B 1 85  ? -9.966  7.540   -22.082 1.00 32.23 ?  85  CYS   B C   1 
ATOM   2928 O  O   . CYS   B 1 85  ? -10.156 8.190   -21.045 1.00 24.63 ?  85  CYS   B O   1 
ATOM   2929 C  CB  . CYS   B 1 85  ? -11.751 5.925   -21.423 1.00 28.52 ?  85  CYS   B CB  1 
ATOM   2930 S  SG  . CYS   B 1 85  ? -13.152 4.911   -21.910 1.00 26.91 ?  85  CYS   B SG  1 
ATOM   2931 N  N   . VAL   B 1 86  ? -8.823  7.631   -22.763 1.00 25.72 ?  86  VAL   B N   1 
ATOM   2932 C  CA  . VAL   B 1 86  ? -7.788  8.569   -22.343 1.00 26.23 ?  86  VAL   B CA  1 
ATOM   2933 C  C   . VAL   B 1 86  ? -7.584  9.627   -23.412 1.00 27.87 ?  86  VAL   B C   1 
ATOM   2934 O  O   . VAL   B 1 86  ? -7.588  9.338   -24.617 1.00 31.44 ?  86  VAL   B O   1 
ATOM   2935 C  CB  . VAL   B 1 86  ? -6.451  7.883   -21.983 1.00 29.95 ?  86  VAL   B CB  1 
ATOM   2936 C  CG1 . VAL   B 1 86  ? -6.641  7.004   -20.737 1.00 29.76 ?  86  VAL   B CG1 1 
ATOM   2937 C  CG2 . VAL   B 1 86  ? -5.894  7.100   -23.141 1.00 34.41 ?  86  VAL   B CG2 1 
ATOM   2938 N  N   . LEU   B 1 87  ? -7.423  10.861  -22.954 1.00 23.73 ?  87  LEU   B N   1 
ATOM   2939 C  CA  . LEU   B 1 87  ? -7.055  11.980  -23.805 1.00 26.39 ?  87  LEU   B CA  1 
ATOM   2940 C  C   . LEU   B 1 87  ? -5.535  12.094  -23.862 1.00 30.59 ?  87  LEU   B C   1 
ATOM   2941 O  O   . LEU   B 1 87  ? -4.865  12.014  -22.826 1.00 25.81 ?  87  LEU   B O   1 
ATOM   2942 C  CB  . LEU   B 1 87  ? -7.669  13.266  -23.260 1.00 26.68 ?  87  LEU   B CB  1 
ATOM   2943 C  CG  . LEU   B 1 87  ? -7.424  14.535  -24.063 1.00 32.49 ?  87  LEU   B CG  1 
ATOM   2944 C  CD1 . LEU   B 1 87  ? -8.277  14.528  -25.337 1.00 26.80 ?  87  LEU   B CD1 1 
ATOM   2945 C  CD2 . LEU   B 1 87  ? -7.704  15.742  -23.177 1.00 30.30 ?  87  LEU   B CD2 1 
ATOM   2946 N  N   . LYS   B 1 88  ? -4.995  12.252  -25.074 1.00 27.80 ?  88  LYS   B N   1 
ATOM   2947 C  CA  . LYS   B 1 88  ? -3.566  12.441  -25.296 1.00 28.58 ?  88  LYS   B CA  1 
ATOM   2948 C  C   . LYS   B 1 88  ? -3.337  13.865  -25.779 1.00 31.62 ?  88  LYS   B C   1 
ATOM   2949 O  O   . LYS   B 1 88  ? -3.854  14.261  -26.830 1.00 33.19 ?  88  LYS   B O   1 
ATOM   2950 C  CB  . LYS   B 1 88  ? -3.019  11.433  -26.312 1.00 26.34 ?  88  LYS   B CB  1 
ATOM   2951 C  CG  . LYS   B 1 88  ? -3.106  9.990   -25.839 1.00 28.31 ?  88  LYS   B CG  1 
ATOM   2952 C  CD  . LYS   B 1 88  ? -2.400  9.017   -26.777 1.00 31.34 ?  88  LYS   B CD  1 
ATOM   2953 C  CE  . LYS   B 1 88  ? -3.193  8.774   -28.043 1.00 39.38 ?  88  LYS   B CE  1 
ATOM   2954 N  NZ  . LYS   B 1 88  ? -2.472  7.838   -28.959 1.00 38.95 ?  88  LYS   B NZ  1 
ATOM   2955 N  N   . LEU   B 1 89  ? -2.561  14.627  -25.017 1.00 28.71 ?  89  LEU   B N   1 
ATOM   2956 C  CA  . LEU   B 1 89  ? -2.262  16.018  -25.327 1.00 29.33 ?  89  LEU   B CA  1 
ATOM   2957 C  C   . LEU   B 1 89  ? -0.789  16.120  -25.695 1.00 32.26 ?  89  LEU   B C   1 
ATOM   2958 O  O   . LEU   B 1 89  ? 0.087   15.919  -24.844 1.00 32.04 ?  89  LEU   B O   1 
ATOM   2959 C  CB  . LEU   B 1 89  ? -2.594  16.930  -24.150 1.00 32.55 ?  89  LEU   B CB  1 
ATOM   2960 C  CG  . LEU   B 1 89  ? -4.066  17.076  -23.750 1.00 33.13 ?  89  LEU   B CG  1 
ATOM   2961 C  CD1 . LEU   B 1 89  ? -4.188  17.972  -22.527 1.00 30.60 ?  89  LEU   B CD1 1 
ATOM   2962 C  CD2 . LEU   B 1 89  ? -4.888  17.632  -24.903 1.00 29.68 ?  89  LEU   B CD2 1 
ATOM   2963 N  N   . LYS   B 1 90  ? -0.518  16.426  -26.959 1.00 33.01 ?  90  LYS   B N   1 
ATOM   2964 C  CA  . LYS   B 1 90  ? 0.849   16.666  -27.400 1.00 30.38 ?  90  LYS   B CA  1 
ATOM   2965 C  C   . LYS   B 1 90  ? 1.283   18.060  -26.963 1.00 33.90 ?  90  LYS   B C   1 
ATOM   2966 O  O   . LYS   B 1 90  ? 0.573   19.042  -27.201 1.00 38.72 ?  90  LYS   B O   1 
ATOM   2967 C  CB  . LYS   B 1 90  ? 0.955   16.521  -28.921 1.00 32.75 ?  90  LYS   B CB  1 
ATOM   2968 N  N   . VAL   B 1 91  ? 2.441   18.148  -26.309 1.00 34.89 ?  91  VAL   B N   1 
ATOM   2969 C  CA  . VAL   B 1 91  ? 2.983   19.425  -25.870 1.00 35.08 ?  91  VAL   B CA  1 
ATOM   2970 C  C   . VAL   B 1 91  ? 4.317   19.657  -26.569 1.00 35.19 ?  91  VAL   B C   1 
ATOM   2971 O  O   . VAL   B 1 91  ? 4.954   18.724  -27.062 1.00 35.97 ?  91  VAL   B O   1 
ATOM   2972 C  CB  . VAL   B 1 91  ? 3.139   19.490  -24.340 1.00 34.83 ?  91  VAL   B CB  1 
ATOM   2973 C  CG1 . VAL   B 1 91  ? 1.776   19.558  -23.695 1.00 36.21 ?  91  VAL   B CG1 1 
ATOM   2974 C  CG2 . VAL   B 1 91  ? 3.926   18.283  -23.836 1.00 38.80 ?  91  VAL   B CG2 1 
ATOM   2975 N  N   . ASP   B 1 92  ? 4.736   20.924  -26.613 1.00 42.18 ?  92  ASP   B N   1 
ATOM   2976 C  CA  . ASP   B 1 92  ? 5.933   21.299  -27.363 1.00 43.31 ?  92  ASP   B CA  1 
ATOM   2977 C  C   . ASP   B 1 92  ? 7.228   21.084  -26.584 1.00 40.10 ?  92  ASP   B C   1 
ATOM   2978 O  O   . ASP   B 1 92  ? 8.303   21.394  -27.110 1.00 43.61 ?  92  ASP   B O   1 
ATOM   2979 C  CB  . ASP   B 1 92  ? 5.835   22.761  -27.830 1.00 36.79 ?  92  ASP   B CB  1 
ATOM   2980 C  CG  . ASP   B 1 92  ? 5.849   23.771  -26.673 1.00 55.50 ?  92  ASP   B CG  1 
ATOM   2981 O  OD1 . ASP   B 1 92  ? 6.125   23.397  -25.509 1.00 54.21 ?  92  ASP   B OD1 1 
ATOM   2982 O  OD2 . ASP   B 1 92  ? 5.580   24.963  -26.940 1.00 58.01 ?  92  ASP   B OD2 1 
ATOM   2983 N  N   . THR   B 1 93  ? 7.161   20.574  -25.355 1.00 42.34 ?  93  THR   B N   1 
ATOM   2984 C  CA  . THR   B 1 93  ? 8.350   20.276  -24.562 1.00 40.18 ?  93  THR   B CA  1 
ATOM   2985 C  C   . THR   B 1 93  ? 8.287   18.822  -24.124 1.00 38.86 ?  93  THR   B C   1 
ATOM   2986 O  O   . THR   B 1 93  ? 7.255   18.371  -23.620 1.00 37.87 ?  93  THR   B O   1 
ATOM   2987 C  CB  . THR   B 1 93  ? 8.456   21.179  -23.323 1.00 44.44 ?  93  THR   B CB  1 
ATOM   2988 O  OG1 . THR   B 1 93  ? 8.056   22.514  -23.653 1.00 47.04 ?  93  THR   B OG1 1 
ATOM   2989 C  CG2 . THR   B 1 93  ? 9.887   21.201  -22.795 1.00 46.74 ?  93  THR   B CG2 1 
ATOM   2990 N  N   . ALA   B 1 94  ? 9.376   18.086  -24.317 1.00 32.52 ?  94  ALA   B N   1 
ATOM   2991 C  CA  . ALA   B 1 94  ? 9.443   16.734  -23.783 1.00 37.09 ?  94  ALA   B CA  1 
ATOM   2992 C  C   . ALA   B 1 94  ? 9.798   16.785  -22.297 1.00 35.55 ?  94  ALA   B C   1 
ATOM   2993 O  O   . ALA   B 1 94  ? 10.576  17.636  -21.861 1.00 33.79 ?  94  ALA   B O   1 
ATOM   2994 C  CB  . ALA   B 1 94  ? 10.462  15.904  -24.560 1.00 37.21 ?  94  ALA   B CB  1 
ATOM   2995 N  N   . ASN   B 1 95  ? 9.190   15.898  -21.512 1.00 36.90 ?  95  ASN   B N   1 
ATOM   2996 C  CA  . ASN   B 1 95  ? 9.442   15.881  -20.072 1.00 35.43 ?  95  ASN   B CA  1 
ATOM   2997 C  C   . ASN   B 1 95  ? 10.851  15.380  -19.801 1.00 33.80 ?  95  ASN   B C   1 
ATOM   2998 O  O   . ASN   B 1 95  ? 11.132  14.196  -20.038 1.00 31.71 ?  95  ASN   B O   1 
ATOM   2999 C  CB  . ASN   B 1 95  ? 8.422   15.004  -19.342 1.00 32.38 ?  95  ASN   B CB  1 
ATOM   3000 C  CG  . ASN   B 1 95  ? 8.585   15.048  -17.823 1.00 34.41 ?  95  ASN   B CG  1 
ATOM   3001 O  OD1 . ASN   B 1 95  ? 9.557   15.596  -17.299 1.00 33.41 ?  95  ASN   B OD1 1 
ATOM   3002 N  ND2 . ASN   B 1 95  ? 7.632   14.456  -17.112 1.00 30.17 ?  95  ASN   B ND2 1 
ATOM   3003 N  N   . PRO   B 1 96  ? 11.754  16.220  -19.287 1.00 37.03 ?  96  PRO   B N   1 
ATOM   3004 C  CA  . PRO   B 1 96  ? 13.135  15.767  -19.081 1.00 37.71 ?  96  PRO   B CA  1 
ATOM   3005 C  C   . PRO   B 1 96  ? 13.261  14.774  -17.947 1.00 41.37 ?  96  PRO   B C   1 
ATOM   3006 O  O   . PRO   B 1 96  ? 14.272  14.066  -17.871 1.00 38.80 ?  96  PRO   B O   1 
ATOM   3007 C  CB  . PRO   B 1 96  ? 13.882  17.069  -18.774 1.00 40.66 ?  96  PRO   B CB  1 
ATOM   3008 C  CG  . PRO   B 1 96  ? 12.842  17.911  -18.081 1.00 41.98 ?  96  PRO   B CG  1 
ATOM   3009 C  CD  . PRO   B 1 96  ? 11.537  17.585  -18.773 1.00 34.77 ?  96  PRO   B CD  1 
ATOM   3010 N  N   . LYS   B 1 97  ? 12.267  14.694  -17.065 1.00 40.04 ?  97  LYS   B N   1 
ATOM   3011 C  CA  . LYS   B 1 97  ? 12.265  13.715  -15.995 1.00 37.54 ?  97  LYS   B CA  1 
ATOM   3012 C  C   . LYS   B 1 97  ? 11.488  12.459  -16.366 1.00 35.90 ?  97  LYS   B C   1 
ATOM   3013 O  O   . LYS   B 1 97  ? 11.106  11.694  -15.475 1.00 35.14 ?  97  LYS   B O   1 
ATOM   3014 C  CB  . LYS   B 1 97  ? 11.716  14.352  -14.718 1.00 39.28 ?  97  LYS   B CB  1 
ATOM   3015 C  CG  . LYS   B 1 97  ? 12.507  15.596  -14.328 1.00 39.20 ?  97  LYS   B CG  1 
ATOM   3016 C  CD  . LYS   B 1 97  ? 12.341  15.973  -12.870 1.00 47.47 ?  97  LYS   B CD  1 
ATOM   3017 C  CE  . LYS   B 1 97  ? 11.127  16.852  -12.641 1.00 45.64 ?  97  LYS   B CE  1 
ATOM   3018 N  NZ  . LYS   B 1 97  ? 11.204  17.483  -11.290 1.00 47.09 ?  97  LYS   B NZ  1 
ATOM   3019 N  N   . THR   B 1 98  ? 11.255  12.229  -17.658 1.00 34.68 ?  98  THR   B N   1 
ATOM   3020 C  CA  . THR   B 1 98  ? 10.568  11.024  -18.102 1.00 34.32 ?  98  THR   B CA  1 
ATOM   3021 C  C   . THR   B 1 98  ? 11.404  9.794   -17.772 1.00 36.28 ?  98  THR   B C   1 
ATOM   3022 O  O   . THR   B 1 98  ? 12.551  9.693   -18.236 1.00 34.57 ?  98  THR   B O   1 
ATOM   3023 C  CB  . THR   B 1 98  ? 10.299  11.056  -19.605 1.00 32.08 ?  98  THR   B CB  1 
ATOM   3024 O  OG1 . THR   B 1 98  ? 9.578   12.242  -19.948 1.00 33.28 ?  98  THR   B OG1 1 
ATOM   3025 C  CG2 . THR   B 1 98  ? 9.482   9.855   -19.998 1.00 32.08 ?  98  THR   B CG2 1 
ATOM   3026 N  N   . PRO   B 1 99  ? 10.886  8.845   -17.002 1.00 32.25 ?  99  PRO   B N   1 
ATOM   3027 C  CA  . PRO   B 1 99  ? 11.636  7.619   -16.723 1.00 30.75 ?  99  PRO   B CA  1 
ATOM   3028 C  C   . PRO   B 1 99  ? 11.464  6.609   -17.849 1.00 30.68 ?  99  PRO   B C   1 
ATOM   3029 O  O   . PRO   B 1 99  ? 10.615  6.757   -18.729 1.00 30.35 ?  99  PRO   B O   1 
ATOM   3030 C  CB  . PRO   B 1 99  ? 10.994  7.110   -15.430 1.00 34.16 ?  99  PRO   B CB  1 
ATOM   3031 C  CG  . PRO   B 1 99  ? 9.566   7.551   -15.557 1.00 30.01 ?  99  PRO   B CG  1 
ATOM   3032 C  CD  . PRO   B 1 99  ? 9.591   8.870   -16.296 1.00 30.41 ?  99  PRO   B CD  1 
ATOM   3033 N  N   . LYS   B 1 100 ? 12.302  5.572   -17.814 1.00 28.54 ?  100 LYS   B N   1 
ATOM   3034 C  CA  . LYS   B 1 100 ? 12.008  4.372   -18.586 1.00 26.86 ?  100 LYS   B CA  1 
ATOM   3035 C  C   . LYS   B 1 100 ? 10.670  3.814   -18.123 1.00 29.09 ?  100 LYS   B C   1 
ATOM   3036 O  O   . LYS   B 1 100 ? 10.454  3.609   -16.923 1.00 31.95 ?  100 LYS   B O   1 
ATOM   3037 C  CB  . LYS   B 1 100 ? 13.113  3.328   -18.404 1.00 30.56 ?  100 LYS   B CB  1 
ATOM   3038 N  N   . TYR   B 1 101 ? 9.756   3.587   -19.062 1.00 29.08 ?  101 TYR   B N   1 
ATOM   3039 C  CA  . TYR   B 1 101 ? 8.412   3.215   -18.656 1.00 28.80 ?  101 TYR   B CA  1 
ATOM   3040 C  C   . TYR   B 1 101 ? 7.767   2.317   -19.697 1.00 32.90 ?  101 TYR   B C   1 
ATOM   3041 O  O   . TYR   B 1 101 ? 8.167   2.281   -20.862 1.00 25.74 ?  101 TYR   B O   1 
ATOM   3042 C  CB  . TYR   B 1 101 ? 7.532   4.448   -18.427 1.00 26.99 ?  101 TYR   B CB  1 
ATOM   3043 C  CG  . TYR   B 1 101 ? 7.015   5.063   -19.707 1.00 32.24 ?  101 TYR   B CG  1 
ATOM   3044 C  CD1 . TYR   B 1 101 ? 7.757   6.012   -20.391 1.00 29.77 ?  101 TYR   B CD1 1 
ATOM   3045 C  CD2 . TYR   B 1 101 ? 5.772   4.703   -20.228 1.00 31.79 ?  101 TYR   B CD2 1 
ATOM   3046 C  CE1 . TYR   B 1 101 ? 7.289   6.579   -21.560 1.00 28.77 ?  101 TYR   B CE1 1 
ATOM   3047 C  CE2 . TYR   B 1 101 ? 5.302   5.259   -21.395 1.00 29.19 ?  101 TYR   B CE2 1 
ATOM   3048 C  CZ  . TYR   B 1 101 ? 6.062   6.199   -22.054 1.00 29.29 ?  101 TYR   B CZ  1 
ATOM   3049 O  OH  . TYR   B 1 101 ? 5.591   6.763   -23.215 1.00 30.90 ?  101 TYR   B OH  1 
ATOM   3050 N  N   . LYS   B 1 102 ? 6.731   1.615   -19.255 1.00 29.25 ?  102 LYS   B N   1 
ATOM   3051 C  CA  . LYS   B 1 102 ? 5.897   0.804   -20.122 1.00 26.82 ?  102 LYS   B CA  1 
ATOM   3052 C  C   . LYS   B 1 102 ? 4.457   0.955   -19.663 1.00 29.84 ?  102 LYS   B C   1 
ATOM   3053 O  O   . LYS   B 1 102 ? 4.200   1.259   -18.495 1.00 28.78 ?  102 LYS   B O   1 
ATOM   3054 C  CB  . LYS   B 1 102 ? 6.320   -0.670  -20.085 1.00 30.93 ?  102 LYS   B CB  1 
ATOM   3055 N  N   . PHE   B 1 103 ? 3.518   0.755   -20.589 1.00 27.85 ?  103 PHE   B N   1 
ATOM   3056 C  CA  . PHE   B 1 103 ? 2.103   0.626   -20.251 1.00 26.46 ?  103 PHE   B CA  1 
ATOM   3057 C  C   . PHE   B 1 103 ? 1.768   -0.858  -20.186 1.00 26.95 ?  103 PHE   B C   1 
ATOM   3058 O  O   . PHE   B 1 103 ? 1.947   -1.577  -21.172 1.00 26.26 ?  103 PHE   B O   1 
ATOM   3059 C  CB  . PHE   B 1 103 ? 1.205   1.312   -21.283 1.00 26.86 ?  103 PHE   B CB  1 
ATOM   3060 C  CG  . PHE   B 1 103 ? 1.300   2.811   -21.291 1.00 27.51 ?  103 PHE   B CG  1 
ATOM   3061 C  CD1 . PHE   B 1 103 ? 1.929   3.489   -20.258 1.00 25.65 ?  103 PHE   B CD1 1 
ATOM   3062 C  CD2 . PHE   B 1 103 ? 0.749   3.541   -22.338 1.00 27.17 ?  103 PHE   B CD2 1 
ATOM   3063 C  CE1 . PHE   B 1 103 ? 2.008   4.869   -20.269 1.00 27.64 ?  103 PHE   B CE1 1 
ATOM   3064 C  CE2 . PHE   B 1 103 ? 0.825   4.915   -22.358 1.00 26.67 ?  103 PHE   B CE2 1 
ATOM   3065 C  CZ  . PHE   B 1 103 ? 1.454   5.582   -21.317 1.00 26.70 ?  103 PHE   B CZ  1 
ATOM   3066 N  N   . VAL   B 1 104 ? 1.294   -1.326  -19.034 1.00 26.94 ?  104 VAL   B N   1 
ATOM   3067 C  CA  . VAL   B 1 104 ? 0.889   -2.720  -18.926 1.00 23.66 ?  104 VAL   B CA  1 
ATOM   3068 C  C   . VAL   B 1 104 ? -0.523  -2.771  -18.363 1.00 26.64 ?  104 VAL   B C   1 
ATOM   3069 O  O   . VAL   B 1 104 ? -0.945  -1.895  -17.601 1.00 32.47 ?  104 VAL   B O   1 
ATOM   3070 C  CB  . VAL   B 1 104 ? 1.854   -3.566  -18.061 1.00 26.91 ?  104 VAL   B CB  1 
ATOM   3071 C  CG1 . VAL   B 1 104 ? 3.317   -3.409  -18.543 1.00 27.13 ?  104 VAL   B CG1 1 
ATOM   3072 C  CG2 . VAL   B 1 104 ? 1.717   -3.215  -16.601 1.00 34.23 ?  104 VAL   B CG2 1 
ATOM   3073 N  N   . ARG   B 1 105 ? -1.260  -3.802  -18.754 1.00 26.00 ?  105 ARG   B N   1 
ATOM   3074 C  CA  . ARG   B 1 105 ? -2.582  -4.077  -18.207 1.00 25.02 ?  105 ARG   B CA  1 
ATOM   3075 C  C   . ARG   B 1 105 ? -2.472  -5.263  -17.258 1.00 28.93 ?  105 ARG   B C   1 
ATOM   3076 O  O   . ARG   B 1 105 ? -1.951  -6.316  -17.636 1.00 30.74 ?  105 ARG   B O   1 
ATOM   3077 C  CB  . ARG   B 1 105 ? -3.592  -4.366  -19.319 1.00 25.20 ?  105 ARG   B CB  1 
ATOM   3078 C  CG  . ARG   B 1 105 ? -5.005  -4.629  -18.802 1.00 24.07 ?  105 ARG   B CG  1 
ATOM   3079 C  CD  . ARG   B 1 105 ? -5.988  -4.819  -19.946 1.00 28.76 ?  105 ARG   B CD  1 
ATOM   3080 N  NE  . ARG   B 1 105 ? -7.363  -4.984  -19.473 1.00 26.77 ?  105 ARG   B NE  1 
ATOM   3081 C  CZ  . ARG   B 1 105 ? -8.160  -3.973  -19.147 1.00 26.76 ?  105 ARG   B CZ  1 
ATOM   3082 N  NH1 . ARG   B 1 105 ? -7.712  -2.726  -19.233 1.00 26.23 ?  105 ARG   B NH1 1 
ATOM   3083 N  NH2 . ARG   B 1 105 ? -9.403  -4.202  -18.735 1.00 25.69 ?  105 ARG   B NH2 1 
ATOM   3084 N  N   . ILE   B 1 106 ? -2.945  -5.086  -16.029 1.00 27.25 ?  106 ILE   B N   1 
ATOM   3085 C  CA  . ILE   B 1 106 ? -2.804  -6.093  -14.998 1.00 28.66 ?  106 ILE   B CA  1 
ATOM   3086 C  C   . ILE   B 1 106 ? -4.083  -6.917  -14.910 1.00 34.20 ?  106 ILE   B C   1 
ATOM   3087 O  O   . ILE   B 1 106 ? -5.108  -6.580  -15.497 1.00 30.04 ?  106 ILE   B O   1 
ATOM   3088 C  CB  . ILE   B 1 106 ? -2.436  -5.463  -13.631 1.00 28.96 ?  106 ILE   B CB  1 
ATOM   3089 C  CG1 . ILE   B 1 106 ? -3.471  -4.413  -13.222 1.00 26.35 ?  106 ILE   B CG1 1 
ATOM   3090 C  CG2 . ILE   B 1 106 ? -1.039  -4.862  -13.694 1.00 32.45 ?  106 ILE   B CG2 1 
ATOM   3091 C  CD1 . ILE   B 1 106 ? -3.403  -4.012  -11.766 1.00 33.05 ?  106 ILE   B CD1 1 
ATOM   3092 N  N   . GLN   B 1 107 ? -4.016  -8.032  -14.180 1.00 35.14 ?  107 GLN   B N   1 
ATOM   3093 C  CA  . GLN   B 1 107 ? -5.120  -8.939  -13.907 1.00 34.22 ?  107 GLN   B CA  1 
ATOM   3094 C  C   . GLN   B 1 107 ? -5.673  -8.681  -12.515 1.00 33.65 ?  107 GLN   B C   1 
ATOM   3095 O  O   . GLN   B 1 107 ? -4.989  -8.104  -11.666 1.00 27.12 ?  107 GLN   B O   1 
ATOM   3096 C  CB  . GLN   B 1 107 ? -4.645  -10.394 -13.986 1.00 40.44 ?  107 GLN   B CB  1 
ATOM   3097 C  CG  . GLN   B 1 107 ? -3.804  -10.714 -15.200 1.00 41.51 ?  107 GLN   B CG  1 
ATOM   3098 C  CD  . GLN   B 1 107 ? -4.649  -10.802 -16.444 1.00 54.04 ?  107 GLN   B CD  1 
ATOM   3099 O  OE1 . GLN   B 1 107 ? -5.534  -11.655 -16.545 1.00 55.71 ?  107 GLN   B OE1 1 
ATOM   3100 N  NE2 . GLN   B 1 107 ? -4.399  -9.907  -17.398 1.00 57.69 ?  107 GLN   B NE2 1 
ATOM   3101 N  N   . PRO   B 1 108 ? -6.916  -9.083  -12.251 1.00 27.79 ?  108 PRO   B N   1 
ATOM   3102 C  CA  . PRO   B 1 108 ? -7.412  -9.087  -10.869 1.00 30.08 ?  108 PRO   B CA  1 
ATOM   3103 C  C   . PRO   B 1 108 ? -6.543  -9.965  -9.985  1.00 28.29 ?  108 PRO   B C   1 
ATOM   3104 O  O   . PRO   B 1 108 ? -6.131  -11.058 -10.380 1.00 32.61 ?  108 PRO   B O   1 
ATOM   3105 C  CB  . PRO   B 1 108 ? -8.826  -9.661  -11.001 1.00 32.16 ?  108 PRO   B CB  1 
ATOM   3106 C  CG  . PRO   B 1 108 ? -9.229  -9.356  -12.384 1.00 30.96 ?  108 PRO   B CG  1 
ATOM   3107 C  CD  . PRO   B 1 108 ? -7.974  -9.411  -13.222 1.00 28.72 ?  108 PRO   B CD  1 
ATOM   3108 N  N   . GLY   B 1 109 ? -6.268  -9.482  -8.778  1.00 32.00 ?  109 GLY   B N   1 
ATOM   3109 C  CA  . GLY   B 1 109 ? -5.389  -10.162 -7.853  1.00 25.79 ?  109 GLY   B CA  1 
ATOM   3110 C  C   . GLY   B 1 109 ? -3.976  -9.612  -7.808  1.00 35.56 ?  109 GLY   B C   1 
ATOM   3111 O  O   . GLY   B 1 109 ? -3.243  -9.897  -6.848  1.00 32.95 ?  109 GLY   B O   1 
ATOM   3112 N  N   . GLN   B 1 110 ? -3.574  -8.839  -8.815  1.00 28.49 ?  110 GLN   B N   1 
ATOM   3113 C  CA  . GLN   B 1 110 ? -2.257  -8.218  -8.833  1.00 29.81 ?  110 GLN   B CA  1 
ATOM   3114 C  C   . GLN   B 1 110 ? -2.307  -6.866  -8.129  1.00 30.68 ?  110 GLN   B C   1 
ATOM   3115 O  O   . GLN   B 1 110 ? -3.331  -6.179  -8.134  1.00 27.84 ?  110 GLN   B O   1 
ATOM   3116 C  CB  . GLN   B 1 110 ? -1.753  -8.056  -10.271 1.00 31.27 ?  110 GLN   B CB  1 
ATOM   3117 C  CG  . GLN   B 1 110 ? -1.642  -9.383  -11.023 1.00 34.83 ?  110 GLN   B CG  1 
ATOM   3118 C  CD  . GLN   B 1 110 ? -0.956  -9.253  -12.373 1.00 38.22 ?  110 GLN   B CD  1 
ATOM   3119 O  OE1 . GLN   B 1 110 ? -1.437  -8.553  -13.268 1.00 39.53 ?  110 GLN   B OE1 1 
ATOM   3120 N  NE2 . GLN   B 1 110 ? 0.172   -9.935  -12.527 1.00 45.87 ?  110 GLN   B NE2 1 
ATOM   3121 N  N   . THR   B 1 111 ? -1.189  -6.495  -7.509  1.00 27.66 ?  111 THR   B N   1 
ATOM   3122 C  CA  . THR   B 1 111 ? -1.088  -5.276  -6.722  1.00 25.72 ?  111 THR   B CA  1 
ATOM   3123 C  C   . THR   B 1 111 ? -0.287  -4.202  -7.453  1.00 24.85 ?  111 THR   B C   1 
ATOM   3124 O  O   . THR   B 1 111 ? 0.490   -4.481  -8.370  1.00 28.98 ?  111 THR   B O   1 
ATOM   3125 C  CB  . THR   B 1 111 ? -0.423  -5.558  -5.369  1.00 30.09 ?  111 THR   B CB  1 
ATOM   3126 O  OG1 . THR   B 1 111 ? 0.859   -6.151  -5.601  1.00 29.83 ?  111 THR   B OG1 1 
ATOM   3127 C  CG2 . THR   B 1 111 ? -1.275  -6.504  -4.534  1.00 30.15 ?  111 THR   B CG2 1 
ATOM   3128 N  N   . PHE   B 1 112 ? -0.472  -2.960  -7.008  1.00 23.11 ?  112 PHE   B N   1 
ATOM   3129 C  CA  . PHE   B 1 112 ? 0.265   -1.834  -7.560  1.00 25.83 ?  112 PHE   B CA  1 
ATOM   3130 C  C   . PHE   B 1 112 ? 0.188   -0.676  -6.581  1.00 27.08 ?  112 PHE   B C   1 
ATOM   3131 O  O   . PHE   B 1 112 ? -0.672  -0.644  -5.698  1.00 29.66 ?  112 PHE   B O   1 
ATOM   3132 C  CB  . PHE   B 1 112 ? -0.298  -1.414  -8.918  1.00 24.96 ?  112 PHE   B CB  1 
ATOM   3133 C  CG  . PHE   B 1 112 ? -1.760  -1.043  -8.871  1.00 23.96 ?  112 PHE   B CG  1 
ATOM   3134 C  CD1 . PHE   B 1 112 ? -2.737  -2.019  -8.964  1.00 25.62 ?  112 PHE   B CD1 1 
ATOM   3135 C  CD2 . PHE   B 1 112 ? -2.151  0.280   -8.735  1.00 22.91 ?  112 PHE   B CD2 1 
ATOM   3136 C  CE1 . PHE   B 1 112 ? -4.089  -1.680  -8.935  1.00 30.16 ?  112 PHE   B CE1 1 
ATOM   3137 C  CE2 . PHE   B 1 112 ? -3.495  0.627   -8.708  1.00 30.36 ?  112 PHE   B CE2 1 
ATOM   3138 C  CZ  . PHE   B 1 112 ? -4.465  -0.356  -8.804  1.00 28.18 ?  112 PHE   B CZ  1 
ATOM   3139 N  N   . SER   B 1 113 ? 1.091   0.284   -6.757  1.00 23.98 ?  113 SER   B N   1 
ATOM   3140 C  CA  . SER   B 1 113 ? 1.133   1.480   -5.930  1.00 25.31 ?  113 SER   B CA  1 
ATOM   3141 C  C   . SER   B 1 113 ? 0.358   2.601   -6.596  1.00 27.23 ?  113 SER   B C   1 
ATOM   3142 O  O   . SER   B 1 113 ? 0.385   2.749   -7.816  1.00 27.38 ?  113 SER   B O   1 
ATOM   3143 C  CB  . SER   B 1 113 ? 2.571   1.940   -5.673  1.00 29.80 ?  113 SER   B CB  1 
ATOM   3144 O  OG  . SER   B 1 113 ? 3.290   0.966   -4.951  1.00 27.50 ?  113 SER   B OG  1 
ATOM   3145 N  N   . VAL   B 1 114 ? -0.330  3.394   -5.783  1.00 29.10 ?  114 VAL   B N   1 
ATOM   3146 C  CA  . VAL   B 1 114 ? -1.092  4.540   -6.257  1.00 28.04 ?  114 VAL   B CA  1 
ATOM   3147 C  C   . VAL   B 1 114 ? -0.422  5.791   -5.715  1.00 28.33 ?  114 VAL   B C   1 
ATOM   3148 O  O   . VAL   B 1 114 ? -0.128  5.866   -4.518  1.00 27.36 ?  114 VAL   B O   1 
ATOM   3149 C  CB  . VAL   B 1 114 ? -2.562  4.477   -5.800  1.00 27.24 ?  114 VAL   B CB  1 
ATOM   3150 C  CG1 . VAL   B 1 114 ? -3.278  5.756   -6.175  1.00 24.14 ?  114 VAL   B CG1 1 
ATOM   3151 C  CG2 . VAL   B 1 114 ? -3.266  3.267   -6.388  1.00 28.62 ?  114 VAL   B CG2 1 
ATOM   3152 N  N   . LEU   B 1 115 ? -0.187  6.767   -6.584  1.00 26.24 ?  115 LEU   B N   1 
ATOM   3153 C  CA  . LEU   B 1 115 ? 0.255   8.096   -6.171  1.00 26.80 ?  115 LEU   B CA  1 
ATOM   3154 C  C   . LEU   B 1 115 ? -0.948  9.027   -6.290  1.00 27.69 ?  115 LEU   B C   1 
ATOM   3155 O  O   . LEU   B 1 115 ? -1.268  9.507   -7.383  1.00 24.70 ?  115 LEU   B O   1 
ATOM   3156 C  CB  . LEU   B 1 115 ? 1.435   8.576   -7.016  1.00 26.46 ?  115 LEU   B CB  1 
ATOM   3157 C  CG  . LEU   B 1 115 ? 1.920   9.996   -6.704  1.00 22.91 ?  115 LEU   B CG  1 
ATOM   3158 C  CD1 . LEU   B 1 115 ? 2.479   10.071  -5.273  1.00 27.16 ?  115 LEU   B CD1 1 
ATOM   3159 C  CD2 . LEU   B 1 115 ? 2.946   10.469  -7.731  1.00 26.17 ?  115 LEU   B CD2 1 
ATOM   3160 N  N   . ALA   B 1 116 ? -1.617  9.275   -5.163  1.00 26.60 ?  116 ALA   B N   1 
ATOM   3161 C  CA  . ALA   B 1 116 ? -2.798  10.127  -5.168  1.00 27.29 ?  116 ALA   B CA  1 
ATOM   3162 C  C   . ALA   B 1 116 ? -2.399  11.575  -5.418  1.00 30.70 ?  116 ALA   B C   1 
ATOM   3163 O  O   . ALA   B 1 116 ? -1.526  12.115  -4.734  1.00 33.61 ?  116 ALA   B O   1 
ATOM   3164 C  CB  . ALA   B 1 116 ? -3.549  10.001  -3.842  1.00 33.14 ?  116 ALA   B CB  1 
ATOM   3165 N  N   . CYS   B 1 117 ? -3.033  12.211  -6.399  1.00 30.15 ?  117 CYS   B N   1 
ATOM   3166 C  CA  . CYS   B 1 117 ? -2.659  13.563  -6.784  1.00 30.00 ?  117 CYS   B CA  1 
ATOM   3167 C  C   . CYS   B 1 117 ? -3.887  14.446  -6.908  1.00 30.93 ?  117 CYS   B C   1 
ATOM   3168 O  O   . CYS   B 1 117 ? -4.988  13.974  -7.197  1.00 30.42 ?  117 CYS   B O   1 
ATOM   3169 C  CB  . CYS   B 1 117 ? -1.887  13.581  -8.105  1.00 29.03 ?  117 CYS   B CB  1 
ATOM   3170 S  SG  . CYS   B 1 117 ? -0.311  12.737  -8.024  1.00 35.81 ?  117 CYS   B SG  1 
ATOM   3171 N  N   . TYR   B 1 118 ? -3.674  15.742  -6.694  1.00 32.44 ?  118 TYR   B N   1 
ATOM   3172 C  CA  . TYR   B 1 118 ? -4.708  16.756  -6.836  1.00 30.92 ?  118 TYR   B CA  1 
ATOM   3173 C  C   . TYR   B 1 118 ? -4.081  17.985  -7.467  1.00 28.72 ?  118 TYR   B C   1 
ATOM   3174 O  O   . TYR   B 1 118 ? -3.033  18.448  -7.012  1.00 34.48 ?  118 TYR   B O   1 
ATOM   3175 C  CB  . TYR   B 1 118 ? -5.338  17.096  -5.474  1.00 34.94 ?  118 TYR   B CB  1 
ATOM   3176 C  CG  . TYR   B 1 118 ? -6.043  15.905  -4.880  1.00 29.58 ?  118 TYR   B CG  1 
ATOM   3177 C  CD1 . TYR   B 1 118 ? -7.335  15.591  -5.263  1.00 31.74 ?  118 TYR   B CD1 1 
ATOM   3178 C  CD2 . TYR   B 1 118 ? -5.398  15.062  -3.975  1.00 31.20 ?  118 TYR   B CD2 1 
ATOM   3179 C  CE1 . TYR   B 1 118 ? -7.980  14.494  -4.757  1.00 32.73 ?  118 TYR   B CE1 1 
ATOM   3180 C  CE2 . TYR   B 1 118 ? -6.041  13.953  -3.462  1.00 31.43 ?  118 TYR   B CE2 1 
ATOM   3181 C  CZ  . TYR   B 1 118 ? -7.334  13.679  -3.858  1.00 30.39 ?  118 TYR   B CZ  1 
ATOM   3182 O  OH  . TYR   B 1 118 ? -7.997  12.584  -3.370  1.00 31.19 ?  118 TYR   B OH  1 
ATOM   3183 N  N   . ASN   B 1 119 ? -4.707  18.491  -8.528  1.00 35.70 ?  119 ASN   B N   1 
ATOM   3184 C  CA  . ASN   B 1 119 ? -4.178  19.628  -9.281  1.00 36.74 ?  119 ASN   B CA  1 
ATOM   3185 C  C   . ASN   B 1 119 ? -2.713  19.409  -9.660  1.00 32.73 ?  119 ASN   B C   1 
ATOM   3186 O  O   . ASN   B 1 119 ? -1.882  20.316  -9.586  1.00 35.45 ?  119 ASN   B O   1 
ATOM   3187 C  CB  . ASN   B 1 119 ? -4.363  20.928  -8.498  1.00 39.86 ?  119 ASN   B CB  1 
ATOM   3188 C  CG  . ASN   B 1 119 ? -5.818  21.197  -8.161  1.00 44.13 ?  119 ASN   B CG  1 
ATOM   3189 O  OD1 . ASN   B 1 119 ? -6.607  21.571  -9.025  1.00 45.01 ?  119 ASN   B OD1 1 
ATOM   3190 N  ND2 . ASN   B 1 119 ? -6.181  21.007  -6.896  1.00 48.57 ?  119 ASN   B ND2 1 
ATOM   3191 N  N   . GLY   B 1 120 ? -2.389  18.180  -10.055 1.00 31.81 ?  120 GLY   B N   1 
ATOM   3192 C  CA  . GLY   B 1 120 ? -1.049  17.859  -10.498 1.00 28.91 ?  120 GLY   B CA  1 
ATOM   3193 C  C   . GLY   B 1 120 ? -0.014  17.732  -9.407  1.00 35.32 ?  120 GLY   B C   1 
ATOM   3194 O  O   . GLY   B 1 120 ? 1.176   17.599  -9.720  1.00 31.21 ?  120 GLY   B O   1 
ATOM   3195 N  N   . SER   B 1 121 ? -0.421  17.756  -8.137  1.00 34.25 ?  121 SER   B N   1 
ATOM   3196 C  CA  . SER   B 1 121 ? 0.514   17.729  -7.024  1.00 36.89 ?  121 SER   B CA  1 
ATOM   3197 C  C   . SER   B 1 121 ? 0.284   16.492  -6.166  1.00 36.46 ?  121 SER   B C   1 
ATOM   3198 O  O   . SER   B 1 121 ? -0.867  16.179  -5.830  1.00 34.53 ?  121 SER   B O   1 
ATOM   3199 C  CB  . SER   B 1 121 ? 0.378   18.994  -6.162  1.00 38.12 ?  121 SER   B CB  1 
ATOM   3200 O  OG  . SER   B 1 121 ? 0.777   20.141  -6.890  1.00 41.15 ?  121 SER   B OG  1 
ATOM   3201 N  N   . PRO   B 1 122 ? 1.338   15.770  -5.795  1.00 38.05 ?  122 PRO   B N   1 
ATOM   3202 C  CA  . PRO   B 1 122 ? 1.152   14.523  -5.044  1.00 40.15 ?  122 PRO   B CA  1 
ATOM   3203 C  C   . PRO   B 1 122 ? 0.734   14.777  -3.606  1.00 38.93 ?  122 PRO   B C   1 
ATOM   3204 O  O   . PRO   B 1 122 ? 1.244   15.678  -2.935  1.00 41.66 ?  122 PRO   B O   1 
ATOM   3205 C  CB  . PRO   B 1 122 ? 2.532   13.861  -5.112  1.00 38.60 ?  122 PRO   B CB  1 
ATOM   3206 C  CG  . PRO   B 1 122 ? 3.479   14.997  -5.327  1.00 43.79 ?  122 PRO   B CG  1 
ATOM   3207 C  CD  . PRO   B 1 122 ? 2.736   15.966  -6.206  1.00 41.26 ?  122 PRO   B CD  1 
ATOM   3208 N  N   . SER   B 1 123 ? -0.207  13.963  -3.136  1.00 35.96 ?  123 SER   B N   1 
ATOM   3209 C  CA  . SER   B 1 123 ? -0.634  13.994  -1.747  1.00 40.75 ?  123 SER   B CA  1 
ATOM   3210 C  C   . SER   B 1 123 ? -0.139  12.805  -0.937  1.00 38.55 ?  123 SER   B C   1 
ATOM   3211 O  O   . SER   B 1 123 ? 0.118   12.957  0.257   1.00 43.38 ?  123 SER   B O   1 
ATOM   3212 C  CB  . SER   B 1 123 ? -2.164  14.061  -1.661  1.00 41.15 ?  123 SER   B CB  1 
ATOM   3213 O  OG  . SER   B 1 123 ? -2.748  12.776  -1.736  1.00 50.44 ?  123 SER   B OG  1 
ATOM   3214 N  N   . GLY   B 1 124 ? 0.012   11.638  -1.552  1.00 33.84 ?  124 GLY   B N   1 
ATOM   3215 C  CA  . GLY   B 1 124 ? 0.466   10.465  -0.828  1.00 31.56 ?  124 GLY   B CA  1 
ATOM   3216 C  C   . GLY   B 1 124 ? 0.513   9.256   -1.736  1.00 31.03 ?  124 GLY   B C   1 
ATOM   3217 O  O   . GLY   B 1 124 ? -0.010  9.263   -2.856  1.00 31.96 ?  124 GLY   B O   1 
ATOM   3218 N  N   . VAL   B 1 125 ? 1.143   8.202   -1.226  1.00 27.21 ?  125 VAL   B N   1 
ATOM   3219 C  CA  . VAL   B 1 125 ? 1.314   6.954   -1.958  1.00 26.85 ?  125 VAL   B CA  1 
ATOM   3220 C  C   . VAL   B 1 125 ? 0.788   5.806   -1.102  1.00 26.19 ?  125 VAL   B C   1 
ATOM   3221 O  O   . VAL   B 1 125 ? 0.949   5.807   0.125   1.00 29.55 ?  125 VAL   B O   1 
ATOM   3222 C  CB  . VAL   B 1 125 ? 2.797   6.746   -2.369  1.00 29.76 ?  125 VAL   B CB  1 
ATOM   3223 C  CG1 . VAL   B 1 125 ? 3.701   6.713   -1.167  1.00 30.81 ?  125 VAL   B CG1 1 
ATOM   3224 C  CG2 . VAL   B 1 125 ? 2.971   5.480   -3.188  1.00 31.09 ?  125 VAL   B CG2 1 
ATOM   3225 N  N   . TYR   B 1 126 ? 0.109   4.850   -1.737  1.00 26.10 ?  126 TYR   B N   1 
ATOM   3226 C  CA  . TYR   B 1 126 ? -0.355  3.672   -1.015  1.00 24.70 ?  126 TYR   B CA  1 
ATOM   3227 C  C   . TYR   B 1 126 ? -0.426  2.480   -1.959  1.00 27.59 ?  126 TYR   B C   1 
ATOM   3228 O  O   . TYR   B 1 126 ? -0.408  2.626   -3.185  1.00 25.88 ?  126 TYR   B O   1 
ATOM   3229 C  CB  . TYR   B 1 126 ? -1.714  3.916   -0.332  1.00 25.97 ?  126 TYR   B CB  1 
ATOM   3230 C  CG  . TYR   B 1 126 ? -2.847  4.380   -1.232  1.00 28.43 ?  126 TYR   B CG  1 
ATOM   3231 C  CD1 . TYR   B 1 126 ? -3.596  3.473   -1.963  1.00 24.13 ?  126 TYR   B CD1 1 
ATOM   3232 C  CD2 . TYR   B 1 126 ? -3.189  5.721   -1.309  1.00 26.93 ?  126 TYR   B CD2 1 
ATOM   3233 C  CE1 . TYR   B 1 126 ? -4.639  3.892   -2.754  1.00 24.57 ?  126 TYR   B CE1 1 
ATOM   3234 C  CE2 . TYR   B 1 126 ? -4.224  6.151   -2.099  1.00 31.64 ?  126 TYR   B CE2 1 
ATOM   3235 C  CZ  . TYR   B 1 126 ? -4.951  5.235   -2.820  1.00 29.23 ?  126 TYR   B CZ  1 
ATOM   3236 O  OH  . TYR   B 1 126 ? -5.991  5.671   -3.616  1.00 35.47 ?  126 TYR   B OH  1 
ATOM   3237 N  N   . GLN   B 1 127 ? -0.505  1.294   -1.363  1.00 26.04 ?  127 GLN   B N   1 
ATOM   3238 C  CA  . GLN   B 1 127 ? -0.470  0.030   -2.089  1.00 28.40 ?  127 GLN   B CA  1 
ATOM   3239 C  C   . GLN   B 1 127 ? -1.887  -0.528  -2.208  1.00 35.62 ?  127 GLN   B C   1 
ATOM   3240 O  O   . GLN   B 1 127 ? -2.621  -0.580  -1.213  1.00 35.48 ?  127 GLN   B O   1 
ATOM   3241 C  CB  . GLN   B 1 127 ? 0.459   -0.960  -1.373  1.00 33.63 ?  127 GLN   B CB  1 
ATOM   3242 C  CG  . GLN   B 1 127 ? 0.777   -2.247  -2.128  1.00 30.89 ?  127 GLN   B CG  1 
ATOM   3243 C  CD  . GLN   B 1 127 ? 1.687   -2.031  -3.312  1.00 28.43 ?  127 GLN   B CD  1 
ATOM   3244 O  OE1 . GLN   B 1 127 ? 2.073   -0.902  -3.622  1.00 30.84 ?  127 GLN   B OE1 1 
ATOM   3245 N  NE2 . GLN   B 1 127 ? 2.051   -3.122  -3.983  1.00 30.02 ?  127 GLN   B NE2 1 
ATOM   3246 N  N   . CYS   B 1 128 ? -2.262  -0.930  -3.434  1.00 32.61 ?  128 CYS   B N   1 
ATOM   3247 C  CA  . CYS   B 1 128 ? -3.602  -1.374  -3.808  1.00 37.46 ?  128 CYS   B CA  1 
ATOM   3248 C  C   . CYS   B 1 128 ? -3.533  -2.754  -4.441  1.00 37.14 ?  128 CYS   B C   1 
ATOM   3249 O  O   . CYS   B 1 128 ? -2.513  -3.134  -5.014  1.00 30.76 ?  128 CYS   B O   1 
ATOM   3250 C  CB  . CYS   B 1 128 ? -4.255  -0.423  -4.847  1.00 28.56 ?  128 CYS   B CB  1 
ATOM   3251 S  SG  . CYS   B 1 128 ? -5.348  0.800   -4.144  1.00 58.59 ?  128 CYS   B SG  1 
ATOM   3252 N  N   . ALA   B 1 129 ? -4.639  -3.486  -4.381  1.00 33.07 ?  129 ALA   B N   1 
ATOM   3253 C  CA  . ALA   B 1 129 ? -4.809  -4.682  -5.195  1.00 27.85 ?  129 ALA   B CA  1 
ATOM   3254 C  C   . ALA   B 1 129 ? -6.024  -4.494  -6.088  1.00 31.07 ?  129 ALA   B C   1 
ATOM   3255 O  O   . ALA   B 1 129 ? -7.030  -3.933  -5.654  1.00 34.40 ?  129 ALA   B O   1 
ATOM   3256 C  CB  . ALA   B 1 129 ? -4.983  -5.930  -4.333  1.00 30.22 ?  129 ALA   B CB  1 
ATOM   3257 N  N   . MET   B 1 130 ? -5.928  -4.944  -7.340  1.00 26.39 ?  130 MET   B N   1 
ATOM   3258 C  CA  . MET   B 1 130 ? -7.107  -4.997  -8.198  1.00 28.14 ?  130 MET   B CA  1 
ATOM   3259 C  C   . MET   B 1 130 ? -8.050  -6.083  -7.695  1.00 29.95 ?  130 MET   B C   1 
ATOM   3260 O  O   . MET   B 1 130 ? -7.670  -7.258  -7.636  1.00 29.29 ?  130 MET   B O   1 
ATOM   3261 C  CB  . MET   B 1 130 ? -6.701  -5.274  -9.642  1.00 29.78 ?  130 MET   B CB  1 
ATOM   3262 C  CG  . MET   B 1 130 ? -7.869  -5.580  -10.565 1.00 36.86 ?  130 MET   B CG  1 
ATOM   3263 S  SD  . MET   B 1 130 ? -8.623  -4.061  -11.144 1.00 43.07 ?  130 MET   B SD  1 
ATOM   3264 C  CE  . MET   B 1 130 ? -7.265  -3.339  -12.037 1.00 26.36 ?  130 MET   B CE  1 
ATOM   3265 N  N   . ARG   B 1 131 ? -9.279  -5.703  -7.336  1.00 30.20 ?  131 ARG   B N   1 
ATOM   3266 C  CA  . ARG   B 1 131 ? -10.220 -6.677  -6.815  1.00 28.11 ?  131 ARG   B CA  1 
ATOM   3267 C  C   . ARG   B 1 131 ? -10.689 -7.597  -7.938  1.00 30.88 ?  131 ARG   B C   1 
ATOM   3268 O  O   . ARG   B 1 131 ? -10.639 -7.229  -9.113  1.00 30.33 ?  131 ARG   B O   1 
ATOM   3269 C  CB  . ARG   B 1 131 ? -11.426 -5.989  -6.175  1.00 27.33 ?  131 ARG   B CB  1 
ATOM   3270 C  CG  . ARG   B 1 131 ? -11.119 -4.959  -5.081  1.00 30.99 ?  131 ARG   B CG  1 
ATOM   3271 C  CD  . ARG   B 1 131 ? -10.358 -5.549  -3.902  1.00 33.26 ?  131 ARG   B CD  1 
ATOM   3272 N  NE  . ARG   B 1 131 ? -10.815 -6.892  -3.565  1.00 32.49 ?  131 ARG   B NE  1 
ATOM   3273 C  CZ  . ARG   B 1 131 ? -10.142 -7.737  -2.789  1.00 36.95 ?  131 ARG   B CZ  1 
ATOM   3274 N  NH1 . ARG   B 1 131 ? -8.975  -7.381  -2.259  1.00 34.58 ?  131 ARG   B NH1 1 
ATOM   3275 N  NH2 . ARG   B 1 131 ? -10.631 -8.946  -2.550  1.00 30.07 ?  131 ARG   B NH2 1 
ATOM   3276 N  N   . PRO   B 1 132 ? -11.145 -8.806  -7.602  1.00 30.40 ?  132 PRO   B N   1 
ATOM   3277 C  CA  . PRO   B 1 132 ? -11.708 -9.682  -8.642  1.00 30.09 ?  132 PRO   B CA  1 
ATOM   3278 C  C   . PRO   B 1 132 ? -12.901 -9.079  -9.373  1.00 31.49 ?  132 PRO   B C   1 
ATOM   3279 O  O   . PRO   B 1 132 ? -13.172 -9.476  -10.517 1.00 28.70 ?  132 PRO   B O   1 
ATOM   3280 C  CB  . PRO   B 1 132 ? -12.097 -10.945 -7.864  1.00 29.74 ?  132 PRO   B CB  1 
ATOM   3281 C  CG  . PRO   B 1 132 ? -11.151 -10.961 -6.700  1.00 33.32 ?  132 PRO   B CG  1 
ATOM   3282 C  CD  . PRO   B 1 132 ? -10.968 -9.512  -6.317  1.00 31.88 ?  132 PRO   B CD  1 
ATOM   3283 N  N   . ASN   B 1 133 ? -13.619 -8.130  -8.774  1.00 28.60 ?  133 ASN   B N   1 
ATOM   3284 C  CA  . ASN   B 1 133 ? -14.683 -7.438  -9.493  1.00 29.47 ?  133 ASN   B CA  1 
ATOM   3285 C  C   . ASN   B 1 133 ? -14.172 -6.199  -10.224 1.00 28.62 ?  133 ASN   B C   1 
ATOM   3286 O  O   . ASN   B 1 133 ? -14.969 -5.343  -10.622 1.00 29.71 ?  133 ASN   B O   1 
ATOM   3287 C  CB  . ASN   B 1 133 ? -15.836 -7.086  -8.543  1.00 30.15 ?  133 ASN   B CB  1 
ATOM   3288 C  CG  . ASN   B 1 133 ? -15.470 -6.035  -7.515  1.00 33.78 ?  133 ASN   B CG  1 
ATOM   3289 O  OD1 . ASN   B 1 133 ? -14.353 -5.509  -7.493  1.00 30.65 ?  133 ASN   B OD1 1 
ATOM   3290 N  ND2 . ASN   B 1 133 ? -16.428 -5.710  -6.658  1.00 31.93 ?  133 ASN   B ND2 1 
ATOM   3291 N  N   . PHE   B 1 134 ? -12.854 -6.081  -10.375 1.00 29.72 ?  134 PHE   B N   1 
ATOM   3292 C  CA  . PHE   B 1 134 ? -12.151 -5.053  -11.138 1.00 29.69 ?  134 PHE   B CA  1 
ATOM   3293 C  C   . PHE   B 1 134 ? -12.236 -3.656  -10.541 1.00 29.26 ?  134 PHE   B C   1 
ATOM   3294 O  O   . PHE   B 1 134 ? -11.835 -2.692  -11.202 1.00 35.94 ?  134 PHE   B O   1 
ATOM   3295 C  CB  . PHE   B 1 134 ? -12.634 -4.997  -12.585 1.00 23.86 ?  134 PHE   B CB  1 
ATOM   3296 C  CG  . PHE   B 1 134 ? -12.236 -6.181  -13.395 1.00 28.91 ?  134 PHE   B CG  1 
ATOM   3297 C  CD1 . PHE   B 1 134 ? -10.968 -6.255  -13.951 1.00 30.30 ?  134 PHE   B CD1 1 
ATOM   3298 C  CD2 . PHE   B 1 134 ? -13.126 -7.222  -13.615 1.00 33.11 ?  134 PHE   B CD2 1 
ATOM   3299 C  CE1 . PHE   B 1 134 ? -10.593 -7.340  -14.711 1.00 32.46 ?  134 PHE   B CE1 1 
ATOM   3300 C  CE2 . PHE   B 1 134 ? -12.750 -8.317  -14.384 1.00 31.14 ?  134 PHE   B CE2 1 
ATOM   3301 C  CZ  . PHE   B 1 134 ? -11.484 -8.373  -14.926 1.00 31.84 ?  134 PHE   B CZ  1 
ATOM   3302 N  N   . THR   B 1 135 ? -12.744 -3.504  -9.329  1.00 27.12 ?  135 THR   B N   1 
ATOM   3303 C  CA  . THR   B 1 135 ? -12.598 -2.231  -8.645  1.00 25.20 ?  135 THR   B CA  1 
ATOM   3304 C  C   . THR   B 1 135 ? -11.305 -2.239  -7.828  1.00 24.60 ?  135 THR   B C   1 
ATOM   3305 O  O   . THR   B 1 135 ? -10.650 -3.271  -7.659  1.00 22.92 ?  135 THR   B O   1 
ATOM   3306 C  CB  . THR   B 1 135 ? -13.799 -1.960  -7.742  1.00 27.74 ?  135 THR   B CB  1 
ATOM   3307 O  OG1 . THR   B 1 135 ? -13.783 -2.887  -6.651  1.00 24.32 ?  135 THR   B OG1 1 
ATOM   3308 C  CG2 . THR   B 1 135 ? -15.114 -2.127  -8.509  1.00 24.61 ?  135 THR   B CG2 1 
ATOM   3309 N  N   . ILE   B 1 136 ? -10.925 -1.068  -7.333  1.00 23.33 ?  136 ILE   B N   1 
ATOM   3310 C  CA  . ILE   B 1 136 ? -9.867  -0.961  -6.337  1.00 24.75 ?  136 ILE   B CA  1 
ATOM   3311 C  C   . ILE   B 1 136 ? -10.439 -0.204  -5.147  1.00 28.65 ?  136 ILE   B C   1 
ATOM   3312 O  O   . ILE   B 1 136 ? -11.250 0.718   -5.309  1.00 26.58 ?  136 ILE   B O   1 
ATOM   3313 C  CB  . ILE   B 1 136 ? -8.580  -0.284  -6.871  1.00 28.70 ?  136 ILE   B CB  1 
ATOM   3314 C  CG1 . ILE   B 1 136 ? -8.641  1.239   -6.747  1.00 29.88 ?  136 ILE   B CG1 1 
ATOM   3315 C  CG2 . ILE   B 1 136 ? -8.285  -0.693  -8.325  1.00 29.71 ?  136 ILE   B CG2 1 
ATOM   3316 C  CD1 . ILE   B 1 136 ? -7.410  1.938   -7.290  1.00 31.44 ?  136 ILE   B CD1 1 
ATOM   3317 N  N   . LYS   B 1 137 ? -10.060 -0.633  -3.947  1.00 30.69 ?  137 LYS   B N   1 
ATOM   3318 C  CA  . LYS   B 1 137 ? -10.497 0.038   -2.725  1.00 30.48 ?  137 LYS   B CA  1 
ATOM   3319 C  C   . LYS   B 1 137 ? -9.486  1.134   -2.416  1.00 34.85 ?  137 LYS   B C   1 
ATOM   3320 O  O   . LYS   B 1 137 ? -8.609  0.995   -1.564  1.00 34.94 ?  137 LYS   B O   1 
ATOM   3321 C  CB  . LYS   B 1 137 ? -10.626 -0.958  -1.581  1.00 31.73 ?  137 LYS   B CB  1 
ATOM   3322 C  CG  . LYS   B 1 137 ? -11.795 -1.909  -1.721  1.00 37.79 ?  137 LYS   B CG  1 
ATOM   3323 C  CD  . LYS   B 1 137 ? -11.849 -2.883  -0.556  1.00 38.08 ?  137 LYS   B CD  1 
ATOM   3324 C  CE  . LYS   B 1 137 ? -12.968 -3.891  -0.739  1.00 45.41 ?  137 LYS   B CE  1 
ATOM   3325 N  NZ  . LYS   B 1 137 ? -12.784 -5.071  0.152   1.00 51.74 ?  137 LYS   B NZ  1 
ATOM   3326 N  N   . GLY   B 1 138 ? -9.610  2.246   -3.137  1.00 31.48 ?  138 GLY   B N   1 
ATOM   3327 C  CA  . GLY   B 1 138 ? -8.660  3.333   -3.040  1.00 31.85 ?  138 GLY   B CA  1 
ATOM   3328 C  C   . GLY   B 1 138 ? -9.054  4.370   -2.006  1.00 30.73 ?  138 GLY   B C   1 
ATOM   3329 O  O   . GLY   B 1 138 ? -9.966  4.186   -1.200  1.00 26.12 ?  138 GLY   B O   1 
ATOM   3330 N  N   . SER   B 1 139 ? -8.335  5.486   -2.040  1.00 27.57 ?  139 SER   B N   1 
ATOM   3331 C  CA  . SER   B 1 139 ? -8.652  6.658   -1.231  1.00 25.58 ?  139 SER   B CA  1 
ATOM   3332 C  C   . SER   B 1 139 ? -8.522  7.853   -2.163  1.00 29.86 ?  139 SER   B C   1 
ATOM   3333 O  O   . SER   B 1 139 ? -7.403  8.262   -2.505  1.00 28.98 ?  139 SER   B O   1 
ATOM   3334 C  CB  . SER   B 1 139 ? -7.719  6.780   -0.021  1.00 27.20 ?  139 SER   B CB  1 
ATOM   3335 O  OG  . SER   B 1 139 ? -8.048  7.908   0.768   1.00 32.19 ?  139 SER   B OG  1 
ATOM   3336 N  N   . PHE   B 1 140 ? -9.665  8.384   -2.593  1.00 25.94 ?  140 PHE   B N   1 
ATOM   3337 C  CA  . PHE   B 1 140 ? -9.724  9.369   -3.664  1.00 27.62 ?  140 PHE   B CA  1 
ATOM   3338 C  C   . PHE   B 1 140 ? -10.833 10.373  -3.382  1.00 28.09 ?  140 PHE   B C   1 
ATOM   3339 O  O   . PHE   B 1 140 ? -11.953 9.982   -3.038  1.00 27.81 ?  140 PHE   B O   1 
ATOM   3340 C  CB  . PHE   B 1 140 ? -9.988  8.692   -5.019  1.00 27.90 ?  140 PHE   B CB  1 
ATOM   3341 C  CG  . PHE   B 1 140 ? -8.817  7.931   -5.583  1.00 25.79 ?  140 PHE   B CG  1 
ATOM   3342 C  CD1 . PHE   B 1 140 ? -7.627  8.570   -5.866  1.00 26.27 ?  140 PHE   B CD1 1 
ATOM   3343 C  CD2 . PHE   B 1 140 ? -8.939  6.585   -5.894  1.00 26.07 ?  140 PHE   B CD2 1 
ATOM   3344 C  CE1 . PHE   B 1 140 ? -6.557  7.873   -6.435  1.00 28.78 ?  140 PHE   B CE1 1 
ATOM   3345 C  CE2 . PHE   B 1 140 ? -7.885  5.883   -6.453  1.00 27.70 ?  140 PHE   B CE2 1 
ATOM   3346 C  CZ  . PHE   B 1 140 ? -6.691  6.526   -6.728  1.00 25.17 ?  140 PHE   B CZ  1 
ATOM   3347 N  N   . LEU   B 1 141 ? -10.533 11.654  -3.565  1.00 29.61 ?  141 LEU   B N   1 
ATOM   3348 C  CA  . LEU   B 1 141 ? -11.489 12.735  -3.379  1.00 33.09 ?  141 LEU   B CA  1 
ATOM   3349 C  C   . LEU   B 1 141 ? -11.766 13.400  -4.726  1.00 35.03 ?  141 LEU   B C   1 
ATOM   3350 O  O   . LEU   B 1 141 ? -11.291 12.947  -5.771  1.00 28.81 ?  141 LEU   B O   1 
ATOM   3351 C  CB  . LEU   B 1 141 ? -10.955 13.739  -2.350  1.00 28.53 ?  141 LEU   B CB  1 
ATOM   3352 C  CG  . LEU   B 1 141 ? -10.631 13.190  -0.957  1.00 33.04 ?  141 LEU   B CG  1 
ATOM   3353 C  CD1 . LEU   B 1 141 ? -9.814  14.186  -0.130  1.00 32.03 ?  141 LEU   B CD1 1 
ATOM   3354 C  CD2 . LEU   B 1 141 ? -11.902 12.802  -0.218  1.00 29.41 ?  141 LEU   B CD2 1 
ATOM   3355 N  N   . ASN   B 1 142 ? -12.536 14.487  -4.700  1.00 33.10 ?  142 ASN   B N   1 
ATOM   3356 C  CA  . ASN   B 1 142 ? -12.724 15.282  -5.908  1.00 37.17 ?  142 ASN   B CA  1 
ATOM   3357 C  C   . ASN   B 1 142 ? -11.393 15.877  -6.355  1.00 34.94 ?  142 ASN   B C   1 
ATOM   3358 O  O   . ASN   B 1 142 ? -10.663 16.466  -5.556  1.00 34.32 ?  142 ASN   B O   1 
ATOM   3359 C  CB  . ASN   B 1 142 ? -13.751 16.394  -5.667  1.00 38.16 ?  142 ASN   B CB  1 
ATOM   3360 C  CG  . ASN   B 1 142 ? -13.930 17.297  -6.887  1.00 41.86 ?  142 ASN   B CG  1 
ATOM   3361 O  OD1 . ASN   B 1 142 ? -13.242 18.311  -7.031  1.00 48.62 ?  142 ASN   B OD1 1 
ATOM   3362 N  ND2 . ASN   B 1 142 ? -14.846 16.923  -7.776  1.00 44.34 ?  142 ASN   B ND2 1 
ATOM   3363 N  N   . GLY   B 1 143 ? -11.071 15.717  -7.637  1.00 32.23 ?  143 GLY   B N   1 
ATOM   3364 C  CA  . GLY   B 1 143 ? -9.812  16.197  -8.165  1.00 29.16 ?  143 GLY   B CA  1 
ATOM   3365 C  C   . GLY   B 1 143 ? -8.737  15.142  -8.292  1.00 30.35 ?  143 GLY   B C   1 
ATOM   3366 O  O   . GLY   B 1 143 ? -7.645  15.448  -8.787  1.00 30.27 ?  143 GLY   B O   1 
ATOM   3367 N  N   . SER   B 1 144 ? -9.018  13.910  -7.872  1.00 30.51 ?  144 SER   B N   1 
ATOM   3368 C  CA  . SER   B 1 144 ? -8.045  12.828  -7.906  1.00 25.92 ?  144 SER   B CA  1 
ATOM   3369 C  C   . SER   B 1 144 ? -7.932  12.163  -9.268  1.00 24.81 ?  144 SER   B C   1 
ATOM   3370 O  O   . SER   B 1 144 ? -6.966  11.427  -9.493  1.00 22.37 ?  144 SER   B O   1 
ATOM   3371 C  CB  . SER   B 1 144 ? -8.421  11.766  -6.879  1.00 26.87 ?  144 SER   B CB  1 
ATOM   3372 O  OG  . SER   B 1 144 ? -9.700  11.234  -7.193  1.00 28.61 ?  144 SER   B OG  1 
ATOM   3373 N  N   . CYS   B 1 145 ? -8.903  12.375  -10.158 1.00 27.66 ?  145 CYS   B N   1 
ATOM   3374 C  CA  . CYS   B 1 145 ? -8.884  11.720  -11.458 1.00 24.12 ?  145 CYS   B CA  1 
ATOM   3375 C  C   . CYS   B 1 145 ? -7.608  12.065  -12.208 1.00 23.91 ?  145 CYS   B C   1 
ATOM   3376 O  O   . CYS   B 1 145 ? -7.110  13.192  -12.141 1.00 25.16 ?  145 CYS   B O   1 
ATOM   3377 C  CB  . CYS   B 1 145 ? -10.105 12.128  -12.273 1.00 24.79 ?  145 CYS   B CB  1 
ATOM   3378 S  SG  . CYS   B 1 145 ? -11.669 11.617  -11.527 1.00 31.80 ?  145 CYS   B SG  1 
ATOM   3379 N  N   . GLY   B 1 146 ? -7.077  11.077  -12.922 1.00 25.52 ?  146 GLY   B N   1 
ATOM   3380 C  CA  . GLY   B 1 146 ? -5.779  11.205  -13.533 1.00 23.74 ?  146 GLY   B CA  1 
ATOM   3381 C  C   . GLY   B 1 146 ? -4.624  10.705  -12.691 1.00 26.02 ?  146 GLY   B C   1 
ATOM   3382 O  O   . GLY   B 1 146 ? -3.516  10.577  -13.219 1.00 26.01 ?  146 GLY   B O   1 
ATOM   3383 N  N   . SER   B 1 147 ? -4.838  10.441  -11.396 1.00 24.32 ?  147 SER   B N   1 
ATOM   3384 C  CA  . SER   B 1 147 ? -3.818  9.775   -10.593 1.00 23.37 ?  147 SER   B CA  1 
ATOM   3385 C  C   . SER   B 1 147 ? -3.549  8.393   -11.170 1.00 22.27 ?  147 SER   B C   1 
ATOM   3386 O  O   . SER   B 1 147 ? -4.436  7.758   -11.743 1.00 23.29 ?  147 SER   B O   1 
ATOM   3387 C  CB  . SER   B 1 147 ? -4.264  9.657   -9.127  1.00 22.53 ?  147 SER   B CB  1 
ATOM   3388 O  OG  . SER   B 1 147 ? -4.459  10.935  -8.544  1.00 24.98 ?  147 SER   B OG  1 
ATOM   3389 N  N   . VAL   B 1 148 ? -2.316  7.921   -11.030 1.00 21.31 ?  148 VAL   B N   1 
ATOM   3390 C  CA  . VAL   B 1 148 ? -1.950  6.684   -11.702 1.00 20.92 ?  148 VAL   B CA  1 
ATOM   3391 C  C   . VAL   B 1 148 ? -1.499  5.633   -10.700 1.00 25.14 ?  148 VAL   B C   1 
ATOM   3392 O  O   . VAL   B 1 148 ? -1.041  5.928   -9.590  1.00 21.96 ?  148 VAL   B O   1 
ATOM   3393 C  CB  . VAL   B 1 148 ? -0.868  6.903   -12.781 1.00 28.84 ?  148 VAL   B CB  1 
ATOM   3394 C  CG1 . VAL   B 1 148 ? -1.422  7.765   -13.914 1.00 25.86 ?  148 VAL   B CG1 1 
ATOM   3395 C  CG2 . VAL   B 1 148 ? 0.368   7.514   -12.166 1.00 24.13 ?  148 VAL   B CG2 1 
ATOM   3396 N  N   . GLY   B 1 149 ? -1.649  4.380   -11.120 1.00 26.69 ?  149 GLY   B N   1 
ATOM   3397 C  CA  . GLY   B 1 149 ? -1.126  3.239   -10.396 1.00 22.98 ?  149 GLY   B CA  1 
ATOM   3398 C  C   . GLY   B 1 149 ? 0.047   2.668   -11.167 1.00 27.77 ?  149 GLY   B C   1 
ATOM   3399 O  O   . GLY   B 1 149 ? 0.122   2.795   -12.394 1.00 25.35 ?  149 GLY   B O   1 
ATOM   3400 N  N   . PHE   B 1 150 ? 0.962   2.021   -10.455 1.00 25.34 ?  150 PHE   B N   1 
ATOM   3401 C  CA  . PHE   B 1 150 ? 2.202   1.658   -11.122 1.00 23.31 ?  150 PHE   B CA  1 
ATOM   3402 C  C   . PHE   B 1 150 ? 2.955   0.611   -10.321 1.00 25.53 ?  150 PHE   B C   1 
ATOM   3403 O  O   . PHE   B 1 150 ? 2.751   0.445   -9.110  1.00 24.87 ?  150 PHE   B O   1 
ATOM   3404 C  CB  . PHE   B 1 150 ? 3.090   2.889   -11.343 1.00 28.50 ?  150 PHE   B CB  1 
ATOM   3405 C  CG  . PHE   B 1 150 ? 3.598   3.506   -10.073 1.00 26.14 ?  150 PHE   B CG  1 
ATOM   3406 C  CD1 . PHE   B 1 150 ? 2.804   4.379   -9.348  1.00 31.21 ?  150 PHE   B CD1 1 
ATOM   3407 C  CD2 . PHE   B 1 150 ? 4.874   3.219   -9.608  1.00 29.24 ?  150 PHE   B CD2 1 
ATOM   3408 C  CE1 . PHE   B 1 150 ? 3.270   4.946   -8.166  1.00 33.81 ?  150 PHE   B CE1 1 
ATOM   3409 C  CE2 . PHE   B 1 150 ? 5.344   3.783   -8.435  1.00 30.12 ?  150 PHE   B CE2 1 
ATOM   3410 C  CZ  . PHE   B 1 150 ? 4.542   4.648   -7.714  1.00 29.09 ?  150 PHE   B CZ  1 
ATOM   3411 N  N   . ASN   B 1 151 ? 3.839   -0.090  -11.026 1.00 27.82 ?  151 ASN   B N   1 
ATOM   3412 C  CA  . ASN   B 1 151 ? 4.830   -0.967  -10.428 1.00 27.17 ?  151 ASN   B CA  1 
ATOM   3413 C  C   . ASN   B 1 151 ? 6.196   -0.563  -10.959 1.00 29.62 ?  151 ASN   B C   1 
ATOM   3414 O  O   . ASN   B 1 151 ? 6.310   0.109   -11.988 1.00 26.07 ?  151 ASN   B O   1 
ATOM   3415 C  CB  . ASN   B 1 151 ? 4.550   -2.446  -10.735 1.00 25.68 ?  151 ASN   B CB  1 
ATOM   3416 C  CG  . ASN   B 1 151 ? 3.391   -3.000  -9.915  1.00 32.14 ?  151 ASN   B CG  1 
ATOM   3417 O  OD1 . ASN   B 1 151 ? 3.561   -3.394  -8.759  1.00 28.37 ?  151 ASN   B OD1 1 
ATOM   3418 N  ND2 . ASN   B 1 151 ? 2.208   -3.024  -10.510 1.00 27.79 ?  151 ASN   B ND2 1 
ATOM   3419 N  N   . ILE   B 1 152 ? 7.241   -0.958  -10.240 1.00 30.31 ?  152 ILE   B N   1 
ATOM   3420 C  CA  . ILE   B 1 152 ? 8.607   -0.657  -10.650 1.00 31.41 ?  152 ILE   B CA  1 
ATOM   3421 C  C   . ILE   B 1 152 ? 9.412   -1.947  -10.668 1.00 35.63 ?  152 ILE   B C   1 
ATOM   3422 O  O   . ILE   B 1 152 ? 9.367   -2.729  -9.712  1.00 35.34 ?  152 ILE   B O   1 
ATOM   3423 C  CB  . ILE   B 1 152 ? 9.257   0.399   -9.737  1.00 28.99 ?  152 ILE   B CB  1 
ATOM   3424 C  CG1 . ILE   B 1 152 ? 8.468   1.706   -9.833  1.00 29.15 ?  152 ILE   B CG1 1 
ATOM   3425 C  CG2 . ILE   B 1 152 ? 10.694  0.653   -10.150 1.00 36.74 ?  152 ILE   B CG2 1 
ATOM   3426 C  CD1 . ILE   B 1 152 ? 9.019   2.823   -8.997  1.00 36.45 ?  152 ILE   B CD1 1 
ATOM   3427 N  N   . ASP   B 1 153 ? 10.125  -2.176  -11.768 1.00 40.26 ?  153 ASP   B N   1 
ATOM   3428 C  CA  . ASP   B 1 153 ? 11.045  -3.296  -11.913 1.00 41.67 ?  153 ASP   B CA  1 
ATOM   3429 C  C   . ASP   B 1 153 ? 12.368  -2.730  -12.400 1.00 44.25 ?  153 ASP   B C   1 
ATOM   3430 O  O   . ASP   B 1 153 ? 12.422  -2.123  -13.476 1.00 46.70 ?  153 ASP   B O   1 
ATOM   3431 C  CB  . ASP   B 1 153 ? 10.504  -4.344  -12.892 1.00 41.44 ?  153 ASP   B CB  1 
ATOM   3432 N  N   . TYR   B 1 154 ? 13.423  -2.917  -11.607 1.00 42.24 ?  154 TYR   B N   1 
ATOM   3433 C  CA  . TYR   B 1 154 ? 14.699  -2.254  -11.842 1.00 48.92 ?  154 TYR   B CA  1 
ATOM   3434 C  C   . TYR   B 1 154 ? 14.483  -0.748  -11.948 1.00 45.83 ?  154 TYR   B C   1 
ATOM   3435 O  O   . TYR   B 1 154 ? 14.087  -0.100  -10.974 1.00 52.67 ?  154 TYR   B O   1 
ATOM   3436 C  CB  . TYR   B 1 154 ? 15.382  -2.805  -13.099 1.00 44.46 ?  154 TYR   B CB  1 
ATOM   3437 N  N   . ASP   B 1 155 ? 14.721  -0.183  -13.127 1.00 42.09 ?  155 ASP   B N   1 
ATOM   3438 C  CA  . ASP   B 1 155 ? 14.576  1.249   -13.345 1.00 42.76 ?  155 ASP   B CA  1 
ATOM   3439 C  C   . ASP   B 1 155 ? 13.337  1.602   -14.161 1.00 41.65 ?  155 ASP   B C   1 
ATOM   3440 O  O   . ASP   B 1 155 ? 13.166  2.769   -14.527 1.00 39.47 ?  155 ASP   B O   1 
ATOM   3441 C  CB  . ASP   B 1 155 ? 15.827  1.793   -14.040 1.00 45.03 ?  155 ASP   B CB  1 
ATOM   3442 C  CG  . ASP   B 1 155 ? 16.285  0.904   -15.189 1.00 49.48 ?  155 ASP   B CG  1 
ATOM   3443 O  OD1 . ASP   B 1 155 ? 15.672  -0.168  -15.395 1.00 47.40 ?  155 ASP   B OD1 1 
ATOM   3444 O  OD2 . ASP   B 1 155 ? 17.263  1.268   -15.880 1.00 53.92 ?  155 ASP   B OD2 1 
ATOM   3445 N  N   . CYS   B 1 156 ? 12.467  0.632   -14.449 1.00 39.13 ?  156 CYS   B N   1 
ATOM   3446 C  CA  . CYS   B 1 156 ? 11.380  0.797   -15.411 1.00 35.06 ?  156 CYS   B CA  1 
ATOM   3447 C  C   . CYS   B 1 156 ? 10.036  0.868   -14.692 1.00 33.94 ?  156 CYS   B C   1 
ATOM   3448 O  O   . CYS   B 1 156 ? 9.643   -0.079  -14.003 1.00 34.66 ?  156 CYS   B O   1 
ATOM   3449 C  CB  . CYS   B 1 156 ? 11.375  -0.345  -16.428 1.00 36.07 ?  156 CYS   B CB  1 
ATOM   3450 S  SG  . CYS   B 1 156 ? 10.004  -0.283  -17.640 1.00 38.51 ?  156 CYS   B SG  1 
ATOM   3451 N  N   . VAL   B 1 157 ? 9.327   1.976   -14.880 1.00 29.07 ?  157 VAL   B N   1 
ATOM   3452 C  CA  . VAL   B 1 157 ? 8.004   2.156   -14.290 1.00 31.74 ?  157 VAL   B CA  1 
ATOM   3453 C  C   . VAL   B 1 157 ? 6.966   1.500   -15.195 1.00 31.30 ?  157 VAL   B C   1 
ATOM   3454 O  O   . VAL   B 1 157 ? 6.876   1.821   -16.385 1.00 26.93 ?  157 VAL   B O   1 
ATOM   3455 C  CB  . VAL   B 1 157 ? 7.692   3.646   -14.090 1.00 28.55 ?  157 VAL   B CB  1 
ATOM   3456 C  CG1 . VAL   B 1 157 ? 6.326   3.817   -13.448 1.00 28.19 ?  157 VAL   B CG1 1 
ATOM   3457 C  CG2 . VAL   B 1 157 ? 8.788   4.318   -13.255 1.00 31.70 ?  157 VAL   B CG2 1 
ATOM   3458 N  N   . SER   B 1 158 ? 6.169   0.590   -14.630 1.00 29.88 ?  158 SER   B N   1 
ATOM   3459 C  CA  . SER   B 1 158 ? 5.072   -0.055  -15.361 1.00 28.90 ?  158 SER   B CA  1 
ATOM   3460 C  C   . SER   B 1 158 ? 3.760   0.581   -14.920 1.00 25.56 ?  158 SER   B C   1 
ATOM   3461 O  O   . SER   B 1 158 ? 3.184   0.204   -13.905 1.00 27.24 ?  158 SER   B O   1 
ATOM   3462 C  CB  . SER   B 1 158 ? 5.064   -1.558  -15.115 1.00 29.13 ?  158 SER   B CB  1 
ATOM   3463 O  OG  . SER   B 1 158 ? 6.037   -2.197  -15.923 1.00 38.44 ?  158 SER   B OG  1 
ATOM   3464 N  N   . PHE   B 1 159 ? 3.282   1.559   -15.690 1.00 26.41 ?  159 PHE   B N   1 
ATOM   3465 C  CA  . PHE   B 1 159 ? 2.002   2.184   -15.379 1.00 26.73 ?  159 PHE   B CA  1 
ATOM   3466 C  C   . PHE   B 1 159 ? 0.866   1.237   -15.742 1.00 25.43 ?  159 PHE   B C   1 
ATOM   3467 O  O   . PHE   B 1 159 ? 0.765   0.787   -16.891 1.00 24.27 ?  159 PHE   B O   1 
ATOM   3468 C  CB  . PHE   B 1 159 ? 1.832   3.499   -16.142 1.00 31.95 ?  159 PHE   B CB  1 
ATOM   3469 C  CG  . PHE   B 1 159 ? 2.839   4.557   -15.789 1.00 28.73 ?  159 PHE   B CG  1 
ATOM   3470 C  CD1 . PHE   B 1 159 ? 2.641   5.377   -14.691 1.00 26.40 ?  159 PHE   B CD1 1 
ATOM   3471 C  CD2 . PHE   B 1 159 ? 3.963   4.758   -16.578 1.00 25.28 ?  159 PHE   B CD2 1 
ATOM   3472 C  CE1 . PHE   B 1 159 ? 3.550   6.362   -14.374 1.00 24.15 ?  159 PHE   B CE1 1 
ATOM   3473 C  CE2 . PHE   B 1 159 ? 4.890   5.740   -16.256 1.00 26.10 ?  159 PHE   B CE2 1 
ATOM   3474 C  CZ  . PHE   B 1 159 ? 4.686   6.544   -15.163 1.00 25.95 ?  159 PHE   B CZ  1 
ATOM   3475 N  N   . CYS   B 1 160 ? -0.005  0.951   -14.774 1.00 23.18 ?  160 CYS   B N   1 
ATOM   3476 C  CA  . CYS   B 1 160 ? -1.087  0.003   -14.989 1.00 23.68 ?  160 CYS   B CA  1 
ATOM   3477 C  C   . CYS   B 1 160 ? -2.480  0.561   -14.752 1.00 27.02 ?  160 CYS   B C   1 
ATOM   3478 O  O   . CYS   B 1 160 ? -3.451  -0.089  -15.156 1.00 29.35 ?  160 CYS   B O   1 
ATOM   3479 C  CB  . CYS   B 1 160 ? -0.903  -1.232  -14.098 1.00 30.64 ?  160 CYS   B CB  1 
ATOM   3480 S  SG  . CYS   B 1 160 ? -0.800  -0.820  -12.344 1.00 29.94 ?  160 CYS   B SG  1 
ATOM   3481 N  N   . TYR   B 1 161 ? -2.617  1.730   -14.130 1.00 24.12 ?  161 TYR   B N   1 
ATOM   3482 C  CA  . TYR   B 1 161 ? -3.918  2.243   -13.726 1.00 26.22 ?  161 TYR   B CA  1 
ATOM   3483 C  C   . TYR   B 1 161 ? -3.940  3.755   -13.874 1.00 26.23 ?  161 TYR   B C   1 
ATOM   3484 O  O   . TYR   B 1 161 ? -2.957  4.428   -13.570 1.00 26.50 ?  161 TYR   B O   1 
ATOM   3485 C  CB  . TYR   B 1 161 ? -4.236  1.858   -12.270 1.00 23.71 ?  161 TYR   B CB  1 
ATOM   3486 C  CG  . TYR   B 1 161 ? -5.593  2.325   -11.767 1.00 23.55 ?  161 TYR   B CG  1 
ATOM   3487 C  CD1 . TYR   B 1 161 ? -6.748  1.622   -12.078 1.00 26.66 ?  161 TYR   B CD1 1 
ATOM   3488 C  CD2 . TYR   B 1 161 ? -5.716  3.461   -10.977 1.00 21.34 ?  161 TYR   B CD2 1 
ATOM   3489 C  CE1 . TYR   B 1 161 ? -7.993  2.037   -11.615 1.00 26.32 ?  161 TYR   B CE1 1 
ATOM   3490 C  CE2 . TYR   B 1 161 ? -6.970  3.885   -10.503 1.00 22.37 ?  161 TYR   B CE2 1 
ATOM   3491 C  CZ  . TYR   B 1 161 ? -8.097  3.171   -10.836 1.00 22.28 ?  161 TYR   B CZ  1 
ATOM   3492 O  OH  . TYR   B 1 161 ? -9.339  3.579   -10.390 1.00 25.16 ?  161 TYR   B OH  1 
ATOM   3493 N  N   . MET   B 1 162 ? -5.053  4.288   -14.362 1.00 24.56 ?  162 MET   B N   1 
ATOM   3494 C  CA  . MET   B 1 162 ? -5.305  5.719   -14.283 1.00 23.58 ?  162 MET   B CA  1 
ATOM   3495 C  C   . MET   B 1 162 ? -6.702  5.889   -13.725 1.00 22.17 ?  162 MET   B C   1 
ATOM   3496 O  O   . MET   B 1 162 ? -7.620  5.200   -14.167 1.00 20.50 ?  162 MET   B O   1 
ATOM   3497 C  CB  . MET   B 1 162 ? -5.187  6.414   -15.642 1.00 23.80 ?  162 MET   B CB  1 
ATOM   3498 C  CG  . MET   B 1 162 ? -5.694  7.846   -15.602 1.00 25.63 ?  162 MET   B CG  1 
ATOM   3499 S  SD  . MET   B 1 162 ? -5.425  8.776   -17.128 1.00 35.36 ?  162 MET   B SD  1 
ATOM   3500 C  CE  . MET   B 1 162 ? -3.764  9.401   -16.774 1.00 35.74 ?  162 MET   B CE  1 
ATOM   3501 N  N   . HIS   B 1 163 ? -6.855  6.773   -12.739 1.00 24.04 ?  163 HIS   B N   1 
ATOM   3502 C  CA  . HIS   B 1 163 ? -8.104  6.849   -11.986 1.00 24.49 ?  163 HIS   B CA  1 
ATOM   3503 C  C   . HIS   B 1 163 ? -9.151  7.671   -12.727 1.00 24.14 ?  163 HIS   B C   1 
ATOM   3504 O  O   . HIS   B 1 163 ? -8.854  8.760   -13.226 1.00 26.27 ?  163 HIS   B O   1 
ATOM   3505 C  CB  . HIS   B 1 163 ? -7.852  7.454   -10.604 1.00 23.76 ?  163 HIS   B CB  1 
ATOM   3506 C  CG  . HIS   B 1 163 ? -9.084  7.505   -9.759  1.00 24.29 ?  163 HIS   B CG  1 
ATOM   3507 N  ND1 . HIS   B 1 163 ? -9.821  6.379   -9.465  1.00 24.38 ?  163 HIS   B ND1 1 
ATOM   3508 C  CD2 . HIS   B 1 163 ? -9.745  8.547   -9.203  1.00 23.02 ?  163 HIS   B CD2 1 
ATOM   3509 C  CE1 . HIS   B 1 163 ? -10.872 6.722   -8.741  1.00 22.86 ?  163 HIS   B CE1 1 
ATOM   3510 N  NE2 . HIS   B 1 163 ? -10.848 8.031   -8.566  1.00 23.35 ?  163 HIS   B NE2 1 
ATOM   3511 N  N   . HIS   B 1 164 ? -10.391 7.161   -12.771 1.00 22.80 ?  164 HIS   B N   1 
ATOM   3512 C  CA  . HIS   B 1 164 ? -11.496 7.827   -13.442 1.00 22.01 ?  164 HIS   B CA  1 
ATOM   3513 C  C   . HIS   B 1 164 ? -12.708 8.128   -12.562 1.00 24.95 ?  164 HIS   B C   1 
ATOM   3514 O  O   . HIS   B 1 164 ? -13.389 9.119   -12.829 1.00 25.44 ?  164 HIS   B O   1 
ATOM   3515 C  CB  . HIS   B 1 164 ? -11.983 6.991   -14.641 1.00 25.35 ?  164 HIS   B CB  1 
ATOM   3516 C  CG  . HIS   B 1 164 ? -11.071 7.042   -15.828 1.00 26.24 ?  164 HIS   B CG  1 
ATOM   3517 N  ND1 . HIS   B 1 164 ? -11.459 7.555   -17.048 1.00 27.86 ?  164 HIS   B ND1 1 
ATOM   3518 C  CD2 . HIS   B 1 164 ? -9.787  6.642   -15.979 1.00 24.85 ?  164 HIS   B CD2 1 
ATOM   3519 C  CE1 . HIS   B 1 164 ? -10.454 7.467   -17.900 1.00 30.93 ?  164 HIS   B CE1 1 
ATOM   3520 N  NE2 . HIS   B 1 164 ? -9.426  6.921   -17.276 1.00 24.78 ?  164 HIS   B NE2 1 
ATOM   3521 N  N   . MET   B 1 165 ? -13.017 7.322   -11.541 1.00 22.25 ?  165 MET   B N   1 
ATOM   3522 C  CA  . MET   B 1 165 ? -14.349 7.498   -10.953 1.00 25.11 ?  165 MET   B CA  1 
ATOM   3523 C  C   . MET   B 1 165 ? -14.491 6.779   -9.618  1.00 25.27 ?  165 MET   B C   1 
ATOM   3524 O  O   . MET   B 1 165 ? -13.762 5.835   -9.310  1.00 27.77 ?  165 MET   B O   1 
ATOM   3525 C  CB  . MET   B 1 165 ? -15.435 6.989   -11.903 1.00 28.26 ?  165 MET   B CB  1 
ATOM   3526 C  CG  . MET   B 1 165 ? -15.476 5.474   -12.006 1.00 27.01 ?  165 MET   B CG  1 
ATOM   3527 S  SD  . MET   B 1 165 ? -16.835 4.872   -13.044 1.00 39.43 ?  165 MET   B SD  1 
ATOM   3528 C  CE  . MET   B 1 165 ? -16.265 5.459   -14.625 1.00 32.18 ?  165 MET   B CE  1 
ATOM   3529 N  N   . GLU   B 1 166 ? -15.490 7.213   -8.856  1.00 25.19 ?  166 GLU   B N   1 
ATOM   3530 C  CA  . GLU   B 1 166 ? -15.885 6.550   -7.626  1.00 26.51 ?  166 GLU   B CA  1 
ATOM   3531 C  C   . GLU   B 1 166 ? -17.308 6.020   -7.773  1.00 26.69 ?  166 GLU   B C   1 
ATOM   3532 O  O   . GLU   B 1 166 ? -18.198 6.743   -8.232  1.00 29.03 ?  166 GLU   B O   1 
ATOM   3533 C  CB  . GLU   B 1 166 ? -15.787 7.513   -6.446  1.00 24.64 ?  166 GLU   B CB  1 
ATOM   3534 C  CG  . GLU   B 1 166 ? -16.110 6.866   -5.114  1.00 28.46 ?  166 GLU   B CG  1 
ATOM   3535 C  CD  . GLU   B 1 166 ? -15.819 7.789   -3.950  1.00 31.63 ?  166 GLU   B CD  1 
ATOM   3536 O  OE1 . GLU   B 1 166 ? -16.775 8.260   -3.289  1.00 32.92 ?  166 GLU   B OE1 1 
ATOM   3537 O  OE2 . GLU   B 1 166 ? -14.624 8.051   -3.703  1.00 30.30 ?  166 GLU   B OE2 1 
ATOM   3538 N  N   . LEU   B 1 167 ? -17.512 4.761   -7.386  1.00 27.29 ?  167 LEU   B N   1 
ATOM   3539 C  CA  . LEU   B 1 167 ? -18.809 4.108   -7.446  1.00 26.31 ?  167 LEU   B CA  1 
ATOM   3540 C  C   . LEU   B 1 167 ? -19.597 4.385   -6.167  1.00 29.76 ?  167 LEU   B C   1 
ATOM   3541 O  O   . LEU   B 1 167 ? -19.026 4.827   -5.163  1.00 32.58 ?  167 LEU   B O   1 
ATOM   3542 C  CB  . LEU   B 1 167 ? -18.611 2.610   -7.668  1.00 23.73 ?  167 LEU   B CB  1 
ATOM   3543 C  CG  . LEU   B 1 167 ? -18.130 2.306   -9.095  1.00 29.36 ?  167 LEU   B CG  1 
ATOM   3544 C  CD1 . LEU   B 1 167 ? -17.435 0.965   -9.167  1.00 31.83 ?  167 LEU   B CD1 1 
ATOM   3545 C  CD2 . LEU   B 1 167 ? -19.309 2.351   -10.066 1.00 33.32 ?  167 LEU   B CD2 1 
ATOM   3546 N  N   . PRO   B 1 168 ? -20.917 4.144   -6.178  1.00 30.05 ?  168 PRO   B N   1 
ATOM   3547 C  CA  . PRO   B 1 168 ? -21.733 4.521   -5.012  1.00 29.42 ?  168 PRO   B CA  1 
ATOM   3548 C  C   . PRO   B 1 168 ? -21.294 3.879   -3.707  1.00 31.25 ?  168 PRO   B C   1 
ATOM   3549 O  O   . PRO   B 1 168 ? -21.468 4.488   -2.643  1.00 33.19 ?  168 PRO   B O   1 
ATOM   3550 C  CB  . PRO   B 1 168 ? -23.141 4.059   -5.412  1.00 25.98 ?  168 PRO   B CB  1 
ATOM   3551 C  CG  . PRO   B 1 168 ? -23.134 4.135   -6.908  1.00 33.30 ?  168 PRO   B CG  1 
ATOM   3552 C  CD  . PRO   B 1 168 ? -21.759 3.703   -7.310  1.00 32.04 ?  168 PRO   B CD  1 
ATOM   3553 N  N   . THR   B 1 169 ? -20.738 2.669   -3.742  1.00 27.16 ?  169 THR   B N   1 
ATOM   3554 C  CA  . THR   B 1 169 ? -20.246 2.055   -2.514  1.00 36.35 ?  169 THR   B CA  1 
ATOM   3555 C  C   . THR   B 1 169 ? -18.920 2.641   -2.040  1.00 35.12 ?  169 THR   B C   1 
ATOM   3556 O  O   . THR   B 1 169 ? -18.385 2.178   -1.026  1.00 30.68 ?  169 THR   B O   1 
ATOM   3557 C  CB  . THR   B 1 169 ? -20.099 0.545   -2.697  1.00 35.96 ?  169 THR   B CB  1 
ATOM   3558 O  OG1 . THR   B 1 169 ? -19.352 0.281   -3.893  1.00 35.04 ?  169 THR   B OG1 1 
ATOM   3559 C  CG2 . THR   B 1 169 ? -21.476 -0.120  -2.787  1.00 38.85 ?  169 THR   B CG2 1 
ATOM   3560 N  N   . GLY   B 1 170 ? -18.373 3.633   -2.740  1.00 32.56 ?  170 GLY   B N   1 
ATOM   3561 C  CA  . GLY   B 1 170 ? -17.134 4.256   -2.316  1.00 27.57 ?  170 GLY   B CA  1 
ATOM   3562 C  C   . GLY   B 1 170 ? -15.877 3.539   -2.743  1.00 30.77 ?  170 GLY   B C   1 
ATOM   3563 O  O   . GLY   B 1 170 ? -14.800 3.844   -2.218  1.00 30.58 ?  170 GLY   B O   1 
ATOM   3564 N  N   . VAL   B 1 171 ? -15.979 2.585   -3.664  1.00 32.55 ?  171 VAL   B N   1 
ATOM   3565 C  CA  . VAL   B 1 171 ? -14.808 1.977   -4.285  1.00 28.62 ?  171 VAL   B CA  1 
ATOM   3566 C  C   . VAL   B 1 171 ? -14.589 2.671   -5.627  1.00 26.86 ?  171 VAL   B C   1 
ATOM   3567 O  O   . VAL   B 1 171 ? -15.406 3.501   -6.043  1.00 28.15 ?  171 VAL   B O   1 
ATOM   3568 C  CB  . VAL   B 1 171 ? -14.988 0.458   -4.441  1.00 29.33 ?  171 VAL   B CB  1 
ATOM   3569 C  CG1 . VAL   B 1 171 ? -15.211 -0.188  -3.075  1.00 28.90 ?  171 VAL   B CG1 1 
ATOM   3570 C  CG2 . VAL   B 1 171 ? -16.153 0.158   -5.384  1.00 23.87 ?  171 VAL   B CG2 1 
ATOM   3571 N  N   . HIS   B 1 172 ? -13.502 2.337   -6.320  1.00 26.09 ?  172 HIS   B N   1 
ATOM   3572 C  CA  . HIS   B 1 172 ? -13.037 3.165   -7.423  1.00 24.43 ?  172 HIS   B CA  1 
ATOM   3573 C  C   . HIS   B 1 172 ? -12.824 2.351   -8.691  1.00 24.76 ?  172 HIS   B C   1 
ATOM   3574 O  O   . HIS   B 1 172 ? -12.636 1.132   -8.650  1.00 26.46 ?  172 HIS   B O   1 
ATOM   3575 C  CB  . HIS   B 1 172 ? -11.764 3.899   -7.015  1.00 27.02 ?  172 HIS   B CB  1 
ATOM   3576 C  CG  . HIS   B 1 172 ? -11.963 4.780   -5.829  1.00 28.14 ?  172 HIS   B CG  1 
ATOM   3577 N  ND1 . HIS   B 1 172 ? -11.612 4.398   -4.553  1.00 28.12 ?  172 HIS   B ND1 1 
ATOM   3578 C  CD2 . HIS   B 1 172 ? -12.543 5.998   -5.711  1.00 28.84 ?  172 HIS   B CD2 1 
ATOM   3579 C  CE1 . HIS   B 1 172 ? -11.929 5.359   -3.706  1.00 28.57 ?  172 HIS   B CE1 1 
ATOM   3580 N  NE2 . HIS   B 1 172 ? -12.495 6.342   -4.382  1.00 26.68 ?  172 HIS   B NE2 1 
ATOM   3581 N  N   . ALA   B 1 173 ? -12.881 3.047   -9.826  1.00 26.85 ?  173 ALA   B N   1 
ATOM   3582 C  CA  . ALA   B 1 173 ? -12.758 2.425   -11.133 1.00 26.27 ?  173 ALA   B CA  1 
ATOM   3583 C  C   . ALA   B 1 173 ? -11.908 3.303   -12.036 1.00 21.89 ?  173 ALA   B C   1 
ATOM   3584 O  O   . ALA   B 1 173 ? -11.921 4.532   -11.928 1.00 23.39 ?  173 ALA   B O   1 
ATOM   3585 C  CB  . ALA   B 1 173 ? -14.128 2.190   -11.796 1.00 27.28 ?  173 ALA   B CB  1 
ATOM   3586 N  N   . GLY   B 1 174 ? -11.182 2.658   -12.935 1.00 27.81 ?  174 GLY   B N   1 
ATOM   3587 C  CA  . GLY   B 1 174 ? -10.338 3.372   -13.866 1.00 22.47 ?  174 GLY   B CA  1 
ATOM   3588 C  C   . GLY   B 1 174 ? -9.989  2.492   -15.040 1.00 22.61 ?  174 GLY   B C   1 
ATOM   3589 O  O   . GLY   B 1 174 ? -10.583 1.432   -15.240 1.00 20.84 ?  174 GLY   B O   1 
ATOM   3590 N  N   . THR   B 1 175 ? -8.978  2.933   -15.794 1.00 22.96 ?  175 THR   B N   1 
ATOM   3591 C  CA  . THR   B 1 175 ? -8.562  2.304   -17.039 1.00 21.60 ?  175 THR   B CA  1 
ATOM   3592 C  C   . THR   B 1 175 ? -7.072  1.999   -16.984 1.00 22.49 ?  175 THR   B C   1 
ATOM   3593 O  O   . THR   B 1 175 ? -6.344  2.525   -16.142 1.00 24.28 ?  175 THR   B O   1 
ATOM   3594 C  CB  . THR   B 1 175 ? -8.827  3.221   -18.248 1.00 25.02 ?  175 THR   B CB  1 
ATOM   3595 O  OG1 . THR   B 1 175 ? -7.977  4.374   -18.154 1.00 25.15 ?  175 THR   B OG1 1 
ATOM   3596 C  CG2 . THR   B 1 175 ? -10.282 3.682   -18.276 1.00 23.39 ?  175 THR   B CG2 1 
ATOM   3597 N  N   . ASP   B 1 176 ? -6.608  1.161   -17.909 1.00 23.90 ?  176 ASP   B N   1 
ATOM   3598 C  CA  . ASP   B 1 176 ? -5.178  1.111   -18.149 1.00 24.73 ?  176 ASP   B CA  1 
ATOM   3599 C  C   . ASP   B 1 176 ? -4.762  2.390   -18.872 1.00 23.87 ?  176 ASP   B C   1 
ATOM   3600 O  O   . ASP   B 1 176 ? -5.591  3.235   -19.228 1.00 25.94 ?  176 ASP   B O   1 
ATOM   3601 C  CB  . ASP   B 1 176 ? -4.802  -0.158  -18.917 1.00 25.00 ?  176 ASP   B CB  1 
ATOM   3602 C  CG  . ASP   B 1 176 ? -5.446  -0.238  -20.305 1.00 24.35 ?  176 ASP   B CG  1 
ATOM   3603 O  OD1 . ASP   B 1 176 ? -5.722  0.809   -20.923 1.00 24.35 ?  176 ASP   B OD1 1 
ATOM   3604 O  OD2 . ASP   B 1 176 ? -5.687  -1.370  -20.777 1.00 26.81 ?  176 ASP   B OD2 1 
ATOM   3605 N  N   . LEU   B 1 177 ? -3.466  2.537   -19.112 1.00 24.83 ?  177 LEU   B N   1 
ATOM   3606 C  CA  . LEU   B 1 177 ? -3.006  3.767   -19.743 1.00 23.43 ?  177 LEU   B CA  1 
ATOM   3607 C  C   . LEU   B 1 177 ? -3.278  3.799   -21.244 1.00 24.33 ?  177 LEU   B C   1 
ATOM   3608 O  O   . LEU   B 1 177 ? -3.031  4.827   -21.880 1.00 25.82 ?  177 LEU   B O   1 
ATOM   3609 C  CB  . LEU   B 1 177 ? -1.521  3.974   -19.468 1.00 23.33 ?  177 LEU   B CB  1 
ATOM   3610 C  CG  . LEU   B 1 177 ? -1.184  4.690   -18.155 1.00 26.96 ?  177 LEU   B CG  1 
ATOM   3611 C  CD1 . LEU   B 1 177 ? -1.537  6.171   -18.263 1.00 29.05 ?  177 LEU   B CD1 1 
ATOM   3612 C  CD2 . LEU   B 1 177 ? -1.885  4.048   -16.945 1.00 22.54 ?  177 LEU   B CD2 1 
ATOM   3613 N  N   . GLU   B 1 178 ? -3.752  2.704   -21.821 1.00 22.99 ?  178 GLU   B N   1 
ATOM   3614 C  CA  . GLU   B 1 178 ? -4.307  2.730   -23.170 1.00 24.31 ?  178 GLU   B CA  1 
ATOM   3615 C  C   . GLU   B 1 178 ? -5.782  3.090   -23.186 1.00 28.23 ?  178 GLU   B C   1 
ATOM   3616 O  O   . GLU   B 1 178 ? -6.403  3.037   -24.256 1.00 25.13 ?  178 GLU   B O   1 
ATOM   3617 C  CB  . GLU   B 1 178 ? -4.113  1.379   -23.852 1.00 24.39 ?  178 GLU   B CB  1 
ATOM   3618 C  CG  . GLU   B 1 178 ? -2.658  1.026   -24.110 1.00 30.28 ?  178 GLU   B CG  1 
ATOM   3619 C  CD  . GLU   B 1 178 ? -2.502  -0.414  -24.545 1.00 39.48 ?  178 GLU   B CD  1 
ATOM   3620 O  OE1 . GLU   B 1 178 ? -2.693  -0.702  -25.743 1.00 39.52 ?  178 GLU   B OE1 1 
ATOM   3621 O  OE2 . GLU   B 1 178 ? -2.216  -1.265  -23.675 1.00 46.22 ?  178 GLU   B OE2 1 
ATOM   3622 N  N   . GLY   B 1 179 ? -6.361  3.422   -22.029 1.00 24.77 ?  179 GLY   B N   1 
ATOM   3623 C  CA  . GLY   B 1 179 ? -7.740  3.861   -21.939 1.00 24.51 ?  179 GLY   B CA  1 
ATOM   3624 C  C   . GLY   B 1 179 ? -8.783  2.769   -21.853 1.00 25.19 ?  179 GLY   B C   1 
ATOM   3625 O  O   . GLY   B 1 179 ? -9.977  3.069   -21.960 1.00 24.67 ?  179 GLY   B O   1 
ATOM   3626 N  N   . ASN   B 1 180 ? -8.382  1.517   -21.681 1.00 22.60 ?  180 ASN   B N   1 
ATOM   3627 C  CA  . ASN   B 1 180 ? -9.333  0.418   -21.590 1.00 24.61 ?  180 ASN   B CA  1 
ATOM   3628 C  C   . ASN   B 1 180 ? -9.743  0.239   -20.134 1.00 27.36 ?  180 ASN   B C   1 
ATOM   3629 O  O   . ASN   B 1 180 ? -8.882  0.081   -19.262 1.00 21.26 ?  180 ASN   B O   1 
ATOM   3630 C  CB  . ASN   B 1 180 ? -8.702  -0.861  -22.138 1.00 29.00 ?  180 ASN   B CB  1 
ATOM   3631 C  CG  . ASN   B 1 180 ? -8.148  -0.676  -23.536 1.00 30.94 ?  180 ASN   B CG  1 
ATOM   3632 O  OD1 . ASN   B 1 180 ? -8.907  -0.533  -24.495 1.00 29.34 ?  180 ASN   B OD1 1 
ATOM   3633 N  ND2 . ASN   B 1 180 ? -6.816  -0.671  -23.662 1.00 26.96 ?  180 ASN   B ND2 1 
ATOM   3634 N  N   . PHE   B 1 181 ? -11.048 0.283   -19.874 1.00 24.97 ?  181 PHE   B N   1 
ATOM   3635 C  CA  . PHE   B 1 181 ? -11.532 0.206   -18.501 1.00 22.73 ?  181 PHE   B CA  1 
ATOM   3636 C  C   . PHE   B 1 181 ? -11.226 -1.151  -17.890 1.00 22.65 ?  181 PHE   B C   1 
ATOM   3637 O  O   . PHE   B 1 181 ? -11.280 -2.185  -18.561 1.00 22.43 ?  181 PHE   B O   1 
ATOM   3638 C  CB  . PHE   B 1 181 ? -13.049 0.466   -18.440 1.00 23.97 ?  181 PHE   B CB  1 
ATOM   3639 C  CG  . PHE   B 1 181 ? -13.395 1.824   -17.926 1.00 24.94 ?  181 PHE   B CG  1 
ATOM   3640 C  CD1 . PHE   B 1 181 ? -13.372 2.079   -16.555 1.00 25.67 ?  181 PHE   B CD1 1 
ATOM   3641 C  CD2 . PHE   B 1 181 ? -13.700 2.857   -18.797 1.00 23.21 ?  181 PHE   B CD2 1 
ATOM   3642 C  CE1 . PHE   B 1 181 ? -13.662 3.333   -16.062 1.00 27.22 ?  181 PHE   B CE1 1 
ATOM   3643 C  CE2 . PHE   B 1 181 ? -13.998 4.117   -18.312 1.00 27.30 ?  181 PHE   B CE2 1 
ATOM   3644 C  CZ  . PHE   B 1 181 ? -13.973 4.356   -16.942 1.00 28.03 ?  181 PHE   B CZ  1 
ATOM   3645 N  N   . TYR   B 1 182 ? -10.910 -1.146  -16.602 1.00 22.18 ?  182 TYR   B N   1 
ATOM   3646 C  CA  . TYR   B 1 182 ? -10.965 -2.362  -15.816 1.00 20.49 ?  182 TYR   B CA  1 
ATOM   3647 C  C   . TYR   B 1 182 ? -12.397 -2.538  -15.334 1.00 24.75 ?  182 TYR   B C   1 
ATOM   3648 O  O   . TYR   B 1 182 ? -12.957 -1.636  -14.702 1.00 26.91 ?  182 TYR   B O   1 
ATOM   3649 C  CB  . TYR   B 1 182 ? -10.007 -2.291  -14.625 1.00 21.52 ?  182 TYR   B CB  1 
ATOM   3650 C  CG  . TYR   B 1 182 ? -8.535  -2.265  -15.000 1.00 24.25 ?  182 TYR   B CG  1 
ATOM   3651 C  CD1 . TYR   B 1 182 ? -7.874  -3.433  -15.356 1.00 25.84 ?  182 TYR   B CD1 1 
ATOM   3652 C  CD2 . TYR   B 1 182 ? -7.807  -1.079  -14.975 1.00 21.89 ?  182 TYR   B CD2 1 
ATOM   3653 C  CE1 . TYR   B 1 182 ? -6.530  -3.421  -15.678 1.00 23.88 ?  182 TYR   B CE1 1 
ATOM   3654 C  CE2 . TYR   B 1 182 ? -6.458  -1.062  -15.291 1.00 21.63 ?  182 TYR   B CE2 1 
ATOM   3655 C  CZ  . TYR   B 1 182 ? -5.830  -2.234  -15.646 1.00 22.69 ?  182 TYR   B CZ  1 
ATOM   3656 O  OH  . TYR   B 1 182 ? -4.492  -2.226  -15.963 1.00 23.42 ?  182 TYR   B OH  1 
ATOM   3657 N  N   . GLY   B 1 183 ? -12.988 -3.688  -15.628 1.00 23.97 ?  183 GLY   B N   1 
ATOM   3658 C  CA  . GLY   B 1 183 ? -14.333 -3.956  -15.172 1.00 23.00 ?  183 GLY   B CA  1 
ATOM   3659 C  C   . GLY   B 1 183 ? -15.391 -3.347  -16.061 1.00 29.31 ?  183 GLY   B C   1 
ATOM   3660 O  O   . GLY   B 1 183 ? -15.102 -2.561  -16.966 1.00 24.75 ?  183 GLY   B O   1 
ATOM   3661 N  N   . PRO   B 1 184 ? -16.668 -3.686  -15.788 1.00 28.50 ?  184 PRO   B N   1 
ATOM   3662 C  CA  . PRO   B 1 184 ? -17.786 -3.307  -16.665 1.00 28.62 ?  184 PRO   B CA  1 
ATOM   3663 C  C   . PRO   B 1 184 ? -18.299 -1.886  -16.441 1.00 30.50 ?  184 PRO   B C   1 
ATOM   3664 O  O   . PRO   B 1 184 ? -19.492 -1.663  -16.247 1.00 27.65 ?  184 PRO   B O   1 
ATOM   3665 C  CB  . PRO   B 1 184 ? -18.853 -4.347  -16.313 1.00 25.07 ?  184 PRO   B CB  1 
ATOM   3666 C  CG  . PRO   B 1 184 ? -18.605 -4.648  -14.841 1.00 27.38 ?  184 PRO   B CG  1 
ATOM   3667 C  CD  . PRO   B 1 184 ? -17.093 -4.557  -14.674 1.00 28.05 ?  184 PRO   B CD  1 
ATOM   3668 N  N   . PHE   B 1 185 ? -17.394 -0.912  -16.487 1.00 29.04 ?  185 PHE   B N   1 
ATOM   3669 C  CA  . PHE   B 1 185 ? -17.751 0.463   -16.168 1.00 28.33 ?  185 PHE   B CA  1 
ATOM   3670 C  C   . PHE   B 1 185 ? -17.512 1.381   -17.363 1.00 25.60 ?  185 PHE   B C   1 
ATOM   3671 O  O   . PHE   B 1 185 ? -16.761 1.054   -18.287 1.00 31.50 ?  185 PHE   B O   1 
ATOM   3672 C  CB  . PHE   B 1 185 ? -16.970 0.937   -14.939 1.00 26.50 ?  185 PHE   B CB  1 
ATOM   3673 C  CG  . PHE   B 1 185 ? -17.059 -0.022  -13.778 1.00 24.94 ?  185 PHE   B CG  1 
ATOM   3674 C  CD1 . PHE   B 1 185 ? -18.253 -0.180  -13.088 1.00 25.87 ?  185 PHE   B CD1 1 
ATOM   3675 C  CD2 . PHE   B 1 185 ? -15.963 -0.781  -13.396 1.00 27.05 ?  185 PHE   B CD2 1 
ATOM   3676 C  CE1 . PHE   B 1 185 ? -18.353 -1.074  -12.030 1.00 24.67 ?  185 PHE   B CE1 1 
ATOM   3677 C  CE2 . PHE   B 1 185 ? -16.051 -1.668  -12.338 1.00 26.32 ?  185 PHE   B CE2 1 
ATOM   3678 C  CZ  . PHE   B 1 185 ? -17.262 -1.815  -11.653 1.00 27.23 ?  185 PHE   B CZ  1 
ATOM   3679 N  N   . VAL   B 1 186 ? -18.184 2.537   -17.349 1.00 24.90 ?  186 VAL   B N   1 
ATOM   3680 C  CA  . VAL   B 1 186 ? -18.120 3.495   -18.449 1.00 27.08 ?  186 VAL   B CA  1 
ATOM   3681 C  C   . VAL   B 1 186 ? -17.973 4.898   -17.876 1.00 25.59 ?  186 VAL   B C   1 
ATOM   3682 O  O   . VAL   B 1 186 ? -18.467 5.193   -16.785 1.00 28.02 ?  186 VAL   B O   1 
ATOM   3683 C  CB  . VAL   B 1 186 ? -19.374 3.413   -19.359 1.00 24.13 ?  186 VAL   B CB  1 
ATOM   3684 C  CG1 . VAL   B 1 186 ? -19.504 2.023   -19.966 1.00 27.87 ?  186 VAL   B CG1 1 
ATOM   3685 C  CG2 . VAL   B 1 186 ? -20.647 3.787   -18.575 1.00 27.22 ?  186 VAL   B CG2 1 
ATOM   3686 N  N   . ASP   B 1 187 ? -17.310 5.779   -18.629 1.00 24.57 ?  187 ASP   B N   1 
ATOM   3687 C  CA  . ASP   B 1 187 ? -17.141 7.163   -18.176 1.00 29.08 ?  187 ASP   B CA  1 
ATOM   3688 C  C   . ASP   B 1 187 ? -18.379 7.975   -18.566 1.00 31.97 ?  187 ASP   B C   1 
ATOM   3689 O  O   . ASP   B 1 187 ? -18.395 8.786   -19.496 1.00 30.07 ?  187 ASP   B O   1 
ATOM   3690 C  CB  . ASP   B 1 187 ? -15.835 7.765   -18.696 1.00 27.20 ?  187 ASP   B CB  1 
ATOM   3691 C  CG  . ASP   B 1 187 ? -15.635 7.598   -20.207 1.00 29.02 ?  187 ASP   B CG  1 
ATOM   3692 O  OD1 . ASP   B 1 187 ? -16.475 6.961   -20.888 1.00 29.45 ?  187 ASP   B OD1 1 
ATOM   3693 O  OD2 . ASP   B 1 187 ? -14.608 8.123   -20.709 1.00 26.72 ?  187 ASP   B OD2 1 
ATOM   3694 N  N   . ARG   B 1 188 ? -19.443 7.724   -17.808 1.00 27.60 ?  188 ARG   B N   1 
ATOM   3695 C  CA  . ARG   B 1 188 ? -20.723 8.389   -17.981 1.00 28.60 ?  188 ARG   B CA  1 
ATOM   3696 C  C   . ARG   B 1 188 ? -21.374 8.480   -16.611 1.00 31.50 ?  188 ARG   B C   1 
ATOM   3697 O  O   . ARG   B 1 188 ? -21.269 7.545   -15.810 1.00 30.43 ?  188 ARG   B O   1 
ATOM   3698 C  CB  . ARG   B 1 188 ? -21.619 7.621   -18.963 1.00 28.25 ?  188 ARG   B CB  1 
ATOM   3699 C  CG  . ARG   B 1 188 ? -23.078 8.098   -19.024 1.00 31.41 ?  188 ARG   B CG  1 
ATOM   3700 C  CD  . ARG   B 1 188 ? -23.885 7.311   -20.069 1.00 36.71 ?  188 ARG   B CD  1 
ATOM   3701 N  NE  . ARG   B 1 188 ? -25.310 7.630   -19.996 1.00 41.93 ?  188 ARG   B NE  1 
ATOM   3702 C  CZ  . ARG   B 1 188 ? -26.270 6.947   -20.614 1.00 46.07 ?  188 ARG   B CZ  1 
ATOM   3703 N  NH1 . ARG   B 1 188 ? -25.972 5.891   -21.362 1.00 42.12 ?  188 ARG   B NH1 1 
ATOM   3704 N  NH2 . ARG   B 1 188 ? -27.536 7.321   -20.481 1.00 48.49 ?  188 ARG   B NH2 1 
ATOM   3705 N  N   . GLN   B 1 189 ? -22.009 9.610   -16.323 1.00 30.08 ?  189 GLN   B N   1 
ATOM   3706 C  CA  . GLN   B 1 189 ? -22.745 9.730   -15.065 1.00 33.84 ?  189 GLN   B CA  1 
ATOM   3707 C  C   . GLN   B 1 189 ? -24.080 9.020   -15.241 1.00 34.97 ?  189 GLN   B C   1 
ATOM   3708 O  O   . GLN   B 1 189 ? -25.061 9.594   -15.714 1.00 33.74 ?  189 GLN   B O   1 
ATOM   3709 C  CB  . GLN   B 1 189 ? -22.939 11.183  -14.659 1.00 35.51 ?  189 GLN   B CB  1 
ATOM   3710 C  CG  . GLN   B 1 189 ? -23.752 11.323  -13.375 1.00 34.21 ?  189 GLN   B CG  1 
ATOM   3711 C  CD  . GLN   B 1 189 ? -23.061 10.665  -12.176 1.00 39.69 ?  189 GLN   B CD  1 
ATOM   3712 O  OE1 . GLN   B 1 189 ? -21.962 11.061  -11.787 1.00 36.32 ?  189 GLN   B OE1 1 
ATOM   3713 N  NE2 . GLN   B 1 189 ? -23.706 9.653   -11.595 1.00 41.18 ?  189 GLN   B NE2 1 
ATOM   3714 N  N   . THR   B 1 190 ? -24.106 7.748   -14.859 1.00 33.67 ?  190 THR   B N   1 
ATOM   3715 C  CA  . THR   B 1 190 ? -25.281 6.906   -14.990 1.00 33.47 ?  190 THR   B CA  1 
ATOM   3716 C  C   . THR   B 1 190 ? -25.214 5.856   -13.890 1.00 37.99 ?  190 THR   B C   1 
ATOM   3717 O  O   . THR   B 1 190 ? -24.211 5.739   -13.184 1.00 36.68 ?  190 THR   B O   1 
ATOM   3718 C  CB  . THR   B 1 190 ? -25.362 6.274   -16.391 1.00 36.60 ?  190 THR   B CB  1 
ATOM   3719 O  OG1 . THR   B 1 190 ? -26.586 5.535   -16.520 1.00 39.74 ?  190 THR   B OG1 1 
ATOM   3720 C  CG2 . THR   B 1 190 ? -24.173 5.341   -16.636 1.00 32.86 ?  190 THR   B CG2 1 
ATOM   3721 N  N   . ALA   B 1 191 ? -26.303 5.104   -13.730 1.00 36.19 ?  191 ALA   B N   1 
ATOM   3722 C  CA  . ALA   B 1 191 ? -26.363 4.087   -12.688 1.00 33.73 ?  191 ALA   B CA  1 
ATOM   3723 C  C   . ALA   B 1 191 ? -25.315 3.004   -12.933 1.00 32.82 ?  191 ALA   B C   1 
ATOM   3724 O  O   . ALA   B 1 191 ? -25.376 2.277   -13.930 1.00 31.32 ?  191 ALA   B O   1 
ATOM   3725 C  CB  . ALA   B 1 191 ? -27.768 3.484   -12.634 1.00 33.64 ?  191 ALA   B CB  1 
ATOM   3726 N  N   . GLN   B 1 192 ? -24.330 2.914   -12.033 1.00 32.21 ?  192 GLN   B N   1 
ATOM   3727 C  CA  . GLN   B 1 192 ? -23.298 1.885   -12.094 1.00 28.66 ?  192 GLN   B CA  1 
ATOM   3728 C  C   . GLN   B 1 192 ? -23.004 1.414   -10.682 1.00 32.38 ?  192 GLN   B C   1 
ATOM   3729 O  O   . GLN   B 1 192 ? -23.125 2.185   -9.730  1.00 27.93 ?  192 GLN   B O   1 
ATOM   3730 C  CB  . GLN   B 1 192 ? -21.998 2.382   -12.724 1.00 28.28 ?  192 GLN   B CB  1 
ATOM   3731 C  CG  . GLN   B 1 192 ? -22.177 3.377   -13.857 1.00 29.19 ?  192 GLN   B CG  1 
ATOM   3732 C  CD  . GLN   B 1 192 ? -20.915 3.548   -14.655 1.00 28.48 ?  192 GLN   B CD  1 
ATOM   3733 O  OE1 . GLN   B 1 192 ? -20.309 2.566   -15.085 1.00 26.58 ?  192 GLN   B OE1 1 
ATOM   3734 N  NE2 . GLN   B 1 192 ? -20.503 4.796   -14.853 1.00 27.96 ?  192 GLN   B NE2 1 
ATOM   3735 N  N   . ALA   B 1 193 ? -22.601 0.152   -10.556 1.00 32.28 ?  193 ALA   B N   1 
ATOM   3736 C  CA  . ALA   B 1 193 ? -22.377 -0.427  -9.238  1.00 36.38 ?  193 ALA   B CA  1 
ATOM   3737 C  C   . ALA   B 1 193 ? -21.304 -1.503  -9.314  1.00 35.23 ?  193 ALA   B C   1 
ATOM   3738 O  O   . ALA   B 1 193 ? -21.182 -2.209  -10.313 1.00 33.88 ?  193 ALA   B O   1 
ATOM   3739 C  CB  . ALA   B 1 193 ? -23.676 -1.016  -8.667  1.00 34.73 ?  193 ALA   B CB  1 
ATOM   3740 N  N   . ALA   B 1 194 ? -20.530 -1.630  -8.241  1.00 38.90 ?  194 ALA   B N   1 
ATOM   3741 C  CA  . ALA   B 1 194 ? -19.572 -2.721  -8.155  1.00 34.33 ?  194 ALA   B CA  1 
ATOM   3742 C  C   . ALA   B 1 194 ? -20.308 -4.045  -7.981  1.00 35.23 ?  194 ALA   B C   1 
ATOM   3743 O  O   . ALA   B 1 194 ? -21.295 -4.129  -7.245  1.00 28.68 ?  194 ALA   B O   1 
ATOM   3744 C  CB  . ALA   B 1 194 ? -18.609 -2.488  -6.989  1.00 33.68 ?  194 ALA   B CB  1 
ATOM   3745 N  N   . GLY   B 1 195 ? -19.839 -5.080  -8.670  1.00 35.96 ?  195 GLY   B N   1 
ATOM   3746 C  CA  . GLY   B 1 195 ? -20.380 -6.408  -8.471  1.00 34.30 ?  195 GLY   B CA  1 
ATOM   3747 C  C   . GLY   B 1 195 ? -19.966 -6.987  -7.127  1.00 42.05 ?  195 GLY   B C   1 
ATOM   3748 O  O   . GLY   B 1 195 ? -19.191 -6.408  -6.362  1.00 37.24 ?  195 GLY   B O   1 
ATOM   3749 N  N   . THR   B 1 196 ? -20.507 -8.167  -6.832  1.00 36.91 ?  196 THR   B N   1 
ATOM   3750 C  CA  . THR   B 1 196 ? -20.058 -8.887  -5.651  1.00 36.73 ?  196 THR   B CA  1 
ATOM   3751 C  C   . THR   B 1 196 ? -18.592 -9.272  -5.814  1.00 33.38 ?  196 THR   B C   1 
ATOM   3752 O  O   . THR   B 1 196 ? -18.165 -9.733  -6.875  1.00 30.26 ?  196 THR   B O   1 
ATOM   3753 C  CB  . THR   B 1 196 ? -20.908 -10.135 -5.421  1.00 41.14 ?  196 THR   B CB  1 
ATOM   3754 O  OG1 . THR   B 1 196 ? -20.800 -10.991 -6.566  1.00 41.86 ?  196 THR   B OG1 1 
ATOM   3755 C  CG2 . THR   B 1 196 ? -22.369 -9.756  -5.204  1.00 33.91 ?  196 THR   B CG2 1 
ATOM   3756 N  N   . ASP   B 1 197 ? -17.826 -9.063  -4.754  1.00 33.09 ?  197 ASP   B N   1 
ATOM   3757 C  CA  . ASP   B 1 197 ? -16.396 -9.315  -4.726  1.00 36.40 ?  197 ASP   B CA  1 
ATOM   3758 C  C   . ASP   B 1 197 ? -16.096 -10.660 -4.072  1.00 37.78 ?  197 ASP   B C   1 
ATOM   3759 O  O   . ASP   B 1 197 ? -16.915 -11.225 -3.344  1.00 37.90 ?  197 ASP   B O   1 
ATOM   3760 C  CB  . ASP   B 1 197 ? -15.683 -8.195  -3.971  1.00 35.76 ?  197 ASP   B CB  1 
ATOM   3761 C  CG  . ASP   B 1 197 ? -14.286 -7.938  -4.488  1.00 39.60 ?  197 ASP   B CG  1 
ATOM   3762 O  OD1 . ASP   B 1 197 ? -13.950 -8.422  -5.598  1.00 34.13 ?  197 ASP   B OD1 1 
ATOM   3763 O  OD2 . ASP   B 1 197 ? -13.525 -7.247  -3.777  1.00 33.78 ?  197 ASP   B OD2 1 
ATOM   3764 N  N   . THR   B 1 198 ? -14.903 -11.175 -4.345  1.00 39.65 ?  198 THR   B N   1 
ATOM   3765 C  CA  . THR   B 1 198 ? -14.418 -12.390 -3.709  1.00 35.64 ?  198 THR   B CA  1 
ATOM   3766 C  C   . THR   B 1 198 ? -13.020 -12.135 -3.153  1.00 35.40 ?  198 THR   B C   1 
ATOM   3767 O  O   . THR   B 1 198 ? -12.430 -11.070 -3.357  1.00 34.91 ?  198 THR   B O   1 
ATOM   3768 C  CB  . THR   B 1 198 ? -14.416 -13.572 -4.690  1.00 36.67 ?  198 THR   B CB  1 
ATOM   3769 O  OG1 . THR   B 1 198 ? -13.560 -13.276 -5.796  1.00 39.33 ?  198 THR   B OG1 1 
ATOM   3770 C  CG2 . THR   B 1 198 ? -15.823 -13.841 -5.215  1.00 38.27 ?  198 THR   B CG2 1 
ATOM   3771 N  N   . THR   B 1 199 ? -12.485 -13.118 -2.437  1.00 36.34 ?  199 THR   B N   1 
ATOM   3772 C  CA  . THR   B 1 199 ? -11.179 -12.982 -1.807  1.00 33.32 ?  199 THR   B CA  1 
ATOM   3773 C  C   . THR   B 1 199 ? -10.115 -13.687 -2.639  1.00 34.14 ?  199 THR   B C   1 
ATOM   3774 O  O   . THR   B 1 199 ? -10.321 -14.810 -3.104  1.00 35.04 ?  199 THR   B O   1 
ATOM   3775 C  CB  . THR   B 1 199 ? -11.193 -13.548 -0.384  1.00 33.04 ?  199 THR   B CB  1 
ATOM   3776 O  OG1 . THR   B 1 199 ? -12.185 -12.863 0.386   1.00 31.58 ?  199 THR   B OG1 1 
ATOM   3777 C  CG2 . THR   B 1 199 ? -9.837  -13.356 0.282   1.00 30.25 ?  199 THR   B CG2 1 
ATOM   3778 N  N   . ILE   B 1 200 ? -8.964  -13.032 -2.791  1.00 33.17 ?  200 ILE   B N   1 
ATOM   3779 C  CA  . ILE   B 1 200 ? -7.885  -13.503 -3.661  1.00 33.53 ?  200 ILE   B CA  1 
ATOM   3780 C  C   . ILE   B 1 200 ? -7.102  -14.572 -2.899  1.00 35.26 ?  200 ILE   B C   1 
ATOM   3781 O  O   . ILE   B 1 200 ? -6.180  -14.267 -2.137  1.00 33.13 ?  200 ILE   B O   1 
ATOM   3782 C  CB  . ILE   B 1 200 ? -6.990  -12.350 -4.121  1.00 31.22 ?  200 ILE   B CB  1 
ATOM   3783 C  CG1 . ILE   B 1 200 ? -7.853  -11.234 -4.719  1.00 34.62 ?  200 ILE   B CG1 1 
ATOM   3784 C  CG2 . ILE   B 1 200 ? -5.972  -12.831 -5.144  1.00 29.95 ?  200 ILE   B CG2 1 
ATOM   3785 C  CD1 . ILE   B 1 200 ? -7.231  -9.851  -4.641  1.00 32.28 ?  200 ILE   B CD1 1 
ATOM   3786 N  N   . THR   B 1 201 ? -7.448  -15.841 -3.141  1.00 30.98 ?  201 THR   B N   1 
ATOM   3787 C  CA  . THR   B 1 201 ? -6.957  -16.937 -2.312  1.00 35.07 ?  201 THR   B CA  1 
ATOM   3788 C  C   . THR   B 1 201 ? -5.442  -17.088 -2.387  1.00 35.62 ?  201 THR   B C   1 
ATOM   3789 O  O   . THR   B 1 201 ? -4.791  -17.356 -1.368  1.00 33.89 ?  201 THR   B O   1 
ATOM   3790 C  CB  . THR   B 1 201 ? -7.641  -18.240 -2.716  1.00 37.87 ?  201 THR   B CB  1 
ATOM   3791 O  OG1 . THR   B 1 201 ? -9.054  -18.093 -2.555  1.00 36.11 ?  201 THR   B OG1 1 
ATOM   3792 C  CG2 . THR   B 1 201 ? -7.154  -19.389 -1.844  1.00 33.42 ?  201 THR   B CG2 1 
ATOM   3793 N  N   . VAL   B 1 202 ? -4.855  -16.946 -3.577  1.00 29.65 ?  202 VAL   B N   1 
ATOM   3794 C  CA  . VAL   B 1 202 ? -3.403  -17.091 -3.666  1.00 32.20 ?  202 VAL   B CA  1 
ATOM   3795 C  C   . VAL   B 1 202 ? -2.705  -16.035 -2.809  1.00 30.28 ?  202 VAL   B C   1 
ATOM   3796 O  O   . VAL   B 1 202 ? -1.676  -16.307 -2.176  1.00 28.45 ?  202 VAL   B O   1 
ATOM   3797 C  CB  . VAL   B 1 202 ? -2.943  -17.043 -5.133  1.00 33.39 ?  202 VAL   B CB  1 
ATOM   3798 C  CG1 . VAL   B 1 202 ? -3.311  -15.717 -5.767  1.00 33.71 ?  202 VAL   B CG1 1 
ATOM   3799 C  CG2 . VAL   B 1 202 ? -1.437  -17.302 -5.222  1.00 33.64 ?  202 VAL   B CG2 1 
ATOM   3800 N  N   . ASN   B 1 203 ? -3.268  -14.826 -2.747  1.00 29.15 ?  203 ASN   B N   1 
ATOM   3801 C  CA  . ASN   B 1 203 ? -2.651  -13.770 -1.955  1.00 29.51 ?  203 ASN   B CA  1 
ATOM   3802 C  C   . ASN   B 1 203 ? -2.774  -14.051 -0.461  1.00 29.14 ?  203 ASN   B C   1 
ATOM   3803 O  O   . ASN   B 1 203 ? -1.853  -13.742 0.304   1.00 26.18 ?  203 ASN   B O   1 
ATOM   3804 C  CB  . ASN   B 1 203 ? -3.268  -12.416 -2.298  1.00 25.64 ?  203 ASN   B CB  1 
ATOM   3805 C  CG  . ASN   B 1 203 ? -2.854  -11.915 -3.671  1.00 28.60 ?  203 ASN   B CG  1 
ATOM   3806 O  OD1 . ASN   B 1 203 ? -2.212  -12.629 -4.441  1.00 30.41 ?  203 ASN   B OD1 1 
ATOM   3807 N  ND2 . ASN   B 1 203 ? -3.220  -10.677 -3.981  1.00 27.83 ?  203 ASN   B ND2 1 
ATOM   3808 N  N   . VAL   B 1 204 ? -3.901  -14.628 -0.023  1.00 28.73 ?  204 VAL   B N   1 
ATOM   3809 C  CA  . VAL   B 1 204 ? -4.054  -14.970 1.394   1.00 30.87 ?  204 VAL   B CA  1 
ATOM   3810 C  C   . VAL   B 1 204 ? -3.018  -16.009 1.807   1.00 31.92 ?  204 VAL   B C   1 
ATOM   3811 O  O   . VAL   B 1 204 ? -2.409  -15.911 2.881   1.00 32.60 ?  204 VAL   B O   1 
ATOM   3812 C  CB  . VAL   B 1 204 ? -5.486  -15.457 1.690   1.00 31.89 ?  204 VAL   B CB  1 
ATOM   3813 C  CG1 . VAL   B 1 204 ? -5.587  -15.984 3.124   1.00 35.34 ?  204 VAL   B CG1 1 
ATOM   3814 C  CG2 . VAL   B 1 204 ? -6.480  -14.338 1.502   1.00 30.46 ?  204 VAL   B CG2 1 
ATOM   3815 N  N   . LEU   B 1 205 ? -2.808  -17.025 0.966   1.00 28.68 ?  205 LEU   B N   1 
ATOM   3816 C  CA  . LEU   B 1 205 ? -1.804  -18.042 1.262   1.00 35.76 ?  205 LEU   B CA  1 
ATOM   3817 C  C   . LEU   B 1 205 ? -0.402  -17.445 1.305   1.00 35.83 ?  205 LEU   B C   1 
ATOM   3818 O  O   . LEU   B 1 205 ? 0.411   -17.816 2.162   1.00 34.66 ?  205 LEU   B O   1 
ATOM   3819 C  CB  . LEU   B 1 205 ? -1.880  -19.168 0.229   1.00 35.13 ?  205 LEU   B CB  1 
ATOM   3820 C  CG  . LEU   B 1 205 ? -3.150  -20.020 0.295   1.00 34.76 ?  205 LEU   B CG  1 
ATOM   3821 C  CD1 . LEU   B 1 205 ? -3.317  -20.861 -0.960  1.00 37.53 ?  205 LEU   B CD1 1 
ATOM   3822 C  CD2 . LEU   B 1 205 ? -3.130  -20.908 1.526   1.00 38.50 ?  205 LEU   B CD2 1 
ATOM   3823 N  N   . ALA   B 1 206 ? -0.096  -16.525 0.384   1.00 31.62 ?  206 ALA   B N   1 
ATOM   3824 C  CA  . ALA   B 1 206 ? 1.197   -15.848 0.422   1.00 32.65 ?  206 ALA   B CA  1 
ATOM   3825 C  C   . ALA   B 1 206 ? 1.384   -15.102 1.735   1.00 36.13 ?  206 ALA   B C   1 
ATOM   3826 O  O   . ALA   B 1 206 ? 2.468   -15.134 2.331   1.00 35.56 ?  206 ALA   B O   1 
ATOM   3827 C  CB  . ALA   B 1 206 ? 1.326   -14.886 -0.759  1.00 31.79 ?  206 ALA   B CB  1 
ATOM   3828 N  N   . TRP   B 1 207 ? 0.331   -14.428 2.205   1.00 30.59 ?  207 TRP   B N   1 
ATOM   3829 C  CA  . TRP   B 1 207 ? 0.412   -13.674 3.454   1.00 32.50 ?  207 TRP   B CA  1 
ATOM   3830 C  C   . TRP   B 1 207 ? 0.532   -14.597 4.664   1.00 35.53 ?  207 TRP   B C   1 
ATOM   3831 O  O   . TRP   B 1 207 ? 1.174   -14.233 5.660   1.00 31.79 ?  207 TRP   B O   1 
ATOM   3832 C  CB  . TRP   B 1 207 ? -0.812  -12.764 3.551   1.00 33.30 ?  207 TRP   B CB  1 
ATOM   3833 C  CG  . TRP   B 1 207 ? -1.020  -12.000 4.825   1.00 32.16 ?  207 TRP   B CG  1 
ATOM   3834 C  CD1 . TRP   B 1 207 ? -0.396  -10.846 5.212   1.00 30.72 ?  207 TRP   B CD1 1 
ATOM   3835 C  CD2 . TRP   B 1 207 ? -1.978  -12.295 5.837   1.00 30.47 ?  207 TRP   B CD2 1 
ATOM   3836 N  NE1 . TRP   B 1 207 ? -0.892  -10.425 6.420   1.00 32.92 ?  207 TRP   B NE1 1 
ATOM   3837 C  CE2 . TRP   B 1 207 ? -1.867  -11.298 6.824   1.00 34.37 ?  207 TRP   B CE2 1 
ATOM   3838 C  CE3 . TRP   B 1 207 ? -2.919  -13.313 6.008   1.00 33.31 ?  207 TRP   B CE3 1 
ATOM   3839 C  CZ2 . TRP   B 1 207 ? -2.661  -11.291 7.969   1.00 35.39 ?  207 TRP   B CZ2 1 
ATOM   3840 C  CZ3 . TRP   B 1 207 ? -3.701  -13.307 7.141   1.00 33.39 ?  207 TRP   B CZ3 1 
ATOM   3841 C  CH2 . TRP   B 1 207 ? -3.571  -12.302 8.107   1.00 33.37 ?  207 TRP   B CH2 1 
ATOM   3842 N  N   . LEU   B 1 208 ? -0.057  -15.794 4.595   1.00 33.32 ?  208 LEU   B N   1 
ATOM   3843 C  CA  . LEU   B 1 208 ? 0.163   -16.783 5.646   1.00 31.15 ?  208 LEU   B CA  1 
ATOM   3844 C  C   . LEU   B 1 208 ? 1.612   -17.270 5.655   1.00 32.02 ?  208 LEU   B C   1 
ATOM   3845 O  O   . LEU   B 1 208 ? 2.158   -17.586 6.717   1.00 33.99 ?  208 LEU   B O   1 
ATOM   3846 C  CB  . LEU   B 1 208 ? -0.804  -17.955 5.478   1.00 33.49 ?  208 LEU   B CB  1 
ATOM   3847 C  CG  . LEU   B 1 208 ? -2.294  -17.667 5.699   1.00 27.88 ?  208 LEU   B CG  1 
ATOM   3848 C  CD1 . LEU   B 1 208 ? -3.102  -18.955 5.654   1.00 34.46 ?  208 LEU   B CD1 1 
ATOM   3849 C  CD2 . LEU   B 1 208 ? -2.516  -16.950 7.022   1.00 32.35 ?  208 LEU   B CD2 1 
ATOM   3850 N  N   . TYR   B 1 209 ? 2.250   -17.358 4.480   1.00 31.48 ?  209 TYR   B N   1 
ATOM   3851 C  CA  . TYR   B 1 209 ? 3.683   -17.647 4.455   1.00 34.55 ?  209 TYR   B CA  1 
ATOM   3852 C  C   . TYR   B 1 209 ? 4.485   -16.509 5.080   1.00 35.54 ?  209 TYR   B C   1 
ATOM   3853 O  O   . TYR   B 1 209 ? 5.429   -16.752 5.843   1.00 36.24 ?  209 TYR   B O   1 
ATOM   3854 C  CB  . TYR   B 1 209 ? 4.153   -17.916 3.025   1.00 36.72 ?  209 TYR   B CB  1 
ATOM   3855 C  CG  . TYR   B 1 209 ? 3.888   -19.332 2.568   1.00 34.29 ?  209 TYR   B CG  1 
ATOM   3856 C  CD1 . TYR   B 1 209 ? 4.624   -20.390 3.079   1.00 34.88 ?  209 TYR   B CD1 1 
ATOM   3857 C  CD2 . TYR   B 1 209 ? 2.901   -19.611 1.635   1.00 34.18 ?  209 TYR   B CD2 1 
ATOM   3858 C  CE1 . TYR   B 1 209 ? 4.390   -21.685 2.675   1.00 39.79 ?  209 TYR   B CE1 1 
ATOM   3859 C  CE2 . TYR   B 1 209 ? 2.660   -20.905 1.219   1.00 37.23 ?  209 TYR   B CE2 1 
ATOM   3860 C  CZ  . TYR   B 1 209 ? 3.406   -21.937 1.745   1.00 40.51 ?  209 TYR   B CZ  1 
ATOM   3861 O  OH  . TYR   B 1 209 ? 3.168   -23.229 1.339   1.00 44.30 ?  209 TYR   B OH  1 
ATOM   3862 N  N   . ALA   B 1 210 ? 4.113   -15.261 4.785   1.00 31.56 ?  210 ALA   B N   1 
ATOM   3863 C  CA  . ALA   B 1 210 ? 4.777   -14.120 5.410   1.00 32.66 ?  210 ALA   B CA  1 
ATOM   3864 C  C   . ALA   B 1 210 ? 4.689   -14.178 6.935   1.00 37.59 ?  210 ALA   B C   1 
ATOM   3865 O  O   . ALA   B 1 210 ? 5.659   -13.849 7.631   1.00 37.91 ?  210 ALA   B O   1 
ATOM   3866 C  CB  . ALA   B 1 210 ? 4.177   -12.816 4.887   1.00 32.74 ?  210 ALA   B CB  1 
ATOM   3867 N  N   . ALA   B 1 211 ? 3.531   -14.579 7.474   1.00 32.26 ?  211 ALA   B N   1 
ATOM   3868 C  CA  . ALA   B 1 211 ? 3.380   -14.676 8.923   1.00 31.57 ?  211 ALA   B CA  1 
ATOM   3869 C  C   . ALA   B 1 211 ? 4.260   -15.776 9.503   1.00 35.98 ?  211 ALA   B C   1 
ATOM   3870 O  O   . ALA   B 1 211 ? 4.862   -15.596 10.566  1.00 40.87 ?  211 ALA   B O   1 
ATOM   3871 C  CB  . ALA   B 1 211 ? 1.917   -14.918 9.287   1.00 33.48 ?  211 ALA   B CB  1 
ATOM   3872 N  N   . VAL   B 1 212 ? 4.338   -16.925 8.830   1.00 36.62 ?  212 VAL   B N   1 
ATOM   3873 C  CA  . VAL   B 1 212 ? 5.221   -17.996 9.292   1.00 37.38 ?  212 VAL   B CA  1 
ATOM   3874 C  C   . VAL   B 1 212 ? 6.679   -17.546 9.250   1.00 37.21 ?  212 VAL   B C   1 
ATOM   3875 O  O   . VAL   B 1 212 ? 7.455   -17.812 10.178  1.00 38.35 ?  212 VAL   B O   1 
ATOM   3876 C  CB  . VAL   B 1 212 ? 4.990   -19.271 8.459   1.00 36.85 ?  212 VAL   B CB  1 
ATOM   3877 C  CG1 . VAL   B 1 212 ? 6.139   -20.247 8.643   1.00 35.20 ?  212 VAL   B CG1 1 
ATOM   3878 C  CG2 . VAL   B 1 212 ? 3.674   -19.920 8.846   1.00 37.33 ?  212 VAL   B CG2 1 
ATOM   3879 N  N   . ILE   B 1 213 ? 7.073   -16.853 8.177   1.00 34.84 ?  213 ILE   B N   1 
ATOM   3880 C  CA  . ILE   B 1 213 ? 8.411   -16.270 8.104   1.00 40.46 ?  213 ILE   B CA  1 
ATOM   3881 C  C   . ILE   B 1 213 ? 8.665   -15.348 9.287   1.00 41.43 ?  213 ILE   B C   1 
ATOM   3882 O  O   . ILE   B 1 213 ? 9.788   -15.279 9.804   1.00 43.16 ?  213 ILE   B O   1 
ATOM   3883 C  CB  . ILE   B 1 213 ? 8.590   -15.529 6.764   1.00 37.01 ?  213 ILE   B CB  1 
ATOM   3884 C  CG1 . ILE   B 1 213 ? 8.573   -16.520 5.600   1.00 34.35 ?  213 ILE   B CG1 1 
ATOM   3885 C  CG2 . ILE   B 1 213 ? 9.881   -14.714 6.759   1.00 41.55 ?  213 ILE   B CG2 1 
ATOM   3886 C  CD1 . ILE   B 1 213 ? 8.615   -15.863 4.241   1.00 42.63 ?  213 ILE   B CD1 1 
ATOM   3887 N  N   . ASN   B 1 214 ? 7.633   -14.646 9.750   1.00 39.79 ?  214 ASN   B N   1 
ATOM   3888 C  CA  . ASN   B 1 214 ? 7.753   -13.712 10.862  1.00 40.53 ?  214 ASN   B CA  1 
ATOM   3889 C  C   . ASN   B 1 214 ? 7.390   -14.322 12.212  1.00 40.49 ?  214 ASN   B C   1 
ATOM   3890 O  O   . ASN   B 1 214 ? 7.199   -13.577 13.179  1.00 38.22 ?  214 ASN   B O   1 
ATOM   3891 C  CB  . ASN   B 1 214 ? 6.885   -12.479 10.605  1.00 36.92 ?  214 ASN   B CB  1 
ATOM   3892 C  CG  . ASN   B 1 214 ? 7.552   -11.485 9.679   1.00 44.10 ?  214 ASN   B CG  1 
ATOM   3893 O  OD1 . ASN   B 1 214 ? 8.352   -10.659 10.120  1.00 44.64 ?  214 ASN   B OD1 1 
ATOM   3894 N  ND2 . ASN   B 1 214 ? 7.233   -11.558 8.388   1.00 43.63 ?  214 ASN   B ND2 1 
ATOM   3895 N  N   . GLY   B 1 215 ? 7.274   -15.645 12.306  1.00 39.62 ?  215 GLY   B N   1 
ATOM   3896 C  CA  . GLY   B 1 215 ? 7.144   -16.289 13.599  1.00 43.01 ?  215 GLY   B CA  1 
ATOM   3897 C  C   . GLY   B 1 215 ? 5.740   -16.603 14.078  1.00 43.23 ?  215 GLY   B C   1 
ATOM   3898 O  O   . GLY   B 1 215 ? 5.597   -17.216 15.142  1.00 49.08 ?  215 GLY   B O   1 
ATOM   3899 N  N   . ASP   B 1 216 ? 4.699   -16.200 13.352  1.00 42.19 ?  216 ASP   B N   1 
ATOM   3900 C  CA  . ASP   B 1 216 ? 3.329   -16.582 13.690  1.00 43.74 ?  216 ASP   B CA  1 
ATOM   3901 C  C   . ASP   B 1 216 ? 3.061   -17.966 13.108  1.00 45.54 ?  216 ASP   B C   1 
ATOM   3902 O  O   . ASP   B 1 216 ? 3.021   -18.129 11.885  1.00 47.93 ?  216 ASP   B O   1 
ATOM   3903 C  CB  . ASP   B 1 216 ? 2.327   -15.565 13.147  1.00 46.37 ?  216 ASP   B CB  1 
ATOM   3904 C  CG  . ASP   B 1 216 ? 2.096   -14.406 14.094  1.00 50.48 ?  216 ASP   B CG  1 
ATOM   3905 O  OD1 . ASP   B 1 216 ? 2.209   -14.610 15.321  1.00 55.29 ?  216 ASP   B OD1 1 
ATOM   3906 O  OD2 . ASP   B 1 216 ? 1.790   -13.295 13.610  1.00 49.08 ?  216 ASP   B OD2 1 
ATOM   3907 N  N   . ARG   B 1 217 ? 2.863   -18.963 13.977  1.00 46.27 ?  217 ARG   B N   1 
ATOM   3908 C  CA  . ARG   B 1 217 ? 2.715   -20.343 13.528  1.00 46.10 ?  217 ARG   B CA  1 
ATOM   3909 C  C   . ARG   B 1 217 ? 1.521   -21.062 14.149  1.00 46.29 ?  217 ARG   B C   1 
ATOM   3910 O  O   . ARG   B 1 217 ? 1.345   -22.262 13.903  1.00 46.57 ?  217 ARG   B O   1 
ATOM   3911 C  CB  . ARG   B 1 217 ? 3.995   -21.140 13.816  1.00 49.00 ?  217 ARG   B CB  1 
ATOM   3912 N  N   . TRP   B 1 218 ? 0.690   -20.368 14.932  1.00 45.53 ?  218 TRP   B N   1 
ATOM   3913 C  CA  . TRP   B 1 218 ? -0.367  -21.050 15.671  1.00 43.46 ?  218 TRP   B CA  1 
ATOM   3914 C  C   . TRP   B 1 218 ? -1.420  -21.674 14.765  1.00 44.19 ?  218 TRP   B C   1 
ATOM   3915 O  O   . TRP   B 1 218 ? -2.110  -22.604 15.196  1.00 44.65 ?  218 TRP   B O   1 
ATOM   3916 C  CB  . TRP   B 1 218 ? -1.038  -20.089 16.650  1.00 44.29 ?  218 TRP   B CB  1 
ATOM   3917 C  CG  . TRP   B 1 218 ? -1.669  -18.878 16.026  1.00 42.21 ?  218 TRP   B CG  1 
ATOM   3918 C  CD1 . TRP   B 1 218 ? -1.129  -17.630 15.943  1.00 42.25 ?  218 TRP   B CD1 1 
ATOM   3919 C  CD2 . TRP   B 1 218 ? -2.973  -18.791 15.433  1.00 43.50 ?  218 TRP   B CD2 1 
ATOM   3920 N  NE1 . TRP   B 1 218 ? -2.009  -16.772 15.324  1.00 40.25 ?  218 TRP   B NE1 1 
ATOM   3921 C  CE2 . TRP   B 1 218 ? -3.148  -17.461 15.003  1.00 43.57 ?  218 TRP   B CE2 1 
ATOM   3922 C  CE3 . TRP   B 1 218 ? -4.009  -19.710 15.219  1.00 41.58 ?  218 TRP   B CE3 1 
ATOM   3923 C  CZ2 . TRP   B 1 218 ? -4.311  -17.027 14.368  1.00 44.21 ?  218 TRP   B CZ2 1 
ATOM   3924 C  CZ3 . TRP   B 1 218 ? -5.159  -19.278 14.593  1.00 42.55 ?  218 TRP   B CZ3 1 
ATOM   3925 C  CH2 . TRP   B 1 218 ? -5.302  -17.949 14.172  1.00 45.57 ?  218 TRP   B CH2 1 
ATOM   3926 N  N   . PHE   B 1 219 ? -1.563  -21.196 13.527  1.00 43.84 ?  219 PHE   B N   1 
ATOM   3927 C  CA  . PHE   B 1 219 ? -2.610  -21.683 12.635  1.00 44.15 ?  219 PHE   B CA  1 
ATOM   3928 C  C   . PHE   B 1 219 ? -2.181  -22.888 11.804  1.00 48.83 ?  219 PHE   B C   1 
ATOM   3929 O  O   . PHE   B 1 219 ? -3.019  -23.464 11.101  1.00 45.49 ?  219 PHE   B O   1 
ATOM   3930 C  CB  . PHE   B 1 219 ? -3.078  -20.555 11.704  1.00 40.84 ?  219 PHE   B CB  1 
ATOM   3931 C  CG  . PHE   B 1 219 ? -1.963  -19.917 10.921  1.00 38.30 ?  219 PHE   B CG  1 
ATOM   3932 C  CD1 . PHE   B 1 219 ? -1.497  -20.498 9.750   1.00 40.57 ?  219 PHE   B CD1 1 
ATOM   3933 C  CD2 . PHE   B 1 219 ? -1.375  -18.740 11.358  1.00 38.59 ?  219 PHE   B CD2 1 
ATOM   3934 C  CE1 . PHE   B 1 219 ? -0.462  -19.922 9.034   1.00 42.84 ?  219 PHE   B CE1 1 
ATOM   3935 C  CE2 . PHE   B 1 219 ? -0.337  -18.157 10.641  1.00 42.49 ?  219 PHE   B CE2 1 
ATOM   3936 C  CZ  . PHE   B 1 219 ? 0.117   -18.750 9.478   1.00 38.21 ?  219 PHE   B CZ  1 
ATOM   3937 N  N   . LEU   B 1 220 ? -0.906  -23.267 11.839  1.00 44.35 ?  220 LEU   B N   1 
ATOM   3938 C  CA  . LEU   B 1 220 ? -0.487  -24.509 11.206  1.00 45.88 ?  220 LEU   B CA  1 
ATOM   3939 C  C   . LEU   B 1 220 ? -1.084  -25.692 11.957  1.00 51.20 ?  220 LEU   B C   1 
ATOM   3940 O  O   . LEU   B 1 220 ? -1.191  -25.673 13.186  1.00 47.47 ?  220 LEU   B O   1 
ATOM   3941 C  CB  . LEU   B 1 220 ? 1.038   -24.610 11.189  1.00 41.79 ?  220 LEU   B CB  1 
ATOM   3942 C  CG  . LEU   B 1 220 ? 1.814   -23.559 10.394  1.00 45.78 ?  220 LEU   B CG  1 
ATOM   3943 C  CD1 . LEU   B 1 220 ? 3.282   -23.552 10.808  1.00 44.35 ?  220 LEU   B CD1 1 
ATOM   3944 C  CD2 . LEU   B 1 220 ? 1.683   -23.817 8.901   1.00 46.31 ?  220 LEU   B CD2 1 
ATOM   3945 N  N   . ASN   B 1 221 ? -1.486  -26.727 11.220  1.00 54.25 ?  221 ASN   B N   1 
ATOM   3946 C  CA  . ASN   B 1 221 ? -2.122  -27.880 11.842  1.00 55.61 ?  221 ASN   B CA  1 
ATOM   3947 C  C   . ASN   B 1 221 ? -1.569  -29.163 11.234  1.00 56.90 ?  221 ASN   B C   1 
ATOM   3948 O  O   . ASN   B 1 221 ? -0.773  -29.141 10.291  1.00 52.37 ?  221 ASN   B O   1 
ATOM   3949 C  CB  . ASN   B 1 221 ? -3.653  -27.807 11.724  1.00 53.57 ?  221 ASN   B CB  1 
ATOM   3950 C  CG  . ASN   B 1 221 ? -4.140  -27.705 10.287  1.00 53.41 ?  221 ASN   B CG  1 
ATOM   3951 O  OD1 . ASN   B 1 221 ? -3.511  -28.204 9.351   1.00 51.77 ?  221 ASN   B OD1 1 
ATOM   3952 N  ND2 . ASN   B 1 221 ? -5.287  -27.062 10.112  1.00 53.92 ?  221 ASN   B ND2 1 
ATOM   3953 N  N   . ARG   B 1 222 ? -2.008  -30.294 11.794  1.00 61.86 ?  222 ARG   B N   1 
ATOM   3954 C  CA  . ARG   B 1 222 ? -1.546  -31.607 11.361  1.00 64.03 ?  222 ARG   B CA  1 
ATOM   3955 C  C   . ARG   B 1 222 ? -2.210  -32.078 10.072  1.00 60.04 ?  222 ARG   B C   1 
ATOM   3956 O  O   . ARG   B 1 222 ? -1.668  -32.961 9.399   1.00 65.37 ?  222 ARG   B O   1 
ATOM   3957 C  CB  . ARG   B 1 222 ? -1.795  -32.636 12.469  1.00 58.20 ?  222 ARG   B CB  1 
ATOM   3958 N  N   . PHE   B 1 223 ? -3.350  -31.501 9.705   1.00 63.80 ?  223 PHE   B N   1 
ATOM   3959 C  CA  . PHE   B 1 223 ? -4.147  -32.028 8.608   1.00 58.69 ?  223 PHE   B CA  1 
ATOM   3960 C  C   . PHE   B 1 223 ? -3.502  -31.739 7.252   1.00 60.22 ?  223 PHE   B C   1 
ATOM   3961 O  O   . PHE   B 1 223 ? -2.581  -30.927 7.120   1.00 61.65 ?  223 PHE   B O   1 
ATOM   3962 C  CB  . PHE   B 1 223 ? -5.558  -31.441 8.651   1.00 50.62 ?  223 PHE   B CB  1 
ATOM   3963 N  N   . THR   B 1 224 ? -3.997  -32.446 6.237   1.00 59.11 ?  224 THR   B N   1 
ATOM   3964 C  CA  . THR   B 1 224 ? -3.678  -32.204 4.839   1.00 59.66 ?  224 THR   B CA  1 
ATOM   3965 C  C   . THR   B 1 224 ? -4.987  -32.162 4.059   1.00 58.05 ?  224 THR   B C   1 
ATOM   3966 O  O   . THR   B 1 224 ? -6.059  -32.457 4.596   1.00 62.72 ?  224 THR   B O   1 
ATOM   3967 C  CB  . THR   B 1 224 ? -2.738  -33.279 4.271   1.00 56.16 ?  224 THR   B CB  1 
ATOM   3968 N  N   . THR   B 1 225 ? -4.906  -31.779 2.786   1.00 62.35 ?  225 THR   B N   1 
ATOM   3969 C  CA  . THR   B 1 225 ? -6.110  -31.635 1.975   1.00 60.87 ?  225 THR   B CA  1 
ATOM   3970 C  C   . THR   B 1 225 ? -5.731  -31.672 0.502   1.00 59.42 ?  225 THR   B C   1 
ATOM   3971 O  O   . THR   B 1 225 ? -4.635  -31.250 0.121   1.00 61.82 ?  225 THR   B O   1 
ATOM   3972 C  CB  . THR   B 1 225 ? -6.856  -30.330 2.308   1.00 60.68 ?  225 THR   B CB  1 
ATOM   3973 O  OG1 . THR   B 1 225 ? -7.226  -30.325 3.695   1.00 64.70 ?  225 THR   B OG1 1 
ATOM   3974 C  CG2 . THR   B 1 225 ? -8.121  -30.179 1.467   1.00 61.25 ?  225 THR   B CG2 1 
ATOM   3975 N  N   . THR   B 1 226 ? -6.643  -32.196 -0.317  1.00 60.55 ?  226 THR   B N   1 
ATOM   3976 C  CA  . THR   B 1 226 ? -6.504  -32.138 -1.763  1.00 61.43 ?  226 THR   B CA  1 
ATOM   3977 C  C   . THR   B 1 226 ? -6.908  -30.761 -2.281  1.00 60.64 ?  226 THR   B C   1 
ATOM   3978 O  O   . THR   B 1 226 ? -7.679  -30.031 -1.650  1.00 61.84 ?  226 THR   B O   1 
ATOM   3979 C  CB  . THR   B 1 226 ? -7.361  -33.211 -2.438  1.00 56.74 ?  226 THR   B CB  1 
ATOM   3980 N  N   . LEU   B 1 227 ? -6.377  -30.411 -3.455  1.00 57.96 ?  227 LEU   B N   1 
ATOM   3981 C  CA  . LEU   B 1 227 ? -6.710  -29.123 -4.056  1.00 54.49 ?  227 LEU   B CA  1 
ATOM   3982 C  C   . LEU   B 1 227 ? -8.203  -29.021 -4.347  1.00 59.94 ?  227 LEU   B C   1 
ATOM   3983 O  O   . LEU   B 1 227 ? -8.822  -27.981 -4.090  1.00 61.17 ?  227 LEU   B O   1 
ATOM   3984 C  CB  . LEU   B 1 227 ? -5.890  -28.912 -5.328  1.00 56.87 ?  227 LEU   B CB  1 
ATOM   3985 C  CG  . LEU   B 1 227 ? -6.127  -27.641 -6.149  1.00 59.28 ?  227 LEU   B CG  1 
ATOM   3986 C  CD1 . LEU   B 1 227 ? -6.258  -26.414 -5.258  1.00 59.43 ?  227 LEU   B CD1 1 
ATOM   3987 C  CD2 . LEU   B 1 227 ? -4.988  -27.453 -7.136  1.00 53.55 ?  227 LEU   B CD2 1 
ATOM   3988 N  N   . ASN   B 1 228 ? -8.803  -30.094 -4.869  1.00 61.08 ?  228 ASN   B N   1 
ATOM   3989 C  CA  . ASN   B 1 228 ? -10.241 -30.076 -5.121  1.00 57.29 ?  228 ASN   B CA  1 
ATOM   3990 C  C   . ASN   B 1 228 ? -11.040 -30.075 -3.822  1.00 57.11 ?  228 ASN   B C   1 
ATOM   3991 O  O   . ASN   B 1 228 ? -12.122 -29.480 -3.765  1.00 64.05 ?  228 ASN   B O   1 
ATOM   3992 C  CB  . ASN   B 1 228 ? -10.640 -31.264 -5.997  1.00 52.43 ?  228 ASN   B CB  1 
ATOM   3993 N  N   . ASP   B 1 229 ? -10.530 -30.729 -2.771  1.00 61.91 ?  229 ASP   B N   1 
ATOM   3994 C  CA  . ASP   B 1 229 ? -11.216 -30.704 -1.481  1.00 60.17 ?  229 ASP   B CA  1 
ATOM   3995 C  C   . ASP   B 1 229 ? -11.118 -29.333 -0.825  1.00 58.92 ?  229 ASP   B C   1 
ATOM   3996 O  O   . ASP   B 1 229 ? -12.062 -28.897 -0.156  1.00 61.39 ?  229 ASP   B O   1 
ATOM   3997 C  CB  . ASP   B 1 229 ? -10.645 -31.782 -0.556  1.00 55.74 ?  229 ASP   B CB  1 
ATOM   3998 N  N   . PHE   B 1 230 ? -9.992  -28.640 -1.005  1.00 62.16 ?  230 PHE   B N   1 
ATOM   3999 C  CA  . PHE   B 1 230 ? -9.888  -27.265 -0.532  1.00 57.60 ?  230 PHE   B CA  1 
ATOM   4000 C  C   . PHE   B 1 230 ? -10.773 -26.339 -1.357  1.00 56.66 ?  230 PHE   B C   1 
ATOM   4001 O  O   . PHE   B 1 230 ? -11.510 -25.512 -0.804  1.00 59.13 ?  230 PHE   B O   1 
ATOM   4002 C  CB  . PHE   B 1 230 ? -8.430  -26.804 -0.577  1.00 55.58 ?  230 PHE   B CB  1 
ATOM   4003 C  CG  . PHE   B 1 230 ? -8.256  -25.319 -0.419  1.00 52.06 ?  230 PHE   B CG  1 
ATOM   4004 C  CD1 . PHE   B 1 230 ? -8.261  -24.738 0.836   1.00 48.78 ?  230 PHE   B CD1 1 
ATOM   4005 C  CD2 . PHE   B 1 230 ? -8.082  -24.504 -1.528  1.00 49.70 ?  230 PHE   B CD2 1 
ATOM   4006 C  CE1 . PHE   B 1 230 ? -8.103  -23.372 0.985   1.00 51.10 ?  230 PHE   B CE1 1 
ATOM   4007 C  CE2 . PHE   B 1 230 ? -7.923  -23.140 -1.386  1.00 50.34 ?  230 PHE   B CE2 1 
ATOM   4008 C  CZ  . PHE   B 1 230 ? -7.933  -22.573 -0.126  1.00 49.81 ?  230 PHE   B CZ  1 
ATOM   4009 N  N   . ASN   B 1 231 ? -10.719 -26.472 -2.688  1.00 55.94 ?  231 ASN   B N   1 
ATOM   4010 C  CA  . ASN   B 1 231 ? -11.472 -25.580 -3.566  1.00 56.46 ?  231 ASN   B CA  1 
ATOM   4011 C  C   . ASN   B 1 231 ? -12.971 -25.647 -3.301  1.00 59.62 ?  231 ASN   B C   1 
ATOM   4012 O  O   . ASN   B 1 231 ? -13.678 -24.649 -3.490  1.00 58.91 ?  231 ASN   B O   1 
ATOM   4013 C  CB  . ASN   B 1 231 ? -11.180 -25.912 -5.029  1.00 55.36 ?  231 ASN   B CB  1 
ATOM   4014 C  CG  . ASN   B 1 231 ? -9.974  -25.169 -5.566  1.00 55.59 ?  231 ASN   B CG  1 
ATOM   4015 O  OD1 . ASN   B 1 231 ? -9.636  -24.085 -5.090  1.00 59.11 ?  231 ASN   B OD1 1 
ATOM   4016 N  ND2 . ASN   B 1 231 ? -9.322  -25.744 -6.568  1.00 54.17 ?  231 ASN   B ND2 1 
ATOM   4017 N  N   . LEU   B 1 232 ? -13.479 -26.803 -2.867  1.00 59.19 ?  232 LEU   B N   1 
ATOM   4018 C  CA  . LEU   B 1 232 ? -14.897 -26.895 -2.543  1.00 55.99 ?  232 LEU   B CA  1 
ATOM   4019 C  C   . LEU   B 1 232 ? -15.224 -26.128 -1.268  1.00 62.08 ?  232 LEU   B C   1 
ATOM   4020 O  O   . LEU   B 1 232 ? -16.306 -25.538 -1.161  1.00 60.85 ?  232 LEU   B O   1 
ATOM   4021 C  CB  . LEU   B 1 232 ? -15.313 -28.362 -2.416  1.00 56.03 ?  232 LEU   B CB  1 
ATOM   4022 N  N   . VAL   B 1 233 ? -14.307 -26.112 -0.299  1.00 60.75 ?  233 VAL   B N   1 
ATOM   4023 C  CA  . VAL   B 1 233 ? -14.550 -25.353 0.922   1.00 56.82 ?  233 VAL   B CA  1 
ATOM   4024 C  C   . VAL   B 1 233 ? -14.386 -23.862 0.669   1.00 55.04 ?  233 VAL   B C   1 
ATOM   4025 O  O   . VAL   B 1 233 ? -15.176 -23.048 1.159   1.00 57.20 ?  233 VAL   B O   1 
ATOM   4026 C  CB  . VAL   B 1 233 ? -13.623 -25.835 2.051   1.00 53.99 ?  233 VAL   B CB  1 
ATOM   4027 C  CG1 . VAL   B 1 233 ? -14.083 -25.260 3.377   1.00 56.29 ?  233 VAL   B CG1 1 
ATOM   4028 C  CG2 . VAL   B 1 233 ? -13.585 -27.350 2.100   1.00 58.87 ?  233 VAL   B CG2 1 
ATOM   4029 N  N   . ALA   B 1 234 ? -13.360 -23.483 -0.096  1.00 56.83 ?  234 ALA   B N   1 
ATOM   4030 C  CA  . ALA   B 1 234 ? -13.116 -22.071 -0.368  1.00 57.25 ?  234 ALA   B CA  1 
ATOM   4031 C  C   . ALA   B 1 234 ? -14.296 -21.428 -1.084  1.00 55.79 ?  234 ALA   B C   1 
ATOM   4032 O  O   . ALA   B 1 234 ? -14.697 -20.306 -0.749  1.00 54.22 ?  234 ALA   B O   1 
ATOM   4033 C  CB  . ALA   B 1 234 ? -11.841 -21.909 -1.196  1.00 53.64 ?  234 ALA   B CB  1 
ATOM   4034 N  N   . MET   B 1 235 ? -14.867 -22.125 -2.071  1.00 58.09 ?  235 MET   B N   1 
ATOM   4035 C  CA  . MET   B 1 235 ? -15.960 -21.562 -2.859  1.00 53.88 ?  235 MET   B CA  1 
ATOM   4036 C  C   . MET   B 1 235 ? -17.189 -21.254 -2.014  1.00 52.29 ?  235 MET   B C   1 
ATOM   4037 O  O   . MET   B 1 235 ? -17.977 -20.380 -2.389  1.00 51.27 ?  235 MET   B O   1 
ATOM   4038 C  CB  . MET   B 1 235 ? -16.337 -22.515 -3.995  1.00 53.02 ?  235 MET   B CB  1 
ATOM   4039 N  N   . LYS   B 1 236 ? -17.371 -21.944 -0.885  1.00 50.44 ?  236 LYS   B N   1 
ATOM   4040 C  CA  . LYS   B 1 236 ? -18.495 -21.654 -0.002  1.00 47.43 ?  236 LYS   B CA  1 
ATOM   4041 C  C   . LYS   B 1 236 ? -18.287 -20.382 0.807   1.00 52.47 ?  236 LYS   B C   1 
ATOM   4042 O  O   . LYS   B 1 236 ? -19.259 -19.838 1.339   1.00 49.79 ?  236 LYS   B O   1 
ATOM   4043 C  CB  . LYS   B 1 236 ? -18.744 -22.827 0.950   1.00 51.00 ?  236 LYS   B CB  1 
ATOM   4044 N  N   . TYR   B 1 237 ? -17.044 -19.906 0.921   1.00 51.81 ?  237 TYR   B N   1 
ATOM   4045 C  CA  . TYR   B 1 237 ? -16.730 -18.680 1.644   1.00 47.40 ?  237 TYR   B CA  1 
ATOM   4046 C  C   . TYR   B 1 237 ? -16.360 -17.536 0.707   1.00 49.48 ?  237 TYR   B C   1 
ATOM   4047 O  O   . TYR   B 1 237 ? -15.717 -16.572 1.136   1.00 50.32 ?  237 TYR   B O   1 
ATOM   4048 C  CB  . TYR   B 1 237 ? -15.609 -18.933 2.654   1.00 48.08 ?  237 TYR   B CB  1 
ATOM   4049 C  CG  . TYR   B 1 237 ? -16.033 -19.846 3.782   1.00 46.87 ?  237 TYR   B CG  1 
ATOM   4050 C  CD1 . TYR   B 1 237 ? -16.714 -19.345 4.882   1.00 48.42 ?  237 TYR   B CD1 1 
ATOM   4051 C  CD2 . TYR   B 1 237 ? -15.776 -21.210 3.735   1.00 44.66 ?  237 TYR   B CD2 1 
ATOM   4052 C  CE1 . TYR   B 1 237 ? -17.119 -20.175 5.914   1.00 50.14 ?  237 TYR   B CE1 1 
ATOM   4053 C  CE2 . TYR   B 1 237 ? -16.175 -22.049 4.760   1.00 46.02 ?  237 TYR   B CE2 1 
ATOM   4054 C  CZ  . TYR   B 1 237 ? -16.849 -21.525 5.848   1.00 51.30 ?  237 TYR   B CZ  1 
ATOM   4055 O  OH  . TYR   B 1 237 ? -17.251 -22.349 6.875   1.00 55.80 ?  237 TYR   B OH  1 
ATOM   4056 N  N   . ASN   B 1 238 ? -16.756 -17.629 -0.565  1.00 43.46 ?  238 ASN   B N   1 
ATOM   4057 C  CA  . ASN   B 1 238 ? -16.512 -16.580 -1.557  1.00 44.83 ?  238 ASN   B CA  1 
ATOM   4058 C  C   . ASN   B 1 238 ? -15.019 -16.299 -1.720  1.00 39.14 ?  238 ASN   B C   1 
ATOM   4059 O  O   . ASN   B 1 238 ? -14.583 -15.150 -1.799  1.00 33.40 ?  238 ASN   B O   1 
ATOM   4060 C  CB  . ASN   B 1 238 ? -17.286 -15.308 -1.215  1.00 37.95 ?  238 ASN   B CB  1 
ATOM   4061 C  CG  . ASN   B 1 238 ? -18.774 -15.476 -1.416  1.00 55.42 ?  238 ASN   B CG  1 
ATOM   4062 O  OD1 . ASN   B 1 238 ? -19.234 -16.533 -1.853  1.00 58.44 ?  238 ASN   B OD1 1 
ATOM   4063 N  ND2 . ASN   B 1 238 ? -19.540 -14.439 -1.091  1.00 60.85 ?  238 ASN   B ND2 1 
ATOM   4064 N  N   . TYR   B 1 239 ? -14.236 -17.366 -1.771  1.00 40.47 ?  239 TYR   B N   1 
ATOM   4065 C  CA  . TYR   B 1 239 ? -12.822 -17.300 -2.099  1.00 38.85 ?  239 TYR   B CA  1 
ATOM   4066 C  C   . TYR   B 1 239 ? -12.629 -17.750 -3.541  1.00 39.96 ?  239 TYR   B C   1 
ATOM   4067 O  O   . TYR   B 1 239 ? -13.279 -18.696 -3.993  1.00 42.53 ?  239 TYR   B O   1 
ATOM   4068 C  CB  . TYR   B 1 239 ? -12.008 -18.190 -1.158  1.00 36.42 ?  239 TYR   B CB  1 
ATOM   4069 C  CG  . TYR   B 1 239 ? -11.442 -17.489 0.060   1.00 36.72 ?  239 TYR   B CG  1 
ATOM   4070 C  CD1 . TYR   B 1 239 ? -12.272 -16.863 0.981   1.00 38.20 ?  239 TYR   B CD1 1 
ATOM   4071 C  CD2 . TYR   B 1 239 ? -10.072 -17.472 0.296   1.00 39.31 ?  239 TYR   B CD2 1 
ATOM   4072 C  CE1 . TYR   B 1 239 ? -11.747 -16.225 2.104   1.00 35.73 ?  239 TYR   B CE1 1 
ATOM   4073 C  CE2 . TYR   B 1 239 ? -9.539  -16.844 1.407   1.00 37.83 ?  239 TYR   B CE2 1 
ATOM   4074 C  CZ  . TYR   B 1 239 ? -10.376 -16.223 2.309   1.00 36.64 ?  239 TYR   B CZ  1 
ATOM   4075 O  OH  . TYR   B 1 239 ? -9.829  -15.604 3.411   1.00 34.57 ?  239 TYR   B OH  1 
ATOM   4076 N  N   . GLU   B 1 240 ? -11.741 -17.067 -4.263  1.00 36.46 ?  240 GLU   B N   1 
ATOM   4077 C  CA  . GLU   B 1 240 ? -11.430 -17.469 -5.625  1.00 42.19 ?  240 GLU   B CA  1 
ATOM   4078 C  C   . GLU   B 1 240 ? -10.844 -18.880 -5.636  1.00 43.14 ?  240 GLU   B C   1 
ATOM   4079 O  O   . GLU   B 1 240 ? -10.126 -19.270 -4.710  1.00 44.37 ?  240 GLU   B O   1 
ATOM   4080 C  CB  . GLU   B 1 240 ? -10.444 -16.491 -6.262  1.00 46.25 ?  240 GLU   B CB  1 
ATOM   4081 C  CG  . GLU   B 1 240 ? -11.031 -15.122 -6.582  1.00 45.43 ?  240 GLU   B CG  1 
ATOM   4082 C  CD  . GLU   B 1 240 ? -11.899 -15.129 -7.831  1.00 46.51 ?  240 GLU   B CD  1 
ATOM   4083 O  OE1 . GLU   B 1 240 ? -11.382 -15.472 -8.917  1.00 50.95 ?  240 GLU   B OE1 1 
ATOM   4084 O  OE2 . GLU   B 1 240 ? -13.098 -14.790 -7.729  1.00 45.53 ?  240 GLU   B OE2 1 
ATOM   4085 N  N   . PRO   B 1 241 ? -11.139 -19.672 -6.665  1.00 46.71 ?  241 PRO   B N   1 
ATOM   4086 C  CA  . PRO   B 1 241 ? -10.550 -21.013 -6.744  1.00 48.69 ?  241 PRO   B CA  1 
ATOM   4087 C  C   . PRO   B 1 241 ? -9.035  -20.947 -6.843  1.00 52.61 ?  241 PRO   B C   1 
ATOM   4088 O  O   . PRO   B 1 241 ? -8.463  -20.033 -7.443  1.00 50.70 ?  241 PRO   B O   1 
ATOM   4089 C  CB  . PRO   B 1 241 ? -11.170 -21.601 -8.020  1.00 52.50 ?  241 PRO   B CB  1 
ATOM   4090 C  CG  . PRO   B 1 241 ? -11.620 -20.419 -8.812  1.00 46.94 ?  241 PRO   B CG  1 
ATOM   4091 C  CD  . PRO   B 1 241 ? -12.049 -19.405 -7.792  1.00 47.08 ?  241 PRO   B CD  1 
ATOM   4092 N  N   . LEU   B 1 242 ? -8.382  -21.932 -6.235  1.00 50.46 ?  242 LEU   B N   1 
ATOM   4093 C  CA  . LEU   B 1 242 ? -6.934  -22.065 -6.317  1.00 49.37 ?  242 LEU   B CA  1 
ATOM   4094 C  C   . LEU   B 1 242 ? -6.594  -22.963 -7.501  1.00 46.81 ?  242 LEU   B C   1 
ATOM   4095 O  O   . LEU   B 1 242 ? -7.046  -24.111 -7.566  1.00 49.21 ?  242 LEU   B O   1 
ATOM   4096 C  CB  . LEU   B 1 242 ? -6.369  -22.639 -5.018  1.00 50.76 ?  242 LEU   B CB  1 
ATOM   4097 C  CG  . LEU   B 1 242 ? -4.867  -22.461 -4.792  1.00 49.05 ?  242 LEU   B CG  1 
ATOM   4098 C  CD1 . LEU   B 1 242 ? -4.539  -20.996 -4.542  1.00 42.15 ?  242 LEU   B CD1 1 
ATOM   4099 C  CD2 . LEU   B 1 242 ? -4.384  -23.331 -3.643  1.00 49.92 ?  242 LEU   B CD2 1 
ATOM   4100 N  N   . THR   B 1 243 ? -5.813  -22.441 -8.439  1.00 50.23 ?  243 THR   B N   1 
ATOM   4101 C  CA  . THR   B 1 243 ? -5.399  -23.221 -9.593  1.00 49.82 ?  243 THR   B CA  1 
ATOM   4102 C  C   . THR   B 1 243 ? -4.041  -23.866 -9.335  1.00 48.12 ?  243 THR   B C   1 
ATOM   4103 O  O   . THR   B 1 243 ? -3.329  -23.529 -8.387  1.00 52.50 ?  243 THR   B O   1 
ATOM   4104 C  CB  . THR   B 1 243 ? -5.337  -22.349 -10.847 1.00 45.82 ?  243 THR   B CB  1 
ATOM   4105 O  OG1 . THR   B 1 243 ? -4.225  -21.447 -10.750 1.00 52.65 ?  243 THR   B OG1 1 
ATOM   4106 C  CG2 . THR   B 1 243 ? -6.611  -21.551 -10.999 1.00 45.51 ?  243 THR   B CG2 1 
ATOM   4107 N  N   . GLN   B 1 244 ? -3.689  -24.820 -10.197 1.00 47.05 ?  244 GLN   B N   1 
ATOM   4108 C  CA  . GLN   B 1 244 ? -2.374  -25.442 -10.101 1.00 49.37 ?  244 GLN   B CA  1 
ATOM   4109 C  C   . GLN   B 1 244 ? -1.266  -24.429 -10.353 1.00 54.94 ?  244 GLN   B C   1 
ATOM   4110 O  O   . GLN   B 1 244 ? -0.182  -24.536 -9.766  1.00 54.08 ?  244 GLN   B O   1 
ATOM   4111 C  CB  . GLN   B 1 244 ? -2.272  -26.608 -11.086 1.00 54.64 ?  244 GLN   B CB  1 
ATOM   4112 C  CG  . GLN   B 1 244 ? -0.921  -27.303 -11.087 1.00 54.61 ?  244 GLN   B CG  1 
ATOM   4113 C  CD  . GLN   B 1 244 ? -0.547  -27.832 -9.716  1.00 56.17 ?  244 GLN   B CD  1 
ATOM   4114 O  OE1 . GLN   B 1 244 ? -1.381  -28.406 -9.011  1.00 56.45 ?  244 GLN   B OE1 1 
ATOM   4115 N  NE2 . GLN   B 1 244 ? 0.708   -27.632 -9.325  1.00 55.70 ?  244 GLN   B NE2 1 
ATOM   4116 N  N   . ASP   B 1 245 ? -1.516  -23.435 -11.212 1.00 44.39 ?  245 ASP   B N   1 
ATOM   4117 C  CA  . ASP   B 1 245 ? -0.515  -22.398 -11.440 1.00 50.34 ?  245 ASP   B CA  1 
ATOM   4118 C  C   . ASP   B 1 245 ? -0.266  -21.584 -10.177 1.00 52.23 ?  245 ASP   B C   1 
ATOM   4119 O  O   . ASP   B 1 245 ? 0.870   -21.179 -9.905  1.00 54.30 ?  245 ASP   B O   1 
ATOM   4120 C  CB  . ASP   B 1 245 ? -0.944  -21.490 -12.592 1.00 54.58 ?  245 ASP   B CB  1 
ATOM   4121 C  CG  . ASP   B 1 245 ? -0.510  -22.023 -13.948 1.00 58.28 ?  245 ASP   B CG  1 
ATOM   4122 O  OD1 . ASP   B 1 245 ? 0.054   -23.140 -14.005 1.00 55.58 ?  245 ASP   B OD1 1 
ATOM   4123 O  OD2 . ASP   B 1 245 ? -0.724  -21.317 -14.955 1.00 62.07 ?  245 ASP   B OD2 1 
ATOM   4124 N  N   . HIS   B 1 246 ? -1.318  -21.332 -9.392  1.00 51.74 ?  246 HIS   B N   1 
ATOM   4125 C  CA  . HIS   B 1 246 ? -1.136  -20.660 -8.109  1.00 44.50 ?  246 HIS   B CA  1 
ATOM   4126 C  C   . HIS   B 1 246 ? -0.205  -21.456 -7.204  1.00 46.67 ?  246 HIS   B C   1 
ATOM   4127 O  O   . HIS   B 1 246 ? 0.652   -20.882 -6.521  1.00 44.68 ?  246 HIS   B O   1 
ATOM   4128 C  CB  . HIS   B 1 246 ? -2.488  -20.454 -7.428  1.00 45.02 ?  246 HIS   B CB  1 
ATOM   4129 C  CG  . HIS   B 1 246 ? -3.348  -19.409 -8.071  1.00 43.58 ?  246 HIS   B CG  1 
ATOM   4130 N  ND1 . HIS   B 1 246 ? -4.720  -19.524 -8.150  1.00 42.97 ?  246 HIS   B ND1 1 
ATOM   4131 C  CD2 . HIS   B 1 246 ? -3.038  -18.222 -8.645  1.00 41.80 ?  246 HIS   B CD2 1 
ATOM   4132 C  CE1 . HIS   B 1 246 ? -5.216  -18.457 -8.751  1.00 45.43 ?  246 HIS   B CE1 1 
ATOM   4133 N  NE2 . HIS   B 1 246 ? -4.216  -17.650 -9.058  1.00 38.27 ?  246 HIS   B NE2 1 
ATOM   4134 N  N   . VAL   B 1 247 ? -0.361  -22.782 -7.189  1.00 46.91 ?  247 VAL   B N   1 
ATOM   4135 C  CA  . VAL   B 1 247 ? 0.485   -23.634 -6.357  1.00 46.65 ?  247 VAL   B CA  1 
ATOM   4136 C  C   . VAL   B 1 247 ? 1.942   -23.508 -6.781  1.00 46.99 ?  247 VAL   B C   1 
ATOM   4137 O  O   . VAL   B 1 247 ? 2.845   -23.379 -5.947  1.00 44.78 ?  247 VAL   B O   1 
ATOM   4138 C  CB  . VAL   B 1 247 ? -0.000  -25.092 -6.426  1.00 49.22 ?  247 VAL   B CB  1 
ATOM   4139 C  CG1 . VAL   B 1 247 ? 0.968   -26.012 -5.701  1.00 47.80 ?  247 VAL   B CG1 1 
ATOM   4140 C  CG2 . VAL   B 1 247 ? -1.402  -25.210 -5.843  1.00 47.16 ?  247 VAL   B CG2 1 
ATOM   4141 N  N   . ASP   B 1 248 ? 2.191   -23.536 -8.091  1.00 51.47 ?  248 ASP   B N   1 
ATOM   4142 C  CA  . ASP   B 1 248 ? 3.548   -23.330 -8.586  1.00 51.27 ?  248 ASP   B CA  1 
ATOM   4143 C  C   . ASP   B 1 248 ? 4.080   -21.964 -8.172  1.00 47.60 ?  248 ASP   B C   1 
ATOM   4144 O  O   . ASP   B 1 248 ? 5.256   -21.830 -7.817  1.00 48.42 ?  248 ASP   B O   1 
ATOM   4145 C  CB  . ASP   B 1 248 ? 3.578   -23.488 -10.109 1.00 51.25 ?  248 ASP   B CB  1 
ATOM   4146 C  CG  . ASP   B 1 248 ? 2.991   -24.815 -10.572 1.00 57.08 ?  248 ASP   B CG  1 
ATOM   4147 O  OD1 . ASP   B 1 248 ? 2.809   -25.714 -9.720  1.00 58.94 ?  248 ASP   B OD1 1 
ATOM   4148 O  OD2 . ASP   B 1 248 ? 2.700   -24.955 -11.782 1.00 60.71 ?  248 ASP   B OD2 1 
ATOM   4149 N  N   . ILE   B 1 249 ? 3.224   -20.937 -8.195  1.00 46.29 ?  249 ILE   B N   1 
ATOM   4150 C  CA  . ILE   B 1 249 ? 3.658   -19.598 -7.811  1.00 41.10 ?  249 ILE   B CA  1 
ATOM   4151 C  C   . ILE   B 1 249 ? 3.976   -19.510 -6.324  1.00 45.26 ?  249 ILE   B C   1 
ATOM   4152 O  O   . ILE   B 1 249 ? 4.702   -18.602 -5.902  1.00 40.98 ?  249 ILE   B O   1 
ATOM   4153 C  CB  . ILE   B 1 249 ? 2.597   -18.553 -8.198  1.00 37.87 ?  249 ILE   B CB  1 
ATOM   4154 N  N   . LEU   B 1 250 ? 3.462   -20.432 -5.517  1.00 40.27 ?  250 LEU   B N   1 
ATOM   4155 C  CA  . LEU   B 1 250 ? 3.767   -20.466 -4.095  1.00 46.19 ?  250 LEU   B CA  1 
ATOM   4156 C  C   . LEU   B 1 250 ? 4.941   -21.379 -3.766  1.00 46.49 ?  250 LEU   B C   1 
ATOM   4157 O  O   . LEU   B 1 250 ? 5.312   -21.490 -2.594  1.00 43.34 ?  250 LEU   B O   1 
ATOM   4158 C  CB  . LEU   B 1 250 ? 2.533   -20.907 -3.303  1.00 40.20 ?  250 LEU   B CB  1 
ATOM   4159 C  CG  . LEU   B 1 250 ? 1.354   -19.934 -3.287  1.00 38.18 ?  250 LEU   B CG  1 
ATOM   4160 C  CD1 . LEU   B 1 250 ? 0.113   -20.616 -2.743  1.00 41.51 ?  250 LEU   B CD1 1 
ATOM   4161 C  CD2 . LEU   B 1 250 ? 1.682   -18.700 -2.462  1.00 38.53 ?  250 LEU   B CD2 1 
ATOM   4162 N  N   . GLY   B 1 251 ? 5.517   -22.038 -4.766  1.00 46.33 ?  251 GLY   B N   1 
ATOM   4163 C  CA  . GLY   B 1 251 ? 6.659   -22.903 -4.578  1.00 45.52 ?  251 GLY   B CA  1 
ATOM   4164 C  C   . GLY   B 1 251 ? 7.818   -22.275 -3.824  1.00 44.83 ?  251 GLY   B C   1 
ATOM   4165 O  O   . GLY   B 1 251 ? 8.315   -22.838 -2.842  1.00 42.35 ?  251 GLY   B O   1 
ATOM   4166 N  N   . PRO   B 1 252 ? 8.297   -21.110 -4.284  1.00 42.64 ?  252 PRO   B N   1 
ATOM   4167 C  CA  . PRO   B 1 252 ? 9.390   -20.435 -3.560  1.00 44.71 ?  252 PRO   B CA  1 
ATOM   4168 C  C   . PRO   B 1 252 ? 9.119   -20.220 -2.078  1.00 46.25 ?  252 PRO   B C   1 
ATOM   4169 O  O   . PRO   B 1 252 ? 10.022  -20.421 -1.255  1.00 43.77 ?  252 PRO   B O   1 
ATOM   4170 C  CB  . PRO   B 1 252 ? 9.519   -19.102 -4.306  1.00 45.87 ?  252 PRO   B CB  1 
ATOM   4171 C  CG  . PRO   B 1 252 ? 9.080   -19.420 -5.702  1.00 45.25 ?  252 PRO   B CG  1 
ATOM   4172 C  CD  . PRO   B 1 252 ? 8.001   -20.454 -5.573  1.00 48.47 ?  252 PRO   B CD  1 
ATOM   4173 N  N   . LEU   B 1 253 ? 7.904   -19.810 -1.711  1.00 42.03 ?  253 LEU   B N   1 
ATOM   4174 C  CA  . LEU   B 1 253 ? 7.612   -19.584 -0.298  1.00 42.67 ?  253 LEU   B CA  1 
ATOM   4175 C  C   . LEU   B 1 253 ? 7.539   -20.898 0.470   1.00 42.20 ?  253 LEU   B C   1 
ATOM   4176 O  O   . LEU   B 1 253 ? 7.952   -20.965 1.632   1.00 41.53 ?  253 LEU   B O   1 
ATOM   4177 C  CB  . LEU   B 1 253 ? 6.306   -18.803 -0.146  1.00 36.60 ?  253 LEU   B CB  1 
ATOM   4178 C  CG  . LEU   B 1 253 ? 6.357   -17.341 -0.589  1.00 37.07 ?  253 LEU   B CG  1 
ATOM   4179 C  CD1 . LEU   B 1 253 ? 4.957   -16.733 -0.696  1.00 37.13 ?  253 LEU   B CD1 1 
ATOM   4180 C  CD2 . LEU   B 1 253 ? 7.234   -16.535 0.355   1.00 35.92 ?  253 LEU   B CD2 1 
ATOM   4181 N  N   . SER   B 1 254 ? 7.004   -21.950 -0.157  1.00 43.38 ?  254 SER   B N   1 
ATOM   4182 C  CA  . SER   B 1 254 ? 6.951   -23.251 0.503   1.00 40.63 ?  254 SER   B CA  1 
ATOM   4183 C  C   . SER   B 1 254 ? 8.348   -23.819 0.723   1.00 45.16 ?  254 SER   B C   1 
ATOM   4184 O  O   . SER   B 1 254 ? 8.615   -24.432 1.761   1.00 42.39 ?  254 SER   B O   1 
ATOM   4185 C  CB  . SER   B 1 254 ? 6.097   -24.217 -0.316  1.00 39.72 ?  254 SER   B CB  1 
ATOM   4186 O  OG  . SER   B 1 254 ? 6.296   -24.007 -1.699  1.00 51.05 ?  254 SER   B OG  1 
ATOM   4187 N  N   . ALA   B 1 255 ? 9.252   -23.627 -0.244  1.00 45.71 ?  255 ALA   B N   1 
ATOM   4188 C  CA  . ALA   B 1 255 ? 10.629  -24.080 -0.067  1.00 46.36 ?  255 ALA   B CA  1 
ATOM   4189 C  C   . ALA   B 1 255 ? 11.314  -23.332 1.069   1.00 44.17 ?  255 ALA   B C   1 
ATOM   4190 O  O   . ALA   B 1 255 ? 12.031  -23.937 1.874   1.00 45.66 ?  255 ALA   B O   1 
ATOM   4191 C  CB  . ALA   B 1 255 ? 11.415  -23.909 -1.368  1.00 45.59 ?  255 ALA   B CB  1 
ATOM   4192 N  N   . GLN   B 1 256 ? 11.099  -22.016 1.152   1.00 41.25 ?  256 GLN   B N   1 
ATOM   4193 C  CA  . GLN   B 1 256 ? 11.748  -21.214 2.184   1.00 47.34 ?  256 GLN   B CA  1 
ATOM   4194 C  C   . GLN   B 1 256 ? 11.304  -21.628 3.585   1.00 44.10 ?  256 GLN   B C   1 
ATOM   4195 O  O   . GLN   B 1 256 ? 12.121  -21.679 4.511   1.00 49.00 ?  256 GLN   B O   1 
ATOM   4196 C  CB  . GLN   B 1 256 ? 11.463  -19.732 1.938   1.00 49.71 ?  256 GLN   B CB  1 
ATOM   4197 C  CG  . GLN   B 1 256 ? 11.788  -18.827 3.118   1.00 47.84 ?  256 GLN   B CG  1 
ATOM   4198 C  CD  . GLN   B 1 256 ? 11.886  -17.365 2.721   1.00 51.80 ?  256 GLN   B CD  1 
ATOM   4199 O  OE1 . GLN   B 1 256 ? 11.718  -17.015 1.553   1.00 49.11 ?  256 GLN   B OE1 1 
ATOM   4200 N  NE2 . GLN   B 1 256 ? 12.164  -16.502 3.696   1.00 52.33 ?  256 GLN   B NE2 1 
ATOM   4201 N  N   . THR   B 1 257 ? 10.019  -21.942 3.760   1.00 41.89 ?  257 THR   B N   1 
ATOM   4202 C  CA  . THR   B 1 257 ? 9.479   -22.275 5.074   1.00 44.31 ?  257 THR   B CA  1 
ATOM   4203 C  C   . THR   B 1 257 ? 9.409   -23.773 5.340   1.00 41.55 ?  257 THR   B C   1 
ATOM   4204 O  O   . THR   B 1 257 ? 9.241   -24.170 6.497   1.00 42.76 ?  257 THR   B O   1 
ATOM   4205 C  CB  . THR   B 1 257 ? 8.077   -21.675 5.238   1.00 41.64 ?  257 THR   B CB  1 
ATOM   4206 O  OG1 . THR   B 1 257 ? 7.214   -22.197 4.219   1.00 39.56 ?  257 THR   B OG1 1 
ATOM   4207 C  CG2 . THR   B 1 257 ? 8.128   -20.156 5.129   1.00 36.46 ?  257 THR   B CG2 1 
ATOM   4208 N  N   . GLY   B 1 258 ? 9.525   -24.608 4.310   1.00 46.77 ?  258 GLY   B N   1 
ATOM   4209 C  CA  . GLY   B 1 258 ? 9.396   -26.042 4.482   1.00 45.73 ?  258 GLY   B CA  1 
ATOM   4210 C  C   . GLY   B 1 258 ? 7.978   -26.549 4.611   1.00 49.42 ?  258 GLY   B C   1 
ATOM   4211 O  O   . GLY   B 1 258 ? 7.782   -27.708 4.996   1.00 51.66 ?  258 GLY   B O   1 
ATOM   4212 N  N   . ILE   B 1 259 ? 6.981   -25.728 4.297   1.00 46.99 ?  259 ILE   B N   1 
ATOM   4213 C  CA  . ILE   B 1 259 ? 5.577   -26.089 4.460   1.00 46.42 ?  259 ILE   B CA  1 
ATOM   4214 C  C   . ILE   B 1 259 ? 4.967   -26.245 3.077   1.00 43.85 ?  259 ILE   B C   1 
ATOM   4215 O  O   . ILE   B 1 259 ? 4.927   -25.285 2.297   1.00 42.56 ?  259 ILE   B O   1 
ATOM   4216 C  CB  . ILE   B 1 259 ? 4.820   -25.041 5.288   1.00 43.30 ?  259 ILE   B CB  1 
ATOM   4217 C  CG1 . ILE   B 1 259 ? 5.475   -24.895 6.660   1.00 45.08 ?  259 ILE   B CG1 1 
ATOM   4218 C  CG2 . ILE   B 1 259 ? 3.352   -25.419 5.423   1.00 45.34 ?  259 ILE   B CG2 1 
ATOM   4219 C  CD1 . ILE   B 1 259 ? 5.144   -23.602 7.357   1.00 42.22 ?  259 ILE   B CD1 1 
ATOM   4220 N  N   . ALA   B 1 260 ? 4.507   -27.458 2.770   1.00 46.99 ?  260 ALA   B N   1 
ATOM   4221 C  CA  . ALA   B 1 260 ? 3.884   -27.720 1.480   1.00 43.70 ?  260 ALA   B CA  1 
ATOM   4222 C  C   . ALA   B 1 260 ? 2.699   -26.791 1.268   1.00 46.22 ?  260 ALA   B C   1 
ATOM   4223 O  O   . ALA   B 1 260 ? 2.048   -26.348 2.219   1.00 45.77 ?  260 ALA   B O   1 
ATOM   4224 C  CB  . ALA   B 1 260 ? 3.425   -29.176 1.387   1.00 43.89 ?  260 ALA   B CB  1 
ATOM   4225 N  N   . VAL   B 1 261 ? 2.426   -26.484 0.000   1.00 45.95 ?  261 VAL   B N   1 
ATOM   4226 C  CA  . VAL   B 1 261 ? 1.324   -25.580 -0.313  1.00 46.60 ?  261 VAL   B CA  1 
ATOM   4227 C  C   . VAL   B 1 261 ? 0.005   -26.158 0.184   1.00 47.46 ?  261 VAL   B C   1 
ATOM   4228 O  O   . VAL   B 1 261 ? -0.812  -25.456 0.790   1.00 45.10 ?  261 VAL   B O   1 
ATOM   4229 C  CB  . VAL   B 1 261 ? 1.290   -25.288 -1.821  1.00 44.44 ?  261 VAL   B CB  1 
ATOM   4230 C  CG1 . VAL   B 1 261 ? 0.101   -24.407 -2.165  1.00 41.95 ?  261 VAL   B CG1 1 
ATOM   4231 C  CG2 . VAL   B 1 261 ? 2.594   -24.634 -2.240  1.00 46.07 ?  261 VAL   B CG2 1 
ATOM   4232 N  N   . LEU   B 1 262 ? -0.212  -27.456 -0.044  1.00 49.40 ?  262 LEU   B N   1 
ATOM   4233 C  CA  . LEU   B 1 262 ? -1.449  -28.087 0.398   1.00 49.11 ?  262 LEU   B CA  1 
ATOM   4234 C  C   . LEU   B 1 262 ? -1.536  -28.214 1.914   1.00 47.96 ?  262 LEU   B C   1 
ATOM   4235 O  O   . LEU   B 1 262 ? -2.643  -28.346 2.445   1.00 48.08 ?  262 LEU   B O   1 
ATOM   4236 C  CB  . LEU   B 1 262 ? -1.604  -29.461 -0.255  1.00 53.06 ?  262 LEU   B CB  1 
ATOM   4237 C  CG  . LEU   B 1 262 ? -2.056  -29.425 -1.717  1.00 51.28 ?  262 LEU   B CG  1 
ATOM   4238 C  CD1 . LEU   B 1 262 ? -2.319  -30.826 -2.246  1.00 52.54 ?  262 LEU   B CD1 1 
ATOM   4239 C  CD2 . LEU   B 1 262 ? -3.294  -28.552 -1.865  1.00 53.45 ?  262 LEU   B CD2 1 
ATOM   4240 N  N   . ASP   B 1 263 ? -0.403  -28.190 2.623   1.00 50.13 ?  263 ASP   B N   1 
ATOM   4241 C  CA  . ASP   B 1 263 ? -0.465  -28.123 4.080   1.00 48.44 ?  263 ASP   B CA  1 
ATOM   4242 C  C   . ASP   B 1 263 ? -0.884  -26.736 4.548   1.00 44.86 ?  263 ASP   B C   1 
ATOM   4243 O  O   . ASP   B 1 263 ? -1.564  -26.605 5.570   1.00 43.85 ?  263 ASP   B O   1 
ATOM   4244 C  CB  . ASP   B 1 263 ? 0.884   -28.509 4.689   1.00 51.38 ?  263 ASP   B CB  1 
ATOM   4245 N  N   . MET   B 1 264 ? -0.490  -25.691 3.817   1.00 43.34 ?  264 MET   B N   1 
ATOM   4246 C  CA  . MET   B 1 264 ? -0.953  -24.349 4.151   1.00 45.01 ?  264 MET   B CA  1 
ATOM   4247 C  C   . MET   B 1 264 ? -2.433  -24.182 3.822   1.00 46.44 ?  264 MET   B C   1 
ATOM   4248 O  O   . MET   B 1 264 ? -3.160  -23.498 4.550   1.00 41.63 ?  264 MET   B O   1 
ATOM   4249 C  CB  . MET   B 1 264 ? -0.117  -23.303 3.414   1.00 43.95 ?  264 MET   B CB  1 
ATOM   4250 C  CG  . MET   B 1 264 ? -0.319  -21.890 3.933   1.00 40.76 ?  264 MET   B CG  1 
ATOM   4251 S  SD  . MET   B 1 264 ? 0.291   -21.677 5.621   1.00 40.10 ?  264 MET   B SD  1 
ATOM   4252 C  CE  . MET   B 1 264 ? 2.024   -21.306 5.318   1.00 37.88 ?  264 MET   B CE  1 
ATOM   4253 N  N   . CYS   B 1 265 ? -2.889  -24.784 2.715   1.00 42.49 ?  265 CYS   B N   1 
ATOM   4254 C  CA  . CYS   B 1 265 ? -4.319  -24.791 2.408   1.00 45.61 ?  265 CYS   B CA  1 
ATOM   4255 C  C   . CYS   B 1 265 ? -5.116  -25.450 3.521   1.00 42.38 ?  265 CYS   B C   1 
ATOM   4256 O  O   . CYS   B 1 265 ? -6.194  -24.970 3.891   1.00 47.01 ?  265 CYS   B O   1 
ATOM   4257 C  CB  . CYS   B 1 265 ? -4.577  -25.513 1.088   1.00 41.91 ?  265 CYS   B CB  1 
ATOM   4258 S  SG  . CYS   B 1 265 ? -3.776  -24.773 -0.330  1.00 47.43 ?  265 CYS   B SG  1 
ATOM   4259 N  N   . ALA   B 1 266 ? -4.610  -26.565 4.052   1.00 44.50 ?  266 ALA   B N   1 
ATOM   4260 C  CA  . ALA   B 1 266 ? -5.263  -27.222 5.177   1.00 46.34 ?  266 ALA   B CA  1 
ATOM   4261 C  C   . ALA   B 1 266 ? -5.422  -26.271 6.355   1.00 46.12 ?  266 ALA   B C   1 
ATOM   4262 O  O   . ALA   B 1 266 ? -6.444  -26.296 7.050   1.00 41.01 ?  266 ALA   B O   1 
ATOM   4263 C  CB  . ALA   B 1 266 ? -4.469  -28.462 5.590   1.00 48.84 ?  266 ALA   B CB  1 
ATOM   4264 N  N   . SER   B 1 267 ? -4.421  -25.423 6.597   1.00 43.31 ?  267 SER   B N   1 
ATOM   4265 C  CA  . SER   B 1 267 ? -4.546  -24.432 7.659   1.00 44.39 ?  267 SER   B CA  1 
ATOM   4266 C  C   . SER   B 1 267 ? -5.559  -23.359 7.289   1.00 42.91 ?  267 SER   B C   1 
ATOM   4267 O  O   . SER   B 1 267 ? -6.398  -22.976 8.116   1.00 41.85 ?  267 SER   B O   1 
ATOM   4268 C  CB  . SER   B 1 267 ? -3.183  -23.811 7.962   1.00 48.15 ?  267 SER   B CB  1 
ATOM   4269 O  OG  . SER   B 1 267 ? -2.293  -24.787 8.470   1.00 50.44 ?  267 SER   B OG  1 
ATOM   4270 N  N   . LEU   B 1 268 ? -5.507  -22.869 6.048   1.00 42.58 ?  268 LEU   B N   1 
ATOM   4271 C  CA  . LEU   B 1 268 ? -6.446  -21.832 5.633   1.00 42.17 ?  268 LEU   B CA  1 
ATOM   4272 C  C   . LEU   B 1 268 ? -7.884  -22.330 5.714   1.00 42.58 ?  268 LEU   B C   1 
ATOM   4273 O  O   . LEU   B 1 268 ? -8.773  -21.603 6.172   1.00 40.38 ?  268 LEU   B O   1 
ATOM   4274 C  CB  . LEU   B 1 268 ? -6.112  -21.349 4.219   1.00 41.35 ?  268 LEU   B CB  1 
ATOM   4275 C  CG  . LEU   B 1 268 ? -7.079  -20.328 3.601   1.00 41.45 ?  268 LEU   B CG  1 
ATOM   4276 C  CD1 . LEU   B 1 268 ? -7.295  -19.119 4.503   1.00 35.42 ?  268 LEU   B CD1 1 
ATOM   4277 C  CD2 . LEU   B 1 268 ? -6.572  -19.882 2.248   1.00 41.20 ?  268 LEU   B CD2 1 
ATOM   4278 N  N   . LYS   B 1 269 ? -8.126  -23.577 5.294   1.00 40.50 ?  269 LYS   B N   1 
ATOM   4279 C  CA  . LYS   B 1 269 ? -9.469  -24.142 5.386   1.00 42.49 ?  269 LYS   B CA  1 
ATOM   4280 C  C   . LYS   B 1 269 ? -9.970  -24.121 6.825   1.00 45.98 ?  269 LYS   B C   1 
ATOM   4281 O  O   . LYS   B 1 269 ? -11.101 -23.703 7.093   1.00 42.91 ?  269 LYS   B O   1 
ATOM   4282 C  CB  . LYS   B 1 269 ? -9.486  -25.567 4.832   1.00 38.28 ?  269 LYS   B CB  1 
ATOM   4283 N  N   . GLU   B 1 270 ? -9.130  -24.556 7.769   1.00 39.69 ?  270 GLU   B N   1 
ATOM   4284 C  CA  . GLU   B 1 270 ? -9.531  -24.535 9.174   1.00 47.46 ?  270 GLU   B CA  1 
ATOM   4285 C  C   . GLU   B 1 270 ? -9.793  -23.114 9.655   1.00 45.93 ?  270 GLU   B C   1 
ATOM   4286 O  O   . GLU   B 1 270 ? -10.695 -22.891 10.470  1.00 47.39 ?  270 GLU   B O   1 
ATOM   4287 C  CB  . GLU   B 1 270 ? -8.461  -25.202 10.040  1.00 38.93 ?  270 GLU   B CB  1 
ATOM   4288 N  N   . LEU   B 1 271 ? -9.023  -22.142 9.160   1.00 42.86 ?  271 LEU   B N   1 
ATOM   4289 C  CA  . LEU   B 1 271 ? -9.272  -20.751 9.523   1.00 41.70 ?  271 LEU   B CA  1 
ATOM   4290 C  C   . LEU   B 1 271 ? -10.618 -20.262 9.000   1.00 49.81 ?  271 LEU   B C   1 
ATOM   4291 O  O   . LEU   B 1 271 ? -11.292 -19.468 9.670   1.00 51.07 ?  271 LEU   B O   1 
ATOM   4292 C  CB  . LEU   B 1 271 ? -8.147  -19.864 8.990   1.00 40.21 ?  271 LEU   B CB  1 
ATOM   4293 C  CG  . LEU   B 1 271 ? -6.857  -19.800 9.805   1.00 36.68 ?  271 LEU   B CG  1 
ATOM   4294 C  CD1 . LEU   B 1 271 ? -5.787  -19.035 9.038   1.00 38.25 ?  271 LEU   B CD1 1 
ATOM   4295 C  CD2 . LEU   B 1 271 ? -7.116  -19.149 11.161  1.00 40.01 ?  271 LEU   B CD2 1 
ATOM   4296 N  N   . LEU   B 1 272 ? -11.028 -20.724 7.817   1.00 41.14 ?  272 LEU   B N   1 
ATOM   4297 C  CA  . LEU   B 1 272 ? -12.249 -20.207 7.209   1.00 48.86 ?  272 LEU   B CA  1 
ATOM   4298 C  C   . LEU   B 1 272 ? -13.492 -20.704 7.932   1.00 49.42 ?  272 LEU   B C   1 
ATOM   4299 O  O   . LEU   B 1 272 ? -14.441 -19.939 8.147   1.00 50.37 ?  272 LEU   B O   1 
ATOM   4300 C  CB  . LEU   B 1 272 ? -12.300 -20.592 5.733   1.00 40.00 ?  272 LEU   B CB  1 
ATOM   4301 C  CG  . LEU   B 1 272 ? -11.340 -19.799 4.848   1.00 43.97 ?  272 LEU   B CG  1 
ATOM   4302 C  CD1 . LEU   B 1 272 ? -11.542 -20.149 3.383   1.00 40.59 ?  272 LEU   B CD1 1 
ATOM   4303 C  CD2 . LEU   B 1 272 ? -11.530 -18.305 5.089   1.00 41.24 ?  272 LEU   B CD2 1 
ATOM   4304 N  N   . GLN   B 1 273 ? -13.508 -21.977 8.316   1.00 50.74 ?  273 GLN   B N   1 
ATOM   4305 C  CA  . GLN   B 1 273 ? -14.691 -22.560 8.931   1.00 53.57 ?  273 GLN   B CA  1 
ATOM   4306 C  C   . GLN   B 1 273 ? -14.659 -22.521 10.450  1.00 50.10 ?  273 GLN   B C   1 
ATOM   4307 O  O   . GLN   B 1 273 ? -15.657 -22.886 11.079  1.00 52.78 ?  273 GLN   B O   1 
ATOM   4308 C  CB  . GLN   B 1 273 ? -14.881 -24.003 8.448   1.00 53.97 ?  273 GLN   B CB  1 
ATOM   4309 C  CG  . GLN   B 1 273 ? -13.645 -24.873 8.558   1.00 51.43 ?  273 GLN   B CG  1 
ATOM   4310 C  CD  . GLN   B 1 273 ? -13.605 -25.952 7.489   1.00 52.83 ?  273 GLN   B CD  1 
ATOM   4311 O  OE1 . GLN   B 1 273 ? -14.279 -25.850 6.463   1.00 53.47 ?  273 GLN   B OE1 1 
ATOM   4312 N  NE2 . GLN   B 1 273 ? -12.812 -26.992 7.724   1.00 53.14 ?  273 GLN   B NE2 1 
ATOM   4313 N  N   . ASN   B 1 274 ? -13.552 -22.083 11.056  1.00 51.32 ?  274 ASN   B N   1 
ATOM   4314 C  CA  . ASN   B 1 274 ? -13.487 -21.913 12.501  1.00 53.63 ?  274 ASN   B CA  1 
ATOM   4315 C  C   . ASN   B 1 274 ? -13.305 -20.475 12.952  1.00 52.23 ?  274 ASN   B C   1 
ATOM   4316 O  O   . ASN   B 1 274 ? -13.636 -20.167 14.101  1.00 49.11 ?  274 ASN   B O   1 
ATOM   4317 C  CB  . ASN   B 1 274 ? -12.337 -22.738 13.103  1.00 50.21 ?  274 ASN   B CB  1 
ATOM   4318 C  CG  . ASN   B 1 274 ? -12.744 -24.152 13.433  1.00 50.98 ?  274 ASN   B CG  1 
ATOM   4319 O  OD1 . ASN   B 1 274 ? -13.466 -24.797 12.674  1.00 60.45 ?  274 ASN   B OD1 1 
ATOM   4320 N  ND2 . ASN   B 1 274 ? -12.294 -24.640 14.582  1.00 63.49 ?  274 ASN   B ND2 1 
ATOM   4321 N  N   . GLY   B 1 275 ? -12.795 -19.595 12.095  1.00 48.24 ?  275 GLY   B N   1 
ATOM   4322 C  CA  . GLY   B 1 275 ? -12.381 -18.279 12.529  1.00 47.92 ?  275 GLY   B CA  1 
ATOM   4323 C  C   . GLY   B 1 275 ? -10.999 -18.329 13.154  1.00 45.01 ?  275 GLY   B C   1 
ATOM   4324 O  O   . GLY   B 1 275 ? -10.321 -19.357 13.171  1.00 44.65 ?  275 GLY   B O   1 
ATOM   4325 N  N   . MET   B 1 276 ? -10.575 -17.184 13.681  1.00 50.17 ?  276 MET   B N   1 
ATOM   4326 C  CA  . MET   B 1 276 ? -9.271  -17.063 14.320  1.00 45.62 ?  276 MET   B CA  1 
ATOM   4327 C  C   . MET   B 1 276 ? -9.333  -17.242 15.830  1.00 49.99 ?  276 MET   B C   1 
ATOM   4328 O  O   . MET   B 1 276 ? -8.282  -17.235 16.482  1.00 49.99 ?  276 MET   B O   1 
ATOM   4329 C  CB  . MET   B 1 276 ? -8.638  -15.707 13.986  1.00 47.19 ?  276 MET   B CB  1 
ATOM   4330 N  N   . ASN   B 1 277 ? -10.531 -17.393 16.396  1.00 47.99 ?  277 ASN   B N   1 
ATOM   4331 C  CA  . ASN   B 1 277 ? -10.705 -17.642 17.827  1.00 47.08 ?  277 ASN   B CA  1 
ATOM   4332 C  C   . ASN   B 1 277 ? -10.037 -16.551 18.664  1.00 44.06 ?  277 ASN   B C   1 
ATOM   4333 O  O   . ASN   B 1 277 ? -9.322  -16.823 19.631  1.00 44.21 ?  277 ASN   B O   1 
ATOM   4334 C  CB  . ASN   B 1 277 ? -10.180 -19.029 18.205  1.00 48.73 ?  277 ASN   B CB  1 
ATOM   4335 N  N   . GLY   B 1 278 ? -10.263 -15.300 18.270  1.00 45.81 ?  278 GLY   B N   1 
ATOM   4336 C  CA  . GLY   B 1 278 ? -9.765  -14.167 19.020  1.00 43.26 ?  278 GLY   B CA  1 
ATOM   4337 C  C   . GLY   B 1 278 ? -8.300  -13.851 18.836  1.00 48.46 ?  278 GLY   B C   1 
ATOM   4338 O  O   . GLY   B 1 278 ? -7.783  -12.970 19.531  1.00 46.65 ?  278 GLY   B O   1 
ATOM   4339 N  N   . ARG   B 1 279 ? -7.612  -14.528 17.923  1.00 48.43 ?  279 ARG   B N   1 
ATOM   4340 C  CA  . ARG   B 1 279 ? -6.193  -14.299 17.718  1.00 46.81 ?  279 ARG   B CA  1 
ATOM   4341 C  C   . ARG   B 1 279 ? -5.988  -13.380 16.515  1.00 46.71 ?  279 ARG   B C   1 
ATOM   4342 O  O   . ARG   B 1 279 ? -6.929  -13.021 15.802  1.00 46.94 ?  279 ARG   B O   1 
ATOM   4343 C  CB  . ARG   B 1 279 ? -5.467  -15.635 17.547  1.00 46.33 ?  279 ARG   B CB  1 
ATOM   4344 C  CG  . ARG   B 1 279 ? -5.957  -16.698 18.514  1.00 48.26 ?  279 ARG   B CG  1 
ATOM   4345 C  CD  . ARG   B 1 279 ? -5.183  -17.993 18.391  1.00 46.59 ?  279 ARG   B CD  1 
ATOM   4346 N  NE  . ARG   B 1 279 ? -3.871  -17.901 19.025  1.00 57.02 ?  279 ARG   B NE  1 
ATOM   4347 C  CZ  . ARG   B 1 279 ? -3.103  -18.951 19.302  1.00 55.71 ?  279 ARG   B CZ  1 
ATOM   4348 N  NH1 . ARG   B 1 279 ? -3.521  -20.174 19.002  1.00 58.87 ?  279 ARG   B NH1 1 
ATOM   4349 N  NH2 . ARG   B 1 279 ? -1.925  -18.780 19.886  1.00 56.42 ?  279 ARG   B NH2 1 
ATOM   4350 N  N   . THR   B 1 280 ? -4.739  -12.983 16.293  1.00 39.50 ?  280 THR   B N   1 
ATOM   4351 C  CA  . THR   B 1 280 ? -4.394  -12.175 15.136  1.00 40.40 ?  280 THR   B CA  1 
ATOM   4352 C  C   . THR   B 1 280 ? -3.217  -12.803 14.409  1.00 42.52 ?  280 THR   B C   1 
ATOM   4353 O  O   . THR   B 1 280 ? -2.510  -13.660 14.944  1.00 39.34 ?  280 THR   B O   1 
ATOM   4354 C  CB  . THR   B 1 280 ? -4.042  -10.736 15.515  1.00 42.79 ?  280 THR   B CB  1 
ATOM   4355 O  OG1 . THR   B 1 280 ? -2.948  -10.749 16.437  1.00 40.27 ?  280 THR   B OG1 1 
ATOM   4356 C  CG2 . THR   B 1 280 ? -5.244  -10.031 16.138  1.00 40.65 ?  280 THR   B CG2 1 
ATOM   4357 N  N   . ILE   B 1 281 ? -3.029  -12.357 13.171  1.00 36.37 ?  281 ILE   B N   1 
ATOM   4358 C  CA  . ILE   B 1 281 ? -1.931  -12.783 12.315  1.00 37.25 ?  281 ILE   B CA  1 
ATOM   4359 C  C   . ILE   B 1 281 ? -1.315  -11.524 11.729  1.00 37.66 ?  281 ILE   B C   1 
ATOM   4360 O  O   . ILE   B 1 281 ? -2.003  -10.762 11.041  1.00 34.82 ?  281 ILE   B O   1 
ATOM   4361 C  CB  . ILE   B 1 281 ? -2.407  -13.732 11.202  1.00 38.47 ?  281 ILE   B CB  1 
ATOM   4362 C  CG1 . ILE   B 1 281 ? -2.928  -15.039 11.796  1.00 37.83 ?  281 ILE   B CG1 1 
ATOM   4363 C  CG2 . ILE   B 1 281 ? -1.297  -14.021 10.204  1.00 34.32 ?  281 ILE   B CG2 1 
ATOM   4364 C  CD1 . ILE   B 1 281 ? -3.565  -15.952 10.768  1.00 39.77 ?  281 ILE   B CD1 1 
ATOM   4365 N  N   . LEU   B 1 282 ? -0.040  -11.279 12.037  1.00 32.24 ?  282 LEU   B N   1 
ATOM   4366 C  CA  . LEU   B 1 282 ? 0.666   -10.099 11.534  1.00 37.68 ?  282 LEU   B CA  1 
ATOM   4367 C  C   . LEU   B 1 282 ? -0.099  -8.820  11.866  1.00 34.16 ?  282 LEU   B C   1 
ATOM   4368 O  O   . LEU   B 1 282 ? -0.148  -7.875  11.075  1.00 34.95 ?  282 LEU   B O   1 
ATOM   4369 C  CB  . LEU   B 1 282 ? 0.922   -10.209 10.023  1.00 32.87 ?  282 LEU   B CB  1 
ATOM   4370 C  CG  . LEU   B 1 282 ? 2.081   -11.121 9.613   1.00 34.36 ?  282 LEU   B CG  1 
ATOM   4371 C  CD1 . LEU   B 1 282 ? 2.191   -11.234 8.091   1.00 32.40 ?  282 LEU   B CD1 1 
ATOM   4372 C  CD2 . LEU   B 1 282 ? 3.408   -10.627 10.206  1.00 37.12 ?  282 LEU   B CD2 1 
ATOM   4373 N  N   . GLY   B 1 283 ? -0.718  -8.802  13.042  1.00 33.61 ?  283 GLY   B N   1 
ATOM   4374 C  CA  . GLY   B 1 283 ? -1.428  -7.627  13.505  1.00 36.57 ?  283 GLY   B CA  1 
ATOM   4375 C  C   . GLY   B 1 283 ? -2.793  -7.415  12.893  1.00 37.95 ?  283 GLY   B C   1 
ATOM   4376 O  O   . GLY   B 1 283 ? -3.330  -6.305  12.973  1.00 38.66 ?  283 GLY   B O   1 
ATOM   4377 N  N   . SER   B 1 284 ? -3.377  -8.442  12.286  1.00 37.64 ?  284 SER   B N   1 
ATOM   4378 C  CA  . SER   B 1 284 ? -4.667  -8.326  11.623  1.00 36.99 ?  284 SER   B CA  1 
ATOM   4379 C  C   . SER   B 1 284 ? -5.637  -9.364  12.166  1.00 35.98 ?  284 SER   B C   1 
ATOM   4380 O  O   . SER   B 1 284 ? -5.257  -10.509 12.429  1.00 37.76 ?  284 SER   B O   1 
ATOM   4381 C  CB  . SER   B 1 284 ? -4.533  -8.503  10.109  1.00 36.86 ?  284 SER   B CB  1 
ATOM   4382 O  OG  . SER   B 1 284 ? -5.809  -8.667  9.523   1.00 36.53 ?  284 SER   B OG  1 
ATOM   4383 N  N   . ALA   B 1 285 ? -6.888  -8.953  12.332  1.00 31.12 ?  285 ALA   B N   1 
ATOM   4384 C  CA  . ALA   B 1 285 ? -7.966  -9.860  12.692  1.00 35.87 ?  285 ALA   B CA  1 
ATOM   4385 C  C   . ALA   B 1 285 ? -8.696  -10.407 11.470  1.00 38.39 ?  285 ALA   B C   1 
ATOM   4386 O  O   . ALA   B 1 285 ? -9.622  -11.211 11.622  1.00 37.02 ?  285 ALA   B O   1 
ATOM   4387 C  CB  . ALA   B 1 285 ? -8.953  -9.149  13.625  1.00 31.69 ?  285 ALA   B CB  1 
ATOM   4388 N  N   . LEU   B 1 286 ? -8.301  -9.992  10.269  1.00 33.98 ?  286 LEU   B N   1 
ATOM   4389 C  CA  . LEU   B 1 286 ? -8.873  -10.477 9.023   1.00 39.02 ?  286 LEU   B CA  1 
ATOM   4390 C  C   . LEU   B 1 286 ? -7.788  -11.126 8.175   1.00 36.88 ?  286 LEU   B C   1 
ATOM   4391 O  O   . LEU   B 1 286 ? -6.609  -10.789 8.281   1.00 37.89 ?  286 LEU   B O   1 
ATOM   4392 C  CB  . LEU   B 1 286 ? -9.512  -9.340  8.218   1.00 40.12 ?  286 LEU   B CB  1 
ATOM   4393 C  CG  . LEU   B 1 286 ? -10.625 -8.532  8.867   1.00 38.21 ?  286 LEU   B CG  1 
ATOM   4394 C  CD1 . LEU   B 1 286 ? -10.834 -7.245  8.079   1.00 43.14 ?  286 LEU   B CD1 1 
ATOM   4395 C  CD2 . LEU   B 1 286 ? -11.907 -9.351  8.936   1.00 41.56 ?  286 LEU   B CD2 1 
ATOM   4396 N  N   . LEU   B 1 287 ? -8.201  -12.043 7.306   1.00 35.30 ?  287 LEU   B N   1 
ATOM   4397 C  CA  . LEU   B 1 287 ? -7.278  -12.648 6.358   1.00 35.59 ?  287 LEU   B CA  1 
ATOM   4398 C  C   . LEU   B 1 287 ? -6.986  -11.650 5.240   1.00 35.71 ?  287 LEU   B C   1 
ATOM   4399 O  O   . LEU   B 1 287 ? -7.896  -11.227 4.523   1.00 35.92 ?  287 LEU   B O   1 
ATOM   4400 C  CB  . LEU   B 1 287 ? -7.862  -13.950 5.817   1.00 33.13 ?  287 LEU   B CB  1 
ATOM   4401 C  CG  . LEU   B 1 287 ? -8.164  -14.934 6.955   1.00 40.18 ?  287 LEU   B CG  1 
ATOM   4402 C  CD1 . LEU   B 1 287 ? -8.843  -16.187 6.442   1.00 43.98 ?  287 LEU   B CD1 1 
ATOM   4403 C  CD2 . LEU   B 1 287 ? -6.899  -15.286 7.727   1.00 38.68 ?  287 LEU   B CD2 1 
ATOM   4404 N  N   . GLU   B 1 288 ? -5.718  -11.273 5.102   1.00 36.19 ?  288 GLU   B N   1 
ATOM   4405 C  CA  . GLU   B 1 288 ? -5.300  -10.206 4.201   1.00 32.98 ?  288 GLU   B CA  1 
ATOM   4406 C  C   . GLU   B 1 288 ? -5.000  -10.770 2.813   1.00 32.24 ?  288 GLU   B C   1 
ATOM   4407 O  O   . GLU   B 1 288 ? -4.310  -11.786 2.687   1.00 30.58 ?  288 GLU   B O   1 
ATOM   4408 C  CB  . GLU   B 1 288 ? -4.073  -9.507  4.793   1.00 35.41 ?  288 GLU   B CB  1 
ATOM   4409 C  CG  . GLU   B 1 288 ? -3.401  -8.497  3.891   1.00 38.72 ?  288 GLU   B CG  1 
ATOM   4410 C  CD  . GLU   B 1 288 ? -4.267  -7.286  3.640   1.00 44.26 ?  288 GLU   B CD  1 
ATOM   4411 O  OE1 . GLU   B 1 288 ? -4.649  -6.622  4.627   1.00 43.40 ?  288 GLU   B OE1 1 
ATOM   4412 O  OE2 . GLU   B 1 288 ? -4.571  -7.007  2.458   1.00 39.72 ?  288 GLU   B OE2 1 
ATOM   4413 N  N   . ASP   B 1 289 ? -5.526  -10.123 1.767   1.00 31.74 ?  289 ASP   B N   1 
ATOM   4414 C  CA  . ASP   B 1 289 ? -5.357  -10.647 0.414   1.00 28.65 ?  289 ASP   B CA  1 
ATOM   4415 C  C   . ASP   B 1 289 ? -4.799  -9.620  -0.568  1.00 32.87 ?  289 ASP   B C   1 
ATOM   4416 O  O   . ASP   B 1 289 ? -4.985  -9.771  -1.781  1.00 32.87 ?  289 ASP   B O   1 
ATOM   4417 C  CB  . ASP   B 1 289 ? -6.676  -11.228 -0.116  1.00 31.57 ?  289 ASP   B CB  1 
ATOM   4418 C  CG  . ASP   B 1 289 ? -7.703  -10.167 -0.500  1.00 34.65 ?  289 ASP   B CG  1 
ATOM   4419 O  OD1 . ASP   B 1 289 ? -7.512  -8.964  -0.218  1.00 30.30 ?  289 ASP   B OD1 1 
ATOM   4420 O  OD2 . ASP   B 1 289 ? -8.728  -10.554 -1.108  1.00 34.21 ?  289 ASP   B OD2 1 
ATOM   4421 N  N   . GLU   B 1 290 ? -4.123  -8.578  -0.087  1.00 31.70 ?  290 GLU   B N   1 
ATOM   4422 C  CA  . GLU   B 1 290 ? -3.543  -7.573  -0.968  1.00 28.75 ?  290 GLU   B CA  1 
ATOM   4423 C  C   . GLU   B 1 290 ? -2.017  -7.671  -1.016  1.00 29.88 ?  290 GLU   B C   1 
ATOM   4424 O  O   . GLU   B 1 290 ? -1.339  -6.672  -1.255  1.00 33.12 ?  290 GLU   B O   1 
ATOM   4425 C  CB  . GLU   B 1 290 ? -3.996  -6.164  -0.570  1.00 33.59 ?  290 GLU   B CB  1 
ATOM   4426 C  CG  . GLU   B 1 290 ? -5.525  -6.031  -0.421  1.00 33.63 ?  290 GLU   B CG  1 
ATOM   4427 C  CD  . GLU   B 1 290 ? -6.150  -4.828  -1.157  1.00 39.43 ?  290 GLU   B CD  1 
ATOM   4428 O  OE1 . GLU   B 1 290 ? -5.489  -3.781  -1.297  1.00 35.75 ?  290 GLU   B OE1 1 
ATOM   4429 O  OE2 . GLU   B 1 290 ? -7.329  -4.925  -1.589  1.00 45.98 ?  290 GLU   B OE2 1 
ATOM   4430 N  N   . PHE   B 1 291 ? -1.471  -8.876  -0.804  1.00 29.50 ?  291 PHE   B N   1 
ATOM   4431 C  CA  . PHE   B 1 291 ? -0.055  -9.177  -1.029  1.00 25.37 ?  291 PHE   B CA  1 
ATOM   4432 C  C   . PHE   B 1 291 ? 0.057   -10.377 -1.957  1.00 27.50 ?  291 PHE   B C   1 
ATOM   4433 O  O   . PHE   B 1 291 ? -0.386  -11.474 -1.607  1.00 27.27 ?  291 PHE   B O   1 
ATOM   4434 C  CB  . PHE   B 1 291 ? 0.682   -9.501  0.280   1.00 31.64 ?  291 PHE   B CB  1 
ATOM   4435 C  CG  . PHE   B 1 291 ? 0.706   -8.379  1.282   1.00 30.19 ?  291 PHE   B CG  1 
ATOM   4436 C  CD1 . PHE   B 1 291 ? -0.295  -8.257  2.233   1.00 35.18 ?  291 PHE   B CD1 1 
ATOM   4437 C  CD2 . PHE   B 1 291 ? 1.751   -7.465  1.295   1.00 32.17 ?  291 PHE   B CD2 1 
ATOM   4438 C  CE1 . PHE   B 1 291 ? -0.266  -7.231  3.170   1.00 34.30 ?  291 PHE   B CE1 1 
ATOM   4439 C  CE2 . PHE   B 1 291 ? 1.782   -6.436  2.228   1.00 34.85 ?  291 PHE   B CE2 1 
ATOM   4440 C  CZ  . PHE   B 1 291 ? 0.774   -6.322  3.166   1.00 35.78 ?  291 PHE   B CZ  1 
ATOM   4441 N  N   . THR   B 1 292 ? 0.708   -10.199 -3.101  1.00 28.01 ?  292 THR   B N   1 
ATOM   4442 C  CA  . THR   B 1 292 ? 0.956   -11.338 -3.971  1.00 29.98 ?  292 THR   B CA  1 
ATOM   4443 C  C   . THR   B 1 292 ? 2.150   -12.155 -3.477  1.00 33.70 ?  292 THR   B C   1 
ATOM   4444 O  O   . THR   B 1 292 ? 2.938   -11.693 -2.638  1.00 31.63 ?  292 THR   B O   1 
ATOM   4445 C  CB  . THR   B 1 292 ? 1.204   -10.867 -5.402  1.00 35.35 ?  292 THR   B CB  1 
ATOM   4446 O  OG1 . THR   B 1 292 ? 2.511   -10.284 -5.487  1.00 33.89 ?  292 THR   B OG1 1 
ATOM   4447 C  CG2 . THR   B 1 292 ? 0.157   -9.838  -5.819  1.00 26.18 ?  292 THR   B CG2 1 
ATOM   4448 N  N   . PRO   B 1 293 ? 2.300   -13.392 -3.968  1.00 33.29 ?  293 PRO   B N   1 
ATOM   4449 C  CA  . PRO   B 1 293 ? 3.511   -14.157 -3.625  1.00 34.97 ?  293 PRO   B CA  1 
ATOM   4450 C  C   . PRO   B 1 293 ? 4.798   -13.403 -3.925  1.00 36.97 ?  293 PRO   B C   1 
ATOM   4451 O  O   . PRO   B 1 293 ? 5.738   -13.446 -3.119  1.00 35.61 ?  293 PRO   B O   1 
ATOM   4452 C  CB  . PRO   B 1 293 ? 3.369   -15.425 -4.476  1.00 34.37 ?  293 PRO   B CB  1 
ATOM   4453 C  CG  . PRO   B 1 293 ? 1.901   -15.610 -4.626  1.00 33.63 ?  293 PRO   B CG  1 
ATOM   4454 C  CD  . PRO   B 1 293 ? 1.284   -14.231 -4.632  1.00 33.79 ?  293 PRO   B CD  1 
ATOM   4455 N  N   . PHE   B 1 294 ? 4.852   -12.680 -5.048  1.00 32.64 ?  294 PHE   B N   1 
ATOM   4456 C  CA  . PHE   B 1 294 ? 6.042   -11.894 -5.362  1.00 37.12 ?  294 PHE   B CA  1 
ATOM   4457 C  C   . PHE   B 1 294 ? 6.238   -10.763 -4.358  1.00 38.35 ?  294 PHE   B C   1 
ATOM   4458 O  O   . PHE   B 1 294 ? 7.372   -10.472 -3.957  1.00 39.12 ?  294 PHE   B O   1 
ATOM   4459 C  CB  . PHE   B 1 294 ? 5.949   -11.348 -6.788  1.00 33.16 ?  294 PHE   B CB  1 
ATOM   4460 N  N   . ASP   B 1 295 ? 5.143   -10.124 -3.933  1.00 36.52 ?  295 ASP   B N   1 
ATOM   4461 C  CA  . ASP   B 1 295 ? 5.230   -9.070  -2.924  1.00 35.86 ?  295 ASP   B CA  1 
ATOM   4462 C  C   . ASP   B 1 295 ? 5.854   -9.582  -1.634  1.00 36.61 ?  295 ASP   B C   1 
ATOM   4463 O  O   . ASP   B 1 295 ? 6.677   -8.894  -1.019  1.00 34.36 ?  295 ASP   B O   1 
ATOM   4464 C  CB  . ASP   B 1 295 ? 3.843   -8.496  -2.631  1.00 33.76 ?  295 ASP   B CB  1 
ATOM   4465 C  CG  . ASP   B 1 295 ? 3.299   -7.647  -3.769  1.00 36.02 ?  295 ASP   B CG  1 
ATOM   4466 O  OD1 . ASP   B 1 295 ? 4.085   -7.251  -4.658  1.00 36.93 ?  295 ASP   B OD1 1 
ATOM   4467 O  OD2 . ASP   B 1 295 ? 2.078   -7.368  -3.761  1.00 33.15 ?  295 ASP   B OD2 1 
ATOM   4468 N  N   . VAL   B 1 296 ? 5.449   -10.776 -1.193  1.00 36.06 ?  296 VAL   B N   1 
ATOM   4469 C  CA  . VAL   B 1 296 ? 6.008   -11.359 0.025   1.00 31.07 ?  296 VAL   B CA  1 
ATOM   4470 C  C   . VAL   B 1 296 ? 7.494   -11.650 -0.158  1.00 34.63 ?  296 VAL   B C   1 
ATOM   4471 O  O   . VAL   B 1 296 ? 8.322   -11.300 0.690   1.00 35.92 ?  296 VAL   B O   1 
ATOM   4472 C  CB  . VAL   B 1 296 ? 5.234   -12.631 0.411   1.00 30.27 ?  296 VAL   B CB  1 
ATOM   4473 C  CG1 . VAL   B 1 296 ? 5.891   -13.305 1.596   1.00 34.47 ?  296 VAL   B CG1 1 
ATOM   4474 C  CG2 . VAL   B 1 296 ? 3.769   -12.303 0.704   1.00 28.19 ?  296 VAL   B CG2 1 
ATOM   4475 N  N   . VAL   B 1 297 ? 7.846   -12.316 -1.261  1.00 32.93 ?  297 VAL   B N   1 
ATOM   4476 C  CA  . VAL   B 1 297 ? 9.245   -12.612 -1.556  1.00 36.82 ?  297 VAL   B CA  1 
ATOM   4477 C  C   . VAL   B 1 297 ? 10.069  -11.332 -1.585  1.00 36.58 ?  297 VAL   B C   1 
ATOM   4478 O  O   . VAL   B 1 297 ? 11.175  -11.279 -1.035  1.00 41.41 ?  297 VAL   B O   1 
ATOM   4479 C  CB  . VAL   B 1 297 ? 9.355   -13.388 -2.883  1.00 37.61 ?  297 VAL   B CB  1 
ATOM   4480 C  CG1 . VAL   B 1 297 ? 10.804  -13.478 -3.336  1.00 37.44 ?  297 VAL   B CG1 1 
ATOM   4481 C  CG2 . VAL   B 1 297 ? 8.762   -14.781 -2.738  1.00 34.93 ?  297 VAL   B CG2 1 
ATOM   4482 N  N   . ARG   B 1 298 ? 9.539   -10.274 -2.208  1.00 36.01 ?  298 ARG   B N   1 
ATOM   4483 C  CA  . ARG   B 1 298 ? 10.301  -9.035  -2.333  1.00 38.62 ?  298 ARG   B CA  1 
ATOM   4484 C  C   . ARG   B 1 298 ? 10.543  -8.394  -0.971  1.00 43.05 ?  298 ARG   B C   1 
ATOM   4485 O  O   . ARG   B 1 298 ? 11.680  -8.049  -0.631  1.00 38.32 ?  298 ARG   B O   1 
ATOM   4486 C  CB  . ARG   B 1 298 ? 9.585   -8.058  -3.270  1.00 35.94 ?  298 ARG   B CB  1 
ATOM   4487 N  N   . GLN   B 1 299 ? 9.486   -8.231  -0.174  1.00 35.39 ?  299 GLN   B N   1 
ATOM   4488 C  CA  . GLN   B 1 299 ? 9.641   -7.539  1.100   1.00 38.72 ?  299 GLN   B CA  1 
ATOM   4489 C  C   . GLN   B 1 299 ? 10.490  -8.348  2.076   1.00 44.35 ?  299 GLN   B C   1 
ATOM   4490 O  O   . GLN   B 1 299 ? 11.228  -7.777  2.893   1.00 44.35 ?  299 GLN   B O   1 
ATOM   4491 C  CB  . GLN   B 1 299 ? 8.269   -7.232  1.700   1.00 35.75 ?  299 GLN   B CB  1 
ATOM   4492 C  CG  . GLN   B 1 299 ? 8.368   -6.570  3.051   1.00 31.59 ?  299 GLN   B CG  1 
ATOM   4493 C  CD  . GLN   B 1 299 ? 7.056   -6.013  3.540   1.00 33.03 ?  299 GLN   B CD  1 
ATOM   4494 O  OE1 . GLN   B 1 299 ? 6.956   -5.586  4.687   1.00 31.12 ?  299 GLN   B OE1 1 
ATOM   4495 N  NE2 . GLN   B 1 299 ? 6.035   -6.010  2.671   1.00 30.27 ?  299 GLN   B NE2 1 
ATOM   4496 N  N   . CYS   B 1 300 ? 10.401  -9.677  2.012   1.00 42.32 ?  300 CYS   B N   1 
ATOM   4497 C  CA  . CYS   B 1 300 ? 11.195  -10.553 2.863   1.00 44.66 ?  300 CYS   B CA  1 
ATOM   4498 C  C   . CYS   B 1 300 ? 12.530  -10.940 2.223   1.00 48.66 ?  300 CYS   B C   1 
ATOM   4499 O  O   . CYS   B 1 300 ? 13.056  -12.024 2.507   1.00 52.42 ?  300 CYS   B O   1 
ATOM   4500 C  CB  . CYS   B 1 300 ? 10.384  -11.799 3.226   1.00 42.20 ?  300 CYS   B CB  1 
ATOM   4501 S  SG  . CYS   B 1 300 ? 8.826   -11.472 4.123   1.00 51.89 ?  300 CYS   B SG  1 
ATOM   4502 N  N   . SER   B 1 301 ? 13.096  -10.081 1.368   1.00 44.27 ?  301 SER   B N   1 
ATOM   4503 C  CA  . SER   B 1 301 ? 14.395  -10.356 0.763   1.00 42.37 ?  301 SER   B CA  1 
ATOM   4504 C  C   . SER   B 1 301 ? 15.066  -9.094  0.231   1.00 50.20 ?  301 SER   B C   1 
ATOM   4505 O  O   . SER   B 1 301 ? 16.233  -9.133  -0.170  1.00 48.15 ?  301 SER   B O   1 
ATOM   4506 C  CB  . SER   B 1 301 ? 14.259  -11.375 -0.369  1.00 48.25 ?  301 SER   B CB  1 
ATOM   4507 O  OG  . SER   B 1 301 ? 13.987  -10.731 -1.603  1.00 47.79 ?  301 SER   B OG  1 
ATOM   4508 N  N   . GLY   B 1 302 ? 14.351  -7.975  0.212   1.00 48.57 ?  302 GLY   B N   1 
ATOM   4509 C  CA  . GLY   B 1 302 ? 14.893  -6.743  -0.345  1.00 51.69 ?  302 GLY   B CA  1 
ATOM   4510 C  C   . GLY   B 1 302 ? 14.903  -6.706  -1.866  1.00 47.34 ?  302 GLY   B C   1 
ATOM   4511 O  O   . GLY   B 1 302 ? 14.498  -5.719  -2.494  1.00 46.65 ?  302 GLY   B O   1 
HETATM 4512 N  N1  . A1D50 C 2 .   ? 16.622  -5.953  10.972  1.00 29.17 ?  401 A1D50 A N1  1 
HETATM 4513 N  N3  . A1D50 C 2 .   ? 21.859  -4.129  15.239  1.00 27.12 ?  401 A1D50 A N3  1 
HETATM 4514 C  C4  . A1D50 C 2 .   ? 19.336  -5.494  11.149  1.00 30.10 ?  401 A1D50 A C4  1 
HETATM 4515 C  C5  . A1D50 C 2 .   ? 18.859  -6.810  10.897  1.00 32.23 ?  401 A1D50 A C5  1 
HETATM 4516 C  C6  . A1D50 C 2 .   ? 19.717  -7.909  10.715  1.00 31.91 ?  401 A1D50 A C6  1 
HETATM 4517 C  C7  . A1D50 C 2 .   ? 19.213  -9.150  10.450  1.00 38.58 ?  401 A1D50 A C7  1 
HETATM 4518 C  C8  . A1D50 C 2 .   ? 17.838  -9.345  10.361  1.00 39.81 ?  401 A1D50 A C8  1 
HETATM 4519 C  C10 . A1D50 C 2 .   ? 20.807  -5.204  11.309  1.00 31.82 ?  401 A1D50 A C10 1 
HETATM 4520 C  C13 . A1D50 C 2 .   ? 24.724  -3.491  12.928  1.00 27.49 ?  401 A1D50 A C13 1 
HETATM 4521 C  C15 . A1D50 C 2 .   ? 24.178  -4.933  14.891  1.00 29.82 ?  401 A1D50 A C15 1 
HETATM 4522 C  C17 . A1D50 C 2 .   ? 21.416  -4.445  16.492  1.00 34.66 ?  401 A1D50 A C17 1 
HETATM 4523 C  C20 . A1D50 C 2 .   ? 20.596  -5.104  19.057  1.00 43.00 ?  401 A1D50 A C20 1 
HETATM 4524 C  C21 . A1D50 C 2 .   ? 20.093  -5.806  18.002  1.00 33.53 ?  401 A1D50 A C21 1 
HETATM 4525 C  C22 . A1D50 C 2 .   ? 20.507  -5.505  16.701  1.00 38.57 ?  401 A1D50 A C22 1 
HETATM 4526 C  C24 . A1D50 C 2 .   ? 19.592  -8.265  14.237  1.00 34.47 ?  401 A1D50 A C24 1 
HETATM 4527 C  C26 . A1D50 C 2 .   ? 21.422  -9.571  15.732  1.00 43.85 ?  401 A1D50 A C26 1 
HETATM 4528 C  C1  . A1D50 C 2 .   ? 17.471  -7.027  10.803  1.00 34.40 ?  401 A1D50 A C1  1 
HETATM 4529 C  C11 . A1D50 C 2 .   ? 22.587  -4.820  12.951  1.00 28.45 ?  401 A1D50 A C11 1 
HETATM 4530 C  C12 . A1D50 C 2 .   ? 23.280  -3.561  12.442  1.00 26.55 ?  401 A1D50 A C12 1 
HETATM 4531 C  C14 . A1D50 C 2 .   ? 24.787  -3.617  14.430  1.00 27.94 ?  401 A1D50 A C14 1 
HETATM 4532 C  C16 . A1D50 C 2 .   ? 22.718  -5.018  14.461  1.00 32.55 ?  401 A1D50 A C16 1 
HETATM 4533 C  C18 . A1D50 C 2 .   ? 21.912  -3.747  17.613  1.00 41.77 ?  401 A1D50 A C18 1 
HETATM 4534 C  C19 . A1D50 C 2 .   ? 21.494  -4.076  18.896  1.00 36.85 ?  401 A1D50 A C19 1 
HETATM 4535 C  C2  . A1D50 C 2 .   ? 17.021  -4.684  11.230  1.00 30.86 ?  401 A1D50 A C2  1 
HETATM 4536 C  C23 . A1D50 C 2 .   ? 19.899  -6.267  15.556  1.00 32.76 ?  401 A1D50 A C23 1 
HETATM 4537 C  C25 . A1D50 C 2 .   ? 19.414  -9.740  14.501  1.00 39.02 ?  401 A1D50 A C25 1 
HETATM 4538 C  C27 . A1D50 C 2 .   ? 20.605  -8.523  16.449  1.00 38.17 ?  401 A1D50 A C27 1 
HETATM 4539 C  C3  . A1D50 C 2 .   ? 18.445  -4.472  11.338  1.00 31.10 ?  401 A1D50 A C3  1 
HETATM 4540 C  C9  . A1D50 C 2 .   ? 16.964  -8.301  10.533  1.00 35.41 ?  401 A1D50 A C9  1 
HETATM 4541 N  N2  . A1D50 C 2 .   ? 21.186  -4.871  12.545  1.00 27.85 ?  401 A1D50 A N2  1 
HETATM 4542 N  N4  . A1D50 C 2 .   ? 22.842  -2.649  17.485  1.00 44.81 ?  401 A1D50 A N4  1 
HETATM 4543 N  N5  . A1D50 C 2 .   ? 20.035  -7.596  15.463  1.00 37.56 ?  401 A1D50 A N5  1 
HETATM 4544 O  O1  . A1D50 C 2 .   ? 16.181  -3.771  11.386  1.00 24.11 ?  401 A1D50 A O1  1 
HETATM 4545 O  O2  . A1D50 C 2 .   ? 21.599  -5.286  10.374  1.00 28.73 ?  401 A1D50 A O2  1 
HETATM 4546 O  O3  . A1D50 C 2 .   ? 19.298  -5.625  14.703  1.00 32.21 ?  401 A1D50 A O3  1 
HETATM 4547 O  O4  . A1D50 C 2 .   ? 20.641  -10.375 14.847  1.00 50.56 ?  401 A1D50 A O4  1 
HETATM 4548 O  O5  . A1D50 C 2 .   ? 23.351  -2.205  18.506  1.00 39.76 -1 401 A1D50 A O5  1 
HETATM 4549 O  O6  . A1D50 C 2 .   ? 23.006  -2.154  16.380  1.00 41.11 ?  401 A1D50 A O6  1 
HETATM 4550 BR BR1 . A1D50 C 2 .   ? 20.047  -5.544  20.823  1.00 38.28 ?  401 A1D50 A BR1 1 
HETATM 4551 N  N1  . A1D50 D 2 .   ? -13.840 10.354  -5.600  1.00 26.84 ?  401 A1D50 B N1  1 
HETATM 4552 N  N3  . A1D50 D 2 .   ? -16.839 10.545  -11.954 1.00 30.16 ?  401 A1D50 B N3  1 
HETATM 4553 C  C4  . A1D50 D 2 .   ? -14.378 11.883  -7.845  1.00 31.30 ?  401 A1D50 B C4  1 
HETATM 4554 C  C5  . A1D50 D 2 .   ? -14.944 12.244  -6.579  1.00 35.24 ?  401 A1D50 B C5  1 
HETATM 4555 C  C6  . A1D50 D 2 .   ? -15.778 13.362  -6.406  1.00 35.09 ?  401 A1D50 B C6  1 
HETATM 4556 C  C7  . A1D50 D 2 .   ? -16.284 13.669  -5.174  1.00 36.76 ?  401 A1D50 B C7  1 
HETATM 4557 C  C8  . A1D50 D 2 .   ? -15.984 12.879  -4.069  1.00 31.90 ?  401 A1D50 B C8  1 
HETATM 4558 C  C10 . A1D50 D 2 .   ? -14.672 12.679  -9.096  1.00 33.63 ?  401 A1D50 B C10 1 
HETATM 4559 C  C13 . A1D50 D 2 .   ? -15.357 13.496  -13.553 1.00 32.31 ?  401 A1D50 B C13 1 
HETATM 4560 C  C15 . A1D50 D 2 .   ? -17.637 12.539  -13.152 1.00 36.31 ?  401 A1D50 B C15 1 
HETATM 4561 C  C17 . A1D50 D 2 .   ? -17.799 9.592   -11.957 1.00 27.45 ?  401 A1D50 B C17 1 
HETATM 4562 C  C20 . A1D50 D 2 .   ? -19.817 7.698   -11.931 1.00 40.43 ?  401 A1D50 B C20 1 
HETATM 4563 C  C21 . A1D50 D 2 .   ? -19.451 8.297   -10.759 1.00 33.53 ?  401 A1D50 B C21 1 
HETATM 4564 C  C22 . A1D50 D 2 .   ? -18.442 9.265   -10.750 1.00 32.34 ?  401 A1D50 B C22 1 
HETATM 4565 C  C24 . A1D50 D 2 .   ? -20.386 10.608  -8.881  1.00 35.04 ?  401 A1D50 B C24 1 
HETATM 4566 C  C26 . A1D50 D 2 .   ? -19.753 11.378  -6.544  1.00 31.83 ?  401 A1D50 B C26 1 
HETATM 4567 C  C1  . A1D50 D 2 .   ? -14.651 11.459  -5.448  1.00 32.13 ?  401 A1D50 B C1  1 
HETATM 4568 C  C11 . A1D50 D 2 .   ? -15.989 12.754  -11.209 1.00 31.99 ?  401 A1D50 B C11 1 
HETATM 4569 C  C12 . A1D50 D 2 .   ? -14.855 12.991  -12.200 1.00 27.49 ?  401 A1D50 B C12 1 
HETATM 4570 C  C14 . A1D50 D 2 .   ? -16.843 13.781  -13.538 1.00 35.36 ?  401 A1D50 B C14 1 
HETATM 4571 C  C16 . A1D50 D 2 .   ? -17.148 11.965  -11.826 1.00 31.18 ?  401 A1D50 B C16 1 
HETATM 4572 C  C18 . A1D50 D 2 .   ? -18.207 8.956   -13.153 1.00 33.84 ?  401 A1D50 B C18 1 
HETATM 4573 C  C19 . A1D50 D 2 .   ? -19.216 8.000   -13.132 1.00 32.70 ?  401 A1D50 B C19 1 
HETATM 4574 C  C2  . A1D50 D 2 .   ? -13.281 9.959   -6.771  1.00 34.15 ?  401 A1D50 B C2  1 
HETATM 4575 C  C23 . A1D50 D 2 .   ? -18.027 9.923   -9.461  1.00 31.80 ?  401 A1D50 B C23 1 
HETATM 4576 C  C25 . A1D50 D 2 .   ? -20.780 12.030  -8.565  1.00 35.04 ?  401 A1D50 B C25 1 
HETATM 4577 C  C27 . A1D50 D 2 .   ? -18.539 10.911  -7.310  1.00 27.07 ?  401 A1D50 B C27 1 
HETATM 4578 C  C3  . A1D50 D 2 .   ? -13.580 10.767  -7.933  1.00 27.54 ?  401 A1D50 B C3  1 
HETATM 4579 C  C9  . A1D50 D 2 .   ? -15.178 11.778  -4.191  1.00 33.49 ?  401 A1D50 B C9  1 
HETATM 4580 N  N2  . A1D50 D 2 .   ? -15.516 12.102  -9.982  1.00 28.09 ?  401 A1D50 B N2  1 
HETATM 4581 N  N4  . A1D50 D 2 .   ? -17.584 9.235   -14.438 1.00 37.10 ?  401 A1D50 B N4  1 
HETATM 4582 N  N5  . A1D50 D 2 .   ? -18.949 10.432  -8.633  1.00 31.30 ?  401 A1D50 B N5  1 
HETATM 4583 O  O1  . A1D50 D 2 .   ? -12.558 8.940   -6.804  1.00 29.60 ?  401 A1D50 B O1  1 
HETATM 4584 O  O2  . A1D50 D 2 .   ? -14.175 13.791  -9.279  1.00 33.26 ?  401 A1D50 B O2  1 
HETATM 4585 O  O3  . A1D50 D 2 .   ? -16.827 10.017  -9.212  1.00 33.18 ?  401 A1D50 B O3  1 
HETATM 4586 O  O4  . A1D50 D 2 .   ? -20.451 12.414  -7.230  1.00 40.37 ?  401 A1D50 B O4  1 
HETATM 4587 O  O5  . A1D50 D 2 .   ? -18.098 8.756   -15.434 1.00 36.72 -1 401 A1D50 B O5  1 
HETATM 4588 O  O6  . A1D50 D 2 .   ? -16.534 9.867   -14.464 1.00 38.13 ?  401 A1D50 B O6  1 
HETATM 4589 BR BR1 . A1D50 D 2 .   ? -21.206 6.399   -11.921 1.00 37.37 ?  401 A1D50 B BR1 1 
HETATM 4590 O  O   . HOH   E 3 .   ? -18.784 14.892  29.741  1.00 40.34 ?  501 HOH   A O   1 
HETATM 4591 O  O   . HOH   E 3 .   ? 26.683  20.022  -5.974  1.00 34.39 ?  502 HOH   A O   1 
HETATM 4592 O  O   . HOH   E 3 .   ? 12.409  21.103  -1.075  1.00 43.05 ?  503 HOH   A O   1 
HETATM 4593 O  O   . HOH   E 3 .   ? 34.621  3.366   27.552  1.00 36.82 ?  504 HOH   A O   1 
HETATM 4594 O  O   . HOH   E 3 .   ? -18.219 10.334  36.961  1.00 30.83 ?  505 HOH   A O   1 
HETATM 4595 O  O   . HOH   E 3 .   ? -13.874 10.009  37.410  1.00 34.44 ?  506 HOH   A O   1 
HETATM 4596 O  O   . HOH   E 3 .   ? 11.211  -6.383  5.158   1.00 32.15 ?  507 HOH   A O   1 
HETATM 4597 O  O   . HOH   E 3 .   ? -1.312  10.231  27.133  1.00 39.36 ?  508 HOH   A O   1 
HETATM 4598 O  O   . HOH   E 3 .   ? 15.568  15.386  -3.375  1.00 32.16 ?  509 HOH   A O   1 
HETATM 4599 O  O   . HOH   E 3 .   ? 2.700   11.156  9.224   1.00 28.05 ?  510 HOH   A O   1 
HETATM 4600 O  O   . HOH   E 3 .   ? 39.417  10.130  13.338  1.00 31.63 ?  511 HOH   A O   1 
HETATM 4601 O  O   . HOH   E 3 .   ? -15.428 -5.224  28.594  1.00 26.15 ?  512 HOH   A O   1 
HETATM 4602 O  O   . HOH   E 3 .   ? 38.465  0.351   20.610  1.00 31.03 ?  513 HOH   A O   1 
HETATM 4603 O  O   . HOH   E 3 .   ? 12.614  -3.131  4.280   1.00 28.21 ?  514 HOH   A O   1 
HETATM 4604 O  O   . HOH   E 3 .   ? -22.231 15.177  19.865  1.00 38.17 ?  515 HOH   A O   1 
HETATM 4605 O  O   . HOH   E 3 .   ? -22.557 -0.065  26.308  1.00 33.65 ?  516 HOH   A O   1 
HETATM 4606 O  O   . HOH   E 3 .   ? 15.801  14.796  14.106  1.00 36.19 ?  517 HOH   A O   1 
HETATM 4607 O  O   . HOH   E 3 .   ? -14.750 15.630  31.448  1.00 33.46 ?  518 HOH   A O   1 
HETATM 4608 O  O   . HOH   E 3 .   ? -20.431 -3.938  18.188  1.00 33.21 ?  519 HOH   A O   1 
HETATM 4609 O  O   . HOH   E 3 .   ? 11.959  -7.059  22.242  1.00 41.72 ?  520 HOH   A O   1 
HETATM 4610 O  O   . HOH   E 3 .   ? 37.004  9.881   18.256  1.00 33.28 ?  521 HOH   A O   1 
HETATM 4611 O  O   . HOH   E 3 .   ? 34.084  7.648   -1.100  1.00 34.47 ?  522 HOH   A O   1 
HETATM 4612 O  O   . HOH   E 3 .   ? -5.397  19.275  15.572  1.00 47.09 ?  523 HOH   A O   1 
HETATM 4613 O  O   . HOH   E 3 .   ? -16.173 1.942   7.599   1.00 36.20 ?  524 HOH   A O   1 
HETATM 4614 O  O   . HOH   E 3 .   ? 17.365  -8.347  18.396  1.00 35.88 ?  525 HOH   A O   1 
HETATM 4615 O  O   . HOH   E 3 .   ? -15.795 12.132  36.294  1.00 33.15 ?  526 HOH   A O   1 
HETATM 4616 O  O   . HOH   E 3 .   ? -19.106 6.535   34.599  1.00 28.92 ?  527 HOH   A O   1 
HETATM 4617 O  O   . HOH   E 3 .   ? -8.404  2.580   35.452  1.00 36.26 ?  528 HOH   A O   1 
HETATM 4618 O  O   . HOH   E 3 .   ? -0.827  15.003  25.852  1.00 43.44 ?  529 HOH   A O   1 
HETATM 4619 O  O   . HOH   E 3 .   ? 33.763  13.319  -4.667  1.00 38.03 ?  530 HOH   A O   1 
HETATM 4620 O  O   . HOH   E 3 .   ? -8.903  17.569  14.721  1.00 38.55 ?  531 HOH   A O   1 
HETATM 4621 O  O   . HOH   E 3 .   ? 32.334  -7.724  11.511  1.00 48.24 ?  532 HOH   A O   1 
HETATM 4622 O  O   . HOH   E 3 .   ? 13.683  3.687   19.213  1.00 29.94 ?  533 HOH   A O   1 
HETATM 4623 O  O   . HOH   E 3 .   ? 24.793  3.501   15.712  1.00 26.30 ?  534 HOH   A O   1 
HETATM 4624 O  O   . HOH   E 3 .   ? 35.543  -1.033  23.841  1.00 34.81 ?  535 HOH   A O   1 
HETATM 4625 O  O   . HOH   E 3 .   ? 4.801   1.279   14.473  1.00 27.13 ?  536 HOH   A O   1 
HETATM 4626 O  O   . HOH   E 3 .   ? 8.673   14.644  11.088  1.00 33.91 ?  537 HOH   A O   1 
HETATM 4627 O  O   . HOH   E 3 .   ? 20.732  8.040   22.552  1.00 29.71 ?  538 HOH   A O   1 
HETATM 4628 O  O   . HOH   E 3 .   ? -9.415  9.380   38.853  1.00 36.03 ?  539 HOH   A O   1 
HETATM 4629 O  O   . HOH   E 3 .   ? -11.601 1.480   38.347  1.00 30.30 ?  540 HOH   A O   1 
HETATM 4630 O  O   . HOH   E 3 .   ? 21.424  5.603   23.479  1.00 29.86 ?  541 HOH   A O   1 
HETATM 4631 O  O   . HOH   E 3 .   ? -16.691 4.723   7.027   1.00 39.02 ?  542 HOH   A O   1 
HETATM 4632 O  O   . HOH   E 3 .   ? 26.540  2.187   22.761  1.00 34.53 ?  543 HOH   A O   1 
HETATM 4633 O  O   . HOH   E 3 .   ? -22.696 12.164  10.415  1.00 34.22 ?  544 HOH   A O   1 
HETATM 4634 O  O   . HOH   E 3 .   ? -18.927 9.829   32.734  1.00 26.20 ?  545 HOH   A O   1 
HETATM 4635 O  O   . HOH   E 3 .   ? -5.596  5.845   14.007  1.00 23.76 ?  546 HOH   A O   1 
HETATM 4636 O  O   . HOH   E 3 .   ? -0.636  7.519   9.277   1.00 33.04 ?  547 HOH   A O   1 
HETATM 4637 O  O   . HOH   E 3 .   ? -3.059  1.001   31.487  1.00 40.80 ?  548 HOH   A O   1 
HETATM 4638 O  O   . HOH   E 3 .   ? 23.613  18.979  6.177   1.00 38.34 ?  549 HOH   A O   1 
HETATM 4639 O  O   . HOH   E 3 .   ? -1.606  7.709   6.625   1.00 30.12 ?  550 HOH   A O   1 
HETATM 4640 O  O   . HOH   E 3 .   ? -23.112 14.188  13.960  1.00 42.52 ?  551 HOH   A O   1 
HETATM 4641 O  O   . HOH   E 3 .   ? -8.363  11.989  33.300  1.00 31.35 ?  552 HOH   A O   1 
HETATM 4642 O  O   . HOH   E 3 .   ? 19.072  -8.059  3.049   1.00 46.05 ?  553 HOH   A O   1 
HETATM 4643 O  O   . HOH   E 3 .   ? -17.715 -8.587  18.796  1.00 41.52 ?  554 HOH   A O   1 
HETATM 4644 O  O   . HOH   E 3 .   ? 11.955  12.303  23.788  1.00 41.96 ?  555 HOH   A O   1 
HETATM 4645 O  O   . HOH   E 3 .   ? -29.179 9.974   25.878  1.00 39.56 ?  556 HOH   A O   1 
HETATM 4646 O  O   . HOH   E 3 .   ? -15.641 -0.503  28.080  1.00 26.62 ?  557 HOH   A O   1 
HETATM 4647 O  O   . HOH   E 3 .   ? 6.989   -2.947  20.539  1.00 38.04 ?  558 HOH   A O   1 
HETATM 4648 O  O   . HOH   E 3 .   ? -24.255 9.620   29.189  1.00 34.81 ?  559 HOH   A O   1 
HETATM 4649 O  O   . HOH   E 3 .   ? 1.733   2.552   4.232   1.00 33.51 ?  560 HOH   A O   1 
HETATM 4650 O  O   . HOH   E 3 .   ? -19.739 6.519   28.184  1.00 30.44 ?  561 HOH   A O   1 
HETATM 4651 O  O   . HOH   E 3 .   ? 28.820  10.415  20.769  1.00 36.13 ?  562 HOH   A O   1 
HETATM 4652 O  O   . HOH   E 3 .   ? 21.980  13.332  -5.871  1.00 35.62 ?  563 HOH   A O   1 
HETATM 4653 O  O   . HOH   E 3 .   ? 11.748  18.720  17.635  1.00 42.87 ?  564 HOH   A O   1 
HETATM 4654 O  O   . HOH   E 3 .   ? -19.906 7.821   30.937  1.00 35.46 ?  565 HOH   A O   1 
HETATM 4655 O  O   . HOH   E 3 .   ? 23.708  4.505   22.635  1.00 30.17 ?  566 HOH   A O   1 
HETATM 4656 O  O   . HOH   E 3 .   ? -13.376 14.630  34.045  1.00 36.66 ?  567 HOH   A O   1 
HETATM 4657 O  O   . HOH   E 3 .   ? -2.870  18.345  28.434  1.00 46.81 ?  568 HOH   A O   1 
HETATM 4658 O  O   . HOH   E 3 .   ? 22.155  -2.626  8.621   1.00 31.72 ?  569 HOH   A O   1 
HETATM 4659 O  O   . HOH   E 3 .   ? -13.164 -5.937  29.327  1.00 31.76 ?  570 HOH   A O   1 
HETATM 4660 O  O   . HOH   E 3 .   ? 0.056   11.378  20.624  1.00 31.72 ?  571 HOH   A O   1 
HETATM 4661 O  O   . HOH   E 3 .   ? 25.268  -2.739  9.082   1.00 36.88 ?  572 HOH   A O   1 
HETATM 4662 O  O   . HOH   E 3 .   ? 37.865  11.054  15.866  1.00 33.46 ?  573 HOH   A O   1 
HETATM 4663 O  O   . HOH   E 3 .   ? -6.664  4.531   34.849  1.00 41.29 ?  574 HOH   A O   1 
HETATM 4664 O  O   . HOH   E 3 .   ? -23.255 13.207  18.703  1.00 39.93 ?  575 HOH   A O   1 
HETATM 4665 O  O   . HOH   E 3 .   ? 7.138   16.914  11.525  1.00 41.34 ?  576 HOH   A O   1 
HETATM 4666 O  O   . HOH   E 3 .   ? 25.678  3.692   24.732  1.00 33.66 ?  577 HOH   A O   1 
HETATM 4667 O  O   . HOH   E 3 .   ? -9.190  1.892   37.818  1.00 33.73 ?  578 HOH   A O   1 
HETATM 4668 O  O   . HOH   E 3 .   ? 19.170  -9.315  20.260  1.00 37.51 ?  579 HOH   A O   1 
HETATM 4669 O  O   . HOH   F 3 .   ? -1.824  -1.166  -21.222 1.00 35.67 ?  501 HOH   B O   1 
HETATM 4670 O  O   . HOH   F 3 .   ? 11.796  -12.985 11.862  1.00 48.85 ?  502 HOH   B O   1 
HETATM 4671 O  O   . HOH   F 3 .   ? 10.494  6.586   -7.408  1.00 35.85 ?  503 HOH   B O   1 
HETATM 4672 O  O   . HOH   F 3 .   ? -1.326  0.340   -18.731 1.00 29.23 ?  504 HOH   B O   1 
HETATM 4673 O  O   . HOH   F 3 .   ? -8.097  -2.695  -3.702  1.00 29.39 ?  505 HOH   B O   1 
HETATM 4674 O  O   . HOH   F 3 .   ? -4.242  -2.578  -22.850 1.00 30.18 ?  506 HOH   B O   1 
HETATM 4675 O  O   . HOH   F 3 .   ? 10.476  11.077  -13.003 1.00 36.96 ?  507 HOH   B O   1 
HETATM 4676 O  O   . HOH   F 3 .   ? 14.023  5.077   -15.244 1.00 33.02 ?  508 HOH   B O   1 
HETATM 4677 O  O   . HOH   F 3 .   ? 2.190   -2.168  -13.542 1.00 32.83 ?  509 HOH   B O   1 
HETATM 4678 O  O   . HOH   F 3 .   ? 3.142   -8.560  -7.328  1.00 38.35 ?  510 HOH   B O   1 
HETATM 4679 O  O   . HOH   F 3 .   ? -0.485  9.898   -9.867  1.00 31.30 ?  511 HOH   B O   1 
HETATM 4680 O  O   . HOH   F 3 .   ? -2.170  -12.668 -7.094  1.00 30.38 ?  512 HOH   B O   1 
HETATM 4681 O  O   . HOH   F 3 .   ? -2.688  6.065   -24.207 1.00 34.10 ?  513 HOH   B O   1 
HETATM 4682 O  O   . HOH   F 3 .   ? -17.634 -4.977  -10.494 1.00 34.85 ?  514 HOH   B O   1 
HETATM 4683 O  O   . HOH   F 3 .   ? 3.054   -4.256  -6.217  1.00 28.54 ?  515 HOH   B O   1 
HETATM 4684 O  O   . HOH   F 3 .   ? 5.559   -6.249  0.024   1.00 34.30 ?  516 HOH   B O   1 
HETATM 4685 O  O   . HOH   F 3 .   ? -27.092 2.527   -16.004 1.00 35.23 ?  517 HOH   B O   1 
HETATM 4686 O  O   . HOH   F 3 .   ? -20.823 6.976   -7.615  1.00 27.15 ?  518 HOH   B O   1 
HETATM 4687 O  O   . HOH   F 3 .   ? -12.516 2.511   -1.513  1.00 29.32 ?  519 HOH   B O   1 
HETATM 4688 O  O   . HOH   F 3 .   ? 8.637   13.452  -2.534  1.00 34.25 ?  520 HOH   B O   1 
HETATM 4689 O  O   . HOH   F 3 .   ? -23.154 14.914  -14.089 1.00 36.86 ?  521 HOH   B O   1 
HETATM 4690 O  O   . HOH   F 3 .   ? -2.205  -11.069 0.976   1.00 28.32 ?  522 HOH   B O   1 
HETATM 4691 O  O   . HOH   F 3 .   ? -21.007 0.464   -6.122  1.00 31.37 ?  523 HOH   B O   1 
HETATM 4692 O  O   . HOH   F 3 .   ? -11.767 -0.203  -12.468 1.00 28.08 ?  524 HOH   B O   1 
HETATM 4693 O  O   . HOH   F 3 .   ? 3.421   -4.309  -0.082  1.00 35.38 ?  525 HOH   B O   1 
HETATM 4694 O  O   . HOH   F 3 .   ? -12.256 -5.715  -17.422 1.00 31.11 ?  526 HOH   B O   1 
HETATM 4695 O  O   . HOH   F 3 .   ? 1.205   -5.507  -1.844  1.00 31.20 ?  527 HOH   B O   1 
HETATM 4696 O  O   . HOH   F 3 .   ? -12.473 7.054   -27.685 1.00 28.65 ?  528 HOH   B O   1 
HETATM 4697 O  O   . HOH   F 3 .   ? -26.308 8.658   -12.161 1.00 38.49 ?  529 HOH   B O   1 
HETATM 4698 O  O   . HOH   F 3 .   ? -6.473  -17.182 -5.922  1.00 36.91 ?  530 HOH   B O   1 
HETATM 4699 O  O   . HOH   F 3 .   ? 0.827   6.576   -26.337 1.00 39.28 ?  531 HOH   B O   1 
HETATM 4700 O  O   . HOH   F 3 .   ? -15.725 -3.595  -4.604  1.00 32.53 ?  532 HOH   B O   1 
HETATM 4701 O  O   . HOH   F 3 .   ? -12.814 9.573   -18.935 1.00 27.25 ?  533 HOH   B O   1 
HETATM 4702 O  O   . HOH   F 3 .   ? -24.174 5.567   -10.248 1.00 31.64 ?  534 HOH   B O   1 
HETATM 4703 O  O   . HOH   F 3 .   ? -11.520 14.503  -10.328 1.00 33.76 ?  535 HOH   B O   1 
HETATM 4704 O  O   . HOH   F 3 .   ? -16.511 4.077   -21.566 1.00 27.51 ?  536 HOH   B O   1 
HETATM 4705 O  O   . HOH   F 3 .   ? 1.430   -7.293  -8.961  1.00 39.93 ?  537 HOH   B O   1 
HETATM 4706 O  O   . HOH   F 3 .   ? -4.898  18.005  -32.843 1.00 41.44 ?  538 HOH   B O   1 
HETATM 4707 O  O   . HOH   F 3 .   ? 10.960  4.223   -21.841 1.00 33.16 ?  539 HOH   B O   1 
HETATM 4708 O  O   . HOH   F 3 .   ? -9.939  -7.410  -18.646 1.00 37.47 ?  540 HOH   B O   1 
HETATM 4709 O  O   . HOH   F 3 .   ? -22.805 7.547   -9.103  1.00 42.24 ?  541 HOH   B O   1 
HETATM 4710 O  O   . HOH   F 3 .   ? -12.350 -5.901  -20.126 1.00 30.70 ?  542 HOH   B O   1 
HETATM 4711 O  O   . HOH   F 3 .   ? -25.767 -3.945  -11.808 1.00 29.15 ?  543 HOH   B O   1 
# 
