data_9GC6
# 
_entry.id   9GC6 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9GC6         pdb_00009gc6 10.2210/pdb9gc6/pdb 
WWPDB D_1292140753 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2025-02-12 
2 'Structure model' 1 1 2025-02-26 
# 
_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             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GC6 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-01 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.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              david.hargreaves@astrazeneca.com 
_pdbx_contact_author.name_first         David 
_pdbx_contact_author.name_last          Hargreaves 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-4441-0039 
# 
_audit_author.name               'Hargreaves, D.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0003-4441-0039 
# 
_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            68 
_citation.language                  ? 
_citation.page_first                3700 
_citation.page_last                 3748 
_citation.title                     'Highly Optimized CNS Penetrant Inhibitors of EGFR Exon20 Insertion Mutations.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c02811 
_citation.pdbx_database_id_PubMed   39869768 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'McCoull, W.'              1  ? 
primary 'Thomson, C.'              2  ? 
primary 'Braybrooke, E.'           3  ? 
primary 'Chan, C.'                 4  ? 
primary 'Colclough, N.'            5  ? 
primary 'Cortes Gonzalez, M.A.'    6  ? 
primary 'Cosulich, S.'             7  ? 
primary 'Davies, N.L.'             8  ? 
primary 
;Floc'h, N.
;
9  ? 
primary 'Greenwood, R.'            10 ? 
primary 'Hargreaves, D.'           11 ? 
primary 'Huang, P.'                12 ? 
primary 'Hunt, T.A.'               13 ? 
primary 'Johnson, T.'              14 ? 
primary 'Johnstrom, P.'            15 ? 
primary 'Kettle, J.G.'             16 ? 
primary 'Kondrashov, M.'           17 ? 
primary 'Kostomiris, D.H.'         18 ? 
primary 'Li, S.'                   19 ? 
primary 'Lister, A.'               20 ? 
primary 'Martin, S.'               21 ? 
primary 'McKerrecher, D.'          22 ? 
primary 'McLean, N.'               23 ? 
primary 'Nissink, J.W.M.'          24 ? 
primary 'Orme, J.P.'               25 ? 
primary 'Orwig, P.'                26 ? 
primary 'Packer, M.J.'             27 ? 
primary 'Pearson, S.'              28 ? 
primary 'Qin, L.'                  29 ? 
primary 'Felisberto-Rodrigues, C.' 30 ? 
primary 'Savoca, A.'               31 ? 
primary 'Schou, M.'                32 ? 
primary 'Stokes, S.'               33 ? 
primary 'Swaih, A.M.'              34 ? 
primary 'Talbot, S.'               35 ? 
primary 'Tucker, M.J.'             36 ? 
primary 'Ward, R.A.'               37 ? 
primary 'Wadforth, E.'             38 ? 
primary 'Wang, C.'                 39 ? 
primary 'Wilson, J.'               40 ? 
primary 'Yang, Y.'                 41 ? 
# 
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 'Epidermal growth factor receptor' 37593.402 2   2.7.10.1 ? ? ? 
2 non-polymer syn 
'1-[2-[5-fluoranyl-4-(2-fluorophenyl)pyridin-2-yl]-3-pyrimidin-4-yl-4,6-dihydropyrrolo[3,4-d]imidazol-5-yl]propan-1-one' 432.425   
2   ?        ? ? ? 
3 water       nat water 18.015    168 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Proto-oncogene c-ErbB-1,Receptor tyrosine-protein kinase erbB-1' 
# 
_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       
;GSSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNP
HVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVK
ITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGER
LPQPPICTIDVYMIMRKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVD
ADEYLIPQQG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GSSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNP
HVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVK
ITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGER
LPQPPICTIDVYMIMRKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVD
ADEYLIPQQG
;
_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 '1-[2-[5-fluoranyl-4-(2-fluorophenyl)pyridin-2-yl]-3-pyrimidin-4-yl-4,6-dihydropyrrolo[3,4-d]imidazol-5-yl]propan-1-one' A1IZ9 
3 water                                                                                                                    HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   SER n 
1 4   GLY n 
1 5   GLU n 
1 6   ALA n 
1 7   PRO n 
1 8   ASN n 
1 9   GLN n 
1 10  ALA n 
1 11  LEU n 
1 12  LEU n 
1 13  ARG n 
1 14  ILE n 
1 15  LEU n 
1 16  LYS n 
1 17  GLU n 
1 18  THR n 
1 19  GLU n 
1 20  PHE n 
1 21  LYS n 
1 22  LYS n 
1 23  ILE n 
1 24  LYS n 
1 25  VAL n 
1 26  LEU n 
1 27  GLY n 
1 28  SER n 
1 29  GLY n 
1 30  ALA n 
1 31  PHE n 
1 32  GLY n 
1 33  THR n 
1 34  VAL n 
1 35  TYR n 
1 36  LYS n 
1 37  GLY n 
1 38  LEU n 
1 39  TRP n 
1 40  ILE n 
1 41  PRO n 
1 42  GLU n 
1 43  GLY n 
1 44  GLU n 
1 45  LYS n 
1 46  VAL n 
1 47  LYS n 
1 48  ILE n 
1 49  PRO n 
1 50  VAL n 
1 51  ALA n 
1 52  ILE n 
1 53  LYS n 
1 54  GLU n 
1 55  LEU n 
1 56  ARG n 
1 57  GLU n 
1 58  ALA n 
1 59  THR n 
1 60  SER n 
1 61  PRO n 
1 62  LYS n 
1 63  ALA n 
1 64  ASN n 
1 65  LYS n 
1 66  GLU n 
1 67  ILE n 
1 68  LEU n 
1 69  ASP n 
1 70  GLU n 
1 71  ALA n 
1 72  TYR n 
1 73  VAL n 
1 74  MET n 
1 75  ALA n 
1 76  SER n 
1 77  VAL n 
1 78  ASP n 
1 79  ASN n 
1 80  PRO n 
1 81  HIS n 
1 82  VAL n 
1 83  CYS n 
1 84  ARG n 
1 85  LEU n 
1 86  LEU n 
1 87  GLY n 
1 88  ILE n 
1 89  CYS n 
1 90  LEU n 
1 91  THR n 
1 92  SER n 
1 93  THR n 
1 94  VAL n 
1 95  GLN n 
1 96  LEU n 
1 97  ILE n 
1 98  THR n 
1 99  GLN n 
1 100 LEU n 
1 101 MET n 
1 102 PRO n 
1 103 PHE n 
1 104 GLY n 
1 105 CYS n 
1 106 LEU n 
1 107 LEU n 
1 108 ASP n 
1 109 TYR n 
1 110 VAL n 
1 111 ARG n 
1 112 GLU n 
1 113 HIS n 
1 114 LYS n 
1 115 ASP n 
1 116 ASN n 
1 117 ILE n 
1 118 GLY n 
1 119 SER n 
1 120 GLN n 
1 121 TYR n 
1 122 LEU n 
1 123 LEU n 
1 124 ASN n 
1 125 TRP n 
1 126 CYS n 
1 127 VAL n 
1 128 GLN n 
1 129 ILE n 
1 130 ALA n 
1 131 LYS n 
1 132 GLY n 
1 133 MET n 
1 134 ASN n 
1 135 TYR n 
1 136 LEU n 
1 137 GLU n 
1 138 ASP n 
1 139 ARG n 
1 140 ARG n 
1 141 LEU n 
1 142 VAL n 
1 143 HIS n 
1 144 ARG n 
1 145 ASP n 
1 146 LEU n 
1 147 ALA n 
1 148 ALA n 
1 149 ARG n 
1 150 ASN n 
1 151 VAL n 
1 152 LEU n 
1 153 VAL n 
1 154 LYS n 
1 155 THR n 
1 156 PRO n 
1 157 GLN n 
1 158 HIS n 
1 159 VAL n 
1 160 LYS n 
1 161 ILE n 
1 162 THR n 
1 163 ASP n 
1 164 PHE n 
1 165 GLY n 
1 166 LEU n 
1 167 ALA n 
1 168 LYS n 
1 169 LEU n 
1 170 LEU n 
1 171 GLY n 
1 172 ALA n 
1 173 GLU n 
1 174 GLU n 
1 175 LYS n 
1 176 GLU n 
1 177 TYR n 
1 178 HIS n 
1 179 ALA n 
1 180 GLU n 
1 181 GLY n 
1 182 GLY n 
1 183 LYS n 
1 184 VAL n 
1 185 PRO n 
1 186 ILE n 
1 187 LYS n 
1 188 TRP n 
1 189 MET n 
1 190 ALA n 
1 191 LEU n 
1 192 GLU n 
1 193 SER n 
1 194 ILE n 
1 195 LEU n 
1 196 HIS n 
1 197 ARG n 
1 198 ILE n 
1 199 TYR n 
1 200 THR n 
1 201 HIS n 
1 202 GLN n 
1 203 SER n 
1 204 ASP n 
1 205 VAL n 
1 206 TRP n 
1 207 SER n 
1 208 TYR n 
1 209 GLY n 
1 210 VAL n 
1 211 THR n 
1 212 VAL n 
1 213 TRP n 
1 214 GLU n 
1 215 LEU n 
1 216 MET n 
1 217 THR n 
1 218 PHE n 
1 219 GLY n 
1 220 SER n 
1 221 LYS n 
1 222 PRO n 
1 223 TYR n 
1 224 ASP n 
1 225 GLY n 
1 226 ILE n 
1 227 PRO n 
1 228 ALA n 
1 229 SER n 
1 230 GLU n 
1 231 ILE n 
1 232 SER n 
1 233 SER n 
1 234 ILE n 
1 235 LEU n 
1 236 GLU n 
1 237 LYS n 
1 238 GLY n 
1 239 GLU n 
1 240 ARG n 
1 241 LEU n 
1 242 PRO n 
1 243 GLN n 
1 244 PRO n 
1 245 PRO n 
1 246 ILE n 
1 247 CYS n 
1 248 THR n 
1 249 ILE n 
1 250 ASP n 
1 251 VAL n 
1 252 TYR n 
1 253 MET n 
1 254 ILE n 
1 255 MET n 
1 256 ARG n 
1 257 LYS n 
1 258 CYS n 
1 259 TRP n 
1 260 MET n 
1 261 ILE n 
1 262 ASP n 
1 263 ALA n 
1 264 ASP n 
1 265 SER n 
1 266 ARG n 
1 267 PRO n 
1 268 LYS n 
1 269 PHE n 
1 270 ARG n 
1 271 GLU n 
1 272 LEU n 
1 273 ILE n 
1 274 ILE n 
1 275 GLU n 
1 276 PHE n 
1 277 SER n 
1 278 LYS n 
1 279 MET n 
1 280 ALA n 
1 281 ARG n 
1 282 ASP n 
1 283 PRO n 
1 284 GLN n 
1 285 ARG n 
1 286 TYR n 
1 287 LEU n 
1 288 VAL n 
1 289 ILE n 
1 290 GLN n 
1 291 GLY n 
1 292 ASP n 
1 293 GLU n 
1 294 ARG n 
1 295 MET n 
1 296 HIS n 
1 297 LEU n 
1 298 PRO n 
1 299 SER n 
1 300 PRO n 
1 301 THR n 
1 302 ASP n 
1 303 SER n 
1 304 ASN n 
1 305 PHE n 
1 306 TYR n 
1 307 ARG n 
1 308 ALA n 
1 309 LEU n 
1 310 MET n 
1 311 ASP n 
1 312 GLU n 
1 313 GLU n 
1 314 ASP n 
1 315 MET n 
1 316 ASP n 
1 317 ASP n 
1 318 VAL n 
1 319 VAL n 
1 320 ASP n 
1 321 ALA n 
1 322 ASP n 
1 323 GLU n 
1 324 TYR n 
1 325 LEU n 
1 326 ILE n 
1 327 PRO n 
1 328 GLN n 
1 329 GLN n 
1 330 GLY 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                   330 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'EGFR, ERBB, ERBB1, HER1' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1IZ9 non-polymer         . 
'1-[2-[5-fluoranyl-4-(2-fluorophenyl)pyridin-2-yl]-3-pyrimidin-4-yl-4,6-dihydropyrrolo[3,4-d]imidazol-5-yl]propan-1-one' ? 
'C23 H18 F2 N6 O' 432.425 
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   GLY 1   693  ?    ?   ?   A . n 
A 1 2   SER 2   694  ?    ?   ?   A . n 
A 1 3   SER 3   695  ?    ?   ?   A . n 
A 1 4   GLY 4   696  ?    ?   ?   A . n 
A 1 5   GLU 5   697  ?    ?   ?   A . n 
A 1 6   ALA 6   698  698  ALA ALA A . n 
A 1 7   PRO 7   699  699  PRO PRO A . n 
A 1 8   ASN 8   700  700  ASN ASN A . n 
A 1 9   GLN 9   701  701  GLN GLN A . n 
A 1 10  ALA 10  702  702  ALA ALA A . n 
A 1 11  LEU 11  703  703  LEU LEU A . n 
A 1 12  LEU 12  704  704  LEU LEU A . n 
A 1 13  ARG 13  705  705  ARG ARG A . n 
A 1 14  ILE 14  706  706  ILE ILE A . n 
A 1 15  LEU 15  707  707  LEU LEU A . n 
A 1 16  LYS 16  708  708  LYS LYS A . n 
A 1 17  GLU 17  709  709  GLU GLU A . n 
A 1 18  THR 18  710  710  THR THR A . n 
A 1 19  GLU 19  711  711  GLU GLU A . n 
A 1 20  PHE 20  712  712  PHE PHE A . n 
A 1 21  LYS 21  713  713  LYS LYS A . n 
A 1 22  LYS 22  714  714  LYS LYS A . n 
A 1 23  ILE 23  715  715  ILE ILE A . n 
A 1 24  LYS 24  716  716  LYS LYS A . n 
A 1 25  VAL 25  717  717  VAL VAL A . n 
A 1 26  LEU 26  718  718  LEU LEU A . n 
A 1 27  GLY 27  719  719  GLY GLY A . n 
A 1 28  SER 28  720  720  SER SER A . n 
A 1 29  GLY 29  721  721  GLY GLY A . n 
A 1 30  ALA 30  722  722  ALA ALA A . n 
A 1 31  PHE 31  723  723  PHE PHE A . n 
A 1 32  GLY 32  724  724  GLY GLY A . n 
A 1 33  THR 33  725  725  THR THR A . n 
A 1 34  VAL 34  726  726  VAL VAL A . n 
A 1 35  TYR 35  727  727  TYR TYR A . n 
A 1 36  LYS 36  728  728  LYS LYS A . n 
A 1 37  GLY 37  729  729  GLY GLY A . n 
A 1 38  LEU 38  730  730  LEU LEU A . n 
A 1 39  TRP 39  731  731  TRP TRP A . n 
A 1 40  ILE 40  732  732  ILE ILE A . n 
A 1 41  PRO 41  733  733  PRO PRO A . n 
A 1 42  GLU 42  734  734  GLU GLU A . n 
A 1 43  GLY 43  735  735  GLY GLY A . n 
A 1 44  GLU 44  736  736  GLU GLU A . n 
A 1 45  LYS 45  737  737  LYS LYS A . n 
A 1 46  VAL 46  738  738  VAL VAL A . n 
A 1 47  LYS 47  739  739  LYS LYS A . n 
A 1 48  ILE 48  740  740  ILE ILE A . n 
A 1 49  PRO 49  741  741  PRO PRO A . n 
A 1 50  VAL 50  742  742  VAL VAL A . n 
A 1 51  ALA 51  743  743  ALA ALA A . n 
A 1 52  ILE 52  744  744  ILE ILE A . n 
A 1 53  LYS 53  745  745  LYS LYS A . n 
A 1 54  GLU 54  746  746  GLU GLU A . n 
A 1 55  LEU 55  747  747  LEU LEU A . n 
A 1 56  ARG 56  748  748  ARG ARG A . n 
A 1 57  GLU 57  749  749  GLU GLU A . n 
A 1 58  ALA 58  750  ?    ?   ?   A . n 
A 1 59  THR 59  751  ?    ?   ?   A . n 
A 1 60  SER 60  752  ?    ?   ?   A . n 
A 1 61  PRO 61  753  ?    ?   ?   A . n 
A 1 62  LYS 62  754  ?    ?   ?   A . n 
A 1 63  ALA 63  755  755  ALA ALA A . n 
A 1 64  ASN 64  756  756  ASN ASN A . n 
A 1 65  LYS 65  757  757  LYS LYS A . n 
A 1 66  GLU 66  758  758  GLU GLU A . n 
A 1 67  ILE 67  759  759  ILE ILE A . n 
A 1 68  LEU 68  760  760  LEU LEU A . n 
A 1 69  ASP 69  761  761  ASP ASP A . n 
A 1 70  GLU 70  762  762  GLU GLU A . n 
A 1 71  ALA 71  763  763  ALA ALA A . n 
A 1 72  TYR 72  764  764  TYR TYR A . n 
A 1 73  VAL 73  765  765  VAL VAL A . n 
A 1 74  MET 74  766  766  MET MET A . n 
A 1 75  ALA 75  767  767  ALA ALA A . n 
A 1 76  SER 76  768  768  SER SER A . n 
A 1 77  VAL 77  769  769  VAL VAL A . n 
A 1 78  ASP 78  770  770  ASP ASP A . n 
A 1 79  ASN 79  771  771  ASN ASN A . n 
A 1 80  PRO 80  772  772  PRO PRO A . n 
A 1 81  HIS 81  773  773  HIS HIS A . n 
A 1 82  VAL 82  774  774  VAL VAL A . n 
A 1 83  CYS 83  775  775  CYS CYS A . n 
A 1 84  ARG 84  776  776  ARG ARG A . n 
A 1 85  LEU 85  777  777  LEU LEU A . n 
A 1 86  LEU 86  778  778  LEU LEU A . n 
A 1 87  GLY 87  779  779  GLY GLY A . n 
A 1 88  ILE 88  780  780  ILE ILE A . n 
A 1 89  CYS 89  781  781  CYS CYS A . n 
A 1 90  LEU 90  782  782  LEU LEU A . n 
A 1 91  THR 91  783  783  THR THR A . n 
A 1 92  SER 92  784  784  SER SER A . n 
A 1 93  THR 93  785  785  THR THR A . n 
A 1 94  VAL 94  786  786  VAL VAL A . n 
A 1 95  GLN 95  787  787  GLN GLN A . n 
A 1 96  LEU 96  788  788  LEU LEU A . n 
A 1 97  ILE 97  789  789  ILE ILE A . n 
A 1 98  THR 98  790  790  THR THR A . n 
A 1 99  GLN 99  791  791  GLN GLN A . n 
A 1 100 LEU 100 792  792  LEU LEU A . n 
A 1 101 MET 101 793  793  MET MET A . n 
A 1 102 PRO 102 794  794  PRO PRO A . n 
A 1 103 PHE 103 795  795  PHE PHE A . n 
A 1 104 GLY 104 796  796  GLY GLY A . n 
A 1 105 CYS 105 797  797  CYS CYS A . n 
A 1 106 LEU 106 798  798  LEU LEU A . n 
A 1 107 LEU 107 799  799  LEU LEU A . n 
A 1 108 ASP 108 800  800  ASP ASP A . n 
A 1 109 TYR 109 801  801  TYR TYR A . n 
A 1 110 VAL 110 802  802  VAL VAL A . n 
A 1 111 ARG 111 803  803  ARG ARG A . n 
A 1 112 GLU 112 804  804  GLU GLU A . n 
A 1 113 HIS 113 805  805  HIS HIS A . n 
A 1 114 LYS 114 806  806  LYS LYS A . n 
A 1 115 ASP 115 807  807  ASP ASP A . n 
A 1 116 ASN 116 808  808  ASN ASN A . n 
A 1 117 ILE 117 809  809  ILE ILE A . n 
A 1 118 GLY 118 810  810  GLY GLY A . n 
A 1 119 SER 119 811  811  SER SER A . n 
A 1 120 GLN 120 812  812  GLN GLN A . n 
A 1 121 TYR 121 813  813  TYR TYR A . n 
A 1 122 LEU 122 814  814  LEU LEU A . n 
A 1 123 LEU 123 815  815  LEU LEU A . n 
A 1 124 ASN 124 816  816  ASN ASN A . n 
A 1 125 TRP 125 817  817  TRP TRP A . n 
A 1 126 CYS 126 818  818  CYS CYS A . n 
A 1 127 VAL 127 819  819  VAL VAL A . n 
A 1 128 GLN 128 820  820  GLN GLN A . n 
A 1 129 ILE 129 821  821  ILE ILE A . n 
A 1 130 ALA 130 822  822  ALA ALA A . n 
A 1 131 LYS 131 823  823  LYS LYS A . n 
A 1 132 GLY 132 824  824  GLY GLY A . n 
A 1 133 MET 133 825  825  MET MET A . n 
A 1 134 ASN 134 826  826  ASN ASN A . n 
A 1 135 TYR 135 827  827  TYR TYR A . n 
A 1 136 LEU 136 828  828  LEU LEU A . n 
A 1 137 GLU 137 829  829  GLU GLU A . n 
A 1 138 ASP 138 830  830  ASP ASP A . n 
A 1 139 ARG 139 831  831  ARG ARG A . n 
A 1 140 ARG 140 832  832  ARG ARG A . n 
A 1 141 LEU 141 833  833  LEU LEU A . n 
A 1 142 VAL 142 834  834  VAL VAL A . n 
A 1 143 HIS 143 835  835  HIS HIS A . n 
A 1 144 ARG 144 836  836  ARG ARG A . n 
A 1 145 ASP 145 837  837  ASP ASP A . n 
A 1 146 LEU 146 838  838  LEU LEU A . n 
A 1 147 ALA 147 839  839  ALA ALA A . n 
A 1 148 ALA 148 840  840  ALA ALA A . n 
A 1 149 ARG 149 841  841  ARG ARG A . n 
A 1 150 ASN 150 842  842  ASN ASN A . n 
A 1 151 VAL 151 843  843  VAL VAL A . n 
A 1 152 LEU 152 844  844  LEU LEU A . n 
A 1 153 VAL 153 845  845  VAL VAL A . n 
A 1 154 LYS 154 846  846  LYS LYS A . n 
A 1 155 THR 155 847  847  THR THR A . n 
A 1 156 PRO 156 848  848  PRO PRO A . n 
A 1 157 GLN 157 849  849  GLN GLN A . n 
A 1 158 HIS 158 850  850  HIS HIS A . n 
A 1 159 VAL 159 851  851  VAL VAL A . n 
A 1 160 LYS 160 852  852  LYS LYS A . n 
A 1 161 ILE 161 853  853  ILE ILE A . n 
A 1 162 THR 162 854  854  THR THR A . n 
A 1 163 ASP 163 855  855  ASP ASP A . n 
A 1 164 PHE 164 856  856  PHE PHE A . n 
A 1 165 GLY 165 857  857  GLY GLY A . n 
A 1 166 LEU 166 858  858  LEU LEU A . n 
A 1 167 ALA 167 859  859  ALA ALA A . n 
A 1 168 LYS 168 860  860  LYS LYS A . n 
A 1 169 LEU 169 861  861  LEU LEU A . n 
A 1 170 LEU 170 862  ?    ?   ?   A . n 
A 1 171 GLY 171 863  ?    ?   ?   A . n 
A 1 172 ALA 172 864  ?    ?   ?   A . n 
A 1 173 GLU 173 865  ?    ?   ?   A . n 
A 1 174 GLU 174 866  ?    ?   ?   A . n 
A 1 175 LYS 175 867  ?    ?   ?   A . n 
A 1 176 GLU 176 868  ?    ?   ?   A . n 
A 1 177 TYR 177 869  ?    ?   ?   A . n 
A 1 178 HIS 178 870  ?    ?   ?   A . n 
A 1 179 ALA 179 871  ?    ?   ?   A . n 
A 1 180 GLU 180 872  ?    ?   ?   A . n 
A 1 181 GLY 181 873  ?    ?   ?   A . n 
A 1 182 GLY 182 874  ?    ?   ?   A . n 
A 1 183 LYS 183 875  ?    ?   ?   A . n 
A 1 184 VAL 184 876  876  VAL VAL A . n 
A 1 185 PRO 185 877  877  PRO PRO A . n 
A 1 186 ILE 186 878  878  ILE ILE A . n 
A 1 187 LYS 187 879  879  LYS LYS A . n 
A 1 188 TRP 188 880  880  TRP TRP A . n 
A 1 189 MET 189 881  881  MET MET A . n 
A 1 190 ALA 190 882  882  ALA ALA A . n 
A 1 191 LEU 191 883  883  LEU LEU A . n 
A 1 192 GLU 192 884  884  GLU GLU A . n 
A 1 193 SER 193 885  885  SER SER A . n 
A 1 194 ILE 194 886  886  ILE ILE A . n 
A 1 195 LEU 195 887  887  LEU LEU A . n 
A 1 196 HIS 196 888  888  HIS HIS A . n 
A 1 197 ARG 197 889  889  ARG ARG A . n 
A 1 198 ILE 198 890  890  ILE ILE A . n 
A 1 199 TYR 199 891  891  TYR TYR A . n 
A 1 200 THR 200 892  892  THR THR A . n 
A 1 201 HIS 201 893  893  HIS HIS A . n 
A 1 202 GLN 202 894  894  GLN GLN A . n 
A 1 203 SER 203 895  895  SER SER A . n 
A 1 204 ASP 204 896  896  ASP ASP A . n 
A 1 205 VAL 205 897  897  VAL VAL A . n 
A 1 206 TRP 206 898  898  TRP TRP A . n 
A 1 207 SER 207 899  899  SER SER A . n 
A 1 208 TYR 208 900  900  TYR TYR A . n 
A 1 209 GLY 209 901  901  GLY GLY A . n 
A 1 210 VAL 210 902  902  VAL VAL A . n 
A 1 211 THR 211 903  903  THR THR A . n 
A 1 212 VAL 212 904  904  VAL VAL A . n 
A 1 213 TRP 213 905  905  TRP TRP A . n 
A 1 214 GLU 214 906  906  GLU GLU A . n 
A 1 215 LEU 215 907  907  LEU LEU A . n 
A 1 216 MET 216 908  908  MET MET A . n 
A 1 217 THR 217 909  909  THR THR A . n 
A 1 218 PHE 218 910  910  PHE PHE A . n 
A 1 219 GLY 219 911  911  GLY GLY A . n 
A 1 220 SER 220 912  912  SER SER A . n 
A 1 221 LYS 221 913  913  LYS LYS A . n 
A 1 222 PRO 222 914  914  PRO PRO A . n 
A 1 223 TYR 223 915  915  TYR TYR A . n 
A 1 224 ASP 224 916  916  ASP ASP A . n 
A 1 225 GLY 225 917  917  GLY GLY A . n 
A 1 226 ILE 226 918  918  ILE ILE A . n 
A 1 227 PRO 227 919  919  PRO PRO A . n 
A 1 228 ALA 228 920  920  ALA ALA A . n 
A 1 229 SER 229 921  921  SER SER A . n 
A 1 230 GLU 230 922  922  GLU GLU A . n 
A 1 231 ILE 231 923  923  ILE ILE A . n 
A 1 232 SER 232 924  924  SER SER A . n 
A 1 233 SER 233 925  925  SER SER A . n 
A 1 234 ILE 234 926  926  ILE ILE A . n 
A 1 235 LEU 235 927  927  LEU LEU A . n 
A 1 236 GLU 236 928  928  GLU GLU A . n 
A 1 237 LYS 237 929  929  LYS LYS A . n 
A 1 238 GLY 238 930  930  GLY GLY A . n 
A 1 239 GLU 239 931  931  GLU GLU A . n 
A 1 240 ARG 240 932  932  ARG ARG A . n 
A 1 241 LEU 241 933  933  LEU LEU A . n 
A 1 242 PRO 242 934  934  PRO PRO A . n 
A 1 243 GLN 243 935  935  GLN GLN A . n 
A 1 244 PRO 244 936  936  PRO PRO A . n 
A 1 245 PRO 245 937  937  PRO PRO A . n 
A 1 246 ILE 246 938  938  ILE ILE A . n 
A 1 247 CYS 247 939  939  CYS CYS A . n 
A 1 248 THR 248 940  940  THR THR A . n 
A 1 249 ILE 249 941  941  ILE ILE A . n 
A 1 250 ASP 250 942  942  ASP ASP A . n 
A 1 251 VAL 251 943  943  VAL VAL A . n 
A 1 252 TYR 252 944  944  TYR TYR A . n 
A 1 253 MET 253 945  945  MET MET A . n 
A 1 254 ILE 254 946  946  ILE ILE A . n 
A 1 255 MET 255 947  947  MET MET A . n 
A 1 256 ARG 256 948  948  ARG ARG A . n 
A 1 257 LYS 257 949  949  LYS LYS A . n 
A 1 258 CYS 258 950  950  CYS CYS A . n 
A 1 259 TRP 259 951  951  TRP TRP A . n 
A 1 260 MET 260 952  952  MET MET A . n 
A 1 261 ILE 261 953  953  ILE ILE A . n 
A 1 262 ASP 262 954  954  ASP ASP A . n 
A 1 263 ALA 263 955  955  ALA ALA A . n 
A 1 264 ASP 264 956  956  ASP ASP A . n 
A 1 265 SER 265 957  957  SER SER A . n 
A 1 266 ARG 266 958  958  ARG ARG A . n 
A 1 267 PRO 267 959  959  PRO PRO A . n 
A 1 268 LYS 268 960  960  LYS LYS A . n 
A 1 269 PHE 269 961  961  PHE PHE A . n 
A 1 270 ARG 270 962  962  ARG ARG A . n 
A 1 271 GLU 271 963  963  GLU GLU A . n 
A 1 272 LEU 272 964  964  LEU LEU A . n 
A 1 273 ILE 273 965  965  ILE ILE A . n 
A 1 274 ILE 274 966  966  ILE ILE A . n 
A 1 275 GLU 275 967  967  GLU GLU A . n 
A 1 276 PHE 276 968  968  PHE PHE A . n 
A 1 277 SER 277 969  969  SER SER A . n 
A 1 278 LYS 278 970  970  LYS LYS A . n 
A 1 279 MET 279 971  971  MET MET A . n 
A 1 280 ALA 280 972  972  ALA ALA A . n 
A 1 281 ARG 281 973  973  ARG ARG A . n 
A 1 282 ASP 282 974  974  ASP ASP A . n 
A 1 283 PRO 283 975  975  PRO PRO A . n 
A 1 284 GLN 284 976  976  GLN GLN A . n 
A 1 285 ARG 285 977  977  ARG ARG A . n 
A 1 286 TYR 286 978  978  TYR TYR A . n 
A 1 287 LEU 287 979  979  LEU LEU A . n 
A 1 288 VAL 288 980  980  VAL VAL A . n 
A 1 289 ILE 289 981  981  ILE ILE A . n 
A 1 290 GLN 290 982  982  GLN GLN A . n 
A 1 291 GLY 291 983  983  GLY GLY A . n 
A 1 292 ASP 292 984  984  ASP ASP A . n 
A 1 293 GLU 293 985  985  GLU GLU A . n 
A 1 294 ARG 294 986  986  ARG ARG A . n 
A 1 295 MET 295 987  987  MET MET A . n 
A 1 296 HIS 296 988  988  HIS HIS A . n 
A 1 297 LEU 297 989  989  LEU LEU A . n 
A 1 298 PRO 298 990  990  PRO PRO A . n 
A 1 299 SER 299 991  991  SER SER A . n 
A 1 300 PRO 300 992  992  PRO PRO A . n 
A 1 301 THR 301 993  993  THR THR A . n 
A 1 302 ASP 302 994  994  ASP ASP A . n 
A 1 303 SER 303 995  995  SER SER A . n 
A 1 304 ASN 304 996  996  ASN ASN A . n 
A 1 305 PHE 305 997  997  PHE PHE A . n 
A 1 306 TYR 306 998  998  TYR TYR A . n 
A 1 307 ARG 307 999  999  ARG ARG A . n 
A 1 308 ALA 308 1000 1000 ALA ALA A . n 
A 1 309 LEU 309 1001 1001 LEU LEU A . n 
A 1 310 MET 310 1002 1002 MET MET A . n 
A 1 311 ASP 311 1003 1003 ASP ASP A . n 
A 1 312 GLU 312 1004 1004 GLU GLU A . n 
A 1 313 GLU 313 1005 1005 GLU GLU A . n 
A 1 314 ASP 314 1006 1006 ASP ASP A . n 
A 1 315 MET 315 1007 1007 MET MET A . n 
A 1 316 ASP 316 1008 1008 ASP ASP A . n 
A 1 317 ASP 317 1009 1009 ASP ASP A . n 
A 1 318 VAL 318 1010 1010 VAL VAL A . n 
A 1 319 VAL 319 1011 1011 VAL VAL A . n 
A 1 320 ASP 320 1012 1012 ASP ASP A . n 
A 1 321 ALA 321 1013 1013 ALA ALA A . n 
A 1 322 ASP 322 1014 1014 ASP ASP A . n 
A 1 323 GLU 323 1015 ?    ?   ?   A . n 
A 1 324 TYR 324 1016 ?    ?   ?   A . n 
A 1 325 LEU 325 1017 ?    ?   ?   A . n 
A 1 326 ILE 326 1018 ?    ?   ?   A . n 
A 1 327 PRO 327 1019 ?    ?   ?   A . n 
A 1 328 GLN 328 1020 ?    ?   ?   A . n 
A 1 329 GLN 329 1021 ?    ?   ?   A . n 
A 1 330 GLY 330 1022 ?    ?   ?   A . n 
B 1 1   GLY 1   693  ?    ?   ?   B . n 
B 1 2   SER 2   694  ?    ?   ?   B . n 
B 1 3   SER 3   695  ?    ?   ?   B . n 
B 1 4   GLY 4   696  ?    ?   ?   B . n 
B 1 5   GLU 5   697  ?    ?   ?   B . n 
B 1 6   ALA 6   698  698  ALA ALA B . n 
B 1 7   PRO 7   699  699  PRO PRO B . n 
B 1 8   ASN 8   700  700  ASN ASN B . n 
B 1 9   GLN 9   701  701  GLN GLN B . n 
B 1 10  ALA 10  702  702  ALA ALA B . n 
B 1 11  LEU 11  703  703  LEU LEU B . n 
B 1 12  LEU 12  704  704  LEU LEU B . n 
B 1 13  ARG 13  705  705  ARG ARG B . n 
B 1 14  ILE 14  706  706  ILE ILE B . n 
B 1 15  LEU 15  707  707  LEU LEU B . n 
B 1 16  LYS 16  708  708  LYS LYS B . n 
B 1 17  GLU 17  709  709  GLU GLU B . n 
B 1 18  THR 18  710  710  THR THR B . n 
B 1 19  GLU 19  711  711  GLU GLU B . n 
B 1 20  PHE 20  712  712  PHE PHE B . n 
B 1 21  LYS 21  713  713  LYS LYS B . n 
B 1 22  LYS 22  714  714  LYS LYS B . n 
B 1 23  ILE 23  715  715  ILE ILE B . n 
B 1 24  LYS 24  716  716  LYS LYS B . n 
B 1 25  VAL 25  717  717  VAL VAL B . n 
B 1 26  LEU 26  718  718  LEU LEU B . n 
B 1 27  GLY 27  719  719  GLY GLY B . n 
B 1 28  SER 28  720  720  SER SER B . n 
B 1 29  GLY 29  721  721  GLY GLY B . n 
B 1 30  ALA 30  722  722  ALA ALA B . n 
B 1 31  PHE 31  723  723  PHE PHE B . n 
B 1 32  GLY 32  724  724  GLY GLY B . n 
B 1 33  THR 33  725  725  THR THR B . n 
B 1 34  VAL 34  726  726  VAL VAL B . n 
B 1 35  TYR 35  727  727  TYR TYR B . n 
B 1 36  LYS 36  728  728  LYS LYS B . n 
B 1 37  GLY 37  729  729  GLY GLY B . n 
B 1 38  LEU 38  730  730  LEU LEU B . n 
B 1 39  TRP 39  731  731  TRP TRP B . n 
B 1 40  ILE 40  732  732  ILE ILE B . n 
B 1 41  PRO 41  733  733  PRO PRO B . n 
B 1 42  GLU 42  734  734  GLU GLU B . n 
B 1 43  GLY 43  735  735  GLY GLY B . n 
B 1 44  GLU 44  736  736  GLU GLU B . n 
B 1 45  LYS 45  737  737  LYS LYS B . n 
B 1 46  VAL 46  738  738  VAL VAL B . n 
B 1 47  LYS 47  739  739  LYS LYS B . n 
B 1 48  ILE 48  740  740  ILE ILE B . n 
B 1 49  PRO 49  741  741  PRO PRO B . n 
B 1 50  VAL 50  742  742  VAL VAL B . n 
B 1 51  ALA 51  743  743  ALA ALA B . n 
B 1 52  ILE 52  744  744  ILE ILE B . n 
B 1 53  LYS 53  745  745  LYS LYS B . n 
B 1 54  GLU 54  746  746  GLU GLU B . n 
B 1 55  LEU 55  747  747  LEU LEU B . n 
B 1 56  ARG 56  748  748  ARG ARG B . n 
B 1 57  GLU 57  749  749  GLU GLU B . n 
B 1 58  ALA 58  750  750  ALA ALA B . n 
B 1 59  THR 59  751  ?    ?   ?   B . n 
B 1 60  SER 60  752  ?    ?   ?   B . n 
B 1 61  PRO 61  753  ?    ?   ?   B . n 
B 1 62  LYS 62  754  754  LYS LYS B . n 
B 1 63  ALA 63  755  755  ALA ALA B . n 
B 1 64  ASN 64  756  756  ASN ASN B . n 
B 1 65  LYS 65  757  757  LYS LYS B . n 
B 1 66  GLU 66  758  758  GLU GLU B . n 
B 1 67  ILE 67  759  759  ILE ILE B . n 
B 1 68  LEU 68  760  760  LEU LEU B . n 
B 1 69  ASP 69  761  761  ASP ASP B . n 
B 1 70  GLU 70  762  762  GLU GLU B . n 
B 1 71  ALA 71  763  763  ALA ALA B . n 
B 1 72  TYR 72  764  764  TYR TYR B . n 
B 1 73  VAL 73  765  765  VAL VAL B . n 
B 1 74  MET 74  766  766  MET MET B . n 
B 1 75  ALA 75  767  767  ALA ALA B . n 
B 1 76  SER 76  768  768  SER SER B . n 
B 1 77  VAL 77  769  769  VAL VAL B . n 
B 1 78  ASP 78  770  770  ASP ASP B . n 
B 1 79  ASN 79  771  771  ASN ASN B . n 
B 1 80  PRO 80  772  772  PRO PRO B . n 
B 1 81  HIS 81  773  773  HIS HIS B . n 
B 1 82  VAL 82  774  774  VAL VAL B . n 
B 1 83  CYS 83  775  775  CYS CYS B . n 
B 1 84  ARG 84  776  776  ARG ARG B . n 
B 1 85  LEU 85  777  777  LEU LEU B . n 
B 1 86  LEU 86  778  778  LEU LEU B . n 
B 1 87  GLY 87  779  779  GLY GLY B . n 
B 1 88  ILE 88  780  780  ILE ILE B . n 
B 1 89  CYS 89  781  781  CYS CYS B . n 
B 1 90  LEU 90  782  782  LEU LEU B . n 
B 1 91  THR 91  783  783  THR THR B . n 
B 1 92  SER 92  784  784  SER SER B . n 
B 1 93  THR 93  785  785  THR THR B . n 
B 1 94  VAL 94  786  786  VAL VAL B . n 
B 1 95  GLN 95  787  787  GLN GLN B . n 
B 1 96  LEU 96  788  788  LEU LEU B . n 
B 1 97  ILE 97  789  789  ILE ILE B . n 
B 1 98  THR 98  790  790  THR THR B . n 
B 1 99  GLN 99  791  791  GLN GLN B . n 
B 1 100 LEU 100 792  792  LEU LEU B . n 
B 1 101 MET 101 793  793  MET MET B . n 
B 1 102 PRO 102 794  794  PRO PRO B . n 
B 1 103 PHE 103 795  795  PHE PHE B . n 
B 1 104 GLY 104 796  796  GLY GLY B . n 
B 1 105 CYS 105 797  797  CYS CYS B . n 
B 1 106 LEU 106 798  798  LEU LEU B . n 
B 1 107 LEU 107 799  799  LEU LEU B . n 
B 1 108 ASP 108 800  800  ASP ASP B . n 
B 1 109 TYR 109 801  801  TYR TYR B . n 
B 1 110 VAL 110 802  802  VAL VAL B . n 
B 1 111 ARG 111 803  803  ARG ARG B . n 
B 1 112 GLU 112 804  804  GLU GLU B . n 
B 1 113 HIS 113 805  805  HIS HIS B . n 
B 1 114 LYS 114 806  806  LYS LYS B . n 
B 1 115 ASP 115 807  807  ASP ASP B . n 
B 1 116 ASN 116 808  808  ASN ASN B . n 
B 1 117 ILE 117 809  809  ILE ILE B . n 
B 1 118 GLY 118 810  810  GLY GLY B . n 
B 1 119 SER 119 811  811  SER SER B . n 
B 1 120 GLN 120 812  812  GLN GLN B . n 
B 1 121 TYR 121 813  813  TYR TYR B . n 
B 1 122 LEU 122 814  814  LEU LEU B . n 
B 1 123 LEU 123 815  815  LEU LEU B . n 
B 1 124 ASN 124 816  816  ASN ASN B . n 
B 1 125 TRP 125 817  817  TRP TRP B . n 
B 1 126 CYS 126 818  818  CYS CYS B . n 
B 1 127 VAL 127 819  819  VAL VAL B . n 
B 1 128 GLN 128 820  820  GLN GLN B . n 
B 1 129 ILE 129 821  821  ILE ILE B . n 
B 1 130 ALA 130 822  822  ALA ALA B . n 
B 1 131 LYS 131 823  823  LYS LYS B . n 
B 1 132 GLY 132 824  824  GLY GLY B . n 
B 1 133 MET 133 825  825  MET MET B . n 
B 1 134 ASN 134 826  826  ASN ASN B . n 
B 1 135 TYR 135 827  827  TYR TYR B . n 
B 1 136 LEU 136 828  828  LEU LEU B . n 
B 1 137 GLU 137 829  829  GLU GLU B . n 
B 1 138 ASP 138 830  830  ASP ASP B . n 
B 1 139 ARG 139 831  831  ARG ARG B . n 
B 1 140 ARG 140 832  832  ARG ARG B . n 
B 1 141 LEU 141 833  833  LEU LEU B . n 
B 1 142 VAL 142 834  834  VAL VAL B . n 
B 1 143 HIS 143 835  835  HIS HIS B . n 
B 1 144 ARG 144 836  836  ARG ARG B . n 
B 1 145 ASP 145 837  837  ASP ASP B . n 
B 1 146 LEU 146 838  838  LEU LEU B . n 
B 1 147 ALA 147 839  839  ALA ALA B . n 
B 1 148 ALA 148 840  840  ALA ALA B . n 
B 1 149 ARG 149 841  841  ARG ARG B . n 
B 1 150 ASN 150 842  842  ASN ASN B . n 
B 1 151 VAL 151 843  843  VAL VAL B . n 
B 1 152 LEU 152 844  844  LEU LEU B . n 
B 1 153 VAL 153 845  845  VAL VAL B . n 
B 1 154 LYS 154 846  846  LYS LYS B . n 
B 1 155 THR 155 847  847  THR THR B . n 
B 1 156 PRO 156 848  848  PRO PRO B . n 
B 1 157 GLN 157 849  849  GLN GLN B . n 
B 1 158 HIS 158 850  850  HIS HIS B . n 
B 1 159 VAL 159 851  851  VAL VAL B . n 
B 1 160 LYS 160 852  852  LYS LYS B . n 
B 1 161 ILE 161 853  853  ILE ILE B . n 
B 1 162 THR 162 854  854  THR THR B . n 
B 1 163 ASP 163 855  855  ASP ASP B . n 
B 1 164 PHE 164 856  856  PHE PHE B . n 
B 1 165 GLY 165 857  857  GLY GLY B . n 
B 1 166 LEU 166 858  858  LEU LEU B . n 
B 1 167 ALA 167 859  859  ALA ALA B . n 
B 1 168 LYS 168 860  860  LYS LYS B . n 
B 1 169 LEU 169 861  861  LEU LEU B . n 
B 1 170 LEU 170 862  862  LEU LEU B . n 
B 1 171 GLY 171 863  ?    ?   ?   B . n 
B 1 172 ALA 172 864  ?    ?   ?   B . n 
B 1 173 GLU 173 865  ?    ?   ?   B . n 
B 1 174 GLU 174 866  ?    ?   ?   B . n 
B 1 175 LYS 175 867  ?    ?   ?   B . n 
B 1 176 GLU 176 868  ?    ?   ?   B . n 
B 1 177 TYR 177 869  ?    ?   ?   B . n 
B 1 178 HIS 178 870  ?    ?   ?   B . n 
B 1 179 ALA 179 871  ?    ?   ?   B . n 
B 1 180 GLU 180 872  ?    ?   ?   B . n 
B 1 181 GLY 181 873  ?    ?   ?   B . n 
B 1 182 GLY 182 874  ?    ?   ?   B . n 
B 1 183 LYS 183 875  ?    ?   ?   B . n 
B 1 184 VAL 184 876  ?    ?   ?   B . n 
B 1 185 PRO 185 877  877  PRO PRO B . n 
B 1 186 ILE 186 878  878  ILE ILE B . n 
B 1 187 LYS 187 879  879  LYS LYS B . n 
B 1 188 TRP 188 880  880  TRP TRP B . n 
B 1 189 MET 189 881  881  MET MET B . n 
B 1 190 ALA 190 882  882  ALA ALA B . n 
B 1 191 LEU 191 883  883  LEU LEU B . n 
B 1 192 GLU 192 884  884  GLU GLU B . n 
B 1 193 SER 193 885  885  SER SER B . n 
B 1 194 ILE 194 886  886  ILE ILE B . n 
B 1 195 LEU 195 887  887  LEU LEU B . n 
B 1 196 HIS 196 888  888  HIS HIS B . n 
B 1 197 ARG 197 889  889  ARG ARG B . n 
B 1 198 ILE 198 890  890  ILE ILE B . n 
B 1 199 TYR 199 891  891  TYR TYR B . n 
B 1 200 THR 200 892  892  THR THR B . n 
B 1 201 HIS 201 893  893  HIS HIS B . n 
B 1 202 GLN 202 894  894  GLN GLN B . n 
B 1 203 SER 203 895  895  SER SER B . n 
B 1 204 ASP 204 896  896  ASP ASP B . n 
B 1 205 VAL 205 897  897  VAL VAL B . n 
B 1 206 TRP 206 898  898  TRP TRP B . n 
B 1 207 SER 207 899  899  SER SER B . n 
B 1 208 TYR 208 900  900  TYR TYR B . n 
B 1 209 GLY 209 901  901  GLY GLY B . n 
B 1 210 VAL 210 902  902  VAL VAL B . n 
B 1 211 THR 211 903  903  THR THR B . n 
B 1 212 VAL 212 904  904  VAL VAL B . n 
B 1 213 TRP 213 905  905  TRP TRP B . n 
B 1 214 GLU 214 906  906  GLU GLU B . n 
B 1 215 LEU 215 907  907  LEU LEU B . n 
B 1 216 MET 216 908  908  MET MET B . n 
B 1 217 THR 217 909  909  THR THR B . n 
B 1 218 PHE 218 910  910  PHE PHE B . n 
B 1 219 GLY 219 911  911  GLY GLY B . n 
B 1 220 SER 220 912  912  SER SER B . n 
B 1 221 LYS 221 913  913  LYS LYS B . n 
B 1 222 PRO 222 914  914  PRO PRO B . n 
B 1 223 TYR 223 915  915  TYR TYR B . n 
B 1 224 ASP 224 916  916  ASP ASP B . n 
B 1 225 GLY 225 917  917  GLY GLY B . n 
B 1 226 ILE 226 918  918  ILE ILE B . n 
B 1 227 PRO 227 919  919  PRO PRO B . n 
B 1 228 ALA 228 920  920  ALA ALA B . n 
B 1 229 SER 229 921  921  SER SER B . n 
B 1 230 GLU 230 922  922  GLU GLU B . n 
B 1 231 ILE 231 923  923  ILE ILE B . n 
B 1 232 SER 232 924  924  SER SER B . n 
B 1 233 SER 233 925  925  SER SER B . n 
B 1 234 ILE 234 926  926  ILE ILE B . n 
B 1 235 LEU 235 927  927  LEU LEU B . n 
B 1 236 GLU 236 928  928  GLU GLU B . n 
B 1 237 LYS 237 929  929  LYS LYS B . n 
B 1 238 GLY 238 930  930  GLY GLY B . n 
B 1 239 GLU 239 931  931  GLU GLU B . n 
B 1 240 ARG 240 932  932  ARG ARG B . n 
B 1 241 LEU 241 933  933  LEU LEU B . n 
B 1 242 PRO 242 934  934  PRO PRO B . n 
B 1 243 GLN 243 935  935  GLN GLN B . n 
B 1 244 PRO 244 936  936  PRO PRO B . n 
B 1 245 PRO 245 937  937  PRO PRO B . n 
B 1 246 ILE 246 938  938  ILE ILE B . n 
B 1 247 CYS 247 939  939  CYS CYS B . n 
B 1 248 THR 248 940  940  THR THR B . n 
B 1 249 ILE 249 941  941  ILE ILE B . n 
B 1 250 ASP 250 942  942  ASP ASP B . n 
B 1 251 VAL 251 943  943  VAL VAL B . n 
B 1 252 TYR 252 944  944  TYR TYR B . n 
B 1 253 MET 253 945  945  MET MET B . n 
B 1 254 ILE 254 946  946  ILE ILE B . n 
B 1 255 MET 255 947  947  MET MET B . n 
B 1 256 ARG 256 948  948  ARG ARG B . n 
B 1 257 LYS 257 949  949  LYS LYS B . n 
B 1 258 CYS 258 950  950  CYS CYS B . n 
B 1 259 TRP 259 951  951  TRP TRP B . n 
B 1 260 MET 260 952  952  MET MET B . n 
B 1 261 ILE 261 953  953  ILE ILE B . n 
B 1 262 ASP 262 954  954  ASP ASP B . n 
B 1 263 ALA 263 955  955  ALA ALA B . n 
B 1 264 ASP 264 956  956  ASP ASP B . n 
B 1 265 SER 265 957  957  SER SER B . n 
B 1 266 ARG 266 958  958  ARG ARG B . n 
B 1 267 PRO 267 959  959  PRO PRO B . n 
B 1 268 LYS 268 960  960  LYS LYS B . n 
B 1 269 PHE 269 961  961  PHE PHE B . n 
B 1 270 ARG 270 962  962  ARG ARG B . n 
B 1 271 GLU 271 963  963  GLU GLU B . n 
B 1 272 LEU 272 964  964  LEU LEU B . n 
B 1 273 ILE 273 965  965  ILE ILE B . n 
B 1 274 ILE 274 966  966  ILE ILE B . n 
B 1 275 GLU 275 967  967  GLU GLU B . n 
B 1 276 PHE 276 968  968  PHE PHE B . n 
B 1 277 SER 277 969  969  SER SER B . n 
B 1 278 LYS 278 970  970  LYS LYS B . n 
B 1 279 MET 279 971  971  MET MET B . n 
B 1 280 ALA 280 972  972  ALA ALA B . n 
B 1 281 ARG 281 973  973  ARG ARG B . n 
B 1 282 ASP 282 974  974  ASP ASP B . n 
B 1 283 PRO 283 975  975  PRO PRO B . n 
B 1 284 GLN 284 976  976  GLN GLN B . n 
B 1 285 ARG 285 977  977  ARG ARG B . n 
B 1 286 TYR 286 978  978  TYR TYR B . n 
B 1 287 LEU 287 979  979  LEU LEU B . n 
B 1 288 VAL 288 980  980  VAL VAL B . n 
B 1 289 ILE 289 981  981  ILE ILE B . n 
B 1 290 GLN 290 982  982  GLN GLN B . n 
B 1 291 GLY 291 983  983  GLY GLY B . n 
B 1 292 ASP 292 984  984  ASP ASP B . n 
B 1 293 GLU 293 985  985  GLU GLU B . n 
B 1 294 ARG 294 986  986  ARG ARG B . n 
B 1 295 MET 295 987  987  MET MET B . n 
B 1 296 HIS 296 988  988  HIS HIS B . n 
B 1 297 LEU 297 989  989  LEU LEU B . n 
B 1 298 PRO 298 990  990  PRO PRO B . n 
B 1 299 SER 299 991  991  SER SER B . n 
B 1 300 PRO 300 992  992  PRO PRO B . n 
B 1 301 THR 301 993  993  THR THR B . n 
B 1 302 ASP 302 994  994  ASP ASP B . n 
B 1 303 SER 303 995  995  SER SER B . n 
B 1 304 ASN 304 996  996  ASN ASN B . n 
B 1 305 PHE 305 997  997  PHE PHE B . n 
B 1 306 TYR 306 998  998  TYR TYR B . n 
B 1 307 ARG 307 999  999  ARG ARG B . n 
B 1 308 ALA 308 1000 1000 ALA ALA B . n 
B 1 309 LEU 309 1001 1001 LEU LEU B . n 
B 1 310 MET 310 1002 1002 MET MET B . n 
B 1 311 ASP 311 1003 1003 ASP ASP B . n 
B 1 312 GLU 312 1004 1004 GLU GLU B . n 
B 1 313 GLU 313 1005 1005 GLU GLU B . n 
B 1 314 ASP 314 1006 1006 ASP ASP B . n 
B 1 315 MET 315 1007 1007 MET MET B . n 
B 1 316 ASP 316 1008 1008 ASP ASP B . n 
B 1 317 ASP 317 1009 1009 ASP ASP B . n 
B 1 318 VAL 318 1010 1010 VAL VAL B . n 
B 1 319 VAL 319 1011 1011 VAL VAL B . n 
B 1 320 ASP 320 1012 1012 ASP ASP B . n 
B 1 321 ALA 321 1013 1013 ALA ALA B . n 
B 1 322 ASP 322 1014 1014 ASP ASP B . n 
B 1 323 GLU 323 1015 ?    ?   ?   B . n 
B 1 324 TYR 324 1016 ?    ?   ?   B . n 
B 1 325 LEU 325 1017 ?    ?   ?   B . n 
B 1 326 ILE 326 1018 ?    ?   ?   B . n 
B 1 327 PRO 327 1019 ?    ?   ?   B . n 
B 1 328 GLN 328 1020 ?    ?   ?   B . n 
B 1 329 GLN 329 1021 ?    ?   ?   B . n 
B 1 330 GLY 330 1022 ?    ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IZ9 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IZ9 
_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 A1IZ9 1  1101 1101 A1IZ9 INH A . 
D 2 A1IZ9 1  1101 1101 A1IZ9 INH B . 
E 3 HOH   1  1201 178  HOH   HOH A . 
E 3 HOH   2  1202 100  HOH   HOH A . 
E 3 HOH   3  1203 224  HOH   HOH A . 
E 3 HOH   4  1204 78   HOH   HOH A . 
E 3 HOH   5  1205 102  HOH   HOH A . 
E 3 HOH   6  1206 169  HOH   HOH A . 
E 3 HOH   7  1207 204  HOH   HOH A . 
E 3 HOH   8  1208 71   HOH   HOH A . 
E 3 HOH   9  1209 37   HOH   HOH A . 
E 3 HOH   10 1210 22   HOH   HOH A . 
E 3 HOH   11 1211 198  HOH   HOH A . 
E 3 HOH   12 1212 105  HOH   HOH A . 
E 3 HOH   13 1213 23   HOH   HOH A . 
E 3 HOH   14 1214 153  HOH   HOH A . 
E 3 HOH   15 1215 68   HOH   HOH A . 
E 3 HOH   16 1216 220  HOH   HOH A . 
E 3 HOH   17 1217 40   HOH   HOH A . 
E 3 HOH   18 1218 219  HOH   HOH A . 
E 3 HOH   19 1219 106  HOH   HOH A . 
E 3 HOH   20 1220 52   HOH   HOH A . 
E 3 HOH   21 1221 3    HOH   HOH A . 
E 3 HOH   22 1222 223  HOH   HOH A . 
E 3 HOH   23 1223 222  HOH   HOH A . 
E 3 HOH   24 1224 218  HOH   HOH A . 
E 3 HOH   25 1225 29   HOH   HOH A . 
E 3 HOH   26 1226 8    HOH   HOH A . 
E 3 HOH   27 1227 31   HOH   HOH A . 
E 3 HOH   28 1228 131  HOH   HOH A . 
E 3 HOH   29 1229 147  HOH   HOH A . 
E 3 HOH   30 1230 17   HOH   HOH A . 
E 3 HOH   31 1231 120  HOH   HOH A . 
E 3 HOH   32 1232 18   HOH   HOH A . 
E 3 HOH   33 1233 227  HOH   HOH A . 
E 3 HOH   34 1234 16   HOH   HOH A . 
E 3 HOH   35 1235 107  HOH   HOH A . 
E 3 HOH   36 1236 191  HOH   HOH A . 
E 3 HOH   37 1237 79   HOH   HOH A . 
E 3 HOH   38 1238 135  HOH   HOH A . 
E 3 HOH   39 1239 10   HOH   HOH A . 
E 3 HOH   40 1240 206  HOH   HOH A . 
E 3 HOH   41 1241 96   HOH   HOH A . 
E 3 HOH   42 1242 88   HOH   HOH A . 
E 3 HOH   43 1243 217  HOH   HOH A . 
E 3 HOH   44 1244 163  HOH   HOH A . 
E 3 HOH   45 1245 205  HOH   HOH A . 
E 3 HOH   46 1246 200  HOH   HOH A . 
E 3 HOH   47 1247 5    HOH   HOH A . 
E 3 HOH   48 1248 11   HOH   HOH A . 
E 3 HOH   49 1249 194  HOH   HOH A . 
E 3 HOH   50 1250 59   HOH   HOH A . 
E 3 HOH   51 1251 144  HOH   HOH A . 
E 3 HOH   52 1252 57   HOH   HOH A . 
E 3 HOH   53 1253 158  HOH   HOH A . 
E 3 HOH   54 1254 94   HOH   HOH A . 
E 3 HOH   55 1255 108  HOH   HOH A . 
E 3 HOH   56 1256 213  HOH   HOH A . 
E 3 HOH   57 1257 111  HOH   HOH A . 
E 3 HOH   58 1258 93   HOH   HOH A . 
E 3 HOH   59 1259 69   HOH   HOH A . 
E 3 HOH   60 1260 203  HOH   HOH A . 
E 3 HOH   61 1261 97   HOH   HOH A . 
E 3 HOH   62 1262 64   HOH   HOH A . 
E 3 HOH   63 1263 119  HOH   HOH A . 
E 3 HOH   64 1264 20   HOH   HOH A . 
E 3 HOH   65 1265 90   HOH   HOH A . 
E 3 HOH   66 1266 36   HOH   HOH A . 
E 3 HOH   67 1267 171  HOH   HOH A . 
E 3 HOH   68 1268 19   HOH   HOH A . 
E 3 HOH   69 1269 81   HOH   HOH A . 
E 3 HOH   70 1270 53   HOH   HOH A . 
E 3 HOH   71 1271 148  HOH   HOH A . 
E 3 HOH   72 1272 73   HOH   HOH A . 
E 3 HOH   73 1273 132  HOH   HOH A . 
E 3 HOH   74 1274 114  HOH   HOH A . 
E 3 HOH   75 1275 187  HOH   HOH A . 
E 3 HOH   76 1276 137  HOH   HOH A . 
E 3 HOH   77 1277 83   HOH   HOH A . 
E 3 HOH   78 1278 170  HOH   HOH A . 
E 3 HOH   79 1279 116  HOH   HOH A . 
E 3 HOH   80 1280 133  HOH   HOH A . 
E 3 HOH   81 1281 125  HOH   HOH A . 
E 3 HOH   82 1282 122  HOH   HOH A . 
F 3 HOH   1  1201 229  HOH   HOH B . 
F 3 HOH   2  1202 41   HOH   HOH B . 
F 3 HOH   3  1203 21   HOH   HOH B . 
F 3 HOH   4  1204 104  HOH   HOH B . 
F 3 HOH   5  1205 25   HOH   HOH B . 
F 3 HOH   6  1206 182  HOH   HOH B . 
F 3 HOH   7  1207 6    HOH   HOH B . 
F 3 HOH   8  1208 15   HOH   HOH B . 
F 3 HOH   9  1209 138  HOH   HOH B . 
F 3 HOH   10 1210 101  HOH   HOH B . 
F 3 HOH   11 1211 51   HOH   HOH B . 
F 3 HOH   12 1212 55   HOH   HOH B . 
F 3 HOH   13 1213 50   HOH   HOH B . 
F 3 HOH   14 1214 165  HOH   HOH B . 
F 3 HOH   15 1215 128  HOH   HOH B . 
F 3 HOH   16 1216 207  HOH   HOH B . 
F 3 HOH   17 1217 221  HOH   HOH B . 
F 3 HOH   18 1218 216  HOH   HOH B . 
F 3 HOH   19 1219 70   HOH   HOH B . 
F 3 HOH   20 1220 126  HOH   HOH B . 
F 3 HOH   21 1221 24   HOH   HOH B . 
F 3 HOH   22 1222 141  HOH   HOH B . 
F 3 HOH   23 1223 65   HOH   HOH B . 
F 3 HOH   24 1224 67   HOH   HOH B . 
F 3 HOH   25 1225 4    HOH   HOH B . 
F 3 HOH   26 1226 7    HOH   HOH B . 
F 3 HOH   27 1227 44   HOH   HOH B . 
F 3 HOH   28 1228 186  HOH   HOH B . 
F 3 HOH   29 1229 115  HOH   HOH B . 
F 3 HOH   30 1230 82   HOH   HOH B . 
F 3 HOH   31 1231 12   HOH   HOH B . 
F 3 HOH   32 1232 27   HOH   HOH B . 
F 3 HOH   33 1233 152  HOH   HOH B . 
F 3 HOH   34 1234 28   HOH   HOH B . 
F 3 HOH   35 1235 118  HOH   HOH B . 
F 3 HOH   36 1236 180  HOH   HOH B . 
F 3 HOH   37 1237 13   HOH   HOH B . 
F 3 HOH   38 1238 112  HOH   HOH B . 
F 3 HOH   39 1239 172  HOH   HOH B . 
F 3 HOH   40 1240 174  HOH   HOH B . 
F 3 HOH   41 1241 121  HOH   HOH B . 
F 3 HOH   42 1242 167  HOH   HOH B . 
F 3 HOH   43 1243 9    HOH   HOH B . 
F 3 HOH   44 1244 26   HOH   HOH B . 
F 3 HOH   45 1245 230  HOH   HOH B . 
F 3 HOH   46 1246 156  HOH   HOH B . 
F 3 HOH   47 1247 228  HOH   HOH B . 
F 3 HOH   48 1248 33   HOH   HOH B . 
F 3 HOH   49 1249 209  HOH   HOH B . 
F 3 HOH   50 1250 39   HOH   HOH B . 
F 3 HOH   51 1251 32   HOH   HOH B . 
F 3 HOH   52 1252 136  HOH   HOH B . 
F 3 HOH   53 1253 193  HOH   HOH B . 
F 3 HOH   54 1254 92   HOH   HOH B . 
F 3 HOH   55 1255 76   HOH   HOH B . 
F 3 HOH   56 1256 63   HOH   HOH B . 
F 3 HOH   57 1257 173  HOH   HOH B . 
F 3 HOH   58 1258 190  HOH   HOH B . 
F 3 HOH   59 1259 62   HOH   HOH B . 
F 3 HOH   60 1260 185  HOH   HOH B . 
F 3 HOH   61 1261 117  HOH   HOH B . 
F 3 HOH   62 1262 142  HOH   HOH B . 
F 3 HOH   63 1263 159  HOH   HOH B . 
F 3 HOH   64 1264 176  HOH   HOH B . 
F 3 HOH   65 1265 189  HOH   HOH B . 
F 3 HOH   66 1266 56   HOH   HOH B . 
F 3 HOH   67 1267 202  HOH   HOH B . 
F 3 HOH   68 1268 75   HOH   HOH B . 
F 3 HOH   69 1269 47   HOH   HOH B . 
F 3 HOH   70 1270 61   HOH   HOH B . 
F 3 HOH   71 1271 195  HOH   HOH B . 
F 3 HOH   72 1272 197  HOH   HOH B . 
F 3 HOH   73 1273 149  HOH   HOH B . 
F 3 HOH   74 1274 2    HOH   HOH B . 
F 3 HOH   75 1275 192  HOH   HOH B . 
F 3 HOH   76 1276 124  HOH   HOH B . 
F 3 HOH   77 1277 183  HOH   HOH B . 
F 3 HOH   78 1278 46   HOH   HOH B . 
F 3 HOH   79 1279 34   HOH   HOH B . 
F 3 HOH   80 1280 85   HOH   HOH B . 
F 3 HOH   81 1281 177  HOH   HOH B . 
F 3 HOH   82 1282 103  HOH   HOH B . 
F 3 HOH   83 1283 38   HOH   HOH B . 
F 3 HOH   84 1284 181  HOH   HOH B . 
F 3 HOH   85 1285 154  HOH   HOH B . 
F 3 HOH   86 1286 166  HOH   HOH B . 
# 
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 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC  ? ? ? .                      1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? STARANISO ? ? ? .                      2 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER    ? ? ? '2.11.8 (26-JUL-2023)' 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? .                      4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   112.88 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GC6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     76.435 
_cell.length_a_esd                 ? 
_cell.length_b                     70.934 
_cell.length_b_esd                 ? 
_cell.length_c                     78.230 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9GC6 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9GC6 
_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             2.60 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          52.67 
_exptl_crystal.description                  'rod like' 
_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, SITTING 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    'Peg 8K' 
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-02-25 
_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   0.9795 
_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                        'DIAMOND BEAMLINE I04' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9795 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GC6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.901 
_reflns.d_resolution_low                               72.073 
_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                                     33926 
_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                           90.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    1.901 
_reflns_shell.d_res_low                                     2.154 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1697 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.729 
_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                                  ? 
_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]                            -0.08730 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.35900 
_refine.aniso_B[2][2]                            0.12240 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            -0.03510 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               29.59 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.916 
_refine.correlation_coeff_Fo_to_Fc_free          0.882 
_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                                 9GC6 
_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                            1.901 
_refine.ls_d_res_low                             64.42 
_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                     33819 
_refine.ls_number_reflns_R_free                  1678 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    55.7 
_refine.ls_percent_reflns_R_free                 4.960 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2690 
_refine.ls_R_factor_R_free                       0.3228 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2662 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.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                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.287 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.281 
_refine.pdbx_overall_SU_R_Blow_DPI               0.362 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.373 
_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_analyze.entry_id                        9GC6 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.37 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.901 
_refine_hist.d_res_low                        64.42 
_refine_hist.number_atoms_solvent             168 
_refine_hist.number_atoms_total               5047 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4815 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         64 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008 ? 4991 ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 0.94  ? 6754 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1771 ? t_dihedral_angle_d        2.00  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_incorr_chiral_ct        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_pseud_angle             ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_trig_c_planes           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 880  ? t_gen_planes              5.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 4991 ? t_it                      10.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 2.96  ? ?    ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 18.42 ? ?    ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 640  ? t_chiral_improper_torsion 5.00  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_sum_occupancies         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_distance        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_angle           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_torsion         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 3992 ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.901 
_refine_ls_shell.d_res_low                        2.06 
_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             643 
_refine_ls_shell.percent_reflns_obs               5.19 
_refine_ls_shell.percent_reflns_R_free            5.02 
_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                  0.3556 
_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                  0.3658 
# 
_struct.entry_id                     9GC6 
_struct.title                        'Highly optimized CNS penetrant inhibitors of EGFR Exon20 Insertion Mutations' 
_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        9GC6 
_struct_keywords.text            'EGFR, Exon20, NPG, SIGNALING PROTEIN' 
_struct_keywords.pdbx_keywords   'SIGNALING 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                    EGFR_HUMAN 
_struct_ref.pdbx_db_accession          P00533 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHV
CRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKIT
DFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLP
QPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDAD
EYLIPQQG
;
_struct_ref.pdbx_align_begin           695 
# 
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 9GC6 A 3 ? 330 ? P00533 695 ? 1022 ? 695 1022 
2 1 9GC6 B 3 ? 330 ? P00533 695 ? 1022 ? 695 1022 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9GC6 GLY A 1   ? UNP P00533 ?   ?   'expression tag'      693 1 
1 9GC6 SER A 2   ? UNP P00533 ?   ?   'expression tag'      694 2 
1 9GC6 ARG A 256 ? UNP P00533 VAL 948 'engineered mutation' 948 3 
2 9GC6 GLY B 1   ? UNP P00533 ?   ?   'expression tag'      693 4 
2 9GC6 SER B 2   ? UNP P00533 ?   ?   'expression tag'      694 5 
2 9GC6 ARG B 256 ? UNP P00533 VAL 948 'engineered mutation' 948 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,E 
2 1 B,D,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 ASN A 8   ? LEU A 12  ? ASN A 700 LEU A 704  5 ? 5  
HELX_P HELX_P2  AA2 ASN A 64  ? SER A 76  ? ASN A 756 SER A 768  1 ? 13 
HELX_P HELX_P3  AA3 CYS A 105 ? HIS A 113 ? CYS A 797 HIS A 805  1 ? 9  
HELX_P HELX_P4  AA4 GLY A 118 ? ARG A 139 ? GLY A 810 ARG A 831  1 ? 22 
HELX_P HELX_P5  AA5 ALA A 147 ? ARG A 149 ? ALA A 839 ARG A 841  5 ? 3  
HELX_P HELX_P6  AA6 PRO A 185 ? MET A 189 ? PRO A 877 MET A 881  5 ? 5  
HELX_P HELX_P7  AA7 ALA A 190 ? ARG A 197 ? ALA A 882 ARG A 889  1 ? 8  
HELX_P HELX_P8  AA8 THR A 200 ? THR A 217 ? THR A 892 THR A 909  1 ? 18 
HELX_P HELX_P9  AA9 GLU A 230 ? LYS A 237 ? GLU A 922 LYS A 929  1 ? 8  
HELX_P HELX_P10 AB1 THR A 248 ? TRP A 259 ? THR A 940 TRP A 951  1 ? 12 
HELX_P HELX_P11 AB2 ASP A 262 ? ARG A 266 ? ASP A 954 ARG A 958  5 ? 5  
HELX_P HELX_P12 AB3 LYS A 268 ? ARG A 281 ? LYS A 960 ARG A 973  1 ? 14 
HELX_P HELX_P13 AB4 ASP A 282 ? LEU A 287 ? ASP A 974 LEU A 979  1 ? 6  
HELX_P HELX_P14 AB5 SER A 299 ? ASP A 311 ? SER A 991 ASP A 1003 1 ? 13 
HELX_P HELX_P15 AB6 ASN B 8   ? LEU B 12  ? ASN B 700 LEU B 704  5 ? 5  
HELX_P HELX_P16 AB7 LYS B 16  ? THR B 18  ? LYS B 708 THR B 710  5 ? 3  
HELX_P HELX_P17 AB8 ALA B 63  ? ALA B 75  ? ALA B 755 ALA B 767  1 ? 13 
HELX_P HELX_P18 AB9 CYS B 105 ? HIS B 113 ? CYS B 797 HIS B 805  1 ? 9  
HELX_P HELX_P19 AC1 GLY B 118 ? ARG B 139 ? GLY B 810 ARG B 831  1 ? 22 
HELX_P HELX_P20 AC2 ALA B 147 ? ARG B 149 ? ALA B 839 ARG B 841  5 ? 3  
HELX_P HELX_P21 AC3 GLY B 165 ? LEU B 170 ? GLY B 857 LEU B 862  1 ? 6  
HELX_P HELX_P22 AC4 PRO B 185 ? MET B 189 ? PRO B 877 MET B 881  5 ? 5  
HELX_P HELX_P23 AC5 ALA B 190 ? ARG B 197 ? ALA B 882 ARG B 889  1 ? 8  
HELX_P HELX_P24 AC6 THR B 200 ? THR B 217 ? THR B 892 THR B 909  1 ? 18 
HELX_P HELX_P25 AC7 PRO B 227 ? SER B 229 ? PRO B 919 SER B 921  5 ? 3  
HELX_P HELX_P26 AC8 GLU B 230 ? LYS B 237 ? GLU B 922 LYS B 929  1 ? 8  
HELX_P HELX_P27 AC9 THR B 248 ? TRP B 259 ? THR B 940 TRP B 951  1 ? 12 
HELX_P HELX_P28 AD1 ASP B 262 ? ARG B 266 ? ASP B 954 ARG B 958  5 ? 5  
HELX_P HELX_P29 AD2 LYS B 268 ? ASP B 282 ? LYS B 960 ASP B 974  1 ? 15 
HELX_P HELX_P30 AD3 ASP B 282 ? LEU B 287 ? ASP B 974 LEU B 979  1 ? 6  
HELX_P HELX_P31 AD4 GLY B 291 ? MET B 295 ? GLY B 983 MET B 987  5 ? 5  
HELX_P HELX_P32 AD5 SER B 299 ? ASP B 311 ? SER B 991 ASP B 1003 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale none ? A CYS 105 SG ? ? ? 1_555 C A1IZ9 . C22 ? ? A CYS 797 A A1IZ9 1101 1_555 ? ? ? ? ? ? ? 1.791 ? ? 
covale2 covale none ? B CYS 105 SG ? ? ? 1_555 D A1IZ9 . C22 ? ? B CYS 797 B A1IZ9 1101 1_555 ? ? ? ? ? ? ? 1.776 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 A1IZ9 C . ? CYS A 105 ? A1IZ9 A 1101 ? 1_555 CYS A 797 ? 1_555 C22 SG CYS 1 A1IZ9 None 'Covalent chemical modification' 
2 A1IZ9 D . ? CYS B 105 ? A1IZ9 B 1101 ? 1_555 CYS B 797 ? 1_555 C22 SG CYS 1 A1IZ9 None 'Covalent chemical modification' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          LYS 
_struct_mon_prot_cis.label_seq_id           114 
_struct_mon_prot_cis.label_asym_id          B 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           LYS 
_struct_mon_prot_cis.auth_seq_id            806 
_struct_mon_prot_cis.auth_asym_id           B 
_struct_mon_prot_cis.pdbx_label_comp_id_2   ASP 
_struct_mon_prot_cis.pdbx_label_seq_id_2    115 
_struct_mon_prot_cis.pdbx_label_asym_id_2   B 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    ASP 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     807 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    B 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -0.18 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 2 ? 
AA3 ? 6 ? 
AA4 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA4 1 2 ? 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 ARG A 13  ? ILE A 14  ? ARG A 705 ILE A 706 
AA1 2 GLY A 87  ? LEU A 90  ? GLY A 779 LEU A 782 
AA1 3 VAL A 94  ? THR A 98  ? VAL A 786 THR A 790 
AA1 4 ILE A 48  ? LEU A 55  ? ILE A 740 LEU A 747 
AA1 5 GLY A 32  ? TRP A 39  ? GLY A 724 TRP A 731 
AA1 6 PHE A 20  ? SER A 28  ? PHE A 712 SER A 720 
AA2 1 VAL A 151 ? THR A 155 ? VAL A 843 THR A 847 
AA2 2 HIS A 158 ? ILE A 161 ? HIS A 850 ILE A 853 
AA3 1 ARG B 13  ? ILE B 14  ? ARG B 705 ILE B 706 
AA3 2 GLY B 87  ? LEU B 90  ? GLY B 779 LEU B 782 
AA3 3 VAL B 94  ? THR B 98  ? VAL B 786 THR B 790 
AA3 4 ILE B 48  ? LEU B 55  ? ILE B 740 LEU B 747 
AA3 5 GLY B 32  ? TRP B 39  ? GLY B 724 TRP B 731 
AA3 6 PHE B 20  ? SER B 28  ? PHE B 712 SER B 720 
AA4 1 VAL B 151 ? THR B 155 ? VAL B 843 THR B 847 
AA4 2 HIS B 158 ? ILE B 161 ? HIS B 850 ILE B 853 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ARG A 13  ? N ARG A 705 O ILE A 88  ? O ILE A 780 
AA1 2 3 N GLY A 87  ? N GLY A 779 O ILE A 97  ? O ILE A 789 
AA1 3 4 O THR A 98  ? O THR A 790 N ALA A 51  ? N ALA A 743 
AA1 4 5 O VAL A 50  ? O VAL A 742 N GLY A 37  ? N GLY A 729 
AA1 5 6 O LYS A 36  ? O LYS A 728 N ILE A 23  ? N ILE A 715 
AA2 1 2 N LYS A 154 ? N LYS A 846 O HIS A 158 ? O HIS A 850 
AA3 1 2 N ARG B 13  ? N ARG B 705 O ILE B 88  ? O ILE B 780 
AA3 2 3 N CYS B 89  ? N CYS B 781 O GLN B 95  ? O GLN B 787 
AA3 3 4 O THR B 98  ? O THR B 790 N ALA B 51  ? N ALA B 743 
AA3 4 5 O ILE B 48  ? O ILE B 740 N TRP B 39  ? N TRP B 731 
AA3 5 6 O VAL B 34  ? O VAL B 726 N GLY B 27  ? N GLY B 719 
AA4 1 2 N LEU B 152 ? N LEU B 844 O LYS B 160 ? O LYS B 852 
# 
_pdbx_entry_details.entry_id                   9GC6 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 PRO A 699 ? ? -79.58  -168.00 
2 1 THR A 783 ? ? -129.40 -129.88 
3 1 ARG A 836 ? ? 79.87   -17.21  
4 1 GLU B 749 ? ? -69.93  99.82   
5 1 ALA B 755 ? ? 73.00   142.65  
6 1 THR B 783 ? ? -128.52 -133.67 
7 1 ASN B 808 ? ? -76.67  40.34   
8 1 ARG B 836 ? ? 77.35   -9.72   
9 1 ASP B 837 ? ? -146.64 46.51   
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       1286 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   9.06 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 GLY 693  ? A GLY 1   
2  1 Y 1 A SER 694  ? A SER 2   
3  1 Y 1 A SER 695  ? A SER 3   
4  1 Y 1 A GLY 696  ? A GLY 4   
5  1 Y 1 A GLU 697  ? A GLU 5   
6  1 Y 1 A ALA 750  ? A ALA 58  
7  1 Y 1 A THR 751  ? A THR 59  
8  1 Y 1 A SER 752  ? A SER 60  
9  1 Y 1 A PRO 753  ? A PRO 61  
10 1 Y 1 A LYS 754  ? A LYS 62  
11 1 Y 1 A LEU 862  ? A LEU 170 
12 1 Y 1 A GLY 863  ? A GLY 171 
13 1 Y 1 A ALA 864  ? A ALA 172 
14 1 Y 1 A GLU 865  ? A GLU 173 
15 1 Y 1 A GLU 866  ? A GLU 174 
16 1 Y 1 A LYS 867  ? A LYS 175 
17 1 Y 1 A GLU 868  ? A GLU 176 
18 1 Y 1 A TYR 869  ? A TYR 177 
19 1 Y 1 A HIS 870  ? A HIS 178 
20 1 Y 1 A ALA 871  ? A ALA 179 
21 1 Y 1 A GLU 872  ? A GLU 180 
22 1 Y 1 A GLY 873  ? A GLY 181 
23 1 Y 1 A GLY 874  ? A GLY 182 
24 1 Y 1 A LYS 875  ? A LYS 183 
25 1 Y 1 A GLU 1015 ? A GLU 323 
26 1 Y 1 A TYR 1016 ? A TYR 324 
27 1 Y 1 A LEU 1017 ? A LEU 325 
28 1 Y 1 A ILE 1018 ? A ILE 326 
29 1 Y 1 A PRO 1019 ? A PRO 327 
30 1 Y 1 A GLN 1020 ? A GLN 328 
31 1 Y 1 A GLN 1021 ? A GLN 329 
32 1 Y 1 A GLY 1022 ? A GLY 330 
33 1 Y 1 B GLY 693  ? B GLY 1   
34 1 Y 1 B SER 694  ? B SER 2   
35 1 Y 1 B SER 695  ? B SER 3   
36 1 Y 1 B GLY 696  ? B GLY 4   
37 1 Y 1 B GLU 697  ? B GLU 5   
38 1 Y 1 B THR 751  ? B THR 59  
39 1 Y 1 B SER 752  ? B SER 60  
40 1 Y 1 B PRO 753  ? B PRO 61  
41 1 Y 1 B GLY 863  ? B GLY 171 
42 1 Y 1 B ALA 864  ? B ALA 172 
43 1 Y 1 B GLU 865  ? B GLU 173 
44 1 Y 1 B GLU 866  ? B GLU 174 
45 1 Y 1 B LYS 867  ? B LYS 175 
46 1 Y 1 B GLU 868  ? B GLU 176 
47 1 Y 1 B TYR 869  ? B TYR 177 
48 1 Y 1 B HIS 870  ? B HIS 178 
49 1 Y 1 B ALA 871  ? B ALA 179 
50 1 Y 1 B GLU 872  ? B GLU 180 
51 1 Y 1 B GLY 873  ? B GLY 181 
52 1 Y 1 B GLY 874  ? B GLY 182 
53 1 Y 1 B LYS 875  ? B LYS 183 
54 1 Y 1 B VAL 876  ? B VAL 184 
55 1 Y 1 B GLU 1015 ? B GLU 323 
56 1 Y 1 B TYR 1016 ? B TYR 324 
57 1 Y 1 B LEU 1017 ? B LEU 325 
58 1 Y 1 B ILE 1018 ? B ILE 326 
59 1 Y 1 B PRO 1019 ? B PRO 327 
60 1 Y 1 B GLN 1020 ? B GLN 328 
61 1 Y 1 B GLN 1021 ? B GLN 329 
62 1 Y 1 B GLY 1022 ? B GLY 330 
# 
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 
A1IZ9 C1   C Y N 1   
A1IZ9 C2   C Y N 2   
A1IZ9 C3   C Y N 3   
A1IZ9 C7   C Y N 4   
A1IZ9 C8   C Y N 5   
A1IZ9 C9   C Y N 6   
A1IZ9 C10  C Y N 7   
A1IZ9 C11  C Y N 8   
A1IZ9 C12  C Y N 9   
A1IZ9 C13  C N N 10  
A1IZ9 C14  C N N 11  
A1IZ9 C15  C Y N 12  
A1IZ9 C16  C Y N 13  
A1IZ9 C19  C Y N 14  
A1IZ9 C20  C N N 15  
A1IZ9 C21  C N N 16  
A1IZ9 C22  C N N 17  
A1IZ9 O    O N N 18  
A1IZ9 N2   N N N 19  
A1IZ9 N1   N Y N 20  
A1IZ9 N3   N Y N 21  
A1IZ9 N5   N Y N 22  
A1IZ9 N4   N Y N 23  
A1IZ9 C18  C Y N 24  
A1IZ9 C17  C Y N 25  
A1IZ9 N    N Y N 26  
A1IZ9 F1   F N N 27  
A1IZ9 C6   C Y N 28  
A1IZ9 C5   C Y N 29  
A1IZ9 C    C Y N 30  
A1IZ9 F    F N N 31  
A1IZ9 C4   C Y N 32  
A1IZ9 H1   H N N 33  
A1IZ9 H2   H N N 34  
A1IZ9 H3   H N N 35  
A1IZ9 H4   H N N 36  
A1IZ9 H5   H N N 37  
A1IZ9 H8   H N N 38  
A1IZ9 H9   H N N 39  
A1IZ9 H10  H N N 40  
A1IZ9 H11  H N N 41  
A1IZ9 H12  H N N 42  
A1IZ9 H13  H N N 43  
A1IZ9 H14  H N N 44  
A1IZ9 H15  H N N 45  
A1IZ9 H16  H N N 46  
A1IZ9 H6   H N N 47  
A1IZ9 H7   H N N 48  
A1IZ9 H17  H N N 49  
A1IZ9 H18  H N N 50  
ALA   N    N N N 51  
ALA   CA   C N S 52  
ALA   C    C N N 53  
ALA   O    O N N 54  
ALA   CB   C N N 55  
ALA   OXT  O N N 56  
ALA   H    H N N 57  
ALA   H2   H N N 58  
ALA   HA   H N N 59  
ALA   HB1  H N N 60  
ALA   HB2  H N N 61  
ALA   HB3  H N N 62  
ALA   HXT  H N N 63  
ARG   N    N N N 64  
ARG   CA   C N S 65  
ARG   C    C N N 66  
ARG   O    O N N 67  
ARG   CB   C N N 68  
ARG   CG   C N N 69  
ARG   CD   C N N 70  
ARG   NE   N N N 71  
ARG   CZ   C N N 72  
ARG   NH1  N N N 73  
ARG   NH2  N N N 74  
ARG   OXT  O N N 75  
ARG   H    H N N 76  
ARG   H2   H N N 77  
ARG   HA   H N N 78  
ARG   HB2  H N N 79  
ARG   HB3  H N N 80  
ARG   HG2  H N N 81  
ARG   HG3  H N N 82  
ARG   HD2  H N N 83  
ARG   HD3  H N N 84  
ARG   HE   H N N 85  
ARG   HH11 H N N 86  
ARG   HH12 H N N 87  
ARG   HH21 H N N 88  
ARG   HH22 H N N 89  
ARG   HXT  H N N 90  
ASN   N    N N N 91  
ASN   CA   C N S 92  
ASN   C    C N N 93  
ASN   O    O N N 94  
ASN   CB   C N N 95  
ASN   CG   C N N 96  
ASN   OD1  O N N 97  
ASN   ND2  N N N 98  
ASN   OXT  O N N 99  
ASN   H    H N N 100 
ASN   H2   H N N 101 
ASN   HA   H N N 102 
ASN   HB2  H N N 103 
ASN   HB3  H N N 104 
ASN   HD21 H N N 105 
ASN   HD22 H N N 106 
ASN   HXT  H N N 107 
ASP   N    N N N 108 
ASP   CA   C N S 109 
ASP   C    C N N 110 
ASP   O    O N N 111 
ASP   CB   C N N 112 
ASP   CG   C N N 113 
ASP   OD1  O N N 114 
ASP   OD2  O N N 115 
ASP   OXT  O N N 116 
ASP   H    H N N 117 
ASP   H2   H N N 118 
ASP   HA   H N N 119 
ASP   HB2  H N N 120 
ASP   HB3  H N N 121 
ASP   HD2  H N N 122 
ASP   HXT  H N N 123 
CYS   N    N N N 124 
CYS   CA   C N R 125 
CYS   C    C N N 126 
CYS   O    O N N 127 
CYS   CB   C N N 128 
CYS   SG   S N N 129 
CYS   OXT  O N N 130 
CYS   H    H N N 131 
CYS   H2   H N N 132 
CYS   HA   H N N 133 
CYS   HB2  H N N 134 
CYS   HB3  H N N 135 
CYS   HG   H N N 136 
CYS   HXT  H N N 137 
GLN   N    N N N 138 
GLN   CA   C N S 139 
GLN   C    C N N 140 
GLN   O    O N N 141 
GLN   CB   C N N 142 
GLN   CG   C N N 143 
GLN   CD   C N N 144 
GLN   OE1  O N N 145 
GLN   NE2  N N N 146 
GLN   OXT  O N N 147 
GLN   H    H N N 148 
GLN   H2   H N N 149 
GLN   HA   H N N 150 
GLN   HB2  H N N 151 
GLN   HB3  H N N 152 
GLN   HG2  H N N 153 
GLN   HG3  H N N 154 
GLN   HE21 H N N 155 
GLN   HE22 H N N 156 
GLN   HXT  H N N 157 
GLU   N    N N N 158 
GLU   CA   C N S 159 
GLU   C    C N N 160 
GLU   O    O N N 161 
GLU   CB   C N N 162 
GLU   CG   C N N 163 
GLU   CD   C N N 164 
GLU   OE1  O N N 165 
GLU   OE2  O N N 166 
GLU   OXT  O N N 167 
GLU   H    H N N 168 
GLU   H2   H N N 169 
GLU   HA   H N N 170 
GLU   HB2  H N N 171 
GLU   HB3  H N N 172 
GLU   HG2  H N N 173 
GLU   HG3  H N N 174 
GLU   HE2  H N N 175 
GLU   HXT  H N N 176 
GLY   N    N N N 177 
GLY   CA   C N N 178 
GLY   C    C N N 179 
GLY   O    O N N 180 
GLY   OXT  O N N 181 
GLY   H    H N N 182 
GLY   H2   H N N 183 
GLY   HA2  H N N 184 
GLY   HA3  H N N 185 
GLY   HXT  H N N 186 
HIS   N    N N N 187 
HIS   CA   C N S 188 
HIS   C    C N N 189 
HIS   O    O N N 190 
HIS   CB   C N N 191 
HIS   CG   C Y N 192 
HIS   ND1  N Y N 193 
HIS   CD2  C Y N 194 
HIS   CE1  C Y N 195 
HIS   NE2  N Y N 196 
HIS   OXT  O N N 197 
HIS   H    H N N 198 
HIS   H2   H N N 199 
HIS   HA   H N N 200 
HIS   HB2  H N N 201 
HIS   HB3  H N N 202 
HIS   HD1  H N N 203 
HIS   HD2  H N N 204 
HIS   HE1  H N N 205 
HIS   HE2  H N N 206 
HIS   HXT  H N N 207 
HOH   O    O N N 208 
HOH   H1   H N N 209 
HOH   H2   H N N 210 
ILE   N    N N N 211 
ILE   CA   C N S 212 
ILE   C    C N N 213 
ILE   O    O N N 214 
ILE   CB   C N S 215 
ILE   CG1  C N N 216 
ILE   CG2  C N N 217 
ILE   CD1  C N N 218 
ILE   OXT  O N N 219 
ILE   H    H N N 220 
ILE   H2   H N N 221 
ILE   HA   H N N 222 
ILE   HB   H N N 223 
ILE   HG12 H N N 224 
ILE   HG13 H N N 225 
ILE   HG21 H N N 226 
ILE   HG22 H N N 227 
ILE   HG23 H N N 228 
ILE   HD11 H N N 229 
ILE   HD12 H N N 230 
ILE   HD13 H N N 231 
ILE   HXT  H N N 232 
LEU   N    N N N 233 
LEU   CA   C N S 234 
LEU   C    C N N 235 
LEU   O    O N N 236 
LEU   CB   C N N 237 
LEU   CG   C N N 238 
LEU   CD1  C N N 239 
LEU   CD2  C N N 240 
LEU   OXT  O N N 241 
LEU   H    H N N 242 
LEU   H2   H N N 243 
LEU   HA   H N N 244 
LEU   HB2  H N N 245 
LEU   HB3  H N N 246 
LEU   HG   H N N 247 
LEU   HD11 H N N 248 
LEU   HD12 H N N 249 
LEU   HD13 H N N 250 
LEU   HD21 H N N 251 
LEU   HD22 H N N 252 
LEU   HD23 H N N 253 
LEU   HXT  H N N 254 
LYS   N    N N N 255 
LYS   CA   C N S 256 
LYS   C    C N N 257 
LYS   O    O N N 258 
LYS   CB   C N N 259 
LYS   CG   C N N 260 
LYS   CD   C N N 261 
LYS   CE   C N N 262 
LYS   NZ   N N N 263 
LYS   OXT  O N N 264 
LYS   H    H N N 265 
LYS   H2   H N N 266 
LYS   HA   H N N 267 
LYS   HB2  H N N 268 
LYS   HB3  H N N 269 
LYS   HG2  H N N 270 
LYS   HG3  H N N 271 
LYS   HD2  H N N 272 
LYS   HD3  H N N 273 
LYS   HE2  H N N 274 
LYS   HE3  H N N 275 
LYS   HZ1  H N N 276 
LYS   HZ2  H N N 277 
LYS   HZ3  H N N 278 
LYS   HXT  H N N 279 
MET   N    N N N 280 
MET   CA   C N S 281 
MET   C    C N N 282 
MET   O    O N N 283 
MET   CB   C N N 284 
MET   CG   C N N 285 
MET   SD   S N N 286 
MET   CE   C N N 287 
MET   OXT  O N N 288 
MET   H    H N N 289 
MET   H2   H N N 290 
MET   HA   H N N 291 
MET   HB2  H N N 292 
MET   HB3  H N N 293 
MET   HG2  H N N 294 
MET   HG3  H N N 295 
MET   HE1  H N N 296 
MET   HE2  H N N 297 
MET   HE3  H N N 298 
MET   HXT  H N N 299 
PHE   N    N N N 300 
PHE   CA   C N S 301 
PHE   C    C N N 302 
PHE   O    O N N 303 
PHE   CB   C N N 304 
PHE   CG   C Y N 305 
PHE   CD1  C Y N 306 
PHE   CD2  C Y N 307 
PHE   CE1  C Y N 308 
PHE   CE2  C Y N 309 
PHE   CZ   C Y N 310 
PHE   OXT  O N N 311 
PHE   H    H N N 312 
PHE   H2   H N N 313 
PHE   HA   H N N 314 
PHE   HB2  H N N 315 
PHE   HB3  H N N 316 
PHE   HD1  H N N 317 
PHE   HD2  H N N 318 
PHE   HE1  H N N 319 
PHE   HE2  H N N 320 
PHE   HZ   H N N 321 
PHE   HXT  H N N 322 
PRO   N    N N N 323 
PRO   CA   C N S 324 
PRO   C    C N N 325 
PRO   O    O N N 326 
PRO   CB   C N N 327 
PRO   CG   C N N 328 
PRO   CD   C N N 329 
PRO   OXT  O N N 330 
PRO   H    H N N 331 
PRO   HA   H N N 332 
PRO   HB2  H N N 333 
PRO   HB3  H N N 334 
PRO   HG2  H N N 335 
PRO   HG3  H N N 336 
PRO   HD2  H N N 337 
PRO   HD3  H N N 338 
PRO   HXT  H N N 339 
SER   N    N N N 340 
SER   CA   C N S 341 
SER   C    C N N 342 
SER   O    O N N 343 
SER   CB   C N N 344 
SER   OG   O N N 345 
SER   OXT  O N N 346 
SER   H    H N N 347 
SER   H2   H N N 348 
SER   HA   H N N 349 
SER   HB2  H N N 350 
SER   HB3  H N N 351 
SER   HG   H N N 352 
SER   HXT  H N N 353 
THR   N    N N N 354 
THR   CA   C N S 355 
THR   C    C N N 356 
THR   O    O N N 357 
THR   CB   C N R 358 
THR   OG1  O N N 359 
THR   CG2  C N N 360 
THR   OXT  O N N 361 
THR   H    H N N 362 
THR   H2   H N N 363 
THR   HA   H N N 364 
THR   HB   H N N 365 
THR   HG1  H N N 366 
THR   HG21 H N N 367 
THR   HG22 H N N 368 
THR   HG23 H N N 369 
THR   HXT  H N N 370 
TRP   N    N N N 371 
TRP   CA   C N S 372 
TRP   C    C N N 373 
TRP   O    O N N 374 
TRP   CB   C N N 375 
TRP   CG   C Y N 376 
TRP   CD1  C Y N 377 
TRP   CD2  C Y N 378 
TRP   NE1  N Y N 379 
TRP   CE2  C Y N 380 
TRP   CE3  C Y N 381 
TRP   CZ2  C Y N 382 
TRP   CZ3  C Y N 383 
TRP   CH2  C Y N 384 
TRP   OXT  O N N 385 
TRP   H    H N N 386 
TRP   H2   H N N 387 
TRP   HA   H N N 388 
TRP   HB2  H N N 389 
TRP   HB3  H N N 390 
TRP   HD1  H N N 391 
TRP   HE1  H N N 392 
TRP   HE3  H N N 393 
TRP   HZ2  H N N 394 
TRP   HZ3  H N N 395 
TRP   HH2  H N N 396 
TRP   HXT  H N N 397 
TYR   N    N N N 398 
TYR   CA   C N S 399 
TYR   C    C N N 400 
TYR   O    O N N 401 
TYR   CB   C N N 402 
TYR   CG   C Y N 403 
TYR   CD1  C Y N 404 
TYR   CD2  C Y N 405 
TYR   CE1  C Y N 406 
TYR   CE2  C Y N 407 
TYR   CZ   C Y N 408 
TYR   OH   O N N 409 
TYR   OXT  O N N 410 
TYR   H    H N N 411 
TYR   H2   H N N 412 
TYR   HA   H N N 413 
TYR   HB2  H N N 414 
TYR   HB3  H N N 415 
TYR   HD1  H N N 416 
TYR   HD2  H N N 417 
TYR   HE1  H N N 418 
TYR   HE2  H N N 419 
TYR   HH   H N N 420 
TYR   HXT  H N N 421 
VAL   N    N N N 422 
VAL   CA   C N S 423 
VAL   C    C N N 424 
VAL   O    O N N 425 
VAL   CB   C N N 426 
VAL   CG1  C N N 427 
VAL   CG2  C N N 428 
VAL   OXT  O N N 429 
VAL   H    H N N 430 
VAL   H2   H N N 431 
VAL   HA   H N N 432 
VAL   HB   H N N 433 
VAL   HG11 H N N 434 
VAL   HG12 H N N 435 
VAL   HG13 H N N 436 
VAL   HG21 H N N 437 
VAL   HG22 H N N 438 
VAL   HG23 H N N 439 
VAL   HXT  H N N 440 
# 
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 
A1IZ9 C1  C2   doub Y N 1   
A1IZ9 C1  C    sing Y N 2   
A1IZ9 F   C    sing N N 3   
A1IZ9 C2  C3   sing Y N 4   
A1IZ9 C   C5   doub Y N 5   
A1IZ9 C3  C4   doub Y N 6   
A1IZ9 C5  C4   sing Y N 7   
A1IZ9 C5  C6   sing N N 8   
A1IZ9 F1  C10  sing N N 9   
A1IZ9 C6  C10  doub Y N 10  
A1IZ9 C6  C7   sing Y N 11  
A1IZ9 C10 C9   sing Y N 12  
A1IZ9 C7  C8   doub Y N 13  
A1IZ9 C9  N    doub Y N 14  
A1IZ9 N1  C11  doub Y N 15  
A1IZ9 N1  C12  sing Y N 16  
A1IZ9 C8  N    sing Y N 17  
A1IZ9 C8  C11  sing N N 18  
A1IZ9 C11 N3   sing Y N 19  
A1IZ9 C12 C13  sing N N 20  
A1IZ9 C12 C15  doub Y N 21  
A1IZ9 C13 N2   sing N N 22  
A1IZ9 C21 C22  sing N N 23  
A1IZ9 C21 C20  sing N N 24  
A1IZ9 N3  C15  sing Y N 25  
A1IZ9 N3  C16  sing N N 26  
A1IZ9 C15 C14  sing N N 27  
A1IZ9 N2  C20  sing N N 28  
A1IZ9 N2  C14  sing N N 29  
A1IZ9 C20 O    doub N N 30  
A1IZ9 C16 N5   doub Y N 31  
A1IZ9 C16 C17  sing Y N 32  
A1IZ9 N5  C19  sing Y N 33  
A1IZ9 C17 C18  doub Y N 34  
A1IZ9 C19 N4   doub Y N 35  
A1IZ9 C18 N4   sing Y N 36  
A1IZ9 C1  H1   sing N N 37  
A1IZ9 C2  H2   sing N N 38  
A1IZ9 C3  H3   sing N N 39  
A1IZ9 C7  H4   sing N N 40  
A1IZ9 C9  H5   sing N N 41  
A1IZ9 C19 H8   sing N N 42  
A1IZ9 C21 H9   sing N N 43  
A1IZ9 C21 H10  sing N N 44  
A1IZ9 C22 H11  sing N N 45  
A1IZ9 C22 H12  sing N N 46  
A1IZ9 C22 H13  sing N N 47  
A1IZ9 C18 H14  sing N N 48  
A1IZ9 C17 H15  sing N N 49  
A1IZ9 C4  H16  sing N N 50  
A1IZ9 C13 H6   sing N N 51  
A1IZ9 C13 H7   sing N N 52  
A1IZ9 C14 H17  sing N N 53  
A1IZ9 C14 H18  sing N N 54  
ALA   N   CA   sing N N 55  
ALA   N   H    sing N N 56  
ALA   N   H2   sing N N 57  
ALA   CA  C    sing N N 58  
ALA   CA  CB   sing N N 59  
ALA   CA  HA   sing N N 60  
ALA   C   O    doub N N 61  
ALA   C   OXT  sing N N 62  
ALA   CB  HB1  sing N N 63  
ALA   CB  HB2  sing N N 64  
ALA   CB  HB3  sing N N 65  
ALA   OXT HXT  sing N N 66  
ARG   N   CA   sing N N 67  
ARG   N   H    sing N N 68  
ARG   N   H2   sing N N 69  
ARG   CA  C    sing N N 70  
ARG   CA  CB   sing N N 71  
ARG   CA  HA   sing N N 72  
ARG   C   O    doub N N 73  
ARG   C   OXT  sing N N 74  
ARG   CB  CG   sing N N 75  
ARG   CB  HB2  sing N N 76  
ARG   CB  HB3  sing N N 77  
ARG   CG  CD   sing N N 78  
ARG   CG  HG2  sing N N 79  
ARG   CG  HG3  sing N N 80  
ARG   CD  NE   sing N N 81  
ARG   CD  HD2  sing N N 82  
ARG   CD  HD3  sing N N 83  
ARG   NE  CZ   sing N N 84  
ARG   NE  HE   sing N N 85  
ARG   CZ  NH1  sing N N 86  
ARG   CZ  NH2  doub N N 87  
ARG   NH1 HH11 sing N N 88  
ARG   NH1 HH12 sing N N 89  
ARG   NH2 HH21 sing N N 90  
ARG   NH2 HH22 sing N N 91  
ARG   OXT HXT  sing N N 92  
ASN   N   CA   sing N N 93  
ASN   N   H    sing N N 94  
ASN   N   H2   sing N N 95  
ASN   CA  C    sing N N 96  
ASN   CA  CB   sing N N 97  
ASN   CA  HA   sing N N 98  
ASN   C   O    doub N N 99  
ASN   C   OXT  sing N N 100 
ASN   CB  CG   sing N N 101 
ASN   CB  HB2  sing N N 102 
ASN   CB  HB3  sing N N 103 
ASN   CG  OD1  doub N N 104 
ASN   CG  ND2  sing N N 105 
ASN   ND2 HD21 sing N N 106 
ASN   ND2 HD22 sing N N 107 
ASN   OXT HXT  sing N N 108 
ASP   N   CA   sing N N 109 
ASP   N   H    sing N N 110 
ASP   N   H2   sing N N 111 
ASP   CA  C    sing N N 112 
ASP   CA  CB   sing N N 113 
ASP   CA  HA   sing N N 114 
ASP   C   O    doub N N 115 
ASP   C   OXT  sing N N 116 
ASP   CB  CG   sing N N 117 
ASP   CB  HB2  sing N N 118 
ASP   CB  HB3  sing N N 119 
ASP   CG  OD1  doub N N 120 
ASP   CG  OD2  sing N N 121 
ASP   OD2 HD2  sing N N 122 
ASP   OXT HXT  sing N N 123 
CYS   N   CA   sing N N 124 
CYS   N   H    sing N N 125 
CYS   N   H2   sing N N 126 
CYS   CA  C    sing N N 127 
CYS   CA  CB   sing N N 128 
CYS   CA  HA   sing N N 129 
CYS   C   O    doub N N 130 
CYS   C   OXT  sing N N 131 
CYS   CB  SG   sing N N 132 
CYS   CB  HB2  sing N N 133 
CYS   CB  HB3  sing N N 134 
CYS   SG  HG   sing N N 135 
CYS   OXT HXT  sing N N 136 
GLN   N   CA   sing N N 137 
GLN   N   H    sing N N 138 
GLN   N   H2   sing N N 139 
GLN   CA  C    sing N N 140 
GLN   CA  CB   sing N N 141 
GLN   CA  HA   sing N N 142 
GLN   C   O    doub N N 143 
GLN   C   OXT  sing N N 144 
GLN   CB  CG   sing N N 145 
GLN   CB  HB2  sing N N 146 
GLN   CB  HB3  sing N N 147 
GLN   CG  CD   sing N N 148 
GLN   CG  HG2  sing N N 149 
GLN   CG  HG3  sing N N 150 
GLN   CD  OE1  doub N N 151 
GLN   CD  NE2  sing N N 152 
GLN   NE2 HE21 sing N N 153 
GLN   NE2 HE22 sing N N 154 
GLN   OXT HXT  sing N N 155 
GLU   N   CA   sing N N 156 
GLU   N   H    sing N N 157 
GLU   N   H2   sing N N 158 
GLU   CA  C    sing N N 159 
GLU   CA  CB   sing N N 160 
GLU   CA  HA   sing N N 161 
GLU   C   O    doub N N 162 
GLU   C   OXT  sing N N 163 
GLU   CB  CG   sing N N 164 
GLU   CB  HB2  sing N N 165 
GLU   CB  HB3  sing N N 166 
GLU   CG  CD   sing N N 167 
GLU   CG  HG2  sing N N 168 
GLU   CG  HG3  sing N N 169 
GLU   CD  OE1  doub N N 170 
GLU   CD  OE2  sing N N 171 
GLU   OE2 HE2  sing N N 172 
GLU   OXT HXT  sing N N 173 
GLY   N   CA   sing N N 174 
GLY   N   H    sing N N 175 
GLY   N   H2   sing N N 176 
GLY   CA  C    sing N N 177 
GLY   CA  HA2  sing N N 178 
GLY   CA  HA3  sing N N 179 
GLY   C   O    doub N N 180 
GLY   C   OXT  sing N N 181 
GLY   OXT HXT  sing N N 182 
HIS   N   CA   sing N N 183 
HIS   N   H    sing N N 184 
HIS   N   H2   sing N N 185 
HIS   CA  C    sing N N 186 
HIS   CA  CB   sing N N 187 
HIS   CA  HA   sing N N 188 
HIS   C   O    doub N N 189 
HIS   C   OXT  sing N N 190 
HIS   CB  CG   sing N N 191 
HIS   CB  HB2  sing N N 192 
HIS   CB  HB3  sing N N 193 
HIS   CG  ND1  sing Y N 194 
HIS   CG  CD2  doub Y N 195 
HIS   ND1 CE1  doub Y N 196 
HIS   ND1 HD1  sing N N 197 
HIS   CD2 NE2  sing Y N 198 
HIS   CD2 HD2  sing N N 199 
HIS   CE1 NE2  sing Y N 200 
HIS   CE1 HE1  sing N N 201 
HIS   NE2 HE2  sing N N 202 
HIS   OXT HXT  sing N N 203 
HOH   O   H1   sing N N 204 
HOH   O   H2   sing N N 205 
ILE   N   CA   sing N N 206 
ILE   N   H    sing N N 207 
ILE   N   H2   sing N N 208 
ILE   CA  C    sing N N 209 
ILE   CA  CB   sing N N 210 
ILE   CA  HA   sing N N 211 
ILE   C   O    doub N N 212 
ILE   C   OXT  sing N N 213 
ILE   CB  CG1  sing N N 214 
ILE   CB  CG2  sing N N 215 
ILE   CB  HB   sing N N 216 
ILE   CG1 CD1  sing N N 217 
ILE   CG1 HG12 sing N N 218 
ILE   CG1 HG13 sing N N 219 
ILE   CG2 HG21 sing N N 220 
ILE   CG2 HG22 sing N N 221 
ILE   CG2 HG23 sing N N 222 
ILE   CD1 HD11 sing N N 223 
ILE   CD1 HD12 sing N N 224 
ILE   CD1 HD13 sing N N 225 
ILE   OXT HXT  sing N N 226 
LEU   N   CA   sing N N 227 
LEU   N   H    sing N N 228 
LEU   N   H2   sing N N 229 
LEU   CA  C    sing N N 230 
LEU   CA  CB   sing N N 231 
LEU   CA  HA   sing N N 232 
LEU   C   O    doub N N 233 
LEU   C   OXT  sing N N 234 
LEU   CB  CG   sing N N 235 
LEU   CB  HB2  sing N N 236 
LEU   CB  HB3  sing N N 237 
LEU   CG  CD1  sing N N 238 
LEU   CG  CD2  sing N N 239 
LEU   CG  HG   sing N N 240 
LEU   CD1 HD11 sing N N 241 
LEU   CD1 HD12 sing N N 242 
LEU   CD1 HD13 sing N N 243 
LEU   CD2 HD21 sing N N 244 
LEU   CD2 HD22 sing N N 245 
LEU   CD2 HD23 sing N N 246 
LEU   OXT HXT  sing N N 247 
LYS   N   CA   sing N N 248 
LYS   N   H    sing N N 249 
LYS   N   H2   sing N N 250 
LYS   CA  C    sing N N 251 
LYS   CA  CB   sing N N 252 
LYS   CA  HA   sing N N 253 
LYS   C   O    doub N N 254 
LYS   C   OXT  sing N N 255 
LYS   CB  CG   sing N N 256 
LYS   CB  HB2  sing N N 257 
LYS   CB  HB3  sing N N 258 
LYS   CG  CD   sing N N 259 
LYS   CG  HG2  sing N N 260 
LYS   CG  HG3  sing N N 261 
LYS   CD  CE   sing N N 262 
LYS   CD  HD2  sing N N 263 
LYS   CD  HD3  sing N N 264 
LYS   CE  NZ   sing N N 265 
LYS   CE  HE2  sing N N 266 
LYS   CE  HE3  sing N N 267 
LYS   NZ  HZ1  sing N N 268 
LYS   NZ  HZ2  sing N N 269 
LYS   NZ  HZ3  sing N N 270 
LYS   OXT HXT  sing N N 271 
MET   N   CA   sing N N 272 
MET   N   H    sing N N 273 
MET   N   H2   sing N N 274 
MET   CA  C    sing N N 275 
MET   CA  CB   sing N N 276 
MET   CA  HA   sing N N 277 
MET   C   O    doub N N 278 
MET   C   OXT  sing N N 279 
MET   CB  CG   sing N N 280 
MET   CB  HB2  sing N N 281 
MET   CB  HB3  sing N N 282 
MET   CG  SD   sing N N 283 
MET   CG  HG2  sing N N 284 
MET   CG  HG3  sing N N 285 
MET   SD  CE   sing N N 286 
MET   CE  HE1  sing N N 287 
MET   CE  HE2  sing N N 288 
MET   CE  HE3  sing N N 289 
MET   OXT HXT  sing N N 290 
PHE   N   CA   sing N N 291 
PHE   N   H    sing N N 292 
PHE   N   H2   sing N N 293 
PHE   CA  C    sing N N 294 
PHE   CA  CB   sing N N 295 
PHE   CA  HA   sing N N 296 
PHE   C   O    doub N N 297 
PHE   C   OXT  sing N N 298 
PHE   CB  CG   sing N N 299 
PHE   CB  HB2  sing N N 300 
PHE   CB  HB3  sing N N 301 
PHE   CG  CD1  doub Y N 302 
PHE   CG  CD2  sing Y N 303 
PHE   CD1 CE1  sing Y N 304 
PHE   CD1 HD1  sing N N 305 
PHE   CD2 CE2  doub Y N 306 
PHE   CD2 HD2  sing N N 307 
PHE   CE1 CZ   doub Y N 308 
PHE   CE1 HE1  sing N N 309 
PHE   CE2 CZ   sing Y N 310 
PHE   CE2 HE2  sing N N 311 
PHE   CZ  HZ   sing N N 312 
PHE   OXT HXT  sing N N 313 
PRO   N   CA   sing N N 314 
PRO   N   CD   sing N N 315 
PRO   N   H    sing N N 316 
PRO   CA  C    sing N N 317 
PRO   CA  CB   sing N N 318 
PRO   CA  HA   sing N N 319 
PRO   C   O    doub N N 320 
PRO   C   OXT  sing N N 321 
PRO   CB  CG   sing N N 322 
PRO   CB  HB2  sing N N 323 
PRO   CB  HB3  sing N N 324 
PRO   CG  CD   sing N N 325 
PRO   CG  HG2  sing N N 326 
PRO   CG  HG3  sing N N 327 
PRO   CD  HD2  sing N N 328 
PRO   CD  HD3  sing N N 329 
PRO   OXT HXT  sing N N 330 
SER   N   CA   sing N N 331 
SER   N   H    sing N N 332 
SER   N   H2   sing N N 333 
SER   CA  C    sing N N 334 
SER   CA  CB   sing N N 335 
SER   CA  HA   sing N N 336 
SER   C   O    doub N N 337 
SER   C   OXT  sing N N 338 
SER   CB  OG   sing N N 339 
SER   CB  HB2  sing N N 340 
SER   CB  HB3  sing N N 341 
SER   OG  HG   sing N N 342 
SER   OXT HXT  sing N N 343 
THR   N   CA   sing N N 344 
THR   N   H    sing N N 345 
THR   N   H2   sing N N 346 
THR   CA  C    sing N N 347 
THR   CA  CB   sing N N 348 
THR   CA  HA   sing N N 349 
THR   C   O    doub N N 350 
THR   C   OXT  sing N N 351 
THR   CB  OG1  sing N N 352 
THR   CB  CG2  sing N N 353 
THR   CB  HB   sing N N 354 
THR   OG1 HG1  sing N N 355 
THR   CG2 HG21 sing N N 356 
THR   CG2 HG22 sing N N 357 
THR   CG2 HG23 sing N N 358 
THR   OXT HXT  sing N N 359 
TRP   N   CA   sing N N 360 
TRP   N   H    sing N N 361 
TRP   N   H2   sing N N 362 
TRP   CA  C    sing N N 363 
TRP   CA  CB   sing N N 364 
TRP   CA  HA   sing N N 365 
TRP   C   O    doub N N 366 
TRP   C   OXT  sing N N 367 
TRP   CB  CG   sing N N 368 
TRP   CB  HB2  sing N N 369 
TRP   CB  HB3  sing N N 370 
TRP   CG  CD1  doub Y N 371 
TRP   CG  CD2  sing Y N 372 
TRP   CD1 NE1  sing Y N 373 
TRP   CD1 HD1  sing N N 374 
TRP   CD2 CE2  doub Y N 375 
TRP   CD2 CE3  sing Y N 376 
TRP   NE1 CE2  sing Y N 377 
TRP   NE1 HE1  sing N N 378 
TRP   CE2 CZ2  sing Y N 379 
TRP   CE3 CZ3  doub Y N 380 
TRP   CE3 HE3  sing N N 381 
TRP   CZ2 CH2  doub Y N 382 
TRP   CZ2 HZ2  sing N N 383 
TRP   CZ3 CH2  sing Y N 384 
TRP   CZ3 HZ3  sing N N 385 
TRP   CH2 HH2  sing N N 386 
TRP   OXT HXT  sing N N 387 
TYR   N   CA   sing N N 388 
TYR   N   H    sing N N 389 
TYR   N   H2   sing N N 390 
TYR   CA  C    sing N N 391 
TYR   CA  CB   sing N N 392 
TYR   CA  HA   sing N N 393 
TYR   C   O    doub N N 394 
TYR   C   OXT  sing N N 395 
TYR   CB  CG   sing N N 396 
TYR   CB  HB2  sing N N 397 
TYR   CB  HB3  sing N N 398 
TYR   CG  CD1  doub Y N 399 
TYR   CG  CD2  sing Y N 400 
TYR   CD1 CE1  sing Y N 401 
TYR   CD1 HD1  sing N N 402 
TYR   CD2 CE2  doub Y N 403 
TYR   CD2 HD2  sing N N 404 
TYR   CE1 CZ   doub Y N 405 
TYR   CE1 HE1  sing N N 406 
TYR   CE2 CZ   sing Y N 407 
TYR   CE2 HE2  sing N N 408 
TYR   CZ  OH   sing N N 409 
TYR   OH  HH   sing N N 410 
TYR   OXT HXT  sing N N 411 
VAL   N   CA   sing N N 412 
VAL   N   H    sing N N 413 
VAL   N   H2   sing N N 414 
VAL   CA  C    sing N N 415 
VAL   CA  CB   sing N N 416 
VAL   CA  HA   sing N N 417 
VAL   C   O    doub N N 418 
VAL   C   OXT  sing N N 419 
VAL   CB  CG1  sing N N 420 
VAL   CB  CG2  sing N N 421 
VAL   CB  HB   sing N N 422 
VAL   CG1 HG11 sing N N 423 
VAL   CG1 HG12 sing N N 424 
VAL   CG1 HG13 sing N N 425 
VAL   CG2 HG21 sing N N 426 
VAL   CG2 HG22 sing N N 427 
VAL   CG2 HG23 sing N N 428 
VAL   OXT HXT  sing N N 429 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'in house' 
# 
_atom_sites.entry_id                    9GC6 
_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]   0.013083 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005521 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014098 
_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]   0.013874 
_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 
C 
F 
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   . ALA   A 1 6   ? 25.486  -7.584  7.009  1.00 57.41 ? 698  ALA   A N   1 
ATOM   2    C CA  . ALA   A 1 6   ? 26.811  -7.922  7.535  1.00 57.72 ? 698  ALA   A CA  1 
ATOM   3    C C   . ALA   A 1 6   ? 26.929  -7.620  9.041  1.00 57.86 ? 698  ALA   A C   1 
ATOM   4    O O   . ALA   A 1 6   ? 27.578  -6.645  9.438  1.00 58.29 ? 698  ALA   A O   1 
ATOM   5    C CB  . ALA   A 1 6   ? 27.886  -7.173  6.758  1.00 57.77 ? 698  ALA   A CB  1 
ATOM   6    N N   . PRO   A 1 7   ? 26.324  -8.459  9.905  1.00 57.07 ? 699  PRO   A N   1 
ATOM   7    C CA  . PRO   A 1 7   ? 26.409  -8.196  11.352 1.00 56.26 ? 699  PRO   A CA  1 
ATOM   8    C C   . PRO   A 1 7   ? 27.742  -8.639  11.985 1.00 54.83 ? 699  PRO   A C   1 
ATOM   9    O O   . PRO   A 1 7   ? 28.700  -8.925  11.260 1.00 55.36 ? 699  PRO   A O   1 
ATOM   10   C CB  . PRO   A 1 7   ? 25.177  -8.928  11.906 1.00 57.25 ? 699  PRO   A CB  1 
ATOM   11   C CG  . PRO   A 1 7   ? 24.988  -10.077 10.975 1.00 57.98 ? 699  PRO   A CG  1 
ATOM   12   C CD  . PRO   A 1 7   ? 25.511  -9.659  9.614  1.00 56.55 ? 699  PRO   A CD  1 
ATOM   13   N N   . ASN   A 1 8   ? 27.824  -8.670  13.330 1.00 52.71 ? 700  ASN   A N   1 
ATOM   14   C CA  . ASN   A 1 8   ? 29.045  -9.070  14.015 1.00 51.04 ? 700  ASN   A CA  1 
ATOM   15   C C   . ASN   A 1 8   ? 29.270  -10.588 13.949 1.00 49.21 ? 700  ASN   A C   1 
ATOM   16   O O   . ASN   A 1 8   ? 28.540  -11.350 14.588 1.00 49.37 ? 700  ASN   A O   1 
ATOM   17   C CB  . ASN   A 1 8   ? 29.011  -8.589  15.459 1.00 51.99 ? 700  ASN   A CB  1 
ATOM   18   C CG  . ASN   A 1 8   ? 30.309  -8.763  16.198 1.00 55.01 ? 700  ASN   A CG  1 
ATOM   19   O OD1 . ASN   A 1 8   ? 31.390  -8.858  15.605 1.00 56.35 ? 700  ASN   A OD1 1 
ATOM   20   N ND2 . ASN   A 1 8   ? 30.229  -8.803  17.517 1.00 55.57 ? 700  ASN   A ND2 1 
ATOM   21   N N   . GLN   A 1 9   ? 30.293  -11.026 13.190 1.00 47.24 ? 701  GLN   A N   1 
ATOM   22   C CA  . GLN   A 1 9   ? 30.638  -12.447 13.073 1.00 45.50 ? 701  GLN   A CA  1 
ATOM   23   C C   . GLN   A 1 9   ? 31.142  -13.064 14.388 1.00 42.83 ? 701  GLN   A C   1 
ATOM   24   O O   . GLN   A 1 9   ? 31.112  -14.282 14.542 1.00 42.77 ? 701  GLN   A O   1 
ATOM   25   C CB  . GLN   A 1 9   ? 31.628  -12.683 11.926 1.00 47.52 ? 701  GLN   A CB  1 
ATOM   26   C CG  . GLN   A 1 9   ? 31.056  -12.286 10.567 1.00 52.00 ? 701  GLN   A CG  1 
ATOM   27   C CD  . GLN   A 1 9   ? 31.728  -12.988 9.410  1.00 57.84 ? 701  GLN   A CD  1 
ATOM   28   O OE1 . GLN   A 1 9   ? 32.836  -13.535 9.524  1.00 59.38 ? 701  GLN   A OE1 1 
ATOM   29   N NE2 . GLN   A 1 9   ? 31.063  -12.986 8.260  1.00 59.22 ? 701  GLN   A NE2 1 
ATOM   30   N N   . ALA   A 1 10  ? 31.561  -12.223 15.347 1.00 40.58 ? 702  ALA   A N   1 
ATOM   31   C CA  . ALA   A 1 10  ? 32.008  -12.662 16.667 1.00 38.98 ? 702  ALA   A CA  1 
ATOM   32   C C   . ALA   A 1 10  ? 30.871  -13.189 17.565 1.00 36.71 ? 702  ALA   A C   1 
ATOM   33   O O   . ALA   A 1 10  ? 31.141  -13.790 18.606 1.00 36.53 ? 702  ALA   A O   1 
ATOM   34   C CB  . ALA   A 1 10  ? 32.759  -11.543 17.372 1.00 39.13 ? 702  ALA   A CB  1 
ATOM   35   N N   . LEU   A 1 11  ? 29.610  -12.975 17.171 1.00 34.77 ? 703  LEU   A N   1 
ATOM   36   C CA  . LEU   A 1 11  ? 28.483  -13.482 17.942 1.00 33.39 ? 703  LEU   A CA  1 
ATOM   37   C C   . LEU   A 1 11  ? 28.199  -14.970 17.675 1.00 32.07 ? 703  LEU   A C   1 
ATOM   38   O O   . LEU   A 1 11  ? 27.594  -15.642 18.507 1.00 31.95 ? 703  LEU   A O   1 
ATOM   39   C CB  . LEU   A 1 11  ? 27.267  -12.603 17.705 1.00 33.41 ? 703  LEU   A CB  1 
ATOM   40   C CG  . LEU   A 1 11  ? 27.438  -11.227 18.308 1.00 35.12 ? 703  LEU   A CG  1 
ATOM   41   C CD1 . LEU   A 1 11  ? 26.485  -10.251 17.713 1.00 35.60 ? 703  LEU   A CD1 1 
ATOM   42   C CD2 . LEU   A 1 11  ? 27.288  -11.278 19.815 1.00 36.07 ? 703  LEU   A CD2 1 
ATOM   43   N N   . LEU   A 1 12  ? 28.683  -15.501 16.545 1.00 31.13 ? 704  LEU   A N   1 
ATOM   44   C CA  . LEU   A 1 12  ? 28.472  -16.897 16.200 1.00 30.60 ? 704  LEU   A CA  1 
ATOM   45   C C   . LEU   A 1 12  ? 29.768  -17.675 16.308 1.00 30.06 ? 704  LEU   A C   1 
ATOM   46   O O   . LEU   A 1 12  ? 30.709  -17.407 15.574 1.00 30.18 ? 704  LEU   A O   1 
ATOM   47   C CB  . LEU   A 1 12  ? 27.901  -17.008 14.783 1.00 30.53 ? 704  LEU   A CB  1 
ATOM   48   C CG  . LEU   A 1 12  ? 27.443  -18.401 14.390 1.00 32.21 ? 704  LEU   A CG  1 
ATOM   49   C CD1 . LEU   A 1 12  ? 26.229  -18.823 15.195 1.00 32.63 ? 704  LEU   A CD1 1 
ATOM   50   C CD2 . LEU   A 1 12  ? 27.145  -18.466 12.920 1.00 32.95 ? 704  LEU   A CD2 1 
ATOM   51   N N   . ARG   A 1 13  ? 29.816  -18.638 17.211 1.00 29.74 ? 705  ARG   A N   1 
ATOM   52   C CA  . ARG   A 1 13  ? 30.998  -19.462 17.380 1.00 29.97 ? 705  ARG   A CA  1 
ATOM   53   C C   . ARG   A 1 13  ? 30.879  -20.720 16.550 1.00 30.10 ? 705  ARG   A C   1 
ATOM   54   O O   . ARG   A 1 13  ? 29.941  -21.486 16.737 1.00 30.30 ? 705  ARG   A O   1 
ATOM   55   C CB  . ARG   A 1 13  ? 31.211  -19.828 18.844 1.00 31.28 ? 705  ARG   A CB  1 
ATOM   56   C CG  . ARG   A 1 13  ? 32.598  -20.393 19.079 1.00 34.52 ? 705  ARG   A CG  1 
ATOM   57   C CD  . ARG   A 1 13  ? 32.517  -21.552 20.019 1.00 37.90 ? 705  ARG   A CD  1 
ATOM   58   N NE  . ARG   A 1 13  ? 33.760  -22.323 20.071 1.00 40.33 ? 705  ARG   A NE  1 
ATOM   59   C CZ  . ARG   A 1 13  ? 34.745  -22.098 20.927 1.00 41.40 ? 705  ARG   A CZ  1 
ATOM   60   N NH1 . ARG   A 1 13  ? 34.676  -21.083 21.778 1.00 41.69 ? 705  ARG   A NH1 1 
ATOM   61   N NH2 . ARG   A 1 13  ? 35.816  -22.878 20.931 1.00 40.66 ? 705  ARG   A NH2 1 
ATOM   62   N N   . ILE   A 1 14  ? 31.833  -20.949 15.644 1.00 29.83 ? 706  ILE   A N   1 
ATOM   63   C CA  . ILE   A 1 14  ? 31.824  -22.135 14.793 1.00 30.27 ? 706  ILE   A CA  1 
ATOM   64   C C   . ILE   A 1 14  ? 32.323  -23.341 15.574 1.00 30.89 ? 706  ILE   A C   1 
ATOM   65   O O   . ILE   A 1 14  ? 33.494  -23.402 15.919 1.00 31.02 ? 706  ILE   A O   1 
ATOM   66   C CB  . ILE   A 1 14  ? 32.663  -21.920 13.511 1.00 30.44 ? 706  ILE   A CB  1 
ATOM   67   C CG1 . ILE   A 1 14  ? 32.325  -20.591 12.825 1.00 31.06 ? 706  ILE   A CG1 1 
ATOM   68   C CG2 . ILE   A 1 14  ? 32.485  -23.091 12.567 1.00 30.73 ? 706  ILE   A CG2 1 
ATOM   69   C CD1 . ILE   A 1 14  ? 30.846  -20.435 12.447 1.00 32.46 ? 706  ILE   A CD1 1 
ATOM   70   N N   . LEU   A 1 15  ? 31.448  -24.294 15.850 1.00 31.32 ? 707  LEU   A N   1 
ATOM   71   C CA  . LEU   A 1 15  ? 31.810  -25.483 16.608 1.00 32.42 ? 707  LEU   A CA  1 
ATOM   72   C C   . LEU   A 1 15  ? 32.210  -26.658 15.742 1.00 33.33 ? 707  LEU   A C   1 
ATOM   73   O O   . LEU   A 1 15  ? 31.567  -26.926 14.734 1.00 33.88 ? 707  LEU   A O   1 
ATOM   74   C CB  . LEU   A 1 15  ? 30.639  -25.903 17.487 1.00 32.72 ? 707  LEU   A CB  1 
ATOM   75   C CG  . LEU   A 1 15  ? 30.383  -25.010 18.665 1.00 34.00 ? 707  LEU   A CG  1 
ATOM   76   C CD1 . LEU   A 1 15  ? 29.077  -25.361 19.305 1.00 34.47 ? 707  LEU   A CD1 1 
ATOM   77   C CD2 . LEU   A 1 15  ? 31.521  -25.104 19.664 1.00 34.51 ? 707  LEU   A CD2 1 
ATOM   78   N N   . LYS   A 1 16  ? 33.242  -27.385 16.161 1.00 33.48 ? 708  LYS   A N   1 
ATOM   79   C CA  . LYS   A 1 16  ? 33.709  -28.605 15.504 1.00 34.45 ? 708  LYS   A CA  1 
ATOM   80   C C   . LYS   A 1 16  ? 33.010  -29.775 16.188 1.00 34.84 ? 708  LYS   A C   1 
ATOM   81   O O   . LYS   A 1 16  ? 32.798  -29.741 17.402 1.00 34.58 ? 708  LYS   A O   1 
ATOM   82   C CB  . LYS   A 1 16  ? 35.232  -28.784 15.684 1.00 37.10 ? 708  LYS   A CB  1 
ATOM   83   C CG  . LYS   A 1 16  ? 36.092  -27.629 15.184 1.00 42.56 ? 708  LYS   A CG  1 
ATOM   84   C CD  . LYS   A 1 16  ? 36.540  -27.857 13.748 1.00 48.70 ? 708  LYS   A CD  1 
ATOM   85   C CE  . LYS   A 1 16  ? 37.663  -26.934 13.326 1.00 53.73 ? 708  LYS   A CE  1 
ATOM   86   N NZ  . LYS   A 1 16  ? 38.913  -27.165 14.105 1.00 56.46 ? 708  LYS   A NZ  1 
ATOM   87   N N   . GLU   A 1 17  ? 32.717  -30.838 15.440 1.00 35.59 ? 709  GLU   A N   1 
ATOM   88   C CA  . GLU   A 1 17  ? 32.047  -32.012 16.007 1.00 36.76 ? 709  GLU   A CA  1 
ATOM   89   C C   . GLU   A 1 17  ? 32.758  -32.627 17.204 1.00 37.49 ? 709  GLU   A C   1 
ATOM   90   O O   . GLU   A 1 17  ? 32.120  -33.323 17.988 1.00 37.92 ? 709  GLU   A O   1 
ATOM   91   C CB  . GLU   A 1 17  ? 31.781  -33.076 14.944 1.00 39.14 ? 709  GLU   A CB  1 
ATOM   92   C CG  . GLU   A 1 17  ? 30.412  -32.930 14.322 1.00 45.29 ? 709  GLU   A CG  1 
ATOM   93   C CD  . GLU   A 1 17  ? 29.821  -34.242 13.856 1.00 53.18 ? 709  GLU   A CD  1 
ATOM   94   O OE1 . GLU   A 1 17  ? 30.426  -34.878 12.962 1.00 54.33 ? 709  GLU   A OE1 1 
ATOM   95   O OE2 . GLU   A 1 17  ? 28.754  -34.634 14.387 1.00 55.78 ? 709  GLU   A OE2 1 
ATOM   96   N N   . THR   A 1 18  ? 34.051  -32.351 17.369 1.00 37.68 ? 710  THR   A N   1 
ATOM   97   C CA  . THR   A 1 18  ? 34.833  -32.866 18.493 1.00 38.76 ? 710  THR   A CA  1 
ATOM   98   C C   . THR   A 1 18  ? 34.631  -32.080 19.809 1.00 39.41 ? 710  THR   A C   1 
ATOM   99   O O   . THR   A 1 18  ? 34.830  -32.637 20.888 1.00 39.52 ? 710  THR   A O   1 
ATOM   100  C CB  . THR   A 1 18  ? 36.309  -32.959 18.105 1.00 40.13 ? 710  THR   A CB  1 
ATOM   101  O OG1 . THR   A 1 18  ? 36.715  -31.745 17.461 1.00 41.44 ? 710  THR   A OG1 1 
ATOM   102  C CG2 . THR   A 1 18  ? 36.579  -34.123 17.176 1.00 40.51 ? 710  THR   A CG2 1 
ATOM   103  N N   . GLU   A 1 19  ? 34.227  -30.802 19.728 1.00 39.50 ? 711  GLU   A N   1 
ATOM   104  C CA  . GLU   A 1 19  ? 34.037  -29.979 20.928 1.00 39.68 ? 711  GLU   A CA  1 
ATOM   105  C C   . GLU   A 1 19  ? 32.712  -30.232 21.654 1.00 39.43 ? 711  GLU   A C   1 
ATOM   106  O O   . GLU   A 1 19  ? 32.534  -29.695 22.744 1.00 39.39 ? 711  GLU   A O   1 
ATOM   107  C CB  . GLU   A 1 19  ? 34.092  -28.481 20.610 1.00 41.82 ? 711  GLU   A CB  1 
ATOM   108  C CG  . GLU   A 1 19  ? 35.017  -28.065 19.493 1.00 46.87 ? 711  GLU   A CG  1 
ATOM   109  C CD  . GLU   A 1 19  ? 35.053  -26.560 19.345 1.00 54.06 ? 711  GLU   A CD  1 
ATOM   110  O OE1 . GLU   A 1 19  ? 35.164  -26.086 18.190 1.00 56.09 ? 711  GLU   A OE1 1 
ATOM   111  O OE2 . GLU   A 1 19  ? 34.963  -25.853 20.378 1.00 55.54 ? 711  GLU   A OE2 1 
ATOM   112  N N   . PHE   A 1 20  ? 31.761  -30.966 21.047 1.00 38.86 ? 712  PHE   A N   1 
ATOM   113  C CA  . PHE   A 1 20  ? 30.469  -31.198 21.709 1.00 38.79 ? 712  PHE   A CA  1 
ATOM   114  C C   . PHE   A 1 20  ? 29.889  -32.583 21.433 1.00 38.54 ? 712  PHE   A C   1 
ATOM   115  O O   . PHE   A 1 20  ? 30.274  -33.235 20.463 1.00 38.37 ? 712  PHE   A O   1 
ATOM   116  C CB  . PHE   A 1 20  ? 29.457  -30.099 21.338 1.00 38.60 ? 712  PHE   A CB  1 
ATOM   117  C CG  . PHE   A 1 20  ? 29.088  -30.122 19.875 1.00 39.30 ? 712  PHE   A CG  1 
ATOM   118  C CD1 . PHE   A 1 20  ? 29.806  -29.384 18.952 1.00 40.13 ? 712  PHE   A CD1 1 
ATOM   119  C CD2 . PHE   A 1 20  ? 28.029  -30.888 19.423 1.00 40.30 ? 712  PHE   A CD2 1 
ATOM   120  C CE1 . PHE   A 1 20  ? 29.482  -29.424 17.605 1.00 41.05 ? 712  PHE   A CE1 1 
ATOM   121  C CE2 . PHE   A 1 20  ? 27.707  -30.931 18.075 1.00 41.09 ? 712  PHE   A CE2 1 
ATOM   122  C CZ  . PHE   A 1 20  ? 28.441  -30.205 17.174 1.00 41.03 ? 712  PHE   A CZ  1 
ATOM   123  N N   . LYS   A 1 21  ? 28.938  -33.015 22.274 1.00 38.28 ? 713  LYS   A N   1 
ATOM   124  C CA  . LYS   A 1 21  ? 28.274  -34.305 22.132 1.00 38.58 ? 713  LYS   A CA  1 
ATOM   125  C C   . LYS   A 1 21  ? 26.806  -34.235 22.611 1.00 38.16 ? 713  LYS   A C   1 
ATOM   126  O O   . LYS   A 1 21  ? 26.553  -33.785 23.731 1.00 38.27 ? 713  LYS   A O   1 
ATOM   127  C CB  . LYS   A 1 21  ? 29.020  -35.401 22.933 1.00 40.51 ? 713  LYS   A CB  1 
ATOM   128  C CG  . LYS   A 1 21  ? 30.380  -35.821 22.374 1.00 44.86 ? 713  LYS   A CG  1 
ATOM   129  C CD  . LYS   A 1 21  ? 30.268  -36.908 21.313 1.00 50.23 ? 713  LYS   A CD  1 
ATOM   130  C CE  . LYS   A 1 21  ? 30.909  -36.507 20.003 1.00 54.40 ? 713  LYS   A CE  1 
ATOM   131  N NZ  . LYS   A 1 21  ? 32.170  -35.751 20.219 1.00 56.73 ? 713  LYS   A NZ  1 
ATOM   132  N N   . LYS   A 1 22  ? 25.854  -34.715 21.792 1.00 37.28 ? 714  LYS   A N   1 
ATOM   133  C CA  . LYS   A 1 22  ? 24.444  -34.784 22.192 1.00 37.38 ? 714  LYS   A CA  1 
ATOM   134  C C   . LYS   A 1 22  ? 24.318  -35.935 23.201 1.00 37.40 ? 714  LYS   A C   1 
ATOM   135  O O   . LYS   A 1 22  ? 24.826  -37.024 22.921 1.00 37.47 ? 714  LYS   A O   1 
ATOM   136  C CB  . LYS   A 1 22  ? 23.550  -35.086 20.972 1.00 38.89 ? 714  LYS   A CB  1 
ATOM   137  C CG  . LYS   A 1 22  ? 23.778  -34.146 19.793 1.00 42.84 ? 714  LYS   A CG  1 
ATOM   138  C CD  . LYS   A 1 22  ? 23.079  -34.614 18.516 1.00 46.76 ? 714  LYS   A CD  1 
ATOM   139  C CE  . LYS   A 1 22  ? 23.865  -35.649 17.744 1.00 50.80 ? 714  LYS   A CE  1 
ATOM   140  N NZ  . LYS   A 1 22  ? 25.073  -35.075 17.083 1.00 52.83 ? 714  LYS   A NZ  1 
ATOM   141  N N   . ILE   A 1 23  ? 23.685  -35.712 24.367 1.00 37.27 ? 715  ILE   A N   1 
ATOM   142  C CA  . ILE   A 1 23  ? 23.563  -36.779 25.364 1.00 38.21 ? 715  ILE   A CA  1 
ATOM   143  C C   . ILE   A 1 23  ? 22.122  -37.264 25.579 1.00 39.45 ? 715  ILE   A C   1 
ATOM   144  O O   . ILE   A 1 23  ? 21.889  -38.473 25.589 1.00 40.11 ? 715  ILE   A O   1 
ATOM   145  C CB  . ILE   A 1 23  ? 24.240  -36.441 26.716 1.00 38.59 ? 715  ILE   A CB  1 
ATOM   146  C CG1 . ILE   A 1 23  ? 23.647  -35.188 27.379 1.00 39.53 ? 715  ILE   A CG1 1 
ATOM   147  C CG2 . ILE   A 1 23  ? 25.747  -36.327 26.551 1.00 39.22 ? 715  ILE   A CG2 1 
ATOM   148  C CD1 . ILE   A 1 23  ? 24.003  -35.008 28.902 1.00 40.95 ? 715  ILE   A CD1 1 
ATOM   149  N N   . LYS   A 1 24  ? 21.167  -36.350 25.776 1.00 39.35 ? 716  LYS   A N   1 
ATOM   150  C CA  . LYS   A 1 24  ? 19.784  -36.731 26.048 1.00 39.65 ? 716  LYS   A CA  1 
ATOM   151  C C   . LYS   A 1 24  ? 18.828  -36.167 24.989 1.00 39.98 ? 716  LYS   A C   1 
ATOM   152  O O   . LYS   A 1 24  ? 19.185  -35.239 24.258 1.00 40.40 ? 716  LYS   A O   1 
ATOM   153  C CB  . LYS   A 1 24  ? 19.389  -36.233 27.457 1.00 41.03 ? 716  LYS   A CB  1 
ATOM   154  C CG  . LYS   A 1 24  ? 18.263  -37.018 28.111 1.00 44.72 ? 716  LYS   A CG  1 
ATOM   155  C CD  . LYS   A 1 24  ? 17.972  -36.526 29.515 1.00 49.51 ? 716  LYS   A CD  1 
ATOM   156  C CE  . LYS   A 1 24  ? 16.822  -37.270 30.159 1.00 53.87 ? 716  LYS   A CE  1 
ATOM   157  N NZ  . LYS   A 1 24  ? 16.777  -37.056 31.634 1.00 56.66 ? 716  LYS   A NZ  1 
ATOM   158  N N   . VAL   A 1 25  ? 17.618  -36.744 24.894 1.00 39.40 ? 717  VAL   A N   1 
ATOM   159  C CA  . VAL   A 1 25  ? 16.569  -36.267 23.995 1.00 39.18 ? 717  VAL   A CA  1 
ATOM   160  C C   . VAL   A 1 25  ? 15.571  -35.409 24.809 1.00 38.46 ? 717  VAL   A C   1 
ATOM   161  O O   . VAL   A 1 25  ? 15.062  -35.854 25.841 1.00 38.53 ? 717  VAL   A O   1 
ATOM   162  C CB  . VAL   A 1 25  ? 15.900  -37.434 23.224 1.00 39.95 ? 717  VAL   A CB  1 
ATOM   163  C CG1 . VAL   A 1 25  ? 14.505  -37.060 22.725 1.00 40.71 ? 717  VAL   A CG1 1 
ATOM   164  C CG2 . VAL   A 1 25  ? 16.780  -37.886 22.061 1.00 40.28 ? 717  VAL   A CG2 1 
ATOM   165  N N   . LEU   A 1 26  ? 15.336  -34.171 24.373 1.00 37.76 ? 718  LEU   A N   1 
ATOM   166  C CA  . LEU   A 1 26  ? 14.416  -33.285 25.085 1.00 37.74 ? 718  LEU   A CA  1 
ATOM   167  C C   . LEU   A 1 26  ? 13.019  -33.233 24.424 1.00 38.20 ? 718  LEU   A C   1 
ATOM   168  O O   . LEU   A 1 26  ? 11.999  -33.160 25.109 1.00 38.57 ? 718  LEU   A O   1 
ATOM   169  C CB  . LEU   A 1 26  ? 15.019  -31.883 25.228 1.00 37.23 ? 718  LEU   A CB  1 
ATOM   170  C CG  . LEU   A 1 26  ? 16.431  -31.795 25.822 1.00 38.09 ? 718  LEU   A CG  1 
ATOM   171  C CD1 . LEU   A 1 26  ? 16.844  -30.334 26.003 1.00 38.61 ? 718  LEU   A CD1 1 
ATOM   172  C CD2 . LEU   A 1 26  ? 16.538  -32.544 27.158 1.00 38.27 ? 718  LEU   A CD2 1 
ATOM   173  N N   . GLY   A 1 27  ? 13.005  -33.293 23.103 1.00 37.74 ? 719  GLY   A N   1 
ATOM   174  C CA  . GLY   A 1 27  ? 11.800  -33.247 22.292 1.00 38.00 ? 719  GLY   A CA  1 
ATOM   175  C C   . GLY   A 1 27  ? 12.133  -33.071 20.823 1.00 38.52 ? 719  GLY   A C   1 
ATOM   176  O O   . GLY   A 1 27  ? 13.298  -33.164 20.435 1.00 38.33 ? 719  GLY   A O   1 
ATOM   177  N N   . SER   A 1 28  ? 11.121  -32.834 19.982 1.00 39.01 ? 720  SER   A N   1 
ATOM   178  C CA  . SER   A 1 28  ? 11.348  -32.588 18.558 1.00 40.14 ? 720  SER   A CA  1 
ATOM   179  C C   . SER   A 1 28  ? 10.129  -31.952 17.920 1.00 40.98 ? 720  SER   A C   1 
ATOM   180  O O   . SER   A 1 28  ? 8.999   -32.237 18.317 1.00 41.55 ? 720  SER   A O   1 
ATOM   181  C CB  . SER   A 1 28  ? 11.773  -33.851 17.811 1.00 41.98 ? 720  SER   A CB  1 
ATOM   182  O OG  . SER   A 1 28  ? 10.690  -34.719 17.526 1.00 45.31 ? 720  SER   A OG  1 
ATOM   183  N N   . GLY   A 1 29  ? 10.368  -31.081 16.953 1.00 40.81 ? 721  GLY   A N   1 
ATOM   184  C CA  . GLY   A 1 29  ? 9.302   -30.380 16.255 1.00 41.05 ? 721  GLY   A CA  1 
ATOM   185  C C   . GLY   A 1 29  ? 9.387   -30.551 14.757 1.00 41.03 ? 721  GLY   A C   1 
ATOM   186  O O   . GLY   A 1 29  ? 9.958   -31.527 14.280 1.00 41.17 ? 721  GLY   A O   1 
ATOM   187  N N   . ALA   A 1 30  ? 8.833   -29.603 14.006 1.00 40.67 ? 722  ALA   A N   1 
ATOM   188  C CA  . ALA   A 1 30  ? 8.811   -29.653 12.547 1.00 40.51 ? 722  ALA   A CA  1 
ATOM   189  C C   . ALA   A 1 30  ? 10.151  -29.369 11.892 1.00 40.06 ? 722  ALA   A C   1 
ATOM   190  O O   . ALA   A 1 30  ? 10.369  -29.787 10.756 1.00 40.47 ? 722  ALA   A O   1 
ATOM   191  C CB  . ALA   A 1 30  ? 7.769   -28.681 12.015 1.00 40.75 ? 722  ALA   A CB  1 
ATOM   192  N N   . PHE   A 1 31  ? 11.033  -28.640 12.573 1.00 39.33 ? 723  PHE   A N   1 
ATOM   193  C CA  . PHE   A 1 31  ? 12.326  -28.289 11.997 1.00 39.39 ? 723  PHE   A CA  1 
ATOM   194  C C   . PHE   A 1 31  ? 13.439  -29.237 12.394 1.00 38.98 ? 723  PHE   A C   1 
ATOM   195  O O   . PHE   A 1 31  ? 14.380  -29.424 11.625 1.00 39.30 ? 723  PHE   A O   1 
ATOM   196  C CB  . PHE   A 1 31  ? 12.703  -26.835 12.318 1.00 39.59 ? 723  PHE   A CB  1 
ATOM   197  C CG  . PHE   A 1 31  ? 11.748  -25.838 11.714 1.00 40.75 ? 723  PHE   A CG  1 
ATOM   198  C CD1 . PHE   A 1 31  ? 11.760  -25.578 10.355 1.00 41.63 ? 723  PHE   A CD1 1 
ATOM   199  C CD2 . PHE   A 1 31  ? 10.809  -25.189 12.499 1.00 41.90 ? 723  PHE   A CD2 1 
ATOM   200  C CE1 . PHE   A 1 31  ? 10.854  -24.686 9.794  1.00 42.44 ? 723  PHE   A CE1 1 
ATOM   201  C CE2 . PHE   A 1 31  ? 9.904   -24.300 11.934 1.00 42.54 ? 723  PHE   A CE2 1 
ATOM   202  C CZ  . PHE   A 1 31  ? 9.939   -24.047 10.587 1.00 42.25 ? 723  PHE   A CZ  1 
ATOM   203  N N   . GLY   A 1 32  ? 13.351  -29.803 13.590 1.00 38.11 ? 724  GLY   A N   1 
ATOM   204  C CA  . GLY   A 1 32  ? 14.379  -30.706 14.070 1.00 37.95 ? 724  GLY   A CA  1 
ATOM   205  C C   . GLY   A 1 32  ? 14.191  -31.220 15.481 1.00 37.53 ? 724  GLY   A C   1 
ATOM   206  O O   . GLY   A 1 32  ? 13.170  -30.971 16.129 1.00 37.82 ? 724  GLY   A O   1 
ATOM   207  N N   . THR   A 1 33  ? 15.204  -31.924 15.967 1.00 36.41 ? 725  THR   A N   1 
ATOM   208  C CA  . THR   A 1 33  ? 15.177  -32.566 17.264 1.00 36.13 ? 725  THR   A CA  1 
ATOM   209  C C   . THR   A 1 33  ? 16.030  -31.802 18.261 1.00 35.00 ? 725  THR   A C   1 
ATOM   210  O O   . THR   A 1 33  ? 17.159  -31.421 17.951 1.00 35.06 ? 725  THR   A O   1 
ATOM   211  C CB  . THR   A 1 33  ? 15.609  -34.051 17.083 1.00 38.02 ? 725  THR   A CB  1 
ATOM   212  O OG1 . THR   A 1 33  ? 14.722  -34.675 16.144 1.00 39.83 ? 725  THR   A OG1 1 
ATOM   213  C CG2 . THR   A 1 33  ? 15.616  -34.838 18.385 1.00 38.09 ? 725  THR   A CG2 1 
ATOM   214  N N   . VAL   A 1 34  ? 15.491  -31.589 19.468 1.00 33.76 ? 726  VAL   A N   1 
ATOM   215  C CA  . VAL   A 1 34  ? 16.197  -30.881 20.519 1.00 32.98 ? 726  VAL   A CA  1 
ATOM   216  C C   . VAL   A 1 34  ? 16.868  -31.867 21.440 1.00 32.97 ? 726  VAL   A C   1 
ATOM   217  O O   . VAL   A 1 34  ? 16.222  -32.769 21.957 1.00 32.92 ? 726  VAL   A O   1 
ATOM   218  C CB  . VAL   A 1 34  ? 15.291  -29.902 21.300 1.00 32.87 ? 726  VAL   A CB  1 
ATOM   219  C CG1 . VAL   A 1 34  ? 16.134  -28.974 22.180 1.00 32.95 ? 726  VAL   A CG1 1 
ATOM   220  C CG2 . VAL   A 1 34  ? 14.407  -29.090 20.357 1.00 32.68 ? 726  VAL   A CG2 1 
ATOM   221  N N   . TYR   A 1 35  ? 18.176  -31.696 21.645 1.00 33.20 ? 727  TYR   A N   1 
ATOM   222  C CA  . TYR   A 1 35  ? 18.990  -32.556 22.502 1.00 33.78 ? 727  TYR   A CA  1 
ATOM   223  C C   . TYR   A 1 35  ? 19.666  -31.754 23.598 1.00 32.98 ? 727  TYR   A C   1 
ATOM   224  O O   . TYR   A 1 35  ? 20.089  -30.622 23.365 1.00 33.17 ? 727  TYR   A O   1 
ATOM   225  C CB  . TYR   A 1 35  ? 20.146  -33.181 21.706 1.00 34.56 ? 727  TYR   A CB  1 
ATOM   226  C CG  . TYR   A 1 35  ? 19.780  -33.963 20.468 1.00 36.48 ? 727  TYR   A CG  1 
ATOM   227  C CD1 . TYR   A 1 35  ? 19.739  -33.349 19.224 1.00 37.63 ? 727  TYR   A CD1 1 
ATOM   228  C CD2 . TYR   A 1 35  ? 19.619  -35.342 20.517 1.00 38.02 ? 727  TYR   A CD2 1 
ATOM   229  C CE1 . TYR   A 1 35  ? 19.457  -34.073 18.073 1.00 39.15 ? 727  TYR   A CE1 1 
ATOM   230  C CE2 . TYR   A 1 35  ? 19.326  -36.075 19.376 1.00 39.24 ? 727  TYR   A CE2 1 
ATOM   231  C CZ  . TYR   A 1 35  ? 19.246  -35.438 18.153 1.00 40.54 ? 727  TYR   A CZ  1 
ATOM   232  O OH  . TYR   A 1 35  ? 18.996  -36.165 17.011 1.00 42.84 ? 727  TYR   A OH  1 
ATOM   233  N N   . LYS   A 1 36  ? 19.844  -32.368 24.763 1.00 31.99 ? 728  LYS   A N   1 
ATOM   234  C CA  . LYS   A 1 36  ? 20.654  -31.764 25.813 1.00 31.74 ? 728  LYS   A CA  1 
ATOM   235  C C   . LYS   A 1 36  ? 22.070  -32.138 25.395 1.00 31.72 ? 728  LYS   A C   1 
ATOM   236  O O   . LYS   A 1 36  ? 22.328  -33.283 25.051 1.00 31.98 ? 728  LYS   A O   1 
ATOM   237  C CB  . LYS   A 1 36  ? 20.318  -32.331 27.200 1.00 32.76 ? 728  LYS   A CB  1 
ATOM   238  C CG  . LYS   A 1 36  ? 21.341  -31.960 28.259 1.00 36.46 ? 728  LYS   A CG  1 
ATOM   239  C CD  . LYS   A 1 36  ? 20.886  -32.305 29.668 1.00 40.97 ? 728  LYS   A CD  1 
ATOM   240  C CE  . LYS   A 1 36  ? 22.025  -32.162 30.655 1.00 45.05 ? 728  LYS   A CE  1 
ATOM   241  N NZ  . LYS   A 1 36  ? 21.537  -32.001 32.054 1.00 47.53 ? 728  LYS   A NZ  1 
ATOM   242  N N   . GLY   A 1 37  ? 22.953  -31.162 25.334 1.00 31.49 ? 729  GLY   A N   1 
ATOM   243  C CA  . GLY   A 1 37  ? 24.322  -31.381 24.900 1.00 31.47 ? 729  GLY   A CA  1 
ATOM   244  C C   . GLY   A 1 37  ? 25.342  -31.096 25.977 1.00 31.22 ? 729  GLY   A C   1 
ATOM   245  O O   . GLY   A 1 37  ? 25.000  -30.690 27.090 1.00 31.11 ? 729  GLY   A O   1 
ATOM   246  N N   . LEU   A 1 38  ? 26.606  -31.337 25.650 1.00 30.93 ? 730  LEU   A N   1 
ATOM   247  C CA  . LEU   A 1 38  ? 27.725  -31.082 26.542 1.00 30.77 ? 730  LEU   A CA  1 
ATOM   248  C C   . LEU   A 1 38  ? 28.878  -30.600 25.688 1.00 30.53 ? 730  LEU   A C   1 
ATOM   249  O O   . LEU   A 1 38  ? 29.297  -31.273 24.744 1.00 31.04 ? 730  LEU   A O   1 
ATOM   250  C CB  . LEU   A 1 38  ? 28.139  -32.317 27.334 1.00 31.08 ? 730  LEU   A CB  1 
ATOM   251  C CG  . LEU   A 1 38  ? 27.302  -32.664 28.557 1.00 32.91 ? 730  LEU   A CG  1 
ATOM   252  C CD1 . LEU   A 1 38  ? 27.882  -33.875 29.259 1.00 33.54 ? 730  LEU   A CD1 1 
ATOM   253  C CD2 . LEU   A 1 38  ? 27.255  -31.516 29.538 1.00 33.34 ? 730  LEU   A CD2 1 
ATOM   254  N N   . TRP   A 1 39  ? 29.328  -29.393 25.978 1.00 29.07 ? 731  TRP   A N   1 
ATOM   255  C CA  . TRP   A 1 39  ? 30.418  -28.759 25.296 1.00 28.19 ? 731  TRP   A CA  1 
ATOM   256  C C   . TRP   A 1 39  ? 31.658  -28.968 26.147 1.00 27.46 ? 731  TRP   A C   1 
ATOM   257  O O   . TRP   A 1 39  ? 31.632  -28.724 27.352 1.00 26.45 ? 731  TRP   A O   1 
ATOM   258  C CB  . TRP   A 1 39  ? 30.116  -27.260 25.178 1.00 27.86 ? 731  TRP   A CB  1 
ATOM   259  C CG  . TRP   A 1 39  ? 31.260  -26.434 24.692 1.00 27.80 ? 731  TRP   A CG  1 
ATOM   260  C CD1 . TRP   A 1 39  ? 31.970  -26.611 23.540 1.00 28.58 ? 731  TRP   A CD1 1 
ATOM   261  C CD2 . TRP   A 1 39  ? 31.768  -25.246 25.299 1.00 27.62 ? 731  TRP   A CD2 1 
ATOM   262  N NE1 . TRP   A 1 39  ? 32.882  -25.598 23.388 1.00 28.77 ? 731  TRP   A NE1 1 
ATOM   263  C CE2 . TRP   A 1 39  ? 32.802  -24.760 24.471 1.00 28.30 ? 731  TRP   A CE2 1 
ATOM   264  C CE3 . TRP   A 1 39  ? 31.472  -24.560 26.479 1.00 28.09 ? 731  TRP   A CE3 1 
ATOM   265  C CZ2 . TRP   A 1 39  ? 33.512  -23.599 24.769 1.00 28.54 ? 731  TRP   A CZ2 1 
ATOM   266  C CZ3 . TRP   A 1 39  ? 32.176  -23.408 26.772 1.00 28.75 ? 731  TRP   A CZ3 1 
ATOM   267  C CH2 . TRP   A 1 39  ? 33.195  -22.950 25.931 1.00 28.82 ? 731  TRP   A CH2 1 
ATOM   268  N N   . ILE   A 1 40  ? 32.732  -29.445 25.524 1.00 27.72 ? 732  ILE   A N   1 
ATOM   269  C CA  . ILE   A 1 40  ? 34.025  -29.647 26.171 1.00 28.11 ? 732  ILE   A CA  1 
ATOM   270  C C   . ILE   A 1 40  ? 34.926  -28.625 25.503 1.00 28.17 ? 732  ILE   A C   1 
ATOM   271  O O   . ILE   A 1 40  ? 35.279  -28.805 24.339 1.00 28.45 ? 732  ILE   A O   1 
ATOM   272  C CB  . ILE   A 1 40  ? 34.587  -31.084 25.983 1.00 29.37 ? 732  ILE   A CB  1 
ATOM   273  C CG1 . ILE   A 1 40  ? 33.596  -32.197 26.453 1.00 30.96 ? 732  ILE   A CG1 1 
ATOM   274  C CG2 . ILE   A 1 40  ? 35.927  -31.208 26.722 1.00 29.95 ? 732  ILE   A CG2 1 
ATOM   275  C CD1 . ILE   A 1 40  ? 32.416  -32.659 25.402 1.00 32.67 ? 732  ILE   A CD1 1 
ATOM   276  N N   . PRO   A 1 41  ? 35.214  -27.486 26.163 1.00 27.89 ? 733  PRO   A N   1 
ATOM   277  C CA  . PRO   A 1 41  ? 36.044  -26.457 25.509 1.00 28.20 ? 733  PRO   A CA  1 
ATOM   278  C C   . PRO   A 1 41  ? 37.494  -26.906 25.303 1.00 29.69 ? 733  PRO   A C   1 
ATOM   279  O O   . PRO   A 1 41  ? 38.043  -27.598 26.159 1.00 29.06 ? 733  PRO   A O   1 
ATOM   280  C CB  . PRO   A 1 41  ? 35.956  -25.264 26.452 1.00 28.33 ? 733  PRO   A CB  1 
ATOM   281  C CG  . PRO   A 1 41  ? 35.526  -25.812 27.749 1.00 28.56 ? 733  PRO   A CG  1 
ATOM   282  C CD  . PRO   A 1 41  ? 34.836  -27.113 27.538 1.00 26.96 ? 733  PRO   A CD  1 
ATOM   283  N N   . GLU   A 1 42  ? 38.087  -26.533 24.142 1.00 30.85 ? 734  GLU   A N   1 
ATOM   284  C CA  . GLU   A 1 42  ? 39.444  -26.881 23.722 1.00 32.24 ? 734  GLU   A CA  1 
ATOM   285  C C   . GLU   A 1 42  ? 40.483  -26.745 24.842 1.00 32.64 ? 734  GLU   A C   1 
ATOM   286  O O   . GLU   A 1 42  ? 40.563  -25.705 25.499 1.00 33.25 ? 734  GLU   A O   1 
ATOM   287  C CB  . GLU   A 1 42  ? 39.870  -26.060 22.486 1.00 35.21 ? 734  GLU   A CB  1 
ATOM   288  C CG  . GLU   A 1 42  ? 39.398  -26.625 21.152 1.00 42.26 ? 734  GLU   A CG  1 
ATOM   289  C CD  . GLU   A 1 42  ? 39.722  -25.739 19.957 1.00 51.06 ? 734  GLU   A CD  1 
ATOM   290  O OE1 . GLU   A 1 42  ? 38.807  -25.465 19.146 1.00 51.12 ? 734  GLU   A OE1 1 
ATOM   291  O OE2 . GLU   A 1 42  ? 40.892  -25.304 19.841 1.00 54.75 ? 734  GLU   A OE2 1 
ATOM   292  N N   . GLY   A 1 43  ? 41.238  -27.814 25.063 1.00 31.88 ? 735  GLY   A N   1 
ATOM   293  C CA  . GLY   A 1 43  ? 42.276  -27.838 26.081 1.00 31.64 ? 735  GLY   A CA  1 
ATOM   294  C C   . GLY   A 1 43  ? 41.750  -27.865 27.501 1.00 31.27 ? 735  GLY   A C   1 
ATOM   295  O O   . GLY   A 1 43  ? 42.512  -27.595 28.435 1.00 31.89 ? 735  GLY   A O   1 
ATOM   296  N N   . GLU   A 1 44  ? 40.441  -28.181 27.686 1.00 29.58 ? 736  GLU   A N   1 
ATOM   297  C CA  . GLU   A 1 44  ? 39.825  -28.237 29.016 1.00 28.42 ? 736  GLU   A CA  1 
ATOM   298  C C   . GLU   A 1 44  ? 39.202  -29.605 29.298 1.00 29.05 ? 736  GLU   A C   1 
ATOM   299  O O   . GLU   A 1 44  ? 38.923  -30.370 28.381 1.00 29.07 ? 736  GLU   A O   1 
ATOM   300  C CB  . GLU   A 1 44  ? 38.783  -27.106 29.216 1.00 27.19 ? 736  GLU   A CB  1 
ATOM   301  C CG  . GLU   A 1 44  ? 39.286  -25.700 28.927 1.00 27.59 ? 736  GLU   A CG  1 
ATOM   302  C CD  . GLU   A 1 44  ? 40.119  -25.047 30.019 1.00 31.20 ? 736  GLU   A CD  1 
ATOM   303  O OE1 . GLU   A 1 44  ? 40.605  -25.770 30.916 1.00 30.48 ? 736  GLU   A OE1 1 
ATOM   304  O OE2 . GLU   A 1 44  ? 40.295  -23.809 29.973 1.00 33.70 ? 736  GLU   A OE2 1 
ATOM   305  N N   . LYS   A 1 45  ? 39.004  -29.917 30.576 1.00 29.69 ? 737  LYS   A N   1 
ATOM   306  C CA  . LYS   A 1 45  ? 38.409  -31.182 31.038 1.00 30.48 ? 737  LYS   A CA  1 
ATOM   307  C C   . LYS   A 1 45  ? 36.887  -31.054 31.360 1.00 29.43 ? 737  LYS   A C   1 
ATOM   308  O O   . LYS   A 1 45  ? 36.167  -32.050 31.468 1.00 29.36 ? 737  LYS   A O   1 
ATOM   309  C CB  . LYS   A 1 45  ? 39.187  -31.661 32.286 1.00 33.87 ? 737  LYS   A CB  1 
ATOM   310  C CG  . LYS   A 1 45  ? 38.619  -32.916 32.966 1.00 40.59 ? 737  LYS   A CG  1 
ATOM   311  C CD  . LYS   A 1 45  ? 39.217  -33.170 34.371 1.00 46.41 ? 737  LYS   A CD  1 
ATOM   312  C CE  . LYS   A 1 45  ? 38.998  -32.026 35.333 1.00 50.18 ? 737  LYS   A CE  1 
ATOM   313  N NZ  . LYS   A 1 45  ? 40.237  -31.736 36.099 1.00 52.66 ? 737  LYS   A NZ  1 
ATOM   314  N N   . VAL   A 1 46  ? 36.408  -29.820 31.473 1.00 28.37 ? 738  VAL   A N   1 
ATOM   315  C CA  . VAL   A 1 46  ? 35.056  -29.471 31.865 1.00 27.42 ? 738  VAL   A CA  1 
ATOM   316  C C   . VAL   A 1 46  ? 33.976  -29.828 30.792 1.00 26.38 ? 738  VAL   A C   1 
ATOM   317  O O   . VAL   A 1 46  ? 34.227  -29.839 29.581 1.00 25.89 ? 738  VAL   A O   1 
ATOM   318  C CB  . VAL   A 1 46  ? 35.065  -27.970 32.284 1.00 27.33 ? 738  VAL   A CB  1 
ATOM   319  C CG1 . VAL   A 1 46  ? 34.876  -27.038 31.104 1.00 27.66 ? 738  VAL   A CG1 1 
ATOM   320  C CG2 . VAL   A 1 46  ? 34.062  -27.689 33.371 1.00 27.56 ? 738  VAL   A CG2 1 
ATOM   321  N N   . LYS   A 1 47  ? 32.791  -30.195 31.276 1.00 25.92 ? 739  LYS   A N   1 
ATOM   322  C CA  . LYS   A 1 47  ? 31.651  -30.531 30.427 1.00 26.30 ? 739  LYS   A CA  1 
ATOM   323  C C   . LYS   A 1 47  ? 30.568  -29.522 30.752 1.00 25.69 ? 739  LYS   A C   1 
ATOM   324  O O   . LYS   A 1 47  ? 30.193  -29.372 31.915 1.00 26.22 ? 739  LYS   A O   1 
ATOM   325  C CB  . LYS   A 1 47  ? 31.194  -31.977 30.661 1.00 28.32 ? 739  LYS   A CB  1 
ATOM   326  C CG  . LYS   A 1 47  ? 32.220  -32.973 30.154 1.00 33.52 ? 739  LYS   A CG  1 
ATOM   327  C CD  . LYS   A 1 47  ? 32.105  -34.300 30.863 1.00 39.60 ? 739  LYS   A CD  1 
ATOM   328  C CE  . LYS   A 1 47  ? 33.194  -35.256 30.430 1.00 44.56 ? 739  LYS   A CE  1 
ATOM   329  N NZ  . LYS   A 1 47  ? 32.943  -36.641 30.914 1.00 47.41 ? 739  LYS   A NZ  1 
ATOM   330  N N   . ILE   A 1 48  ? 30.169  -28.743 29.755 1.00 24.58 ? 740  ILE   A N   1 
ATOM   331  C CA  . ILE   A 1 48  ? 29.235  -27.626 29.936 1.00 24.10 ? 740  ILE   A CA  1 
ATOM   332  C C   . ILE   A 1 48  ? 27.929  -27.881 29.242 1.00 23.71 ? 740  ILE   A C   1 
ATOM   333  O O   . ILE   A 1 48  ? 27.891  -27.922 28.017 1.00 23.53 ? 740  ILE   A O   1 
ATOM   334  C CB  . ILE   A 1 48  ? 29.871  -26.285 29.433 1.00 23.79 ? 740  ILE   A CB  1 
ATOM   335  C CG1 . ILE   A 1 48  ? 31.271  -26.046 30.025 1.00 24.19 ? 740  ILE   A CG1 1 
ATOM   336  C CG2 . ILE   A 1 48  ? 28.956  -25.094 29.661 1.00 23.71 ? 740  ILE   A CG2 1 
ATOM   337  C CD1 . ILE   A 1 48  ? 31.305  -26.011 31.475 1.00 25.65 ? 740  ILE   A CD1 1 
ATOM   338  N N   . PRO   A 1 49  ? 26.838  -28.019 30.009 1.00 23.83 ? 741  PRO   A N   1 
ATOM   339  C CA  . PRO   A 1 49  ? 25.525  -28.240 29.386 1.00 24.34 ? 741  PRO   A CA  1 
ATOM   340  C C   . PRO   A 1 49  ? 25.133  -27.150 28.395 1.00 25.21 ? 741  PRO   A C   1 
ATOM   341  O O   . PRO   A 1 49  ? 25.365  -25.962 28.642 1.00 25.63 ? 741  PRO   A O   1 
ATOM   342  C CB  . PRO   A 1 49  ? 24.567  -28.261 30.583 1.00 24.92 ? 741  PRO   A CB  1 
ATOM   343  C CG  . PRO   A 1 49  ? 25.434  -28.644 31.762 1.00 24.91 ? 741  PRO   A CG  1 
ATOM   344  C CD  . PRO   A 1 49  ? 26.740  -27.971 31.483 1.00 23.37 ? 741  PRO   A CD  1 
ATOM   345  N N   . VAL   A 1 50  ? 24.591  -27.567 27.247 1.00 24.88 ? 742  VAL   A N   1 
ATOM   346  C CA  . VAL   A 1 50  ? 24.137  -26.686 26.169 1.00 25.08 ? 742  VAL   A CA  1 
ATOM   347  C C   . VAL   A 1 50  ? 22.851  -27.296 25.558 1.00 25.23 ? 742  VAL   A C   1 
ATOM   348  O O   . VAL   A 1 50  ? 22.591  -28.484 25.752 1.00 25.11 ? 742  VAL   A O   1 
ATOM   349  C CB  . VAL   A 1 50  ? 25.221  -26.512 25.058 1.00 25.49 ? 742  VAL   A CB  1 
ATOM   350  C CG1 . VAL   A 1 50  ? 26.413  -25.687 25.535 1.00 25.90 ? 742  VAL   A CG1 1 
ATOM   351  C CG2 . VAL   A 1 50  ? 25.678  -27.859 24.513 1.00 25.69 ? 742  VAL   A CG2 1 
ATOM   352  N N   . ALA   A 1 51  ? 22.080  -26.508 24.789 1.00 24.92 ? 743  ALA   A N   1 
ATOM   353  C CA  . ALA   A 1 51  ? 20.916  -27.060 24.094 1.00 25.68 ? 743  ALA   A CA  1 
ATOM   354  C C   . ALA   A 1 51  ? 21.258  -27.114 22.615 1.00 26.14 ? 743  ALA   A C   1 
ATOM   355  O O   . ALA   A 1 51  ? 21.729  -26.118 22.060 1.00 26.32 ? 743  ALA   A O   1 
ATOM   356  C CB  . ALA   A 1 51  ? 19.696  -26.197 24.316 1.00 25.84 ? 743  ALA   A CB  1 
ATOM   357  N N   . ILE   A 1 52  ? 21.076  -28.281 21.986 1.00 26.00 ? 744  ILE   A N   1 
ATOM   358  C CA  . ILE   A 1 52  ? 21.404  -28.426 20.569 1.00 26.90 ? 744  ILE   A CA  1 
ATOM   359  C C   . ILE   A 1 52  ? 20.170  -28.807 19.758 1.00 27.83 ? 744  ILE   A C   1 
ATOM   360  O O   . ILE   A 1 52  ? 19.472  -29.744 20.124 1.00 28.16 ? 744  ILE   A O   1 
ATOM   361  C CB  . ILE   A 1 52  ? 22.545  -29.475 20.344 1.00 27.17 ? 744  ILE   A CB  1 
ATOM   362  C CG1 . ILE   A 1 52  ? 23.782  -29.179 21.211 1.00 28.06 ? 744  ILE   A CG1 1 
ATOM   363  C CG2 . ILE   A 1 52  ? 22.916  -29.586 18.858 1.00 27.31 ? 744  ILE   A CG2 1 
ATOM   364  C CD1 . ILE   A 1 52  ? 24.842  -30.236 21.192 1.00 29.29 ? 744  ILE   A CD1 1 
ATOM   365  N N   . LYS   A 1 53  ? 19.918  -28.111 18.649 1.00 27.88 ? 745  LYS   A N   1 
ATOM   366  C CA  . LYS   A 1 53  ? 18.853  -28.483 17.737 1.00 28.64 ? 745  LYS   A CA  1 
ATOM   367  C C   . LYS   A 1 53  ? 19.508  -28.959 16.427 1.00 30.53 ? 745  LYS   A C   1 
ATOM   368  O O   . LYS   A 1 53  ? 20.166  -28.180 15.737 1.00 29.81 ? 745  LYS   A O   1 
ATOM   369  C CB  . LYS   A 1 53  ? 17.867  -27.325 17.471 1.00 29.21 ? 745  LYS   A CB  1 
ATOM   370  C CG  . LYS   A 1 53  ? 16.869  -27.643 16.342 1.00 31.00 ? 745  LYS   A CG  1 
ATOM   371  C CD  . LYS   A 1 53  ? 15.666  -26.733 16.302 1.00 33.57 ? 745  LYS   A CD  1 
ATOM   372  C CE  . LYS   A 1 53  ? 14.650  -27.077 17.357 1.00 36.51 ? 745  LYS   A CE  1 
ATOM   373  N NZ  . LYS   A 1 53  ? 13.782  -25.913 17.692 1.00 38.12 ? 745  LYS   A NZ  1 
ATOM   374  N N   . GLU   A 1 54  ? 19.329  -30.243 16.094 1.00 32.67 ? 746  GLU   A N   1 
ATOM   375  C CA  . GLU   A 1 54  ? 19.844  -30.778 14.840 1.00 34.99 ? 746  GLU   A CA  1 
ATOM   376  C C   . GLU   A 1 54  ? 18.691  -30.716 13.823 1.00 37.40 ? 746  GLU   A C   1 
ATOM   377  O O   . GLU   A 1 54  ? 17.606  -31.237 14.089 1.00 37.00 ? 746  GLU   A O   1 
ATOM   378  C CB  . GLU   A 1 54  ? 20.362  -32.209 15.017 1.00 36.32 ? 746  GLU   A CB  1 
ATOM   379  C CG  . GLU   A 1 54  ? 20.886  -32.802 13.723 1.00 39.28 ? 746  GLU   A CG  1 
ATOM   380  C CD  . GLU   A 1 54  ? 21.836  -33.958 13.955 1.00 44.56 ? 746  GLU   A CD  1 
ATOM   381  O OE1 . GLU   A 1 54  ? 21.438  -34.931 14.637 1.00 45.10 ? 746  GLU   A OE1 1 
ATOM   382  O OE2 . GLU   A 1 54  ? 22.992  -33.877 13.481 1.00 46.26 ? 746  GLU   A OE2 1 
ATOM   383  N N   . LEU   A 1 55  ? 18.910  -30.034 12.687 1.00 39.59 ? 747  LEU   A N   1 
ATOM   384  C CA  . LEU   A 1 55  ? 17.871  -29.837 11.680 1.00 41.97 ? 747  LEU   A CA  1 
ATOM   385  C C   . LEU   A 1 55  ? 17.569  -31.074 10.825 1.00 45.46 ? 747  LEU   A C   1 
ATOM   386  O O   . LEU   A 1 55  ? 18.414  -31.952 10.665 1.00 45.50 ? 747  LEU   A O   1 
ATOM   387  C CB  . LEU   A 1 55  ? 18.169  -28.623 10.792 1.00 41.59 ? 747  LEU   A CB  1 
ATOM   388  C CG  . LEU   A 1 55  ? 18.347  -27.270 11.485 1.00 42.55 ? 747  LEU   A CG  1 
ATOM   389  C CD1 . LEU   A 1 55  ? 18.408  -26.157 10.465 1.00 42.91 ? 747  LEU   A CD1 1 
ATOM   390  C CD2 . LEU   A 1 55  ? 17.235  -26.987 12.496 1.00 43.04 ? 747  LEU   A CD2 1 
ATOM   391  N N   . ARG   A 1 56  ? 16.349  -31.104 10.257 1.00 48.02 ? 748  ARG   A N   1 
ATOM   392  C CA  . ARG   A 1 56  ? 15.767  -32.178 9.458  1.00 50.86 ? 748  ARG   A CA  1 
ATOM   393  C C   . ARG   A 1 56  ? 16.379  -32.436 8.071  1.00 53.49 ? 748  ARG   A C   1 
ATOM   394  O O   . ARG   A 1 56  ? 16.564  -33.601 7.719  1.00 53.87 ? 748  ARG   A O   1 
ATOM   395  C CB  . ARG   A 1 56  ? 14.270  -31.916 9.298  1.00 52.60 ? 748  ARG   A CB  1 
ATOM   396  C CG  . ARG   A 1 56  ? 13.409  -33.112 9.617  1.00 56.05 ? 748  ARG   A CG  1 
ATOM   397  C CD  . ARG   A 1 56  ? 12.254  -32.702 10.493 1.00 59.20 ? 748  ARG   A CD  1 
ATOM   398  N NE  . ARG   A 1 56  ? 12.527  -33.024 11.891 1.00 62.12 ? 748  ARG   A NE  1 
ATOM   399  C CZ  . ARG   A 1 56  ? 11.607  -33.430 12.758 1.00 64.65 ? 748  ARG   A CZ  1 
ATOM   400  N NH1 . ARG   A 1 56  ? 11.944  -33.703 14.013 1.00 63.91 ? 748  ARG   A NH1 1 
ATOM   401  N NH2 . ARG   A 1 56  ? 10.336  -33.540 12.389 1.00 65.48 ? 748  ARG   A NH2 1 
ATOM   402  N N   . GLU   A 1 57  ? 16.622  -31.393 7.257  1.00 55.17 ? 749  GLU   A N   1 
ATOM   403  C CA  . GLU   A 1 57  ? 17.139  -31.605 5.895  1.00 57.26 ? 749  GLU   A CA  1 
ATOM   404  C C   . GLU   A 1 57  ? 18.647  -31.749 5.816  1.00 58.37 ? 749  GLU   A C   1 
ATOM   405  O O   . GLU   A 1 57  ? 19.232  -31.460 4.769  1.00 58.97 ? 749  GLU   A O   1 
ATOM   406  C CB  . GLU   A 1 57  ? 16.657  -30.503 4.932  1.00 60.90 ? 749  GLU   A CB  1 
ATOM   407  C CG  . GLU   A 1 57  ? 15.151  -30.479 4.734  1.00 68.39 ? 749  GLU   A CG  1 
ATOM   408  C CD  . GLU   A 1 57  ? 14.568  -31.807 4.286  1.00 78.04 ? 749  GLU   A CD  1 
ATOM   409  O OE1 . GLU   A 1 57  ? 14.962  -32.290 3.199  1.00 80.29 ? 749  GLU   A OE1 1 
ATOM   410  O OE2 . GLU   A 1 57  ? 13.730  -32.371 5.028  1.00 80.76 ? 749  GLU   A OE2 1 
ATOM   411  N N   . ALA   A 1 63  ? 25.264  -24.427 -0.189 1.00 52.80 ? 755  ALA   A N   1 
ATOM   412  C CA  . ALA   A 1 63  ? 24.351  -23.624 0.624  1.00 53.28 ? 755  ALA   A CA  1 
ATOM   413  C C   . ALA   A 1 63  ? 25.000  -23.102 1.919  1.00 53.82 ? 755  ALA   A C   1 
ATOM   414  O O   . ALA   A 1 63  ? 24.470  -22.161 2.506  1.00 54.10 ? 755  ALA   A O   1 
ATOM   415  C CB  . ALA   A 1 63  ? 23.088  -24.416 0.948  1.00 53.19 ? 755  ALA   A CB  1 
ATOM   416  N N   . ASN   A 1 64  ? 26.143  -23.694 2.349  1.00 53.49 ? 756  ASN   A N   1 
ATOM   417  C CA  . ASN   A 1 64  ? 26.880  -23.334 3.567  1.00 53.48 ? 756  ASN   A CA  1 
ATOM   418  C C   . ASN   A 1 64  ? 27.111  -21.853 3.752  1.00 52.79 ? 756  ASN   A C   1 
ATOM   419  O O   . ASN   A 1 64  ? 26.962  -21.351 4.864  1.00 53.26 ? 756  ASN   A O   1 
ATOM   420  C CB  . ASN   A 1 64  ? 28.208  -24.076 3.655  1.00 55.01 ? 756  ASN   A CB  1 
ATOM   421  C CG  . ASN   A 1 64  ? 28.092  -25.411 4.337  1.00 58.99 ? 756  ASN   A CG  1 
ATOM   422  O OD1 . ASN   A 1 64  ? 27.004  -25.993 4.441  1.00 60.38 ? 756  ASN   A OD1 1 
ATOM   423  N ND2 . ASN   A 1 64  ? 29.217  -25.926 4.822  1.00 59.86 ? 756  ASN   A ND2 1 
ATOM   424  N N   . LYS   A 1 65  ? 27.466  -21.143 2.677  1.00 51.51 ? 757  LYS   A N   1 
ATOM   425  C CA  . LYS   A 1 65  ? 27.687  -19.703 2.743  1.00 50.73 ? 757  LYS   A CA  1 
ATOM   426  C C   . LYS   A 1 65  ? 26.374  -18.999 3.135  1.00 49.69 ? 757  LYS   A C   1 
ATOM   427  O O   . LYS   A 1 65  ? 26.367  -18.169 4.038  1.00 49.66 ? 757  LYS   A O   1 
ATOM   428  C CB  . LYS   A 1 65  ? 28.252  -19.197 1.393  1.00 52.13 ? 757  LYS   A CB  1 
ATOM   429  C CG  . LYS   A 1 65  ? 27.888  -17.763 0.979  1.00 55.44 ? 757  LYS   A CG  1 
ATOM   430  C CD  . LYS   A 1 65  ? 28.721  -16.700 1.669  1.00 58.94 ? 757  LYS   A CD  1 
ATOM   431  C CE  . LYS   A 1 65  ? 28.377  -15.326 1.142  1.00 62.00 ? 757  LYS   A CE  1 
ATOM   432  N NZ  . LYS   A 1 65  ? 29.235  -14.270 1.740  1.00 63.87 ? 757  LYS   A NZ  1 
ATOM   433  N N   . GLU   A 1 66  ? 25.272  -19.389 2.500  1.00 48.57 ? 758  GLU   A N   1 
ATOM   434  C CA  . GLU   A 1 66  ? 23.963  -18.803 2.754  1.00 48.11 ? 758  GLU   A CA  1 
ATOM   435  C C   . GLU   A 1 66  ? 23.400  -19.147 4.150  1.00 46.55 ? 758  GLU   A C   1 
ATOM   436  O O   . GLU   A 1 66  ? 22.781  -18.289 4.770  1.00 46.58 ? 758  GLU   A O   1 
ATOM   437  C CB  . GLU   A 1 66  ? 22.991  -19.173 1.621  1.00 50.78 ? 758  GLU   A CB  1 
ATOM   438  C CG  . GLU   A 1 66  ? 23.482  -18.668 0.270  1.00 56.65 ? 758  GLU   A CG  1 
ATOM   439  C CD  . GLU   A 1 66  ? 23.122  -19.500 -0.950 1.00 63.72 ? 758  GLU   A CD  1 
ATOM   440  O OE1 . GLU   A 1 66  ? 22.470  -18.947 -1.866 1.00 65.69 ? 758  GLU   A OE1 1 
ATOM   441  O OE2 . GLU   A 1 66  ? 23.500  -20.695 -0.999 1.00 64.95 ? 758  GLU   A OE2 1 
ATOM   442  N N   . ILE   A 1 67  ? 23.658  -20.361 4.658  1.00 45.13 ? 759  ILE   A N   1 
ATOM   443  C CA  . ILE   A 1 67  ? 23.209  -20.787 5.986  1.00 44.57 ? 759  ILE   A CA  1 
ATOM   444  C C   . ILE   A 1 67  ? 23.889  -19.936 7.068  1.00 43.30 ? 759  ILE   A C   1 
ATOM   445  O O   . ILE   A 1 67  ? 23.236  -19.464 8.003  1.00 43.52 ? 759  ILE   A O   1 
ATOM   446  C CB  . ILE   A 1 67  ? 23.520  -22.293 6.199  1.00 45.30 ? 759  ILE   A CB  1 
ATOM   447  C CG1 . ILE   A 1 67  ? 22.789  -23.166 5.168  1.00 46.19 ? 759  ILE   A CG1 1 
ATOM   448  C CG2 . ILE   A 1 67  ? 23.195  -22.724 7.639  1.00 45.76 ? 759  ILE   A CG2 1 
ATOM   449  C CD1 . ILE   A 1 67  ? 23.444  -24.480 4.927  1.00 47.56 ? 759  ILE   A CD1 1 
ATOM   450  N N   . LEU   A 1 68  ? 25.195  -19.723 6.908  1.00 41.46 ? 760  LEU   A N   1 
ATOM   451  C CA  . LEU   A 1 68  ? 26.003  -18.940 7.817  1.00 40.33 ? 760  LEU   A CA  1 
ATOM   452  C C   . LEU   A 1 68  ? 25.533  -17.491 7.804  1.00 38.98 ? 760  LEU   A C   1 
ATOM   453  O O   . LEU   A 1 68  ? 25.342  -16.916 8.865  1.00 39.09 ? 760  LEU   A O   1 
ATOM   454  C CB  . LEU   A 1 68  ? 27.468  -19.045 7.379  1.00 40.66 ? 760  LEU   A CB  1 
ATOM   455  C CG  . LEU   A 1 68  ? 28.510  -19.332 8.451  1.00 42.00 ? 760  LEU   A CG  1 
ATOM   456  C CD1 . LEU   A 1 68  ? 28.172  -20.581 9.248  1.00 42.18 ? 760  LEU   A CD1 1 
ATOM   457  C CD2 . LEU   A 1 68  ? 29.879  -19.477 7.823  1.00 42.66 ? 760  LEU   A CD2 1 
ATOM   458  N N   . ASP   A 1 69  ? 25.242  -16.926 6.626  1.00 37.73 ? 761  ASP   A N   1 
ATOM   459  C CA  . ASP   A 1 69  ? 24.741  -15.552 6.506  1.00 37.18 ? 761  ASP   A CA  1 
ATOM   460  C C   . ASP   A 1 69  ? 23.489  -15.328 7.370  1.00 35.70 ? 761  ASP   A C   1 
ATOM   461  O O   . ASP   A 1 69  ? 23.382  -14.305 8.043  1.00 35.84 ? 761  ASP   A O   1 
ATOM   462  C CB  . ASP   A 1 69  ? 24.400  -15.227 5.041  1.00 39.55 ? 761  ASP   A CB  1 
ATOM   463  C CG  . ASP   A 1 69  ? 25.580  -15.217 4.095  1.00 45.70 ? 761  ASP   A CG  1 
ATOM   464  O OD1 . ASP   A 1 69  ? 26.719  -15.018 4.568  1.00 46.62 ? 761  ASP   A OD1 1 
ATOM   465  O OD2 . ASP   A 1 69  ? 25.365  -15.419 2.876  1.00 48.79 ? 761  ASP   A OD2 1 
ATOM   466  N N   . GLU   A 1 70  ? 22.565  -16.305 7.366  1.00 34.09 ? 762  GLU   A N   1 
ATOM   467  C CA  . GLU   A 1 70  ? 21.332  -16.239 8.146  1.00 33.06 ? 762  GLU   A CA  1 
ATOM   468  C C   . GLU   A 1 70  ? 21.633  -16.469 9.636  1.00 30.77 ? 762  GLU   A C   1 
ATOM   469  O O   . GLU   A 1 70  ? 21.150  -15.720 10.486 1.00 30.57 ? 762  GLU   A O   1 
ATOM   470  C CB  . GLU   A 1 70  ? 20.271  -17.223 7.589  1.00 36.52 ? 762  GLU   A CB  1 
ATOM   471  C CG  . GLU   A 1 70  ? 19.957  -16.971 6.116  1.00 43.58 ? 762  GLU   A CG  1 
ATOM   472  C CD  . GLU   A 1 70  ? 18.690  -17.580 5.531  1.00 51.88 ? 762  GLU   A CD  1 
ATOM   473  O OE1 . GLU   A 1 70  ? 18.664  -17.824 4.302  1.00 53.43 ? 762  GLU   A OE1 1 
ATOM   474  O OE2 . GLU   A 1 70  ? 17.719  -17.799 6.291  1.00 55.19 ? 762  GLU   A OE2 1 
ATOM   475  N N   . ALA   A 1 71  ? 22.497  -17.451 9.943  1.00 28.86 ? 763  ALA   A N   1 
ATOM   476  C CA  . ALA   A 1 71  ? 22.931  -17.723 11.310 1.00 27.56 ? 763  ALA   A CA  1 
ATOM   477  C C   . ALA   A 1 71  ? 23.597  -16.509 11.990 1.00 26.51 ? 763  ALA   A C   1 
ATOM   478  O O   . ALA   A 1 71  ? 23.411  -16.356 13.186 1.00 26.25 ? 763  ALA   A O   1 
ATOM   479  C CB  . ALA   A 1 71  ? 23.848  -18.931 11.352 1.00 27.22 ? 763  ALA   A CB  1 
ATOM   480  N N   . TYR   A 1 72  ? 24.310  -15.630 11.253 1.00 26.13 ? 764  TYR   A N   1 
ATOM   481  C CA  . TYR   A 1 72  ? 24.895  -14.426 11.876 1.00 27.09 ? 764  TYR   A CA  1 
ATOM   482  C C   . TYR   A 1 72  ? 23.792  -13.463 12.321 1.00 25.96 ? 764  TYR   A C   1 
ATOM   483  O O   . TYR   A 1 72  ? 23.926  -12.807 13.352 1.00 25.66 ? 764  TYR   A O   1 
ATOM   484  C CB  . TYR   A 1 72  ? 25.877  -13.672 10.954 1.00 28.27 ? 764  TYR   A CB  1 
ATOM   485  C CG  . TYR   A 1 72  ? 27.124  -14.449 10.596 1.00 30.35 ? 764  TYR   A CG  1 
ATOM   486  C CD1 . TYR   A 1 72  ? 27.935  -14.995 11.581 1.00 31.95 ? 764  TYR   A CD1 1 
ATOM   487  C CD2 . TYR   A 1 72  ? 27.511  -14.611 9.271  1.00 31.99 ? 764  TYR   A CD2 1 
ATOM   488  C CE1 . TYR   A 1 72  ? 29.068  -15.734 11.257 1.00 33.27 ? 764  TYR   A CE1 1 
ATOM   489  C CE2 . TYR   A 1 72  ? 28.631  -15.362 8.932  1.00 33.34 ? 764  TYR   A CE2 1 
ATOM   490  C CZ  . TYR   A 1 72  ? 29.414  -15.912 9.930  1.00 34.57 ? 764  TYR   A CZ  1 
ATOM   491  O OH  . TYR   A 1 72  ? 30.541  -16.622 9.609  1.00 36.98 ? 764  TYR   A OH  1 
ATOM   492  N N   . VAL   A 1 73  ? 22.705  -13.376 11.543 1.00 24.99 ? 765  VAL   A N   1 
ATOM   493  C CA  . VAL   A 1 73  ? 21.585  -12.518 11.897 1.00 24.55 ? 765  VAL   A CA  1 
ATOM   494  C C   . VAL   A 1 73  ? 20.914  -13.093 13.161 1.00 23.50 ? 765  VAL   A C   1 
ATOM   495  O O   . VAL   A 1 73  ? 20.696  -12.350 14.116 1.00 22.73 ? 765  VAL   A O   1 
ATOM   496  C CB  . VAL   A 1 73  ? 20.614  -12.396 10.710 1.00 25.37 ? 765  VAL   A CB  1 
ATOM   497  C CG1 . VAL   A 1 73  ? 19.398  -11.544 11.077 1.00 25.71 ? 765  VAL   A CG1 1 
ATOM   498  C CG2 . VAL   A 1 73  ? 21.336  -11.842 9.485  1.00 25.71 ? 765  VAL   A CG2 1 
ATOM   499  N N   . MET   A 1 74  ? 20.731  -14.435 13.196 1.00 22.82 ? 766  MET   A N   1 
ATOM   500  C CA  . MET   A 1 74  ? 20.167  -15.207 14.300 1.00 22.72 ? 766  MET   A CA  1 
ATOM   501  C C   . MET   A 1 74  ? 21.008  -15.107 15.576 1.00 22.38 ? 766  MET   A C   1 
ATOM   502  O O   . MET   A 1 74  ? 20.479  -15.210 16.681 1.00 22.73 ? 766  MET   A O   1 
ATOM   503  C CB  . MET   A 1 74  ? 20.059  -16.678 13.879 1.00 23.41 ? 766  MET   A CB  1 
ATOM   504  C CG  . MET   A 1 74  ? 18.987  -16.942 12.847 1.00 24.59 ? 766  MET   A CG  1 
ATOM   505  S SD  . MET   A 1 74  ? 19.171  -18.580 12.064 1.00 29.85 ? 766  MET   A SD  1 
ATOM   506  C CE  . MET   A 1 74  ? 18.891  -19.641 13.402 1.00 22.69 ? 766  MET   A CE  1 
ATOM   507  N N   . ALA   A 1 75  ? 22.319  -14.939 15.430 1.00 21.68 ? 767  ALA   A N   1 
ATOM   508  C CA  . ALA   A 1 75  ? 23.222  -14.800 16.563 1.00 21.23 ? 767  ALA   A CA  1 
ATOM   509  C C   . ALA   A 1 75  ? 23.295  -13.368 17.080 1.00 20.24 ? 767  ALA   A C   1 
ATOM   510  O O   . ALA   A 1 75  ? 23.726  -13.186 18.209 1.00 20.40 ? 767  ALA   A O   1 
ATOM   511  C CB  . ALA   A 1 75  ? 24.613  -15.303 16.213 1.00 21.47 ? 767  ALA   A CB  1 
ATOM   512  N N   . SER   A 1 76  ? 22.872  -12.363 16.288 1.00 19.08 ? 768  SER   A N   1 
ATOM   513  C CA  . SER   A 1 76  ? 22.894  -10.935 16.670 1.00 18.88 ? 768  SER   A CA  1 
ATOM   514  C C   . SER   A 1 76  ? 21.715  -10.489 17.567 1.00 18.26 ? 768  SER   A C   1 
ATOM   515  O O   . SER   A 1 76  ? 21.754  -9.369  18.091 1.00 17.74 ? 768  SER   A O   1 
ATOM   516  C CB  . SER   A 1 76  ? 22.868  -10.056 15.423 1.00 19.80 ? 768  SER   A CB  1 
ATOM   517  O OG  . SER   A 1 76  ? 21.613  -10.144 14.759 1.00 21.94 ? 768  SER   A OG  1 
ATOM   518  N N   . VAL   A 1 77  ? 20.647  -11.301 17.666 1.00 18.09 ? 769  VAL   A N   1 
ATOM   519  C CA  . VAL   A 1 77  ? 19.488  -10.911 18.482 1.00 18.75 ? 769  VAL   A CA  1 
ATOM   520  C C   . VAL   A 1 77  ? 19.859  -10.894 19.965 1.00 19.37 ? 769  VAL   A C   1 
ATOM   521  O O   . VAL   A 1 77  ? 20.065  -11.934 20.607 1.00 18.97 ? 769  VAL   A O   1 
ATOM   522  C CB  . VAL   A 1 77  ? 18.170  -11.678 18.194 1.00 19.22 ? 769  VAL   A CB  1 
ATOM   523  C CG1 . VAL   A 1 77  ? 17.705  -11.438 16.757 1.00 19.52 ? 769  VAL   A CG1 1 
ATOM   524  C CG2 . VAL   A 1 77  ? 18.307  -13.162 18.470 1.00 19.57 ? 769  VAL   A CG2 1 
ATOM   525  N N   . ASP   A 1 78  ? 20.042  -9.670  20.470 1.00 19.80 ? 770  ASP   A N   1 
ATOM   526  C CA  . ASP   A 1 78  ? 20.406  -9.433  21.856 1.00 20.28 ? 770  ASP   A CA  1 
ATOM   527  C C   . ASP   A 1 78  ? 19.258  -8.770  22.590 1.00 19.02 ? 770  ASP   A C   1 
ATOM   528  O O   . ASP   A 1 78  ? 19.168  -7.540  22.598 1.00 19.01 ? 770  ASP   A O   1 
ATOM   529  C CB  . ASP   A 1 78  ? 21.684  -8.573  21.955 1.00 22.87 ? 770  ASP   A CB  1 
ATOM   530  C CG  . ASP   A 1 78  ? 22.133  -8.315  23.386 1.00 29.24 ? 770  ASP   A CG  1 
ATOM   531  O OD1 . ASP   A 1 78  ? 21.846  -9.164  24.263 1.00 29.78 ? 770  ASP   A OD1 1 
ATOM   532  O OD2 . ASP   A 1 78  ? 22.769  -7.262  23.629 1.00 32.61 ? 770  ASP   A OD2 1 
ATOM   533  N N   . ASN   A 1 79  ? 18.397  -9.579  23.222 1.00 17.83 ? 771  ASN   A N   1 
ATOM   534  C CA  . ASN   A 1 79  ? 17.265  -9.071  24.011 1.00 16.60 ? 771  ASN   A CA  1 
ATOM   535  C C   . ASN   A 1 79  ? 16.914  -10.074 25.135 1.00 16.01 ? 771  ASN   A C   1 
ATOM   536  O O   . ASN   A 1 79  ? 17.064  -11.260 24.921 1.00 15.78 ? 771  ASN   A O   1 
ATOM   537  C CB  . ASN   A 1 79  ? 16.082  -8.794  23.098 1.00 16.15 ? 771  ASN   A CB  1 
ATOM   538  C CG  . ASN   A 1 79  ? 14.974  -8.068  23.783 1.00 16.58 ? 771  ASN   A CG  1 
ATOM   539  O OD1 . ASN   A 1 79  ? 14.008  -8.665  24.257 1.00 16.18 ? 771  ASN   A OD1 1 
ATOM   540  N ND2 . ASN   A 1 79  ? 15.119  -6.770  23.903 1.00 17.92 ? 771  ASN   A ND2 1 
ATOM   541  N N   . PRO   A 1 80  ? 16.499  -9.648  26.351 1.00 15.98 ? 772  PRO   A N   1 
ATOM   542  C CA  . PRO   A 1 80  ? 16.221  -10.628 27.423 1.00 15.76 ? 772  PRO   A CA  1 
ATOM   543  C C   . PRO   A 1 80  ? 15.100  -11.616 27.108 1.00 16.15 ? 772  PRO   A C   1 
ATOM   544  O O   . PRO   A 1 80  ? 15.007  -12.673 27.732 1.00 16.29 ? 772  PRO   A O   1 
ATOM   545  C CB  . PRO   A 1 80  ? 15.814  -9.743  28.606 1.00 16.50 ? 772  PRO   A CB  1 
ATOM   546  C CG  . PRO   A 1 80  ? 16.397  -8.406  28.308 1.00 17.12 ? 772  PRO   A CG  1 
ATOM   547  C CD  . PRO   A 1 80  ? 16.275  -8.268  26.828 1.00 15.40 ? 772  PRO   A CD  1 
ATOM   548  N N   . HIS   A 1 81  ? 14.239  -11.263 26.163 1.00 15.57 ? 773  HIS   A N   1 
ATOM   549  C CA  . HIS   A 1 81  ? 13.126  -12.087 25.788 1.00 15.75 ? 773  HIS   A CA  1 
ATOM   550  C C   . HIS   A 1 81  ? 13.266  -12.662 24.403 1.00 16.64 ? 773  HIS   A C   1 
ATOM   551  O O   . HIS   A 1 81  ? 12.245  -12.990 23.790 1.00 16.58 ? 773  HIS   A O   1 
ATOM   552  C CB  . HIS   A 1 81  ? 11.822  -11.287 25.929 1.00 15.65 ? 773  HIS   A CB  1 
ATOM   553  C CG  . HIS   A 1 81  ? 11.688  -10.739 27.309 1.00 17.00 ? 773  HIS   A CG  1 
ATOM   554  N ND1 . HIS   A 1 81  ? 11.932  -9.402  27.578 1.00 19.05 ? 773  HIS   A ND1 1 
ATOM   555  C CD2 . HIS   A 1 81  ? 11.528  -11.398 28.476 1.00 17.13 ? 773  HIS   A CD2 1 
ATOM   556  C CE1 . HIS   A 1 81  ? 11.813  -9.279  28.885 1.00 18.70 ? 773  HIS   A CE1 1 
ATOM   557  N NE2 . HIS   A 1 81  ? 11.572  -10.455 29.464 1.00 18.65 ? 773  HIS   A NE2 1 
ATOM   558  N N   . VAL   A 1 82  ? 14.503  -12.791 23.894 1.00 16.40 ? 774  VAL   A N   1 
ATOM   559  C CA  . VAL   A 1 82  ? 14.759  -13.430 22.613 1.00 16.37 ? 774  VAL   A CA  1 
ATOM   560  C C   . VAL   A 1 82  ? 15.960  -14.384 22.788 1.00 15.99 ? 774  VAL   A C   1 
ATOM   561  O O   . VAL   A 1 82  ? 17.017  -13.982 23.271 1.00 14.92 ? 774  VAL   A O   1 
ATOM   562  C CB  . VAL   A 1 82  ? 14.953  -12.467 21.412 1.00 17.18 ? 774  VAL   A CB  1 
ATOM   563  C CG1 . VAL   A 1 82  ? 14.973  -13.252 20.109 1.00 17.82 ? 774  VAL   A CG1 1 
ATOM   564  C CG2 . VAL   A 1 82  ? 13.870  -11.391 21.356 1.00 17.06 ? 774  VAL   A CG2 1 
ATOM   565  N N   . CYS   A 1 83  ? 15.765  -15.666 22.450 1.00 16.14 ? 775  CYS   A N   1 
ATOM   566  C CA  . CYS   A 1 83  ? 16.836  -16.644 22.517 1.00 16.23 ? 775  CYS   A CA  1 
ATOM   567  C C   . CYS   A 1 83  ? 17.821  -16.323 21.400 1.00 16.28 ? 775  CYS   A C   1 
ATOM   568  O O   . CYS   A 1 83  ? 17.446  -16.215 20.210 1.00 16.08 ? 775  CYS   A O   1 
ATOM   569  C CB  . CYS   A 1 83  ? 16.290  -18.062 22.378 1.00 17.03 ? 775  CYS   A CB  1 
ATOM   570  S SG  . CYS   A 1 83  ? 15.284  -18.611 23.778 1.00 20.35 ? 775  CYS   A SG  1 
ATOM   571  N N   . ARG   A 1 84  ? 19.080  -16.140 21.786 1.00 15.87 ? 776  ARG   A N   1 
ATOM   572  C CA  . ARG   A 1 84  ? 20.136  -15.827 20.842 1.00 16.13 ? 776  ARG   A CA  1 
ATOM   573  C C   . ARG   A 1 84  ? 20.783  -17.144 20.401 1.00 16.98 ? 776  ARG   A C   1 
ATOM   574  O O   . ARG   A 1 84  ? 21.065  -18.006 21.250 1.00 17.12 ? 776  ARG   A O   1 
ATOM   575  C CB  . ARG   A 1 84  ? 21.179  -14.961 21.577 1.00 16.88 ? 776  ARG   A CB  1 
ATOM   576  C CG  . ARG   A 1 84  ? 22.283  -14.442 20.689 1.00 18.94 ? 776  ARG   A CG  1 
ATOM   577  C CD  . ARG   A 1 84  ? 23.143  -13.343 21.326 1.00 18.68 ? 776  ARG   A CD  1 
ATOM   578  N NE  . ARG   A 1 84  ? 24.309  -13.857 22.051 1.00 20.43 ? 776  ARG   A NE  1 
ATOM   579  C CZ  . ARG   A 1 84  ? 25.425  -14.305 21.475 1.00 22.22 ? 776  ARG   A CZ  1 
ATOM   580  N NH1 . ARG   A 1 84  ? 25.516  -14.377 20.149 1.00 21.56 ? 776  ARG   A NH1 1 
ATOM   581  N NH2 . ARG   A 1 84  ? 26.436  -14.735 22.219 1.00 20.41 ? 776  ARG   A NH2 1 
ATOM   582  N N   . LEU   A 1 85  ? 21.046  -17.292 19.087 1.00 16.97 ? 777  LEU   A N   1 
ATOM   583  C CA  . LEU   A 1 85  ? 21.788  -18.445 18.560 1.00 17.20 ? 777  LEU   A CA  1 
ATOM   584  C C   . LEU   A 1 85  ? 23.277  -18.216 18.985 1.00 17.40 ? 777  LEU   A C   1 
ATOM   585  O O   . LEU   A 1 85  ? 23.779  -17.108 18.824 1.00 17.69 ? 777  LEU   A O   1 
ATOM   586  C CB  . LEU   A 1 85  ? 21.672  -18.501 17.013 1.00 17.24 ? 777  LEU   A CB  1 
ATOM   587  C CG  . LEU   A 1 85  ? 22.573  -19.546 16.325 1.00 18.51 ? 777  LEU   A CG  1 
ATOM   588  C CD1 . LEU   A 1 85  ? 22.239  -20.952 16.794 1.00 18.95 ? 777  LEU   A CD1 1 
ATOM   589  C CD2 . LEU   A 1 85  ? 22.501  -19.438 14.816 1.00 19.30 ? 777  LEU   A CD2 1 
ATOM   590  N N   . LEU   A 1 86  ? 23.942  -19.204 19.582 1.00 17.46 ? 778  LEU   A N   1 
ATOM   591  C CA  . LEU   A 1 86  ? 25.316  -19.006 20.081 1.00 18.33 ? 778  LEU   A CA  1 
ATOM   592  C C   . LEU   A 1 86  ? 26.391  -19.668 19.220 1.00 19.82 ? 778  LEU   A C   1 
ATOM   593  O O   . LEU   A 1 86  ? 27.433  -19.071 18.950 1.00 19.83 ? 778  LEU   A O   1 
ATOM   594  C CB  . LEU   A 1 86  ? 25.437  -19.448 21.551 1.00 18.10 ? 778  LEU   A CB  1 
ATOM   595  C CG  . LEU   A 1 86  ? 24.323  -18.945 22.492 1.00 18.77 ? 778  LEU   A CG  1 
ATOM   596  C CD1 . LEU   A 1 86  ? 24.500  -19.488 23.864 1.00 19.46 ? 778  LEU   A CD1 1 
ATOM   597  C CD2 . LEU   A 1 86  ? 24.292  -17.441 22.553 1.00 18.86 ? 778  LEU   A CD2 1 
ATOM   598  N N   . GLY   A 1 87  ? 26.129  -20.892 18.798 1.00 20.92 ? 779  GLY   A N   1 
ATOM   599  C CA  . GLY   A 1 87  ? 27.068  -21.634 17.978 1.00 22.35 ? 779  GLY   A CA  1 
ATOM   600  C C   . GLY   A 1 87  ? 26.414  -22.441 16.877 1.00 24.11 ? 779  GLY   A C   1 
ATOM   601  O O   . GLY   A 1 87  ? 25.228  -22.774 16.956 1.00 23.69 ? 779  GLY   A O   1 
ATOM   602  N N   . ILE   A 1 88  ? 27.187  -22.751 15.830 1.00 25.66 ? 780  ILE   A N   1 
ATOM   603  C CA  . ILE   A 1 88  ? 26.687  -23.569 14.733 1.00 27.81 ? 780  ILE   A CA  1 
ATOM   604  C C   . ILE   A 1 88  ? 27.718  -24.640 14.357 1.00 30.21 ? 780  ILE   A C   1 
ATOM   605  O O   . ILE   A 1 88  ? 28.918  -24.430 14.512 1.00 30.69 ? 780  ILE   A O   1 
ATOM   606  C CB  . ILE   A 1 88  ? 26.294  -22.701 13.526 1.00 28.31 ? 780  ILE   A CB  1 
ATOM   607  C CG1 . ILE   A 1 88  ? 25.359  -23.458 12.557 1.00 29.23 ? 780  ILE   A CG1 1 
ATOM   608  C CG2 . ILE   A 1 88  ? 27.519  -22.155 12.808 1.00 28.91 ? 780  ILE   A CG2 1 
ATOM   609  C CD1 . ILE   A 1 88  ? 24.660  -22.568 11.559 1.00 30.07 ? 780  ILE   A CD1 1 
ATOM   610  N N   . CYS   A 1 89  ? 27.250  -25.804 13.914 1.00 31.37 ? 781  CYS   A N   1 
ATOM   611  C CA  . CYS   A 1 89  ? 28.130  -26.864 13.454 1.00 32.98 ? 781  CYS   A CA  1 
ATOM   612  C C   . CYS   A 1 89  ? 27.567  -27.366 12.129 1.00 34.11 ? 781  CYS   A C   1 
ATOM   613  O O   . CYS   A 1 89  ? 26.554  -28.065 12.113 1.00 33.53 ? 781  CYS   A O   1 
ATOM   614  C CB  . CYS   A 1 89  ? 28.252  -27.984 14.485 1.00 34.40 ? 781  CYS   A CB  1 
ATOM   615  S SG  . CYS   A 1 89  ? 29.418  -29.311 14.028 1.00 39.53 ? 781  CYS   A SG  1 
ATOM   616  N N   . LEU   A 1 90  ? 28.198  -26.950 11.018 1.00 35.42 ? 782  LEU   A N   1 
ATOM   617  C CA  . LEU   A 1 90  ? 27.816  -27.327 9.660  1.00 37.11 ? 782  LEU   A CA  1 
ATOM   618  C C   . LEU   A 1 90  ? 28.629  -28.536 9.188  1.00 39.03 ? 782  LEU   A C   1 
ATOM   619  O O   . LEU   A 1 90  ? 29.827  -28.408 8.943  1.00 39.29 ? 782  LEU   A O   1 
ATOM   620  C CB  . LEU   A 1 90  ? 28.073  -26.159 8.703  1.00 37.33 ? 782  LEU   A CB  1 
ATOM   621  C CG  . LEU   A 1 90  ? 27.136  -24.964 8.795  1.00 38.88 ? 782  LEU   A CG  1 
ATOM   622  C CD1 . LEU   A 1 90  ? 27.555  -23.873 7.829  1.00 39.25 ? 782  LEU   A CD1 1 
ATOM   623  C CD2 . LEU   A 1 90  ? 25.709  -25.366 8.489  1.00 39.20 ? 782  LEU   A CD2 1 
ATOM   624  N N   . THR   A 1 91  ? 27.992  -29.707 9.088  1.00 40.27 ? 783  THR   A N   1 
ATOM   625  C CA  . THR   A 1 91  ? 28.605  -30.946 8.593  1.00 42.03 ? 783  THR   A CA  1 
ATOM   626  C C   . THR   A 1 91  ? 27.615  -31.496 7.491  1.00 43.07 ? 783  THR   A C   1 
ATOM   627  O O   . THR   A 1 91  ? 27.233  -30.720 6.615  1.00 43.30 ? 783  THR   A O   1 
ATOM   628  C CB  . THR   A 1 91  ? 28.965  -31.886 9.788  1.00 43.91 ? 783  THR   A CB  1 
ATOM   629  O OG1 . THR   A 1 91  ? 27.755  -32.375 10.373 1.00 45.29 ? 783  THR   A OG1 1 
ATOM   630  C CG2 . THR   A 1 91  ? 29.867  -31.227 10.832 1.00 44.35 ? 783  THR   A CG2 1 
ATOM   631  N N   . SER   A 1 92  ? 27.197  -32.783 7.515  1.00 43.43 ? 784  SER   A N   1 
ATOM   632  C CA  . SER   A 1 92  ? 26.161  -33.280 6.608  1.00 44.20 ? 784  SER   A CA  1 
ATOM   633  C C   . SER   A 1 92  ? 24.796  -32.708 7.090  1.00 44.50 ? 784  SER   A C   1 
ATOM   634  O O   . SER   A 1 92  ? 23.906  -32.456 6.268  1.00 45.03 ? 784  SER   A O   1 
ATOM   635  C CB  . SER   A 1 92  ? 26.113  -34.805 6.631  1.00 45.94 ? 784  SER   A CB  1 
ATOM   636  O OG  . SER   A 1 92  ? 25.781  -35.282 7.926  1.00 48.74 ? 784  SER   A OG  1 
ATOM   637  N N   . THR   A 1 93  ? 24.649  -32.509 8.434  1.00 43.62 ? 785  THR   A N   1 
ATOM   638  C CA  . THR   A 1 93  ? 23.506  -31.914 9.122  1.00 43.25 ? 785  THR   A CA  1 
ATOM   639  C C   . THR   A 1 93  ? 23.850  -30.466 9.596  1.00 42.40 ? 785  THR   A C   1 
ATOM   640  O O   . THR   A 1 93  ? 25.021  -30.078 9.638  1.00 42.57 ? 785  THR   A O   1 
ATOM   641  C CB  . THR   A 1 93  ? 23.145  -32.783 10.339 1.00 44.55 ? 785  THR   A CB  1 
ATOM   642  O OG1 . THR   A 1 93  ? 24.197  -32.704 11.308 1.00 45.22 ? 785  THR   A OG1 1 
ATOM   643  C CG2 . THR   A 1 93  ? 22.895  -34.236 9.972  1.00 45.18 ? 785  THR   A CG2 1 
ATOM   644  N N   . VAL   A 1 94  ? 22.829  -29.686 9.977  1.00 40.94 ? 786  VAL   A N   1 
ATOM   645  C CA  . VAL   A 1 94  ? 23.039  -28.349 10.512 1.00 39.72 ? 786  VAL   A CA  1 
ATOM   646  C C   . VAL   A 1 94  ? 22.668  -28.380 12.000 1.00 38.06 ? 786  VAL   A C   1 
ATOM   647  O O   . VAL   A 1 94  ? 21.508  -28.643 12.339 1.00 38.21 ? 786  VAL   A O   1 
ATOM   648  C CB  . VAL   A 1 94  ? 22.202  -27.296 9.760  1.00 40.41 ? 786  VAL   A CB  1 
ATOM   649  C CG1 . VAL   A 1 94  ? 22.283  -25.944 10.459 1.00 41.05 ? 786  VAL   A CG1 1 
ATOM   650  C CG2 . VAL   A 1 94  ? 22.643  -27.186 8.303  1.00 40.79 ? 786  VAL   A CG2 1 
ATOM   651  N N   . GLN   A 1 95  ? 23.649  -28.153 12.890 1.00 35.96 ? 787  GLN   A N   1 
ATOM   652  C CA  . GLN   A 1 95  ? 23.380  -28.152 14.333 1.00 34.26 ? 787  GLN   A CA  1 
ATOM   653  C C   . GLN   A 1 95  ? 23.454  -26.749 14.929 1.00 32.89 ? 787  GLN   A C   1 
ATOM   654  O O   . GLN   A 1 95  ? 24.410  -26.006 14.687 1.00 32.98 ? 787  GLN   A O   1 
ATOM   655  C CB  . GLN   A 1 95  ? 24.285  -29.133 15.082 1.00 34.58 ? 787  GLN   A CB  1 
ATOM   656  C CG  . GLN   A 1 95  ? 23.949  -30.575 14.737 1.00 37.01 ? 787  GLN   A CG  1 
ATOM   657  C CD  . GLN   A 1 95  ? 24.820  -31.560 15.471 1.00 40.22 ? 787  GLN   A CD  1 
ATOM   658  O OE1 . GLN   A 1 95  ? 24.503  -32.012 16.578 1.00 41.10 ? 787  GLN   A OE1 1 
ATOM   659  N NE2 . GLN   A 1 95  ? 25.937  -31.919 14.863 1.00 40.88 ? 787  GLN   A NE2 1 
ATOM   660  N N   . LEU   A 1 96  ? 22.411  -26.370 15.671 1.00 31.21 ? 788  LEU   A N   1 
ATOM   661  C CA  . LEU   A 1 96  ? 22.334  -25.059 16.291 1.00 29.95 ? 788  LEU   A CA  1 
ATOM   662  C C   . LEU   A 1 96  ? 22.480  -25.203 17.789 1.00 28.43 ? 788  LEU   A C   1 
ATOM   663  O O   . LEU   A 1 96  ? 21.848  -26.063 18.382 1.00 28.87 ? 788  LEU   A O   1 
ATOM   664  C CB  . LEU   A 1 96  ? 21.004  -24.375 15.931 1.00 30.26 ? 788  LEU   A CB  1 
ATOM   665  C CG  . LEU   A 1 96  ? 20.825  -24.030 14.451 1.00 32.02 ? 788  LEU   A CG  1 
ATOM   666  C CD1 . LEU   A 1 96  ? 19.460  -23.387 14.191 1.00 32.69 ? 788  LEU   A CD1 1 
ATOM   667  C CD2 . LEU   A 1 96  ? 21.928  -23.115 13.953 1.00 32.53 ? 788  LEU   A CD2 1 
ATOM   668  N N   . ILE   A 1 97  ? 23.324  -24.376 18.411 1.00 26.55 ? 789  ILE   A N   1 
ATOM   669  C CA  . ILE   A 1 97  ? 23.578  -24.445 19.851 1.00 24.81 ? 789  ILE   A CA  1 
ATOM   670  C C   . ILE   A 1 97  ? 23.178  -23.135 20.510 1.00 22.41 ? 789  ILE   A C   1 
ATOM   671  O O   . ILE   A 1 97  ? 23.422  -22.069 19.951 1.00 21.36 ? 789  ILE   A O   1 
ATOM   672  C CB  . ILE   A 1 97  ? 25.077  -24.812 20.124 1.00 25.49 ? 789  ILE   A CB  1 
ATOM   673  C CG1 . ILE   A 1 97  ? 25.421  -26.239 19.607 1.00 26.52 ? 789  ILE   A CG1 1 
ATOM   674  C CG2 . ILE   A 1 97  ? 25.437  -24.663 21.605 1.00 25.74 ? 789  ILE   A CG2 1 
ATOM   675  C CD1 . ILE   A 1 97  ? 25.791  -26.369 18.092 1.00 27.51 ? 789  ILE   A CD1 1 
ATOM   676  N N   . THR   A 1 98  ? 22.518  -23.228 21.674 1.00 21.47 ? 790  THR   A N   1 
ATOM   677  C CA  . THR   A 1 98  ? 22.035  -22.122 22.489 1.00 21.82 ? 790  THR   A CA  1 
ATOM   678  C C   . THR   A 1 98  ? 22.097  -22.519 23.990 1.00 21.79 ? 790  THR   A C   1 
ATOM   679  O O   . THR   A 1 98  ? 22.383  -23.667 24.316 1.00 21.85 ? 790  THR   A O   1 
ATOM   680  C CB  . THR   A 1 98  ? 20.577  -21.761 22.080 1.00 24.34 ? 790  THR   A CB  1 
ATOM   681  O OG1 . THR   A 1 98  ? 19.771  -22.928 22.188 1.00 26.63 ? 790  THR   A OG1 1 
ATOM   682  C CG2 . THR   A 1 98  ? 20.454  -21.250 20.679 1.00 24.97 ? 790  THR   A CG2 1 
ATOM   683  N N   . GLN   A 1 99  ? 21.844  -21.577 24.905 1.00 22.01 ? 791  GLN   A N   1 
ATOM   684  C CA  . GLN   A 1 99  ? 21.845  -21.849 26.338 1.00 23.04 ? 791  GLN   A CA  1 
ATOM   685  C C   . GLN   A 1 99  ? 20.725  -22.843 26.733 1.00 23.98 ? 791  GLN   A C   1 
ATOM   686  O O   . GLN   A 1 99  ? 19.578  -22.656 26.355 1.00 24.13 ? 791  GLN   A O   1 
ATOM   687  C CB  . GLN   A 1 99  ? 21.697  -20.537 27.123 1.00 25.05 ? 791  GLN   A CB  1 
ATOM   688  C CG  . GLN   A 1 99  ? 21.736  -20.744 28.629 1.00 29.26 ? 791  GLN   A CG  1 
ATOM   689  C CD  . GLN   A 1 99  ? 21.610  -19.461 29.401 1.00 34.72 ? 791  GLN   A CD  1 
ATOM   690  O OE1 . GLN   A 1 99  ? 20.615  -18.728 29.292 1.00 36.23 ? 791  GLN   A OE1 1 
ATOM   691  N NE2 . GLN   A 1 99  ? 22.619  -19.170 30.221 1.00 35.95 ? 791  GLN   A NE2 1 
ATOM   692  N N   . LEU   A 1 100 ? 21.069  -23.910 27.454 1.00 24.20 ? 792  LEU   A N   1 
ATOM   693  C CA  . LEU   A 1 100 ? 20.101  -24.910 27.870 1.00 24.81 ? 792  LEU   A CA  1 
ATOM   694  C C   . LEU   A 1 100 ? 19.080  -24.346 28.865 1.00 26.13 ? 792  LEU   A C   1 
ATOM   695  O O   . LEU   A 1 100 ? 19.425  -23.654 29.833 1.00 26.16 ? 792  LEU   A O   1 
ATOM   696  C CB  . LEU   A 1 100 ? 20.805  -26.156 28.440 1.00 24.36 ? 792  LEU   A CB  1 
ATOM   697  C CG  . LEU   A 1 100 ? 19.877  -27.257 28.982 1.00 25.12 ? 792  LEU   A CG  1 
ATOM   698  C CD1 . LEU   A 1 100 ? 19.157  -27.974 27.850 1.00 25.13 ? 792  LEU   A CD1 1 
ATOM   699  C CD2 . LEU   A 1 100 ? 20.648  -28.270 29.794 1.00 25.56 ? 792  LEU   A CD2 1 
ATOM   700  N N   . MET   A 1 101 ? 17.811  -24.619 28.601 1.00 26.69 ? 793  MET   A N   1 
ATOM   701  C CA  . MET   A 1 101 ? 16.739  -24.171 29.469 1.00 27.79 ? 793  MET   A CA  1 
ATOM   702  C C   . MET   A 1 101 ? 15.956  -25.363 30.008 1.00 27.53 ? 793  MET   A C   1 
ATOM   703  O O   . MET   A 1 101 ? 15.144  -25.976 29.291 1.00 27.52 ? 793  MET   A O   1 
ATOM   704  C CB  . MET   A 1 101 ? 15.870  -23.099 28.812 1.00 29.35 ? 793  MET   A CB  1 
ATOM   705  C CG  . MET   A 1 101 ? 16.445  -21.707 29.008 1.00 32.78 ? 793  MET   A CG  1 
ATOM   706  S SD  . MET   A 1 101 ? 15.653  -20.537 27.904 1.00 44.69 ? 793  MET   A SD  1 
ATOM   707  C CE  . MET   A 1 101 ? 16.406  -21.046 26.377 1.00 42.13 ? 793  MET   A CE  1 
ATOM   708  N N   . PRO   A 1 102 ? 16.291  -25.750 31.264 1.00 26.48 ? 794  PRO   A N   1 
ATOM   709  C CA  . PRO   A 1 102 ? 15.647  -26.919 31.870 1.00 25.96 ? 794  PRO   A CA  1 
ATOM   710  C C   . PRO   A 1 102 ? 14.117  -26.944 31.794 1.00 25.32 ? 794  PRO   A C   1 
ATOM   711  O O   . PRO   A 1 102 ? 13.552  -28.023 31.568 1.00 25.42 ? 794  PRO   A O   1 
ATOM   712  C CB  . PRO   A 1 102 ? 16.118  -26.857 33.330 1.00 26.95 ? 794  PRO   A CB  1 
ATOM   713  C CG  . PRO   A 1 102 ? 17.420  -26.128 33.284 1.00 27.31 ? 794  PRO   A CG  1 
ATOM   714  C CD  . PRO   A 1 102 ? 17.264  -25.125 32.190 1.00 25.77 ? 794  PRO   A CD  1 
ATOM   715  N N   . PHE   A 1 103 ? 13.447  -25.773 31.987 1.00 23.86 ? 795  PHE   A N   1 
ATOM   716  C CA  . PHE   A 1 103 ? 11.988  -25.688 32.010 1.00 22.68 ? 795  PHE   A CA  1 
ATOM   717  C C   . PHE   A 1 103 ? 11.282  -25.948 30.682 1.00 22.16 ? 795  PHE   A C   1 
ATOM   718  O O   . PHE   A 1 103 ? 10.071  -26.185 30.661 1.00 21.91 ? 795  PHE   A O   1 
ATOM   719  C CB  . PHE   A 1 103 ? 11.545  -24.344 32.566 1.00 22.82 ? 795  PHE   A CB  1 
ATOM   720  C CG  . PHE   A 1 103 ? 11.609  -24.162 34.066 1.00 23.59 ? 795  PHE   A CG  1 
ATOM   721  C CD1 . PHE   A 1 103 ? 10.642  -24.713 34.889 1.00 24.39 ? 795  PHE   A CD1 1 
ATOM   722  C CD2 . PHE   A 1 103 ? 12.570  -23.346 34.641 1.00 23.85 ? 795  PHE   A CD2 1 
ATOM   723  C CE1 . PHE   A 1 103 ? 10.665  -24.488 36.259 1.00 24.74 ? 795  PHE   A CE1 1 
ATOM   724  C CE2 . PHE   A 1 103 ? 12.590  -23.129 36.005 1.00 24.29 ? 795  PHE   A CE2 1 
ATOM   725  C CZ  . PHE   A 1 103 ? 11.636  -23.698 36.804 1.00 24.17 ? 795  PHE   A CZ  1 
ATOM   726  N N   . GLY   A 1 104 ? 12.013  -25.858 29.582 1.00 21.71 ? 796  GLY   A N   1 
ATOM   727  C CA  . GLY   A 1 104 ? 11.457  -26.137 28.270 1.00 21.56 ? 796  GLY   A CA  1 
ATOM   728  C C   . GLY   A 1 104 ? 10.496  -25.079 27.785 1.00 21.80 ? 796  GLY   A C   1 
ATOM   729  O O   . GLY   A 1 104 ? 10.637  -23.923 28.170 1.00 21.86 ? 796  GLY   A O   1 
ATOM   730  N N   . CYS   A 1 105 ? 9.525   -25.455 26.920 1.00 21.54 ? 797  CYS   A N   1 
ATOM   731  C CA  . CYS   A 1 105 ? 8.582   -24.491 26.361 1.00 22.41 ? 797  CYS   A CA  1 
ATOM   732  C C   . CYS   A 1 105 ? 7.371   -24.207 27.248 1.00 22.33 ? 797  CYS   A C   1 
ATOM   733  O O   . CYS   A 1 105 ? 6.928   -25.051 28.042 1.00 22.60 ? 797  CYS   A O   1 
ATOM   734  C CB  . CYS   A 1 105 ? 8.151   -24.880 24.950 1.00 24.20 ? 797  CYS   A CB  1 
ATOM   735  S SG  . CYS   A 1 105 ? 7.080   -26.344 24.875 1.00 29.12 ? 797  CYS   A SG  1 
ATOM   736  N N   . LEU   A 1 106 ? 6.828   -22.995 27.070 1.00 21.49 ? 798  LEU   A N   1 
ATOM   737  C CA  . LEU   A 1 106 ? 5.682   -22.473 27.787 1.00 21.09 ? 798  LEU   A CA  1 
ATOM   738  C C   . LEU   A 1 106 ? 4.426   -23.261 27.497 1.00 21.10 ? 798  LEU   A C   1 
ATOM   739  O O   . LEU   A 1 106 ? 3.629   -23.445 28.409 1.00 20.94 ? 798  LEU   A O   1 
ATOM   740  C CB  . LEU   A 1 106 ? 5.496   -20.983 27.441 1.00 20.59 ? 798  LEU   A CB  1 
ATOM   741  C CG  . LEU   A 1 106 ? 4.614   -20.128 28.327 1.00 20.01 ? 798  LEU   A CG  1 
ATOM   742  C CD1 . LEU   A 1 106 ? 4.962   -20.266 29.775 1.00 19.78 ? 798  LEU   A CD1 1 
ATOM   743  C CD2 . LEU   A 1 106 ? 4.738   -18.704 27.943 1.00 20.26 ? 798  LEU   A CD2 1 
ATOM   744  N N   . LEU   A 1 107 ? 4.264   -23.776 26.265 1.00 21.30 ? 799  LEU   A N   1 
ATOM   745  C CA  . LEU   A 1 107 ? 3.092   -24.580 25.901 1.00 22.72 ? 799  LEU   A CA  1 
ATOM   746  C C   . LEU   A 1 107 ? 2.949   -25.801 26.823 1.00 24.51 ? 799  LEU   A C   1 
ATOM   747  O O   . LEU   A 1 107 ? 1.884   -25.993 27.414 1.00 24.52 ? 799  LEU   A O   1 
ATOM   748  C CB  . LEU   A 1 107 ? 3.162   -25.024 24.428 1.00 22.80 ? 799  LEU   A CB  1 
ATOM   749  C CG  . LEU   A 1 107 ? 2.061   -25.979 23.954 1.00 23.70 ? 799  LEU   A CG  1 
ATOM   750  C CD1 . LEU   A 1 107 ? 0.696   -25.318 24.021 1.00 24.16 ? 799  LEU   A CD1 1 
ATOM   751  C CD2 . LEU   A 1 107 ? 2.351   -26.488 22.542 1.00 23.65 ? 799  LEU   A CD2 1 
ATOM   752  N N   . ASP   A 1 108 ? 4.040   -26.595 26.981 1.00 25.12 ? 800  ASP   A N   1 
ATOM   753  C CA  . ASP   A 1 108 ? 4.050   -27.756 27.863 1.00 26.06 ? 800  ASP   A CA  1 
ATOM   754  C C   . ASP   A 1 108 ? 4.007   -27.359 29.332 1.00 26.52 ? 800  ASP   A C   1 
ATOM   755  O O   . ASP   A 1 108 ? 3.491   -28.114 30.137 1.00 27.67 ? 800  ASP   A O   1 
ATOM   756  C CB  . ASP   A 1 108 ? 5.274   -28.639 27.580 1.00 28.30 ? 800  ASP   A CB  1 
ATOM   757  C CG  . ASP   A 1 108 ? 5.273   -29.238 26.186 1.00 33.86 ? 800  ASP   A CG  1 
ATOM   758  O OD1 . ASP   A 1 108 ? 4.189   -29.264 25.544 1.00 34.06 ? 800  ASP   A OD1 1 
ATOM   759  O OD2 . ASP   A 1 108 ? 6.347   -29.688 25.737 1.00 37.19 ? 800  ASP   A OD2 1 
ATOM   760  N N   . TYR   A 1 109 ? 4.559   -26.204 29.693 1.00 25.72 ? 801  TYR   A N   1 
ATOM   761  C CA  . TYR   A 1 109 ? 4.533   -25.729 31.076 1.00 25.09 ? 801  TYR   A CA  1 
ATOM   762  C C   . TYR   A 1 109 ? 3.117   -25.420 31.484 1.00 24.90 ? 801  TYR   A C   1 
ATOM   763  O O   . TYR   A 1 109 ? 2.726   -25.807 32.578 1.00 24.81 ? 801  TYR   A O   1 
ATOM   764  C CB  . TYR   A 1 109 ? 5.410   -24.473 31.249 1.00 24.51 ? 801  TYR   A CB  1 
ATOM   765  C CG  . TYR   A 1 109 ? 5.509   -23.982 32.678 1.00 24.14 ? 801  TYR   A CG  1 
ATOM   766  C CD1 . TYR   A 1 109 ? 6.407   -24.553 33.570 1.00 24.60 ? 801  TYR   A CD1 1 
ATOM   767  C CD2 . TYR   A 1 109 ? 4.771   -22.889 33.110 1.00 24.38 ? 801  TYR   A CD2 1 
ATOM   768  C CE1 . TYR   A 1 109 ? 6.545   -24.067 34.867 1.00 25.07 ? 801  TYR   A CE1 1 
ATOM   769  C CE2 . TYR   A 1 109 ? 4.876   -22.413 34.410 1.00 24.97 ? 801  TYR   A CE2 1 
ATOM   770  C CZ  . TYR   A 1 109 ? 5.759   -23.009 35.292 1.00 25.65 ? 801  TYR   A CZ  1 
ATOM   771  O OH  . TYR   A 1 109 ? 5.865   -22.520 36.574 1.00 26.05 ? 801  TYR   A OH  1 
ATOM   772  N N   . VAL   A 1 110 ? 2.345   -24.705 30.627 1.00 24.75 ? 802  VAL   A N   1 
ATOM   773  C CA  . VAL   A 1 110 ? 0.955   -24.345 30.953 1.00 24.89 ? 802  VAL   A CA  1 
ATOM   774  C C   . VAL   A 1 110 ? 0.038   -25.564 30.937 1.00 24.91 ? 802  VAL   A C   1 
ATOM   775  O O   . VAL   A 1 110 ? -0.880  -25.621 31.737 1.00 24.69 ? 802  VAL   A O   1 
ATOM   776  C CB  . VAL   A 1 110 ? 0.368   -23.161 30.146 1.00 25.25 ? 802  VAL   A CB  1 
ATOM   777  C CG1 . VAL   A 1 110 ? 1.217   -21.914 30.314 1.00 25.44 ? 802  VAL   A CG1 1 
ATOM   778  C CG2 . VAL   A 1 110 ? 0.175   -23.505 28.671 1.00 25.60 ? 802  VAL   A CG2 1 
ATOM   779  N N   . ARG   A 1 111 ? 0.339   -26.568 30.101 1.00 25.28 ? 803  ARG   A N   1 
ATOM   780  C CA  . ARG   A 1 111 ? -0.409  -27.822 30.020 1.00 25.75 ? 803  ARG   A CA  1 
ATOM   781  C C   . ARG   A 1 111 ? -0.123  -28.625 31.279 1.00 27.41 ? 803  ARG   A C   1 
ATOM   782  O O   . ARG   A 1 111 ? -1.055  -29.085 31.934 1.00 28.03 ? 803  ARG   A O   1 
ATOM   783  C CB  . ARG   A 1 111 ? -0.004  -28.628 28.766 1.00 25.36 ? 803  ARG   A CB  1 
ATOM   784  C CG  . ARG   A 1 111 ? -0.670  -28.157 27.491 1.00 25.28 ? 803  ARG   A CG  1 
ATOM   785  C CD  . ARG   A 1 111 ? -0.248  -28.974 26.298 1.00 26.26 ? 803  ARG   A CD  1 
ATOM   786  N NE  . ARG   A 1 111 ? -0.896  -28.489 25.081 1.00 29.23 ? 803  ARG   A NE  1 
ATOM   787  C CZ  . ARG   A 1 111 ? -0.615  -28.915 23.854 1.00 32.46 ? 803  ARG   A CZ  1 
ATOM   788  N NH1 . ARG   A 1 111 ? 0.310   -29.847 23.661 1.00 32.38 ? 803  ARG   A NH1 1 
ATOM   789  N NH2 . ARG   A 1 111 ? -1.247  -28.401 22.806 1.00 33.12 ? 803  ARG   A NH2 1 
ATOM   790  N N   . GLU   A 1 112 ? 1.161   -28.732 31.665 1.00 28.14 ? 804  GLU   A N   1 
ATOM   791  C CA  . GLU   A 1 112 ? 1.567   -29.422 32.887 1.00 29.07 ? 804  GLU   A CA  1 
ATOM   792  C C   . GLU   A 1 112 ? 1.158   -28.656 34.159 1.00 29.75 ? 804  GLU   A C   1 
ATOM   793  O O   . GLU   A 1 112 ? 1.175   -29.226 35.233 1.00 30.12 ? 804  GLU   A O   1 
ATOM   794  C CB  . GLU   A 1 112 ? 3.067   -29.777 32.854 1.00 32.02 ? 804  GLU   A CB  1 
ATOM   795  C CG  . GLU   A 1 112 ? 3.316   -31.074 32.091 1.00 38.71 ? 804  GLU   A CG  1 
ATOM   796  C CD  . GLU   A 1 112 ? 4.611   -31.239 31.315 1.00 48.17 ? 804  GLU   A CD  1 
ATOM   797  O OE1 . GLU   A 1 112 ? 5.689   -31.291 31.949 1.00 50.85 ? 804  GLU   A OE1 1 
ATOM   798  O OE2 . GLU   A 1 112 ? 4.544   -31.355 30.068 1.00 51.08 ? 804  GLU   A OE2 1 
ATOM   799  N N   . HIS   A 1 113 ? 0.766   -27.391 34.048 1.00 30.45 ? 805  HIS   A N   1 
ATOM   800  C CA  . HIS   A 1 113 ? 0.285   -26.602 35.177 1.00 32.19 ? 805  HIS   A CA  1 
ATOM   801  C C   . HIS   A 1 113 ? -1.140  -26.104 34.889 1.00 34.38 ? 805  HIS   A C   1 
ATOM   802  O O   . HIS   A 1 113 ? -1.493  -25.005 35.302 1.00 34.35 ? 805  HIS   A O   1 
ATOM   803  C CB  . HIS   A 1 113 ? 1.206   -25.407 35.435 1.00 33.24 ? 805  HIS   A CB  1 
ATOM   804  C CG  . HIS   A 1 113 ? 2.500   -25.744 36.104 1.00 35.20 ? 805  HIS   A CG  1 
ATOM   805  N ND1 . HIS   A 1 113 ? 2.649   -25.639 37.478 1.00 36.93 ? 805  HIS   A ND1 1 
ATOM   806  C CD2 . HIS   A 1 113 ? 3.675   -26.138 35.563 1.00 36.15 ? 805  HIS   A CD2 1 
ATOM   807  C CE1 . HIS   A 1 113 ? 3.899   -25.991 37.727 1.00 37.38 ? 805  HIS   A CE1 1 
ATOM   808  N NE2 . HIS   A 1 113 ? 4.552   -26.308 36.607 1.00 37.30 ? 805  HIS   A NE2 1 
ATOM   809  N N   . LYS   A 1 114 ? -1.956  -26.916 34.155 1.00 36.17 ? 806  LYS   A N   1 
ATOM   810  C CA  . LYS   A 1 114 ? -3.354  -26.651 33.780 1.00 38.17 ? 806  LYS   A CA  1 
ATOM   811  C C   . LYS   A 1 114 ? -4.150  -26.217 35.015 1.00 39.93 ? 806  LYS   A C   1 
ATOM   812  O O   . LYS   A 1 114 ? -4.061  -26.856 36.080 1.00 39.97 ? 806  LYS   A O   1 
ATOM   813  C CB  . LYS   A 1 114 ? -3.997  -27.918 33.160 1.00 40.14 ? 806  LYS   A CB  1 
ATOM   814  C CG  . LYS   A 1 114 ? -4.747  -27.700 31.842 1.00 44.68 ? 806  LYS   A CG  1 
ATOM   815  C CD  . LYS   A 1 114 ? -6.135  -27.084 32.064 1.00 49.86 ? 806  LYS   A CD  1 
ATOM   816  C CE  . LYS   A 1 114 ? -6.973  -26.894 30.811 1.00 53.43 ? 806  LYS   A CE  1 
ATOM   817  N NZ  . LYS   A 1 114 ? -8.222  -26.117 31.076 1.00 54.57 ? 806  LYS   A NZ  1 
ATOM   818  N N   . ASP   A 1 115 ? -4.855  -25.073 34.881 1.00 40.77 ? 807  ASP   A N   1 
ATOM   819  C CA  . ASP   A 1 115 ? -5.676  -24.460 35.930 1.00 41.58 ? 807  ASP   A CA  1 
ATOM   820  C C   . ASP   A 1 115 ? -4.913  -24.239 37.249 1.00 41.53 ? 807  ASP   A C   1 
ATOM   821  O O   . ASP   A 1 115 ? -5.522  -24.212 38.318 1.00 41.74 ? 807  ASP   A O   1 
ATOM   822  C CB  . ASP   A 1 115 ? -6.979  -25.249 36.150 1.00 43.71 ? 807  ASP   A CB  1 
ATOM   823  C CG  . ASP   A 1 115 ? -7.681  -25.593 34.853 1.00 48.96 ? 807  ASP   A CG  1 
ATOM   824  O OD1 . ASP   A 1 115 ? -7.736  -24.720 33.959 1.00 49.52 ? 807  ASP   A OD1 1 
ATOM   825  O OD2 . ASP   A 1 115 ? -8.154  -26.745 34.721 1.00 51.46 ? 807  ASP   A OD2 1 
ATOM   826  N N   . ASN   A 1 116 ? -3.583  -24.100 37.172 1.00 40.82 ? 808  ASN   A N   1 
ATOM   827  C CA  . ASN   A 1 116 ? -2.777  -23.847 38.361 1.00 40.15 ? 808  ASN   A CA  1 
ATOM   828  C C   . ASN   A 1 116 ? -1.779  -22.704 38.145 1.00 38.16 ? 808  ASN   A C   1 
ATOM   829  O O   . ASN   A 1 116 ? -0.724  -22.677 38.767 1.00 38.76 ? 808  ASN   A O   1 
ATOM   830  C CB  . ASN   A 1 116 ? -2.081  -25.108 38.842 1.00 42.02 ? 808  ASN   A CB  1 
ATOM   831  C CG  . ASN   A 1 116 ? -1.702  -25.026 40.300 1.00 46.28 ? 808  ASN   A CG  1 
ATOM   832  O OD1 . ASN   A 1 116 ? -0.524  -25.116 40.671 1.00 46.99 ? 808  ASN   A OD1 1 
ATOM   833  N ND2 . ASN   A 1 116 ? -2.698  -24.821 41.157 1.00 47.54 ? 808  ASN   A ND2 1 
ATOM   834  N N   . ILE   A 1 117 ? -2.119  -21.747 37.286 1.00 35.70 ? 809  ILE   A N   1 
ATOM   835  C CA  . ILE   A 1 117 ? -1.238  -20.620 36.997 1.00 33.80 ? 809  ILE   A CA  1 
ATOM   836  C C   . ILE   A 1 117 ? -1.940  -19.344 37.367 1.00 31.65 ? 809  ILE   A C   1 
ATOM   837  O O   . ILE   A 1 117 ? -3.084  -19.158 36.997 1.00 31.44 ? 809  ILE   A O   1 
ATOM   838  C CB  . ILE   A 1 117 ? -0.814  -20.653 35.507 1.00 33.87 ? 809  ILE   A CB  1 
ATOM   839  C CG1 . ILE   A 1 117 ? -0.072  -21.970 35.209 1.00 34.43 ? 809  ILE   A CG1 1 
ATOM   840  C CG2 . ILE   A 1 117 ? 0.032   -19.423 35.137 1.00 34.20 ? 809  ILE   A CG2 1 
ATOM   841  C CD1 . ILE   A 1 117 ? 0.158   -22.243 33.851 1.00 35.57 ? 809  ILE   A CD1 1 
ATOM   842  N N   . GLY   A 1 118 ? -1.271  -18.491 38.122 1.00 30.11 ? 810  GLY   A N   1 
ATOM   843  C CA  . GLY   A 1 118 ? -1.855  -17.235 38.549 1.00 29.10 ? 810  GLY   A CA  1 
ATOM   844  C C   . GLY   A 1 118 ? -2.050  -16.245 37.426 1.00 28.04 ? 810  GLY   A C   1 
ATOM   845  O O   . GLY   A 1 118 ? -1.457  -16.381 36.357 1.00 28.42 ? 810  GLY   A O   1 
ATOM   846  N N   . SER   A 1 119 ? -2.875  -15.228 37.665 1.00 26.44 ? 811  SER   A N   1 
ATOM   847  C CA  . SER   A 1 119 ? -3.105  -14.158 36.710 1.00 25.27 ? 811  SER   A CA  1 
ATOM   848  C C   . SER   A 1 119 ? -1.847  -13.299 36.521 1.00 24.32 ? 811  SER   A C   1 
ATOM   849  O O   . SER   A 1 119 ? -1.628  -12.777 35.425 1.00 24.64 ? 811  SER   A O   1 
ATOM   850  C CB  . SER   A 1 119 ? -4.231  -13.265 37.193 1.00 26.10 ? 811  SER   A CB  1 
ATOM   851  O OG  . SER   A 1 119 ? -3.893  -12.772 38.479 1.00 28.17 ? 811  SER   A OG  1 
ATOM   852  N N   . GLN   A 1 120 ? -1.039  -13.127 37.572 1.00 23.36 ? 812  GLN   A N   1 
ATOM   853  C CA  . GLN   A 1 120 ? 0.172   -12.309 37.453 1.00 23.09 ? 812  GLN   A CA  1 
ATOM   854  C C   . GLN   A 1 120 ? 1.156   -12.907 36.443 1.00 22.37 ? 812  GLN   A C   1 
ATOM   855  O O   . GLN   A 1 120 ? 1.748   -12.172 35.674 1.00 22.46 ? 812  GLN   A O   1 
ATOM   856  C CB  . GLN   A 1 120 ? 0.826   -12.032 38.808 1.00 24.13 ? 812  GLN   A CB  1 
ATOM   857  C CG  . GLN   A 1 120 ? -0.137  -11.486 39.836 1.00 28.79 ? 812  GLN   A CG  1 
ATOM   858  C CD  . GLN   A 1 120 ? 0.541   -10.551 40.798 1.00 35.96 ? 812  GLN   A CD  1 
ATOM   859  O OE1 . GLN   A 1 120 ? 0.588   -10.784 42.016 1.00 36.32 ? 812  GLN   A OE1 1 
ATOM   860  N NE2 . GLN   A 1 120 ? 1.086   -9.463  40.259 1.00 38.63 ? 812  GLN   A NE2 1 
ATOM   861  N N   . TYR   A 1 121 ? 1.283   -14.232 36.411 1.00 21.37 ? 813  TYR   A N   1 
ATOM   862  C CA  . TYR   A 1 121 ? 2.157   -14.930 35.482 1.00 20.81 ? 813  TYR   A CA  1 
ATOM   863  C C   . TYR   A 1 121 ? 1.726   -14.770 34.022 1.00 19.61 ? 813  TYR   A C   1 
ATOM   864  O O   . TYR   A 1 121 ? 2.534   -14.372 33.186 1.00 19.02 ? 813  TYR   A O   1 
ATOM   865  C CB  . TYR   A 1 121 ? 2.209   -16.412 35.837 1.00 21.10 ? 813  TYR   A CB  1 
ATOM   866  C CG  . TYR   A 1 121 ? 3.116   -16.705 36.999 1.00 22.51 ? 813  TYR   A CG  1 
ATOM   867  C CD1 . TYR   A 1 121 ? 4.476   -16.882 36.814 1.00 23.28 ? 813  TYR   A CD1 1 
ATOM   868  C CD2 . TYR   A 1 121 ? 2.613   -16.804 38.290 1.00 24.43 ? 813  TYR   A CD2 1 
ATOM   869  C CE1 . TYR   A 1 121 ? 5.307   -17.196 37.871 1.00 24.82 ? 813  TYR   A CE1 1 
ATOM   870  C CE2 . TYR   A 1 121 ? 3.440   -17.097 39.363 1.00 25.61 ? 813  TYR   A CE2 1 
ATOM   871  C CZ  . TYR   A 1 121 ? 4.787   -17.296 39.147 1.00 26.64 ? 813  TYR   A CZ  1 
ATOM   872  O OH  . TYR   A 1 121 ? 5.604   -17.609 40.199 1.00 29.66 ? 813  TYR   A OH  1 
ATOM   873  N N   . LEU   A 1 122 ? 0.446   -15.062 33.724 1.00 18.78 ? 814  LEU   A N   1 
ATOM   874  C CA  . LEU   A 1 122 ? -0.114  -14.963 32.387 1.00 18.30 ? 814  LEU   A CA  1 
ATOM   875  C C   . LEU   A 1 122 ? 0.084   -13.561 31.802 1.00 17.01 ? 814  LEU   A C   1 
ATOM   876  O O   . LEU   A 1 122 ? 0.777   -13.425 30.796 1.00 16.69 ? 814  LEU   A O   1 
ATOM   877  C CB  . LEU   A 1 122 ? -1.587  -15.394 32.405 1.00 18.77 ? 814  LEU   A CB  1 
ATOM   878  C CG  . LEU   A 1 122 ? -1.791  -16.833 32.866 1.00 20.53 ? 814  LEU   A CG  1 
ATOM   879  C CD1 . LEU   A 1 122 ? -3.234  -17.109 33.258 1.00 21.07 ? 814  LEU   A CD1 1 
ATOM   880  C CD2 . LEU   A 1 122 ? -1.285  -17.807 31.834 1.00 21.28 ? 814  LEU   A CD2 1 
ATOM   881  N N   . LEU   A 1 123 ? -0.373  -12.531 32.506 1.00 15.89 ? 815  LEU   A N   1 
ATOM   882  C CA  . LEU   A 1 123 ? -0.210  -11.145 32.057 1.00 15.55 ? 815  LEU   A CA  1 
ATOM   883  C C   . LEU   A 1 123 ? 1.267   -10.732 31.865 1.00 16.06 ? 815  LEU   A C   1 
ATOM   884  O O   . LEU   A 1 123 ? 1.606   -10.160 30.823 1.00 16.13 ? 815  LEU   A O   1 
ATOM   885  C CB  . LEU   A 1 123 ? -0.962  -10.199 33.001 1.00 14.78 ? 815  LEU   A CB  1 
ATOM   886  C CG  . LEU   A 1 123 ? -2.474  -10.456 32.952 1.00 14.69 ? 815  LEU   A CG  1 
ATOM   887  C CD1 . LEU   A 1 123 ? -3.194  -9.943  34.192 1.00 14.46 ? 815  LEU   A CD1 1 
ATOM   888  C CD2 . LEU   A 1 123 ? -3.076  -9.983  31.631 1.00 14.10 ? 815  LEU   A CD2 1 
ATOM   889  N N   . ASN   A 1 124 ? 2.155   -11.124 32.797 1.00 15.82 ? 816  ASN   A N   1 
ATOM   890  C CA  . ASN   A 1 124 ? 3.563   -10.824 32.662 1.00 16.81 ? 816  ASN   A CA  1 
ATOM   891  C C   . ASN   A 1 124 ? 4.204   -11.543 31.486 1.00 17.58 ? 816  ASN   A C   1 
ATOM   892  O O   . ASN   A 1 124 ? 5.048   -10.953 30.818 1.00 18.04 ? 816  ASN   A O   1 
ATOM   893  C CB  . ASN   A 1 124 ? 4.309   -11.090 33.957 1.00 18.18 ? 816  ASN   A CB  1 
ATOM   894  C CG  . ASN   A 1 124 ? 4.263   -9.900  34.850 1.00 21.08 ? 816  ASN   A CG  1 
ATOM   895  O OD1 . ASN   A 1 124 ? 5.047   -8.975  34.691 1.00 21.89 ? 816  ASN   A OD1 1 
ATOM   896  N ND2 . ASN   A 1 124 ? 3.300   -9.869  35.769 1.00 22.31 ? 816  ASN   A ND2 1 
ATOM   897  N N   . TRP   A 1 125 ? 3.794   -12.787 31.202 1.00 17.43 ? 817  TRP   A N   1 
ATOM   898  C CA  . TRP   A 1 125 ? 4.315   -13.510 30.046 1.00 18.33 ? 817  TRP   A CA  1 
ATOM   899  C C   . TRP   A 1 125 ? 3.877   -12.803 28.758 1.00 17.35 ? 817  TRP   A C   1 
ATOM   900  O O   . TRP   A 1 125 ? 4.685   -12.631 27.851 1.00 17.80 ? 817  TRP   A O   1 
ATOM   901  C CB  . TRP   A 1 125 ? 3.810   -14.955 30.019 1.00 19.25 ? 817  TRP   A CB  1 
ATOM   902  C CG  . TRP   A 1 125 ? 4.323   -15.832 31.115 1.00 21.02 ? 817  TRP   A CG  1 
ATOM   903  C CD1 . TRP   A 1 125 ? 5.468   -15.674 31.846 1.00 22.60 ? 817  TRP   A CD1 1 
ATOM   904  C CD2 . TRP   A 1 125 ? 3.737   -17.061 31.545 1.00 21.54 ? 817  TRP   A CD2 1 
ATOM   905  N NE1 . TRP   A 1 125 ? 5.599   -16.709 32.747 1.00 23.10 ? 817  TRP   A NE1 1 
ATOM   906  C CE2 . TRP   A 1 125 ? 4.554   -17.583 32.572 1.00 22.79 ? 817  TRP   A CE2 1 
ATOM   907  C CE3 . TRP   A 1 125 ? 2.598   -17.769 31.166 1.00 22.12 ? 817  TRP   A CE3 1 
ATOM   908  C CZ2 . TRP   A 1 125 ? 4.255   -18.777 33.227 1.00 23.56 ? 817  TRP   A CZ2 1 
ATOM   909  C CZ3 . TRP   A 1 125 ? 2.292   -18.935 31.834 1.00 23.45 ? 817  TRP   A CZ3 1 
ATOM   910  C CH2 . TRP   A 1 125 ? 3.117   -19.433 32.846 1.00 23.67 ? 817  TRP   A CH2 1 
ATOM   911  N N   . CYS   A 1 126 ? 2.609   -12.364 28.699 1.00 15.75 ? 818  CYS   A N   1 
ATOM   912  C CA  . CYS   A 1 126 ? 2.064   -11.614 27.562 1.00 14.70 ? 818  CYS   A CA  1 
ATOM   913  C C   . CYS   A 1 126 ? 2.873   -10.331 27.340 1.00 14.30 ? 818  CYS   A C   1 
ATOM   914  O O   . CYS   A 1 126 ? 3.184   -10.008 26.199 1.00 13.78 ? 818  CYS   A O   1 
ATOM   915  C CB  . CYS   A 1 126 ? 0.573   -11.318 27.765 1.00 13.76 ? 818  CYS   A CB  1 
ATOM   916  S SG  . CYS   A 1 126 ? -0.478  -12.799 27.715 1.00 13.44 ? 818  CYS   A SG  1 
ATOM   917  N N   . VAL   A 1 127 ? 3.278   -9.658  28.441 1.00 14.41 ? 819  VAL   A N   1 
ATOM   918  C CA  . VAL   A 1 127 ? 4.104   -8.439  28.424 1.00 14.85 ? 819  VAL   A CA  1 
ATOM   919  C C   . VAL   A 1 127 ? 5.474   -8.749  27.800 1.00 15.83 ? 819  VAL   A C   1 
ATOM   920  O O   . VAL   A 1 127 ? 5.904   -8.033  26.902 1.00 17.44 ? 819  VAL   A O   1 
ATOM   921  C CB  . VAL   A 1 127 ? 4.247   -7.869  29.882 1.00 14.88 ? 819  VAL   A CB  1 
ATOM   922  C CG1 . VAL   A 1 127 ? 5.438   -6.935  30.033 1.00 14.77 ? 819  VAL   A CG1 1 
ATOM   923  C CG2 . VAL   A 1 127 ? 2.976   -7.181  30.336 1.00 15.03 ? 819  VAL   A CG2 1 
ATOM   924  N N   . GLN   A 1 128 ? 6.153   -9.796  28.303 1.00 14.64 ? 820  GLN   A N   1 
ATOM   925  C CA  . GLN   A 1 128 ? 7.492   -10.209 27.926 1.00 14.47 ? 820  GLN   A CA  1 
ATOM   926  C C   . GLN   A 1 128 ? 7.563   -10.675 26.479 1.00 14.57 ? 820  GLN   A C   1 
ATOM   927  O O   . GLN   A 1 128 ? 8.505   -10.317 25.747 1.00 14.45 ? 820  GLN   A O   1 
ATOM   928  C CB  . GLN   A 1 128 ? 7.972   -11.325 28.871 1.00 15.32 ? 820  GLN   A CB  1 
ATOM   929  C CG  . GLN   A 1 128 ? 8.259   -10.846 30.286 1.00 16.74 ? 820  GLN   A CG  1 
ATOM   930  C CD  . GLN   A 1 128 ? 8.800   -11.949 31.154 1.00 19.93 ? 820  GLN   A CD  1 
ATOM   931  O OE1 . GLN   A 1 128 ? 9.457   -12.868 30.685 1.00 21.04 ? 820  GLN   A OE1 1 
ATOM   932  N NE2 . GLN   A 1 128 ? 8.566   -11.861 32.455 1.00 20.63 ? 820  GLN   A NE2 1 
ATOM   933  N N   . ILE   A 1 129 ? 6.525   -11.405 26.035 1.00 13.63 ? 821  ILE   A N   1 
ATOM   934  C CA  . ILE   A 1 129 ? 6.460   -11.871 24.654 1.00 13.35 ? 821  ILE   A CA  1 
ATOM   935  C C   . ILE   A 1 129 ? 6.345   -10.680 23.712 1.00 14.50 ? 821  ILE   A C   1 
ATOM   936  O O   . ILE   A 1 129 ? 7.024   -10.648 22.681 1.00 15.48 ? 821  ILE   A O   1 
ATOM   937  C CB  . ILE   A 1 129 ? 5.339   -12.942 24.452 1.00 12.73 ? 821  ILE   A CB  1 
ATOM   938  C CG1 . ILE   A 1 129 ? 5.622   -14.191 25.295 1.00 13.54 ? 821  ILE   A CG1 1 
ATOM   939  C CG2 . ILE   A 1 129 ? 5.239   -13.353 23.003 1.00 12.30 ? 821  ILE   A CG2 1 
ATOM   940  C CD1 . ILE   A 1 129 ? 4.373   -15.236 25.390 1.00 15.25 ? 821  ILE   A CD1 1 
ATOM   941  N N   . ALA   A 1 130 ? 5.554   -9.666  24.106 1.00 14.54 ? 822  ALA   A N   1 
ATOM   942  C CA  . ALA   A 1 130 ? 5.388   -8.409  23.368 1.00 14.69 ? 822  ALA   A CA  1 
ATOM   943  C C   . ALA   A 1 130 ? 6.698   -7.602  23.321 1.00 14.77 ? 822  ALA   A C   1 
ATOM   944  O O   . ALA   A 1 130 ? 7.011   -7.004  22.292 1.00 14.74 ? 822  ALA   A O   1 
ATOM   945  C CB  . ALA   A 1 130 ? 4.294   -7.577  24.002 1.00 14.33 ? 822  ALA   A CB  1 
ATOM   946  N N   . LYS   A 1 131 ? 7.481   -7.617  24.406 1.00 14.63 ? 823  LYS   A N   1 
ATOM   947  C CA  . LYS   A 1 131 ? 8.773   -6.918  24.421 1.00 14.12 ? 823  LYS   A CA  1 
ATOM   948  C C   . LYS   A 1 131 ? 9.800   -7.618  23.508 1.00 14.49 ? 823  LYS   A C   1 
ATOM   949  O O   . LYS   A 1 131 ? 10.666  -6.952  22.945 1.00 14.66 ? 823  LYS   A O   1 
ATOM   950  C CB  . LYS   A 1 131 ? 9.317   -6.800  25.836 1.00 14.73 ? 823  LYS   A CB  1 
ATOM   951  C CG  . LYS   A 1 131 ? 8.549   -5.863  26.760 1.00 17.80 ? 823  LYS   A CG  1 
ATOM   952  C CD  . LYS   A 1 131 ? 9.037   -6.030  28.211 1.00 21.05 ? 823  LYS   A CD  1 
ATOM   953  C CE  . LYS   A 1 131 ? 8.587   -4.911  29.110 1.00 26.03 ? 823  LYS   A CE  1 
ATOM   954  N NZ  . LYS   A 1 131 ? 9.077   -5.077  30.514 1.00 29.38 ? 823  LYS   A NZ  1 
ATOM   955  N N   . GLY   A 1 132 ? 9.729   -8.953  23.406 1.00 14.15 ? 824  GLY   A N   1 
ATOM   956  C CA  . GLY   A 1 132 ? 10.637  -9.709  22.547 1.00 13.78 ? 824  GLY   A CA  1 
ATOM   957  C C   . GLY   A 1 132 ? 10.359  -9.446  21.072 1.00 13.68 ? 824  GLY   A C   1 
ATOM   958  O O   . GLY   A 1 132 ? 11.272  -9.192  20.274 1.00 13.92 ? 824  GLY   A O   1 
ATOM   959  N N   . MET   A 1 133 ? 9.076   -9.454  20.717 1.00 13.58 ? 825  MET   A N   1 
ATOM   960  C CA  . MET   A 1 133 ? 8.621   -9.206  19.363 1.00 13.20 ? 825  MET   A CA  1 
ATOM   961  C C   . MET   A 1 133 ? 8.847   -7.774  18.993 1.00 13.80 ? 825  MET   A C   1 
ATOM   962  O O   . MET   A 1 133 ? 9.243   -7.512  17.867 1.00 14.00 ? 825  MET   A O   1 
ATOM   963  C CB  . MET   A 1 133 ? 7.144   -9.559  19.211 1.00 12.71 ? 825  MET   A CB  1 
ATOM   964  C CG  . MET   A 1 133 ? 6.827   -11.031 19.393 1.00 14.46 ? 825  MET   A CG  1 
ATOM   965  S SD  . MET   A 1 133 ? 7.760   -12.146 18.313 1.00 16.74 ? 825  MET   A SD  1 
ATOM   966  C CE  . MET   A 1 133 ? 7.078   -11.716 16.747 1.00 9.37  ? 825  MET   A CE  1 
ATOM   967  N N   . ASN   A 1 134 ? 8.598   -6.827  19.918 1.00 14.13 ? 826  ASN   A N   1 
ATOM   968  C CA  . ASN   A 1 134 ? 8.840   -5.402  19.685 1.00 14.63 ? 826  ASN   A CA  1 
ATOM   969  C C   . ASN   A 1 134 ? 10.321  -5.174  19.360 1.00 15.30 ? 826  ASN   A C   1 
ATOM   970  O O   . ASN   A 1 134 ? 10.631  -4.374  18.492 1.00 15.69 ? 826  ASN   A O   1 
ATOM   971  C CB  . ASN   A 1 134 ? 8.461   -4.606  20.918 1.00 16.39 ? 826  ASN   A CB  1 
ATOM   972  C CG  . ASN   A 1 134 ? 8.589   -3.119  20.735 1.00 21.39 ? 826  ASN   A CG  1 
ATOM   973  O OD1 . ASN   A 1 134 ? 7.839   -2.513  19.984 1.00 23.39 ? 826  ASN   A OD1 1 
ATOM   974  N ND2 . ASN   A 1 134 ? 9.554   -2.503  21.409 1.00 22.62 ? 826  ASN   A ND2 1 
ATOM   975  N N   . TYR   A 1 135 ? 11.236  -5.909  20.018 1.00 15.53 ? 827  TYR   A N   1 
ATOM   976  C CA  . TYR   A 1 135 ? 12.657  -5.814  19.722 1.00 16.12 ? 827  TYR   A CA  1 
ATOM   977  C C   . TYR   A 1 135 ? 12.911  -6.283  18.284 1.00 15.88 ? 827  TYR   A C   1 
ATOM   978  O O   . TYR   A 1 135 ? 13.687  -5.664  17.562 1.00 16.30 ? 827  TYR   A O   1 
ATOM   979  C CB  . TYR   A 1 135 ? 13.498  -6.653  20.717 1.00 16.99 ? 827  TYR   A CB  1 
ATOM   980  C CG  . TYR   A 1 135 ? 14.940  -6.852  20.281 1.00 18.06 ? 827  TYR   A CG  1 
ATOM   981  C CD1 . TYR   A 1 135 ? 15.874  -5.828  20.402 1.00 18.66 ? 827  TYR   A CD1 1 
ATOM   982  C CD2 . TYR   A 1 135 ? 15.358  -8.049  19.705 1.00 18.57 ? 827  TYR   A CD2 1 
ATOM   983  C CE1 . TYR   A 1 135 ? 17.184  -5.990  19.966 1.00 19.32 ? 827  TYR   A CE1 1 
ATOM   984  C CE2 . TYR   A 1 135 ? 16.672  -8.225  19.277 1.00 19.47 ? 827  TYR   A CE2 1 
ATOM   985  C CZ  . TYR   A 1 135 ? 17.575  -7.180  19.379 1.00 20.49 ? 827  TYR   A CZ  1 
ATOM   986  O OH  . TYR   A 1 135 ? 18.884  -7.347  18.963 1.00 21.85 ? 827  TYR   A OH  1 
ATOM   987  N N   . LEU   A 1 136 ? 12.279  -7.384  17.883 1.00 15.27 ? 828  LEU   A N   1 
ATOM   988  C CA  . LEU   A 1 136 ? 12.431  -7.914  16.543 1.00 15.65 ? 828  LEU   A CA  1 
ATOM   989  C C   . LEU   A 1 136 ? 11.933  -6.932  15.507 1.00 17.31 ? 828  LEU   A C   1 
ATOM   990  O O   . LEU   A 1 136 ? 12.630  -6.717  14.528 1.00 17.68 ? 828  LEU   A O   1 
ATOM   991  C CB  . LEU   A 1 136 ? 11.761  -9.285  16.400 1.00 14.67 ? 828  LEU   A CB  1 
ATOM   992  C CG  . LEU   A 1 136 ? 12.343  -10.394 17.260 1.00 14.74 ? 828  LEU   A CG  1 
ATOM   993  C CD1 . LEU   A 1 136 ? 11.615  -11.717 17.001 1.00 14.61 ? 828  LEU   A CD1 1 
ATOM   994  C CD2 . LEU   A 1 136 ? 13.823  -10.590 16.981 1.00 14.89 ? 828  LEU   A CD2 1 
ATOM   995  N N   . GLU   A 1 137 ? 10.790  -6.272  15.760 1.00 18.24 ? 829  GLU   A N   1 
ATOM   996  C CA  . GLU   A 1 137 ? 10.219  -5.235  14.875 1.00 19.40 ? 829  GLU   A CA  1 
ATOM   997  C C   . GLU   A 1 137 ? 11.160  -4.008  14.769 1.00 20.77 ? 829  GLU   A C   1 
ATOM   998  O O   . GLU   A 1 137 ? 11.407  -3.538  13.660 1.00 21.56 ? 829  GLU   A O   1 
ATOM   999  C CB  . GLU   A 1 137 ? 8.805   -4.815  15.334 1.00 21.07 ? 829  GLU   A CB  1 
ATOM   1000 C CG  . GLU   A 1 137 ? 8.181   -3.723  14.470 1.00 24.29 ? 829  GLU   A CG  1 
ATOM   1001 C CD  . GLU   A 1 137 ? 6.702   -3.425  14.660 1.00 28.07 ? 829  GLU   A CD  1 
ATOM   1002 O OE1 . GLU   A 1 137 ? 6.151   -3.767  15.732 1.00 29.37 ? 829  GLU   A OE1 1 
ATOM   1003 O OE2 . GLU   A 1 137 ? 6.094   -2.833  13.739 1.00 28.34 ? 829  GLU   A OE2 1 
ATOM   1004 N N   . ASP   A 1 138 ? 11.767  -3.562  15.877 1.00 20.78 ? 830  ASP   A N   1 
ATOM   1005 C CA  . ASP   A 1 138 ? 12.752  -2.468  15.830 1.00 21.51 ? 830  ASP   A CA  1 
ATOM   1006 C C   . ASP   A 1 138 ? 13.939  -2.809  14.932 1.00 22.25 ? 830  ASP   A C   1 
ATOM   1007 O O   . ASP   A 1 138 ? 14.514  -1.918  14.318 1.00 22.52 ? 830  ASP   A O   1 
ATOM   1008 C CB  . ASP   A 1 138 ? 13.268  -2.125  17.234 1.00 22.24 ? 830  ASP   A CB  1 
ATOM   1009 C CG  . ASP   A 1 138 ? 12.239  -1.419  18.087 1.00 27.63 ? 830  ASP   A CG  1 
ATOM   1010 O OD1 . ASP   A 1 138 ? 11.326  -0.792  17.517 1.00 28.82 ? 830  ASP   A OD1 1 
ATOM   1011 O OD2 . ASP   A 1 138 ? 12.357  -1.476  19.334 1.00 30.70 ? 830  ASP   A OD2 1 
ATOM   1012 N N   . ARG   A 1 139 ? 14.326  -4.099  14.884 1.00 22.50 ? 831  ARG   A N   1 
ATOM   1013 C CA  . ARG   A 1 139 ? 15.423  -4.597  14.038 1.00 22.70 ? 831  ARG   A CA  1 
ATOM   1014 C C   . ARG   A 1 139 ? 14.955  -4.926  12.596 1.00 23.82 ? 831  ARG   A C   1 
ATOM   1015 O O   . ARG   A 1 139 ? 15.757  -5.411  11.805 1.00 24.68 ? 831  ARG   A O   1 
ATOM   1016 C CB  . ARG   A 1 139 ? 16.004  -5.882  14.645 1.00 22.76 ? 831  ARG   A CB  1 
ATOM   1017 C CG  . ARG   A 1 139 ? 16.852  -5.704  15.887 1.00 24.32 ? 831  ARG   A CG  1 
ATOM   1018 C CD  . ARG   A 1 139 ? 18.274  -5.286  15.570 1.00 27.21 ? 831  ARG   A CD  1 
ATOM   1019 N NE  . ARG   A 1 139 ? 18.961  -6.192  14.643 1.00 29.13 ? 831  ARG   A NE  1 
ATOM   1020 C CZ  . ARG   A 1 139 ? 19.727  -7.212  15.019 1.00 29.42 ? 831  ARG   A CZ  1 
ATOM   1021 N NH1 . ARG   A 1 139 ? 19.884  -7.496  16.308 1.00 27.64 ? 831  ARG   A NH1 1 
ATOM   1022 N NH2 . ARG   A 1 139 ? 20.327  -7.968  14.109 1.00 28.38 ? 831  ARG   A NH2 1 
ATOM   1023 N N   . ARG   A 1 140 ? 13.662  -4.726  12.288 1.00 24.08 ? 832  ARG   A N   1 
ATOM   1024 C CA  . ARG   A 1 140 ? 12.994  -5.050  11.033 1.00 24.62 ? 832  ARG   A CA  1 
ATOM   1025 C C   . ARG   A 1 140 ? 13.062  -6.545  10.749 1.00 23.31 ? 832  ARG   A C   1 
ATOM   1026 O O   . ARG   A 1 140 ? 13.284  -6.953  9.615  1.00 23.82 ? 832  ARG   A O   1 
ATOM   1027 C CB  . ARG   A 1 140 ? 13.508  -4.188  9.869  1.00 27.46 ? 832  ARG   A CB  1 
ATOM   1028 C CG  . ARG   A 1 140 ? 13.272  -2.694  10.125 1.00 33.02 ? 832  ARG   A CG  1 
ATOM   1029 C CD  . ARG   A 1 140 ? 14.073  -1.760  9.202  1.00 38.54 ? 832  ARG   A CD  1 
ATOM   1030 N NE  . ARG   A 1 140 ? 15.504  -2.083  9.110  1.00 42.57 ? 832  ARG   A NE  1 
ATOM   1031 C CZ  . ARG   A 1 140 ? 16.398  -1.832  10.065 1.00 45.96 ? 832  ARG   A CZ  1 
ATOM   1032 N NH1 . ARG   A 1 140 ? 16.016  -1.286  11.215 1.00 46.26 ? 832  ARG   A NH1 1 
ATOM   1033 N NH2 . ARG   A 1 140 ? 17.673  -2.162  9.892  1.00 46.12 ? 832  ARG   A NH2 1 
ATOM   1034 N N   . LEU   A 1 141 ? 12.896  -7.359  11.783 1.00 21.83 ? 833  LEU   A N   1 
ATOM   1035 C CA  . LEU   A 1 141 ? 12.946  -8.810  11.640 1.00 21.68 ? 833  LEU   A CA  1 
ATOM   1036 C C   . LEU   A 1 141 ? 11.565  -9.411  11.862 1.00 21.22 ? 833  LEU   A C   1 
ATOM   1037 O O   . LEU   A 1 141 ? 10.885  -9.071  12.825 1.00 21.90 ? 833  LEU   A O   1 
ATOM   1038 C CB  . LEU   A 1 141 ? 13.941  -9.429  12.630 1.00 21.60 ? 833  LEU   A CB  1 
ATOM   1039 C CG  . LEU   A 1 141 ? 15.397  -8.992  12.484 1.00 23.04 ? 833  LEU   A CG  1 
ATOM   1040 C CD1 . LEU   A 1 141 ? 16.229  -9.424  13.684 1.00 23.29 ? 833  LEU   A CD1 1 
ATOM   1041 C CD2 . LEU   A 1 141 ? 16.003  -9.521  11.206 1.00 23.58 ? 833  LEU   A CD2 1 
ATOM   1042 N N   . VAL   A 1 142 ? 11.166  -10.323 10.988 1.00 19.75 ? 834  VAL   A N   1 
ATOM   1043 C CA  . VAL   A 1 142 ? 9.873   -10.977 11.097 1.00 18.88 ? 834  VAL   A CA  1 
ATOM   1044 C C   . VAL   A 1 142 ? 10.105  -12.402 11.573 1.00 18.44 ? 834  VAL   A C   1 
ATOM   1045 O O   . VAL   A 1 142 ? 10.918  -13.113 10.988 1.00 19.00 ? 834  VAL   A O   1 
ATOM   1046 C CB  . VAL   A 1 142 ? 9.115   -10.919 9.757  1.00 18.71 ? 834  VAL   A CB  1 
ATOM   1047 C CG1 . VAL   A 1 142 ? 7.771   -11.641 9.860  1.00 19.41 ? 834  VAL   A CG1 1 
ATOM   1048 C CG2 . VAL   A 1 142 ? 8.929   -9.471  9.312  1.00 18.22 ? 834  VAL   A CG2 1 
ATOM   1049 N N   . HIS   A 1 143 ? 9.446   -12.800 12.666 1.00 17.14 ? 835  HIS   A N   1 
ATOM   1050 C CA  . HIS   A 1 143 ? 9.648   -14.134 13.220 1.00 16.65 ? 835  HIS   A CA  1 
ATOM   1051 C C   . HIS   A 1 143 ? 9.032   -15.201 12.327 1.00 17.22 ? 835  HIS   A C   1 
ATOM   1052 O O   . HIS   A 1 143 ? 9.697   -16.181 12.015 1.00 17.02 ? 835  HIS   A O   1 
ATOM   1053 C CB  . HIS   A 1 143 ? 9.141   -14.224 14.671 1.00 15.66 ? 835  HIS   A CB  1 
ATOM   1054 C CG  . HIS   A 1 143 ? 9.490   -15.519 15.321 1.00 14.74 ? 835  HIS   A CG  1 
ATOM   1055 N ND1 . HIS   A 1 143 ? 8.876   -16.695 14.950 1.00 15.18 ? 835  HIS   A ND1 1 
ATOM   1056 C CD2 . HIS   A 1 143 ? 10.370  -15.783 16.310 1.00 15.07 ? 835  HIS   A CD2 1 
ATOM   1057 C CE1 . HIS   A 1 143 ? 9.424   -17.644 15.684 1.00 15.00 ? 835  HIS   A CE1 1 
ATOM   1058 N NE2 . HIS   A 1 143 ? 10.305  -17.143 16.538 1.00 15.62 ? 835  HIS   A NE2 1 
ATOM   1059 N N   . ARG   A 1 144 ? 7.759   -15.017 11.933 1.00 18.31 ? 836  ARG   A N   1 
ATOM   1060 C CA  . ARG   A 1 144 ? 7.028   -15.912 11.039 1.00 19.70 ? 836  ARG   A CA  1 
ATOM   1061 C C   . ARG   A 1 144 ? 6.473   -17.159 11.714 1.00 20.35 ? 836  ARG   A C   1 
ATOM   1062 O O   . ARG   A 1 144 ? 5.584   -17.786 11.150 1.00 21.65 ? 836  ARG   A O   1 
ATOM   1063 C CB  . ARG   A 1 144 ? 7.853   -16.315 9.795  1.00 21.83 ? 836  ARG   A CB  1 
ATOM   1064 C CG  . ARG   A 1 144 ? 8.162   -15.209 8.818  1.00 26.61 ? 836  ARG   A CG  1 
ATOM   1065 C CD  . ARG   A 1 144 ? 8.964   -15.760 7.644  1.00 32.71 ? 836  ARG   A CD  1 
ATOM   1066 N NE  . ARG   A 1 144 ? 9.245   -14.726 6.645  1.00 38.72 ? 836  ARG   A NE  1 
ATOM   1067 C CZ  . ARG   A 1 144 ? 10.270  -13.874 6.709  1.00 43.69 ? 836  ARG   A CZ  1 
ATOM   1068 N NH1 . ARG   A 1 144 ? 11.143  -13.944 7.712  1.00 43.70 ? 836  ARG   A NH1 1 
ATOM   1069 N NH2 . ARG   A 1 144 ? 10.425  -12.941 5.776  1.00 44.63 ? 836  ARG   A NH2 1 
ATOM   1070 N N   . ASP   A 1 145 ? 6.960   -17.516 12.899 1.00 19.41 ? 837  ASP   A N   1 
ATOM   1071 C CA  . ASP   A 1 145 ? 6.489   -18.694 13.600 1.00 19.11 ? 837  ASP   A CA  1 
ATOM   1072 C C   . ASP   A 1 145 ? 6.272   -18.507 15.129 1.00 18.30 ? 837  ASP   A C   1 
ATOM   1073 O O   . ASP   A 1 145 ? 6.726   -19.336 15.932 1.00 18.65 ? 837  ASP   A O   1 
ATOM   1074 C CB  . ASP   A 1 145 ? 7.417   -19.890 13.328 1.00 20.80 ? 837  ASP   A CB  1 
ATOM   1075 C CG  . ASP   A 1 145 ? 6.738   -21.240 13.468 1.00 25.42 ? 837  ASP   A CG  1 
ATOM   1076 O OD1 . ASP   A 1 145 ? 5.489   -21.270 13.689 1.00 24.89 ? 837  ASP   A OD1 1 
ATOM   1077 O OD2 . ASP   A 1 145 ? 7.441   -22.267 13.362 1.00 28.07 ? 837  ASP   A OD2 1 
ATOM   1078 N N   . LEU   A 1 146 ? 5.602   -17.430 15.521 1.00 16.79 ? 838  LEU   A N   1 
ATOM   1079 C CA  . LEU   A 1 146 ? 5.294   -17.205 16.932 1.00 16.15 ? 838  LEU   A CA  1 
ATOM   1080 C C   . LEU   A 1 146 ? 4.128   -18.137 17.296 1.00 16.04 ? 838  LEU   A C   1 
ATOM   1081 O O   . LEU   A 1 146 ? 3.132   -18.236 16.555 1.00 15.69 ? 838  LEU   A O   1 
ATOM   1082 C CB  . LEU   A 1 146 ? 4.925   -15.737 17.220 1.00 15.63 ? 838  LEU   A CB  1 
ATOM   1083 C CG  . LEU   A 1 146 ? 4.670   -15.417 18.696 1.00 16.36 ? 838  LEU   A CG  1 
ATOM   1084 C CD1 . LEU   A 1 146 ? 5.889   -15.708 19.557 1.00 16.07 ? 838  LEU   A CD1 1 
ATOM   1085 C CD2 . LEU   A 1 146 ? 4.336   -13.984 18.857 1.00 17.29 ? 838  LEU   A CD2 1 
ATOM   1086 N N   . ALA   A 1 147 ? 4.304   -18.873 18.387 1.00 15.27 ? 839  ALA   A N   1 
ATOM   1087 C CA  . ALA   A 1 147 ? 3.377   -19.860 18.940 1.00 15.48 ? 839  ALA   A CA  1 
ATOM   1088 C C   . ALA   A 1 147 ? 3.858   -20.182 20.350 1.00 16.01 ? 839  ALA   A C   1 
ATOM   1089 O O   . ALA   A 1 147 ? 5.030   -19.929 20.625 1.00 16.20 ? 839  ALA   A O   1 
ATOM   1090 C CB  . ALA   A 1 147 ? 3.394   -21.108 18.083 1.00 15.49 ? 839  ALA   A CB  1 
ATOM   1091 N N   . ALA   A 1 148 ? 3.005   -20.701 21.255 1.00 16.06 ? 840  ALA   A N   1 
ATOM   1092 C CA  . ALA   A 1 148 ? 3.479   -21.003 22.620 1.00 17.64 ? 840  ALA   A CA  1 
ATOM   1093 C C   . ALA   A 1 148 ? 4.536   -22.150 22.662 1.00 18.46 ? 840  ALA   A C   1 
ATOM   1094 O O   . ALA   A 1 148 ? 5.251   -22.293 23.648 1.00 18.23 ? 840  ALA   A O   1 
ATOM   1095 C CB  . ALA   A 1 148 ? 2.314   -21.278 23.571 1.00 17.99 ? 840  ALA   A CB  1 
ATOM   1096 N N   . ARG   A 1 149 ? 4.640   -22.946 21.584 1.00 19.01 ? 841  ARG   A N   1 
ATOM   1097 C CA  . ARG   A 1 149 ? 5.686   -23.971 21.492 1.00 19.67 ? 841  ARG   A CA  1 
ATOM   1098 C C   . ARG   A 1 149 ? 7.086   -23.305 21.290 1.00 19.15 ? 841  ARG   A C   1 
ATOM   1099 O O   . ARG   A 1 149 ? 8.117   -23.913 21.617 1.00 18.73 ? 841  ARG   A O   1 
ATOM   1100 C CB  . ARG   A 1 149 ? 5.391   -24.964 20.336 1.00 21.10 ? 841  ARG   A CB  1 
ATOM   1101 C CG  . ARG   A 1 149 ? 5.372   -24.304 18.956 1.00 23.64 ? 841  ARG   A CG  1 
ATOM   1102 C CD  . ARG   A 1 149 ? 5.199   -25.316 17.861 1.00 26.99 ? 841  ARG   A CD  1 
ATOM   1103 N NE  . ARG   A 1 149 ? 5.083   -24.692 16.547 1.00 31.86 ? 841  ARG   A NE  1 
ATOM   1104 C CZ  . ARG   A 1 149 ? 3.940   -24.259 16.015 1.00 36.58 ? 841  ARG   A CZ  1 
ATOM   1105 N NH1 . ARG   A 1 149 ? 3.930   -23.713 14.805 1.00 37.52 ? 841  ARG   A NH1 1 
ATOM   1106 N NH2 . ARG   A 1 149 ? 2.800   -24.357 16.694 1.00 35.95 ? 841  ARG   A NH2 1 
ATOM   1107 N N   . ASN   A 1 150 ? 7.105   -22.074 20.729 1.00 18.87 ? 842  ASN   A N   1 
ATOM   1108 C CA  . ASN   A 1 150 ? 8.308   -21.284 20.452 1.00 19.53 ? 842  ASN   A CA  1 
ATOM   1109 C C   . ASN   A 1 150 ? 8.568   -20.178 21.492 1.00 18.28 ? 842  ASN   A C   1 
ATOM   1110 O O   . ASN   A 1 150 ? 9.223   -19.185 21.192 1.00 17.87 ? 842  ASN   A O   1 
ATOM   1111 C CB  . ASN   A 1 150 ? 8.258   -20.687 19.046 1.00 22.32 ? 842  ASN   A CB  1 
ATOM   1112 C CG  . ASN   A 1 150 ? 8.550   -21.704 17.994 1.00 27.55 ? 842  ASN   A CG  1 
ATOM   1113 O OD1 . ASN   A 1 150 ? 9.481   -22.501 18.122 1.00 30.56 ? 842  ASN   A OD1 1 
ATOM   1114 N ND2 . ASN   A 1 150 ? 7.764   -21.713 16.943 1.00 28.30 ? 842  ASN   A ND2 1 
ATOM   1115 N N   . VAL   A 1 151 ? 8.053   -20.356 22.700 1.00 17.28 ? 843  VAL   A N   1 
ATOM   1116 C CA  . VAL   A 1 151 ? 8.310   -19.455 23.792 1.00 17.50 ? 843  VAL   A CA  1 
ATOM   1117 C C   . VAL   A 1 151 ? 8.887   -20.357 24.866 1.00 19.16 ? 843  VAL   A C   1 
ATOM   1118 O O   . VAL   A 1 151 ? 8.236   -21.341 25.241 1.00 20.07 ? 843  VAL   A O   1 
ATOM   1119 C CB  . VAL   A 1 151 ? 7.086   -18.666 24.309 1.00 16.85 ? 843  VAL   A CB  1 
ATOM   1120 C CG1 . VAL   A 1 151 ? 7.463   -17.919 25.582 1.00 17.39 ? 843  VAL   A CG1 1 
ATOM   1121 C CG2 . VAL   A 1 151 ? 6.534   -17.702 23.252 1.00 15.67 ? 843  VAL   A CG2 1 
ATOM   1122 N N   . LEU   A 1 152 ? 10.146  -20.092 25.290 1.00 18.50 ? 844  LEU   A N   1 
ATOM   1123 C CA  . LEU   A 1 152 ? 10.798  -20.906 26.301 1.00 18.68 ? 844  LEU   A CA  1 
ATOM   1124 C C   . LEU   A 1 152 ? 10.730  -20.278 27.672 1.00 17.21 ? 844  LEU   A C   1 
ATOM   1125 O O   . LEU   A 1 152 ? 10.681  -19.067 27.797 1.00 17.58 ? 844  LEU   A O   1 
ATOM   1126 C CB  . LEU   A 1 152 ? 12.253  -21.224 25.910 1.00 20.03 ? 844  LEU   A CB  1 
ATOM   1127 C CG  . LEU   A 1 152 ? 12.421  -22.019 24.604 1.00 22.91 ? 844  LEU   A CG  1 
ATOM   1128 C CD1 . LEU   A 1 152 ? 13.850  -22.380 24.376 1.00 23.56 ? 844  LEU   A CD1 1 
ATOM   1129 C CD2 . LEU   A 1 152 ? 11.593  -23.299 24.612 1.00 23.55 ? 844  LEU   A CD2 1 
ATOM   1130 N N   . VAL   A 1 153 ? 10.715  -21.096 28.698 1.00 16.04 ? 845  VAL   A N   1 
ATOM   1131 C CA  . VAL   A 1 153 ? 10.685  -20.638 30.082 1.00 15.83 ? 845  VAL   A CA  1 
ATOM   1132 C C   . VAL   A 1 153 ? 12.135  -20.706 30.626 1.00 16.30 ? 845  VAL   A C   1 
ATOM   1133 O O   . VAL   A 1 153 ? 12.713  -21.795 30.658 1.00 15.80 ? 845  VAL   A O   1 
ATOM   1134 C CB  . VAL   A 1 153 ? 9.747   -21.568 30.876 1.00 15.98 ? 845  VAL   A CB  1 
ATOM   1135 C CG1 . VAL   A 1 153 ? 9.754   -21.249 32.362 1.00 16.61 ? 845  VAL   A CG1 1 
ATOM   1136 C CG2 . VAL   A 1 153 ? 8.342   -21.511 30.328 1.00 16.07 ? 845  VAL   A CG2 1 
ATOM   1137 N N   . LYS   A 1 154 ? 12.734  -19.538 31.002 1.00 16.42 ? 846  LYS   A N   1 
ATOM   1138 C CA  . LYS   A 1 154 ? 14.088  -19.418 31.569 1.00 16.64 ? 846  LYS   A CA  1 
ATOM   1139 C C   . LYS   A 1 154 ? 13.972  -19.774 33.067 1.00 19.18 ? 846  LYS   A C   1 
ATOM   1140 O O   . LYS   A 1 154 ? 14.709  -20.624 33.563 1.00 20.47 ? 846  LYS   A O   1 
ATOM   1141 C CB  . LYS   A 1 154 ? 14.635  -17.994 31.348 1.00 16.64 ? 846  LYS   A CB  1 
ATOM   1142 C CG  . LYS   A 1 154 ? 15.988  -17.685 31.994 1.00 18.36 ? 846  LYS   A CG  1 
ATOM   1143 C CD  . LYS   A 1 154 ? 17.176  -18.028 31.114 1.00 20.28 ? 846  LYS   A CD  1 
ATOM   1144 C CE  . LYS   A 1 154 ? 18.506  -17.626 31.730 1.00 21.89 ? 846  LYS   A CE  1 
ATOM   1145 N NZ  . LYS   A 1 154 ? 18.924  -16.241 31.372 1.00 21.75 ? 846  LYS   A NZ  1 
ATOM   1146 N N   . THR   A 1 155 ? 13.007  -19.156 33.755 1.00 19.45 ? 847  THR   A N   1 
ATOM   1147 C CA  . THR   A 1 155 ? 12.495  -19.379 35.113 1.00 19.68 ? 847  THR   A CA  1 
ATOM   1148 C C   . THR   A 1 155 ? 10.968  -19.143 34.938 1.00 20.71 ? 847  THR   A C   1 
ATOM   1149 O O   . THR   A 1 155 ? 10.565  -18.493 33.952 1.00 20.52 ? 847  THR   A O   1 
ATOM   1150 C CB  . THR   A 1 155 ? 13.058  -18.344 36.142 1.00 20.61 ? 847  THR   A CB  1 
ATOM   1151 O OG1 . THR   A 1 155 ? 12.499  -17.041 35.950 1.00 21.04 ? 847  THR   A OG1 1 
ATOM   1152 C CG2 . THR   A 1 155 ? 14.578  -18.264 36.169 1.00 21.16 ? 847  THR   A CG2 1 
ATOM   1153 N N   . PRO   A 1 156 ? 10.106  -19.513 35.913 1.00 20.91 ? 848  PRO   A N   1 
ATOM   1154 C CA  . PRO   A 1 156 ? 8.672   -19.235 35.755 1.00 21.12 ? 848  PRO   A CA  1 
ATOM   1155 C C   . PRO   A 1 156 ? 8.351   -17.747 35.616 1.00 20.77 ? 848  PRO   A C   1 
ATOM   1156 O O   . PRO   A 1 156 ? 7.284   -17.408 35.120 1.00 21.24 ? 848  PRO   A O   1 
ATOM   1157 C CB  . PRO   A 1 156 ? 8.055   -19.871 37.011 1.00 22.13 ? 848  PRO   A CB  1 
ATOM   1158 C CG  . PRO   A 1 156 ? 9.014   -20.955 37.381 1.00 22.20 ? 848  PRO   A CG  1 
ATOM   1159 C CD  . PRO   A 1 156 ? 10.353  -20.290 37.138 1.00 20.77 ? 848  PRO   A CD  1 
ATOM   1160 N N   . GLN   A 1 157 ? 9.278   -16.852 35.997 1.00 19.88 ? 849  GLN   A N   1 
ATOM   1161 C CA  . GLN   A 1 157 ? 9.074   -15.403 35.860 1.00 19.37 ? 849  GLN   A CA  1 
ATOM   1162 C C   . GLN   A 1 157 ? 9.770   -14.818 34.625 1.00 17.43 ? 849  GLN   A C   1 
ATOM   1163 O O   . GLN   A 1 157 ? 9.788   -13.582 34.499 1.00 18.97 ? 849  GLN   A O   1 
ATOM   1164 C CB  . GLN   A 1 157 ? 9.699   -14.677 37.050 1.00 22.37 ? 849  GLN   A CB  1 
ATOM   1165 C CG  . GLN   A 1 157 ? 8.915   -14.686 38.346 1.00 28.53 ? 849  GLN   A CG  1 
ATOM   1166 C CD  . GLN   A 1 157 ? 9.596   -13.720 39.296 1.00 35.58 ? 849  GLN   A CD  1 
ATOM   1167 O OE1 . GLN   A 1 157 ? 10.832  -13.675 39.408 1.00 36.07 ? 849  GLN   A OE1 1 
ATOM   1168 N NE2 . GLN   A 1 157 ? 8.807   -12.889 39.976 1.00 38.45 ? 849  GLN   A NE2 1 
ATOM   1169 N N   . HIS   A 1 158 ? 10.413  -15.640 33.781 1.00 13.66 ? 850  HIS   A N   1 
ATOM   1170 C CA  . HIS   A 1 158 ? 11.172  -15.104 32.664 1.00 12.38 ? 850  HIS   A CA  1 
ATOM   1171 C C   . HIS   A 1 158 ? 11.026  -16.001 31.452 1.00 11.40 ? 850  HIS   A C   1 
ATOM   1172 O O   . HIS   A 1 158 ? 11.475  -17.159 31.452 1.00 11.96 ? 850  HIS   A O   1 
ATOM   1173 C CB  . HIS   A 1 158 ? 12.674  -14.907 33.082 1.00 12.84 ? 850  HIS   A CB  1 
ATOM   1174 C CG  . HIS   A 1 158 ? 13.522  -14.133 32.104 1.00 13.96 ? 850  HIS   A CG  1 
ATOM   1175 N ND1 . HIS   A 1 158 ? 14.861  -13.857 32.366 1.00 15.78 ? 850  HIS   A ND1 1 
ATOM   1176 C CD2 . HIS   A 1 158 ? 13.218  -13.660 30.872 1.00 14.29 ? 850  HIS   A CD2 1 
ATOM   1177 C CE1 . HIS   A 1 158 ? 15.304  -13.197 31.308 1.00 16.07 ? 850  HIS   A CE1 1 
ATOM   1178 N NE2 . HIS   A 1 158 ? 14.350  -13.060 30.382 1.00 15.51 ? 850  HIS   A NE2 1 
ATOM   1179 N N   . VAL   A 1 159 ? 10.335  -15.497 30.444 1.00 9.64  ? 851  VAL   A N   1 
ATOM   1180 C CA  . VAL   A 1 159 ? 10.129  -16.227 29.216 1.00 9.33  ? 851  VAL   A CA  1 
ATOM   1181 C C   . VAL   A 1 159 ? 10.866  -15.537 28.080 1.00 10.33 ? 851  VAL   A C   1 
ATOM   1182 O O   . VAL   A 1 159 ? 11.197  -14.336 28.176 1.00 10.74 ? 851  VAL   A O   1 
ATOM   1183 C CB  . VAL   A 1 159 ? 8.642   -16.487 28.914 1.00 9.36  ? 851  VAL   A CB  1 
ATOM   1184 C CG1 . VAL   A 1 159 ? 8.038   -17.387 29.963 1.00 10.04 ? 851  VAL   A CG1 1 
ATOM   1185 C CG2 . VAL   A 1 159 ? 7.851   -15.190 28.812 1.00 9.82  ? 851  VAL   A CG2 1 
ATOM   1186 N N   . LYS   A 1 160 ? 11.196  -16.300 27.033 1.00 10.45 ? 852  LYS   A N   1 
ATOM   1187 C CA  . LYS   A 1 160 ? 11.981  -15.785 25.903 1.00 11.49 ? 852  LYS   A CA  1 
ATOM   1188 C C   . LYS   A 1 160 ? 11.504  -16.439 24.619 1.00 13.44 ? 852  LYS   A C   1 
ATOM   1189 O O   . LYS   A 1 160 ? 11.289  -17.648 24.615 1.00 14.55 ? 852  LYS   A O   1 
ATOM   1190 C CB  . LYS   A 1 160 ? 13.514  -16.094 26.110 1.00 11.59 ? 852  LYS   A CB  1 
ATOM   1191 C CG  . LYS   A 1 160 ? 14.037  -15.754 27.519 1.00 13.94 ? 852  LYS   A CG  1 
ATOM   1192 C CD  . LYS   A 1 160 ? 15.499  -16.095 27.806 1.00 18.55 ? 852  LYS   A CD  1 
ATOM   1193 C CE  . LYS   A 1 160 ? 16.458  -15.511 26.818 1.00 21.74 ? 852  LYS   A CE  1 
ATOM   1194 N NZ  . LYS   A 1 160 ? 17.751  -16.249 26.823 1.00 24.92 ? 852  LYS   A NZ  1 
ATOM   1195 N N   . ILE   A 1 161 ? 11.388  -15.677 23.520 1.00 13.61 ? 853  ILE   A N   1 
ATOM   1196 C CA  . ILE   A 1 161 ? 10.993  -16.216 22.225 1.00 14.85 ? 853  ILE   A CA  1 
ATOM   1197 C C   . ILE   A 1 161 ? 12.132  -16.991 21.607 1.00 15.72 ? 853  ILE   A C   1 
ATOM   1198 O O   . ILE   A 1 161 ? 13.226  -16.462 21.520 1.00 16.11 ? 853  ILE   A O   1 
ATOM   1199 C CB  . ILE   A 1 161 ? 10.558  -15.056 21.289 1.00 15.78 ? 853  ILE   A CB  1 
ATOM   1200 C CG1 . ILE   A 1 161 ? 9.345   -14.315 21.885 1.00 16.60 ? 853  ILE   A CG1 1 
ATOM   1201 C CG2 . ILE   A 1 161 ? 10.234  -15.573 19.867 1.00 16.05 ? 853  ILE   A CG2 1 
ATOM   1202 C CD1 . ILE   A 1 161 ? 9.264   -12.946 21.471 1.00 17.61 ? 853  ILE   A CD1 1 
ATOM   1203 N N   . THR   A 1 162 ? 11.880  -18.209 21.109 1.00 16.47 ? 854  THR   A N   1 
ATOM   1204 C CA  . THR   A 1 162 ? 12.922  -19.019 20.476 1.00 17.69 ? 854  THR   A CA  1 
ATOM   1205 C C   . THR   A 1 162 ? 12.683  -19.225 18.943 1.00 18.67 ? 854  THR   A C   1 
ATOM   1206 O O   . THR   A 1 162 ? 11.720  -18.695 18.372 1.00 18.21 ? 854  THR   A O   1 
ATOM   1207 C CB  . THR   A 1 162 ? 13.103  -20.335 21.255 1.00 20.26 ? 854  THR   A CB  1 
ATOM   1208 O OG1 . THR   A 1 162 ? 14.388  -20.867 20.927 1.00 22.39 ? 854  THR   A OG1 1 
ATOM   1209 C CG2 . THR   A 1 162 ? 12.025  -21.369 20.929 1.00 20.87 ? 854  THR   A CG2 1 
ATOM   1210 N N   . ASP   A 1 163 ? 13.645  -19.887 18.278 1.00 19.67 ? 855  ASP   A N   1 
ATOM   1211 C CA  . ASP   A 1 163 ? 13.634  -20.283 16.890 1.00 21.45 ? 855  ASP   A CA  1 
ATOM   1212 C C   . ASP   A 1 163 ? 13.528  -19.153 15.892 1.00 23.08 ? 855  ASP   A C   1 
ATOM   1213 O O   . ASP   A 1 163 ? 13.094  -19.404 14.762 1.00 23.44 ? 855  ASP   A O   1 
ATOM   1214 C CB  . ASP   A 1 163 ? 12.529  -21.315 16.651 1.00 23.69 ? 855  ASP   A CB  1 
ATOM   1215 C CG  . ASP   A 1 163 ? 12.856  -22.719 17.127 1.00 28.70 ? 855  ASP   A CG  1 
ATOM   1216 O OD1 . ASP   A 1 163 ? 14.007  -22.957 17.527 1.00 29.11 ? 855  ASP   A OD1 1 
ATOM   1217 O OD2 . ASP   A 1 163 ? 11.964  -23.583 17.074 1.00 32.10 ? 855  ASP   A OD2 1 
ATOM   1218 N N   . PHE   A 1 164 ? 13.979  -17.925 16.246 1.00 23.83 ? 856  PHE   A N   1 
ATOM   1219 C CA  . PHE   A 1 164 ? 13.948  -16.826 15.276 1.00 25.15 ? 856  PHE   A CA  1 
ATOM   1220 C C   . PHE   A 1 164 ? 14.892  -17.189 14.085 1.00 26.33 ? 856  PHE   A C   1 
ATOM   1221 O O   . PHE   A 1 164 ? 16.052  -17.539 14.308 1.00 25.80 ? 856  PHE   A O   1 
ATOM   1222 C CB  . PHE   A 1 164 ? 14.363  -15.459 15.906 1.00 24.98 ? 856  PHE   A CB  1 
ATOM   1223 C CG  . PHE   A 1 164 ? 14.584  -14.431 14.815 1.00 25.81 ? 856  PHE   A CG  1 
ATOM   1224 C CD1 . PHE   A 1 164 ? 13.512  -13.915 14.104 1.00 26.74 ? 856  PHE   A CD1 1 
ATOM   1225 C CD2 . PHE   A 1 164 ? 15.860  -14.145 14.360 1.00 26.58 ? 856  PHE   A CD2 1 
ATOM   1226 C CE1 . PHE   A 1 164 ? 13.716  -13.089 13.008 1.00 27.60 ? 856  PHE   A CE1 1 
ATOM   1227 C CE2 . PHE   A 1 164 ? 16.059  -13.320 13.262 1.00 27.26 ? 856  PHE   A CE2 1 
ATOM   1228 C CZ  . PHE   A 1 164 ? 14.989  -12.815 12.582 1.00 27.15 ? 856  PHE   A CZ  1 
ATOM   1229 N N   . GLY   A 1 165 ? 14.377  -17.086 12.869 1.00 27.23 ? 857  GLY   A N   1 
ATOM   1230 C CA  . GLY   A 1 165 ? 15.156  -17.367 11.678 1.00 29.18 ? 857  GLY   A CA  1 
ATOM   1231 C C   . GLY   A 1 165 ? 15.067  -18.794 11.187 1.00 32.00 ? 857  GLY   A C   1 
ATOM   1232 O O   . GLY   A 1 165 ? 15.558  -19.094 10.096 1.00 33.00 ? 857  GLY   A O   1 
ATOM   1233 N N   . LEU   A 1 166 ? 14.472  -19.693 11.977 1.00 33.32 ? 858  LEU   A N   1 
ATOM   1234 C CA  . LEU   A 1 166 ? 14.342  -21.085 11.575 1.00 35.57 ? 858  LEU   A CA  1 
ATOM   1235 C C   . LEU   A 1 166 ? 13.344  -21.223 10.431 1.00 37.77 ? 858  LEU   A C   1 
ATOM   1236 O O   . LEU   A 1 166 ? 13.591  -21.999 9.513  1.00 37.92 ? 858  LEU   A O   1 
ATOM   1237 C CB  . LEU   A 1 166 ? 13.918  -21.955 12.768 1.00 36.20 ? 858  LEU   A CB  1 
ATOM   1238 C CG  . LEU   A 1 166 ? 14.391  -23.433 12.865 1.00 38.11 ? 858  LEU   A CG  1 
ATOM   1239 C CD1 . LEU   A 1 166 ? 15.497  -23.806 11.845 1.00 38.98 ? 858  LEU   A CD1 1 
ATOM   1240 C CD2 . LEU   A 1 166 ? 14.871  -23.744 14.266 1.00 38.46 ? 858  LEU   A CD2 1 
ATOM   1241 N N   . ALA   A 1 167 ? 12.251  -20.437 10.446 1.00 39.21 ? 859  ALA   A N   1 
ATOM   1242 C CA  . ALA   A 1 167 ? 11.260  -20.473 9.368  1.00 41.05 ? 859  ALA   A CA  1 
ATOM   1243 C C   . ALA   A 1 167 ? 11.902  -20.087 8.021  1.00 43.08 ? 859  ALA   A C   1 
ATOM   1244 O O   . ALA   A 1 167 ? 11.604  -20.719 7.013  1.00 43.56 ? 859  ALA   A O   1 
ATOM   1245 C CB  . ALA   A 1 167 ? 10.090  -19.554 9.684  1.00 41.06 ? 859  ALA   A CB  1 
ATOM   1246 N N   . LYS   A 1 168 ? 12.829  -19.108 8.015  1.00 43.97 ? 860  LYS   A N   1 
ATOM   1247 C CA  . LYS   A 1 168 ? 13.554  -18.717 6.801  1.00 45.17 ? 860  LYS   A CA  1 
ATOM   1248 C C   . LYS   A 1 168 ? 14.534  -19.830 6.360  1.00 45.97 ? 860  LYS   A C   1 
ATOM   1249 O O   . LYS   A 1 168 ? 14.750  -20.006 5.163  1.00 45.93 ? 860  LYS   A O   1 
ATOM   1250 C CB  . LYS   A 1 168 ? 14.313  -17.396 7.033  1.00 47.29 ? 860  LYS   A CB  1 
ATOM   1251 C CG  . LYS   A 1 168 ? 14.583  -16.615 5.758  1.00 51.48 ? 860  LYS   A CG  1 
ATOM   1252 C CD  . LYS   A 1 168 ? 15.368  -15.333 6.017  1.00 55.88 ? 860  LYS   A CD  1 
ATOM   1253 C CE  . LYS   A 1 168 ? 15.842  -14.718 4.717  1.00 59.53 ? 860  LYS   A CE  1 
ATOM   1254 N NZ  . LYS   A 1 168 ? 16.559  -13.435 4.929  1.00 61.44 ? 860  LYS   A NZ  1 
ATOM   1255 N N   . LEU   A 1 169 ? 15.111  -20.563 7.348  1.00 46.39 ? 861  LEU   A N   1 
ATOM   1256 C CA  . LEU   A 1 169 ? 16.047  -21.704 7.283  1.00 47.12 ? 861  LEU   A CA  1 
ATOM   1257 C C   . LEU   A 1 169 ? 17.517  -21.282 7.406  1.00 47.74 ? 861  LEU   A C   1 
ATOM   1258 O O   . LEU   A 1 169 ? 18.248  -21.817 8.250  1.00 47.79 ? 861  LEU   A O   1 
ATOM   1259 C CB  . LEU   A 1 169 ? 15.840  -22.646 6.068  1.00 47.10 ? 861  LEU   A CB  1 
ATOM   1260 C CG  . LEU   A 1 169 ? 14.926  -23.893 6.258  1.00 48.24 ? 861  LEU   A CG  1 
ATOM   1261 C CD1 . LEU   A 1 169 ? 15.202  -24.633 7.576  1.00 48.55 ? 861  LEU   A CD1 1 
ATOM   1262 C CD2 . LEU   A 1 169 ? 13.466  -23.545 6.121  1.00 48.64 ? 861  LEU   A CD2 1 
ATOM   1263 N N   . VAL   A 1 184 ? 4.165   -25.680 8.007  1.00 35.36 ? 876  VAL   A N   1 
ATOM   1264 C CA  . VAL   A 1 184 ? 3.329   -24.469 7.893  1.00 35.51 ? 876  VAL   A CA  1 
ATOM   1265 C C   . VAL   A 1 184 ? 2.293   -24.356 9.021  1.00 34.55 ? 876  VAL   A C   1 
ATOM   1266 O O   . VAL   A 1 184 ? 1.292   -25.071 9.013  1.00 35.18 ? 876  VAL   A O   1 
ATOM   1267 C CB  . VAL   A 1 184 ? 2.660   -24.307 6.498  1.00 36.55 ? 876  VAL   A CB  1 
ATOM   1268 C CG1 . VAL   A 1 184 ? 3.618   -23.666 5.504  1.00 37.15 ? 876  VAL   A CG1 1 
ATOM   1269 C CG2 . VAL   A 1 184 ? 2.135   -25.644 5.968  1.00 37.37 ? 876  VAL   A CG2 1 
ATOM   1270 N N   . PRO   A 1 185 ? 2.501   -23.446 9.988  1.00 32.87 ? 877  PRO   A N   1 
ATOM   1271 C CA  . PRO   A 1 185 ? 1.512   -23.277 11.077 1.00 31.57 ? 877  PRO   A CA  1 
ATOM   1272 C C   . PRO   A 1 185 ? 0.231   -22.522 10.657 1.00 29.59 ? 877  PRO   A C   1 
ATOM   1273 O O   . PRO   A 1 185 ? -0.021  -21.424 11.156 1.00 30.18 ? 877  PRO   A O   1 
ATOM   1274 C CB  . PRO   A 1 185 ? 2.303   -22.472 12.109 1.00 32.41 ? 877  PRO   A CB  1 
ATOM   1275 C CG  . PRO   A 1 185 ? 3.215   -21.634 11.266 1.00 33.09 ? 877  PRO   A CG  1 
ATOM   1276 C CD  . PRO   A 1 185 ? 3.636   -22.513 10.132 1.00 31.93 ? 877  PRO   A CD  1 
ATOM   1277 N N   . ILE   A 1 186 ? -0.599  -23.113 9.766  1.00 27.34 ? 878  ILE   A N   1 
ATOM   1278 C CA  . ILE   A 1 186 ? -1.836  -22.502 9.263  1.00 25.30 ? 878  ILE   A CA  1 
ATOM   1279 C C   . ILE   A 1 186 ? -2.719  -21.892 10.373 1.00 23.14 ? 878  ILE   A C   1 
ATOM   1280 O O   . ILE   A 1 186 ? -3.164  -20.747 10.246 1.00 22.58 ? 878  ILE   A O   1 
ATOM   1281 C CB  . ILE   A 1 186 ? -2.633  -23.497 8.369  1.00 25.65 ? 878  ILE   A CB  1 
ATOM   1282 C CG1 . ILE   A 1 186 ? -1.834  -23.886 7.099  1.00 26.05 ? 878  ILE   A CG1 1 
ATOM   1283 C CG2 . ILE   A 1 186 ? -4.027  -22.942 7.996  1.00 26.15 ? 878  ILE   A CG2 1 
ATOM   1284 C CD1 . ILE   A 1 186 ? -1.782  -22.813 5.944  1.00 26.48 ? 878  ILE   A CD1 1 
ATOM   1285 N N   . LYS   A 1 187 ? -2.915  -22.623 11.479 1.00 22.04 ? 879  LYS   A N   1 
ATOM   1286 C CA  . LYS   A 1 187 ? -3.758  -22.182 12.609 1.00 21.11 ? 879  LYS   A CA  1 
ATOM   1287 C C   . LYS   A 1 187 ? -3.184  -21.026 13.433 1.00 20.83 ? 879  LYS   A C   1 
ATOM   1288 O O   . LYS   A 1 187 ? -3.900  -20.438 14.223 1.00 21.30 ? 879  LYS   A O   1 
ATOM   1289 C CB  . LYS   A 1 187 ? -4.115  -23.362 13.503 1.00 21.64 ? 879  LYS   A CB  1 
ATOM   1290 C CG  . LYS   A 1 187 ? -4.984  -24.357 12.743 1.00 23.65 ? 879  LYS   A CG  1 
ATOM   1291 C CD  . LYS   A 1 187 ? -5.270  -25.629 13.472 1.00 27.04 ? 879  LYS   A CD  1 
ATOM   1292 C CE  . LYS   A 1 187 ? -6.330  -26.415 12.739 1.00 31.03 ? 879  LYS   A CE  1 
ATOM   1293 N NZ  . LYS   A 1 187 ? -6.814  -27.592 13.521 1.00 33.42 ? 879  LYS   A NZ  1 
ATOM   1294 N N   . TRP   A 1 188 ? -1.927  -20.665 13.216 1.00 20.04 ? 880  TRP   A N   1 
ATOM   1295 C CA  . TRP   A 1 188 ? -1.318  -19.507 13.879 1.00 20.10 ? 880  TRP   A CA  1 
ATOM   1296 C C   . TRP   A 1 188 ? -1.102  -18.345 12.870 1.00 20.47 ? 880  TRP   A C   1 
ATOM   1297 O O   . TRP   A 1 188 ? -0.731  -17.249 13.282 1.00 20.37 ? 880  TRP   A O   1 
ATOM   1298 C CB  . TRP   A 1 188 ? 0.034   -19.890 14.551 1.00 19.17 ? 880  TRP   A CB  1 
ATOM   1299 C CG  . TRP   A 1 188 ? -0.090  -20.617 15.867 1.00 18.71 ? 880  TRP   A CG  1 
ATOM   1300 C CD1 . TRP   A 1 188 ? 0.030   -20.080 17.116 1.00 18.99 ? 880  TRP   A CD1 1 
ATOM   1301 C CD2 . TRP   A 1 188 ? -0.418  -22.007 16.057 1.00 18.42 ? 880  TRP   A CD2 1 
ATOM   1302 N NE1 . TRP   A 1 188 ? -0.177  -21.052 18.071 1.00 18.94 ? 880  TRP   A NE1 1 
ATOM   1303 C CE2 . TRP   A 1 188 ? -0.474  -22.238 17.449 1.00 18.56 ? 880  TRP   A CE2 1 
ATOM   1304 C CE3 . TRP   A 1 188 ? -0.671  -23.077 15.185 1.00 18.88 ? 880  TRP   A CE3 1 
ATOM   1305 C CZ2 . TRP   A 1 188 ? -0.739  -23.494 17.985 1.00 18.83 ? 880  TRP   A CZ2 1 
ATOM   1306 C CZ3 . TRP   A 1 188 ? -0.962  -24.316 15.722 1.00 19.47 ? 880  TRP   A CZ3 1 
ATOM   1307 C CH2 . TRP   A 1 188 ? -1.011  -24.510 17.107 1.00 19.27 ? 880  TRP   A CH2 1 
ATOM   1308 N N   . MET   A 1 189 ? -1.297  -18.600 11.551 1.00 20.24 ? 881  MET   A N   1 
ATOM   1309 C CA  . MET   A 1 189 ? -1.064  -17.638 10.487 1.00 20.16 ? 881  MET   A CA  1 
ATOM   1310 C C   . MET   A 1 189 ? -2.175  -16.642 10.270 1.00 19.61 ? 881  MET   A C   1 
ATOM   1311 O O   . MET   A 1 189 ? -3.360  -16.954 10.411 1.00 18.36 ? 881  MET   A O   1 
ATOM   1312 C CB  . MET   A 1 189 ? -0.736  -18.345 9.152  1.00 20.99 ? 881  MET   A CB  1 
ATOM   1313 C CG  . MET   A 1 189 ? 0.615   -19.050 9.137  1.00 23.52 ? 881  MET   A CG  1 
ATOM   1314 S SD  . MET   A 1 189 ? 0.760   -20.258 7.778  1.00 29.14 ? 881  MET   A SD  1 
ATOM   1315 C CE  . MET   A 1 189 ? 0.794   -19.189 6.418  1.00 22.30 ? 881  MET   A CE  1 
ATOM   1316 N N   . ALA   A 1 190 ? -1.775  -15.428 9.884  1.00 20.10 ? 882  ALA   A N   1 
ATOM   1317 C CA  . ALA   A 1 190 ? -2.736  -14.404 9.531  1.00 20.92 ? 882  ALA   A CA  1 
ATOM   1318 C C   . ALA   A 1 190 ? -3.316  -14.801 8.151  1.00 21.27 ? 882  ALA   A C   1 
ATOM   1319 O O   . ALA   A 1 190 ? -2.651  -15.511 7.389  1.00 21.25 ? 882  ALA   A O   1 
ATOM   1320 C CB  . ALA   A 1 190 ? -2.049  -13.038 9.477  1.00 20.61 ? 882  ALA   A CB  1 
ATOM   1321 N N   . LEU   A 1 191 ? -4.552  -14.392 7.844  1.00 21.05 ? 883  LEU   A N   1 
ATOM   1322 C CA  . LEU   A 1 191 ? -5.188  -14.731 6.572  1.00 21.79 ? 883  LEU   A CA  1 
ATOM   1323 C C   . LEU   A 1 191 ? -4.315  -14.376 5.334  1.00 22.68 ? 883  LEU   A C   1 
ATOM   1324 O O   . LEU   A 1 191 ? -4.122  -15.218 4.445  1.00 22.90 ? 883  LEU   A O   1 
ATOM   1325 C CB  . LEU   A 1 191 ? -6.542  -14.019 6.475  1.00 21.93 ? 883  LEU   A CB  1 
ATOM   1326 C CG  . LEU   A 1 191 ? -7.398  -14.414 5.299  1.00 23.18 ? 883  LEU   A CG  1 
ATOM   1327 C CD1 . LEU   A 1 191 ? -7.905  -15.853 5.443  1.00 24.06 ? 883  LEU   A CD1 1 
ATOM   1328 C CD2 . LEU   A 1 191 ? -8.552  -13.461 5.150  1.00 23.21 ? 883  LEU   A CD2 1 
ATOM   1329 N N   . GLU   A 1 192 ? -3.723  -13.166 5.321  1.00 22.35 ? 884  GLU   A N   1 
ATOM   1330 C CA  . GLU   A 1 192 ? -2.871  -12.755 4.208  1.00 21.51 ? 884  GLU   A CA  1 
ATOM   1331 C C   . GLU   A 1 192 ? -1.637  -13.655 4.062  1.00 22.70 ? 884  GLU   A C   1 
ATOM   1332 O O   . GLU   A 1 192 ? -1.167  -13.861 2.936  1.00 23.30 ? 884  GLU   A O   1 
ATOM   1333 C CB  . GLU   A 1 192 ? -2.514  -11.257 4.272  1.00 20.39 ? 884  GLU   A CB  1 
ATOM   1334 C CG  . GLU   A 1 192 ? -1.510  -10.853 5.335  1.00 20.60 ? 884  GLU   A CG  1 
ATOM   1335 C CD  . GLU   A 1 192 ? -2.081  -10.539 6.709  1.00 22.46 ? 884  GLU   A CD  1 
ATOM   1336 O OE1 . GLU   A 1 192 ? -3.257  -10.885 6.967  1.00 22.40 ? 884  GLU   A OE1 1 
ATOM   1337 O OE2 . GLU   A 1 192 ? -1.348  -9.945  7.531  1.00 22.17 ? 884  GLU   A OE2 1 
ATOM   1338 N N   . SER   A 1 193 ? -1.155  -14.243 5.164  1.00 22.56 ? 885  SER   A N   1 
ATOM   1339 C CA  . SER   A 1 193 ? -0.023  -15.162 5.084  1.00 23.09 ? 885  SER   A CA  1 
ATOM   1340 C C   . SER   A 1 193 ? -0.466  -16.479 4.488  1.00 23.59 ? 885  SER   A C   1 
ATOM   1341 O O   . SER   A 1 193 ? 0.266   -17.036 3.676  1.00 23.54 ? 885  SER   A O   1 
ATOM   1342 C CB  . SER   A 1 193 ? 0.618   -15.377 6.448  1.00 23.25 ? 885  SER   A CB  1 
ATOM   1343 O OG  . SER   A 1 193 ? 1.076   -14.122 6.917  1.00 24.56 ? 885  SER   A OG  1 
ATOM   1344 N N   . ILE   A 1 194 ? -1.670  -16.967 4.861  1.00 23.73 ? 886  ILE   A N   1 
ATOM   1345 C CA  . ILE   A 1 194 ? -2.226  -18.223 4.329  1.00 24.25 ? 886  ILE   A CA  1 
ATOM   1346 C C   . ILE   A 1 194 ? -2.499  -18.098 2.816  1.00 25.05 ? 886  ILE   A C   1 
ATOM   1347 O O   . ILE   A 1 194 ? -2.205  -19.020 2.038  1.00 25.76 ? 886  ILE   A O   1 
ATOM   1348 C CB  . ILE   A 1 194 ? -3.536  -18.616 5.075  1.00 24.03 ? 886  ILE   A CB  1 
ATOM   1349 C CG1 . ILE   A 1 194 ? -3.311  -18.790 6.591  1.00 24.23 ? 886  ILE   A CG1 1 
ATOM   1350 C CG2 . ILE   A 1 194 ? -4.181  -19.864 4.461  1.00 24.15 ? 886  ILE   A CG2 1 
ATOM   1351 C CD1 . ILE   A 1 194 ? -4.577  -19.006 7.408  1.00 24.45 ? 886  ILE   A CD1 1 
ATOM   1352 N N   . LEU   A 1 195 ? -3.072  -16.953 2.411  1.00 24.20 ? 887  LEU   A N   1 
ATOM   1353 C CA  . LEU   A 1 195 ? -3.482  -16.748 1.033  1.00 23.79 ? 887  LEU   A CA  1 
ATOM   1354 C C   . LEU   A 1 195 ? -2.356  -16.351 0.109  1.00 23.41 ? 887  LEU   A C   1 
ATOM   1355 O O   . LEU   A 1 195 ? -2.292  -16.821 -1.014 1.00 22.67 ? 887  LEU   A O   1 
ATOM   1356 C CB  . LEU   A 1 195 ? -4.591  -15.682 0.956  1.00 23.35 ? 887  LEU   A CB  1 
ATOM   1357 C CG  . LEU   A 1 195 ? -5.890  -15.959 1.695  1.00 24.35 ? 887  LEU   A CG  1 
ATOM   1358 C CD1 . LEU   A 1 195 ? -6.849  -14.775 1.550  1.00 24.66 ? 887  LEU   A CD1 1 
ATOM   1359 C CD2 . LEU   A 1 195 ? -6.552  -17.213 1.185  1.00 24.59 ? 887  LEU   A CD2 1 
ATOM   1360 N N   . HIS   A 1 196 ? -1.509  -15.437 0.559  1.00 23.74 ? 888  HIS   A N   1 
ATOM   1361 C CA  . HIS   A 1 196 ? -0.489  -14.861 -0.284 1.00 23.94 ? 888  HIS   A CA  1 
ATOM   1362 C C   . HIS   A 1 196 ? 0.929   -14.995 0.223  1.00 25.07 ? 888  HIS   A C   1 
ATOM   1363 O O   . HIS   A 1 196 ? 1.784   -14.302 -0.295 1.00 25.58 ? 888  HIS   A O   1 
ATOM   1364 C CB  . HIS   A 1 196 ? -0.837  -13.387 -0.523 1.00 24.15 ? 888  HIS   A CB  1 
ATOM   1365 C CG  . HIS   A 1 196 ? -2.203  -13.200 -1.121 1.00 26.95 ? 888  HIS   A CG  1 
ATOM   1366 N ND1 . HIS   A 1 196 ? -2.495  -13.627 -2.417 1.00 28.98 ? 888  HIS   A ND1 1 
ATOM   1367 C CD2 . HIS   A 1 196 ? -3.335  -12.700 -0.565 1.00 27.78 ? 888  HIS   A CD2 1 
ATOM   1368 C CE1 . HIS   A 1 196 ? -3.773  -13.337 -2.612 1.00 28.75 ? 888  HIS   A CE1 1 
ATOM   1369 N NE2 . HIS   A 1 196 ? -4.325  -12.786 -1.525 1.00 28.45 ? 888  HIS   A NE2 1 
ATOM   1370 N N   . ARG   A 1 197 ? 1.208   -15.856 1.213  1.00 25.58 ? 889  ARG   A N   1 
ATOM   1371 C CA  . ARG   A 1 197 ? 2.558   -15.999 1.789  1.00 26.59 ? 889  ARG   A CA  1 
ATOM   1372 C C   . ARG   A 1 197 ? 3.205   -14.646 2.178  1.00 25.90 ? 889  ARG   A C   1 
ATOM   1373 O O   . ARG   A 1 197 ? 4.423   -14.477 2.041  1.00 25.97 ? 889  ARG   A O   1 
ATOM   1374 C CB  . ARG   A 1 197 ? 3.480   -16.826 0.886  1.00 30.28 ? 889  ARG   A CB  1 
ATOM   1375 C CG  . ARG   A 1 197 ? 3.040   -18.279 0.785  1.00 38.21 ? 889  ARG   A CG  1 
ATOM   1376 C CD  . ARG   A 1 197 ? 2.383   -18.575 -0.551 1.00 46.13 ? 889  ARG   A CD  1 
ATOM   1377 N NE  . ARG   A 1 197 ? 1.624   -19.830 -0.553 1.00 53.09 ? 889  ARG   A NE  1 
ATOM   1378 C CZ  . ARG   A 1 197 ? 2.139   -21.026 -0.841 1.00 57.38 ? 889  ARG   A CZ  1 
ATOM   1379 N NH1 . ARG   A 1 197 ? 3.433   -21.150 -1.123 1.00 56.76 ? 889  ARG   A NH1 1 
ATOM   1380 N NH2 . ARG   A 1 197 ? 1.365   -22.108 -0.837 1.00 58.21 ? 889  ARG   A NH2 1 
ATOM   1381 N N   . ILE   A 1 198 ? 2.376   -13.683 2.627  1.00 24.76 ? 890  ILE   A N   1 
ATOM   1382 C CA  . ILE   A 1 198 ? 2.829   -12.366 3.042  1.00 24.74 ? 890  ILE   A CA  1 
ATOM   1383 C C   . ILE   A 1 198 ? 3.121   -12.398 4.545  1.00 23.69 ? 890  ILE   A C   1 
ATOM   1384 O O   . ILE   A 1 198 ? 2.248   -12.752 5.335  1.00 23.27 ? 890  ILE   A O   1 
ATOM   1385 C CB  . ILE   A 1 198 ? 1.780   -11.276 2.661  1.00 25.74 ? 890  ILE   A CB  1 
ATOM   1386 C CG1 . ILE   A 1 198 ? 1.770   -11.033 1.135  1.00 27.79 ? 890  ILE   A CG1 1 
ATOM   1387 C CG2 . ILE   A 1 198 ? 2.016   -9.960  3.405  1.00 25.70 ? 890  ILE   A CG2 1 
ATOM   1388 C CD1 . ILE   A 1 198 ? 0.600   -10.221 0.653  1.00 29.37 ? 890  ILE   A CD1 1 
ATOM   1389 N N   . TYR   A 1 199 ? 4.357   -12.072 4.936  1.00 23.08 ? 891  TYR   A N   1 
ATOM   1390 C CA  . TYR   A 1 199 ? 4.735   -12.060 6.344  1.00 22.67 ? 891  TYR   A CA  1 
ATOM   1391 C C   . TYR   A 1 199 ? 5.302   -10.715 6.720  1.00 22.32 ? 891  TYR   A C   1 
ATOM   1392 O O   . TYR   A 1 199 ? 6.300   -10.279 6.164  1.00 22.98 ? 891  TYR   A O   1 
ATOM   1393 C CB  . TYR   A 1 199 ? 5.749   -13.144 6.676  1.00 22.51 ? 891  TYR   A CB  1 
ATOM   1394 C CG  . TYR   A 1 199 ? 5.266   -14.542 6.371  1.00 23.55 ? 891  TYR   A CG  1 
ATOM   1395 C CD1 . TYR   A 1 199 ? 4.563   -15.277 7.315  1.00 24.44 ? 891  TYR   A CD1 1 
ATOM   1396 C CD2 . TYR   A 1 199 ? 5.578   -15.158 5.168  1.00 24.39 ? 891  TYR   A CD2 1 
ATOM   1397 C CE1 . TYR   A 1 199 ? 4.147   -16.577 7.052  1.00 25.52 ? 891  TYR   A CE1 1 
ATOM   1398 C CE2 . TYR   A 1 199 ? 5.153   -16.445 4.886  1.00 25.53 ? 891  TYR   A CE2 1 
ATOM   1399 C CZ  . TYR   A 1 199 ? 4.450   -17.159 5.835  1.00 27.07 ? 891  TYR   A CZ  1 
ATOM   1400 O OH  . TYR   A 1 199 ? 4.077   -18.450 5.555  1.00 29.91 ? 891  TYR   A OH  1 
ATOM   1401 N N   . THR   A 1 200 ? 4.645   -10.039 7.636  1.00 21.14 ? 892  THR   A N   1 
ATOM   1402 C CA  . THR   A 1 200 ? 5.081   -8.741  8.116  1.00 20.62 ? 892  THR   A CA  1 
ATOM   1403 C C   . THR   A 1 200 ? 5.078   -8.751  9.663  1.00 20.15 ? 892  THR   A C   1 
ATOM   1404 O O   . THR   A 1 200 ? 4.693   -9.751  10.276 1.00 20.11 ? 892  THR   A O   1 
ATOM   1405 C CB  . THR   A 1 200 ? 4.145   -7.660  7.547  1.00 21.11 ? 892  THR   A CB  1 
ATOM   1406 O OG1 . THR   A 1 200 ? 2.877   -7.761  8.193  1.00 21.11 ? 892  THR   A OG1 1 
ATOM   1407 C CG2 . THR   A 1 200 ? 4.018   -7.715  6.032  1.00 21.85 ? 892  THR   A CG2 1 
ATOM   1408 N N   . HIS   A 1 201 ? 5.457   -7.627  10.297 1.00 19.35 ? 893  HIS   A N   1 
ATOM   1409 C CA  . HIS   A 1 201 ? 5.349   -7.467  11.736 1.00 19.18 ? 893  HIS   A CA  1 
ATOM   1410 C C   . HIS   A 1 201 ? 3.861   -7.581  12.137 1.00 18.29 ? 893  HIS   A C   1 
ATOM   1411 O O   . HIS   A 1 201 ? 3.569   -8.144  13.181 1.00 18.81 ? 893  HIS   A O   1 
ATOM   1412 C CB  . HIS   A 1 201 ? 5.929   -6.101  12.170 1.00 20.04 ? 893  HIS   A CB  1 
ATOM   1413 C CG  . HIS   A 1 201 ? 7.349   -5.895  11.744 1.00 22.41 ? 893  HIS   A CG  1 
ATOM   1414 N ND1 . HIS   A 1 201 ? 8.364   -6.707  12.211 1.00 24.42 ? 893  HIS   A ND1 1 
ATOM   1415 C CD2 . HIS   A 1 201 ? 7.877   -4.985  10.894 1.00 23.99 ? 893  HIS   A CD2 1 
ATOM   1416 C CE1 . HIS   A 1 201 ? 9.472   -6.279  11.622 1.00 25.13 ? 893  HIS   A CE1 1 
ATOM   1417 N NE2 . HIS   A 1 201 ? 9.230   -5.245  10.820 1.00 25.08 ? 893  HIS   A NE2 1 
ATOM   1418 N N   . GLN   A 1 202 ? 2.933   -7.101  11.285 1.00 16.96 ? 894  GLN   A N   1 
ATOM   1419 C CA  . GLN   A 1 202 ? 1.505   -7.172  11.571 1.00 16.47 ? 894  GLN   A CA  1 
ATOM   1420 C C   . GLN   A 1 202 ? 0.938   -8.601  11.431 1.00 15.12 ? 894  GLN   A C   1 
ATOM   1421 O O   . GLN   A 1 202 ? 0.040   -8.929  12.186 1.00 14.91 ? 894  GLN   A O   1 
ATOM   1422 C CB  . GLN   A 1 202 ? 0.700   -6.122  10.795 1.00 18.32 ? 894  GLN   A CB  1 
ATOM   1423 C CG  . GLN   A 1 202 ? 1.016   -4.678  11.257 1.00 21.35 ? 894  GLN   A CG  1 
ATOM   1424 C CD  . GLN   A 1 202 ? 0.892   -4.454  12.763 1.00 26.61 ? 894  GLN   A CD  1 
ATOM   1425 O OE1 . GLN   A 1 202 ? 1.897   -4.304  13.497 1.00 29.35 ? 894  GLN   A OE1 1 
ATOM   1426 N NE2 . GLN   A 1 202 ? -0.334  -4.421  13.261 1.00 25.23 ? 894  GLN   A NE2 1 
ATOM   1427 N N   . SER   A 1 203 ? 1.523   -9.482  10.601 1.00 14.37 ? 895  SER   A N   1 
ATOM   1428 C CA  . SER   A 1 203 ? 1.105   -10.895 10.592 1.00 14.36 ? 895  SER   A CA  1 
ATOM   1429 C C   . SER   A 1 203 ? 1.610   -11.585 11.867 1.00 15.26 ? 895  SER   A C   1 
ATOM   1430 O O   . SER   A 1 203 ? 0.888   -12.392 12.437 1.00 16.25 ? 895  SER   A O   1 
ATOM   1431 C CB  . SER   A 1 203 ? 1.577   -11.626 9.346  1.00 14.53 ? 895  SER   A CB  1 
ATOM   1432 O OG  . SER   A 1 203 ? 2.979   -11.578 9.202  1.00 16.48 ? 895  SER   A OG  1 
ATOM   1433 N N   . ASP   A 1 204 ? 2.790   -11.186 12.377 1.00 14.39 ? 896  ASP   A N   1 
ATOM   1434 C CA  . ASP   A 1 204 ? 3.350   -11.662 13.637 1.00 13.86 ? 896  ASP   A CA  1 
ATOM   1435 C C   . ASP   A 1 204 ? 2.419   -11.315 14.818 1.00 13.87 ? 896  ASP   A C   1 
ATOM   1436 O O   . ASP   A 1 204 ? 2.347   -12.067 15.794 1.00 13.75 ? 896  ASP   A O   1 
ATOM   1437 C CB  . ASP   A 1 204 ? 4.736   -11.037 13.871 1.00 14.30 ? 896  ASP   A CB  1 
ATOM   1438 C CG  . ASP   A 1 204 ? 5.912   -11.838 13.339 1.00 18.51 ? 896  ASP   A CG  1 
ATOM   1439 O OD1 . ASP   A 1 204 ? 5.704   -12.990 12.910 1.00 19.56 ? 896  ASP   A OD1 1 
ATOM   1440 O OD2 . ASP   A 1 204 ? 7.043   -11.314 13.362 1.00 20.24 ? 896  ASP   A OD2 1 
ATOM   1441 N N   . VAL   A 1 205 ? 1.739   -10.164 14.744 1.00 13.70 ? 897  VAL   A N   1 
ATOM   1442 C CA  . VAL   A 1 205 ? 0.773   -9.720  15.742 1.00 13.99 ? 897  VAL   A CA  1 
ATOM   1443 C C   . VAL   A 1 205 ? -0.394  -10.710 15.805 1.00 14.95 ? 897  VAL   A C   1 
ATOM   1444 O O   . VAL   A 1 205 ? -0.878  -11.018 16.899 1.00 15.16 ? 897  VAL   A O   1 
ATOM   1445 C CB  . VAL   A 1 205 ? 0.307   -8.283  15.416 1.00 14.36 ? 897  VAL   A CB  1 
ATOM   1446 C CG1 . VAL   A 1 205 ? -0.961  -7.901  16.189 1.00 14.76 ? 897  VAL   A CG1 1 
ATOM   1447 C CG2 . VAL   A 1 205 ? 1.430   -7.302  15.709 1.00 15.16 ? 897  VAL   A CG2 1 
ATOM   1448 N N   . TRP   A 1 206 ? -0.855  -11.208 14.636 1.00 15.24 ? 898  TRP   A N   1 
ATOM   1449 C CA  . TRP   A 1 206 ? -1.936  -12.189 14.565 1.00 15.95 ? 898  TRP   A CA  1 
ATOM   1450 C C   . TRP   A 1 206 ? -1.527  -13.467 15.316 1.00 16.93 ? 898  TRP   A C   1 
ATOM   1451 O O   . TRP   A 1 206 ? -2.289  -13.963 16.151 1.00 17.11 ? 898  TRP   A O   1 
ATOM   1452 C CB  . TRP   A 1 206 ? -2.261  -12.527 13.102 1.00 15.82 ? 898  TRP   A CB  1 
ATOM   1453 C CG  . TRP   A 1 206 ? -3.343  -13.560 12.940 1.00 16.68 ? 898  TRP   A CG  1 
ATOM   1454 C CD1 . TRP   A 1 206 ? -3.322  -14.853 13.370 1.00 17.43 ? 898  TRP   A CD1 1 
ATOM   1455 C CD2 . TRP   A 1 206 ? -4.584  -13.386 12.250 1.00 16.90 ? 898  TRP   A CD2 1 
ATOM   1456 N NE1 . TRP   A 1 206 ? -4.498  -15.474 13.043 1.00 17.88 ? 898  TRP   A NE1 1 
ATOM   1457 C CE2 . TRP   A 1 206 ? -5.269  -14.612 12.308 1.00 17.91 ? 898  TRP   A CE2 1 
ATOM   1458 C CE3 . TRP   A 1 206 ? -5.133  -12.348 11.495 1.00 17.84 ? 898  TRP   A CE3 1 
ATOM   1459 C CZ2 . TRP   A 1 206 ? -6.512  -14.800 11.706 1.00 19.05 ? 898  TRP   A CZ2 1 
ATOM   1460 C CZ3 . TRP   A 1 206 ? -6.369  -12.530 10.913 1.00 18.81 ? 898  TRP   A CZ3 1 
ATOM   1461 C CH2 . TRP   A 1 206 ? -7.049  -13.743 11.026 1.00 19.24 ? 898  TRP   A CH2 1 
ATOM   1462 N N   . SER   A 1 207 ? -0.302  -13.973 15.027 1.00 16.52 ? 899  SER   A N   1 
ATOM   1463 C CA  . SER   A 1 207 ? 0.271   -15.153 15.662 1.00 16.38 ? 899  SER   A CA  1 
ATOM   1464 C C   . SER   A 1 207 ? 0.383   -14.955 17.177 1.00 16.71 ? 899  SER   A C   1 
ATOM   1465 O O   . SER   A 1 207 ? 0.187   -15.908 17.935 1.00 17.71 ? 899  SER   A O   1 
ATOM   1466 C CB  . SER   A 1 207 ? 1.643   -15.429 15.080 1.00 16.96 ? 899  SER   A CB  1 
ATOM   1467 O OG  . SER   A 1 207 ? 1.579   -15.434 13.660 1.00 20.62 ? 899  SER   A OG  1 
ATOM   1468 N N   . TYR   A 1 208 ? 0.689   -13.723 17.610 1.00 15.38 ? 900  TYR   A N   1 
ATOM   1469 C CA  . TYR   A 1 208 ? 0.820   -13.367 19.003 1.00 15.52 ? 900  TYR   A CA  1 
ATOM   1470 C C   . TYR   A 1 208 ? -0.530  -13.533 19.710 1.00 15.93 ? 900  TYR   A C   1 
ATOM   1471 O O   . TYR   A 1 208 ? -0.581  -14.153 20.775 1.00 15.50 ? 900  TYR   A O   1 
ATOM   1472 C CB  . TYR   A 1 208 ? 1.420   -11.951 19.146 1.00 15.37 ? 900  TYR   A CB  1 
ATOM   1473 C CG  . TYR   A 1 208 ? 1.335   -11.389 20.550 1.00 15.74 ? 900  TYR   A CG  1 
ATOM   1474 C CD1 . TYR   A 1 208 ? 0.201   -10.711 20.981 1.00 16.18 ? 900  TYR   A CD1 1 
ATOM   1475 C CD2 . TYR   A 1 208 ? 2.384   -11.540 21.447 1.00 16.41 ? 900  TYR   A CD2 1 
ATOM   1476 C CE1 . TYR   A 1 208 ? 0.113   -10.191 22.261 1.00 16.72 ? 900  TYR   A CE1 1 
ATOM   1477 C CE2 . TYR   A 1 208 ? 2.300   -11.039 22.745 1.00 16.87 ? 900  TYR   A CE2 1 
ATOM   1478 C CZ  . TYR   A 1 208 ? 1.161   -10.360 23.147 1.00 17.35 ? 900  TYR   A CZ  1 
ATOM   1479 O OH  . TYR   A 1 208 ? 1.032   -9.861  24.428 1.00 17.67 ? 900  TYR   A OH  1 
ATOM   1480 N N   . GLY   A 1 209 ? -1.604  -13.060 19.066 1.00 16.46 ? 901  GLY   A N   1 
ATOM   1481 C CA  . GLY   A 1 209 ? -2.973  -13.192 19.542 1.00 16.31 ? 901  GLY   A CA  1 
ATOM   1482 C C   . GLY   A 1 209 ? -3.334  -14.653 19.731 1.00 16.84 ? 901  GLY   A C   1 
ATOM   1483 O O   . GLY   A 1 209 ? -3.864  -15.035 20.780 1.00 17.71 ? 901  GLY   A O   1 
ATOM   1484 N N   . VAL   A 1 210 ? -2.978  -15.494 18.753 1.00 16.31 ? 902  VAL   A N   1 
ATOM   1485 C CA  . VAL   A 1 210 ? -3.185  -16.943 18.865 1.00 16.73 ? 902  VAL   A CA  1 
ATOM   1486 C C   . VAL   A 1 210 ? -2.361  -17.508 20.033 1.00 16.45 ? 902  VAL   A C   1 
ATOM   1487 O O   . VAL   A 1 210 ? -2.876  -18.356 20.755 1.00 17.49 ? 902  VAL   A O   1 
ATOM   1488 C CB  . VAL   A 1 210 ? -2.917  -17.725 17.541 1.00 17.64 ? 902  VAL   A CB  1 
ATOM   1489 C CG1 . VAL   A 1 210 ? -3.227  -19.214 17.709 1.00 18.19 ? 902  VAL   A CG1 1 
ATOM   1490 C CG2 . VAL   A 1 210 ? -3.727  -17.145 16.379 1.00 17.66 ? 902  VAL   A CG2 1 
ATOM   1491 N N   . THR   A 1 211 ? -1.098  -17.034 20.235 1.00 14.95 ? 903  THR   A N   1 
ATOM   1492 C CA  . THR   A 1 211 ? -0.210  -17.465 21.334 1.00 13.81 ? 903  THR   A CA  1 
ATOM   1493 C C   . THR   A 1 211 ? -0.815  -17.114 22.736 1.00 13.30 ? 903  THR   A C   1 
ATOM   1494 O O   . THR   A 1 211 ? -0.768  -17.942 23.647 1.00 12.21 ? 903  THR   A O   1 
ATOM   1495 C CB  . THR   A 1 211 ? 1.218   -16.855 21.168 1.00 14.64 ? 903  THR   A CB  1 
ATOM   1496 O OG1 . THR   A 1 211 ? 1.748   -17.122 19.847 1.00 17.06 ? 903  THR   A OG1 1 
ATOM   1497 C CG2 . THR   A 1 211 ? 2.200   -17.347 22.242 1.00 12.81 ? 903  THR   A CG2 1 
ATOM   1498 N N   . VAL   A 1 212 ? -1.364  -15.870 22.896 1.00 13.16 ? 904  VAL   A N   1 
ATOM   1499 C CA  . VAL   A 1 212 ? -2.027  -15.405 24.125 1.00 13.63 ? 904  VAL   A CA  1 
ATOM   1500 C C   . VAL   A 1 212 ? -3.235  -16.301 24.407 1.00 14.63 ? 904  VAL   A C   1 
ATOM   1501 O O   . VAL   A 1 212 ? -3.492  -16.637 25.557 1.00 14.78 ? 904  VAL   A O   1 
ATOM   1502 C CB  . VAL   A 1 212 ? -2.483  -13.917 24.047 1.00 13.82 ? 904  VAL   A CB  1 
ATOM   1503 C CG1 . VAL   A 1 212 ? -3.161  -13.489 25.346 1.00 13.63 ? 904  VAL   A CG1 1 
ATOM   1504 C CG2 . VAL   A 1 212 ? -1.303  -12.995 23.746 1.00 14.15 ? 904  VAL   A CG2 1 
ATOM   1505 N N   . TRP   A 1 213 ? -3.966  -16.696 23.344 1.00 14.67 ? 905  TRP   A N   1 
ATOM   1506 C CA  . TRP   A 1 213 ? -5.125  -17.572 23.420 1.00 15.22 ? 905  TRP   A CA  1 
ATOM   1507 C C   . TRP   A 1 213 ? -4.709  -18.953 23.962 1.00 16.48 ? 905  TRP   A C   1 
ATOM   1508 O O   . TRP   A 1 213 ? -5.376  -19.480 24.842 1.00 17.04 ? 905  TRP   A O   1 
ATOM   1509 C CB  . TRP   A 1 213 ? -5.809  -17.676 22.036 1.00 14.58 ? 905  TRP   A CB  1 
ATOM   1510 C CG  . TRP   A 1 213 ? -7.071  -18.463 22.077 1.00 14.42 ? 905  TRP   A CG  1 
ATOM   1511 C CD1 . TRP   A 1 213 ? -8.324  -18.004 22.363 1.00 14.65 ? 905  TRP   A CD1 1 
ATOM   1512 C CD2 . TRP   A 1 213 ? -7.197  -19.875 21.859 1.00 14.15 ? 905  TRP   A CD2 1 
ATOM   1513 N NE1 . TRP   A 1 213 ? -9.210  -19.049 22.376 1.00 14.57 ? 905  TRP   A NE1 1 
ATOM   1514 C CE2 . TRP   A 1 213 ? -8.542  -20.211 22.077 1.00 14.20 ? 905  TRP   A CE2 1 
ATOM   1515 C CE3 . TRP   A 1 213 ? -6.284  -20.896 21.555 1.00 14.81 ? 905  TRP   A CE3 1 
ATOM   1516 C CZ2 . TRP   A 1 213 ? -9.007  -21.515 21.958 1.00 15.03 ? 905  TRP   A CZ2 1 
ATOM   1517 C CZ3 . TRP   A 1 213 ? -6.743  -22.187 21.460 1.00 15.38 ? 905  TRP   A CZ3 1 
ATOM   1518 C CH2 . TRP   A 1 213 ? -8.096  -22.481 21.621 1.00 15.34 ? 905  TRP   A CH2 1 
ATOM   1519 N N   . GLU   A 1 214 ? -3.586  -19.511 23.474 1.00 16.47 ? 906  GLU   A N   1 
ATOM   1520 C CA  . GLU   A 1 214 ? -3.049  -20.777 23.966 1.00 16.85 ? 906  GLU   A CA  1 
ATOM   1521 C C   . GLU   A 1 214 ? -2.747  -20.702 25.460 1.00 17.88 ? 906  GLU   A C   1 
ATOM   1522 O O   . GLU   A 1 214 ? -2.934  -21.691 26.156 1.00 18.12 ? 906  GLU   A O   1 
ATOM   1523 C CB  . GLU   A 1 214 ? -1.736  -21.113 23.271 1.00 16.82 ? 906  GLU   A CB  1 
ATOM   1524 C CG  . GLU   A 1 214 ? -1.869  -21.381 21.797 1.00 19.98 ? 906  GLU   A CG  1 
ATOM   1525 C CD  . GLU   A 1 214 ? -0.508  -21.754 21.254 1.00 21.49 ? 906  GLU   A CD  1 
ATOM   1526 O OE1 . GLU   A 1 214 ? 0.226   -20.824 20.850 1.00 18.84 ? 906  GLU   A OE1 1 
ATOM   1527 O OE2 . GLU   A 1 214 ? -0.149  -22.958 21.296 1.00 21.75 ? 906  GLU   A OE2 1 
ATOM   1528 N N   . LEU   A 1 215 ? -2.232  -19.566 25.940 1.00 18.38 ? 907  LEU   A N   1 
ATOM   1529 C CA  . LEU   A 1 215 ? -1.875  -19.421 27.346 1.00 19.80 ? 907  LEU   A CA  1 
ATOM   1530 C C   . LEU   A 1 215 ? -3.123  -19.359 28.218 1.00 20.79 ? 907  LEU   A C   1 
ATOM   1531 O O   . LEU   A 1 215 ? -3.232  -20.102 29.191 1.00 21.01 ? 907  LEU   A O   1 
ATOM   1532 C CB  . LEU   A 1 215 ? -0.995  -18.164 27.571 1.00 19.91 ? 907  LEU   A CB  1 
ATOM   1533 C CG  . LEU   A 1 215 ? 0.279   -18.084 26.740 1.00 20.67 ? 907  LEU   A CG  1 
ATOM   1534 C CD1 . LEU   A 1 215 ? 1.014   -16.758 26.994 1.00 21.09 ? 907  LEU   A CD1 1 
ATOM   1535 C CD2 . LEU   A 1 215 ? 1.177   -19.286 26.998 1.00 20.97 ? 907  LEU   A CD2 1 
ATOM   1536 N N   . MET   A 1 216 ? -4.069  -18.486 27.853 1.00 21.19 ? 908  MET   A N   1 
ATOM   1537 C CA  . MET   A 1 216 ? -5.330  -18.306 28.557 1.00 21.67 ? 908  MET   A CA  1 
ATOM   1538 C C   . MET   A 1 216 ? -6.170  -19.558 28.638 1.00 22.40 ? 908  MET   A C   1 
ATOM   1539 O O   . MET   A 1 216 ? -6.920  -19.711 29.593 1.00 23.33 ? 908  MET   A O   1 
ATOM   1540 C CB  . MET   A 1 216 ? -6.100  -17.159 27.943 1.00 21.64 ? 908  MET   A CB  1 
ATOM   1541 C CG  . MET   A 1 216 ? -5.304  -15.861 27.929 1.00 23.83 ? 908  MET   A CG  1 
ATOM   1542 S SD  . MET   A 1 216 ? -4.730  -15.354 29.565 1.00 28.95 ? 908  MET   A SD  1 
ATOM   1543 C CE  . MET   A 1 216 ? -4.191  -13.659 29.206 1.00 27.27 ? 908  MET   A CE  1 
ATOM   1544 N N   . THR   A 1 217 ? -6.018  -20.473 27.679 1.00 22.37 ? 909  THR   A N   1 
ATOM   1545 C CA  . THR   A 1 217 ? -6.714  -21.769 27.669 1.00 22.79 ? 909  THR   A CA  1 
ATOM   1546 C C   . THR   A 1 217 ? -5.878  -22.895 28.300 1.00 24.45 ? 909  THR   A C   1 
ATOM   1547 O O   . THR   A 1 217 ? -6.277  -24.062 28.223 1.00 25.01 ? 909  THR   A O   1 
ATOM   1548 C CB  . THR   A 1 217 ? -7.108  -22.171 26.241 1.00 23.21 ? 909  THR   A CB  1 
ATOM   1549 O OG1 . THR   A 1 217 ? -5.957  -22.195 25.390 1.00 23.85 ? 909  THR   A OG1 1 
ATOM   1550 C CG2 . THR   A 1 217 ? -8.193  -21.294 25.661 1.00 23.11 ? 909  THR   A CG2 1 
ATOM   1551 N N   . PHE   A 1 218 ? -4.697  -22.558 28.867 1.00 24.61 ? 910  PHE   A N   1 
ATOM   1552 C CA  . PHE   A 1 218 ? -3.783  -23.482 29.501 1.00 25.52 ? 910  PHE   A CA  1 
ATOM   1553 C C   . PHE   A 1 218 ? -3.361  -24.585 28.560 1.00 27.02 ? 910  PHE   A C   1 
ATOM   1554 O O   . PHE   A 1 218 ? -3.330  -25.756 28.952 1.00 27.91 ? 910  PHE   A O   1 
ATOM   1555 C CB  . PHE   A 1 218 ? -4.335  -24.014 30.837 1.00 25.78 ? 910  PHE   A CB  1 
ATOM   1556 C CG  . PHE   A 1 218 ? -4.784  -22.925 31.797 1.00 26.72 ? 910  PHE   A CG  1 
ATOM   1557 C CD1 . PHE   A 1 218 ? -3.875  -22.276 32.612 1.00 27.81 ? 910  PHE   A CD1 1 
ATOM   1558 C CD2 . PHE   A 1 218 ? -6.109  -22.540 31.865 1.00 27.43 ? 910  PHE   A CD2 1 
ATOM   1559 C CE1 . PHE   A 1 218 ? -4.285  -21.251 33.461 1.00 28.51 ? 910  PHE   A CE1 1 
ATOM   1560 C CE2 . PHE   A 1 218 ? -6.514  -21.519 32.720 1.00 28.02 ? 910  PHE   A CE2 1 
ATOM   1561 C CZ  . PHE   A 1 218 ? -5.601  -20.868 33.495 1.00 27.98 ? 910  PHE   A CZ  1 
ATOM   1562 N N   . GLY   A 1 219 ? -3.058  -24.204 27.315 1.00 27.03 ? 911  GLY   A N   1 
ATOM   1563 C CA  . GLY   A 1 219 ? -2.541  -25.100 26.294 1.00 27.29 ? 911  GLY   A CA  1 
ATOM   1564 C C   . GLY   A 1 219 ? -3.485  -25.689 25.273 1.00 28.25 ? 911  GLY   A C   1 
ATOM   1565 O O   . GLY   A 1 219 ? -3.059  -26.573 24.529 1.00 29.00 ? 911  GLY   A O   1 
ATOM   1566 N N   . SER   A 1 220 ? -4.746  -25.201 25.165 1.00 28.23 ? 912  SER   A N   1 
ATOM   1567 C CA  . SER   A 1 220 ? -5.674  -25.755 24.166 1.00 28.42 ? 912  SER   A CA  1 
ATOM   1568 C C   . SER   A 1 220 ? -5.159  -25.583 22.721 1.00 29.06 ? 912  SER   A C   1 
ATOM   1569 O O   . SER   A 1 220 ? -4.442  -24.623 22.414 1.00 28.96 ? 912  SER   A O   1 
ATOM   1570 C CB  . SER   A 1 220 ? -7.069  -25.140 24.293 1.00 29.25 ? 912  SER   A CB  1 
ATOM   1571 O OG  . SER   A 1 220 ? -7.677  -25.387 25.551 1.00 31.18 ? 912  SER   A OG  1 
ATOM   1572 N N   . LYS   A 1 221 ? -5.527  -26.518 21.838 1.00 29.28 ? 913  LYS   A N   1 
ATOM   1573 C CA  . LYS   A 1 221 ? -5.136  -26.448 20.434 1.00 30.09 ? 913  LYS   A CA  1 
ATOM   1574 C C   . LYS   A 1 221 ? -6.141  -25.554 19.706 1.00 30.34 ? 913  LYS   A C   1 
ATOM   1575 O O   . LYS   A 1 221 ? -7.342  -25.744 19.871 1.00 30.81 ? 913  LYS   A O   1 
ATOM   1576 C CB  . LYS   A 1 221 ? -5.129  -27.860 19.821 1.00 32.27 ? 913  LYS   A CB  1 
ATOM   1577 C CG  . LYS   A 1 221 ? -3.941  -28.713 20.257 1.00 36.09 ? 913  LYS   A CG  1 
ATOM   1578 C CD  . LYS   A 1 221 ? -4.367  -30.068 20.824 1.00 40.84 ? 913  LYS   A CD  1 
ATOM   1579 C CE  . LYS   A 1 221 ? -4.971  -30.984 19.791 1.00 44.97 ? 913  LYS   A CE  1 
ATOM   1580 N NZ  . LYS   A 1 221 ? -4.003  -32.019 19.333 1.00 47.81 ? 913  LYS   A NZ  1 
ATOM   1581 N N   . PRO   A 1 222 ? -5.694  -24.537 18.947 1.00 29.94 ? 914  PRO   A N   1 
ATOM   1582 C CA  . PRO   A 1 222 ? -6.666  -23.654 18.263 1.00 29.47 ? 914  PRO   A CA  1 
ATOM   1583 C C   . PRO   A 1 222 ? -7.393  -24.360 17.124 1.00 28.79 ? 914  PRO   A C   1 
ATOM   1584 O O   . PRO   A 1 222 ? -6.760  -25.135 16.410 1.00 29.03 ? 914  PRO   A O   1 
ATOM   1585 C CB  . PRO   A 1 222 ? -5.801  -22.496 17.758 1.00 30.07 ? 914  PRO   A CB  1 
ATOM   1586 C CG  . PRO   A 1 222 ? -4.441  -23.082 17.607 1.00 30.49 ? 914  PRO   A CG  1 
ATOM   1587 C CD  . PRO   A 1 222 ? -4.301  -24.135 18.679 1.00 29.24 ? 914  PRO   A CD  1 
ATOM   1588 N N   . TYR   A 1 223 ? -8.708  -24.094 16.949 1.00 28.08 ? 915  TYR   A N   1 
ATOM   1589 C CA  . TYR   A 1 223 ? -9.542  -24.709 15.899 1.00 27.91 ? 915  TYR   A CA  1 
ATOM   1590 C C   . TYR   A 1 223 ? -9.424  -26.248 15.933 1.00 29.91 ? 915  TYR   A C   1 
ATOM   1591 O O   . TYR   A 1 223 ? -9.106  -26.877 14.917 1.00 29.75 ? 915  TYR   A O   1 
ATOM   1592 C CB  . TYR   A 1 223 ? -9.208  -24.176 14.489 1.00 26.05 ? 915  TYR   A CB  1 
ATOM   1593 C CG  . TYR   A 1 223 ? -8.868  -22.703 14.424 1.00 24.89 ? 915  TYR   A CG  1 
ATOM   1594 C CD1 . TYR   A 1 223 ? -9.869  -21.735 14.366 1.00 24.76 ? 915  TYR   A CD1 1 
ATOM   1595 C CD2 . TYR   A 1 223 ? -7.550  -22.278 14.362 1.00 24.20 ? 915  TYR   A CD2 1 
ATOM   1596 C CE1 . TYR   A 1 223 ? -9.560  -20.383 14.270 1.00 24.52 ? 915  TYR   A CE1 1 
ATOM   1597 C CE2 . TYR   A 1 223 ? -7.232  -20.934 14.268 1.00 24.28 ? 915  TYR   A CE2 1 
ATOM   1598 C CZ  . TYR   A 1 223 ? -8.235  -19.987 14.224 1.00 24.79 ? 915  TYR   A CZ  1 
ATOM   1599 O OH  . TYR   A 1 223 ? -7.893  -18.662 14.132 1.00 25.19 ? 915  TYR   A OH  1 
ATOM   1600 N N   . ASP   A 1 224 ? -9.606  -26.837 17.123 1.00 31.37 ? 916  ASP   A N   1 
ATOM   1601 C CA  . ASP   A 1 224 ? -9.506  -28.282 17.268 1.00 33.56 ? 916  ASP   A CA  1 
ATOM   1602 C C   . ASP   A 1 224 ? -10.635 -28.959 16.496 1.00 35.41 ? 916  ASP   A C   1 
ATOM   1603 O O   . ASP   A 1 224 ? -11.788 -28.507 16.528 1.00 34.90 ? 916  ASP   A O   1 
ATOM   1604 C CB  . ASP   A 1 224 ? -9.523  -28.698 18.752 1.00 35.72 ? 916  ASP   A CB  1 
ATOM   1605 C CG  . ASP   A 1 224 ? -8.810  -30.016 19.039 1.00 41.13 ? 916  ASP   A CG  1 
ATOM   1606 O OD1 . ASP   A 1 224 ? -8.123  -30.541 18.121 1.00 41.44 ? 916  ASP   A OD1 1 
ATOM   1607 O OD2 . ASP   A 1 224 ? -8.924  -30.517 20.185 1.00 43.78 ? 916  ASP   A OD2 1 
ATOM   1608 N N   . GLY   A 1 225 ? -10.273 -30.001 15.760 1.00 37.08 ? 917  GLY   A N   1 
ATOM   1609 C CA  . GLY   A 1 225 ? -11.228 -30.748 14.947 1.00 38.65 ? 917  GLY   A CA  1 
ATOM   1610 C C   . GLY   A 1 225 ? -11.497 -30.154 13.574 1.00 39.68 ? 917  GLY   A C   1 
ATOM   1611 O O   . GLY   A 1 225 ? -12.265 -30.729 12.793 1.00 40.04 ? 917  GLY   A O   1 
ATOM   1612 N N   . ILE   A 1 226 ? -10.881 -28.999 13.264 1.00 39.44 ? 918  ILE   A N   1 
ATOM   1613 C CA  . ILE   A 1 226 ? -11.078 -28.351 11.979 1.00 39.82 ? 918  ILE   A CA  1 
ATOM   1614 C C   . ILE   A 1 226 ? -9.881  -28.607 11.101 1.00 40.75 ? 918  ILE   A C   1 
ATOM   1615 O O   . ILE   A 1 226 ? -8.758  -28.294 11.494 1.00 41.12 ? 918  ILE   A O   1 
ATOM   1616 C CB  . ILE   A 1 226 ? -11.299 -26.835 12.158 1.00 39.96 ? 918  ILE   A CB  1 
ATOM   1617 C CG1 . ILE   A 1 226 ? -12.545 -26.549 13.013 1.00 40.82 ? 918  ILE   A CG1 1 
ATOM   1618 C CG2 . ILE   A 1 226 ? -11.357 -26.138 10.803 1.00 40.12 ? 918  ILE   A CG2 1 
ATOM   1619 C CD1 . ILE   A 1 226 ? -12.888 -25.054 13.216 1.00 41.97 ? 918  ILE   A CD1 1 
ATOM   1620 N N   . PRO   A 1 227 ? -10.087 -29.141 9.889  1.00 40.91 ? 919  PRO   A N   1 
ATOM   1621 C CA  . PRO   A 1 227 ? -8.939  -29.368 8.997  1.00 40.85 ? 919  PRO   A CA  1 
ATOM   1622 C C   . PRO   A 1 227 ? -8.291  -28.057 8.596  1.00 40.70 ? 919  PRO   A C   1 
ATOM   1623 O O   . PRO   A 1 227 ? -8.985  -27.075 8.360  1.00 41.01 ? 919  PRO   A O   1 
ATOM   1624 C CB  . PRO   A 1 227 ? -9.551  -30.079 7.785  1.00 41.55 ? 919  PRO   A CB  1 
ATOM   1625 C CG  . PRO   A 1 227 ? -10.994 -29.738 7.824  1.00 42.04 ? 919  PRO   A CG  1 
ATOM   1626 C CD  . PRO   A 1 227 ? -11.356 -29.566 9.272  1.00 40.50 ? 919  PRO   A CD  1 
ATOM   1627 N N   . ALA   A 1 228 ? -6.959  -28.055 8.514  1.00 40.41 ? 920  ALA   A N   1 
ATOM   1628 C CA  . ALA   A 1 228 ? -6.136  -26.911 8.130  1.00 40.27 ? 920  ALA   A CA  1 
ATOM   1629 C C   . ALA   A 1 228 ? -6.615  -26.237 6.840  1.00 39.93 ? 920  ALA   A C   1 
ATOM   1630 O O   . ALA   A 1 228 ? -6.449  -25.023 6.684  1.00 40.43 ? 920  ALA   A O   1 
ATOM   1631 C CB  . ALA   A 1 228 ? -4.691  -27.359 7.976  1.00 40.27 ? 920  ALA   A CB  1 
ATOM   1632 N N   . SER   A 1 229 ? -7.219  -27.016 5.928  1.00 38.87 ? 921  SER   A N   1 
ATOM   1633 C CA  . SER   A 1 229 ? -7.725  -26.506 4.656  1.00 38.74 ? 921  SER   A CA  1 
ATOM   1634 C C   . SER   A 1 229 ? -8.943  -25.600 4.795  1.00 37.38 ? 921  SER   A C   1 
ATOM   1635 O O   . SER   A 1 229 ? -9.164  -24.731 3.952  1.00 37.01 ? 921  SER   A O   1 
ATOM   1636 C CB  . SER   A 1 229 ? -8.007  -27.645 3.675  1.00 41.34 ? 921  SER   A CB  1 
ATOM   1637 O OG  . SER   A 1 229 ? -8.501  -28.830 4.285  1.00 44.97 ? 921  SER   A OG  1 
ATOM   1638 N N   . GLU   A 1 230 ? -9.721  -25.784 5.866  1.00 36.50 ? 922  GLU   A N   1 
ATOM   1639 C CA  . GLU   A 1 230 ? -10.925 -25.001 6.095  1.00 35.76 ? 922  GLU   A CA  1 
ATOM   1640 C C   . GLU   A 1 230 ? -10.692 -23.649 6.767  1.00 33.74 ? 922  GLU   A C   1 
ATOM   1641 O O   . GLU   A 1 230 ? -11.541 -22.762 6.663  1.00 33.93 ? 922  GLU   A O   1 
ATOM   1642 C CB  . GLU   A 1 230 ? -11.953 -25.825 6.884  1.00 39.47 ? 922  GLU   A CB  1 
ATOM   1643 C CG  . GLU   A 1 230 ? -12.620 -26.931 6.073  1.00 47.60 ? 922  GLU   A CG  1 
ATOM   1644 C CD  . GLU   A 1 230 ? -13.093 -26.540 4.682  1.00 57.49 ? 922  GLU   A CD  1 
ATOM   1645 O OE1 . GLU   A 1 230 ? -14.027 -25.708 4.583  1.00 60.45 ? 922  GLU   A OE1 1 
ATOM   1646 O OE2 . GLU   A 1 230 ? -12.514 -27.047 3.691  1.00 59.31 ? 922  GLU   A OE2 1 
ATOM   1647 N N   . ILE   A 1 231 ? -9.556  -23.497 7.460  1.00 31.53 ? 923  ILE   A N   1 
ATOM   1648 C CA  . ILE   A 1 231 ? -9.203  -22.289 8.203  1.00 29.57 ? 923  ILE   A CA  1 
ATOM   1649 C C   . ILE   A 1 231 ? -9.364  -20.963 7.431  1.00 27.90 ? 923  ILE   A C   1 
ATOM   1650 O O   . ILE   A 1 231 ? -9.945  -20.041 7.983  1.00 27.42 ? 923  ILE   A O   1 
ATOM   1651 C CB  . ILE   A 1 231 ? -7.781  -22.431 8.774  1.00 29.37 ? 923  ILE   A CB  1 
ATOM   1652 C CG1 . ILE   A 1 231 ? -7.681  -23.677 9.668  1.00 30.04 ? 923  ILE   A CG1 1 
ATOM   1653 C CG2 . ILE   A 1 231 ? -7.353  -21.170 9.520  1.00 29.57 ? 923  ILE   A CG2 1 
ATOM   1654 C CD1 . ILE   A 1 231 ? -8.615  -23.668 10.883 1.00 30.81 ? 923  ILE   A CD1 1 
ATOM   1655 N N   . SER   A 1 232 ? -8.887  -20.863 6.183  1.00 27.36 ? 924  SER   A N   1 
ATOM   1656 C CA  . SER   A 1 232 ? -8.980  -19.612 5.423  1.00 27.69 ? 924  SER   A CA  1 
ATOM   1657 C C   . SER   A 1 232 ? -10.408 -19.185 5.129  1.00 28.62 ? 924  SER   A C   1 
ATOM   1658 O O   . SER   A 1 232 ? -10.723 -17.991 5.195  1.00 29.01 ? 924  SER   A O   1 
ATOM   1659 C CB  . SER   A 1 232 ? -8.162  -19.679 4.138  1.00 28.58 ? 924  SER   A CB  1 
ATOM   1660 O OG  . SER   A 1 232 ? -8.673  -20.631 3.221  1.00 30.53 ? 924  SER   A OG  1 
ATOM   1661 N N   . SER   A 1 233 ? -11.277 -20.149 4.810  1.00 28.89 ? 925  SER   A N   1 
ATOM   1662 C CA  . SER   A 1 233 ? -12.684 -19.837 4.555  1.00 29.53 ? 925  SER   A CA  1 
ATOM   1663 C C   . SER   A 1 233 ? -13.442 -19.570 5.862  1.00 28.70 ? 925  SER   A C   1 
ATOM   1664 O O   . SER   A 1 233 ? -14.359 -18.754 5.887  1.00 28.41 ? 925  SER   A O   1 
ATOM   1665 C CB  . SER   A 1 233 ? -13.361 -20.950 3.772  1.00 32.24 ? 925  SER   A CB  1 
ATOM   1666 O OG  . SER   A 1 233 ? -14.586 -20.419 3.290  1.00 37.02 ? 925  SER   A OG  1 
ATOM   1667 N N   . ILE   A 1 234 ? -13.021 -20.224 6.957  1.00 28.07 ? 926  ILE   A N   1 
ATOM   1668 C CA  . ILE   A 1 234 ? -13.573 -20.004 8.295  1.00 27.53 ? 926  ILE   A CA  1 
ATOM   1669 C C   . ILE   A 1 234 ? -13.253 -18.581 8.747  1.00 26.26 ? 926  ILE   A C   1 
ATOM   1670 O O   . ILE   A 1 234 ? -14.116 -17.919 9.301  1.00 25.72 ? 926  ILE   A O   1 
ATOM   1671 C CB  . ILE   A 1 234 ? -13.010 -21.105 9.224  1.00 28.69 ? 926  ILE   A CB  1 
ATOM   1672 C CG1 . ILE   A 1 234 ? -13.855 -22.372 9.094  1.00 29.72 ? 926  ILE   A CG1 1 
ATOM   1673 C CG2 . ILE   A 1 234 ? -12.860 -20.668 10.688 1.00 29.47 ? 926  ILE   A CG2 1 
ATOM   1674 C CD1 . ILE   A 1 234 ? -13.200 -23.545 9.639  1.00 31.14 ? 926  ILE   A CD1 1 
ATOM   1675 N N   . LEU   A 1 235 ? -12.040 -18.078 8.423  1.00 25.89 ? 927  LEU   A N   1 
ATOM   1676 C CA  . LEU   A 1 235 ? -11.618 -16.723 8.765  1.00 25.97 ? 927  LEU   A CA  1 
ATOM   1677 C C   . LEU   A 1 235 ? -12.357 -15.701 7.949  1.00 27.04 ? 927  LEU   A C   1 
ATOM   1678 O O   . LEU   A 1 235 ? -12.836 -14.707 8.501  1.00 27.09 ? 927  LEU   A O   1 
ATOM   1679 C CB  . LEU   A 1 235 ? -10.099 -16.545 8.576  1.00 25.18 ? 927  LEU   A CB  1 
ATOM   1680 C CG  . LEU   A 1 235 ? -9.222  -17.332 9.522  1.00 25.89 ? 927  LEU   A CG  1 
ATOM   1681 C CD1 . LEU   A 1 235 ? -7.758  -17.133 9.189  1.00 26.29 ? 927  LEU   A CD1 1 
ATOM   1682 C CD2 . LEU   A 1 235 ? -9.542  -17.007 10.985 1.00 25.83 ? 927  LEU   A CD2 1 
ATOM   1683 N N   . GLU   A 1 236 ? -12.487 -15.950 6.636  1.00 27.94 ? 928  GLU   A N   1 
ATOM   1684 C CA  . GLU   A 1 236 ? -13.221 -15.058 5.743  1.00 29.00 ? 928  GLU   A CA  1 
ATOM   1685 C C   . GLU   A 1 236 ? -14.690 -14.908 6.173  1.00 29.39 ? 928  GLU   A C   1 
ATOM   1686 O O   . GLU   A 1 236 ? -15.232 -13.812 6.082  1.00 30.03 ? 928  GLU   A O   1 
ATOM   1687 C CB  . GLU   A 1 236 ? -13.050 -15.488 4.276  1.00 31.99 ? 928  GLU   A CB  1 
ATOM   1688 C CG  . GLU   A 1 236 ? -11.705 -15.017 3.743  1.00 38.01 ? 928  GLU   A CG  1 
ATOM   1689 C CD  . GLU   A 1 236 ? -11.186 -15.575 2.428  1.00 46.59 ? 928  GLU   A CD  1 
ATOM   1690 O OE1 . GLU   A 1 236 ? -11.182 -16.818 2.255  1.00 47.92 ? 928  GLU   A OE1 1 
ATOM   1691 O OE2 . GLU   A 1 236 ? -10.728 -14.761 1.590  1.00 48.54 ? 928  GLU   A OE2 1 
ATOM   1692 N N   . LYS   A 1 237 ? -15.295 -15.962 6.745  1.00 29.10 ? 929  LYS   A N   1 
ATOM   1693 C CA  . LYS   A 1 237 ? -16.671 -15.897 7.282  1.00 29.79 ? 929  LYS   A CA  1 
ATOM   1694 C C   . LYS   A 1 237 ? -16.778 -15.018 8.568  1.00 29.06 ? 929  LYS   A C   1 
ATOM   1695 O O   . LYS   A 1 237 ? -17.883 -14.640 8.974  1.00 29.18 ? 929  LYS   A O   1 
ATOM   1696 C CB  . LYS   A 1 237 ? -17.194 -17.315 7.629  1.00 32.91 ? 929  LYS   A CB  1 
ATOM   1697 C CG  . LYS   A 1 237 ? -17.639 -18.159 6.446  1.00 38.71 ? 929  LYS   A CG  1 
ATOM   1698 C CD  . LYS   A 1 237 ? -18.268 -19.476 6.928  1.00 45.12 ? 929  LYS   A CD  1 
ATOM   1699 C CE  . LYS   A 1 237 ? -17.263 -20.416 7.566  1.00 49.76 ? 929  LYS   A CE  1 
ATOM   1700 N NZ  . LYS   A 1 237 ? -17.916 -21.550 8.284  1.00 52.14 ? 929  LYS   A NZ  1 
ATOM   1701 N N   . GLY   A 1 238 ? -15.647 -14.771 9.226  1.00 27.89 ? 930  GLY   A N   1 
ATOM   1702 C CA  . GLY   A 1 238 ? -15.604 -13.981 10.446 1.00 27.06 ? 930  GLY   A CA  1 
ATOM   1703 C C   . GLY   A 1 238 ? -15.489 -14.798 11.714 1.00 25.86 ? 930  GLY   A C   1 
ATOM   1704 O O   . GLY   A 1 238 ? -15.553 -14.236 12.808 1.00 26.38 ? 930  GLY   A O   1 
ATOM   1705 N N   . GLU   A 1 239 ? -15.332 -16.117 11.595 1.00 24.43 ? 931  GLU   A N   1 
ATOM   1706 C CA  . GLU   A 1 239 ? -15.151 -16.967 12.764 1.00 24.29 ? 931  GLU   A CA  1 
ATOM   1707 C C   . GLU   A 1 239 ? -13.759 -16.705 13.356 1.00 23.69 ? 931  GLU   A C   1 
ATOM   1708 O O   . GLU   A 1 239 ? -12.803 -16.539 12.605 1.00 24.68 ? 931  GLU   A O   1 
ATOM   1709 C CB  . GLU   A 1 239 ? -15.238 -18.452 12.387 1.00 26.66 ? 931  GLU   A CB  1 
ATOM   1710 C CG  . GLU   A 1 239 ? -16.641 -18.953 12.104 1.00 32.50 ? 931  GLU   A CG  1 
ATOM   1711 C CD  . GLU   A 1 239 ? -16.705 -20.463 12.209 1.00 41.80 ? 931  GLU   A CD  1 
ATOM   1712 O OE1 . GLU   A 1 239 ? -17.104 -21.119 11.217 1.00 44.60 ? 931  GLU   A OE1 1 
ATOM   1713 O OE2 . GLU   A 1 239 ? -16.329 -20.994 13.280 1.00 44.04 ? 931  GLU   A OE2 1 
ATOM   1714 N N   . ARG   A 1 240 ? -13.648 -16.657 14.689 1.00 21.73 ? 932  ARG   A N   1 
ATOM   1715 C CA  . ARG   A 1 240 ? -12.385 -16.476 15.405 1.00 20.47 ? 932  ARG   A CA  1 
ATOM   1716 C C   . ARG   A 1 240 ? -12.328 -17.455 16.599 1.00 19.20 ? 932  ARG   A C   1 
ATOM   1717 O O   . ARG   A 1 240 ? -13.301 -18.158 16.878 1.00 19.76 ? 932  ARG   A O   1 
ATOM   1718 C CB  . ARG   A 1 240 ? -12.221 -15.012 15.883 1.00 21.47 ? 932  ARG   A CB  1 
ATOM   1719 C CG  . ARG   A 1 240 ? -12.124 -13.976 14.762 1.00 23.16 ? 932  ARG   A CG  1 
ATOM   1720 C CD  . ARG   A 1 240 ? -10.908 -14.163 13.881 1.00 24.62 ? 932  ARG   A CD  1 
ATOM   1721 N NE  . ARG   A 1 240 ? -10.742 -13.039 12.956 1.00 26.38 ? 932  ARG   A NE  1 
ATOM   1722 C CZ  . ARG   A 1 240 ? -11.229 -13.007 11.719 1.00 26.60 ? 932  ARG   A CZ  1 
ATOM   1723 N NH1 . ARG   A 1 240 ? -11.906 -14.043 11.236 1.00 25.53 ? 932  ARG   A NH1 1 
ATOM   1724 N NH2 . ARG   A 1 240 ? -11.044 -11.937 10.956 1.00 24.79 ? 932  ARG   A NH2 1 
ATOM   1725 N N   . LEU   A 1 241 ? -11.209 -17.517 17.289 1.00 18.11 ? 933  LEU   A N   1 
ATOM   1726 C CA  . LEU   A 1 241 ? -11.043 -18.396 18.451 1.00 18.00 ? 933  LEU   A CA  1 
ATOM   1727 C C   . LEU   A 1 241 ? -11.985 -17.973 19.590 1.00 18.84 ? 933  LEU   A C   1 
ATOM   1728 O O   . LEU   A 1 241 ? -12.285 -16.784 19.728 1.00 19.14 ? 933  LEU   A O   1 
ATOM   1729 C CB  . LEU   A 1 241 ? -9.575  -18.381 18.898 1.00 16.77 ? 933  LEU   A CB  1 
ATOM   1730 C CG  . LEU   A 1 241 ? -8.651  -18.986 17.877 1.00 15.60 ? 933  LEU   A CG  1 
ATOM   1731 C CD1 . LEU   A 1 241 ? -7.220  -18.583 18.143 1.00 16.29 ? 933  LEU   A CD1 1 
ATOM   1732 C CD2 . LEU   A 1 241 ? -8.834  -20.476 17.820 1.00 14.64 ? 933  LEU   A CD2 1 
ATOM   1733 N N   . PRO   A 1 242 ? -12.578 -18.938 20.319 1.00 18.67 ? 934  PRO   A N   1 
ATOM   1734 C CA  . PRO   A 1 242 ? -13.552 -18.559 21.357 1.00 18.41 ? 934  PRO   A CA  1 
ATOM   1735 C C   . PRO   A 1 242 ? -12.923 -17.810 22.515 1.00 18.61 ? 934  PRO   A C   1 
ATOM   1736 O O   . PRO   A 1 242 ? -11.715 -17.898 22.741 1.00 18.64 ? 934  PRO   A O   1 
ATOM   1737 C CB  . PRO   A 1 242 ? -14.120 -19.906 21.827 1.00 18.65 ? 934  PRO   A CB  1 
ATOM   1738 C CG  . PRO   A 1 242 ? -13.081 -20.904 21.502 1.00 18.92 ? 934  PRO   A CG  1 
ATOM   1739 C CD  . PRO   A 1 242 ? -12.408 -20.405 20.237 1.00 17.72 ? 934  PRO   A CD  1 
ATOM   1740 N N   . GLN   A 1 243 ? -13.743 -17.098 23.277 1.00 18.48 ? 935  GLN   A N   1 
ATOM   1741 C CA  . GLN   A 1 243 ? -13.268 -16.394 24.464 1.00 19.32 ? 935  GLN   A CA  1 
ATOM   1742 C C   . GLN   A 1 243 ? -12.854 -17.417 25.499 1.00 19.04 ? 935  GLN   A C   1 
ATOM   1743 O O   . GLN   A 1 243 ? -13.714 -18.156 25.925 1.00 18.56 ? 935  GLN   A O   1 
ATOM   1744 C CB  . GLN   A 1 243 ? -14.411 -15.562 25.073 1.00 20.81 ? 935  GLN   A CB  1 
ATOM   1745 C CG  . GLN   A 1 243 ? -13.978 -14.652 26.223 1.00 23.39 ? 935  GLN   A CG  1 
ATOM   1746 C CD  . GLN   A 1 243 ? -15.072 -13.665 26.581 1.00 27.07 ? 935  GLN   A CD  1 
ATOM   1747 O OE1 . GLN   A 1 243 ? -15.899 -13.278 25.741 1.00 27.72 ? 935  GLN   A OE1 1 
ATOM   1748 N NE2 . GLN   A 1 243 ? -15.109 -13.225 27.838 1.00 26.42 ? 935  GLN   A NE2 1 
ATOM   1749 N N   . PRO   A 1 244 ? -11.577 -17.493 25.926 1.00 19.33 ? 936  PRO   A N   1 
ATOM   1750 C CA  . PRO   A 1 244 ? -11.218 -18.442 26.999 1.00 19.27 ? 936  PRO   A CA  1 
ATOM   1751 C C   . PRO   A 1 244 ? -11.988 -18.123 28.286 1.00 19.26 ? 936  PRO   A C   1 
ATOM   1752 O O   . PRO   A 1 244 ? -12.204 -16.959 28.602 1.00 19.59 ? 936  PRO   A O   1 
ATOM   1753 C CB  . PRO   A 1 244 ? -9.704  -18.219 27.186 1.00 19.99 ? 936  PRO   A CB  1 
ATOM   1754 C CG  . PRO   A 1 244 ? -9.244  -17.526 25.933 1.00 20.33 ? 936  PRO   A CG  1 
ATOM   1755 C CD  . PRO   A 1 244 ? -10.427 -16.661 25.542 1.00 19.14 ? 936  PRO   A CD  1 
ATOM   1756 N N   . PRO   A 1 245 ? -12.419 -19.140 29.031 1.00 19.32 ? 937  PRO   A N   1 
ATOM   1757 C CA  . PRO   A 1 245 ? -13.240 -18.884 30.236 1.00 19.51 ? 937  PRO   A CA  1 
ATOM   1758 C C   . PRO   A 1 245 ? -12.683 -17.928 31.310 1.00 20.48 ? 937  PRO   A C   1 
ATOM   1759 O O   . PRO   A 1 245 ? -13.446 -17.437 32.148 1.00 20.95 ? 937  PRO   A O   1 
ATOM   1760 C CB  . PRO   A 1 245 ? -13.448 -20.281 30.832 1.00 19.90 ? 937  PRO   A CB  1 
ATOM   1761 C CG  . PRO   A 1 245 ? -13.158 -21.235 29.747 1.00 20.23 ? 937  PRO   A CG  1 
ATOM   1762 C CD  . PRO   A 1 245 ? -12.292 -20.582 28.731 1.00 18.83 ? 937  PRO   A CD  1 
ATOM   1763 N N   . ILE   A 1 246 ? -11.367 -17.720 31.352 1.00 20.22 ? 938  ILE   A N   1 
ATOM   1764 C CA  . ILE   A 1 246 ? -10.754 -16.867 32.372 1.00 20.86 ? 938  ILE   A CA  1 
ATOM   1765 C C   . ILE   A 1 246 ? -10.618 -15.388 31.943 1.00 22.05 ? 938  ILE   A C   1 
ATOM   1766 O O   . ILE   A 1 246 ? -10.297 -14.527 32.758 1.00 22.55 ? 938  ILE   A O   1 
ATOM   1767 C CB  . ILE   A 1 246 ? -9.372  -17.456 32.741 1.00 21.25 ? 938  ILE   A CB  1 
ATOM   1768 C CG1 . ILE   A 1 246 ? -8.377  -17.336 31.547 1.00 22.38 ? 938  ILE   A CG1 1 
ATOM   1769 C CG2 . ILE   A 1 246 ? -9.489  -18.913 33.195 1.00 21.31 ? 938  ILE   A CG2 1 
ATOM   1770 C CD1 . ILE   A 1 246 ? -6.907  -17.100 31.994 1.00 22.91 ? 938  ILE   A CD1 1 
ATOM   1771 N N   . CYS   A 1 247 ? -10.812 -15.109 30.666 1.00 21.68 ? 939  CYS   A N   1 
ATOM   1772 C CA  . CYS   A 1 247 ? -10.618 -13.801 30.107 1.00 21.94 ? 939  CYS   A CA  1 
ATOM   1773 C C   . CYS   A 1 247 ? -11.834 -12.954 30.222 1.00 21.66 ? 939  CYS   A C   1 
ATOM   1774 O O   . CYS   A 1 247 ? -12.846 -13.286 29.619 1.00 21.17 ? 939  CYS   A O   1 
ATOM   1775 C CB  . CYS   A 1 247 ? -10.206 -13.922 28.637 1.00 23.22 ? 939  CYS   A CB  1 
ATOM   1776 S SG  . CYS   A 1 247 ? -8.549  -14.603 28.368 1.00 26.99 ? 939  CYS   A SG  1 
ATOM   1777 N N   . THR   A 1 248 ? -11.675 -11.757 30.771 1.00 21.45 ? 940  THR   A N   1 
ATOM   1778 C CA  . THR   A 1 248 ? -12.735 -10.775 30.727 1.00 21.57 ? 940  THR   A CA  1 
ATOM   1779 C C   . THR   A 1 248 ? -12.867 -10.258 29.268 1.00 22.67 ? 940  THR   A C   1 
ATOM   1780 O O   . THR   A 1 248 ? -11.982 -10.482 28.418 1.00 22.90 ? 940  THR   A O   1 
ATOM   1781 C CB  . THR   A 1 248 ? -12.448 -9.674  31.724 1.00 21.57 ? 940  THR   A CB  1 
ATOM   1782 O OG1 . THR   A 1 248 ? -11.194 -9.100  31.404 1.00 22.43 ? 940  THR   A OG1 1 
ATOM   1783 C CG2 . THR   A 1 248 ? -12.494 -10.161 33.164 1.00 20.74 ? 940  THR   A CG2 1 
ATOM   1784 N N   . ILE   A 1 249 ? -13.961 -9.557  28.979 1.00 22.92 ? 941  ILE   A N   1 
ATOM   1785 C CA  . ILE   A 1 249 ? -14.196 -9.003  27.648 1.00 23.85 ? 941  ILE   A CA  1 
ATOM   1786 C C   . ILE   A 1 249 ? -13.081 -8.030  27.182 1.00 24.51 ? 941  ILE   A C   1 
ATOM   1787 O O   . ILE   A 1 249 ? -12.775 -8.006  25.993 1.00 24.69 ? 941  ILE   A O   1 
ATOM   1788 C CB  . ILE   A 1 249 ? -15.598 -8.369  27.582 1.00 24.15 ? 941  ILE   A CB  1 
ATOM   1789 C CG1 . ILE   A 1 249 ? -16.062 -8.202  26.134 1.00 25.01 ? 941  ILE   A CG1 1 
ATOM   1790 C CG2 . ILE   A 1 249 ? -15.677 -7.080  28.390 1.00 24.63 ? 941  ILE   A CG2 1 
ATOM   1791 C CD1 . ILE   A 1 249 ? -16.233 -9.541  25.432 1.00 26.27 ? 941  ILE   A CD1 1 
ATOM   1792 N N   . ASP   A 1 250 ? -12.451 -7.265  28.104 1.00 24.39 ? 942  ASP   A N   1 
ATOM   1793 C CA  . ASP   A 1 250 ? -11.342 -6.388  27.720 1.00 24.89 ? 942  ASP   A CA  1 
ATOM   1794 C C   . ASP   A 1 250 ? -10.121 -7.220  27.240 1.00 24.01 ? 942  ASP   A C   1 
ATOM   1795 O O   . ASP   A 1 250 ? -9.452  -6.825  26.280 1.00 23.33 ? 942  ASP   A O   1 
ATOM   1796 C CB  . ASP   A 1 250 ? -10.942 -5.461  28.872 1.00 27.71 ? 942  ASP   A CB  1 
ATOM   1797 C CG  . ASP   A 1 250 ? -11.910 -4.321  29.114 1.00 34.24 ? 942  ASP   A CG  1 
ATOM   1798 O OD1 . ASP   A 1 250 ? -12.419 -3.747  28.117 1.00 34.96 ? 942  ASP   A OD1 1 
ATOM   1799 O OD2 . ASP   A 1 250 ? -12.146 -3.985  30.302 1.00 37.10 ? 942  ASP   A OD2 1 
ATOM   1800 N N   . VAL   A 1 251 ? -9.871  -8.389  27.862 1.00 23.78 ? 943  VAL   A N   1 
ATOM   1801 C CA  . VAL   A 1 251 ? -8.763  -9.244  27.417 1.00 24.37 ? 943  VAL   A CA  1 
ATOM   1802 C C   . VAL   A 1 251 ? -9.116  -9.853  26.061 1.00 24.12 ? 943  VAL   A C   1 
ATOM   1803 O O   . VAL   A 1 251 ? -8.315  -9.800  25.118 1.00 24.26 ? 943  VAL   A O   1 
ATOM   1804 C CB  . VAL   A 1 251 ? -8.359  -10.311 28.462 1.00 25.75 ? 943  VAL   A CB  1 
ATOM   1805 C CG1 . VAL   A 1 251 ? -7.220  -11.178 27.938 1.00 26.24 ? 943  VAL   A CG1 1 
ATOM   1806 C CG2 . VAL   A 1 251 ? -7.938  -9.647  29.769 1.00 26.69 ? 943  VAL   A CG2 1 
ATOM   1807 N N   . TYR   A 1 252 ? -10.349 -10.365 25.940 1.00 23.42 ? 944  TYR   A N   1 
ATOM   1808 C CA  . TYR   A 1 252 ? -10.805 -10.930 24.685 1.00 23.48 ? 944  TYR   A CA  1 
ATOM   1809 C C   . TYR   A 1 252 ? -10.790 -9.926  23.542 1.00 23.51 ? 944  TYR   A C   1 
ATOM   1810 O O   . TYR   A 1 252 ? -10.325 -10.276 22.470 1.00 23.24 ? 944  TYR   A O   1 
ATOM   1811 C CB  . TYR   A 1 252 ? -12.162 -11.598 24.832 1.00 23.73 ? 944  TYR   A CB  1 
ATOM   1812 C CG  . TYR   A 1 252 ? -12.548 -12.418 23.622 1.00 24.22 ? 944  TYR   A CG  1 
ATOM   1813 C CD1 . TYR   A 1 252 ? -11.659 -13.324 23.059 1.00 24.56 ? 944  TYR   A CD1 1 
ATOM   1814 C CD2 . TYR   A 1 252 ? -13.821 -12.319 23.065 1.00 24.74 ? 944  TYR   A CD2 1 
ATOM   1815 C CE1 . TYR   A 1 252 ? -12.015 -14.097 21.963 1.00 25.28 ? 944  TYR   A CE1 1 
ATOM   1816 C CE2 . TYR   A 1 252 ? -14.190 -13.089 21.966 1.00 25.43 ? 944  TYR   A CE2 1 
ATOM   1817 C CZ  . TYR   A 1 252 ? -13.287 -13.987 21.428 1.00 26.32 ? 944  TYR   A CZ  1 
ATOM   1818 O OH  . TYR   A 1 252 ? -13.628 -14.746 20.339 1.00 27.84 ? 944  TYR   A OH  1 
ATOM   1819 N N   . MET   A 1 253 ? -11.181 -8.664  23.783 1.00 24.18 ? 945  MET   A N   1 
ATOM   1820 C CA  . MET   A 1 253 ? -11.152 -7.631  22.741 1.00 25.55 ? 945  MET   A CA  1 
ATOM   1821 C C   . MET   A 1 253 ? -9.763  -7.367  22.181 1.00 25.58 ? 945  MET   A C   1 
ATOM   1822 O O   . MET   A 1 253 ? -9.621  -7.141  20.978 1.00 25.73 ? 945  MET   A O   1 
ATOM   1823 C CB  . MET   A 1 253 ? -11.807 -6.325  23.188 1.00 27.76 ? 945  MET   A CB  1 
ATOM   1824 C CG  . MET   A 1 253 ? -13.350 -6.359  23.164 1.00 33.31 ? 945  MET   A CG  1 
ATOM   1825 S SD  . MET   A 1 253 ? -14.140 -7.043  21.670 1.00 43.92 ? 945  MET   A SD  1 
ATOM   1826 C CE  . MET   A 1 253 ? -14.558 -8.715  22.276 1.00 42.08 ? 945  MET   A CE  1 
ATOM   1827 N N   . ILE   A 1 254 ? -8.736  -7.480  23.023 1.00 25.16 ? 946  ILE   A N   1 
ATOM   1828 C CA  . ILE   A 1 254 ? -7.362  -7.314  22.565 1.00 24.87 ? 946  ILE   A CA  1 
ATOM   1829 C C   . ILE   A 1 254 ? -6.966  -8.479  21.650 1.00 24.32 ? 946  ILE   A C   1 
ATOM   1830 O O   . ILE   A 1 254 ? -6.405  -8.229  20.585 1.00 24.35 ? 946  ILE   A O   1 
ATOM   1831 C CB  . ILE   A 1 254 ? -6.419  -7.136  23.776 1.00 24.99 ? 946  ILE   A CB  1 
ATOM   1832 C CG1 . ILE   A 1 254 ? -6.716  -5.789  24.465 1.00 25.81 ? 946  ILE   A CG1 1 
ATOM   1833 C CG2 . ILE   A 1 254 ? -4.962  -7.244  23.353 1.00 25.02 ? 946  ILE   A CG2 1 
ATOM   1834 C CD1 . ILE   A 1 254 ? -6.122  -5.674  25.751 1.00 27.34 ? 946  ILE   A CD1 1 
ATOM   1835 N N   . MET   A 1 255 ? -7.341  -9.727  22.012 1.00 23.80 ? 947  MET   A N   1 
ATOM   1836 C CA  . MET   A 1 255 ? -7.059  -10.905 21.195 1.00 24.45 ? 947  MET   A CA  1 
ATOM   1837 C C   . MET   A 1 255 ? -7.818  -10.793 19.869 1.00 25.28 ? 947  MET   A C   1 
ATOM   1838 O O   . MET   A 1 255 ? -7.245  -11.011 18.801 1.00 25.79 ? 947  MET   A O   1 
ATOM   1839 C CB  . MET   A 1 255 ? -7.504  -12.169 21.916 1.00 25.99 ? 947  MET   A CB  1 
ATOM   1840 C CG  . MET   A 1 255 ? -6.469  -12.779 22.812 1.00 29.61 ? 947  MET   A CG  1 
ATOM   1841 S SD  . MET   A 1 255 ? -7.285  -13.767 24.094 1.00 36.10 ? 947  MET   A SD  1 
ATOM   1842 C CE  . MET   A 1 255 ? -8.129  -14.949 23.096 1.00 35.52 ? 947  MET   A CE  1 
ATOM   1843 N N   . ARG   A 1 256 ? -9.093  -10.377 19.924 1.00 24.89 ? 948  ARG   A N   1 
ATOM   1844 C CA  . ARG   A 1 256 ? -9.907  -10.149 18.738 1.00 24.73 ? 948  ARG   A CA  1 
ATOM   1845 C C   . ARG   A 1 256 ? -9.242  -9.103  17.824 1.00 23.64 ? 948  ARG   A C   1 
ATOM   1846 O O   . ARG   A 1 256 ? -9.128  -9.332  16.627 1.00 23.82 ? 948  ARG   A O   1 
ATOM   1847 C CB  . ARG   A 1 256 ? -11.319 -9.657  19.142 1.00 26.06 ? 948  ARG   A CB  1 
ATOM   1848 C CG  . ARG   A 1 256 ? -12.215 -10.725 19.744 1.00 29.58 ? 948  ARG   A CG  1 
ATOM   1849 C CD  . ARG   A 1 256 ? -12.400 -11.902 18.802 1.00 34.17 ? 948  ARG   A CD  1 
ATOM   1850 N NE  . ARG   A 1 256 ? -13.203 -11.562 17.619 1.00 37.12 ? 948  ARG   A NE  1 
ATOM   1851 C CZ  . ARG   A 1 256 ? -14.454 -11.964 17.420 1.00 36.95 ? 948  ARG   A CZ  1 
ATOM   1852 N NH1 . ARG   A 1 256 ? -15.098 -11.620 16.312 1.00 36.96 ? 948  ARG   A NH1 1 
ATOM   1853 N NH2 . ARG   A 1 256 ? -15.062 -12.730 18.315 1.00 35.01 ? 948  ARG   A NH2 1 
ATOM   1854 N N   . LYS   A 1 257 ? -8.757  -7.997  18.399 1.00 22.33 ? 949  LYS   A N   1 
ATOM   1855 C CA  . LYS   A 1 257 ? -8.114  -6.931  17.636 1.00 22.33 ? 949  LYS   A CA  1 
ATOM   1856 C C   . LYS   A 1 257 ? -6.904  -7.431  16.850 1.00 21.00 ? 949  LYS   A C   1 
ATOM   1857 O O   . LYS   A 1 257 ? -6.582  -6.867  15.805 1.00 20.77 ? 949  LYS   A O   1 
ATOM   1858 C CB  . LYS   A 1 257 ? -7.710  -5.779  18.568 1.00 25.38 ? 949  LYS   A CB  1 
ATOM   1859 C CG  . LYS   A 1 257 ? -7.684  -4.418  17.913 1.00 30.87 ? 949  LYS   A CG  1 
ATOM   1860 C CD  . LYS   A 1 257 ? -8.412  -3.395  18.780 1.00 36.76 ? 949  LYS   A CD  1 
ATOM   1861 C CE  . LYS   A 1 257 ? -8.318  -1.997  18.203 1.00 41.04 ? 949  LYS   A CE  1 
ATOM   1862 N NZ  . LYS   A 1 257 ? -6.912  -1.498  18.199 1.00 43.34 ? 949  LYS   A NZ  1 
ATOM   1863 N N   . CYS   A 1 258 ? -6.215  -8.477  17.373 1.00 19.46 ? 950  CYS   A N   1 
ATOM   1864 C CA  . CYS   A 1 258 ? -5.060  -9.082  16.724 1.00 18.27 ? 950  CYS   A CA  1 
ATOM   1865 C C   . CYS   A 1 258 ? -5.448  -9.860  15.458 1.00 18.23 ? 950  CYS   A C   1 
ATOM   1866 O O   . CYS   A 1 258 ? -4.604  -10.078 14.593 1.00 18.31 ? 950  CYS   A O   1 
ATOM   1867 C CB  . CYS   A 1 258 ? -4.298  -9.973  17.709 1.00 17.78 ? 950  CYS   A CB  1 
ATOM   1868 S SG  . CYS   A 1 258 ? -3.341  -9.070  18.958 1.00 14.82 ? 950  CYS   A SG  1 
ATOM   1869 N N   . TRP   A 1 259 ? -6.706  -10.292 15.354 1.00 18.00 ? 951  TRP   A N   1 
ATOM   1870 C CA  . TRP   A 1 259 ? -7.164  -11.064 14.231 1.00 18.86 ? 951  TRP   A CA  1 
ATOM   1871 C C   . TRP   A 1 259 ? -8.044  -10.281 13.266 1.00 19.72 ? 951  TRP   A C   1 
ATOM   1872 O O   . TRP   A 1 259 ? -8.803  -10.899 12.530 1.00 20.39 ? 951  TRP   A O   1 
ATOM   1873 C CB  . TRP   A 1 259 ? -7.841  -12.363 14.685 1.00 18.94 ? 951  TRP   A CB  1 
ATOM   1874 C CG  . TRP   A 1 259 ? -7.080  -13.103 15.761 1.00 19.29 ? 951  TRP   A CG  1 
ATOM   1875 C CD1 . TRP   A 1 259 ? -5.741  -13.375 15.788 1.00 19.73 ? 951  TRP   A CD1 1 
ATOM   1876 C CD2 . TRP   A 1 259 ? -7.626  -13.644 16.973 1.00 19.33 ? 951  TRP   A CD2 1 
ATOM   1877 N NE1 . TRP   A 1 259 ? -5.423  -14.063 16.931 1.00 19.94 ? 951  TRP   A NE1 1 
ATOM   1878 C CE2 . TRP   A 1 259 ? -6.564  -14.242 17.679 1.00 20.08 ? 951  TRP   A CE2 1 
ATOM   1879 C CE3 . TRP   A 1 259 ? -8.915  -13.681 17.531 1.00 19.73 ? 951  TRP   A CE3 1 
ATOM   1880 C CZ2 . TRP   A 1 259 ? -6.753  -14.871 18.914 1.00 20.51 ? 951  TRP   A CZ2 1 
ATOM   1881 C CZ3 . TRP   A 1 259 ? -9.093  -14.285 18.759 1.00 20.43 ? 951  TRP   A CZ3 1 
ATOM   1882 C CH2 . TRP   A 1 259 ? -8.020  -14.869 19.439 1.00 20.43 ? 951  TRP   A CH2 1 
ATOM   1883 N N   . MET   A 1 260 ? -7.907  -8.942  13.206 1.00 19.91 ? 952  MET   A N   1 
ATOM   1884 C CA  . MET   A 1 260 ? -8.615  -8.116  12.213 1.00 21.22 ? 952  MET   A CA  1 
ATOM   1885 C C   . MET   A 1 260 ? -8.117  -8.504  10.797 1.00 21.61 ? 952  MET   A C   1 
ATOM   1886 O O   . MET   A 1 260 ? -6.967  -8.913  10.652 1.00 21.15 ? 952  MET   A O   1 
ATOM   1887 C CB  . MET   A 1 260 ? -8.279  -6.622  12.422 1.00 22.84 ? 952  MET   A CB  1 
ATOM   1888 C CG  . MET   A 1 260 ? -8.745  -6.052  13.727 1.00 27.61 ? 952  MET   A CG  1 
ATOM   1889 S SD  . MET   A 1 260 ? -10.519 -5.767  13.763 1.00 43.26 ? 952  MET   A SD  1 
ATOM   1890 C CE  . MET   A 1 260 ? -11.042 -7.086  14.886 1.00 40.92 ? 952  MET   A CE  1 
ATOM   1891 N N   . ILE   A 1 261 ? -8.935  -8.321  9.756  1.00 22.05 ? 953  ILE   A N   1 
ATOM   1892 C CA  . ILE   A 1 261 ? -8.518  -8.631  8.378  1.00 22.88 ? 953  ILE   A CA  1 
ATOM   1893 C C   . ILE   A 1 261 ? -7.493  -7.610  7.909  1.00 23.44 ? 953  ILE   A C   1 
ATOM   1894 O O   . ILE   A 1 261 ? -6.479  -7.977  7.310  1.00 23.64 ? 953  ILE   A O   1 
ATOM   1895 C CB  . ILE   A 1 261 ? -9.740  -8.683  7.422  1.00 24.08 ? 953  ILE   A CB  1 
ATOM   1896 C CG1 . ILE   A 1 261 ? -10.649 -9.881  7.732  1.00 25.26 ? 953  ILE   A CG1 1 
ATOM   1897 C CG2 . ILE   A 1 261 ? -9.310  -8.695  5.946  1.00 24.86 ? 953  ILE   A CG2 1 
ATOM   1898 C CD1 . ILE   A 1 261 ? -10.010 -11.223 7.579  1.00 26.64 ? 953  ILE   A CD1 1 
ATOM   1899 N N   . ASP   A 1 262 ? -7.757  -6.328  8.187  1.00 23.76 ? 954  ASP   A N   1 
ATOM   1900 C CA  . ASP   A 1 262 ? -6.881  -5.217  7.836  1.00 24.68 ? 954  ASP   A CA  1 
ATOM   1901 C C   . ASP   A 1 262 ? -5.711  -5.260  8.810  1.00 25.46 ? 954  ASP   A C   1 
ATOM   1902 O O   . ASP   A 1 262 ? -5.912  -5.086  10.013 1.00 25.99 ? 954  ASP   A O   1 
ATOM   1903 C CB  . ASP   A 1 262 ? -7.664  -3.897  7.973  1.00 26.39 ? 954  ASP   A CB  1 
ATOM   1904 C CG  . ASP   A 1 262 ? -6.887  -2.623  7.703  1.00 32.30 ? 954  ASP   A CG  1 
ATOM   1905 O OD1 . ASP   A 1 262 ? -5.780  -2.707  7.137  1.00 33.01 ? 954  ASP   A OD1 1 
ATOM   1906 O OD2 . ASP   A 1 262 ? -7.400  -1.534  8.039  1.00 35.81 ? 954  ASP   A OD2 1 
ATOM   1907 N N   . ALA   A 1 263 ? -4.512  -5.546  8.306  1.00 25.47 ? 955  ALA   A N   1 
ATOM   1908 C CA  . ALA   A 1 263 ? -3.304  -5.665  9.122  1.00 26.86 ? 955  ALA   A CA  1 
ATOM   1909 C C   . ALA   A 1 263 ? -2.973  -4.400  9.899  1.00 28.21 ? 955  ALA   A C   1 
ATOM   1910 O O   . ALA   A 1 263 ? -2.607  -4.489  11.067 1.00 28.51 ? 955  ALA   A O   1 
ATOM   1911 C CB  . ALA   A 1 263 ? -2.118  -6.058  8.247  1.00 27.03 ? 955  ALA   A CB  1 
ATOM   1912 N N   . ASP   A 1 264 ? -3.131  -3.217  9.277  1.00 28.84 ? 956  ASP   A N   1 
ATOM   1913 C CA  . ASP   A 1 264 ? -2.818  -1.945  9.945  1.00 29.91 ? 956  ASP   A CA  1 
ATOM   1914 C C   . ASP   A 1 264 ? -3.820  -1.563  11.054 1.00 29.61 ? 956  ASP   A C   1 
ATOM   1915 O O   . ASP   A 1 264 ? -3.556  -0.626  11.801 1.00 30.31 ? 956  ASP   A O   1 
ATOM   1916 C CB  . ASP   A 1 264 ? -2.636  -0.790  8.946  1.00 33.44 ? 956  ASP   A CB  1 
ATOM   1917 C CG  . ASP   A 1 264 ? -2.129  -1.203  7.572  1.00 42.19 ? 956  ASP   A CG  1 
ATOM   1918 O OD1 . ASP   A 1 264 ? -2.940  -1.747  6.773  1.00 44.26 ? 956  ASP   A OD1 1 
ATOM   1919 O OD2 . ASP   A 1 264 ? -0.928  -0.984  7.292  1.00 45.36 ? 956  ASP   A OD2 1 
ATOM   1920 N N   . SER   A 1 265 ? -4.954  -2.278  11.163 1.00 28.34 ? 957  SER   A N   1 
ATOM   1921 C CA  . SER   A 1 265 ? -5.942  -2.072  12.231 1.00 27.77 ? 957  SER   A CA  1 
ATOM   1922 C C   . SER   A 1 265 ? -5.554  -2.819  13.508 1.00 26.67 ? 957  SER   A C   1 
ATOM   1923 O O   . SER   A 1 265 ? -6.019  -2.462  14.595 1.00 27.03 ? 957  SER   A O   1 
ATOM   1924 C CB  . SER   A 1 265 ? -7.318  -2.563  11.793 1.00 29.54 ? 957  SER   A CB  1 
ATOM   1925 O OG  . SER   A 1 265 ? -7.929  -1.676  10.874 1.00 32.46 ? 957  SER   A OG  1 
ATOM   1926 N N   . ARG   A 1 266 ? -4.758  -3.904  13.365 1.00 25.31 ? 958  ARG   A N   1 
ATOM   1927 C CA  . ARG   A 1 266 ? -4.271  -4.738  14.455 1.00 23.71 ? 958  ARG   A CA  1 
ATOM   1928 C C   . ARG   A 1 266 ? -3.345  -3.925  15.351 1.00 22.31 ? 958  ARG   A C   1 
ATOM   1929 O O   . ARG   A 1 266 ? -2.670  -3.021  14.860 1.00 22.72 ? 958  ARG   A O   1 
ATOM   1930 C CB  . ARG   A 1 266 ? -3.512  -5.936  13.876 1.00 23.82 ? 958  ARG   A CB  1 
ATOM   1931 C CG  . ARG   A 1 266 ? -4.355  -6.785  12.950 1.00 24.53 ? 958  ARG   A CG  1 
ATOM   1932 C CD  . ARG   A 1 266 ? -3.540  -7.929  12.383 1.00 25.00 ? 958  ARG   A CD  1 
ATOM   1933 N NE  . ARG   A 1 266 ? -4.236  -8.536  11.257 1.00 24.57 ? 958  ARG   A NE  1 
ATOM   1934 C CZ  . ARG   A 1 266 ? -3.640  -9.162  10.246 1.00 24.29 ? 958  ARG   A CZ  1 
ATOM   1935 N NH1 . ARG   A 1 266 ? -2.318  -9.308  10.231 1.00 19.31 ? 958  ARG   A NH1 1 
ATOM   1936 N NH2 . ARG   A 1 266 ? -4.364  -9.655  9.245  1.00 24.39 ? 958  ARG   A NH2 1 
ATOM   1937 N N   . PRO   A 1 267 ? -3.286  -4.218  16.664 1.00 20.89 ? 959  PRO   A N   1 
ATOM   1938 C CA  . PRO   A 1 267 ? -2.389  -3.442  17.531 1.00 20.32 ? 959  PRO   A CA  1 
ATOM   1939 C C   . PRO   A 1 267 ? -0.902  -3.602  17.188 1.00 20.20 ? 959  PRO   A C   1 
ATOM   1940 O O   . PRO   A 1 267 ? -0.491  -4.537  16.503 1.00 20.28 ? 959  PRO   A O   1 
ATOM   1941 C CB  . PRO   A 1 267 ? -2.714  -3.944  18.947 1.00 20.65 ? 959  PRO   A CB  1 
ATOM   1942 C CG  . PRO   A 1 267 ? -3.425  -5.218  18.769 1.00 21.05 ? 959  PRO   A CG  1 
ATOM   1943 C CD  . PRO   A 1 267 ? -4.029  -5.252  17.415 1.00 19.86 ? 959  PRO   A CD  1 
ATOM   1944 N N   . LYS   A 1 268 ? -0.097  -2.667  17.656 1.00 19.97 ? 960  LYS   A N   1 
ATOM   1945 C CA  . LYS   A 1 268 ? 1.349   -2.742  17.503 1.00 19.97 ? 960  LYS   A CA  1 
ATOM   1946 C C   . LYS   A 1 268 ? 1.897   -3.473  18.736 1.00 19.29 ? 960  LYS   A C   1 
ATOM   1947 O O   . LYS   A 1 268 ? 1.313   -3.369  19.813 1.00 19.95 ? 960  LYS   A O   1 
ATOM   1948 C CB  . LYS   A 1 268 ? 1.959   -1.322  17.430 1.00 22.04 ? 960  LYS   A CB  1 
ATOM   1949 C CG  . LYS   A 1 268 ? 1.482   -0.507  16.244 1.00 25.26 ? 960  LYS   A CG  1 
ATOM   1950 C CD  . LYS   A 1 268 ? 2.028   -1.072  14.965 1.00 29.69 ? 960  LYS   A CD  1 
ATOM   1951 C CE  . LYS   A 1 268 ? 2.933   -0.107  14.247 1.00 33.81 ? 960  LYS   A CE  1 
ATOM   1952 N NZ  . LYS   A 1 268 ? 4.357   -0.235  14.666 1.00 35.77 ? 960  LYS   A NZ  1 
ATOM   1953 N N   . PHE   A 1 269 ? 3.055   -4.149  18.631 1.00 18.37 ? 961  PHE   A N   1 
ATOM   1954 C CA  . PHE   A 1 269 ? 3.683   -4.795  19.798 1.00 17.84 ? 961  PHE   A CA  1 
ATOM   1955 C C   . PHE   A 1 269 ? 3.897   -3.778  20.940 1.00 19.28 ? 961  PHE   A C   1 
ATOM   1956 O O   . PHE   A 1 269 ? 3.532   -4.040  22.080 1.00 19.31 ? 961  PHE   A O   1 
ATOM   1957 C CB  . PHE   A 1 269 ? 4.977   -5.479  19.378 1.00 16.47 ? 961  PHE   A CB  1 
ATOM   1958 C CG  . PHE   A 1 269 ? 4.681   -6.794  18.712 1.00 15.64 ? 961  PHE   A CG  1 
ATOM   1959 C CD1 . PHE   A 1 269 ? 3.985   -7.788  19.384 1.00 15.33 ? 961  PHE   A CD1 1 
ATOM   1960 C CD2 . PHE   A 1 269 ? 5.085   -7.036  17.410 1.00 15.73 ? 961  PHE   A CD2 1 
ATOM   1961 C CE1 . PHE   A 1 269 ? 3.682   -8.989  18.757 1.00 15.64 ? 961  PHE   A CE1 1 
ATOM   1962 C CE2 . PHE   A 1 269 ? 4.782   -8.244  16.783 1.00 15.83 ? 961  PHE   A CE2 1 
ATOM   1963 C CZ  . PHE   A 1 269 ? 4.092   -9.217  17.461 1.00 15.39 ? 961  PHE   A CZ  1 
ATOM   1964 N N   . ARG   A 1 270 ? 4.301   -2.559  20.555 1.00 20.51 ? 962  ARG   A N   1 
ATOM   1965 C CA  . ARG   A 1 270 ? 4.456   -1.328  21.334 1.00 22.36 ? 962  ARG   A CA  1 
ATOM   1966 C C   . ARG   A 1 270 ? 3.213   -1.069  22.233 1.00 21.89 ? 962  ARG   A C   1 
ATOM   1967 O O   . ARG   A 1 270 ? 3.340   -0.741  23.411 1.00 22.01 ? 962  ARG   A O   1 
ATOM   1968 C CB  . ARG   A 1 270 ? 4.514   -0.184  20.306 1.00 26.00 ? 962  ARG   A CB  1 
ATOM   1969 C CG  . ARG   A 1 270 ? 5.615   0.810   20.471 1.00 32.90 ? 962  ARG   A CG  1 
ATOM   1970 C CD  . ARG   A 1 270 ? 5.437   1.955   19.470 1.00 39.12 ? 962  ARG   A CD  1 
ATOM   1971 N NE  . ARG   A 1 270 ? 5.284   1.522   18.074 1.00 43.67 ? 962  ARG   A NE  1 
ATOM   1972 C CZ  . ARG   A 1 270 ? 6.288   1.122   17.299 1.00 48.36 ? 962  ARG   A CZ  1 
ATOM   1973 N NH1 . ARG   A 1 270 ? 7.527   1.066   17.778 1.00 48.37 ? 962  ARG   A NH1 1 
ATOM   1974 N NH2 . ARG   A 1 270 ? 6.060   0.765   16.041 1.00 49.52 ? 962  ARG   A NH2 1 
ATOM   1975 N N   . GLU   A 1 271 ? 2.027   -1.183  21.644 1.00 21.50 ? 963  GLU   A N   1 
ATOM   1976 C CA  . GLU   A 1 271 ? 0.755   -0.962  22.302 1.00 22.15 ? 963  GLU   A CA  1 
ATOM   1977 C C   . GLU   A 1 271 ? 0.366   -2.160  23.161 1.00 22.65 ? 963  GLU   A C   1 
ATOM   1978 O O   . GLU   A 1 271 ? -0.262  -1.975  24.216 1.00 22.99 ? 963  GLU   A O   1 
ATOM   1979 C CB  . GLU   A 1 271 ? -0.331  -0.714  21.257 1.00 24.65 ? 963  GLU   A CB  1 
ATOM   1980 C CG  . GLU   A 1 271 ? -0.055  0.458   20.332 1.00 30.35 ? 963  GLU   A CG  1 
ATOM   1981 C CD  . GLU   A 1 271 ? -1.024  0.593   19.166 1.00 35.35 ? 963  GLU   A CD  1 
ATOM   1982 O OE1 . GLU   A 1 271 ? -1.944  -0.248  19.044 1.00 35.88 ? 963  GLU   A OE1 1 
ATOM   1983 O OE2 . GLU   A 1 271 ? -0.851  1.537   18.364 1.00 36.88 ? 963  GLU   A OE2 1 
ATOM   1984 N N   . LEU   A 1 272 ? 0.696   -3.392  22.700 1.00 21.88 ? 964  LEU   A N   1 
ATOM   1985 C CA  . LEU   A 1 272 ? 0.406   -4.584  23.475 1.00 21.96 ? 964  LEU   A CA  1 
ATOM   1986 C C   . LEU   A 1 272 ? 1.216   -4.600  24.799 1.00 22.31 ? 964  LEU   A C   1 
ATOM   1987 O O   . LEU   A 1 272 ? 0.673   -5.019  25.824 1.00 22.43 ? 964  LEU   A O   1 
ATOM   1988 C CB  . LEU   A 1 272 ? 0.647   -5.847  22.631 1.00 22.28 ? 964  LEU   A CB  1 
ATOM   1989 C CG  . LEU   A 1 272 ? -0.346  -6.034  21.461 1.00 23.67 ? 964  LEU   A CG  1 
ATOM   1990 C CD1 . LEU   A 1 272 ? 0.132   -7.085  20.454 1.00 23.35 ? 964  LEU   A CD1 1 
ATOM   1991 C CD2 . LEU   A 1 272 ? -1.744  -6.357  21.975 1.00 23.92 ? 964  LEU   A CD2 1 
ATOM   1992 N N   . ILE   A 1 273 ? 2.499   -4.115  24.789 1.00 22.01 ? 965  ILE   A N   1 
ATOM   1993 C CA  . ILE   A 1 273 ? 3.346   -4.053  25.999 1.00 22.14 ? 965  ILE   A CA  1 
ATOM   1994 C C   . ILE   A 1 273 ? 2.671   -3.185  27.056 1.00 22.81 ? 965  ILE   A C   1 
ATOM   1995 O O   . ILE   A 1 273 ? 2.653   -3.543  28.226 1.00 23.34 ? 965  ILE   A O   1 
ATOM   1996 C CB  . ILE   A 1 273 ? 4.781   -3.494  25.742 1.00 22.10 ? 965  ILE   A CB  1 
ATOM   1997 C CG1 . ILE   A 1 273 ? 5.513   -4.196  24.583 1.00 22.71 ? 965  ILE   A CG1 1 
ATOM   1998 C CG2 . ILE   A 1 273 ? 5.614   -3.521  27.019 1.00 22.15 ? 965  ILE   A CG2 1 
ATOM   1999 C CD1 . ILE   A 1 273 ? 6.874   -3.610  24.217 1.00 23.27 ? 965  ILE   A CD1 1 
ATOM   2000 N N   . ILE   A 1 274 ? 2.151   -2.025  26.642 1.00 22.49 ? 966  ILE   A N   1 
ATOM   2001 C CA  . ILE   A 1 274 ? 1.523   -1.058  27.526 1.00 22.65 ? 966  ILE   A CA  1 
ATOM   2002 C C   . ILE   A 1 274 ? 0.190   -1.567  28.075 1.00 22.39 ? 966  ILE   A C   1 
ATOM   2003 O O   . ILE   A 1 274 ? -0.051  -1.479  29.287 1.00 22.80 ? 966  ILE   A O   1 
ATOM   2004 C CB  . ILE   A 1 274 ? 1.369   0.269   26.735 1.00 23.67 ? 966  ILE   A CB  1 
ATOM   2005 C CG1 . ILE   A 1 274 ? 2.752   0.862   26.402 1.00 24.98 ? 966  ILE   A CG1 1 
ATOM   2006 C CG2 . ILE   A 1 274 ? 0.479   1.280   27.463 1.00 24.08 ? 966  ILE   A CG2 1 
ATOM   2007 C CD1 . ILE   A 1 274 ? 2.720   2.020   25.447 1.00 26.13 ? 966  ILE   A CD1 1 
ATOM   2008 N N   . GLU   A 1 275 ? -0.655  -2.117  27.197 1.00 21.59 ? 967  GLU   A N   1 
ATOM   2009 C CA  . GLU   A 1 275 ? -1.974  -2.614  27.571 1.00 21.49 ? 967  GLU   A CA  1 
ATOM   2010 C C   . GLU   A 1 275 ? -1.861  -3.764  28.518 1.00 20.63 ? 967  GLU   A C   1 
ATOM   2011 O O   . GLU   A 1 275 ? -2.562  -3.789  29.543 1.00 20.50 ? 967  GLU   A O   1 
ATOM   2012 C CB  . GLU   A 1 275 ? -2.795  -3.034  26.340 1.00 24.79 ? 967  GLU   A CB  1 
ATOM   2013 C CG  . GLU   A 1 275 ? -4.031  -2.182  26.088 1.00 33.83 ? 967  GLU   A CG  1 
ATOM   2014 C CD  . GLU   A 1 275 ? -4.946  -1.913  27.275 1.00 44.53 ? 967  GLU   A CD  1 
ATOM   2015 O OE1 . GLU   A 1 275 ? -5.764  -2.800  27.617 1.00 46.72 ? 967  GLU   A OE1 1 
ATOM   2016 O OE2 . GLU   A 1 275 ? -4.865  -0.798  27.845 1.00 47.93 ? 967  GLU   A OE2 1 
ATOM   2017 N N   . PHE   A 1 276 ? -0.979  -4.722  28.192 1.00 19.39 ? 968  PHE   A N   1 
ATOM   2018 C CA  . PHE   A 1 276 ? -0.820  -5.881  29.054 1.00 19.54 ? 968  PHE   A CA  1 
ATOM   2019 C C   . PHE   A 1 276 ? -0.109  -5.501  30.393 1.00 20.39 ? 968  PHE   A C   1 
ATOM   2020 O O   . PHE   A 1 276 ? -0.410  -6.110  31.428 1.00 20.75 ? 968  PHE   A O   1 
ATOM   2021 C CB  . PHE   A 1 276 ? -0.157  -7.071  28.307 1.00 18.66 ? 968  PHE   A CB  1 
ATOM   2022 C CG  . PHE   A 1 276 ? -1.147  -7.981  27.624 1.00 18.53 ? 968  PHE   A CG  1 
ATOM   2023 C CD1 . PHE   A 1 276 ? -2.018  -8.767  28.366 1.00 19.18 ? 968  PHE   A CD1 1 
ATOM   2024 C CD2 . PHE   A 1 276 ? -1.243  -8.020  26.242 1.00 19.11 ? 968  PHE   A CD2 1 
ATOM   2025 C CE1 . PHE   A 1 276 ? -2.974  -9.575  27.740 1.00 19.45 ? 968  PHE   A CE1 1 
ATOM   2026 C CE2 . PHE   A 1 276 ? -2.204  -8.821  25.614 1.00 19.68 ? 968  PHE   A CE2 1 
ATOM   2027 C CZ  . PHE   A 1 276 ? -3.061  -9.596  26.369 1.00 19.26 ? 968  PHE   A CZ  1 
ATOM   2028 N N   . SER   A 1 277 ? 0.771   -4.464  30.394 1.00 20.34 ? 969  SER   A N   1 
ATOM   2029 C CA  . SER   A 1 277 ? 1.444   -4.037  31.638 1.00 20.98 ? 969  SER   A CA  1 
ATOM   2030 C C   . SER   A 1 277 ? 0.441   -3.338  32.559 1.00 22.21 ? 969  SER   A C   1 
ATOM   2031 O O   . SER   A 1 277 ? 0.452   -3.542  33.772 1.00 22.08 ? 969  SER   A O   1 
ATOM   2032 C CB  . SER   A 1 277 ? 2.610   -3.102  31.348 1.00 21.37 ? 969  SER   A CB  1 
ATOM   2033 O OG  . SER   A 1 277 ? 3.603   -3.709  30.539 1.00 23.21 ? 969  SER   A OG  1 
ATOM   2034 N N   . LYS   A 1 278 ? -0.446  -2.529  31.970 1.00 23.06 ? 970  LYS   A N   1 
ATOM   2035 C CA  . LYS   A 1 278 ? -1.518  -1.863  32.692 1.00 24.63 ? 970  LYS   A CA  1 
ATOM   2036 C C   . LYS   A 1 278 ? -2.446  -2.937  33.322 1.00 25.59 ? 970  LYS   A C   1 
ATOM   2037 O O   . LYS   A 1 278 ? -2.875  -2.783  34.470 1.00 27.04 ? 970  LYS   A O   1 
ATOM   2038 C CB  . LYS   A 1 278 ? -2.295  -0.967  31.710 1.00 27.13 ? 970  LYS   A CB  1 
ATOM   2039 C CG  . LYS   A 1 278 ? -3.486  -0.242  32.308 1.00 31.80 ? 970  LYS   A CG  1 
ATOM   2040 C CD  . LYS   A 1 278 ? -4.703  -0.300  31.389 1.00 37.09 ? 970  LYS   A CD  1 
ATOM   2041 C CE  . LYS   A 1 278 ? -5.187  -1.722  31.205 1.00 41.96 ? 970  LYS   A CE  1 
ATOM   2042 N NZ  . LYS   A 1 278 ? -6.286  -1.826  30.199 1.00 45.32 ? 970  LYS   A NZ  1 
ATOM   2043 N N   . MET   A 1 279 ? -2.695  -4.045  32.604 1.00 24.50 ? 971  MET   A N   1 
ATOM   2044 C CA  . MET   A 1 279 ? -3.534  -5.112  33.119 1.00 24.91 ? 971  MET   A CA  1 
ATOM   2045 C C   . MET   A 1 279 ? -2.884  -5.912  34.236 1.00 25.61 ? 971  MET   A C   1 
ATOM   2046 O O   . MET   A 1 279 ? -3.579  -6.426  35.121 1.00 26.11 ? 971  MET   A O   1 
ATOM   2047 C CB  . MET   A 1 279 ? -3.961  -6.040  31.989 1.00 25.73 ? 971  MET   A CB  1 
ATOM   2048 C CG  . MET   A 1 279 ? -4.989  -5.420  31.062 1.00 27.54 ? 971  MET   A CG  1 
ATOM   2049 S SD  . MET   A 1 279 ? -5.431  -6.600  29.797 1.00 29.73 ? 971  MET   A SD  1 
ATOM   2050 C CE  . MET   A 1 279 ? -6.934  -5.897  29.234 1.00 28.25 ? 971  MET   A CE  1 
ATOM   2051 N N   . ALA   A 1 280 ? -1.549  -6.050  34.181 1.00 25.20 ? 972  ALA   A N   1 
ATOM   2052 C CA  . ALA   A 1 280 ? -0.757  -6.754  35.192 1.00 24.64 ? 972  ALA   A CA  1 
ATOM   2053 C C   . ALA   A 1 280 ? -0.790  -6.038  36.561 1.00 24.16 ? 972  ALA   A C   1 
ATOM   2054 O O   . ALA   A 1 280 ? -0.615  -6.687  37.585 1.00 23.22 ? 972  ALA   A O   1 
ATOM   2055 C CB  . ALA   A 1 280 ? 0.681   -6.918  34.709 1.00 24.21 ? 972  ALA   A CB  1 
ATOM   2056 N N   . ARG   A 1 281 ? -0.993  -4.696  36.559 1.00 24.51 ? 973  ARG   A N   1 
ATOM   2057 C CA  . ARG   A 1 281 ? -1.094  -3.863  37.761 1.00 25.44 ? 973  ARG   A CA  1 
ATOM   2058 C C   . ARG   A 1 281 ? -2.407  -4.117  38.550 1.00 25.66 ? 973  ARG   A C   1 
ATOM   2059 O O   . ARG   A 1 281 ? -2.483  -3.835  39.746 1.00 24.95 ? 973  ARG   A O   1 
ATOM   2060 C CB  . ARG   A 1 281 ? -0.959  -2.377  37.381 1.00 27.51 ? 973  ARG   A CB  1 
ATOM   2061 C CG  . ARG   A 1 281 ? 0.453   -2.017  36.936 1.00 31.84 ? 973  ARG   A CG  1 
ATOM   2062 C CD  . ARG   A 1 281 ? 0.615   -0.577  36.445 1.00 36.35 ? 973  ARG   A CD  1 
ATOM   2063 N NE  . ARG   A 1 281 ? 1.970   -0.360  35.919 1.00 40.00 ? 973  ARG   A NE  1 
ATOM   2064 C CZ  . ARG   A 1 281 ? 2.257   -0.099  34.645 1.00 41.09 ? 973  ARG   A CZ  1 
ATOM   2065 N NH1 . ARG   A 1 281 ? 1.285   0.040   33.752 1.00 39.97 ? 973  ARG   A NH1 1 
ATOM   2066 N NH2 . ARG   A 1 281 ? 3.517   0.055   34.263 1.00 40.67 ? 973  ARG   A NH2 1 
ATOM   2067 N N   . ASP   A 1 282 ? -3.426  -4.666  37.878 1.00 26.19 ? 974  ASP   A N   1 
ATOM   2068 C CA  . ASP   A 1 282 ? -4.700  -5.021  38.490 1.00 27.40 ? 974  ASP   A CA  1 
ATOM   2069 C C   . ASP   A 1 282 ? -5.085  -6.395  37.928 1.00 28.25 ? 974  ASP   A C   1 
ATOM   2070 O O   . ASP   A 1 282 ? -5.973  -6.487  37.088 1.00 28.86 ? 974  ASP   A O   1 
ATOM   2071 C CB  . ASP   A 1 282 ? -5.756  -3.964  38.109 1.00 29.03 ? 974  ASP   A CB  1 
ATOM   2072 C CG  . ASP   A 1 282 ? -6.957  -3.916  39.028 1.00 35.12 ? 974  ASP   A CG  1 
ATOM   2073 O OD1 . ASP   A 1 282 ? -7.076  -4.812  39.917 1.00 35.73 ? 974  ASP   A OD1 1 
ATOM   2074 O OD2 . ASP   A 1 282 ? -7.775  -2.981  38.878 1.00 38.17 ? 974  ASP   A OD2 1 
ATOM   2075 N N   . PRO   A 1 283 ? -4.397  -7.468  38.335 1.00 28.11 ? 975  PRO   A N   1 
ATOM   2076 C CA  . PRO   A 1 283 ? -4.643  -8.784  37.712 1.00 28.81 ? 975  PRO   A CA  1 
ATOM   2077 C C   . PRO   A 1 283 ? -6.049  -9.378  37.825 1.00 30.15 ? 975  PRO   A C   1 
ATOM   2078 O O   . PRO   A 1 283 ? -6.505  -9.965  36.843 1.00 30.48 ? 975  PRO   A O   1 
ATOM   2079 C CB  . PRO   A 1 283 ? -3.609  -9.704  38.374 1.00 29.09 ? 975  PRO   A CB  1 
ATOM   2080 C CG  . PRO   A 1 283 ? -3.200  -9.007  39.610 1.00 29.38 ? 975  PRO   A CG  1 
ATOM   2081 C CD  . PRO   A 1 283 ? -3.301  -7.532  39.312 1.00 27.48 ? 975  PRO   A CD  1 
ATOM   2082 N N   . GLN   A 1 284 ? -6.726  -9.247  38.988 1.00 30.47 ? 976  GLN   A N   1 
ATOM   2083 C CA  . GLN   A 1 284 ? -8.068  -9.802  39.222 1.00 31.13 ? 976  GLN   A CA  1 
ATOM   2084 C C   . GLN   A 1 284 ? -9.164  -9.147  38.361 1.00 31.05 ? 976  GLN   A C   1 
ATOM   2085 O O   . GLN   A 1 284 ? -10.173 -9.775  38.046 1.00 31.62 ? 976  GLN   A O   1 
ATOM   2086 C CB  . GLN   A 1 284 ? -8.438  -9.700  40.713 1.00 33.58 ? 976  GLN   A CB  1 
ATOM   2087 C CG  . GLN   A 1 284 ? -7.548  -10.537 41.629 1.00 39.04 ? 976  GLN   A CG  1 
ATOM   2088 C CD  . GLN   A 1 284 ? -8.225  -10.831 42.961 1.00 45.47 ? 976  GLN   A CD  1 
ATOM   2089 O OE1 . GLN   A 1 284 ? -8.821  -9.944  43.601 1.00 47.45 ? 976  GLN   A OE1 1 
ATOM   2090 N NE2 . GLN   A 1 284 ? -8.144  -12.087 43.412 1.00 45.87 ? 976  GLN   A NE2 1 
ATOM   2091 N N   . ARG   A 1 285 ? -8.977  -7.882  38.009 1.00 29.95 ? 977  ARG   A N   1 
ATOM   2092 C CA  . ARG   A 1 285 ? -9.918  -7.151  37.193 1.00 29.42 ? 977  ARG   A CA  1 
ATOM   2093 C C   . ARG   A 1 285 ? -9.892  -7.616  35.717 1.00 29.14 ? 977  ARG   A C   1 
ATOM   2094 O O   . ARG   A 1 285 ? -10.848 -7.347  34.984 1.00 29.84 ? 977  ARG   A O   1 
ATOM   2095 C CB  . ARG   A 1 285 ? -9.567  -5.668  37.273 1.00 30.92 ? 977  ARG   A CB  1 
ATOM   2096 C CG  . ARG   A 1 285 ? -10.553 -4.760  36.578 1.00 36.05 ? 977  ARG   A CG  1 
ATOM   2097 C CD  . ARG   A 1 285 ? -9.952  -3.411  36.267 1.00 41.61 ? 977  ARG   A CD  1 
ATOM   2098 N NE  . ARG   A 1 285 ? -10.521 -2.361  37.106 1.00 47.45 ? 977  ARG   A NE  1 
ATOM   2099 C CZ  . ARG   A 1 285 ? -10.384 -1.058  36.871 1.00 52.55 ? 977  ARG   A CZ  1 
ATOM   2100 N NH1 . ARG   A 1 285 ? -9.682  -0.632  35.823 1.00 52.51 ? 977  ARG   A NH1 1 
ATOM   2101 N NH2 . ARG   A 1 285 ? -10.955 -0.168  37.676 1.00 53.89 ? 977  ARG   A NH2 1 
ATOM   2102 N N   . TYR   A 1 286 ? -8.826  -8.313  35.271 1.00 27.67 ? 978  TYR   A N   1 
ATOM   2103 C CA  . TYR   A 1 286 ? -8.730  -8.701  33.872 1.00 26.81 ? 978  TYR   A CA  1 
ATOM   2104 C C   . TYR   A 1 286 ? -8.785  -10.191 33.638 1.00 25.88 ? 978  TYR   A C   1 
ATOM   2105 O O   . TYR   A 1 286 ? -9.212  -10.605 32.558 1.00 25.33 ? 978  TYR   A O   1 
ATOM   2106 C CB  . TYR   A 1 286 ? -7.515  -8.059  33.226 1.00 26.81 ? 978  TYR   A CB  1 
ATOM   2107 C CG  . TYR   A 1 286 ? -7.684  -6.556  33.215 1.00 27.07 ? 978  TYR   A CG  1 
ATOM   2108 C CD1 . TYR   A 1 286 ? -8.646  -5.953  32.417 1.00 27.99 ? 978  TYR   A CD1 1 
ATOM   2109 C CD2 . TYR   A 1 286 ? -6.982  -5.753  34.100 1.00 27.35 ? 978  TYR   A CD2 1 
ATOM   2110 C CE1 . TYR   A 1 286 ? -8.827  -4.574  32.423 1.00 29.06 ? 978  TYR   A CE1 1 
ATOM   2111 C CE2 . TYR   A 1 286 ? -7.162  -4.374  34.125 1.00 28.45 ? 978  TYR   A CE2 1 
ATOM   2112 C CZ  . TYR   A 1 286 ? -8.085  -3.788  33.284 1.00 29.98 ? 978  TYR   A CZ  1 
ATOM   2113 O OH  . TYR   A 1 286 ? -8.283  -2.434  33.318 1.00 32.50 ? 978  TYR   A OH  1 
ATOM   2114 N N   . LEU   A 1 287 ? -8.460  -11.001 34.650 1.00 25.37 ? 979  LEU   A N   1 
ATOM   2115 C CA  . LEU   A 1 287 ? -8.580  -12.452 34.514 1.00 25.57 ? 979  LEU   A CA  1 
ATOM   2116 C C   . LEU   A 1 287 ? -9.300  -13.026 35.734 1.00 26.62 ? 979  LEU   A C   1 
ATOM   2117 O O   . LEU   A 1 287 ? -9.074  -12.585 36.859 1.00 26.82 ? 979  LEU   A O   1 
ATOM   2118 C CB  . LEU   A 1 287 ? -7.232  -13.158 34.273 1.00 25.28 ? 979  LEU   A CB  1 
ATOM   2119 C CG  . LEU   A 1 287 ? -6.453  -12.815 32.973 1.00 25.87 ? 979  LEU   A CG  1 
ATOM   2120 C CD1 . LEU   A 1 287 ? -5.050  -13.395 33.010 1.00 26.59 ? 979  LEU   A CD1 1 
ATOM   2121 C CD2 . LEU   A 1 287 ? -7.149  -13.334 31.745 1.00 25.73 ? 979  LEU   A CD2 1 
ATOM   2122 N N   . VAL   A 1 288 ? -10.200 -13.982 35.496 1.00 27.03 ? 980  VAL   A N   1 
ATOM   2123 C CA  . VAL   A 1 288 ? -10.969 -14.653 36.523 1.00 28.42 ? 980  VAL   A CA  1 
ATOM   2124 C C   . VAL   A 1 288 ? -10.401 -16.063 36.683 1.00 30.91 ? 980  VAL   A C   1 
ATOM   2125 O O   . VAL   A 1 288 ? -10.665 -16.942 35.856 1.00 30.93 ? 980  VAL   A O   1 
ATOM   2126 C CB  . VAL   A 1 288 ? -12.478 -14.678 36.161 1.00 28.44 ? 980  VAL   A CB  1 
ATOM   2127 C CG1 . VAL   A 1 288 ? -13.282 -15.341 37.263 1.00 29.11 ? 980  VAL   A CG1 1 
ATOM   2128 C CG2 . VAL   A 1 288 ? -12.999 -13.274 35.909 1.00 28.33 ? 980  VAL   A CG2 1 
ATOM   2129 N N   . ILE   A 1 289 ? -9.567  -16.266 37.714 1.00 32.69 ? 981  ILE   A N   1 
ATOM   2130 C CA  . ILE   A 1 289 ? -8.948  -17.565 37.971 1.00 34.59 ? 981  ILE   A CA  1 
ATOM   2131 C C   . ILE   A 1 289 ? -9.327  -18.075 39.372 1.00 37.12 ? 981  ILE   A C   1 
ATOM   2132 O O   . ILE   A 1 289 ? -9.262  -17.317 40.347 1.00 37.50 ? 981  ILE   A O   1 
ATOM   2133 C CB  . ILE   A 1 289 ? -7.418  -17.456 37.730 1.00 34.77 ? 981  ILE   A CB  1 
ATOM   2134 C CG1 . ILE   A 1 289 ? -7.110  -17.449 36.213 1.00 35.37 ? 981  ILE   A CG1 1 
ATOM   2135 C CG2 . ILE   A 1 289 ? -6.620  -18.545 38.463 1.00 34.95 ? 981  ILE   A CG2 1 
ATOM   2136 C CD1 . ILE   A 1 289 ? -5.803  -16.778 35.847 1.00 35.98 ? 981  ILE   A CD1 1 
ATOM   2137 N N   . GLN   A 1 290 ? -9.779  -19.338 39.468 1.00 38.70 ? 982  GLN   A N   1 
ATOM   2138 C CA  . GLN   A 1 290 ? -10.182 -19.890 40.762 1.00 40.45 ? 982  GLN   A CA  1 
ATOM   2139 C C   . GLN   A 1 290 ? -8.969  -20.315 41.538 1.00 40.68 ? 982  GLN   A C   1 
ATOM   2140 O O   . GLN   A 1 290 ? -8.181  -21.119 41.047 1.00 40.72 ? 982  GLN   A O   1 
ATOM   2141 C CB  . GLN   A 1 290 ? -11.194 -21.042 40.616 1.00 43.59 ? 982  GLN   A CB  1 
ATOM   2142 C CG  . GLN   A 1 290 ? -11.708 -21.618 41.956 1.00 49.68 ? 982  GLN   A CG  1 
ATOM   2143 C CD  . GLN   A 1 290 ? -12.660 -20.717 42.753 1.00 55.33 ? 982  GLN   A CD  1 
ATOM   2144 O OE1 . GLN   A 1 290 ? -12.271 -19.675 43.312 1.00 56.92 ? 982  GLN   A OE1 1 
ATOM   2145 N NE2 . GLN   A 1 290 ? -13.935 -21.112 42.848 1.00 55.42 ? 982  GLN   A NE2 1 
ATOM   2146 N N   . GLY   A 1 291 ? -8.816  -19.741 42.728 1.00 40.75 ? 983  GLY   A N   1 
ATOM   2147 C CA  . GLY   A 1 291 ? -7.683  -20.007 43.613 1.00 41.21 ? 983  GLY   A CA  1 
ATOM   2148 C C   . GLY   A 1 291 ? -6.492  -19.101 43.345 1.00 41.25 ? 983  GLY   A C   1 
ATOM   2149 O O   . GLY   A 1 291 ? -5.353  -19.456 43.660 1.00 41.10 ? 983  GLY   A O   1 
ATOM   2150 N N   . ASP   A 1 292 ? -6.768  -17.906 42.777 1.00 41.27 ? 984  ASP   A N   1 
ATOM   2151 C CA  . ASP   A 1 292 ? -5.785  -16.909 42.358 1.00 41.37 ? 984  ASP   A CA  1 
ATOM   2152 C C   . ASP   A 1 292 ? -5.157  -16.111 43.492 1.00 42.32 ? 984  ASP   A C   1 
ATOM   2153 O O   . ASP   A 1 292 ? -3.995  -15.708 43.374 1.00 41.97 ? 984  ASP   A O   1 
ATOM   2154 C CB  . ASP   A 1 292 ? -6.396  -15.970 41.315 1.00 40.98 ? 984  ASP   A CB  1 
ATOM   2155 C CG  . ASP   A 1 292 ? -5.375  -15.263 40.461 1.00 40.64 ? 984  ASP   A CG  1 
ATOM   2156 O OD1 . ASP   A 1 292 ? -4.264  -15.808 40.294 1.00 39.50 ? 984  ASP   A OD1 1 
ATOM   2157 O OD2 . ASP   A 1 292 ? -5.682  -14.163 39.965 1.00 41.37 ? 984  ASP   A OD2 1 
ATOM   2158 N N   . GLU   A 1 293 ? -5.895  -15.884 44.582 1.00 43.45 ? 985  GLU   A N   1 
ATOM   2159 C CA  . GLU   A 1 293 ? -5.341  -15.171 45.741 1.00 45.48 ? 985  GLU   A CA  1 
ATOM   2160 C C   . GLU   A 1 293 ? -4.143  -15.941 46.362 1.00 47.12 ? 985  GLU   A C   1 
ATOM   2161 O O   . GLU   A 1 293 ? -3.241  -15.325 46.925 1.00 46.99 ? 985  GLU   A O   1 
ATOM   2162 C CB  . GLU   A 1 293 ? -6.435  -14.878 46.787 1.00 48.21 ? 985  GLU   A CB  1 
ATOM   2163 C CG  . GLU   A 1 293 ? -7.184  -16.118 47.247 1.00 53.73 ? 985  GLU   A CG  1 
ATOM   2164 C CD  . GLU   A 1 293 ? -8.549  -15.876 47.863 1.00 61.36 ? 985  GLU   A CD  1 
ATOM   2165 O OE1 . GLU   A 1 293 ? -8.971  -14.701 47.965 1.00 61.79 ? 985  GLU   A OE1 1 
ATOM   2166 O OE2 . GLU   A 1 293 ? -9.203  -16.876 48.240 1.00 64.75 ? 985  GLU   A OE2 1 
ATOM   2167 N N   . ARG   A 1 294 ? -4.114  -17.279 46.198 1.00 48.49 ? 986  ARG   A N   1 
ATOM   2168 C CA  . ARG   A 1 294 ? -3.038  -18.143 46.665 1.00 50.17 ? 986  ARG   A CA  1 
ATOM   2169 C C   . ARG   A 1 294 ? -1.834  -18.043 45.704 1.00 51.07 ? 986  ARG   A C   1 
ATOM   2170 O O   . ARG   A 1 294 ? -0.711  -17.798 46.142 1.00 51.60 ? 986  ARG   A O   1 
ATOM   2171 C CB  . ARG   A 1 294 ? -3.552  -19.595 46.765 1.00 52.81 ? 986  ARG   A CB  1 
ATOM   2172 C CG  . ARG   A 1 294 ? -4.796  -19.728 47.654 1.00 58.72 ? 986  ARG   A CG  1 
ATOM   2173 C CD  . ARG   A 1 294 ? -5.392  -21.131 47.659 1.00 64.48 ? 986  ARG   A CD  1 
ATOM   2174 N NE  . ARG   A 1 294 ? -6.443  -21.285 48.674 1.00 69.58 ? 986  ARG   A NE  1 
ATOM   2175 C CZ  . ARG   A 1 294 ? -6.282  -21.922 49.834 1.00 73.35 ? 986  ARG   A CZ  1 
ATOM   2176 N NH1 . ARG   A 1 294 ? -5.117  -22.488 50.135 1.00 73.63 ? 986  ARG   A NH1 1 
ATOM   2177 N NH2 . ARG   A 1 294 ? -7.291  -22.018 50.691 1.00 73.64 ? 986  ARG   A NH2 1 
ATOM   2178 N N   . MET   A 1 295 ? -2.081  -18.170 44.391 1.00 51.10 ? 987  MET   A N   1 
ATOM   2179 C CA  . MET   A 1 295 ? -1.046  -18.128 43.356 1.00 51.43 ? 987  MET   A CA  1 
ATOM   2180 C C   . MET   A 1 295 ? -0.467  -16.735 43.101 1.00 51.50 ? 987  MET   A C   1 
ATOM   2181 O O   . MET   A 1 295 ? -0.801  -16.101 42.093 1.00 52.10 ? 987  MET   A O   1 
ATOM   2182 C CB  . MET   A 1 295 ? -1.559  -18.722 42.021 1.00 52.04 ? 987  MET   A CB  1 
ATOM   2183 C CG  . MET   A 1 295 ? -2.349  -19.989 42.154 1.00 54.26 ? 987  MET   A CG  1 
ATOM   2184 S SD  . MET   A 1 295 ? -3.509  -20.113 40.781 1.00 57.92 ? 987  MET   A SD  1 
ATOM   2185 C CE  . MET   A 1 295 ? -4.263  -21.673 41.152 1.00 57.36 ? 987  MET   A CE  1 
ATOM   2186 N N   . HIS   A 1 296 ? 0.438   -16.276 43.964 1.00 50.81 ? 988  HIS   A N   1 
ATOM   2187 C CA  . HIS   A 1 296 ? 1.076   -14.972 43.759 1.00 50.84 ? 988  HIS   A CA  1 
ATOM   2188 C C   . HIS   A 1 296 ? 2.484   -15.120 43.132 1.00 48.82 ? 988  HIS   A C   1 
ATOM   2189 O O   . HIS   A 1 296 ? 2.991   -16.244 42.995 1.00 48.74 ? 988  HIS   A O   1 
ATOM   2190 C CB  . HIS   A 1 296 ? 1.114   -14.170 45.079 1.00 53.33 ? 988  HIS   A CB  1 
ATOM   2191 C CG  . HIS   A 1 296 ? 1.966   -14.789 46.150 1.00 58.34 ? 988  HIS   A CG  1 
ATOM   2192 N ND1 . HIS   A 1 296 ? 1.854   -16.134 46.482 1.00 60.80 ? 988  HIS   A ND1 1 
ATOM   2193 C CD2 . HIS   A 1 296 ? 2.895   -14.215 46.957 1.00 60.13 ? 988  HIS   A CD2 1 
ATOM   2194 C CE1 . HIS   A 1 296 ? 2.727   -16.335 47.459 1.00 61.61 ? 988  HIS   A CE1 1 
ATOM   2195 N NE2 . HIS   A 1 296 ? 3.377   -15.210 47.780 1.00 61.45 ? 988  HIS   A NE2 1 
ATOM   2196 N N   . LEU   A 1 297 ? 3.109   -13.992 42.724 1.00 47.03 ? 989  LEU   A N   1 
ATOM   2197 C CA  . LEU   A 1 297 ? 4.487   -14.018 42.213 1.00 45.98 ? 989  LEU   A CA  1 
ATOM   2198 C C   . LEU   A 1 297 ? 5.411   -14.446 43.373 1.00 45.07 ? 989  LEU   A C   1 
ATOM   2199 O O   . LEU   A 1 297 ? 5.080   -14.234 44.549 1.00 44.70 ? 989  LEU   A O   1 
ATOM   2200 C CB  . LEU   A 1 297 ? 4.913   -12.644 41.676 1.00 45.79 ? 989  LEU   A CB  1 
ATOM   2201 C CG  . LEU   A 1 297 ? 4.327   -12.228 40.332 1.00 46.75 ? 989  LEU   A CG  1 
ATOM   2202 C CD1 . LEU   A 1 297 ? 4.682   -10.796 40.016 1.00 47.05 ? 989  LEU   A CD1 1 
ATOM   2203 C CD2 . LEU   A 1 297 ? 4.767   -13.159 39.220 1.00 47.02 ? 989  LEU   A CD2 1 
ATOM   2204 N N   . PRO   A 1 298 ? 6.532   -15.116 43.079 1.00 44.43 ? 990  PRO   A N   1 
ATOM   2205 C CA  . PRO   A 1 298 ? 7.398   -15.587 44.177 1.00 43.69 ? 990  PRO   A CA  1 
ATOM   2206 C C   . PRO   A 1 298 ? 7.871   -14.465 45.100 1.00 42.48 ? 990  PRO   A C   1 
ATOM   2207 O O   . PRO   A 1 298 ? 7.889   -13.291 44.708 1.00 42.53 ? 990  PRO   A O   1 
ATOM   2208 C CB  . PRO   A 1 298 ? 8.561   -16.284 43.459 1.00 44.50 ? 990  PRO   A CB  1 
ATOM   2209 C CG  . PRO   A 1 298 ? 8.516   -15.787 42.053 1.00 45.31 ? 990  PRO   A CG  1 
ATOM   2210 C CD  . PRO   A 1 298 ? 7.083   -15.460 41.754 1.00 43.87 ? 990  PRO   A CD  1 
ATOM   2211 N N   . SER   A 1 299 ? 8.203   -14.825 46.349 1.00 40.96 ? 991  SER   A N   1 
ATOM   2212 C CA  . SER   A 1 299 ? 8.741   -13.879 47.323 1.00 39.89 ? 991  SER   A CA  1 
ATOM   2213 C C   . SER   A 1 299 ? 10.105  -13.349 46.809 1.00 38.69 ? 991  SER   A C   1 
ATOM   2214 O O   . SER   A 1 299 ? 10.752  -14.008 45.980 1.00 38.37 ? 991  SER   A O   1 
ATOM   2215 C CB  . SER   A 1 299 ? 8.949   -14.588 48.661 1.00 40.89 ? 991  SER   A CB  1 
ATOM   2216 O OG  . SER   A 1 299 ? 9.859   -15.669 48.531 1.00 42.87 ? 991  SER   A OG  1 
ATOM   2217 N N   . PRO   A 1 300 ? 10.597  -12.188 47.307 1.00 37.72 ? 992  PRO   A N   1 
ATOM   2218 C CA  . PRO   A 1 300 ? 11.937  -11.731 46.895 1.00 37.04 ? 992  PRO   A CA  1 
ATOM   2219 C C   . PRO   A 1 300 ? 13.000  -12.799 47.177 1.00 36.15 ? 992  PRO   A C   1 
ATOM   2220 O O   . PRO   A 1 300 ? 13.878  -12.984 46.356 1.00 36.29 ? 992  PRO   A O   1 
ATOM   2221 C CB  . PRO   A 1 300 ? 12.158  -10.471 47.742 1.00 37.81 ? 992  PRO   A CB  1 
ATOM   2222 C CG  . PRO   A 1 300 ? 10.791  -10.015 48.111 1.00 38.37 ? 992  PRO   A CG  1 
ATOM   2223 C CD  . PRO   A 1 300 ? 10.002  -11.271 48.299 1.00 36.95 ? 992  PRO   A CD  1 
ATOM   2224 N N   . THR   A 1 301 ? 12.841  -13.565 48.280 1.00 35.30 ? 993  THR   A N   1 
ATOM   2225 C CA  . THR   A 1 301 ? 13.706  -14.678 48.677 1.00 35.10 ? 993  THR   A CA  1 
ATOM   2226 C C   . THR   A 1 301 ? 13.840  -15.720 47.558 1.00 34.73 ? 993  THR   A C   1 
ATOM   2227 O O   . THR   A 1 301 ? 14.961  -16.042 47.163 1.00 35.10 ? 993  THR   A O   1 
ATOM   2228 C CB  . THR   A 1 301 ? 13.168  -15.338 49.979 1.00 36.13 ? 993  THR   A CB  1 
ATOM   2229 O OG1 . THR   A 1 301 ? 13.282  -14.428 51.062 1.00 37.57 ? 993  THR   A OG1 1 
ATOM   2230 C CG2 . THR   A 1 301 ? 13.877  -16.641 50.323 1.00 35.94 ? 993  THR   A CG2 1 
ATOM   2231 N N   . ASP   A 1 302 ? 12.709  -16.223 47.029 1.00 33.90 ? 994  ASP   A N   1 
ATOM   2232 C CA  . ASP   A 1 302 ? 12.716  -17.253 45.995 1.00 33.80 ? 994  ASP   A CA  1 
ATOM   2233 C C   . ASP   A 1 302 ? 13.141  -16.740 44.599 1.00 32.73 ? 994  ASP   A C   1 
ATOM   2234 O O   . ASP   A 1 302 ? 13.716  -17.497 43.820 1.00 32.94 ? 994  ASP   A O   1 
ATOM   2235 C CB  . ASP   A 1 302 ? 11.359  -17.980 45.960 1.00 35.88 ? 994  ASP   A CB  1 
ATOM   2236 C CG  . ASP   A 1 302 ? 11.107  -18.873 47.170 1.00 40.64 ? 994  ASP   A CG  1 
ATOM   2237 O OD1 . ASP   A 1 302 ? 11.971  -18.912 48.075 1.00 41.23 ? 994  ASP   A OD1 1 
ATOM   2238 O OD2 . ASP   A 1 302 ? 10.051  -19.544 47.204 1.00 43.15 ? 994  ASP   A OD2 1 
ATOM   2239 N N   . SER   A 1 303 ? 12.897  -15.465 44.305 1.00 31.43 ? 995  SER   A N   1 
ATOM   2240 C CA  . SER   A 1 303 ? 13.341  -14.865 43.047 1.00 30.61 ? 995  SER   A CA  1 
ATOM   2241 C C   . SER   A 1 303 ? 14.853  -14.617 43.104 1.00 29.68 ? 995  SER   A C   1 
ATOM   2242 O O   . SER   A 1 303 ? 15.543  -14.809 42.101 1.00 29.74 ? 995  SER   A O   1 
ATOM   2243 C CB  . SER   A 1 303 ? 12.615  -13.552 42.800 1.00 31.40 ? 995  SER   A CB  1 
ATOM   2244 O OG  . SER   A 1 303 ? 11.250  -13.828 42.555 1.00 33.26 ? 995  SER   A OG  1 
ATOM   2245 N N   . ASN   A 1 304 ? 15.385  -14.229 44.282 1.00 28.44 ? 996  ASN   A N   1 
ATOM   2246 C CA  . ASN   A 1 304 ? 16.821  -14.031 44.425 1.00 28.73 ? 996  ASN   A CA  1 
ATOM   2247 C C   . ASN   A 1 304 ? 17.550  -15.361 44.183 1.00 27.47 ? 996  ASN   A C   1 
ATOM   2248 O O   . ASN   A 1 304 ? 18.542  -15.381 43.443 1.00 28.40 ? 996  ASN   A O   1 
ATOM   2249 C CB  . ASN   A 1 304 ? 17.186  -13.413 45.786 1.00 31.12 ? 996  ASN   A CB  1 
ATOM   2250 C CG  . ASN   A 1 304 ? 16.862  -11.928 45.896 1.00 35.08 ? 996  ASN   A CG  1 
ATOM   2251 O OD1 . ASN   A 1 304 ? 16.755  -11.210 44.887 1.00 36.23 ? 996  ASN   A OD1 1 
ATOM   2252 N ND2 . ASN   A 1 304 ? 16.669  -11.444 47.132 1.00 35.16 ? 996  ASN   A ND2 1 
ATOM   2253 N N   . PHE   A 1 305 ? 16.987  -16.469 44.717 1.00 25.19 ? 997  PHE   A N   1 
ATOM   2254 C CA  . PHE   A 1 305 ? 17.498  -17.824 44.539 1.00 23.77 ? 997  PHE   A CA  1 
ATOM   2255 C C   . PHE   A 1 305 ? 17.527  -18.218 43.061 1.00 23.52 ? 997  PHE   A C   1 
ATOM   2256 O O   . PHE   A 1 305 ? 18.598  -18.536 42.542 1.00 23.20 ? 997  PHE   A O   1 
ATOM   2257 C CB  . PHE   A 1 305 ? 16.667  -18.828 45.356 1.00 22.73 ? 997  PHE   A CB  1 
ATOM   2258 C CG  . PHE   A 1 305 ? 17.387  -20.129 45.617 1.00 21.98 ? 997  PHE   A CG  1 
ATOM   2259 C CD1 . PHE   A 1 305 ? 18.486  -20.173 46.450 1.00 22.54 ? 997  PHE   A CD1 1 
ATOM   2260 C CD2 . PHE   A 1 305 ? 16.942  -21.307 45.056 1.00 22.09 ? 997  PHE   A CD2 1 
ATOM   2261 C CE1 . PHE   A 1 305 ? 19.147  -21.366 46.692 1.00 22.98 ? 997  PHE   A CE1 1 
ATOM   2262 C CE2 . PHE   A 1 305 ? 17.582  -22.501 45.320 1.00 22.73 ? 997  PHE   A CE2 1 
ATOM   2263 C CZ  . PHE   A 1 305 ? 18.695  -22.522 46.121 1.00 22.97 ? 997  PHE   A CZ  1 
ATOM   2264 N N   . TYR   A 1 306 ? 16.372  -18.165 42.376 1.00 23.58 ? 998  TYR   A N   1 
ATOM   2265 C CA  . TYR   A 1 306 ? 16.255  -18.487 40.953 1.00 24.56 ? 998  TYR   A CA  1 
ATOM   2266 C C   . TYR   A 1 306 ? 17.259  -17.657 40.097 1.00 25.10 ? 998  TYR   A C   1 
ATOM   2267 O O   . TYR   A 1 306 ? 17.962  -18.218 39.267 1.00 25.26 ? 998  TYR   A O   1 
ATOM   2268 C CB  . TYR   A 1 306 ? 14.810  -18.217 40.477 1.00 24.73 ? 998  TYR   A CB  1 
ATOM   2269 C CG  . TYR   A 1 306 ? 13.900  -19.429 40.395 1.00 25.72 ? 998  TYR   A CG  1 
ATOM   2270 C CD1 . TYR   A 1 306 ? 14.137  -20.439 39.473 1.00 26.59 ? 998  TYR   A CD1 1 
ATOM   2271 C CD2 . TYR   A 1 306 ? 12.737  -19.503 41.152 1.00 26.52 ? 998  TYR   A CD2 1 
ATOM   2272 C CE1 . TYR   A 1 306 ? 13.278  -21.524 39.354 1.00 27.46 ? 998  TYR   A CE1 1 
ATOM   2273 C CE2 . TYR   A 1 306 ? 11.857  -20.572 41.025 1.00 27.44 ? 998  TYR   A CE2 1 
ATOM   2274 C CZ  . TYR   A 1 306 ? 12.134  -21.586 40.127 1.00 28.49 ? 998  TYR   A CZ  1 
ATOM   2275 O OH  . TYR   A 1 306 ? 11.268  -22.645 39.976 1.00 29.60 ? 998  TYR   A OH  1 
ATOM   2276 N N   . ARG   A 1 307 ? 17.333  -16.335 40.324 1.00 25.32 ? 999  ARG   A N   1 
ATOM   2277 C CA  . ARG   A 1 307 ? 18.235  -15.441 39.617 1.00 26.42 ? 999  ARG   A CA  1 
ATOM   2278 C C   . ARG   A 1 307 ? 19.718  -15.854 39.727 1.00 27.01 ? 999  ARG   A C   1 
ATOM   2279 O O   . ARG   A 1 307 ? 20.349  -16.081 38.701 1.00 26.95 ? 999  ARG   A O   1 
ATOM   2280 C CB  . ARG   A 1 307 ? 18.047  -13.996 40.109 1.00 28.85 ? 999  ARG   A CB  1 
ATOM   2281 C CG  . ARG   A 1 307 ? 16.941  -13.243 39.398 1.00 34.26 ? 999  ARG   A CG  1 
ATOM   2282 C CD  . ARG   A 1 307 ? 17.156  -11.743 39.440 1.00 39.66 ? 999  ARG   A CD  1 
ATOM   2283 N NE  . ARG   A 1 307 ? 18.493  -11.346 38.988 1.00 44.80 ? 999  ARG   A NE  1 
ATOM   2284 C CZ  . ARG   A 1 307 ? 18.827  -11.120 37.717 1.00 47.75 ? 999  ARG   A CZ  1 
ATOM   2285 N NH1 . ARG   A 1 307 ? 17.933  -11.284 36.748 1.00 47.38 ? 999  ARG   A NH1 1 
ATOM   2286 N NH2 . ARG   A 1 307 ? 20.061  -10.752 37.406 1.00 47.55 ? 999  ARG   A NH2 1 
ATOM   2287 N N   . ALA   A 1 308 ? 20.265  -15.978 40.952 1.00 27.13 ? 1000 ALA   A N   1 
ATOM   2288 C CA  . ALA   A 1 308 ? 21.672  -16.338 41.151 1.00 27.87 ? 1000 ALA   A CA  1 
ATOM   2289 C C   . ALA   A 1 308 ? 22.011  -17.719 40.600 1.00 28.95 ? 1000 ALA   A C   1 
ATOM   2290 O O   . ALA   A 1 308 ? 23.084  -17.919 40.037 1.00 29.04 ? 1000 ALA   A O   1 
ATOM   2291 C CB  . ALA   A 1 308 ? 22.033  -16.258 42.628 1.00 27.85 ? 1000 ALA   A CB  1 
ATOM   2292 N N   . LEU   A 1 309 ? 21.074  -18.648 40.702 1.00 29.71 ? 1001 LEU   A N   1 
ATOM   2293 C CA  . LEU   A 1 309 ? 21.277  -20.004 40.234 1.00 30.99 ? 1001 LEU   A CA  1 
ATOM   2294 C C   . LEU   A 1 309 ? 21.174  -20.164 38.689 1.00 32.41 ? 1001 LEU   A C   1 
ATOM   2295 O O   . LEU   A 1 309 ? 22.122  -20.647 38.057 1.00 33.22 ? 1001 LEU   A O   1 
ATOM   2296 C CB  . LEU   A 1 309 ? 20.250  -20.888 40.956 1.00 31.28 ? 1001 LEU   A CB  1 
ATOM   2297 C CG  . LEU   A 1 309 ? 20.680  -22.219 41.544 1.00 32.71 ? 1001 LEU   A CG  1 
ATOM   2298 C CD1 . LEU   A 1 309 ? 21.987  -22.118 42.327 1.00 33.06 ? 1001 LEU   A CD1 1 
ATOM   2299 C CD2 . LEU   A 1 309 ? 19.595  -22.753 42.431 1.00 33.24 ? 1001 LEU   A CD2 1 
ATOM   2300 N N   . MET   A 1 310 ? 20.051  -19.741 38.080 1.00 32.43 ? 1002 MET   A N   1 
ATOM   2301 C CA  . MET   A 1 310 ? 19.853  -19.961 36.653 1.00 32.71 ? 1002 MET   A CA  1 
ATOM   2302 C C   . MET   A 1 310 ? 19.494  -18.741 35.799 1.00 32.82 ? 1002 MET   A C   1 
ATOM   2303 O O   . MET   A 1 310 ? 19.322  -18.937 34.603 1.00 33.79 ? 1002 MET   A O   1 
ATOM   2304 C CB  . MET   A 1 310 ? 18.808  -21.070 36.421 1.00 32.81 ? 1002 MET   A CB  1 
ATOM   2305 C CG  . MET   A 1 310 ? 17.470  -20.833 37.078 1.00 33.66 ? 1002 MET   A CG  1 
ATOM   2306 S SD  . MET   A 1 310 ? 16.383  -22.319 37.090 1.00 38.39 ? 1002 MET   A SD  1 
ATOM   2307 C CE  . MET   A 1 310 ? 16.428  -22.818 35.373 1.00 36.24 ? 1002 MET   A CE  1 
ATOM   2308 N N   . ASP   A 1 311 ? 19.439  -17.515 36.339 1.00 31.71 ? 1003 ASP   A N   1 
ATOM   2309 C CA  . ASP   A 1 311 ? 19.111  -16.347 35.509 1.00 31.38 ? 1003 ASP   A CA  1 
ATOM   2310 C C   . ASP   A 1 311 ? 19.869  -15.115 35.948 1.00 31.74 ? 1003 ASP   A C   1 
ATOM   2311 O O   . ASP   A 1 311 ? 19.298  -14.207 36.554 1.00 31.08 ? 1003 ASP   A O   1 
ATOM   2312 C CB  . ASP   A 1 311 ? 17.594  -16.085 35.496 1.00 32.29 ? 1003 ASP   A CB  1 
ATOM   2313 C CG  . ASP   A 1 311 ? 17.125  -15.066 34.470 1.00 34.28 ? 1003 ASP   A CG  1 
ATOM   2314 O OD1 . ASP   A 1 311 ? 17.873  -14.804 33.506 1.00 34.55 ? 1003 ASP   A OD1 1 
ATOM   2315 O OD2 . ASP   A 1 311 ? 16.007  -14.539 34.628 1.00 35.59 ? 1003 ASP   A OD2 1 
ATOM   2316 N N   . GLU   A 1 312 ? 21.168  -15.095 35.670 1.00 32.82 ? 1004 GLU   A N   1 
ATOM   2317 C CA  . GLU   A 1 312 ? 22.023  -13.973 36.035 1.00 34.46 ? 1004 GLU   A CA  1 
ATOM   2318 C C   . GLU   A 1 312 ? 21.832  -12.760 35.104 1.00 36.07 ? 1004 GLU   A C   1 
ATOM   2319 O O   . GLU   A 1 312 ? 22.142  -11.641 35.510 1.00 35.90 ? 1004 GLU   A O   1 
ATOM   2320 C CB  . GLU   A 1 312 ? 23.503  -14.399 36.018 1.00 36.45 ? 1004 GLU   A CB  1 
ATOM   2321 C CG  . GLU   A 1 312 ? 23.885  -15.461 37.035 1.00 40.44 ? 1004 GLU   A CG  1 
ATOM   2322 C CD  . GLU   A 1 312 ? 25.385  -15.661 37.206 1.00 45.25 ? 1004 GLU   A CD  1 
ATOM   2323 O OE1 . GLU   A 1 312 ? 25.836  -15.683 38.373 1.00 47.99 ? 1004 GLU   A OE1 1 
ATOM   2324 O OE2 . GLU   A 1 312 ? 26.107  -15.791 36.188 1.00 44.48 ? 1004 GLU   A OE2 1 
ATOM   2325 N N   . GLU   A 1 313 ? 21.352  -12.983 33.854 1.00 37.32 ? 1005 GLU   A N   1 
ATOM   2326 C CA  . GLU   A 1 313 ? 21.181  -11.918 32.867 1.00 38.78 ? 1005 GLU   A CA  1 
ATOM   2327 C C   . GLU   A 1 313 ? 20.227  -10.820 33.321 1.00 40.39 ? 1005 GLU   A C   1 
ATOM   2328 O O   . GLU   A 1 313 ? 19.309  -11.050 34.110 1.00 40.54 ? 1005 GLU   A O   1 
ATOM   2329 C CB  . GLU   A 1 313 ? 20.793  -12.461 31.470 1.00 40.57 ? 1005 GLU   A CB  1 
ATOM   2330 C CG  . GLU   A 1 313 ? 19.311  -12.695 31.204 1.00 43.37 ? 1005 GLU   A CG  1 
ATOM   2331 C CD  . GLU   A 1 313 ? 18.964  -13.018 29.759 1.00 46.69 ? 1005 GLU   A CD  1 
ATOM   2332 O OE1 . GLU   A 1 313 ? 18.269  -14.035 29.534 1.00 49.21 ? 1005 GLU   A OE1 1 
ATOM   2333 O OE2 . GLU   A 1 313 ? 19.389  -12.268 28.849 1.00 45.82 ? 1005 GLU   A OE2 1 
ATOM   2334 N N   . ASP   A 1 314 ? 20.473  -9.616  32.824 1.00 41.27 ? 1006 ASP   A N   1 
ATOM   2335 C CA  . ASP   A 1 314 ? 19.683  -8.452  33.165 1.00 42.53 ? 1006 ASP   A CA  1 
ATOM   2336 C C   . ASP   A 1 314 ? 18.387  -8.406  32.344 1.00 42.53 ? 1006 ASP   A C   1 
ATOM   2337 O O   . ASP   A 1 314 ? 18.424  -8.508  31.116 1.00 42.30 ? 1006 ASP   A O   1 
ATOM   2338 C CB  . ASP   A 1 314 ? 20.522  -7.186  32.928 1.00 45.83 ? 1006 ASP   A CB  1 
ATOM   2339 C CG  . ASP   A 1 314 ? 20.034  -5.978  33.697 1.00 53.73 ? 1006 ASP   A CG  1 
ATOM   2340 O OD1 . ASP   A 1 314 ? 19.507  -6.163  34.825 1.00 55.12 ? 1006 ASP   A OD1 1 
ATOM   2341 O OD2 . ASP   A 1 314 ? 20.178  -4.843  33.174 1.00 56.93 ? 1006 ASP   A OD2 1 
ATOM   2342 N N   . MET   A 1 315 ? 17.245  -8.267  33.037 1.00 42.58 ? 1007 MET   A N   1 
ATOM   2343 C CA  . MET   A 1 315 ? 15.914  -8.133  32.426 1.00 43.12 ? 1007 MET   A CA  1 
ATOM   2344 C C   . MET   A 1 315 ? 15.085  -7.067  33.182 1.00 43.32 ? 1007 MET   A C   1 
ATOM   2345 O O   . MET   A 1 315 ? 15.356  -6.789  34.355 1.00 43.24 ? 1007 MET   A O   1 
ATOM   2346 C CB  . MET   A 1 315 ? 15.169  -9.490  32.313 1.00 43.88 ? 1007 MET   A CB  1 
ATOM   2347 C CG  . MET   A 1 315 ? 14.359  -9.890  33.553 1.00 46.14 ? 1007 MET   A CG  1 
ATOM   2348 S SD  . MET   A 1 315 ? 12.891  -10.890 33.173 1.00 47.99 ? 1007 MET   A SD  1 
ATOM   2349 C CE  . MET   A 1 315 ? 12.070  -10.897 34.757 1.00 42.53 ? 1007 MET   A CE  1 
ATOM   2350 N N   . ASP   A 1 316 ? 14.094  -6.467  32.516 1.00 43.27 ? 1008 ASP   A N   1 
ATOM   2351 C CA  . ASP   A 1 316 ? 13.243  -5.457  33.144 1.00 43.96 ? 1008 ASP   A CA  1 
ATOM   2352 C C   . ASP   A 1 316 ? 12.464  -6.057  34.309 1.00 43.51 ? 1008 ASP   A C   1 
ATOM   2353 O O   . ASP   A 1 316 ? 12.240  -7.275  34.346 1.00 43.77 ? 1008 ASP   A O   1 
ATOM   2354 C CB  . ASP   A 1 316 ? 12.266  -4.836  32.126 1.00 46.81 ? 1008 ASP   A CB  1 
ATOM   2355 C CG  . ASP   A 1 316 ? 12.928  -3.899  31.136 1.00 53.32 ? 1008 ASP   A CG  1 
ATOM   2356 O OD1 . ASP   A 1 316 ? 14.159  -4.011  30.943 1.00 54.19 ? 1008 ASP   A OD1 1 
ATOM   2357 O OD2 . ASP   A 1 316 ? 12.213  -3.060  30.542 1.00 56.65 ? 1008 ASP   A OD2 1 
ATOM   2358 N N   . ASP   A 1 317 ? 12.066  -5.214  35.269 1.00 42.55 ? 1009 ASP   A N   1 
ATOM   2359 C CA  . ASP   A 1 317 ? 11.321  -5.700  36.426 1.00 42.47 ? 1009 ASP   A CA  1 
ATOM   2360 C C   . ASP   A 1 317 ? 9.976   -6.275  36.008 1.00 42.05 ? 1009 ASP   A C   1 
ATOM   2361 O O   . ASP   A 1 317 ? 9.310   -5.748  35.115 1.00 41.78 ? 1009 ASP   A O   1 
ATOM   2362 C CB  . ASP   A 1 317 ? 11.113  -4.591  37.471 1.00 44.12 ? 1009 ASP   A CB  1 
ATOM   2363 C CG  . ASP   A 1 317 ? 12.383  -4.109  38.141 1.00 48.34 ? 1009 ASP   A CG  1 
ATOM   2364 O OD1 . ASP   A 1 317 ? 13.398  -4.833  38.079 1.00 48.24 ? 1009 ASP   A OD1 1 
ATOM   2365 O OD2 . ASP   A 1 317 ? 12.360  -3.005  38.724 1.00 50.97 ? 1009 ASP   A OD2 1 
ATOM   2366 N N   . VAL   A 1 318 ? 9.609   -7.389  36.622 1.00 41.76 ? 1010 VAL   A N   1 
ATOM   2367 C CA  . VAL   A 1 318 ? 8.326   -8.018  36.368 1.00 41.91 ? 1010 VAL   A CA  1 
ATOM   2368 C C   . VAL   A 1 318 ? 7.254   -7.095  37.018 1.00 42.24 ? 1010 VAL   A C   1 
ATOM   2369 O O   . VAL   A 1 318 ? 7.492   -6.540  38.096 1.00 42.49 ? 1010 VAL   A O   1 
ATOM   2370 C CB  . VAL   A 1 318 ? 8.363   -9.495  36.858 1.00 42.23 ? 1010 VAL   A CB  1 
ATOM   2371 C CG1 . VAL   A 1 318 ? 7.179   -9.862  37.731 1.00 42.93 ? 1010 VAL   A CG1 1 
ATOM   2372 C CG2 . VAL   A 1 318 ? 8.490   -10.454 35.688 1.00 42.46 ? 1010 VAL   A CG2 1 
ATOM   2373 N N   . VAL   A 1 319 ? 6.156   -6.820  36.290 1.00 41.92 ? 1011 VAL   A N   1 
ATOM   2374 C CA  . VAL   A 1 319 ? 5.099   -5.905  36.727 1.00 42.09 ? 1011 VAL   A CA  1 
ATOM   2375 C C   . VAL   A 1 319 ? 4.335   -6.463  37.936 1.00 42.95 ? 1011 VAL   A C   1 
ATOM   2376 O O   . VAL   A 1 319 ? 3.730   -7.536  37.856 1.00 43.21 ? 1011 VAL   A O   1 
ATOM   2377 C CB  . VAL   A 1 319 ? 4.145   -5.531  35.567 1.00 42.59 ? 1011 VAL   A CB  1 
ATOM   2378 C CG1 . VAL   A 1 319 ? 3.238   -4.376  35.965 1.00 43.06 ? 1011 VAL   A CG1 1 
ATOM   2379 C CG2 . VAL   A 1 319 ? 4.913   -5.197  34.287 1.00 42.81 ? 1011 VAL   A CG2 1 
ATOM   2380 N N   . ASP   A 1 320 ? 4.368   -5.743  39.058 1.00 43.02 ? 1012 ASP   A N   1 
ATOM   2381 C CA  . ASP   A 1 320 ? 3.709   -6.197  40.279 1.00 43.94 ? 1012 ASP   A CA  1 
ATOM   2382 C C   . ASP   A 1 320 ? 2.308   -5.592  40.480 1.00 44.24 ? 1012 ASP   A C   1 
ATOM   2383 O O   . ASP   A 1 320 ? 2.045   -4.471  40.046 1.00 44.07 ? 1012 ASP   A O   1 
ATOM   2384 C CB  . ASP   A 1 320 ? 4.602   -5.884  41.489 1.00 46.52 ? 1012 ASP   A CB  1 
ATOM   2385 C CG  . ASP   A 1 320 ? 4.614   -6.971  42.536 1.00 52.42 ? 1012 ASP   A CG  1 
ATOM   2386 O OD1 . ASP   A 1 320 ? 3.513   -7.449  42.914 1.00 53.17 ? 1012 ASP   A OD1 1 
ATOM   2387 O OD2 . ASP   A 1 320 ? 5.719   -7.343  42.987 1.00 55.22 ? 1012 ASP   A OD2 1 
ATOM   2388 N N   . ALA   A 1 321 ? 1.420   -6.333  41.164 1.00 44.57 ? 1013 ALA   A N   1 
ATOM   2389 C CA  . ALA   A 1 321 ? 0.061   -5.886  41.463 1.00 45.30 ? 1013 ALA   A CA  1 
ATOM   2390 C C   . ALA   A 1 321 ? 0.090   -4.818  42.549 1.00 46.22 ? 1013 ALA   A C   1 
ATOM   2391 O O   . ALA   A 1 321 ? 0.606   -5.079  43.634 1.00 46.19 ? 1013 ALA   A O   1 
ATOM   2392 C CB  . ALA   A 1 321 ? -0.775  -7.061  41.932 1.00 45.31 ? 1013 ALA   A CB  1 
ATOM   2393 N N   . ASP   A 1 322 ? -0.459  -3.622  42.254 1.00 46.98 ? 1014 ASP   A N   1 
ATOM   2394 C CA  . ASP   A 1 322 ? -0.520  -2.475  43.172 1.00 48.26 ? 1014 ASP   A CA  1 
ATOM   2395 C C   . ASP   A 1 322 ? -1.230  -2.809  44.495 1.00 49.14 ? 1014 ASP   A C   1 
ATOM   2396 O O   . ASP   A 1 322 ? -2.191  -3.583  44.517 1.00 49.49 ? 1014 ASP   A O   1 
ATOM   2397 C CB  . ASP   A 1 322 ? -1.212  -1.271  42.500 1.00 50.16 ? 1014 ASP   A CB  1 
ATOM   2398 C CG  . ASP   A 1 322 ? -0.647  -0.898  41.143 1.00 55.79 ? 1014 ASP   A CG  1 
ATOM   2399 O OD1 . ASP   A 1 322 ? 0.576   -1.062  40.942 1.00 57.24 ? 1014 ASP   A OD1 1 
ATOM   2400 O OD2 . ASP   A 1 322 ? -1.425  -0.438  40.283 1.00 58.26 ? 1014 ASP   A OD2 1 
ATOM   2401 N N   . ALA   B 1 6   ? 20.812  -6.894  62.038 1.00 57.90 ? 698  ALA   B N   1 
ATOM   2402 C CA  . ALA   B 1 6   ? 19.870  -7.644  61.208 1.00 58.35 ? 698  ALA   B CA  1 
ATOM   2403 C C   . ALA   B 1 6   ? 20.036  -7.350  59.712 1.00 58.33 ? 698  ALA   B C   1 
ATOM   2404 O O   . ALA   B 1 6   ? 19.427  -6.409  59.194 1.00 58.69 ? 698  ALA   B O   1 
ATOM   2405 C CB  . ALA   B 1 6   ? 18.440  -7.346  61.636 1.00 58.66 ? 698  ALA   B CB  1 
ATOM   2406 N N   . PRO   B 1 7   ? 20.819  -8.173  58.984 1.00 57.49 ? 699  PRO   B N   1 
ATOM   2407 C CA  . PRO   B 1 7   ? 20.976  -7.935  57.536 1.00 56.83 ? 699  PRO   B CA  1 
ATOM   2408 C C   . PRO   B 1 7   ? 19.745  -8.380  56.709 1.00 55.89 ? 699  PRO   B C   1 
ATOM   2409 O O   . PRO   B 1 7   ? 18.689  -8.675  57.296 1.00 56.48 ? 699  PRO   B O   1 
ATOM   2410 C CB  . PRO   B 1 7   ? 22.266  -8.707  57.193 1.00 57.55 ? 699  PRO   B CB  1 
ATOM   2411 C CG  . PRO   B 1 7   ? 22.347  -9.792  58.202 1.00 58.07 ? 699  PRO   B CG  1 
ATOM   2412 C CD  . PRO   B 1 7   ? 21.598  -9.344  59.440 1.00 56.89 ? 699  PRO   B CD  1 
ATOM   2413 N N   . ASN   B 1 8   ? 19.849  -8.399  55.354 1.00 54.02 ? 700  ASN   B N   1 
ATOM   2414 C CA  . ASN   B 1 8   ? 18.724  -8.850  54.542 1.00 52.72 ? 700  ASN   B CA  1 
ATOM   2415 C C   . ASN   B 1 8   ? 18.617  -10.369 54.581 1.00 50.99 ? 700  ASN   B C   1 
ATOM   2416 O O   . ASN   B 1 8   ? 19.319  -11.062 53.839 1.00 51.04 ? 700  ASN   B O   1 
ATOM   2417 C CB  . ASN   B 1 8   ? 18.802  -8.357  53.102 1.00 53.88 ? 700  ASN   B CB  1 
ATOM   2418 C CG  . ASN   B 1 8   ? 17.507  -8.560  52.347 1.00 57.01 ? 700  ASN   B CG  1 
ATOM   2419 O OD1 . ASN   B 1 8   ? 16.435  -8.777  52.930 1.00 58.21 ? 700  ASN   B OD1 1 
ATOM   2420 N ND2 . ASN   B 1 8   ? 17.570  -8.477  51.032 1.00 57.76 ? 700  ASN   B ND2 1 
ATOM   2421 N N   . GLN   B 1 9   ? 17.714  -10.885 55.437 1.00 49.26 ? 701  GLN   B N   1 
ATOM   2422 C CA  . GLN   B 1 9   ? 17.486  -12.324 55.550 1.00 47.62 ? 701  GLN   B CA  1 
ATOM   2423 C C   . GLN   B 1 9   ? 16.844  -12.919 54.272 1.00 45.38 ? 701  GLN   B C   1 
ATOM   2424 O O   . GLN   B 1 9   ? 16.889  -14.133 54.081 1.00 45.46 ? 701  GLN   B O   1 
ATOM   2425 C CB  . GLN   B 1 9   ? 16.724  -12.671 56.839 1.00 49.28 ? 701  GLN   B CB  1 
ATOM   2426 C CG  . GLN   B 1 9   ? 15.212  -12.813 56.738 1.00 53.30 ? 701  GLN   B CG  1 
ATOM   2427 C CD  . GLN   B 1 9   ? 14.603  -13.352 58.024 1.00 57.56 ? 701  GLN   B CD  1 
ATOM   2428 O OE1 . GLN   B 1 9   ? 15.249  -13.423 59.083 1.00 58.93 ? 701  GLN   B OE1 1 
ATOM   2429 N NE2 . GLN   B 1 9   ? 13.333  -13.736 57.959 1.00 57.63 ? 701  GLN   B NE2 1 
ATOM   2430 N N   . ALA   B 1 10  ? 16.339  -12.064 53.358 1.00 43.48 ? 702  ALA   B N   1 
ATOM   2431 C CA  . ALA   B 1 10  ? 15.831  -12.506 52.058 1.00 42.18 ? 702  ALA   B CA  1 
ATOM   2432 C C   . ALA   B 1 10  ? 16.979  -12.941 51.099 1.00 40.10 ? 702  ALA   B C   1 
ATOM   2433 O O   . ALA   B 1 10  ? 16.701  -13.475 50.026 1.00 39.94 ? 702  ALA   B O   1 
ATOM   2434 C CB  . ALA   B 1 10  ? 14.995  -11.412 51.410 1.00 42.29 ? 702  ALA   B CB  1 
ATOM   2435 N N   . LEU   B 1 11  ? 18.257  -12.707 51.472 1.00 38.06 ? 703  LEU   B N   1 
ATOM   2436 C CA  . LEU   B 1 11  ? 19.379  -13.163 50.650 1.00 36.42 ? 703  LEU   B CA  1 
ATOM   2437 C C   . LEU   B 1 11  ? 19.746  -14.641 50.920 1.00 34.56 ? 703  LEU   B C   1 
ATOM   2438 O O   . LEU   B 1 11  ? 20.532  -15.218 50.178 1.00 34.58 ? 703  LEU   B O   1 
ATOM   2439 C CB  . LEU   B 1 11  ? 20.592  -12.234 50.797 1.00 36.38 ? 703  LEU   B CB  1 
ATOM   2440 C CG  . LEU   B 1 11  ? 20.297  -10.755 50.545 1.00 37.78 ? 703  LEU   B CG  1 
ATOM   2441 C CD1 . LEU   B 1 11  ? 21.486  -9.900  50.812 1.00 38.26 ? 703  LEU   B CD1 1 
ATOM   2442 C CD2 . LEU   B 1 11  ? 19.820  -10.515 49.133 1.00 38.67 ? 703  LEU   B CD2 1 
ATOM   2443 N N   . LEU   B 1 12  ? 19.140  -15.265 51.944 1.00 33.00 ? 704  LEU   B N   1 
ATOM   2444 C CA  . LEU   B 1 12  ? 19.396  -16.659 52.282 1.00 32.18 ? 704  LEU   B CA  1 
ATOM   2445 C C   . LEU   B 1 12  ? 18.103  -17.484 52.218 1.00 31.96 ? 704  LEU   B C   1 
ATOM   2446 O O   . LEU   B 1 12  ? 17.175  -17.265 52.999 1.00 32.15 ? 704  LEU   B O   1 
ATOM   2447 C CB  . LEU   B 1 12  ? 20.012  -16.753 53.682 1.00 31.55 ? 704  LEU   B CB  1 
ATOM   2448 C CG  . LEU   B 1 12  ? 20.267  -18.152 54.198 1.00 32.62 ? 704  LEU   B CG  1 
ATOM   2449 C CD1 . LEU   B 1 12  ? 21.306  -18.859 53.344 1.00 33.47 ? 704  LEU   B CD1 1 
ATOM   2450 C CD2 . LEU   B 1 12  ? 20.697  -18.117 55.654 1.00 32.96 ? 704  LEU   B CD2 1 
ATOM   2451 N N   . ARG   B 1 13  ? 18.061  -18.444 51.307 1.00 31.48 ? 705  ARG   B N   1 
ATOM   2452 C CA  . ARG   B 1 13  ? 16.913  -19.323 51.172 1.00 31.71 ? 705  ARG   B CA  1 
ATOM   2453 C C   . ARG   B 1 13  ? 17.061  -20.493 52.142 1.00 31.29 ? 705  ARG   B C   1 
ATOM   2454 O O   . ARG   B 1 13  ? 18.125  -21.125 52.192 1.00 31.70 ? 705  ARG   B O   1 
ATOM   2455 C CB  . ARG   B 1 13  ? 16.784  -19.845 49.730 1.00 33.27 ? 705  ARG   B CB  1 
ATOM   2456 C CG  . ARG   B 1 13  ? 15.353  -20.187 49.368 1.00 36.78 ? 705  ARG   B CG  1 
ATOM   2457 C CD  . ARG   B 1 13  ? 15.314  -21.322 48.388 1.00 40.73 ? 705  ARG   B CD  1 
ATOM   2458 N NE  . ARG   B 1 13  ? 14.134  -22.170 48.566 1.00 44.32 ? 705  ARG   B NE  1 
ATOM   2459 C CZ  . ARG   B 1 13  ? 13.143  -22.275 47.687 1.00 47.13 ? 705  ARG   B CZ  1 
ATOM   2460 N NH1 . ARG   B 1 13  ? 13.161  -21.565 46.566 1.00 47.63 ? 705  ARG   B NH1 1 
ATOM   2461 N NH2 . ARG   B 1 13  ? 12.128  -23.097 47.919 1.00 47.06 ? 705  ARG   B NH2 1 
ATOM   2462 N N   . ILE   B 1 14  ? 16.015  -20.763 52.931 1.00 29.90 ? 706  ILE   B N   1 
ATOM   2463 C CA  . ILE   B 1 14  ? 16.047  -21.877 53.865 1.00 29.53 ? 706  ILE   B CA  1 
ATOM   2464 C C   . ILE   B 1 14  ? 15.550  -23.096 53.107 1.00 29.77 ? 706  ILE   B C   1 
ATOM   2465 O O   . ILE   B 1 14  ? 14.441  -23.070 52.587 1.00 29.79 ? 706  ILE   B O   1 
ATOM   2466 C CB  . ILE   B 1 14  ? 15.197  -21.564 55.120 1.00 29.46 ? 706  ILE   B CB  1 
ATOM   2467 C CG1 . ILE   B 1 14  ? 15.629  -20.229 55.750 1.00 29.89 ? 706  ILE   B CG1 1 
ATOM   2468 C CG2 . ILE   B 1 14  ? 15.276  -22.704 56.132 1.00 29.65 ? 706  ILE   B CG2 1 
ATOM   2469 C CD1 . ILE   B 1 14  ? 17.110  -20.165 56.191 1.00 30.47 ? 706  ILE   B CD1 1 
ATOM   2470 N N   . LEU   B 1 15  ? 16.377  -24.132 52.984 1.00 30.12 ? 707  LEU   B N   1 
ATOM   2471 C CA  . LEU   B 1 15  ? 16.003  -25.318 52.217 1.00 31.75 ? 707  LEU   B CA  1 
ATOM   2472 C C   . LEU   B 1 15  ? 15.573  -26.484 53.073 1.00 32.83 ? 707  LEU   B C   1 
ATOM   2473 O O   . LEU   B 1 15  ? 16.146  -26.727 54.130 1.00 33.33 ? 707  LEU   B O   1 
ATOM   2474 C CB  . LEU   B 1 15  ? 17.163  -25.779 51.321 1.00 32.32 ? 707  LEU   B CB  1 
ATOM   2475 C CG  . LEU   B 1 15  ? 17.508  -24.891 50.151 1.00 34.33 ? 707  LEU   B CG  1 
ATOM   2476 C CD1 . LEU   B 1 15  ? 18.812  -25.307 49.546 1.00 35.19 ? 707  LEU   B CD1 1 
ATOM   2477 C CD2 . LEU   B 1 15  ? 16.425  -24.936 49.098 1.00 35.48 ? 707  LEU   B CD2 1 
ATOM   2478 N N   . LYS   B 1 16  ? 14.603  -27.240 52.587 1.00 33.23 ? 708  LYS   B N   1 
ATOM   2479 C CA  . LYS   B 1 16  ? 14.130  -28.452 53.246 1.00 34.37 ? 708  LYS   B CA  1 
ATOM   2480 C C   . LYS   B 1 16  ? 14.841  -29.633 52.584 1.00 34.83 ? 708  LYS   B C   1 
ATOM   2481 O O   . LYS   B 1 16  ? 15.109  -29.610 51.376 1.00 34.13 ? 708  LYS   B O   1 
ATOM   2482 C CB  . LYS   B 1 16  ? 12.602  -28.609 53.090 1.00 36.98 ? 708  LYS   B CB  1 
ATOM   2483 C CG  . LYS   B 1 16  ? 11.780  -27.452 53.651 1.00 42.15 ? 708  LYS   B CG  1 
ATOM   2484 C CD  . LYS   B 1 16  ? 11.375  -27.697 55.105 1.00 47.75 ? 708  LYS   B CD  1 
ATOM   2485 C CE  . LYS   B 1 16  ? 9.906   -27.405 55.354 1.00 51.59 ? 708  LYS   B CE  1 
ATOM   2486 N NZ  . LYS   B 1 16  ? 9.521   -27.617 56.781 1.00 53.32 ? 708  LYS   B NZ  1 
ATOM   2487 N N   . GLU   B 1 17  ? 15.103  -30.691 53.357 1.00 35.77 ? 709  GLU   B N   1 
ATOM   2488 C CA  . GLU   B 1 17  ? 15.773  -31.893 52.853 1.00 36.98 ? 709  GLU   B CA  1 
ATOM   2489 C C   . GLU   B 1 17  ? 15.114  -32.469 51.595 1.00 37.44 ? 709  GLU   B C   1 
ATOM   2490 O O   . GLU   B 1 17  ? 15.802  -32.989 50.723 1.00 37.56 ? 709  GLU   B O   1 
ATOM   2491 C CB  . GLU   B 1 17  ? 15.849  -32.953 53.949 1.00 39.98 ? 709  GLU   B CB  1 
ATOM   2492 C CG  . GLU   B 1 17  ? 17.057  -33.859 53.813 1.00 47.89 ? 709  GLU   B CG  1 
ATOM   2493 C CD  . GLU   B 1 17  ? 17.554  -34.466 55.115 1.00 57.69 ? 709  GLU   B CD  1 
ATOM   2494 O OE1 . GLU   B 1 17  ? 16.858  -34.332 56.150 1.00 60.18 ? 709  GLU   B OE1 1 
ATOM   2495 O OE2 . GLU   B 1 17  ? 18.645  -35.080 55.097 1.00 60.57 ? 709  GLU   B OE2 1 
ATOM   2496 N N   . THR   B 1 18  ? 13.794  -32.322 51.474 1.00 37.58 ? 710  THR   B N   1 
ATOM   2497 C CA  . THR   B 1 18  ? 13.041  -32.818 50.320 1.00 38.33 ? 710  THR   B CA  1 
ATOM   2498 C C   . THR   B 1 18  ? 13.202  -31.987 49.041 1.00 39.38 ? 710  THR   B C   1 
ATOM   2499 O O   . THR   B 1 18  ? 12.878  -32.480 47.961 1.00 39.78 ? 710  THR   B O   1 
ATOM   2500 C CB  . THR   B 1 18  ? 11.563  -32.904 50.675 1.00 39.07 ? 710  THR   B CB  1 
ATOM   2501 O OG1 . THR   B 1 18  ? 11.112  -31.607 51.077 1.00 40.10 ? 710  THR   B OG1 1 
ATOM   2502 C CG2 . THR   B 1 18  ? 11.291  -33.921 51.767 1.00 38.84 ? 710  THR   B CG2 1 
ATOM   2503 N N   . GLU   B 1 19  ? 13.666  -30.726 49.155 1.00 39.63 ? 711  GLU   B N   1 
ATOM   2504 C CA  . GLU   B 1 19  ? 13.801  -29.826 48.006 1.00 39.83 ? 711  GLU   B CA  1 
ATOM   2505 C C   . GLU   B 1 19  ? 15.040  -30.099 47.153 1.00 39.75 ? 711  GLU   B C   1 
ATOM   2506 O O   . GLU   B 1 19  ? 15.074  -29.667 46.003 1.00 40.19 ? 711  GLU   B O   1 
ATOM   2507 C CB  . GLU   B 1 19  ? 13.846  -28.363 48.462 1.00 41.77 ? 711  GLU   B CB  1 
ATOM   2508 C CG  . GLU   B 1 19  ? 12.735  -27.934 49.396 1.00 46.31 ? 711  GLU   B CG  1 
ATOM   2509 C CD  . GLU   B 1 19  ? 12.642  -26.425 49.555 1.00 52.21 ? 711  GLU   B CD  1 
ATOM   2510 O OE1 . GLU   B 1 19  ? 12.159  -25.961 50.615 1.00 51.93 ? 711  GLU   B OE1 1 
ATOM   2511 O OE2 . GLU   B 1 19  ? 13.048  -25.704 48.615 1.00 55.10 ? 711  GLU   B OE2 1 
ATOM   2512 N N   . PHE   B 1 20  ? 16.066  -30.761 47.711 1.00 38.80 ? 712  PHE   B N   1 
ATOM   2513 C CA  . PHE   B 1 20  ? 17.322  -31.003 46.993 1.00 38.75 ? 712  PHE   B CA  1 
ATOM   2514 C C   . PHE   B 1 20  ? 17.917  -32.377 47.295 1.00 38.23 ? 712  PHE   B C   1 
ATOM   2515 O O   . PHE   B 1 20  ? 17.562  -32.973 48.305 1.00 38.29 ? 712  PHE   B O   1 
ATOM   2516 C CB  . PHE   B 1 20  ? 18.356  -29.911 47.358 1.00 38.71 ? 712  PHE   B CB  1 
ATOM   2517 C CG  . PHE   B 1 20  ? 18.844  -29.958 48.792 1.00 39.03 ? 712  PHE   B CG  1 
ATOM   2518 C CD1 . PHE   B 1 20  ? 18.131  -29.341 49.805 1.00 39.68 ? 712  PHE   B CD1 1 
ATOM   2519 C CD2 . PHE   B 1 20  ? 20.038  -30.585 49.116 1.00 39.59 ? 712  PHE   B CD2 1 
ATOM   2520 C CE1 . PHE   B 1 20  ? 18.584  -29.378 51.118 1.00 40.40 ? 712  PHE   B CE1 1 
ATOM   2521 C CE2 . PHE   B 1 20  ? 20.480  -30.636 50.431 1.00 40.09 ? 712  PHE   B CE2 1 
ATOM   2522 C CZ  . PHE   B 1 20  ? 19.754  -30.029 51.424 1.00 40.05 ? 712  PHE   B CZ  1 
ATOM   2523 N N   . LYS   B 1 21  ? 18.866  -32.852 46.455 1.00 37.56 ? 713  LYS   B N   1 
ATOM   2524 C CA  . LYS   B 1 21  ? 19.542  -34.148 46.620 1.00 37.47 ? 713  LYS   B CA  1 
ATOM   2525 C C   . LYS   B 1 21  ? 21.005  -34.094 46.167 1.00 37.39 ? 713  LYS   B C   1 
ATOM   2526 O O   . LYS   B 1 21  ? 21.287  -33.546 45.106 1.00 37.96 ? 713  LYS   B O   1 
ATOM   2527 C CB  . LYS   B 1 21  ? 18.840  -35.253 45.802 1.00 38.86 ? 713  LYS   B CB  1 
ATOM   2528 C CG  . LYS   B 1 21  ? 17.444  -35.637 46.276 1.00 42.37 ? 713  LYS   B CG  1 
ATOM   2529 C CD  . LYS   B 1 21  ? 17.442  -36.225 47.680 1.00 46.17 ? 713  LYS   B CD  1 
ATOM   2530 C CE  . LYS   B 1 21  ? 16.042  -36.351 48.236 1.00 49.82 ? 713  LYS   B CE  1 
ATOM   2531 N NZ  . LYS   B 1 21  ? 15.339  -35.036 48.284 1.00 52.27 ? 713  LYS   B NZ  1 
ATOM   2532 N N   . LYS   B 1 22  ? 21.929  -34.707 46.932 1.00 36.50 ? 714  LYS   B N   1 
ATOM   2533 C CA  . LYS   B 1 22  ? 23.341  -34.778 46.540 1.00 36.03 ? 714  LYS   B CA  1 
ATOM   2534 C C   . LYS   B 1 22  ? 23.482  -35.944 45.571 1.00 35.50 ? 714  LYS   B C   1 
ATOM   2535 O O   . LYS   B 1 22  ? 23.024  -37.043 45.895 1.00 35.91 ? 714  LYS   B O   1 
ATOM   2536 C CB  . LYS   B 1 22  ? 24.234  -35.042 47.763 1.00 37.69 ? 714  LYS   B CB  1 
ATOM   2537 C CG  . LYS   B 1 22  ? 24.188  -33.952 48.837 1.00 41.84 ? 714  LYS   B CG  1 
ATOM   2538 C CD  . LYS   B 1 22  ? 24.987  -34.360 50.087 1.00 45.77 ? 714  LYS   B CD  1 
ATOM   2539 C CE  . LYS   B 1 22  ? 24.167  -34.978 51.200 1.00 49.53 ? 714  LYS   B CE  1 
ATOM   2540 N NZ  . LYS   B 1 22  ? 23.529  -36.262 50.804 1.00 52.22 ? 714  LYS   B NZ  1 
ATOM   2541 N N   . ILE   B 1 23  ? 24.091  -35.734 44.392 1.00 34.63 ? 715  ILE   B N   1 
ATOM   2542 C CA  . ILE   B 1 23  ? 24.217  -36.830 43.434 1.00 34.73 ? 715  ILE   B CA  1 
ATOM   2543 C C   . ILE   B 1 23  ? 25.658  -37.302 43.237 1.00 35.42 ? 715  ILE   B C   1 
ATOM   2544 O O   . ILE   B 1 23  ? 25.862  -38.458 42.863 1.00 35.89 ? 715  ILE   B O   1 
ATOM   2545 C CB  . ILE   B 1 23  ? 23.526  -36.516 42.080 1.00 34.90 ? 715  ILE   B CB  1 
ATOM   2546 C CG1 . ILE   B 1 23  ? 24.272  -35.446 41.281 1.00 35.47 ? 715  ILE   B CG1 1 
ATOM   2547 C CG2 . ILE   B 1 23  ? 22.042  -36.156 42.274 1.00 35.36 ? 715  ILE   B CG2 1 
ATOM   2548 C CD1 . ILE   B 1 23  ? 23.774  -35.279 39.846 1.00 36.56 ? 715  ILE   B CD1 1 
ATOM   2549 N N   . LYS   B 1 24  ? 26.653  -36.457 43.527 1.00 35.32 ? 716  LYS   B N   1 
ATOM   2550 C CA  . LYS   B 1 24  ? 28.046  -36.829 43.281 1.00 35.89 ? 716  LYS   B CA  1 
ATOM   2551 C C   . LYS   B 1 24  ? 29.001  -36.140 44.258 1.00 36.14 ? 716  LYS   B C   1 
ATOM   2552 O O   . LYS   B 1 24  ? 28.702  -35.036 44.716 1.00 36.44 ? 716  LYS   B O   1 
ATOM   2553 C CB  . LYS   B 1 24  ? 28.379  -36.381 41.846 1.00 37.65 ? 716  LYS   B CB  1 
ATOM   2554 C CG  . LYS   B 1 24  ? 29.496  -37.119 41.154 1.00 41.52 ? 716  LYS   B CG  1 
ATOM   2555 C CD  . LYS   B 1 24  ? 29.723  -36.489 39.791 1.00 46.25 ? 716  LYS   B CD  1 
ATOM   2556 C CE  . LYS   B 1 24  ? 30.518  -37.359 38.846 1.00 50.65 ? 716  LYS   B CE  1 
ATOM   2557 N NZ  . LYS   B 1 24  ? 31.940  -37.488 39.258 1.00 52.99 ? 716  LYS   B NZ  1 
ATOM   2558 N N   . VAL   B 1 25  ? 30.163  -36.755 44.553 1.00 35.77 ? 717  VAL   B N   1 
ATOM   2559 C CA  . VAL   B 1 25  ? 31.159  -36.096 45.409 1.00 35.85 ? 717  VAL   B CA  1 
ATOM   2560 C C   . VAL   B 1 25  ? 32.179  -35.403 44.491 1.00 35.42 ? 717  VAL   B C   1 
ATOM   2561 O O   . VAL   B 1 25  ? 32.783  -36.054 43.635 1.00 35.92 ? 717  VAL   B O   1 
ATOM   2562 C CB  . VAL   B 1 25  ? 31.858  -37.043 46.423 1.00 36.93 ? 717  VAL   B CB  1 
ATOM   2563 C CG1 . VAL   B 1 25  ? 32.716  -36.248 47.406 1.00 37.49 ? 717  VAL   B CG1 1 
ATOM   2564 C CG2 . VAL   B 1 25  ? 30.846  -37.895 47.176 1.00 37.73 ? 717  VAL   B CG2 1 
ATOM   2565 N N   . LEU   B 1 26  ? 32.351  -34.084 44.642 1.00 34.32 ? 718  LEU   B N   1 
ATOM   2566 C CA  . LEU   B 1 26  ? 33.297  -33.321 43.818 1.00 33.51 ? 718  LEU   B CA  1 
ATOM   2567 C C   . LEU   B 1 26  ? 34.704  -33.271 44.423 1.00 32.99 ? 718  LEU   B C   1 
ATOM   2568 O O   . LEU   B 1 26  ? 35.705  -33.282 43.699 1.00 33.25 ? 718  LEU   B O   1 
ATOM   2569 C CB  . LEU   B 1 26  ? 32.783  -31.889 43.588 1.00 33.12 ? 718  LEU   B CB  1 
ATOM   2570 C CG  . LEU   B 1 26  ? 31.461  -31.746 42.835 1.00 33.85 ? 718  LEU   B CG  1 
ATOM   2571 C CD1 . LEU   B 1 26  ? 31.092  -30.270 42.647 1.00 34.00 ? 718  LEU   B CD1 1 
ATOM   2572 C CD2 . LEU   B 1 26  ? 31.501  -32.460 41.498 1.00 34.38 ? 718  LEU   B CD2 1 
ATOM   2573 N N   . GLY   B 1 27  ? 34.749  -33.189 45.742 1.00 31.90 ? 719  GLY   B N   1 
ATOM   2574 C CA  . GLY   B 1 27  ? 35.969  -33.107 46.525 1.00 31.86 ? 719  GLY   B CA  1 
ATOM   2575 C C   . GLY   B 1 27  ? 35.662  -32.900 47.995 1.00 31.95 ? 719  GLY   B C   1 
ATOM   2576 O O   . GLY   B 1 27  ? 34.527  -32.592 48.364 1.00 31.49 ? 719  GLY   B O   1 
ATOM   2577 N N   . SER   B 1 28  ? 36.656  -33.107 48.860 1.00 32.36 ? 720  SER   B N   1 
ATOM   2578 C CA  . SER   B 1 28  ? 36.461  -32.891 50.299 1.00 32.88 ? 720  SER   B CA  1 
ATOM   2579 C C   . SER   B 1 28  ? 37.617  -32.128 50.875 1.00 32.93 ? 720  SER   B C   1 
ATOM   2580 O O   . SER   B 1 28  ? 38.717  -32.163 50.325 1.00 33.36 ? 720  SER   B O   1 
ATOM   2581 C CB  . SER   B 1 28  ? 36.159  -34.186 51.054 1.00 34.26 ? 720  SER   B CB  1 
ATOM   2582 O OG  . SER   B 1 28  ? 37.250  -35.082 51.128 1.00 37.04 ? 720  SER   B OG  1 
ATOM   2583 N N   . GLY   B 1 29  ? 37.343  -31.348 51.903 1.00 32.74 ? 721  GLY   B N   1 
ATOM   2584 C CA  . GLY   B 1 29  ? 38.360  -30.507 52.513 1.00 33.18 ? 721  GLY   B CA  1 
ATOM   2585 C C   . GLY   B 1 29  ? 38.370  -30.577 54.021 1.00 33.28 ? 721  GLY   B C   1 
ATOM   2586 O O   . GLY   B 1 29  ? 37.772  -31.475 54.615 1.00 33.24 ? 721  GLY   B O   1 
ATOM   2587 N N   . ALA   B 1 30  ? 39.042  -29.613 54.647 1.00 33.05 ? 722  ALA   B N   1 
ATOM   2588 C CA  . ALA   B 1 30  ? 39.169  -29.545 56.099 1.00 32.97 ? 722  ALA   B CA  1 
ATOM   2589 C C   . ALA   B 1 30  ? 37.869  -29.199 56.809 1.00 32.36 ? 722  ALA   B C   1 
ATOM   2590 O O   . ALA   B 1 30  ? 37.693  -29.574 57.967 1.00 32.57 ? 722  ALA   B O   1 
ATOM   2591 C CB  . ALA   B 1 30  ? 40.239  -28.525 56.473 1.00 33.07 ? 722  ALA   B CB  1 
ATOM   2592 N N   . PHE   B 1 31  ? 36.969  -28.481 56.136 1.00 31.57 ? 723  PHE   B N   1 
ATOM   2593 C CA  . PHE   B 1 31  ? 35.731  -28.029 56.765 1.00 31.97 ? 723  PHE   B CA  1 
ATOM   2594 C C   . PHE   B 1 31  ? 34.472  -28.814 56.399 1.00 31.50 ? 723  PHE   B C   1 
ATOM   2595 O O   . PHE   B 1 31  ? 33.453  -28.706 57.089 1.00 31.69 ? 723  PHE   B O   1 
ATOM   2596 C CB  . PHE   B 1 31  ? 35.505  -26.538 56.481 1.00 32.23 ? 723  PHE   B CB  1 
ATOM   2597 C CG  . PHE   B 1 31  ? 36.469  -25.651 57.222 1.00 33.35 ? 723  PHE   B CG  1 
ATOM   2598 C CD1 . PHE   B 1 31  ? 37.731  -25.395 56.715 1.00 34.17 ? 723  PHE   B CD1 1 
ATOM   2599 C CD2 . PHE   B 1 31  ? 36.121  -25.085 58.432 1.00 34.64 ? 723  PHE   B CD2 1 
ATOM   2600 C CE1 . PHE   B 1 31  ? 38.621  -24.592 57.401 1.00 35.00 ? 723  PHE   B CE1 1 
ATOM   2601 C CE2 . PHE   B 1 31  ? 37.014  -24.270 59.113 1.00 35.65 ? 723  PHE   B CE2 1 
ATOM   2602 C CZ  . PHE   B 1 31  ? 38.258  -24.030 58.593 1.00 35.12 ? 723  PHE   B CZ  1 
ATOM   2603 N N   . GLY   B 1 32  ? 34.537  -29.564 55.320 1.00 30.50 ? 724  GLY   B N   1 
ATOM   2604 C CA  . GLY   B 1 32  ? 33.393  -30.318 54.857 1.00 30.24 ? 724  GLY   B CA  1 
ATOM   2605 C C   . GLY   B 1 32  ? 33.619  -30.967 53.515 1.00 29.62 ? 724  GLY   B C   1 
ATOM   2606 O O   . GLY   B 1 32  ? 34.751  -31.050 53.025 1.00 29.52 ? 724  GLY   B O   1 
ATOM   2607 N N   . THR   B 1 33  ? 32.527  -31.435 52.913 1.00 28.44 ? 725  THR   B N   1 
ATOM   2608 C CA  . THR   B 1 33  ? 32.604  -32.150 51.664 1.00 27.73 ? 725  THR   B CA  1 
ATOM   2609 C C   . THR   B 1 33  ? 31.735  -31.499 50.616 1.00 27.10 ? 725  THR   B C   1 
ATOM   2610 O O   . THR   B 1 33  ? 30.597  -31.133 50.893 1.00 26.66 ? 725  THR   B O   1 
ATOM   2611 C CB  . THR   B 1 33  ? 32.298  -33.615 51.945 1.00 28.25 ? 725  THR   B CB  1 
ATOM   2612 O OG1 . THR   B 1 33  ? 33.358  -34.096 52.772 1.00 28.76 ? 725  THR   B OG1 1 
ATOM   2613 C CG2 . THR   B 1 33  ? 32.177  -34.445 50.684 1.00 28.08 ? 725  THR   B CG2 1 
ATOM   2614 N N   . VAL   B 1 34  ? 32.300  -31.318 49.418 1.00 27.04 ? 726  VAL   B N   1 
ATOM   2615 C CA  . VAL   B 1 34  ? 31.640  -30.661 48.295 1.00 27.21 ? 726  VAL   B CA  1 
ATOM   2616 C C   . VAL   B 1 34  ? 31.010  -31.662 47.381 1.00 27.23 ? 726  VAL   B C   1 
ATOM   2617 O O   . VAL   B 1 34  ? 31.647  -32.614 46.970 1.00 27.21 ? 726  VAL   B O   1 
ATOM   2618 C CB  . VAL   B 1 34  ? 32.525  -29.646 47.515 1.00 27.33 ? 726  VAL   B CB  1 
ATOM   2619 C CG1 . VAL   B 1 34  ? 31.643  -28.646 46.771 1.00 27.63 ? 726  VAL   B CG1 1 
ATOM   2620 C CG2 . VAL   B 1 34  ? 33.497  -28.912 48.437 1.00 27.28 ? 726  VAL   B CG2 1 
ATOM   2621 N N   . TYR   B 1 35  ? 29.749  -31.429 47.062 1.00 27.76 ? 727  TYR   B N   1 
ATOM   2622 C CA  . TYR   B 1 35  ? 28.907  -32.282 46.237 1.00 28.22 ? 727  TYR   B CA  1 
ATOM   2623 C C   . TYR   B 1 35  ? 28.316  -31.550 45.059 1.00 27.89 ? 727  TYR   B C   1 
ATOM   2624 O O   . TYR   B 1 35  ? 28.038  -30.350 45.138 1.00 27.93 ? 727  TYR   B O   1 
ATOM   2625 C CB  . TYR   B 1 35  ? 27.700  -32.749 47.070 1.00 28.41 ? 727  TYR   B CB  1 
ATOM   2626 C CG  . TYR   B 1 35  ? 28.052  -33.603 48.255 1.00 29.79 ? 727  TYR   B CG  1 
ATOM   2627 C CD1 . TYR   B 1 35  ? 28.224  -34.974 48.122 1.00 30.88 ? 727  TYR   B CD1 1 
ATOM   2628 C CD2 . TYR   B 1 35  ? 28.236  -33.042 49.510 1.00 30.92 ? 727  TYR   B CD2 1 
ATOM   2629 C CE1 . TYR   B 1 35  ? 28.559  -35.767 49.210 1.00 31.73 ? 727  TYR   B CE1 1 
ATOM   2630 C CE2 . TYR   B 1 35  ? 28.568  -33.826 50.606 1.00 31.84 ? 727  TYR   B CE2 1 
ATOM   2631 C CZ  . TYR   B 1 35  ? 28.713  -35.191 50.454 1.00 32.61 ? 727  TYR   B CZ  1 
ATOM   2632 O OH  . TYR   B 1 35  ? 29.045  -35.977 51.527 1.00 34.31 ? 727  TYR   B OH  1 
ATOM   2633 N N   . LYS   B 1 36  ? 28.030  -32.294 44.001 1.00 27.43 ? 728  LYS   B N   1 
ATOM   2634 C CA  . LYS   B 1 36  ? 27.252  -31.759 42.892 1.00 27.52 ? 728  LYS   B CA  1 
ATOM   2635 C C   . LYS   B 1 36  ? 25.859  -32.216 43.258 1.00 27.27 ? 728  LYS   B C   1 
ATOM   2636 O O   . LYS   B 1 36  ? 25.645  -33.402 43.444 1.00 27.43 ? 728  LYS   B O   1 
ATOM   2637 C CB  . LYS   B 1 36  ? 27.682  -32.346 41.534 1.00 28.87 ? 728  LYS   B CB  1 
ATOM   2638 C CG  . LYS   B 1 36  ? 26.673  -32.053 40.427 1.00 32.45 ? 728  LYS   B CG  1 
ATOM   2639 C CD  . LYS   B 1 36  ? 27.254  -32.258 39.029 1.00 36.84 ? 728  LYS   B CD  1 
ATOM   2640 C CE  . LYS   B 1 36  ? 26.197  -32.042 37.974 1.00 40.19 ? 728  LYS   B CE  1 
ATOM   2641 N NZ  . LYS   B 1 36  ? 26.726  -32.290 36.603 1.00 42.89 ? 728  LYS   B NZ  1 
ATOM   2642 N N   . GLY   B 1 37  ? 24.946  -31.284 43.436 1.00 27.35 ? 729  GLY   B N   1 
ATOM   2643 C CA  . GLY   B 1 37  ? 23.577  -31.586 43.823 1.00 27.25 ? 729  GLY   B CA  1 
ATOM   2644 C C   . GLY   B 1 37  ? 22.544  -31.147 42.805 1.00 27.45 ? 729  GLY   B C   1 
ATOM   2645 O O   . GLY   B 1 37  ? 22.877  -30.553 41.776 1.00 27.23 ? 729  GLY   B O   1 
ATOM   2646 N N   . LEU   B 1 38  ? 21.281  -31.475 43.067 1.00 27.26 ? 730  LEU   B N   1 
ATOM   2647 C CA  . LEU   B 1 38  ? 20.192  -31.114 42.175 1.00 27.73 ? 730  LEU   B CA  1 
ATOM   2648 C C   . LEU   B 1 38  ? 19.042  -30.598 43.005 1.00 27.76 ? 730  LEU   B C   1 
ATOM   2649 O O   . LEU   B 1 38  ? 18.508  -31.333 43.827 1.00 28.11 ? 730  LEU   B O   1 
ATOM   2650 C CB  . LEU   B 1 38  ? 19.714  -32.316 41.357 1.00 28.24 ? 730  LEU   B CB  1 
ATOM   2651 C CG  . LEU   B 1 38  ? 20.579  -32.752 40.175 1.00 30.31 ? 730  LEU   B CG  1 
ATOM   2652 C CD1 . LEU   B 1 38  ? 19.930  -33.905 39.435 1.00 30.79 ? 730  LEU   B CD1 1 
ATOM   2653 C CD2 . LEU   B 1 38  ? 20.766  -31.623 39.188 1.00 31.20 ? 730  LEU   B CD2 1 
ATOM   2654 N N   . TRP   B 1 39  ? 18.685  -29.323 42.813 1.00 27.05 ? 731  TRP   B N   1 
ATOM   2655 C CA  . TRP   B 1 39  ? 17.564  -28.693 43.482 1.00 26.87 ? 731  TRP   B CA  1 
ATOM   2656 C C   . TRP   B 1 39  ? 16.327  -28.873 42.597 1.00 27.29 ? 731  TRP   B C   1 
ATOM   2657 O O   . TRP   B 1 39  ? 16.358  -28.543 41.409 1.00 26.66 ? 731  TRP   B O   1 
ATOM   2658 C CB  . TRP   B 1 39  ? 17.847  -27.198 43.679 1.00 26.42 ? 731  TRP   B CB  1 
ATOM   2659 C CG  . TRP   B 1 39  ? 16.661  -26.390 44.118 1.00 26.56 ? 731  TRP   B CG  1 
ATOM   2660 C CD1 . TRP   B 1 39  ? 15.887  -26.595 45.225 1.00 27.23 ? 731  TRP   B CD1 1 
ATOM   2661 C CD2 . TRP   B 1 39  ? 16.113  -25.248 43.451 1.00 26.32 ? 731  TRP   B CD2 1 
ATOM   2662 N NE1 . TRP   B 1 39  ? 14.914  -25.627 45.307 1.00 27.15 ? 731  TRP   B NE1 1 
ATOM   2663 C CE2 . TRP   B 1 39  ? 15.041  -24.776 44.238 1.00 26.83 ? 731  TRP   B CE2 1 
ATOM   2664 C CE3 . TRP   B 1 39  ? 16.436  -24.563 42.272 1.00 26.55 ? 731  TRP   B CE3 1 
ATOM   2665 C CZ2 . TRP   B 1 39  ? 14.311  -23.638 43.898 1.00 27.18 ? 731  TRP   B CZ2 1 
ATOM   2666 C CZ3 . TRP   B 1 39  ? 15.703  -23.443 41.930 1.00 27.11 ? 731  TRP   B CZ3 1 
ATOM   2667 C CH2 . TRP   B 1 39  ? 14.642  -23.004 42.728 1.00 27.38 ? 731  TRP   B CH2 1 
ATOM   2668 N N   . ILE   B 1 40  ? 15.242  -29.409 43.177 1.00 28.05 ? 732  ILE   B N   1 
ATOM   2669 C CA  . ILE   B 1 40  ? 13.974  -29.585 42.478 1.00 28.64 ? 732  ILE   B CA  1 
ATOM   2670 C C   . ILE   B 1 40  ? 13.029  -28.586 43.126 1.00 28.54 ? 732  ILE   B C   1 
ATOM   2671 O O   . ILE   B 1 40  ? 12.694  -28.762 44.293 1.00 28.99 ? 732  ILE   B O   1 
ATOM   2672 C CB  . ILE   B 1 40  ? 13.428  -31.040 42.570 1.00 29.95 ? 732  ILE   B CB  1 
ATOM   2673 C CG1 . ILE   B 1 40  ? 14.412  -32.074 41.968 1.00 31.30 ? 732  ILE   B CG1 1 
ATOM   2674 C CG2 . ILE   B 1 40  ? 12.059  -31.139 41.875 1.00 30.75 ? 732  ILE   B CG2 1 
ATOM   2675 C CD1 . ILE   B 1 40  ? 15.440  -32.713 42.974 1.00 32.51 ? 732  ILE   B CD1 1 
ATOM   2676 N N   . PRO   B 1 41  ? 12.690  -27.472 42.445 1.00 28.18 ? 733  PRO   B N   1 
ATOM   2677 C CA  . PRO   B 1 41  ? 11.797  -26.475 43.071 1.00 28.46 ? 733  PRO   B CA  1 
ATOM   2678 C C   . PRO   B 1 41  ? 10.344  -26.961 43.276 1.00 29.66 ? 733  PRO   B C   1 
ATOM   2679 O O   . PRO   B 1 41  ? 9.822   -27.704 42.456 1.00 28.91 ? 733  PRO   B O   1 
ATOM   2680 C CB  . PRO   B 1 41  ? 11.872  -25.268 42.132 1.00 28.68 ? 733  PRO   B CB  1 
ATOM   2681 C CG  . PRO   B 1 41  ? 12.432  -25.778 40.848 1.00 29.09 ? 733  PRO   B CG  1 
ATOM   2682 C CD  . PRO   B 1 41  ? 13.060  -27.111 41.060 1.00 27.60 ? 733  PRO   B CD  1 
ATOM   2683 N N   . GLU   B 1 42  ? 9.704   -26.534 44.382 1.00 30.95 ? 734  GLU   B N   1 
ATOM   2684 C CA  . GLU   B 1 42  ? 8.350   -26.928 44.750 1.00 32.81 ? 734  GLU   B CA  1 
ATOM   2685 C C   . GLU   B 1 42  ? 7.325   -26.798 43.596 1.00 33.77 ? 734  GLU   B C   1 
ATOM   2686 O O   . GLU   B 1 42  ? 7.158   -25.724 43.006 1.00 34.23 ? 734  GLU   B O   1 
ATOM   2687 C CB  . GLU   B 1 42  ? 7.878   -26.193 46.022 1.00 35.59 ? 734  GLU   B CB  1 
ATOM   2688 C CG  . GLU   B 1 42  ? 8.615   -26.662 47.273 1.00 41.84 ? 734  GLU   B CG  1 
ATOM   2689 C CD  . GLU   B 1 42  ? 7.922   -26.398 48.598 1.00 50.15 ? 734  GLU   B CD  1 
ATOM   2690 O OE1 . GLU   B 1 42  ? 6.747   -26.810 48.752 1.00 52.63 ? 734  GLU   B OE1 1 
ATOM   2691 O OE2 . GLU   B 1 42  ? 8.561   -25.787 49.487 1.00 50.97 ? 734  GLU   B OE2 1 
ATOM   2692 N N   . GLY   B 1 43  ? 6.714   -27.934 43.261 1.00 33.48 ? 735  GLY   B N   1 
ATOM   2693 C CA  . GLY   B 1 43  ? 5.716   -28.035 42.206 1.00 33.73 ? 735  GLY   B CA  1 
ATOM   2694 C C   . GLY   B 1 43  ? 6.277   -28.118 40.801 1.00 33.72 ? 735  GLY   B C   1 
ATOM   2695 O O   . GLY   B 1 43  ? 5.512   -28.080 39.829 1.00 34.14 ? 735  GLY   B O   1 
ATOM   2696 N N   . GLU   B 1 44  ? 7.615   -28.232 40.665 1.00 32.58 ? 736  GLU   B N   1 
ATOM   2697 C CA  . GLU   B 1 44  ? 8.234   -28.270 39.343 1.00 31.74 ? 736  GLU   B CA  1 
ATOM   2698 C C   . GLU   B 1 44  ? 8.794   -29.632 38.980 1.00 32.88 ? 736  GLU   B C   1 
ATOM   2699 O O   . GLU   B 1 44  ? 8.964   -30.491 39.836 1.00 33.26 ? 736  GLU   B O   1 
ATOM   2700 C CB  . GLU   B 1 44  ? 9.302   -27.159 39.191 1.00 30.37 ? 736  GLU   B CB  1 
ATOM   2701 C CG  . GLU   B 1 44  ? 8.780   -25.766 39.479 1.00 29.74 ? 736  GLU   B CG  1 
ATOM   2702 C CD  . GLU   B 1 44  ? 7.862   -25.159 38.434 1.00 33.52 ? 736  GLU   B CD  1 
ATOM   2703 O OE1 . GLU   B 1 44  ? 7.666   -25.772 37.358 1.00 32.92 ? 736  GLU   B OE1 1 
ATOM   2704 O OE2 . GLU   B 1 44  ? 7.337   -24.055 38.699 1.00 35.43 ? 736  GLU   B OE2 1 
ATOM   2705 N N   . LYS   B 1 45  ? 9.082   -29.817 37.696 1.00 33.58 ? 737  LYS   B N   1 
ATOM   2706 C CA  . LYS   B 1 45  ? 9.619   -31.037 37.095 1.00 34.56 ? 737  LYS   B CA  1 
ATOM   2707 C C   . LYS   B 1 45  ? 11.165  -30.987 36.965 1.00 34.15 ? 737  LYS   B C   1 
ATOM   2708 O O   . LYS   B 1 45  ? 11.829  -32.025 36.926 1.00 34.74 ? 737  LYS   B O   1 
ATOM   2709 C CB  . LYS   B 1 45  ? 8.965   -31.167 35.700 1.00 37.58 ? 737  LYS   B CB  1 
ATOM   2710 C CG  . LYS   B 1 45  ? 9.277   -32.423 34.901 1.00 43.63 ? 737  LYS   B CG  1 
ATOM   2711 C CD  . LYS   B 1 45  ? 8.538   -32.370 33.549 1.00 49.71 ? 737  LYS   B CD  1 
ATOM   2712 C CE  . LYS   B 1 45  ? 8.744   -33.603 32.684 1.00 54.85 ? 737  LYS   B CE  1 
ATOM   2713 N NZ  . LYS   B 1 45  ? 8.106   -34.824 33.261 1.00 57.30 ? 737  LYS   B NZ  1 
ATOM   2714 N N   . VAL   B 1 46  ? 11.727  -29.782 36.886 1.00 33.00 ? 738  VAL   B N   1 
ATOM   2715 C CA  . VAL   B 1 46  ? 13.147  -29.550 36.684 1.00 32.25 ? 738  VAL   B CA  1 
ATOM   2716 C C   . VAL   B 1 46  ? 14.052  -29.940 37.840 1.00 31.53 ? 738  VAL   B C   1 
ATOM   2717 O O   . VAL   B 1 46  ? 13.689  -29.838 39.018 1.00 31.52 ? 738  VAL   B O   1 
ATOM   2718 C CB  . VAL   B 1 46  ? 13.396  -28.075 36.303 1.00 32.63 ? 738  VAL   B CB  1 
ATOM   2719 C CG1 . VAL   B 1 46  ? 12.836  -27.786 34.930 1.00 32.94 ? 738  VAL   B CG1 1 
ATOM   2720 C CG2 . VAL   B 1 46  ? 12.795  -27.130 37.340 1.00 32.82 ? 738  VAL   B CG2 1 
ATOM   2721 N N   . LYS   B 1 47  ? 15.274  -30.339 37.476 1.00 30.72 ? 739  LYS   B N   1 
ATOM   2722 C CA  . LYS   B 1 47  ? 16.343  -30.662 38.410 1.00 30.28 ? 739  LYS   B CA  1 
ATOM   2723 C C   . LYS   B 1 47  ? 17.457  -29.666 38.080 1.00 29.20 ? 739  LYS   B C   1 
ATOM   2724 O O   . LYS   B 1 47  ? 18.013  -29.714 36.985 1.00 29.87 ? 739  LYS   B O   1 
ATOM   2725 C CB  . LYS   B 1 47  ? 16.796  -32.113 38.217 1.00 32.29 ? 739  LYS   B CB  1 
ATOM   2726 C CG  . LYS   B 1 47  ? 15.653  -33.101 38.436 1.00 37.32 ? 739  LYS   B CG  1 
ATOM   2727 C CD  . LYS   B 1 47  ? 16.109  -34.542 38.303 1.00 43.07 ? 739  LYS   B CD  1 
ATOM   2728 C CE  . LYS   B 1 47  ? 15.026  -35.524 38.688 1.00 47.47 ? 739  LYS   B CE  1 
ATOM   2729 N NZ  . LYS   B 1 47  ? 14.548  -35.301 40.078 1.00 50.19 ? 739  LYS   B NZ  1 
ATOM   2730 N N   . ILE   B 1 48  ? 17.695  -28.698 38.970 1.00 27.50 ? 740  ILE   B N   1 
ATOM   2731 C CA  . ILE   B 1 48  ? 18.668  -27.618 38.773 1.00 26.32 ? 740  ILE   B CA  1 
ATOM   2732 C C   . ILE   B 1 48  ? 20.010  -27.912 39.442 1.00 25.22 ? 740  ILE   B C   1 
ATOM   2733 O O   . ILE   B 1 48  ? 20.076  -28.015 40.664 1.00 25.21 ? 740  ILE   B O   1 
ATOM   2734 C CB  . ILE   B 1 48  ? 18.076  -26.267 39.294 1.00 26.40 ? 740  ILE   B CB  1 
ATOM   2735 C CG1 . ILE   B 1 48  ? 16.672  -25.970 38.710 1.00 27.54 ? 740  ILE   B CG1 1 
ATOM   2736 C CG2 . ILE   B 1 48  ? 19.035  -25.104 39.081 1.00 26.61 ? 740  ILE   B CG2 1 
ATOM   2737 C CD1 . ILE   B 1 48  ? 16.584  -26.012 37.206 1.00 29.28 ? 740  ILE   B CD1 1 
ATOM   2738 N N   . PRO   B 1 49  ? 21.098  -28.016 38.667 1.00 24.31 ? 741  PRO   B N   1 
ATOM   2739 C CA  . PRO   B 1 49  ? 22.419  -28.247 39.284 1.00 24.53 ? 741  PRO   B CA  1 
ATOM   2740 C C   . PRO   B 1 49  ? 22.832  -27.163 40.281 1.00 25.67 ? 741  PRO   B C   1 
ATOM   2741 O O   . PRO   B 1 49  ? 22.714  -25.972 39.992 1.00 26.29 ? 741  PRO   B O   1 
ATOM   2742 C CB  . PRO   B 1 49  ? 23.384  -28.254 38.094 1.00 24.60 ? 741  PRO   B CB  1 
ATOM   2743 C CG  . PRO   B 1 49  ? 22.527  -28.462 36.889 1.00 24.63 ? 741  PRO   B CG  1 
ATOM   2744 C CD  . PRO   B 1 49  ? 21.179  -27.914 37.200 1.00 23.21 ? 741  PRO   B CD  1 
ATOM   2745 N N   . VAL   B 1 50  ? 23.275  -27.579 41.480 1.00 25.49 ? 742  VAL   B N   1 
ATOM   2746 C CA  . VAL   B 1 50  ? 23.771  -26.693 42.531 1.00 25.49 ? 742  VAL   B CA  1 
ATOM   2747 C C   . VAL   B 1 50  ? 25.044  -27.310 43.160 1.00 25.59 ? 742  VAL   B C   1 
ATOM   2748 O O   . VAL   B 1 50  ? 25.298  -28.511 42.996 1.00 25.28 ? 742  VAL   B O   1 
ATOM   2749 C CB  . VAL   B 1 50  ? 22.700  -26.377 43.627 1.00 26.13 ? 742  VAL   B CB  1 
ATOM   2750 C CG1 . VAL   B 1 50  ? 21.386  -25.904 43.020 1.00 27.16 ? 742  VAL   B CG1 1 
ATOM   2751 C CG2 . VAL   B 1 50  ? 22.464  -27.558 44.557 1.00 26.06 ? 742  VAL   B CG2 1 
ATOM   2752 N N   . ALA   B 1 51  ? 25.837  -26.501 43.884 1.00 25.47 ? 743  ALA   B N   1 
ATOM   2753 C CA  . ALA   B 1 51  ? 26.967  -27.043 44.632 1.00 26.35 ? 743  ALA   B CA  1 
ATOM   2754 C C   . ALA   B 1 51  ? 26.546  -27.045 46.103 1.00 27.21 ? 743  ALA   B C   1 
ATOM   2755 O O   . ALA   B 1 51  ? 25.938  -26.079 46.587 1.00 27.30 ? 743  ALA   B O   1 
ATOM   2756 C CB  . ALA   B 1 51  ? 28.202  -26.203 44.451 1.00 26.71 ? 743  ALA   B CB  1 
ATOM   2757 N N   . ILE   B 1 52  ? 26.803  -28.162 46.798 1.00 27.24 ? 744  ILE   B N   1 
ATOM   2758 C CA  . ILE   B 1 52  ? 26.423  -28.306 48.200 1.00 27.51 ? 744  ILE   B CA  1 
ATOM   2759 C C   . ILE   B 1 52  ? 27.664  -28.622 49.033 1.00 27.76 ? 744  ILE   B C   1 
ATOM   2760 O O   . ILE   B 1 52  ? 28.469  -29.444 48.621 1.00 27.89 ? 744  ILE   B O   1 
ATOM   2761 C CB  . ILE   B 1 52  ? 25.366  -29.439 48.388 1.00 27.52 ? 744  ILE   B CB  1 
ATOM   2762 C CG1 . ILE   B 1 52  ? 24.160  -29.296 47.449 1.00 28.05 ? 744  ILE   B CG1 1 
ATOM   2763 C CG2 . ILE   B 1 52  ? 24.927  -29.551 49.850 1.00 27.57 ? 744  ILE   B CG2 1 
ATOM   2764 C CD1 . ILE   B 1 52  ? 23.312  -30.565 47.394 1.00 29.34 ? 744  ILE   B CD1 1 
ATOM   2765 N N   . LYS   B 1 53  ? 27.798  -28.009 50.209 1.00 27.56 ? 745  LYS   B N   1 
ATOM   2766 C CA  . LYS   B 1 53  ? 28.892  -28.303 51.107 1.00 28.10 ? 745  LYS   B CA  1 
ATOM   2767 C C   . LYS   B 1 53  ? 28.327  -28.789 52.450 1.00 29.60 ? 745  LYS   B C   1 
ATOM   2768 O O   . LYS   B 1 53  ? 27.694  -28.018 53.175 1.00 29.43 ? 745  LYS   B O   1 
ATOM   2769 C CB  . LYS   B 1 53  ? 29.809  -27.081 51.318 1.00 28.58 ? 745  LYS   B CB  1 
ATOM   2770 C CG  . LYS   B 1 53  ? 31.212  -27.492 51.748 1.00 30.70 ? 745  LYS   B CG  1 
ATOM   2771 C CD  . LYS   B 1 53  ? 31.994  -26.377 52.372 1.00 34.12 ? 745  LYS   B CD  1 
ATOM   2772 C CE  . LYS   B 1 53  ? 33.466  -26.537 52.107 1.00 37.97 ? 745  LYS   B CE  1 
ATOM   2773 N NZ  . LYS   B 1 53  ? 33.878  -25.938 50.798 1.00 40.31 ? 745  LYS   B NZ  1 
ATOM   2774 N N   . GLU   B 1 54  ? 28.566  -30.066 52.786 1.00 30.72 ? 746  GLU   B N   1 
ATOM   2775 C CA  . GLU   B 1 54  ? 28.111  -30.608 54.060 1.00 32.11 ? 746  GLU   B CA  1 
ATOM   2776 C C   . GLU   B 1 54  ? 29.250  -30.510 55.032 1.00 33.78 ? 746  GLU   B C   1 
ATOM   2777 O O   . GLU   B 1 54  ? 30.305  -31.093 54.808 1.00 33.60 ? 746  GLU   B O   1 
ATOM   2778 C CB  . GLU   B 1 54  ? 27.670  -32.059 53.929 1.00 33.43 ? 746  GLU   B CB  1 
ATOM   2779 C CG  . GLU   B 1 54  ? 27.004  -32.546 55.194 1.00 37.47 ? 746  GLU   B CG  1 
ATOM   2780 C CD  . GLU   B 1 54  ? 26.099  -33.734 54.950 1.00 44.27 ? 746  GLU   B CD  1 
ATOM   2781 O OE1 . GLU   B 1 54  ? 26.553  -34.695 54.289 1.00 45.64 ? 746  GLU   B OE1 1 
ATOM   2782 O OE2 . GLU   B 1 54  ? 24.927  -33.693 55.389 1.00 46.62 ? 746  GLU   B OE2 1 
ATOM   2783 N N   . LEU   B 1 55  ? 29.052  -29.755 56.092 1.00 35.58 ? 747  LEU   B N   1 
ATOM   2784 C CA  . LEU   B 1 55  ? 30.094  -29.526 57.077 1.00 38.03 ? 747  LEU   B CA  1 
ATOM   2785 C C   . LEU   B 1 55  ? 30.217  -30.671 58.080 1.00 41.42 ? 747  LEU   B C   1 
ATOM   2786 O O   . LEU   B 1 55  ? 29.270  -31.427 58.300 1.00 41.09 ? 747  LEU   B O   1 
ATOM   2787 C CB  . LEU   B 1 55  ? 29.888  -28.178 57.796 1.00 37.69 ? 747  LEU   B CB  1 
ATOM   2788 C CG  . LEU   B 1 55  ? 29.632  -26.955 56.908 1.00 38.61 ? 747  LEU   B CG  1 
ATOM   2789 C CD1 . LEU   B 1 55  ? 29.422  -25.722 57.747 1.00 38.87 ? 747  LEU   B CD1 1 
ATOM   2790 C CD2 . LEU   B 1 55  ? 30.761  -26.733 55.911 1.00 39.08 ? 747  LEU   B CD2 1 
ATOM   2791 N N   . ARG   B 1 56  ? 31.410  -30.784 58.685 1.00 44.34 ? 748  ARG   B N   1 
ATOM   2792 C CA  . ARG   B 1 56  ? 31.759  -31.779 59.699 1.00 47.41 ? 748  ARG   B CA  1 
ATOM   2793 C C   . ARG   B 1 56  ? 31.183  -31.362 61.072 1.00 50.23 ? 748  ARG   B C   1 
ATOM   2794 O O   . ARG   B 1 56  ? 30.679  -30.244 61.215 1.00 50.54 ? 748  ARG   B O   1 
ATOM   2795 C CB  . ARG   B 1 56  ? 33.302  -31.900 59.805 1.00 49.14 ? 748  ARG   B CB  1 
ATOM   2796 C CG  . ARG   B 1 56  ? 34.060  -31.674 58.504 1.00 52.35 ? 748  ARG   B CG  1 
ATOM   2797 C CD  . ARG   B 1 56  ? 35.479  -32.206 58.578 1.00 55.77 ? 748  ARG   B CD  1 
ATOM   2798 N NE  . ARG   B 1 56  ? 36.034  -32.506 57.254 1.00 59.07 ? 748  ARG   B NE  1 
ATOM   2799 C CZ  . ARG   B 1 56  ? 35.744  -33.596 56.548 1.00 61.82 ? 748  ARG   B CZ  1 
ATOM   2800 N NH1 . ARG   B 1 56  ? 36.295  -33.787 55.357 1.00 61.77 ? 748  ARG   B NH1 1 
ATOM   2801 N NH2 . ARG   B 1 56  ? 34.883  -34.492 57.017 1.00 62.00 ? 748  ARG   B NH2 1 
ATOM   2802 N N   . GLU   B 1 57  ? 31.274  -32.244 62.085 1.00 52.09 ? 749  GLU   B N   1 
ATOM   2803 C CA  . GLU   B 1 57  ? 30.818  -31.899 63.430 1.00 54.38 ? 749  GLU   B CA  1 
ATOM   2804 C C   . GLU   B 1 57  ? 31.788  -30.861 63.995 1.00 56.09 ? 749  GLU   B C   1 
ATOM   2805 O O   . GLU   B 1 57  ? 32.894  -31.214 64.418 1.00 56.68 ? 749  GLU   B O   1 
ATOM   2806 C CB  . GLU   B 1 57  ? 30.789  -33.142 64.325 1.00 57.62 ? 749  GLU   B CB  1 
ATOM   2807 C CG  . GLU   B 1 57  ? 30.237  -32.865 65.709 1.00 64.40 ? 749  GLU   B CG  1 
ATOM   2808 C CD  . GLU   B 1 57  ? 29.275  -33.924 66.209 1.00 73.38 ? 749  GLU   B CD  1 
ATOM   2809 O OE1 . GLU   B 1 57  ? 29.482  -35.118 65.886 1.00 74.91 ? 749  GLU   B OE1 1 
ATOM   2810 O OE2 . GLU   B 1 57  ? 28.312  -33.560 66.925 1.00 76.23 ? 749  GLU   B OE2 1 
ATOM   2811 N N   . ALA   B 1 58  ? 31.399  -29.573 63.945 1.00 56.66 ? 750  ALA   B N   1 
ATOM   2812 C CA  . ALA   B 1 58  ? 32.239  -28.464 64.401 1.00 57.64 ? 750  ALA   B CA  1 
ATOM   2813 C C   . ALA   B 1 58  ? 32.587  -28.525 65.899 1.00 58.51 ? 750  ALA   B C   1 
ATOM   2814 O O   . ALA   B 1 58  ? 31.837  -29.091 66.699 1.00 58.93 ? 750  ALA   B O   1 
ATOM   2815 C CB  . ALA   B 1 58  ? 31.573  -27.136 64.068 1.00 57.75 ? 750  ALA   B CB  1 
ATOM   2816 N N   . LYS   B 1 62  ? 26.894  -24.834 67.940 1.00 50.97 ? 754  LYS   B N   1 
ATOM   2817 C CA  . LYS   B 1 62  ? 26.651  -23.392 67.931 1.00 51.41 ? 754  LYS   B CA  1 
ATOM   2818 C C   . LYS   B 1 62  ? 25.167  -23.014 68.079 1.00 51.60 ? 754  LYS   B C   1 
ATOM   2819 O O   . LYS   B 1 62  ? 24.870  -21.850 68.352 1.00 52.27 ? 754  LYS   B O   1 
ATOM   2820 C CB  . LYS   B 1 62  ? 27.213  -22.747 66.649 1.00 53.02 ? 754  LYS   B CB  1 
ATOM   2821 C CG  . LYS   B 1 62  ? 28.703  -22.467 66.707 1.00 56.93 ? 754  LYS   B CG  1 
ATOM   2822 C CD  . LYS   B 1 62  ? 29.090  -21.296 65.816 1.00 60.73 ? 754  LYS   B CD  1 
ATOM   2823 C CE  . LYS   B 1 62  ? 30.463  -20.785 66.165 1.00 63.83 ? 754  LYS   B CE  1 
ATOM   2824 N NZ  . LYS   B 1 62  ? 30.756  -19.490 65.500 1.00 66.12 ? 754  LYS   B NZ  1 
ATOM   2825 N N   . ALA   B 1 63  ? 24.240  -23.981 67.896 1.00 50.63 ? 755  ALA   B N   1 
ATOM   2826 C CA  . ALA   B 1 63  ? 22.777  -23.802 67.905 1.00 50.24 ? 755  ALA   B CA  1 
ATOM   2827 C C   . ALA   B 1 63  ? 22.323  -23.091 66.628 1.00 49.70 ? 755  ALA   B C   1 
ATOM   2828 O O   . ALA   B 1 63  ? 23.031  -22.224 66.112 1.00 49.65 ? 755  ALA   B O   1 
ATOM   2829 C CB  . ALA   B 1 63  ? 22.283  -23.074 69.154 1.00 50.29 ? 755  ALA   B CB  1 
ATOM   2830 N N   . ASN   B 1 64  ? 21.164  -23.491 66.095 1.00 49.14 ? 756  ASN   B N   1 
ATOM   2831 C CA  . ASN   B 1 64  ? 20.627  -22.951 64.849 1.00 49.05 ? 756  ASN   B CA  1 
ATOM   2832 C C   . ASN   B 1 64  ? 20.530  -21.434 64.799 1.00 48.66 ? 756  ASN   B C   1 
ATOM   2833 O O   . ASN   B 1 64  ? 20.690  -20.861 63.721 1.00 49.06 ? 756  ASN   B O   1 
ATOM   2834 C CB  . ASN   B 1 64  ? 19.287  -23.577 64.516 1.00 50.16 ? 756  ASN   B CB  1 
ATOM   2835 C CG  . ASN   B 1 64  ? 19.428  -24.929 63.874 1.00 53.52 ? 756  ASN   B CG  1 
ATOM   2836 O OD1 . ASN   B 1 64  ? 20.440  -25.628 64.044 1.00 54.32 ? 756  ASN   B OD1 1 
ATOM   2837 N ND2 . ASN   B 1 64  ? 18.413  -25.323 63.113 1.00 54.47 ? 756  ASN   B ND2 1 
ATOM   2838 N N   . LYS   B 1 65  ? 20.298  -20.775 65.944 1.00 47.63 ? 757  LYS   B N   1 
ATOM   2839 C CA  . LYS   B 1 65  ? 20.204  -19.317 65.964 1.00 46.82 ? 757  LYS   B CA  1 
ATOM   2840 C C   . LYS   B 1 65  ? 21.512  -18.667 65.498 1.00 45.51 ? 757  LYS   B C   1 
ATOM   2841 O O   . LYS   B 1 65  ? 21.478  -17.831 64.599 1.00 45.59 ? 757  LYS   B O   1 
ATOM   2842 C CB  . LYS   B 1 65  ? 19.793  -18.804 67.354 1.00 48.38 ? 757  LYS   B CB  1 
ATOM   2843 C CG  . LYS   B 1 65  ? 19.136  -17.430 67.312 1.00 51.62 ? 757  LYS   B CG  1 
ATOM   2844 C CD  . LYS   B 1 65  ? 20.056  -16.346 67.833 1.00 55.39 ? 757  LYS   B CD  1 
ATOM   2845 C CE  . LYS   B 1 65  ? 19.577  -14.977 67.429 1.00 58.43 ? 757  LYS   B CE  1 
ATOM   2846 N NZ  . LYS   B 1 65  ? 20.629  -13.949 67.632 1.00 60.12 ? 757  LYS   B NZ  1 
ATOM   2847 N N   . GLU   B 1 66  ? 22.658  -19.101 66.057 1.00 44.01 ? 758  GLU   B N   1 
ATOM   2848 C CA  . GLU   B 1 66  ? 23.966  -18.544 65.712 1.00 42.97 ? 758  GLU   B CA  1 
ATOM   2849 C C   . GLU   B 1 66  ? 24.468  -18.905 64.308 1.00 40.56 ? 758  GLU   B C   1 
ATOM   2850 O O   . GLU   B 1 66  ? 25.086  -18.073 63.657 1.00 40.38 ? 758  GLU   B O   1 
ATOM   2851 C CB  . GLU   B 1 66  ? 25.019  -18.903 66.765 1.00 46.19 ? 758  GLU   B CB  1 
ATOM   2852 C CG  . GLU   B 1 66  ? 25.019  -17.962 67.955 1.00 53.57 ? 758  GLU   B CG  1 
ATOM   2853 C CD  . GLU   B 1 66  ? 24.003  -18.311 69.023 1.00 63.56 ? 758  GLU   B CD  1 
ATOM   2854 O OE1 . GLU   B 1 66  ? 24.137  -19.400 69.629 1.00 65.73 ? 758  GLU   B OE1 1 
ATOM   2855 O OE2 . GLU   B 1 66  ? 23.073  -17.503 69.254 1.00 66.79 ? 758  GLU   B OE2 1 
ATOM   2856 N N   . ILE   B 1 67  ? 24.196  -20.118 63.835 1.00 38.73 ? 759  ILE   B N   1 
ATOM   2857 C CA  . ILE   B 1 67  ? 24.592  -20.556 62.500 1.00 37.51 ? 759  ILE   B CA  1 
ATOM   2858 C C   . ILE   B 1 67  ? 23.940  -19.658 61.443 1.00 36.14 ? 759  ILE   B C   1 
ATOM   2859 O O   . ILE   B 1 67  ? 24.640  -19.087 60.607 1.00 35.92 ? 759  ILE   B O   1 
ATOM   2860 C CB  . ILE   B 1 67  ? 24.201  -22.046 62.286 1.00 37.80 ? 759  ILE   B CB  1 
ATOM   2861 C CG1 . ILE   B 1 67  ? 24.910  -22.954 63.313 1.00 38.69 ? 759  ILE   B CG1 1 
ATOM   2862 C CG2 . ILE   B 1 67  ? 24.480  -22.465 60.841 1.00 37.97 ? 759  ILE   B CG2 1 
ATOM   2863 C CD1 . ILE   B 1 67  ? 24.506  -24.374 63.290 1.00 39.92 ? 759  ILE   B CD1 1 
ATOM   2864 N N   . LEU   B 1 68  ? 22.610  -19.471 61.552 1.00 34.84 ? 760  LEU   B N   1 
ATOM   2865 C CA  . LEU   B 1 68  ? 21.821  -18.647 60.657 1.00 34.32 ? 760  LEU   B CA  1 
ATOM   2866 C C   . LEU   B 1 68  ? 22.315  -17.198 60.702 1.00 33.53 ? 760  LEU   B C   1 
ATOM   2867 O O   . LEU   B 1 68  ? 22.569  -16.618 59.649 1.00 33.74 ? 760  LEU   B O   1 
ATOM   2868 C CB  . LEU   B 1 68  ? 20.348  -18.740 61.067 1.00 34.83 ? 760  LEU   B CB  1 
ATOM   2869 C CG  . LEU   B 1 68  ? 19.328  -19.109 59.997 1.00 36.33 ? 760  LEU   B CG  1 
ATOM   2870 C CD1 . LEU   B 1 68  ? 19.736  -20.351 59.227 1.00 36.76 ? 760  LEU   B CD1 1 
ATOM   2871 C CD2 . LEU   B 1 68  ? 17.960  -19.308 60.614 1.00 36.98 ? 760  LEU   B CD2 1 
ATOM   2872 N N   . ASP   B 1 69  ? 22.593  -16.650 61.899 1.00 32.35 ? 761  ASP   B N   1 
ATOM   2873 C CA  . ASP   B 1 69  ? 23.132  -15.291 62.047 1.00 31.74 ? 761  ASP   B CA  1 
ATOM   2874 C C   . ASP   B 1 69  ? 24.366  -15.065 61.181 1.00 30.30 ? 761  ASP   B C   1 
ATOM   2875 O O   . ASP   B 1 69  ? 24.544  -13.968 60.638 1.00 30.03 ? 761  ASP   B O   1 
ATOM   2876 C CB  . ASP   B 1 69  ? 23.552  -15.042 63.497 1.00 34.34 ? 761  ASP   B CB  1 
ATOM   2877 C CG  . ASP   B 1 69  ? 22.419  -14.810 64.455 1.00 40.76 ? 761  ASP   B CG  1 
ATOM   2878 O OD1 . ASP   B 1 69  ? 21.455  -14.109 64.073 1.00 41.74 ? 761  ASP   B OD1 1 
ATOM   2879 O OD2 . ASP   B 1 69  ? 22.498  -15.320 65.598 1.00 43.63 ? 761  ASP   B OD2 1 
ATOM   2880 N N   . GLU   B 1 70  ? 25.217  -16.119 61.073 1.00 28.84 ? 762  GLU   B N   1 
ATOM   2881 C CA  . GLU   B 1 70  ? 26.474  -16.092 60.325 1.00 28.25 ? 762  GLU   B CA  1 
ATOM   2882 C C   . GLU   B 1 70  ? 26.245  -16.304 58.838 1.00 27.48 ? 762  GLU   B C   1 
ATOM   2883 O O   . GLU   B 1 70  ? 26.886  -15.651 58.013 1.00 27.48 ? 762  GLU   B O   1 
ATOM   2884 C CB  . GLU   B 1 70  ? 27.488  -17.120 60.887 1.00 30.16 ? 762  GLU   B CB  1 
ATOM   2885 C CG  . GLU   B 1 70  ? 27.927  -16.798 62.306 1.00 34.53 ? 762  GLU   B CG  1 
ATOM   2886 C CD  . GLU   B 1 70  ? 29.286  -17.309 62.749 1.00 40.46 ? 762  GLU   B CD  1 
ATOM   2887 O OE1 . GLU   B 1 70  ? 29.413  -17.677 63.939 1.00 41.45 ? 762  GLU   B OE1 1 
ATOM   2888 O OE2 . GLU   B 1 70  ? 30.229  -17.312 61.924 1.00 44.14 ? 762  GLU   B OE2 1 
ATOM   2889 N N   . ALA   B 1 71  ? 25.311  -17.207 58.496 1.00 26.64 ? 763  ALA   B N   1 
ATOM   2890 C CA  . ALA   B 1 71  ? 24.940  -17.489 57.116 1.00 25.99 ? 763  ALA   B CA  1 
ATOM   2891 C C   . ALA   B 1 71  ? 24.229  -16.293 56.459 1.00 25.54 ? 763  ALA   B C   1 
ATOM   2892 O O   . ALA   B 1 71  ? 24.327  -16.153 55.247 1.00 25.79 ? 763  ALA   B O   1 
ATOM   2893 C CB  . ALA   B 1 71  ? 24.091  -18.743 57.036 1.00 25.63 ? 763  ALA   B CB  1 
ATOM   2894 N N   . TYR   B 1 72  ? 23.581  -15.406 57.234 1.00 25.02 ? 764  TYR   B N   1 
ATOM   2895 C CA  . TYR   B 1 72  ? 22.969  -14.189 56.649 1.00 25.72 ? 764  TYR   B CA  1 
ATOM   2896 C C   . TYR   B 1 72  ? 24.096  -13.222 56.179 1.00 24.75 ? 764  TYR   B C   1 
ATOM   2897 O O   . TYR   B 1 72  ? 23.956  -12.524 55.174 1.00 24.43 ? 764  TYR   B O   1 
ATOM   2898 C CB  . TYR   B 1 72  ? 22.068  -13.429 57.663 1.00 26.72 ? 764  TYR   B CB  1 
ATOM   2899 C CG  . TYR   B 1 72  ? 20.809  -14.146 58.104 1.00 28.32 ? 764  TYR   B CG  1 
ATOM   2900 C CD1 . TYR   B 1 72  ? 20.011  -14.819 57.190 1.00 30.05 ? 764  TYR   B CD1 1 
ATOM   2901 C CD2 . TYR   B 1 72  ? 20.415  -14.143 59.434 1.00 29.93 ? 764  TYR   B CD2 1 
ATOM   2902 C CE1 . TYR   B 1 72  ? 18.878  -15.517 57.595 1.00 31.68 ? 764  TYR   B CE1 1 
ATOM   2903 C CE2 . TYR   B 1 72  ? 19.285  -14.840 59.854 1.00 31.58 ? 764  TYR   B CE2 1 
ATOM   2904 C CZ  . TYR   B 1 72  ? 18.522  -15.532 58.932 1.00 33.51 ? 764  TYR   B CZ  1 
ATOM   2905 O OH  . TYR   B 1 72  ? 17.375  -16.181 59.334 1.00 37.01 ? 764  TYR   B OH  1 
ATOM   2906 N N   . VAL   B 1 73  ? 25.192  -13.165 56.936 1.00 23.76 ? 765  VAL   B N   1 
ATOM   2907 C CA  . VAL   B 1 73  ? 26.316  -12.320 56.605 1.00 23.69 ? 765  VAL   B CA  1 
ATOM   2908 C C   . VAL   B 1 73  ? 27.008  -12.862 55.330 1.00 23.48 ? 765  VAL   B C   1 
ATOM   2909 O O   . VAL   B 1 73  ? 27.300  -12.087 54.417 1.00 23.43 ? 765  VAL   B O   1 
ATOM   2910 C CB  . VAL   B 1 73  ? 27.273  -12.243 57.809 1.00 24.40 ? 765  VAL   B CB  1 
ATOM   2911 C CG1 . VAL   B 1 73  ? 28.547  -11.477 57.447 1.00 25.14 ? 765  VAL   B CG1 1 
ATOM   2912 C CG2 . VAL   B 1 73  ? 26.573  -11.616 59.008 1.00 24.47 ? 765  VAL   B CG2 1 
ATOM   2913 N N   . MET   B 1 74  ? 27.192  -14.198 55.255 1.00 22.58 ? 766  MET   B N   1 
ATOM   2914 C CA  . MET   B 1 74  ? 27.784  -14.919 54.130 1.00 21.96 ? 766  MET   B CA  1 
ATOM   2915 C C   . MET   B 1 74  ? 26.931  -14.803 52.872 1.00 21.26 ? 766  MET   B C   1 
ATOM   2916 O O   . MET   B 1 74  ? 27.466  -14.746 51.767 1.00 21.12 ? 766  MET   B O   1 
ATOM   2917 C CB  . MET   B 1 74  ? 27.953  -16.387 54.517 1.00 22.43 ? 766  MET   B CB  1 
ATOM   2918 C CG  . MET   B 1 74  ? 29.010  -16.577 55.587 1.00 24.35 ? 766  MET   B CG  1 
ATOM   2919 S SD  . MET   B 1 74  ? 28.792  -18.092 56.540 1.00 30.54 ? 766  MET   B SD  1 
ATOM   2920 C CE  . MET   B 1 74  ? 28.950  -19.321 55.252 1.00 21.53 ? 766  MET   B CE  1 
ATOM   2921 N N   . ALA   B 1 75  ? 25.605  -14.772 53.036 1.00 20.67 ? 767  ALA   B N   1 
ATOM   2922 C CA  . ALA   B 1 75  ? 24.689  -14.604 51.918 1.00 20.42 ? 767  ALA   B CA  1 
ATOM   2923 C C   . ALA   B 1 75  ? 24.617  -13.148 51.450 1.00 20.04 ? 767  ALA   B C   1 
ATOM   2924 O O   . ALA   B 1 75  ? 24.050  -12.905 50.388 1.00 20.84 ? 767  ALA   B O   1 
ATOM   2925 C CB  . ALA   B 1 75  ? 23.295  -15.097 52.291 1.00 20.57 ? 767  ALA   B CB  1 
ATOM   2926 N N   . SER   B 1 76  ? 25.134  -12.179 52.227 1.00 18.80 ? 768  SER   B N   1 
ATOM   2927 C CA  . SER   B 1 76  ? 25.112  -10.767 51.837 1.00 18.75 ? 768  SER   B CA  1 
ATOM   2928 C C   . SER   B 1 76  ? 26.307  -10.325 50.984 1.00 18.99 ? 768  SER   B C   1 
ATOM   2929 O O   . SER   B 1 76  ? 26.307  -9.164  50.562 1.00 19.85 ? 768  SER   B O   1 
ATOM   2930 C CB  . SER   B 1 76  ? 25.032  -9.859  53.054 1.00 19.10 ? 768  SER   B CB  1 
ATOM   2931 O OG  . SER   B 1 76  ? 26.243  -9.927  53.785 1.00 21.62 ? 768  SER   B OG  1 
ATOM   2932 N N   . VAL   B 1 77  ? 27.315  -11.185 50.753 1.00 18.08 ? 769  VAL   B N   1 
ATOM   2933 C CA  . VAL   B 1 77  ? 28.458  -10.756 49.945 1.00 18.90 ? 769  VAL   B CA  1 
ATOM   2934 C C   . VAL   B 1 77  ? 28.075  -10.652 48.478 1.00 19.44 ? 769  VAL   B C   1 
ATOM   2935 O O   . VAL   B 1 77  ? 27.832  -11.658 47.807 1.00 19.57 ? 769  VAL   B O   1 
ATOM   2936 C CB  . VAL   B 1 77  ? 29.757  -11.551 50.148 1.00 19.91 ? 769  VAL   B CB  1 
ATOM   2937 C CG1 . VAL   B 1 77  ? 30.101  -11.685 51.628 1.00 20.53 ? 769  VAL   B CG1 1 
ATOM   2938 C CG2 . VAL   B 1 77  ? 29.667  -12.904 49.487 1.00 20.71 ? 769  VAL   B CG2 1 
ATOM   2939 N N   . ASP   B 1 78  ? 27.999  -9.415  47.984 1.00 19.15 ? 770  ASP   B N   1 
ATOM   2940 C CA  . ASP   B 1 78  ? 27.623  -9.179  46.606 1.00 19.28 ? 770  ASP   B CA  1 
ATOM   2941 C C   . ASP   B 1 78  ? 28.766  -8.533  45.847 1.00 18.32 ? 770  ASP   B C   1 
ATOM   2942 O O   . ASP   B 1 78  ? 28.884  -7.304  45.814 1.00 18.91 ? 770  ASP   B O   1 
ATOM   2943 C CB  . ASP   B 1 78  ? 26.367  -8.313  46.554 1.00 21.22 ? 770  ASP   B CB  1 
ATOM   2944 C CG  . ASP   B 1 78  ? 25.753  -8.108  45.177 1.00 25.95 ? 770  ASP   B CG  1 
ATOM   2945 O OD1 . ASP   B 1 78  ? 26.100  -8.880  44.240 1.00 25.10 ? 770  ASP   B OD1 1 
ATOM   2946 O OD2 . ASP   B 1 78  ? 24.916  -7.182  45.037 1.00 29.43 ? 770  ASP   B OD2 1 
ATOM   2947 N N   . ASN   B 1 79  ? 29.600  -9.363  45.223 1.00 16.35 ? 771  ASN   B N   1 
ATOM   2948 C CA  . ASN   B 1 79  ? 30.729  -8.869  44.440 1.00 14.65 ? 771  ASN   B CA  1 
ATOM   2949 C C   . ASN   B 1 79  ? 31.039  -9.878  43.285 1.00 14.21 ? 771  ASN   B C   1 
ATOM   2950 O O   . ASN   B 1 79  ? 30.903  -11.082 43.476 1.00 13.90 ? 771  ASN   B O   1 
ATOM   2951 C CB  . ASN   B 1 79  ? 31.935  -8.648  45.372 1.00 13.62 ? 771  ASN   B CB  1 
ATOM   2952 C CG  . ASN   B 1 79  ? 33.127  -8.080  44.663 1.00 12.83 ? 771  ASN   B CG  1 
ATOM   2953 O OD1 . ASN   B 1 79  ? 33.983  -8.810  44.168 1.00 11.10 ? 771  ASN   B OD1 1 
ATOM   2954 N ND2 . ASN   B 1 79  ? 33.179  -6.757  44.545 1.00 13.87 ? 771  ASN   B ND2 1 
ATOM   2955 N N   . PRO   B 1 80  ? 31.431  -9.428  42.080 1.00 14.39 ? 772  PRO   B N   1 
ATOM   2956 C CA  . PRO   B 1 80  ? 31.693  -10.399 40.992 1.00 14.03 ? 772  PRO   B CA  1 
ATOM   2957 C C   . PRO   B 1 80  ? 32.831  -11.378 41.294 1.00 12.96 ? 772  PRO   B C   1 
ATOM   2958 O O   . PRO   B 1 80  ? 32.886  -12.456 40.719 1.00 12.13 ? 772  PRO   B O   1 
ATOM   2959 C CB  . PRO   B 1 80  ? 31.981  -9.514  39.773 1.00 14.76 ? 772  PRO   B CB  1 
ATOM   2960 C CG  . PRO   B 1 80  ? 31.414  -8.153  40.118 1.00 15.23 ? 772  PRO   B CG  1 
ATOM   2961 C CD  . PRO   B 1 80  ? 31.616  -8.037  41.614 1.00 13.94 ? 772  PRO   B CD  1 
ATOM   2962 N N   . HIS   B 1 81  ? 33.697  -11.035 42.252 1.00 12.65 ? 773  HIS   B N   1 
ATOM   2963 C CA  . HIS   B 1 81  ? 34.849  -11.840 42.613 1.00 11.12 ? 773  HIS   B CA  1 
ATOM   2964 C C   . HIS   B 1 81  ? 34.743  -12.456 43.988 1.00 10.48 ? 773  HIS   B C   1 
ATOM   2965 O O   . HIS   B 1 81  ? 35.760  -12.803 44.555 1.00 9.80  ? 773  HIS   B O   1 
ATOM   2966 C CB  . HIS   B 1 81  ? 36.125  -11.017 42.434 1.00 11.09 ? 773  HIS   B CB  1 
ATOM   2967 C CG  . HIS   B 1 81  ? 36.232  -10.555 41.022 1.00 13.48 ? 773  HIS   B CG  1 
ATOM   2968 N ND1 . HIS   B 1 81  ? 36.063  -9.223  40.686 1.00 16.02 ? 773  HIS   B ND1 1 
ATOM   2969 C CD2 . HIS   B 1 81  ? 36.254  -11.290 39.886 1.00 14.24 ? 773  HIS   B CD2 1 
ATOM   2970 C CE1 . HIS   B 1 81  ? 36.077  -9.185  39.361 1.00 16.47 ? 773  HIS   B CE1 1 
ATOM   2971 N NE2 . HIS   B 1 81  ? 36.176  -10.410 38.838 1.00 15.79 ? 773  HIS   B NE2 1 
ATOM   2972 N N   . VAL   B 1 82  ? 33.517  -12.642 44.508 1.00 10.91 ? 774  VAL   B N   1 
ATOM   2973 C CA  . VAL   B 1 82  ? 33.246  -13.328 45.769 1.00 11.89 ? 774  VAL   B CA  1 
ATOM   2974 C C   . VAL   B 1 82  ? 32.006  -14.249 45.650 1.00 12.36 ? 774  VAL   B C   1 
ATOM   2975 O O   . VAL   B 1 82  ? 30.923  -13.801 45.250 1.00 11.79 ? 774  VAL   B O   1 
ATOM   2976 C CB  . VAL   B 1 82  ? 33.146  -12.408 47.013 1.00 13.92 ? 774  VAL   B CB  1 
ATOM   2977 C CG1 . VAL   B 1 82  ? 32.981  -13.251 48.275 1.00 14.86 ? 774  VAL   B CG1 1 
ATOM   2978 C CG2 . VAL   B 1 82  ? 34.383  -11.507 47.163 1.00 14.09 ? 774  VAL   B CG2 1 
ATOM   2979 N N   . CYS   B 1 83  ? 32.181  -15.555 45.936 1.00 12.52 ? 775  CYS   B N   1 
ATOM   2980 C CA  . CYS   B 1 83  ? 31.049  -16.483 45.939 1.00 12.64 ? 775  CYS   B CA  1 
ATOM   2981 C C   . CYS   B 1 83  ? 30.063  -16.144 47.060 1.00 12.58 ? 775  CYS   B C   1 
ATOM   2982 O O   . CYS   B 1 83  ? 30.446  -16.105 48.238 1.00 11.84 ? 775  CYS   B O   1 
ATOM   2983 C CB  . CYS   B 1 83  ? 31.544  -17.912 46.092 1.00 13.42 ? 775  CYS   B CB  1 
ATOM   2984 S SG  . CYS   B 1 83  ? 32.556  -18.476 44.723 1.00 17.65 ? 775  CYS   B SG  1 
ATOM   2985 N N   . ARG   B 1 84  ? 28.786  -15.976 46.695 1.00 12.94 ? 776  ARG   B N   1 
ATOM   2986 C CA  . ARG   B 1 84  ? 27.706  -15.675 47.636 1.00 13.36 ? 776  ARG   B CA  1 
ATOM   2987 C C   . ARG   B 1 84  ? 27.052  -16.982 48.087 1.00 14.64 ? 776  ARG   B C   1 
ATOM   2988 O O   . ARG   B 1 84  ? 26.800  -17.867 47.262 1.00 14.69 ? 776  ARG   B O   1 
ATOM   2989 C CB  . ARG   B 1 84  ? 26.652  -14.800 46.936 1.00 13.46 ? 776  ARG   B CB  1 
ATOM   2990 C CG  . ARG   B 1 84  ? 25.642  -14.154 47.874 1.00 15.26 ? 776  ARG   B CG  1 
ATOM   2991 C CD  . ARG   B 1 84  ? 24.726  -13.132 47.197 1.00 14.68 ? 776  ARG   B CD  1 
ATOM   2992 N NE  . ARG   B 1 84  ? 23.596  -13.746 46.480 1.00 16.42 ? 776  ARG   B NE  1 
ATOM   2993 C CZ  . ARG   B 1 84  ? 22.506  -14.244 47.072 1.00 18.30 ? 776  ARG   B CZ  1 
ATOM   2994 N NH1 . ARG   B 1 84  ? 22.390  -14.222 48.398 1.00 17.09 ? 776  ARG   B NH1 1 
ATOM   2995 N NH2 . ARG   B 1 84  ? 21.522  -14.766 46.340 1.00 16.72 ? 776  ARG   B NH2 1 
ATOM   2996 N N   . LEU   B 1 85  ? 26.764  -17.099 49.390 1.00 15.02 ? 777  LEU   B N   1 
ATOM   2997 C CA  . LEU   B 1 85  ? 26.047  -18.256 49.893 1.00 15.98 ? 777  LEU   B CA  1 
ATOM   2998 C C   . LEU   B 1 85  ? 24.585  -18.054 49.471 1.00 17.52 ? 777  LEU   B C   1 
ATOM   2999 O O   . LEU   B 1 85  ? 24.049  -16.959 49.624 1.00 18.49 ? 777  LEU   B O   1 
ATOM   3000 C CB  . LEU   B 1 85  ? 26.139  -18.325 51.418 1.00 16.26 ? 777  LEU   B CB  1 
ATOM   3001 C CG  . LEU   B 1 85  ? 25.356  -19.479 52.048 1.00 17.70 ? 777  LEU   B CG  1 
ATOM   3002 C CD1 . LEU   B 1 85  ? 25.876  -20.812 51.560 1.00 18.25 ? 777  LEU   B CD1 1 
ATOM   3003 C CD2 . LEU   B 1 85  ? 25.373  -19.395 53.573 1.00 18.36 ? 777  LEU   B CD2 1 
ATOM   3004 N N   . LEU   B 1 86  ? 23.968  -19.068 48.883 1.00 17.55 ? 778  LEU   B N   1 
ATOM   3005 C CA  . LEU   B 1 86  ? 22.609  -18.960 48.381 1.00 18.43 ? 778  LEU   B CA  1 
ATOM   3006 C C   . LEU   B 1 86  ? 21.602  -19.654 49.305 1.00 19.71 ? 778  LEU   B C   1 
ATOM   3007 O O   . LEU   B 1 86  ? 20.589  -19.054 49.682 1.00 19.02 ? 778  LEU   B O   1 
ATOM   3008 C CB  . LEU   B 1 86  ? 22.558  -19.559 46.961 1.00 18.42 ? 778  LEU   B CB  1 
ATOM   3009 C CG  . LEU   B 1 86  ? 22.831  -18.663 45.738 1.00 19.63 ? 778  LEU   B CG  1 
ATOM   3010 C CD1 . LEU   B 1 86  ? 23.791  -17.520 46.003 1.00 19.32 ? 778  LEU   B CD1 1 
ATOM   3011 C CD2 . LEU   B 1 86  ? 23.331  -19.479 44.597 1.00 20.78 ? 778  LEU   B CD2 1 
ATOM   3012 N N   . GLY   B 1 87  ? 21.894  -20.901 49.675 1.00 20.86 ? 779  GLY   B N   1 
ATOM   3013 C CA  . GLY   B 1 87  ? 20.993  -21.656 50.528 1.00 22.43 ? 779  GLY   B CA  1 
ATOM   3014 C C   . GLY   B 1 87  ? 21.641  -22.319 51.721 1.00 23.66 ? 779  GLY   B C   1 
ATOM   3015 O O   . GLY   B 1 87  ? 22.855  -22.457 51.778 1.00 23.26 ? 779  GLY   B O   1 
ATOM   3016 N N   . ILE   B 1 88  ? 20.815  -22.729 52.680 1.00 24.88 ? 780  ILE   B N   1 
ATOM   3017 C CA  . ILE   B 1 88  ? 21.233  -23.438 53.872 1.00 26.50 ? 780  ILE   B CA  1 
ATOM   3018 C C   . ILE   B 1 88  ? 20.147  -24.423 54.326 1.00 28.47 ? 780  ILE   B C   1 
ATOM   3019 O O   . ILE   B 1 88  ? 18.953  -24.114 54.299 1.00 28.43 ? 780  ILE   B O   1 
ATOM   3020 C CB  . ILE   B 1 88  ? 21.597  -22.466 54.996 1.00 27.39 ? 780  ILE   B CB  1 
ATOM   3021 C CG1 . ILE   B 1 88  ? 22.335  -23.198 56.135 1.00 28.83 ? 780  ILE   B CG1 1 
ATOM   3022 C CG2 . ILE   B 1 88  ? 20.369  -21.750 55.501 1.00 27.71 ? 780  ILE   B CG2 1 
ATOM   3023 C CD1 . ILE   B 1 88  ? 23.187  -22.335 57.000 1.00 29.94 ? 780  ILE   B CD1 1 
ATOM   3024 N N   . CYS   B 1 89  ? 20.561  -25.624 54.701 1.00 29.65 ? 781  CYS   B N   1 
ATOM   3025 C CA  . CYS   B 1 89  ? 19.657  -26.626 55.225 1.00 31.06 ? 781  CYS   B CA  1 
ATOM   3026 C C   . CYS   B 1 89  ? 20.247  -27.101 56.538 1.00 31.78 ? 781  CYS   B C   1 
ATOM   3027 O O   . CYS   B 1 89  ? 21.327  -27.699 56.531 1.00 31.65 ? 781  CYS   B O   1 
ATOM   3028 C CB  . CYS   B 1 89  ? 19.493  -27.778 54.247 1.00 33.07 ? 781  CYS   B CB  1 
ATOM   3029 S SG  . CYS   B 1 89  ? 18.397  -29.096 54.841 1.00 40.39 ? 781  CYS   B SG  1 
ATOM   3030 N N   . LEU   B 1 90  ? 19.561  -26.823 57.662 1.00 32.29 ? 782  LEU   B N   1 
ATOM   3031 C CA  . LEU   B 1 90  ? 20.025  -27.230 58.989 1.00 33.49 ? 782  LEU   B CA  1 
ATOM   3032 C C   . LEU   B 1 90  ? 19.251  -28.420 59.534 1.00 34.45 ? 782  LEU   B C   1 
ATOM   3033 O O   . LEU   B 1 90  ? 18.055  -28.325 59.781 1.00 34.61 ? 782  LEU   B O   1 
ATOM   3034 C CB  . LEU   B 1 90  ? 19.929  -26.070 59.967 1.00 33.94 ? 782  LEU   B CB  1 
ATOM   3035 C CG  . LEU   B 1 90  ? 20.697  -24.826 59.563 1.00 36.00 ? 782  LEU   B CG  1 
ATOM   3036 C CD1 . LEU   B 1 90  ? 20.395  -23.675 60.499 1.00 36.53 ? 782  LEU   B CD1 1 
ATOM   3037 C CD2 . LEU   B 1 90  ? 22.189  -25.100 59.506 1.00 36.36 ? 782  LEU   B CD2 1 
ATOM   3038 N N   . THR   B 1 91  ? 19.929  -29.552 59.688 1.00 35.10 ? 783  THR   B N   1 
ATOM   3039 C CA  . THR   B 1 91  ? 19.363  -30.791 60.234 1.00 36.08 ? 783  THR   B CA  1 
ATOM   3040 C C   . THR   B 1 91  ? 20.373  -31.215 61.375 1.00 37.18 ? 783  THR   B C   1 
ATOM   3041 O O   . THR   B 1 91  ? 20.767  -30.356 62.173 1.00 37.48 ? 783  THR   B O   1 
ATOM   3042 C CB  . THR   B 1 91  ? 19.124  -31.806 59.066 1.00 37.06 ? 783  THR   B CB  1 
ATOM   3043 O OG1 . THR   B 1 91  ? 20.373  -32.381 58.708 1.00 38.00 ? 783  THR   B OG1 1 
ATOM   3044 C CG2 . THR   B 1 91  ? 18.467  -31.186 57.840 1.00 37.80 ? 783  THR   B CG2 1 
ATOM   3045 N N   . SER   B 1 92  ? 20.793  -32.495 61.459 1.00 37.39 ? 784  SER   B N   1 
ATOM   3046 C CA  . SER   B 1 92  ? 21.866  -32.945 62.330 1.00 37.98 ? 784  SER   B CA  1 
ATOM   3047 C C   . SER   B 1 92  ? 23.209  -32.375 61.764 1.00 37.84 ? 784  SER   B C   1 
ATOM   3048 O O   . SER   B 1 92  ? 24.149  -32.148 62.520 1.00 38.08 ? 784  SER   B O   1 
ATOM   3049 C CB  . SER   B 1 92  ? 21.927  -34.469 62.322 1.00 40.12 ? 784  SER   B CB  1 
ATOM   3050 O OG  . SER   B 1 92  ? 22.067  -34.953 60.995 1.00 43.19 ? 784  SER   B OG  1 
ATOM   3051 N N   . THR   B 1 93  ? 23.268  -32.124 60.431 1.00 37.30 ? 785  THR   B N   1 
ATOM   3052 C CA  . THR   B 1 93  ? 24.376  -31.568 59.664 1.00 37.08 ? 785  THR   B CA  1 
ATOM   3053 C C   . THR   B 1 93  ? 24.014  -30.131 59.181 1.00 36.57 ? 785  THR   B C   1 
ATOM   3054 O O   . THR   B 1 93  ? 22.840  -29.754 59.172 1.00 37.02 ? 785  THR   B O   1 
ATOM   3055 C CB  . THR   B 1 93  ? 24.602  -32.475 58.424 1.00 38.45 ? 785  THR   B CB  1 
ATOM   3056 O OG1 . THR   B 1 93  ? 23.537  -32.296 57.478 1.00 38.90 ? 785  THR   B OG1 1 
ATOM   3057 C CG2 . THR   B 1 93  ? 24.707  -33.968 58.779 1.00 39.30 ? 785  THR   B CG2 1 
ATOM   3058 N N   . VAL   B 1 94  ? 25.004  -29.372 58.704 1.00 35.07 ? 786  VAL   B N   1 
ATOM   3059 C CA  . VAL   B 1 94  ? 24.762  -28.065 58.116 1.00 33.95 ? 786  VAL   B CA  1 
ATOM   3060 C C   . VAL   B 1 94  ? 25.110  -28.199 56.643 1.00 32.77 ? 786  VAL   B C   1 
ATOM   3061 O O   . VAL   B 1 94  ? 26.265  -28.485 56.327 1.00 32.91 ? 786  VAL   B O   1 
ATOM   3062 C CB  . VAL   B 1 94  ? 25.632  -26.965 58.760 1.00 34.54 ? 786  VAL   B CB  1 
ATOM   3063 C CG1 . VAL   B 1 94  ? 25.509  -25.654 57.989 1.00 34.93 ? 786  VAL   B CG1 1 
ATOM   3064 C CG2 . VAL   B 1 94  ? 25.281  -26.777 60.236 1.00 34.80 ? 786  VAL   B CG2 1 
ATOM   3065 N N   . GLN   B 1 95  ? 24.139  -28.007 55.745 1.00 31.25 ? 787  GLN   B N   1 
ATOM   3066 C CA  . GLN   B 1 95  ? 24.418  -28.069 54.315 1.00 30.17 ? 787  GLN   B CA  1 
ATOM   3067 C C   . GLN   B 1 95  ? 24.309  -26.693 53.667 1.00 29.28 ? 787  GLN   B C   1 
ATOM   3068 O O   . GLN   B 1 95  ? 23.250  -26.066 53.710 1.00 29.56 ? 787  GLN   B O   1 
ATOM   3069 C CB  . GLN   B 1 95  ? 23.535  -29.096 53.607 1.00 30.88 ? 787  GLN   B CB  1 
ATOM   3070 C CG  . GLN   B 1 95  ? 24.085  -30.507 53.754 1.00 33.73 ? 787  GLN   B CG  1 
ATOM   3071 C CD  . GLN   B 1 95  ? 23.265  -31.505 52.986 1.00 36.96 ? 787  GLN   B CD  1 
ATOM   3072 O OE1 . GLN   B 1 95  ? 23.622  -31.928 51.887 1.00 38.65 ? 787  GLN   B OE1 1 
ATOM   3073 N NE2 . GLN   B 1 95  ? 22.139  -31.897 53.542 1.00 37.01 ? 787  GLN   B NE2 1 
ATOM   3074 N N   . LEU   B 1 96  ? 25.416  -26.221 53.074 1.00 27.86 ? 788  LEU   B N   1 
ATOM   3075 C CA  . LEU   B 1 96  ? 25.471  -24.932 52.399 1.00 27.35 ? 788  LEU   B CA  1 
ATOM   3076 C C   . LEU   B 1 96  ? 25.300  -25.105 50.895 1.00 26.62 ? 788  LEU   B C   1 
ATOM   3077 O O   . LEU   B 1 96  ? 25.841  -26.041 50.335 1.00 26.97 ? 788  LEU   B O   1 
ATOM   3078 C CB  . LEU   B 1 96  ? 26.802  -24.237 52.716 1.00 27.45 ? 788  LEU   B CB  1 
ATOM   3079 C CG  . LEU   B 1 96  ? 27.083  -24.005 54.208 1.00 29.01 ? 788  LEU   B CG  1 
ATOM   3080 C CD1 . LEU   B 1 96  ? 28.396  -23.275 54.400 1.00 29.29 ? 788  LEU   B CD1 1 
ATOM   3081 C CD2 . LEU   B 1 96  ? 25.974  -23.208 54.864 1.00 29.58 ? 788  LEU   B CD2 1 
ATOM   3082 N N   . ILE   B 1 97  ? 24.528  -24.232 50.237 1.00 25.42 ? 789  ILE   B N   1 
ATOM   3083 C CA  . ILE   B 1 97  ? 24.264  -24.364 48.803 1.00 24.58 ? 789  ILE   B CA  1 
ATOM   3084 C C   . ILE   B 1 97  ? 24.637  -23.083 48.094 1.00 23.42 ? 789  ILE   B C   1 
ATOM   3085 O O   . ILE   B 1 97  ? 24.329  -22.000 48.590 1.00 22.92 ? 789  ILE   B O   1 
ATOM   3086 C CB  . ILE   B 1 97  ? 22.789  -24.805 48.531 1.00 25.33 ? 789  ILE   B CB  1 
ATOM   3087 C CG1 . ILE   B 1 97  ? 22.543  -26.278 48.923 1.00 26.10 ? 789  ILE   B CG1 1 
ATOM   3088 C CG2 . ILE   B 1 97  ? 22.386  -24.583 47.089 1.00 26.26 ? 789  ILE   B CG2 1 
ATOM   3089 C CD1 . ILE   B 1 97  ? 22.124  -26.524 50.394 1.00 27.18 ? 789  ILE   B CD1 1 
ATOM   3090 N N   . THR   B 1 98  ? 25.361  -23.211 46.963 1.00 22.59 ? 790  THR   B N   1 
ATOM   3091 C CA  . THR   B 1 98  ? 25.833  -22.104 46.132 1.00 22.46 ? 790  THR   B CA  1 
ATOM   3092 C C   . THR   B 1 98  ? 25.762  -22.483 44.632 1.00 21.73 ? 790  THR   B C   1 
ATOM   3093 O O   . THR   B 1 98  ? 25.529  -23.642 44.292 1.00 21.86 ? 790  THR   B O   1 
ATOM   3094 C CB  . THR   B 1 98  ? 27.303  -21.740 46.515 1.00 24.27 ? 790  THR   B CB  1 
ATOM   3095 O OG1 . THR   B 1 98  ? 28.094  -22.912 46.360 1.00 25.78 ? 790  THR   B OG1 1 
ATOM   3096 C CG2 . THR   B 1 98  ? 27.446  -21.229 47.921 1.00 25.02 ? 790  THR   B CG2 1 
ATOM   3097 N N   . GLN   B 1 99  ? 25.987  -21.514 43.728 1.00 21.51 ? 791  GLN   B N   1 
ATOM   3098 C CA  . GLN   B 1 99  ? 25.991  -21.780 42.292 1.00 21.91 ? 791  GLN   B CA  1 
ATOM   3099 C C   . GLN   B 1 99  ? 27.128  -22.750 41.948 1.00 22.24 ? 791  GLN   B C   1 
ATOM   3100 O O   . GLN   B 1 99  ? 28.249  -22.600 42.446 1.00 22.34 ? 791  GLN   B O   1 
ATOM   3101 C CB  . GLN   B 1 99  ? 26.145  -20.473 41.499 1.00 23.16 ? 791  GLN   B CB  1 
ATOM   3102 C CG  . GLN   B 1 99  ? 25.947  -20.661 40.003 1.00 26.07 ? 791  GLN   B CG  1 
ATOM   3103 C CD  . GLN   B 1 99  ? 26.286  -19.417 39.247 1.00 29.21 ? 791  GLN   B CD  1 
ATOM   3104 O OE1 . GLN   B 1 99  ? 27.287  -18.742 39.526 1.00 30.32 ? 791  GLN   B OE1 1 
ATOM   3105 N NE2 . GLN   B 1 99  ? 25.454  -19.074 38.281 1.00 28.60 ? 791  GLN   B NE2 1 
ATOM   3106 N N   . LEU   B 1 100 ? 26.820  -23.768 41.142 1.00 22.22 ? 792  LEU   B N   1 
ATOM   3107 C CA  . LEU   B 1 100 ? 27.792  -24.777 40.751 1.00 22.70 ? 792  LEU   B CA  1 
ATOM   3108 C C   . LEU   B 1 100 ? 28.829  -24.189 39.798 1.00 23.41 ? 792  LEU   B C   1 
ATOM   3109 O O   . LEU   B 1 100 ? 28.466  -23.525 38.823 1.00 23.20 ? 792  LEU   B O   1 
ATOM   3110 C CB  . LEU   B 1 100 ? 27.072  -25.970 40.087 1.00 22.38 ? 792  LEU   B CB  1 
ATOM   3111 C CG  . LEU   B 1 100 ? 27.958  -27.136 39.633 1.00 22.82 ? 792  LEU   B CG  1 
ATOM   3112 C CD1 . LEU   B 1 100 ? 28.625  -27.769 40.819 1.00 23.19 ? 792  LEU   B CD1 1 
ATOM   3113 C CD2 . LEU   B 1 100 ? 27.127  -28.211 38.917 1.00 23.22 ? 792  LEU   B CD2 1 
ATOM   3114 N N   . MET   B 1 101 ? 30.120  -24.409 40.103 1.00 23.98 ? 793  MET   B N   1 
ATOM   3115 C CA  . MET   B 1 101 ? 31.245  -23.963 39.281 1.00 25.26 ? 793  MET   B CA  1 
ATOM   3116 C C   . MET   B 1 101 ? 32.019  -25.203 38.800 1.00 25.92 ? 793  MET   B C   1 
ATOM   3117 O O   . MET   B 1 101 ? 32.853  -25.755 39.537 1.00 26.19 ? 793  MET   B O   1 
ATOM   3118 C CB  . MET   B 1 101 ? 32.139  -22.961 40.031 1.00 26.19 ? 793  MET   B CB  1 
ATOM   3119 C CG  . MET   B 1 101 ? 31.378  -21.699 40.402 1.00 29.85 ? 793  MET   B CG  1 
ATOM   3120 S SD  . MET   B 1 101 ? 32.324  -20.204 40.812 1.00 40.91 ? 793  MET   B SD  1 
ATOM   3121 C CE  . MET   B 1 101 ? 30.953  -19.008 40.813 1.00 44.65 ? 793  MET   B CE  1 
ATOM   3122 N N   . PRO   B 1 102 ? 31.682  -25.684 37.579 1.00 25.32 ? 794  PRO   B N   1 
ATOM   3123 C CA  . PRO   B 1 102 ? 32.279  -26.929 37.080 1.00 25.06 ? 794  PRO   B CA  1 
ATOM   3124 C C   . PRO   B 1 102 ? 33.790  -26.924 36.860 1.00 24.62 ? 794  PRO   B C   1 
ATOM   3125 O O   . PRO   B 1 102 ? 34.391  -27.996 36.837 1.00 25.21 ? 794  PRO   B O   1 
ATOM   3126 C CB  . PRO   B 1 102 ? 31.520  -27.188 35.771 1.00 26.17 ? 794  PRO   B CB  1 
ATOM   3127 C CG  . PRO   B 1 102 ? 30.985  -25.857 35.339 1.00 26.45 ? 794  PRO   B CG  1 
ATOM   3128 C CD  . PRO   B 1 102 ? 30.664  -25.162 36.645 1.00 25.05 ? 794  PRO   B CD  1 
ATOM   3129 N N   . PHE   B 1 103 ? 34.409  -25.748 36.709 1.00 23.47 ? 795  PHE   B N   1 
ATOM   3130 C CA  . PHE   B 1 103 ? 35.852  -25.668 36.515 1.00 22.55 ? 795  PHE   B CA  1 
ATOM   3131 C C   . PHE   B 1 103 ? 36.677  -25.958 37.765 1.00 22.27 ? 795  PHE   B C   1 
ATOM   3132 O O   . PHE   B 1 103 ? 37.874  -26.194 37.652 1.00 22.49 ? 795  PHE   B O   1 
ATOM   3133 C CB  . PHE   B 1 103 ? 36.238  -24.306 35.992 1.00 22.56 ? 795  PHE   B CB  1 
ATOM   3134 C CG  . PHE   B 1 103 ? 36.252  -24.153 34.494 1.00 23.18 ? 795  PHE   B CG  1 
ATOM   3135 C CD1 . PHE   B 1 103 ? 37.319  -24.615 33.747 1.00 23.93 ? 795  PHE   B CD1 1 
ATOM   3136 C CD2 . PHE   B 1 103 ? 35.244  -23.456 33.844 1.00 23.93 ? 795  PHE   B CD2 1 
ATOM   3137 C CE1 . PHE   B 1 103 ? 37.358  -24.421 32.373 1.00 24.82 ? 795  PHE   B CE1 1 
ATOM   3138 C CE2 . PHE   B 1 103 ? 35.288  -23.257 32.475 1.00 24.44 ? 795  PHE   B CE2 1 
ATOM   3139 C CZ  . PHE   B 1 103 ? 36.345  -23.735 31.748 1.00 24.53 ? 795  PHE   B CZ  1 
ATOM   3140 N N   . GLY   B 1 104 ? 36.060  -25.894 38.938 1.00 21.63 ? 796  GLY   B N   1 
ATOM   3141 C CA  . GLY   B 1 104 ? 36.731  -26.179 40.191 1.00 21.41 ? 796  GLY   B CA  1 
ATOM   3142 C C   . GLY   B 1 104 ? 37.555  -25.035 40.733 1.00 21.32 ? 796  GLY   B C   1 
ATOM   3143 O O   . GLY   B 1 104 ? 37.364  -23.880 40.345 1.00 20.44 ? 796  GLY   B O   1 
ATOM   3144 N N   . CYS   B 1 105 ? 38.493  -25.361 41.640 1.00 21.80 ? 797  CYS   B N   1 
ATOM   3145 C CA  . CYS   B 1 105 ? 39.369  -24.363 42.234 1.00 22.32 ? 797  CYS   B CA  1 
ATOM   3146 C C   . CYS   B 1 105 ? 40.561  -24.044 41.336 1.00 22.71 ? 797  CYS   B C   1 
ATOM   3147 O O   . CYS   B 1 105 ? 41.037  -24.879 40.550 1.00 22.97 ? 797  CYS   B O   1 
ATOM   3148 C CB  . CYS   B 1 105 ? 39.817  -24.776 43.634 1.00 23.59 ? 797  CYS   B CB  1 
ATOM   3149 S SG  . CYS   B 1 105 ? 40.851  -26.268 43.680 1.00 27.23 ? 797  CYS   B SG  1 
ATOM   3150 N N   . LEU   B 1 106 ? 41.030  -22.810 41.462 1.00 21.98 ? 798  LEU   B N   1 
ATOM   3151 C CA  . LEU   B 1 106 ? 42.154  -22.278 40.738 1.00 21.80 ? 798  LEU   B CA  1 
ATOM   3152 C C   . LEU   B 1 106 ? 43.430  -23.053 41.049 1.00 22.18 ? 798  LEU   B C   1 
ATOM   3153 O O   . LEU   B 1 106 ? 44.267  -23.166 40.155 1.00 23.18 ? 798  LEU   B O   1 
ATOM   3154 C CB  . LEU   B 1 106 ? 42.304  -20.779 41.067 1.00 21.70 ? 798  LEU   B CB  1 
ATOM   3155 C CG  . LEU   B 1 106 ? 43.214  -19.948 40.178 1.00 22.00 ? 798  LEU   B CG  1 
ATOM   3156 C CD1 . LEU   B 1 106 ? 42.856  -20.084 38.716 1.00 21.70 ? 798  LEU   B CD1 1 
ATOM   3157 C CD2 . LEU   B 1 106 ? 43.180  -18.514 40.601 1.00 22.81 ? 798  LEU   B CD2 1 
ATOM   3158 N N   . LEU   B 1 107 ? 43.564  -23.638 42.259 1.00 21.33 ? 799  LEU   B N   1 
ATOM   3159 C CA  . LEU   B 1 107 ? 44.728  -24.463 42.605 1.00 22.32 ? 799  LEU   B CA  1 
ATOM   3160 C C   . LEU   B 1 107 ? 44.884  -25.645 41.638 1.00 22.81 ? 799  LEU   B C   1 
ATOM   3161 O O   . LEU   B 1 107 ? 45.962  -25.829 41.074 1.00 22.72 ? 799  LEU   B O   1 
ATOM   3162 C CB  . LEU   B 1 107 ? 44.647  -24.973 44.066 1.00 22.74 ? 799  LEU   B CB  1 
ATOM   3163 C CG  . LEU   B 1 107 ? 45.814  -25.841 44.542 1.00 24.13 ? 799  LEU   B CG  1 
ATOM   3164 C CD1 . LEU   B 1 107 ? 47.137  -25.078 44.488 1.00 24.69 ? 799  LEU   B CD1 1 
ATOM   3165 C CD2 . LEU   B 1 107 ? 45.560  -26.364 45.949 1.00 24.38 ? 799  LEU   B CD2 1 
ATOM   3166 N N   . ASP   B 1 108 ? 43.813  -26.442 41.444 1.00 22.71 ? 800  ASP   B N   1 
ATOM   3167 C CA  . ASP   B 1 108 ? 43.878  -27.567 40.525 1.00 23.19 ? 800  ASP   B CA  1 
ATOM   3168 C C   . ASP   B 1 108 ? 43.924  -27.113 39.076 1.00 24.54 ? 800  ASP   B C   1 
ATOM   3169 O O   . ASP   B 1 108 ? 44.485  -27.820 38.251 1.00 25.22 ? 800  ASP   B O   1 
ATOM   3170 C CB  . ASP   B 1 108 ? 42.718  -28.537 40.750 1.00 24.30 ? 800  ASP   B CB  1 
ATOM   3171 C CG  . ASP   B 1 108 ? 42.588  -29.058 42.168 1.00 27.79 ? 800  ASP   B CG  1 
ATOM   3172 O OD1 . ASP   B 1 108 ? 43.484  -28.811 42.965 1.00 28.48 ? 800  ASP   B OD1 1 
ATOM   3173 O OD2 . ASP   B 1 108 ? 41.570  -29.716 42.469 1.00 30.83 ? 800  ASP   B OD2 1 
ATOM   3174 N N   . TYR   B 1 109 ? 43.348  -25.949 38.744 1.00 24.84 ? 801  TYR   B N   1 
ATOM   3175 C CA  . TYR   B 1 109 ? 43.384  -25.446 37.365 1.00 24.87 ? 801  TYR   B CA  1 
ATOM   3176 C C   . TYR   B 1 109 ? 44.834  -25.114 36.959 1.00 25.12 ? 801  TYR   B C   1 
ATOM   3177 O O   . TYR   B 1 109 ? 45.258  -25.461 35.856 1.00 25.11 ? 801  TYR   B O   1 
ATOM   3178 C CB  . TYR   B 1 109 ? 42.461  -24.224 37.204 1.00 24.39 ? 801  TYR   B CB  1 
ATOM   3179 C CG  . TYR   B 1 109 ? 42.301  -23.770 35.769 1.00 24.44 ? 801  TYR   B CG  1 
ATOM   3180 C CD1 . TYR   B 1 109 ? 41.390  -24.388 34.919 1.00 24.93 ? 801  TYR   B CD1 1 
ATOM   3181 C CD2 . TYR   B 1 109 ? 43.054  -22.715 35.263 1.00 24.57 ? 801  TYR   B CD2 1 
ATOM   3182 C CE1 . TYR   B 1 109 ? 41.223  -23.958 33.608 1.00 25.41 ? 801  TYR   B CE1 1 
ATOM   3183 C CE2 . TYR   B 1 109 ? 42.919  -22.298 33.945 1.00 25.08 ? 801  TYR   B CE2 1 
ATOM   3184 C CZ  . TYR   B 1 109 ? 42.007  -22.926 33.115 1.00 26.10 ? 801  TYR   B CZ  1 
ATOM   3185 O OH  . TYR   B 1 109 ? 41.863  -22.504 31.808 1.00 27.40 ? 801  TYR   B OH  1 
ATOM   3186 N N   . VAL   B 1 110 ? 45.592  -24.446 37.847 1.00 25.06 ? 802  VAL   B N   1 
ATOM   3187 C CA  . VAL   B 1 110 ? 46.982  -24.097 37.540 1.00 25.55 ? 802  VAL   B CA  1 
ATOM   3188 C C   . VAL   B 1 110 ? 47.883  -25.329 37.527 1.00 26.55 ? 802  VAL   B C   1 
ATOM   3189 O O   . VAL   B 1 110 ? 48.806  -25.400 36.723 1.00 26.96 ? 802  VAL   B O   1 
ATOM   3190 C CB  . VAL   B 1 110 ? 47.563  -22.961 38.411 1.00 25.92 ? 802  VAL   B CB  1 
ATOM   3191 C CG1 . VAL   B 1 110 ? 46.744  -21.691 38.260 1.00 26.26 ? 802  VAL   B CG1 1 
ATOM   3192 C CG2 . VAL   B 1 110 ? 47.680  -23.379 39.872 1.00 26.17 ? 802  VAL   B CG2 1 
ATOM   3193 N N   . ARG   B 1 111 ? 47.583  -26.333 38.360 1.00 26.71 ? 803  ARG   B N   1 
ATOM   3194 C CA  . ARG   B 1 111 ? 48.309  -27.590 38.359 1.00 27.08 ? 803  ARG   B CA  1 
ATOM   3195 C C   . ARG   B 1 111 ? 48.075  -28.286 37.008 1.00 29.50 ? 803  ARG   B C   1 
ATOM   3196 O O   . ARG   B 1 111 ? 49.032  -28.481 36.257 1.00 30.63 ? 803  ARG   B O   1 
ATOM   3197 C CB  . ARG   B 1 111 ? 47.847  -28.465 39.528 1.00 26.20 ? 803  ARG   B CB  1 
ATOM   3198 C CG  . ARG   B 1 111 ? 48.560  -28.101 40.805 1.00 26.16 ? 803  ARG   B CG  1 
ATOM   3199 C CD  . ARG   B 1 111 ? 48.021  -28.837 42.002 1.00 25.40 ? 803  ARG   B CD  1 
ATOM   3200 N NE  . ARG   B 1 111 ? 48.699  -28.390 43.209 1.00 25.03 ? 803  ARG   B NE  1 
ATOM   3201 C CZ  . ARG   B 1 111 ? 48.353  -28.733 44.443 1.00 27.01 ? 803  ARG   B CZ  1 
ATOM   3202 N NH1 . ARG   B 1 111 ? 47.318  -29.538 44.651 1.00 25.82 ? 803  ARG   B NH1 1 
ATOM   3203 N NH2 . ARG   B 1 111 ? 49.039  -28.274 45.481 1.00 27.57 ? 803  ARG   B NH2 1 
ATOM   3204 N N   . GLU   B 1 112 ? 46.803  -28.521 36.639 1.00 29.82 ? 804  GLU   B N   1 
ATOM   3205 C CA  . GLU   B 1 112 ? 46.439  -29.156 35.385 1.00 30.98 ? 804  GLU   B CA  1 
ATOM   3206 C C   . GLU   B 1 112 ? 46.899  -28.376 34.153 1.00 31.65 ? 804  GLU   B C   1 
ATOM   3207 O O   . GLU   B 1 112 ? 47.060  -28.954 33.085 1.00 31.63 ? 804  GLU   B O   1 
ATOM   3208 C CB  . GLU   B 1 112 ? 44.925  -29.436 35.349 1.00 35.09 ? 804  GLU   B CB  1 
ATOM   3209 C CG  . GLU   B 1 112 ? 44.536  -30.836 35.820 1.00 42.65 ? 804  GLU   B CG  1 
ATOM   3210 C CD  . GLU   B 1 112 ? 44.004  -30.983 37.238 1.00 51.80 ? 804  GLU   B CD  1 
ATOM   3211 O OE1 . GLU   B 1 112 ? 42.962  -31.658 37.414 1.00 53.77 ? 804  GLU   B OE1 1 
ATOM   3212 O OE2 . GLU   B 1 112 ? 44.633  -30.436 38.174 1.00 53.62 ? 804  GLU   B OE2 1 
ATOM   3213 N N   . HIS   B 1 113 ? 47.123  -27.071 34.292 1.00 32.40 ? 805  HIS   B N   1 
ATOM   3214 C CA  . HIS   B 1 113 ? 47.586  -26.249 33.179 1.00 33.05 ? 805  HIS   B CA  1 
ATOM   3215 C C   . HIS   B 1 113 ? 49.021  -25.801 33.337 1.00 34.45 ? 805  HIS   B C   1 
ATOM   3216 O O   . HIS   B 1 113 ? 49.382  -24.751 32.835 1.00 34.41 ? 805  HIS   B O   1 
ATOM   3217 C CB  . HIS   B 1 113 ? 46.650  -25.065 32.922 1.00 33.02 ? 805  HIS   B CB  1 
ATOM   3218 C CG  . HIS   B 1 113 ? 45.323  -25.470 32.360 1.00 33.28 ? 805  HIS   B CG  1 
ATOM   3219 N ND1 . HIS   B 1 113 ? 45.150  -25.683 31.004 1.00 34.64 ? 805  HIS   B ND1 1 
ATOM   3220 C CD2 . HIS   B 1 113 ? 44.153  -25.715 32.994 1.00 33.96 ? 805  HIS   B CD2 1 
ATOM   3221 C CE1 . HIS   B 1 113 ? 43.887  -26.047 30.857 1.00 34.99 ? 805  HIS   B CE1 1 
ATOM   3222 N NE2 . HIS   B 1 113 ? 43.244  -26.072 32.024 1.00 34.82 ? 805  HIS   B NE2 1 
ATOM   3223 N N   . LYS   B 1 114 ? 49.851  -26.599 34.009 1.00 35.96 ? 806  LYS   B N   1 
ATOM   3224 C CA  . LYS   B 1 114 ? 51.274  -26.293 34.138 1.00 38.01 ? 806  LYS   B CA  1 
ATOM   3225 C C   . LYS   B 1 114 ? 51.963  -26.868 32.893 1.00 39.70 ? 806  LYS   B C   1 
ATOM   3226 O O   . LYS   B 1 114 ? 51.818  -28.068 32.625 1.00 40.04 ? 806  LYS   B O   1 
ATOM   3227 C CB  . LYS   B 1 114 ? 51.862  -26.969 35.388 1.00 40.28 ? 806  LYS   B CB  1 
ATOM   3228 C CG  . LYS   B 1 114 ? 53.334  -26.654 35.554 1.00 45.39 ? 806  LYS   B CG  1 
ATOM   3229 C CD  . LYS   B 1 114 ? 54.094  -27.698 36.334 1.00 50.22 ? 806  LYS   B CD  1 
ATOM   3230 C CE  . LYS   B 1 114 ? 55.563  -27.355 36.346 1.00 53.61 ? 806  LYS   B CE  1 
ATOM   3231 N NZ  . LYS   B 1 114 ? 55.791  -25.918 36.642 1.00 55.07 ? 806  LYS   B NZ  1 
ATOM   3232 N N   . ASP   B 1 115 ? 52.709  -26.053 32.129 1.00 40.42 ? 807  ASP   B N   1 
ATOM   3233 C CA  . ASP   B 1 115 ? 52.942  -24.626 32.360 1.00 41.39 ? 807  ASP   B CA  1 
ATOM   3234 C C   . ASP   B 1 115 ? 52.246  -23.780 31.268 1.00 41.65 ? 807  ASP   B C   1 
ATOM   3235 O O   . ASP   B 1 115 ? 52.684  -22.653 31.005 1.00 42.08 ? 807  ASP   B O   1 
ATOM   3236 C CB  . ASP   B 1 115 ? 54.459  -24.330 32.312 1.00 43.94 ? 807  ASP   B CB  1 
ATOM   3237 C CG  . ASP   B 1 115 ? 55.330  -25.195 33.213 1.00 50.38 ? 807  ASP   B CG  1 
ATOM   3238 O OD1 . ASP   B 1 115 ? 55.483  -26.408 32.914 1.00 51.69 ? 807  ASP   B OD1 1 
ATOM   3239 O OD2 . ASP   B 1 115 ? 55.869  -24.662 34.205 1.00 52.78 ? 807  ASP   B OD2 1 
ATOM   3240 N N   . ASN   B 1 116 ? 51.159  -24.312 30.650 1.00 40.74 ? 808  ASN   B N   1 
ATOM   3241 C CA  . ASN   B 1 116 ? 50.412  -23.675 29.570 1.00 39.86 ? 808  ASN   B CA  1 
ATOM   3242 C C   . ASN   B 1 116 ? 49.457  -22.531 30.010 1.00 37.24 ? 808  ASN   B C   1 
ATOM   3243 O O   . ASN   B 1 116 ? 48.370  -22.402 29.456 1.00 37.26 ? 808  ASN   B O   1 
ATOM   3244 C CB  . ASN   B 1 116 ? 49.651  -24.730 28.765 1.00 42.15 ? 808  ASN   B CB  1 
ATOM   3245 C CG  . ASN   B 1 116 ? 49.686  -24.515 27.262 1.00 46.99 ? 808  ASN   B CG  1 
ATOM   3246 O OD1 . ASN   B 1 116 ? 50.664  -23.998 26.696 1.00 48.74 ? 808  ASN   B OD1 1 
ATOM   3247 N ND2 . ASN   B 1 116 ? 48.621  -24.931 26.575 1.00 47.75 ? 808  ASN   B ND2 1 
ATOM   3248 N N   . ILE   B 1 117 ? 49.876  -21.680 30.951 1.00 34.87 ? 809  ILE   B N   1 
ATOM   3249 C CA  . ILE   B 1 117 ? 49.057  -20.542 31.384 1.00 32.88 ? 809  ILE   B CA  1 
ATOM   3250 C C   . ILE   B 1 117 ? 49.770  -19.269 31.007 1.00 31.07 ? 809  ILE   B C   1 
ATOM   3251 O O   . ILE   B 1 117 ? 50.935  -19.117 31.330 1.00 31.14 ? 809  ILE   B O   1 
ATOM   3252 C CB  . ILE   B 1 117 ? 48.776  -20.578 32.902 1.00 32.45 ? 809  ILE   B CB  1 
ATOM   3253 C CG1 . ILE   B 1 117 ? 48.006  -21.840 33.282 1.00 32.58 ? 809  ILE   B CG1 1 
ATOM   3254 C CG2 . ILE   B 1 117 ? 48.024  -19.330 33.340 1.00 32.72 ? 809  ILE   B CG2 1 
ATOM   3255 C CD1 . ILE   B 1 117 ? 47.985  -22.100 34.693 1.00 33.37 ? 809  ILE   B CD1 1 
ATOM   3256 N N   . GLY   B 1 118 ? 49.084  -18.376 30.316 1.00 29.74 ? 810  GLY   B N   1 
ATOM   3257 C CA  . GLY   B 1 118 ? 49.676  -17.115 29.902 1.00 29.01 ? 810  GLY   B CA  1 
ATOM   3258 C C   . GLY   B 1 118 ? 49.831  -16.134 31.033 1.00 28.13 ? 810  GLY   B C   1 
ATOM   3259 O O   . GLY   B 1 118 ? 49.126  -16.227 32.039 1.00 28.93 ? 810  GLY   B O   1 
ATOM   3260 N N   . SER   B 1 119 ? 50.745  -15.180 30.880 1.00 26.63 ? 811  SER   B N   1 
ATOM   3261 C CA  . SER   B 1 119 ? 50.940  -14.145 31.895 1.00 25.64 ? 811  SER   B CA  1 
ATOM   3262 C C   . SER   B 1 119 ? 49.707  -13.230 32.010 1.00 23.92 ? 811  SER   B C   1 
ATOM   3263 O O   . SER   B 1 119 ? 49.449  -12.679 33.076 1.00 23.23 ? 811  SER   B O   1 
ATOM   3264 C CB  . SER   B 1 119 ? 52.174  -13.321 31.578 1.00 26.66 ? 811  SER   B CB  1 
ATOM   3265 O OG  . SER   B 1 119 ? 51.953  -12.667 30.343 1.00 29.47 ? 811  SER   B OG  1 
ATOM   3266 N N   . GLN   B 1 120 ? 48.959  -13.063 30.915 1.00 23.23 ? 812  GLN   B N   1 
ATOM   3267 C CA  . GLN   B 1 120 ? 47.744  -12.257 30.935 1.00 23.23 ? 812  GLN   B CA  1 
ATOM   3268 C C   . GLN   B 1 120 ? 46.675  -12.839 31.898 1.00 22.25 ? 812  GLN   B C   1 
ATOM   3269 O O   . GLN   B 1 120 ? 45.975  -12.070 32.547 1.00 21.94 ? 812  GLN   B O   1 
ATOM   3270 C CB  . GLN   B 1 120 ? 47.187  -12.076 29.522 1.00 24.89 ? 812  GLN   B CB  1 
ATOM   3271 C CG  . GLN   B 1 120 ? 47.106  -10.612 29.125 1.00 29.44 ? 812  GLN   B CG  1 
ATOM   3272 C CD  . GLN   B 1 120 ? 46.982  -10.419 27.628 1.00 33.61 ? 812  GLN   B CD  1 
ATOM   3273 O OE1 . GLN   B 1 120 ? 47.357  -11.280 26.822 1.00 33.73 ? 812  GLN   B OE1 1 
ATOM   3274 N NE2 . GLN   B 1 120 ? 46.459  -9.266  27.233 1.00 34.25 ? 812  GLN   B NE2 1 
ATOM   3275 N N   . TYR   B 1 121 ? 46.572  -14.181 32.001 1.00 21.17 ? 813  TYR   B N   1 
ATOM   3276 C CA  . TYR   B 1 121 ? 45.630  -14.831 32.908 1.00 20.55 ? 813  TYR   B CA  1 
ATOM   3277 C C   . TYR   B 1 121 ? 46.103  -14.635 34.349 1.00 19.91 ? 813  TYR   B C   1 
ATOM   3278 O O   . TYR   B 1 121 ? 45.336  -14.194 35.205 1.00 19.98 ? 813  TYR   B O   1 
ATOM   3279 C CB  . TYR   B 1 121 ? 45.521  -16.342 32.617 1.00 20.50 ? 813  TYR   B CB  1 
ATOM   3280 C CG  . TYR   B 1 121 ? 44.752  -16.656 31.366 1.00 21.50 ? 813  TYR   B CG  1 
ATOM   3281 C CD1 . TYR   B 1 121 ? 43.374  -16.792 31.390 1.00 22.04 ? 813  TYR   B CD1 1 
ATOM   3282 C CD2 . TYR   B 1 121 ? 45.396  -16.766 30.144 1.00 23.11 ? 813  TYR   B CD2 1 
ATOM   3283 C CE1 . TYR   B 1 121 ? 42.658  -17.053 30.233 1.00 23.36 ? 813  TYR   B CE1 1 
ATOM   3284 C CE2 . TYR   B 1 121 ? 44.692  -17.012 28.980 1.00 24.08 ? 813  TYR   B CE2 1 
ATOM   3285 C CZ  . TYR   B 1 121 ? 43.324  -17.161 29.028 1.00 25.01 ? 813  TYR   B CZ  1 
ATOM   3286 O OH  . TYR   B 1 121 ? 42.661  -17.459 27.869 1.00 27.51 ? 813  TYR   B OH  1 
ATOM   3287 N N   . LEU   B 1 122 ? 47.371  -14.953 34.603 1.00 18.51 ? 814  LEU   B N   1 
ATOM   3288 C CA  . LEU   B 1 122 ? 47.993  -14.846 35.901 1.00 17.65 ? 814  LEU   B CA  1 
ATOM   3289 C C   . LEU   B 1 122 ? 47.824  -13.470 36.543 1.00 16.41 ? 814  LEU   B C   1 
ATOM   3290 O O   . LEU   B 1 122 ? 47.282  -13.379 37.642 1.00 16.30 ? 814  LEU   B O   1 
ATOM   3291 C CB  . LEU   B 1 122 ? 49.463  -15.224 35.764 1.00 17.97 ? 814  LEU   B CB  1 
ATOM   3292 C CG  . LEU   B 1 122 ? 49.665  -16.705 35.542 1.00 20.40 ? 814  LEU   B CG  1 
ATOM   3293 C CD1 . LEU   B 1 122 ? 51.091  -17.004 35.151 1.00 21.31 ? 814  LEU   B CD1 1 
ATOM   3294 C CD2 . LEU   B 1 122 ? 49.327  -17.479 36.780 1.00 21.22 ? 814  LEU   B CD2 1 
ATOM   3295 N N   . LEU   B 1 123 ? 48.223  -12.408 35.834 1.00 14.97 ? 815  LEU   B N   1 
ATOM   3296 C CA  . LEU   B 1 123 ? 48.116  -11.044 36.339 1.00 14.03 ? 815  LEU   B CA  1 
ATOM   3297 C C   . LEU   B 1 123 ? 46.651  -10.611 36.519 1.00 14.04 ? 815  LEU   B C   1 
ATOM   3298 O O   . LEU   B 1 123 ? 46.336  -9.994  37.527 1.00 13.66 ? 815  LEU   B O   1 
ATOM   3299 C CB  . LEU   B 1 123 ? 48.901  -10.089 35.430 1.00 13.30 ? 815  LEU   B CB  1 
ATOM   3300 C CG  . LEU   B 1 123 ? 50.424  -10.410 35.402 1.00 12.87 ? 815  LEU   B CG  1 
ATOM   3301 C CD1 . LEU   B 1 123 ? 51.123  -9.756  34.219 1.00 12.51 ? 815  LEU   B CD1 1 
ATOM   3302 C CD2 . LEU   B 1 123 ? 51.101  -10.096 36.760 1.00 12.22 ? 815  LEU   B CD2 1 
ATOM   3303 N N   . ASN   B 1 124 ? 45.746  -11.034 35.614 1.00 13.87 ? 816  ASN   B N   1 
ATOM   3304 C CA  . ASN   B 1 124 ? 44.326  -10.712 35.739 1.00 14.17 ? 816  ASN   B CA  1 
ATOM   3305 C C   . ASN   B 1 124 ? 43.656  -11.424 36.896 1.00 14.06 ? 816  ASN   B C   1 
ATOM   3306 O O   . ASN   B 1 124 ? 42.817  -10.820 37.541 1.00 14.60 ? 816  ASN   B O   1 
ATOM   3307 C CB  . ASN   B 1 124 ? 43.582  -10.941 34.437 1.00 15.25 ? 816  ASN   B CB  1 
ATOM   3308 C CG  . ASN   B 1 124 ? 43.617  -9.698  33.616 1.00 18.57 ? 816  ASN   B CG  1 
ATOM   3309 O OD1 . ASN   B 1 124 ? 42.890  -8.742  33.886 1.00 19.23 ? 816  ASN   B OD1 1 
ATOM   3310 N ND2 . ASN   B 1 124 ? 44.494  -9.662  32.616 1.00 20.02 ? 816  ASN   B ND2 1 
ATOM   3311 N N   . TRP   B 1 125 ? 44.050  -12.664 37.199 1.00 13.71 ? 817  TRP   B N   1 
ATOM   3312 C CA  . TRP   B 1 125 ? 43.528  -13.369 38.362 1.00 14.90 ? 817  TRP   B CA  1 
ATOM   3313 C C   . TRP   B 1 125 ? 43.978  -12.665 39.634 1.00 14.94 ? 817  TRP   B C   1 
ATOM   3314 O O   . TRP   B 1 125 ? 43.174  -12.505 40.547 1.00 15.12 ? 817  TRP   B O   1 
ATOM   3315 C CB  . TRP   B 1 125 ? 44.007  -14.814 38.396 1.00 15.71 ? 817  TRP   B CB  1 
ATOM   3316 C CG  . TRP   B 1 125 ? 43.480  -15.690 37.302 1.00 17.56 ? 817  TRP   B CG  1 
ATOM   3317 C CD1 . TRP   B 1 125 ? 42.342  -15.512 36.557 1.00 18.85 ? 817  TRP   B CD1 1 
ATOM   3318 C CD2 . TRP   B 1 125 ? 44.063  -16.918 36.858 1.00 18.19 ? 817  TRP   B CD2 1 
ATOM   3319 N NE1 . TRP   B 1 125 ? 42.203  -16.546 35.656 1.00 19.31 ? 817  TRP   B NE1 1 
ATOM   3320 C CE2 . TRP   B 1 125 ? 43.248  -17.425 35.824 1.00 19.34 ? 817  TRP   B CE2 1 
ATOM   3321 C CE3 . TRP   B 1 125 ? 45.218  -17.626 37.217 1.00 19.04 ? 817  TRP   B CE3 1 
ATOM   3322 C CZ2 . TRP   B 1 125 ? 43.526  -18.634 35.184 1.00 20.27 ? 817  TRP   B CZ2 1 
ATOM   3323 C CZ3 . TRP   B 1 125 ? 45.503  -18.808 36.570 1.00 20.15 ? 817  TRP   B CZ3 1 
ATOM   3324 C CH2 . TRP   B 1 125 ? 44.666  -19.301 35.566 1.00 20.38 ? 817  TRP   B CH2 1 
ATOM   3325 N N   . CYS   B 1 126 ? 45.258  -12.209 39.679 1.00 14.34 ? 818  CYS   B N   1 
ATOM   3326 C CA  . CYS   B 1 126 ? 45.819  -11.440 40.787 1.00 14.14 ? 818  CYS   B CA  1 
ATOM   3327 C C   . CYS   B 1 126 ? 45.015  -10.178 41.059 1.00 14.23 ? 818  CYS   B C   1 
ATOM   3328 O O   . CYS   B 1 126 ? 44.765  -9.866  42.215 1.00 14.48 ? 818  CYS   B O   1 
ATOM   3329 C CB  . CYS   B 1 126 ? 47.292  -11.122 40.539 1.00 14.56 ? 818  CYS   B CB  1 
ATOM   3330 S SG  . CYS   B 1 126 ? 48.370  -12.579 40.633 1.00 16.51 ? 818  CYS   B SG  1 
ATOM   3331 N N   . VAL   B 1 127 ? 44.592  -9.475  39.998 1.00 14.03 ? 819  VAL   B N   1 
ATOM   3332 C CA  . VAL   B 1 127 ? 43.748  -8.266  40.029 1.00 14.79 ? 819  VAL   B CA  1 
ATOM   3333 C C   . VAL   B 1 127 ? 42.351  -8.602  40.590 1.00 15.28 ? 819  VAL   B C   1 
ATOM   3334 O O   . VAL   B 1 127 ? 41.779  -7.814  41.354 1.00 15.71 ? 819  VAL   B O   1 
ATOM   3335 C CB  . VAL   B 1 127 ? 43.633  -7.705  38.567 1.00 14.83 ? 819  VAL   B CB  1 
ATOM   3336 C CG1 . VAL   B 1 127 ? 42.435  -6.792  38.376 1.00 15.31 ? 819  VAL   B CG1 1 
ATOM   3337 C CG2 . VAL   B 1 127 ? 44.909  -6.994  38.152 1.00 14.77 ? 819  VAL   B CG2 1 
ATOM   3338 N N   . GLN   B 1 128 ? 41.771  -9.733  40.125 1.00 14.77 ? 820  GLN   B N   1 
ATOM   3339 C CA  . GLN   B 1 128 ? 40.412  -10.143 40.489 1.00 14.36 ? 820  GLN   B CA  1 
ATOM   3340 C C   . GLN   B 1 128 ? 40.339  -10.604 41.934 1.00 14.30 ? 820  GLN   B C   1 
ATOM   3341 O O   . GLN   B 1 128 ? 39.407  -10.246 42.651 1.00 14.27 ? 820  GLN   B O   1 
ATOM   3342 C CB  . GLN   B 1 128 ? 39.912  -11.230 39.539 1.00 15.09 ? 820  GLN   B CB  1 
ATOM   3343 C CG  . GLN   B 1 128 ? 39.594  -10.714 38.128 1.00 17.14 ? 820  GLN   B CG  1 
ATOM   3344 C CD  . GLN   B 1 128 ? 39.055  -11.810 37.219 1.00 19.86 ? 820  GLN   B CD  1 
ATOM   3345 O OE1 . GLN   B 1 128 ? 38.493  -12.800 37.679 1.00 19.49 ? 820  GLN   B OE1 1 
ATOM   3346 N NE2 . GLN   B 1 128 ? 39.224  -11.661 35.893 1.00 21.07 ? 820  GLN   B NE2 1 
ATOM   3347 N N   . ILE   B 1 129 ? 41.362  -11.311 42.390 1.00 13.87 ? 821  ILE   B N   1 
ATOM   3348 C CA  . ILE   B 1 129 ? 41.422  -11.785 43.765 1.00 14.06 ? 821  ILE   B CA  1 
ATOM   3349 C C   . ILE   B 1 129 ? 41.547  -10.588 44.707 1.00 14.96 ? 821  ILE   B C   1 
ATOM   3350 O O   . ILE   B 1 129 ? 40.872  -10.549 45.742 1.00 15.63 ? 821  ILE   B O   1 
ATOM   3351 C CB  . ILE   B 1 129 ? 42.552  -12.852 43.928 1.00 13.74 ? 821  ILE   B CB  1 
ATOM   3352 C CG1 . ILE   B 1 129 ? 42.221  -14.118 43.107 1.00 14.18 ? 821  ILE   B CG1 1 
ATOM   3353 C CG2 . ILE   B 1 129 ? 42.759  -13.224 45.396 1.00 13.50 ? 821  ILE   B CG2 1 
ATOM   3354 C CD1 . ILE   B 1 129 ? 43.457  -15.139 42.973 1.00 15.18 ? 821  ILE   B CD1 1 
ATOM   3355 N N   . ALA   B 1 130 ? 42.319  -9.570  44.302 1.00 14.83 ? 822  ALA   B N   1 
ATOM   3356 C CA  . ALA   B 1 130 ? 42.445  -8.331  45.064 1.00 15.25 ? 822  ALA   B CA  1 
ATOM   3357 C C   . ALA   B 1 130 ? 41.134  -7.527  45.045 1.00 15.04 ? 822  ALA   B C   1 
ATOM   3358 O O   . ALA   B 1 130 ? 40.768  -7.001  46.082 1.00 15.28 ? 822  ALA   B O   1 
ATOM   3359 C CB  . ALA   B 1 130 ? 43.600  -7.491  44.533 1.00 15.30 ? 822  ALA   B CB  1 
ATOM   3360 N N   . LYS   B 1 131 ? 40.408  -7.458  43.912 1.00 14.66 ? 823  LYS   B N   1 
ATOM   3361 C CA  . LYS   B 1 131 ? 39.104  -6.759  43.898 1.00 15.33 ? 823  LYS   B CA  1 
ATOM   3362 C C   . LYS   B 1 131 ? 38.109  -7.420  44.893 1.00 15.82 ? 823  LYS   B C   1 
ATOM   3363 O O   . LYS   B 1 131 ? 37.410  -6.724  45.621 1.00 16.34 ? 823  LYS   B O   1 
ATOM   3364 C CB  . LYS   B 1 131 ? 38.476  -6.727  42.489 1.00 16.77 ? 823  LYS   B CB  1 
ATOM   3365 C CG  . LYS   B 1 131 ? 39.134  -5.745  41.529 1.00 19.57 ? 823  LYS   B CG  1 
ATOM   3366 C CD  . LYS   B 1 131 ? 38.677  -5.951  40.083 1.00 21.63 ? 823  LYS   B CD  1 
ATOM   3367 C CE  . LYS   B 1 131 ? 39.141  -4.795  39.247 1.00 26.14 ? 823  LYS   B CE  1 
ATOM   3368 N NZ  . LYS   B 1 131 ? 39.125  -5.105  37.792 1.00 30.45 ? 823  LYS   B NZ  1 
ATOM   3369 N N   . GLY   B 1 132 ? 38.055  -8.749  44.901 1.00 15.29 ? 824  GLY   B N   1 
ATOM   3370 C CA  . GLY   B 1 132 ? 37.177  -9.485  45.799 1.00 15.30 ? 824  GLY   B CA  1 
ATOM   3371 C C   . GLY   B 1 132 ? 37.533  -9.289  47.261 1.00 15.31 ? 824  GLY   B C   1 
ATOM   3372 O O   . GLY   B 1 132 ? 36.655  -9.133  48.104 1.00 16.21 ? 824  GLY   B O   1 
ATOM   3373 N N   . MET   B 1 133 ? 38.823  -9.276  47.567 1.00 14.76 ? 825  MET   B N   1 
ATOM   3374 C CA  . MET   B 1 133 ? 39.302  -9.083  48.918 1.00 14.47 ? 825  MET   B CA  1 
ATOM   3375 C C   . MET   B 1 133 ? 39.076  -7.659  49.366 1.00 15.50 ? 825  MET   B C   1 
ATOM   3376 O O   . MET   B 1 133 ? 38.717  -7.431  50.521 1.00 16.18 ? 825  MET   B O   1 
ATOM   3377 C CB  . MET   B 1 133 ? 40.793  -9.483  49.047 1.00 13.05 ? 825  MET   B CB  1 
ATOM   3378 C CG  . MET   B 1 133 ? 41.030  -10.964 48.999 1.00 14.19 ? 825  MET   B CG  1 
ATOM   3379 S SD  . MET   B 1 133 ? 40.049  -11.915 50.215 1.00 19.12 ? 825  MET   B SD  1 
ATOM   3380 C CE  . MET   B 1 133 ? 40.805  -11.371 51.675 1.00 15.46 ? 825  MET   B CE  1 
ATOM   3381 N N   . ASN   B 1 134 ? 39.275  -6.691  48.470 1.00 15.54 ? 826  ASN   B N   1 
ATOM   3382 C CA  . ASN   B 1 134 ? 39.029  -5.288  48.791 1.00 16.04 ? 826  ASN   B CA  1 
ATOM   3383 C C   . ASN   B 1 134 ? 37.564  -5.060  49.130 1.00 16.23 ? 826  ASN   B C   1 
ATOM   3384 O O   . ASN   B 1 134 ? 37.296  -4.266  50.029 1.00 17.03 ? 826  ASN   B O   1 
ATOM   3385 C CB  . ASN   B 1 134 ? 39.429  -4.389  47.649 1.00 17.46 ? 826  ASN   B CB  1 
ATOM   3386 C CG  . ASN   B 1 134 ? 39.472  -2.969  48.086 1.00 21.36 ? 826  ASN   B CG  1 
ATOM   3387 O OD1 . ASN   B 1 134 ? 39.983  -2.658  49.161 1.00 23.01 ? 826  ASN   B OD1 1 
ATOM   3388 N ND2 . ASN   B 1 134 ? 38.903  -2.091  47.284 1.00 22.19 ? 826  ASN   B ND2 1 
ATOM   3389 N N   . TYR   B 1 135 ? 36.617  -5.791  48.463 1.00 15.42 ? 827  TYR   B N   1 
ATOM   3390 C CA  . TYR   B 1 135 ? 35.191  -5.689  48.771 1.00 15.63 ? 827  TYR   B CA  1 
ATOM   3391 C C   . TYR   B 1 135 ? 34.946  -6.124  50.212 1.00 16.31 ? 827  TYR   B C   1 
ATOM   3392 O O   . TYR   B 1 135 ? 34.215  -5.455  50.933 1.00 16.75 ? 827  TYR   B O   1 
ATOM   3393 C CB  . TYR   B 1 135 ? 34.327  -6.534  47.821 1.00 15.39 ? 827  TYR   B CB  1 
ATOM   3394 C CG  . TYR   B 1 135 ? 32.888  -6.707  48.294 1.00 15.98 ? 827  TYR   B CG  1 
ATOM   3395 C CD1 . TYR   B 1 135 ? 31.979  -5.656  48.222 1.00 16.31 ? 827  TYR   B CD1 1 
ATOM   3396 C CD2 . TYR   B 1 135 ? 32.441  -7.922  48.807 1.00 16.14 ? 827  TYR   B CD2 1 
ATOM   3397 C CE1 . TYR   B 1 135 ? 30.660  -5.816  48.626 1.00 16.92 ? 827  TYR   B CE1 1 
ATOM   3398 C CE2 . TYR   B 1 135 ? 31.123  -8.090  49.215 1.00 16.99 ? 827  TYR   B CE2 1 
ATOM   3399 C CZ  . TYR   B 1 135 ? 30.239  -7.025  49.149 1.00 18.03 ? 827  TYR   B CZ  1 
ATOM   3400 O OH  . TYR   B 1 135 ? 28.932  -7.170  49.581 1.00 19.08 ? 827  TYR   B OH  1 
ATOM   3401 N N   . LEU   B 1 136 ? 35.549  -7.245  50.626 1.00 16.41 ? 828  LEU   B N   1 
ATOM   3402 C CA  . LEU   B 1 136 ? 35.434  -7.750  51.980 1.00 17.14 ? 828  LEU   B CA  1 
ATOM   3403 C C   . LEU   B 1 136 ? 35.998  -6.718  52.951 1.00 19.72 ? 828  LEU   B C   1 
ATOM   3404 O O   . LEU   B 1 136 ? 35.286  -6.342  53.869 1.00 20.72 ? 828  LEU   B O   1 
ATOM   3405 C CB  . LEU   B 1 136 ? 36.159  -9.095  52.116 1.00 15.91 ? 828  LEU   B CB  1 
ATOM   3406 C CG  . LEU   B 1 136 ? 35.619  -10.246 51.265 1.00 15.34 ? 828  LEU   B CG  1 
ATOM   3407 C CD1 . LEU   B 1 136 ? 36.389  -11.558 51.582 1.00 15.11 ? 828  LEU   B CD1 1 
ATOM   3408 C CD2 . LEU   B 1 136 ? 34.145  -10.458 51.513 1.00 15.37 ? 828  LEU   B CD2 1 
ATOM   3409 N N   . GLU   B 1 137 ? 37.182  -6.144  52.668 1.00 20.27 ? 829  GLU   B N   1 
ATOM   3410 C CA  . GLU   B 1 137 ? 37.730  -5.085  53.530 1.00 21.17 ? 829  GLU   B CA  1 
ATOM   3411 C C   . GLU   B 1 137 ? 36.773  -3.878  53.676 1.00 22.31 ? 829  GLU   B C   1 
ATOM   3412 O O   . GLU   B 1 137 ? 36.513  -3.451  54.806 1.00 22.80 ? 829  GLU   B O   1 
ATOM   3413 C CB  . GLU   B 1 137 ? 39.133  -4.627  53.095 1.00 22.39 ? 829  GLU   B CB  1 
ATOM   3414 C CG  . GLU   B 1 137 ? 39.696  -3.571  54.036 1.00 24.82 ? 829  GLU   B CG  1 
ATOM   3415 C CD  . GLU   B 1 137 ? 41.170  -3.265  53.950 1.00 28.29 ? 829  GLU   B CD  1 
ATOM   3416 O OE1 . GLU   B 1 137 ? 41.764  -3.481  52.871 1.00 29.67 ? 829  GLU   B OE1 1 
ATOM   3417 O OE2 . GLU   B 1 137 ? 41.731  -2.796  54.965 1.00 30.40 ? 829  GLU   B OE2 1 
ATOM   3418 N N   . ASP   B 1 138 ? 36.198  -3.376  52.571 1.00 22.31 ? 830  ASP   B N   1 
ATOM   3419 C CA  . ASP   B 1 138 ? 35.236  -2.272  52.653 1.00 23.17 ? 830  ASP   B CA  1 
ATOM   3420 C C   . ASP   B 1 138 ? 34.029  -2.604  53.539 1.00 23.22 ? 830  ASP   B C   1 
ATOM   3421 O O   . ASP   B 1 138 ? 33.484  -1.709  54.181 1.00 23.39 ? 830  ASP   B O   1 
ATOM   3422 C CB  . ASP   B 1 138 ? 34.745  -1.878  51.257 1.00 25.96 ? 830  ASP   B CB  1 
ATOM   3423 C CG  . ASP   B 1 138 ? 35.693  -0.941  50.548 1.00 33.64 ? 830  ASP   B CG  1 
ATOM   3424 O OD1 . ASP   B 1 138 ? 36.409  -0.169  51.249 1.00 34.83 ? 830  ASP   B OD1 1 
ATOM   3425 O OD2 . ASP   B 1 138 ? 35.720  -0.964  49.293 1.00 36.84 ? 830  ASP   B OD2 1 
ATOM   3426 N N   . ARG   B 1 139 ? 33.582  -3.882  53.532 1.00 22.98 ? 831  ARG   B N   1 
ATOM   3427 C CA  . ARG   B 1 139 ? 32.457  -4.380  54.355 1.00 22.79 ? 831  ARG   B CA  1 
ATOM   3428 C C   . ARG   B 1 139 ? 32.902  -4.786  55.788 1.00 23.18 ? 831  ARG   B C   1 
ATOM   3429 O O   . ARG   B 1 139 ? 32.114  -5.401  56.503 1.00 23.39 ? 831  ARG   B O   1 
ATOM   3430 C CB  . ARG   B 1 139 ? 31.830  -5.636  53.710 1.00 22.71 ? 831  ARG   B CB  1 
ATOM   3431 C CG  . ARG   B 1 139 ? 31.000  -5.437  52.441 1.00 22.93 ? 831  ARG   B CG  1 
ATOM   3432 C CD  . ARG   B 1 139 ? 29.531  -5.115  52.660 1.00 23.73 ? 831  ARG   B CD  1 
ATOM   3433 N NE  . ARG   B 1 139 ? 28.856  -5.910  53.694 1.00 23.57 ? 831  ARG   B NE  1 
ATOM   3434 C CZ  . ARG   B 1 139 ? 28.233  -7.065  53.472 1.00 20.82 ? 831  ARG   B CZ  1 
ATOM   3435 N NH1 . ARG   B 1 139 ? 28.237  -7.607  52.260 1.00 18.04 ? 831  ARG   B NH1 1 
ATOM   3436 N NH2 . ARG   B 1 139 ? 27.634  -7.704  54.468 1.00 18.28 ? 831  ARG   B NH2 1 
ATOM   3437 N N   . ARG   B 1 140 ? 34.181  -4.543  56.132 1.00 23.40 ? 832  ARG   B N   1 
ATOM   3438 C CA  . ARG   B 1 140 ? 34.886  -4.870  57.367 1.00 23.96 ? 832  ARG   B CA  1 
ATOM   3439 C C   . ARG   B 1 140 ? 34.873  -6.372  57.636 1.00 21.84 ? 832  ARG   B C   1 
ATOM   3440 O O   . ARG   B 1 140 ? 34.659  -6.814  58.766 1.00 22.30 ? 832  ARG   B O   1 
ATOM   3441 C CB  . ARG   B 1 140 ? 34.350  -4.028  58.538 1.00 27.55 ? 832  ARG   B CB  1 
ATOM   3442 C CG  . ARG   B 1 140 ? 34.501  -2.531  58.232 1.00 34.10 ? 832  ARG   B CG  1 
ATOM   3443 C CD  . ARG   B 1 140 ? 33.912  -1.557  59.259 1.00 40.49 ? 832  ARG   B CD  1 
ATOM   3444 N NE  . ARG   B 1 140 ? 32.673  -2.009  59.903 1.00 45.93 ? 832  ARG   B NE  1 
ATOM   3445 C CZ  . ARG   B 1 140 ? 31.459  -1.899  59.370 1.00 49.74 ? 832  ARG   B CZ  1 
ATOM   3446 N NH1 . ARG   B 1 140 ? 31.303  -1.392  58.151 1.00 49.23 ? 832  ARG   B NH1 1 
ATOM   3447 N NH2 . ARG   B 1 140 ? 30.393  -2.321  60.042 1.00 50.50 ? 832  ARG   B NH2 1 
ATOM   3448 N N   . LEU   B 1 141 ? 35.061  -7.151  56.589 1.00 19.45 ? 833  LEU   B N   1 
ATOM   3449 C CA  . LEU   B 1 141 ? 35.035  -8.599  56.701 1.00 18.79 ? 833  LEU   B CA  1 
ATOM   3450 C C   . LEU   B 1 141 ? 36.389  -9.212  56.492 1.00 18.42 ? 833  LEU   B C   1 
ATOM   3451 O O   . LEU   B 1 141 ? 37.057  -8.932  55.507 1.00 18.78 ? 833  LEU   B O   1 
ATOM   3452 C CB  . LEU   B 1 141 ? 34.020  -9.206  55.728 1.00 18.68 ? 833  LEU   B CB  1 
ATOM   3453 C CG  . LEU   B 1 141 ? 32.601  -8.690  55.891 1.00 20.19 ? 833  LEU   B CG  1 
ATOM   3454 C CD1 . LEU   B 1 141 ? 31.736  -9.151  54.770 1.00 20.88 ? 833  LEU   B CD1 1 
ATOM   3455 C CD2 . LEU   B 1 141 ? 32.014  -9.096  57.234 1.00 20.75 ? 833  LEU   B CD2 1 
ATOM   3456 N N   . VAL   B 1 142 ? 36.797  -10.054 57.417 1.00 17.55 ? 834  VAL   B N   1 
ATOM   3457 C CA  . VAL   B 1 142 ? 38.066  -10.756 57.319 1.00 16.91 ? 834  VAL   B CA  1 
ATOM   3458 C C   . VAL   B 1 142 ? 37.754  -12.186 56.894 1.00 16.03 ? 834  VAL   B C   1 
ATOM   3459 O O   . VAL   B 1 142 ? 36.895  -12.815 57.495 1.00 15.85 ? 834  VAL   B O   1 
ATOM   3460 C CB  . VAL   B 1 142 ? 38.899  -10.663 58.635 1.00 17.25 ? 834  VAL   B CB  1 
ATOM   3461 C CG1 . VAL   B 1 142 ? 40.181  -11.478 58.525 1.00 17.77 ? 834  VAL   B CG1 1 
ATOM   3462 C CG2 . VAL   B 1 142 ? 39.230  -9.207  58.958 1.00 17.09 ? 834  VAL   B CG2 1 
ATOM   3463 N N   . HIS   B 1 143 ? 38.378  -12.658 55.795 1.00 15.50 ? 835  HIS   B N   1 
ATOM   3464 C CA  . HIS   B 1 143 ? 38.159  -14.012 55.258 1.00 15.19 ? 835  HIS   B CA  1 
ATOM   3465 C C   . HIS   B 1 143 ? 38.785  -15.060 56.189 1.00 15.84 ? 835  HIS   B C   1 
ATOM   3466 O O   . HIS   B 1 143 ? 38.147  -16.059 56.495 1.00 15.40 ? 835  HIS   B O   1 
ATOM   3467 C CB  . HIS   B 1 143 ? 38.683  -14.159 53.789 1.00 13.55 ? 835  HIS   B CB  1 
ATOM   3468 C CG  . HIS   B 1 143 ? 38.306  -15.461 53.127 1.00 12.38 ? 835  HIS   B CG  1 
ATOM   3469 N ND1 . HIS   B 1 143 ? 38.889  -16.658 53.501 1.00 12.91 ? 835  HIS   B ND1 1 
ATOM   3470 C CD2 . HIS   B 1 143 ? 37.418  -15.713 52.134 1.00 12.34 ? 835  HIS   B CD2 1 
ATOM   3471 C CE1 . HIS   B 1 143 ? 38.337  -17.591 52.744 1.00 12.03 ? 835  HIS   B CE1 1 
ATOM   3472 N NE2 . HIS   B 1 143 ? 37.454  -17.077 51.905 1.00 12.18 ? 835  HIS   B NE2 1 
ATOM   3473 N N   . ARG   B 1 144 ? 40.028  -14.822 56.630 1.00 17.19 ? 836  ARG   B N   1 
ATOM   3474 C CA  . ARG   B 1 144 ? 40.765  -15.714 57.534 1.00 18.90 ? 836  ARG   B CA  1 
ATOM   3475 C C   . ARG   B 1 144 ? 41.350  -16.957 56.845 1.00 19.73 ? 836  ARG   B C   1 
ATOM   3476 O O   . ARG   B 1 144 ? 42.172  -17.641 57.453 1.00 20.87 ? 836  ARG   B O   1 
ATOM   3477 C CB  . ARG   B 1 144 ? 39.937  -16.133 58.775 1.00 21.19 ? 836  ARG   B CB  1 
ATOM   3478 C CG  . ARG   B 1 144 ? 39.597  -15.018 59.741 1.00 25.39 ? 836  ARG   B CG  1 
ATOM   3479 C CD  . ARG   B 1 144 ? 38.680  -15.525 60.835 1.00 31.67 ? 836  ARG   B CD  1 
ATOM   3480 N NE  . ARG   B 1 144 ? 38.901  -14.856 62.120 1.00 38.48 ? 836  ARG   B NE  1 
ATOM   3481 C CZ  . ARG   B 1 144 ? 38.325  -13.709 62.486 1.00 43.15 ? 836  ARG   B CZ  1 
ATOM   3482 N NH1 . ARG   B 1 144 ? 37.484  -13.087 61.667 1.00 42.80 ? 836  ARG   B NH1 1 
ATOM   3483 N NH2 . ARG   B 1 144 ? 38.597  -13.169 63.667 1.00 44.44 ? 836  ARG   B NH2 1 
ATOM   3484 N N   . ASP   B 1 145 ? 40.986  -17.223 55.581 1.00 18.72 ? 837  ASP   B N   1 
ATOM   3485 C CA  . ASP   B 1 145 ? 41.465  -18.416 54.898 1.00 17.86 ? 837  ASP   B CA  1 
ATOM   3486 C C   . ASP   B 1 145 ? 41.683  -18.240 53.386 1.00 16.93 ? 837  ASP   B C   1 
ATOM   3487 O O   . ASP   B 1 145 ? 41.246  -19.085 52.598 1.00 17.93 ? 837  ASP   B O   1 
ATOM   3488 C CB  . ASP   B 1 145 ? 40.504  -19.595 55.188 1.00 18.60 ? 837  ASP   B CB  1 
ATOM   3489 C CG  . ASP   B 1 145 ? 41.107  -20.962 54.976 1.00 22.29 ? 837  ASP   B CG  1 
ATOM   3490 O OD1 . ASP   B 1 145 ? 42.335  -21.044 54.715 1.00 22.98 ? 837  ASP   B OD1 1 
ATOM   3491 O OD2 . ASP   B 1 145 ? 40.361  -21.956 55.063 1.00 24.50 ? 837  ASP   B OD2 1 
ATOM   3492 N N   . LEU   B 1 146 ? 42.331  -17.166 52.979 1.00 15.33 ? 838  LEU   B N   1 
ATOM   3493 C CA  . LEU   B 1 146 ? 42.589  -16.942 51.554 1.00 15.21 ? 838  LEU   B CA  1 
ATOM   3494 C C   . LEU   B 1 146 ? 43.730  -17.869 51.116 1.00 15.37 ? 838  LEU   B C   1 
ATOM   3495 O O   . LEU   B 1 146 ? 44.782  -17.936 51.769 1.00 14.55 ? 838  LEU   B O   1 
ATOM   3496 C CB  . LEU   B 1 146 ? 42.899  -15.468 51.261 1.00 14.82 ? 838  LEU   B CB  1 
ATOM   3497 C CG  . LEU   B 1 146 ? 43.257  -15.127 49.823 1.00 16.14 ? 838  LEU   B CG  1 
ATOM   3498 C CD1 . LEU   B 1 146 ? 42.166  -15.560 48.831 1.00 15.65 ? 838  LEU   B CD1 1 
ATOM   3499 C CD2 . LEU   B 1 146 ? 43.447  -13.621 49.684 1.00 17.54 ? 838  LEU   B CD2 1 
ATOM   3500 N N   . ALA   B 1 147 ? 43.474  -18.643 50.068 1.00 15.42 ? 839  ALA   B N   1 
ATOM   3501 C CA  . ALA   B 1 147 ? 44.396  -19.630 49.521 1.00 16.26 ? 839  ALA   B CA  1 
ATOM   3502 C C   . ALA   B 1 147 ? 43.934  -19.983 48.096 1.00 17.64 ? 839  ALA   B C   1 
ATOM   3503 O O   . ALA   B 1 147 ? 42.770  -19.732 47.765 1.00 17.73 ? 839  ALA   B O   1 
ATOM   3504 C CB  . ALA   B 1 147 ? 44.382  -20.870 50.392 1.00 16.11 ? 839  ALA   B CB  1 
ATOM   3505 N N   . ALA   B 1 148 ? 44.811  -20.582 47.253 1.00 17.84 ? 840  ALA   B N   1 
ATOM   3506 C CA  . ALA   B 1 148 ? 44.402  -20.943 45.891 1.00 19.07 ? 840  ALA   B CA  1 
ATOM   3507 C C   . ALA   B 1 148 ? 43.317  -22.063 45.836 1.00 20.16 ? 840  ALA   B C   1 
ATOM   3508 O O   . ALA   B 1 148 ? 42.610  -22.176 44.840 1.00 20.47 ? 840  ALA   B O   1 
ATOM   3509 C CB  . ALA   B 1 148 ? 45.614  -21.294 45.029 1.00 18.97 ? 840  ALA   B CB  1 
ATOM   3510 N N   . ARG   B 1 149 ? 43.167  -22.861 46.904 1.00 20.54 ? 841  ARG   B N   1 
ATOM   3511 C CA  . ARG   B 1 149 ? 42.109  -23.878 46.971 1.00 21.40 ? 841  ARG   B CA  1 
ATOM   3512 C C   . ARG   B 1 149 ? 40.719  -23.238 47.298 1.00 20.78 ? 841  ARG   B C   1 
ATOM   3513 O O   . ARG   B 1 149 ? 39.687  -23.889 47.136 1.00 20.33 ? 841  ARG   B O   1 
ATOM   3514 C CB  . ARG   B 1 149 ? 42.457  -24.949 48.026 1.00 24.00 ? 841  ARG   B CB  1 
ATOM   3515 C CG  . ARG   B 1 149 ? 42.469  -24.376 49.436 1.00 29.47 ? 841  ARG   B CG  1 
ATOM   3516 C CD  . ARG   B 1 149 ? 42.860  -25.375 50.495 1.00 34.76 ? 841  ARG   B CD  1 
ATOM   3517 N NE  . ARG   B 1 149 ? 42.101  -25.148 51.720 1.00 40.41 ? 841  ARG   B NE  1 
ATOM   3518 C CZ  . ARG   B 1 149 ? 42.469  -24.320 52.695 1.00 44.78 ? 841  ARG   B CZ  1 
ATOM   3519 N NH1 . ARG   B 1 149 ? 41.706  -24.177 53.776 1.00 45.07 ? 841  ARG   B NH1 1 
ATOM   3520 N NH2 . ARG   B 1 149 ? 43.607  -23.639 52.605 1.00 45.00 ? 841  ARG   B NH2 1 
ATOM   3521 N N   . ASN   B 1 150 ? 40.713  -21.980 47.791 1.00 20.59 ? 842  ASN   B N   1 
ATOM   3522 C CA  . ASN   B 1 150 ? 39.528  -21.180 48.117 1.00 20.56 ? 842  ASN   B CA  1 
ATOM   3523 C C   . ASN   B 1 150 ? 39.283  -20.065 47.094 1.00 19.18 ? 842  ASN   B C   1 
ATOM   3524 O O   . ASN   B 1 150 ? 38.697  -19.056 47.428 1.00 19.20 ? 842  ASN   B O   1 
ATOM   3525 C CB  . ASN   B 1 150 ? 39.624  -20.599 49.532 1.00 23.06 ? 842  ASN   B CB  1 
ATOM   3526 C CG  . ASN   B 1 150 ? 39.402  -21.645 50.594 1.00 28.78 ? 842  ASN   B CG  1 
ATOM   3527 O OD1 . ASN   B 1 150 ? 38.722  -22.658 50.369 1.00 32.00 ? 842  ASN   B OD1 1 
ATOM   3528 N ND2 . ASN   B 1 150 ? 39.965  -21.441 51.768 1.00 29.09 ? 842  ASN   B ND2 1 
ATOM   3529 N N   . VAL   B 1 151 ? 39.762  -20.239 45.859 1.00 18.28 ? 843  VAL   B N   1 
ATOM   3530 C CA  . VAL   B 1 151 ? 39.516  -19.326 44.754 1.00 17.80 ? 843  VAL   B CA  1 
ATOM   3531 C C   . VAL   B 1 151 ? 38.998  -20.233 43.640 1.00 18.38 ? 843  VAL   B C   1 
ATOM   3532 O O   . VAL   B 1 151 ? 39.716  -21.157 43.251 1.00 18.82 ? 843  VAL   B O   1 
ATOM   3533 C CB  . VAL   B 1 151 ? 40.740  -18.528 44.259 1.00 17.15 ? 843  VAL   B CB  1 
ATOM   3534 C CG1 . VAL   B 1 151 ? 40.368  -17.750 43.003 1.00 17.37 ? 843  VAL   B CG1 1 
ATOM   3535 C CG2 . VAL   B 1 151 ? 41.289  -17.603 45.335 1.00 15.96 ? 843  VAL   B CG2 1 
ATOM   3536 N N   . LEU   B 1 152 ? 37.745  -20.010 43.164 1.00 17.09 ? 844  LEU   B N   1 
ATOM   3537 C CA  . LEU   B 1 152 ? 37.136  -20.836 42.133 1.00 16.74 ? 844  LEU   B CA  1 
ATOM   3538 C C   . LEU   B 1 152 ? 37.156  -20.211 40.768 1.00 15.96 ? 844  LEU   B C   1 
ATOM   3539 O O   . LEU   B 1 152 ? 37.085  -18.992 40.638 1.00 16.30 ? 844  LEU   B O   1 
ATOM   3540 C CB  . LEU   B 1 152 ? 35.693  -21.177 42.502 1.00 17.47 ? 844  LEU   B CB  1 
ATOM   3541 C CG  . LEU   B 1 152 ? 35.472  -21.794 43.865 1.00 20.38 ? 844  LEU   B CG  1 
ATOM   3542 C CD1 . LEU   B 1 152 ? 34.038  -22.184 44.021 1.00 21.38 ? 844  LEU   B CD1 1 
ATOM   3543 C CD2 . LEU   B 1 152 ? 36.318  -23.035 44.063 1.00 21.49 ? 844  LEU   B CD2 1 
ATOM   3544 N N   . VAL   B 1 153 ? 37.206  -21.047 39.739 1.00 15.10 ? 845  VAL   B N   1 
ATOM   3545 C CA  . VAL   B 1 153 ? 37.182  -20.592 38.346 1.00 14.85 ? 845  VAL   B CA  1 
ATOM   3546 C C   . VAL   B 1 153 ? 35.740  -20.617 37.826 1.00 13.91 ? 845  VAL   B C   1 
ATOM   3547 O O   . VAL   B 1 153 ? 35.167  -21.700 37.744 1.00 13.44 ? 845  VAL   B O   1 
ATOM   3548 C CB  . VAL   B 1 153 ? 38.078  -21.503 37.475 1.00 15.51 ? 845  VAL   B CB  1 
ATOM   3549 C CG1 . VAL   B 1 153 ? 37.927  -21.188 35.994 1.00 15.98 ? 845  VAL   B CG1 1 
ATOM   3550 C CG2 . VAL   B 1 153 ? 39.533  -21.419 37.903 1.00 15.91 ? 845  VAL   B CG2 1 
ATOM   3551 N N   . LYS   B 1 154 ? 35.152  -19.431 37.490 1.00 13.27 ? 846  LYS   B N   1 
ATOM   3552 C CA  . LYS   B 1 154 ? 33.795  -19.288 36.895 1.00 12.93 ? 846  LYS   B CA  1 
ATOM   3553 C C   . LYS   B 1 154 ? 33.940  -19.607 35.369 1.00 14.66 ? 846  LYS   B C   1 
ATOM   3554 O O   . LYS   B 1 154 ? 33.166  -20.370 34.786 1.00 15.63 ? 846  LYS   B O   1 
ATOM   3555 C CB  . LYS   B 1 154 ? 33.245  -17.864 37.144 1.00 12.23 ? 846  LYS   B CB  1 
ATOM   3556 C CG  . LYS   B 1 154 ? 31.890  -17.544 36.511 1.00 14.74 ? 846  LYS   B CG  1 
ATOM   3557 C CD  . LYS   B 1 154 ? 30.717  -17.769 37.450 1.00 16.47 ? 846  LYS   B CD  1 
ATOM   3558 C CE  . LYS   B 1 154 ? 29.383  -17.489 36.820 1.00 18.47 ? 846  LYS   B CE  1 
ATOM   3559 N NZ  . LYS   B 1 154 ? 28.833  -16.176 37.248 1.00 20.48 ? 846  LYS   B NZ  1 
ATOM   3560 N N   . THR   B 1 155 ? 34.953  -19.026 34.751 1.00 14.82 ? 847  THR   B N   1 
ATOM   3561 C CA  . THR   B 1 155 ? 35.470  -19.253 33.399 1.00 15.68 ? 847  THR   B CA  1 
ATOM   3562 C C   . THR   B 1 155 ? 36.996  -19.011 33.585 1.00 17.73 ? 847  THR   B C   1 
ATOM   3563 O O   . THR   B 1 155 ? 37.392  -18.332 34.550 1.00 17.66 ? 847  THR   B O   1 
ATOM   3564 C CB  . THR   B 1 155 ? 34.932  -18.228 32.355 1.00 15.63 ? 847  THR   B CB  1 
ATOM   3565 O OG1 . THR   B 1 155 ? 35.459  -16.918 32.591 1.00 16.15 ? 847  THR   B OG1 1 
ATOM   3566 C CG2 . THR   B 1 155 ? 33.422  -18.190 32.242 1.00 16.02 ? 847  THR   B CG2 1 
ATOM   3567 N N   . PRO   B 1 156 ? 37.850  -19.404 32.620 1.00 18.47 ? 848  PRO   B N   1 
ATOM   3568 C CA  . PRO   B 1 156 ? 39.280  -19.095 32.751 1.00 18.65 ? 848  PRO   B CA  1 
ATOM   3569 C C   . PRO   B 1 156 ? 39.578  -17.601 32.888 1.00 19.01 ? 848  PRO   B C   1 
ATOM   3570 O O   . PRO   B 1 156 ? 40.631  -17.242 33.384 1.00 19.34 ? 848  PRO   B O   1 
ATOM   3571 C CB  . PRO   B 1 156 ? 39.883  -19.672 31.467 1.00 19.96 ? 848  PRO   B CB  1 
ATOM   3572 C CG  . PRO   B 1 156 ? 38.922  -20.777 31.062 1.00 20.71 ? 848  PRO   B CG  1 
ATOM   3573 C CD  . PRO   B 1 156 ? 37.571  -20.199 31.408 1.00 18.69 ? 848  PRO   B CD  1 
ATOM   3574 N N   . GLN   B 1 157 ? 38.664  -16.727 32.463 1.00 19.20 ? 849  GLN   B N   1 
ATOM   3575 C CA  . GLN   B 1 157 ? 38.862  -15.275 32.553 1.00 19.54 ? 849  GLN   B CA  1 
ATOM   3576 C C   . GLN   B 1 157 ? 38.137  -14.654 33.766 1.00 18.14 ? 849  GLN   B C   1 
ATOM   3577 O O   . GLN   B 1 157 ? 38.137  -13.430 33.885 1.00 19.11 ? 849  GLN   B O   1 
ATOM   3578 C CB  . GLN   B 1 157 ? 38.355  -14.587 31.272 1.00 23.34 ? 849  GLN   B CB  1 
ATOM   3579 C CG  . GLN   B 1 157 ? 38.755  -15.272 29.951 1.00 32.39 ? 849  GLN   B CG  1 
ATOM   3580 C CD  . GLN   B 1 157 ? 37.935  -16.517 29.559 1.00 42.81 ? 849  GLN   B CD  1 
ATOM   3581 O OE1 . GLN   B 1 157 ? 36.690  -16.560 29.645 1.00 45.01 ? 849  GLN   B OE1 1 
ATOM   3582 N NE2 . GLN   B 1 157 ? 38.627  -17.569 29.108 1.00 45.04 ? 849  GLN   B NE2 1 
ATOM   3583 N N   . HIS   B 1 158 ? 37.493  -15.463 34.636 1.00 15.56 ? 850  HIS   B N   1 
ATOM   3584 C CA  . HIS   B 1 158 ? 36.727  -14.931 35.764 1.00 14.57 ? 850  HIS   B CA  1 
ATOM   3585 C C   . HIS   B 1 158 ? 36.844  -15.860 36.972 1.00 14.10 ? 850  HIS   B C   1 
ATOM   3586 O O   . HIS   B 1 158 ? 36.377  -16.994 36.921 1.00 14.04 ? 850  HIS   B O   1 
ATOM   3587 C CB  . HIS   B 1 158 ? 35.242  -14.758 35.334 1.00 14.58 ? 850  HIS   B CB  1 
ATOM   3588 C CG  . HIS   B 1 158 ? 34.351  -14.151 36.373 1.00 16.04 ? 850  HIS   B CG  1 
ATOM   3589 N ND1 . HIS   B 1 158 ? 33.049  -13.828 36.090 1.00 18.36 ? 850  HIS   B ND1 1 
ATOM   3590 C CD2 . HIS   B 1 158 ? 34.601  -13.833 37.663 1.00 16.79 ? 850  HIS   B CD2 1 
ATOM   3591 C CE1 . HIS   B 1 158 ? 32.546  -13.333 37.206 1.00 18.46 ? 850  HIS   B CE1 1 
ATOM   3592 N NE2 . HIS   B 1 158 ? 33.451  -13.306 38.171 1.00 17.99 ? 850  HIS   B NE2 1 
ATOM   3593 N N   . VAL   B 1 159 ? 37.499  -15.402 38.047 1.00 13.84 ? 851  VAL   B N   1 
ATOM   3594 C CA  . VAL   B 1 159 ? 37.687  -16.185 39.274 1.00 13.73 ? 851  VAL   B CA  1 
ATOM   3595 C C   . VAL   B 1 159 ? 37.004  -15.503 40.463 1.00 13.69 ? 851  VAL   B C   1 
ATOM   3596 O O   . VAL   B 1 159 ? 36.805  -14.279 40.443 1.00 14.21 ? 851  VAL   B O   1 
ATOM   3597 C CB  . VAL   B 1 159 ? 39.183  -16.453 39.549 1.00 14.49 ? 851  VAL   B CB  1 
ATOM   3598 C CG1 . VAL   B 1 159 ? 39.789  -17.355 38.477 1.00 15.21 ? 851  VAL   B CG1 1 
ATOM   3599 C CG2 . VAL   B 1 159 ? 39.962  -15.141 39.648 1.00 14.99 ? 851  VAL   B CG2 1 
ATOM   3600 N N   . LYS   B 1 160 ? 36.651  -16.272 41.505 1.00 12.98 ? 852  LYS   B N   1 
ATOM   3601 C CA  . LYS   B 1 160 ? 35.915  -15.736 42.660 1.00 13.36 ? 852  LYS   B CA  1 
ATOM   3602 C C   . LYS   B 1 160 ? 36.360  -16.390 43.974 1.00 14.57 ? 852  LYS   B C   1 
ATOM   3603 O O   . LYS   B 1 160 ? 36.509  -17.616 44.023 1.00 15.87 ? 852  LYS   B O   1 
ATOM   3604 C CB  . LYS   B 1 160 ? 34.381  -16.000 42.491 1.00 13.80 ? 852  LYS   B CB  1 
ATOM   3605 C CG  . LYS   B 1 160 ? 33.766  -15.437 41.206 1.00 16.10 ? 852  LYS   B CG  1 
ATOM   3606 C CD  . LYS   B 1 160 ? 32.284  -15.796 40.988 1.00 19.24 ? 852  LYS   B CD  1 
ATOM   3607 C CE  . LYS   B 1 160 ? 31.358  -15.270 42.056 1.00 23.27 ? 852  LYS   B CE  1 
ATOM   3608 N NZ  . LYS   B 1 160 ? 29.918  -15.617 41.782 1.00 26.88 ? 852  LYS   B NZ  1 
ATOM   3609 N N   . ILE   B 1 161 ? 36.490  -15.608 45.052 1.00 13.56 ? 853  ILE   B N   1 
ATOM   3610 C CA  . ILE   B 1 161 ? 36.854  -16.162 46.346 1.00 14.27 ? 853  ILE   B CA  1 
ATOM   3611 C C   . ILE   B 1 161 ? 35.691  -16.881 46.986 1.00 13.99 ? 853  ILE   B C   1 
ATOM   3612 O O   . ILE   B 1 161 ? 34.628  -16.297 47.168 1.00 13.76 ? 853  ILE   B O   1 
ATOM   3613 C CB  . ILE   B 1 161 ? 37.452  -15.070 47.271 1.00 16.14 ? 853  ILE   B CB  1 
ATOM   3614 C CG1 . ILE   B 1 161 ? 38.644  -14.361 46.582 1.00 17.82 ? 853  ILE   B CG1 1 
ATOM   3615 C CG2 . ILE   B 1 161 ? 37.880  -15.636 48.629 1.00 16.34 ? 853  ILE   B CG2 1 
ATOM   3616 C CD1 . ILE   B 1 161 ? 38.662  -12.853 46.859 1.00 19.94 ? 853  ILE   B CD1 1 
ATOM   3617 N N   . THR   B 1 162 ? 35.885  -18.158 47.342 1.00 14.52 ? 854  THR   B N   1 
ATOM   3618 C CA  . THR   B 1 162 ? 34.838  -18.945 48.002 1.00 15.51 ? 854  THR   B CA  1 
ATOM   3619 C C   . THR   B 1 162 ? 35.137  -19.160 49.533 1.00 17.04 ? 854  THR   B C   1 
ATOM   3620 O O   . THR   B 1 162 ? 36.179  -18.717 50.041 1.00 16.58 ? 854  THR   B O   1 
ATOM   3621 C CB  . THR   B 1 162 ? 34.638  -20.255 47.254 1.00 17.39 ? 854  THR   B CB  1 
ATOM   3622 O OG1 . THR   B 1 162 ? 33.465  -20.844 47.779 1.00 19.84 ? 854  THR   B OG1 1 
ATOM   3623 C CG2 . THR   B 1 162 ? 35.795  -21.234 47.472 1.00 17.72 ? 854  THR   B CG2 1 
ATOM   3624 N N   . ASP   B 1 163 ? 34.192  -19.780 50.256 1.00 18.47 ? 855  ASP   B N   1 
ATOM   3625 C CA  . ASP   B 1 163 ? 34.307  -20.154 51.651 1.00 20.52 ? 855  ASP   B CA  1 
ATOM   3626 C C   . ASP   B 1 163 ? 34.414  -18.999 52.620 1.00 21.63 ? 855  ASP   B C   1 
ATOM   3627 O O   . ASP   B 1 163 ? 34.920  -19.207 53.722 1.00 21.74 ? 855  ASP   B O   1 
ATOM   3628 C CB  . ASP   B 1 163 ? 35.469  -21.150 51.870 1.00 23.52 ? 855  ASP   B CB  1 
ATOM   3629 C CG  . ASP   B 1 163 ? 35.202  -22.543 51.316 1.00 31.62 ? 855  ASP   B CG  1 
ATOM   3630 O OD1 . ASP   B 1 163 ? 34.035  -22.840 50.981 1.00 32.48 ? 855  ASP   B OD1 1 
ATOM   3631 O OD2 . ASP   B 1 163 ? 36.159  -23.338 51.224 1.00 36.57 ? 855  ASP   B OD2 1 
ATOM   3632 N N   . PHE   B 1 164 ? 33.876  -17.808 52.277 1.00 22.41 ? 856  PHE   B N   1 
ATOM   3633 C CA  . PHE   B 1 164 ? 33.889  -16.691 53.233 1.00 23.29 ? 856  PHE   B CA  1 
ATOM   3634 C C   . PHE   B 1 164 ? 33.002  -17.062 54.433 1.00 24.04 ? 856  PHE   B C   1 
ATOM   3635 O O   . PHE   B 1 164 ? 31.897  -17.541 54.236 1.00 23.27 ? 856  PHE   B O   1 
ATOM   3636 C CB  . PHE   B 1 164 ? 33.364  -15.381 52.608 1.00 23.20 ? 856  PHE   B CB  1 
ATOM   3637 C CG  . PHE   B 1 164 ? 33.247  -14.320 53.676 1.00 23.99 ? 856  PHE   B CG  1 
ATOM   3638 C CD1 . PHE   B 1 164 ? 34.375  -13.712 54.191 1.00 24.79 ? 856  PHE   B CD1 1 
ATOM   3639 C CD2 . PHE   B 1 164 ? 32.028  -14.040 54.263 1.00 25.09 ? 856  PHE   B CD2 1 
ATOM   3640 C CE1 . PHE   B 1 164 ? 34.283  -12.834 55.257 1.00 25.89 ? 856  PHE   B CE1 1 
ATOM   3641 C CE2 . PHE   B 1 164 ? 31.936  -13.156 55.327 1.00 25.96 ? 856  PHE   B CE2 1 
ATOM   3642 C CZ  . PHE   B 1 164 ? 33.063  -12.572 55.828 1.00 26.05 ? 856  PHE   B CZ  1 
ATOM   3643 N N   . GLY   B 1 165 ? 33.488  -16.823 55.646 1.00 25.29 ? 857  GLY   B N   1 
ATOM   3644 C CA  . GLY   B 1 165 ? 32.712  -17.099 56.841 1.00 27.00 ? 857  GLY   B CA  1 
ATOM   3645 C C   . GLY   B 1 165 ? 32.834  -18.503 57.383 1.00 29.36 ? 857  GLY   B C   1 
ATOM   3646 O O   . GLY   B 1 165 ? 32.389  -18.757 58.498 1.00 30.31 ? 857  GLY   B O   1 
ATOM   3647 N N   . LEU   B 1 166 ? 33.434  -19.426 56.626 1.00 30.53 ? 858  LEU   B N   1 
ATOM   3648 C CA  . LEU   B 1 166 ? 33.587  -20.805 57.071 1.00 32.36 ? 858  LEU   B CA  1 
ATOM   3649 C C   . LEU   B 1 166 ? 34.522  -20.933 58.264 1.00 33.90 ? 858  LEU   B C   1 
ATOM   3650 O O   . LEU   B 1 166 ? 34.093  -21.445 59.279 1.00 34.14 ? 858  LEU   B O   1 
ATOM   3651 C CB  . LEU   B 1 166 ? 34.046  -21.705 55.919 1.00 33.15 ? 858  LEU   B CB  1 
ATOM   3652 C CG  . LEU   B 1 166 ? 33.215  -22.950 55.692 1.00 35.50 ? 858  LEU   B CG  1 
ATOM   3653 C CD1 . LEU   B 1 166 ? 31.803  -22.590 55.330 1.00 36.14 ? 858  LEU   B CD1 1 
ATOM   3654 C CD2 . LEU   B 1 166 ? 33.797  -23.790 54.578 1.00 36.67 ? 858  LEU   B CD2 1 
ATOM   3655 N N   . ALA   B 1 167 ? 35.767  -20.421 58.172 1.00 35.00 ? 859  ALA   B N   1 
ATOM   3656 C CA  . ALA   B 1 167 ? 36.764  -20.455 59.247 1.00 36.64 ? 859  ALA   B CA  1 
ATOM   3657 C C   . ALA   B 1 167 ? 36.181  -20.020 60.614 1.00 39.03 ? 859  ALA   B C   1 
ATOM   3658 O O   . ALA   B 1 167 ? 36.340  -20.745 61.604 1.00 39.11 ? 859  ALA   B O   1 
ATOM   3659 C CB  . ALA   B 1 167 ? 37.959  -19.583 58.878 1.00 36.37 ? 859  ALA   B CB  1 
ATOM   3660 N N   . LYS   B 1 168 ? 35.454  -18.868 60.640 1.00 40.44 ? 860  LYS   B N   1 
ATOM   3661 C CA  . LYS   B 1 168 ? 34.829  -18.313 61.838 1.00 42.09 ? 860  LYS   B CA  1 
ATOM   3662 C C   . LYS   B 1 168 ? 33.673  -19.189 62.330 1.00 43.09 ? 860  LYS   B C   1 
ATOM   3663 O O   . LYS   B 1 168 ? 33.563  -19.442 63.530 1.00 43.15 ? 860  LYS   B O   1 
ATOM   3664 C CB  . LYS   B 1 168 ? 34.337  -16.876 61.570 1.00 44.02 ? 860  LYS   B CB  1 
ATOM   3665 C CG  . LYS   B 1 168 ? 33.931  -16.109 62.817 1.00 48.22 ? 860  LYS   B CG  1 
ATOM   3666 C CD  . LYS   B 1 168 ? 33.272  -14.800 62.442 1.00 53.06 ? 860  LYS   B CD  1 
ATOM   3667 C CE  . LYS   B 1 168 ? 33.022  -13.912 63.636 1.00 56.88 ? 860  LYS   B CE  1 
ATOM   3668 N NZ  . LYS   B 1 168 ? 31.918  -12.950 63.376 1.00 58.70 ? 860  LYS   B NZ  1 
ATOM   3669 N N   . LEU   B 1 169 ? 32.827  -19.657 61.410 1.00 43.78 ? 861  LEU   B N   1 
ATOM   3670 C CA  . LEU   B 1 169 ? 31.678  -20.488 61.751 1.00 45.12 ? 861  LEU   B CA  1 
ATOM   3671 C C   . LEU   B 1 169 ? 32.082  -21.832 62.366 1.00 46.38 ? 861  LEU   B C   1 
ATOM   3672 O O   . LEU   B 1 169 ? 31.486  -22.252 63.360 1.00 46.68 ? 861  LEU   B O   1 
ATOM   3673 C CB  . LEU   B 1 169 ? 30.791  -20.694 60.521 1.00 45.31 ? 861  LEU   B CB  1 
ATOM   3674 C CG  . LEU   B 1 169 ? 29.493  -21.478 60.736 1.00 47.07 ? 861  LEU   B CG  1 
ATOM   3675 C CD1 . LEU   B 1 169 ? 28.623  -20.841 61.829 1.00 47.83 ? 861  LEU   B CD1 1 
ATOM   3676 C CD2 . LEU   B 1 169 ? 28.715  -21.614 59.432 1.00 47.41 ? 861  LEU   B CD2 1 
ATOM   3677 N N   . LEU   B 1 170 ? 33.106  -22.490 61.805 1.00 46.65 ? 862  LEU   B N   1 
ATOM   3678 C CA  . LEU   B 1 170 ? 33.551  -23.778 62.319 1.00 47.55 ? 862  LEU   B CA  1 
ATOM   3679 C C   . LEU   B 1 170 ? 34.742  -23.633 63.248 1.00 48.35 ? 862  LEU   B C   1 
ATOM   3680 O O   . LEU   B 1 170 ? 34.691  -24.114 64.377 1.00 48.79 ? 862  LEU   B O   1 
ATOM   3681 C CB  . LEU   B 1 170 ? 33.882  -24.747 61.186 1.00 48.08 ? 862  LEU   B CB  1 
ATOM   3682 C CG  . LEU   B 1 170 ? 32.692  -25.283 60.408 1.00 50.24 ? 862  LEU   B CG  1 
ATOM   3683 C CD1 . LEU   B 1 170 ? 32.446  -24.452 59.170 1.00 51.04 ? 862  LEU   B CD1 1 
ATOM   3684 C CD2 . LEU   B 1 170 ? 32.906  -26.751 60.014 1.00 51.05 ? 862  LEU   B CD2 1 
ATOM   3685 N N   . PRO   B 1 185 ? 45.614  -23.691 58.535 1.00 25.07 ? 877  PRO   B N   1 
ATOM   3686 C CA  . PRO   B 1 185 ? 46.407  -23.251 57.372 1.00 25.31 ? 877  PRO   B CA  1 
ATOM   3687 C C   . PRO   B 1 185 ? 47.649  -22.444 57.776 1.00 25.33 ? 877  PRO   B C   1 
ATOM   3688 O O   . PRO   B 1 185 ? 47.847  -21.334 57.288 1.00 25.64 ? 877  PRO   B O   1 
ATOM   3689 C CB  . PRO   B 1 185 ? 45.414  -22.387 56.589 1.00 25.67 ? 877  PRO   B CB  1 
ATOM   3690 C CG  . PRO   B 1 185 ? 44.552  -21.777 57.656 1.00 26.09 ? 877  PRO   B CG  1 
ATOM   3691 C CD  . PRO   B 1 185 ? 44.475  -22.784 58.789 1.00 24.65 ? 877  PRO   B CD  1 
ATOM   3692 N N   . ILE   B 1 186 ? 48.495  -23.001 58.661 1.00 24.84 ? 878  ILE   B N   1 
ATOM   3693 C CA  . ILE   B 1 186 ? 49.690  -22.294 59.133 1.00 23.89 ? 878  ILE   B CA  1 
ATOM   3694 C C   . ILE   B 1 186 ? 50.589  -21.788 57.980 1.00 22.34 ? 878  ILE   B C   1 
ATOM   3695 O O   . ILE   B 1 186 ? 51.027  -20.632 58.028 1.00 22.34 ? 878  ILE   B O   1 
ATOM   3696 C CB  . ILE   B 1 186 ? 50.457  -23.146 60.182 1.00 24.51 ? 878  ILE   B CB  1 
ATOM   3697 C CG1 . ILE   B 1 186 ? 49.664  -23.167 61.503 1.00 25.52 ? 878  ILE   B CG1 1 
ATOM   3698 C CG2 . ILE   B 1 186 ? 51.872  -22.601 60.449 1.00 24.76 ? 878  ILE   B CG2 1 
ATOM   3699 C CD1 . ILE   B 1 186 ? 49.693  -24.425 62.174 1.00 27.06 ? 878  ILE   B CD1 1 
ATOM   3700 N N   . LYS   B 1 187 ? 50.769  -22.583 56.915 1.00 21.32 ? 879  LYS   B N   1 
ATOM   3701 C CA  . LYS   B 1 187 ? 51.619  -22.203 55.763 1.00 21.07 ? 879  LYS   B CA  1 
ATOM   3702 C C   . LYS   B 1 187 ? 51.121  -20.968 54.979 1.00 21.18 ? 879  LYS   B C   1 
ATOM   3703 O O   . LYS   B 1 187 ? 51.912  -20.315 54.312 1.00 21.26 ? 879  LYS   B O   1 
ATOM   3704 C CB  . LYS   B 1 187 ? 51.846  -23.394 54.829 1.00 22.17 ? 879  LYS   B CB  1 
ATOM   3705 C CG  . LYS   B 1 187 ? 52.353  -24.633 55.579 1.00 25.31 ? 879  LYS   B CG  1 
ATOM   3706 C CD  . LYS   B 1 187 ? 53.557  -25.297 54.953 1.00 28.71 ? 879  LYS   B CD  1 
ATOM   3707 C CE  . LYS   B 1 187 ? 53.963  -26.493 55.783 1.00 33.17 ? 879  LYS   B CE  1 
ATOM   3708 N NZ  . LYS   B 1 187 ? 54.562  -27.580 54.957 1.00 35.54 ? 879  LYS   B NZ  1 
ATOM   3709 N N   . TRP   B 1 188 ? 49.851  -20.590 55.154 1.00 21.16 ? 880  TRP   B N   1 
ATOM   3710 C CA  . TRP   B 1 188 ? 49.251  -19.399 54.542 1.00 21.62 ? 880  TRP   B CA  1 
ATOM   3711 C C   . TRP   B 1 188 ? 49.054  -18.270 55.558 1.00 21.99 ? 880  TRP   B C   1 
ATOM   3712 O O   . TRP   B 1 188 ? 48.694  -17.170 55.147 1.00 22.32 ? 880  TRP   B O   1 
ATOM   3713 C CB  . TRP   B 1 188 ? 47.863  -19.721 53.939 1.00 21.35 ? 880  TRP   B CB  1 
ATOM   3714 C CG  . TRP   B 1 188 ? 47.903  -20.466 52.640 1.00 21.60 ? 880  TRP   B CG  1 
ATOM   3715 C CD1 . TRP   B 1 188 ? 47.683  -19.959 51.392 1.00 21.98 ? 880  TRP   B CD1 1 
ATOM   3716 C CD2 . TRP   B 1 188 ? 48.212  -21.859 52.463 1.00 21.63 ? 880  TRP   B CD2 1 
ATOM   3717 N NE1 . TRP   B 1 188 ? 47.817  -20.953 50.448 1.00 22.21 ? 880  TRP   B NE1 1 
ATOM   3718 C CE2 . TRP   B 1 188 ? 48.166  -22.124 51.077 1.00 22.13 ? 880  TRP   B CE2 1 
ATOM   3719 C CE3 . TRP   B 1 188 ? 48.520  -22.909 53.343 1.00 21.83 ? 880  TRP   B CE3 1 
ATOM   3720 C CZ2 . TRP   B 1 188 ? 48.444  -23.386 50.552 1.00 22.54 ? 880  TRP   B CZ2 1 
ATOM   3721 C CZ3 . TRP   B 1 188 ? 48.808  -24.153 52.820 1.00 22.51 ? 880  TRP   B CZ3 1 
ATOM   3722 C CH2 . TRP   B 1 188 ? 48.782  -24.379 51.438 1.00 22.76 ? 880  TRP   B CH2 1 
ATOM   3723 N N   . MET   B 1 189 ? 49.198  -18.541 56.872 1.00 21.56 ? 881  MET   B N   1 
ATOM   3724 C CA  . MET   B 1 189 ? 48.938  -17.548 57.908 1.00 21.42 ? 881  MET   B CA  1 
ATOM   3725 C C   . MET   B 1 189 ? 50.060  -16.566 58.144 1.00 20.95 ? 881  MET   B C   1 
ATOM   3726 O O   . MET   B 1 189 ? 51.226  -16.927 58.061 1.00 20.89 ? 881  MET   B O   1 
ATOM   3727 C CB  . MET   B 1 189 ? 48.571  -18.227 59.236 1.00 22.06 ? 881  MET   B CB  1 
ATOM   3728 C CG  . MET   B 1 189 ? 47.160  -18.790 59.274 1.00 24.29 ? 881  MET   B CG  1 
ATOM   3729 S SD  . MET   B 1 189 ? 46.980  -20.045 60.577 1.00 30.20 ? 881  MET   B SD  1 
ATOM   3730 C CE  . MET   B 1 189 ? 47.176  -19.092 61.968 1.00 25.28 ? 881  MET   B CE  1 
ATOM   3731 N N   . ALA   B 1 190 ? 49.697  -15.331 58.498 1.00 20.37 ? 882  ALA   B N   1 
ATOM   3732 C CA  . ALA   B 1 190 ? 50.640  -14.295 58.862 1.00 20.73 ? 882  ALA   B CA  1 
ATOM   3733 C C   . ALA   B 1 190 ? 51.264  -14.646 60.233 1.00 21.06 ? 882  ALA   B C   1 
ATOM   3734 O O   . ALA   B 1 190 ? 50.665  -15.409 60.996 1.00 21.18 ? 882  ALA   B O   1 
ATOM   3735 C CB  . ALA   B 1 190 ? 49.918  -12.970 58.939 1.00 20.68 ? 882  ALA   B CB  1 
ATOM   3736 N N   . LEU   B 1 191 ? 52.467  -14.135 60.537 1.00 20.89 ? 883  LEU   B N   1 
ATOM   3737 C CA  . LEU   B 1 191 ? 53.125  -14.438 61.825 1.00 21.35 ? 883  LEU   B CA  1 
ATOM   3738 C C   . LEU   B 1 191 ? 52.235  -14.095 63.062 1.00 21.35 ? 883  LEU   B C   1 
ATOM   3739 O O   . LEU   B 1 191 ? 51.932  -14.978 63.865 1.00 21.52 ? 883  LEU   B O   1 
ATOM   3740 C CB  . LEU   B 1 191 ? 54.500  -13.756 61.915 1.00 21.50 ? 883  LEU   B CB  1 
ATOM   3741 C CG  . LEU   B 1 191 ? 55.313  -14.121 63.146 1.00 23.93 ? 883  LEU   B CG  1 
ATOM   3742 C CD1 . LEU   B 1 191 ? 55.920  -15.518 63.012 1.00 25.00 ? 883  LEU   B CD1 1 
ATOM   3743 C CD2 . LEU   B 1 191 ? 56.400  -13.120 63.371 1.00 24.33 ? 883  LEU   B CD2 1 
ATOM   3744 N N   . GLU   B 1 192 ? 51.710  -12.856 63.131 1.00 20.75 ? 884  GLU   B N   1 
ATOM   3745 C CA  . GLU   B 1 192 ? 50.810  -12.430 64.198 1.00 20.13 ? 884  GLU   B CA  1 
ATOM   3746 C C   . GLU   B 1 192 ? 49.619  -13.342 64.363 1.00 21.31 ? 884  GLU   B C   1 
ATOM   3747 O O   . GLU   B 1 192 ? 49.125  -13.474 65.479 1.00 21.92 ? 884  GLU   B O   1 
ATOM   3748 C CB  . GLU   B 1 192 ? 50.375  -10.960 64.029 1.00 19.80 ? 884  GLU   B CB  1 
ATOM   3749 C CG  . GLU   B 1 192 ? 49.378  -10.666 62.919 1.00 19.29 ? 884  GLU   B CG  1 
ATOM   3750 C CD  . GLU   B 1 192 ? 49.938  -10.380 61.530 1.00 19.80 ? 884  GLU   B CD  1 
ATOM   3751 O OE1 . GLU   B 1 192 ? 51.069  -10.827 61.224 1.00 19.16 ? 884  GLU   B OE1 1 
ATOM   3752 O OE2 . GLU   B 1 192 ? 49.238  -9.700  60.745 1.00 19.05 ? 884  GLU   B OE2 1 
ATOM   3753 N N   . SER   B 1 193 ? 49.179  -14.011 63.284 1.00 21.50 ? 885  SER   B N   1 
ATOM   3754 C CA  . SER   B 1 193 ? 48.053  -14.934 63.361 1.00 22.26 ? 885  SER   B CA  1 
ATOM   3755 C C   . SER   B 1 193 ? 48.491  -16.288 63.909 1.00 23.06 ? 885  SER   B C   1 
ATOM   3756 O O   . SER   B 1 193 ? 47.739  -16.896 64.665 1.00 22.52 ? 885  SER   B O   1 
ATOM   3757 C CB  . SER   B 1 193 ? 47.412  -15.139 61.994 1.00 22.84 ? 885  SER   B CB  1 
ATOM   3758 O OG  . SER   B 1 193 ? 46.891  -13.932 61.471 1.00 24.40 ? 885  SER   B OG  1 
ATOM   3759 N N   . ILE   B 1 194 ? 49.679  -16.788 63.508 1.00 23.58 ? 886  ILE   B N   1 
ATOM   3760 C CA  . ILE   B 1 194 ? 50.159  -18.088 64.001 1.00 24.28 ? 886  ILE   B CA  1 
ATOM   3761 C C   . ILE   B 1 194 ? 50.410  -17.989 65.513 1.00 25.33 ? 886  ILE   B C   1 
ATOM   3762 O O   . ILE   B 1 194 ? 50.013  -18.876 66.272 1.00 26.18 ? 886  ILE   B O   1 
ATOM   3763 C CB  . ILE   B 1 194 ? 51.478  -18.516 63.285 1.00 24.53 ? 886  ILE   B CB  1 
ATOM   3764 C CG1 . ILE   B 1 194 ? 51.323  -18.683 61.767 1.00 24.96 ? 886  ILE   B CG1 1 
ATOM   3765 C CG2 . ILE   B 1 194 ? 52.074  -19.766 63.908 1.00 25.09 ? 886  ILE   B CG2 1 
ATOM   3766 C CD1 . ILE   B 1 194 ? 52.665  -18.741 61.062 1.00 25.01 ? 886  ILE   B CD1 1 
ATOM   3767 N N   . LEU   B 1 195 ? 51.054  -16.893 65.944 1.00 24.79 ? 887  LEU   B N   1 
ATOM   3768 C CA  . LEU   B 1 195 ? 51.442  -16.715 67.331 1.00 24.90 ? 887  LEU   B CA  1 
ATOM   3769 C C   . LEU   B 1 195 ? 50.318  -16.280 68.256 1.00 24.83 ? 887  LEU   B C   1 
ATOM   3770 O O   . LEU   B 1 195 ? 50.306  -16.680 69.418 1.00 25.20 ? 887  LEU   B O   1 
ATOM   3771 C CB  . LEU   B 1 195 ? 52.612  -15.710 67.448 1.00 24.57 ? 887  LEU   B CB  1 
ATOM   3772 C CG  . LEU   B 1 195 ? 53.921  -16.041 66.742 1.00 24.97 ? 887  LEU   B CG  1 
ATOM   3773 C CD1 . LEU   B 1 195 ? 54.947  -14.951 66.990 1.00 25.59 ? 887  LEU   B CD1 1 
ATOM   3774 C CD2 . LEU   B 1 195 ? 54.478  -17.353 67.207 1.00 24.99 ? 887  LEU   B CD2 1 
ATOM   3775 N N   . HIS   B 1 196 ? 49.440  -15.390 67.781 1.00 23.90 ? 888  HIS   B N   1 
ATOM   3776 C CA  . HIS   B 1 196 ? 48.410  -14.824 68.628 1.00 23.56 ? 888  HIS   B CA  1 
ATOM   3777 C C   . HIS   B 1 196 ? 46.986  -14.959 68.111 1.00 23.86 ? 888  HIS   B C   1 
ATOM   3778 O O   . HIS   B 1 196 ? 46.111  -14.280 68.638 1.00 24.26 ? 888  HIS   B O   1 
ATOM   3779 C CB  . HIS   B 1 196 ? 48.734  -13.355 68.900 1.00 24.18 ? 888  HIS   B CB  1 
ATOM   3780 C CG  . HIS   B 1 196 ? 50.053  -13.165 69.581 1.00 27.74 ? 888  HIS   B CG  1 
ATOM   3781 N ND1 . HIS   B 1 196 ? 50.172  -13.219 70.960 1.00 29.96 ? 888  HIS   B ND1 1 
ATOM   3782 C CD2 . HIS   B 1 196 ? 51.279  -12.964 69.050 1.00 28.83 ? 888  HIS   B CD2 1 
ATOM   3783 C CE1 . HIS   B 1 196 ? 51.457  -13.035 71.220 1.00 30.22 ? 888  HIS   B CE1 1 
ATOM   3784 N NE2 . HIS   B 1 196 ? 52.161  -12.876 70.106 1.00 30.08 ? 888  HIS   B NE2 1 
ATOM   3785 N N   . ARG   B 1 197 ? 46.720  -15.831 67.118 1.00 23.68 ? 889  ARG   B N   1 
ATOM   3786 C CA  . ARG   B 1 197 ? 45.364  -16.024 66.555 1.00 24.25 ? 889  ARG   B CA  1 
ATOM   3787 C C   . ARG   B 1 197 ? 44.618  -14.710 66.256 1.00 23.78 ? 889  ARG   B C   1 
ATOM   3788 O O   . ARG   B 1 197 ? 43.397  -14.637 66.430 1.00 23.88 ? 889  ARG   B O   1 
ATOM   3789 C CB  . ARG   B 1 197 ? 44.516  -16.922 67.462 1.00 27.46 ? 889  ARG   B CB  1 
ATOM   3790 C CG  . ARG   B 1 197 ? 44.964  -18.373 67.474 1.00 34.58 ? 889  ARG   B CG  1 
ATOM   3791 C CD  . ARG   B 1 197 ? 44.431  -19.128 68.692 1.00 41.23 ? 889  ARG   B CD  1 
ATOM   3792 N NE  . ARG   B 1 197 ? 42.966  -19.099 68.788 1.00 46.47 ? 889  ARG   B NE  1 
ATOM   3793 C CZ  . ARG   B 1 197 ? 42.271  -19.512 69.847 1.00 50.70 ? 889  ARG   B CZ  1 
ATOM   3794 N NH1 . ARG   B 1 197 ? 42.897  -19.973 70.923 1.00 51.10 ? 889  ARG   B NH1 1 
ATOM   3795 N NH2 . ARG   B 1 197 ? 40.944  -19.448 69.844 1.00 50.95 ? 889  ARG   B NH2 1 
ATOM   3796 N N   . ILE   B 1 198 ? 45.367  -13.662 65.861 1.00 23.22 ? 890  ILE   B N   1 
ATOM   3797 C CA  . ILE   B 1 198 ? 44.844  -12.343 65.519 1.00 23.59 ? 890  ILE   B CA  1 
ATOM   3798 C C   . ILE   B 1 198 ? 44.613  -12.252 63.974 1.00 23.35 ? 890  ILE   B C   1 
ATOM   3799 O O   . ILE   B 1 198 ? 45.557  -12.416 63.196 1.00 23.29 ? 890  ILE   B O   1 
ATOM   3800 C CB  . ILE   B 1 198 ? 45.824  -11.284 66.090 1.00 24.61 ? 890  ILE   B CB  1 
ATOM   3801 C CG1 . ILE   B 1 198 ? 45.518  -11.032 67.595 1.00 26.25 ? 890  ILE   B CG1 1 
ATOM   3802 C CG2 . ILE   B 1 198 ? 45.849  -9.972  65.283 1.00 24.60 ? 890  ILE   B CG2 1 
ATOM   3803 C CD1 . ILE   B 1 198 ? 46.664  -10.371 68.401 1.00 26.97 ? 890  ILE   B CD1 1 
ATOM   3804 N N   . TYR   B 1 199 ? 43.348  -12.073 63.532 1.00 22.72 ? 891  TYR   B N   1 
ATOM   3805 C CA  . TYR   B 1 199 ? 43.052  -12.023 62.099 1.00 22.58 ? 891  TYR   B CA  1 
ATOM   3806 C C   . TYR   B 1 199 ? 42.511  -10.683 61.681 1.00 21.05 ? 891  TYR   B C   1 
ATOM   3807 O O   . TYR   B 1 199 ? 41.516  -10.251 62.215 1.00 21.59 ? 891  TYR   B O   1 
ATOM   3808 C CB  . TYR   B 1 199 ? 42.075  -13.117 61.715 1.00 23.34 ? 891  TYR   B CB  1 
ATOM   3809 C CG  . TYR   B 1 199 ? 42.587  -14.505 62.030 1.00 24.80 ? 891  TYR   B CG  1 
ATOM   3810 C CD1 . TYR   B 1 199 ? 42.342  -15.096 63.265 1.00 25.80 ? 891  TYR   B CD1 1 
ATOM   3811 C CD2 . TYR   B 1 199 ? 43.276  -15.243 61.082 1.00 25.94 ? 891  TYR   B CD2 1 
ATOM   3812 C CE1 . TYR   B 1 199 ? 42.773  -16.384 63.546 1.00 27.07 ? 891  TYR   B CE1 1 
ATOM   3813 C CE2 . TYR   B 1 199 ? 43.717  -16.531 61.353 1.00 27.35 ? 891  TYR   B CE2 1 
ATOM   3814 C CZ  . TYR   B 1 199 ? 43.473  -17.095 62.591 1.00 28.77 ? 891  TYR   B CZ  1 
ATOM   3815 O OH  . TYR   B 1 199 ? 43.916  -18.368 62.862 1.00 31.38 ? 891  TYR   B OH  1 
ATOM   3816 N N   . THR   B 1 200 ? 43.199  -9.998  60.776 1.00 19.33 ? 892  THR   B N   1 
ATOM   3817 C CA  . THR   B 1 200 ? 42.849  -8.667  60.292 1.00 18.26 ? 892  THR   B CA  1 
ATOM   3818 C C   . THR   B 1 200 ? 42.883  -8.622  58.729 1.00 18.08 ? 892  THR   B C   1 
ATOM   3819 O O   . THR   B 1 200 ? 43.259  -9.602  58.079 1.00 17.81 ? 892  THR   B O   1 
ATOM   3820 C CB  . THR   B 1 200 ? 43.857  -7.665  60.864 1.00 18.63 ? 892  THR   B CB  1 
ATOM   3821 O OG1 . THR   B 1 200 ? 45.132  -7.882  60.236 1.00 19.00 ? 892  THR   B OG1 1 
ATOM   3822 C CG2 . THR   B 1 200 ? 43.969  -7.730  62.380 1.00 19.25 ? 892  THR   B CG2 1 
ATOM   3823 N N   . HIS   B 1 201 ? 42.529  -7.467  58.129 1.00 17.69 ? 893  HIS   B N   1 
ATOM   3824 C CA  . HIS   B 1 201 ? 42.629  -7.286  56.698 1.00 17.88 ? 893  HIS   B CA  1 
ATOM   3825 C C   . HIS   B 1 201 ? 44.102  -7.424  56.251 1.00 18.05 ? 893  HIS   B C   1 
ATOM   3826 O O   . HIS   B 1 201 ? 44.354  -7.967  55.186 1.00 18.44 ? 893  HIS   B O   1 
ATOM   3827 C CB  . HIS   B 1 201 ? 42.053  -5.917  56.305 1.00 18.52 ? 893  HIS   B CB  1 
ATOM   3828 C CG  . HIS   B 1 201 ? 40.621  -5.721  56.701 1.00 19.46 ? 893  HIS   B CG  1 
ATOM   3829 N ND1 . HIS   B 1 201 ? 39.645  -6.635  56.354 1.00 20.69 ? 893  HIS   B ND1 1 
ATOM   3830 C CD2 . HIS   B 1 201 ? 40.053  -4.739  57.438 1.00 20.43 ? 893  HIS   B CD2 1 
ATOM   3831 C CE1 . HIS   B 1 201 ? 38.517  -6.177  56.875 1.00 20.93 ? 893  HIS   B CE1 1 
ATOM   3832 N NE2 . HIS   B 1 201 ? 38.707  -5.034  57.522 1.00 21.02 ? 893  HIS   B NE2 1 
ATOM   3833 N N   . GLN   B 1 202 ? 45.068  -7.021  57.109 1.00 17.72 ? 894  GLN   B N   1 
ATOM   3834 C CA  . GLN   B 1 202 ? 46.510  -7.091  56.824 1.00 16.90 ? 894  GLN   B CA  1 
ATOM   3835 C C   . GLN   B 1 202 ? 47.066  -8.537  56.948 1.00 15.75 ? 894  GLN   B C   1 
ATOM   3836 O O   . GLN   B 1 202 ? 47.982  -8.876  56.217 1.00 15.45 ? 894  GLN   B O   1 
ATOM   3837 C CB  . GLN   B 1 202 ? 47.306  -6.045  57.639 1.00 17.45 ? 894  GLN   B CB  1 
ATOM   3838 C CG  . GLN   B 1 202 ? 46.970  -4.573  57.243 1.00 19.94 ? 894  GLN   B CG  1 
ATOM   3839 C CD  . GLN   B 1 202 ? 47.025  -4.285  55.733 1.00 25.38 ? 894  GLN   B CD  1 
ATOM   3840 O OE1 . GLN   B 1 202 ? 45.998  -4.142  55.051 1.00 27.26 ? 894  GLN   B OE1 1 
ATOM   3841 N NE2 . GLN   B 1 202 ? 48.228  -4.203  55.164 1.00 25.33 ? 894  GLN   B NE2 1 
ATOM   3842 N N   . SER   B 1 203 ? 46.452  -9.407  57.748 1.00 15.24 ? 895  SER   B N   1 
ATOM   3843 C CA  . SER   B 1 203 ? 46.822  -10.834 57.743 1.00 15.40 ? 895  SER   B CA  1 
ATOM   3844 C C   . SER   B 1 203 ? 46.198  -11.522 56.490 1.00 16.30 ? 895  SER   B C   1 
ATOM   3845 O O   . SER   B 1 203 ? 46.760  -12.490 55.992 1.00 17.04 ? 895  SER   B O   1 
ATOM   3846 C CB  . SER   B 1 203 ? 46.412  -11.546 59.029 1.00 14.81 ? 895  SER   B CB  1 
ATOM   3847 O OG  . SER   B 1 203 ? 45.027  -11.419 59.275 1.00 15.40 ? 895  SER   B OG  1 
ATOM   3848 N N   . ASP   B 1 204 ? 45.085  -10.994 55.949 1.00 16.05 ? 896  ASP   B N   1 
ATOM   3849 C CA  . ASP   B 1 204 ? 44.519  -11.499 54.703 1.00 15.83 ? 896  ASP   B CA  1 
ATOM   3850 C C   . ASP   B 1 204 ? 45.482  -11.163 53.532 1.00 16.27 ? 896  ASP   B C   1 
ATOM   3851 O O   . ASP   B 1 204 ? 45.606  -11.939 52.579 1.00 15.98 ? 896  ASP   B O   1 
ATOM   3852 C CB  . ASP   B 1 204 ? 43.117  -10.904 54.451 1.00 16.07 ? 896  ASP   B CB  1 
ATOM   3853 C CG  . ASP   B 1 204 ? 41.964  -11.687 55.081 1.00 19.48 ? 896  ASP   B CG  1 
ATOM   3854 O OD1 . ASP   B 1 204 ? 42.222  -12.741 55.686 1.00 20.79 ? 896  ASP   B OD1 1 
ATOM   3855 O OD2 . ASP   B 1 204 ? 40.813  -11.233 54.978 1.00 20.45 ? 896  ASP   B OD2 1 
ATOM   3856 N N   . VAL   B 1 205 ? 46.160  -9.999  53.613 1.00 16.66 ? 897  VAL   B N   1 
ATOM   3857 C CA  . VAL   B 1 205 ? 47.154  -9.537  52.656 1.00 17.22 ? 897  VAL   B CA  1 
ATOM   3858 C C   . VAL   B 1 205 ? 48.314  -10.527 52.595 1.00 17.91 ? 897  VAL   B C   1 
ATOM   3859 O O   . VAL   B 1 205 ? 48.782  -10.844 51.494 1.00 18.48 ? 897  VAL   B O   1 
ATOM   3860 C CB  . VAL   B 1 205 ? 47.601  -8.092  52.980 1.00 18.18 ? 897  VAL   B CB  1 
ATOM   3861 C CG1 . VAL   B 1 205 ? 48.874  -7.713  52.236 1.00 18.93 ? 897  VAL   B CG1 1 
ATOM   3862 C CG2 . VAL   B 1 205 ? 46.484  -7.105  52.659 1.00 18.92 ? 897  VAL   B CG2 1 
ATOM   3863 N N   . TRP   B 1 206 ? 48.735  -11.071 53.752 1.00 17.68 ? 898  TRP   B N   1 
ATOM   3864 C CA  . TRP   B 1 206 ? 49.805  -12.076 53.825 1.00 18.06 ? 898  TRP   B CA  1 
ATOM   3865 C C   . TRP   B 1 206 ? 49.360  -13.369 53.108 1.00 18.00 ? 898  TRP   B C   1 
ATOM   3866 O O   . TRP   B 1 206 ? 50.129  -13.902 52.303 1.00 18.92 ? 898  TRP   B O   1 
ATOM   3867 C CB  . TRP   B 1 206 ? 50.166  -12.367 55.290 1.00 17.88 ? 898  TRP   B CB  1 
ATOM   3868 C CG  . TRP   B 1 206 ? 51.200  -13.441 55.501 1.00 18.73 ? 898  TRP   B CG  1 
ATOM   3869 C CD1 . TRP   B 1 206 ? 51.093  -14.763 55.195 1.00 19.25 ? 898  TRP   B CD1 1 
ATOM   3870 C CD2 . TRP   B 1 206 ? 52.464  -13.284 56.161 1.00 18.87 ? 898  TRP   B CD2 1 
ATOM   3871 N NE1 . TRP   B 1 206 ? 52.234  -15.426 55.567 1.00 19.56 ? 898  TRP   B NE1 1 
ATOM   3872 C CE2 . TRP   B 1 206 ? 53.071  -14.551 56.205 1.00 19.52 ? 898  TRP   B CE2 1 
ATOM   3873 C CE3 . TRP   B 1 206 ? 53.079  -12.224 56.832 1.00 19.78 ? 898  TRP   B CE3 1 
ATOM   3874 C CZ2 . TRP   B 1 206 ? 54.288  -14.771 56.846 1.00 20.40 ? 898  TRP   B CZ2 1 
ATOM   3875 C CZ3 . TRP   B 1 206 ? 54.302  -12.437 57.432 1.00 20.35 ? 898  TRP   B CZ3 1 
ATOM   3876 C CH2 . TRP   B 1 206 ? 54.896  -13.695 57.426 1.00 20.49 ? 898  TRP   B CH2 1 
ATOM   3877 N N   . SER   B 1 207 ? 48.129  -13.853 53.396 1.00 16.60 ? 899  SER   B N   1 
ATOM   3878 C CA  . SER   B 1 207 ? 47.518  -15.012 52.748 1.00 16.06 ? 899  SER   B CA  1 
ATOM   3879 C C   . SER   B 1 207 ? 47.406  -14.827 51.234 1.00 15.37 ? 899  SER   B C   1 
ATOM   3880 O O   . SER   B 1 207 ? 47.571  -15.802 50.491 1.00 15.74 ? 899  SER   B O   1 
ATOM   3881 C CB  . SER   B 1 207 ? 46.138  -15.269 53.321 1.00 17.09 ? 899  SER   B CB  1 
ATOM   3882 O OG  . SER   B 1 207 ? 46.265  -15.621 54.689 1.00 20.46 ? 899  SER   B OG  1 
ATOM   3883 N N   . TYR   B 1 208 ? 47.146  -13.580 50.789 1.00 13.91 ? 900  TYR   B N   1 
ATOM   3884 C CA  . TYR   B 1 208 ? 47.032  -13.184 49.383 1.00 13.63 ? 900  TYR   B CA  1 
ATOM   3885 C C   . TYR   B 1 208 ? 48.399  -13.329 48.674 1.00 14.42 ? 900  TYR   B C   1 
ATOM   3886 O O   . TYR   B 1 208 ? 48.460  -13.790 47.528 1.00 14.34 ? 900  TYR   B O   1 
ATOM   3887 C CB  . TYR   B 1 208 ? 46.478  -11.735 49.261 1.00 13.02 ? 900  TYR   B CB  1 
ATOM   3888 C CG  . TYR   B 1 208 ? 46.541  -11.175 47.853 1.00 13.61 ? 900  TYR   B CG  1 
ATOM   3889 C CD1 . TYR   B 1 208 ? 45.496  -11.374 46.952 1.00 14.81 ? 900  TYR   B CD1 1 
ATOM   3890 C CD2 . TYR   B 1 208 ? 47.656  -10.478 47.408 1.00 13.74 ? 900  TYR   B CD2 1 
ATOM   3891 C CE1 . TYR   B 1 208 ? 45.569  -10.900 45.643 1.00 14.91 ? 900  TYR   B CE1 1 
ATOM   3892 C CE2 . TYR   B 1 208 ? 47.749  -10.025 46.098 1.00 14.51 ? 900  TYR   B CE2 1 
ATOM   3893 C CZ  . TYR   B 1 208 ? 46.696  -10.222 45.221 1.00 15.24 ? 900  TYR   B CZ  1 
ATOM   3894 O OH  . TYR   B 1 208 ? 46.805  -9.801  43.916 1.00 15.88 ? 900  TYR   B OH  1 
ATOM   3895 N N   . GLY   B 1 209 ? 49.467  -12.957 49.378 1.00 14.66 ? 901  GLY   B N   1 
ATOM   3896 C CA  . GLY   B 1 209 ? 50.830  -13.032 48.874 1.00 14.65 ? 901  GLY   B CA  1 
ATOM   3897 C C   . GLY   B 1 209 ? 51.249  -14.462 48.602 1.00 14.72 ? 901  GLY   B C   1 
ATOM   3898 O O   . GLY   B 1 209 ? 51.903  -14.752 47.590 1.00 15.21 ? 901  GLY   B O   1 
ATOM   3899 N N   . VAL   B 1 210 ? 50.857  -15.361 49.510 1.00 13.90 ? 902  VAL   B N   1 
ATOM   3900 C CA  . VAL   B 1 210 ? 51.095  -16.798 49.425 1.00 14.15 ? 902  VAL   B CA  1 
ATOM   3901 C C   . VAL   B 1 210 ? 50.227  -17.423 48.338 1.00 13.84 ? 902  VAL   B C   1 
ATOM   3902 O O   . VAL   B 1 210 ? 50.672  -18.375 47.689 1.00 14.65 ? 902  VAL   B O   1 
ATOM   3903 C CB  . VAL   B 1 210 ? 50.849  -17.462 50.800 1.00 15.96 ? 902  VAL   B CB  1 
ATOM   3904 C CG1 . VAL   B 1 210 ? 51.032  -18.981 50.734 1.00 17.19 ? 902  VAL   B CG1 1 
ATOM   3905 C CG2 . VAL   B 1 210 ? 51.752  -16.846 51.873 1.00 16.09 ? 902  VAL   B CG2 1 
ATOM   3906 N N   . THR   B 1 211 ? 48.977  -16.909 48.134 1.00 12.42 ? 903  THR   B N   1 
ATOM   3907 C CA  . THR   B 1 211 ? 48.083  -17.395 47.094 1.00 11.80 ? 903  THR   B CA  1 
ATOM   3908 C C   . THR   B 1 211 ? 48.673  -16.996 45.711 1.00 12.11 ? 903  THR   B C   1 
ATOM   3909 O O   . THR   B 1 211 ? 48.691  -17.803 44.771 1.00 11.83 ? 903  THR   B O   1 
ATOM   3910 C CB  . THR   B 1 211 ? 46.684  -16.759 47.271 1.00 12.43 ? 903  THR   B CB  1 
ATOM   3911 O OG1 . THR   B 1 211 ? 46.148  -17.119 48.549 1.00 13.94 ? 903  THR   B OG1 1 
ATOM   3912 C CG2 . THR   B 1 211 ? 45.709  -17.143 46.138 1.00 10.74 ? 903  THR   B CG2 1 
ATOM   3913 N N   . VAL   B 1 212 ? 49.159  -15.748 45.592 1.00 11.60 ? 904  VAL   B N   1 
ATOM   3914 C CA  . VAL   B 1 212 ? 49.794  -15.289 44.361 1.00 13.02 ? 904  VAL   B CA  1 
ATOM   3915 C C   . VAL   B 1 212 ? 51.052  -16.153 44.066 1.00 15.16 ? 904  VAL   B C   1 
ATOM   3916 O O   . VAL   B 1 212 ? 51.304  -16.479 42.913 1.00 15.63 ? 904  VAL   B O   1 
ATOM   3917 C CB  . VAL   B 1 212 ? 50.115  -13.763 44.429 1.00 13.27 ? 904  VAL   B CB  1 
ATOM   3918 C CG1 . VAL   B 1 212 ? 51.145  -13.353 43.370 1.00 13.34 ? 904  VAL   B CG1 1 
ATOM   3919 C CG2 . VAL   B 1 212 ? 48.835  -12.945 44.283 1.00 12.94 ? 904  VAL   B CG2 1 
ATOM   3920 N N   . TRP   B 1 213 ? 51.777  -16.582 45.124 1.00 15.56 ? 905  TRP   B N   1 
ATOM   3921 C CA  . TRP   B 1 213 ? 52.941  -17.454 45.025 1.00 16.44 ? 905  TRP   B CA  1 
ATOM   3922 C C   . TRP   B 1 213 ? 52.532  -18.806 44.439 1.00 17.30 ? 905  TRP   B C   1 
ATOM   3923 O O   . TRP   B 1 213 ? 53.170  -19.278 43.498 1.00 17.39 ? 905  TRP   B O   1 
ATOM   3924 C CB  . TRP   B 1 213 ? 53.604  -17.625 46.417 1.00 16.29 ? 905  TRP   B CB  1 
ATOM   3925 C CG  . TRP   B 1 213 ? 54.886  -18.385 46.384 1.00 16.69 ? 905  TRP   B CG  1 
ATOM   3926 C CD1 . TRP   B 1 213 ? 56.139  -17.886 46.166 1.00 17.67 ? 905  TRP   B CD1 1 
ATOM   3927 C CD2 . TRP   B 1 213 ? 55.037  -19.804 46.547 1.00 16.85 ? 905  TRP   B CD2 1 
ATOM   3928 N NE1 . TRP   B 1 213 ? 57.062  -18.909 46.183 1.00 17.87 ? 905  TRP   B NE1 1 
ATOM   3929 C CE2 . TRP   B 1 213 ? 56.411  -20.095 46.429 1.00 17.56 ? 905  TRP   B CE2 1 
ATOM   3930 C CE3 . TRP   B 1 213 ? 54.137  -20.858 46.775 1.00 17.31 ? 905  TRP   B CE3 1 
ATOM   3931 C CZ2 . TRP   B 1 213 ? 56.901  -21.394 46.518 1.00 18.33 ? 905  TRP   B CZ2 1 
ATOM   3932 C CZ3 . TRP   B 1 213 ? 54.625  -22.139 46.881 1.00 18.21 ? 905  TRP   B CZ3 1 
ATOM   3933 C CH2 . TRP   B 1 213 ? 55.995  -22.397 46.771 1.00 18.48 ? 905  TRP   B CH2 1 
ATOM   3934 N N   . GLU   B 1 214 ? 51.443  -19.405 44.975 1.00 17.62 ? 906  GLU   B N   1 
ATOM   3935 C CA  . GLU   B 1 214 ? 50.868  -20.657 44.479 1.00 17.82 ? 906  GLU   B CA  1 
ATOM   3936 C C   . GLU   B 1 214 ? 50.509  -20.564 42.992 1.00 18.59 ? 906  GLU   B C   1 
ATOM   3937 O O   . GLU   B 1 214 ? 50.549  -21.573 42.310 1.00 19.18 ? 906  GLU   B O   1 
ATOM   3938 C CB  . GLU   B 1 214 ? 49.573  -20.992 45.224 1.00 17.06 ? 906  GLU   B CB  1 
ATOM   3939 C CG  . GLU   B 1 214 ? 49.743  -21.297 46.697 1.00 17.09 ? 906  GLU   B CG  1 
ATOM   3940 C CD  . GLU   B 1 214 ? 48.396  -21.650 47.288 1.00 17.45 ? 906  GLU   B CD  1 
ATOM   3941 O OE1 . GLU   B 1 214 ? 47.660  -20.710 47.675 1.00 16.04 ? 906  GLU   B OE1 1 
ATOM   3942 O OE2 . GLU   B 1 214 ? 48.039  -22.854 47.284 1.00 16.47 ? 906  GLU   B OE2 1 
ATOM   3943 N N   . LEU   B 1 215 ? 50.123  -19.389 42.513 1.00 18.23 ? 907  LEU   B N   1 
ATOM   3944 C CA  . LEU   B 1 215 ? 49.719  -19.214 41.131 1.00 19.43 ? 907  LEU   B CA  1 
ATOM   3945 C C   . LEU   B 1 215 ? 50.926  -19.192 40.201 1.00 20.63 ? 907  LEU   B C   1 
ATOM   3946 O O   . LEU   B 1 215 ? 50.928  -19.862 39.169 1.00 20.54 ? 907  LEU   B O   1 
ATOM   3947 C CB  . LEU   B 1 215 ? 48.879  -17.920 40.969 1.00 19.79 ? 907  LEU   B CB  1 
ATOM   3948 C CG  . LEU   B 1 215 ? 47.467  -17.925 41.584 1.00 22.00 ? 907  LEU   B CG  1 
ATOM   3949 C CD1 . LEU   B 1 215 ? 46.684  -16.676 41.148 1.00 22.74 ? 907  LEU   B CD1 1 
ATOM   3950 C CD2 . LEU   B 1 215 ? 46.677  -19.188 41.167 1.00 22.71 ? 907  LEU   B CD2 1 
ATOM   3951 N N   . MET   B 1 216 ? 51.951  -18.415 40.574 1.00 21.54 ? 908  MET   B N   1 
ATOM   3952 C CA  . MET   B 1 216 ? 53.207  -18.280 39.845 1.00 22.50 ? 908  MET   B CA  1 
ATOM   3953 C C   . MET   B 1 216 ? 54.019  -19.552 39.818 1.00 22.98 ? 908  MET   B C   1 
ATOM   3954 O O   . MET   B 1 216 ? 54.805  -19.731 38.900 1.00 24.15 ? 908  MET   B O   1 
ATOM   3955 C CB  . MET   B 1 216 ? 54.039  -17.157 40.438 1.00 23.59 ? 908  MET   B CB  1 
ATOM   3956 C CG  . MET   B 1 216 ? 53.298  -15.832 40.499 1.00 27.49 ? 908  MET   B CG  1 
ATOM   3957 S SD  . MET   B 1 216 ? 52.670  -15.252 38.905 1.00 35.64 ? 908  MET   B SD  1 
ATOM   3958 C CE  . MET   B 1 216 ? 51.929  -13.683 39.409 1.00 34.21 ? 908  MET   B CE  1 
ATOM   3959 N N   . THR   B 1 217 ? 53.859  -20.432 40.807 1.00 22.30 ? 909  THR   B N   1 
ATOM   3960 C CA  . THR   B 1 217 ? 54.567  -21.713 40.823 1.00 22.31 ? 909  THR   B CA  1 
ATOM   3961 C C   . THR   B 1 217 ? 53.732  -22.874 40.281 1.00 23.98 ? 909  THR   B C   1 
ATOM   3962 O O   . THR   B 1 217 ? 54.178  -24.018 40.369 1.00 24.47 ? 909  THR   B O   1 
ATOM   3963 C CB  . THR   B 1 217 ? 55.065  -22.046 42.228 1.00 22.48 ? 909  THR   B CB  1 
ATOM   3964 O OG1 . THR   B 1 217 ? 53.959  -22.200 43.136 1.00 22.86 ? 909  THR   B OG1 1 
ATOM   3965 C CG2 . THR   B 1 217 ? 56.085  -21.047 42.733 1.00 22.21 ? 909  THR   B CG2 1 
ATOM   3966 N N   . PHE   B 1 218 ? 52.514  -22.588 39.755 1.00 24.68 ? 910  PHE   B N   1 
ATOM   3967 C CA  . PHE   B 1 218 ? 51.578  -23.550 39.198 1.00 25.91 ? 910  PHE   B CA  1 
ATOM   3968 C C   . PHE   B 1 218 ? 51.160  -24.587 40.214 1.00 27.17 ? 910  PHE   B C   1 
ATOM   3969 O O   . PHE   B 1 218 ? 51.111  -25.780 39.916 1.00 27.81 ? 910  PHE   B O   1 
ATOM   3970 C CB  . PHE   B 1 218 ? 52.092  -24.178 37.897 1.00 26.17 ? 910  PHE   B CB  1 
ATOM   3971 C CG  . PHE   B 1 218 ? 52.595  -23.166 36.886 1.00 27.32 ? 910  PHE   B CG  1 
ATOM   3972 C CD1 . PHE   B 1 218 ? 51.711  -22.440 36.105 1.00 28.07 ? 910  PHE   B CD1 1 
ATOM   3973 C CD2 . PHE   B 1 218 ? 53.952  -22.930 36.729 1.00 28.35 ? 910  PHE   B CD2 1 
ATOM   3974 C CE1 . PHE   B 1 218 ? 52.176  -21.503 35.184 1.00 28.43 ? 910  PHE   B CE1 1 
ATOM   3975 C CE2 . PHE   B 1 218 ? 54.411  -21.981 35.811 1.00 28.69 ? 910  PHE   B CE2 1 
ATOM   3976 C CZ  . PHE   B 1 218 ? 53.518  -21.280 35.046 1.00 28.02 ? 910  PHE   B CZ  1 
ATOM   3977 N N   . GLY   B 1 219 ? 50.865  -24.118 41.414 1.00 27.37 ? 911  GLY   B N   1 
ATOM   3978 C CA  . GLY   B 1 219 ? 50.365  -24.949 42.488 1.00 28.46 ? 911  GLY   B CA  1 
ATOM   3979 C C   . GLY   B 1 219 ? 51.379  -25.702 43.313 1.00 29.83 ? 911  GLY   B C   1 
ATOM   3980 O O   . GLY   B 1 219 ? 51.048  -26.768 43.835 1.00 30.67 ? 911  GLY   B O   1 
ATOM   3981 N N   . SER   B 1 220 ? 52.601  -25.170 43.470 1.00 30.11 ? 912  SER   B N   1 
ATOM   3982 C CA  . SER   B 1 220 ? 53.580  -25.829 44.342 1.00 30.99 ? 912  SER   B CA  1 
ATOM   3983 C C   . SER   B 1 220 ? 53.135  -25.633 45.805 1.00 31.90 ? 912  SER   B C   1 
ATOM   3984 O O   . SER   B 1 220 ? 52.457  -24.646 46.117 1.00 32.80 ? 912  SER   B O   1 
ATOM   3985 C CB  . SER   B 1 220 ? 54.982  -25.258 44.135 1.00 31.82 ? 912  SER   B CB  1 
ATOM   3986 O OG  . SER   B 1 220 ? 55.384  -25.356 42.779 1.00 33.25 ? 912  SER   B OG  1 
ATOM   3987 N N   . LYS   B 1 221 ? 53.458  -26.583 46.685 1.00 31.54 ? 913  LYS   B N   1 
ATOM   3988 C CA  . LYS   B 1 221 ? 53.094  -26.472 48.097 1.00 31.78 ? 913  LYS   B CA  1 
ATOM   3989 C C   . LYS   B 1 221 ? 54.056  -25.510 48.769 1.00 31.99 ? 913  LYS   B C   1 
ATOM   3990 O O   . LYS   B 1 221 ? 55.258  -25.589 48.537 1.00 32.41 ? 913  LYS   B O   1 
ATOM   3991 C CB  . LYS   B 1 221 ? 53.178  -27.840 48.782 1.00 33.60 ? 913  LYS   B CB  1 
ATOM   3992 C CG  . LYS   B 1 221 ? 52.095  -28.805 48.334 1.00 36.90 ? 913  LYS   B CG  1 
ATOM   3993 C CD  . LYS   B 1 221 ? 52.595  -30.239 48.315 1.00 40.16 ? 913  LYS   B CD  1 
ATOM   3994 C CE  . LYS   B 1 221 ? 51.551  -31.180 47.781 1.00 43.61 ? 913  LYS   B CE  1 
ATOM   3995 N NZ  . LYS   B 1 221 ? 51.117  -30.810 46.403 1.00 45.88 ? 913  LYS   B NZ  1 
ATOM   3996 N N   . PRO   B 1 222 ? 53.557  -24.548 49.559 1.00 31.41 ? 914  PRO   B N   1 
ATOM   3997 C CA  . PRO   B 1 222 ? 54.477  -23.594 50.212 1.00 30.53 ? 914  PRO   B CA  1 
ATOM   3998 C C   . PRO   B 1 222 ? 55.278  -24.297 51.297 1.00 29.95 ? 914  PRO   B C   1 
ATOM   3999 O O   . PRO   B 1 222 ? 54.737  -25.187 51.940 1.00 30.00 ? 914  PRO   B O   1 
ATOM   4000 C CB  . PRO   B 1 222 ? 53.536  -22.523 50.796 1.00 31.17 ? 914  PRO   B CB  1 
ATOM   4001 C CG  . PRO   B 1 222 ? 52.166  -22.810 50.220 1.00 31.75 ? 914  PRO   B CG  1 
ATOM   4002 C CD  . PRO   B 1 222 ? 52.151  -24.284 49.917 1.00 30.49 ? 914  PRO   B CD  1 
ATOM   4003 N N   . TYR   B 1 223 ? 56.568  -23.956 51.483 1.00 29.73 ? 915  TYR   B N   1 
ATOM   4004 C CA  . TYR   B 1 223 ? 57.418  -24.589 52.514 1.00 29.94 ? 915  TYR   B CA  1 
ATOM   4005 C C   . TYR   B 1 223 ? 57.349  -26.132 52.454 1.00 32.46 ? 915  TYR   B C   1 
ATOM   4006 O O   . TYR   B 1 223 ? 57.035  -26.782 53.458 1.00 32.62 ? 915  TYR   B O   1 
ATOM   4007 C CB  . TYR   B 1 223 ? 57.048  -24.096 53.925 1.00 28.18 ? 915  TYR   B CB  1 
ATOM   4008 C CG  . TYR   B 1 223 ? 56.756  -22.617 54.013 1.00 26.94 ? 915  TYR   B CG  1 
ATOM   4009 C CD1 . TYR   B 1 223 ? 57.785  -21.681 54.025 1.00 26.49 ? 915  TYR   B CD1 1 
ATOM   4010 C CD2 . TYR   B 1 223 ? 55.454  -22.153 54.117 1.00 27.00 ? 915  TYR   B CD2 1 
ATOM   4011 C CE1 . TYR   B 1 223 ? 57.522  -20.323 54.135 1.00 26.70 ? 915  TYR   B CE1 1 
ATOM   4012 C CE2 . TYR   B 1 223 ? 55.179  -20.798 54.210 1.00 27.26 ? 915  TYR   B CE2 1 
ATOM   4013 C CZ  . TYR   B 1 223 ? 56.214  -19.887 54.215 1.00 27.88 ? 915  TYR   B CZ  1 
ATOM   4014 O OH  . TYR   B 1 223 ? 55.924  -18.554 54.291 1.00 29.76 ? 915  TYR   B OH  1 
ATOM   4015 N N   . ASP   B 1 224 ? 57.519  -26.696 51.247 1.00 34.06 ? 916  ASP   B N   1 
ATOM   4016 C CA  . ASP   B 1 224 ? 57.413  -28.136 51.072 1.00 36.46 ? 916  ASP   B CA  1 
ATOM   4017 C C   . ASP   B 1 224 ? 58.465  -28.899 51.871 1.00 38.05 ? 916  ASP   B C   1 
ATOM   4018 O O   . ASP   B 1 224 ? 59.666  -28.625 51.755 1.00 37.59 ? 916  ASP   B O   1 
ATOM   4019 C CB  . ASP   B 1 224 ? 57.475  -28.531 49.586 1.00 39.11 ? 916  ASP   B CB  1 
ATOM   4020 C CG  . ASP   B 1 224 ? 56.770  -29.846 49.275 1.00 44.85 ? 916  ASP   B CG  1 
ATOM   4021 O OD1 . ASP   B 1 224 ? 56.015  -30.347 50.156 1.00 45.75 ? 916  ASP   B OD1 1 
ATOM   4022 O OD2 . ASP   B 1 224 ? 56.960  -30.369 48.151 1.00 47.16 ? 916  ASP   B OD2 1 
ATOM   4023 N N   . GLY   B 1 225 ? 57.987  -29.834 52.691 1.00 39.32 ? 917  GLY   B N   1 
ATOM   4024 C CA  . GLY   B 1 225 ? 58.850  -30.650 53.532 1.00 40.85 ? 917  GLY   B CA  1 
ATOM   4025 C C   . GLY   B 1 225 ? 59.006  -30.105 54.935 1.00 42.05 ? 917  GLY   B C   1 
ATOM   4026 O O   . GLY   B 1 225 ? 59.234  -30.875 55.875 1.00 42.48 ? 917  GLY   B O   1 
ATOM   4027 N N   . ILE   B 1 226 ? 58.918  -28.768 55.088 1.00 42.06 ? 918  ILE   B N   1 
ATOM   4028 C CA  . ILE   B 1 226 ? 59.023  -28.133 56.400 1.00 42.60 ? 918  ILE   B CA  1 
ATOM   4029 C C   . ILE   B 1 226 ? 57.745  -28.402 57.187 1.00 43.08 ? 918  ILE   B C   1 
ATOM   4030 O O   . ILE   B 1 226 ? 56.667  -28.014 56.738 1.00 43.37 ? 918  ILE   B O   1 
ATOM   4031 C CB  . ILE   B 1 226 ? 59.235  -26.608 56.264 1.00 42.99 ? 918  ILE   B CB  1 
ATOM   4032 C CG1 . ILE   B 1 226 ? 60.516  -26.283 55.481 1.00 44.03 ? 918  ILE   B CG1 1 
ATOM   4033 C CG2 . ILE   B 1 226 ? 59.217  -25.939 57.637 1.00 43.09 ? 918  ILE   B CG2 1 
ATOM   4034 C CD1 . ILE   B 1 226 ? 60.710  -24.796 55.181 1.00 45.31 ? 918  ILE   B CD1 1 
ATOM   4035 N N   . PRO   B 1 227 ? 57.830  -29.046 58.365 1.00 42.76 ? 919  PRO   B N   1 
ATOM   4036 C CA  . PRO   B 1 227 ? 56.606  -29.289 59.145 1.00 42.30 ? 919  PRO   B CA  1 
ATOM   4037 C C   . PRO   B 1 227 ? 56.010  -27.999 59.669 1.00 41.59 ? 919  PRO   B C   1 
ATOM   4038 O O   . PRO   B 1 227 ? 56.749  -27.076 59.998 1.00 41.61 ? 919  PRO   B O   1 
ATOM   4039 C CB  . PRO   B 1 227 ? 57.065  -30.208 60.279 1.00 43.26 ? 919  PRO   B CB  1 
ATOM   4040 C CG  . PRO   B 1 227 ? 58.513  -29.987 60.386 1.00 43.82 ? 919  PRO   B CG  1 
ATOM   4041 C CD  . PRO   B 1 227 ? 59.031  -29.565 59.041 1.00 42.21 ? 919  PRO   B CD  1 
ATOM   4042 N N   . ALA   B 1 228 ? 54.665  -27.937 59.721 1.00 41.15 ? 920  ALA   B N   1 
ATOM   4043 C CA  . ALA   B 1 228 ? 53.886  -26.772 60.153 1.00 40.58 ? 920  ALA   B CA  1 
ATOM   4044 C C   . ALA   B 1 228 ? 54.350  -26.180 61.475 1.00 40.15 ? 920  ALA   B C   1 
ATOM   4045 O O   . ALA   B 1 228 ? 54.398  -24.952 61.611 1.00 40.55 ? 920  ALA   B O   1 
ATOM   4046 C CB  . ALA   B 1 228 ? 52.416  -27.133 60.236 1.00 40.46 ? 920  ALA   B CB  1 
ATOM   4047 N N   . SER   B 1 229 ? 54.723  -27.047 62.435 1.00 39.00 ? 921  SER   B N   1 
ATOM   4048 C CA  . SER   B 1 229 ? 55.190  -26.632 63.756 1.00 38.58 ? 921  SER   B CA  1 
ATOM   4049 C C   . SER   B 1 229 ? 56.475  -25.790 63.744 1.00 37.69 ? 921  SER   B C   1 
ATOM   4050 O O   . SER   B 1 229 ? 56.751  -25.072 64.708 1.00 37.44 ? 921  SER   B O   1 
ATOM   4051 C CB  . SER   B 1 229 ? 55.342  -27.837 64.681 1.00 40.23 ? 921  SER   B CB  1 
ATOM   4052 O OG  . SER   B 1 229 ? 55.873  -28.978 64.027 1.00 43.06 ? 921  SER   B OG  1 
ATOM   4053 N N   . GLU   B 1 230 ? 57.238  -25.838 62.645 1.00 37.00 ? 922  GLU   B N   1 
ATOM   4054 C CA  . GLU   B 1 230 ? 58.481  -25.083 62.542 1.00 36.56 ? 922  GLU   B CA  1 
ATOM   4055 C C   . GLU   B 1 230 ? 58.362  -23.756 61.812 1.00 35.16 ? 922  GLU   B C   1 
ATOM   4056 O O   . GLU   B 1 230 ? 59.289  -22.957 61.892 1.00 35.54 ? 922  GLU   B O   1 
ATOM   4057 C CB  . GLU   B 1 230 ? 59.549  -25.928 61.856 1.00 40.16 ? 922  GLU   B CB  1 
ATOM   4058 C CG  . GLU   B 1 230 ? 59.869  -27.207 62.604 1.00 48.30 ? 922  GLU   B CG  1 
ATOM   4059 C CD  . GLU   B 1 230 ? 60.896  -28.107 61.942 1.00 57.92 ? 922  GLU   B CD  1 
ATOM   4060 O OE1 . GLU   B 1 230 ? 61.448  -27.718 60.885 1.00 59.46 ? 922  GLU   B OE1 1 
ATOM   4061 O OE2 . GLU   B 1 230 ? 61.136  -29.214 62.478 1.00 61.55 ? 922  GLU   B OE2 1 
ATOM   4062 N N   . ILE   B 1 231 ? 57.265  -23.535 61.069 1.00 33.42 ? 923  ILE   B N   1 
ATOM   4063 C CA  . ILE   B 1 231 ? 57.054  -22.339 60.243 1.00 31.81 ? 923  ILE   B CA  1 
ATOM   4064 C C   . ILE   B 1 231 ? 57.308  -21.003 60.960 1.00 29.79 ? 923  ILE   B C   1 
ATOM   4065 O O   . ILE   B 1 231 ? 57.965  -20.146 60.383 1.00 29.46 ? 923  ILE   B O   1 
ATOM   4066 C CB  . ILE   B 1 231 ? 55.649  -22.365 59.595 1.00 32.07 ? 923  ILE   B CB  1 
ATOM   4067 C CG1 . ILE   B 1 231 ? 55.500  -23.564 58.635 1.00 32.98 ? 923  ILE   B CG1 1 
ATOM   4068 C CG2 . ILE   B 1 231 ? 55.296  -21.033 58.903 1.00 32.29 ? 923  ILE   B CG2 1 
ATOM   4069 C CD1 . ILE   B 1 231 ? 56.426  -23.523 57.458 1.00 34.05 ? 923  ILE   B CD1 1 
ATOM   4070 N N   . SER   B 1 232 ? 56.785  -20.810 62.174 1.00 28.64 ? 924  SER   B N   1 
ATOM   4071 C CA  . SER   B 1 232 ? 56.970  -19.545 62.901 1.00 28.61 ? 924  SER   B CA  1 
ATOM   4072 C C   . SER   B 1 232 ? 58.441  -19.202 63.200 1.00 28.42 ? 924  SER   B C   1 
ATOM   4073 O O   . SER   B 1 232 ? 58.830  -18.032 63.108 1.00 28.47 ? 924  SER   B O   1 
ATOM   4074 C CB  . SER   B 1 232 ? 56.134  -19.519 64.179 1.00 29.55 ? 924  SER   B CB  1 
ATOM   4075 O OG  . SER   B 1 232 ? 56.432  -20.598 65.052 1.00 31.16 ? 924  SER   B OG  1 
ATOM   4076 N N   . SER   B 1 233 ? 59.262  -20.218 63.513 1.00 28.08 ? 925  SER   B N   1 
ATOM   4077 C CA  . SER   B 1 233 ? 60.696  -20.029 63.773 1.00 28.31 ? 925  SER   B CA  1 
ATOM   4078 C C   . SER   B 1 233 ? 61.370  -19.570 62.497 1.00 27.88 ? 925  SER   B C   1 
ATOM   4079 O O   . SER   B 1 233 ? 62.143  -18.606 62.509 1.00 28.02 ? 925  SER   B O   1 
ATOM   4080 C CB  . SER   B 1 233 ? 61.337  -21.335 64.241 1.00 30.20 ? 925  SER   B CB  1 
ATOM   4081 O OG  . SER   B 1 233 ? 60.700  -21.851 65.398 1.00 33.41 ? 925  SER   B OG  1 
ATOM   4082 N N   . ILE   B 1 234 ? 61.040  -20.246 61.378 1.00 27.09 ? 926  ILE   B N   1 
ATOM   4083 C CA  . ILE   B 1 234 ? 61.551  -19.935 60.048 1.00 26.88 ? 926  ILE   B CA  1 
ATOM   4084 C C   . ILE   B 1 234 ? 61.149  -18.513 59.635 1.00 25.54 ? 926  ILE   B C   1 
ATOM   4085 O O   . ILE   B 1 234 ? 61.963  -17.792 59.071 1.00 25.15 ? 926  ILE   B O   1 
ATOM   4086 C CB  . ILE   B 1 234 ? 61.050  -21.057 59.116 1.00 28.56 ? 926  ILE   B CB  1 
ATOM   4087 C CG1 . ILE   B 1 234 ? 62.038  -22.221 59.139 1.00 30.19 ? 926  ILE   B CG1 1 
ATOM   4088 C CG2 . ILE   B 1 234 ? 60.711  -20.604 57.681 1.00 29.40 ? 926  ILE   B CG2 1 
ATOM   4089 C CD1 . ILE   B 1 234 ? 61.480  -23.466 58.609 1.00 32.07 ? 926  ILE   B CD1 1 
ATOM   4090 N N   . LEU   B 1 235 ? 59.927  -18.074 60.007 1.00 24.73 ? 927  LEU   B N   1 
ATOM   4091 C CA  . LEU   B 1 235 ? 59.453  -16.734 59.686 1.00 24.55 ? 927  LEU   B CA  1 
ATOM   4092 C C   . LEU   B 1 235 ? 60.207  -15.676 60.476 1.00 25.11 ? 927  LEU   B C   1 
ATOM   4093 O O   . LEU   B 1 235 ? 60.760  -14.758 59.879 1.00 25.06 ? 927  LEU   B O   1 
ATOM   4094 C CB  . LEU   B 1 235 ? 57.933  -16.605 59.894 1.00 24.06 ? 927  LEU   B CB  1 
ATOM   4095 C CG  . LEU   B 1 235 ? 57.061  -17.432 58.965 1.00 25.01 ? 927  LEU   B CG  1 
ATOM   4096 C CD1 . LEU   B 1 235 ? 55.628  -17.226 59.285 1.00 25.31 ? 927  LEU   B CD1 1 
ATOM   4097 C CD2 . LEU   B 1 235 ? 57.347  -17.126 57.472 1.00 25.38 ? 927  LEU   B CD2 1 
ATOM   4098 N N   . GLU   B 1 236 ? 60.271  -15.811 61.803 1.00 25.67 ? 928  GLU   B N   1 
ATOM   4099 C CA  . GLU   B 1 236 ? 61.016  -14.876 62.647 1.00 26.76 ? 928  GLU   B CA  1 
ATOM   4100 C C   . GLU   B 1 236 ? 62.516  -14.747 62.238 1.00 27.35 ? 928  GLU   B C   1 
ATOM   4101 O O   . GLU   B 1 236 ? 63.104  -13.691 62.449 1.00 28.03 ? 928  GLU   B O   1 
ATOM   4102 C CB  . GLU   B 1 236 ? 60.853  -15.255 64.123 1.00 29.35 ? 928  GLU   B CB  1 
ATOM   4103 C CG  . GLU   B 1 236 ? 59.402  -15.220 64.540 1.00 36.05 ? 928  GLU   B CG  1 
ATOM   4104 C CD  . GLU   B 1 236 ? 59.109  -15.548 65.991 1.00 46.41 ? 928  GLU   B CD  1 
ATOM   4105 O OE1 . GLU   B 1 236 ? 58.994  -16.753 66.320 1.00 48.50 ? 928  GLU   B OE1 1 
ATOM   4106 O OE2 . GLU   B 1 236 ? 58.951  -14.596 66.793 1.00 49.11 ? 928  GLU   B OE2 1 
ATOM   4107 N N   . LYS   B 1 237 ? 63.118  -15.785 61.618 1.00 27.14 ? 929  LYS   B N   1 
ATOM   4108 C CA  . LYS   B 1 237 ? 64.509  -15.696 61.120 1.00 27.88 ? 929  LYS   B CA  1 
ATOM   4109 C C   . LYS   B 1 237 ? 64.634  -14.830 59.841 1.00 27.22 ? 929  LYS   B C   1 
ATOM   4110 O O   . LYS   B 1 237 ? 65.749  -14.533 59.418 1.00 27.31 ? 929  LYS   B O   1 
ATOM   4111 C CB  . LYS   B 1 237 ? 65.058  -17.080 60.714 1.00 30.91 ? 929  LYS   B CB  1 
ATOM   4112 C CG  . LYS   B 1 237 ? 65.436  -18.051 61.821 1.00 36.55 ? 929  LYS   B CG  1 
ATOM   4113 C CD  . LYS   B 1 237 ? 66.210  -19.283 61.256 1.00 42.07 ? 929  LYS   B CD  1 
ATOM   4114 C CE  . LYS   B 1 237 ? 65.704  -19.801 59.911 1.00 45.72 ? 929  LYS   B CE  1 
ATOM   4115 N NZ  . LYS   B 1 237 ? 65.734  -21.286 59.821 1.00 47.74 ? 929  LYS   B NZ  1 
ATOM   4116 N N   . GLY   B 1 238 ? 63.523  -14.550 59.172 1.00 26.31 ? 930  GLY   B N   1 
ATOM   4117 C CA  . GLY   B 1 238 ? 63.536  -13.803 57.923 1.00 26.13 ? 930  GLY   B CA  1 
ATOM   4118 C C   . GLY   B 1 238 ? 63.325  -14.667 56.690 1.00 25.74 ? 930  GLY   B C   1 
ATOM   4119 O O   . GLY   B 1 238 ? 63.197  -14.138 55.586 1.00 26.07 ? 930  GLY   B O   1 
ATOM   4120 N N   . GLU   B 1 239 ? 63.292  -16.001 56.855 1.00 25.00 ? 931  GLU   B N   1 
ATOM   4121 C CA  . GLU   B 1 239 ? 63.065  -16.914 55.744 1.00 25.37 ? 931  GLU   B CA  1 
ATOM   4122 C C   . GLU   B 1 239 ? 61.655  -16.678 55.177 1.00 25.02 ? 931  GLU   B C   1 
ATOM   4123 O O   . GLU   B 1 239 ? 60.707  -16.495 55.939 1.00 26.08 ? 931  GLU   B O   1 
ATOM   4124 C CB  . GLU   B 1 239 ? 63.177  -18.373 56.206 1.00 28.39 ? 931  GLU   B CB  1 
ATOM   4125 C CG  . GLU   B 1 239 ? 64.554  -18.988 56.060 1.00 35.45 ? 931  GLU   B CG  1 
ATOM   4126 C CD  . GLU   B 1 239 ? 64.510  -20.362 55.415 1.00 46.57 ? 931  GLU   B CD  1 
ATOM   4127 O OE1 . GLU   B 1 239 ? 64.534  -21.371 56.159 1.00 48.22 ? 931  GLU   B OE1 1 
ATOM   4128 O OE2 . GLU   B 1 239 ? 64.433  -20.428 54.164 1.00 50.37 ? 931  GLU   B OE2 1 
ATOM   4129 N N   . ARG   B 1 240 ? 61.540  -16.633 53.850 1.00 23.06 ? 932  ARG   B N   1 
ATOM   4130 C CA  . ARG   B 1 240 ? 60.297  -16.408 53.130 1.00 21.45 ? 932  ARG   B CA  1 
ATOM   4131 C C   . ARG   B 1 240 ? 60.208  -17.388 51.961 1.00 21.04 ? 932  ARG   B C   1 
ATOM   4132 O O   . ARG   B 1 240 ? 61.184  -18.084 51.669 1.00 22.17 ? 932  ARG   B O   1 
ATOM   4133 C CB  . ARG   B 1 240 ? 60.244  -14.963 52.596 1.00 21.61 ? 932  ARG   B CB  1 
ATOM   4134 C CG  . ARG   B 1 240 ? 60.017  -13.882 53.655 1.00 22.71 ? 932  ARG   B CG  1 
ATOM   4135 C CD  . ARG   B 1 240 ? 58.762  -14.077 54.486 1.00 23.69 ? 932  ARG   B CD  1 
ATOM   4136 N NE  . ARG   B 1 240 ? 58.610  -13.000 55.465 1.00 25.72 ? 932  ARG   B NE  1 
ATOM   4137 C CZ  . ARG   B 1 240 ? 59.147  -13.007 56.687 1.00 25.24 ? 932  ARG   B CZ  1 
ATOM   4138 N NH1 . ARG   B 1 240 ? 59.847  -14.053 57.107 1.00 22.65 ? 932  ARG   B NH1 1 
ATOM   4139 N NH2 . ARG   B 1 240 ? 58.978  -11.970 57.498 1.00 24.29 ? 932  ARG   B NH2 1 
ATOM   4140 N N   . LEU   B 1 241 ? 59.049  -17.463 51.289 1.00 19.57 ? 933  LEU   B N   1 
ATOM   4141 C CA  . LEU   B 1 241 ? 58.872  -18.338 50.132 1.00 18.49 ? 933  LEU   B CA  1 
ATOM   4142 C C   . LEU   B 1 241 ? 59.832  -17.904 48.994 1.00 18.94 ? 933  LEU   B C   1 
ATOM   4143 O O   . LEU   B 1 241 ? 60.109  -16.712 48.837 1.00 18.89 ? 933  LEU   B O   1 
ATOM   4144 C CB  . LEU   B 1 241 ? 57.425  -18.263 49.652 1.00 16.98 ? 933  LEU   B CB  1 
ATOM   4145 C CG  . LEU   B 1 241 ? 56.393  -18.923 50.536 1.00 16.37 ? 933  LEU   B CG  1 
ATOM   4146 C CD1 . LEU   B 1 241 ? 54.948  -18.580 50.042 1.00 16.14 ? 933  LEU   B CD1 1 
ATOM   4147 C CD2 . LEU   B 1 241 ? 56.620  -20.434 50.613 1.00 15.69 ? 933  LEU   B CD2 1 
ATOM   4148 N N   . PRO   B 1 242 ? 60.420  -18.858 48.249 1.00 18.90 ? 934  PRO   B N   1 
ATOM   4149 C CA  . PRO   B 1 242 ? 61.383  -18.460 47.200 1.00 19.40 ? 934  PRO   B CA  1 
ATOM   4150 C C   . PRO   B 1 242 ? 60.758  -17.726 46.000 1.00 20.43 ? 934  PRO   B C   1 
ATOM   4151 O O   . PRO   B 1 242 ? 59.540  -17.737 45.799 1.00 20.72 ? 934  PRO   B O   1 
ATOM   4152 C CB  . PRO   B 1 242 ? 62.038  -19.784 46.798 1.00 19.44 ? 934  PRO   B CB  1 
ATOM   4153 C CG  . PRO   B 1 242 ? 60.992  -20.827 47.139 1.00 19.49 ? 934  PRO   B CG  1 
ATOM   4154 C CD  . PRO   B 1 242 ? 60.279  -20.328 48.352 1.00 17.63 ? 934  PRO   B CD  1 
ATOM   4155 N N   . GLN   B 1 243 ? 61.602  -17.077 45.207 1.00 20.60 ? 935  GLN   B N   1 
ATOM   4156 C CA  . GLN   B 1 243 ? 61.159  -16.372 44.019 1.00 21.21 ? 935  GLN   B CA  1 
ATOM   4157 C C   . GLN   B 1 243 ? 60.773  -17.370 42.930 1.00 21.40 ? 935  GLN   B C   1 
ATOM   4158 O O   . GLN   B 1 243 ? 61.624  -18.122 42.495 1.00 21.23 ? 935  GLN   B O   1 
ATOM   4159 C CB  . GLN   B 1 243 ? 62.256  -15.421 43.530 1.00 22.18 ? 935  GLN   B CB  1 
ATOM   4160 C CG  . GLN   B 1 243 ? 61.900  -14.727 42.231 1.00 25.56 ? 935  GLN   B CG  1 
ATOM   4161 C CD  . GLN   B 1 243 ? 62.963  -13.770 41.773 1.00 30.25 ? 935  GLN   B CD  1 
ATOM   4162 O OE1 . GLN   B 1 243 ? 63.728  -13.196 42.567 1.00 32.38 ? 935  GLN   B OE1 1 
ATOM   4163 N NE2 . GLN   B 1 243 ? 63.021  -13.562 40.477 1.00 30.41 ? 935  GLN   B NE2 1 
ATOM   4164 N N   . PRO   B 1 244 ? 59.496  -17.400 42.486 1.00 21.89 ? 936  PRO   B N   1 
ATOM   4165 C CA  . PRO   B 1 244 ? 59.107  -18.330 41.409 1.00 21.98 ? 936  PRO   B CA  1 
ATOM   4166 C C   . PRO   B 1 244 ? 59.844  -18.031 40.099 1.00 22.01 ? 936  PRO   B C   1 
ATOM   4167 O O   . PRO   B 1 244 ? 60.070  -16.880 39.759 1.00 21.95 ? 936  PRO   B O   1 
ATOM   4168 C CB  . PRO   B 1 244 ? 57.594  -18.101 41.276 1.00 23.11 ? 936  PRO   B CB  1 
ATOM   4169 C CG  . PRO   B 1 244 ? 57.179  -17.441 42.584 1.00 23.46 ? 936  PRO   B CG  1 
ATOM   4170 C CD  . PRO   B 1 244 ? 58.358  -16.566 42.907 1.00 21.54 ? 936  PRO   B CD  1 
ATOM   4171 N N   . PRO   B 1 245 ? 60.247  -19.070 39.358 1.00 22.65 ? 937  PRO   B N   1 
ATOM   4172 C CA  . PRO   B 1 245 ? 61.050  -18.857 38.133 1.00 22.64 ? 937  PRO   B CA  1 
ATOM   4173 C C   . PRO   B 1 245 ? 60.437  -17.996 37.018 1.00 22.61 ? 937  PRO   B C   1 
ATOM   4174 O O   . PRO   B 1 245 ? 61.161  -17.561 36.116 1.00 22.53 ? 937  PRO   B O   1 
ATOM   4175 C CB  . PRO   B 1 245 ? 61.315  -20.284 37.634 1.00 23.40 ? 937  PRO   B CB  1 
ATOM   4176 C CG  . PRO   B 1 245 ? 61.186  -21.142 38.850 1.00 24.15 ? 937  PRO   B CG  1 
ATOM   4177 C CD  . PRO   B 1 245 ? 60.108  -20.507 39.675 1.00 22.62 ? 937  PRO   B CD  1 
ATOM   4178 N N   . ILE   B 1 246 ? 59.122  -17.786 37.032 1.00 22.12 ? 938  ILE   B N   1 
ATOM   4179 C CA  . ILE   B 1 246 ? 58.489  -16.935 36.011 1.00 22.20 ? 938  ILE   B CA  1 
ATOM   4180 C C   . ILE   B 1 246 ? 58.408  -15.457 36.443 1.00 22.48 ? 938  ILE   B C   1 
ATOM   4181 O O   . ILE   B 1 246 ? 58.073  -14.607 35.629 1.00 22.63 ? 938  ILE   B O   1 
ATOM   4182 C CB  . ILE   B 1 246 ? 57.107  -17.482 35.604 1.00 22.33 ? 938  ILE   B CB  1 
ATOM   4183 C CG1 . ILE   B 1 246 ? 56.070  -17.283 36.729 1.00 23.39 ? 938  ILE   B CG1 1 
ATOM   4184 C CG2 . ILE   B 1 246 ? 57.212  -18.940 35.195 1.00 22.53 ? 938  ILE   B CG2 1 
ATOM   4185 C CD1 . ILE   B 1 246 ? 54.632  -17.580 36.303 1.00 24.06 ? 938  ILE   B CD1 1 
ATOM   4186 N N   . CYS   B 1 247 ? 58.696  -15.154 37.716 1.00 22.02 ? 939  CYS   B N   1 
ATOM   4187 C CA  . CYS   B 1 247 ? 58.573  -13.818 38.261 1.00 22.66 ? 939  CYS   B CA  1 
ATOM   4188 C C   . CYS   B 1 247 ? 59.792  -12.945 38.130 1.00 22.37 ? 939  CYS   B C   1 
ATOM   4189 O O   . CYS   B 1 247 ? 60.829  -13.274 38.667 1.00 22.02 ? 939  CYS   B O   1 
ATOM   4190 C CB  . CYS   B 1 247 ? 58.147  -13.892 39.726 1.00 24.16 ? 939  CYS   B CB  1 
ATOM   4191 S SG  . CYS   B 1 247 ? 56.534  -14.652 39.990 1.00 28.91 ? 939  CYS   B SG  1 
ATOM   4192 N N   . THR   B 1 248 ? 59.593  -11.740 37.636 1.00 22.55 ? 940  THR   B N   1 
ATOM   4193 C CA  . THR   B 1 248 ? 60.615  -10.719 37.665 1.00 23.35 ? 940  THR   B CA  1 
ATOM   4194 C C   . THR   B 1 248 ? 60.727  -10.209 39.119 1.00 24.42 ? 940  THR   B C   1 
ATOM   4195 O O   . THR   B 1 248 ? 59.846  -10.450 39.956 1.00 24.38 ? 940  THR   B O   1 
ATOM   4196 C CB  . THR   B 1 248 ? 60.271  -9.614  36.700 1.00 24.43 ? 940  THR   B CB  1 
ATOM   4197 O OG1 . THR   B 1 248 ? 58.987  -9.127  37.051 1.00 25.85 ? 940  THR   B OG1 1 
ATOM   4198 C CG2 . THR   B 1 248 ? 60.320  -10.067 35.244 1.00 24.44 ? 940  THR   B CG2 1 
ATOM   4199 N N   . ILE   B 1 249 ? 61.814  -9.510  39.419 1.00 25.34 ? 941  ILE   B N   1 
ATOM   4200 C CA  . ILE   B 1 249 ? 62.077  -9.013  40.761 1.00 26.67 ? 941  ILE   B CA  1 
ATOM   4201 C C   . ILE   B 1 249 ? 60.976  -8.050  41.248 1.00 27.82 ? 941  ILE   B C   1 
ATOM   4202 O O   . ILE   B 1 249 ? 60.680  -8.046  42.440 1.00 28.42 ? 941  ILE   B O   1 
ATOM   4203 C CB  . ILE   B 1 249 ? 63.522  -8.427  40.873 1.00 27.05 ? 941  ILE   B CB  1 
ATOM   4204 C CG1 . ILE   B 1 249 ? 63.958  -8.291  42.331 1.00 28.03 ? 941  ILE   B CG1 1 
ATOM   4205 C CG2 . ILE   B 1 249 ? 63.697  -7.134  40.096 1.00 27.46 ? 941  ILE   B CG2 1 
ATOM   4206 C CD1 . ILE   B 1 249 ? 63.998  -9.607  43.052 1.00 29.40 ? 941  ILE   B CD1 1 
ATOM   4207 N N   . ASP   B 1 250 ? 60.315  -7.309  40.332 1.00 27.59 ? 942  ASP   B N   1 
ATOM   4208 C CA  . ASP   B 1 250 ? 59.229  -6.398  40.694 1.00 28.00 ? 942  ASP   B CA  1 
ATOM   4209 C C   . ASP   B 1 250 ? 58.023  -7.174  41.250 1.00 27.36 ? 942  ASP   B C   1 
ATOM   4210 O O   . ASP   B 1 250 ? 57.395  -6.741  42.205 1.00 27.78 ? 942  ASP   B O   1 
ATOM   4211 C CB  . ASP   B 1 250 ? 58.793  -5.579  39.475 1.00 30.78 ? 942  ASP   B CB  1 
ATOM   4212 C CG  . ASP   B 1 250 ? 59.822  -4.575  39.014 1.00 38.22 ? 942  ASP   B CG  1 
ATOM   4213 O OD1 . ASP   B 1 250 ? 60.558  -4.041  39.875 1.00 39.82 ? 942  ASP   B OD1 1 
ATOM   4214 O OD2 . ASP   B 1 250 ? 59.888  -4.313  37.790 1.00 41.17 ? 942  ASP   B OD2 1 
ATOM   4215 N N   . VAL   B 1 251 ? 57.732  -8.331  40.677 1.00 26.41 ? 943  VAL   B N   1 
ATOM   4216 C CA  . VAL   B 1 251 ? 56.630  -9.172  41.127 1.00 26.18 ? 943  VAL   B CA  1 
ATOM   4217 C C   . VAL   B 1 251 ? 56.975  -9.810  42.480 1.00 25.12 ? 943  VAL   B C   1 
ATOM   4218 O O   . VAL   B 1 251 ? 56.161  -9.797  43.417 1.00 24.79 ? 943  VAL   B O   1 
ATOM   4219 C CB  . VAL   B 1 251 ? 56.323  -10.215 40.038 1.00 27.52 ? 943  VAL   B CB  1 
ATOM   4220 C CG1 . VAL   B 1 251 ? 55.213  -11.160 40.472 1.00 28.06 ? 943  VAL   B CG1 1 
ATOM   4221 C CG2 . VAL   B 1 251 ? 55.945  -9.518  38.736 1.00 28.65 ? 943  VAL   B CG2 1 
ATOM   4222 N N   . TYR   B 1 252 ? 58.210  -10.314 42.598 1.00 24.29 ? 944  TYR   B N   1 
ATOM   4223 C CA  . TYR   B 1 252 ? 58.660  -10.918 43.832 1.00 24.40 ? 944  TYR   B CA  1 
ATOM   4224 C C   . TYR   B 1 252 ? 58.683  -9.916  44.992 1.00 24.23 ? 944  TYR   B C   1 
ATOM   4225 O O   . TYR   B 1 252 ? 58.250  -10.271 46.081 1.00 23.95 ? 944  TYR   B O   1 
ATOM   4226 C CB  . TYR   B 1 252 ? 60.006  -11.622 43.649 1.00 25.12 ? 944  TYR   B CB  1 
ATOM   4227 C CG  . TYR   B 1 252 ? 60.392  -12.461 44.844 1.00 26.37 ? 944  TYR   B CG  1 
ATOM   4228 C CD1 . TYR   B 1 252 ? 59.510  -13.384 45.382 1.00 27.24 ? 944  TYR   B CD1 1 
ATOM   4229 C CD2 . TYR   B 1 252 ? 61.639  -12.326 45.442 1.00 27.47 ? 944  TYR   B CD2 1 
ATOM   4230 C CE1 . TYR   B 1 252 ? 59.847  -14.141 46.492 1.00 28.17 ? 944  TYR   B CE1 1 
ATOM   4231 C CE2 . TYR   B 1 252 ? 62.001  -13.104 46.538 1.00 28.15 ? 944  TYR   B CE2 1 
ATOM   4232 C CZ  . TYR   B 1 252 ? 61.105  -14.019 47.051 1.00 29.09 ? 944  TYR   B CZ  1 
ATOM   4233 O OH  . TYR   B 1 252 ? 61.423  -14.791 48.141 1.00 30.40 ? 944  TYR   B OH  1 
ATOM   4234 N N   . MET   B 1 253 ? 59.088  -8.652  44.755 1.00 24.19 ? 945  MET   B N   1 
ATOM   4235 C CA  . MET   B 1 253 ? 59.066  -7.642  45.821 1.00 24.59 ? 945  MET   B CA  1 
ATOM   4236 C C   . MET   B 1 253 ? 57.646  -7.314  46.347 1.00 23.79 ? 945  MET   B C   1 
ATOM   4237 O O   . MET   B 1 253 ? 57.496  -7.119  47.555 1.00 23.77 ? 945  MET   B O   1 
ATOM   4238 C CB  . MET   B 1 253 ? 59.817  -6.369  45.438 1.00 26.54 ? 945  MET   B CB  1 
ATOM   4239 C CG  . MET   B 1 253 ? 61.337  -6.565  45.281 1.00 31.95 ? 945  MET   B CG  1 
ATOM   4240 S SD  . MET   B 1 253 ? 62.198  -7.682  46.458 1.00 46.18 ? 945  MET   B SD  1 
ATOM   4241 C CE  . MET   B 1 253 ? 61.883  -6.828  48.043 1.00 42.13 ? 945  MET   B CE  1 
ATOM   4242 N N   . ILE   B 1 254 ? 56.603  -7.319  45.475 1.00 22.86 ? 946  ILE   B N   1 
ATOM   4243 C CA  . ILE   B 1 254 ? 55.212  -7.111  45.912 1.00 21.84 ? 946  ILE   B CA  1 
ATOM   4244 C C   . ILE   B 1 254 ? 54.819  -8.290  46.826 1.00 20.38 ? 946  ILE   B C   1 
ATOM   4245 O O   . ILE   B 1 254 ? 54.271  -8.067  47.916 1.00 20.54 ? 946  ILE   B O   1 
ATOM   4246 C CB  . ILE   B 1 254 ? 54.243  -7.064  44.707 1.00 22.39 ? 946  ILE   B CB  1 
ATOM   4247 C CG1 . ILE   B 1 254 ? 54.602  -5.980  43.695 1.00 23.37 ? 946  ILE   B CG1 1 
ATOM   4248 C CG2 . ILE   B 1 254 ? 52.821  -6.934  45.189 1.00 22.49 ? 946  ILE   B CG2 1 
ATOM   4249 C CD1 . ILE   B 1 254 ? 53.782  -6.129  42.424 1.00 24.57 ? 946  ILE   B CD1 1 
ATOM   4250 N N   . MET   B 1 255 ? 55.157  -9.541  46.401 1.00 18.92 ? 947  MET   B N   1 
ATOM   4251 C CA  . MET   B 1 255 ? 54.901  -10.740 47.188 1.00 19.15 ? 947  MET   B CA  1 
ATOM   4252 C C   . MET   B 1 255 ? 55.636  -10.651 48.534 1.00 19.61 ? 947  MET   B C   1 
ATOM   4253 O O   . MET   B 1 255 ? 55.057  -10.952 49.583 1.00 19.37 ? 947  MET   B O   1 
ATOM   4254 C CB  . MET   B 1 255 ? 55.373  -11.986 46.441 1.00 20.11 ? 947  MET   B CB  1 
ATOM   4255 C CG  . MET   B 1 255 ? 54.545  -12.333 45.247 1.00 24.56 ? 947  MET   B CG  1 
ATOM   4256 S SD  . MET   B 1 255 ? 55.229  -13.708 44.268 1.00 29.82 ? 947  MET   B SD  1 
ATOM   4257 C CE  . MET   B 1 255 ? 55.450  -14.891 45.552 1.00 25.77 ? 947  MET   B CE  1 
ATOM   4258 N N   . ARG   B 1 256 ? 56.908  -10.190 48.496 1.00 19.79 ? 948  ARG   B N   1 
ATOM   4259 C CA  . ARG   B 1 256 ? 57.745  -10.032 49.679 1.00 20.71 ? 948  ARG   B CA  1 
ATOM   4260 C C   . ARG   B 1 256 ? 57.131  -9.023  50.652 1.00 20.68 ? 948  ARG   B C   1 
ATOM   4261 O O   . ARG   B 1 256 ? 57.127  -9.277  51.860 1.00 20.81 ? 948  ARG   B O   1 
ATOM   4262 C CB  . ARG   B 1 256 ? 59.198  -9.632  49.306 1.00 22.25 ? 948  ARG   B CB  1 
ATOM   4263 C CG  . ARG   B 1 256 ? 60.069  -10.788 48.794 1.00 26.39 ? 948  ARG   B CG  1 
ATOM   4264 C CD  . ARG   B 1 256 ? 60.281  -11.886 49.821 1.00 31.31 ? 948  ARG   B CD  1 
ATOM   4265 N NE  . ARG   B 1 256 ? 61.158  -11.427 50.906 1.00 35.52 ? 948  ARG   B NE  1 
ATOM   4266 C CZ  . ARG   B 1 256 ? 62.444  -11.744 51.023 1.00 36.46 ? 948  ARG   B CZ  1 
ATOM   4267 N NH1 . ARG   B 1 256 ? 63.162  -11.264 52.028 1.00 35.63 ? 948  ARG   B NH1 1 
ATOM   4268 N NH2 . ARG   B 1 256 ? 63.021  -12.542 50.132 1.00 35.68 ? 948  ARG   B NH2 1 
ATOM   4269 N N   . LYS   B 1 257 ? 56.611  -7.896  50.127 1.00 19.96 ? 949  LYS   B N   1 
ATOM   4270 C CA  . LYS   B 1 257 ? 55.976  -6.846  50.916 1.00 20.37 ? 949  LYS   B CA  1 
ATOM   4271 C C   . LYS   B 1 257 ? 54.788  -7.436  51.726 1.00 20.03 ? 949  LYS   B C   1 
ATOM   4272 O O   . LYS   B 1 257 ? 54.598  -7.091  52.892 1.00 19.93 ? 949  LYS   B O   1 
ATOM   4273 C CB  . LYS   B 1 257 ? 55.471  -5.731  49.969 1.00 22.75 ? 949  LYS   B CB  1 
ATOM   4274 C CG  . LYS   B 1 257 ? 56.202  -4.390  50.047 1.00 25.88 ? 949  LYS   B CG  1 
ATOM   4275 C CD  . LYS   B 1 257 ? 55.806  -3.480  48.870 1.00 29.92 ? 949  LYS   B CD  1 
ATOM   4276 C CE  . LYS   B 1 257 ? 56.698  -3.690  47.645 1.00 33.93 ? 949  LYS   B CE  1 
ATOM   4277 N NZ  . LYS   B 1 257 ? 55.932  -3.703  46.352 1.00 36.06 ? 949  LYS   B NZ  1 
ATOM   4278 N N   . CYS   B 1 258 ? 53.999  -8.340  51.087 1.00 19.40 ? 950  CYS   B N   1 
ATOM   4279 C CA  . CYS   B 1 258 ? 52.861  -9.024  51.695 1.00 18.51 ? 950  CYS   B CA  1 
ATOM   4280 C C   . CYS   B 1 258 ? 53.272  -9.810  52.951 1.00 18.97 ? 950  CYS   B C   1 
ATOM   4281 O O   . CYS   B 1 258 ? 52.422  -10.037 53.822 1.00 19.44 ? 950  CYS   B O   1 
ATOM   4282 C CB  . CYS   B 1 258 ? 52.183  -9.940  50.683 1.00 18.29 ? 950  CYS   B CB  1 
ATOM   4283 S SG  . CYS   B 1 258 ? 51.355  -9.078  49.316 1.00 18.94 ? 950  CYS   B SG  1 
ATOM   4284 N N   . TRP   B 1 259 ? 54.546  -10.242 53.041 1.00 18.11 ? 951  TRP   B N   1 
ATOM   4285 C CA  . TRP   B 1 259 ? 54.980  -11.011 54.189 1.00 19.05 ? 951  TRP   B CA  1 
ATOM   4286 C C   . TRP   B 1 259 ? 55.898  -10.261 55.146 1.00 20.26 ? 951  TRP   B C   1 
ATOM   4287 O O   . TRP   B 1 259 ? 56.684  -10.890 55.860 1.00 20.65 ? 951  TRP   B O   1 
ATOM   4288 C CB  . TRP   B 1 259 ? 55.602  -12.357 53.807 1.00 19.15 ? 951  TRP   B CB  1 
ATOM   4289 C CG  . TRP   B 1 259 ? 54.860  -13.081 52.730 1.00 19.32 ? 951  TRP   B CG  1 
ATOM   4290 C CD1 . TRP   B 1 259 ? 53.508  -13.261 52.630 1.00 19.97 ? 951  TRP   B CD1 1 
ATOM   4291 C CD2 . TRP   B 1 259 ? 55.438  -13.698 51.580 1.00 19.18 ? 951  TRP   B CD2 1 
ATOM   4292 N NE1 . TRP   B 1 259 ? 53.209  -13.953 51.483 1.00 20.12 ? 951  TRP   B NE1 1 
ATOM   4293 C CE2 . TRP   B 1 259 ? 54.381  -14.248 50.824 1.00 19.93 ? 951  TRP   B CE2 1 
ATOM   4294 C CE3 . TRP   B 1 259 ? 56.751  -13.827 51.102 1.00 19.29 ? 951  TRP   B CE3 1 
ATOM   4295 C CZ2 . TRP   B 1 259 ? 54.603  -14.928 49.624 1.00 19.84 ? 951  TRP   B CZ2 1 
ATOM   4296 C CZ3 . TRP   B 1 259 ? 56.961  -14.505 49.921 1.00 19.86 ? 951  TRP   B CZ3 1 
ATOM   4297 C CH2 . TRP   B 1 259 ? 55.891  -15.038 49.191 1.00 19.70 ? 951  TRP   B CH2 1 
ATOM   4298 N N   . MET   B 1 260 ? 55.762  -8.939  55.216 1.00 20.76 ? 952  MET   B N   1 
ATOM   4299 C CA  . MET   B 1 260 ? 56.491  -8.167  56.200 1.00 22.27 ? 952  MET   B CA  1 
ATOM   4300 C C   . MET   B 1 260 ? 55.934  -8.427  57.614 1.00 22.67 ? 952  MET   B C   1 
ATOM   4301 O O   . MET   B 1 260 ? 54.757  -8.746  57.756 1.00 22.60 ? 952  MET   B O   1 
ATOM   4302 C CB  . MET   B 1 260 ? 56.498  -6.695  55.826 1.00 24.13 ? 952  MET   B CB  1 
ATOM   4303 C CG  . MET   B 1 260 ? 57.670  -6.375  54.954 1.00 29.53 ? 952  MET   B CG  1 
ATOM   4304 S SD  . MET   B 1 260 ? 57.389  -4.827  54.107 1.00 45.45 ? 952  MET   B SD  1 
ATOM   4305 C CE  . MET   B 1 260 ? 58.793  -3.878  54.753 1.00 43.69 ? 952  MET   B CE  1 
ATOM   4306 N N   . ILE   B 1 261 ? 56.790  -8.366  58.652 1.00 22.79 ? 953  ILE   B N   1 
ATOM   4307 C CA  . ILE   B 1 261 ? 56.395  -8.644  60.043 1.00 23.42 ? 953  ILE   B CA  1 
ATOM   4308 C C   . ILE   B 1 261 ? 55.420  -7.598  60.558 1.00 23.18 ? 953  ILE   B C   1 
ATOM   4309 O O   . ILE   B 1 261 ? 54.458  -7.917  61.258 1.00 22.97 ? 953  ILE   B O   1 
ATOM   4310 C CB  . ILE   B 1 261 ? 57.661  -8.702  60.942 1.00 25.02 ? 953  ILE   B CB  1 
ATOM   4311 C CG1 . ILE   B 1 261 ? 58.613  -9.829  60.505 1.00 26.36 ? 953  ILE   B CG1 1 
ATOM   4312 C CG2 . ILE   B 1 261 ? 57.293  -8.797  62.435 1.00 25.73 ? 953  ILE   B CG2 1 
ATOM   4313 C CD1 . ILE   B 1 261 ? 58.096  -11.236 60.725 1.00 28.02 ? 953  ILE   B CD1 1 
ATOM   4314 N N   . ASP   B 1 262 ? 55.696  -6.340  60.236 1.00 23.34 ? 954  ASP   B N   1 
ATOM   4315 C CA  . ASP   B 1 262 ? 54.860  -5.232  60.625 1.00 24.55 ? 954  ASP   B CA  1 
ATOM   4316 C C   . ASP   B 1 262 ? 53.702  -5.255  59.642 1.00 25.58 ? 954  ASP   B C   1 
ATOM   4317 O O   . ASP   B 1 262 ? 53.913  -5.068  58.437 1.00 26.40 ? 954  ASP   B O   1 
ATOM   4318 C CB  . ASP   B 1 262 ? 55.654  -3.940  60.495 1.00 26.84 ? 954  ASP   B CB  1 
ATOM   4319 C CG  . ASP   B 1 262 ? 54.840  -2.714  60.802 1.00 34.28 ? 954  ASP   B CG  1 
ATOM   4320 O OD1 . ASP   B 1 262 ? 53.985  -2.784  61.711 1.00 35.83 ? 954  ASP   B OD1 1 
ATOM   4321 O OD2 . ASP   B 1 262 ? 55.050  -1.685  60.133 1.00 37.49 ? 954  ASP   B OD2 1 
ATOM   4322 N N   . ALA   B 1 263 ? 52.502  -5.557  60.141 1.00 25.35 ? 955  ALA   B N   1 
ATOM   4323 C CA  . ALA   B 1 263 ? 51.276  -5.702  59.361 1.00 26.18 ? 955  ALA   B CA  1 
ATOM   4324 C C   . ALA   B 1 263 ? 50.929  -4.468  58.547 1.00 27.26 ? 955  ALA   B C   1 
ATOM   4325 O O   . ALA   B 1 263 ? 50.512  -4.590  57.406 1.00 27.21 ? 955  ALA   B O   1 
ATOM   4326 C CB  . ALA   B 1 263 ? 50.113  -6.056  60.283 1.00 26.09 ? 955  ALA   B CB  1 
ATOM   4327 N N   . ASP   B 1 264 ? 51.124  -3.277  59.128 1.00 27.98 ? 956  ASP   B N   1 
ATOM   4328 C CA  . ASP   B 1 264 ? 50.811  -2.003  58.483 1.00 28.83 ? 956  ASP   B CA  1 
ATOM   4329 C C   . ASP   B 1 264 ? 51.775  -1.638  57.349 1.00 28.73 ? 956  ASP   B C   1 
ATOM   4330 O O   . ASP   B 1 264 ? 51.466  -0.743  56.576 1.00 29.33 ? 956  ASP   B O   1 
ATOM   4331 C CB  . ASP   B 1 264 ? 50.735  -0.878  59.517 1.00 32.01 ? 956  ASP   B CB  1 
ATOM   4332 C CG  . ASP   B 1 264 ? 49.936  -1.214  60.770 1.00 40.32 ? 956  ASP   B CG  1 
ATOM   4333 O OD1 . ASP   B 1 264 ? 48.918  -0.529  61.025 1.00 42.83 ? 956  ASP   B OD1 1 
ATOM   4334 O OD2 . ASP   B 1 264 ? 50.343  -2.152  61.514 1.00 42.57 ? 956  ASP   B OD2 1 
ATOM   4335 N N   . SER   B 1 265 ? 52.937  -2.307  57.255 1.00 27.90 ? 957  SER   B N   1 
ATOM   4336 C CA  . SER   B 1 265 ? 53.896  -2.117  56.173 1.00 27.78 ? 957  SER   B CA  1 
ATOM   4337 C C   . SER   B 1 265 ? 53.490  -2.880  54.904 1.00 27.50 ? 957  SER   B C   1 
ATOM   4338 O O   . SER   B 1 265 ? 54.012  -2.597  53.826 1.00 27.56 ? 957  SER   B O   1 
ATOM   4339 C CB  . SER   B 1 265 ? 55.279  -2.582  56.605 1.00 29.50 ? 957  SER   B CB  1 
ATOM   4340 O OG  . SER   B 1 265 ? 55.919  -1.553  57.334 1.00 33.07 ? 957  SER   B OG  1 
ATOM   4341 N N   . ARG   B 1 266 ? 52.606  -3.887  55.038 1.00 26.78 ? 958  ARG   B N   1 
ATOM   4342 C CA  . ARG   B 1 266 ? 52.140  -4.676  53.915 1.00 25.88 ? 958  ARG   B CA  1 
ATOM   4343 C C   . ARG   B 1 266 ? 51.268  -3.802  53.015 1.00 24.87 ? 958  ARG   B C   1 
ATOM   4344 O O   . ARG   B 1 266 ? 50.600  -2.877  53.498 1.00 24.86 ? 958  ARG   B O   1 
ATOM   4345 C CB  . ARG   B 1 266 ? 51.352  -5.893  54.427 1.00 26.84 ? 958  ARG   B CB  1 
ATOM   4346 C CG  . ARG   B 1 266 ? 52.205  -6.864  55.218 1.00 28.77 ? 958  ARG   B CG  1 
ATOM   4347 C CD  . ARG   B 1 266 ? 51.356  -7.903  55.914 1.00 29.57 ? 958  ARG   B CD  1 
ATOM   4348 N NE  . ARG   B 1 266 ? 52.097  -8.437  57.052 1.00 29.37 ? 958  ARG   B NE  1 
ATOM   4349 C CZ  . ARG   B 1 266 ? 51.547  -9.005  58.117 1.00 28.36 ? 958  ARG   B CZ  1 
ATOM   4350 N NH1 . ARG   B 1 266 ? 50.231  -9.165  58.187 1.00 24.41 ? 958  ARG   B NH1 1 
ATOM   4351 N NH2 . ARG   B 1 266 ? 52.310  -9.420  59.122 1.00 27.53 ? 958  ARG   B NH2 1 
ATOM   4352 N N   . PRO   B 1 267 ? 51.259  -4.074  51.700 1.00 23.83 ? 959  PRO   B N   1 
ATOM   4353 C CA  . PRO   B 1 267 ? 50.404  -3.284  50.817 1.00 23.64 ? 959  PRO   B CA  1 
ATOM   4354 C C   . PRO   B 1 267 ? 48.919  -3.438  51.152 1.00 23.33 ? 959  PRO   B C   1 
ATOM   4355 O O   . PRO   B 1 267 ? 48.518  -4.304  51.925 1.00 23.50 ? 959  PRO   B O   1 
ATOM   4356 C CB  . PRO   B 1 267 ? 50.751  -3.794  49.409 1.00 24.30 ? 959  PRO   B CB  1 
ATOM   4357 C CG  . PRO   B 1 267 ? 51.396  -5.102  49.600 1.00 24.55 ? 959  PRO   B CG  1 
ATOM   4358 C CD  . PRO   B 1 267 ? 51.965  -5.150  50.976 1.00 23.15 ? 959  PRO   B CD  1 
ATOM   4359 N N   . LYS   B 1 268 ? 48.115  -2.551  50.606 1.00 22.79 ? 960  LYS   B N   1 
ATOM   4360 C CA  . LYS   B 1 268 ? 46.676  -2.599  50.776 1.00 22.54 ? 960  LYS   B CA  1 
ATOM   4361 C C   . LYS   B 1 268 ? 46.092  -3.271  49.534 1.00 20.93 ? 960  LYS   B C   1 
ATOM   4362 O O   . LYS   B 1 268 ? 46.687  -3.206  48.450 1.00 20.82 ? 960  LYS   B O   1 
ATOM   4363 C CB  . LYS   B 1 268 ? 46.109  -1.169  50.981 1.00 24.82 ? 960  LYS   B CB  1 
ATOM   4364 C CG  . LYS   B 1 268 ? 46.664  -0.489  52.237 1.00 28.63 ? 960  LYS   B CG  1 
ATOM   4365 C CD  . LYS   B 1 268 ? 45.854  -0.823  53.491 1.00 34.44 ? 960  LYS   B CD  1 
ATOM   4366 C CE  . LYS   B 1 268 ? 46.596  -0.485  54.779 1.00 39.34 ? 960  LYS   B CE  1 
ATOM   4367 N NZ  . LYS   B 1 268 ? 45.671  -0.275  55.944 1.00 42.13 ? 960  LYS   B NZ  1 
ATOM   4368 N N   . PHE   B 1 269 ? 44.920  -3.901  49.677 1.00 19.57 ? 961  PHE   B N   1 
ATOM   4369 C CA  . PHE   B 1 269 ? 44.267  -4.555  48.549 1.00 18.75 ? 961  PHE   B CA  1 
ATOM   4370 C C   . PHE   B 1 269 ? 43.978  -3.576  47.390 1.00 20.24 ? 961  PHE   B C   1 
ATOM   4371 O O   . PHE   B 1 269 ? 44.192  -3.933  46.228 1.00 19.77 ? 961  PHE   B O   1 
ATOM   4372 C CB  . PHE   B 1 269 ? 43.013  -5.284  49.018 1.00 17.33 ? 961  PHE   B CB  1 
ATOM   4373 C CG  . PHE   B 1 269 ? 43.302  -6.604  49.690 1.00 16.31 ? 961  PHE   B CG  1 
ATOM   4374 C CD1 . PHE   B 1 269 ? 44.049  -7.582  49.044 1.00 15.43 ? 961  PHE   B CD1 1 
ATOM   4375 C CD2 . PHE   B 1 269 ? 42.799  -6.885  50.956 1.00 16.33 ? 961  PHE   B CD2 1 
ATOM   4376 C CE1 . PHE   B 1 269 ? 44.316  -8.792  49.664 1.00 15.58 ? 961  PHE   B CE1 1 
ATOM   4377 C CE2 . PHE   B 1 269 ? 43.088  -8.097  51.584 1.00 16.09 ? 961  PHE   B CE2 1 
ATOM   4378 C CZ  . PHE   B 1 269 ? 43.814  -9.053  50.925 1.00 15.47 ? 961  PHE   B CZ  1 
ATOM   4379 N N   . ARG   B 1 270 ? 43.603  -2.311  47.727 1.00 21.75 ? 962  ARG   B N   1 
ATOM   4380 C CA  . ARG   B 1 270 ? 43.360  -1.199  46.794 1.00 23.76 ? 962  ARG   B CA  1 
ATOM   4381 C C   . ARG   B 1 270 ? 44.617  -0.906  45.961 1.00 23.58 ? 962  ARG   B C   1 
ATOM   4382 O O   . ARG   B 1 270 ? 44.530  -0.679  44.759 1.00 24.21 ? 962  ARG   B O   1 
ATOM   4383 C CB  . ARG   B 1 270 ? 43.005  0.069   47.585 1.00 28.05 ? 962  ARG   B CB  1 
ATOM   4384 C CG  . ARG   B 1 270 ? 41.560  0.528   47.482 1.00 36.35 ? 962  ARG   B CG  1 
ATOM   4385 C CD  . ARG   B 1 270 ? 41.250  1.588   48.538 1.00 44.12 ? 962  ARG   B CD  1 
ATOM   4386 N NE  . ARG   B 1 270 ? 41.564  1.117   49.895 1.00 51.07 ? 962  ARG   B NE  1 
ATOM   4387 C CZ  . ARG   B 1 270 ? 40.657  0.690   50.771 1.00 55.90 ? 962  ARG   B CZ  1 
ATOM   4388 N NH1 . ARG   B 1 270 ? 39.365  0.690   50.454 1.00 55.93 ? 962  ARG   B NH1 1 
ATOM   4389 N NH2 . ARG   B 1 270 ? 41.034  0.260   51.971 1.00 56.88 ? 962  ARG   B NH2 1 
ATOM   4390 N N   . GLU   B 1 271 ? 45.786  -0.906  46.607 1.00 22.90 ? 963  GLU   B N   1 
ATOM   4391 C CA  . GLU   B 1 271 ? 47.061  -0.667  45.949 1.00 22.23 ? 963  GLU   B CA  1 
ATOM   4392 C C   . GLU   B 1 271 ? 47.444  -1.870  45.084 1.00 21.35 ? 963  GLU   B C   1 
ATOM   4393 O O   . GLU   B 1 271 ? 48.023  -1.678  44.003 1.00 22.04 ? 963  GLU   B O   1 
ATOM   4394 C CB  . GLU   B 1 271 ? 48.151  -0.429  46.998 1.00 24.50 ? 963  GLU   B CB  1 
ATOM   4395 C CG  . GLU   B 1 271 ? 47.855  0.683   47.992 1.00 29.89 ? 963  GLU   B CG  1 
ATOM   4396 C CD  . GLU   B 1 271 ? 48.887  0.822   49.107 1.00 37.24 ? 963  GLU   B CD  1 
ATOM   4397 O OE1 . GLU   B 1 271 ? 48.823  1.825   49.853 1.00 38.52 ? 963  GLU   B OE1 1 
ATOM   4398 O OE2 . GLU   B 1 271 ? 49.748  -0.078  49.248 1.00 38.77 ? 963  GLU   B OE2 1 
ATOM   4399 N N   . LEU   B 1 272 ? 47.149  -3.116  45.572 1.00 19.18 ? 964  LEU   B N   1 
ATOM   4400 C CA  . LEU   B 1 272 ? 47.444  -4.344  44.837 1.00 17.51 ? 964  LEU   B CA  1 
ATOM   4401 C C   . LEU   B 1 272 ? 46.637  -4.437  43.560 1.00 16.65 ? 964  LEU   B C   1 
ATOM   4402 O O   . LEU   B 1 272 ? 47.145  -4.960  42.567 1.00 16.35 ? 964  LEU   B O   1 
ATOM   4403 C CB  . LEU   B 1 272 ? 47.204  -5.574  45.692 1.00 17.38 ? 964  LEU   B CB  1 
ATOM   4404 C CG  . LEU   B 1 272 ? 48.241  -5.823  46.767 1.00 18.51 ? 964  LEU   B CG  1 
ATOM   4405 C CD1 . LEU   B 1 272 ? 47.725  -6.815  47.817 1.00 18.88 ? 964  LEU   B CD1 1 
ATOM   4406 C CD2 . LEU   B 1 272 ? 49.564  -6.258  46.154 1.00 17.73 ? 964  LEU   B CD2 1 
ATOM   4407 N N   . ILE   B 1 273 ? 45.373  -3.911  43.562 1.00 16.22 ? 965  ILE   B N   1 
ATOM   4408 C CA  . ILE   B 1 273 ? 44.522  -3.902  42.360 1.00 15.26 ? 965  ILE   B CA  1 
ATOM   4409 C C   . ILE   B 1 273 ? 45.207  -3.087  41.277 1.00 17.09 ? 965  ILE   B C   1 
ATOM   4410 O O   . ILE   B 1 273 ? 45.235  -3.508  40.127 1.00 18.05 ? 965  ILE   B O   1 
ATOM   4411 C CB  . ILE   B 1 273 ? 43.109  -3.324  42.608 1.00 13.88 ? 965  ILE   B CB  1 
ATOM   4412 C CG1 . ILE   B 1 273 ? 42.324  -4.075  43.701 1.00 13.18 ? 965  ILE   B CG1 1 
ATOM   4413 C CG2 . ILE   B 1 273 ? 42.302  -3.294  41.298 1.00 14.12 ? 965  ILE   B CG2 1 
ATOM   4414 C CD1 . ILE   B 1 273 ? 41.077  -3.380  44.139 1.00 12.95 ? 965  ILE   B CD1 1 
ATOM   4415 N N   . ILE   B 1 274 ? 45.764  -1.919  41.644 1.00 17.47 ? 966  ILE   B N   1 
ATOM   4416 C CA  . ILE   B 1 274 ? 46.407  -0.996  40.716 1.00 18.78 ? 966  ILE   B CA  1 
ATOM   4417 C C   . ILE   B 1 274 ? 47.755  -1.514  40.199 1.00 19.59 ? 966  ILE   B C   1 
ATOM   4418 O O   . ILE   B 1 274 ? 48.035  -1.413  38.993 1.00 20.03 ? 966  ILE   B O   1 
ATOM   4419 C CB  . ILE   B 1 274 ? 46.525  0.396   41.389 1.00 19.81 ? 966  ILE   B CB  1 
ATOM   4420 C CG1 . ILE   B 1 274 ? 45.135  1.005   41.642 1.00 20.55 ? 966  ILE   B CG1 1 
ATOM   4421 C CG2 . ILE   B 1 274 ? 47.427  1.351   40.602 1.00 20.19 ? 966  ILE   B CG2 1 
ATOM   4422 C CD1 . ILE   B 1 274 ? 45.174  2.195   42.554 1.00 21.64 ? 966  ILE   B CD1 1 
ATOM   4423 N N   . GLU   B 1 275 ? 48.562  -2.105  41.091 1.00 19.67 ? 967  GLU   B N   1 
ATOM   4424 C CA  . GLU   B 1 275 ? 49.867  -2.657  40.730 1.00 20.52 ? 967  GLU   B CA  1 
ATOM   4425 C C   . GLU   B 1 275 ? 49.710  -3.775  39.726 1.00 20.44 ? 967  GLU   B C   1 
ATOM   4426 O O   . GLU   B 1 275 ? 50.278  -3.692  38.628 1.00 20.68 ? 967  GLU   B O   1 
ATOM   4427 C CB  . GLU   B 1 275 ? 50.634  -3.162  41.967 1.00 24.27 ? 967  GLU   B CB  1 
ATOM   4428 C CG  . GLU   B 1 275 ? 51.825  -2.314  42.366 1.00 33.20 ? 967  GLU   B CG  1 
ATOM   4429 C CD  . GLU   B 1 275 ? 52.849  -2.054  41.277 1.00 44.76 ? 967  GLU   B CD  1 
ATOM   4430 O OE1 . GLU   B 1 275 ? 53.654  -2.967  40.983 1.00 46.65 ? 967  GLU   B OE1 1 
ATOM   4431 O OE2 . GLU   B 1 275 ? 52.868  -0.921  40.741 1.00 48.93 ? 967  GLU   B OE2 1 
ATOM   4432 N N   . PHE   B 1 276 ? 48.894  -4.796  40.058 1.00 19.75 ? 968  PHE   B N   1 
ATOM   4433 C CA  . PHE   B 1 276 ? 48.711  -5.917  39.139 1.00 19.15 ? 968  PHE   B CA  1 
ATOM   4434 C C   . PHE   B 1 276 ? 48.011  -5.507  37.850 1.00 19.95 ? 968  PHE   B C   1 
ATOM   4435 O O   . PHE   B 1 276 ? 48.252  -6.130  36.814 1.00 20.39 ? 968  PHE   B O   1 
ATOM   4436 C CB  . PHE   B 1 276 ? 48.031  -7.100  39.829 1.00 17.94 ? 968  PHE   B CB  1 
ATOM   4437 C CG  . PHE   B 1 276 ? 49.019  -7.921  40.627 1.00 17.64 ? 968  PHE   B CG  1 
ATOM   4438 C CD1 . PHE   B 1 276 ? 49.918  -8.765  39.991 1.00 18.20 ? 968  PHE   B CD1 1 
ATOM   4439 C CD2 . PHE   B 1 276 ? 49.076  -7.821  42.007 1.00 17.52 ? 968  PHE   B CD2 1 
ATOM   4440 C CE1 . PHE   B 1 276 ? 50.833  -9.522  40.726 1.00 18.85 ? 968  PHE   B CE1 1 
ATOM   4441 C CE2 . PHE   B 1 276 ? 50.001  -8.563  42.737 1.00 18.63 ? 968  PHE   B CE2 1 
ATOM   4442 C CZ  . PHE   B 1 276 ? 50.874  -9.412  42.094 1.00 18.69 ? 968  PHE   B CZ  1 
ATOM   4443 N N   . SER   B 1 277 ? 47.198  -4.431  37.880 1.00 19.99 ? 969  SER   B N   1 
ATOM   4444 C CA  . SER   B 1 277 ? 46.512  -3.961  36.683 1.00 20.78 ? 969  SER   B CA  1 
ATOM   4445 C C   . SER   B 1 277 ? 47.501  -3.272  35.747 1.00 22.02 ? 969  SER   B C   1 
ATOM   4446 O O   . SER   B 1 277 ? 47.462  -3.482  34.537 1.00 22.12 ? 969  SER   B O   1 
ATOM   4447 C CB  . SER   B 1 277 ? 45.375  -3.020  37.052 1.00 21.73 ? 969  SER   B CB  1 
ATOM   4448 O OG  . SER   B 1 277 ? 44.467  -3.630  37.952 1.00 23.56 ? 969  SER   B OG  1 
ATOM   4449 N N   . LYS   B 1 278 ? 48.415  -2.473  36.313 1.00 22.75 ? 970  LYS   B N   1 
ATOM   4450 C CA  . LYS   B 1 278 ? 49.484  -1.834  35.548 1.00 23.52 ? 970  LYS   B CA  1 
ATOM   4451 C C   . LYS   B 1 278 ? 50.397  -2.940  34.967 1.00 23.35 ? 970  LYS   B C   1 
ATOM   4452 O O   . LYS   B 1 278 ? 50.772  -2.874  33.797 1.00 24.05 ? 970  LYS   B O   1 
ATOM   4453 C CB  . LYS   B 1 278 ? 50.266  -0.863  36.454 1.00 26.23 ? 970  LYS   B CB  1 
ATOM   4454 C CG  . LYS   B 1 278 ? 51.581  -0.371  35.884 1.00 32.27 ? 970  LYS   B CG  1 
ATOM   4455 C CD  . LYS   B 1 278 ? 52.701  -0.396  36.924 1.00 38.66 ? 970  LYS   B CD  1 
ATOM   4456 C CE  . LYS   B 1 278 ? 53.019  -1.794  37.409 1.00 43.52 ? 970  LYS   B CE  1 
ATOM   4457 N NZ  . LYS   B 1 278 ? 54.086  -1.805  38.454 1.00 46.46 ? 970  LYS   B NZ  1 
ATOM   4458 N N   . MET   B 1 279 ? 50.676  -3.985  35.748 1.00 22.60 ? 971  MET   B N   1 
ATOM   4459 C CA  . MET   B 1 279 ? 51.477  -5.104  35.276 1.00 22.99 ? 971  MET   B CA  1 
ATOM   4460 C C   . MET   B 1 279 ? 50.816  -5.852  34.116 1.00 23.66 ? 971  MET   B C   1 
ATOM   4461 O O   . MET   B 1 279 ? 51.495  -6.243  33.162 1.00 23.96 ? 971  MET   B O   1 
ATOM   4462 C CB  . MET   B 1 279 ? 51.789  -6.054  36.424 1.00 23.51 ? 971  MET   B CB  1 
ATOM   4463 C CG  . MET   B 1 279 ? 52.776  -5.472  37.386 1.00 25.89 ? 971  MET   B CG  1 
ATOM   4464 S SD  . MET   B 1 279 ? 53.379  -6.649  38.586 1.00 28.87 ? 971  MET   B SD  1 
ATOM   4465 C CE  . MET   B 1 279 ? 54.798  -5.766  39.135 1.00 27.09 ? 971  MET   B CE  1 
ATOM   4466 N N   . ALA   B 1 280 ? 49.488  -6.031  34.197 1.00 23.22 ? 972  ALA   B N   1 
ATOM   4467 C CA  . ALA   B 1 280 ? 48.676  -6.694  33.181 1.00 23.09 ? 972  ALA   B CA  1 
ATOM   4468 C C   . ALA   B 1 280 ? 48.693  -5.951  31.845 1.00 23.31 ? 972  ALA   B C   1 
ATOM   4469 O O   . ALA   B 1 280 ? 48.500  -6.582  30.818 1.00 22.88 ? 972  ALA   B O   1 
ATOM   4470 C CB  . ALA   B 1 280 ? 47.241  -6.851  33.676 1.00 22.94 ? 972  ALA   B CB  1 
ATOM   4471 N N   . ARG   B 1 281 ? 48.904  -4.615  31.856 1.00 23.76 ? 973  ARG   B N   1 
ATOM   4472 C CA  . ARG   B 1 281 ? 49.003  -3.805  30.640 1.00 24.65 ? 973  ARG   B CA  1 
ATOM   4473 C C   . ARG   B 1 281 ? 50.318  -4.084  29.857 1.00 24.85 ? 973  ARG   B C   1 
ATOM   4474 O O   . ARG   B 1 281 ? 50.373  -3.898  28.645 1.00 24.45 ? 973  ARG   B O   1 
ATOM   4475 C CB  . ARG   B 1 281 ? 48.862  -2.312  30.986 1.00 27.00 ? 973  ARG   B CB  1 
ATOM   4476 C CG  . ARG   B 1 281 ? 47.407  -1.862  31.071 1.00 32.66 ? 973  ARG   B CG  1 
ATOM   4477 C CD  . ARG   B 1 281 ? 47.228  -0.530  31.786 1.00 38.70 ? 973  ARG   B CD  1 
ATOM   4478 N NE  . ARG   B 1 281 ? 46.226  -0.623  32.859 1.00 44.55 ? 973  ARG   B NE  1 
ATOM   4479 C CZ  . ARG   B 1 281 ? 46.322  -0.003  34.033 1.00 48.19 ? 973  ARG   B CZ  1 
ATOM   4480 N NH1 . ARG   B 1 281 ? 47.358  0.790   34.292 1.00 48.53 ? 973  ARG   B NH1 1 
ATOM   4481 N NH2 . ARG   B 1 281 ? 45.373  -0.151  34.946 1.00 48.02 ? 973  ARG   B NH2 1 
ATOM   4482 N N   . ASP   B 1 282 ? 51.351  -4.579  30.538 1.00 25.33 ? 974  ASP   B N   1 
ATOM   4483 C CA  . ASP   B 1 282 ? 52.649  -4.929  29.943 1.00 25.83 ? 974  ASP   B CA  1 
ATOM   4484 C C   . ASP   B 1 282 ? 53.019  -6.331  30.481 1.00 26.26 ? 974  ASP   B C   1 
ATOM   4485 O O   . ASP   B 1 282 ? 53.953  -6.453  31.261 1.00 26.71 ? 974  ASP   B O   1 
ATOM   4486 C CB  . ASP   B 1 282 ? 53.673  -3.874  30.418 1.00 27.45 ? 974  ASP   B CB  1 
ATOM   4487 C CG  . ASP   B 1 282 ? 54.895  -3.739  29.551 1.00 33.49 ? 974  ASP   B CG  1 
ATOM   4488 O OD1 . ASP   B 1 282 ? 55.149  -4.656  28.731 1.00 34.77 ? 974  ASP   B OD1 1 
ATOM   4489 O OD2 . ASP   B 1 282 ? 55.596  -2.707  29.674 1.00 36.36 ? 974  ASP   B OD2 1 
ATOM   4490 N N   . PRO   B 1 283 ? 52.277  -7.400  30.134 1.00 26.23 ? 975  PRO   B N   1 
ATOM   4491 C CA  . PRO   B 1 283 ? 52.501  -8.707  30.792 1.00 26.71 ? 975  PRO   B CA  1 
ATOM   4492 C C   . PRO   B 1 283 ? 53.844  -9.407  30.611 1.00 28.45 ? 975  PRO   B C   1 
ATOM   4493 O O   . PRO   B 1 283 ? 54.154  -10.293 31.407 1.00 28.60 ? 975  PRO   B O   1 
ATOM   4494 C CB  . PRO   B 1 283 ? 51.380  -9.585  30.237 1.00 26.77 ? 975  PRO   B CB  1 
ATOM   4495 C CG  . PRO   B 1 283 ? 50.944  -8.918  28.987 1.00 27.02 ? 975  PRO   B CG  1 
ATOM   4496 C CD  . PRO   B 1 283 ? 51.110  -7.451  29.239 1.00 25.48 ? 975  PRO   B CD  1 
ATOM   4497 N N   . GLN   B 1 284 ? 54.610  -9.068  29.560 1.00 29.29 ? 976  GLN   B N   1 
ATOM   4498 C CA  . GLN   B 1 284 ? 55.902  -9.701  29.279 1.00 30.06 ? 976  GLN   B CA  1 
ATOM   4499 C C   . GLN   B 1 284 ? 57.052  -9.075  30.070 1.00 30.14 ? 976  GLN   B C   1 
ATOM   4500 O O   . GLN   B 1 284 ? 58.067  -9.724  30.305 1.00 30.55 ? 976  GLN   B O   1 
ATOM   4501 C CB  . GLN   B 1 284 ? 56.211  -9.598  27.793 1.00 32.61 ? 976  GLN   B CB  1 
ATOM   4502 C CG  . GLN   B 1 284 ? 55.333  -10.464 26.915 1.00 37.85 ? 976  GLN   B CG  1 
ATOM   4503 C CD  . GLN   B 1 284 ? 55.920  -10.435 25.531 1.00 43.40 ? 976  GLN   B CD  1 
ATOM   4504 O OE1 . GLN   B 1 284 ? 55.974  -9.376  24.882 1.00 44.98 ? 976  GLN   B OE1 1 
ATOM   4505 N NE2 . GLN   B 1 284 ? 56.416  -11.583 25.071 1.00 43.85 ? 976  GLN   B NE2 1 
ATOM   4506 N N   . ARG   B 1 285 ? 56.916  -7.800  30.427 1.00 29.60 ? 977  ARG   B N   1 
ATOM   4507 C CA  . ARG   B 1 285 ? 57.884  -7.074  31.226 1.00 29.64 ? 977  ARG   B CA  1 
ATOM   4508 C C   . ARG   B 1 285 ? 57.868  -7.561  32.719 1.00 28.38 ? 977  ARG   B C   1 
ATOM   4509 O O   . ARG   B 1 285 ? 58.841  -7.325  33.451 1.00 29.50 ? 977  ARG   B O   1 
ATOM   4510 C CB  . ARG   B 1 285 ? 57.546  -5.570  31.137 1.00 32.20 ? 977  ARG   B CB  1 
ATOM   4511 C CG  . ARG   B 1 285 ? 58.509  -4.648  31.867 1.00 38.13 ? 977  ARG   B CG  1 
ATOM   4512 C CD  . ARG   B 1 285 ? 58.011  -3.217  31.924 1.00 44.57 ? 977  ARG   B CD  1 
ATOM   4513 N NE  . ARG   B 1 285 ? 58.497  -2.532  33.125 1.00 51.55 ? 977  ARG   B NE  1 
ATOM   4514 C CZ  . ARG   B 1 285 ? 58.366  -1.226  33.353 1.00 55.79 ? 977  ARG   B CZ  1 
ATOM   4515 N NH1 . ARG   B 1 285 ? 58.832  -0.692  34.477 1.00 55.58 ? 977  ARG   B NH1 1 
ATOM   4516 N NH2 . ARG   B 1 285 ? 57.745  -0.449  32.470 1.00 56.10 ? 977  ARG   B NH2 1 
ATOM   4517 N N   . TYR   B 1 286 ? 56.804  -8.268  33.160 1.00 25.84 ? 978  TYR   B N   1 
ATOM   4518 C CA  . TYR   B 1 286 ? 56.692  -8.668  34.550 1.00 24.01 ? 978  TYR   B CA  1 
ATOM   4519 C C   . TYR   B 1 286 ? 56.695  -10.165 34.786 1.00 23.76 ? 978  TYR   B C   1 
ATOM   4520 O O   . TYR   B 1 286 ? 57.103  -10.590 35.870 1.00 23.66 ? 978  TYR   B O   1 
ATOM   4521 C CB  . TYR   B 1 286 ? 55.493  -8.016  35.184 1.00 22.98 ? 978  TYR   B CB  1 
ATOM   4522 C CG  . TYR   B 1 286 ? 55.596  -6.514  35.120 1.00 22.86 ? 978  TYR   B CG  1 
ATOM   4523 C CD1 . TYR   B 1 286 ? 56.506  -5.825  35.909 1.00 24.07 ? 978  TYR   B CD1 1 
ATOM   4524 C CD2 . TYR   B 1 286 ? 54.828  -5.786  34.231 1.00 23.13 ? 978  TYR   B CD2 1 
ATOM   4525 C CE1 . TYR   B 1 286 ? 56.597  -4.437  35.857 1.00 24.99 ? 978  TYR   B CE1 1 
ATOM   4526 C CE2 . TYR   B 1 286 ? 54.928  -4.404  34.150 1.00 24.10 ? 978  TYR   B CE2 1 
ATOM   4527 C CZ  . TYR   B 1 286 ? 55.820  -3.733  34.955 1.00 25.55 ? 978  TYR   B CZ  1 
ATOM   4528 O OH  . TYR   B 1 286 ? 55.886  -2.372  34.889 1.00 27.75 ? 978  TYR   B OH  1 
ATOM   4529 N N   . LEU   B 1 287 ? 56.351  -10.971 33.782 1.00 23.28 ? 979  LEU   B N   1 
ATOM   4530 C CA  . LEU   B 1 287 ? 56.435  -12.426 33.932 1.00 24.05 ? 979  LEU   B CA  1 
ATOM   4531 C C   . LEU   B 1 287 ? 57.160  -13.012 32.731 1.00 25.87 ? 979  LEU   B C   1 
ATOM   4532 O O   . LEU   B 1 287 ? 56.873  -12.633 31.598 1.00 27.02 ? 979  LEU   B O   1 
ATOM   4533 C CB  . LEU   B 1 287 ? 55.068  -13.092 34.107 1.00 23.80 ? 979  LEU   B CB  1 
ATOM   4534 C CG  . LEU   B 1 287 ? 54.274  -12.754 35.370 1.00 24.70 ? 979  LEU   B CG  1 
ATOM   4535 C CD1 . LEU   B 1 287 ? 52.898  -13.363 35.314 1.00 25.34 ? 979  LEU   B CD1 1 
ATOM   4536 C CD2 . LEU   B 1 287 ? 54.983  -13.230 36.629 1.00 24.80 ? 979  LEU   B CD2 1 
ATOM   4537 N N   . VAL   B 1 288 ? 58.093  -13.928 32.965 1.00 26.05 ? 980  VAL   B N   1 
ATOM   4538 C CA  . VAL   B 1 288 ? 58.836  -14.570 31.901 1.00 27.55 ? 980  VAL   B CA  1 
ATOM   4539 C C   . VAL   B 1 288 ? 58.315  -15.990 31.753 1.00 29.60 ? 980  VAL   B C   1 
ATOM   4540 O O   . VAL   B 1 288 ? 58.624  -16.853 32.574 1.00 29.42 ? 980  VAL   B O   1 
ATOM   4541 C CB  . VAL   B 1 288 ? 60.367  -14.516 32.145 1.00 28.40 ? 980  VAL   B CB  1 
ATOM   4542 C CG1 . VAL   B 1 288 ? 61.102  -15.225 31.024 1.00 29.36 ? 980  VAL   B CG1 1 
ATOM   4543 C CG2 . VAL   B 1 288 ? 60.852  -13.071 32.262 1.00 28.32 ? 980  VAL   B CG2 1 
ATOM   4544 N N   . ILE   B 1 289 ? 57.443  -16.206 30.738 1.00 31.64 ? 981  ILE   B N   1 
ATOM   4545 C CA  . ILE   B 1 289 ? 56.785  -17.487 30.475 1.00 33.73 ? 981  ILE   B CA  1 
ATOM   4546 C C   . ILE   B 1 289 ? 57.109  -18.000 29.082 1.00 35.99 ? 981  ILE   B C   1 
ATOM   4547 O O   . ILE   B 1 289 ? 57.089  -17.228 28.115 1.00 36.20 ? 981  ILE   B O   1 
ATOM   4548 C CB  . ILE   B 1 289 ? 55.253  -17.364 30.682 1.00 34.30 ? 981  ILE   B CB  1 
ATOM   4549 C CG1 . ILE   B 1 289 ? 54.931  -16.988 32.140 1.00 35.14 ? 981  ILE   B CG1 1 
ATOM   4550 C CG2 . ILE   B 1 289 ? 54.543  -18.656 30.273 1.00 34.64 ? 981  ILE   B CG2 1 
ATOM   4551 C CD1 . ILE   B 1 289 ? 53.540  -16.722 32.410 1.00 36.28 ? 981  ILE   B CD1 1 
ATOM   4552 N N   . GLN   B 1 290 ? 57.380  -19.310 28.969 1.00 37.46 ? 982  GLN   B N   1 
ATOM   4553 C CA  . GLN   B 1 290 ? 57.728  -19.886 27.681 1.00 39.23 ? 982  GLN   B CA  1 
ATOM   4554 C C   . GLN   B 1 290 ? 56.563  -20.174 26.783 1.00 39.68 ? 982  GLN   B C   1 
ATOM   4555 O O   . GLN   B 1 290 ? 55.755  -21.062 27.058 1.00 39.94 ? 982  GLN   B O   1 
ATOM   4556 C CB  . GLN   B 1 290 ? 58.612  -21.130 27.819 1.00 41.98 ? 982  GLN   B CB  1 
ATOM   4557 C CG  . GLN   B 1 290 ? 60.084  -20.781 28.017 1.00 46.98 ? 982  GLN   B CG  1 
ATOM   4558 C CD  . GLN   B 1 290 ? 60.534  -19.656 27.104 1.00 53.44 ? 982  GLN   B CD  1 
ATOM   4559 O OE1 . GLN   B 1 290 ? 60.822  -18.534 27.563 1.00 54.93 ? 982  GLN   B OE1 1 
ATOM   4560 N NE2 . GLN   B 1 290 ? 60.538  -19.921 25.785 1.00 54.58 ? 982  GLN   B NE2 1 
ATOM   4561 N N   . GLY   B 1 291 ? 56.549  -19.464 25.665 1.00 39.56 ? 983  GLY   B N   1 
ATOM   4562 C CA  . GLY   B 1 291 ? 55.493  -19.585 24.676 1.00 40.16 ? 983  GLY   B CA  1 
ATOM   4563 C C   . GLY   B 1 291 ? 54.325  -18.679 25.000 1.00 40.28 ? 983  GLY   B C   1 
ATOM   4564 O O   . GLY   B 1 291 ? 53.175  -19.026 24.728 1.00 40.26 ? 983  GLY   B O   1 
ATOM   4565 N N   . ASP   B 1 292 ? 54.628  -17.498 25.571 1.00 40.05 ? 984  ASP   B N   1 
ATOM   4566 C CA  . ASP   B 1 292 ? 53.642  -16.511 25.989 1.00 40.00 ? 984  ASP   B CA  1 
ATOM   4567 C C   . ASP   B 1 292 ? 52.945  -15.806 24.831 1.00 41.00 ? 984  ASP   B C   1 
ATOM   4568 O O   . ASP   B 1 292 ? 51.811  -15.353 25.000 1.00 40.57 ? 984  ASP   B O   1 
ATOM   4569 C CB  . ASP   B 1 292 ? 54.257  -15.501 26.967 1.00 39.21 ? 984  ASP   B CB  1 
ATOM   4570 C CG  . ASP   B 1 292 ? 53.255  -14.956 27.960 1.00 38.85 ? 984  ASP   B CG  1 
ATOM   4571 O OD1 . ASP   B 1 292 ? 52.248  -15.649 28.232 1.00 37.93 ? 984  ASP   B OD1 1 
ATOM   4572 O OD2 . ASP   B 1 292 ? 53.470  -13.833 28.459 1.00 39.47 ? 984  ASP   B OD2 1 
ATOM   4573 N N   . GLU   B 1 293 ? 53.596  -15.752 23.653 1.00 42.24 ? 985  GLU   B N   1 
ATOM   4574 C CA  . GLU   B 1 293 ? 53.051  -15.163 22.425 1.00 44.05 ? 985  GLU   B CA  1 
ATOM   4575 C C   . GLU   B 1 293 ? 51.757  -15.895 22.004 1.00 45.05 ? 985  GLU   B C   1 
ATOM   4576 O O   . GLU   B 1 293 ? 50.832  -15.264 21.508 1.00 45.32 ? 985  GLU   B O   1 
ATOM   4577 C CB  . GLU   B 1 293 ? 54.077  -15.275 21.276 1.00 47.59 ? 985  GLU   B CB  1 
ATOM   4578 C CG  . GLU   B 1 293 ? 55.442  -14.657 21.545 1.00 55.53 ? 985  GLU   B CG  1 
ATOM   4579 C CD  . GLU   B 1 293 ? 56.457  -14.847 20.425 1.00 64.84 ? 985  GLU   B CD  1 
ATOM   4580 O OE1 . GLU   B 1 293 ? 56.226  -15.715 19.552 1.00 66.87 ? 985  GLU   B OE1 1 
ATOM   4581 O OE2 . GLU   B 1 293 ? 57.487  -14.133 20.422 1.00 67.39 ? 985  GLU   B OE2 1 
ATOM   4582 N N   . ARG   B 1 294 ? 51.705  -17.223 22.215 1.00 45.57 ? 986  ARG   B N   1 
ATOM   4583 C CA  . ARG   B 1 294 ? 50.587  -18.094 21.864 1.00 46.60 ? 986  ARG   B CA  1 
ATOM   4584 C C   . ARG   B 1 294 ? 49.540  -18.282 22.981 1.00 46.90 ? 986  ARG   B C   1 
ATOM   4585 O O   . ARG   B 1 294 ? 48.598  -19.059 22.802 1.00 47.38 ? 986  ARG   B O   1 
ATOM   4586 C CB  . ARG   B 1 294 ? 51.134  -19.468 21.451 1.00 48.83 ? 986  ARG   B CB  1 
ATOM   4587 C CG  . ARG   B 1 294 ? 51.882  -19.446 20.122 1.00 53.91 ? 986  ARG   B CG  1 
ATOM   4588 C CD  . ARG   B 1 294 ? 53.310  -19.949 20.253 1.00 58.62 ? 986  ARG   B CD  1 
ATOM   4589 N NE  . ARG   B 1 294 ? 54.229  -18.908 20.729 1.00 62.79 ? 986  ARG   B NE  1 
ATOM   4590 C CZ  . ARG   B 1 294 ? 55.471  -19.140 21.152 1.00 64.97 ? 986  ARG   B CZ  1 
ATOM   4591 N NH1 . ARG   B 1 294 ? 55.948  -20.380 21.188 1.00 64.49 ? 986  ARG   B NH1 1 
ATOM   4592 N NH2 . ARG   B 1 294 ? 56.234  -18.137 21.569 1.00 64.54 ? 986  ARG   B NH2 1 
ATOM   4593 N N   . MET   B 1 295 ? 49.708  -17.620 24.135 1.00 46.39 ? 987  MET   B N   1 
ATOM   4594 C CA  . MET   B 1 295 ? 48.773  -17.800 25.244 1.00 46.37 ? 987  MET   B CA  1 
ATOM   4595 C C   . MET   B 1 295 ? 48.059  -16.521 25.613 1.00 45.93 ? 987  MET   B C   1 
ATOM   4596 O O   . MET   B 1 295 ? 47.907  -16.207 26.792 1.00 46.16 ? 987  MET   B O   1 
ATOM   4597 C CB  . MET   B 1 295 ? 49.459  -18.449 26.453 1.00 47.09 ? 987  MET   B CB  1 
ATOM   4598 C CG  . MET   B 1 295 ? 49.994  -19.835 26.153 1.00 49.31 ? 987  MET   B CG  1 
ATOM   4599 S SD  . MET   B 1 295 ? 50.874  -20.611 27.525 1.00 53.37 ? 987  MET   B SD  1 
ATOM   4600 C CE  . MET   B 1 295 ? 52.079  -19.382 27.868 1.00 47.15 ? 987  MET   B CE  1 
ATOM   4601 N N   . HIS   B 1 296 ? 47.583  -15.798 24.593 1.00 45.14 ? 988  HIS   B N   1 
ATOM   4602 C CA  . HIS   B 1 296 ? 46.845  -14.545 24.760 1.00 44.55 ? 988  HIS   B CA  1 
ATOM   4603 C C   . HIS   B 1 296 ? 45.437  -14.788 25.360 1.00 41.91 ? 988  HIS   B C   1 
ATOM   4604 O O   . HIS   B 1 296 ? 44.974  -15.931 25.423 1.00 41.32 ? 988  HIS   B O   1 
ATOM   4605 C CB  . HIS   B 1 296 ? 46.731  -13.837 23.390 1.00 46.92 ? 988  HIS   B CB  1 
ATOM   4606 C CG  . HIS   B 1 296 ? 45.811  -14.534 22.428 1.00 52.12 ? 988  HIS   B CG  1 
ATOM   4607 N ND1 . HIS   B 1 296 ? 45.922  -15.896 22.176 1.00 54.86 ? 988  HIS   B ND1 1 
ATOM   4608 C CD2 . HIS   B 1 296 ? 44.790  -14.036 21.688 1.00 53.97 ? 988  HIS   B CD2 1 
ATOM   4609 C CE1 . HIS   B 1 296 ? 44.964  -16.180 21.306 1.00 55.58 ? 988  HIS   B CE1 1 
ATOM   4610 N NE2 . HIS   B 1 296 ? 44.252  -15.094 20.987 1.00 55.36 ? 988  HIS   B NE2 1 
ATOM   4611 N N   . LEU   B 1 297 ? 44.757  -13.711 25.797 1.00 40.36 ? 989  LEU   B N   1 
ATOM   4612 C CA  . LEU   B 1 297 ? 43.381  -13.815 26.306 1.00 39.49 ? 989  LEU   B CA  1 
ATOM   4613 C C   . LEU   B 1 297 ? 42.458  -14.289 25.155 1.00 39.01 ? 989  LEU   B C   1 
ATOM   4614 O O   . LEU   B 1 297 ? 42.806  -14.105 23.980 1.00 39.03 ? 989  LEU   B O   1 
ATOM   4615 C CB  . LEU   B 1 297 ? 42.911  -12.466 26.868 1.00 39.12 ? 989  LEU   B CB  1 
ATOM   4616 C CG  . LEU   B 1 297 ? 43.607  -11.991 28.141 1.00 39.61 ? 989  LEU   B CG  1 
ATOM   4617 C CD1 . LEU   B 1 297 ? 43.149  -10.592 28.512 1.00 39.73 ? 989  LEU   B CD1 1 
ATOM   4618 C CD2 . LEU   B 1 297 ? 43.406  -12.978 29.287 1.00 39.66 ? 989  LEU   B CD2 1 
ATOM   4619 N N   . PRO   B 1 298 ? 41.328  -14.970 25.434 1.00 38.48 ? 990  PRO   B N   1 
ATOM   4620 C CA  . PRO   B 1 298 ? 40.504  -15.471 24.320 1.00 37.96 ? 990  PRO   B CA  1 
ATOM   4621 C C   . PRO   B 1 298 ? 40.001  -14.352 23.416 1.00 37.18 ? 990  PRO   B C   1 
ATOM   4622 O O   . PRO   B 1 298 ? 39.911  -13.188 23.820 1.00 37.16 ? 990  PRO   B O   1 
ATOM   4623 C CB  . PRO   B 1 298 ? 39.380  -16.245 25.014 1.00 38.59 ? 990  PRO   B CB  1 
ATOM   4624 C CG  . PRO   B 1 298 ? 39.297  -15.653 26.360 1.00 39.32 ? 990  PRO   B CG  1 
ATOM   4625 C CD  . PRO   B 1 298 ? 40.713  -15.290 26.738 1.00 37.89 ? 990  PRO   B CD  1 
ATOM   4626 N N   . SER   B 1 299 ? 39.739  -14.710 22.160 1.00 36.23 ? 991  SER   B N   1 
ATOM   4627 C CA  . SER   B 1 299 ? 39.191  -13.808 21.152 1.00 35.42 ? 991  SER   B CA  1 
ATOM   4628 C C   . SER   B 1 299 ? 37.805  -13.319 21.617 1.00 34.08 ? 991  SER   B C   1 
ATOM   4629 O O   . SER   B 1 299 ? 37.164  -13.978 22.445 1.00 33.55 ? 991  SER   B O   1 
ATOM   4630 C CB  . SER   B 1 299 ? 39.021  -14.582 19.847 1.00 36.74 ? 991  SER   B CB  1 
ATOM   4631 O OG  . SER   B 1 299 ? 38.078  -15.632 20.008 1.00 38.80 ? 991  SER   B OG  1 
ATOM   4632 N N   . PRO   B 1 300 ? 37.291  -12.203 21.065 1.00 33.46 ? 992  PRO   B N   1 
ATOM   4633 C CA  . PRO   B 1 300 ? 35.925  -11.780 21.416 1.00 32.97 ? 992  PRO   B CA  1 
ATOM   4634 C C   . PRO   B 1 300 ? 34.886  -12.876 21.157 1.00 31.96 ? 992  PRO   B C   1 
ATOM   4635 O O   . PRO   B 1 300 ? 33.942  -12.995 21.923 1.00 31.86 ? 992  PRO   B O   1 
ATOM   4636 C CB  . PRO   B 1 300 ? 35.694  -10.552 20.526 1.00 33.84 ? 992  PRO   B CB  1 
ATOM   4637 C CG  . PRO   B 1 300 ? 37.091  -10.034 20.232 1.00 34.35 ? 992  PRO   B CG  1 
ATOM   4638 C CD  . PRO   B 1 300 ? 37.899  -11.292 20.073 1.00 32.83 ? 992  PRO   B CD  1 
ATOM   4639 N N   . THR   B 1 301 ? 35.112  -13.729 20.147 1.00 31.36 ? 993  THR   B N   1 
ATOM   4640 C CA  . THR   B 1 301 ? 34.208  -14.843 19.833 1.00 31.39 ? 993  THR   B CA  1 
ATOM   4641 C C   . THR   B 1 301 ? 34.112  -15.841 20.992 1.00 31.17 ? 993  THR   B C   1 
ATOM   4642 O O   . THR   B 1 301 ? 33.010  -16.159 21.445 1.00 30.82 ? 993  THR   B O   1 
ATOM   4643 C CB  . THR   B 1 301 ? 34.638  -15.534 18.523 1.00 32.45 ? 993  THR   B CB  1 
ATOM   4644 O OG1 . THR   B 1 301 ? 34.420  -14.645 17.438 1.00 33.90 ? 993  THR   B OG1 1 
ATOM   4645 C CG2 . THR   B 1 301 ? 33.890  -16.818 18.268 1.00 32.51 ? 993  THR   B CG2 1 
ATOM   4646 N N   . ASP   B 1 302 ? 35.262  -16.315 21.489 1.00 30.97 ? 994  ASP   B N   1 
ATOM   4647 C CA  . ASP   B 1 302 ? 35.273  -17.292 22.570 1.00 31.35 ? 994  ASP   B CA  1 
ATOM   4648 C C   . ASP   B 1 302 ? 34.856  -16.692 23.917 1.00 30.85 ? 994  ASP   B C   1 
ATOM   4649 O O   . ASP   B 1 302 ? 34.279  -17.397 24.733 1.00 30.65 ? 994  ASP   B O   1 
ATOM   4650 C CB  . ASP   B 1 302 ? 36.632  -18.017 22.622 1.00 33.76 ? 994  ASP   B CB  1 
ATOM   4651 C CG  . ASP   B 1 302 ? 36.965  -18.661 21.276 1.00 39.56 ? 994  ASP   B CG  1 
ATOM   4652 O OD1 . ASP   B 1 302 ? 36.016  -19.028 20.537 1.00 39.15 ? 994  ASP   B OD1 1 
ATOM   4653 O OD2 . ASP   B 1 302 ? 38.172  -18.763 20.941 1.00 43.05 ? 994  ASP   B OD2 1 
ATOM   4654 N N   . SER   B 1 303 ? 35.051  -15.384 24.115 1.00 30.47 ? 995  SER   B N   1 
ATOM   4655 C CA  . SER   B 1 303 ? 34.625  -14.717 25.348 1.00 30.42 ? 995  SER   B CA  1 
ATOM   4656 C C   . SER   B 1 303 ? 33.109  -14.586 25.383 1.00 29.83 ? 995  SER   B C   1 
ATOM   4657 O O   . SER   B 1 303 ? 32.494  -14.780 26.437 1.00 30.34 ? 995  SER   B O   1 
ATOM   4658 C CB  . SER   B 1 303 ? 35.258  -13.334 25.456 1.00 31.72 ? 995  SER   B CB  1 
ATOM   4659 O OG  . SER   B 1 303 ? 36.640  -13.436 25.752 1.00 34.62 ? 995  SER   B OG  1 
ATOM   4660 N N   . ASN   B 1 304 ? 32.501  -14.269 24.229 1.00 28.56 ? 996  ASN   B N   1 
ATOM   4661 C CA  . ASN   B 1 304 ? 31.061  -14.130 24.137 1.00 28.12 ? 996  ASN   B CA  1 
ATOM   4662 C C   . ASN   B 1 304 ? 30.387  -15.466 24.405 1.00 26.60 ? 996  ASN   B C   1 
ATOM   4663 O O   . ASN   B 1 304 ? 29.390  -15.512 25.121 1.00 26.96 ? 996  ASN   B O   1 
ATOM   4664 C CB  . ASN   B 1 304 ? 30.651  -13.583 22.768 1.00 30.66 ? 996  ASN   B CB  1 
ATOM   4665 C CG  . ASN   B 1 304 ? 30.972  -12.113 22.548 1.00 35.66 ? 996  ASN   B CG  1 
ATOM   4666 O OD1 . ASN   B 1 304 ? 30.965  -11.295 23.478 1.00 36.99 ? 996  ASN   B OD1 1 
ATOM   4667 N ND2 . ASN   B 1 304 ? 31.267  -11.746 21.294 1.00 36.92 ? 996  ASN   B ND2 1 
ATOM   4668 N N   . PHE   B 1 305 ? 30.944  -16.554 23.855 1.00 24.69 ? 997  PHE   B N   1 
ATOM   4669 C CA  . PHE   B 1 305 ? 30.404  -17.900 24.031 1.00 22.57 ? 997  PHE   B CA  1 
ATOM   4670 C C   . PHE   B 1 305 ? 30.385  -18.300 25.498 1.00 21.59 ? 997  PHE   B C   1 
ATOM   4671 O O   . PHE   B 1 305 ? 29.356  -18.754 25.997 1.00 20.91 ? 997  PHE   B O   1 
ATOM   4672 C CB  . PHE   B 1 305 ? 31.187  -18.914 23.180 1.00 21.30 ? 997  PHE   B CB  1 
ATOM   4673 C CG  . PHE   B 1 305 ? 30.455  -20.208 22.901 1.00 20.31 ? 997  PHE   B CG  1 
ATOM   4674 C CD1 . PHE   B 1 305 ? 29.289  -20.218 22.154 1.00 20.33 ? 997  PHE   B CD1 1 
ATOM   4675 C CD2 . PHE   B 1 305 ? 30.967  -21.418 23.332 1.00 20.42 ? 997  PHE   B CD2 1 
ATOM   4676 C CE1 . PHE   B 1 305 ? 28.633  -21.410 21.874 1.00 20.49 ? 997  PHE   B CE1 1 
ATOM   4677 C CE2 . PHE   B 1 305 ? 30.312  -22.610 23.042 1.00 20.81 ? 997  PHE   B CE2 1 
ATOM   4678 C CZ  . PHE   B 1 305 ? 29.140  -22.596 22.326 1.00 20.27 ? 997  PHE   B CZ  1 
ATOM   4679 N N   . TYR   B 1 306 ? 31.518  -18.125 26.193 1.00 21.70 ? 998  TYR   B N   1 
ATOM   4680 C CA  . TYR   B 1 306 ? 31.648  -18.436 27.618 1.00 22.15 ? 998  TYR   B CA  1 
ATOM   4681 C C   . TYR   B 1 306 ? 30.639  -17.636 28.440 1.00 22.19 ? 998  TYR   B C   1 
ATOM   4682 O O   . TYR   B 1 306 ? 29.950  -18.210 29.266 1.00 22.34 ? 998  TYR   B O   1 
ATOM   4683 C CB  . TYR   B 1 306 ? 33.082  -18.133 28.111 1.00 22.31 ? 998  TYR   B CB  1 
ATOM   4684 C CG  . TYR   B 1 306 ? 34.011  -19.326 28.096 1.00 23.49 ? 998  TYR   B CG  1 
ATOM   4685 C CD1 . TYR   B 1 306 ? 33.826  -20.387 28.968 1.00 24.33 ? 998  TYR   B CD1 1 
ATOM   4686 C CD2 . TYR   B 1 306 ? 35.116  -19.358 27.258 1.00 24.80 ? 998  TYR   B CD2 1 
ATOM   4687 C CE1 . TYR   B 1 306 ? 34.697  -21.467 28.986 1.00 25.40 ? 998  TYR   B CE1 1 
ATOM   4688 C CE2 . TYR   B 1 306 ? 36.003  -20.427 27.274 1.00 25.86 ? 998  TYR   B CE2 1 
ATOM   4689 C CZ  . TYR   B 1 306 ? 35.779  -21.489 28.127 1.00 26.91 ? 998  TYR   B CZ  1 
ATOM   4690 O OH  . TYR   B 1 306 ? 36.649  -22.549 28.139 1.00 28.68 ? 998  TYR   B OH  1 
ATOM   4691 N N   . ARG   B 1 307 ? 30.521  -16.326 28.184 1.00 22.69 ? 999  ARG   B N   1 
ATOM   4692 C CA  . ARG   B 1 307 ? 29.577  -15.464 28.885 1.00 24.23 ? 999  ARG   B CA  1 
ATOM   4693 C C   . ARG   B 1 307 ? 28.107  -15.895 28.708 1.00 25.37 ? 999  ARG   B C   1 
ATOM   4694 O O   . ARG   B 1 307 ? 27.419  -16.120 29.700 1.00 25.76 ? 999  ARG   B O   1 
ATOM   4695 C CB  . ARG   B 1 307 ? 29.766  -14.004 28.458 1.00 26.33 ? 999  ARG   B CB  1 
ATOM   4696 C CG  . ARG   B 1 307 ? 30.958  -13.349 29.112 1.00 31.58 ? 999  ARG   B CG  1 
ATOM   4697 C CD  . ARG   B 1 307 ? 30.793  -11.855 29.221 1.00 37.02 ? 999  ARG   B CD  1 
ATOM   4698 N NE  . ARG   B 1 307 ? 29.577  -11.466 29.943 1.00 41.94 ? 999  ARG   B NE  1 
ATOM   4699 C CZ  . ARG   B 1 307 ? 29.528  -11.197 31.246 1.00 44.83 ? 999  ARG   B CZ  1 
ATOM   4700 N NH1 . ARG   B 1 307 ? 30.619  -11.307 31.996 1.00 45.04 ? 999  ARG   B NH1 1 
ATOM   4701 N NH2 . ARG   B 1 307 ? 28.384  -10.842 31.813 1.00 44.39 ? 999  ARG   B NH2 1 
ATOM   4702 N N   . ALA   B 1 308 ? 27.642  -16.054 27.467 1.00 25.36 ? 1000 ALA   B N   1 
ATOM   4703 C CA  . ALA   B 1 308 ? 26.263  -16.454 27.203 1.00 26.37 ? 1000 ALA   B CA  1 
ATOM   4704 C C   . ALA   B 1 308 ? 25.913  -17.812 27.791 1.00 27.49 ? 1000 ALA   B C   1 
ATOM   4705 O O   . ALA   B 1 308 ? 24.783  -17.995 28.223 1.00 27.90 ? 1000 ALA   B O   1 
ATOM   4706 C CB  . ALA   B 1 308 ? 25.993  -16.456 25.709 1.00 26.49 ? 1000 ALA   B CB  1 
ATOM   4707 N N   . LEU   B 1 309 ? 26.866  -18.755 27.835 1.00 27.85 ? 1001 LEU   B N   1 
ATOM   4708 C CA  . LEU   B 1 309 ? 26.588  -20.087 28.375 1.00 28.70 ? 1001 LEU   B CA  1 
ATOM   4709 C C   . LEU   B 1 309 ? 26.664  -20.163 29.881 1.00 29.15 ? 1001 LEU   B C   1 
ATOM   4710 O O   . LEU   B 1 309 ? 25.780  -20.764 30.478 1.00 29.77 ? 1001 LEU   B O   1 
ATOM   4711 C CB  . LEU   B 1 309 ? 27.554  -21.143 27.808 1.00 29.26 ? 1001 LEU   B CB  1 
ATOM   4712 C CG  . LEU   B 1 309 ? 27.355  -21.574 26.381 1.00 31.40 ? 1001 LEU   B CG  1 
ATOM   4713 C CD1 . LEU   B 1 309 ? 28.415  -22.574 26.002 1.00 32.07 ? 1001 LEU   B CD1 1 
ATOM   4714 C CD2 . LEU   B 1 309 ? 25.942  -22.142 26.165 1.00 31.78 ? 1001 LEU   B CD2 1 
ATOM   4715 N N   . MET   B 1 310 ? 27.732  -19.619 30.503 1.00 28.96 ? 1002 MET   B N   1 
ATOM   4716 C CA  . MET   B 1 310 ? 27.903  -19.795 31.950 1.00 29.38 ? 1002 MET   B CA  1 
ATOM   4717 C C   . MET   B 1 310 ? 28.224  -18.546 32.787 1.00 28.53 ? 1002 MET   B C   1 
ATOM   4718 O O   . MET   B 1 310 ? 28.316  -18.687 34.006 1.00 29.47 ? 1002 MET   B O   1 
ATOM   4719 C CB  . MET   B 1 310 ? 28.984  -20.868 32.227 1.00 30.18 ? 1002 MET   B CB  1 
ATOM   4720 C CG  . MET   B 1 310 ? 30.288  -20.644 31.485 1.00 31.87 ? 1002 MET   B CG  1 
ATOM   4721 S SD  . MET   B 1 310 ? 31.234  -22.180 31.210 1.00 38.49 ? 1002 MET   B SD  1 
ATOM   4722 C CE  . MET   B 1 310 ? 31.557  -22.660 32.847 1.00 38.27 ? 1002 MET   B CE  1 
ATOM   4723 N N   . ASP   B 1 311 ? 28.399  -17.367 32.186 1.00 26.68 ? 1003 ASP   B N   1 
ATOM   4724 C CA  . ASP   B 1 311 ? 28.765  -16.184 32.970 1.00 25.64 ? 1003 ASP   B CA  1 
ATOM   4725 C C   . ASP   B 1 311 ? 28.032  -14.949 32.521 1.00 25.52 ? 1003 ASP   B C   1 
ATOM   4726 O O   . ASP   B 1 311 ? 28.601  -14.123 31.808 1.00 24.54 ? 1003 ASP   B O   1 
ATOM   4727 C CB  . ASP   B 1 311 ? 30.288  -15.959 32.925 1.00 25.24 ? 1003 ASP   B CB  1 
ATOM   4728 C CG  . ASP   B 1 311 ? 30.830  -15.026 33.991 1.00 26.22 ? 1003 ASP   B CG  1 
ATOM   4729 O OD1 . ASP   B 1 311 ? 30.070  -14.665 34.909 1.00 26.62 ? 1003 ASP   B OD1 1 
ATOM   4730 O OD2 . ASP   B 1 311 ? 32.027  -14.681 33.923 1.00 25.94 ? 1003 ASP   B OD2 1 
ATOM   4731 N N   . GLU   B 1 312 ? 26.761  -14.834 32.907 1.00 26.48 ? 1004 GLU   B N   1 
ATOM   4732 C CA  . GLU   B 1 312 ? 25.989  -13.650 32.549 1.00 28.17 ? 1004 GLU   B CA  1 
ATOM   4733 C C   . GLU   B 1 312 ? 26.099  -12.522 33.607 1.00 28.81 ? 1004 GLU   B C   1 
ATOM   4734 O O   . GLU   B 1 312 ? 25.759  -11.387 33.295 1.00 28.88 ? 1004 GLU   B O   1 
ATOM   4735 C CB  . GLU   B 1 312 ? 24.531  -14.005 32.220 1.00 31.71 ? 1004 GLU   B CB  1 
ATOM   4736 C CG  . GLU   B 1 312 ? 24.355  -14.564 30.817 1.00 38.52 ? 1004 GLU   B CG  1 
ATOM   4737 C CD  . GLU   B 1 312 ? 22.945  -15.009 30.463 1.00 47.91 ? 1004 GLU   B CD  1 
ATOM   4738 O OE1 . GLU   B 1 312 ? 22.493  -14.685 29.338 1.00 50.97 ? 1004 GLU   B OE1 1 
ATOM   4739 O OE2 . GLU   B 1 312 ? 22.287  -15.664 31.310 1.00 48.78 ? 1004 GLU   B OE2 1 
ATOM   4740 N N   . GLU   B 1 313 ? 26.615  -12.809 34.825 1.00 29.15 ? 1005 GLU   B N   1 
ATOM   4741 C CA  . GLU   B 1 313 ? 26.758  -11.767 35.845 1.00 30.19 ? 1005 GLU   B CA  1 
ATOM   4742 C C   . GLU   B 1 313 ? 27.736  -10.692 35.372 1.00 31.39 ? 1005 GLU   B C   1 
ATOM   4743 O O   . GLU   B 1 313 ? 28.736  -11.018 34.722 1.00 31.64 ? 1005 GLU   B O   1 
ATOM   4744 C CB  . GLU   B 1 313 ? 27.154  -12.340 37.220 1.00 31.53 ? 1005 GLU   B CB  1 
ATOM   4745 C CG  . GLU   B 1 313 ? 28.610  -12.768 37.343 1.00 34.26 ? 1005 GLU   B CG  1 
ATOM   4746 C CD  . GLU   B 1 313 ? 29.050  -13.176 38.738 1.00 37.79 ? 1005 GLU   B CD  1 
ATOM   4747 O OE1 . GLU   B 1 313 ? 29.798  -14.172 38.856 1.00 39.03 ? 1005 GLU   B OE1 1 
ATOM   4748 O OE2 . GLU   B 1 313 ? 28.638  -12.511 39.715 1.00 38.46 ? 1005 GLU   B OE2 1 
ATOM   4749 N N   . ASP   B 1 314 ? 27.408  -9.417  35.613 1.00 32.19 ? 1006 ASP   B N   1 
ATOM   4750 C CA  . ASP   B 1 314 ? 28.274  -8.351  35.145 1.00 34.28 ? 1006 ASP   B CA  1 
ATOM   4751 C C   . ASP   B 1 314 ? 29.512  -8.231  36.031 1.00 34.95 ? 1006 ASP   B C   1 
ATOM   4752 O O   . ASP   B 1 314 ? 29.423  -8.388  37.244 1.00 35.28 ? 1006 ASP   B O   1 
ATOM   4753 C CB  . ASP   B 1 314 ? 27.519  -7.024  34.939 1.00 38.24 ? 1006 ASP   B CB  1 
ATOM   4754 C CG  . ASP   B 1 314 ? 27.309  -6.175  36.173 1.00 46.45 ? 1006 ASP   B CG  1 
ATOM   4755 O OD1 . ASP   B 1 314 ? 27.006  -6.748  37.244 1.00 48.17 ? 1006 ASP   B OD1 1 
ATOM   4756 O OD2 . ASP   B 1 314 ? 27.436  -4.929  36.065 1.00 49.54 ? 1006 ASP   B OD2 1 
ATOM   4757 N N   . MET   B 1 315 ? 30.674  -8.054  35.411 1.00 35.01 ? 1007 MET   B N   1 
ATOM   4758 C CA  . MET   B 1 315 ? 31.943  -7.895  36.116 1.00 35.72 ? 1007 MET   B CA  1 
ATOM   4759 C C   . MET   B 1 315 ? 32.814  -6.854  35.388 1.00 36.67 ? 1007 MET   B C   1 
ATOM   4760 O O   . MET   B 1 315 ? 32.594  -6.583  34.201 1.00 36.71 ? 1007 MET   B O   1 
ATOM   4761 C CB  . MET   B 1 315 ? 32.683  -9.242  36.274 1.00 36.27 ? 1007 MET   B CB  1 
ATOM   4762 C CG  . MET   B 1 315 ? 33.373  -9.730  35.012 1.00 38.57 ? 1007 MET   B CG  1 
ATOM   4763 S SD  . MET   B 1 315 ? 34.752  -10.857 35.346 1.00 41.48 ? 1007 MET   B SD  1 
ATOM   4764 C CE  . MET   B 1 315 ? 35.399  -11.038 33.735 1.00 40.04 ? 1007 MET   B CE  1 
ATOM   4765 N N   . ASP   B 1 316 ? 33.810  -6.276  36.085 1.00 36.91 ? 1008 ASP   B N   1 
ATOM   4766 C CA  . ASP   B 1 316 ? 34.698  -5.286  35.469 1.00 37.83 ? 1008 ASP   B CA  1 
ATOM   4767 C C   . ASP   B 1 316 ? 35.463  -5.913  34.307 1.00 37.20 ? 1008 ASP   B C   1 
ATOM   4768 O O   . ASP   B 1 316 ? 35.712  -7.121  34.317 1.00 37.26 ? 1008 ASP   B O   1 
ATOM   4769 C CB  . ASP   B 1 316 ? 35.712  -4.714  36.477 1.00 41.47 ? 1008 ASP   B CB  1 
ATOM   4770 C CG  . ASP   B 1 316 ? 35.183  -4.494  37.877 1.00 50.02 ? 1008 ASP   B CG  1 
ATOM   4771 O OD1 . ASP   B 1 316 ? 34.802  -5.506  38.540 1.00 52.69 ? 1008 ASP   B OD1 1 
ATOM   4772 O OD2 . ASP   B 1 316 ? 35.175  -3.321  38.331 1.00 52.01 ? 1008 ASP   B OD2 1 
ATOM   4773 N N   . ASP   B 1 317 ? 35.804  -5.108  33.298 1.00 36.44 ? 1009 ASP   B N   1 
ATOM   4774 C CA  . ASP   B 1 317 ? 36.524  -5.623  32.145 1.00 36.50 ? 1009 ASP   B CA  1 
ATOM   4775 C C   . ASP   B 1 317 ? 37.927  -6.117  32.531 1.00 36.10 ? 1009 ASP   B C   1 
ATOM   4776 O O   . ASP   B 1 317 ? 38.628  -5.496  33.325 1.00 35.80 ? 1009 ASP   B O   1 
ATOM   4777 C CB  . ASP   B 1 317 ? 36.594  -4.582  31.021 1.00 38.81 ? 1009 ASP   B CB  1 
ATOM   4778 C CG  . ASP   B 1 317 ? 35.275  -4.317  30.321 1.00 44.54 ? 1009 ASP   B CG  1 
ATOM   4779 O OD1 . ASP   B 1 317 ? 34.213  -4.472  30.969 1.00 45.55 ? 1009 ASP   B OD1 1 
ATOM   4780 O OD2 . ASP   B 1 317 ? 35.304  -3.937  29.133 1.00 47.11 ? 1009 ASP   B OD2 1 
ATOM   4781 N N   . VAL   B 1 318 ? 38.297  -7.269  31.997 1.00 35.76 ? 1010 VAL   B N   1 
ATOM   4782 C CA  . VAL   B 1 318 ? 39.601  -7.879  32.191 1.00 35.63 ? 1010 VAL   B CA  1 
ATOM   4783 C C   . VAL   B 1 318 ? 40.641  -6.974  31.503 1.00 35.24 ? 1010 VAL   B C   1 
ATOM   4784 O O   . VAL   B 1 318 ? 40.369  -6.422  30.435 1.00 35.46 ? 1010 VAL   B O   1 
ATOM   4785 C CB  . VAL   B 1 318 ? 39.535  -9.311  31.615 1.00 36.56 ? 1010 VAL   B CB  1 
ATOM   4786 C CG1 . VAL   B 1 318 ? 40.905  -9.863  31.274 1.00 37.53 ? 1010 VAL   B CG1 1 
ATOM   4787 C CG2 . VAL   B 1 318 ? 38.795  -10.234 32.568 1.00 37.08 ? 1010 VAL   B CG2 1 
ATOM   4788 N N   . VAL   B 1 319 ? 41.780  -6.739  32.164 1.00 34.53 ? 1011 VAL   B N   1 
ATOM   4789 C CA  . VAL   B 1 319 ? 42.844  -5.861  31.671 1.00 34.06 ? 1011 VAL   B CA  1 
ATOM   4790 C C   . VAL   B 1 319 ? 43.590  -6.500  30.497 1.00 34.95 ? 1011 VAL   B C   1 
ATOM   4791 O O   . VAL   B 1 319 ? 44.156  -7.588  30.632 1.00 35.57 ? 1011 VAL   B O   1 
ATOM   4792 C CB  . VAL   B 1 319 ? 43.828  -5.424  32.787 1.00 33.75 ? 1011 VAL   B CB  1 
ATOM   4793 C CG1 . VAL   B 1 319 ? 44.658  -4.232  32.333 1.00 33.69 ? 1011 VAL   B CG1 1 
ATOM   4794 C CG2 . VAL   B 1 319 ? 43.102  -5.103  34.092 1.00 33.93 ? 1011 VAL   B CG2 1 
ATOM   4795 N N   . ASP   B 1 320 ? 43.596  -5.829  29.348 1.00 34.82 ? 1012 ASP   B N   1 
ATOM   4796 C CA  . ASP   B 1 320 ? 44.284  -6.333  28.167 1.00 35.81 ? 1012 ASP   B CA  1 
ATOM   4797 C C   . ASP   B 1 320 ? 45.650  -5.651  27.997 1.00 35.69 ? 1012 ASP   B C   1 
ATOM   4798 O O   . ASP   B 1 320 ? 45.852  -4.528  28.462 1.00 35.31 ? 1012 ASP   B O   1 
ATOM   4799 C CB  . ASP   B 1 320 ? 43.413  -6.091  26.919 1.00 39.18 ? 1012 ASP   B CB  1 
ATOM   4800 C CG  . ASP   B 1 320 ? 43.630  -7.050  25.759 1.00 46.89 ? 1012 ASP   B CG  1 
ATOM   4801 O OD1 . ASP   B 1 320 ? 44.754  -7.602  25.635 1.00 47.63 ? 1012 ASP   B OD1 1 
ATOM   4802 O OD2 . ASP   B 1 320 ? 42.680  -7.243  24.965 1.00 51.07 ? 1012 ASP   B OD2 1 
ATOM   4803 N N   . ALA   B 1 321 ? 46.590  -6.332  27.308 1.00 35.95 ? 1013 ALA   B N   1 
ATOM   4804 C CA  . ALA   B 1 321 ? 47.919  -5.794  27.005 1.00 36.43 ? 1013 ALA   B CA  1 
ATOM   4805 C C   . ALA   B 1 321 ? 47.774  -4.508  26.197 1.00 37.59 ? 1013 ALA   B C   1 
ATOM   4806 O O   . ALA   B 1 321 ? 47.088  -4.485  25.179 1.00 37.91 ? 1013 ALA   B O   1 
ATOM   4807 C CB  . ALA   B 1 321 ? 48.734  -6.805  26.220 1.00 36.00 ? 1013 ALA   B CB  1 
ATOM   4808 N N   . ASP   B 1 322 ? 48.369  -3.437  26.700 1.00 38.18 ? 1014 ASP   B N   1 
ATOM   4809 C CA  . ASP   B 1 322 ? 48.351  -2.096  26.139 1.00 39.42 ? 1014 ASP   B CA  1 
ATOM   4810 C C   . ASP   B 1 322 ? 49.108  -1.969  24.796 1.00 39.86 ? 1014 ASP   B C   1 
ATOM   4811 O O   . ASP   B 1 322 ? 49.608  -2.949  24.233 1.00 39.94 ? 1014 ASP   B O   1 
ATOM   4812 C CB  . ASP   B 1 322 ? 48.924  -1.122  27.184 1.00 42.04 ? 1014 ASP   B CB  1 
ATOM   4813 C CG  . ASP   B 1 322 ? 48.313  0.251   27.123 1.00 48.80 ? 1014 ASP   B CG  1 
ATOM   4814 O OD1 . ASP   B 1 322 ? 47.548  0.600   28.050 1.00 49.31 ? 1014 ASP   B OD1 1 
ATOM   4815 O OD2 . ASP   B 1 322 ? 48.587  0.977   26.138 1.00 52.70 ? 1014 ASP   B OD2 1 
HETATM 4816 C C1  . A1IZ9 C 2 .   ? 17.609  -21.163 16.415 1.00 31.00 ? 1101 A1IZ9 A C1  1 
HETATM 4817 C C2  . A1IZ9 C 2 .   ? 17.668  -19.947 17.070 1.00 30.96 ? 1101 A1IZ9 A C2  1 
HETATM 4818 C C3  . A1IZ9 C 2 .   ? 17.489  -19.883 18.434 1.00 31.04 ? 1101 A1IZ9 A C3  1 
HETATM 4819 C C7  . A1IZ9 C 2 .   ? 15.961  -23.846 20.035 1.00 31.46 ? 1101 A1IZ9 A C7  1 
HETATM 4820 C C8  . A1IZ9 C 2 .   ? 15.960  -24.930 20.914 1.00 31.62 ? 1101 A1IZ9 A C8  1 
HETATM 4821 C C9  . A1IZ9 C 2 .   ? 18.158  -25.391 20.497 1.00 31.82 ? 1101 A1IZ9 A C9  1 
HETATM 4822 C C10 . A1IZ9 C 2 .   ? 18.222  -24.354 19.612 1.00 31.64 ? 1101 A1IZ9 A C10 1 
HETATM 4823 C C11 . A1IZ9 C 2 .   ? 14.694  -25.326 21.553 1.00 31.43 ? 1101 A1IZ9 A C11 1 
HETATM 4824 C C12 . A1IZ9 C 2 .   ? 12.644  -25.966 21.777 1.00 31.03 ? 1101 A1IZ9 A C12 1 
HETATM 4825 C C13 . A1IZ9 C 2 .   ? 11.213  -26.375 21.835 1.00 30.89 ? 1101 A1IZ9 A C13 1 
HETATM 4826 C C14 . A1IZ9 C 2 .   ? 12.235  -26.678 23.993 1.00 30.85 ? 1101 A1IZ9 A C14 1 
HETATM 4827 C C15 . A1IZ9 C 2 .   ? 13.210  -26.115 23.012 1.00 31.06 ? 1101 A1IZ9 A C15 1 
HETATM 4828 C C16 . A1IZ9 C 2 .   ? 15.446  -25.642 23.976 1.00 31.69 ? 1101 A1IZ9 A C16 1 
HETATM 4829 C C19 . A1IZ9 C 2 .   ? 16.955  -24.464 25.155 1.00 31.97 ? 1101 A1IZ9 A C19 1 
HETATM 4830 C C20 . A1IZ9 C 2 .   ? 9.924   -27.439 23.693 1.00 31.05 ? 1101 A1IZ9 A C20 1 
HETATM 4831 C C21 . A1IZ9 C 2 .   ? 8.737   -27.573 22.755 1.00 30.05 ? 1101 A1IZ9 A C21 1 
HETATM 4832 C C22 . A1IZ9 C 2 .   ? 7.440   -27.375 23.455 1.00 29.19 ? 1101 A1IZ9 A C22 1 
HETATM 4833 O O   . A1IZ9 C 2 .   ? 9.863   -27.822 24.853 1.00 31.68 ? 1101 A1IZ9 A O   1 
HETATM 4834 N N2  . A1IZ9 C 2 .   ? 11.035  -26.863 23.197 1.00 30.93 ? 1101 A1IZ9 A N2  1 
HETATM 4835 N N1  . A1IZ9 C 2 .   ? 13.566  -25.474 20.878 1.00 31.28 ? 1101 A1IZ9 A N1  1 
HETATM 4836 N N3  . A1IZ9 C 2 .   ? 14.523  -25.689 22.875 1.00 31.42 ? 1101 A1IZ9 A N3  1 
HETATM 4837 N N5  . A1IZ9 C 2 .   ? 16.221  -24.561 24.045 1.00 32.09 ? 1101 A1IZ9 A N5  1 
HETATM 4838 N N4  . A1IZ9 C 2 .   ? 17.017  -25.322 26.168 1.00 31.96 ? 1101 A1IZ9 A N4  1 
HETATM 4839 C C18 . A1IZ9 C 2 .   ? 16.241  -26.400 26.039 1.00 31.94 ? 1101 A1IZ9 A C18 1 
HETATM 4840 C C17 . A1IZ9 C 2 .   ? 15.424  -26.626 24.952 1.00 31.73 ? 1101 A1IZ9 A C17 1 
HETATM 4841 N N   . A1IZ9 C 2 .   ? 17.043  -25.682 21.169 1.00 31.89 ? 1101 A1IZ9 A N   1 
HETATM 4842 F F1  . A1IZ9 C 2 .   ? 19.399  -24.105 18.991 1.00 31.48 ? 1101 A1IZ9 A F1  1 
HETATM 4843 C C6  . A1IZ9 C 2 .   ? 17.140  -23.521 19.363 1.00 31.38 ? 1101 A1IZ9 A C6  1 
HETATM 4844 C C5  . A1IZ9 C 2 .   ? 17.212  -22.280 18.535 1.00 31.02 ? 1101 A1IZ9 A C5  1 
HETATM 4845 C C   . A1IZ9 C 2 .   ? 17.396  -22.298 17.160 1.00 31.10 ? 1101 A1IZ9 A C   1 
HETATM 4846 F F   . A1IZ9 C 2 .   ? 17.443  -23.493 16.534 1.00 31.38 ? 1101 A1IZ9 A F   1 
HETATM 4847 C C4  . A1IZ9 C 2 .   ? 17.244  -21.035 19.163 1.00 30.98 ? 1101 A1IZ9 A C4  1 
HETATM 4848 C C1  . A1IZ9 D 2 .   ? 30.478  -21.123 52.274 1.00 27.60 ? 1101 A1IZ9 B C1  1 
HETATM 4849 C C2  . A1IZ9 D 2 .   ? 30.434  -19.871 51.690 1.00 27.57 ? 1101 A1IZ9 B C2  1 
HETATM 4850 C C3  . A1IZ9 D 2 .   ? 30.502  -19.744 50.323 1.00 28.08 ? 1101 A1IZ9 B C3  1 
HETATM 4851 C C7  . A1IZ9 D 2 .   ? 31.812  -23.730 48.592 1.00 27.11 ? 1101 A1IZ9 B C7  1 
HETATM 4852 C C8  . A1IZ9 D 2 .   ? 31.862  -24.897 47.831 1.00 26.78 ? 1101 A1IZ9 B C8  1 
HETATM 4853 C C9  . A1IZ9 D 2 .   ? 29.660  -25.353 48.224 1.00 27.36 ? 1101 A1IZ9 B C9  1 
HETATM 4854 C C10 . A1IZ9 D 2 .   ? 29.550  -24.225 48.994 1.00 27.41 ? 1101 A1IZ9 B C10 1 
HETATM 4855 C C11 . A1IZ9 D 2 .   ? 33.144  -25.291 47.222 1.00 26.18 ? 1101 A1IZ9 B C11 1 
HETATM 4856 C C12 . A1IZ9 D 2 .   ? 35.228  -25.815 47.006 1.00 26.04 ? 1101 A1IZ9 B C12 1 
HETATM 4857 C C13 . A1IZ9 D 2 .   ? 36.692  -26.154 46.922 1.00 26.33 ? 1101 A1IZ9 B C13 1 
HETATM 4858 C C14 . A1IZ9 D 2 .   ? 35.671  -26.443 44.759 1.00 26.79 ? 1101 A1IZ9 B C14 1 
HETATM 4859 C C15 . A1IZ9 D 2 .   ? 34.678  -25.963 45.761 1.00 26.18 ? 1101 A1IZ9 B C15 1 
HETATM 4860 C C16 . A1IZ9 D 2 .   ? 32.469  -25.563 44.781 1.00 24.75 ? 1101 A1IZ9 B C16 1 
HETATM 4861 C C19 . A1IZ9 D 2 .   ? 30.934  -24.416 43.615 1.00 24.66 ? 1101 A1IZ9 B C19 1 
HETATM 4862 C C20 . A1IZ9 D 2 .   ? 37.907  -27.367 45.093 1.00 27.72 ? 1101 A1IZ9 B C20 1 
HETATM 4863 C C21 . A1IZ9 D 2 .   ? 39.153  -27.380 45.955 1.00 27.19 ? 1101 A1IZ9 B C21 1 
HETATM 4864 C C22 . A1IZ9 D 2 .   ? 40.403  -27.155 45.152 1.00 26.77 ? 1101 A1IZ9 B C22 1 
HETATM 4865 O O   . A1IZ9 D 2 .   ? 37.906  -27.848 43.967 1.00 28.28 ? 1101 A1IZ9 B O   1 
HETATM 4866 N N2  . A1IZ9 D 2 .   ? 36.835  -26.716 45.583 1.00 26.93 ? 1101 A1IZ9 B N2  1 
HETATM 4867 N N1  . A1IZ9 D 2 .   ? 34.270  -25.396 47.909 1.00 25.97 ? 1101 A1IZ9 B N1  1 
HETATM 4868 N N3  . A1IZ9 D 2 .   ? 33.351  -25.617 45.899 1.00 25.68 ? 1101 A1IZ9 B N3  1 
HETATM 4869 N N5  . A1IZ9 D 2 .   ? 31.635  -24.533 44.746 1.00 24.81 ? 1101 A1IZ9 B N5  1 
HETATM 4870 N N4  . A1IZ9 D 2 .   ? 30.963  -25.210 42.552 1.00 23.97 ? 1101 A1IZ9 B N4  1 
HETATM 4871 C C18 . A1IZ9 D 2 .   ? 31.802  -26.238 42.652 1.00 23.95 ? 1101 A1IZ9 B C18 1 
HETATM 4872 C C17 . A1IZ9 D 2 .   ? 32.591  -26.474 43.756 1.00 24.21 ? 1101 A1IZ9 B C17 1 
HETATM 4873 N N   . A1IZ9 D 2 .   ? 30.807  -25.702 47.634 1.00 27.13 ? 1101 A1IZ9 B N   1 
HETATM 4874 F F1  . A1IZ9 D 2 .   ? 28.341  -23.921 49.520 1.00 26.97 ? 1101 A1IZ9 B F1  1 
HETATM 4875 C C6  . A1IZ9 D 2 .   ? 30.620  -23.365 49.214 1.00 27.50 ? 1101 A1IZ9 B C6  1 
HETATM 4876 C C5  . A1IZ9 D 2 .   ? 30.615  -22.143 50.076 1.00 27.83 ? 1101 A1IZ9 B C5  1 
HETATM 4877 C C   . A1IZ9 D 2 .   ? 30.569  -22.225 51.458 1.00 27.79 ? 1101 A1IZ9 B C   1 
HETATM 4878 F F   . A1IZ9 D 2 .   ? 30.644  -23.445 52.027 1.00 28.21 ? 1101 A1IZ9 B F   1 
HETATM 4879 C C4  . A1IZ9 D 2 .   ? 30.601  -20.866 49.515 1.00 28.19 ? 1101 A1IZ9 B C4  1 
HETATM 4880 O O   . HOH   E 3 .   ? -5.705  -9.882  6.105  1.00 24.74 ? 1201 HOH   A O   1 
HETATM 4881 O O   . HOH   E 3 .   ? -5.080  -18.585 10.920 1.00 29.23 ? 1202 HOH   A O   1 
HETATM 4882 O O   . HOH   E 3 .   ? 7.840   -26.889 29.415 1.00 20.87 ? 1203 HOH   A O   1 
HETATM 4883 O O   . HOH   E 3 .   ? 3.406   -20.056 14.265 1.00 18.19 ? 1204 HOH   A O   1 
HETATM 4884 O O   . HOH   E 3 .   ? -9.010  -16.629 15.136 1.00 27.79 ? 1205 HOH   A O   1 
HETATM 4885 O O   . HOH   E 3 .   ? 3.067   -17.516 11.306 1.00 31.24 ? 1206 HOH   A O   1 
HETATM 4886 O O   . HOH   E 3 .   ? -3.661  -3.888  42.005 1.00 29.49 ? 1207 HOH   A O   1 
HETATM 4887 O O   . HOH   E 3 .   ? 30.721  -15.944 19.927 1.00 34.62 ? 1208 HOH   A O   1 
HETATM 4888 O O   . HOH   E 3 .   ? 5.680   -2.371  17.841 1.00 19.03 ? 1209 HOH   A O   1 
HETATM 4889 O O   . HOH   E 3 .   ? 4.785   -15.193 13.902 1.00 18.56 ? 1210 HOH   A O   1 
HETATM 4890 O O   . HOH   E 3 .   ? 17.192  -16.080 48.556 1.00 27.10 ? 1211 HOH   A O   1 
HETATM 4891 O O   . HOH   E 3 .   ? 11.263  -4.393  23.069 1.00 21.82 ? 1212 HOH   A O   1 
HETATM 4892 O O   . HOH   E 3 .   ? 14.770  -22.832 32.115 1.00 24.62 ? 1213 HOH   A O   1 
HETATM 4893 O O   . HOH   E 3 .   ? -1.809  -14.319 40.415 1.00 27.36 ? 1214 HOH   A O   1 
HETATM 4894 O O   . HOH   E 3 .   ? 25.911  -11.200 14.303 1.00 36.54 ? 1215 HOH   A O   1 
HETATM 4895 O O   . HOH   E 3 .   ? 3.559   -4.441  15.557 1.00 32.59 ? 1216 HOH   A O   1 
HETATM 4896 O O   . HOH   E 3 .   ? 18.249  -16.491 17.328 1.00 22.86 ? 1217 HOH   A O   1 
HETATM 4897 O O   . HOH   E 3 .   ? 0.702   -8.425  6.793  1.00 39.20 ? 1218 HOH   A O   1 
HETATM 4898 O O   . HOH   E 3 .   ? 4.425   -13.408 10.481 1.00 19.30 ? 1219 HOH   A O   1 
HETATM 4899 O O   . HOH   E 3 .   ? 19.225  -12.506 23.119 1.00 3.00  ? 1220 HOH   A O   1 
HETATM 4900 O O   . HOH   E 3 .   ? 15.109  -16.759 19.046 1.00 24.28 ? 1221 HOH   A O   1 
HETATM 4901 O O   . HOH   E 3 .   ? 26.334  -30.921 12.116 1.00 49.72 ? 1222 HOH   A O   1 
HETATM 4902 O O   . HOH   E 3 .   ? 14.282  -14.104 36.635 1.00 28.99 ? 1223 HOH   A O   1 
HETATM 4903 O O   . HOH   E 3 .   ? 27.119  -15.236 40.711 1.00 33.73 ? 1224 HOH   A O   1 
HETATM 4904 O O   . HOH   E 3 .   ? -10.975 -10.722 15.179 1.00 31.14 ? 1225 HOH   A O   1 
HETATM 4905 O O   . HOH   E 3 .   ? 8.078   -8.675  14.082 1.00 18.89 ? 1226 HOH   A O   1 
HETATM 4906 O O   . HOH   E 3 .   ? -5.319  -18.255 13.295 1.00 18.66 ? 1227 HOH   A O   1 
HETATM 4907 O O   . HOH   E 3 .   ? 1.079   0.450   30.879 1.00 16.94 ? 1228 HOH   A O   1 
HETATM 4908 O O   . HOH   E 3 .   ? 14.625  -2.356  20.620 1.00 37.89 ? 1229 HOH   A O   1 
HETATM 4909 O O   . HOH   E 3 .   ? 28.195  -16.609 21.016 1.00 15.55 ? 1230 HOH   A O   1 
HETATM 4910 O O   . HOH   E 3 .   ? 17.731  -5.540  23.848 1.00 52.21 ? 1231 HOH   A O   1 
HETATM 4911 O O   . HOH   E 3 .   ? 10.981  -19.490 12.969 1.00 16.92 ? 1232 HOH   A O   1 
HETATM 4912 O O   . HOH   E 3 .   ? 18.471  -18.432 25.240 1.00 32.60 ? 1233 HOH   A O   1 
HETATM 4913 O O   . HOH   E 3 .   ? 20.785  -5.307  19.138 1.00 29.53 ? 1234 HOH   A O   1 
HETATM 4914 O O   . HOH   E 3 .   ? 18.897  -13.258 25.699 1.00 13.08 ? 1235 HOH   A O   1 
HETATM 4915 O O   . HOH   E 3 .   ? -1.485  0.574   24.302 1.00 23.36 ? 1236 HOH   A O   1 
HETATM 4916 O O   . HOH   E 3 .   ? -1.857  -25.302 21.448 1.00 12.33 ? 1237 HOH   A O   1 
HETATM 4917 O O   . HOH   E 3 .   ? 19.822  -8.575  26.179 1.00 27.68 ? 1238 HOH   A O   1 
HETATM 4918 O O   . HOH   E 3 .   ? 23.675  -23.642 28.577 1.00 19.76 ? 1239 HOH   A O   1 
HETATM 4919 O O   . HOH   E 3 .   ? 13.613  -7.028  29.759 1.00 41.05 ? 1240 HOH   A O   1 
HETATM 4920 O O   . HOH   E 3 .   ? 23.442  -14.193 24.759 1.00 23.77 ? 1241 HOH   A O   1 
HETATM 4921 O O   . HOH   E 3 .   ? -13.247 -20.926 25.330 1.00 47.53 ? 1242 HOH   A O   1 
HETATM 4922 O O   . HOH   E 3 .   ? 2.293   -23.597 19.923 1.00 13.99 ? 1243 HOH   A O   1 
HETATM 4923 O O   . HOH   E 3 .   ? -16.242 -16.364 15.903 1.00 21.00 ? 1244 HOH   A O   1 
HETATM 4924 O O   . HOH   E 3 .   ? 10.331  -5.890  8.230  1.00 37.00 ? 1245 HOH   A O   1 
HETATM 4925 O O   . HOH   E 3 .   ? -15.087 -11.373 12.749 1.00 28.53 ? 1246 HOH   A O   1 
HETATM 4926 O O   . HOH   E 3 .   ? -13.283 -11.619 9.130  1.00 30.02 ? 1247 HOH   A O   1 
HETATM 4927 O O   . HOH   E 3 .   ? -11.737 -8.301  10.577 1.00 22.50 ? 1248 HOH   A O   1 
HETATM 4928 O O   . HOH   E 3 .   ? 12.876  -10.941 8.688  1.00 25.53 ? 1249 HOH   A O   1 
HETATM 4929 O O   . HOH   E 3 .   ? 12.369  -16.891 9.891  1.00 28.86 ? 1250 HOH   A O   1 
HETATM 4930 O O   . HOH   E 3 .   ? 27.079  -35.654 19.269 1.00 26.40 ? 1251 HOH   A O   1 
HETATM 4931 O O   . HOH   E 3 .   ? 16.746  -21.645 22.590 1.00 23.34 ? 1252 HOH   A O   1 
HETATM 4932 O O   . HOH   E 3 .   ? -0.024  -28.752 37.931 1.00 50.19 ? 1253 HOH   A O   1 
HETATM 4933 O O   . HOH   E 3 .   ? 20.198  -30.498 8.751  1.00 47.81 ? 1254 HOH   A O   1 
HETATM 4934 O O   . HOH   E 3 .   ? 4.379   -21.538 39.014 1.00 38.54 ? 1255 HOH   A O   1 
HETATM 4935 O O   . HOH   E 3 .   ? 19.693  -15.353 24.684 1.00 19.20 ? 1256 HOH   A O   1 
HETATM 4936 O O   . HOH   E 3 .   ? 21.121  -18.541 24.231 1.00 23.55 ? 1257 HOH   A O   1 
HETATM 4937 O O   . HOH   E 3 .   ? -4.295  -6.562  5.449  1.00 24.55 ? 1258 HOH   A O   1 
HETATM 4938 O O   . HOH   E 3 .   ? -16.534 -16.309 22.359 1.00 28.10 ? 1259 HOH   A O   1 
HETATM 4939 O O   . HOH   E 3 .   ? 7.340   -8.523  32.733 1.00 40.48 ? 1260 HOH   A O   1 
HETATM 4940 O O   . HOH   E 3 .   ? -10.850 -23.417 19.015 1.00 39.73 ? 1261 HOH   A O   1 
HETATM 4941 O O   . HOH   E 3 .   ? 1.382   -15.158 9.816  1.00 28.69 ? 1262 HOH   A O   1 
HETATM 4942 O O   . HOH   E 3 .   ? 10.760  -8.088  31.363 1.00 14.11 ? 1263 HOH   A O   1 
HETATM 4943 O O   . HOH   E 3 .   ? -10.368 -5.152  9.579  1.00 28.90 ? 1264 HOH   A O   1 
HETATM 4944 O O   . HOH   E 3 .   ? 22.197  -37.912 15.535 1.00 34.73 ? 1265 HOH   A O   1 
HETATM 4945 O O   . HOH   E 3 .   ? 18.199  -15.126 9.366  1.00 32.09 ? 1266 HOH   A O   1 
HETATM 4946 O O   . HOH   E 3 .   ? -15.931 -17.428 3.403  1.00 39.59 ? 1267 HOH   A O   1 
HETATM 4947 O O   . HOH   E 3 .   ? 11.511  -27.783 15.674 1.00 30.80 ? 1268 HOH   A O   1 
HETATM 4948 O O   . HOH   E 3 .   ? 22.695  -17.792 34.683 1.00 35.26 ? 1269 HOH   A O   1 
HETATM 4949 O O   . HOH   E 3 .   ? -1.784  -25.615 12.159 1.00 30.03 ? 1270 HOH   A O   1 
HETATM 4950 O O   . HOH   E 3 .   ? -4.336  -28.879 28.750 1.00 34.46 ? 1271 HOH   A O   1 
HETATM 4951 O O   . HOH   E 3 .   ? 3.813   -4.619  9.314  1.00 29.56 ? 1272 HOH   A O   1 
HETATM 4952 O O   . HOH   E 3 .   ? 18.842  -3.116  12.831 1.00 43.52 ? 1273 HOH   A O   1 
HETATM 4953 O O   . HOH   E 3 .   ? 7.193   -5.984  7.880  1.00 27.02 ? 1274 HOH   A O   1 
HETATM 4954 O O   . HOH   E 3 .   ? 42.819  -23.206 26.026 1.00 33.05 ? 1275 HOH   A O   1 
HETATM 4955 O O   . HOH   E 3 .   ? 24.039  -31.450 34.368 1.00 43.93 ? 1276 HOH   A O   1 
HETATM 4956 O O   . HOH   E 3 .   ? 1.096   -27.358 16.329 1.00 50.36 ? 1277 HOH   A O   1 
HETATM 4957 O O   . HOH   E 3 .   ? -12.490 -9.851  13.372 1.00 37.34 ? 1278 HOH   A O   1 
HETATM 4958 O O   . HOH   E 3 .   ? 12.910  -5.770  27.206 1.00 23.77 ? 1279 HOH   A O   1 
HETATM 4959 O O   . HOH   E 3 .   ? 24.974  -9.961  22.015 1.00 38.98 ? 1280 HOH   A O   1 
HETATM 4960 O O   . HOH   E 3 .   ? -2.431  -27.863 17.197 1.00 26.93 ? 1281 HOH   A O   1 
HETATM 4961 O O   . HOH   E 3 .   ? 0.644   -23.113 -5.800 1.00 31.53 ? 1282 HOH   A O   1 
HETATM 4962 O O   . HOH   F 3 .   ? 40.257  -26.661 39.113 1.00 37.06 ? 1201 HOH   B O   1 
HETATM 4963 O O   . HOH   F 3 .   ? 61.253  -7.324  33.240 1.00 28.07 ? 1202 HOH   B O   1 
HETATM 4964 O O   . HOH   F 3 .   ? 44.502  -20.091 54.168 1.00 28.28 ? 1203 HOH   B O   1 
HETATM 4965 O O   . HOH   F 3 .   ? 28.861  -12.507 45.201 1.00 9.95  ? 1204 HOH   B O   1 
HETATM 4966 O O   . HOH   F 3 .   ? 56.971  -16.664 53.150 1.00 30.34 ? 1205 HOH   B O   1 
HETATM 4967 O O   . HOH   F 3 .   ? 57.810  -22.882 65.172 1.00 28.08 ? 1206 HOH   B O   1 
HETATM 4968 O O   . HOH   F 3 .   ? 44.125  -4.203  52.572 1.00 10.43 ? 1207 HOH   B O   1 
HETATM 4969 O O   . HOH   F 3 .   ? 52.962  -18.621 57.507 1.00 15.10 ? 1208 HOH   B O   1 
HETATM 4970 O O   . HOH   F 3 .   ? 63.332  -18.088 40.653 1.00 29.68 ? 1209 HOH   B O   1 
HETATM 4971 O O   . HOH   F 3 .   ? 33.198  -22.832 36.656 1.00 11.67 ? 1210 HOH   B O   1 
HETATM 4972 O O   . HOH   F 3 .   ? 53.114  -18.170 54.999 1.00 22.31 ? 1211 HOH   B O   1 
HETATM 4973 O O   . HOH   F 3 .   ? 24.269  -23.918 39.799 1.00 24.43 ? 1212 HOH   B O   1 
HETATM 4974 O O   . HOH   F 3 .   ? 42.148  -2.365  50.540 1.00 28.60 ? 1213 HOH   B O   1 
HETATM 4975 O O   . HOH   F 3 .   ? 29.919  -16.143 50.768 1.00 24.61 ? 1214 HOH   B O   1 
HETATM 4976 O O   . HOH   F 3 .   ? 29.167  -35.262 54.029 1.00 42.05 ? 1215 HOH   B O   1 
HETATM 4977 O O   . HOH   F 3 .   ? 33.718  -30.515 36.662 1.00 40.21 ? 1216 HOH   B O   1 
HETATM 4978 O O   . HOH   F 3 .   ? 59.072  -10.626 53.030 1.00 34.12 ? 1217 HOH   B O   1 
HETATM 4979 O O   . HOH   F 3 .   ? 53.683  -10.298 62.116 1.00 23.58 ? 1218 HOH   B O   1 
HETATM 4980 O O   . HOH   F 3 .   ? 28.942  -12.758 42.339 1.00 16.71 ? 1219 HOH   B O   1 
HETATM 4981 O O   . HOH   F 3 .   ? 63.979  -23.975 56.090 1.00 50.18 ? 1220 HOH   B O   1 
HETATM 4982 O O   . HOH   F 3 .   ? 43.099  -15.046 54.659 1.00 23.63 ? 1221 HOH   B O   1 
HETATM 4983 O O   . HOH   F 3 .   ? 43.376  -13.638 57.940 1.00 10.04 ? 1222 HOH   B O   1 
HETATM 4984 O O   . HOH   F 3 .   ? 45.056  -15.328 57.072 1.00 25.44 ? 1223 HOH   B O   1 
HETATM 4985 O O   . HOH   F 3 .   ? 32.808  -16.575 49.490 1.00 16.79 ? 1224 HOH   B O   1 
HETATM 4986 O O   . HOH   F 3 .   ? 45.727  -23.536 48.539 1.00 28.03 ? 1225 HOH   B O   1 
HETATM 4987 O O   . HOH   F 3 .   ? 39.828  -8.581  54.438 1.00 16.19 ? 1226 HOH   B O   1 
HETATM 4988 O O   . HOH   F 3 .   ? 33.942  -14.685 31.955 1.00 33.36 ? 1227 HOH   B O   1 
HETATM 4989 O O   . HOH   F 3 .   ? 23.192  -29.049 62.473 1.00 39.53 ? 1228 HOH   B O   1 
HETATM 4990 O O   . HOH   F 3 .   ? 28.157  -15.126 43.887 1.00 24.50 ? 1229 HOH   B O   1 
HETATM 4991 O O   . HOH   F 3 .   ? 21.691  -30.468 56.393 1.00 36.91 ? 1230 HOH   B O   1 
HETATM 4992 O O   . HOH   F 3 .   ? 37.001  -18.510 55.699 1.00 25.18 ? 1231 HOH   B O   1 
HETATM 4993 O O   . HOH   F 3 .   ? 59.985  -4.324  34.954 1.00 31.20 ? 1232 HOH   B O   1 
HETATM 4994 O O   . HOH   F 3 .   ? 47.895  -29.205 47.923 1.00 23.53 ? 1233 HOH   B O   1 
HETATM 4995 O O   . HOH   F 3 .   ? 44.888  -17.951 56.622 1.00 31.81 ? 1234 HOH   B O   1 
HETATM 4996 O O   . HOH   F 3 .   ? 36.824  -3.956  45.193 1.00 15.37 ? 1235 HOH   B O   1 
HETATM 4997 O O   . HOH   F 3 .   ? 46.709  -14.995 58.810 1.00 15.41 ? 1236 HOH   B O   1 
HETATM 4998 O O   . HOH   F 3 .   ? 49.499  -25.174 56.779 1.00 26.74 ? 1237 HOH   B O   1 
HETATM 4999 O O   . HOH   F 3 .   ? 27.581  -29.564 59.998 1.00 35.18 ? 1238 HOH   B O   1 
HETATM 5000 O O   . HOH   F 3 .   ? 42.002  0.130   43.611 1.00 22.40 ? 1239 HOH   B O   1 
HETATM 5001 O O   . HOH   F 3 .   ? 52.262  -5.634  63.053 1.00 24.21 ? 1240 HOH   B O   1 
HETATM 5002 O O   . HOH   F 3 .   ? 55.766  -21.815 29.885 1.00 46.24 ? 1241 HOH   B O   1 
HETATM 5003 O O   . HOH   F 3 .   ? 24.572  -13.674 43.719 1.00 31.38 ? 1242 HOH   B O   1 
HETATM 5004 O O   . HOH   F 3 .   ? 19.700  -16.818 47.367 1.00 13.21 ? 1243 HOH   B O   1 
HETATM 5005 O O   . HOH   F 3 .   ? 49.597  -25.329 47.037 1.00 33.15 ? 1244 HOH   B O   1 
HETATM 5006 O O   . HOH   F 3 .   ? 52.378  -8.213  63.310 1.00 41.07 ? 1245 HOH   B O   1 
HETATM 5007 O O   . HOH   F 3 .   ? 61.514  -20.858 52.607 1.00 26.67 ? 1246 HOH   B O   1 
HETATM 5008 O O   . HOH   F 3 .   ? 29.609  -20.329 43.771 1.00 43.46 ? 1247 HOH   B O   1 
HETATM 5009 O O   . HOH   F 3 .   ? 54.451  -22.576 63.386 1.00 37.44 ? 1248 HOH   B O   1 
HETATM 5010 O O   . HOH   F 3 .   ? 29.547  -14.969 59.133 1.00 32.11 ? 1249 HOH   B O   1 
HETATM 5011 O O   . HOH   F 3 .   ? 30.642  -5.213  44.598 1.00 33.55 ? 1250 HOH   B O   1 
HETATM 5012 O O   . HOH   F 3 .   ? 31.338  -21.468 45.794 1.00 10.81 ? 1251 HOH   B O   1 
HETATM 5013 O O   . HOH   F 3 .   ? 41.418  -11.438 65.732 1.00 24.52 ? 1252 HOH   B O   1 
HETATM 5014 O O   . HOH   F 3 .   ? 34.992  -10.757 59.709 1.00 23.30 ? 1253 HOH   B O   1 
HETATM 5015 O O   . HOH   F 3 .   ? 26.717  -18.286 44.291 1.00 10.54 ? 1254 HOH   B O   1 
HETATM 5016 O O   . HOH   F 3 .   ? 60.764  -9.133  31.495 1.00 24.28 ? 1255 HOH   B O   1 
HETATM 5017 O O   . HOH   F 3 .   ? 52.390  -28.508 40.195 1.00 50.70 ? 1256 HOH   B O   1 
HETATM 5018 O O   . HOH   F 3 .   ? 41.237  -28.411 52.941 1.00 44.25 ? 1257 HOH   B O   1 
HETATM 5019 O O   . HOH   F 3 .   ? 55.017  -29.062 45.796 1.00 34.11 ? 1258 HOH   B O   1 
HETATM 5020 O O   . HOH   F 3 .   ? 58.681  -23.607 49.285 1.00 35.68 ? 1259 HOH   B O   1 
HETATM 5021 O O   . HOH   F 3 .   ? 32.272  -33.577 55.598 1.00 51.11 ? 1260 HOH   B O   1 
HETATM 5022 O O   . HOH   F 3 .   ? 12.507  -36.078 48.885 1.00 54.23 ? 1261 HOH   B O   1 
HETATM 5023 O O   . HOH   F 3 .   ? 26.581  -11.909 43.883 1.00 18.70 ? 1262 HOH   B O   1 
HETATM 5024 O O   . HOH   F 3 .   ? 29.198  -20.936 37.303 1.00 20.69 ? 1263 HOH   B O   1 
HETATM 5025 O O   . HOH   F 3 .   ? 34.865  -5.856  41.623 1.00 26.33 ? 1264 HOH   B O   1 
HETATM 5026 O O   . HOH   F 3 .   ? 34.340  -14.629 28.938 1.00 31.32 ? 1265 HOH   B O   1 
HETATM 5027 O O   . HOH   F 3 .   ? 35.426  -16.487 58.590 1.00 35.72 ? 1266 HOH   B O   1 
HETATM 5028 O O   . HOH   F 3 .   ? 51.801  -1.397  47.217 1.00 43.35 ? 1267 HOH   B O   1 
HETATM 5029 O O   . HOH   F 3 .   ? 45.208  -24.050 61.665 1.00 29.50 ? 1268 HOH   B O   1 
HETATM 5030 O O   . HOH   F 3 .   ? 59.812  -8.029  57.663 1.00 20.04 ? 1269 HOH   B O   1 
HETATM 5031 O O   . HOH   F 3 .   ? 20.552  -35.231 49.785 1.00 29.76 ? 1270 HOH   B O   1 
HETATM 5032 O O   . HOH   F 3 .   ? 27.090  -31.380 63.661 1.00 56.23 ? 1271 HOH   B O   1 
HETATM 5033 O O   . HOH   F 3 .   ? 15.707  -7.461  56.554 1.00 52.94 ? 1272 HOH   B O   1 
HETATM 5034 O O   . HOH   F 3 .   ? 58.125  -25.229 46.751 1.00 45.43 ? 1273 HOH   B O   1 
HETATM 5035 O O   . HOH   F 3 .   ? 36.503  -27.566 52.625 1.00 19.63 ? 1274 HOH   B O   1 
HETATM 5036 O O   . HOH   F 3 .   ? 28.448  -6.482  42.048 1.00 48.11 ? 1275 HOH   B O   1 
HETATM 5037 O O   . HOH   F 3 .   ? 60.171  -9.122  55.011 1.00 38.38 ? 1276 HOH   B O   1 
HETATM 5038 O O   . HOH   F 3 .   ? 44.660  -21.352 65.920 1.00 30.81 ? 1277 HOH   B O   1 
HETATM 5039 O O   . HOH   F 3 .   ? 22.255  -16.568 25.291 1.00 21.12 ? 1278 HOH   B O   1 
HETATM 5040 O O   . HOH   F 3 .   ? 48.795  -27.123 59.068 1.00 41.17 ? 1279 HOH   B O   1 
HETATM 5041 O O   . HOH   F 3 .   ? 57.566  -4.591  63.566 1.00 41.85 ? 1280 HOH   B O   1 
HETATM 5042 O O   . HOH   F 3 .   ? 25.697  -16.161 43.344 1.00 12.61 ? 1281 HOH   B O   1 
HETATM 5043 O O   . HOH   F 3 .   ? 46.121  -26.183 49.483 1.00 29.72 ? 1282 HOH   B O   1 
HETATM 5044 O O   . HOH   F 3 .   ? 44.539  -28.251 49.316 1.00 34.97 ? 1283 HOH   B O   1 
HETATM 5045 O O   . HOH   F 3 .   ? 50.410  -27.390 51.893 1.00 39.47 ? 1284 HOH   B O   1 
HETATM 5046 O O   . HOH   F 3 .   ? 44.364  -23.581 66.854 1.00 41.28 ? 1285 HOH   B O   1 
HETATM 5047 O O   . HOH   F 3 .   ? 46.474  -30.013 64.961 1.00 40.82 ? 1286 HOH   B O   1 
# 
