data_9HBO
# 
_entry.id   9HBO 
# 
_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   9HBO         pdb_00009hbo 10.2210/pdb9hbo/pdb 
WWPDB D_1292143044 ?            ?                   
# 
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 2025-02-05 
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                        9HBO 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-07 
_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              catarina.felisbertorodrigues@astrazeneca.com 
_pdbx_contact_author.name_first         Catarina 
_pdbx_contact_author.name_last          Felisberto-Rodrigues 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1928-6091 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Felisberto-Rodrigues, C.' 1 0000-0002-1928-6091 
'Hargreaves, D.'           2 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' 37774.594 2   2.7.10.1 V948R ? ? 
2 non-polymer syn 
;1-[2-[5-[1-[bis(fluoranyl)methyl]-5-methyl-pyrazol-4-yl]-2,4-bis(fluoranyl)phenyl]-3-pyrimidin-4-yl-4,6-dihydropyrrolo[3,4-d]imidazol-5-yl]propan-1-one
;
485.437   2   ?        ?     ? ? 
3 water       nat water 18.015    120 ?        ?     ? ? 
# 
_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       
;GSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPG
NPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQH
VKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKG
ERLPQPPICTIDVYMIMRKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDV
VDADEYLIPQQG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPG
NPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQH
VKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKG
ERLPQPPICTIDVYMIMRKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDV
VDADEYLIPQQG
;
_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-[1-[bis(fluoranyl)methyl]-5-methyl-pyrazol-4-yl]-2,4-bis(fluoranyl)phenyl]-3-pyrimidin-4-yl-4,6-dihydropyrrolo[3,4-d]imidazol-5-yl]propan-1-one
;
A1IUK 
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   GLY n 
1 4   GLU n 
1 5   ALA n 
1 6   PRO n 
1 7   ASN n 
1 8   GLN n 
1 9   ALA n 
1 10  LEU n 
1 11  LEU n 
1 12  ARG n 
1 13  ILE n 
1 14  LEU n 
1 15  LYS n 
1 16  GLU n 
1 17  THR n 
1 18  GLU n 
1 19  PHE n 
1 20  LYS n 
1 21  LYS n 
1 22  ILE n 
1 23  LYS n 
1 24  VAL n 
1 25  LEU n 
1 26  GLY n 
1 27  SER n 
1 28  GLY n 
1 29  ALA n 
1 30  PHE n 
1 31  GLY n 
1 32  THR n 
1 33  VAL n 
1 34  TYR n 
1 35  LYS n 
1 36  GLY n 
1 37  LEU n 
1 38  TRP n 
1 39  ILE n 
1 40  PRO n 
1 41  GLU n 
1 42  GLY n 
1 43  GLU n 
1 44  LYS n 
1 45  VAL n 
1 46  LYS n 
1 47  ILE n 
1 48  PRO n 
1 49  VAL n 
1 50  ALA n 
1 51  ILE n 
1 52  LYS n 
1 53  GLU n 
1 54  LEU n 
1 55  ARG n 
1 56  GLU n 
1 57  ALA n 
1 58  THR n 
1 59  SER n 
1 60  PRO n 
1 61  LYS n 
1 62  ALA n 
1 63  ASN n 
1 64  LYS n 
1 65  GLU n 
1 66  ILE n 
1 67  LEU n 
1 68  ASP n 
1 69  GLU n 
1 70  ALA n 
1 71  TYR n 
1 72  VAL n 
1 73  MET n 
1 74  ALA n 
1 75  SER n 
1 76  VAL n 
1 77  ASP n 
1 78  ASN n 
1 79  PRO n 
1 80  GLY n 
1 81  ASN n 
1 82  PRO n 
1 83  HIS n 
1 84  VAL n 
1 85  CYS n 
1 86  ARG n 
1 87  LEU n 
1 88  LEU n 
1 89  GLY n 
1 90  ILE n 
1 91  CYS n 
1 92  LEU n 
1 93  THR n 
1 94  SER n 
1 95  THR n 
1 96  VAL n 
1 97  GLN n 
1 98  LEU n 
1 99  ILE n 
1 100 THR n 
1 101 GLN n 
1 102 LEU n 
1 103 MET n 
1 104 PRO n 
1 105 PHE n 
1 106 GLY n 
1 107 CYS n 
1 108 LEU n 
1 109 LEU n 
1 110 ASP n 
1 111 TYR n 
1 112 VAL n 
1 113 ARG n 
1 114 GLU n 
1 115 HIS n 
1 116 LYS n 
1 117 ASP n 
1 118 ASN n 
1 119 ILE n 
1 120 GLY n 
1 121 SER n 
1 122 GLN n 
1 123 TYR n 
1 124 LEU n 
1 125 LEU n 
1 126 ASN n 
1 127 TRP n 
1 128 CYS n 
1 129 VAL n 
1 130 GLN n 
1 131 ILE n 
1 132 ALA n 
1 133 LYS n 
1 134 GLY n 
1 135 MET n 
1 136 ASN n 
1 137 TYR n 
1 138 LEU n 
1 139 GLU n 
1 140 ASP n 
1 141 ARG n 
1 142 ARG n 
1 143 LEU n 
1 144 VAL n 
1 145 HIS n 
1 146 ARG n 
1 147 ASP n 
1 148 LEU n 
1 149 ALA n 
1 150 ALA n 
1 151 ARG n 
1 152 ASN n 
1 153 VAL n 
1 154 LEU n 
1 155 VAL n 
1 156 LYS n 
1 157 THR n 
1 158 PRO n 
1 159 GLN n 
1 160 HIS n 
1 161 VAL n 
1 162 LYS n 
1 163 ILE n 
1 164 THR n 
1 165 ASP n 
1 166 PHE n 
1 167 GLY n 
1 168 LEU n 
1 169 ALA n 
1 170 LYS n 
1 171 LEU n 
1 172 LEU n 
1 173 GLY n 
1 174 ALA n 
1 175 GLU n 
1 176 GLU n 
1 177 LYS n 
1 178 GLU n 
1 179 TYR n 
1 180 HIS n 
1 181 ALA n 
1 182 GLU n 
1 183 GLY n 
1 184 GLY n 
1 185 LYS n 
1 186 VAL n 
1 187 PRO n 
1 188 ILE n 
1 189 LYS n 
1 190 TRP n 
1 191 MET n 
1 192 ALA n 
1 193 LEU n 
1 194 GLU n 
1 195 SER n 
1 196 ILE n 
1 197 LEU n 
1 198 HIS n 
1 199 ARG n 
1 200 ILE n 
1 201 TYR n 
1 202 THR n 
1 203 HIS n 
1 204 GLN n 
1 205 SER n 
1 206 ASP n 
1 207 VAL n 
1 208 TRP n 
1 209 SER n 
1 210 TYR n 
1 211 GLY n 
1 212 VAL n 
1 213 THR n 
1 214 VAL n 
1 215 TRP n 
1 216 GLU n 
1 217 LEU n 
1 218 MET n 
1 219 THR n 
1 220 PHE n 
1 221 GLY n 
1 222 SER n 
1 223 LYS n 
1 224 PRO n 
1 225 TYR n 
1 226 ASP n 
1 227 GLY n 
1 228 ILE n 
1 229 PRO n 
1 230 ALA n 
1 231 SER n 
1 232 GLU n 
1 233 ILE n 
1 234 SER n 
1 235 SER n 
1 236 ILE n 
1 237 LEU n 
1 238 GLU n 
1 239 LYS n 
1 240 GLY n 
1 241 GLU n 
1 242 ARG n 
1 243 LEU n 
1 244 PRO n 
1 245 GLN n 
1 246 PRO n 
1 247 PRO n 
1 248 ILE n 
1 249 CYS n 
1 250 THR n 
1 251 ILE n 
1 252 ASP n 
1 253 VAL n 
1 254 TYR n 
1 255 MET n 
1 256 ILE n 
1 257 MET n 
1 258 ARG n 
1 259 LYS n 
1 260 CYS n 
1 261 TRP n 
1 262 MET n 
1 263 ILE n 
1 264 ASP n 
1 265 ALA n 
1 266 ASP n 
1 267 SER n 
1 268 ARG n 
1 269 PRO n 
1 270 LYS n 
1 271 PHE n 
1 272 ARG n 
1 273 GLU n 
1 274 LEU n 
1 275 ILE n 
1 276 ILE n 
1 277 GLU n 
1 278 PHE n 
1 279 SER n 
1 280 LYS n 
1 281 MET n 
1 282 ALA n 
1 283 ARG n 
1 284 ASP n 
1 285 PRO n 
1 286 GLN n 
1 287 ARG n 
1 288 TYR n 
1 289 LEU n 
1 290 VAL n 
1 291 ILE n 
1 292 GLN n 
1 293 GLY n 
1 294 ASP n 
1 295 GLU n 
1 296 ARG n 
1 297 MET n 
1 298 HIS n 
1 299 LEU n 
1 300 PRO n 
1 301 SER n 
1 302 PRO n 
1 303 THR n 
1 304 ASP n 
1 305 SER n 
1 306 ASN n 
1 307 PHE n 
1 308 TYR n 
1 309 ARG n 
1 310 ALA n 
1 311 LEU n 
1 312 MET n 
1 313 ASP n 
1 314 GLU n 
1 315 GLU n 
1 316 ASP n 
1 317 MET n 
1 318 ASP n 
1 319 ASP n 
1 320 VAL n 
1 321 VAL n 
1 322 ASP n 
1 323 ALA n 
1 324 ASP n 
1 325 GLU n 
1 326 TYR n 
1 327 LEU n 
1 328 ILE n 
1 329 PRO n 
1 330 GLN n 
1 331 GLN n 
1 332 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                   332 
_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 
A1IUK non-polymer         . 
;1-[2-[5-[1-[bis(fluoranyl)methyl]-5-methyl-pyrazol-4-yl]-2,4-bis(fluoranyl)phenyl]-3-pyrimidin-4-yl-4,6-dihydropyrrolo[3,4-d]imidazol-5-yl]propan-1-one
;
? 'C23 H19 F4 N7 O' 485.437 
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   694  ?   ?   ?   A . n 
A 1 2   SER 2   695  ?   ?   ?   A . n 
A 1 3   GLY 3   696  ?   ?   ?   A . n 
A 1 4   GLU 4   697  ?   ?   ?   A . n 
A 1 5   ALA 5   698  ?   ?   ?   A . n 
A 1 6   PRO 6   699  ?   ?   ?   A . n 
A 1 7   ASN 7   700  ?   ?   ?   A . n 
A 1 8   GLN 8   701  ?   ?   ?   A . n 
A 1 9   ALA 9   702  702 ALA ALA A . n 
A 1 10  LEU 10  703  703 LEU LEU A . n 
A 1 11  LEU 11  704  704 LEU LEU A . n 
A 1 12  ARG 12  705  705 ARG ARG A . n 
A 1 13  ILE 13  706  706 ILE ILE A . n 
A 1 14  LEU 14  707  707 LEU LEU A . n 
A 1 15  LYS 15  708  708 LYS LYS A . n 
A 1 16  GLU 16  709  709 GLU GLU A . n 
A 1 17  THR 17  710  710 THR THR A . n 
A 1 18  GLU 18  711  711 GLU GLU A . n 
A 1 19  PHE 19  712  712 PHE PHE A . n 
A 1 20  LYS 20  713  713 LYS LYS A . n 
A 1 21  LYS 21  714  714 LYS LYS A . n 
A 1 22  ILE 22  715  715 ILE ILE A . n 
A 1 23  LYS 23  716  716 LYS LYS A . n 
A 1 24  VAL 24  717  717 VAL VAL A . n 
A 1 25  LEU 25  718  718 LEU LEU A . n 
A 1 26  GLY 26  719  719 GLY GLY A . n 
A 1 27  SER 27  720  720 SER SER A . n 
A 1 28  GLY 28  721  721 GLY GLY A . n 
A 1 29  ALA 29  722  722 ALA ALA A . n 
A 1 30  PHE 30  723  723 PHE PHE A . n 
A 1 31  GLY 31  724  724 GLY GLY A . n 
A 1 32  THR 32  725  725 THR THR A . n 
A 1 33  VAL 33  726  726 VAL VAL A . n 
A 1 34  TYR 34  727  727 TYR TYR A . n 
A 1 35  LYS 35  728  728 LYS LYS A . n 
A 1 36  GLY 36  729  729 GLY GLY A . n 
A 1 37  LEU 37  730  730 LEU LEU A . n 
A 1 38  TRP 38  731  731 TRP TRP A . n 
A 1 39  ILE 39  732  732 ILE ILE A . n 
A 1 40  PRO 40  733  733 PRO PRO A . n 
A 1 41  GLU 41  734  734 GLU GLU A . n 
A 1 42  GLY 42  735  735 GLY GLY A . n 
A 1 43  GLU 43  736  736 GLU GLU A . n 
A 1 44  LYS 44  737  737 LYS LYS A . n 
A 1 45  VAL 45  738  738 VAL VAL A . n 
A 1 46  LYS 46  739  739 LYS LYS A . n 
A 1 47  ILE 47  740  740 ILE ILE A . n 
A 1 48  PRO 48  741  741 PRO PRO A . n 
A 1 49  VAL 49  742  742 VAL VAL A . n 
A 1 50  ALA 50  743  743 ALA ALA A . n 
A 1 51  ILE 51  744  744 ILE ILE A . n 
A 1 52  LYS 52  745  745 LYS LYS A . n 
A 1 53  GLU 53  746  746 GLU GLU A . n 
A 1 54  LEU 54  747  747 LEU LEU A . n 
A 1 55  ARG 55  748  748 ARG ARG A . n 
A 1 56  GLU 56  749  749 GLU GLU A . n 
A 1 57  ALA 57  750  750 ALA ALA A . n 
A 1 58  THR 58  751  751 THR THR A . n 
A 1 59  SER 59  752  752 SER SER A . n 
A 1 60  PRO 60  753  753 PRO PRO A . n 
A 1 61  LYS 61  754  754 LYS LYS A . n 
A 1 62  ALA 62  755  755 ALA ALA A . n 
A 1 63  ASN 63  756  756 ASN ASN A . n 
A 1 64  LYS 64  757  757 LYS LYS A . n 
A 1 65  GLU 65  758  758 GLU GLU A . n 
A 1 66  ILE 66  759  759 ILE ILE A . n 
A 1 67  LEU 67  760  760 LEU LEU A . n 
A 1 68  ASP 68  761  761 ASP ASP A . n 
A 1 69  GLU 69  762  762 GLU GLU A . n 
A 1 70  ALA 70  763  763 ALA ALA A . n 
A 1 71  TYR 71  764  764 TYR TYR A . n 
A 1 72  VAL 72  765  765 VAL VAL A . n 
A 1 73  MET 73  766  766 MET MET A . n 
A 1 74  ALA 74  767  767 ALA ALA A . n 
A 1 75  SER 75  768  768 SER SER A . n 
A 1 76  VAL 76  769  769 VAL VAL A . n 
A 1 77  ASP 77  770  770 ASP ASP A . n 
A 1 78  ASN 78  771  771 ASN ASN A . n 
A 1 79  PRO 79  772  772 PRO PRO A . n 
A 1 80  GLY 80  773  773 GLY GLY A . n 
A 1 81  ASN 81  774  774 ASN ASN A . n 
A 1 82  PRO 82  775  775 PRO PRO A . n 
A 1 83  HIS 83  776  776 HIS HIS A . n 
A 1 84  VAL 84  777  777 VAL VAL A . n 
A 1 85  CYS 85  778  778 CYS CYS A . n 
A 1 86  ARG 86  779  779 ARG ARG A . n 
A 1 87  LEU 87  780  780 LEU LEU A . n 
A 1 88  LEU 88  781  781 LEU LEU A . n 
A 1 89  GLY 89  782  782 GLY GLY A . n 
A 1 90  ILE 90  783  783 ILE ILE A . n 
A 1 91  CYS 91  784  784 CYS CYS A . n 
A 1 92  LEU 92  785  785 LEU LEU A . n 
A 1 93  THR 93  786  786 THR THR A . n 
A 1 94  SER 94  787  787 SER SER A . n 
A 1 95  THR 95  788  788 THR THR A . n 
A 1 96  VAL 96  789  789 VAL VAL A . n 
A 1 97  GLN 97  790  790 GLN GLN A . n 
A 1 98  LEU 98  791  791 LEU LEU A . n 
A 1 99  ILE 99  792  792 ILE ILE A . n 
A 1 100 THR 100 793  793 THR THR A . n 
A 1 101 GLN 101 794  794 GLN GLN A . n 
A 1 102 LEU 102 795  795 LEU LEU A . n 
A 1 103 MET 103 796  796 MET MET A . n 
A 1 104 PRO 104 797  797 PRO PRO A . n 
A 1 105 PHE 105 798  798 PHE PHE A . n 
A 1 106 GLY 106 799  799 GLY GLY A . n 
A 1 107 CYS 107 800  800 CYS CYS A . n 
A 1 108 LEU 108 801  801 LEU LEU A . n 
A 1 109 LEU 109 802  802 LEU LEU A . n 
A 1 110 ASP 110 803  803 ASP ASP A . n 
A 1 111 TYR 111 804  804 TYR TYR A . n 
A 1 112 VAL 112 805  805 VAL VAL A . n 
A 1 113 ARG 113 806  806 ARG ARG A . n 
A 1 114 GLU 114 807  807 GLU GLU A . n 
A 1 115 HIS 115 808  808 HIS HIS A . n 
A 1 116 LYS 116 809  809 LYS LYS A . n 
A 1 117 ASP 117 810  810 ASP ASP A . n 
A 1 118 ASN 118 811  811 ASN ASN A . n 
A 1 119 ILE 119 812  812 ILE ILE A . n 
A 1 120 GLY 120 813  813 GLY GLY A . n 
A 1 121 SER 121 814  814 SER SER A . n 
A 1 122 GLN 122 815  815 GLN GLN A . n 
A 1 123 TYR 123 816  816 TYR TYR A . n 
A 1 124 LEU 124 817  817 LEU LEU A . n 
A 1 125 LEU 125 818  818 LEU LEU A . n 
A 1 126 ASN 126 819  819 ASN ASN A . n 
A 1 127 TRP 127 820  820 TRP TRP A . n 
A 1 128 CYS 128 821  821 CYS CYS A . n 
A 1 129 VAL 129 822  822 VAL VAL A . n 
A 1 130 GLN 130 823  823 GLN GLN A . n 
A 1 131 ILE 131 824  824 ILE ILE A . n 
A 1 132 ALA 132 825  825 ALA ALA A . n 
A 1 133 LYS 133 826  826 LYS LYS A . n 
A 1 134 GLY 134 827  827 GLY GLY A . n 
A 1 135 MET 135 828  828 MET MET A . n 
A 1 136 ASN 136 829  829 ASN ASN A . n 
A 1 137 TYR 137 830  830 TYR TYR A . n 
A 1 138 LEU 138 831  831 LEU LEU A . n 
A 1 139 GLU 139 832  832 GLU GLU A . n 
A 1 140 ASP 140 833  833 ASP ASP A . n 
A 1 141 ARG 141 834  834 ARG ARG A . n 
A 1 142 ARG 142 835  835 ARG ARG A . n 
A 1 143 LEU 143 836  836 LEU LEU A . n 
A 1 144 VAL 144 837  837 VAL VAL A . n 
A 1 145 HIS 145 838  838 HIS HIS A . n 
A 1 146 ARG 146 839  839 ARG ARG A . n 
A 1 147 ASP 147 840  840 ASP ASP A . n 
A 1 148 LEU 148 841  841 LEU LEU A . n 
A 1 149 ALA 149 842  842 ALA ALA A . n 
A 1 150 ALA 150 843  843 ALA ALA A . n 
A 1 151 ARG 151 844  844 ARG ARG A . n 
A 1 152 ASN 152 845  845 ASN ASN A . n 
A 1 153 VAL 153 846  846 VAL VAL A . n 
A 1 154 LEU 154 847  847 LEU LEU A . n 
A 1 155 VAL 155 848  848 VAL VAL A . n 
A 1 156 LYS 156 849  849 LYS LYS A . n 
A 1 157 THR 157 850  850 THR THR A . n 
A 1 158 PRO 158 851  851 PRO PRO A . n 
A 1 159 GLN 159 852  852 GLN GLN A . n 
A 1 160 HIS 160 853  853 HIS HIS A . n 
A 1 161 VAL 161 854  854 VAL VAL A . n 
A 1 162 LYS 162 855  855 LYS LYS A . n 
A 1 163 ILE 163 856  856 ILE ILE A . n 
A 1 164 THR 164 857  857 THR THR A . n 
A 1 165 ASP 165 858  858 ASP ASP A . n 
A 1 166 PHE 166 859  859 PHE PHE A . n 
A 1 167 GLY 167 860  860 GLY GLY A . n 
A 1 168 LEU 168 861  861 LEU LEU A . n 
A 1 169 ALA 169 862  862 ALA ALA A . n 
A 1 170 LYS 170 863  863 LYS LYS A . n 
A 1 171 LEU 171 864  864 LEU LEU A . n 
A 1 172 LEU 172 865  865 LEU LEU A . n 
A 1 173 GLY 173 866  866 GLY GLY A . n 
A 1 174 ALA 174 867  ?   ?   ?   A . n 
A 1 175 GLU 175 868  ?   ?   ?   A . n 
A 1 176 GLU 176 869  ?   ?   ?   A . n 
A 1 177 LYS 177 870  ?   ?   ?   A . n 
A 1 178 GLU 178 871  ?   ?   ?   A . n 
A 1 179 TYR 179 872  ?   ?   ?   A . n 
A 1 180 HIS 180 873  ?   ?   ?   A . n 
A 1 181 ALA 181 874  ?   ?   ?   A . n 
A 1 182 GLU 182 875  ?   ?   ?   A . n 
A 1 183 GLY 183 876  ?   ?   ?   A . n 
A 1 184 GLY 184 877  ?   ?   ?   A . n 
A 1 185 LYS 185 878  878 LYS LYS A . n 
A 1 186 VAL 186 879  879 VAL VAL A . n 
A 1 187 PRO 187 880  880 PRO PRO A . n 
A 1 188 ILE 188 881  881 ILE ILE A . n 
A 1 189 LYS 189 882  882 LYS LYS A . n 
A 1 190 TRP 190 883  883 TRP TRP A . n 
A 1 191 MET 191 884  884 MET MET A . n 
A 1 192 ALA 192 885  885 ALA ALA A . n 
A 1 193 LEU 193 886  886 LEU LEU A . n 
A 1 194 GLU 194 887  887 GLU GLU A . n 
A 1 195 SER 195 888  888 SER SER A . n 
A 1 196 ILE 196 889  889 ILE ILE A . n 
A 1 197 LEU 197 890  890 LEU LEU A . n 
A 1 198 HIS 198 891  891 HIS HIS A . n 
A 1 199 ARG 199 892  892 ARG ARG A . n 
A 1 200 ILE 200 893  893 ILE ILE A . n 
A 1 201 TYR 201 894  894 TYR TYR A . n 
A 1 202 THR 202 895  895 THR THR A . n 
A 1 203 HIS 203 896  896 HIS HIS A . n 
A 1 204 GLN 204 897  897 GLN GLN A . n 
A 1 205 SER 205 898  898 SER SER A . n 
A 1 206 ASP 206 899  899 ASP ASP A . n 
A 1 207 VAL 207 900  900 VAL VAL A . n 
A 1 208 TRP 208 901  901 TRP TRP A . n 
A 1 209 SER 209 902  902 SER SER A . n 
A 1 210 TYR 210 903  903 TYR TYR A . n 
A 1 211 GLY 211 904  904 GLY GLY A . n 
A 1 212 VAL 212 905  905 VAL VAL A . n 
A 1 213 THR 213 906  906 THR THR A . n 
A 1 214 VAL 214 907  907 VAL VAL A . n 
A 1 215 TRP 215 908  908 TRP TRP A . n 
A 1 216 GLU 216 909  909 GLU GLU A . n 
A 1 217 LEU 217 910  910 LEU LEU A . n 
A 1 218 MET 218 911  911 MET MET A . n 
A 1 219 THR 219 912  912 THR THR A . n 
A 1 220 PHE 220 913  913 PHE PHE A . n 
A 1 221 GLY 221 914  914 GLY GLY A . n 
A 1 222 SER 222 915  915 SER SER A . n 
A 1 223 LYS 223 916  916 LYS LYS A . n 
A 1 224 PRO 224 917  917 PRO PRO A . n 
A 1 225 TYR 225 918  918 TYR TYR A . n 
A 1 226 ASP 226 919  919 ASP ASP A . n 
A 1 227 GLY 227 920  920 GLY GLY A . n 
A 1 228 ILE 228 921  921 ILE ILE A . n 
A 1 229 PRO 229 922  922 PRO PRO A . n 
A 1 230 ALA 230 923  923 ALA ALA A . n 
A 1 231 SER 231 924  924 SER SER A . n 
A 1 232 GLU 232 925  925 GLU GLU A . n 
A 1 233 ILE 233 926  926 ILE ILE A . n 
A 1 234 SER 234 927  927 SER SER A . n 
A 1 235 SER 235 928  928 SER SER A . n 
A 1 236 ILE 236 929  929 ILE ILE A . n 
A 1 237 LEU 237 930  930 LEU LEU A . n 
A 1 238 GLU 238 931  931 GLU GLU A . n 
A 1 239 LYS 239 932  932 LYS LYS A . n 
A 1 240 GLY 240 933  933 GLY GLY A . n 
A 1 241 GLU 241 934  934 GLU GLU A . n 
A 1 242 ARG 242 935  935 ARG ARG A . n 
A 1 243 LEU 243 936  936 LEU LEU A . n 
A 1 244 PRO 244 937  937 PRO PRO A . n 
A 1 245 GLN 245 938  938 GLN GLN A . n 
A 1 246 PRO 246 939  939 PRO PRO A . n 
A 1 247 PRO 247 940  940 PRO PRO A . n 
A 1 248 ILE 248 941  941 ILE ILE A . n 
A 1 249 CYS 249 942  942 CYS CYS A . n 
A 1 250 THR 250 943  943 THR THR A . n 
A 1 251 ILE 251 944  944 ILE ILE A . n 
A 1 252 ASP 252 945  945 ASP ASP A . n 
A 1 253 VAL 253 946  946 VAL VAL A . n 
A 1 254 TYR 254 947  947 TYR TYR A . n 
A 1 255 MET 255 948  948 MET MET A . n 
A 1 256 ILE 256 949  949 ILE ILE A . n 
A 1 257 MET 257 950  950 MET MET A . n 
A 1 258 ARG 258 951  951 ARG ARG A . n 
A 1 259 LYS 259 952  952 LYS LYS A . n 
A 1 260 CYS 260 953  953 CYS CYS A . n 
A 1 261 TRP 261 954  954 TRP TRP A . n 
A 1 262 MET 262 955  955 MET MET A . n 
A 1 263 ILE 263 956  956 ILE ILE A . n 
A 1 264 ASP 264 957  957 ASP ASP A . n 
A 1 265 ALA 265 958  958 ALA ALA A . n 
A 1 266 ASP 266 959  959 ASP ASP A . n 
A 1 267 SER 267 960  960 SER SER A . n 
A 1 268 ARG 268 961  961 ARG ARG A . n 
A 1 269 PRO 269 962  962 PRO PRO A . n 
A 1 270 LYS 270 963  963 LYS LYS A . n 
A 1 271 PHE 271 964  964 PHE PHE A . n 
A 1 272 ARG 272 965  965 ARG ARG A . n 
A 1 273 GLU 273 966  966 GLU GLU A . n 
A 1 274 LEU 274 967  967 LEU LEU A . n 
A 1 275 ILE 275 968  968 ILE ILE A . n 
A 1 276 ILE 276 969  969 ILE ILE A . n 
A 1 277 GLU 277 970  970 GLU GLU A . n 
A 1 278 PHE 278 971  971 PHE PHE A . n 
A 1 279 SER 279 972  972 SER SER A . n 
A 1 280 LYS 280 973  973 LYS LYS A . n 
A 1 281 MET 281 974  974 MET MET A . n 
A 1 282 ALA 282 975  975 ALA ALA A . n 
A 1 283 ARG 283 976  976 ARG ARG A . n 
A 1 284 ASP 284 977  977 ASP ASP A . n 
A 1 285 PRO 285 978  978 PRO PRO A . n 
A 1 286 GLN 286 979  979 GLN GLN A . n 
A 1 287 ARG 287 980  980 ARG ARG A . n 
A 1 288 TYR 288 981  981 TYR TYR A . n 
A 1 289 LEU 289 982  982 LEU LEU A . n 
A 1 290 VAL 290 983  983 VAL VAL A . n 
A 1 291 ILE 291 984  984 ILE ILE A . n 
A 1 292 GLN 292 985  985 GLN GLN A . n 
A 1 293 GLY 293 986  986 GLY GLY A . n 
A 1 294 ASP 294 987  987 ASP ASP A . n 
A 1 295 GLU 295 988  988 GLU GLU A . n 
A 1 296 ARG 296 989  989 ARG ARG A . n 
A 1 297 MET 297 990  ?   ?   ?   A . n 
A 1 298 HIS 298 991  ?   ?   ?   A . n 
A 1 299 LEU 299 992  ?   ?   ?   A . n 
A 1 300 PRO 300 993  ?   ?   ?   A . n 
A 1 301 SER 301 994  ?   ?   ?   A . n 
A 1 302 PRO 302 995  ?   ?   ?   A . n 
A 1 303 THR 303 996  ?   ?   ?   A . n 
A 1 304 ASP 304 997  ?   ?   ?   A . n 
A 1 305 SER 305 998  ?   ?   ?   A . n 
A 1 306 ASN 306 999  ?   ?   ?   A . n 
A 1 307 PHE 307 1000 ?   ?   ?   A . n 
A 1 308 TYR 308 1001 ?   ?   ?   A . n 
A 1 309 ARG 309 1002 ?   ?   ?   A . n 
A 1 310 ALA 310 1003 ?   ?   ?   A . n 
A 1 311 LEU 311 1004 ?   ?   ?   A . n 
A 1 312 MET 312 1005 ?   ?   ?   A . n 
A 1 313 ASP 313 1006 ?   ?   ?   A . n 
A 1 314 GLU 314 1007 ?   ?   ?   A . n 
A 1 315 GLU 315 1008 ?   ?   ?   A . n 
A 1 316 ASP 316 1009 ?   ?   ?   A . n 
A 1 317 MET 317 1010 ?   ?   ?   A . n 
A 1 318 ASP 318 1011 ?   ?   ?   A . n 
A 1 319 ASP 319 1012 ?   ?   ?   A . n 
A 1 320 VAL 320 1013 ?   ?   ?   A . n 
A 1 321 VAL 321 1014 ?   ?   ?   A . n 
A 1 322 ASP 322 1015 ?   ?   ?   A . n 
A 1 323 ALA 323 1016 ?   ?   ?   A . n 
A 1 324 ASP 324 1017 ?   ?   ?   A . n 
A 1 325 GLU 325 1018 ?   ?   ?   A . n 
A 1 326 TYR 326 1019 ?   ?   ?   A . n 
A 1 327 LEU 327 1020 ?   ?   ?   A . n 
A 1 328 ILE 328 1021 ?   ?   ?   A . n 
A 1 329 PRO 329 1022 ?   ?   ?   A . n 
A 1 330 GLN 330 1023 ?   ?   ?   A . n 
A 1 331 GLN 331 1024 ?   ?   ?   A . n 
A 1 332 GLY 332 1025 ?   ?   ?   A . n 
B 1 1   GLY 1   694  ?   ?   ?   B . n 
B 1 2   SER 2   695  ?   ?   ?   B . n 
B 1 3   GLY 3   696  ?   ?   ?   B . n 
B 1 4   GLU 4   697  ?   ?   ?   B . n 
B 1 5   ALA 5   698  ?   ?   ?   B . n 
B 1 6   PRO 6   699  ?   ?   ?   B . n 
B 1 7   ASN 7   700  ?   ?   ?   B . n 
B 1 8   GLN 8   701  ?   ?   ?   B . n 
B 1 9   ALA 9   702  702 ALA ALA B . n 
B 1 10  LEU 10  703  703 LEU LEU B . n 
B 1 11  LEU 11  704  704 LEU LEU B . n 
B 1 12  ARG 12  705  705 ARG ARG B . n 
B 1 13  ILE 13  706  706 ILE ILE B . n 
B 1 14  LEU 14  707  707 LEU LEU B . n 
B 1 15  LYS 15  708  708 LYS LYS B . n 
B 1 16  GLU 16  709  709 GLU GLU B . n 
B 1 17  THR 17  710  710 THR THR B . n 
B 1 18  GLU 18  711  711 GLU GLU B . n 
B 1 19  PHE 19  712  712 PHE PHE B . n 
B 1 20  LYS 20  713  713 LYS LYS B . n 
B 1 21  LYS 21  714  714 LYS LYS B . n 
B 1 22  ILE 22  715  715 ILE ILE B . n 
B 1 23  LYS 23  716  716 LYS LYS B . n 
B 1 24  VAL 24  717  717 VAL VAL B . n 
B 1 25  LEU 25  718  718 LEU LEU B . n 
B 1 26  GLY 26  719  719 GLY GLY B . n 
B 1 27  SER 27  720  720 SER SER B . n 
B 1 28  GLY 28  721  721 GLY GLY B . n 
B 1 29  ALA 29  722  722 ALA ALA B . n 
B 1 30  PHE 30  723  723 PHE PHE B . n 
B 1 31  GLY 31  724  724 GLY GLY B . n 
B 1 32  THR 32  725  725 THR THR B . n 
B 1 33  VAL 33  726  726 VAL VAL B . n 
B 1 34  TYR 34  727  727 TYR TYR B . n 
B 1 35  LYS 35  728  728 LYS LYS B . n 
B 1 36  GLY 36  729  729 GLY GLY B . n 
B 1 37  LEU 37  730  730 LEU LEU B . n 
B 1 38  TRP 38  731  731 TRP TRP B . n 
B 1 39  ILE 39  732  732 ILE ILE B . n 
B 1 40  PRO 40  733  733 PRO PRO B . n 
B 1 41  GLU 41  734  734 GLU GLU B . n 
B 1 42  GLY 42  735  735 GLY GLY B . n 
B 1 43  GLU 43  736  736 GLU GLU B . n 
B 1 44  LYS 44  737  737 LYS LYS B . n 
B 1 45  VAL 45  738  738 VAL VAL B . n 
B 1 46  LYS 46  739  739 LYS LYS B . n 
B 1 47  ILE 47  740  740 ILE ILE B . n 
B 1 48  PRO 48  741  741 PRO PRO B . n 
B 1 49  VAL 49  742  742 VAL VAL B . n 
B 1 50  ALA 50  743  743 ALA ALA B . n 
B 1 51  ILE 51  744  744 ILE ILE B . n 
B 1 52  LYS 52  745  745 LYS LYS B . n 
B 1 53  GLU 53  746  746 GLU GLU B . n 
B 1 54  LEU 54  747  747 LEU LEU B . n 
B 1 55  ARG 55  748  748 ARG ARG B . n 
B 1 56  GLU 56  749  749 GLU GLU B . n 
B 1 57  ALA 57  750  750 ALA ALA B . n 
B 1 58  THR 58  751  751 THR THR B . n 
B 1 59  SER 59  752  752 SER SER B . n 
B 1 60  PRO 60  753  753 PRO PRO B . n 
B 1 61  LYS 61  754  754 LYS LYS B . n 
B 1 62  ALA 62  755  755 ALA ALA B . n 
B 1 63  ASN 63  756  756 ASN ASN B . n 
B 1 64  LYS 64  757  757 LYS LYS B . n 
B 1 65  GLU 65  758  758 GLU GLU B . n 
B 1 66  ILE 66  759  759 ILE ILE B . n 
B 1 67  LEU 67  760  760 LEU LEU B . n 
B 1 68  ASP 68  761  761 ASP ASP B . n 
B 1 69  GLU 69  762  762 GLU GLU B . n 
B 1 70  ALA 70  763  763 ALA ALA B . n 
B 1 71  TYR 71  764  764 TYR TYR B . n 
B 1 72  VAL 72  765  765 VAL VAL B . n 
B 1 73  MET 73  766  766 MET MET B . n 
B 1 74  ALA 74  767  767 ALA ALA B . n 
B 1 75  SER 75  768  768 SER SER B . n 
B 1 76  VAL 76  769  769 VAL VAL B . n 
B 1 77  ASP 77  770  770 ASP ASP B . n 
B 1 78  ASN 78  771  771 ASN ASN B . n 
B 1 79  PRO 79  772  772 PRO PRO B . n 
B 1 80  GLY 80  773  773 GLY GLY B . n 
B 1 81  ASN 81  774  774 ASN ASN B . n 
B 1 82  PRO 82  775  775 PRO PRO B . n 
B 1 83  HIS 83  776  776 HIS HIS B . n 
B 1 84  VAL 84  777  777 VAL VAL B . n 
B 1 85  CYS 85  778  778 CYS CYS B . n 
B 1 86  ARG 86  779  779 ARG ARG B . n 
B 1 87  LEU 87  780  780 LEU LEU B . n 
B 1 88  LEU 88  781  781 LEU LEU B . n 
B 1 89  GLY 89  782  782 GLY GLY B . n 
B 1 90  ILE 90  783  783 ILE ILE B . n 
B 1 91  CYS 91  784  784 CYS CYS B . n 
B 1 92  LEU 92  785  785 LEU LEU B . n 
B 1 93  THR 93  786  786 THR THR B . n 
B 1 94  SER 94  787  787 SER SER B . n 
B 1 95  THR 95  788  788 THR THR B . n 
B 1 96  VAL 96  789  789 VAL VAL B . n 
B 1 97  GLN 97  790  790 GLN GLN B . n 
B 1 98  LEU 98  791  791 LEU LEU B . n 
B 1 99  ILE 99  792  792 ILE ILE B . n 
B 1 100 THR 100 793  793 THR THR B . n 
B 1 101 GLN 101 794  794 GLN GLN B . n 
B 1 102 LEU 102 795  795 LEU LEU B . n 
B 1 103 MET 103 796  796 MET MET B . n 
B 1 104 PRO 104 797  797 PRO PRO B . n 
B 1 105 PHE 105 798  798 PHE PHE B . n 
B 1 106 GLY 106 799  799 GLY GLY B . n 
B 1 107 CYS 107 800  800 CYS CYS B . n 
B 1 108 LEU 108 801  801 LEU LEU B . n 
B 1 109 LEU 109 802  802 LEU LEU B . n 
B 1 110 ASP 110 803  803 ASP ASP B . n 
B 1 111 TYR 111 804  804 TYR TYR B . n 
B 1 112 VAL 112 805  805 VAL VAL B . n 
B 1 113 ARG 113 806  806 ARG ARG B . n 
B 1 114 GLU 114 807  807 GLU GLU B . n 
B 1 115 HIS 115 808  808 HIS HIS B . n 
B 1 116 LYS 116 809  809 LYS LYS B . n 
B 1 117 ASP 117 810  810 ASP ASP B . n 
B 1 118 ASN 118 811  811 ASN ASN B . n 
B 1 119 ILE 119 812  812 ILE ILE B . n 
B 1 120 GLY 120 813  813 GLY GLY B . n 
B 1 121 SER 121 814  814 SER SER B . n 
B 1 122 GLN 122 815  815 GLN GLN B . n 
B 1 123 TYR 123 816  816 TYR TYR B . n 
B 1 124 LEU 124 817  817 LEU LEU B . n 
B 1 125 LEU 125 818  818 LEU LEU B . n 
B 1 126 ASN 126 819  819 ASN ASN B . n 
B 1 127 TRP 127 820  820 TRP TRP B . n 
B 1 128 CYS 128 821  821 CYS CYS B . n 
B 1 129 VAL 129 822  822 VAL VAL B . n 
B 1 130 GLN 130 823  823 GLN GLN B . n 
B 1 131 ILE 131 824  824 ILE ILE B . n 
B 1 132 ALA 132 825  825 ALA ALA B . n 
B 1 133 LYS 133 826  826 LYS LYS B . n 
B 1 134 GLY 134 827  827 GLY GLY B . n 
B 1 135 MET 135 828  828 MET MET B . n 
B 1 136 ASN 136 829  829 ASN ASN B . n 
B 1 137 TYR 137 830  830 TYR TYR B . n 
B 1 138 LEU 138 831  831 LEU LEU B . n 
B 1 139 GLU 139 832  832 GLU GLU B . n 
B 1 140 ASP 140 833  833 ASP ASP B . n 
B 1 141 ARG 141 834  834 ARG ARG B . n 
B 1 142 ARG 142 835  835 ARG ARG B . n 
B 1 143 LEU 143 836  836 LEU LEU B . n 
B 1 144 VAL 144 837  837 VAL VAL B . n 
B 1 145 HIS 145 838  838 HIS HIS B . n 
B 1 146 ARG 146 839  839 ARG ARG B . n 
B 1 147 ASP 147 840  840 ASP ASP B . n 
B 1 148 LEU 148 841  841 LEU LEU B . n 
B 1 149 ALA 149 842  842 ALA ALA B . n 
B 1 150 ALA 150 843  843 ALA ALA B . n 
B 1 151 ARG 151 844  844 ARG ARG B . n 
B 1 152 ASN 152 845  845 ASN ASN B . n 
B 1 153 VAL 153 846  846 VAL VAL B . n 
B 1 154 LEU 154 847  847 LEU LEU B . n 
B 1 155 VAL 155 848  848 VAL VAL B . n 
B 1 156 LYS 156 849  849 LYS LYS B . n 
B 1 157 THR 157 850  850 THR THR B . n 
B 1 158 PRO 158 851  851 PRO PRO B . n 
B 1 159 GLN 159 852  852 GLN GLN B . n 
B 1 160 HIS 160 853  853 HIS HIS B . n 
B 1 161 VAL 161 854  854 VAL VAL B . n 
B 1 162 LYS 162 855  855 LYS LYS B . n 
B 1 163 ILE 163 856  856 ILE ILE B . n 
B 1 164 THR 164 857  857 THR THR B . n 
B 1 165 ASP 165 858  858 ASP ASP B . n 
B 1 166 PHE 166 859  859 PHE PHE B . n 
B 1 167 GLY 167 860  860 GLY GLY B . n 
B 1 168 LEU 168 861  861 LEU LEU B . n 
B 1 169 ALA 169 862  862 ALA ALA B . n 
B 1 170 LYS 170 863  863 LYS LYS B . n 
B 1 171 LEU 171 864  864 LEU LEU B . n 
B 1 172 LEU 172 865  865 LEU LEU B . n 
B 1 173 GLY 173 866  866 GLY GLY B . n 
B 1 174 ALA 174 867  867 ALA ALA B . n 
B 1 175 GLU 175 868  868 GLU GLU B . n 
B 1 176 GLU 176 869  869 GLU GLU B . n 
B 1 177 LYS 177 870  870 LYS LYS B . n 
B 1 178 GLU 178 871  ?   ?   ?   B . n 
B 1 179 TYR 179 872  ?   ?   ?   B . n 
B 1 180 HIS 180 873  ?   ?   ?   B . n 
B 1 181 ALA 181 874  ?   ?   ?   B . n 
B 1 182 GLU 182 875  ?   ?   ?   B . n 
B 1 183 GLY 183 876  ?   ?   ?   B . n 
B 1 184 GLY 184 877  877 GLY GLY B . n 
B 1 185 LYS 185 878  878 LYS LYS B . n 
B 1 186 VAL 186 879  879 VAL VAL B . n 
B 1 187 PRO 187 880  880 PRO PRO B . n 
B 1 188 ILE 188 881  881 ILE ILE B . n 
B 1 189 LYS 189 882  882 LYS LYS B . n 
B 1 190 TRP 190 883  883 TRP TRP B . n 
B 1 191 MET 191 884  884 MET MET B . n 
B 1 192 ALA 192 885  885 ALA ALA B . n 
B 1 193 LEU 193 886  886 LEU LEU B . n 
B 1 194 GLU 194 887  887 GLU GLU B . n 
B 1 195 SER 195 888  888 SER SER B . n 
B 1 196 ILE 196 889  889 ILE ILE B . n 
B 1 197 LEU 197 890  890 LEU LEU B . n 
B 1 198 HIS 198 891  891 HIS HIS B . n 
B 1 199 ARG 199 892  892 ARG ARG B . n 
B 1 200 ILE 200 893  893 ILE ILE B . n 
B 1 201 TYR 201 894  894 TYR TYR B . n 
B 1 202 THR 202 895  895 THR THR B . n 
B 1 203 HIS 203 896  896 HIS HIS B . n 
B 1 204 GLN 204 897  897 GLN GLN B . n 
B 1 205 SER 205 898  898 SER SER B . n 
B 1 206 ASP 206 899  899 ASP ASP B . n 
B 1 207 VAL 207 900  900 VAL VAL B . n 
B 1 208 TRP 208 901  901 TRP TRP B . n 
B 1 209 SER 209 902  902 SER SER B . n 
B 1 210 TYR 210 903  903 TYR TYR B . n 
B 1 211 GLY 211 904  904 GLY GLY B . n 
B 1 212 VAL 212 905  905 VAL VAL B . n 
B 1 213 THR 213 906  906 THR THR B . n 
B 1 214 VAL 214 907  907 VAL VAL B . n 
B 1 215 TRP 215 908  908 TRP TRP B . n 
B 1 216 GLU 216 909  909 GLU GLU B . n 
B 1 217 LEU 217 910  910 LEU LEU B . n 
B 1 218 MET 218 911  911 MET MET B . n 
B 1 219 THR 219 912  912 THR THR B . n 
B 1 220 PHE 220 913  913 PHE PHE B . n 
B 1 221 GLY 221 914  914 GLY GLY B . n 
B 1 222 SER 222 915  915 SER SER B . n 
B 1 223 LYS 223 916  916 LYS LYS B . n 
B 1 224 PRO 224 917  917 PRO PRO B . n 
B 1 225 TYR 225 918  918 TYR TYR B . n 
B 1 226 ASP 226 919  919 ASP ASP B . n 
B 1 227 GLY 227 920  920 GLY GLY B . n 
B 1 228 ILE 228 921  921 ILE ILE B . n 
B 1 229 PRO 229 922  922 PRO PRO B . n 
B 1 230 ALA 230 923  923 ALA ALA B . n 
B 1 231 SER 231 924  924 SER SER B . n 
B 1 232 GLU 232 925  925 GLU GLU B . n 
B 1 233 ILE 233 926  926 ILE ILE B . n 
B 1 234 SER 234 927  927 SER SER B . n 
B 1 235 SER 235 928  928 SER SER B . n 
B 1 236 ILE 236 929  929 ILE ILE B . n 
B 1 237 LEU 237 930  930 LEU LEU B . n 
B 1 238 GLU 238 931  931 GLU GLU B . n 
B 1 239 LYS 239 932  932 LYS LYS B . n 
B 1 240 GLY 240 933  933 GLY GLY B . n 
B 1 241 GLU 241 934  934 GLU GLU B . n 
B 1 242 ARG 242 935  935 ARG ARG B . n 
B 1 243 LEU 243 936  936 LEU LEU B . n 
B 1 244 PRO 244 937  937 PRO PRO B . n 
B 1 245 GLN 245 938  938 GLN GLN B . n 
B 1 246 PRO 246 939  939 PRO PRO B . n 
B 1 247 PRO 247 940  940 PRO PRO B . n 
B 1 248 ILE 248 941  941 ILE ILE B . n 
B 1 249 CYS 249 942  942 CYS CYS B . n 
B 1 250 THR 250 943  943 THR THR B . n 
B 1 251 ILE 251 944  944 ILE ILE B . n 
B 1 252 ASP 252 945  945 ASP ASP B . n 
B 1 253 VAL 253 946  946 VAL VAL B . n 
B 1 254 TYR 254 947  947 TYR TYR B . n 
B 1 255 MET 255 948  948 MET MET B . n 
B 1 256 ILE 256 949  949 ILE ILE B . n 
B 1 257 MET 257 950  950 MET MET B . n 
B 1 258 ARG 258 951  951 ARG ARG B . n 
B 1 259 LYS 259 952  952 LYS LYS B . n 
B 1 260 CYS 260 953  953 CYS CYS B . n 
B 1 261 TRP 261 954  954 TRP TRP B . n 
B 1 262 MET 262 955  955 MET MET B . n 
B 1 263 ILE 263 956  956 ILE ILE B . n 
B 1 264 ASP 264 957  957 ASP ASP B . n 
B 1 265 ALA 265 958  958 ALA ALA B . n 
B 1 266 ASP 266 959  959 ASP ASP B . n 
B 1 267 SER 267 960  960 SER SER B . n 
B 1 268 ARG 268 961  961 ARG ARG B . n 
B 1 269 PRO 269 962  962 PRO PRO B . n 
B 1 270 LYS 270 963  963 LYS LYS B . n 
B 1 271 PHE 271 964  964 PHE PHE B . n 
B 1 272 ARG 272 965  965 ARG ARG B . n 
B 1 273 GLU 273 966  966 GLU GLU B . n 
B 1 274 LEU 274 967  967 LEU LEU B . n 
B 1 275 ILE 275 968  968 ILE ILE B . n 
B 1 276 ILE 276 969  969 ILE ILE B . n 
B 1 277 GLU 277 970  970 GLU GLU B . n 
B 1 278 PHE 278 971  971 PHE PHE B . n 
B 1 279 SER 279 972  972 SER SER B . n 
B 1 280 LYS 280 973  973 LYS LYS B . n 
B 1 281 MET 281 974  974 MET MET B . n 
B 1 282 ALA 282 975  975 ALA ALA B . n 
B 1 283 ARG 283 976  976 ARG ARG B . n 
B 1 284 ASP 284 977  977 ASP ASP B . n 
B 1 285 PRO 285 978  978 PRO PRO B . n 
B 1 286 GLN 286 979  979 GLN GLN B . n 
B 1 287 ARG 287 980  980 ARG ARG B . n 
B 1 288 TYR 288 981  981 TYR TYR B . n 
B 1 289 LEU 289 982  982 LEU LEU B . n 
B 1 290 VAL 290 983  983 VAL VAL B . n 
B 1 291 ILE 291 984  984 ILE ILE B . n 
B 1 292 GLN 292 985  985 GLN GLN B . n 
B 1 293 GLY 293 986  986 GLY GLY B . n 
B 1 294 ASP 294 987  987 ASP ASP B . n 
B 1 295 GLU 295 988  988 GLU GLU B . n 
B 1 296 ARG 296 989  ?   ?   ?   B . n 
B 1 297 MET 297 990  ?   ?   ?   B . n 
B 1 298 HIS 298 991  ?   ?   ?   B . n 
B 1 299 LEU 299 992  ?   ?   ?   B . n 
B 1 300 PRO 300 993  ?   ?   ?   B . n 
B 1 301 SER 301 994  ?   ?   ?   B . n 
B 1 302 PRO 302 995  ?   ?   ?   B . n 
B 1 303 THR 303 996  ?   ?   ?   B . n 
B 1 304 ASP 304 997  ?   ?   ?   B . n 
B 1 305 SER 305 998  ?   ?   ?   B . n 
B 1 306 ASN 306 999  ?   ?   ?   B . n 
B 1 307 PHE 307 1000 ?   ?   ?   B . n 
B 1 308 TYR 308 1001 ?   ?   ?   B . n 
B 1 309 ARG 309 1002 ?   ?   ?   B . n 
B 1 310 ALA 310 1003 ?   ?   ?   B . n 
B 1 311 LEU 311 1004 ?   ?   ?   B . n 
B 1 312 MET 312 1005 ?   ?   ?   B . n 
B 1 313 ASP 313 1006 ?   ?   ?   B . n 
B 1 314 GLU 314 1007 ?   ?   ?   B . n 
B 1 315 GLU 315 1008 ?   ?   ?   B . n 
B 1 316 ASP 316 1009 ?   ?   ?   B . n 
B 1 317 MET 317 1010 ?   ?   ?   B . n 
B 1 318 ASP 318 1011 ?   ?   ?   B . n 
B 1 319 ASP 319 1012 ?   ?   ?   B . n 
B 1 320 VAL 320 1013 ?   ?   ?   B . n 
B 1 321 VAL 321 1014 ?   ?   ?   B . n 
B 1 322 ASP 322 1015 ?   ?   ?   B . n 
B 1 323 ALA 323 1016 ?   ?   ?   B . n 
B 1 324 ASP 324 1017 ?   ?   ?   B . n 
B 1 325 GLU 325 1018 ?   ?   ?   B . n 
B 1 326 TYR 326 1019 ?   ?   ?   B . n 
B 1 327 LEU 327 1020 ?   ?   ?   B . n 
B 1 328 ILE 328 1021 ?   ?   ?   B . n 
B 1 329 PRO 329 1022 ?   ?   ?   B . n 
B 1 330 GLN 330 1023 ?   ?   ?   B . n 
B 1 331 GLN 331 1024 ?   ?   ?   B . n 
B 1 332 GLY 332 1025 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IUK 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IUK 
_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 A1IUK 1  1101 1001 A1IUK 51X A . 
D 2 A1IUK 1  1101 1001 A1IUK 51X B . 
E 3 HOH   1  1201 43   HOH   HOH A . 
E 3 HOH   2  1202 180  HOH   HOH A . 
E 3 HOH   3  1203 155  HOH   HOH A . 
E 3 HOH   4  1204 41   HOH   HOH A . 
E 3 HOH   5  1205 37   HOH   HOH A . 
E 3 HOH   6  1206 10   HOH   HOH A . 
E 3 HOH   7  1207 12   HOH   HOH A . 
E 3 HOH   8  1208 4    HOH   HOH A . 
E 3 HOH   9  1209 57   HOH   HOH A . 
E 3 HOH   10 1210 31   HOH   HOH A . 
E 3 HOH   11 1211 32   HOH   HOH A . 
E 3 HOH   12 1212 80   HOH   HOH A . 
E 3 HOH   13 1213 19   HOH   HOH A . 
E 3 HOH   14 1214 145  HOH   HOH A . 
E 3 HOH   15 1215 8    HOH   HOH A . 
E 3 HOH   16 1216 5    HOH   HOH A . 
E 3 HOH   17 1217 17   HOH   HOH A . 
E 3 HOH   18 1218 107  HOH   HOH A . 
E 3 HOH   19 1219 103  HOH   HOH A . 
E 3 HOH   20 1220 29   HOH   HOH A . 
E 3 HOH   21 1221 46   HOH   HOH A . 
E 3 HOH   22 1222 33   HOH   HOH A . 
E 3 HOH   23 1223 48   HOH   HOH A . 
E 3 HOH   24 1224 77   HOH   HOH A . 
E 3 HOH   25 1225 154  HOH   HOH A . 
E 3 HOH   26 1226 39   HOH   HOH A . 
E 3 HOH   27 1227 24   HOH   HOH A . 
E 3 HOH   28 1228 95   HOH   HOH A . 
E 3 HOH   29 1229 163  HOH   HOH A . 
E 3 HOH   30 1230 140  HOH   HOH A . 
E 3 HOH   31 1231 98   HOH   HOH A . 
E 3 HOH   32 1232 53   HOH   HOH A . 
E 3 HOH   33 1233 36   HOH   HOH A . 
E 3 HOH   34 1234 82   HOH   HOH A . 
E 3 HOH   35 1235 56   HOH   HOH A . 
E 3 HOH   36 1236 38   HOH   HOH A . 
E 3 HOH   37 1237 136  HOH   HOH A . 
E 3 HOH   38 1238 70   HOH   HOH A . 
E 3 HOH   39 1239 40   HOH   HOH A . 
E 3 HOH   40 1240 96   HOH   HOH A . 
E 3 HOH   41 1241 79   HOH   HOH A . 
E 3 HOH   42 1242 76   HOH   HOH A . 
E 3 HOH   43 1243 151  HOH   HOH A . 
E 3 HOH   44 1244 119  HOH   HOH A . 
E 3 HOH   45 1245 152  HOH   HOH A . 
E 3 HOH   46 1246 172  HOH   HOH A . 
E 3 HOH   47 1247 135  HOH   HOH A . 
E 3 HOH   48 1248 21   HOH   HOH A . 
E 3 HOH   49 1249 20   HOH   HOH A . 
E 3 HOH   50 1250 101  HOH   HOH A . 
E 3 HOH   51 1251 124  HOH   HOH A . 
E 3 HOH   52 1252 85   HOH   HOH A . 
E 3 HOH   53 1253 139  HOH   HOH A . 
E 3 HOH   54 1254 50   HOH   HOH A . 
E 3 HOH   55 1255 156  HOH   HOH A . 
E 3 HOH   56 1256 102  HOH   HOH A . 
E 3 HOH   57 1257 143  HOH   HOH A . 
E 3 HOH   58 1258 112  HOH   HOH A . 
E 3 HOH   59 1259 92   HOH   HOH A . 
E 3 HOH   60 1260 187  HOH   HOH A . 
E 3 HOH   61 1261 165  HOH   HOH A . 
F 3 HOH   1  1201 62   HOH   HOH B . 
F 3 HOH   2  1202 6    HOH   HOH B . 
F 3 HOH   3  1203 179  HOH   HOH B . 
F 3 HOH   4  1204 52   HOH   HOH B . 
F 3 HOH   5  1205 25   HOH   HOH B . 
F 3 HOH   6  1206 126  HOH   HOH B . 
F 3 HOH   7  1207 71   HOH   HOH B . 
F 3 HOH   8  1208 44   HOH   HOH B . 
F 3 HOH   9  1209 13   HOH   HOH B . 
F 3 HOH   10 1210 146  HOH   HOH B . 
F 3 HOH   11 1211 18   HOH   HOH B . 
F 3 HOH   12 1212 15   HOH   HOH B . 
F 3 HOH   13 1213 11   HOH   HOH B . 
F 3 HOH   14 1214 147  HOH   HOH B . 
F 3 HOH   15 1215 7    HOH   HOH B . 
F 3 HOH   16 1216 22   HOH   HOH B . 
F 3 HOH   17 1217 16   HOH   HOH B . 
F 3 HOH   18 1218 67   HOH   HOH B . 
F 3 HOH   19 1219 73   HOH   HOH B . 
F 3 HOH   20 1220 26   HOH   HOH B . 
F 3 HOH   21 1221 105  HOH   HOH B . 
F 3 HOH   22 1222 45   HOH   HOH B . 
F 3 HOH   23 1223 58   HOH   HOH B . 
F 3 HOH   24 1224 166  HOH   HOH B . 
F 3 HOH   25 1225 9    HOH   HOH B . 
F 3 HOH   26 1226 35   HOH   HOH B . 
F 3 HOH   27 1227 3    HOH   HOH B . 
F 3 HOH   28 1228 30   HOH   HOH B . 
F 3 HOH   29 1229 14   HOH   HOH B . 
F 3 HOH   30 1230 28   HOH   HOH B . 
F 3 HOH   31 1231 42   HOH   HOH B . 
F 3 HOH   32 1232 122  HOH   HOH B . 
F 3 HOH   33 1233 161  HOH   HOH B . 
F 3 HOH   34 1234 93   HOH   HOH B . 
F 3 HOH   35 1235 90   HOH   HOH B . 
F 3 HOH   36 1236 65   HOH   HOH B . 
F 3 HOH   37 1237 86   HOH   HOH B . 
F 3 HOH   38 1238 66   HOH   HOH B . 
F 3 HOH   39 1239 178  HOH   HOH B . 
F 3 HOH   40 1240 87   HOH   HOH B . 
F 3 HOH   41 1241 131  HOH   HOH B . 
F 3 HOH   42 1242 106  HOH   HOH B . 
F 3 HOH   43 1243 89   HOH   HOH B . 
F 3 HOH   44 1244 64   HOH   HOH B . 
F 3 HOH   45 1245 23   HOH   HOH B . 
F 3 HOH   46 1246 123  HOH   HOH B . 
F 3 HOH   47 1247 61   HOH   HOH B . 
F 3 HOH   48 1248 55   HOH   HOH B . 
F 3 HOH   49 1249 142  HOH   HOH B . 
F 3 HOH   50 1250 63   HOH   HOH B . 
F 3 HOH   51 1251 137  HOH   HOH B . 
F 3 HOH   52 1252 149  HOH   HOH B . 
F 3 HOH   53 1253 2    HOH   HOH B . 
F 3 HOH   54 1254 94   HOH   HOH B . 
F 3 HOH   55 1255 49   HOH   HOH B . 
F 3 HOH   56 1256 188  HOH   HOH B . 
F 3 HOH   57 1257 84   HOH   HOH B . 
F 3 HOH   58 1258 91   HOH   HOH B . 
F 3 HOH   59 1259 141  HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A ILE 706 ? CD1 ? A ILE 13  CD1 
2   1 Y 1 A LYS 708 ? CD  ? A LYS 15  CD  
3   1 Y 1 A LYS 708 ? CE  ? A LYS 15  CE  
4   1 Y 1 A LYS 708 ? NZ  ? A LYS 15  NZ  
5   1 Y 1 A LYS 713 ? CG  ? A LYS 20  CG  
6   1 Y 1 A LYS 713 ? CD  ? A LYS 20  CD  
7   1 Y 1 A LYS 713 ? CE  ? A LYS 20  CE  
8   1 Y 1 A LYS 713 ? NZ  ? A LYS 20  NZ  
9   1 Y 1 A LYS 714 ? NZ  ? A LYS 21  NZ  
10  1 Y 1 A ILE 715 ? CD1 ? A ILE 22  CD1 
11  1 Y 1 A LYS 716 ? CD  ? A LYS 23  CD  
12  1 Y 1 A LYS 716 ? CE  ? A LYS 23  CE  
13  1 Y 1 A LYS 716 ? NZ  ? A LYS 23  NZ  
14  1 Y 1 A LYS 728 ? CG  ? A LYS 35  CG  
15  1 Y 1 A LYS 728 ? CD  ? A LYS 35  CD  
16  1 Y 1 A LYS 728 ? CE  ? A LYS 35  CE  
17  1 Y 1 A LYS 728 ? NZ  ? A LYS 35  NZ  
18  1 Y 1 A ILE 732 ? CD1 ? A ILE 39  CD1 
19  1 Y 1 A GLU 734 ? CD  ? A GLU 41  CD  
20  1 Y 1 A GLU 734 ? OE1 ? A GLU 41  OE1 
21  1 Y 1 A GLU 734 ? OE2 ? A GLU 41  OE2 
22  1 Y 1 A LYS 737 ? CG  ? A LYS 44  CG  
23  1 Y 1 A LYS 737 ? CD  ? A LYS 44  CD  
24  1 Y 1 A LYS 737 ? CE  ? A LYS 44  CE  
25  1 Y 1 A LYS 737 ? NZ  ? A LYS 44  NZ  
26  1 Y 1 A VAL 738 ? CG1 ? A VAL 45  CG1 
27  1 Y 1 A VAL 738 ? CG2 ? A VAL 45  CG2 
28  1 Y 1 A LYS 739 ? NZ  ? A LYS 46  NZ  
29  1 Y 1 A ARG 748 ? CG  ? A ARG 55  CG  
30  1 Y 1 A ARG 748 ? CD  ? A ARG 55  CD  
31  1 Y 1 A ARG 748 ? NE  ? A ARG 55  NE  
32  1 Y 1 A ARG 748 ? CZ  ? A ARG 55  CZ  
33  1 Y 1 A ARG 748 ? NH1 ? A ARG 55  NH1 
34  1 Y 1 A ARG 748 ? NH2 ? A ARG 55  NH2 
35  1 Y 1 A THR 751 ? OG1 ? A THR 58  OG1 
36  1 Y 1 A THR 751 ? CG2 ? A THR 58  CG2 
37  1 Y 1 A LYS 757 ? CD  ? A LYS 64  CD  
38  1 Y 1 A LYS 757 ? CE  ? A LYS 64  CE  
39  1 Y 1 A LYS 757 ? NZ  ? A LYS 64  NZ  
40  1 Y 1 A GLU 758 ? CG  ? A GLU 65  CG  
41  1 Y 1 A GLU 758 ? CD  ? A GLU 65  CD  
42  1 Y 1 A GLU 758 ? OE1 ? A GLU 65  OE1 
43  1 Y 1 A GLU 758 ? OE2 ? A GLU 65  OE2 
44  1 Y 1 A GLU 762 ? CD  ? A GLU 69  CD  
45  1 Y 1 A GLU 762 ? OE1 ? A GLU 69  OE1 
46  1 Y 1 A GLU 762 ? OE2 ? A GLU 69  OE2 
47  1 Y 1 A ASP 770 ? OD1 ? A ASP 77  OD1 
48  1 Y 1 A ASP 770 ? OD2 ? A ASP 77  OD2 
49  1 Y 1 A GLN 794 ? CG  ? A GLN 101 CG  
50  1 Y 1 A GLN 794 ? CD  ? A GLN 101 CD  
51  1 Y 1 A GLN 794 ? OE1 ? A GLN 101 OE1 
52  1 Y 1 A GLN 794 ? NE2 ? A GLN 101 NE2 
53  1 Y 1 A LYS 826 ? NZ  ? A LYS 133 NZ  
54  1 Y 1 A ARG 835 ? NE  ? A ARG 142 NE  
55  1 Y 1 A ARG 835 ? CZ  ? A ARG 142 CZ  
56  1 Y 1 A ARG 835 ? NH1 ? A ARG 142 NH1 
57  1 Y 1 A ARG 835 ? NH2 ? A ARG 142 NH2 
58  1 Y 1 A LYS 863 ? CE  ? A LYS 170 CE  
59  1 Y 1 A LYS 863 ? NZ  ? A LYS 170 NZ  
60  1 Y 1 A LYS 878 ? CG  ? A LYS 185 CG  
61  1 Y 1 A LYS 878 ? CD  ? A LYS 185 CD  
62  1 Y 1 A LYS 878 ? CE  ? A LYS 185 CE  
63  1 Y 1 A LYS 878 ? NZ  ? A LYS 185 NZ  
64  1 Y 1 A VAL 879 ? CG1 ? A VAL 186 CG1 
65  1 Y 1 A VAL 879 ? CG2 ? A VAL 186 CG2 
66  1 Y 1 A ILE 881 ? CD1 ? A ILE 188 CD1 
67  1 Y 1 A ARG 892 ? CD  ? A ARG 199 CD  
68  1 Y 1 A ARG 892 ? NE  ? A ARG 199 NE  
69  1 Y 1 A ARG 892 ? CZ  ? A ARG 199 CZ  
70  1 Y 1 A ARG 892 ? NH1 ? A ARG 199 NH1 
71  1 Y 1 A ARG 892 ? NH2 ? A ARG 199 NH2 
72  1 Y 1 A ILE 893 ? CD1 ? A ILE 200 CD1 
73  1 Y 1 A LYS 916 ? CE  ? A LYS 223 CE  
74  1 Y 1 A LYS 916 ? NZ  ? A LYS 223 NZ  
75  1 Y 1 A ILE 921 ? CD1 ? A ILE 228 CD1 
76  1 Y 1 A ILE 926 ? CD1 ? A ILE 233 CD1 
77  1 Y 1 A GLU 931 ? CG  ? A GLU 238 CG  
78  1 Y 1 A GLU 931 ? CD  ? A GLU 238 CD  
79  1 Y 1 A GLU 931 ? OE1 ? A GLU 238 OE1 
80  1 Y 1 A GLU 931 ? OE2 ? A GLU 238 OE2 
81  1 Y 1 A LYS 932 ? CE  ? A LYS 239 CE  
82  1 Y 1 A LYS 932 ? NZ  ? A LYS 239 NZ  
83  1 Y 1 A GLU 934 ? CG  ? A GLU 241 CG  
84  1 Y 1 A GLU 934 ? CD  ? A GLU 241 CD  
85  1 Y 1 A GLU 934 ? OE1 ? A GLU 241 OE1 
86  1 Y 1 A GLU 934 ? OE2 ? A GLU 241 OE2 
87  1 Y 1 A LYS 952 ? NZ  ? A LYS 259 NZ  
88  1 Y 1 A LYS 963 ? CE  ? A LYS 270 CE  
89  1 Y 1 A LYS 963 ? NZ  ? A LYS 270 NZ  
90  1 Y 1 A GLU 970 ? CD  ? A GLU 277 CD  
91  1 Y 1 A GLU 970 ? OE1 ? A GLU 277 OE1 
92  1 Y 1 A GLU 970 ? OE2 ? A GLU 277 OE2 
93  1 Y 1 A LYS 973 ? CD  ? A LYS 280 CD  
94  1 Y 1 A LYS 973 ? CE  ? A LYS 280 CE  
95  1 Y 1 A LYS 973 ? NZ  ? A LYS 280 NZ  
96  1 Y 1 A GLN 979 ? CD  ? A GLN 286 CD  
97  1 Y 1 A GLN 979 ? OE1 ? A GLN 286 OE1 
98  1 Y 1 A GLN 979 ? NE2 ? A GLN 286 NE2 
99  1 Y 1 A GLU 988 ? CG  ? A GLU 295 CG  
100 1 Y 1 A GLU 988 ? CD  ? A GLU 295 CD  
101 1 Y 1 A GLU 988 ? OE1 ? A GLU 295 OE1 
102 1 Y 1 A GLU 988 ? OE2 ? A GLU 295 OE2 
103 1 Y 1 B LEU 703 ? CG  ? B LEU 10  CG  
104 1 Y 1 B LEU 703 ? CD1 ? B LEU 10  CD1 
105 1 Y 1 B LEU 703 ? CD2 ? B LEU 10  CD2 
106 1 Y 1 B ILE 706 ? CD1 ? B ILE 13  CD1 
107 1 Y 1 B LYS 708 ? CD  ? B LYS 15  CD  
108 1 Y 1 B LYS 708 ? CE  ? B LYS 15  CE  
109 1 Y 1 B LYS 708 ? NZ  ? B LYS 15  NZ  
110 1 Y 1 B LYS 713 ? CG  ? B LYS 20  CG  
111 1 Y 1 B LYS 713 ? CD  ? B LYS 20  CD  
112 1 Y 1 B LYS 713 ? CE  ? B LYS 20  CE  
113 1 Y 1 B LYS 713 ? NZ  ? B LYS 20  NZ  
114 1 Y 1 B LYS 714 ? NZ  ? B LYS 21  NZ  
115 1 Y 1 B ILE 715 ? CD1 ? B ILE 22  CD1 
116 1 Y 1 B LYS 716 ? CD  ? B LYS 23  CD  
117 1 Y 1 B LYS 716 ? CE  ? B LYS 23  CE  
118 1 Y 1 B LYS 716 ? NZ  ? B LYS 23  NZ  
119 1 Y 1 B LYS 728 ? CD  ? B LYS 35  CD  
120 1 Y 1 B LYS 728 ? CE  ? B LYS 35  CE  
121 1 Y 1 B LYS 728 ? NZ  ? B LYS 35  NZ  
122 1 Y 1 B GLU 736 ? CG  ? B GLU 43  CG  
123 1 Y 1 B GLU 736 ? CD  ? B GLU 43  CD  
124 1 Y 1 B GLU 736 ? OE1 ? B GLU 43  OE1 
125 1 Y 1 B GLU 736 ? OE2 ? B GLU 43  OE2 
126 1 Y 1 B LYS 737 ? CG  ? B LYS 44  CG  
127 1 Y 1 B LYS 737 ? CD  ? B LYS 44  CD  
128 1 Y 1 B LYS 737 ? CE  ? B LYS 44  CE  
129 1 Y 1 B LYS 737 ? NZ  ? B LYS 44  NZ  
130 1 Y 1 B VAL 738 ? CG1 ? B VAL 45  CG1 
131 1 Y 1 B VAL 738 ? CG2 ? B VAL 45  CG2 
132 1 Y 1 B LYS 739 ? CD  ? B LYS 46  CD  
133 1 Y 1 B LYS 739 ? CE  ? B LYS 46  CE  
134 1 Y 1 B LYS 739 ? NZ  ? B LYS 46  NZ  
135 1 Y 1 B ILE 740 ? CD1 ? B ILE 47  CD1 
136 1 Y 1 B LYS 757 ? CD  ? B LYS 64  CD  
137 1 Y 1 B LYS 757 ? CE  ? B LYS 64  CE  
138 1 Y 1 B LYS 757 ? NZ  ? B LYS 64  NZ  
139 1 Y 1 B GLU 758 ? CG  ? B GLU 65  CG  
140 1 Y 1 B GLU 758 ? CD  ? B GLU 65  CD  
141 1 Y 1 B GLU 758 ? OE1 ? B GLU 65  OE1 
142 1 Y 1 B GLU 758 ? OE2 ? B GLU 65  OE2 
143 1 Y 1 B ILE 759 ? CD1 ? B ILE 66  CD1 
144 1 Y 1 B LEU 760 ? CD1 ? B LEU 67  CD1 
145 1 Y 1 B LEU 760 ? CD2 ? B LEU 67  CD2 
146 1 Y 1 B GLU 762 ? OE1 ? B GLU 69  OE1 
147 1 Y 1 B GLU 762 ? OE2 ? B GLU 69  OE2 
148 1 Y 1 B MET 766 ? CE  ? B MET 73  CE  
149 1 Y 1 B ASP 770 ? OD1 ? B ASP 77  OD1 
150 1 Y 1 B ASP 770 ? OD2 ? B ASP 77  OD2 
151 1 Y 1 B ILE 783 ? CD1 ? B ILE 90  CD1 
152 1 Y 1 B GLU 807 ? CG  ? B GLU 114 CG  
153 1 Y 1 B GLU 807 ? CD  ? B GLU 114 CD  
154 1 Y 1 B GLU 807 ? OE1 ? B GLU 114 OE1 
155 1 Y 1 B GLU 807 ? OE2 ? B GLU 114 OE2 
156 1 Y 1 B ARG 835 ? CD  ? B ARG 142 CD  
157 1 Y 1 B ARG 835 ? NE  ? B ARG 142 NE  
158 1 Y 1 B ARG 835 ? CZ  ? B ARG 142 CZ  
159 1 Y 1 B ARG 835 ? NH1 ? B ARG 142 NH1 
160 1 Y 1 B ARG 835 ? NH2 ? B ARG 142 NH2 
161 1 Y 1 B LYS 849 ? NZ  ? B LYS 156 NZ  
162 1 Y 1 B LYS 863 ? CE  ? B LYS 170 CE  
163 1 Y 1 B LYS 863 ? NZ  ? B LYS 170 NZ  
164 1 Y 1 B GLU 868 ? CG  ? B GLU 175 CG  
165 1 Y 1 B GLU 868 ? CD  ? B GLU 175 CD  
166 1 Y 1 B GLU 868 ? OE1 ? B GLU 175 OE1 
167 1 Y 1 B GLU 868 ? OE2 ? B GLU 175 OE2 
168 1 Y 1 B GLU 869 ? CG  ? B GLU 176 CG  
169 1 Y 1 B GLU 869 ? CD  ? B GLU 176 CD  
170 1 Y 1 B GLU 869 ? OE1 ? B GLU 176 OE1 
171 1 Y 1 B GLU 869 ? OE2 ? B GLU 176 OE2 
172 1 Y 1 B LYS 870 ? CG  ? B LYS 177 CG  
173 1 Y 1 B LYS 870 ? CD  ? B LYS 177 CD  
174 1 Y 1 B LYS 870 ? CE  ? B LYS 177 CE  
175 1 Y 1 B LYS 870 ? NZ  ? B LYS 177 NZ  
176 1 Y 1 B LYS 878 ? CG  ? B LYS 185 CG  
177 1 Y 1 B LYS 878 ? CD  ? B LYS 185 CD  
178 1 Y 1 B LYS 878 ? CE  ? B LYS 185 CE  
179 1 Y 1 B LYS 878 ? NZ  ? B LYS 185 NZ  
180 1 Y 1 B ILE 893 ? CD1 ? B ILE 200 CD1 
181 1 Y 1 B LYS 916 ? CE  ? B LYS 223 CE  
182 1 Y 1 B LYS 916 ? NZ  ? B LYS 223 NZ  
183 1 Y 1 B ILE 921 ? CD1 ? B ILE 228 CD1 
184 1 Y 1 B ILE 929 ? CD1 ? B ILE 236 CD1 
185 1 Y 1 B GLU 934 ? CD  ? B GLU 241 CD  
186 1 Y 1 B GLU 934 ? OE1 ? B GLU 241 OE1 
187 1 Y 1 B GLU 934 ? OE2 ? B GLU 241 OE2 
188 1 Y 1 B ILE 944 ? CD1 ? B ILE 251 CD1 
189 1 Y 1 B LYS 952 ? CD  ? B LYS 259 CD  
190 1 Y 1 B LYS 952 ? CE  ? B LYS 259 CE  
191 1 Y 1 B LYS 952 ? NZ  ? B LYS 259 NZ  
192 1 Y 1 B LYS 963 ? CE  ? B LYS 270 CE  
193 1 Y 1 B LYS 963 ? NZ  ? B LYS 270 NZ  
194 1 Y 1 B GLU 970 ? CD  ? B GLU 277 CD  
195 1 Y 1 B GLU 970 ? OE1 ? B GLU 277 OE1 
196 1 Y 1 B GLU 970 ? OE2 ? B GLU 277 OE2 
197 1 Y 1 B LYS 973 ? CE  ? B LYS 280 CE  
198 1 Y 1 B LYS 973 ? NZ  ? B LYS 280 NZ  
199 1 Y 1 B GLN 985 ? CG  ? B GLN 292 CG  
200 1 Y 1 B GLN 985 ? CD  ? B GLN 292 CD  
201 1 Y 1 B GLN 985 ? OE1 ? B GLN 292 OE1 
202 1 Y 1 B GLN 985 ? NE2 ? B GLN 292 NE2 
203 1 Y 1 B GLU 988 ? CG  ? B GLU 295 CG  
204 1 Y 1 B GLU 988 ? CD  ? B GLU 295 CD  
205 1 Y 1 B GLU 988 ? OE1 ? B GLU 295 OE1 
206 1 Y 1 B GLU 988 ? OE2 ? B GLU 295 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER  ? ? ? '2.11.8 (21-NOV-2022)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? 0.7.13                 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? 2.8.3                  4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   121.81 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HBO 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     139.393 
_cell.length_a_esd                 ? 
_cell.length_b                     86.284 
_cell.length_b_esd                 ? 
_cell.length_c                     98.062 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9HBO 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 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                   9HBO 
_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             2.45 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          63.18 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_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 15%w/v , PCPT 0.1M pH 6.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293.15 
# 
_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         2021-08-03 
_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   0.9999 
_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 I24' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9999 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I24 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9HBO 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.45 
_reflns.d_resolution_low                               69.74 
_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                                     35948 
_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                           98.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.94 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.163 
_reflns.pdbx_Rpim_I_all                                0.082 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       145374 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.991 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.140 
_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                                    2.45 
_reflns_shell.d_res_low                                     2.55 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           16549 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4062 
_reflns_shell.percent_possible_obs                          99.4 
_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                               4.1 
_reflns_shell.pdbx_chi_squared                              0.89 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.7 
_reflns_shell.pdbx_Rrim_I_all                               1.684 
_reflns_shell.pdbx_Rpim_I_all                               0.844 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.302 
_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                                  1.450 
_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]                            -17.24890 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -9.84230 
_refine.aniso_B[2][2]                            6.89770 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            10.35120 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               59.37 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.914 
_refine.correlation_coeff_Fo_to_Fc_free          0.891 
_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                                 9HBO 
_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                            2.450 
_refine.ls_d_res_low                             32.09 
_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                     35934 
_refine.ls_number_reflns_R_free                  1802 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.7 
_refine.ls_percent_reflns_R_free                 5.010 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2280 
_refine.ls_R_factor_R_free                       0.2545 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2266 
_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   0.220 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.214 
_refine.pdbx_overall_SU_R_Blow_DPI               0.266 
_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             0.275 
_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                        9HBO 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.36 
_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                       2.450 
_refine_hist.d_res_low                        32.09 
_refine_hist.number_atoms_solvent             120 
_refine_hist.number_atoms_total               4453 
_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        4263 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         70 
_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' ? 0.007 ? 4444 ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 0.87  ? 6058 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1478 ? 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' ? ?     ? 790  ? t_gen_planes              5.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 4444 ? t_it                      10.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 2.92  ? ?    ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 16.73 ? ?    ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 594  ? 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' ? ?     ? 3299 ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.45 
_refine_ls_shell.d_res_low                        2.47 
_refine_ls_shell.number_reflns_all                719 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             ? 
_refine_ls_shell.number_reflns_R_work             696 
_refine_ls_shell.percent_reflns_obs               98.76 
_refine_ls_shell.percent_reflns_R_free            3.20 
_refine_ls_shell.R_factor_all                     0.3384 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.3370 
_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   51 
_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                  0.3823 
# 
_struct.entry_id                     9HBO 
_struct.title                        
'Highly optimized CNS penetrant inhibitors of EGFR Exon20 Insertion Mutations. Compound 51 bound to EGFRinsNPG [V948R]' 
_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        9HBO 
_struct_keywords.text            'inhibitor, EGFR, kinase, 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 9HBO A 2 ? 332 ? P00533 695 ? 1022 ? 695 1025 
2 1 9HBO B 2 ? 332 ? P00533 695 ? 1022 ? 695 1025 
# 
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 9HBO GLY A 1   ? UNP P00533 ?   ?   'expression tag'      694 1  
1 9HBO GLY A 80  ? UNP P00533 ?   ?   insertion             773 2  
1 9HBO ASN A 81  ? UNP P00533 ?   ?   insertion             774 3  
1 9HBO PRO A 82  ? UNP P00533 ?   ?   insertion             775 4  
1 9HBO ARG A 258 ? UNP P00533 VAL 948 'engineered mutation' 951 5  
2 9HBO GLY B 1   ? UNP P00533 ?   ?   'expression tag'      694 6  
2 9HBO GLY B 80  ? UNP P00533 ?   ?   insertion             773 7  
2 9HBO ASN B 81  ? UNP P00533 ?   ?   insertion             774 8  
2 9HBO PRO B 82  ? UNP P00533 ?   ?   insertion             775 9  
2 9HBO ARG B 258 ? UNP P00533 VAL 948 'engineered mutation' 951 10 
# 
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   none 
_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 ALA A 62  ? VAL A 76  ? ALA A 755 VAL A 769 1 ? 15 
HELX_P HELX_P2  AA2 CYS A 107 ? LYS A 116 ? CYS A 800 LYS A 809 1 ? 10 
HELX_P HELX_P3  AA3 ASP A 117 ? ILE A 119 ? ASP A 810 ILE A 812 5 ? 3  
HELX_P HELX_P4  AA4 GLY A 120 ? ARG A 141 ? GLY A 813 ARG A 834 1 ? 22 
HELX_P HELX_P5  AA5 ALA A 149 ? ARG A 151 ? ALA A 842 ARG A 844 5 ? 3  
HELX_P HELX_P6  AA6 GLY A 167 ? GLY A 173 ? GLY A 860 GLY A 866 1 ? 7  
HELX_P HELX_P7  AA7 PRO A 187 ? MET A 191 ? PRO A 880 MET A 884 5 ? 5  
HELX_P HELX_P8  AA8 ALA A 192 ? ARG A 199 ? ALA A 885 ARG A 892 1 ? 8  
HELX_P HELX_P9  AA9 THR A 202 ? THR A 219 ? THR A 895 THR A 912 1 ? 18 
HELX_P HELX_P10 AB1 PRO A 229 ? SER A 231 ? PRO A 922 SER A 924 5 ? 3  
HELX_P HELX_P11 AB2 GLU A 232 ? LYS A 239 ? GLU A 925 LYS A 932 1 ? 8  
HELX_P HELX_P12 AB3 THR A 250 ? TRP A 261 ? THR A 943 TRP A 954 1 ? 12 
HELX_P HELX_P13 AB4 ASP A 264 ? ARG A 268 ? ASP A 957 ARG A 961 5 ? 5  
HELX_P HELX_P14 AB5 LYS A 270 ? ASP A 284 ? LYS A 963 ASP A 977 1 ? 15 
HELX_P HELX_P15 AB6 PRO A 285 ? TYR A 288 ? PRO A 978 TYR A 981 5 ? 4  
HELX_P HELX_P16 AB7 ALA B 62  ? VAL B 76  ? ALA B 755 VAL B 769 1 ? 15 
HELX_P HELX_P17 AB8 CYS B 107 ? HIS B 115 ? CYS B 800 HIS B 808 1 ? 9  
HELX_P HELX_P18 AB9 LYS B 116 ? ILE B 119 ? LYS B 809 ILE B 812 5 ? 4  
HELX_P HELX_P19 AC1 GLY B 120 ? ARG B 141 ? GLY B 813 ARG B 834 1 ? 22 
HELX_P HELX_P20 AC2 ALA B 149 ? ARG B 151 ? ALA B 842 ARG B 844 5 ? 3  
HELX_P HELX_P21 AC3 GLY B 167 ? LEU B 172 ? GLY B 860 LEU B 865 1 ? 6  
HELX_P HELX_P22 AC4 PRO B 187 ? MET B 191 ? PRO B 880 MET B 884 5 ? 5  
HELX_P HELX_P23 AC5 ALA B 192 ? ARG B 199 ? ALA B 885 ARG B 892 1 ? 8  
HELX_P HELX_P24 AC6 THR B 202 ? THR B 219 ? THR B 895 THR B 912 1 ? 18 
HELX_P HELX_P25 AC7 PRO B 229 ? SER B 231 ? PRO B 922 SER B 924 5 ? 3  
HELX_P HELX_P26 AC8 GLU B 232 ? LYS B 239 ? GLU B 925 LYS B 932 1 ? 8  
HELX_P HELX_P27 AC9 THR B 250 ? TRP B 261 ? THR B 943 TRP B 954 1 ? 12 
HELX_P HELX_P28 AD1 ASP B 264 ? ARG B 268 ? ASP B 957 ARG B 961 5 ? 5  
HELX_P HELX_P29 AD2 LYS B 270 ? ASP B 284 ? LYS B 963 ASP B 977 1 ? 15 
HELX_P HELX_P30 AD3 PRO B 285 ? TYR B 288 ? PRO B 978 TYR B 981 5 ? 4  
# 
_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 107 SG ? ? ? 1_555 C A1IUK . C22 ? ? A CYS 800 A A1IUK 1101 1_555 ? ? ? ? ? ? ? 1.660 ? ? 
covale2 covale none ? B CYS 107 SG ? ? ? 1_555 D A1IUK . C22 ? ? B CYS 800 B A1IUK 1101 1_555 ? ? ? ? ? ? ? 1.758 ? ? 
# 
_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 A1IUK C . ? CYS A 107 ? A1IUK A 1101 ? 1_555 CYS A 800 ? 1_555 C22 SG CYS 1 A1IUK None 'Covalent chemical modification' 
2 A1IUK D . ? CYS B 107 ? A1IUK B 1101 ? 1_555 CYS B 800 ? 1_555 C22 SG CYS 1 A1IUK None 'Covalent chemical modification' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ASN 78 A . ? ASN 771 A PRO 79 A ? PRO 772 A 1 0.04  
2 ASN 78 B . ? ASN 771 B PRO 79 B ? PRO 772 B 1 -0.23 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
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 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? 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 PHE A 19  ? SER A 27  ? PHE A 712 SER A 720 
AA1 2 GLY A 31  ? TRP A 38  ? GLY A 724 TRP A 731 
AA1 3 ILE A 47  ? LEU A 54  ? ILE A 740 LEU A 747 
AA1 4 VAL A 96  ? GLN A 101 ? VAL A 789 GLN A 794 
AA1 5 GLY A 89  ? LEU A 92  ? GLY A 782 LEU A 785 
AA2 1 VAL A 153 ? THR A 157 ? VAL A 846 THR A 850 
AA2 2 HIS A 160 ? ILE A 163 ? HIS A 853 ILE A 856 
AA3 1 ARG B 12  ? ILE B 13  ? ARG B 705 ILE B 706 
AA3 2 LEU B 87  ? LEU B 92  ? LEU B 780 LEU B 785 
AA3 3 VAL B 96  ? GLN B 101 ? VAL B 789 GLN B 794 
AA3 4 ILE B 47  ? LEU B 54  ? ILE B 740 LEU B 747 
AA3 5 GLY B 31  ? TRP B 38  ? GLY B 724 TRP B 731 
AA3 6 PHE B 19  ? SER B 27  ? PHE B 712 SER B 720 
AA4 1 VAL B 153 ? THR B 157 ? VAL B 846 THR B 850 
AA4 2 HIS B 160 ? ILE B 163 ? HIS B 853 ILE B 856 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 25  ? N LEU A 718 O VAL A 33  ? O VAL A 726 
AA1 2 3 N THR A 32  ? N THR A 725 O GLU A 53  ? O GLU A 746 
AA1 3 4 N LEU A 54  ? N LEU A 747 O VAL A 96  ? O VAL A 789 
AA1 4 5 O ILE A 99  ? O ILE A 792 N GLY A 89  ? N GLY A 782 
AA2 1 2 N LEU A 154 ? N LEU A 847 O LYS A 162 ? O LYS A 855 
AA3 1 2 N ARG B 12  ? N ARG B 705 O ILE B 90  ? O ILE B 783 
AA3 2 3 N GLY B 89  ? N GLY B 782 O ILE B 99  ? O ILE B 792 
AA3 3 4 O THR B 100 ? O THR B 793 N ALA B 50  ? N ALA B 743 
AA3 4 5 O VAL B 49  ? O VAL B 742 N GLY B 36  ? N GLY B 729 
AA3 5 6 O VAL B 33  ? O VAL B 726 N LEU B 25  ? N LEU B 718 
AA4 1 2 N LEU B 154 ? N LEU B 847 O LYS B 162 ? O LYS B 855 
# 
_pdbx_entry_details.entry_id                   9HBO 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_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 LYS A 737 ? ? -116.84 58.78   
2 1 THR A 786 ? ? -122.65 -134.29 
3 1 ARG A 839 ? ? 79.88   -14.14  
4 1 ASP A 840 ? ? -145.68 47.26   
5 1 GLU B 734 ? ? -10.89  -61.18  
6 1 THR B 786 ? ? -120.41 -137.51 
7 1 ARG B 839 ? ? 79.37   -12.83  
8 1 ASP B 840 ? ? -145.92 47.05   
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 20.4552 -26.6309 39.3743 -0.2033 ? 0.0529  ? -0.0559 ? -0.0716 ? 0.0489  ? -0.0702 ? 1.1212 ? 
-0.6323 ? -0.8703 ? 3.7827 ? 1.2536  ? 2.8403 ? -0.1705 ? -0.1091 ? -0.0836 ? 0.2361  ? 0.1483 ? 0.1668  ? -0.0013 ? -0.1721 ? 
0.0221  ? 
2 'X-RAY DIFFRACTION' ? refined 37.9617 -17.6757 11.2257 -0.0331 ? -0.0293 ? -0.0571 ? -0.0977 ? -0.0016 ? -0.0934 ? 1.0913 ? 
0.0455  ? -0.1910 ? 3.9495 ? -0.1611 ? 2.7889 ? 0.0077  ? 0.0872  ? 0.0028  ? -0.3095 ? 0.0072 ? -0.0908 ? -0.4187 ? 0.0567  ? 
-0.0149 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? '{ A|* }' 
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? '{ B|* }' 
# 
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 694  ? A GLY 1   
2   1 Y 1 A SER 695  ? A SER 2   
3   1 Y 1 A GLY 696  ? A GLY 3   
4   1 Y 1 A GLU 697  ? A GLU 4   
5   1 Y 1 A ALA 698  ? A ALA 5   
6   1 Y 1 A PRO 699  ? A PRO 6   
7   1 Y 1 A ASN 700  ? A ASN 7   
8   1 Y 1 A GLN 701  ? A GLN 8   
9   1 Y 1 A ALA 867  ? A ALA 174 
10  1 Y 1 A GLU 868  ? A GLU 175 
11  1 Y 1 A GLU 869  ? A GLU 176 
12  1 Y 1 A LYS 870  ? A LYS 177 
13  1 Y 1 A GLU 871  ? A GLU 178 
14  1 Y 1 A TYR 872  ? A TYR 179 
15  1 Y 1 A HIS 873  ? A HIS 180 
16  1 Y 1 A ALA 874  ? A ALA 181 
17  1 Y 1 A GLU 875  ? A GLU 182 
18  1 Y 1 A GLY 876  ? A GLY 183 
19  1 Y 1 A GLY 877  ? A GLY 184 
20  1 Y 1 A MET 990  ? A MET 297 
21  1 Y 1 A HIS 991  ? A HIS 298 
22  1 Y 1 A LEU 992  ? A LEU 299 
23  1 Y 1 A PRO 993  ? A PRO 300 
24  1 Y 1 A SER 994  ? A SER 301 
25  1 Y 1 A PRO 995  ? A PRO 302 
26  1 Y 1 A THR 996  ? A THR 303 
27  1 Y 1 A ASP 997  ? A ASP 304 
28  1 Y 1 A SER 998  ? A SER 305 
29  1 Y 1 A ASN 999  ? A ASN 306 
30  1 Y 1 A PHE 1000 ? A PHE 307 
31  1 Y 1 A TYR 1001 ? A TYR 308 
32  1 Y 1 A ARG 1002 ? A ARG 309 
33  1 Y 1 A ALA 1003 ? A ALA 310 
34  1 Y 1 A LEU 1004 ? A LEU 311 
35  1 Y 1 A MET 1005 ? A MET 312 
36  1 Y 1 A ASP 1006 ? A ASP 313 
37  1 Y 1 A GLU 1007 ? A GLU 314 
38  1 Y 1 A GLU 1008 ? A GLU 315 
39  1 Y 1 A ASP 1009 ? A ASP 316 
40  1 Y 1 A MET 1010 ? A MET 317 
41  1 Y 1 A ASP 1011 ? A ASP 318 
42  1 Y 1 A ASP 1012 ? A ASP 319 
43  1 Y 1 A VAL 1013 ? A VAL 320 
44  1 Y 1 A VAL 1014 ? A VAL 321 
45  1 Y 1 A ASP 1015 ? A ASP 322 
46  1 Y 1 A ALA 1016 ? A ALA 323 
47  1 Y 1 A ASP 1017 ? A ASP 324 
48  1 Y 1 A GLU 1018 ? A GLU 325 
49  1 Y 1 A TYR 1019 ? A TYR 326 
50  1 Y 1 A LEU 1020 ? A LEU 327 
51  1 Y 1 A ILE 1021 ? A ILE 328 
52  1 Y 1 A PRO 1022 ? A PRO 329 
53  1 Y 1 A GLN 1023 ? A GLN 330 
54  1 Y 1 A GLN 1024 ? A GLN 331 
55  1 Y 1 A GLY 1025 ? A GLY 332 
56  1 Y 1 B GLY 694  ? B GLY 1   
57  1 Y 1 B SER 695  ? B SER 2   
58  1 Y 1 B GLY 696  ? B GLY 3   
59  1 Y 1 B GLU 697  ? B GLU 4   
60  1 Y 1 B ALA 698  ? B ALA 5   
61  1 Y 1 B PRO 699  ? B PRO 6   
62  1 Y 1 B ASN 700  ? B ASN 7   
63  1 Y 1 B GLN 701  ? B GLN 8   
64  1 Y 1 B GLU 871  ? B GLU 178 
65  1 Y 1 B TYR 872  ? B TYR 179 
66  1 Y 1 B HIS 873  ? B HIS 180 
67  1 Y 1 B ALA 874  ? B ALA 181 
68  1 Y 1 B GLU 875  ? B GLU 182 
69  1 Y 1 B GLY 876  ? B GLY 183 
70  1 Y 1 B ARG 989  ? B ARG 296 
71  1 Y 1 B MET 990  ? B MET 297 
72  1 Y 1 B HIS 991  ? B HIS 298 
73  1 Y 1 B LEU 992  ? B LEU 299 
74  1 Y 1 B PRO 993  ? B PRO 300 
75  1 Y 1 B SER 994  ? B SER 301 
76  1 Y 1 B PRO 995  ? B PRO 302 
77  1 Y 1 B THR 996  ? B THR 303 
78  1 Y 1 B ASP 997  ? B ASP 304 
79  1 Y 1 B SER 998  ? B SER 305 
80  1 Y 1 B ASN 999  ? B ASN 306 
81  1 Y 1 B PHE 1000 ? B PHE 307 
82  1 Y 1 B TYR 1001 ? B TYR 308 
83  1 Y 1 B ARG 1002 ? B ARG 309 
84  1 Y 1 B ALA 1003 ? B ALA 310 
85  1 Y 1 B LEU 1004 ? B LEU 311 
86  1 Y 1 B MET 1005 ? B MET 312 
87  1 Y 1 B ASP 1006 ? B ASP 313 
88  1 Y 1 B GLU 1007 ? B GLU 314 
89  1 Y 1 B GLU 1008 ? B GLU 315 
90  1 Y 1 B ASP 1009 ? B ASP 316 
91  1 Y 1 B MET 1010 ? B MET 317 
92  1 Y 1 B ASP 1011 ? B ASP 318 
93  1 Y 1 B ASP 1012 ? B ASP 319 
94  1 Y 1 B VAL 1013 ? B VAL 320 
95  1 Y 1 B VAL 1014 ? B VAL 321 
96  1 Y 1 B ASP 1015 ? B ASP 322 
97  1 Y 1 B ALA 1016 ? B ALA 323 
98  1 Y 1 B ASP 1017 ? B ASP 324 
99  1 Y 1 B GLU 1018 ? B GLU 325 
100 1 Y 1 B TYR 1019 ? B TYR 326 
101 1 Y 1 B LEU 1020 ? B LEU 327 
102 1 Y 1 B ILE 1021 ? B ILE 328 
103 1 Y 1 B PRO 1022 ? B PRO 329 
104 1 Y 1 B GLN 1023 ? B GLN 330 
105 1 Y 1 B GLN 1024 ? B GLN 331 
106 1 Y 1 B GLY 1025 ? B GLY 332 
# 
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 
A1IUK C3   C Y N 1   
A1IUK C4   C N N 2   
A1IUK C5   C Y N 3   
A1IUK C6   C Y N 4   
A1IUK C7   C Y N 5   
A1IUK C8   C Y N 6   
A1IUK C9   C Y N 7   
A1IUK C10  C Y N 8   
A1IUK C11  C Y N 9   
A1IUK C12  C Y N 10  
A1IUK O    O N N 11  
A1IUK N1   N Y N 12  
A1IUK C20  C N N 13  
A1IUK C21  C N N 14  
A1IUK C22  C N N 15  
A1IUK N3   N N N 16  
A1IUK C13  C N N 17  
A1IUK C14  C N N 18  
A1IUK C15  C Y N 19  
A1IUK N2   N Y N 20  
A1IUK N4   N Y N 21  
A1IUK C16  C Y N 22  
A1IUK N6   N Y N 23  
A1IUK C19  C Y N 24  
A1IUK N5   N Y N 25  
A1IUK C18  C Y N 26  
A1IUK C17  C Y N 27  
A1IUK F2   F N N 28  
A1IUK F3   F N N 29  
A1IUK C2   C Y N 30  
A1IUK N    N Y N 31  
A1IUK F1   F N N 32  
A1IUK F    F N N 33  
A1IUK C1   C Y N 34  
A1IUK C    C N N 35  
A1IUK H1   H N N 36  
A1IUK H2   H N N 37  
A1IUK H3   H N N 38  
A1IUK H4   H N N 39  
A1IUK H5   H N N 40  
A1IUK H6   H N N 41  
A1IUK H7   H N N 42  
A1IUK H8   H N N 43  
A1IUK H9   H N N 44  
A1IUK H10  H N N 45  
A1IUK H11  H N N 46  
A1IUK H12  H N N 47  
A1IUK H13  H N N 48  
A1IUK H14  H N N 49  
A1IUK H15  H N N 50  
A1IUK H16  H N N 51  
A1IUK H17  H N N 52  
A1IUK H18  H N N 53  
A1IUK H19  H N N 54  
ALA   N    N N N 55  
ALA   CA   C N S 56  
ALA   C    C N N 57  
ALA   O    O N N 58  
ALA   CB   C N N 59  
ALA   OXT  O N N 60  
ALA   H    H N N 61  
ALA   H2   H N N 62  
ALA   HA   H N N 63  
ALA   HB1  H N N 64  
ALA   HB2  H N N 65  
ALA   HB3  H N N 66  
ALA   HXT  H N N 67  
ARG   N    N N N 68  
ARG   CA   C N S 69  
ARG   C    C N N 70  
ARG   O    O N N 71  
ARG   CB   C N N 72  
ARG   CG   C N N 73  
ARG   CD   C N N 74  
ARG   NE   N N N 75  
ARG   CZ   C N N 76  
ARG   NH1  N N N 77  
ARG   NH2  N N N 78  
ARG   OXT  O N N 79  
ARG   H    H N N 80  
ARG   H2   H N N 81  
ARG   HA   H N N 82  
ARG   HB2  H N N 83  
ARG   HB3  H N N 84  
ARG   HG2  H N N 85  
ARG   HG3  H N N 86  
ARG   HD2  H N N 87  
ARG   HD3  H N N 88  
ARG   HE   H N N 89  
ARG   HH11 H N N 90  
ARG   HH12 H N N 91  
ARG   HH21 H N N 92  
ARG   HH22 H N N 93  
ARG   HXT  H N N 94  
ASN   N    N N N 95  
ASN   CA   C N S 96  
ASN   C    C N N 97  
ASN   O    O N N 98  
ASN   CB   C N N 99  
ASN   CG   C N N 100 
ASN   OD1  O N N 101 
ASN   ND2  N N N 102 
ASN   OXT  O N N 103 
ASN   H    H N N 104 
ASN   H2   H N N 105 
ASN   HA   H N N 106 
ASN   HB2  H N N 107 
ASN   HB3  H N N 108 
ASN   HD21 H N N 109 
ASN   HD22 H N N 110 
ASN   HXT  H N N 111 
ASP   N    N N N 112 
ASP   CA   C N S 113 
ASP   C    C N N 114 
ASP   O    O N N 115 
ASP   CB   C N N 116 
ASP   CG   C N N 117 
ASP   OD1  O N N 118 
ASP   OD2  O N N 119 
ASP   OXT  O N N 120 
ASP   H    H N N 121 
ASP   H2   H N N 122 
ASP   HA   H N N 123 
ASP   HB2  H N N 124 
ASP   HB3  H N N 125 
ASP   HD2  H N N 126 
ASP   HXT  H N N 127 
CYS   N    N N N 128 
CYS   CA   C N R 129 
CYS   C    C N N 130 
CYS   O    O N N 131 
CYS   CB   C N N 132 
CYS   SG   S N N 133 
CYS   OXT  O N N 134 
CYS   H    H N N 135 
CYS   H2   H N N 136 
CYS   HA   H N N 137 
CYS   HB2  H N N 138 
CYS   HB3  H N N 139 
CYS   HG   H N N 140 
CYS   HXT  H N N 141 
GLN   N    N N N 142 
GLN   CA   C N S 143 
GLN   C    C N N 144 
GLN   O    O N N 145 
GLN   CB   C N N 146 
GLN   CG   C N N 147 
GLN   CD   C N N 148 
GLN   OE1  O N N 149 
GLN   NE2  N N N 150 
GLN   OXT  O N N 151 
GLN   H    H N N 152 
GLN   H2   H N N 153 
GLN   HA   H N N 154 
GLN   HB2  H N N 155 
GLN   HB3  H N N 156 
GLN   HG2  H N N 157 
GLN   HG3  H N N 158 
GLN   HE21 H N N 159 
GLN   HE22 H N N 160 
GLN   HXT  H N N 161 
GLU   N    N N N 162 
GLU   CA   C N S 163 
GLU   C    C N N 164 
GLU   O    O N N 165 
GLU   CB   C N N 166 
GLU   CG   C N N 167 
GLU   CD   C N N 168 
GLU   OE1  O N N 169 
GLU   OE2  O N N 170 
GLU   OXT  O N N 171 
GLU   H    H N N 172 
GLU   H2   H N N 173 
GLU   HA   H N N 174 
GLU   HB2  H N N 175 
GLU   HB3  H N N 176 
GLU   HG2  H N N 177 
GLU   HG3  H N N 178 
GLU   HE2  H N N 179 
GLU   HXT  H N N 180 
GLY   N    N N N 181 
GLY   CA   C N N 182 
GLY   C    C N N 183 
GLY   O    O N N 184 
GLY   OXT  O N N 185 
GLY   H    H N N 186 
GLY   H2   H N N 187 
GLY   HA2  H N N 188 
GLY   HA3  H N N 189 
GLY   HXT  H N N 190 
HIS   N    N N N 191 
HIS   CA   C N S 192 
HIS   C    C N N 193 
HIS   O    O N N 194 
HIS   CB   C N N 195 
HIS   CG   C Y N 196 
HIS   ND1  N Y N 197 
HIS   CD2  C Y N 198 
HIS   CE1  C Y N 199 
HIS   NE2  N Y N 200 
HIS   OXT  O N N 201 
HIS   H    H N N 202 
HIS   H2   H N N 203 
HIS   HA   H N N 204 
HIS   HB2  H N N 205 
HIS   HB3  H N N 206 
HIS   HD1  H N N 207 
HIS   HD2  H N N 208 
HIS   HE1  H N N 209 
HIS   HE2  H N N 210 
HIS   HXT  H N N 211 
HOH   O    O N N 212 
HOH   H1   H N N 213 
HOH   H2   H N N 214 
ILE   N    N N N 215 
ILE   CA   C N S 216 
ILE   C    C N N 217 
ILE   O    O N N 218 
ILE   CB   C N S 219 
ILE   CG1  C N N 220 
ILE   CG2  C N N 221 
ILE   CD1  C N N 222 
ILE   OXT  O N N 223 
ILE   H    H N N 224 
ILE   H2   H N N 225 
ILE   HA   H N N 226 
ILE   HB   H N N 227 
ILE   HG12 H N N 228 
ILE   HG13 H N N 229 
ILE   HG21 H N N 230 
ILE   HG22 H N N 231 
ILE   HG23 H N N 232 
ILE   HD11 H N N 233 
ILE   HD12 H N N 234 
ILE   HD13 H N N 235 
ILE   HXT  H N N 236 
LEU   N    N N N 237 
LEU   CA   C N S 238 
LEU   C    C N N 239 
LEU   O    O N N 240 
LEU   CB   C N N 241 
LEU   CG   C N N 242 
LEU   CD1  C N N 243 
LEU   CD2  C N N 244 
LEU   OXT  O N N 245 
LEU   H    H N N 246 
LEU   H2   H N N 247 
LEU   HA   H N N 248 
LEU   HB2  H N N 249 
LEU   HB3  H N N 250 
LEU   HG   H N N 251 
LEU   HD11 H N N 252 
LEU   HD12 H N N 253 
LEU   HD13 H N N 254 
LEU   HD21 H N N 255 
LEU   HD22 H N N 256 
LEU   HD23 H N N 257 
LEU   HXT  H N N 258 
LYS   N    N N N 259 
LYS   CA   C N S 260 
LYS   C    C N N 261 
LYS   O    O N N 262 
LYS   CB   C N N 263 
LYS   CG   C N N 264 
LYS   CD   C N N 265 
LYS   CE   C N N 266 
LYS   NZ   N N N 267 
LYS   OXT  O N N 268 
LYS   H    H N N 269 
LYS   H2   H N N 270 
LYS   HA   H N N 271 
LYS   HB2  H N N 272 
LYS   HB3  H N N 273 
LYS   HG2  H N N 274 
LYS   HG3  H N N 275 
LYS   HD2  H N N 276 
LYS   HD3  H N N 277 
LYS   HE2  H N N 278 
LYS   HE3  H N N 279 
LYS   HZ1  H N N 280 
LYS   HZ2  H N N 281 
LYS   HZ3  H N N 282 
LYS   HXT  H N N 283 
MET   N    N N N 284 
MET   CA   C N S 285 
MET   C    C N N 286 
MET   O    O N N 287 
MET   CB   C N N 288 
MET   CG   C N N 289 
MET   SD   S N N 290 
MET   CE   C N N 291 
MET   OXT  O N N 292 
MET   H    H N N 293 
MET   H2   H N N 294 
MET   HA   H N N 295 
MET   HB2  H N N 296 
MET   HB3  H N N 297 
MET   HG2  H N N 298 
MET   HG3  H N N 299 
MET   HE1  H N N 300 
MET   HE2  H N N 301 
MET   HE3  H N N 302 
MET   HXT  H N N 303 
PHE   N    N N N 304 
PHE   CA   C N S 305 
PHE   C    C N N 306 
PHE   O    O N N 307 
PHE   CB   C N N 308 
PHE   CG   C Y N 309 
PHE   CD1  C Y N 310 
PHE   CD2  C Y N 311 
PHE   CE1  C Y N 312 
PHE   CE2  C Y N 313 
PHE   CZ   C Y N 314 
PHE   OXT  O N N 315 
PHE   H    H N N 316 
PHE   H2   H N N 317 
PHE   HA   H N N 318 
PHE   HB2  H N N 319 
PHE   HB3  H N N 320 
PHE   HD1  H N N 321 
PHE   HD2  H N N 322 
PHE   HE1  H N N 323 
PHE   HE2  H N N 324 
PHE   HZ   H N N 325 
PHE   HXT  H N N 326 
PRO   N    N N N 327 
PRO   CA   C N S 328 
PRO   C    C N N 329 
PRO   O    O N N 330 
PRO   CB   C N N 331 
PRO   CG   C N N 332 
PRO   CD   C N N 333 
PRO   OXT  O N N 334 
PRO   H    H N N 335 
PRO   HA   H N N 336 
PRO   HB2  H N N 337 
PRO   HB3  H N N 338 
PRO   HG2  H N N 339 
PRO   HG3  H N N 340 
PRO   HD2  H N N 341 
PRO   HD3  H N N 342 
PRO   HXT  H N N 343 
SER   N    N N N 344 
SER   CA   C N S 345 
SER   C    C N N 346 
SER   O    O N N 347 
SER   CB   C N N 348 
SER   OG   O N N 349 
SER   OXT  O N N 350 
SER   H    H N N 351 
SER   H2   H N N 352 
SER   HA   H N N 353 
SER   HB2  H N N 354 
SER   HB3  H N N 355 
SER   HG   H N N 356 
SER   HXT  H N N 357 
THR   N    N N N 358 
THR   CA   C N S 359 
THR   C    C N N 360 
THR   O    O N N 361 
THR   CB   C N R 362 
THR   OG1  O N N 363 
THR   CG2  C N N 364 
THR   OXT  O N N 365 
THR   H    H N N 366 
THR   H2   H N N 367 
THR   HA   H N N 368 
THR   HB   H N N 369 
THR   HG1  H N N 370 
THR   HG21 H N N 371 
THR   HG22 H N N 372 
THR   HG23 H N N 373 
THR   HXT  H N N 374 
TRP   N    N N N 375 
TRP   CA   C N S 376 
TRP   C    C N N 377 
TRP   O    O N N 378 
TRP   CB   C N N 379 
TRP   CG   C Y N 380 
TRP   CD1  C Y N 381 
TRP   CD2  C Y N 382 
TRP   NE1  N Y N 383 
TRP   CE2  C Y N 384 
TRP   CE3  C Y N 385 
TRP   CZ2  C Y N 386 
TRP   CZ3  C Y N 387 
TRP   CH2  C Y N 388 
TRP   OXT  O N N 389 
TRP   H    H N N 390 
TRP   H2   H N N 391 
TRP   HA   H N N 392 
TRP   HB2  H N N 393 
TRP   HB3  H N N 394 
TRP   HD1  H N N 395 
TRP   HE1  H N N 396 
TRP   HE3  H N N 397 
TRP   HZ2  H N N 398 
TRP   HZ3  H N N 399 
TRP   HH2  H N N 400 
TRP   HXT  H N N 401 
TYR   N    N N N 402 
TYR   CA   C N S 403 
TYR   C    C N N 404 
TYR   O    O N N 405 
TYR   CB   C N N 406 
TYR   CG   C Y N 407 
TYR   CD1  C Y N 408 
TYR   CD2  C Y N 409 
TYR   CE1  C Y N 410 
TYR   CE2  C Y N 411 
TYR   CZ   C Y N 412 
TYR   OH   O N N 413 
TYR   OXT  O N N 414 
TYR   H    H N N 415 
TYR   H2   H N N 416 
TYR   HA   H N N 417 
TYR   HB2  H N N 418 
TYR   HB3  H N N 419 
TYR   HD1  H N N 420 
TYR   HD2  H N N 421 
TYR   HE1  H N N 422 
TYR   HE2  H N N 423 
TYR   HH   H N N 424 
TYR   HXT  H N N 425 
VAL   N    N N N 426 
VAL   CA   C N S 427 
VAL   C    C N N 428 
VAL   O    O N N 429 
VAL   CB   C N N 430 
VAL   CG1  C N N 431 
VAL   CG2  C N N 432 
VAL   OXT  O N N 433 
VAL   H    H N N 434 
VAL   H2   H N N 435 
VAL   HA   H N N 436 
VAL   HB   H N N 437 
VAL   HG11 H N N 438 
VAL   HG12 H N N 439 
VAL   HG13 H N N 440 
VAL   HG21 H N N 441 
VAL   HG22 H N N 442 
VAL   HG23 H N N 443 
VAL   HXT  H N N 444 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1IUK F1  C4   sing N N 1   
A1IUK C4  F    sing N N 2   
A1IUK C4  N1   sing N N 3   
A1IUK N1  C1   sing Y N 4   
A1IUK N1  N    sing Y N 5   
A1IUK C   C1   sing N N 6   
A1IUK C1  C2   doub Y N 7   
A1IUK N   C3   doub Y N 8   
A1IUK F3  C10  sing N N 9   
A1IUK C2  C3   sing Y N 10  
A1IUK C2  C5   sing N N 11  
A1IUK C10 C5   doub Y N 12  
A1IUK C10 C9   sing Y N 13  
A1IUK C5  C6   sing Y N 14  
A1IUK C9  C8   doub Y N 15  
A1IUK C6  C7   doub Y N 16  
A1IUK C8  C7   sing Y N 17  
A1IUK C8  F2   sing N N 18  
A1IUK C7  C11  sing N N 19  
A1IUK C19 N6   doub Y N 20  
A1IUK C19 N5   sing Y N 21  
A1IUK N6  C16  sing Y N 22  
A1IUK N5  C18  doub Y N 23  
A1IUK C11 N4   sing Y N 24  
A1IUK C11 N2   doub Y N 25  
A1IUK C16 N4   sing N N 26  
A1IUK C16 C17  doub Y N 27  
A1IUK C18 C17  sing Y N 28  
A1IUK N4  C15  sing Y N 29  
A1IUK N2  C12  sing Y N 30  
A1IUK C12 C15  doub Y N 31  
A1IUK C12 C13  sing N N 32  
A1IUK C15 C14  sing N N 33  
A1IUK C13 N3   sing N N 34  
A1IUK C14 N3   sing N N 35  
A1IUK N3  C20  sing N N 36  
A1IUK C20 O    doub N N 37  
A1IUK C20 C21  sing N N 38  
A1IUK C21 C22  sing N N 39  
A1IUK C3  H1   sing N N 40  
A1IUK C4  H2   sing N N 41  
A1IUK C6  H3   sing N N 42  
A1IUK C9  H4   sing N N 43  
A1IUK C21 H5   sing N N 44  
A1IUK C21 H6   sing N N 45  
A1IUK C22 H7   sing N N 46  
A1IUK C22 H8   sing N N 47  
A1IUK C22 H9   sing N N 48  
A1IUK C13 H10  sing N N 49  
A1IUK C13 H11  sing N N 50  
A1IUK C14 H12  sing N N 51  
A1IUK C14 H13  sing N N 52  
A1IUK C19 H14  sing N N 53  
A1IUK C18 H15  sing N N 54  
A1IUK C17 H16  sing N N 55  
A1IUK C   H17  sing N N 56  
A1IUK C   H18  sing N N 57  
A1IUK C   H19  sing N N 58  
ALA   N   CA   sing N N 59  
ALA   N   H    sing N N 60  
ALA   N   H2   sing N N 61  
ALA   CA  C    sing N N 62  
ALA   CA  CB   sing N N 63  
ALA   CA  HA   sing N N 64  
ALA   C   O    doub N N 65  
ALA   C   OXT  sing N N 66  
ALA   CB  HB1  sing N N 67  
ALA   CB  HB2  sing N N 68  
ALA   CB  HB3  sing N N 69  
ALA   OXT HXT  sing N N 70  
ARG   N   CA   sing N N 71  
ARG   N   H    sing N N 72  
ARG   N   H2   sing N N 73  
ARG   CA  C    sing N N 74  
ARG   CA  CB   sing N N 75  
ARG   CA  HA   sing N N 76  
ARG   C   O    doub N N 77  
ARG   C   OXT  sing N N 78  
ARG   CB  CG   sing N N 79  
ARG   CB  HB2  sing N N 80  
ARG   CB  HB3  sing N N 81  
ARG   CG  CD   sing N N 82  
ARG   CG  HG2  sing N N 83  
ARG   CG  HG3  sing N N 84  
ARG   CD  NE   sing N N 85  
ARG   CD  HD2  sing N N 86  
ARG   CD  HD3  sing N N 87  
ARG   NE  CZ   sing N N 88  
ARG   NE  HE   sing N N 89  
ARG   CZ  NH1  sing N N 90  
ARG   CZ  NH2  doub N N 91  
ARG   NH1 HH11 sing N N 92  
ARG   NH1 HH12 sing N N 93  
ARG   NH2 HH21 sing N N 94  
ARG   NH2 HH22 sing N N 95  
ARG   OXT HXT  sing N N 96  
ASN   N   CA   sing N N 97  
ASN   N   H    sing N N 98  
ASN   N   H2   sing N N 99  
ASN   CA  C    sing N N 100 
ASN   CA  CB   sing N N 101 
ASN   CA  HA   sing N N 102 
ASN   C   O    doub N N 103 
ASN   C   OXT  sing N N 104 
ASN   CB  CG   sing N N 105 
ASN   CB  HB2  sing N N 106 
ASN   CB  HB3  sing N N 107 
ASN   CG  OD1  doub N N 108 
ASN   CG  ND2  sing N N 109 
ASN   ND2 HD21 sing N N 110 
ASN   ND2 HD22 sing N N 111 
ASN   OXT HXT  sing N N 112 
ASP   N   CA   sing N N 113 
ASP   N   H    sing N N 114 
ASP   N   H2   sing N N 115 
ASP   CA  C    sing N N 116 
ASP   CA  CB   sing N N 117 
ASP   CA  HA   sing N N 118 
ASP   C   O    doub N N 119 
ASP   C   OXT  sing N N 120 
ASP   CB  CG   sing N N 121 
ASP   CB  HB2  sing N N 122 
ASP   CB  HB3  sing N N 123 
ASP   CG  OD1  doub N N 124 
ASP   CG  OD2  sing N N 125 
ASP   OD2 HD2  sing N N 126 
ASP   OXT HXT  sing N N 127 
CYS   N   CA   sing N N 128 
CYS   N   H    sing N N 129 
CYS   N   H2   sing N N 130 
CYS   CA  C    sing N N 131 
CYS   CA  CB   sing N N 132 
CYS   CA  HA   sing N N 133 
CYS   C   O    doub N N 134 
CYS   C   OXT  sing N N 135 
CYS   CB  SG   sing N N 136 
CYS   CB  HB2  sing N N 137 
CYS   CB  HB3  sing N N 138 
CYS   SG  HG   sing N N 139 
CYS   OXT HXT  sing N N 140 
GLN   N   CA   sing N N 141 
GLN   N   H    sing N N 142 
GLN   N   H2   sing N N 143 
GLN   CA  C    sing N N 144 
GLN   CA  CB   sing N N 145 
GLN   CA  HA   sing N N 146 
GLN   C   O    doub N N 147 
GLN   C   OXT  sing N N 148 
GLN   CB  CG   sing N N 149 
GLN   CB  HB2  sing N N 150 
GLN   CB  HB3  sing N N 151 
GLN   CG  CD   sing N N 152 
GLN   CG  HG2  sing N N 153 
GLN   CG  HG3  sing N N 154 
GLN   CD  OE1  doub N N 155 
GLN   CD  NE2  sing N N 156 
GLN   NE2 HE21 sing N N 157 
GLN   NE2 HE22 sing N N 158 
GLN   OXT HXT  sing N N 159 
GLU   N   CA   sing N N 160 
GLU   N   H    sing N N 161 
GLU   N   H2   sing N N 162 
GLU   CA  C    sing N N 163 
GLU   CA  CB   sing N N 164 
GLU   CA  HA   sing N N 165 
GLU   C   O    doub N N 166 
GLU   C   OXT  sing N N 167 
GLU   CB  CG   sing N N 168 
GLU   CB  HB2  sing N N 169 
GLU   CB  HB3  sing N N 170 
GLU   CG  CD   sing N N 171 
GLU   CG  HG2  sing N N 172 
GLU   CG  HG3  sing N N 173 
GLU   CD  OE1  doub N N 174 
GLU   CD  OE2  sing N N 175 
GLU   OE2 HE2  sing N N 176 
GLU   OXT HXT  sing N N 177 
GLY   N   CA   sing N N 178 
GLY   N   H    sing N N 179 
GLY   N   H2   sing N N 180 
GLY   CA  C    sing N N 181 
GLY   CA  HA2  sing N N 182 
GLY   CA  HA3  sing N N 183 
GLY   C   O    doub N N 184 
GLY   C   OXT  sing N N 185 
GLY   OXT HXT  sing N N 186 
HIS   N   CA   sing N N 187 
HIS   N   H    sing N N 188 
HIS   N   H2   sing N N 189 
HIS   CA  C    sing N N 190 
HIS   CA  CB   sing N N 191 
HIS   CA  HA   sing N N 192 
HIS   C   O    doub N N 193 
HIS   C   OXT  sing N N 194 
HIS   CB  CG   sing N N 195 
HIS   CB  HB2  sing N N 196 
HIS   CB  HB3  sing N N 197 
HIS   CG  ND1  sing Y N 198 
HIS   CG  CD2  doub Y N 199 
HIS   ND1 CE1  doub Y N 200 
HIS   ND1 HD1  sing N N 201 
HIS   CD2 NE2  sing Y N 202 
HIS   CD2 HD2  sing N N 203 
HIS   CE1 NE2  sing Y N 204 
HIS   CE1 HE1  sing N N 205 
HIS   NE2 HE2  sing N N 206 
HIS   OXT HXT  sing N N 207 
HOH   O   H1   sing N N 208 
HOH   O   H2   sing N N 209 
ILE   N   CA   sing N N 210 
ILE   N   H    sing N N 211 
ILE   N   H2   sing N N 212 
ILE   CA  C    sing N N 213 
ILE   CA  CB   sing N N 214 
ILE   CA  HA   sing N N 215 
ILE   C   O    doub N N 216 
ILE   C   OXT  sing N N 217 
ILE   CB  CG1  sing N N 218 
ILE   CB  CG2  sing N N 219 
ILE   CB  HB   sing N N 220 
ILE   CG1 CD1  sing N N 221 
ILE   CG1 HG12 sing N N 222 
ILE   CG1 HG13 sing N N 223 
ILE   CG2 HG21 sing N N 224 
ILE   CG2 HG22 sing N N 225 
ILE   CG2 HG23 sing N N 226 
ILE   CD1 HD11 sing N N 227 
ILE   CD1 HD12 sing N N 228 
ILE   CD1 HD13 sing N N 229 
ILE   OXT HXT  sing N N 230 
LEU   N   CA   sing N N 231 
LEU   N   H    sing N N 232 
LEU   N   H2   sing N N 233 
LEU   CA  C    sing N N 234 
LEU   CA  CB   sing N N 235 
LEU   CA  HA   sing N N 236 
LEU   C   O    doub N N 237 
LEU   C   OXT  sing N N 238 
LEU   CB  CG   sing N N 239 
LEU   CB  HB2  sing N N 240 
LEU   CB  HB3  sing N N 241 
LEU   CG  CD1  sing N N 242 
LEU   CG  CD2  sing N N 243 
LEU   CG  HG   sing N N 244 
LEU   CD1 HD11 sing N N 245 
LEU   CD1 HD12 sing N N 246 
LEU   CD1 HD13 sing N N 247 
LEU   CD2 HD21 sing N N 248 
LEU   CD2 HD22 sing N N 249 
LEU   CD2 HD23 sing N N 250 
LEU   OXT HXT  sing N N 251 
LYS   N   CA   sing N N 252 
LYS   N   H    sing N N 253 
LYS   N   H2   sing N N 254 
LYS   CA  C    sing N N 255 
LYS   CA  CB   sing N N 256 
LYS   CA  HA   sing N N 257 
LYS   C   O    doub N N 258 
LYS   C   OXT  sing N N 259 
LYS   CB  CG   sing N N 260 
LYS   CB  HB2  sing N N 261 
LYS   CB  HB3  sing N N 262 
LYS   CG  CD   sing N N 263 
LYS   CG  HG2  sing N N 264 
LYS   CG  HG3  sing N N 265 
LYS   CD  CE   sing N N 266 
LYS   CD  HD2  sing N N 267 
LYS   CD  HD3  sing N N 268 
LYS   CE  NZ   sing N N 269 
LYS   CE  HE2  sing N N 270 
LYS   CE  HE3  sing N N 271 
LYS   NZ  HZ1  sing N N 272 
LYS   NZ  HZ2  sing N N 273 
LYS   NZ  HZ3  sing N N 274 
LYS   OXT HXT  sing N N 275 
MET   N   CA   sing N N 276 
MET   N   H    sing N N 277 
MET   N   H2   sing N N 278 
MET   CA  C    sing N N 279 
MET   CA  CB   sing N N 280 
MET   CA  HA   sing N N 281 
MET   C   O    doub N N 282 
MET   C   OXT  sing N N 283 
MET   CB  CG   sing N N 284 
MET   CB  HB2  sing N N 285 
MET   CB  HB3  sing N N 286 
MET   CG  SD   sing N N 287 
MET   CG  HG2  sing N N 288 
MET   CG  HG3  sing N N 289 
MET   SD  CE   sing N N 290 
MET   CE  HE1  sing N N 291 
MET   CE  HE2  sing N N 292 
MET   CE  HE3  sing N N 293 
MET   OXT HXT  sing N N 294 
PHE   N   CA   sing N N 295 
PHE   N   H    sing N N 296 
PHE   N   H2   sing N N 297 
PHE   CA  C    sing N N 298 
PHE   CA  CB   sing N N 299 
PHE   CA  HA   sing N N 300 
PHE   C   O    doub N N 301 
PHE   C   OXT  sing N N 302 
PHE   CB  CG   sing N N 303 
PHE   CB  HB2  sing N N 304 
PHE   CB  HB3  sing N N 305 
PHE   CG  CD1  doub Y N 306 
PHE   CG  CD2  sing Y N 307 
PHE   CD1 CE1  sing Y N 308 
PHE   CD1 HD1  sing N N 309 
PHE   CD2 CE2  doub Y N 310 
PHE   CD2 HD2  sing N N 311 
PHE   CE1 CZ   doub Y N 312 
PHE   CE1 HE1  sing N N 313 
PHE   CE2 CZ   sing Y N 314 
PHE   CE2 HE2  sing N N 315 
PHE   CZ  HZ   sing N N 316 
PHE   OXT HXT  sing N N 317 
PRO   N   CA   sing N N 318 
PRO   N   CD   sing N N 319 
PRO   N   H    sing N N 320 
PRO   CA  C    sing N N 321 
PRO   CA  CB   sing N N 322 
PRO   CA  HA   sing N N 323 
PRO   C   O    doub N N 324 
PRO   C   OXT  sing N N 325 
PRO   CB  CG   sing N N 326 
PRO   CB  HB2  sing N N 327 
PRO   CB  HB3  sing N N 328 
PRO   CG  CD   sing N N 329 
PRO   CG  HG2  sing N N 330 
PRO   CG  HG3  sing N N 331 
PRO   CD  HD2  sing N N 332 
PRO   CD  HD3  sing N N 333 
PRO   OXT HXT  sing N N 334 
SER   N   CA   sing N N 335 
SER   N   H    sing N N 336 
SER   N   H2   sing N N 337 
SER   CA  C    sing N N 338 
SER   CA  CB   sing N N 339 
SER   CA  HA   sing N N 340 
SER   C   O    doub N N 341 
SER   C   OXT  sing N N 342 
SER   CB  OG   sing N N 343 
SER   CB  HB2  sing N N 344 
SER   CB  HB3  sing N N 345 
SER   OG  HG   sing N N 346 
SER   OXT HXT  sing N N 347 
THR   N   CA   sing N N 348 
THR   N   H    sing N N 349 
THR   N   H2   sing N N 350 
THR   CA  C    sing N N 351 
THR   CA  CB   sing N N 352 
THR   CA  HA   sing N N 353 
THR   C   O    doub N N 354 
THR   C   OXT  sing N N 355 
THR   CB  OG1  sing N N 356 
THR   CB  CG2  sing N N 357 
THR   CB  HB   sing N N 358 
THR   OG1 HG1  sing N N 359 
THR   CG2 HG21 sing N N 360 
THR   CG2 HG22 sing N N 361 
THR   CG2 HG23 sing N N 362 
THR   OXT HXT  sing N N 363 
TRP   N   CA   sing N N 364 
TRP   N   H    sing N N 365 
TRP   N   H2   sing N N 366 
TRP   CA  C    sing N N 367 
TRP   CA  CB   sing N N 368 
TRP   CA  HA   sing N N 369 
TRP   C   O    doub N N 370 
TRP   C   OXT  sing N N 371 
TRP   CB  CG   sing N N 372 
TRP   CB  HB2  sing N N 373 
TRP   CB  HB3  sing N N 374 
TRP   CG  CD1  doub Y N 375 
TRP   CG  CD2  sing Y N 376 
TRP   CD1 NE1  sing Y N 377 
TRP   CD1 HD1  sing N N 378 
TRP   CD2 CE2  doub Y N 379 
TRP   CD2 CE3  sing Y N 380 
TRP   NE1 CE2  sing Y N 381 
TRP   NE1 HE1  sing N N 382 
TRP   CE2 CZ2  sing Y N 383 
TRP   CE3 CZ3  doub Y N 384 
TRP   CE3 HE3  sing N N 385 
TRP   CZ2 CH2  doub Y N 386 
TRP   CZ2 HZ2  sing N N 387 
TRP   CZ3 CH2  sing Y N 388 
TRP   CZ3 HZ3  sing N N 389 
TRP   CH2 HH2  sing N N 390 
TRP   OXT HXT  sing N N 391 
TYR   N   CA   sing N N 392 
TYR   N   H    sing N N 393 
TYR   N   H2   sing N N 394 
TYR   CA  C    sing N N 395 
TYR   CA  CB   sing N N 396 
TYR   CA  HA   sing N N 397 
TYR   C   O    doub N N 398 
TYR   C   OXT  sing N N 399 
TYR   CB  CG   sing N N 400 
TYR   CB  HB2  sing N N 401 
TYR   CB  HB3  sing N N 402 
TYR   CG  CD1  doub Y N 403 
TYR   CG  CD2  sing Y N 404 
TYR   CD1 CE1  sing Y N 405 
TYR   CD1 HD1  sing N N 406 
TYR   CD2 CE2  doub Y N 407 
TYR   CD2 HD2  sing N N 408 
TYR   CE1 CZ   doub Y N 409 
TYR   CE1 HE1  sing N N 410 
TYR   CE2 CZ   sing Y N 411 
TYR   CE2 HE2  sing N N 412 
TYR   CZ  OH   sing N N 413 
TYR   OH  HH   sing N N 414 
TYR   OXT HXT  sing N N 415 
VAL   N   CA   sing N N 416 
VAL   N   H    sing N N 417 
VAL   N   H2   sing N N 418 
VAL   CA  C    sing N N 419 
VAL   CA  CB   sing N N 420 
VAL   CA  HA   sing N N 421 
VAL   C   O    doub N N 422 
VAL   C   OXT  sing N N 423 
VAL   CB  CG1  sing N N 424 
VAL   CB  CG2  sing N N 425 
VAL   CB  HB   sing N N 426 
VAL   CG1 HG11 sing N N 427 
VAL   CG1 HG12 sing N N 428 
VAL   CG1 HG13 sing N N 429 
VAL   CG2 HG21 sing N N 430 
VAL   CG2 HG22 sing N N 431 
VAL   CG2 HG23 sing N N 432 
VAL   OXT HXT  sing N N 433 
# 
_pdbx_audit_support.funding_organization   'Other private' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8PO1 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9HBO 
_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]   0.007174 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004450 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011590 
_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]   0.012000 
_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 9   ? 20.358 -33.979 19.887  1.00 72.23  ? 702  ALA   A N   1 
ATOM   2    C CA  . ALA   A 1 9   ? 20.747 -34.188 18.495  1.00 72.54  ? 702  ALA   A CA  1 
ATOM   3    C C   . ALA   A 1 9   ? 21.594 -35.466 18.391  1.00 72.25  ? 702  ALA   A C   1 
ATOM   4    O O   . ALA   A 1 9   ? 21.372 -36.281 17.494  1.00 72.60  ? 702  ALA   A O   1 
ATOM   5    C CB  . ALA   A 1 9   ? 21.496 -32.975 17.966  1.00 72.74  ? 702  ALA   A CB  1 
ATOM   6    N N   . LEU   A 1 10  ? 22.519 -35.675 19.344  1.00 71.30  ? 703  LEU   A N   1 
ATOM   7    C CA  . LEU   A 1 10  ? 23.303 -36.914 19.381  1.00 70.75  ? 703  LEU   A CA  1 
ATOM   8    C C   . LEU   A 1 10  ? 23.108 -37.612 20.722  1.00 69.31  ? 703  LEU   A C   1 
ATOM   9    O O   . LEU   A 1 10  ? 23.774 -37.298 21.708  1.00 69.57  ? 703  LEU   A O   1 
ATOM   10   C CB  . LEU   A 1 10  ? 24.803 -36.714 19.054  1.00 71.26  ? 703  LEU   A CB  1 
ATOM   11   C CG  . LEU   A 1 10  ? 25.722 -37.968 18.835  1.00 73.09  ? 703  LEU   A CG  1 
ATOM   12   C CD1 . LEU   A 1 10  ? 26.643 -38.219 20.010  1.00 73.67  ? 703  LEU   A CD1 1 
ATOM   13   C CD2 . LEU   A 1 10  ? 24.970 -39.231 18.360  1.00 73.72  ? 703  LEU   A CD2 1 
ATOM   14   N N   . LEU   A 1 11  ? 22.167 -38.548 20.750  1.00 67.66  ? 704  LEU   A N   1 
ATOM   15   C CA  . LEU   A 1 11  ? 21.877 -39.331 21.939  1.00 66.35  ? 704  LEU   A CA  1 
ATOM   16   C C   . LEU   A 1 11  ? 22.547 -40.691 21.760  1.00 64.70  ? 704  LEU   A C   1 
ATOM   17   O O   . LEU   A 1 11  ? 22.257 -41.391 20.793  1.00 64.67  ? 704  LEU   A O   1 
ATOM   18   C CB  . LEU   A 1 11  ? 20.355 -39.495 22.089  1.00 66.25  ? 704  LEU   A CB  1 
ATOM   19   C CG  . LEU   A 1 11  ? 19.890 -40.298 23.284  1.00 67.16  ? 704  LEU   A CG  1 
ATOM   20   C CD1 . LEU   A 1 11  ? 20.328 -39.640 24.594  1.00 67.50  ? 704  LEU   A CD1 1 
ATOM   21   C CD2 . LEU   A 1 11  ? 18.388 -40.507 23.236  1.00 67.59  ? 704  LEU   A CD2 1 
ATOM   22   N N   . ARG   A 1 12  ? 23.486 -41.035 22.643  1.00 63.39  ? 705  ARG   A N   1 
ATOM   23   C CA  . ARG   A 1 12  ? 24.186 -42.314 22.548  1.00 62.48  ? 705  ARG   A CA  1 
ATOM   24   C C   . ARG   A 1 12  ? 23.470 -43.341 23.399  1.00 61.43  ? 705  ARG   A C   1 
ATOM   25   O O   . ARG   A 1 12  ? 23.266 -43.115 24.583  1.00 60.56  ? 705  ARG   A O   1 
ATOM   26   C CB  . ARG   A 1 12  ? 25.646 -42.205 23.023  1.00 63.24  ? 705  ARG   A CB  1 
ATOM   27   C CG  . ARG   A 1 12  ? 26.530 -41.264 22.218  1.00 65.60  ? 705  ARG   A CG  1 
ATOM   28   C CD  . ARG   A 1 12  ? 27.911 -41.272 22.847  1.00 68.93  ? 705  ARG   A CD  1 
ATOM   29   N NE  . ARG   A 1 12  ? 28.755 -40.135 22.467  1.00 71.62  ? 705  ARG   A NE  1 
ATOM   30   C CZ  . ARG   A 1 12  ? 28.681 -38.923 23.012  1.00 73.26  ? 705  ARG   A CZ  1 
ATOM   31   N NH1 . ARG   A 1 12  ? 29.504 -37.961 22.617  1.00 74.53  ? 705  ARG   A NH1 1 
ATOM   32   N NH2 . ARG   A 1 12  ? 27.769 -38.657 23.937  1.00 71.57  ? 705  ARG   A NH2 1 
ATOM   33   N N   . ILE   A 1 13  ? 23.071 -44.460 22.791  1.00 61.31  ? 706  ILE   A N   1 
ATOM   34   C CA  . ILE   A 1 13  ? 22.448 -45.539 23.532  1.00 61.71  ? 706  ILE   A CA  1 
ATOM   35   C C   . ILE   A 1 13  ? 23.587 -46.476 23.916  1.00 62.40  ? 706  ILE   A C   1 
ATOM   36   O O   . ILE   A 1 13  ? 24.239 -47.054 23.048  1.00 62.29  ? 706  ILE   A O   1 
ATOM   37   C CB  . ILE   A 1 13  ? 21.329 -46.229 22.732  1.00 61.74  ? 706  ILE   A CB  1 
ATOM   38   C CG1 . ILE   A 1 13  ? 20.157 -45.263 22.508  1.00 62.31  ? 706  ILE   A CG1 1 
ATOM   39   C CG2 . ILE   A 1 13  ? 20.867 -47.472 23.453  1.00 61.97  ? 706  ILE   A CG2 1 
ATOM   40   N N   . LEU   A 1 14  ? 23.875 -46.557 25.212  1.00 62.88  ? 707  LEU   A N   1 
ATOM   41   C CA  . LEU   A 1 14  ? 24.984 -47.339 25.731  1.00 63.67  ? 707  LEU   A CA  1 
ATOM   42   C C   . LEU   A 1 14  ? 24.598 -48.769 26.045  1.00 64.44  ? 707  LEU   A C   1 
ATOM   43   O O   . LEU   A 1 14  ? 23.524 -49.018 26.580  1.00 64.78  ? 707  LEU   A O   1 
ATOM   44   C CB  . LEU   A 1 14  ? 25.518 -46.672 27.016  1.00 63.75  ? 707  LEU   A CB  1 
ATOM   45   C CG  . LEU   A 1 14  ? 26.685 -45.705 26.873  1.00 65.05  ? 707  LEU   A CG  1 
ATOM   46   C CD1 . LEU   A 1 14  ? 26.295 -44.472 26.099  1.00 65.23  ? 707  LEU   A CD1 1 
ATOM   47   C CD2 . LEU   A 1 14  ? 27.212 -45.298 28.231  1.00 65.94  ? 707  LEU   A CD2 1 
ATOM   48   N N   . LYS   A 1 15  ? 25.479 -49.713 25.729  1.00 64.90  ? 708  LYS   A N   1 
ATOM   49   C CA  . LYS   A 1 15  ? 25.282 -51.113 26.101  1.00 65.77  ? 708  LYS   A CA  1 
ATOM   50   C C   . LYS   A 1 15  ? 25.905 -51.271 27.500  1.00 66.90  ? 708  LYS   A C   1 
ATOM   51   O O   . LYS   A 1 15  ? 26.860 -50.563 27.830  1.00 67.00  ? 708  LYS   A O   1 
ATOM   52   C CB  . LYS   A 1 15  ? 25.979 -52.055 25.103  1.00 67.31  ? 708  LYS   A CB  1 
ATOM   53   C CG  . LYS   A 1 15  ? 25.366 -52.060 23.709  1.00 70.84  ? 708  LYS   A CG  1 
ATOM   54   N N   . GLU   A 1 16  ? 25.394 -52.193 28.317  1.00 67.79  ? 709  GLU   A N   1 
ATOM   55   C CA  . GLU   A 1 16  ? 25.910 -52.392 29.674  1.00 69.19  ? 709  GLU   A CA  1 
ATOM   56   C C   . GLU   A 1 16  ? 27.374 -52.861 29.734  1.00 69.76  ? 709  GLU   A C   1 
ATOM   57   O O   . GLU   A 1 16  ? 27.996 -52.766 30.790  1.00 70.30  ? 709  GLU   A O   1 
ATOM   58   C CB  . GLU   A 1 16  ? 25.000 -53.325 30.475  1.00 72.60  ? 709  GLU   A CB  1 
ATOM   59   C CG  . GLU   A 1 16  ? 24.135 -52.572 31.474  1.00 79.45  ? 709  GLU   A CG  1 
ATOM   60   C CD  . GLU   A 1 16  ? 23.025 -53.394 32.099  1.00 87.42  ? 709  GLU   A CD  1 
ATOM   61   O OE1 . GLU   A 1 16  ? 22.697 -54.472 31.548  1.00 88.61  ? 709  GLU   A OE1 1 
ATOM   62   O OE2 . GLU   A 1 16  ? 22.470 -52.951 33.132  1.00 90.03  ? 709  GLU   A OE2 1 
ATOM   63   N N   . THR   A 1 17  ? 27.933 -53.331 28.608  1.00 69.43  ? 710  THR   A N   1 
ATOM   64   C CA  . THR   A 1 17  ? 29.335 -53.763 28.535  1.00 69.19  ? 710  THR   A CA  1 
ATOM   65   C C   . THR   A 1 17  ? 30.307 -52.575 28.290  1.00 68.45  ? 710  THR   A C   1 
ATOM   66   O O   . THR   A 1 17  ? 31.498 -52.682 28.591  1.00 68.76  ? 710  THR   A O   1 
ATOM   67   C CB  . THR   A 1 17  ? 29.499 -54.853 27.471  1.00 70.48  ? 710  THR   A CB  1 
ATOM   68   O OG1 . THR   A 1 17  ? 29.380 -54.266 26.178  1.00 71.42  ? 710  THR   A OG1 1 
ATOM   69   C CG2 . THR   A 1 17  ? 28.488 -55.981 27.629  1.00 71.00  ? 710  THR   A CG2 1 
ATOM   70   N N   . GLU   A 1 18  ? 29.791 -51.457 27.739  1.00 67.11  ? 711  GLU   A N   1 
ATOM   71   C CA  . GLU   A 1 18  ? 30.552 -50.249 27.451  1.00 66.36  ? 711  GLU   A CA  1 
ATOM   72   C C   . GLU   A 1 18  ? 30.992 -49.529 28.717  1.00 66.06  ? 711  GLU   A C   1 
ATOM   73   O O   . GLU   A 1 18  ? 32.015 -48.854 28.703  1.00 66.15  ? 711  GLU   A O   1 
ATOM   74   C CB  . GLU   A 1 18  ? 29.695 -49.275 26.641  1.00 68.25  ? 711  GLU   A CB  1 
ATOM   75   C CG  . GLU   A 1 18  ? 29.615 -49.574 25.162  1.00 72.74  ? 711  GLU   A CG  1 
ATOM   76   C CD  . GLU   A 1 18  ? 28.818 -48.525 24.412  1.00 79.21  ? 711  GLU   A CD  1 
ATOM   77   O OE1 . GLU   A 1 18  ? 29.310 -47.379 24.282  1.00 80.79  ? 711  GLU   A OE1 1 
ATOM   78   O OE2 . GLU   A 1 18  ? 27.692 -48.847 23.966  1.00 80.98  ? 711  GLU   A OE2 1 
ATOM   79   N N   . PHE   A 1 19  ? 30.200 -49.612 29.790  1.00 65.53  ? 712  PHE   A N   1 
ATOM   80   C CA  . PHE   A 1 19  ? 30.510 -48.903 31.021  1.00 65.26  ? 712  PHE   A CA  1 
ATOM   81   C C   . PHE   A 1 19  ? 30.457 -49.793 32.257  1.00 65.62  ? 712  PHE   A C   1 
ATOM   82   O O   . PHE   A 1 19  ? 29.798 -50.825 32.245  1.00 65.84  ? 712  PHE   A O   1 
ATOM   83   C CB  . PHE   A 1 19  ? 29.600 -47.676 31.171  1.00 64.73  ? 712  PHE   A CB  1 
ATOM   84   C CG  . PHE   A 1 19  ? 28.139 -47.992 31.390  1.00 64.80  ? 712  PHE   A CG  1 
ATOM   85   C CD1 . PHE   A 1 19  ? 27.323 -48.347 30.331  1.00 65.17  ? 712  PHE   A CD1 1 
ATOM   86   C CD2 . PHE   A 1 19  ? 27.573 -47.893 32.649  1.00 65.26  ? 712  PHE   A CD2 1 
ATOM   87   C CE1 . PHE   A 1 19  ? 25.982 -48.628 30.532  1.00 65.57  ? 712  PHE   A CE1 1 
ATOM   88   C CE2 . PHE   A 1 19  ? 26.233 -48.178 32.847  1.00 65.83  ? 712  PHE   A CE2 1 
ATOM   89   C CZ  . PHE   A 1 19  ? 25.447 -48.547 31.788  1.00 65.49  ? 712  PHE   A CZ  1 
ATOM   90   N N   . LYS   A 1 20  ? 31.157 -49.395 33.322  1.00 65.89  ? 713  LYS   A N   1 
ATOM   91   C CA  . LYS   A 1 20  ? 31.207 -50.147 34.577  1.00 66.84  ? 713  LYS   A CA  1 
ATOM   92   C C   . LYS   A 1 20  ? 30.984 -49.221 35.772  1.00 67.77  ? 713  LYS   A C   1 
ATOM   93   O O   . LYS   A 1 20  ? 31.421 -48.077 35.747  1.00 67.81  ? 713  LYS   A O   1 
ATOM   94   C CB  . LYS   A 1 20  ? 32.554 -50.879 34.723  1.00 68.03  ? 713  LYS   A CB  1 
ATOM   95   N N   . LYS   A 1 21  ? 30.300 -49.711 36.813  1.00 68.19  ? 714  LYS   A N   1 
ATOM   96   C CA  . LYS   A 1 21  ? 30.050 -48.930 38.022  1.00 68.77  ? 714  LYS   A CA  1 
ATOM   97   C C   . LYS   A 1 21  ? 31.144 -49.275 39.035  1.00 70.07  ? 714  LYS   A C   1 
ATOM   98   O O   . LYS   A 1 21  ? 31.392 -50.459 39.286  1.00 70.67  ? 714  LYS   A O   1 
ATOM   99   C CB  . LYS   A 1 21  ? 28.658 -49.246 38.593  1.00 69.46  ? 714  LYS   A CB  1 
ATOM   100  C CG  . LYS   A 1 21  ? 27.520 -48.549 37.865  1.00 71.82  ? 714  LYS   A CG  1 
ATOM   101  C CD  . LYS   A 1 21  ? 26.184 -49.043 38.371  1.00 75.09  ? 714  LYS   A CD  1 
ATOM   102  C CE  . LYS   A 1 21  ? 25.794 -50.370 37.762  1.00 78.73  ? 714  LYS   A CE  1 
ATOM   103  N N   . ILE   A 1 22  ? 31.838 -48.260 39.573  1.00 70.33  ? 715  ILE   A N   1 
ATOM   104  C CA  . ILE   A 1 22  ? 32.929 -48.504 40.515  1.00 70.99  ? 715  ILE   A CA  1 
ATOM   105  C C   . ILE   A 1 22  ? 32.473 -48.351 41.982  1.00 71.22  ? 715  ILE   A C   1 
ATOM   106  O O   . ILE   A 1 22  ? 32.562 -49.317 42.744  1.00 71.76  ? 715  ILE   A O   1 
ATOM   107  C CB  . ILE   A 1 22  ? 34.184 -47.654 40.174  1.00 71.65  ? 715  ILE   A CB  1 
ATOM   108  C CG1 . ILE   A 1 22  ? 34.599 -47.845 38.700  1.00 72.59  ? 715  ILE   A CG1 1 
ATOM   109  C CG2 . ILE   A 1 22  ? 35.340 -47.989 41.110  1.00 72.08  ? 715  ILE   A CG2 1 
ATOM   110  N N   . LYS   A 1 23  ? 31.977 -47.170 42.376  1.00 70.33  ? 716  LYS   A N   1 
ATOM   111  C CA  . LYS   A 1 23  ? 31.520 -46.954 43.753  1.00 70.26  ? 716  LYS   A CA  1 
ATOM   112  C C   . LYS   A 1 23  ? 30.291 -46.043 43.838  1.00 70.20  ? 716  LYS   A C   1 
ATOM   113  O O   . LYS   A 1 23  ? 30.032 -45.279 42.919  1.00 70.12  ? 716  LYS   A O   1 
ATOM   114  C CB  . LYS   A 1 23  ? 32.662 -46.424 44.649  1.00 71.59  ? 716  LYS   A CB  1 
ATOM   115  C CG  . LYS   A 1 23  ? 33.005 -44.955 44.444  1.00 75.28  ? 716  LYS   A CG  1 
ATOM   116  N N   . VAL   A 1 24  ? 29.539 -46.116 44.943  1.00 70.05  ? 717  VAL   A N   1 
ATOM   117  C CA  . VAL   A 1 24  ? 28.362 -45.275 45.134  1.00 70.58  ? 717  VAL   A CA  1 
ATOM   118  C C   . VAL   A 1 24  ? 28.783 -43.895 45.616  1.00 71.44  ? 717  VAL   A C   1 
ATOM   119  O O   . VAL   A 1 24  ? 29.564 -43.788 46.558  1.00 71.67  ? 717  VAL   A O   1 
ATOM   120  C CB  . VAL   A 1 24  ? 27.361 -45.916 46.125  1.00 71.02  ? 717  VAL   A CB  1 
ATOM   121  C CG1 . VAL   A 1 24  ? 26.152 -45.012 46.360  1.00 71.38  ? 717  VAL   A CG1 1 
ATOM   122  C CG2 . VAL   A 1 24  ? 26.931 -47.298 45.654  1.00 71.53  ? 717  VAL   A CG2 1 
ATOM   123  N N   . LEU   A 1 25  ? 28.264 -42.841 44.980  1.00 71.79  ? 718  LEU   A N   1 
ATOM   124  C CA  . LEU   A 1 25  ? 28.528 -41.456 45.357  1.00 72.71  ? 718  LEU   A CA  1 
ATOM   125  C C   . LEU   A 1 25  ? 27.433 -40.914 46.279  1.00 73.97  ? 718  LEU   A C   1 
ATOM   126  O O   . LEU   A 1 25  ? 27.720 -40.137 47.183  1.00 74.18  ? 718  LEU   A O   1 
ATOM   127  C CB  . LEU   A 1 25  ? 28.632 -40.563 44.111  1.00 72.63  ? 718  LEU   A CB  1 
ATOM   128  C CG  . LEU   A 1 25  ? 29.772 -40.859 43.154  1.00 73.80  ? 718  LEU   A CG  1 
ATOM   129  C CD1 . LEU   A 1 25  ? 29.707 -39.943 41.957  1.00 74.51  ? 718  LEU   A CD1 1 
ATOM   130  C CD2 . LEU   A 1 25  ? 31.113 -40.727 43.846  1.00 74.31  ? 718  LEU   A CD2 1 
ATOM   131  N N   . GLY   A 1 26  ? 26.191 -41.303 46.029  1.00 74.84  ? 719  GLY   A N   1 
ATOM   132  C CA  . GLY   A 1 26  ? 25.056 -40.851 46.818  1.00 76.34  ? 719  GLY   A CA  1 
ATOM   133  C C   . GLY   A 1 26  ? 23.794 -41.617 46.493  1.00 77.99  ? 719  GLY   A C   1 
ATOM   134  O O   . GLY   A 1 26  ? 23.668 -42.170 45.402  1.00 77.98  ? 719  GLY   A O   1 
ATOM   135  N N   . SER   A 1 27  ? 22.853 -41.659 47.436  1.00 79.27  ? 720  SER   A N   1 
ATOM   136  C CA  . SER   A 1 27  ? 21.598 -42.396 47.288  1.00 81.03  ? 720  SER   A CA  1 
ATOM   137  C C   . SER   A 1 27  ? 20.375 -41.484 47.539  1.00 82.47  ? 720  SER   A C   1 
ATOM   138  O O   . SER   A 1 27  ? 20.530 -40.295 47.830  1.00 82.61  ? 720  SER   A O   1 
ATOM   139  C CB  . SER   A 1 27  ? 21.590 -43.593 48.240  1.00 82.92  ? 720  SER   A CB  1 
ATOM   140  O OG  . SER   A 1 27  ? 22.561 -44.569 47.895  1.00 85.92  ? 720  SER   A OG  1 
ATOM   141  N N   . GLY   A 1 28  ? 19.173 -42.036 47.410  1.00 83.24  ? 721  GLY   A N   1 
ATOM   142  C CA  . GLY   A 1 28  ? 17.949 -41.284 47.647  1.00 84.45  ? 721  GLY   A CA  1 
ATOM   143  C C   . GLY   A 1 28  ? 16.703 -42.010 47.187  1.00 85.50  ? 721  GLY   A C   1 
ATOM   144  O O   . GLY   A 1 28  ? 16.763 -43.185 46.799  1.00 85.91  ? 721  GLY   A O   1 
ATOM   145  N N   . ALA   A 1 29  ? 15.555 -41.317 47.243  1.00 85.56  ? 722  ALA   A N   1 
ATOM   146  C CA  . ALA   A 1 29  ? 14.281 -41.881 46.787  1.00 85.74  ? 722  ALA   A CA  1 
ATOM   147  C C   . ALA   A 1 29  ? 14.259 -41.986 45.241  1.00 85.50  ? 722  ALA   A C   1 
ATOM   148  O O   . ALA   A 1 29  ? 13.665 -42.926 44.699  1.00 85.72  ? 722  ALA   A O   1 
ATOM   149  C CB  . ALA   A 1 29  ? 13.122 -41.028 47.283  1.00 85.91  ? 722  ALA   A CB  1 
ATOM   150  N N   . PHE   A 1 30  ? 14.959 -41.039 44.547  1.00 84.58  ? 723  PHE   A N   1 
ATOM   151  C CA  . PHE   A 1 30  ? 15.121 -40.963 43.088  1.00 83.90  ? 723  PHE   A CA  1 
ATOM   152  C C   . PHE   A 1 30  ? 15.844 -42.199 42.508  1.00 82.26  ? 723  PHE   A C   1 
ATOM   153  O O   . PHE   A 1 30  ? 15.585 -42.596 41.370  1.00 82.58  ? 723  PHE   A O   1 
ATOM   154  C CB  . PHE   A 1 30  ? 15.923 -39.690 42.709  1.00 84.20  ? 723  PHE   A CB  1 
ATOM   155  C CG  . PHE   A 1 30  ? 17.381 -39.721 43.126  1.00 85.36  ? 723  PHE   A CG  1 
ATOM   156  C CD1 . PHE   A 1 30  ? 17.763 -39.351 44.406  1.00 86.32  ? 723  PHE   A CD1 1 
ATOM   157  C CD2 . PHE   A 1 30  ? 18.363 -40.170 42.254  1.00 86.27  ? 723  PHE   A CD2 1 
ATOM   158  C CE1 . PHE   A 1 30  ? 19.094 -39.422 44.798  1.00 87.05  ? 723  PHE   A CE1 1 
ATOM   159  C CE2 . PHE   A 1 30  ? 19.687 -40.262 42.660  1.00 86.98  ? 723  PHE   A CE2 1 
ATOM   160  C CZ  . PHE   A 1 30  ? 20.046 -39.881 43.924  1.00 86.82  ? 723  PHE   A CZ  1 
ATOM   161  N N   . GLY   A 1 31  ? 16.767 -42.755 43.285  1.00 80.17  ? 724  GLY   A N   1 
ATOM   162  C CA  . GLY   A 1 31  ? 17.623 -43.855 42.874  1.00 78.52  ? 724  GLY   A CA  1 
ATOM   163  C C   . GLY   A 1 31  ? 19.028 -43.681 43.429  1.00 76.19  ? 724  GLY   A C   1 
ATOM   164  O O   . GLY   A 1 31  ? 19.190 -43.276 44.583  1.00 76.72  ? 724  GLY   A O   1 
ATOM   165  N N   . THR   A 1 32  ? 20.063 -43.980 42.628  1.00 73.35  ? 725  THR   A N   1 
ATOM   166  C CA  . THR   A 1 32  ? 21.445 -43.920 43.114  1.00 70.91  ? 725  THR   A CA  1 
ATOM   167  C C   . THR   A 1 32  ? 22.417 -43.331 42.085  1.00 68.06  ? 725  THR   A C   1 
ATOM   168  O O   . THR   A 1 32  ? 22.233 -43.518 40.885  1.00 68.09  ? 725  THR   A O   1 
ATOM   169  C CB  . THR   A 1 32  ? 21.880 -45.336 43.544  1.00 72.07  ? 725  THR   A CB  1 
ATOM   170  O OG1 . THR   A 1 32  ? 20.920 -45.882 44.446  1.00 73.16  ? 725  THR   A OG1 1 
ATOM   171  C CG2 . THR   A 1 32  ? 23.250 -45.374 44.189  1.00 72.38  ? 725  THR   A CG2 1 
ATOM   172  N N   . VAL   A 1 33  ? 23.464 -42.642 42.561  1.00 65.39  ? 726  VAL   A N   1 
ATOM   173  C CA  . VAL   A 1 33  ? 24.503 -42.073 41.711  1.00 63.53  ? 726  VAL   A CA  1 
ATOM   174  C C   . VAL   A 1 33  ? 25.810 -42.860 41.916  1.00 61.95  ? 726  VAL   A C   1 
ATOM   175  O O   . VAL   A 1 33  ? 26.235 -43.070 43.043  1.00 61.95  ? 726  VAL   A O   1 
ATOM   176  C CB  . VAL   A 1 33  ? 24.688 -40.547 41.944  1.00 63.37  ? 726  VAL   A CB  1 
ATOM   177  C CG1 . VAL   A 1 33  ? 25.916 -40.021 41.206  1.00 63.21  ? 726  VAL   A CG1 1 
ATOM   178  C CG2 . VAL   A 1 33  ? 23.435 -39.777 41.533  1.00 63.68  ? 726  VAL   A CG2 1 
ATOM   179  N N   . TYR   A 1 34  ? 26.417 -43.325 40.831  1.00 60.50  ? 727  TYR   A N   1 
ATOM   180  C CA  . TYR   A 1 34  ? 27.639 -44.111 40.874  1.00 59.72  ? 727  TYR   A CA  1 
ATOM   181  C C   . TYR   A 1 34  ? 28.779 -43.403 40.161  1.00 59.32  ? 727  TYR   A C   1 
ATOM   182  O O   . TYR   A 1 34  ? 28.562 -42.714 39.179  1.00 59.16  ? 727  TYR   A O   1 
ATOM   183  C CB  . TYR   A 1 34  ? 27.417 -45.451 40.162  1.00 59.41  ? 727  TYR   A CB  1 
ATOM   184  C CG  . TYR   A 1 34  ? 26.341 -46.319 40.771  1.00 60.29  ? 727  TYR   A CG  1 
ATOM   185  C CD1 . TYR   A 1 34  ? 25.005 -46.151 40.429  1.00 61.13  ? 727  TYR   A CD1 1 
ATOM   186  C CD2 . TYR   A 1 34  ? 26.668 -47.372 41.615  1.00 61.28  ? 727  TYR   A CD2 1 
ATOM   187  C CE1 . TYR   A 1 34  ? 24.016 -46.966 40.965  1.00 62.15  ? 727  TYR   A CE1 1 
ATOM   188  C CE2 . TYR   A 1 34  ? 25.692 -48.208 42.138  1.00 62.14  ? 727  TYR   A CE2 1 
ATOM   189  C CZ  . TYR   A 1 34  ? 24.363 -47.993 41.820  1.00 63.28  ? 727  TYR   A CZ  1 
ATOM   190  O OH  . TYR   A 1 34  ? 23.377 -48.795 42.343  1.00 65.04  ? 727  TYR   A OH  1 
ATOM   191  N N   . LYS   A 1 35  ? 30.004 -43.619 40.625  1.00 59.19  ? 728  LYS   A N   1 
ATOM   192  C CA  . LYS   A 1 35  ? 31.217 -43.129 39.980  1.00 59.24  ? 728  LYS   A CA  1 
ATOM   193  C C   . LYS   A 1 35  ? 31.647 -44.314 39.150  1.00 59.21  ? 728  LYS   A C   1 
ATOM   194  O O   . LYS   A 1 35  ? 31.822 -45.396 39.700  1.00 59.80  ? 728  LYS   A O   1 
ATOM   195  C CB  . LYS   A 1 35  ? 32.305 -42.819 41.021  1.00 60.88  ? 728  LYS   A CB  1 
ATOM   196  N N   . GLY   A 1 36  ? 31.756 -44.139 37.841  1.00 58.55  ? 729  GLY   A N   1 
ATOM   197  C CA  . GLY   A 1 36  ? 32.117 -45.242 36.966  1.00 58.29  ? 729  GLY   A CA  1 
ATOM   198  C C   . GLY   A 1 36  ? 33.125 -44.941 35.885  1.00 57.86  ? 729  GLY   A C   1 
ATOM   199  O O   . GLY   A 1 36  ? 33.798 -43.915 35.903  1.00 57.91  ? 729  GLY   A O   1 
ATOM   200  N N   . LEU   A 1 37  ? 33.207 -45.832 34.915  1.00 57.65  ? 730  LEU   A N   1 
ATOM   201  C CA  . LEU   A 1 37  ? 34.155 -45.721 33.823  1.00 58.03  ? 730  LEU   A CA  1 
ATOM   202  C C   . LEU   A 1 37  ? 33.491 -46.140 32.524  1.00 57.81  ? 730  LEU   A C   1 
ATOM   203  O O   . LEU   A 1 37  ? 32.764 -47.125 32.497  1.00 57.44  ? 730  LEU   A O   1 
ATOM   204  C CB  . LEU   A 1 37  ? 35.340 -46.648 34.129  1.00 58.54  ? 730  LEU   A CB  1 
ATOM   205  C CG  . LEU   A 1 37  ? 36.729 -46.221 33.667  1.00 60.20  ? 730  LEU   A CG  1 
ATOM   206  C CD1 . LEU   A 1 37  ? 37.009 -44.719 33.930  1.00 60.43  ? 730  LEU   A CD1 1 
ATOM   207  C CD2 . LEU   A 1 37  ? 37.779 -47.080 34.347  1.00 61.00  ? 730  LEU   A CD2 1 
ATOM   208  N N   . TRP   A 1 38  ? 33.742 -45.400 31.449  1.00 57.86  ? 731  TRP   A N   1 
ATOM   209  C CA  . TRP   A 1 38  ? 33.120 -45.685 30.166  1.00 58.14  ? 731  TRP   A CA  1 
ATOM   210  C C   . TRP   A 1 38  ? 34.132 -45.804 29.040  1.00 59.38  ? 731  TRP   A C   1 
ATOM   211  O O   . TRP   A 1 38  ? 35.057 -45.006 28.937  1.00 59.40  ? 731  TRP   A O   1 
ATOM   212  C CB  . TRP   A 1 38  ? 32.061 -44.611 29.860  1.00 57.20  ? 731  TRP   A CB  1 
ATOM   213  C CG  . TRP   A 1 38  ? 31.411 -44.723 28.517  1.00 56.82  ? 731  TRP   A CG  1 
ATOM   214  C CD1 . TRP   A 1 38  ? 30.890 -45.844 27.943  1.00 57.36  ? 731  TRP   A CD1 1 
ATOM   215  C CD2 . TRP   A 1 38  ? 31.108 -43.641 27.634  1.00 56.62  ? 731  TRP   A CD2 1 
ATOM   216  N NE1 . TRP   A 1 38  ? 30.341 -45.536 26.723  1.00 57.50  ? 731  TRP   A NE1 1 
ATOM   217  C CE2 . TRP   A 1 38  ? 30.452 -44.186 26.514  1.00 57.23  ? 731  TRP   A CE2 1 
ATOM   218  C CE3 . TRP   A 1 38  ? 31.317 -42.257 27.687  1.00 57.23  ? 731  TRP   A CE3 1 
ATOM   219  C CZ2 . TRP   A 1 38  ? 30.032 -43.402 25.444  1.00 58.11  ? 731  TRP   A CZ2 1 
ATOM   220  C CZ3 . TRP   A 1 38  ? 30.894 -41.480 26.629  1.00 58.19  ? 731  TRP   A CZ3 1 
ATOM   221  C CH2 . TRP   A 1 38  ? 30.261 -42.052 25.522  1.00 58.33  ? 731  TRP   A CH2 1 
ATOM   222  N N   . ILE   A 1 39  ? 33.953 -46.817 28.202  1.00 60.22  ? 732  ILE   A N   1 
ATOM   223  C CA  . ILE   A 1 39  ? 34.771 -47.066 27.032  1.00 61.52  ? 732  ILE   A CA  1 
ATOM   224  C C   . ILE   A 1 39  ? 33.841 -46.969 25.821  1.00 62.74  ? 732  ILE   A C   1 
ATOM   225  O O   . ILE   A 1 39  ? 33.111 -47.921 25.539  1.00 62.60  ? 732  ILE   A O   1 
ATOM   226  C CB  . ILE   A 1 39  ? 35.429 -48.464 27.084  1.00 62.17  ? 732  ILE   A CB  1 
ATOM   227  C CG1 . ILE   A 1 39  ? 36.062 -48.770 28.450  1.00 63.15  ? 732  ILE   A CG1 1 
ATOM   228  C CG2 . ILE   A 1 39  ? 36.441 -48.604 25.955  1.00 62.86  ? 732  ILE   A CG2 1 
ATOM   229  N N   . PRO   A 1 40  ? 33.833 -45.833 25.102  1.00 63.52  ? 733  PRO   A N   1 
ATOM   230  C CA  . PRO   A 1 40  ? 32.937 -45.707 23.940  1.00 64.55  ? 733  PRO   A CA  1 
ATOM   231  C C   . PRO   A 1 40  ? 33.204 -46.762 22.871  1.00 66.71  ? 733  PRO   A C   1 
ATOM   232  O O   . PRO   A 1 40  ? 34.341 -47.191 22.707  1.00 66.86  ? 733  PRO   A O   1 
ATOM   233  C CB  . PRO   A 1 40  ? 33.179 -44.279 23.453  1.00 64.73  ? 733  PRO   A CB  1 
ATOM   234  C CG  . PRO   A 1 40  ? 33.767 -43.568 24.633  1.00 64.84  ? 733  PRO   A CG  1 
ATOM   235  C CD  . PRO   A 1 40  ? 34.608 -44.603 25.321  1.00 63.04  ? 733  PRO   A CD  1 
ATOM   236  N N   . GLU   A 1 41  ? 32.132 -47.209 22.191  1.00 68.24  ? 734  GLU   A N   1 
ATOM   237  C CA  . GLU   A 1 41  ? 32.080 -48.302 21.212  1.00 70.06  ? 734  GLU   A CA  1 
ATOM   238  C C   . GLU   A 1 41  ? 33.311 -48.429 20.276  1.00 71.64  ? 734  GLU   A C   1 
ATOM   239  O O   . GLU   A 1 41  ? 34.001 -49.456 20.317  1.00 71.94  ? 734  GLU   A O   1 
ATOM   240  C CB  . GLU   A 1 41  ? 30.771 -48.248 20.389  1.00 72.11  ? 734  GLU   A CB  1 
ATOM   241  C CG  . GLU   A 1 41  ? 30.601 -49.418 19.435  1.00 75.80  ? 734  GLU   A CG  1 
ATOM   242  N N   . GLY   A 1 42  ? 33.567 -47.421 19.447  1.00 72.26  ? 735  GLY   A N   1 
ATOM   243  C CA  . GLY   A 1 42  ? 34.685 -47.477 18.511  1.00 73.13  ? 735  GLY   A CA  1 
ATOM   244  C C   . GLY   A 1 42  ? 35.899 -46.704 18.983  1.00 73.62  ? 735  GLY   A C   1 
ATOM   245  O O   . GLY   A 1 42  ? 36.637 -46.125 18.174  1.00 73.97  ? 735  GLY   A O   1 
ATOM   246  N N   . GLU   A 1 43  ? 36.103 -46.681 20.309  1.00 73.24  ? 736  GLU   A N   1 
ATOM   247  C CA  . GLU   A 1 43  ? 37.197 -45.963 20.948  1.00 72.94  ? 736  GLU   A CA  1 
ATOM   248  C C   . GLU   A 1 43  ? 37.971 -46.853 21.912  1.00 72.97  ? 736  GLU   A C   1 
ATOM   249  O O   . GLU   A 1 43  ? 37.422 -47.802 22.475  1.00 73.35  ? 736  GLU   A O   1 
ATOM   250  C CB  . GLU   A 1 43  ? 36.660 -44.744 21.702  1.00 74.00  ? 736  GLU   A CB  1 
ATOM   251  C CG  . GLU   A 1 43  ? 35.954 -43.746 20.808  1.00 77.73  ? 736  GLU   A CG  1 
ATOM   252  C CD  . GLU   A 1 43  ? 36.079 -42.311 21.278  1.00 82.99  ? 736  GLU   A CD  1 
ATOM   253  O OE1 . GLU   A 1 43  ? 37.202 -41.758 21.221  1.00 83.82  ? 736  GLU   A OE1 1 
ATOM   254  O OE2 . GLU   A 1 43  ? 35.049 -41.741 21.702  1.00 84.27  ? 736  GLU   A OE2 1 
ATOM   255  N N   . LYS   A 1 44  ? 39.248 -46.530 22.107  1.00 72.37  ? 737  LYS   A N   1 
ATOM   256  C CA  . LYS   A 1 44  ? 40.127 -47.244 23.021  1.00 72.00  ? 737  LYS   A CA  1 
ATOM   257  C C   . LYS   A 1 44  ? 40.535 -46.241 24.105  1.00 71.18  ? 737  LYS   A C   1 
ATOM   258  O O   . LYS   A 1 44  ? 41.718 -45.945 24.269  1.00 71.71  ? 737  LYS   A O   1 
ATOM   259  C CB  . LYS   A 1 44  ? 41.357 -47.788 22.266  1.00 73.51  ? 737  LYS   A CB  1 
ATOM   260  N N   . VAL   A 1 45  ? 39.546 -45.686 24.817  1.00 69.64  ? 738  VAL   A N   1 
ATOM   261  C CA  . VAL   A 1 45  ? 39.813 -44.691 25.851  1.00 68.75  ? 738  VAL   A CA  1 
ATOM   262  C C   . VAL   A 1 45  ? 38.868 -44.859 27.047  1.00 67.52  ? 738  VAL   A C   1 
ATOM   263  O O   . VAL   A 1 45  ? 37.688 -45.138 26.863  1.00 67.88  ? 738  VAL   A O   1 
ATOM   264  C CB  . VAL   A 1 45  ? 39.751 -43.251 25.273  1.00 69.38  ? 738  VAL   A CB  1 
ATOM   265  N N   . LYS   A 1 46  ? 39.387 -44.691 28.269  1.00 66.06  ? 739  LYS   A N   1 
ATOM   266  C CA  . LYS   A 1 46  ? 38.593 -44.794 29.491  1.00 65.01  ? 739  LYS   A CA  1 
ATOM   267  C C   . LYS   A 1 46  ? 38.178 -43.390 29.941  1.00 63.35  ? 739  LYS   A C   1 
ATOM   268  O O   . LYS   A 1 46  ? 39.026 -42.516 30.113  1.00 63.77  ? 739  LYS   A O   1 
ATOM   269  C CB  . LYS   A 1 46  ? 39.382 -45.507 30.609  1.00 66.92  ? 739  LYS   A CB  1 
ATOM   270  C CG  . LYS   A 1 46  ? 39.027 -46.983 30.777  1.00 71.09  ? 739  LYS   A CG  1 
ATOM   271  C CD  . LYS   A 1 46  ? 39.648 -47.875 29.707  1.00 75.12  ? 739  LYS   A CD  1 
ATOM   272  C CE  . LYS   A 1 46  ? 40.879 -48.598 30.204  1.00 78.26  ? 739  LYS   A CE  1 
ATOM   273  N N   . ILE   A 1 47  ? 36.874 -43.167 30.104  1.00 61.20  ? 740  ILE   A N   1 
ATOM   274  C CA  . ILE   A 1 47  ? 36.358 -41.873 30.503  1.00 59.70  ? 740  ILE   A CA  1 
ATOM   275  C C   . ILE   A 1 47  ? 35.674 -41.964 31.854  1.00 58.04  ? 740  ILE   A C   1 
ATOM   276  O O   . ILE   A 1 47  ? 34.749 -42.758 32.030  1.00 58.13  ? 740  ILE   A O   1 
ATOM   277  C CB  . ILE   A 1 47  ? 35.382 -41.325 29.428  1.00 60.18  ? 740  ILE   A CB  1 
ATOM   278  C CG1 . ILE   A 1 47  ? 36.063 -41.217 28.049  1.00 61.18  ? 740  ILE   A CG1 1 
ATOM   279  C CG2 . ILE   A 1 47  ? 34.764 -39.994 29.870  1.00 60.33  ? 740  ILE   A CG2 1 
ATOM   280  C CD1 . ILE   A 1 47  ? 35.117 -40.872 26.920  1.00 62.49  ? 740  ILE   A CD1 1 
ATOM   281  N N   . PRO   A 1 48  ? 36.092 -41.126 32.817  1.00 56.21  ? 741  PRO   A N   1 
ATOM   282  C CA  . PRO   A 1 48  ? 35.449 -41.142 34.140  1.00 54.52  ? 741  PRO   A CA  1 
ATOM   283  C C   . PRO   A 1 48  ? 34.056 -40.536 34.056  1.00 51.64  ? 741  PRO   A C   1 
ATOM   284  O O   . PRO   A 1 48  ? 33.896 -39.381 33.657  1.00 51.50  ? 741  PRO   A O   1 
ATOM   285  C CB  . PRO   A 1 48  ? 36.386 -40.272 35.001  1.00 55.63  ? 741  PRO   A CB  1 
ATOM   286  C CG  . PRO   A 1 48  ? 37.652 -40.127 34.192  1.00 56.40  ? 741  PRO   A CG  1 
ATOM   287  C CD  . PRO   A 1 48  ? 37.184 -40.141 32.770  1.00 55.44  ? 741  PRO   A CD  1 
ATOM   288  N N   . VAL   A 1 49  ? 33.047 -41.328 34.399  1.00 49.11  ? 742  VAL   A N   1 
ATOM   289  C CA  . VAL   A 1 49  ? 31.666 -40.884 34.301  1.00 46.92  ? 742  VAL   A CA  1 
ATOM   290  C C   . VAL   A 1 49  ? 30.927 -40.944 35.637  1.00 45.53  ? 742  VAL   A C   1 
ATOM   291  O O   . VAL   A 1 49  ? 31.395 -41.560 36.595  1.00 45.46  ? 742  VAL   A O   1 
ATOM   292  C CB  . VAL   A 1 49  ? 30.918 -41.723 33.227  1.00 46.65  ? 742  VAL   A CB  1 
ATOM   293  C CG1 . VAL   A 1 49  ? 31.448 -41.453 31.824  1.00 47.32  ? 742  VAL   A CG1 1 
ATOM   294  C CG2 . VAL   A 1 49  ? 30.959 -43.196 33.569  1.00 46.16  ? 742  VAL   A CG2 1 
ATOM   295  N N   . ALA   A 1 50  ? 29.766 -40.292 35.694  1.00 44.58  ? 743  ALA   A N   1 
ATOM   296  C CA  . ALA   A 1 50  ? 28.847 -40.360 36.807  1.00 44.64  ? 743  ALA   A CA  1 
ATOM   297  C C   . ALA   A 1 50  ? 27.581 -40.991 36.213  1.00 44.76  ? 743  ALA   A C   1 
ATOM   298  O O   . ALA   A 1 50  ? 27.099 -40.560 35.163  1.00 44.59  ? 743  ALA   A O   1 
ATOM   299  C CB  . ALA   A 1 50  ? 28.559 -38.974 37.348  1.00 44.34  ? 743  ALA   A CB  1 
ATOM   300  N N   . ILE   A 1 51  ? 27.102 -42.059 36.831  1.00 44.79  ? 744  ILE   A N   1 
ATOM   301  C CA  . ILE   A 1 51  ? 25.924 -42.768 36.353  1.00 45.87  ? 744  ILE   A CA  1 
ATOM   302  C C   . ILE   A 1 51  ? 24.769 -42.572 37.312  1.00 46.72  ? 744  ILE   A C   1 
ATOM   303  O O   . ILE   A 1 51  ? 24.902 -42.914 38.474  1.00 47.24  ? 744  ILE   A O   1 
ATOM   304  C CB  . ILE   A 1 51  ? 26.237 -44.281 36.186  1.00 46.37  ? 744  ILE   A CB  1 
ATOM   305  C CG1 . ILE   A 1 51  ? 27.368 -44.504 35.177  1.00 47.30  ? 744  ILE   A CG1 1 
ATOM   306  C CG2 . ILE   A 1 51  ? 24.995 -45.052 35.792  1.00 46.74  ? 744  ILE   A CG2 1 
ATOM   307  C CD1 . ILE   A 1 51  ? 28.448 -45.342 35.681  1.00 48.23  ? 744  ILE   A CD1 1 
ATOM   308  N N   . LYS   A 1 52  ? 23.636 -42.041 36.842  1.00 46.86  ? 745  LYS   A N   1 
ATOM   309  C CA  . LYS   A 1 52  ? 22.455 -41.911 37.682  1.00 47.73  ? 745  LYS   A CA  1 
ATOM   310  C C   . LYS   A 1 52  ? 21.493 -43.050 37.329  1.00 48.60  ? 745  LYS   A C   1 
ATOM   311  O O   . LYS   A 1 52  ? 20.937 -43.076 36.234  1.00 48.51  ? 745  LYS   A O   1 
ATOM   312  C CB  . LYS   A 1 52  ? 21.775 -40.559 37.469  1.00 49.61  ? 745  LYS   A CB  1 
ATOM   313  C CG  . LYS   A 1 52  ? 20.685 -40.242 38.487  1.00 53.02  ? 745  LYS   A CG  1 
ATOM   314  C CD  . LYS   A 1 52  ? 20.228 -38.800 38.307  1.00 57.35  ? 745  LYS   A CD  1 
ATOM   315  C CE  . LYS   A 1 52  ? 19.729 -38.227 39.602  1.00 60.92  ? 745  LYS   A CE  1 
ATOM   316  N NZ  . LYS   A 1 52  ? 19.957 -36.765 39.687  1.00 62.61  ? 745  LYS   A NZ  1 
ATOM   317  N N   . GLU   A 1 53  ? 21.331 -44.006 38.229  1.00 49.65  ? 746  GLU   A N   1 
ATOM   318  C CA  . GLU   A 1 53  ? 20.406 -45.111 38.013  1.00 51.59  ? 746  GLU   A CA  1 
ATOM   319  C C   . GLU   A 1 53  ? 19.078 -44.776 38.684  1.00 53.14  ? 746  GLU   A C   1 
ATOM   320  O O   . GLU   A 1 53  ? 19.010 -44.714 39.909  1.00 54.42  ? 746  GLU   A O   1 
ATOM   321  C CB  . GLU   A 1 53  ? 20.974 -46.414 38.567  1.00 54.35  ? 746  GLU   A CB  1 
ATOM   322  C CG  . GLU   A 1 53  ? 20.068 -47.587 38.269  1.00 61.16  ? 746  GLU   A CG  1 
ATOM   323  C CD  . GLU   A 1 53  ? 20.727 -48.945 38.415  1.00 69.83  ? 746  GLU   A CD  1 
ATOM   324  O OE1 . GLU   A 1 53  ? 21.595 -49.091 39.305  1.00 71.68  ? 746  GLU   A OE1 1 
ATOM   325  O OE2 . GLU   A 1 53  ? 20.380 -49.865 37.640  1.00 72.52  ? 746  GLU   A OE2 1 
ATOM   326  N N   . LEU   A 1 54  ? 18.036 -44.516 37.896  1.00 53.19  ? 747  LEU   A N   1 
ATOM   327  C CA  . LEU   A 1 54  ? 16.733 -44.158 38.443  1.00 53.74  ? 747  LEU   A CA  1 
ATOM   328  C C   . LEU   A 1 54  ? 15.979 -45.378 38.947  1.00 55.06  ? 747  LEU   A C   1 
ATOM   329  O O   . LEU   A 1 54  ? 16.168 -46.484 38.437  1.00 55.18  ? 747  LEU   A O   1 
ATOM   330  C CB  . LEU   A 1 54  ? 15.902 -43.407 37.398  1.00 53.43  ? 747  LEU   A CB  1 
ATOM   331  C CG  . LEU   A 1 54  ? 16.589 -42.179 36.776  1.00 54.50  ? 747  LEU   A CG  1 
ATOM   332  C CD1 . LEU   A 1 54  ? 15.709 -41.547 35.693  1.00 55.04  ? 747  LEU   A CD1 1 
ATOM   333  C CD2 . LEU   A 1 54  ? 16.979 -41.149 37.844  1.00 54.66  ? 747  LEU   A CD2 1 
ATOM   334  N N   . ARG   A 1 55  ? 15.080 -45.153 39.919  1.00 56.19  ? 748  ARG   A N   1 
ATOM   335  C CA  . ARG   A 1 55  ? 14.236 -46.185 40.514  1.00 58.01  ? 748  ARG   A CA  1 
ATOM   336  C C   . ARG   A 1 55  ? 13.236 -46.782 39.504  1.00 59.60  ? 748  ARG   A C   1 
ATOM   337  O O   . ARG   A 1 55  ? 12.472 -46.055 38.868  1.00 59.74  ? 748  ARG   A O   1 
ATOM   338  C CB  . ARG   A 1 55  ? 13.507 -45.640 41.752  1.00 59.21  ? 748  ARG   A CB  1 
ATOM   339  N N   . GLU   A 1 56  ? 13.277 -48.110 39.358  1.00 60.66  ? 749  GLU   A N   1 
ATOM   340  C CA  . GLU   A 1 56  ? 12.465 -48.929 38.464  1.00 62.53  ? 749  GLU   A CA  1 
ATOM   341  C C   . GLU   A 1 56  ? 10.957 -48.714 38.611  1.00 64.73  ? 749  GLU   A C   1 
ATOM   342  O O   . GLU   A 1 56  ? 10.465 -48.508 39.718  1.00 64.63  ? 749  GLU   A O   1 
ATOM   343  C CB  . GLU   A 1 56  ? 12.787 -50.405 38.723  1.00 63.99  ? 749  GLU   A CB  1 
ATOM   344  C CG  . GLU   A 1 56  ? 12.121 -51.390 37.784  1.00 67.82  ? 749  GLU   A CG  1 
ATOM   345  C CD  . GLU   A 1 56  ? 12.640 -52.803 37.929  1.00 74.56  ? 749  GLU   A CD  1 
ATOM   346  O OE1 . GLU   A 1 56  ? 13.480 -53.059 38.825  1.00 77.15  ? 749  GLU   A OE1 1 
ATOM   347  O OE2 . GLU   A 1 56  ? 12.187 -53.668 37.149  1.00 76.00  ? 749  GLU   A OE2 1 
ATOM   348  N N   . ALA   A 1 57  ? 10.239 -48.746 37.470  1.00 66.36  ? 750  ALA   A N   1 
ATOM   349  C CA  . ALA   A 1 57  ? 8.786  -48.622 37.307  1.00 68.00  ? 750  ALA   A CA  1 
ATOM   350  C C   . ALA   A 1 57  ? 8.151  -47.414 38.006  1.00 69.64  ? 750  ALA   A C   1 
ATOM   351  O O   . ALA   A 1 57  ? 7.006  -47.500 38.452  1.00 69.89  ? 750  ALA   A O   1 
ATOM   352  C CB  . ALA   A 1 57  ? 8.091  -49.914 37.735  1.00 67.89  ? 750  ALA   A CB  1 
ATOM   353  N N   . THR   A 1 58  ? 8.868  -46.299 38.086  1.00 70.85  ? 751  THR   A N   1 
ATOM   354  C CA  . THR   A 1 58  ? 8.317  -45.077 38.686  1.00 72.88  ? 751  THR   A CA  1 
ATOM   355  C C   . THR   A 1 58  ? 7.430  -44.395 37.633  1.00 74.72  ? 751  THR   A C   1 
ATOM   356  O O   . THR   A 1 58  ? 6.290  -44.022 37.914  1.00 74.88  ? 751  THR   A O   1 
ATOM   357  C CB  . THR   A 1 58  ? 9.452  -44.138 39.174  1.00 73.93  ? 751  THR   A CB  1 
ATOM   358  N N   . SER   A 1 59  ? 7.968  -44.272 36.407  1.00 75.54  ? 752  SER   A N   1 
ATOM   359  C CA  . SER   A 1 59  ? 7.331  -43.640 35.267  1.00 76.32  ? 752  SER   A CA  1 
ATOM   360  C C   . SER   A 1 59  ? 6.474  -44.625 34.465  1.00 76.69  ? 752  SER   A C   1 
ATOM   361  O O   . SER   A 1 59  ? 6.885  -45.755 34.179  1.00 76.77  ? 752  SER   A O   1 
ATOM   362  C CB  . SER   A 1 59  ? 8.401  -43.029 34.364  1.00 77.86  ? 752  SER   A CB  1 
ATOM   363  O OG  . SER   A 1 59  ? 7.877  -42.569 33.132  1.00 80.13  ? 752  SER   A OG  1 
ATOM   364  N N   . PRO   A 1 60  ? 5.300  -44.153 34.012  1.00 76.61  ? 753  PRO   A N   1 
ATOM   365  C CA  . PRO   A 1 60  ? 4.451  -45.013 33.179  1.00 76.55  ? 753  PRO   A CA  1 
ATOM   366  C C   . PRO   A 1 60  ? 4.845  -45.029 31.698  1.00 76.84  ? 753  PRO   A C   1 
ATOM   367  O O   . PRO   A 1 60  ? 4.211  -45.749 30.933  1.00 76.71  ? 753  PRO   A O   1 
ATOM   368  C CB  . PRO   A 1 60  ? 3.059  -44.414 33.372  1.00 77.14  ? 753  PRO   A CB  1 
ATOM   369  C CG  . PRO   A 1 60  ? 3.316  -42.956 33.610  1.00 77.66  ? 753  PRO   A CG  1 
ATOM   370  C CD  . PRO   A 1 60  ? 4.683  -42.826 34.239  1.00 76.16  ? 753  PRO   A CD  1 
ATOM   371  N N   . LYS   A 1 61  ? 5.868  -44.233 31.283  1.00 77.14  ? 754  LYS   A N   1 
ATOM   372  C CA  . LYS   A 1 61  ? 6.317  -44.155 29.897  1.00 77.60  ? 754  LYS   A CA  1 
ATOM   373  C C   . LYS   A 1 61  ? 7.037  -45.402 29.449  1.00 77.85  ? 754  LYS   A C   1 
ATOM   374  O O   . LYS   A 1 61  ? 7.889  -45.923 30.180  1.00 78.15  ? 754  LYS   A O   1 
ATOM   375  C CB  . LYS   A 1 61  ? 7.291  -42.994 29.691  1.00 79.49  ? 754  LYS   A CB  1 
ATOM   376  C CG  . LYS   A 1 61  ? 6.721  -41.622 29.959  1.00 83.66  ? 754  LYS   A CG  1 
ATOM   377  C CD  . LYS   A 1 61  ? 7.760  -40.559 29.534  1.00 87.99  ? 754  LYS   A CD  1 
ATOM   378  C CE  . LYS   A 1 61  ? 7.323  -39.155 29.834  1.00 92.02  ? 754  LYS   A CE  1 
ATOM   379  N NZ  . LYS   A 1 61  ? 7.240  -38.907 31.297  1.00 94.40  ? 754  LYS   A NZ  1 
ATOM   380  N N   . ALA   A 1 62  ? 6.755  -45.830 28.203  1.00 77.38  ? 755  ALA   A N   1 
ATOM   381  C CA  . ALA   A 1 62  ? 7.449  -46.953 27.588  1.00 77.24  ? 755  ALA   A CA  1 
ATOM   382  C C   . ALA   A 1 62  ? 8.869  -46.477 27.194  1.00 77.23  ? 755  ALA   A C   1 
ATOM   383  O O   . ALA   A 1 62  ? 9.134  -45.265 27.126  1.00 77.10  ? 755  ALA   A O   1 
ATOM   384  C CB  . ALA   A 1 62  ? 6.680  -47.427 26.363  1.00 77.27  ? 755  ALA   A CB  1 
ATOM   385  N N   . ASN   A 1 63  ? 9.780  -47.427 26.933  1.00 76.99  ? 756  ASN   A N   1 
ATOM   386  C CA  . ASN   A 1 63  ? 11.159 -47.121 26.567  1.00 77.22  ? 756  ASN   A CA  1 
ATOM   387  C C   . ASN   A 1 63  ? 11.286 -46.158 25.376  1.00 76.82  ? 756  ASN   A C   1 
ATOM   388  O O   . ASN   A 1 63  ? 12.205 -45.341 25.363  1.00 77.27  ? 756  ASN   A O   1 
ATOM   389  C CB  . ASN   A 1 63  ? 11.959 -48.416 26.344  1.00 78.62  ? 756  ASN   A CB  1 
ATOM   390  C CG  . ASN   A 1 63  ? 12.505 -49.058 27.622  1.00 82.35  ? 756  ASN   A CG  1 
ATOM   391  O OD1 . ASN   A 1 63  ? 13.156 -50.118 27.591  1.00 83.29  ? 756  ASN   A OD1 1 
ATOM   392  N ND2 . ASN   A 1 63  ? 12.287 -48.430 28.786  1.00 83.40  ? 756  ASN   A ND2 1 
ATOM   393  N N   . LYS   A 1 64  ? 10.351 -46.212 24.413  1.00 75.94  ? 757  LYS   A N   1 
ATOM   394  C CA  . LYS   A 1 64  ? 10.349 -45.315 23.256  1.00 75.66  ? 757  LYS   A CA  1 
ATOM   395  C C   . LYS   A 1 64  ? 10.100 -43.870 23.686  1.00 75.14  ? 757  LYS   A C   1 
ATOM   396  O O   . LYS   A 1 64  ? 10.834 -42.989 23.251  1.00 75.60  ? 757  LYS   A O   1 
ATOM   397  C CB  . LYS   A 1 64  ? 9.311  -45.755 22.210  1.00 77.62  ? 757  LYS   A CB  1 
ATOM   398  C CG  . LYS   A 1 64  ? 9.240  -44.857 20.986  1.00 81.23  ? 757  LYS   A CG  1 
ATOM   399  N N   . GLU   A 1 65  ? 9.116  -43.622 24.574  1.00 74.02  ? 758  GLU   A N   1 
ATOM   400  C CA  . GLU   A 1 65  ? 8.821  -42.268 25.072  1.00 73.21  ? 758  GLU   A CA  1 
ATOM   401  C C   . GLU   A 1 65  ? 9.909  -41.729 26.024  1.00 72.46  ? 758  GLU   A C   1 
ATOM   402  O O   . GLU   A 1 65  ? 10.075 -40.514 26.161  1.00 72.39  ? 758  GLU   A O   1 
ATOM   403  C CB  . GLU   A 1 65  ? 7.442  -42.210 25.736  1.00 74.92  ? 758  GLU   A CB  1 
ATOM   404  N N   . ILE   A 1 66  ? 10.624 -42.635 26.702  1.00 71.47  ? 759  ILE   A N   1 
ATOM   405  C CA  . ILE   A 1 66  ? 11.737 -42.271 27.570  1.00 70.67  ? 759  ILE   A CA  1 
ATOM   406  C C   . ILE   A 1 66  ? 12.873 -41.746 26.676  1.00 69.89  ? 759  ILE   A C   1 
ATOM   407  O O   . ILE   A 1 66  ? 13.488 -40.724 26.992  1.00 69.96  ? 759  ILE   A O   1 
ATOM   408  C CB  . ILE   A 1 66  ? 12.181 -43.513 28.401  1.00 71.05  ? 759  ILE   A CB  1 
ATOM   409  C CG1 . ILE   A 1 66  ? 11.141 -43.866 29.485  1.00 71.79  ? 759  ILE   A CG1 1 
ATOM   410  C CG2 . ILE   A 1 66  ? 13.584 -43.321 29.003  1.00 71.55  ? 759  ILE   A CG2 1 
ATOM   411  C CD1 . ILE   A 1 66  ? 11.341 -45.210 30.059  1.00 72.82  ? 759  ILE   A CD1 1 
ATOM   412  N N   . LEU   A 1 67  ? 13.123 -42.436 25.542  1.00 68.72  ? 760  LEU   A N   1 
ATOM   413  C CA  . LEU   A 1 67  ? 14.145 -42.073 24.575  1.00 67.96  ? 760  LEU   A CA  1 
ATOM   414  C C   . LEU   A 1 67  ? 13.893 -40.700 23.971  1.00 67.09  ? 760  LEU   A C   1 
ATOM   415  O O   . LEU   A 1 67  ? 14.834 -39.933 23.820  1.00 67.08  ? 760  LEU   A O   1 
ATOM   416  C CB  . LEU   A 1 67  ? 14.247 -43.153 23.492  1.00 68.07  ? 760  LEU   A CB  1 
ATOM   417  C CG  . LEU   A 1 67  ? 15.526 -43.992 23.447  1.00 69.35  ? 760  LEU   A CG  1 
ATOM   418  C CD1 . LEU   A 1 67  ? 16.073 -44.326 24.829  1.00 70.01  ? 760  LEU   A CD1 1 
ATOM   419  C CD2 . LEU   A 1 67  ? 15.301 -45.258 22.680  1.00 69.58  ? 760  LEU   A CD2 1 
ATOM   420  N N   . ASP   A 1 68  ? 12.629 -40.356 23.696  1.00 66.31  ? 761  ASP   A N   1 
ATOM   421  C CA  . ASP   A 1 68  ? 12.292 -39.033 23.168  1.00 65.91  ? 761  ASP   A CA  1 
ATOM   422  C C   . ASP   A 1 68  ? 12.680 -37.925 24.155  1.00 64.52  ? 761  ASP   A C   1 
ATOM   423  O O   . ASP   A 1 68  ? 13.209 -36.898 23.738  1.00 64.41  ? 761  ASP   A O   1 
ATOM   424  C CB  . ASP   A 1 68  ? 10.795 -38.932 22.838  1.00 68.21  ? 761  ASP   A CB  1 
ATOM   425  C CG  . ASP   A 1 68  ? 10.308 -39.979 21.862  1.00 75.78  ? 761  ASP   A CG  1 
ATOM   426  O OD1 . ASP   A 1 68  ? 11.159 -40.576 21.151  1.00 77.22  ? 761  ASP   A OD1 1 
ATOM   427  O OD2 . ASP   A 1 68  ? 9.069  -40.217 21.810  1.00 78.92  ? 761  ASP   A OD2 1 
ATOM   428  N N   . GLU   A 1 69  ? 12.423 -38.136 25.451  1.00 63.29  ? 762  GLU   A N   1 
ATOM   429  C CA  . GLU   A 1 69  ? 12.746 -37.160 26.489  1.00 62.78  ? 762  GLU   A CA  1 
ATOM   430  C C   . GLU   A 1 69  ? 14.269 -37.011 26.632  1.00 61.53  ? 762  GLU   A C   1 
ATOM   431  O O   . GLU   A 1 69  ? 14.783 -35.893 26.743  1.00 61.46  ? 762  GLU   A O   1 
ATOM   432  C CB  . GLU   A 1 69  ? 12.097 -37.576 27.824  1.00 65.35  ? 762  GLU   A CB  1 
ATOM   433  C CG  . GLU   A 1 69  ? 10.785 -36.867 28.132  1.00 70.25  ? 762  GLU   A CG  1 
ATOM   434  N N   . ALA   A 1 70  ? 14.985 -38.145 26.567  1.00 60.27  ? 763  ALA   A N   1 
ATOM   435  C CA  . ALA   A 1 70  ? 16.445 -38.184 26.630  1.00 59.70  ? 763  ALA   A CA  1 
ATOM   436  C C   . ALA   A 1 70  ? 17.077 -37.502 25.411  1.00 59.10  ? 763  ALA   A C   1 
ATOM   437  O O   . ALA   A 1 70  ? 18.127 -36.874 25.534  1.00 58.81  ? 763  ALA   A O   1 
ATOM   438  C CB  . ALA   A 1 70  ? 16.930 -39.619 26.739  1.00 59.60  ? 763  ALA   A CB  1 
ATOM   439  N N   . TYR   A 1 71  ? 16.424 -37.584 24.249  1.00 58.68  ? 764  TYR   A N   1 
ATOM   440  C CA  . TYR   A 1 71  ? 16.895 -36.922 23.044  1.00 58.88  ? 764  TYR   A CA  1 
ATOM   441  C C   . TYR   A 1 71  ? 16.890 -35.396 23.260  1.00 57.52  ? 764  TYR   A C   1 
ATOM   442  O O   . TYR   A 1 71  ? 17.857 -34.716 22.908  1.00 57.02  ? 764  TYR   A O   1 
ATOM   443  C CB  . TYR   A 1 71  ? 16.021 -37.318 21.847  1.00 60.03  ? 764  TYR   A CB  1 
ATOM   444  C CG  . TYR   A 1 71  ? 16.480 -36.699 20.547  1.00 62.57  ? 764  TYR   A CG  1 
ATOM   445  C CD1 . TYR   A 1 71  ? 15.988 -35.467 20.127  1.00 64.21  ? 764  TYR   A CD1 1 
ATOM   446  C CD2 . TYR   A 1 71  ? 17.417 -37.334 19.744  1.00 64.29  ? 764  TYR   A CD2 1 
ATOM   447  C CE1 . TYR   A 1 71  ? 16.434 -34.874 18.953  1.00 65.59  ? 764  TYR   A CE1 1 
ATOM   448  C CE2 . TYR   A 1 71  ? 17.852 -36.762 18.552  1.00 65.78  ? 764  TYR   A CE2 1 
ATOM   449  C CZ  . TYR   A 1 71  ? 17.358 -35.529 18.160  1.00 67.02  ? 764  TYR   A CZ  1 
ATOM   450  O OH  . TYR   A 1 71  ? 17.765 -34.964 16.974  1.00 69.40  ? 764  TYR   A OH  1 
ATOM   451  N N   . VAL   A 1 72  ? 15.824 -34.881 23.889  1.00 56.44  ? 765  VAL   A N   1 
ATOM   452  C CA  . VAL   A 1 72  ? 15.703 -33.464 24.204  1.00 55.65  ? 765  VAL   A CA  1 
ATOM   453  C C   . VAL   A 1 72  ? 16.802 -33.032 25.179  1.00 55.15  ? 765  VAL   A C   1 
ATOM   454  O O   . VAL   A 1 72  ? 17.452 -32.016 24.935  1.00 55.40  ? 765  VAL   A O   1 
ATOM   455  C CB  . VAL   A 1 72  ? 14.289 -33.119 24.725  1.00 55.78  ? 765  VAL   A CB  1 
ATOM   456  C CG1 . VAL   A 1 72  ? 14.223 -31.673 25.196  1.00 55.77  ? 765  VAL   A CG1 1 
ATOM   457  C CG2 . VAL   A 1 72  ? 13.240 -33.388 23.656  1.00 55.91  ? 765  VAL   A CG2 1 
ATOM   458  N N   . MET   A 1 73  ? 17.067 -33.827 26.236  1.00 54.40  ? 766  MET   A N   1 
ATOM   459  C CA  . MET   A 1 73  ? 18.139 -33.520 27.184  1.00 54.06  ? 766  MET   A CA  1 
ATOM   460  C C   . MET   A 1 73  ? 19.496 -33.488 26.475  1.00 53.03  ? 766  MET   A C   1 
ATOM   461  O O   . MET   A 1 73  ? 20.337 -32.660 26.816  1.00 53.31  ? 766  MET   A O   1 
ATOM   462  C CB  . MET   A 1 73  ? 18.219 -34.562 28.313  1.00 55.37  ? 766  MET   A CB  1 
ATOM   463  C CG  . MET   A 1 73  ? 16.996 -34.649 29.196  1.00 59.12  ? 766  MET   A CG  1 
ATOM   464  S SD  . MET   A 1 73  ? 17.258 -35.957 30.442  1.00 70.29  ? 766  MET   A SD  1 
ATOM   465  C CE  . MET   A 1 73  ? 15.686 -36.774 30.393  1.00 69.75  ? 766  MET   A CE  1 
ATOM   466  N N   . ALA   A 1 74  ? 19.710 -34.389 25.492  1.00 51.76  ? 767  ALA   A N   1 
ATOM   467  C CA  . ALA   A 1 74  ? 20.957 -34.468 24.724  1.00 50.90  ? 767  ALA   A CA  1 
ATOM   468  C C   . ALA   A 1 74  ? 21.109 -33.339 23.718  1.00 50.64  ? 767  ALA   A C   1 
ATOM   469  O O   . ALA   A 1 74  ? 22.232 -32.933 23.420  1.00 51.27  ? 767  ALA   A O   1 
ATOM   470  C CB  . ALA   A 1 74  ? 21.057 -35.806 24.016  1.00 50.66  ? 767  ALA   A CB  1 
ATOM   471  N N   . SER   A 1 75  ? 19.987 -32.828 23.183  1.00 49.65  ? 768  SER   A N   1 
ATOM   472  C CA  . SER   A 1 75  ? 19.987 -31.741 22.207  1.00 49.41  ? 768  SER   A CA  1 
ATOM   473  C C   . SER   A 1 75  ? 20.541 -30.430 22.786  1.00 48.78  ? 768  SER   A C   1 
ATOM   474  O O   . SER   A 1 75  ? 21.048 -29.616 22.047  1.00 49.00  ? 768  SER   A O   1 
ATOM   475  C CB  . SER   A 1 75  ? 18.586 -31.521 21.646  1.00 51.07  ? 768  SER   A CB  1 
ATOM   476  O OG  . SER   A 1 75  ? 17.727 -30.943 22.616  1.00 54.00  ? 768  SER   A OG  1 
ATOM   477  N N   . VAL   A 1 76  ? 20.467 -30.246 24.098  1.00 48.22  ? 769  VAL   A N   1 
ATOM   478  C CA  . VAL   A 1 76  ? 20.961 -29.097 24.841  1.00 48.41  ? 769  VAL   A CA  1 
ATOM   479  C C   . VAL   A 1 76  ? 22.484 -28.895 24.638  1.00 49.24  ? 769  VAL   A C   1 
ATOM   480  O O   . VAL   A 1 76  ? 22.955 -27.761 24.667  1.00 49.95  ? 769  VAL   A O   1 
ATOM   481  C CB  . VAL   A 1 76  ? 20.564 -29.281 26.316  1.00 48.86  ? 769  VAL   A CB  1 
ATOM   482  C CG1 . VAL   A 1 76  ? 21.190 -28.217 27.209  1.00 49.46  ? 769  VAL   A CG1 1 
ATOM   483  C CG2 . VAL   A 1 76  ? 19.054 -29.292 26.459  1.00 48.94  ? 769  VAL   A CG2 1 
ATOM   484  N N   . ASP   A 1 77  ? 23.240 -29.972 24.334  1.00 48.71  ? 770  ASP   A N   1 
ATOM   485  C CA  . ASP   A 1 77  ? 24.666 -29.871 23.994  1.00 48.49  ? 770  ASP   A CA  1 
ATOM   486  C C   . ASP   A 1 77  ? 24.915 -29.094 22.679  1.00 48.05  ? 770  ASP   A C   1 
ATOM   487  O O   . ASP   A 1 77  ? 26.064 -28.800 22.359  1.00 48.27  ? 770  ASP   A O   1 
ATOM   488  C CB  . ASP   A 1 77  ? 25.279 -31.262 23.811  1.00 50.65  ? 770  ASP   A CB  1 
ATOM   489  C CG  . ASP   A 1 77  ? 25.322 -32.097 25.059  1.00 56.23  ? 770  ASP   A CG  1 
ATOM   490  N N   . ASN   A 1 78  ? 23.860 -28.762 21.915  1.00 47.54  ? 771  ASN   A N   1 
ATOM   491  C CA  . ASN   A 1 78  ? 24.003 -28.032 20.664  1.00 47.79  ? 771  ASN   A CA  1 
ATOM   492  C C   . ASN   A 1 78  ? 23.172 -26.737 20.676  1.00 46.98  ? 771  ASN   A C   1 
ATOM   493  O O   . ASN   A 1 78  ? 21.948 -26.796 20.753  1.00 46.92  ? 771  ASN   A O   1 
ATOM   494  C CB  . ASN   A 1 78  ? 23.602 -28.951 19.505  1.00 49.20  ? 771  ASN   A CB  1 
ATOM   495  C CG  . ASN   A 1 78  ? 23.630 -28.315 18.156  1.00 52.96  ? 771  ASN   A CG  1 
ATOM   496  O OD1 . ASN   A 1 78  ? 24.308 -27.331 17.922  1.00 54.63  ? 771  ASN   A OD1 1 
ATOM   497  N ND2 . ASN   A 1 78  ? 22.880 -28.866 17.233  1.00 54.05  ? 771  ASN   A ND2 1 
ATOM   498  N N   . PRO   A 1 79  ? 23.804 -25.552 20.592  1.00 46.45  ? 772  PRO   A N   1 
ATOM   499  C CA  . PRO   A 1 79  ? 25.250 -25.306 20.484  1.00 45.82  ? 772  PRO   A CA  1 
ATOM   500  C C   . PRO   A 1 79  ? 26.038 -25.475 21.786  1.00 45.20  ? 772  PRO   A C   1 
ATOM   501  O O   . PRO   A 1 79  ? 27.263 -25.586 21.741  1.00 45.94  ? 772  PRO   A O   1 
ATOM   502  C CB  . PRO   A 1 79  ? 25.304 -23.877 19.935  1.00 46.29  ? 772  PRO   A CB  1 
ATOM   503  C CG  . PRO   A 1 79  ? 24.111 -23.220 20.546  1.00 46.86  ? 772  PRO   A CG  1 
ATOM   504  C CD  . PRO   A 1 79  ? 23.044 -24.283 20.569  1.00 45.57  ? 772  PRO   A CD  1 
ATOM   505  N N   . GLY   A 1 80  ? 25.345 -25.523 22.921  1.00 43.81  ? 773  GLY   A N   1 
ATOM   506  C CA  . GLY   A 1 80  ? 25.962 -25.724 24.224  1.00 43.25  ? 773  GLY   A CA  1 
ATOM   507  C C   . GLY   A 1 80  ? 26.278 -24.473 25.026  1.00 42.94  ? 773  GLY   A C   1 
ATOM   508  O O   . GLY   A 1 80  ? 26.311 -23.369 24.484  1.00 43.43  ? 773  GLY   A O   1 
ATOM   509  N N   . ASN   A 1 81  ? 26.518 -24.644 26.342  1.00 42.12  ? 774  ASN   A N   1 
ATOM   510  C CA  . ASN   A 1 81  ? 26.869 -23.594 27.287  1.00 41.74  ? 774  ASN   A CA  1 
ATOM   511  C C   . ASN   A 1 81  ? 27.770 -24.218 28.357  1.00 41.97  ? 774  ASN   A C   1 
ATOM   512  O O   . ASN   A 1 81  ? 27.461 -25.304 28.851  1.00 42.77  ? 774  ASN   A O   1 
ATOM   513  C CB  . ASN   A 1 81  ? 25.618 -23.050 27.946  1.00 41.81  ? 774  ASN   A CB  1 
ATOM   514  C CG  . ASN   A 1 81  ? 25.842 -21.794 28.735  1.00 42.02  ? 774  ASN   A CG  1 
ATOM   515  O OD1 . ASN   A 1 81  ? 25.776 -20.678 28.195  1.00 43.93  ? 774  ASN   A OD1 1 
ATOM   516  N ND2 . ASN   A 1 81  ? 26.105 -21.947 30.018  1.00 39.50  ? 774  ASN   A ND2 1 
ATOM   517  N N   . PRO   A 1 82  ? 28.842 -23.529 28.785  1.00 40.57  ? 775  PRO   A N   1 
ATOM   518  C CA  . PRO   A 1 82  ? 29.722 -24.134 29.802  1.00 40.08  ? 775  PRO   A CA  1 
ATOM   519  C C   . PRO   A 1 82  ? 29.080 -24.391 31.159  1.00 40.07  ? 775  PRO   A C   1 
ATOM   520  O O   . PRO   A 1 82  ? 29.630 -25.145 31.951  1.00 40.18  ? 775  PRO   A O   1 
ATOM   521  C CB  . PRO   A 1 82  ? 30.903 -23.150 29.919  1.00 40.70  ? 775  PRO   A CB  1 
ATOM   522  C CG  . PRO   A 1 82  ? 30.481 -21.898 29.198  1.00 40.61  ? 775  PRO   A CG  1 
ATOM   523  C CD  . PRO   A 1 82  ? 29.347 -22.235 28.281  1.00 39.30  ? 775  PRO   A CD  1 
ATOM   524  N N   . HIS   A 1 83  ? 27.940 -23.762 31.443  1.00 39.98  ? 776  HIS   A N   1 
ATOM   525  C CA  . HIS   A 1 83  ? 27.292 -23.898 32.744  1.00 40.15  ? 776  HIS   A CA  1 
ATOM   526  C C   . HIS   A 1 83  ? 26.060 -24.778 32.735  1.00 40.97  ? 776  HIS   A C   1 
ATOM   527  O O   . HIS   A 1 83  ? 25.229 -24.682 33.622  1.00 40.99  ? 776  HIS   A O   1 
ATOM   528  C CB  . HIS   A 1 83  ? 27.002 -22.515 33.320  1.00 40.32  ? 776  HIS   A CB  1 
ATOM   529  C CG  . HIS   A 1 83  ? 28.251 -21.697 33.371  1.00 40.94  ? 776  HIS   A CG  1 
ATOM   530  N ND1 . HIS   A 1 83  ? 28.437 -20.612 32.534  1.00 42.60  ? 776  HIS   A ND1 1 
ATOM   531  C CD2 . HIS   A 1 83  ? 29.409 -21.952 34.015  1.00 41.24  ? 776  HIS   A CD2 1 
ATOM   532  C CE1 . HIS   A 1 83  ? 29.669 -20.191 32.762  1.00 42.61  ? 776  HIS   A CE1 1 
ATOM   533  N NE2 . HIS   A 1 83  ? 30.294 -20.973 33.637  1.00 42.56  ? 776  HIS   A NE2 1 
ATOM   534  N N   . VAL   A 1 84  ? 26.000 -25.704 31.799  1.00 42.01  ? 777  VAL   A N   1 
ATOM   535  C CA  . VAL   A 1 84  ? 24.921 -26.659 31.668  1.00 44.05  ? 777  VAL   A CA  1 
ATOM   536  C C   . VAL   A 1 84  ? 25.596 -28.033 31.437  1.00 46.52  ? 777  VAL   A C   1 
ATOM   537  O O   . VAL   A 1 84  ? 26.495 -28.140 30.607  1.00 47.35  ? 777  VAL   A O   1 
ATOM   538  C CB  . VAL   A 1 84  ? 23.988 -26.237 30.499  1.00 44.64  ? 777  VAL   A CB  1 
ATOM   539  C CG1 . VAL   A 1 84  ? 23.160 -27.392 30.015  1.00 45.85  ? 777  VAL   A CG1 1 
ATOM   540  C CG2 . VAL   A 1 84  ? 23.085 -25.069 30.886  1.00 44.53  ? 777  VAL   A CG2 1 
ATOM   541  N N   . CYS   A 1 85  ? 25.206 -29.062 32.202  1.00 47.36  ? 778  CYS   A N   1 
ATOM   542  C CA  . CYS   A 1 85  ? 25.767 -30.403 32.037  1.00 48.40  ? 778  CYS   A CA  1 
ATOM   543  C C   . CYS   A 1 85  ? 25.424 -31.029 30.680  1.00 48.63  ? 778  CYS   A C   1 
ATOM   544  O O   . CYS   A 1 85  ? 24.527 -30.561 29.978  1.00 48.94  ? 778  CYS   A O   1 
ATOM   545  C CB  . CYS   A 1 85  ? 25.361 -31.315 33.192  1.00 50.17  ? 778  CYS   A CB  1 
ATOM   546  S SG  . CYS   A 1 85  ? 26.195 -30.944 34.758  1.00 56.58  ? 778  CYS   A SG  1 
ATOM   547  N N   . ARG   A 1 86  ? 26.184 -32.060 30.294  1.00 48.37  ? 779  ARG   A N   1 
ATOM   548  C CA  . ARG   A 1 86  ? 26.040 -32.766 29.032  1.00 48.52  ? 779  ARG   A CA  1 
ATOM   549  C C   . ARG   A 1 86  ? 25.678 -34.225 29.252  1.00 48.32  ? 779  ARG   A C   1 
ATOM   550  O O   . ARG   A 1 86  ? 26.490 -34.960 29.803  1.00 49.05  ? 779  ARG   A O   1 
ATOM   551  C CB  . ARG   A 1 86  ? 27.357 -32.692 28.243  1.00 50.40  ? 779  ARG   A CB  1 
ATOM   552  C CG  . ARG   A 1 86  ? 27.592 -31.323 27.639  1.00 56.01  ? 779  ARG   A CG  1 
ATOM   553  C CD  . ARG   A 1 86  ? 28.990 -30.798 27.865  1.00 61.09  ? 779  ARG   A CD  1 
ATOM   554  N NE  . ARG   A 1 86  ? 29.956 -31.316 26.891  1.00 65.51  ? 779  ARG   A NE  1 
ATOM   555  C CZ  . ARG   A 1 86  ? 31.021 -30.639 26.460  1.00 68.04  ? 779  ARG   A CZ  1 
ATOM   556  N NH1 . ARG   A 1 86  ? 31.257 -29.406 26.898  1.00 66.13  ? 779  ARG   A NH1 1 
ATOM   557  N NH2 . ARG   A 1 86  ? 31.852 -31.186 25.584  1.00 69.29  ? 779  ARG   A NH2 1 
ATOM   558  N N   . LEU   A 1 87  ? 24.498 -34.661 28.792  1.00 47.32  ? 780  LEU   A N   1 
ATOM   559  C CA  . LEU   A 1 87  ? 24.128 -36.069 28.872  1.00 46.96  ? 780  LEU   A CA  1 
ATOM   560  C C   . LEU   A 1 87  ? 24.963 -36.819 27.828  1.00 47.32  ? 780  LEU   A C   1 
ATOM   561  O O   . LEU   A 1 87  ? 24.806 -36.579 26.628  1.00 47.93  ? 780  LEU   A O   1 
ATOM   562  C CB  . LEU   A 1 87  ? 22.628 -36.288 28.585  1.00 46.30  ? 780  LEU   A CB  1 
ATOM   563  C CG  . LEU   A 1 87  ? 22.162 -37.727 28.799  1.00 46.61  ? 780  LEU   A CG  1 
ATOM   564  C CD1 . LEU   A 1 87  ? 22.229 -38.102 30.257  1.00 46.43  ? 780  LEU   A CD1 1 
ATOM   565  C CD2 . LEU   A 1 87  ? 20.759 -37.958 28.252  1.00 46.89  ? 780  LEU   A CD2 1 
ATOM   566  N N   . LEU   A 1 88  ? 25.886 -37.672 28.281  1.00 46.76  ? 781  LEU   A N   1 
ATOM   567  C CA  . LEU   A 1 88  ? 26.747 -38.453 27.403  1.00 47.43  ? 781  LEU   A CA  1 
ATOM   568  C C   . LEU   A 1 88  ? 26.037 -39.662 26.789  1.00 48.50  ? 781  LEU   A C   1 
ATOM   569  O O   . LEU   A 1 88  ? 26.422 -40.114 25.718  1.00 49.08  ? 781  LEU   A O   1 
ATOM   570  C CB  . LEU   A 1 88  ? 27.991 -38.947 28.155  1.00 47.57  ? 781  LEU   A CB  1 
ATOM   571  C CG  . LEU   A 1 88  ? 28.933 -37.898 28.715  1.00 49.36  ? 781  LEU   A CG  1 
ATOM   572  C CD1 . LEU   A 1 88  ? 30.130 -38.557 29.341  1.00 50.26  ? 781  LEU   A CD1 1 
ATOM   573  C CD2 . LEU   A 1 88  ? 29.398 -36.938 27.640  1.00 50.20  ? 781  LEU   A CD2 1 
ATOM   574  N N   . GLY   A 1 89  ? 25.067 -40.217 27.494  1.00 48.46  ? 782  GLY   A N   1 
ATOM   575  C CA  . GLY   A 1 89  ? 24.354 -41.387 27.023  1.00 48.87  ? 782  GLY   A CA  1 
ATOM   576  C C   . GLY   A 1 89  ? 23.301 -41.907 27.969  1.00 49.23  ? 782  GLY   A C   1 
ATOM   577  O O   . GLY   A 1 89  ? 23.178 -41.444 29.100  1.00 48.94  ? 782  GLY   A O   1 
ATOM   578  N N   . ILE   A 1 90  ? 22.535 -42.877 27.500  1.00 49.84  ? 783  ILE   A N   1 
ATOM   579  C CA  . ILE   A 1 90  ? 21.483 -43.489 28.291  1.00 51.12  ? 783  ILE   A CA  1 
ATOM   580  C C   . ILE   A 1 90  ? 21.513 -44.995 28.113  1.00 51.48  ? 783  ILE   A C   1 
ATOM   581  O O   . ILE   A 1 90  ? 21.744 -45.490 27.012  1.00 50.91  ? 783  ILE   A O   1 
ATOM   582  C CB  . ILE   A 1 90  ? 20.083 -42.873 27.965  1.00 52.23  ? 783  ILE   A CB  1 
ATOM   583  C CG1 . ILE   A 1 90  ? 18.976 -43.464 28.859  1.00 53.18  ? 783  ILE   A CG1 1 
ATOM   584  C CG2 . ILE   A 1 90  ? 19.740 -43.008 26.486  1.00 52.83  ? 783  ILE   A CG2 1 
ATOM   585  C CD1 . ILE   A 1 90  ? 17.627 -42.824 28.717  1.00 54.58  ? 783  ILE   A CD1 1 
ATOM   586  N N   . CYS   A 1 91  ? 21.345 -45.722 29.214  1.00 52.59  ? 784  CYS   A N   1 
ATOM   587  C CA  . CYS   A 1 91  ? 21.290 -47.165 29.177  1.00 54.47  ? 784  CYS   A CA  1 
ATOM   588  C C   . CYS   A 1 91  ? 19.931 -47.615 29.693  1.00 55.96  ? 784  CYS   A C   1 
ATOM   589  O O   . CYS   A 1 91  ? 19.628 -47.429 30.866  1.00 55.91  ? 784  CYS   A O   1 
ATOM   590  C CB  . CYS   A 1 91  ? 22.427 -47.792 29.971  1.00 55.80  ? 784  CYS   A CB  1 
ATOM   591  S SG  . CYS   A 1 91  ? 22.497 -49.599 29.838  1.00 61.99  ? 784  CYS   A SG  1 
ATOM   592  N N   . LEU   A 1 92  ? 19.095 -48.170 28.812  1.00 57.21  ? 785  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 92  ? 17.765 -48.625 29.213  1.00 58.73  ? 785  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 92  ? 17.650 -50.123 29.366  1.00 59.43  ? 785  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 92  ? 17.667 -50.858 28.381  1.00 59.48  ? 785  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 92  ? 16.679 -48.153 28.237  1.00 59.55  ? 785  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 92  ? 16.290 -46.668 28.224  1.00 61.62  ? 785  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 92  ? 15.016 -46.460 27.416  1.00 62.08  ? 785  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 92  ? 16.067 -46.145 29.631  1.00 62.54  ? 785  LEU   A CD2 1 
ATOM   600  N N   . THR   A 1 93  ? 17.507 -50.577 30.604  1.00 59.68  ? 786  THR   A N   1 
ATOM   601  C CA  . THR   A 1 93  ? 17.251 -51.981 30.931  1.00 60.30  ? 786  THR   A CA  1 
ATOM   602  C C   . THR   A 1 93  ? 15.914 -51.917 31.744  1.00 59.97  ? 786  THR   A C   1 
ATOM   603  O O   . THR   A 1 93  ? 15.010 -51.177 31.317  1.00 60.06  ? 786  THR   A O   1 
ATOM   604  C CB  . THR   A 1 93  ? 18.516 -52.611 31.607  1.00 62.25  ? 786  THR   A CB  1 
ATOM   605  O OG1 . THR   A 1 93  ? 18.741 -51.961 32.870  1.00 63.45  ? 786  THR   A OG1 1 
ATOM   606  C CG2 . THR   A 1 93  ? 19.753 -52.551 30.719  1.00 62.54  ? 786  THR   A CG2 1 
ATOM   607  N N   . SER   A 1 94  ? 15.784 -52.623 32.908  1.00 59.34  ? 787  SER   A N   1 
ATOM   608  C CA  . SER   A 1 94  ? 14.607 -52.487 33.769  1.00 59.03  ? 787  SER   A CA  1 
ATOM   609  C C   . SER   A 1 94  ? 14.570 -51.078 34.386  1.00 58.50  ? 787  SER   A C   1 
ATOM   610  O O   . SER   A 1 94  ? 13.495 -50.625 34.760  1.00 58.85  ? 787  SER   A O   1 
ATOM   611  C CB  . SER   A 1 94  ? 14.622 -53.514 34.896  1.00 60.35  ? 787  SER   A CB  1 
ATOM   612  O OG  . SER   A 1 94  ? 14.829 -54.841 34.460  1.00 62.83  ? 787  SER   A OG  1 
ATOM   613  N N   . THR   A 1 95  ? 15.745 -50.396 34.509  1.00 57.65  ? 788  THR   A N   1 
ATOM   614  C CA  . THR   A 1 95  ? 15.881 -49.042 35.037  1.00 57.06  ? 788  THR   A CA  1 
ATOM   615  C C   . THR   A 1 95  ? 16.449 -48.106 33.957  1.00 55.44  ? 788  THR   A C   1 
ATOM   616  O O   . THR   A 1 95  ? 16.988 -48.552 32.947  1.00 55.48  ? 788  THR   A O   1 
ATOM   617  C CB  . THR   A 1 95  ? 16.820 -49.055 36.278  1.00 58.96  ? 788  THR   A CB  1 
ATOM   618  O OG1 . THR   A 1 95  ? 18.159 -49.350 35.860  1.00 60.22  ? 788  THR   A OG1 1 
ATOM   619  C CG2 . THR   A 1 95  ? 16.369 -50.020 37.358  1.00 59.32  ? 788  THR   A CG2 1 
ATOM   620  N N   . VAL   A 1 96  ? 16.357 -46.805 34.196  1.00 53.93  ? 789  VAL   A N   1 
ATOM   621  C CA  . VAL   A 1 96  ? 16.953 -45.805 33.328  1.00 52.83  ? 789  VAL   A CA  1 
ATOM   622  C C   . VAL   A 1 96  ? 18.309 -45.458 33.915  1.00 51.28  ? 789  VAL   A C   1 
ATOM   623  O O   . VAL   A 1 96  ? 18.400 -45.193 35.112  1.00 51.30  ? 789  VAL   A O   1 
ATOM   624  C CB  . VAL   A 1 96  ? 16.063 -44.547 33.259  1.00 53.31  ? 789  VAL   A CB  1 
ATOM   625  C CG1 . VAL   A 1 96  ? 16.689 -43.487 32.370  1.00 53.30  ? 789  VAL   A CG1 1 
ATOM   626  C CG2 . VAL   A 1 96  ? 14.654 -44.907 32.783  1.00 53.99  ? 789  VAL   A CG2 1 
ATOM   627  N N   . GLN   A 1 97  ? 19.363 -45.483 33.101  1.00 49.76  ? 790  GLN   A N   1 
ATOM   628  C CA  . GLN   A 1 97  ? 20.688 -45.085 33.562  1.00 48.43  ? 790  GLN   A CA  1 
ATOM   629  C C   . GLN   A 1 97  ? 21.154 -43.912 32.725  1.00 47.05  ? 790  GLN   A C   1 
ATOM   630  O O   . GLN   A 1 97  ? 21.128 -43.985 31.508  1.00 46.58  ? 790  GLN   A O   1 
ATOM   631  C CB  . GLN   A 1 97  ? 21.671 -46.243 33.516  1.00 49.32  ? 790  GLN   A CB  1 
ATOM   632  C CG  . GLN   A 1 97  ? 21.481 -47.162 34.697  1.00 52.92  ? 790  GLN   A CG  1 
ATOM   633  C CD  . GLN   A 1 97  ? 22.470 -48.290 34.704  1.00 57.71  ? 790  GLN   A CD  1 
ATOM   634  O OE1 . GLN   A 1 97  ? 23.444 -48.278 35.449  1.00 59.92  ? 790  GLN   A OE1 1 
ATOM   635  N NE2 . GLN   A 1 97  ? 22.248 -49.290 33.883  1.00 57.59  ? 790  GLN   A NE2 1 
ATOM   636  N N   . LEU   A 1 98  ? 21.472 -42.793 33.372  1.00 46.08  ? 791  LEU   A N   1 
ATOM   637  C CA  . LEU   A 1 98  ? 21.915 -41.592 32.672  1.00 45.36  ? 791  LEU   A CA  1 
ATOM   638  C C   . LEU   A 1 98  ? 23.415 -41.420 32.910  1.00 45.34  ? 791  LEU   A C   1 
ATOM   639  O O   . LEU   A 1 98  ? 23.865 -41.568 34.039  1.00 45.34  ? 791  LEU   A O   1 
ATOM   640  C CB  . LEU   A 1 98  ? 21.141 -40.371 33.183  1.00 44.87  ? 791  LEU   A CB  1 
ATOM   641  C CG  . LEU   A 1 98  ? 19.620 -40.467 33.075  1.00 45.81  ? 791  LEU   A CG  1 
ATOM   642  C CD1 . LEU   A 1 98  ? 18.950 -39.273 33.727  1.00 46.22  ? 791  LEU   A CD1 1 
ATOM   643  C CD2 . LEU   A 1 98  ? 19.168 -40.599 31.637  1.00 46.21  ? 791  LEU   A CD2 1 
ATOM   644  N N   . ILE   A 1 99  ? 24.193 -41.115 31.865  1.00 45.02  ? 792  ILE   A N   1 
ATOM   645  C CA  . ILE   A 1 99  ? 25.640 -40.988 31.997  1.00 45.32  ? 792  ILE   A CA  1 
ATOM   646  C C   . ILE   A 1 99  ? 26.112 -39.579 31.653  1.00 46.25  ? 792  ILE   A C   1 
ATOM   647  O O   . ILE   A 1 99  ? 25.587 -38.981 30.732  1.00 46.48  ? 792  ILE   A O   1 
ATOM   648  C CB  . ILE   A 1 99  ? 26.336 -42.097 31.149  1.00 45.66  ? 792  ILE   A CB  1 
ATOM   649  C CG1 . ILE   A 1 99  ? 26.051 -43.511 31.715  1.00 46.00  ? 792  ILE   A CG1 1 
ATOM   650  C CG2 . ILE   A 1 99  ? 27.841 -41.869 30.988  1.00 46.26  ? 792  ILE   A CG2 1 
ATOM   651  C CD1 . ILE   A 1 99  ? 24.985 -44.288 30.951  1.00 46.78  ? 792  ILE   A CD1 1 
ATOM   652  N N   . THR   A 1 100 ? 27.018 -39.014 32.456  1.00 46.83  ? 793  THR   A N   1 
ATOM   653  C CA  . THR   A 1 100 ? 27.647 -37.696 32.257  1.00 48.22  ? 793  THR   A CA  1 
ATOM   654  C C   . THR   A 1 100 ? 29.111 -37.756 32.702  1.00 48.33  ? 793  THR   A C   1 
ATOM   655  O O   . THR   A 1 100 ? 29.506 -38.700 33.359  1.00 47.92  ? 793  THR   A O   1 
ATOM   656  C CB  . THR   A 1 100 ? 26.955 -36.555 33.064  1.00 50.85  ? 793  THR   A CB  1 
ATOM   657  O OG1 . THR   A 1 100 ? 26.864 -36.878 34.457  1.00 52.95  ? 793  THR   A OG1 1 
ATOM   658  C CG2 . THR   A 1 100 ? 25.679 -36.173 32.522  1.00 51.84  ? 793  THR   A CG2 1 
ATOM   659  N N   . GLN   A 1 101 ? 29.910 -36.728 32.374  1.00 49.10  ? 794  GLN   A N   1 
ATOM   660  C CA  . GLN   A 1 101 ? 31.281 -36.608 32.834  1.00 50.31  ? 794  GLN   A CA  1 
ATOM   661  C C   . GLN   A 1 101 ? 31.239 -36.422 34.363  1.00 51.26  ? 794  GLN   A C   1 
ATOM   662  O O   . GLN   A 1 101 ? 30.343 -35.747 34.884  1.00 51.75  ? 794  GLN   A O   1 
ATOM   663  C CB  . GLN   A 1 101 ? 31.942 -35.395 32.155  1.00 51.71  ? 794  GLN   A CB  1 
ATOM   664  N N   . LEU   A 1 102 ? 32.146 -37.068 35.071  1.00 51.58  ? 795  LEU   A N   1 
ATOM   665  C CA  . LEU   A 1 102 ? 32.191 -36.982 36.518  1.00 53.03  ? 795  LEU   A CA  1 
ATOM   666  C C   . LEU   A 1 102 ? 32.625 -35.578 36.992  1.00 54.94  ? 795  LEU   A C   1 
ATOM   667  O O   . LEU   A 1 102 ? 33.663 -35.088 36.546  1.00 55.42  ? 795  LEU   A O   1 
ATOM   668  C CB  . LEU   A 1 102 ? 33.157 -38.057 37.013  1.00 53.37  ? 795  LEU   A CB  1 
ATOM   669  C CG  . LEU   A 1 102 ? 33.435 -38.138 38.498  1.00 54.54  ? 795  LEU   A CG  1 
ATOM   670  C CD1 . LEU   A 1 102 ? 32.160 -38.370 39.287  1.00 54.93  ? 795  LEU   A CD1 1 
ATOM   671  C CD2 . LEU   A 1 102 ? 34.429 -39.212 38.763  1.00 55.08  ? 795  LEU   A CD2 1 
ATOM   672  N N   . MET   A 1 103 ? 31.797 -34.916 37.859  1.00 55.99  ? 796  MET   A N   1 
ATOM   673  C CA  . MET   A 1 103 ? 32.078 -33.611 38.490  1.00 57.01  ? 796  MET   A CA  1 
ATOM   674  C C   . MET   A 1 103 ? 32.691 -33.981 39.845  1.00 57.46  ? 796  MET   A C   1 
ATOM   675  O O   . MET   A 1 103 ? 32.011 -34.508 40.724  1.00 57.47  ? 796  MET   A O   1 
ATOM   676  C CB  . MET   A 1 103 ? 30.799 -32.765 38.641  1.00 57.92  ? 796  MET   A CB  1 
ATOM   677  C CG  . MET   A 1 103 ? 30.133 -32.470 37.307  1.00 60.21  ? 796  MET   A CG  1 
ATOM   678  S SD  . MET   A 1 103 ? 31.041 -31.249 36.320  1.00 67.53  ? 796  MET   A SD  1 
ATOM   679  C CE  . MET   A 1 103 ? 31.570 -32.228 34.951  1.00 65.68  ? 796  MET   A CE  1 
ATOM   680  N N   . PRO   A 1 104 ? 34.020 -33.859 39.960  1.00 57.72  ? 797  PRO   A N   1 
ATOM   681  C CA  . PRO   A 1 104 ? 34.707 -34.387 41.152  1.00 57.25  ? 797  PRO   A CA  1 
ATOM   682  C C   . PRO   A 1 104 ? 34.394 -33.723 42.488  1.00 55.92  ? 797  PRO   A C   1 
ATOM   683  O O   . PRO   A 1 104 ? 34.594 -34.354 43.527  1.00 55.62  ? 797  PRO   A O   1 
ATOM   684  C CB  . PRO   A 1 104 ? 36.196 -34.248 40.803  1.00 58.46  ? 797  PRO   A CB  1 
ATOM   685  C CG  . PRO   A 1 104 ? 36.246 -34.005 39.326  1.00 59.24  ? 797  PRO   A CG  1 
ATOM   686  C CD  . PRO   A 1 104 ? 34.975 -33.299 38.983  1.00 57.69  ? 797  PRO   A CD  1 
ATOM   687  N N   . PHE   A 1 105 ? 33.920 -32.474 42.473  1.00 54.78  ? 798  PHE   A N   1 
ATOM   688  C CA  . PHE   A 1 105 ? 33.613 -31.789 43.722  1.00 54.16  ? 798  PHE   A CA  1 
ATOM   689  C C   . PHE   A 1 105 ? 32.146 -31.904 44.161  1.00 52.63  ? 798  PHE   A C   1 
ATOM   690  O O   . PHE   A 1 105 ? 31.770 -31.264 45.136  1.00 53.02  ? 798  PHE   A O   1 
ATOM   691  C CB  . PHE   A 1 105 ? 34.058 -30.328 43.678  1.00 54.62  ? 798  PHE   A CB  1 
ATOM   692  C CG  . PHE   A 1 105 ? 35.534 -30.133 43.443  1.00 55.64  ? 798  PHE   A CG  1 
ATOM   693  C CD1 . PHE   A 1 105 ? 36.430 -30.150 44.496  1.00 57.12  ? 798  PHE   A CD1 1 
ATOM   694  C CD2 . PHE   A 1 105 ? 36.022 -29.902 42.175  1.00 56.41  ? 798  PHE   A CD2 1 
ATOM   695  C CE1 . PHE   A 1 105 ? 37.795 -29.983 44.272  1.00 58.11  ? 798  PHE   A CE1 1 
ATOM   696  C CE2 . PHE   A 1 105 ? 37.380 -29.704 41.955  1.00 57.40  ? 798  PHE   A CE2 1 
ATOM   697  C CZ  . PHE   A 1 105 ? 38.260 -29.748 43.005  1.00 57.70  ? 798  PHE   A CZ  1 
ATOM   698  N N   . GLY   A 1 106 ? 31.353 -32.732 43.489  1.00 51.04  ? 799  GLY   A N   1 
ATOM   699  C CA  . GLY   A 1 106 ? 29.959 -32.928 43.851  1.00 50.50  ? 799  GLY   A CA  1 
ATOM   700  C C   . GLY   A 1 106 ? 29.084 -31.726 43.566  1.00 50.21  ? 799  GLY   A C   1 
ATOM   701  O O   . GLY   A 1 106 ? 29.406 -30.913 42.703  1.00 50.34  ? 799  GLY   A O   1 
ATOM   702  N N   . CYS   A 1 107 ? 27.970 -31.602 44.288  1.00 49.39  ? 800  CYS   A N   1 
ATOM   703  C CA  . CYS   A 1 107 ? 27.051 -30.493 44.093  1.00 48.77  ? 800  CYS   A CA  1 
ATOM   704  C C   . CYS   A 1 107 ? 27.424 -29.280 44.935  1.00 48.08  ? 800  CYS   A C   1 
ATOM   705  O O   . CYS   A 1 107 ? 28.059 -29.413 45.979  1.00 48.14  ? 800  CYS   A O   1 
ATOM   706  C CB  . CYS   A 1 107 ? 25.614 -30.929 44.347  1.00 49.15  ? 800  CYS   A CB  1 
ATOM   707  S SG  . CYS   A 1 107 ? 25.318 -31.464 46.040  1.00 52.76  ? 800  CYS   A SG  1 
ATOM   708  N N   . LEU   A 1 108 ? 27.006 -28.098 44.471  1.00 47.19  ? 801  LEU   A N   1 
ATOM   709  C CA  . LEU   A 1 108 ? 27.274 -26.819 45.096  1.00 47.56  ? 801  LEU   A CA  1 
ATOM   710  C C   . LEU   A 1 108 ? 26.713 -26.725 46.513  1.00 48.17  ? 801  LEU   A C   1 
ATOM   711  O O   . LEU   A 1 108 ? 27.350 -26.119 47.373  1.00 48.09  ? 801  LEU   A O   1 
ATOM   712  C CB  . LEU   A 1 108 ? 26.766 -25.677 44.196  1.00 47.35  ? 801  LEU   A CB  1 
ATOM   713  C CG  . LEU   A 1 108 ? 27.330 -24.276 44.439  1.00 47.86  ? 801  LEU   A CG  1 
ATOM   714  C CD1 . LEU   A 1 108 ? 28.874 -24.277 44.480  1.00 47.69  ? 801  LEU   A CD1 1 
ATOM   715  C CD2 . LEU   A 1 108 ? 26.822 -23.303 43.372  1.00 47.94  ? 801  LEU   A CD2 1 
ATOM   716  N N   . LEU   A 1 109 ? 25.572 -27.382 46.775  1.00 48.55  ? 802  LEU   A N   1 
ATOM   717  C CA  . LEU   A 1 109 ? 24.962 -27.405 48.101  1.00 49.66  ? 802  LEU   A CA  1 
ATOM   718  C C   . LEU   A 1 109 ? 25.886 -28.036 49.147  1.00 50.97  ? 802  LEU   A C   1 
ATOM   719  O O   . LEU   A 1 109 ? 26.117 -27.432 50.191  1.00 51.68  ? 802  LEU   A O   1 
ATOM   720  C CB  . LEU   A 1 109 ? 23.620 -28.153 48.073  1.00 49.67  ? 802  LEU   A CB  1 
ATOM   721  C CG  . LEU   A 1 109 ? 22.895 -28.234 49.415  1.00 50.19  ? 802  LEU   A CG  1 
ATOM   722  C CD1 . LEU   A 1 109 ? 22.532 -26.857 49.919  1.00 50.42  ? 802  LEU   A CD1 1 
ATOM   723  C CD2 . LEU   A 1 109 ? 21.673 -29.116 49.320  1.00 50.72  ? 802  LEU   A CD2 1 
ATOM   724  N N   . ASP   A 1 110 ? 26.409 -29.237 48.878  1.00 51.07  ? 803  ASP   A N   1 
ATOM   725  C CA  . ASP   A 1 110 ? 27.324 -29.894 49.799  1.00 51.90  ? 803  ASP   A CA  1 
ATOM   726  C C   . ASP   A 1 110 ? 28.629 -29.116 49.908  1.00 52.05  ? 803  ASP   A C   1 
ATOM   727  O O   . ASP   A 1 110 ? 29.179 -29.010 50.999  1.00 52.98  ? 803  ASP   A O   1 
ATOM   728  C CB  . ASP   A 1 110 ? 27.609 -31.337 49.356  1.00 54.29  ? 803  ASP   A CB  1 
ATOM   729  C CG  . ASP   A 1 110 ? 26.398 -32.254 49.370  1.00 61.02  ? 803  ASP   A CG  1 
ATOM   730  O OD1 . ASP   A 1 110 ? 25.343 -31.853 49.948  1.00 62.50  ? 803  ASP   A OD1 1 
ATOM   731  O OD2 . ASP   A 1 110 ? 26.497 -33.372 48.808  1.00 63.51  ? 803  ASP   A OD2 1 
ATOM   732  N N   . TYR   A 1 111 ? 29.112 -28.566 48.792  1.00 51.41  ? 804  TYR   A N   1 
ATOM   733  C CA  . TYR   A 1 111 ? 30.344 -27.792 48.723  1.00 51.44  ? 804  TYR   A CA  1 
ATOM   734  C C   . TYR   A 1 111 ? 30.316 -26.568 49.625  1.00 52.24  ? 804  TYR   A C   1 
ATOM   735  O O   . TYR   A 1 111 ? 31.285 -26.343 50.342  1.00 52.46  ? 804  TYR   A O   1 
ATOM   736  C CB  . TYR   A 1 111 ? 30.663 -27.403 47.259  1.00 51.18  ? 804  TYR   A CB  1 
ATOM   737  C CG  . TYR   A 1 111 ? 32.039 -26.793 47.097  1.00 51.58  ? 804  TYR   A CG  1 
ATOM   738  C CD1 . TYR   A 1 111 ? 33.157 -27.592 46.906  1.00 52.17  ? 804  TYR   A CD1 1 
ATOM   739  C CD2 . TYR   A 1 111 ? 32.227 -25.419 47.180  1.00 52.39  ? 804  TYR   A CD2 1 
ATOM   740  C CE1 . TYR   A 1 111 ? 34.426 -27.040 46.795  1.00 52.87  ? 804  TYR   A CE1 1 
ATOM   741  C CE2 . TYR   A 1 111 ? 33.492 -24.858 47.098  1.00 53.14  ? 804  TYR   A CE2 1 
ATOM   742  C CZ  . TYR   A 1 111 ? 34.590 -25.670 46.899  1.00 54.01  ? 804  TYR   A CZ  1 
ATOM   743  O OH  . TYR   A 1 111 ? 35.834 -25.089 46.801  1.00 56.09  ? 804  TYR   A OH  1 
ATOM   744  N N   . VAL   A 1 112 ? 29.224 -25.764 49.595  1.00 52.91  ? 805  VAL   A N   1 
ATOM   745  C CA  . VAL   A 1 112 ? 29.138 -24.564 50.433  1.00 53.74  ? 805  VAL   A CA  1 
ATOM   746  C C   . VAL   A 1 112 ? 28.990 -24.922 51.907  1.00 55.09  ? 805  VAL   A C   1 
ATOM   747  O O   . VAL   A 1 112 ? 29.520 -24.207 52.756  1.00 55.77  ? 805  VAL   A O   1 
ATOM   748  C CB  . VAL   A 1 112 ? 28.089 -23.512 49.979  1.00 54.22  ? 805  VAL   A CB  1 
ATOM   749  C CG1 . VAL   A 1 112 ? 28.399 -22.991 48.583  1.00 54.92  ? 805  VAL   A CG1 1 
ATOM   750  C CG2 . VAL   A 1 112 ? 26.674 -24.055 50.051  1.00 54.35  ? 805  VAL   A CG2 1 
ATOM   751  N N   . ARG   A 1 113 ? 28.321 -26.037 52.223  1.00 55.53  ? 806  ARG   A N   1 
ATOM   752  C CA  . ARG   A 1 113 ? 28.188 -26.482 53.610  1.00 56.27  ? 806  ARG   A CA  1 
ATOM   753  C C   . ARG   A 1 113 ? 29.535 -26.941 54.141  1.00 57.43  ? 806  ARG   A C   1 
ATOM   754  O O   . ARG   A 1 113 ? 29.883 -26.624 55.271  1.00 57.74  ? 806  ARG   A O   1 
ATOM   755  C CB  . ARG   A 1 113 ? 27.183 -27.633 53.721  1.00 56.62  ? 806  ARG   A CB  1 
ATOM   756  C CG  . ARG   A 1 113 ? 25.741 -27.220 53.540  1.00 58.18  ? 806  ARG   A CG  1 
ATOM   757  C CD  . ARG   A 1 113 ? 24.882 -28.452 53.447  1.00 60.31  ? 806  ARG   A CD  1 
ATOM   758  N NE  . ARG   A 1 113 ? 23.462 -28.128 53.387  1.00 62.68  ? 806  ARG   A NE  1 
ATOM   759  C CZ  . ARG   A 1 113 ? 22.504 -29.004 53.103  1.00 64.78  ? 806  ARG   A CZ  1 
ATOM   760  N NH1 . ARG   A 1 113 ? 22.810 -30.271 52.838  1.00 63.76  ? 806  ARG   A NH1 1 
ATOM   761  N NH2 . ARG   A 1 113 ? 21.228 -28.621 53.080  1.00 64.87  ? 806  ARG   A NH2 1 
ATOM   762  N N   . GLU   A 1 114 ? 30.296 -27.677 53.332  1.00 58.44  ? 807  GLU   A N   1 
ATOM   763  C CA  . GLU   A 1 114 ? 31.587 -28.196 53.768  1.00 60.05  ? 807  GLU   A CA  1 
ATOM   764  C C   . GLU   A 1 114 ? 32.703 -27.152 53.742  1.00 60.43  ? 807  GLU   A C   1 
ATOM   765  O O   . GLU   A 1 114 ? 33.660 -27.303 54.483  1.00 60.11  ? 807  GLU   A O   1 
ATOM   766  C CB  . GLU   A 1 114 ? 31.963 -29.450 52.961  1.00 63.90  ? 807  GLU   A CB  1 
ATOM   767  C CG  . GLU   A 1 114 ? 31.370 -30.737 53.536  1.00 71.57  ? 807  GLU   A CG  1 
ATOM   768  C CD  . GLU   A 1 114 ? 30.210 -31.372 52.779  1.00 80.29  ? 807  GLU   A CD  1 
ATOM   769  O OE1 . GLU   A 1 114 ? 30.454 -32.328 52.005  1.00 82.12  ? 807  GLU   A OE1 1 
ATOM   770  O OE2 . GLU   A 1 114 ? 29.055 -30.919 52.965  1.00 82.35  ? 807  GLU   A OE2 1 
ATOM   771  N N   . HIS   A 1 115 ? 32.583 -26.082 52.916  1.00 60.98  ? 808  HIS   A N   1 
ATOM   772  C CA  . HIS   A 1 115 ? 33.666 -25.099 52.806  1.00 61.77  ? 808  HIS   A CA  1 
ATOM   773  C C   . HIS   A 1 115 ? 33.324 -23.690 53.276  1.00 62.89  ? 808  HIS   A C   1 
ATOM   774  O O   . HIS   A 1 115 ? 34.085 -22.771 52.990  1.00 63.04  ? 808  HIS   A O   1 
ATOM   775  C CB  . HIS   A 1 115 ? 34.211 -25.061 51.373  1.00 62.12  ? 808  HIS   A CB  1 
ATOM   776  C CG  . HIS   A 1 115 ? 34.776 -26.382 50.949  1.00 63.76  ? 808  HIS   A CG  1 
ATOM   777  N ND1 . HIS   A 1 115 ? 34.103 -27.207 50.064  1.00 65.20  ? 808  HIS   A ND1 1 
ATOM   778  C CD2 . HIS   A 1 115 ? 35.893 -27.020 51.379  1.00 64.63  ? 808  HIS   A CD2 1 
ATOM   779  C CE1 . HIS   A 1 115 ? 34.844 -28.299 49.960  1.00 65.80  ? 808  HIS   A CE1 1 
ATOM   780  N NE2 . HIS   A 1 115 ? 35.932 -28.229 50.732  1.00 65.63  ? 808  HIS   A NE2 1 
ATOM   781  N N   . LYS   A 1 116 ? 32.221 -23.538 54.032  1.00 63.35  ? 809  LYS   A N   1 
ATOM   782  C CA  . LYS   A 1 116 ? 31.682 -22.289 54.575  1.00 64.25  ? 809  LYS   A CA  1 
ATOM   783  C C   . LYS   A 1 116 ? 32.713 -21.188 54.953  1.00 65.25  ? 809  LYS   A C   1 
ATOM   784  O O   . LYS   A 1 116 ? 32.624 -20.084 54.415  1.00 65.74  ? 809  LYS   A O   1 
ATOM   785  C CB  . LYS   A 1 116 ? 30.779 -22.592 55.783  1.00 66.24  ? 809  LYS   A CB  1 
ATOM   786  C CG  . LYS   A 1 116 ? 29.990 -21.380 56.254  1.00 70.67  ? 809  LYS   A CG  1 
ATOM   787  C CD  . LYS   A 1 116 ? 30.351 -20.940 57.657  1.00 75.22  ? 809  LYS   A CD  1 
ATOM   788  C CE  . LYS   A 1 116 ? 29.796 -19.572 57.974  1.00 78.24  ? 809  LYS   A CE  1 
ATOM   789  N NZ  . LYS   A 1 116 ? 28.312 -19.571 57.986  1.00 79.62  ? 809  LYS   A NZ  1 
ATOM   790  N N   . ASP   A 1 117 ? 33.669 -21.457 55.873  1.00 65.44  ? 810  ASP   A N   1 
ATOM   791  C CA  . ASP   A 1 117 ? 34.621 -20.428 56.301  1.00 65.85  ? 810  ASP   A CA  1 
ATOM   792  C C   . ASP   A 1 117 ? 35.738 -20.098 55.295  1.00 64.96  ? 810  ASP   A C   1 
ATOM   793  O O   . ASP   A 1 117 ? 36.616 -19.289 55.599  1.00 65.37  ? 810  ASP   A O   1 
ATOM   794  C CB  . ASP   A 1 117 ? 35.221 -20.785 57.662  1.00 68.97  ? 810  ASP   A CB  1 
ATOM   795  C CG  . ASP   A 1 117 ? 34.407 -20.270 58.854  1.00 75.53  ? 810  ASP   A CG  1 
ATOM   796  O OD1 . ASP   A 1 117 ? 33.192 -19.986 58.676  1.00 76.36  ? 810  ASP   A OD1 1 
ATOM   797  O OD2 . ASP   A 1 117 ? 34.987 -20.139 59.961  1.00 78.06  ? 810  ASP   A OD2 1 
ATOM   798  N N   . ASN   A 1 118 ? 35.716 -20.713 54.115  1.00 63.68  ? 811  ASN   A N   1 
ATOM   799  C CA  . ASN   A 1 118 ? 36.718 -20.449 53.083  1.00 62.83  ? 811  ASN   A CA  1 
ATOM   800  C C   . ASN   A 1 118 ? 36.151 -19.885 51.787  1.00 61.78  ? 811  ASN   A C   1 
ATOM   801  O O   . ASN   A 1 118 ? 36.903 -19.710 50.831  1.00 62.70  ? 811  ASN   A O   1 
ATOM   802  C CB  . ASN   A 1 118 ? 37.535 -21.691 52.802  1.00 63.93  ? 811  ASN   A CB  1 
ATOM   803  C CG  . ASN   A 1 118 ? 38.350 -22.104 53.998  1.00 67.87  ? 811  ASN   A CG  1 
ATOM   804  O OD1 . ASN   A 1 118 ? 38.283 -23.246 54.450  1.00 70.21  ? 811  ASN   A OD1 1 
ATOM   805  N ND2 . ASN   A 1 118 ? 39.126 -21.178 54.550  1.00 67.74  ? 811  ASN   A ND2 1 
ATOM   806  N N   . ILE   A 1 119 ? 34.839 -19.624 51.739  1.00 59.83  ? 812  ILE   A N   1 
ATOM   807  C CA  . ILE   A 1 119 ? 34.205 -19.068 50.561  1.00 58.59  ? 812  ILE   A CA  1 
ATOM   808  C C   . ILE   A 1 119 ? 34.077 -17.563 50.730  1.00 57.32  ? 812  ILE   A C   1 
ATOM   809  O O   . ILE   A 1 119 ? 33.479 -17.090 51.696  1.00 56.66  ? 812  ILE   A O   1 
ATOM   810  C CB  . ILE   A 1 119 ? 32.840 -19.739 50.306  1.00 58.48  ? 812  ILE   A CB  1 
ATOM   811  C CG1 . ILE   A 1 119 ? 33.004 -21.254 50.141  1.00 59.12  ? 812  ILE   A CG1 1 
ATOM   812  C CG2 . ILE   A 1 119 ? 32.163 -19.125 49.101  1.00 58.69  ? 812  ILE   A CG2 1 
ATOM   813  C CD1 . ILE   A 1 119 ? 31.738 -22.005 50.154  1.00 60.12  ? 812  ILE   A CD1 1 
ATOM   814  N N   . GLY   A 1 120 ? 34.685 -16.830 49.811  1.00 56.82  ? 813  GLY   A N   1 
ATOM   815  C CA  . GLY   A 1 120 ? 34.631 -15.376 49.798  1.00 56.64  ? 813  GLY   A CA  1 
ATOM   816  C C   . GLY   A 1 120 ? 33.562 -14.859 48.851  1.00 56.31  ? 813  GLY   A C   1 
ATOM   817  O O   . GLY   A 1 120 ? 33.009 -15.624 48.049  1.00 56.16  ? 813  GLY   A O   1 
ATOM   818  N N   . SER   A 1 121 ? 33.273 -13.550 48.927  1.00 55.79  ? 814  SER   A N   1 
ATOM   819  C CA  . SER   A 1 121 ? 32.245 -12.884 48.125  1.00 56.20  ? 814  SER   A CA  1 
ATOM   820  C C   . SER   A 1 121 ? 32.427 -13.061 46.628  1.00 55.80  ? 814  SER   A C   1 
ATOM   821  O O   . SER   A 1 121 ? 31.440 -13.146 45.909  1.00 55.77  ? 814  SER   A O   1 
ATOM   822  C CB  . SER   A 1 121 ? 32.181 -11.401 48.465  1.00 58.12  ? 814  SER   A CB  1 
ATOM   823  O OG  . SER   A 1 121 ? 33.460 -10.807 48.313  1.00 61.22  ? 814  SER   A OG  1 
ATOM   824  N N   . GLN   A 1 122 ? 33.684 -13.123 46.160  1.00 55.50  ? 815  GLN   A N   1 
ATOM   825  C CA  . GLN   A 1 122 ? 34.006 -13.294 44.746  1.00 55.72  ? 815  GLN   A CA  1 
ATOM   826  C C   . GLN   A 1 122 ? 33.429 -14.590 44.194  1.00 55.34  ? 815  GLN   A C   1 
ATOM   827  O O   . GLN   A 1 122 ? 32.835 -14.581 43.121  1.00 55.32  ? 815  GLN   A O   1 
ATOM   828  C CB  . GLN   A 1 122 ? 35.521 -13.238 44.521  1.00 57.96  ? 815  GLN   A CB  1 
ATOM   829  C CG  . GLN   A 1 122 ? 35.928 -13.032 43.065  1.00 62.66  ? 815  GLN   A CG  1 
ATOM   830  C CD  . GLN   A 1 122 ? 35.579 -11.648 42.552  1.00 68.08  ? 815  GLN   A CD  1 
ATOM   831  O OE1 . GLN   A 1 122 ? 36.328 -10.677 42.736  1.00 69.90  ? 815  GLN   A OE1 1 
ATOM   832  N NE2 . GLN   A 1 122 ? 34.443 -11.536 41.873  1.00 68.41  ? 815  GLN   A NE2 1 
ATOM   833  N N   . TYR   A 1 123 ? 33.565 -15.682 44.960  1.00 54.71  ? 816  TYR   A N   1 
ATOM   834  C CA  . TYR   A 1 123 ? 33.062 -17.001 44.623  1.00 54.45  ? 816  TYR   A CA  1 
ATOM   835  C C   . TYR   A 1 123 ? 31.540 -17.054 44.558  1.00 52.27  ? 816  TYR   A C   1 
ATOM   836  O O   . TYR   A 1 123 ? 30.988 -17.556 43.586  1.00 51.78  ? 816  TYR   A O   1 
ATOM   837  C CB  . TYR   A 1 123 ? 33.569 -18.022 45.651  1.00 56.00  ? 816  TYR   A CB  1 
ATOM   838  C CG  . TYR   A 1 123 ? 34.903 -18.620 45.291  1.00 58.92  ? 816  TYR   A CG  1 
ATOM   839  C CD1 . TYR   A 1 123 ? 34.992 -19.688 44.413  1.00 60.73  ? 816  TYR   A CD1 1 
ATOM   840  C CD2 . TYR   A 1 123 ? 36.077 -18.125 45.835  1.00 61.06  ? 816  TYR   A CD2 1 
ATOM   841  C CE1 . TYR   A 1 123 ? 36.217 -20.253 44.085  1.00 62.29  ? 816  TYR   A CE1 1 
ATOM   842  C CE2 . TYR   A 1 123 ? 37.309 -18.688 45.523  1.00 62.64  ? 816  TYR   A CE2 1 
ATOM   843  C CZ  . TYR   A 1 123 ? 37.374 -19.751 44.642  1.00 63.84  ? 816  TYR   A CZ  1 
ATOM   844  O OH  . TYR   A 1 123 ? 38.588 -20.306 44.312  1.00 66.23  ? 816  TYR   A OH  1 
ATOM   845  N N   . LEU   A 1 124 ? 30.863 -16.571 45.608  1.00 50.94  ? 817  LEU   A N   1 
ATOM   846  C CA  . LEU   A 1 124 ? 29.409 -16.586 45.695  1.00 49.94  ? 817  LEU   A CA  1 
ATOM   847  C C   . LEU   A 1 124 ? 28.750 -15.815 44.559  1.00 49.13  ? 817  LEU   A C   1 
ATOM   848  O O   . LEU   A 1 124 ? 27.786 -16.305 43.966  1.00 49.28  ? 817  LEU   A O   1 
ATOM   849  C CB  . LEU   A 1 124 ? 28.959 -16.044 47.048  1.00 49.82  ? 817  LEU   A CB  1 
ATOM   850  C CG  . LEU   A 1 124 ? 29.261 -16.928 48.237  1.00 50.75  ? 817  LEU   A CG  1 
ATOM   851  C CD1 . LEU   A 1 124 ? 29.012 -16.200 49.527  1.00 51.22  ? 817  LEU   A CD1 1 
ATOM   852  C CD2 . LEU   A 1 124 ? 28.432 -18.171 48.205  1.00 51.06  ? 817  LEU   A CD2 1 
ATOM   853  N N   . LEU   A 1 125 ? 29.284 -14.632 44.223  1.00 48.19  ? 818  LEU   A N   1 
ATOM   854  C CA  . LEU   A 1 125 ? 28.704 -13.816 43.156  1.00 48.00  ? 818  LEU   A CA  1 
ATOM   855  C C   . LEU   A 1 125 ? 28.982 -14.372 41.765  1.00 47.60  ? 818  LEU   A C   1 
ATOM   856  O O   . LEU   A 1 125 ? 28.117 -14.297 40.902  1.00 47.46  ? 818  LEU   A O   1 
ATOM   857  C CB  . LEU   A 1 125 ? 29.131 -12.345 43.276  1.00 48.15  ? 818  LEU   A CB  1 
ATOM   858  C CG  . LEU   A 1 125 ? 28.544 -11.617 44.487  1.00 49.19  ? 818  LEU   A CG  1 
ATOM   859  C CD1 . LEU   A 1 125 ? 29.278 -10.332 44.765  1.00 49.80  ? 818  LEU   A CD1 1 
ATOM   860  C CD2 . LEU   A 1 125 ? 27.079 -11.341 44.293  1.00 49.68  ? 818  LEU   A CD2 1 
ATOM   861  N N   . ASN   A 1 126 ? 30.157 -14.977 41.559  1.00 47.29  ? 819  ASN   A N   1 
ATOM   862  C CA  . ASN   A 1 126 ? 30.509 -15.591 40.290  1.00 47.17  ? 819  ASN   A CA  1 
ATOM   863  C C   . ASN   A 1 126 ? 29.645 -16.819 40.031  1.00 46.03  ? 819  ASN   A C   1 
ATOM   864  O O   . ASN   A 1 126 ? 29.235 -17.026 38.890  1.00 46.27  ? 819  ASN   A O   1 
ATOM   865  C CB  . ASN   A 1 126 ? 31.980 -15.957 40.243  1.00 49.84  ? 819  ASN   A CB  1 
ATOM   866  C CG  . ASN   A 1 126 ? 32.902 -14.761 40.059  1.00 56.18  ? 819  ASN   A CG  1 
ATOM   867  O OD1 . ASN   A 1 126 ? 32.482 -13.650 39.707  1.00 58.15  ? 819  ASN   A OD1 1 
ATOM   868  N ND2 . ASN   A 1 126 ? 34.193 -14.955 40.305  1.00 57.76  ? 819  ASN   A ND2 1 
ATOM   869  N N   . TRP   A 1 127 ? 29.326 -17.606 41.076  1.00 44.57  ? 820  TRP   A N   1 
ATOM   870  C CA  . TRP   A 1 127 ? 28.447 -18.766 40.925  1.00 43.86  ? 820  TRP   A CA  1 
ATOM   871  C C   . TRP   A 1 127 ? 27.041 -18.316 40.547  1.00 43.32  ? 820  TRP   A C   1 
ATOM   872  O O   . TRP   A 1 127 ? 26.425 -18.955 39.715  1.00 43.39  ? 820  TRP   A O   1 
ATOM   873  C CB  . TRP   A 1 127 ? 28.382 -19.607 42.205  1.00 43.46  ? 820  TRP   A CB  1 
ATOM   874  C CG  . TRP   A 1 127 ? 29.652 -20.309 42.554  1.00 44.09  ? 820  TRP   A CG  1 
ATOM   875  C CD1 . TRP   A 1 127 ? 30.590 -20.791 41.693  1.00 45.21  ? 820  TRP   A CD1 1 
ATOM   876  C CD2 . TRP   A 1 127 ? 30.088 -20.676 43.870  1.00 44.29  ? 820  TRP   A CD2 1 
ATOM   877  N NE1 . TRP   A 1 127 ? 31.609 -21.394 42.394  1.00 45.52  ? 820  TRP   A NE1 1 
ATOM   878  C CE2 . TRP   A 1 127 ? 31.324 -21.338 43.735  1.00 45.26  ? 820  TRP   A CE2 1 
ATOM   879  C CE3 . TRP   A 1 127 ? 29.584 -20.455 45.157  1.00 44.76  ? 820  TRP   A CE3 1 
ATOM   880  C CZ2 . TRP   A 1 127 ? 32.055 -21.793 44.839  1.00 45.96  ? 820  TRP   A CZ2 1 
ATOM   881  C CZ3 . TRP   A 1 127 ? 30.299 -20.929 46.245  1.00 45.75  ? 820  TRP   A CZ3 1 
ATOM   882  C CH2 . TRP   A 1 127 ? 31.518 -21.587 46.080  1.00 45.91  ? 820  TRP   A CH2 1 
ATOM   883  N N   . CYS   A 1 128 ? 26.537 -17.219 41.129  1.00 42.79  ? 821  CYS   A N   1 
ATOM   884  C CA  . CYS   A 1 128 ? 25.225 -16.671 40.787  1.00 43.45  ? 821  CYS   A CA  1 
ATOM   885  C C   . CYS   A 1 128 ? 25.164 -16.306 39.300  1.00 42.96  ? 821  CYS   A C   1 
ATOM   886  O O   . CYS   A 1 128 ? 24.155 -16.557 38.652  1.00 43.30  ? 821  CYS   A O   1 
ATOM   887  C CB  . CYS   A 1 128 ? 24.898 -15.455 41.653  1.00 45.26  ? 821  CYS   A CB  1 
ATOM   888  S SG  . CYS   A 1 128 ? 24.664 -15.828 43.413  1.00 51.42  ? 821  CYS   A SG  1 
ATOM   889  N N   . VAL   A 1 129 ? 26.240 -15.713 38.769  1.00 42.32  ? 822  VAL   A N   1 
ATOM   890  C CA  . VAL   A 1 129 ? 26.349 -15.328 37.366  1.00 42.13  ? 822  VAL   A CA  1 
ATOM   891  C C   . VAL   A 1 129 ? 26.309 -16.577 36.488  1.00 41.66  ? 822  VAL   A C   1 
ATOM   892  O O   . VAL   A 1 129 ? 25.585 -16.613 35.489  1.00 42.55  ? 822  VAL   A O   1 
ATOM   893  C CB  . VAL   A 1 129 ? 27.648 -14.520 37.102  1.00 42.98  ? 822  VAL   A CB  1 
ATOM   894  C CG1 . VAL   A 1 129 ? 27.851 -14.278 35.612  1.00 43.65  ? 822  VAL   A CG1 1 
ATOM   895  C CG2 . VAL   A 1 129 ? 27.657 -13.202 37.862  1.00 43.39  ? 822  VAL   A CG2 1 
ATOM   896  N N   . GLN   A 1 130 ? 27.096 -17.593 36.856  1.00 39.66  ? 823  GLN   A N   1 
ATOM   897  C CA  . GLN   A 1 130 ? 27.196 -18.824 36.120  1.00 38.17  ? 823  GLN   A CA  1 
ATOM   898  C C   . GLN   A 1 130 ? 25.882 -19.566 36.075  1.00 37.89  ? 823  GLN   A C   1 
ATOM   899  O O   . GLN   A 1 130 ? 25.474 -19.983 34.996  1.00 38.39  ? 823  GLN   A O   1 
ATOM   900  C CB  . GLN   A 1 130 ? 28.325 -19.681 36.681  1.00 39.06  ? 823  GLN   A CB  1 
ATOM   901  C CG  . GLN   A 1 130 ? 29.698 -19.022 36.469  1.00 41.74  ? 823  GLN   A CG  1 
ATOM   902  C CD  . GLN   A 1 130 ? 30.849 -19.909 36.892  1.00 46.32  ? 823  GLN   A CD  1 
ATOM   903  O OE1 . GLN   A 1 130 ? 30.697 -21.097 37.168  1.00 47.02  ? 823  GLN   A OE1 1 
ATOM   904  N NE2 . GLN   A 1 130 ? 32.035 -19.351 36.956  1.00 47.60  ? 823  GLN   A NE2 1 
ATOM   905  N N   . ILE   A 1 131 ? 25.176 -19.677 37.205  1.00 36.95  ? 824  ILE   A N   1 
ATOM   906  C CA  . ILE   A 1 131 ? 23.874 -20.325 37.226  1.00 36.46  ? 824  ILE   A CA  1 
ATOM   907  C C   . ILE   A 1 131 ? 22.865 -19.556 36.351  1.00 37.31  ? 824  ILE   A C   1 
ATOM   908  O O   . ILE   A 1 131 ? 22.130 -20.180 35.591  1.00 38.00  ? 824  ILE   A O   1 
ATOM   909  C CB  . ILE   A 1 131 ? 23.382 -20.545 38.675  1.00 36.06  ? 824  ILE   A CB  1 
ATOM   910  C CG1 . ILE   A 1 131 ? 24.383 -21.407 39.475  1.00 35.23  ? 824  ILE   A CG1 1 
ATOM   911  C CG2 . ILE   A 1 131 ? 21.967 -21.157 38.700  1.00 36.17  ? 824  ILE   A CG2 1 
ATOM   912  C CD1 . ILE   A 1 131 ? 24.188 -21.372 40.891  1.00 35.67  ? 824  ILE   A CD1 1 
ATOM   913  N N   . ALA   A 1 132 ? 22.895 -18.210 36.373  1.00 36.76  ? 825  ALA   A N   1 
ATOM   914  C CA  . ALA   A 1 132 ? 22.005 -17.422 35.519  1.00 36.57  ? 825  ALA   A CA  1 
ATOM   915  C C   . ALA   A 1 132 ? 22.362 -17.578 34.033  1.00 35.77  ? 825  ALA   A C   1 
ATOM   916  O O   . ALA   A 1 132 ? 21.482 -17.556 33.195  1.00 35.44  ? 825  ALA   A O   1 
ATOM   917  C CB  . ALA   A 1 132 ? 22.029 -15.956 35.933  1.00 36.82  ? 825  ALA   A CB  1 
ATOM   918  N N   . LYS   A 1 133 ? 23.645 -17.754 33.706  1.00 35.30  ? 826  LYS   A N   1 
ATOM   919  C CA  . LYS   A 1 133 ? 24.080 -17.982 32.329  1.00 34.66  ? 826  LYS   A CA  1 
ATOM   920  C C   . LYS   A 1 133 ? 23.580 -19.336 31.790  1.00 35.13  ? 826  LYS   A C   1 
ATOM   921  O O   . LYS   A 1 133 ? 23.151 -19.429 30.634  1.00 36.16  ? 826  LYS   A O   1 
ATOM   922  C CB  . LYS   A 1 133 ? 25.595 -17.888 32.216  1.00 34.30  ? 826  LYS   A CB  1 
ATOM   923  C CG  . LYS   A 1 133 ? 26.066 -16.454 32.105  1.00 34.19  ? 826  LYS   A CG  1 
ATOM   924  C CD  . LYS   A 1 133 ? 27.562 -16.369 32.192  1.00 34.89  ? 826  LYS   A CD  1 
ATOM   925  C CE  . LYS   A 1 133 ? 28.006 -14.945 32.010  1.00 37.52  ? 826  LYS   A CE  1 
ATOM   926  N N   . GLY   A 1 134 ? 23.637 -20.359 32.623  1.00 34.41  ? 827  GLY   A N   1 
ATOM   927  C CA  . GLY   A 1 134 ? 23.144 -21.671 32.261  1.00 35.29  ? 827  GLY   A CA  1 
ATOM   928  C C   . GLY   A 1 134 ? 21.637 -21.665 32.156  1.00 36.26  ? 827  GLY   A C   1 
ATOM   929  O O   . GLY   A 1 134 ? 21.086 -22.192 31.195  1.00 36.76  ? 827  GLY   A O   1 
ATOM   930  N N   . MET   A 1 135 ? 20.951 -21.026 33.104  1.00 36.77  ? 828  MET   A N   1 
ATOM   931  C CA  . MET   A 1 135 ? 19.490 -20.930 33.070  1.00 37.88  ? 828  MET   A CA  1 
ATOM   932  C C   . MET   A 1 135 ? 18.988 -20.125 31.893  1.00 39.18  ? 828  MET   A C   1 
ATOM   933  O O   . MET   A 1 135 ? 18.006 -20.512 31.258  1.00 40.21  ? 828  MET   A O   1 
ATOM   934  C CB  . MET   A 1 135 ? 18.949 -20.367 34.372  1.00 38.86  ? 828  MET   A CB  1 
ATOM   935  C CG  . MET   A 1 135 ? 19.058 -21.324 35.530  1.00 42.05  ? 828  MET   A CG  1 
ATOM   936  S SD  . MET   A 1 135 ? 18.289 -22.928 35.231  1.00 49.32  ? 828  MET   A SD  1 
ATOM   937  C CE  . MET   A 1 135 ? 16.597 -22.433 35.061  1.00 44.97  ? 828  MET   A CE  1 
ATOM   938  N N   . ASN   A 1 136 ? 19.696 -19.043 31.560  1.00 38.90  ? 829  ASN   A N   1 
ATOM   939  C CA  . ASN   A 1 136 ? 19.373 -18.216 30.414  1.00 39.55  ? 829  ASN   A CA  1 
ATOM   940  C C   . ASN   A 1 136 ? 19.557 -18.997 29.102  1.00 40.13  ? 829  ASN   A C   1 
ATOM   941  O O   . ASN   A 1 136 ? 18.858 -18.723 28.125  1.00 40.90  ? 829  ASN   A O   1 
ATOM   942  C CB  . ASN   A 1 136 ? 20.237 -16.961 30.430  1.00 40.53  ? 829  ASN   A CB  1 
ATOM   943  C CG  . ASN   A 1 136 ? 19.958 -16.015 29.297  1.00 43.10  ? 829  ASN   A CG  1 
ATOM   944  O OD1 . ASN   A 1 136 ? 18.857 -15.462 29.165  1.00 43.93  ? 829  ASN   A OD1 1 
ATOM   945  N ND2 . ASN   A 1 136 ? 20.960 -15.816 28.451  1.00 43.64  ? 829  ASN   A ND2 1 
ATOM   946  N N   . TYR   A 1 137 ? 20.519 -19.939 29.067  1.00 39.73  ? 830  TYR   A N   1 
ATOM   947  C CA  . TYR   A 1 137 ? 20.771 -20.768 27.901  1.00 40.10  ? 830  TYR   A CA  1 
ATOM   948  C C   . TYR   A 1 137 ? 19.628 -21.778 27.744  1.00 40.46  ? 830  TYR   A C   1 
ATOM   949  O O   . TYR   A 1 137 ? 19.155 -21.974 26.637  1.00 40.71  ? 830  TYR   A O   1 
ATOM   950  C CB  . TYR   A 1 137 ? 22.133 -21.480 27.996  1.00 40.40  ? 830  TYR   A CB  1 
ATOM   951  C CG  . TYR   A 1 137 ? 22.307 -22.515 26.903  1.00 41.66  ? 830  TYR   A CG  1 
ATOM   952  C CD1 . TYR   A 1 137 ? 22.360 -22.139 25.569  1.00 42.60  ? 830  TYR   A CD1 1 
ATOM   953  C CD2 . TYR   A 1 137 ? 22.281 -23.874 27.194  1.00 42.60  ? 830  TYR   A CD2 1 
ATOM   954  C CE1 . TYR   A 1 137 ? 22.471 -23.082 24.560  1.00 43.37  ? 830  TYR   A CE1 1 
ATOM   955  C CE2 . TYR   A 1 137 ? 22.358 -24.826 26.191  1.00 43.59  ? 830  TYR   A CE2 1 
ATOM   956  C CZ  . TYR   A 1 137 ? 22.467 -24.425 24.874  1.00 44.53  ? 830  TYR   A CZ  1 
ATOM   957  O OH  . TYR   A 1 137 ? 22.527 -25.366 23.879  1.00 45.90  ? 830  TYR   A OH  1 
ATOM   958  N N   . LEU   A 1 138 ? 19.177 -22.400 28.841  1.00 40.95  ? 831  LEU   A N   1 
ATOM   959  C CA  . LEU   A 1 138 ? 18.047 -23.323 28.809  1.00 41.98  ? 831  LEU   A CA  1 
ATOM   960  C C   . LEU   A 1 138 ? 16.782 -22.612 28.335  1.00 43.43  ? 831  LEU   A C   1 
ATOM   961  O O   . LEU   A 1 138 ? 16.029 -23.190 27.566  1.00 43.35  ? 831  LEU   A O   1 
ATOM   962  C CB  . LEU   A 1 138 ? 17.834 -23.990 30.179  1.00 41.68  ? 831  LEU   A CB  1 
ATOM   963  C CG  . LEU   A 1 138 ? 18.949 -24.961 30.593  1.00 42.30  ? 831  LEU   A CG  1 
ATOM   964  C CD1 . LEU   A 1 138 ? 18.784 -25.437 32.018  1.00 42.51  ? 831  LEU   A CD1 1 
ATOM   965  C CD2 . LEU   A 1 138 ? 19.058 -26.130 29.627  1.00 42.39  ? 831  LEU   A CD2 1 
ATOM   966  N N   . GLU   A 1 139 ? 16.589 -21.342 28.725  1.00 44.63  ? 832  GLU   A N   1 
ATOM   967  C CA  . GLU   A 1 139 ? 15.452 -20.541 28.272  1.00 46.70  ? 832  GLU   A CA  1 
ATOM   968  C C   . GLU   A 1 139 ? 15.545 -20.265 26.754  1.00 48.32  ? 832  GLU   A C   1 
ATOM   969  O O   . GLU   A 1 139 ? 14.527 -20.293 26.054  1.00 48.52  ? 832  GLU   A O   1 
ATOM   970  C CB  . GLU   A 1 139 ? 15.362 -19.234 29.073  1.00 49.85  ? 832  GLU   A CB  1 
ATOM   971  C CG  . GLU   A 1 139 ? 14.292 -18.285 28.567  1.00 57.08  ? 832  GLU   A CG  1 
ATOM   972  C CD  . GLU   A 1 139 ? 13.952 -17.120 29.474  1.00 67.80  ? 832  GLU   A CD  1 
ATOM   973  O OE1 . GLU   A 1 139 ? 14.590 -16.992 30.545  1.00 70.62  ? 832  GLU   A OE1 1 
ATOM   974  O OE2 . GLU   A 1 139 ? 13.038 -16.339 29.117  1.00 71.14  ? 832  GLU   A OE2 1 
ATOM   975  N N   . ASP   A 1 140 ? 16.768 -20.070 26.239  1.00 49.27  ? 833  ASP   A N   1 
ATOM   976  C CA  . ASP   A 1 140 ? 17.037 -19.895 24.809  1.00 50.72  ? 833  ASP   A CA  1 
ATOM   977  C C   . ASP   A 1 140 ? 16.671 -21.188 24.036  1.00 50.99  ? 833  ASP   A C   1 
ATOM   978  O O   . ASP   A 1 140 ? 16.181 -21.121 22.917  1.00 50.95  ? 833  ASP   A O   1 
ATOM   979  C CB  . ASP   A 1 140 ? 18.524 -19.545 24.602  1.00 53.44  ? 833  ASP   A CB  1 
ATOM   980  C CG  . ASP   A 1 140 ? 18.952 -19.457 23.150  1.00 59.82  ? 833  ASP   A CG  1 
ATOM   981  O OD1 . ASP   A 1 140 ? 18.452 -18.563 22.443  1.00 61.81  ? 833  ASP   A OD1 1 
ATOM   982  O OD2 . ASP   A 1 140 ? 19.788 -20.296 22.718  1.00 62.22  ? 833  ASP   A OD2 1 
ATOM   983  N N   . ARG   A 1 141 ? 16.919 -22.356 24.640  1.00 51.23  ? 834  ARG   A N   1 
ATOM   984  C CA  . ARG   A 1 141 ? 16.569 -23.651 24.058  1.00 52.10  ? 834  ARG   A CA  1 
ATOM   985  C C   . ARG   A 1 141 ? 15.099 -24.025 24.275  1.00 54.15  ? 834  ARG   A C   1 
ATOM   986  O O   . ARG   A 1 141 ? 14.728 -25.143 23.916  1.00 54.98  ? 834  ARG   A O   1 
ATOM   987  C CB  . ARG   A 1 141 ? 17.430 -24.786 24.655  1.00 52.30  ? 834  ARG   A CB  1 
ATOM   988  C CG  . ARG   A 1 141 ? 18.936 -24.780 24.392  1.00 53.66  ? 834  ARG   A CG  1 
ATOM   989  C CD  . ARG   A 1 141 ? 19.411 -23.881 23.266  1.00 56.37  ? 834  ARG   A CD  1 
ATOM   990  N NE  . ARG   A 1 141 ? 19.292 -24.496 21.950  1.00 59.01  ? 834  ARG   A NE  1 
ATOM   991  C CZ  . ARG   A 1 141 ? 19.437 -23.838 20.805  1.00 61.17  ? 834  ARG   A CZ  1 
ATOM   992  N NH1 . ARG   A 1 141 ? 19.331 -24.477 19.647  1.00 61.63  ? 834  ARG   A NH1 1 
ATOM   993  N NH2 . ARG   A 1 141 ? 19.684 -22.530 20.808  1.00 60.76  ? 834  ARG   A NH2 1 
ATOM   994  N N   . ARG   A 1 142 ? 14.275 -23.126 24.873  1.00 54.79  ? 835  ARG   A N   1 
ATOM   995  C CA  . ARG   A 1 142 ? 12.860 -23.326 25.184  1.00 55.52  ? 835  ARG   A CA  1 
ATOM   996  C C   . ARG   A 1 142 ? 12.672 -24.498 26.156  1.00 56.00  ? 835  ARG   A C   1 
ATOM   997  O O   . ARG   A 1 142 ? 11.743 -25.284 25.998  1.00 56.77  ? 835  ARG   A O   1 
ATOM   998  C CB  . ARG   A 1 142 ? 12.033 -23.530 23.896  1.00 56.74  ? 835  ARG   A CB  1 
ATOM   999  C CG  . ARG   A 1 142 ? 12.232 -22.438 22.857  1.00 59.83  ? 835  ARG   A CG  1 
ATOM   1000 C CD  . ARG   A 1 142 ? 11.705 -22.850 21.489  1.00 63.53  ? 835  ARG   A CD  1 
ATOM   1001 N N   . LEU   A 1 143 ? 13.565 -24.635 27.140  1.00 55.47  ? 836  LEU   A N   1 
ATOM   1002 C CA  . LEU   A 1 143 ? 13.497 -25.740 28.091  1.00 55.72  ? 836  LEU   A CA  1 
ATOM   1003 C C   . LEU   A 1 143 ? 13.277 -25.224 29.509  1.00 55.47  ? 836  LEU   A C   1 
ATOM   1004 O O   . LEU   A 1 143 ? 14.098 -24.469 30.036  1.00 56.15  ? 836  LEU   A O   1 
ATOM   1005 C CB  . LEU   A 1 143 ? 14.785 -26.591 28.022  1.00 56.27  ? 836  LEU   A CB  1 
ATOM   1006 C CG  . LEU   A 1 143 ? 14.734 -28.004 28.632  1.00 58.31  ? 836  LEU   A CG  1 
ATOM   1007 C CD1 . LEU   A 1 143 ? 15.617 -28.966 27.876  1.00 59.08  ? 836  LEU   A CD1 1 
ATOM   1008 C CD2 . LEU   A 1 143 ? 15.184 -28.012 30.075  1.00 59.17  ? 836  LEU   A CD2 1 
ATOM   1009 N N   . VAL   A 1 144 ? 12.175 -25.636 30.134  1.00 54.16  ? 837  VAL   A N   1 
ATOM   1010 C CA  . VAL   A 1 144 ? 11.894 -25.256 31.511  1.00 53.17  ? 837  VAL   A CA  1 
ATOM   1011 C C   . VAL   A 1 144 ? 12.538 -26.337 32.387  1.00 52.52  ? 837  VAL   A C   1 
ATOM   1012 O O   . VAL   A 1 144 ? 12.297 -27.521 32.173  1.00 52.65  ? 837  VAL   A O   1 
ATOM   1013 C CB  . VAL   A 1 144 ? 10.371 -25.118 31.749  1.00 53.14  ? 837  VAL   A CB  1 
ATOM   1014 C CG1 . VAL   A 1 144 ? 10.065 -24.857 33.221  1.00 53.73  ? 837  VAL   A CG1 1 
ATOM   1015 C CG2 . VAL   A 1 144 ? 9.778  -24.025 30.869  1.00 52.47  ? 837  VAL   A CG2 1 
ATOM   1016 N N   . HIS   A 1 145 ? 13.407 -25.948 33.321  1.00 51.80  ? 838  HIS   A N   1 
ATOM   1017 C CA  . HIS   A 1 145 ? 14.104 -26.907 34.181  1.00 51.42  ? 838  HIS   A CA  1 
ATOM   1018 C C   . HIS   A 1 145 ? 13.143 -27.636 35.136  1.00 52.49  ? 838  HIS   A C   1 
ATOM   1019 O O   . HIS   A 1 145 ? 13.167 -28.871 35.190  1.00 52.92  ? 838  HIS   A O   1 
ATOM   1020 C CB  . HIS   A 1 145 ? 15.236 -26.208 34.948  1.00 50.18  ? 838  HIS   A CB  1 
ATOM   1021 C CG  . HIS   A 1 145 ? 16.181 -27.142 35.641  1.00 49.55  ? 838  HIS   A CG  1 
ATOM   1022 N ND1 . HIS   A 1 145 ? 15.750 -28.013 36.621  1.00 50.56  ? 838  HIS   A ND1 1 
ATOM   1023 C CD2 . HIS   A 1 145 ? 17.523 -27.260 35.520  1.00 49.68  ? 838  HIS   A CD2 1 
ATOM   1024 C CE1 . HIS   A 1 145 ? 16.830 -28.652 37.036  1.00 50.52  ? 838  HIS   A CE1 1 
ATOM   1025 N NE2 . HIS   A 1 145 ? 17.920 -28.221 36.412  1.00 50.21  ? 838  HIS   A NE2 1 
ATOM   1026 N N   . ARG   A 1 146 ? 12.315 -26.865 35.889  1.00 52.47  ? 839  ARG   A N   1 
ATOM   1027 C CA  . ARG   A 1 146 ? 11.319 -27.333 36.865  1.00 52.77  ? 839  ARG   A CA  1 
ATOM   1028 C C   . ARG   A 1 146 ? 11.901 -27.718 38.233  1.00 52.51  ? 839  ARG   A C   1 
ATOM   1029 O O   . ARG   A 1 146 ? 11.134 -27.873 39.186  1.00 53.35  ? 839  ARG   A O   1 
ATOM   1030 C CB  . ARG   A 1 146 ? 10.455 -28.485 36.324  1.00 54.37  ? 839  ARG   A CB  1 
ATOM   1031 C CG  . ARG   A 1 146 ? 9.505  -28.119 35.204  1.00 58.70  ? 839  ARG   A CG  1 
ATOM   1032 C CD  . ARG   A 1 146 ? 8.770  -29.370 34.752  1.00 63.91  ? 839  ARG   A CD  1 
ATOM   1033 N NE  . ARG   A 1 146 ? 7.635  -29.063 33.882  1.00 69.49  ? 839  ARG   A NE  1 
ATOM   1034 C CZ  . ARG   A 1 146 ? 6.389  -29.465 34.109  1.00 73.93  ? 839  ARG   A CZ  1 
ATOM   1035 N NH1 . ARG   A 1 146 ? 5.413  -29.123 33.275  1.00 73.68  ? 839  ARG   A NH1 1 
ATOM   1036 N NH2 . ARG   A 1 146 ? 6.103  -30.196 35.182  1.00 75.27  ? 839  ARG   A NH2 1 
ATOM   1037 N N   . ASP   A 1 147 ? 13.227 -27.880 38.343  1.00 51.07  ? 840  ASP   A N   1 
ATOM   1038 C CA  . ASP   A 1 147 ? 13.823 -28.281 39.609  1.00 50.53  ? 840  ASP   A CA  1 
ATOM   1039 C C   . ASP   A 1 147 ? 15.198 -27.656 39.845  1.00 48.59  ? 840  ASP   A C   1 
ATOM   1040 O O   . ASP   A 1 147 ? 16.140 -28.363 40.216  1.00 48.78  ? 840  ASP   A O   1 
ATOM   1041 C CB  . ASP   A 1 147 ? 13.854 -29.820 39.737  1.00 54.16  ? 840  ASP   A CB  1 
ATOM   1042 C CG  . ASP   A 1 147 ? 14.148 -30.349 41.134  1.00 62.15  ? 840  ASP   A CG  1 
ATOM   1043 O OD1 . ASP   A 1 147 ? 13.941 -29.591 42.115  1.00 64.05  ? 840  ASP   A OD1 1 
ATOM   1044 O OD2 . ASP   A 1 147 ? 14.622 -31.508 41.246  1.00 65.05  ? 840  ASP   A OD2 1 
ATOM   1045 N N   . LEU   A 1 148 ? 15.323 -26.339 39.624  1.00 46.34  ? 841  LEU   A N   1 
ATOM   1046 C CA  . LEU   A 1 148 ? 16.585 -25.663 39.890  1.00 44.32  ? 841  LEU   A CA  1 
ATOM   1047 C C   . LEU   A 1 148 ? 16.722 -25.521 41.407  1.00 43.52  ? 841  LEU   A C   1 
ATOM   1048 O O   . LEU   A 1 148 ? 15.810 -25.055 42.066  1.00 43.63  ? 841  LEU   A O   1 
ATOM   1049 C CB  . LEU   A 1 148 ? 16.662 -24.290 39.201  1.00 43.24  ? 841  LEU   A CB  1 
ATOM   1050 C CG  . LEU   A 1 148 ? 17.947 -23.505 39.490  1.00 43.23  ? 841  LEU   A CG  1 
ATOM   1051 C CD1 . LEU   A 1 148 ? 19.220 -24.275 39.030  1.00 42.60  ? 841  LEU   A CD1 1 
ATOM   1052 C CD2 . LEU   A 1 148 ? 17.886 -22.144 38.880  1.00 43.69  ? 841  LEU   A CD2 1 
ATOM   1053 N N   . ALA   A 1 149 ? 17.830 -25.994 41.951  1.00 42.87  ? 842  ALA   A N   1 
ATOM   1054 C CA  . ALA   A 1 149 ? 18.156 -25.949 43.377  1.00 43.00  ? 842  ALA   A CA  1 
ATOM   1055 C C   . ALA   A 1 149 ? 19.677 -26.078 43.514  1.00 43.47  ? 842  ALA   A C   1 
ATOM   1056 O O   . ALA   A 1 149 ? 20.325 -26.539 42.575  1.00 43.73  ? 842  ALA   A O   1 
ATOM   1057 C CB  . ALA   A 1 149 ? 17.457 -27.072 44.122  1.00 42.97  ? 842  ALA   A CB  1 
ATOM   1058 N N   . ALA   A 1 150 ? 20.262 -25.675 44.652  1.00 43.48  ? 843  ALA   A N   1 
ATOM   1059 C CA  . ALA   A 1 150 ? 21.716 -25.784 44.819  1.00 43.93  ? 843  ALA   A CA  1 
ATOM   1060 C C   . ALA   A 1 150 ? 22.204 -27.253 44.750  1.00 44.79  ? 843  ALA   A C   1 
ATOM   1061 O O   . ALA   A 1 150 ? 23.355 -27.502 44.379  1.00 45.64  ? 843  ALA   A O   1 
ATOM   1062 C CB  . ALA   A 1 150 ? 22.167 -25.109 46.100  1.00 43.79  ? 843  ALA   A CB  1 
ATOM   1063 N N   . ARG   A 1 151 ? 21.320 -28.225 45.039  1.00 44.20  ? 844  ARG   A N   1 
ATOM   1064 C CA  . ARG   A 1 151 ? 21.667 -29.645 44.906  1.00 44.38  ? 844  ARG   A CA  1 
ATOM   1065 C C   . ARG   A 1 151 ? 21.794 -30.054 43.408  1.00 43.95  ? 844  ARG   A C   1 
ATOM   1066 O O   . ARG   A 1 151 ? 22.435 -31.056 43.097  1.00 43.79  ? 844  ARG   A O   1 
ATOM   1067 C CB  . ARG   A 1 151 ? 20.624 -30.527 45.619  1.00 45.93  ? 844  ARG   A CB  1 
ATOM   1068 C CG  . ARG   A 1 151 ? 19.262 -30.475 44.959  1.00 49.48  ? 844  ARG   A CG  1 
ATOM   1069 C CD  . ARG   A 1 151 ? 18.224 -31.372 45.604  1.00 53.90  ? 844  ARG   A CD  1 
ATOM   1070 N NE  . ARG   A 1 151 ? 16.898 -31.075 45.046  1.00 59.65  ? 844  ARG   A NE  1 
ATOM   1071 C CZ  . ARG   A 1 151 ? 16.069 -30.146 45.525  1.00 63.80  ? 844  ARG   A CZ  1 
ATOM   1072 N NH1 . ARG   A 1 151 ? 14.907 -29.913 44.928  1.00 64.68  ? 844  ARG   A NH1 1 
ATOM   1073 N NH2 . ARG   A 1 151 ? 16.395 -29.447 46.608  1.00 63.80  ? 844  ARG   A NH2 1 
ATOM   1074 N N   . ASN   A 1 152 ? 21.183 -29.276 42.491  1.00 43.13  ? 845  ASN   A N   1 
ATOM   1075 C CA  . ASN   A 1 152 ? 21.233 -29.519 41.057  1.00 42.94  ? 845  ASN   A CA  1 
ATOM   1076 C C   . ASN   A 1 152 ? 22.250 -28.652 40.317  1.00 42.14  ? 845  ASN   A C   1 
ATOM   1077 O O   . ASN   A 1 152 ? 22.147 -28.493 39.106  1.00 42.16  ? 845  ASN   A O   1 
ATOM   1078 C CB  . ASN   A 1 152 ? 19.848 -29.399 40.423  1.00 44.26  ? 845  ASN   A CB  1 
ATOM   1079 C CG  . ASN   A 1 152 ? 18.913 -30.531 40.774  1.00 48.09  ? 845  ASN   A CG  1 
ATOM   1080 O OD1 . ASN   A 1 152 ? 17.693 -30.351 40.763  1.00 49.74  ? 845  ASN   A OD1 1 
ATOM   1081 N ND2 . ASN   A 1 152 ? 19.426 -31.693 41.120  1.00 48.78  ? 845  ASN   A ND2 1 
ATOM   1082 N N   . VAL   A 1 153 ? 23.207 -28.084 41.039  1.00 41.27  ? 846  VAL   A N   1 
ATOM   1083 C CA  . VAL   A 1 153 ? 24.295 -27.327 40.470  1.00 41.63  ? 846  VAL   A CA  1 
ATOM   1084 C C   . VAL   A 1 153 ? 25.528 -28.111 40.870  1.00 42.99  ? 846  VAL   A C   1 
ATOM   1085 O O   . VAL   A 1 153 ? 25.721 -28.379 42.048  1.00 43.43  ? 846  VAL   A O   1 
ATOM   1086 C CB  . VAL   A 1 153 ? 24.343 -25.875 40.990  1.00 41.80  ? 846  VAL   A CB  1 
ATOM   1087 C CG1 . VAL   A 1 153 ? 25.527 -25.135 40.385  1.00 41.84  ? 846  VAL   A CG1 1 
ATOM   1088 C CG2 . VAL   A 1 153 ? 23.033 -25.137 40.704  1.00 41.98  ? 846  VAL   A CG2 1 
ATOM   1089 N N   . LEU   A 1 154 ? 26.312 -28.551 39.906  1.00 43.64  ? 847  LEU   A N   1 
ATOM   1090 C CA  . LEU   A 1 154 ? 27.508 -29.344 40.169  1.00 45.09  ? 847  LEU   A CA  1 
ATOM   1091 C C   . LEU   A 1 154 ? 28.766 -28.510 40.054  1.00 45.68  ? 847  LEU   A C   1 
ATOM   1092 O O   . LEU   A 1 154 ? 28.810 -27.523 39.325  1.00 46.15  ? 847  LEU   A O   1 
ATOM   1093 C CB  . LEU   A 1 154 ? 27.577 -30.542 39.224  1.00 46.09  ? 847  LEU   A CB  1 
ATOM   1094 C CG  . LEU   A 1 154 ? 26.293 -31.372 39.135  1.00 48.97  ? 847  LEU   A CG  1 
ATOM   1095 C CD1 . LEU   A 1 154 ? 26.443 -32.464 38.126  1.00 49.85  ? 847  LEU   A CD1 1 
ATOM   1096 C CD2 . LEU   A 1 154 ? 25.906 -31.969 40.490  1.00 50.07  ? 847  LEU   A CD2 1 
ATOM   1097 N N   . VAL   A 1 155 ? 29.779 -28.893 40.793  1.00 45.59  ? 848  VAL   A N   1 
ATOM   1098 C CA  . VAL   A 1 155 ? 31.044 -28.189 40.819  1.00 46.28  ? 848  VAL   A CA  1 
ATOM   1099 C C   . VAL   A 1 155 ? 32.073 -28.970 40.000  1.00 47.32  ? 848  VAL   A C   1 
ATOM   1100 O O   . VAL   A 1 155 ? 32.446 -30.067 40.383  1.00 47.35  ? 848  VAL   A O   1 
ATOM   1101 C CB  . VAL   A 1 155 ? 31.505 -27.986 42.291  1.00 46.48  ? 848  VAL   A CB  1 
ATOM   1102 C CG1 . VAL   A 1 155 ? 32.799 -27.185 42.372  1.00 47.03  ? 848  VAL   A CG1 1 
ATOM   1103 C CG2 . VAL   A 1 155 ? 30.418 -27.320 43.119  1.00 46.25  ? 848  VAL   A CG2 1 
ATOM   1104 N N   . LYS   A 1 156 ? 32.471 -28.440 38.839  1.00 48.29  ? 849  LYS   A N   1 
ATOM   1105 C CA  . LYS   A 1 156 ? 33.508 -29.046 38.010  1.00 49.62  ? 849  LYS   A CA  1 
ATOM   1106 C C   . LYS   A 1 156 ? 34.830 -28.677 38.701  1.00 50.70  ? 849  LYS   A C   1 
ATOM   1107 O O   . LYS   A 1 156 ? 35.614 -29.555 39.050  1.00 51.06  ? 849  LYS   A O   1 
ATOM   1108 C CB  . LYS   A 1 156 ? 33.451 -28.499 36.571  1.00 51.67  ? 849  LYS   A CB  1 
ATOM   1109 C CG  . LYS   A 1 156 ? 34.437 -29.184 35.641  1.00 55.95  ? 849  LYS   A CG  1 
ATOM   1110 C CD  . LYS   A 1 156 ? 34.227 -28.742 34.205  1.00 60.27  ? 849  LYS   A CD  1 
ATOM   1111 C CE  . LYS   A 1 156 ? 35.172 -29.434 33.258  1.00 64.02  ? 849  LYS   A CE  1 
ATOM   1112 N NZ  . LYS   A 1 156 ? 36.579 -29.064 33.546  1.00 67.39  ? 849  LYS   A NZ  1 
ATOM   1113 N N   . THR   A 1 157 ? 35.048 -27.365 38.911  1.00 51.00  ? 850  THR   A N   1 
ATOM   1114 C CA  . THR   A 1 157 ? 36.132 -26.752 39.685  1.00 51.89  ? 850  THR   A CA  1 
ATOM   1115 C C   . THR   A 1 157 ? 35.453 -25.681 40.558  1.00 52.06  ? 850  THR   A C   1 
ATOM   1116 O O   . THR   A 1 157 ? 34.386 -25.192 40.191  1.00 52.41  ? 850  THR   A O   1 
ATOM   1117 C CB  . THR   A 1 157 ? 37.276 -26.150 38.803  1.00 53.79  ? 850  THR   A CB  1 
ATOM   1118 O OG1 . THR   A 1 157 ? 36.906 -24.881 38.253  1.00 55.10  ? 850  THR   A OG1 1 
ATOM   1119 C CG2 . THR   A 1 157 ? 37.765 -27.085 37.724  1.00 54.46  ? 850  THR   A CG2 1 
ATOM   1120 N N   . PRO   A 1 158 ? 36.057 -25.250 41.679  1.00 51.75  ? 851  PRO   A N   1 
ATOM   1121 C CA  . PRO   A 1 158 ? 35.420 -24.207 42.501  1.00 51.51  ? 851  PRO   A CA  1 
ATOM   1122 C C   . PRO   A 1 158 ? 35.038 -22.939 41.745  1.00 51.40  ? 851  PRO   A C   1 
ATOM   1123 O O   . PRO   A 1 158 ? 34.135 -22.228 42.175  1.00 51.45  ? 851  PRO   A O   1 
ATOM   1124 C CB  . PRO   A 1 158 ? 36.480 -23.909 43.560  1.00 52.14  ? 851  PRO   A CB  1 
ATOM   1125 C CG  . PRO   A 1 158 ? 37.281 -25.153 43.639  1.00 52.37  ? 851  PRO   A CG  1 
ATOM   1126 C CD  . PRO   A 1 158 ? 37.329 -25.709 42.274  1.00 50.95  ? 851  PRO   A CD  1 
ATOM   1127 N N   . GLN   A 1 159 ? 35.706 -22.648 40.623  1.00 51.39  ? 852  GLN   A N   1 
ATOM   1128 C CA  . GLN   A 1 159 ? 35.383 -21.445 39.856  1.00 51.55  ? 852  GLN   A CA  1 
ATOM   1129 C C   . GLN   A 1 159 ? 34.584 -21.757 38.558  1.00 50.16  ? 852  GLN   A C   1 
ATOM   1130 O O   . GLN   A 1 159 ? 34.444 -20.887 37.712  1.00 51.40  ? 852  GLN   A O   1 
ATOM   1131 C CB  . GLN   A 1 159 ? 36.641 -20.576 39.609  1.00 54.66  ? 852  GLN   A CB  1 
ATOM   1132 C CG  . GLN   A 1 159 ? 37.911 -21.329 39.193  1.00 61.22  ? 852  GLN   A CG  1 
ATOM   1133 C CD  . GLN   A 1 159 ? 38.686 -22.013 40.313  1.00 68.29  ? 852  GLN   A CD  1 
ATOM   1134 O OE1 . GLN   A 1 159 ? 39.143 -23.162 40.165  1.00 71.14  ? 852  GLN   A OE1 1 
ATOM   1135 N NE2 . GLN   A 1 159 ? 38.856 -21.341 41.450  1.00 68.62  ? 852  GLN   A NE2 1 
ATOM   1136 N N   . HIS   A 1 160 ? 33.975 -22.946 38.454  1.00 47.86  ? 853  HIS   A N   1 
ATOM   1137 C CA  . HIS   A 1 160 ? 33.214 -23.377 37.283  1.00 46.58  ? 853  HIS   A CA  1 
ATOM   1138 C C   . HIS   A 1 160 ? 32.065 -24.332 37.704  1.00 45.43  ? 853  HIS   A C   1 
ATOM   1139 O O   . HIS   A 1 160 ? 32.306 -25.505 37.988  1.00 45.71  ? 853  HIS   A O   1 
ATOM   1140 C CB  . HIS   A 1 160 ? 34.174 -24.082 36.301  1.00 47.02  ? 853  HIS   A CB  1 
ATOM   1141 C CG  . HIS   A 1 160 ? 33.621 -24.453 34.946  1.00 48.22  ? 853  HIS   A CG  1 
ATOM   1142 N ND1 . HIS   A 1 160 ? 32.262 -24.517 34.696  1.00 49.42  ? 853  HIS   A ND1 1 
ATOM   1143 C CD2 . HIS   A 1 160 ? 34.284 -24.814 33.821  1.00 49.02  ? 853  HIS   A CD2 1 
ATOM   1144 C CE1 . HIS   A 1 160 ? 32.146 -24.915 33.441  1.00 49.76  ? 853  HIS   A CE1 1 
ATOM   1145 N NE2 . HIS   A 1 160 ? 33.335 -25.102 32.873  1.00 49.83  ? 853  HIS   A NE2 1 
ATOM   1146 N N   . VAL   A 1 161 ? 30.820 -23.829 37.729  1.00 43.81  ? 854  VAL   A N   1 
ATOM   1147 C CA  . VAL   A 1 161 ? 29.658 -24.631 38.106  1.00 42.68  ? 854  VAL   A CA  1 
ATOM   1148 C C   . VAL   A 1 161 ? 28.751 -24.912 36.902  1.00 41.54  ? 854  VAL   A C   1 
ATOM   1149 O O   . VAL   A 1 161 ? 28.791 -24.192 35.914  1.00 41.02  ? 854  VAL   A O   1 
ATOM   1150 C CB  . VAL   A 1 161 ? 28.883 -24.061 39.323  1.00 43.04  ? 854  VAL   A CB  1 
ATOM   1151 C CG1 . VAL   A 1 161 ? 29.806 -23.930 40.542  1.00 43.79  ? 854  VAL   A CG1 1 
ATOM   1152 C CG2 . VAL   A 1 161 ? 28.227 -22.729 38.996  1.00 43.05  ? 854  VAL   A CG2 1 
ATOM   1153 N N   . LYS   A 1 162 ? 28.013 -26.026 36.951  1.00 41.09  ? 855  LYS   A N   1 
ATOM   1154 C CA  . LYS   A 1 162 ? 27.137 -26.456 35.864  1.00 40.66  ? 855  LYS   A CA  1 
ATOM   1155 C C   . LYS   A 1 162 ? 25.787 -26.910 36.405  1.00 40.69  ? 855  LYS   A C   1 
ATOM   1156 O O   . LYS   A 1 162 ? 25.742 -27.609 37.402  1.00 41.08  ? 855  LYS   A O   1 
ATOM   1157 C CB  . LYS   A 1 162 ? 27.769 -27.643 35.146  1.00 41.38  ? 855  LYS   A CB  1 
ATOM   1158 C CG  . LYS   A 1 162 ? 28.885 -27.288 34.196  1.00 45.82  ? 855  LYS   A CG  1 
ATOM   1159 C CD  . LYS   A 1 162 ? 29.703 -28.527 33.870  1.00 51.12  ? 855  LYS   A CD  1 
ATOM   1160 C CE  . LYS   A 1 162 ? 30.407 -28.426 32.547  1.00 56.12  ? 855  LYS   A CE  1 
ATOM   1161 N NZ  . LYS   A 1 162 ? 29.443 -28.527 31.411  1.00 61.00  ? 855  LYS   A NZ  1 
ATOM   1162 N N   . ILE   A 1 163 ? 24.707 -26.604 35.711  1.00 40.30  ? 856  ILE   A N   1 
ATOM   1163 C CA  . ILE   A 1 163 ? 23.370 -27.034 36.099  1.00 40.87  ? 856  ILE   A CA  1 
ATOM   1164 C C   . ILE   A 1 163 ? 23.086 -28.420 35.553  1.00 41.49  ? 856  ILE   A C   1 
ATOM   1165 O O   . ILE   A 1 163 ? 23.317 -28.683 34.379  1.00 41.11  ? 856  ILE   A O   1 
ATOM   1166 C CB  . ILE   A 1 163 ? 22.333 -26.008 35.579  1.00 41.55  ? 856  ILE   A CB  1 
ATOM   1167 C CG1 . ILE   A 1 163 ? 22.600 -24.633 36.176  1.00 42.46  ? 856  ILE   A CG1 1 
ATOM   1168 C CG2 . ILE   A 1 163 ? 20.893 -26.467 35.828  1.00 41.99  ? 856  ILE   A CG2 1 
ATOM   1169 C CD1 . ILE   A 1 163 ? 22.037 -23.623 35.378  1.00 44.40  ? 856  ILE   A CD1 1 
ATOM   1170 N N   . THR   A 1 164 ? 22.559 -29.299 36.394  1.00 42.71  ? 857  THR   A N   1 
ATOM   1171 C CA  . THR   A 1 164 ? 22.204 -30.661 36.017  1.00 44.76  ? 857  THR   A CA  1 
ATOM   1172 C C   . THR   A 1 164 ? 20.691 -30.919 36.231  1.00 46.94  ? 857  THR   A C   1 
ATOM   1173 O O   . THR   A 1 164 ? 19.999 -30.041 36.735  1.00 47.33  ? 857  THR   A O   1 
ATOM   1174 C CB  . THR   A 1 164 ? 23.077 -31.657 36.804  1.00 46.04  ? 857  THR   A CB  1 
ATOM   1175 O OG1 . THR   A 1 164 ? 22.841 -32.957 36.261  1.00 47.81  ? 857  THR   A OG1 1 
ATOM   1176 C CG2 . THR   A 1 164 ? 22.733 -31.689 38.275  1.00 45.70  ? 857  THR   A CG2 1 
ATOM   1177 N N   . ASP   A 1 165 ? 20.189 -32.113 35.834  1.00 48.29  ? 858  ASP   A N   1 
ATOM   1178 C CA  . ASP   A 1 165 ? 18.815 -32.581 36.026  1.00 50.53  ? 858  ASP   A CA  1 
ATOM   1179 C C   . ASP   A 1 165 ? 17.759 -31.807 35.257  1.00 52.53  ? 858  ASP   A C   1 
ATOM   1180 O O   . ASP   A 1 165 ? 16.586 -31.889 35.617  1.00 53.46  ? 858  ASP   A O   1 
ATOM   1181 C CB  . ASP   A 1 165 ? 18.423 -32.675 37.510  1.00 53.21  ? 858  ASP   A CB  1 
ATOM   1182 C CG  . ASP   A 1 165 ? 19.053 -33.853 38.250  1.00 59.89  ? 858  ASP   A CG  1 
ATOM   1183 O OD1 . ASP   A 1 165 ? 20.171 -34.266 37.875  1.00 60.73  ? 858  ASP   A OD1 1 
ATOM   1184 O OD2 . ASP   A 1 165 ? 18.444 -34.336 39.226  1.00 63.05  ? 858  ASP   A OD2 1 
ATOM   1185 N N   . PHE   A 1 166 ? 18.141 -31.097 34.191  1.00 53.18  ? 859  PHE   A N   1 
ATOM   1186 C CA  . PHE   A 1 166 ? 17.155 -30.425 33.344  1.00 55.16  ? 859  PHE   A CA  1 
ATOM   1187 C C   . PHE   A 1 166 ? 16.447 -31.524 32.528  1.00 57.58  ? 859  PHE   A C   1 
ATOM   1188 O O   . PHE   A 1 166 ? 17.089 -32.495 32.112  1.00 57.81  ? 859  PHE   A O   1 
ATOM   1189 C CB  . PHE   A 1 166 ? 17.813 -29.349 32.439  1.00 54.95  ? 859  PHE   A CB  1 
ATOM   1190 C CG  . PHE   A 1 166 ? 19.024 -29.816 31.667  1.00 55.09  ? 859  PHE   A CG  1 
ATOM   1191 C CD1 . PHE   A 1 166 ? 18.884 -30.443 30.444  1.00 55.41  ? 859  PHE   A CD1 1 
ATOM   1192 C CD2 . PHE   A 1 166 ? 20.305 -29.609 32.158  1.00 55.74  ? 859  PHE   A CD2 1 
ATOM   1193 C CE1 . PHE   A 1 166 ? 19.993 -30.918 29.760  1.00 55.85  ? 859  PHE   A CE1 1 
ATOM   1194 C CE2 . PHE   A 1 166 ? 21.418 -30.065 31.460  1.00 56.34  ? 859  PHE   A CE2 1 
ATOM   1195 C CZ  . PHE   A 1 166 ? 21.254 -30.700 30.256  1.00 55.91  ? 859  PHE   A CZ  1 
ATOM   1196 N N   . GLY   A 1 167 ? 15.126 -31.448 32.416  1.00 59.16  ? 860  GLY   A N   1 
ATOM   1197 C CA  . GLY   A 1 167 ? 14.365 -32.459 31.685  1.00 60.98  ? 860  GLY   A CA  1 
ATOM   1198 C C   . GLY   A 1 167 ? 14.121 -33.758 32.436  1.00 62.97  ? 860  GLY   A C   1 
ATOM   1199 O O   . GLY   A 1 167 ? 13.371 -34.614 31.963  1.00 62.90  ? 860  GLY   A O   1 
ATOM   1200 N N   . LEU   A 1 168 ? 14.750 -33.930 33.610  1.00 64.61  ? 861  LEU   A N   1 
ATOM   1201 C CA  . LEU   A 1 168 ? 14.580 -35.145 34.402  1.00 66.62  ? 861  LEU   A CA  1 
ATOM   1202 C C   . LEU   A 1 168 ? 13.161 -35.238 35.009  1.00 69.64  ? 861  LEU   A C   1 
ATOM   1203 O O   . LEU   A 1 168 ? 12.620 -36.337 35.151  1.00 69.83  ? 861  LEU   A O   1 
ATOM   1204 C CB  . LEU   A 1 168 ? 15.668 -35.248 35.477  1.00 66.16  ? 861  LEU   A CB  1 
ATOM   1205 C CG  . LEU   A 1 168 ? 15.702 -36.550 36.264  1.00 67.15  ? 861  LEU   A CG  1 
ATOM   1206 C CD1 . LEU   A 1 168 ? 15.966 -37.730 35.365  1.00 67.78  ? 861  LEU   A CD1 1 
ATOM   1207 C CD2 . LEU   A 1 168 ? 16.731 -36.497 37.342  1.00 67.46  ? 861  LEU   A CD2 1 
ATOM   1208 N N   . ALA   A 1 169 ? 12.540 -34.083 35.312  1.00 71.54  ? 862  ALA   A N   1 
ATOM   1209 C CA  . ALA   A 1 169 ? 11.179 -34.050 35.834  1.00 73.56  ? 862  ALA   A CA  1 
ATOM   1210 C C   . ALA   A 1 169 ? 10.197 -34.497 34.740  1.00 75.78  ? 862  ALA   A C   1 
ATOM   1211 O O   . ALA   A 1 169 ? 9.327  -35.325 35.010  1.00 76.21  ? 862  ALA   A O   1 
ATOM   1212 C CB  . ALA   A 1 169 ? 10.837 -32.652 36.322  1.00 73.64  ? 862  ALA   A CB  1 
ATOM   1213 N N   . LYS   A 1 170 ? 10.374 -34.014 33.493  1.00 77.06  ? 863  LYS   A N   1 
ATOM   1214 C CA  . LYS   A 1 170 ? 9.506  -34.429 32.381  1.00 78.82  ? 863  LYS   A CA  1 
ATOM   1215 C C   . LYS   A 1 170 ? 9.656  -35.918 32.055  1.00 80.19  ? 863  LYS   A C   1 
ATOM   1216 O O   . LYS   A 1 170 ? 8.696  -36.557 31.638  1.00 80.78  ? 863  LYS   A O   1 
ATOM   1217 C CB  . LYS   A 1 170 ? 9.740  -33.572 31.119  1.00 81.14  ? 863  LYS   A CB  1 
ATOM   1218 C CG  . LYS   A 1 170 ? 8.671  -33.798 30.039  1.00 85.46  ? 863  LYS   A CG  1 
ATOM   1219 C CD  . LYS   A 1 170 ? 8.779  -32.837 28.867  1.00 89.63  ? 863  LYS   A CD  1 
ATOM   1220 N N   . LEU   A 1 171 ? 10.851 -36.475 32.258  1.00 80.81  ? 864  LEU   A N   1 
ATOM   1221 C CA  . LEU   A 1 171 ? 11.112 -37.893 32.021  1.00 81.83  ? 864  LEU   A CA  1 
ATOM   1222 C C   . LEU   A 1 171 ? 10.345 -38.764 33.023  1.00 83.09  ? 864  LEU   A C   1 
ATOM   1223 O O   . LEU   A 1 171 ? 9.854  -39.835 32.667  1.00 83.67  ? 864  LEU   A O   1 
ATOM   1224 C CB  . LEU   A 1 171 ? 12.615 -38.160 32.151  1.00 81.87  ? 864  LEU   A CB  1 
ATOM   1225 C CG  . LEU   A 1 171 ? 13.062 -39.585 31.892  1.00 83.05  ? 864  LEU   A CG  1 
ATOM   1226 C CD1 . LEU   A 1 171 ? 12.890 -39.938 30.450  1.00 83.55  ? 864  LEU   A CD1 1 
ATOM   1227 C CD2 . LEU   A 1 171 ? 14.508 -39.780 32.290  1.00 83.70  ? 864  LEU   A CD2 1 
ATOM   1228 N N   . LEU   A 1 172 ? 10.224 -38.301 34.270  1.00 83.42  ? 865  LEU   A N   1 
ATOM   1229 C CA  . LEU   A 1 172 ? 9.541  -39.059 35.312  1.00 84.16  ? 865  LEU   A CA  1 
ATOM   1230 C C   . LEU   A 1 172 ? 8.016  -38.936 35.294  1.00 85.05  ? 865  LEU   A C   1 
ATOM   1231 O O   . LEU   A 1 172 ? 7.322  -39.840 35.760  1.00 85.24  ? 865  LEU   A O   1 
ATOM   1232 C CB  . LEU   A 1 172 ? 10.098 -38.676 36.684  1.00 84.08  ? 865  LEU   A CB  1 
ATOM   1233 C CG  . LEU   A 1 172 ? 11.582 -38.939 36.859  1.00 85.01  ? 865  LEU   A CG  1 
ATOM   1234 C CD1 . LEU   A 1 172 ? 12.098 -38.319 38.137  1.00 85.49  ? 865  LEU   A CD1 1 
ATOM   1235 C CD2 . LEU   A 1 172 ? 11.885 -40.417 36.804  1.00 85.41  ? 865  LEU   A CD2 1 
ATOM   1236 N N   . GLY   A 1 173 ? 7.509  -37.830 34.766  1.00 85.31  ? 866  GLY   A N   1 
ATOM   1237 C CA  . GLY   A 1 173 ? 6.072  -37.589 34.708  1.00 85.77  ? 866  GLY   A CA  1 
ATOM   1238 C C   . GLY   A 1 173 ? 5.606  -36.634 35.789  1.00 86.03  ? 866  GLY   A C   1 
ATOM   1239 O O   . GLY   A 1 173 ? 6.349  -35.739 36.202  1.00 85.99  ? 866  GLY   A O   1 
ATOM   1240 N N   . LYS   A 1 185 ? 9.031  -36.955 46.255  1.00 72.30  ? 878  LYS   A N   1 
ATOM   1241 C CA  . LYS   A 1 185 ? 8.871  -35.712 47.017  1.00 72.58  ? 878  LYS   A CA  1 
ATOM   1242 C C   . LYS   A 1 185 ? 8.964  -34.466 46.122  1.00 71.94  ? 878  LYS   A C   1 
ATOM   1243 O O   . LYS   A 1 185 ? 10.002 -34.222 45.497  1.00 72.30  ? 878  LYS   A O   1 
ATOM   1244 C CB  . LYS   A 1 185 ? 9.890  -35.634 48.170  1.00 74.63  ? 878  LYS   A CB  1 
ATOM   1245 N N   . VAL   A 1 186 ? 7.869  -33.683 46.065  1.00 70.60  ? 879  VAL   A N   1 
ATOM   1246 C CA  . VAL   A 1 186 ? 7.785  -32.456 45.270  1.00 69.50  ? 879  VAL   A CA  1 
ATOM   1247 C C   . VAL   A 1 186 ? 8.558  -31.326 45.985  1.00 67.93  ? 879  VAL   A C   1 
ATOM   1248 O O   . VAL   A 1 186 ? 8.439  -31.182 47.207  1.00 68.38  ? 879  VAL   A O   1 
ATOM   1249 C CB  . VAL   A 1 186 ? 6.306  -32.092 44.994  1.00 70.13  ? 879  VAL   A CB  1 
ATOM   1250 N N   . PRO   A 1 187 ? 9.404  -30.554 45.264  1.00 65.65  ? 880  PRO   A N   1 
ATOM   1251 C CA  . PRO   A 1 187 ? 10.205 -29.512 45.936  1.00 63.99  ? 880  PRO   A CA  1 
ATOM   1252 C C   . PRO   A 1 187 ? 9.459  -28.188 46.146  1.00 62.20  ? 880  PRO   A C   1 
ATOM   1253 O O   . PRO   A 1 187 ? 9.848  -27.159 45.592  1.00 62.31  ? 880  PRO   A O   1 
ATOM   1254 C CB  . PRO   A 1 187 ? 11.409 -29.357 45.013  1.00 64.56  ? 880  PRO   A CB  1 
ATOM   1255 C CG  . PRO   A 1 187 ? 10.880 -29.699 43.656  1.00 65.48  ? 880  PRO   A CG  1 
ATOM   1256 C CD  . PRO   A 1 187 ? 9.683  -30.602 43.816  1.00 64.57  ? 880  PRO   A CD  1 
ATOM   1257 N N   . ILE   A 1 188 ? 8.401  -28.229 46.973  1.00 59.98  ? 881  ILE   A N   1 
ATOM   1258 C CA  . ILE   A 1 188 ? 7.522  -27.113 47.306  1.00 58.56  ? 881  ILE   A CA  1 
ATOM   1259 C C   . ILE   A 1 188 ? 8.271  -25.840 47.739  1.00 56.41  ? 881  ILE   A C   1 
ATOM   1260 O O   . ILE   A 1 188 ? 7.918  -24.740 47.312  1.00 55.93  ? 881  ILE   A O   1 
ATOM   1261 C CB  . ILE   A 1 188 ? 6.492  -27.570 48.385  1.00 58.92  ? 881  ILE   A CB  1 
ATOM   1262 C CG1 . ILE   A 1 188 ? 5.731  -28.824 47.936  1.00 59.63  ? 881  ILE   A CG1 1 
ATOM   1263 C CG2 . ILE   A 1 188 ? 5.522  -26.457 48.742  1.00 59.47  ? 881  ILE   A CG2 1 
ATOM   1264 N N   . LYS   A 1 189 ? 9.324  -25.998 48.552  1.00 54.61  ? 882  LYS   A N   1 
ATOM   1265 C CA  . LYS   A 1 189 ? 10.086 -24.868 49.074  1.00 53.14  ? 882  LYS   A CA  1 
ATOM   1266 C C   . LYS   A 1 189 ? 10.988 -24.158 48.050  1.00 50.73  ? 882  LYS   A C   1 
ATOM   1267 O O   . LYS   A 1 189 ? 11.603 -23.152 48.382  1.00 50.51  ? 882  LYS   A O   1 
ATOM   1268 C CB  . LYS   A 1 189 ? 10.873 -25.300 50.305  1.00 55.59  ? 882  LYS   A CB  1 
ATOM   1269 C CG  . LYS   A 1 189 ? 9.919  -25.690 51.411  1.00 60.50  ? 882  LYS   A CG  1 
ATOM   1270 C CD  . LYS   A 1 189 ? 10.601 -26.324 52.595  1.00 65.82  ? 882  LYS   A CD  1 
ATOM   1271 C CE  . LYS   A 1 189 ? 9.596  -26.605 53.688  1.00 69.19  ? 882  LYS   A CE  1 
ATOM   1272 N NZ  . LYS   A 1 189 ? 10.257 -26.744 55.009  1.00 71.48  ? 882  LYS   A NZ  1 
ATOM   1273 N N   . TRP   A 1 190 ? 11.027 -24.642 46.810  1.00 49.03  ? 883  TRP   A N   1 
ATOM   1274 C CA  . TRP   A 1 190 ? 11.759 -24.018 45.696  1.00 47.87  ? 883  TRP   A CA  1 
ATOM   1275 C C   . TRP   A 1 190 ? 10.818 -23.536 44.576  1.00 48.26  ? 883  TRP   A C   1 
ATOM   1276 O O   . TRP   A 1 190 ? 11.252 -22.814 43.684  1.00 48.07  ? 883  TRP   A O   1 
ATOM   1277 C CB  . TRP   A 1 190 ? 12.769 -24.996 45.087  1.00 46.60  ? 883  TRP   A CB  1 
ATOM   1278 C CG  . TRP   A 1 190 ? 14.038 -25.110 45.860  1.00 45.26  ? 883  TRP   A CG  1 
ATOM   1279 C CD1 . TRP   A 1 190 ? 15.209 -24.450 45.627  1.00 45.30  ? 883  TRP   A CD1 1 
ATOM   1280 C CD2 . TRP   A 1 190 ? 14.254 -25.924 47.018  1.00 44.43  ? 883  TRP   A CD2 1 
ATOM   1281 N NE1 . TRP   A 1 190 ? 16.143 -24.800 46.576  1.00 45.42  ? 883  TRP   A NE1 1 
ATOM   1282 C CE2 . TRP   A 1 190 ? 15.578 -25.698 47.448  1.00 45.10  ? 883  TRP   A CE2 1 
ATOM   1283 C CE3 . TRP   A 1 190 ? 13.458 -26.826 47.731  1.00 44.46  ? 883  TRP   A CE3 1 
ATOM   1284 C CZ2 . TRP   A 1 190 ? 16.122 -26.352 48.556  1.00 45.61  ? 883  TRP   A CZ2 1 
ATOM   1285 C CZ3 . TRP   A 1 190 ? 13.985 -27.441 48.852  1.00 45.40  ? 883  TRP   A CZ3 1 
ATOM   1286 C CH2 . TRP   A 1 190 ? 15.306 -27.214 49.246  1.00 45.42  ? 883  TRP   A CH2 1 
ATOM   1287 N N   . MET   A 1 191 ? 9.555  -23.971 44.605  1.00 48.91  ? 884  MET   A N   1 
ATOM   1288 C CA  . MET   A 1 191 ? 8.550  -23.673 43.613  1.00 50.57  ? 884  MET   A CA  1 
ATOM   1289 C C   . MET   A 1 191 ? 7.875  -22.326 43.783  1.00 51.49  ? 884  MET   A C   1 
ATOM   1290 O O   . MET   A 1 191 ? 7.593  -21.881 44.899  1.00 51.28  ? 884  MET   A O   1 
ATOM   1291 C CB  . MET   A 1 191 ? 7.484  -24.774 43.615  1.00 51.88  ? 884  MET   A CB  1 
ATOM   1292 C CG  . MET   A 1 191 ? 7.961  -26.074 43.043  1.00 55.68  ? 884  MET   A CG  1 
ATOM   1293 S SD  . MET   A 1 191 ? 6.888  -27.471 43.459  1.00 66.21  ? 884  MET   A SD  1 
ATOM   1294 C CE  . MET   A 1 191 ? 5.376  -26.943 42.787  1.00 63.49  ? 884  MET   A CE  1 
ATOM   1295 N N   . ALA   A 1 192 ? 7.566  -21.711 42.646  1.00 52.25  ? 885  ALA   A N   1 
ATOM   1296 C CA  . ALA   A 1 192 ? 6.818  -20.469 42.599  1.00 53.57  ? 885  ALA   A CA  1 
ATOM   1297 C C   . ALA   A 1 192 ? 5.374  -20.757 43.041  1.00 55.20  ? 885  ALA   A C   1 
ATOM   1298 O O   . ALA   A 1 192 ? 4.891  -21.882 42.886  1.00 55.73  ? 885  ALA   A O   1 
ATOM   1299 C CB  . ALA   A 1 192 ? 6.841  -19.913 41.184  1.00 53.55  ? 885  ALA   A CB  1 
ATOM   1300 N N   . LEU   A 1 193 ? 4.679  -19.758 43.595  1.00 55.86  ? 886  LEU   A N   1 
ATOM   1301 C CA  . LEU   A 1 193 ? 3.307  -19.933 44.059  1.00 56.78  ? 886  LEU   A CA  1 
ATOM   1302 C C   . LEU   A 1 193 ? 2.365  -20.517 42.992  1.00 58.09  ? 886  LEU   A C   1 
ATOM   1303 O O   . LEU   A 1 193 ? 1.551  -21.374 43.319  1.00 58.55  ? 886  LEU   A O   1 
ATOM   1304 C CB  . LEU   A 1 193 ? 2.764  -18.613 44.616  1.00 56.87  ? 886  LEU   A CB  1 
ATOM   1305 C CG  . LEU   A 1 193 ? 1.376  -18.687 45.239  1.00 57.95  ? 886  LEU   A CG  1 
ATOM   1306 C CD1 . LEU   A 1 193 ? 1.394  -19.501 46.507  1.00 58.43  ? 886  LEU   A CD1 1 
ATOM   1307 C CD2 . LEU   A 1 193 ? 0.826  -17.318 45.496  1.00 58.02  ? 886  LEU   A CD2 1 
ATOM   1308 N N   . GLU   A 1 194 ? 2.508  -20.106 41.718  1.00 58.65  ? 887  GLU   A N   1 
ATOM   1309 C CA  . GLU   A 1 194 ? 1.654  -20.613 40.632  1.00 59.66  ? 887  GLU   A CA  1 
ATOM   1310 C C   . GLU   A 1 194 ? 1.924  -22.084 40.305  1.00 60.60  ? 887  GLU   A C   1 
ATOM   1311 O O   . GLU   A 1 194 ? 1.023  -22.777 39.842  1.00 60.82  ? 887  GLU   A O   1 
ATOM   1312 C CB  . GLU   A 1 194 ? 1.724  -19.724 39.368  1.00 61.49  ? 887  GLU   A CB  1 
ATOM   1313 C CG  . GLU   A 1 194 ? 2.989  -19.875 38.537  1.00 66.83  ? 887  GLU   A CG  1 
ATOM   1314 C CD  . GLU   A 1 194 ? 4.141  -18.961 38.929  1.00 73.28  ? 887  GLU   A CD  1 
ATOM   1315 O OE1 . GLU   A 1 194 ? 4.054  -18.316 40.001  1.00 75.05  ? 887  GLU   A OE1 1 
ATOM   1316 O OE2 . GLU   A 1 194 ? 5.129  -18.888 38.162  1.00 73.80  ? 887  GLU   A OE2 1 
ATOM   1317 N N   . SER   A 1 195 ? 3.145  -22.570 40.567  1.00 61.03  ? 888  SER   A N   1 
ATOM   1318 C CA  . SER   A 1 195 ? 3.481  -23.977 40.355  1.00 61.85  ? 888  SER   A CA  1 
ATOM   1319 C C   . SER   A 1 195 ? 2.891  -24.834 41.476  1.00 62.68  ? 888  SER   A C   1 
ATOM   1320 O O   . SER   A 1 195 ? 2.468  -25.954 41.220  1.00 62.94  ? 888  SER   A O   1 
ATOM   1321 C CB  . SER   A 1 195 ? 4.994  -24.168 40.312  1.00 63.21  ? 888  SER   A CB  1 
ATOM   1322 O OG  . SER   A 1 195 ? 5.588  -23.406 39.273  1.00 65.24  ? 888  SER   A OG  1 
ATOM   1323 N N   . ILE   A 1 196 ? 2.859  -24.316 42.712  1.00 63.16  ? 889  ILE   A N   1 
ATOM   1324 C CA  . ILE   A 1 196 ? 2.287  -25.030 43.849  1.00 64.30  ? 889  ILE   A CA  1 
ATOM   1325 C C   . ILE   A 1 196 ? 0.774  -25.164 43.683  1.00 65.34  ? 889  ILE   A C   1 
ATOM   1326 O O   . ILE   A 1 196 ? 0.224  -26.253 43.836  1.00 65.71  ? 889  ILE   A O   1 
ATOM   1327 C CB  . ILE   A 1 196 ? 2.633  -24.312 45.185  1.00 64.82  ? 889  ILE   A CB  1 
ATOM   1328 C CG1 . ILE   A 1 196 ? 4.160  -24.217 45.405  1.00 65.74  ? 889  ILE   A CG1 1 
ATOM   1329 C CG2 . ILE   A 1 196 ? 1.937  -24.989 46.361  1.00 65.22  ? 889  ILE   A CG2 1 
ATOM   1330 C CD1 . ILE   A 1 196 ? 4.568  -23.372 46.605  1.00 66.70  ? 889  ILE   A CD1 1 
ATOM   1331 N N   . LEU   A 1 197 ? 0.110  -24.065 43.325  1.00 65.70  ? 890  LEU   A N   1 
ATOM   1332 C CA  . LEU   A 1 197 ? -1.337 -24.032 43.203  1.00 66.61  ? 890  LEU   A CA  1 
ATOM   1333 C C   . LEU   A 1 197 ? -1.914 -24.598 41.926  1.00 68.39  ? 890  LEU   A C   1 
ATOM   1334 O O   . LEU   A 1 197 ? -3.048 -25.087 41.957  1.00 69.23  ? 890  LEU   A O   1 
ATOM   1335 C CB  . LEU   A 1 197 ? -1.852 -22.597 43.386  1.00 66.27  ? 890  LEU   A CB  1 
ATOM   1336 C CG  . LEU   A 1 197 ? -1.414 -21.866 44.645  1.00 66.84  ? 890  LEU   A CG  1 
ATOM   1337 C CD1 . LEU   A 1 197 ? -1.948 -20.453 44.655  1.00 66.91  ? 890  LEU   A CD1 1 
ATOM   1338 C CD2 . LEU   A 1 197 ? -1.828 -22.622 45.895  1.00 67.07  ? 890  LEU   A CD2 1 
ATOM   1339 N N   . HIS   A 1 198 ? -1.215 -24.456 40.787  1.00 68.88  ? 891  HIS   A N   1 
ATOM   1340 C CA  . HIS   A 1 198 ? -1.785 -24.892 39.510  1.00 69.88  ? 891  HIS   A CA  1 
ATOM   1341 C C   . HIS   A 1 198 ? -0.894 -25.741 38.641  1.00 70.00  ? 891  HIS   A C   1 
ATOM   1342 O O   . HIS   A 1 198 ? -1.263 -26.004 37.495  1.00 70.11  ? 891  HIS   A O   1 
ATOM   1343 C CB  . HIS   A 1 198 ? -2.256 -23.676 38.703  1.00 71.58  ? 891  HIS   A CB  1 
ATOM   1344 C CG  . HIS   A 1 198 ? -3.205 -22.797 39.450  1.00 75.34  ? 891  HIS   A CG  1 
ATOM   1345 N ND1 . HIS   A 1 198 ? -2.827 -21.541 39.894  1.00 77.76  ? 891  HIS   A ND1 1 
ATOM   1346 C CD2 . HIS   A 1 198 ? -4.477 -23.038 39.847  1.00 76.84  ? 891  HIS   A CD2 1 
ATOM   1347 C CE1 . HIS   A 1 198 ? -3.884 -21.047 40.523  1.00 78.33  ? 891  HIS   A CE1 1 
ATOM   1348 N NE2 . HIS   A 1 198 ? -4.900 -21.913 40.523  1.00 78.23  ? 891  HIS   A NE2 1 
ATOM   1349 N N   . ARG   A 1 199 ? 0.281  -26.145 39.148  1.00 69.73  ? 892  ARG   A N   1 
ATOM   1350 C CA  . ARG   A 1 199 ? 1.247  -26.929 38.385  1.00 69.73  ? 892  ARG   A CA  1 
ATOM   1351 C C   . ARG   A 1 199 ? 1.667  -26.217 37.091  1.00 69.09  ? 892  ARG   A C   1 
ATOM   1352 O O   . ARG   A 1 199 ? 1.889  -26.862 36.065  1.00 69.75  ? 892  ARG   A O   1 
ATOM   1353 C CB  . ARG   A 1 199 ? 0.744  -28.363 38.137  1.00 71.39  ? 892  ARG   A CB  1 
ATOM   1354 C CG  . ARG   A 1 199 ? 0.777  -29.236 39.388  1.00 74.35  ? 892  ARG   A CG  1 
ATOM   1355 N N   . ILE   A 1 200 ? 1.770  -24.879 37.145  1.00 67.62  ? 893  ILE   A N   1 
ATOM   1356 C CA  . ILE   A 1 200 ? 2.196  -24.069 36.013  1.00 66.55  ? 893  ILE   A CA  1 
ATOM   1357 C C   . ILE   A 1 200 ? 3.716  -23.902 36.083  1.00 65.23  ? 893  ILE   A C   1 
ATOM   1358 O O   . ILE   A 1 200 ? 4.242  -23.370 37.064  1.00 65.31  ? 893  ILE   A O   1 
ATOM   1359 C CB  . ILE   A 1 200 ? 1.466  -22.703 36.002  1.00 67.22  ? 893  ILE   A CB  1 
ATOM   1360 C CG1 . ILE   A 1 200 ? -0.040 -22.873 35.703  1.00 68.41  ? 893  ILE   A CG1 1 
ATOM   1361 C CG2 . ILE   A 1 200 ? 2.111  -21.733 35.017  1.00 67.70  ? 893  ILE   A CG2 1 
ATOM   1362 N N   . TYR   A 1 201 ? 4.424  -24.378 35.056  1.00 63.85  ? 894  TYR   A N   1 
ATOM   1363 C CA  . TYR   A 1 201 ? 5.874  -24.266 35.012  1.00 62.92  ? 894  TYR   A CA  1 
ATOM   1364 C C   . TYR   A 1 201 ? 6.296  -23.494 33.783  1.00 61.73  ? 894  TYR   A C   1 
ATOM   1365 O O   . TYR   A 1 201 ? 5.947  -23.856 32.663  1.00 61.87  ? 894  TYR   A O   1 
ATOM   1366 C CB  . TYR   A 1 201 ? 6.541  -25.637 35.042  1.00 62.90  ? 894  TYR   A CB  1 
ATOM   1367 C CG  . TYR   A 1 201 ? 6.349  -26.385 36.339  1.00 63.99  ? 894  TYR   A CG  1 
ATOM   1368 C CD1 . TYR   A 1 201 ? 7.220  -26.206 37.402  1.00 65.02  ? 894  TYR   A CD1 1 
ATOM   1369 C CD2 . TYR   A 1 201 ? 5.329  -27.315 36.484  1.00 65.22  ? 894  TYR   A CD2 1 
ATOM   1370 C CE1 . TYR   A 1 201 ? 7.066  -26.914 38.587  1.00 66.08  ? 894  TYR   A CE1 1 
ATOM   1371 C CE2 . TYR   A 1 201 ? 5.179  -28.045 37.656  1.00 66.28  ? 894  TYR   A CE2 1 
ATOM   1372 C CZ  . TYR   A 1 201 ? 6.044  -27.836 38.709  1.00 67.28  ? 894  TYR   A CZ  1 
ATOM   1373 O OH  . TYR   A 1 201 ? 5.882  -28.550 39.868  1.00 69.30  ? 894  TYR   A OH  1 
ATOM   1374 N N   . THR   A 1 202 ? 7.014  -22.393 34.002  1.00 60.36  ? 895  THR   A N   1 
ATOM   1375 C CA  . THR   A 1 202 ? 7.500  -21.497 32.959  1.00 59.34  ? 895  THR   A CA  1 
ATOM   1376 C C   . THR   A 1 202 ? 8.967  -21.120 33.263  1.00 58.12  ? 895  THR   A C   1 
ATOM   1377 O O   . THR   A 1 202 ? 9.519  -21.537 34.290  1.00 58.00  ? 895  THR   A O   1 
ATOM   1378 C CB  . THR   A 1 202 ? 6.592  -20.223 32.915  1.00 60.34  ? 895  THR   A CB  1 
ATOM   1379 O OG1 . THR   A 1 202 ? 6.829  -19.428 34.083  1.00 61.51  ? 895  THR   A OG1 1 
ATOM   1380 C CG2 . THR   A 1 202 ? 5.121  -20.539 32.772  1.00 60.30  ? 895  THR   A CG2 1 
ATOM   1381 N N   . HIS   A 1 203 ? 9.601  -20.325 32.382  1.00 57.21  ? 896  HIS   A N   1 
ATOM   1382 C CA  . HIS   A 1 203 ? 10.931 -19.812 32.670  1.00 56.67  ? 896  HIS   A CA  1 
ATOM   1383 C C   . HIS   A 1 203 ? 10.865 -18.807 33.837  1.00 55.42  ? 896  HIS   A C   1 
ATOM   1384 O O   . HIS   A 1 203 ? 11.844 -18.676 34.568  1.00 55.62  ? 896  HIS   A O   1 
ATOM   1385 C CB  . HIS   A 1 203 ? 11.558 -19.207 31.423  1.00 57.87  ? 896  HIS   A CB  1 
ATOM   1386 C CG  . HIS   A 1 203 ? 11.704 -20.210 30.324  1.00 59.89  ? 896  HIS   A CG  1 
ATOM   1387 N ND1 . HIS   A 1 203 ? 10.974 -20.110 29.152  1.00 61.56  ? 896  HIS   A ND1 1 
ATOM   1388 C CD2 . HIS   A 1 203 ? 12.462 -21.330 30.279  1.00 60.92  ? 896  HIS   A CD2 1 
ATOM   1389 C CE1 . HIS   A 1 203 ? 11.322 -21.160 28.428  1.00 62.29  ? 896  HIS   A CE1 1 
ATOM   1390 N NE2 . HIS   A 1 203 ? 12.213 -21.928 29.071  1.00 62.08  ? 896  HIS   A NE2 1 
ATOM   1391 N N   . GLN   A 1 204 ? 9.688  -18.182 34.087  1.00 53.96  ? 897  GLN   A N   1 
ATOM   1392 C CA  . GLN   A 1 204 ? 9.523  -17.265 35.203  1.00 53.06  ? 897  GLN   A CA  1 
ATOM   1393 C C   . GLN   A 1 204 ? 9.363  -17.994 36.532  1.00 52.30  ? 897  GLN   A C   1 
ATOM   1394 O O   . GLN   A 1 204 ? 9.832  -17.478 37.546  1.00 53.46  ? 897  GLN   A O   1 
ATOM   1395 C CB  . GLN   A 1 204 ? 8.412  -16.246 34.943  1.00 53.66  ? 897  GLN   A CB  1 
ATOM   1396 C CG  . GLN   A 1 204 ? 8.746  -15.307 33.776  1.00 55.75  ? 897  GLN   A CG  1 
ATOM   1397 C CD  . GLN   A 1 204 ? 10.101 -14.615 33.903  1.00 60.59  ? 897  GLN   A CD  1 
ATOM   1398 O OE1 . GLN   A 1 204 ? 10.308 -13.719 34.739  1.00 62.54  ? 897  GLN   A OE1 1 
ATOM   1399 N NE2 . GLN   A 1 204 ? 11.056 -15.025 33.079  1.00 60.50  ? 897  GLN   A NE2 1 
ATOM   1400 N N   . SER   A 1 205 ? 8.808  -19.213 36.538  1.00 50.36  ? 898  SER   A N   1 
ATOM   1401 C CA  . SER   A 1 205 ? 8.770  -20.010 37.764  1.00 49.27  ? 898  SER   A CA  1 
ATOM   1402 C C   . SER   A 1 205 ? 10.183 -20.563 38.093  1.00 47.36  ? 898  SER   A C   1 
ATOM   1403 O O   . SER   A 1 205 ? 10.486 -20.799 39.259  1.00 46.95  ? 898  SER   A O   1 
ATOM   1404 C CB  . SER   A 1 205 ? 7.715  -21.108 37.692  1.00 51.42  ? 898  SER   A CB  1 
ATOM   1405 O OG  . SER   A 1 205 ? 8.024  -22.073 36.705  1.00 54.76  ? 898  SER   A OG  1 
ATOM   1406 N N   . ASP   A 1 206 ? 11.057 -20.723 37.073  1.00 46.23  ? 899  ASP   A N   1 
ATOM   1407 C CA  . ASP   A 1 206 ? 12.461 -21.096 37.242  1.00 45.47  ? 899  ASP   A CA  1 
ATOM   1408 C C   . ASP   A 1 206 ? 13.233 -19.934 37.891  1.00 45.01  ? 899  ASP   A C   1 
ATOM   1409 O O   . ASP   A 1 206 ? 14.203 -20.175 38.607  1.00 45.63  ? 899  ASP   A O   1 
ATOM   1410 C CB  . ASP   A 1 206 ? 13.111 -21.424 35.892  1.00 47.29  ? 899  ASP   A CB  1 
ATOM   1411 C CG  . ASP   A 1 206 ? 12.886 -22.846 35.402  1.00 52.86  ? 899  ASP   A CG  1 
ATOM   1412 O OD1 . ASP   A 1 206 ? 12.563 -23.730 36.244  1.00 53.69  ? 899  ASP   A OD1 1 
ATOM   1413 O OD2 . ASP   A 1 206 ? 13.032 -23.081 34.178  1.00 54.55  ? 899  ASP   A OD2 1 
ATOM   1414 N N   . VAL   A 1 207 ? 12.833 -18.675 37.605  1.00 44.20  ? 900  VAL   A N   1 
ATOM   1415 C CA  . VAL   A 1 207 ? 13.410 -17.471 38.184  1.00 43.83  ? 900  VAL   A CA  1 
ATOM   1416 C C   . VAL   A 1 207 ? 13.176 -17.478 39.684  1.00 43.52  ? 900  VAL   A C   1 
ATOM   1417 O O   . VAL   A 1 207 ? 14.110 -17.187 40.441  1.00 44.16  ? 900  VAL   A O   1 
ATOM   1418 C CB  . VAL   A 1 207 ? 12.907 -16.186 37.489  1.00 44.47  ? 900  VAL   A CB  1 
ATOM   1419 C CG1 . VAL   A 1 207 ? 13.217 -14.946 38.319  1.00 44.89  ? 900  VAL   A CG1 1 
ATOM   1420 C CG2 . VAL   A 1 207 ? 13.529 -16.068 36.106  1.00 44.80  ? 900  VAL   A CG2 1 
ATOM   1421 N N   . TRP   A 1 208 ? 11.967 -17.900 40.128  1.00 42.21  ? 901  TRP   A N   1 
ATOM   1422 C CA  . TRP   A 1 208 ? 11.661 -18.062 41.543  1.00 41.60  ? 901  TRP   A CA  1 
ATOM   1423 C C   . TRP   A 1 208 ? 12.637 -19.065 42.184  1.00 41.56  ? 901  TRP   A C   1 
ATOM   1424 O O   . TRP   A 1 208 ? 13.284 -18.712 43.164  1.00 42.42  ? 901  TRP   A O   1 
ATOM   1425 C CB  . TRP   A 1 208 ? 10.211 -18.525 41.748  1.00 41.13  ? 901  TRP   A CB  1 
ATOM   1426 C CG  . TRP   A 1 208 ? 9.826  -18.662 43.192  1.00 40.70  ? 901  TRP   A CG  1 
ATOM   1427 C CD1 . TRP   A 1 208 ? 10.366 -19.511 44.115  1.00 41.04  ? 901  TRP   A CD1 1 
ATOM   1428 C CD2 . TRP   A 1 208 ? 8.803  -17.926 43.871  1.00 40.53  ? 901  TRP   A CD2 1 
ATOM   1429 N NE1 . TRP   A 1 208 ? 9.755  -19.335 45.331  1.00 41.34  ? 901  TRP   A NE1 1 
ATOM   1430 C CE2 . TRP   A 1 208 ? 8.785  -18.372 45.207  1.00 41.33  ? 901  TRP   A CE2 1 
ATOM   1431 C CE3 . TRP   A 1 208 ? 7.843  -16.998 43.460  1.00 40.88  ? 901  TRP   A CE3 1 
ATOM   1432 C CZ2 . TRP   A 1 208 ? 7.873  -17.884 46.139  1.00 42.17  ? 901  TRP   A CZ2 1 
ATOM   1433 C CZ3 . TRP   A 1 208 ? 6.970  -16.491 44.393  1.00 41.79  ? 901  TRP   A CZ3 1 
ATOM   1434 C CH2 . TRP   A 1 208 ? 6.987  -16.937 45.714  1.00 42.16  ? 901  TRP   A CH2 1 
ATOM   1435 N N   . SER   A 1 209 ? 12.799 -20.267 41.594  1.00 40.78  ? 902  SER   A N   1 
ATOM   1436 C CA  . SER   A 1 209 ? 13.731 -21.314 42.063  1.00 40.63  ? 902  SER   A CA  1 
ATOM   1437 C C   . SER   A 1 209 ? 15.176 -20.832 42.075  1.00 39.48  ? 902  SER   A C   1 
ATOM   1438 O O   . SER   A 1 209 ? 15.957 -21.272 42.911  1.00 39.61  ? 902  SER   A O   1 
ATOM   1439 C CB  . SER   A 1 209 ? 13.626 -22.565 41.199  1.00 42.19  ? 902  SER   A CB  1 
ATOM   1440 O OG  . SER   A 1 209 ? 12.272 -22.965 41.076  1.00 45.88  ? 902  SER   A OG  1 
ATOM   1441 N N   . TYR   A 1 210 ? 15.533 -19.952 41.143  1.00 38.59  ? 903  TYR   A N   1 
ATOM   1442 C CA  . TYR   A 1 210 ? 16.851 -19.346 41.083  1.00 38.91  ? 903  TYR   A CA  1 
ATOM   1443 C C   . TYR   A 1 210 ? 17.081 -18.464 42.312  1.00 40.03  ? 903  TYR   A C   1 
ATOM   1444 O O   . TYR   A 1 210 ? 18.178 -18.493 42.866  1.00 40.98  ? 903  TYR   A O   1 
ATOM   1445 C CB  . TYR   A 1 210 ? 17.007 -18.533 39.795  1.00 38.44  ? 903  TYR   A CB  1 
ATOM   1446 C CG  . TYR   A 1 210 ? 18.306 -17.764 39.734  1.00 38.01  ? 903  TYR   A CG  1 
ATOM   1447 C CD1 . TYR   A 1 210 ? 19.488 -18.388 39.380  1.00 37.59  ? 903  TYR   A CD1 1 
ATOM   1448 C CD2 . TYR   A 1 210 ? 18.352 -16.416 40.052  1.00 38.32  ? 903  TYR   A CD2 1 
ATOM   1449 C CE1 . TYR   A 1 210 ? 20.682 -17.691 39.343  1.00 38.15  ? 903  TYR   A CE1 1 
ATOM   1450 C CE2 . TYR   A 1 210 ? 19.543 -15.718 40.041  1.00 38.79  ? 903  TYR   A CE2 1 
ATOM   1451 C CZ  . TYR   A 1 210 ? 20.706 -16.357 39.679  1.00 39.10  ? 903  TYR   A CZ  1 
ATOM   1452 O OH  . TYR   A 1 210 ? 21.869 -15.644 39.622  1.00 40.91  ? 903  TYR   A OH  1 
ATOM   1453 N N   . GLY   A 1 211 ? 16.052 -17.722 42.742  1.00 39.76  ? 904  GLY   A N   1 
ATOM   1454 C CA  . GLY   A 1 211 ? 16.112 -16.876 43.928  1.00 39.94  ? 904  GLY   A CA  1 
ATOM   1455 C C   . GLY   A 1 211 ? 16.330 -17.695 45.185  1.00 41.17  ? 904  GLY   A C   1 
ATOM   1456 O O   . GLY   A 1 211 ? 17.111 -17.304 46.057  1.00 41.54  ? 904  GLY   A O   1 
ATOM   1457 N N   . VAL   A 1 212 ? 15.648 -18.863 45.285  1.00 40.83  ? 905  VAL   A N   1 
ATOM   1458 C CA  . VAL   A 1 212 ? 15.793 -19.777 46.408  1.00 40.40  ? 905  VAL   A CA  1 
ATOM   1459 C C   . VAL   A 1 212 ? 17.187 -20.415 46.397  1.00 41.76  ? 905  VAL   A C   1 
ATOM   1460 O O   . VAL   A 1 212 ? 17.761 -20.622 47.460  1.00 42.72  ? 905  VAL   A O   1 
ATOM   1461 C CB  . VAL   A 1 212 ? 14.659 -20.831 46.450  1.00 40.16  ? 905  VAL   A CB  1 
ATOM   1462 C CG1 . VAL   A 1 212 ? 14.848 -21.801 47.625  1.00 40.38  ? 905  VAL   A CG1 1 
ATOM   1463 C CG2 . VAL   A 1 212 ? 13.290 -20.158 46.534  1.00 40.14  ? 905  VAL   A CG2 1 
ATOM   1464 N N   . THR   A 1 213 ? 17.755 -20.682 45.198  1.00 41.83  ? 906  THR   A N   1 
ATOM   1465 C CA  . THR   A 1 213 ? 19.097 -21.243 45.016  1.00 42.23  ? 906  THR   A CA  1 
ATOM   1466 C C   . THR   A 1 213 ? 20.156 -20.233 45.455  1.00 43.00  ? 906  THR   A C   1 
ATOM   1467 O O   . THR   A 1 213 ? 21.102 -20.608 46.131  1.00 43.82  ? 906  THR   A O   1 
ATOM   1468 C CB  . THR   A 1 213 ? 19.288 -21.707 43.567  1.00 43.11  ? 906  THR   A CB  1 
ATOM   1469 O OG1 . THR   A 1 213 ? 18.304 -22.697 43.276  1.00 44.22  ? 906  THR   A OG1 1 
ATOM   1470 C CG2 . THR   A 1 213 ? 20.670 -22.284 43.305  1.00 42.96  ? 906  THR   A CG2 1 
ATOM   1471 N N   . VAL   A 1 214 ? 19.983 -18.947 45.110  1.00 42.97  ? 907  VAL   A N   1 
ATOM   1472 C CA  . VAL   A 1 214 ? 20.890 -17.879 45.526  1.00 42.84  ? 907  VAL   A CA  1 
ATOM   1473 C C   . VAL   A 1 214 ? 20.829 -17.754 47.047  1.00 42.75  ? 907  VAL   A C   1 
ATOM   1474 O O   . VAL   A 1 214 ? 21.874 -17.671 47.679  1.00 42.91  ? 907  VAL   A O   1 
ATOM   1475 C CB  . VAL   A 1 214 ? 20.568 -16.532 44.814  1.00 43.52  ? 907  VAL   A CB  1 
ATOM   1476 C CG1 . VAL   A 1 214 ? 21.321 -15.371 45.449  1.00 43.91  ? 907  VAL   A CG1 1 
ATOM   1477 C CG2 . VAL   A 1 214 ? 20.877 -16.615 43.332  1.00 43.90  ? 907  VAL   A CG2 1 
ATOM   1478 N N   . TRP   A 1 215 ? 19.621 -17.831 47.639  1.00 42.72  ? 908  TRP   A N   1 
ATOM   1479 C CA  . TRP   A 1 215 ? 19.401 -17.791 49.086  1.00 42.82  ? 908  TRP   A CA  1 
ATOM   1480 C C   . TRP   A 1 215 ? 20.113 -18.947 49.777  1.00 44.43  ? 908  TRP   A C   1 
ATOM   1481 O O   . TRP   A 1 215 ? 20.669 -18.756 50.850  1.00 45.31  ? 908  TRP   A O   1 
ATOM   1482 C CB  . TRP   A 1 215 ? 17.896 -17.800 49.421  1.00 41.87  ? 908  TRP   A CB  1 
ATOM   1483 C CG  . TRP   A 1 215 ? 17.615 -17.606 50.880  1.00 41.15  ? 908  TRP   A CG  1 
ATOM   1484 C CD1 . TRP   A 1 215 ? 17.448 -16.423 51.532  1.00 41.48  ? 908  TRP   A CD1 1 
ATOM   1485 C CD2 . TRP   A 1 215 ? 17.541 -18.633 51.884  1.00 40.94  ? 908  TRP   A CD2 1 
ATOM   1486 N NE1 . TRP   A 1 215 ? 17.257 -16.646 52.875  1.00 41.60  ? 908  TRP   A NE1 1 
ATOM   1487 C CE2 . TRP   A 1 215 ? 17.327 -17.993 53.120  1.00 41.36  ? 908  TRP   A CE2 1 
ATOM   1488 C CE3 . TRP   A 1 215 ? 17.645 -20.032 51.857  1.00 41.32  ? 908  TRP   A CE3 1 
ATOM   1489 C CZ2 . TRP   A 1 215 ? 17.203 -18.699 54.309  1.00 42.18  ? 908  TRP   A CZ2 1 
ATOM   1490 C CZ3 . TRP   A 1 215 ? 17.558 -20.727 53.041  1.00 42.27  ? 908  TRP   A CZ3 1 
ATOM   1491 C CH2 . TRP   A 1 215 ? 17.321 -20.067 54.248  1.00 42.50  ? 908  TRP   A CH2 1 
ATOM   1492 N N   . GLU   A 1 216 ? 20.105 -20.146 49.178  1.00 45.00  ? 909  GLU   A N   1 
ATOM   1493 C CA  . GLU   A 1 216 ? 20.816 -21.298 49.731  1.00 45.84  ? 909  GLU   A CA  1 
ATOM   1494 C C   . GLU   A 1 216 ? 22.314 -21.031 49.742  1.00 46.97  ? 909  GLU   A C   1 
ATOM   1495 O O   . GLU   A 1 216 ? 22.983 -21.431 50.680  1.00 48.03  ? 909  GLU   A O   1 
ATOM   1496 C CB  . GLU   A 1 216 ? 20.581 -22.553 48.887  1.00 47.59  ? 909  GLU   A CB  1 
ATOM   1497 C CG  . GLU   A 1 216 ? 19.211 -23.181 48.998  1.00 52.79  ? 909  GLU   A CG  1 
ATOM   1498 C CD  . GLU   A 1 216 ? 19.095 -24.412 48.114  1.00 60.53  ? 909  GLU   A CD  1 
ATOM   1499 O OE1 . GLU   A 1 216 ? 18.762 -24.261 46.914  1.00 60.77  ? 909  GLU   A OE1 1 
ATOM   1500 O OE2 . GLU   A 1 216 ? 19.355 -25.531 48.621  1.00 62.69  ? 909  GLU   A OE2 1 
ATOM   1501 N N   . LEU   A 1 217 ? 22.856 -20.399 48.694  1.00 46.97  ? 910  LEU   A N   1 
ATOM   1502 C CA  . LEU   A 1 217 ? 24.288 -20.129 48.604  1.00 47.71  ? 910  LEU   A CA  1 
ATOM   1503 C C   . LEU   A 1 217 ? 24.719 -19.061 49.584  1.00 48.92  ? 910  LEU   A C   1 
ATOM   1504 O O   . LEU   A 1 217 ? 25.752 -19.217 50.230  1.00 49.50  ? 910  LEU   A O   1 
ATOM   1505 C CB  . LEU   A 1 217 ? 24.689 -19.707 47.178  1.00 47.51  ? 910  LEU   A CB  1 
ATOM   1506 C CG  . LEU   A 1 217 ? 24.353 -20.651 46.042  1.00 48.20  ? 910  LEU   A CG  1 
ATOM   1507 C CD1 . LEU   A 1 217 ? 24.791 -20.056 44.690  1.00 47.98  ? 910  LEU   A CD1 1 
ATOM   1508 C CD2 . LEU   A 1 217 ? 24.960 -22.025 46.277  1.00 49.08  ? 910  LEU   A CD2 1 
ATOM   1509 N N   . MET   A 1 218 ? 23.927 -17.985 49.701  1.00 49.53  ? 911  MET   A N   1 
ATOM   1510 C CA  . MET   A 1 218 ? 24.188 -16.866 50.600  1.00 50.36  ? 911  MET   A CA  1 
ATOM   1511 C C   . MET   A 1 218 ? 24.086 -17.259 52.063  1.00 51.46  ? 911  MET   A C   1 
ATOM   1512 O O   . MET   A 1 218 ? 24.701 -16.606 52.894  1.00 52.11  ? 911  MET   A O   1 
ATOM   1513 C CB  . MET   A 1 218 ? 23.254 -15.690 50.300  1.00 51.14  ? 911  MET   A CB  1 
ATOM   1514 C CG  . MET   A 1 218 ? 23.363 -15.157 48.900  1.00 54.67  ? 911  MET   A CG  1 
ATOM   1515 S SD  . MET   A 1 218 ? 25.028 -14.691 48.358  1.00 64.50  ? 911  MET   A SD  1 
ATOM   1516 C CE  . MET   A 1 218 ? 24.641 -13.835 46.823  1.00 61.79  ? 911  MET   A CE  1 
ATOM   1517 N N   . THR   A 1 219 ? 23.309 -18.306 52.391  1.00 52.04  ? 912  THR   A N   1 
ATOM   1518 C CA  . THR   A 1 219 ? 23.214 -18.826 53.763  1.00 53.11  ? 912  THR   A CA  1 
ATOM   1519 C C   . THR   A 1 219 ? 24.163 -20.004 54.026  1.00 54.37  ? 912  THR   A C   1 
ATOM   1520 O O   . THR   A 1 219 ? 24.117 -20.583 55.116  1.00 55.38  ? 912  THR   A O   1 
ATOM   1521 C CB  . THR   A 1 219 ? 21.782 -19.233 54.093  1.00 54.30  ? 912  THR   A CB  1 
ATOM   1522 O OG1 . THR   A 1 219 ? 21.345 -20.186 53.128  1.00 55.09  ? 912  THR   A OG1 1 
ATOM   1523 C CG2 . THR   A 1 219 ? 20.831 -18.049 54.132  1.00 54.47  ? 912  THR   A CG2 1 
ATOM   1524 N N   . PHE   A 1 220 ? 25.005 -20.369 53.036  1.00 54.57  ? 913  PHE   A N   1 
ATOM   1525 C CA  . PHE   A 1 220 ? 25.988 -21.447 53.084  1.00 55.33  ? 913  PHE   A CA  1 
ATOM   1526 C C   . PHE   A 1 220 ? 25.353 -22.821 53.241  1.00 55.75  ? 913  PHE   A C   1 
ATOM   1527 O O   . PHE   A 1 220 ? 25.902 -23.693 53.897  1.00 56.00  ? 913  PHE   A O   1 
ATOM   1528 C CB  . PHE   A 1 220 ? 27.077 -21.187 54.136  1.00 55.52  ? 913  PHE   A CB  1 
ATOM   1529 C CG  . PHE   A 1 220 ? 27.876 -19.940 53.841  1.00 56.93  ? 913  PHE   A CG  1 
ATOM   1530 C CD1 . PHE   A 1 220 ? 28.920 -19.962 52.929  1.00 58.18  ? 913  PHE   A CD1 1 
ATOM   1531 C CD2 . PHE   A 1 220 ? 27.559 -18.740 54.442  1.00 57.67  ? 913  PHE   A CD2 1 
ATOM   1532 C CE1 . PHE   A 1 220 ? 29.645 -18.814 52.643  1.00 59.02  ? 913  PHE   A CE1 1 
ATOM   1533 C CE2 . PHE   A 1 220 ? 28.280 -17.595 54.149  1.00 58.55  ? 913  PHE   A CE2 1 
ATOM   1534 C CZ  . PHE   A 1 220 ? 29.322 -17.640 53.258  1.00 58.61  ? 913  PHE   A CZ  1 
ATOM   1535 N N   . GLY   A 1 221 ? 24.221 -23.014 52.592  1.00 55.83  ? 914  GLY   A N   1 
ATOM   1536 C CA  . GLY   A 1 221 ? 23.546 -24.299 52.583  1.00 56.45  ? 914  GLY   A CA  1 
ATOM   1537 C C   . GLY   A 1 221 ? 22.419 -24.482 53.571  1.00 56.84  ? 914  GLY   A C   1 
ATOM   1538 O O   . GLY   A 1 221 ? 22.068 -25.621 53.876  1.00 57.33  ? 914  GLY   A O   1 
ATOM   1539 N N   . SER   A 1 222 ? 21.825 -23.392 54.062  1.00 56.73  ? 915  SER   A N   1 
ATOM   1540 C CA  . SER   A 1 222 ? 20.695 -23.498 54.989  1.00 57.28  ? 915  SER   A CA  1 
ATOM   1541 C C   . SER   A 1 222 ? 19.467 -24.075 54.298  1.00 58.25  ? 915  SER   A C   1 
ATOM   1542 O O   . SER   A 1 222 ? 19.304 -23.927 53.083  1.00 57.99  ? 915  SER   A O   1 
ATOM   1543 C CB  . SER   A 1 222 ? 20.348 -22.145 55.599  1.00 58.33  ? 915  SER   A CB  1 
ATOM   1544 O OG  . SER   A 1 222 ? 21.357 -21.725 56.498  1.00 61.28  ? 915  SER   A OG  1 
ATOM   1545 N N   . LYS   A 1 223 ? 18.599 -24.734 55.072  1.00 59.25  ? 916  LYS   A N   1 
ATOM   1546 C CA  . LYS   A 1 223 ? 17.380 -25.317 54.532  1.00 60.75  ? 916  LYS   A CA  1 
ATOM   1547 C C   . LYS   A 1 223 ? 16.276 -24.261 54.515  1.00 62.10  ? 916  LYS   A C   1 
ATOM   1548 O O   . LYS   A 1 223 ? 15.979 -23.655 55.550  1.00 62.26  ? 916  LYS   A O   1 
ATOM   1549 C CB  . LYS   A 1 223 ? 16.969 -26.558 55.341  1.00 62.29  ? 916  LYS   A CB  1 
ATOM   1550 C CG  . LYS   A 1 223 ? 18.059 -27.623 55.376  1.00 66.12  ? 916  LYS   A CG  1 
ATOM   1551 C CD  . LYS   A 1 223 ? 17.741 -28.744 56.343  1.00 70.24  ? 916  LYS   A CD  1 
ATOM   1552 N N   . PRO   A 1 224 ? 15.692 -23.996 53.331  1.00 62.94  ? 917  PRO   A N   1 
ATOM   1553 C CA  . PRO   A 1 224 ? 14.648 -22.957 53.238  1.00 63.93  ? 917  PRO   A CA  1 
ATOM   1554 C C   . PRO   A 1 224 ? 13.369 -23.274 54.008  1.00 65.56  ? 917  PRO   A C   1 
ATOM   1555 O O   . PRO   A 1 224 ? 12.868 -24.385 53.904  1.00 65.65  ? 917  PRO   A O   1 
ATOM   1556 C CB  . PRO   A 1 224 ? 14.399 -22.835 51.727  1.00 64.33  ? 917  PRO   A CB  1 
ATOM   1557 C CG  . PRO   A 1 224 ? 14.839 -24.120 51.159  1.00 64.46  ? 917  PRO   A CG  1 
ATOM   1558 C CD  . PRO   A 1 224 ? 15.970 -24.613 52.020  1.00 62.53  ? 917  PRO   A CD  1 
ATOM   1559 N N   . TYR   A 1 225 ? 12.844 -22.294 54.773  1.00 66.92  ? 918  TYR   A N   1 
ATOM   1560 C CA  . TYR   A 1 225 ? 11.642 -22.431 55.605  1.00 69.00  ? 918  TYR   A CA  1 
ATOM   1561 C C   . TYR   A 1 225 ? 11.767 -23.638 56.549  1.00 71.84  ? 918  TYR   A C   1 
ATOM   1562 O O   . TYR   A 1 225 ? 10.884 -24.496 56.584  1.00 72.42  ? 918  TYR   A O   1 
ATOM   1563 C CB  . TYR   A 1 225 ? 10.351 -22.534 54.764  1.00 68.66  ? 918  TYR   A CB  1 
ATOM   1564 C CG  . TYR   A 1 225 ? 10.262 -21.625 53.559  1.00 69.00  ? 918  TYR   A CG  1 
ATOM   1565 C CD1 . TYR   A 1 225 ? 9.795  -20.322 53.680  1.00 69.62  ? 918  TYR   A CD1 1 
ATOM   1566 C CD2 . TYR   A 1 225 ? 10.522 -22.104 52.284  1.00 69.46  ? 918  TYR   A CD2 1 
ATOM   1567 C CE1 . TYR   A 1 225 ? 9.666  -19.497 52.572  1.00 70.20  ? 918  TYR   A CE1 1 
ATOM   1568 C CE2 . TYR   A 1 225 ? 10.398 -21.289 51.170  1.00 70.28  ? 918  TYR   A CE2 1 
ATOM   1569 C CZ  . TYR   A 1 225 ? 9.959  -19.988 51.316  1.00 71.00  ? 918  TYR   A CZ  1 
ATOM   1570 O OH  . TYR   A 1 225 ? 9.825  -19.188 50.213  1.00 72.18  ? 918  TYR   A OH  1 
ATOM   1571 N N   . ASP   A 1 226 ? 12.885 -23.730 57.274  1.00 73.41  ? 919  ASP   A N   1 
ATOM   1572 C CA  . ASP   A 1 226 ? 13.137 -24.870 58.153  1.00 75.30  ? 919  ASP   A CA  1 
ATOM   1573 C C   . ASP   A 1 226 ? 12.133 -24.995 59.292  1.00 76.54  ? 919  ASP   A C   1 
ATOM   1574 O O   . ASP   A 1 226 ? 11.921 -24.043 60.043  1.00 77.03  ? 919  ASP   A O   1 
ATOM   1575 C CB  . ASP   A 1 226 ? 14.572 -24.842 58.693  1.00 77.95  ? 919  ASP   A CB  1 
ATOM   1576 C CG  . ASP   A 1 226 ? 15.217 -26.211 58.765  1.00 84.37  ? 919  ASP   A CG  1 
ATOM   1577 O OD1 . ASP   A 1 226 ? 14.471 -27.222 58.824  1.00 85.33  ? 919  ASP   A OD1 1 
ATOM   1578 O OD2 . ASP   A 1 226 ? 16.467 -26.277 58.763  1.00 87.28  ? 919  ASP   A OD2 1 
ATOM   1579 N N   . GLY   A 1 227 ? 11.518 -26.169 59.406  1.00 76.86  ? 920  GLY   A N   1 
ATOM   1580 C CA  . GLY   A 1 227 ? 10.526 -26.429 60.445  1.00 77.59  ? 920  GLY   A CA  1 
ATOM   1581 C C   . GLY   A 1 227 ? 9.089  -26.252 59.983  1.00 78.05  ? 920  GLY   A C   1 
ATOM   1582 O O   . GLY   A 1 227 ? 8.165  -26.864 60.537  1.00 78.29  ? 920  GLY   A O   1 
ATOM   1583 N N   . ILE   A 1 228 ? 8.886  -25.395 58.971  1.00 77.78  ? 921  ILE   A N   1 
ATOM   1584 C CA  . ILE   A 1 228 ? 7.573  -25.148 58.394  1.00 77.63  ? 921  ILE   A CA  1 
ATOM   1585 C C   . ILE   A 1 228 ? 7.209  -26.334 57.503  1.00 77.54  ? 921  ILE   A C   1 
ATOM   1586 O O   . ILE   A 1 228 ? 7.994  -26.708 56.635  1.00 77.41  ? 921  ILE   A O   1 
ATOM   1587 C CB  . ILE   A 1 228 ? 7.608  -23.832 57.585  1.00 77.91  ? 921  ILE   A CB  1 
ATOM   1588 C CG1 . ILE   A 1 228 ? 8.033  -22.648 58.470  1.00 78.67  ? 921  ILE   A CG1 1 
ATOM   1589 C CG2 . ILE   A 1 228 ? 6.277  -23.568 56.895  1.00 78.36  ? 921  ILE   A CG2 1 
ATOM   1590 N N   . PRO   A 1 229 ? 6.052  -26.978 57.731  1.00 77.46  ? 922  PRO   A N   1 
ATOM   1591 C CA  . PRO   A 1 229 ? 5.666  -28.112 56.871  1.00 77.32  ? 922  PRO   A CA  1 
ATOM   1592 C C   . PRO   A 1 229 ? 5.395  -27.655 55.435  1.00 77.44  ? 922  PRO   A C   1 
ATOM   1593 O O   . PRO   A 1 229 ? 4.963  -26.518 55.223  1.00 77.81  ? 922  PRO   A O   1 
ATOM   1594 C CB  . PRO   A 1 229 ? 4.395  -28.657 57.541  1.00 77.92  ? 922  PRO   A CB  1 
ATOM   1595 C CG  . PRO   A 1 229 ? 4.313  -27.981 58.887  1.00 78.26  ? 922  PRO   A CG  1 
ATOM   1596 C CD  . PRO   A 1 229 ? 5.014  -26.675 58.733  1.00 76.90  ? 922  PRO   A CD  1 
ATOM   1597 N N   . ALA   A 1 230 ? 5.658  -28.520 54.444  1.00 76.94  ? 923  ALA   A N   1 
ATOM   1598 C CA  . ALA   A 1 230 ? 5.443  -28.163 53.035  1.00 77.00  ? 923  ALA   A CA  1 
ATOM   1599 C C   . ALA   A 1 230 ? 3.990  -27.813 52.727  1.00 76.90  ? 923  ALA   A C   1 
ATOM   1600 O O   . ALA   A 1 230 ? 3.732  -27.001 51.843  1.00 77.05  ? 923  ALA   A O   1 
ATOM   1601 C CB  . ALA   A 1 230 ? 5.921  -29.278 52.119  1.00 77.17  ? 923  ALA   A CB  1 
ATOM   1602 N N   . SER   A 1 231 ? 3.042  -28.386 53.485  1.00 76.60  ? 924  SER   A N   1 
ATOM   1603 C CA  . SER   A 1 231 ? 1.619  -28.110 53.322  1.00 76.58  ? 924  SER   A CA  1 
ATOM   1604 C C   . SER   A 1 231 ? 1.245  -26.657 53.671  1.00 76.16  ? 924  SER   A C   1 
ATOM   1605 O O   . SER   A 1 231 ? 0.200  -26.185 53.236  1.00 76.28  ? 924  SER   A O   1 
ATOM   1606 C CB  . SER   A 1 231 ? 0.803  -29.069 54.178  1.00 78.15  ? 924  SER   A CB  1 
ATOM   1607 O OG  . SER   A 1 231 ? 1.077  -28.880 55.558  1.00 80.94  ? 924  SER   A OG  1 
ATOM   1608 N N   . GLU   A 1 232 ? 2.078  -25.956 54.453  1.00 75.58  ? 925  GLU   A N   1 
ATOM   1609 C CA  . GLU   A 1 232 ? 1.793  -24.583 54.856  1.00 75.71  ? 925  GLU   A CA  1 
ATOM   1610 C C   . GLU   A 1 232 ? 2.504  -23.508 54.032  1.00 74.38  ? 925  GLU   A C   1 
ATOM   1611 O O   . GLU   A 1 232 ? 2.247  -22.325 54.251  1.00 74.25  ? 925  GLU   A O   1 
ATOM   1612 C CB  . GLU   A 1 232 ? 2.123  -24.385 56.338  1.00 79.41  ? 925  GLU   A CB  1 
ATOM   1613 C CG  . GLU   A 1 232 ? 1.407  -25.356 57.255  1.00 86.97  ? 925  GLU   A CG  1 
ATOM   1614 C CD  . GLU   A 1 232 ? 1.806  -25.260 58.717  1.00 96.86  ? 925  GLU   A CD  1 
ATOM   1615 O OE1 . GLU   A 1 232 ? 2.520  -24.297 59.088  1.00 98.58  ? 925  GLU   A OE1 1 
ATOM   1616 O OE2 . GLU   A 1 232 ? 1.412  -26.162 59.493  1.00 100.23 ? 925  GLU   A OE2 1 
ATOM   1617 N N   . ILE   A 1 233 ? 3.391  -23.901 53.106  1.00 73.15  ? 926  ILE   A N   1 
ATOM   1618 C CA  . ILE   A 1 233 ? 4.177  -22.976 52.294  1.00 72.47  ? 926  ILE   A CA  1 
ATOM   1619 C C   . ILE   A 1 233 ? 3.316  -22.024 51.444  1.00 71.99  ? 926  ILE   A C   1 
ATOM   1620 O O   . ILE   A 1 233 ? 3.554  -20.819 51.472  1.00 71.81  ? 926  ILE   A O   1 
ATOM   1621 C CB  . ILE   A 1 233 ? 5.218  -23.755 51.445  1.00 72.61  ? 926  ILE   A CB  1 
ATOM   1622 C CG1 . ILE   A 1 233 ? 6.256  -24.432 52.350  1.00 73.34  ? 926  ILE   A CG1 1 
ATOM   1623 C CG2 . ILE   A 1 233 ? 5.908  -22.864 50.416  1.00 72.90  ? 926  ILE   A CG2 1 
ATOM   1624 N N   . SER   A 1 234 ? 2.310  -22.543 50.727  1.00 71.61  ? 927  SER   A N   1 
ATOM   1625 C CA  . SER   A 1 234 ? 1.459  -21.719 49.871  1.00 71.79  ? 927  SER   A CA  1 
ATOM   1626 C C   . SER   A 1 234 ? 0.722  -20.610 50.626  1.00 71.77  ? 927  SER   A C   1 
ATOM   1627 O O   . SER   A 1 234 ? 0.660  -19.482 50.136  1.00 71.90  ? 927  SER   A O   1 
ATOM   1628 C CB  . SER   A 1 234 ? 0.483  -22.583 49.077  1.00 73.40  ? 927  SER   A CB  1 
ATOM   1629 O OG  . SER   A 1 234 ? -0.504 -23.166 49.912  1.00 76.11  ? 927  SER   A OG  1 
ATOM   1630 N N   . SER   A 1 235 ? 0.192  -20.910 51.822  1.00 71.42  ? 928  SER   A N   1 
ATOM   1631 C CA  . SER   A 1 235 ? -0.509 -19.898 52.615  1.00 71.41  ? 928  SER   A CA  1 
ATOM   1632 C C   . SER   A 1 235 ? 0.458  -18.868 53.202  1.00 70.77  ? 928  SER   A C   1 
ATOM   1633 O O   . SER   A 1 235 ? 0.103  -17.693 53.315  1.00 71.56  ? 928  SER   A O   1 
ATOM   1634 C CB  . SER   A 1 235 ? -1.350 -20.541 53.714  1.00 73.25  ? 928  SER   A CB  1 
ATOM   1635 O OG  . SER   A 1 235 ? -0.562 -21.400 54.519  1.00 76.07  ? 928  SER   A OG  1 
ATOM   1636 N N   . ILE   A 1 236 ? 1.677  -19.292 53.548  1.00 69.24  ? 929  ILE   A N   1 
ATOM   1637 C CA  . ILE   A 1 236 ? 2.704  -18.401 54.076  1.00 68.43  ? 929  ILE   A CA  1 
ATOM   1638 C C   . ILE   A 1 236 ? 3.139  -17.400 52.982  1.00 67.20  ? 929  ILE   A C   1 
ATOM   1639 O O   . ILE   A 1 236 ? 3.338  -16.223 53.277  1.00 67.42  ? 929  ILE   A O   1 
ATOM   1640 C CB  . ILE   A 1 236 ? 3.866  -19.241 54.699  1.00 69.27  ? 929  ILE   A CB  1 
ATOM   1641 C CG1 . ILE   A 1 236 ? 3.791  -19.227 56.233  1.00 70.71  ? 929  ILE   A CG1 1 
ATOM   1642 C CG2 . ILE   A 1 236 ? 5.276  -18.850 54.207  1.00 69.51  ? 929  ILE   A CG2 1 
ATOM   1643 C CD1 . ILE   A 1 236 ? 2.463  -19.726 56.845  1.00 72.64  ? 929  ILE   A CD1 1 
ATOM   1644 N N   . LEU   A 1 237 ? 3.233  -17.860 51.721  1.00 65.62  ? 930  LEU   A N   1 
ATOM   1645 C CA  . LEU   A 1 237 ? 3.602  -17.006 50.600  1.00 64.61  ? 930  LEU   A CA  1 
ATOM   1646 C C   . LEU   A 1 237 ? 2.494  -16.003 50.290  1.00 64.78  ? 930  LEU   A C   1 
ATOM   1647 O O   . LEU   A 1 237 ? 2.786  -14.854 49.955  1.00 64.89  ? 930  LEU   A O   1 
ATOM   1648 C CB  . LEU   A 1 237 ? 3.923  -17.840 49.358  1.00 63.98  ? 930  LEU   A CB  1 
ATOM   1649 C CG  . LEU   A 1 237 ? 5.149  -18.741 49.454  1.00 64.12  ? 930  LEU   A CG  1 
ATOM   1650 C CD1 . LEU   A 1 237 ? 5.278  -19.604 48.219  1.00 64.06  ? 930  LEU   A CD1 1 
ATOM   1651 C CD2 . LEU   A 1 237 ? 6.407  -17.927 49.695  1.00 64.32  ? 930  LEU   A CD2 1 
ATOM   1652 N N   . GLU   A 1 238 ? 1.226  -16.419 50.430  1.00 64.46  ? 931  GLU   A N   1 
ATOM   1653 C CA  . GLU   A 1 238 ? 0.093  -15.532 50.202  1.00 64.82  ? 931  GLU   A CA  1 
ATOM   1654 C C   . GLU   A 1 238 ? 0.005  -14.413 51.269  1.00 65.32  ? 931  GLU   A C   1 
ATOM   1655 O O   . GLU   A 1 238 ? -0.525 -13.342 50.985  1.00 65.61  ? 931  GLU   A O   1 
ATOM   1656 C CB  . GLU   A 1 238 ? -1.215 -16.326 50.070  1.00 66.58  ? 931  GLU   A CB  1 
ATOM   1657 N N   . LYS   A 1 239 ? 0.563  -14.643 52.472  1.00 65.20  ? 932  LYS   A N   1 
ATOM   1658 C CA  . LYS   A 1 239 ? 0.628  -13.635 53.541  1.00 65.34  ? 932  LYS   A CA  1 
ATOM   1659 C C   . LYS   A 1 239 ? 1.799  -12.623 53.347  1.00 64.62  ? 932  LYS   A C   1 
ATOM   1660 O O   . LYS   A 1 239 ? 1.930  -11.684 54.129  1.00 64.80  ? 932  LYS   A O   1 
ATOM   1661 C CB  . LYS   A 1 239 ? 0.781  -14.306 54.917  1.00 67.85  ? 932  LYS   A CB  1 
ATOM   1662 C CG  . LYS   A 1 239 ? -0.398 -15.160 55.342  1.00 72.91  ? 932  LYS   A CG  1 
ATOM   1663 C CD  . LYS   A 1 239 ? -0.215 -15.712 56.753  1.00 77.84  ? 932  LYS   A CD  1 
ATOM   1664 N N   . GLY   A 1 240 ? 2.651  -12.842 52.349  1.00 63.56  ? 933  GLY   A N   1 
ATOM   1665 C CA  . GLY   A 1 240 ? 3.773  -11.957 52.069  1.00 62.99  ? 933  GLY   A CA  1 
ATOM   1666 C C   . GLY   A 1 240 ? 5.083  -12.311 52.737  1.00 61.93  ? 933  GLY   A C   1 
ATOM   1667 O O   . GLY   A 1 240 ? 6.036  -11.527 52.682  1.00 62.17  ? 933  GLY   A O   1 
ATOM   1668 N N   . GLU   A 1 241 ? 5.137  -13.482 53.384  1.00 60.45  ? 934  GLU   A N   1 
ATOM   1669 C CA  . GLU   A 1 241 ? 6.334  -13.938 54.072  1.00 59.44  ? 934  GLU   A CA  1 
ATOM   1670 C C   . GLU   A 1 241 ? 7.261  -14.569 53.060  1.00 58.00  ? 934  GLU   A C   1 
ATOM   1671 O O   . GLU   A 1 241 ? 6.835  -15.402 52.267  1.00 58.52  ? 934  GLU   A O   1 
ATOM   1672 C CB  . GLU   A 1 241 ? 5.980  -14.940 55.189  1.00 61.43  ? 934  GLU   A CB  1 
ATOM   1673 N N   . ARG   A 1 242 ? 8.519  -14.147 53.052  1.00 56.13  ? 935  ARG   A N   1 
ATOM   1674 C CA  . ARG   A 1 242 ? 9.533  -14.666 52.134  1.00 54.66  ? 935  ARG   A CA  1 
ATOM   1675 C C   . ARG   A 1 242 ? 10.742 -15.192 52.933  1.00 54.00  ? 935  ARG   A C   1 
ATOM   1676 O O   . ARG   A 1 242 ? 10.779 -15.052 54.158  1.00 54.52  ? 935  ARG   A O   1 
ATOM   1677 C CB  . ARG   A 1 242 ? 9.970  -13.548 51.161  1.00 54.27  ? 935  ARG   A CB  1 
ATOM   1678 C CG  . ARG   A 1 242 ? 8.883  -13.085 50.211  1.00 54.47  ? 935  ARG   A CG  1 
ATOM   1679 C CD  . ARG   A 1 242 ? 8.444  -14.189 49.273  1.00 55.77  ? 935  ARG   A CD  1 
ATOM   1680 N NE  . ARG   A 1 242 ? 7.474  -13.707 48.286  1.00 55.98  ? 935  ARG   A NE  1 
ATOM   1681 C CZ  . ARG   A 1 242 ? 6.157  -13.730 48.458  1.00 55.76  ? 935  ARG   A CZ  1 
ATOM   1682 N NH1 . ARG   A 1 242 ? 5.353  -13.271 47.512  1.00 55.67  ? 935  ARG   A NH1 1 
ATOM   1683 N NH2 . ARG   A 1 242 ? 5.634  -14.209 49.579  1.00 53.78  ? 935  ARG   A NH2 1 
ATOM   1684 N N   . LEU   A 1 243 ? 11.736 -15.785 52.257  1.00 53.04  ? 936  LEU   A N   1 
ATOM   1685 C CA  . LEU   A 1 243 ? 12.959 -16.247 52.927  1.00 52.88  ? 936  LEU   A CA  1 
ATOM   1686 C C   . LEU   A 1 243 ? 13.684 -15.034 53.534  1.00 53.83  ? 936  LEU   A C   1 
ATOM   1687 O O   . LEU   A 1 243 ? 13.717 -13.962 52.920  1.00 54.15  ? 936  LEU   A O   1 
ATOM   1688 C CB  . LEU   A 1 243 ? 13.862 -16.980 51.929  1.00 51.79  ? 936  LEU   A CB  1 
ATOM   1689 C CG  . LEU   A 1 243 ? 13.321 -18.316 51.495  1.00 51.83  ? 936  LEU   A CG  1 
ATOM   1690 C CD1 . LEU   A 1 243 ? 13.890 -18.737 50.159  1.00 52.00  ? 936  LEU   A CD1 1 
ATOM   1691 C CD2 . LEU   A 1 243 ? 13.532 -19.345 52.570  1.00 51.97  ? 936  LEU   A CD2 1 
ATOM   1692 N N   . PRO   A 1 244 ? 14.162 -15.144 54.780  1.00 54.02  ? 937  PRO   A N   1 
ATOM   1693 C CA  . PRO   A 1 244 ? 14.786 -13.976 55.428  1.00 54.51  ? 937  PRO   A CA  1 
ATOM   1694 C C   . PRO   A 1 244 ? 16.068 -13.493 54.761  1.00 55.23  ? 937  PRO   A C   1 
ATOM   1695 O O   . PRO   A 1 244 ? 16.701 -14.243 54.024  1.00 55.38  ? 937  PRO   A O   1 
ATOM   1696 C CB  . PRO   A 1 244 ? 15.049 -14.466 56.850  1.00 55.02  ? 937  PRO   A CB  1 
ATOM   1697 C CG  . PRO   A 1 244 ? 15.157 -15.957 56.718  1.00 55.11  ? 937  PRO   A CG  1 
ATOM   1698 C CD  . PRO   A 1 244 ? 14.164 -16.326 55.661  1.00 53.46  ? 937  PRO   A CD  1 
ATOM   1699 N N   . GLN   A 1 245 ? 16.437 -12.233 54.998  1.00 55.58  ? 938  GLN   A N   1 
ATOM   1700 C CA  . GLN   A 1 245 ? 17.661 -11.677 54.429  1.00 56.35  ? 938  GLN   A CA  1 
ATOM   1701 C C   . GLN   A 1 245 ? 18.885 -12.341 55.076  1.00 57.07  ? 938  GLN   A C   1 
ATOM   1702 O O   . GLN   A 1 245 ? 19.050 -12.258 56.299  1.00 57.41  ? 938  GLN   A O   1 
ATOM   1703 C CB  . GLN   A 1 245 ? 17.711 -10.168 54.661  1.00 57.73  ? 938  GLN   A CB  1 
ATOM   1704 C CG  . GLN   A 1 245 ? 18.967 -9.521  54.095  1.00 60.85  ? 938  GLN   A CG  1 
ATOM   1705 C CD  . GLN   A 1 245 ? 18.978 -8.013  54.167  1.00 64.82  ? 938  GLN   A CD  1 
ATOM   1706 O OE1 . GLN   A 1 245 ? 20.016 -7.386  53.958  1.00 66.10  ? 938  GLN   A OE1 1 
ATOM   1707 N NE2 . GLN   A 1 245 ? 17.841 -7.387  54.453  1.00 65.35  ? 938  GLN   A NE2 1 
ATOM   1708 N N   . PRO   A 1 246 ? 19.744 -13.021 54.285  1.00 56.96  ? 939  PRO   A N   1 
ATOM   1709 C CA  . PRO   A 1 246 ? 20.931 -13.669 54.880  1.00 56.82  ? 939  PRO   A CA  1 
ATOM   1710 C C   . PRO   A 1 246 ? 21.888 -12.645 55.500  1.00 57.12  ? 939  PRO   A C   1 
ATOM   1711 O O   . PRO   A 1 246 ? 21.995 -11.525 55.008  1.00 57.03  ? 939  PRO   A O   1 
ATOM   1712 C CB  . PRO   A 1 246 ? 21.564 -14.423 53.697  1.00 57.06  ? 939  PRO   A CB  1 
ATOM   1713 C CG  . PRO   A 1 246 ? 20.484 -14.504 52.653  1.00 57.59  ? 939  PRO   A CG  1 
ATOM   1714 C CD  . PRO   A 1 246 ? 19.687 -13.238 52.826  1.00 56.19  ? 939  PRO   A CD  1 
ATOM   1715 N N   . PRO   A 1 247 ? 22.551 -13.008 56.615  1.00 57.33  ? 940  PRO   A N   1 
ATOM   1716 C CA  . PRO   A 1 247 ? 23.451 -12.051 57.295  1.00 57.47  ? 940  PRO   A CA  1 
ATOM   1717 C C   . PRO   A 1 247 ? 24.516 -11.363 56.432  1.00 57.72  ? 940  PRO   A C   1 
ATOM   1718 O O   . PRO   A 1 247 ? 24.804 -10.190 56.654  1.00 57.88  ? 940  PRO   A O   1 
ATOM   1719 C CB  . PRO   A 1 247 ? 24.111 -12.896 58.396  1.00 58.01  ? 940  PRO   A CB  1 
ATOM   1720 C CG  . PRO   A 1 247 ? 23.212 -14.050 58.604  1.00 58.29  ? 940  PRO   A CG  1 
ATOM   1721 C CD  . PRO   A 1 247 ? 22.492 -14.307 57.319  1.00 56.72  ? 940  PRO   A CD  1 
ATOM   1722 N N   . ILE   A 1 248 ? 25.104 -12.083 55.460  1.00 57.41  ? 941  ILE   A N   1 
ATOM   1723 C CA  . ILE   A 1 248 ? 26.157 -11.526 54.614  1.00 57.51  ? 941  ILE   A CA  1 
ATOM   1724 C C   . ILE   A 1 248 ? 25.657 -10.590 53.515  1.00 58.32  ? 941  ILE   A C   1 
ATOM   1725 O O   . ILE   A 1 248 ? 26.458 -9.853  52.950  1.00 58.34  ? 941  ILE   A O   1 
ATOM   1726 C CB  . ILE   A 1 248 ? 27.036 -12.645 54.015  1.00 57.52  ? 941  ILE   A CB  1 
ATOM   1727 C CG1 . ILE   A 1 248 ? 26.268 -13.462 52.953  1.00 58.07  ? 941  ILE   A CG1 1 
ATOM   1728 C CG2 . ILE   A 1 248 ? 27.615 -13.536 55.107  1.00 57.69  ? 941  ILE   A CG2 1 
ATOM   1729 C CD1 . ILE   A 1 248 ? 27.150 -14.285 52.086  1.00 58.62  ? 941  ILE   A CD1 1 
ATOM   1730 N N   . CYS   A 1 249 ? 24.357 -10.614 53.197  1.00 58.84  ? 942  CYS   A N   1 
ATOM   1731 C CA  . CYS   A 1 249 ? 23.820 -9.802  52.113  1.00 59.50  ? 942  CYS   A CA  1 
ATOM   1732 C C   . CYS   A 1 249 ? 23.547 -8.383  52.468  1.00 59.99  ? 942  CYS   A C   1 
ATOM   1733 O O   . CYS   A 1 249 ? 22.929 -8.108  53.489  1.00 60.39  ? 942  CYS   A O   1 
ATOM   1734 C CB  . CYS   A 1 249 ? 22.568 -10.441 51.529  1.00 60.61  ? 942  CYS   A CB  1 
ATOM   1735 S SG  . CYS   A 1 249 ? 22.839 -12.077 50.821  1.00 66.09  ? 942  CYS   A SG  1 
ATOM   1736 N N   . THR   A 1 250 ? 23.879 -7.479  51.548  1.00 60.04  ? 943  THR   A N   1 
ATOM   1737 C CA  . THR   A 1 250 ? 23.482 -6.084  51.678  1.00 60.30  ? 943  THR   A CA  1 
ATOM   1738 C C   . THR   A 1 250 ? 22.018 -5.995  51.157  1.00 60.42  ? 943  THR   A C   1 
ATOM   1739 O O   . THR   A 1 250 ? 21.488 -6.990  50.632  1.00 60.71  ? 943  THR   A O   1 
ATOM   1740 C CB  . THR   A 1 250 ? 24.437 -5.189  50.881  1.00 61.38  ? 943  THR   A CB  1 
ATOM   1741 O OG1 . THR   A 1 250 ? 24.485 -5.655  49.530  1.00 62.04  ? 943  THR   A OG1 1 
ATOM   1742 C CG2 . THR   A 1 250 ? 25.844 -5.123  51.503  1.00 61.63  ? 943  THR   A CG2 1 
ATOM   1743 N N   . ILE   A 1 251 ? 21.363 -4.825  51.290  1.00 60.07  ? 944  ILE   A N   1 
ATOM   1744 C CA  . ILE   A 1 251 ? 19.991 -4.687  50.804  1.00 60.37  ? 944  ILE   A CA  1 
ATOM   1745 C C   . ILE   A 1 251 ? 19.921 -4.829  49.265  1.00 60.10  ? 944  ILE   A C   1 
ATOM   1746 O O   . ILE   A 1 251 ? 18.930 -5.344  48.753  1.00 60.33  ? 944  ILE   A O   1 
ATOM   1747 C CB  . ILE   A 1 251 ? 19.292 -3.407  51.345  1.00 61.17  ? 944  ILE   A CB  1 
ATOM   1748 C CG1 . ILE   A 1 251 ? 17.762 -3.584  51.409  1.00 61.94  ? 944  ILE   A CG1 1 
ATOM   1749 C CG2 . ILE   A 1 251 ? 19.665 -2.174  50.542  1.00 61.74  ? 944  ILE   A CG2 1 
ATOM   1750 C CD1 . ILE   A 1 251 ? 17.250 -4.905  52.038  1.00 62.63  ? 944  ILE   A CD1 1 
ATOM   1751 N N   . ASP   A 1 252 ? 21.005 -4.475  48.547  1.00 59.49  ? 945  ASP   A N   1 
ATOM   1752 C CA  . ASP   A 1 252 ? 21.095 -4.563  47.087  1.00 59.42  ? 945  ASP   A CA  1 
ATOM   1753 C C   . ASP   A 1 252 ? 20.996 -5.996  46.589  1.00 58.76  ? 945  ASP   A C   1 
ATOM   1754 O O   . ASP   A 1 252 ? 20.379 -6.250  45.552  1.00 59.03  ? 945  ASP   A O   1 
ATOM   1755 C CB  . ASP   A 1 252 ? 22.410 -3.944  46.592  1.00 62.03  ? 945  ASP   A CB  1 
ATOM   1756 C CG  . ASP   A 1 252 ? 22.712 -2.579  47.183  1.00 68.59  ? 945  ASP   A CG  1 
ATOM   1757 O OD1 . ASP   A 1 252 ? 23.084 -2.519  48.384  1.00 70.32  ? 945  ASP   A OD1 1 
ATOM   1758 O OD2 . ASP   A 1 252 ? 22.574 -1.571  46.449  1.00 70.82  ? 945  ASP   A OD2 1 
ATOM   1759 N N   . VAL   A 1 253 ? 21.635 -6.934  47.305  1.00 57.52  ? 946  VAL   A N   1 
ATOM   1760 C CA  . VAL   A 1 253 ? 21.593 -8.331  46.922  1.00 56.73  ? 946  VAL   A CA  1 
ATOM   1761 C C   . VAL   A 1 253 ? 20.248 -8.935  47.294  1.00 55.86  ? 946  VAL   A C   1 
ATOM   1762 O O   . VAL   A 1 253 ? 19.633 -9.627  46.482  1.00 56.51  ? 946  VAL   A O   1 
ATOM   1763 C CB  . VAL   A 1 253 ? 22.765 -9.116  47.538  1.00 57.31  ? 946  VAL   A CB  1 
ATOM   1764 C CG1 . VAL   A 1 253 ? 22.690 -10.583 47.144  1.00 57.40  ? 946  VAL   A CG1 1 
ATOM   1765 C CG2 . VAL   A 1 253 ? 24.090 -8.515  47.104  1.00 57.90  ? 946  VAL   A CG2 1 
ATOM   1766 N N   . TYR   A 1 254 ? 19.772 -8.642  48.504  1.00 54.64  ? 947  TYR   A N   1 
ATOM   1767 C CA  . TYR   A 1 254 ? 18.488 -9.155  48.959  1.00 54.32  ? 947  TYR   A CA  1 
ATOM   1768 C C   . TYR   A 1 254 ? 17.319 -8.714  48.085  1.00 54.18  ? 947  TYR   A C   1 
ATOM   1769 O O   . TYR   A 1 254 ? 16.419 -9.511  47.828  1.00 54.27  ? 947  TYR   A O   1 
ATOM   1770 C CB  . TYR   A 1 254 ? 18.228 -8.838  50.435  1.00 54.20  ? 947  TYR   A CB  1 
ATOM   1771 C CG  . TYR   A 1 254 ? 16.985 -9.540  50.919  1.00 54.70  ? 947  TYR   A CG  1 
ATOM   1772 C CD1 . TYR   A 1 254 ? 16.888 -10.923 50.877  1.00 55.15  ? 947  TYR   A CD1 1 
ATOM   1773 C CD2 . TYR   A 1 254 ? 15.863 -8.820  51.305  1.00 55.56  ? 947  TYR   A CD2 1 
ATOM   1774 C CE1 . TYR   A 1 254 ? 15.726 -11.576 51.257  1.00 56.15  ? 947  TYR   A CE1 1 
ATOM   1775 C CE2 . TYR   A 1 254 ? 14.691 -9.463  51.683  1.00 56.54  ? 947  TYR   A CE2 1 
ATOM   1776 C CZ  . TYR   A 1 254 ? 14.628 -10.843 51.663  1.00 57.38  ? 947  TYR   A CZ  1 
ATOM   1777 O OH  . TYR   A 1 254 ? 13.475 -11.488 52.044  1.00 59.11  ? 947  TYR   A OH  1 
ATOM   1778 N N   . MET   A 1 255 ? 17.351 -7.478  47.590  1.00 53.96  ? 948  MET   A N   1 
ATOM   1779 C CA  . MET   A 1 255 ? 16.286 -6.985  46.732  1.00 54.70  ? 948  MET   A CA  1 
ATOM   1780 C C   . MET   A 1 255 ? 16.173 -7.753  45.433  1.00 54.83  ? 948  MET   A C   1 
ATOM   1781 O O   . MET   A 1 255 ? 15.065 -7.915  44.929  1.00 54.87  ? 948  MET   A O   1 
ATOM   1782 C CB  . MET   A 1 255 ? 16.401 -5.475  46.501  1.00 56.18  ? 948  MET   A CB  1 
ATOM   1783 C CG  . MET   A 1 255 ? 15.855 -4.649  47.662  1.00 59.79  ? 948  MET   A CG  1 
ATOM   1784 S SD  . MET   A 1 255 ? 14.104 -4.988  48.025  1.00 69.14  ? 948  MET   A SD  1 
ATOM   1785 C CE  . MET   A 1 255 ? 14.278 -6.093  49.486  1.00 63.83  ? 948  MET   A CE  1 
ATOM   1786 N N   . ILE   A 1 256 ? 17.296 -8.276  44.917  1.00 54.65  ? 949  ILE   A N   1 
ATOM   1787 C CA  . ILE   A 1 256 ? 17.295 -9.077  43.701  1.00 54.58  ? 949  ILE   A CA  1 
ATOM   1788 C C   . ILE   A 1 256 ? 16.603 -10.422 43.956  1.00 53.96  ? 949  ILE   A C   1 
ATOM   1789 O O   . ILE   A 1 256 ? 15.752 -10.811 43.147  1.00 54.31  ? 949  ILE   A O   1 
ATOM   1790 C CB  . ILE   A 1 256 ? 18.726 -9.242  43.153  1.00 55.41  ? 949  ILE   A CB  1 
ATOM   1791 C CG1 . ILE   A 1 256 ? 19.284 -7.891  42.666  1.00 56.48  ? 949  ILE   A CG1 1 
ATOM   1792 C CG2 . ILE   A 1 256 ? 18.748 -10.273 42.028  1.00 56.03  ? 949  ILE   A CG2 1 
ATOM   1793 C CD1 . ILE   A 1 256 ? 20.741 -7.945  42.258  1.00 57.83  ? 949  ILE   A CD1 1 
ATOM   1794 N N   . MET   A 1 257 ? 16.937 -11.123 45.084  1.00 52.52  ? 950  MET   A N   1 
ATOM   1795 C CA  . MET   A 1 257 ? 16.264 -12.388 45.425  1.00 52.02  ? 950  MET   A CA  1 
ATOM   1796 C C   . MET   A 1 257 ? 14.773 -12.120 45.665  1.00 51.27  ? 950  MET   A C   1 
ATOM   1797 O O   . MET   A 1 257 ? 13.942 -12.908 45.240  1.00 51.45  ? 950  MET   A O   1 
ATOM   1798 C CB  . MET   A 1 257 ? 16.829 -13.052 46.702  1.00 52.74  ? 950  MET   A CB  1 
ATOM   1799 C CG  . MET   A 1 257 ? 18.312 -13.189 46.758  1.00 55.75  ? 950  MET   A CG  1 
ATOM   1800 S SD  . MET   A 1 257 ? 18.805 -13.908 48.359  1.00 63.36  ? 950  MET   A SD  1 
ATOM   1801 C CE  . MET   A 1 257 ? 19.782 -12.628 48.969  1.00 60.16  ? 950  MET   A CE  1 
ATOM   1802 N N   . ARG   A 1 258 ? 14.447 -11.021 46.360  1.00 50.43  ? 951  ARG   A N   1 
ATOM   1803 C CA  . ARG   A 1 258 ? 13.091 -10.600 46.670  1.00 50.59  ? 951  ARG   A CA  1 
ATOM   1804 C C   . ARG   A 1 258 ? 12.255 -10.381 45.387  1.00 49.99  ? 951  ARG   A C   1 
ATOM   1805 O O   . ARG   A 1 258 ? 11.085 -10.764 45.361  1.00 50.58  ? 951  ARG   A O   1 
ATOM   1806 C CB  . ARG   A 1 258 ? 13.152 -9.332  47.541  1.00 52.72  ? 951  ARG   A CB  1 
ATOM   1807 C CG  . ARG   A 1 258 ? 11.839 -8.829  48.122  1.00 57.26  ? 951  ARG   A CG  1 
ATOM   1808 C CD  . ARG   A 1 258 ? 11.100 -9.883  48.923  1.00 61.54  ? 951  ARG   A CD  1 
ATOM   1809 N NE  . ARG   A 1 258 ? 9.994  -10.414 48.128  1.00 65.18  ? 951  ARG   A NE  1 
ATOM   1810 C CZ  . ARG   A 1 258 ? 8.726  -10.051 48.267  1.00 66.18  ? 951  ARG   A CZ  1 
ATOM   1811 N NH1 . ARG   A 1 258 ? 8.370  -9.211  49.231  1.00 65.42  ? 951  ARG   A NH1 1 
ATOM   1812 N NH2 . ARG   A 1 258 ? 7.797  -10.569 47.482  1.00 65.69  ? 951  ARG   A NH2 1 
ATOM   1813 N N   . LYS   A 1 259 ? 12.856 -9.827  44.314  1.00 48.43  ? 952  LYS   A N   1 
ATOM   1814 C CA  . LYS   A 1 259 ? 12.153 -9.640  43.038  1.00 47.67  ? 952  LYS   A CA  1 
ATOM   1815 C C   . LYS   A 1 259 ? 11.885 -10.981 42.319  1.00 47.30  ? 952  LYS   A C   1 
ATOM   1816 O O   . LYS   A 1 259 ? 10.922 -11.083 41.554  1.00 48.02  ? 952  LYS   A O   1 
ATOM   1817 C CB  . LYS   A 1 259 ? 12.882 -8.649  42.114  1.00 48.52  ? 952  LYS   A CB  1 
ATOM   1818 C CG  . LYS   A 1 259 ? 12.883 -7.217  42.626  1.00 51.37  ? 952  LYS   A CG  1 
ATOM   1819 C CD  . LYS   A 1 259 ? 13.738 -6.289  41.772  1.00 55.30  ? 952  LYS   A CD  1 
ATOM   1820 C CE  . LYS   A 1 259 ? 13.565 -4.834  42.171  1.00 58.88  ? 952  LYS   A CE  1 
ATOM   1821 N N   . CYS   A 1 260 ? 12.724 -12.005 42.564  1.00 45.73  ? 953  CYS   A N   1 
ATOM   1822 C CA  . CYS   A 1 260 ? 12.497 -13.355 42.042  1.00 45.05  ? 953  CYS   A CA  1 
ATOM   1823 C C   . CYS   A 1 260 ? 11.239 -13.991 42.651  1.00 44.63  ? 953  CYS   A C   1 
ATOM   1824 O O   . CYS   A 1 260 ? 10.697 -14.929 42.074  1.00 44.51  ? 953  CYS   A O   1 
ATOM   1825 C CB  . CYS   A 1 260 ? 13.713 -14.244 42.287  1.00 45.36  ? 953  CYS   A CB  1 
ATOM   1826 S SG  . CYS   A 1 260 ? 15.183 -13.781 41.336  1.00 48.59  ? 953  CYS   A SG  1 
ATOM   1827 N N   . TRP   A 1 261 ? 10.805 -13.510 43.836  1.00 44.42  ? 954  TRP   A N   1 
ATOM   1828 C CA  . TRP   A 1 261 ? 9.688  -14.051 44.576  1.00 44.77  ? 954  TRP   A CA  1 
ATOM   1829 C C   . TRP   A 1 261 ? 8.433  -13.201 44.494  1.00 46.85  ? 954  TRP   A C   1 
ATOM   1830 O O   . TRP   A 1 261 ? 7.661  -13.135 45.457  1.00 47.10  ? 954  TRP   A O   1 
ATOM   1831 C CB  . TRP   A 1 261 ? 10.079 -14.309 46.029  1.00 43.66  ? 954  TRP   A CB  1 
ATOM   1832 C CG  . TRP   A 1 261 ? 11.330 -15.108 46.182  1.00 43.41  ? 954  TRP   A CG  1 
ATOM   1833 C CD1 . TRP   A 1 261 ? 11.738 -16.161 45.411  1.00 44.01  ? 954  TRP   A CD1 1 
ATOM   1834 C CD2 . TRP   A 1 261 ? 12.347 -14.911 47.165  1.00 42.97  ? 954  TRP   A CD2 1 
ATOM   1835 N NE1 . TRP   A 1 261 ? 12.951 -16.626 45.851  1.00 44.11  ? 954  TRP   A NE1 1 
ATOM   1836 C CE2 . TRP   A 1 261 ? 13.340 -15.888 46.943  1.00 43.63  ? 954  TRP   A CE2 1 
ATOM   1837 C CE3 . TRP   A 1 261 ? 12.501 -14.024 48.236  1.00 43.26  ? 954  TRP   A CE3 1 
ATOM   1838 C CZ2 . TRP   A 1 261 ? 14.469 -15.999 47.753  1.00 43.63  ? 954  TRP   A CZ2 1 
ATOM   1839 C CZ3 . TRP   A 1 261 ? 13.639 -14.117 49.016  1.00 44.00  ? 954  TRP   A CZ3 1 
ATOM   1840 C CH2 . TRP   A 1 261 ? 14.609 -15.092 48.767  1.00 43.61  ? 954  TRP   A CH2 1 
ATOM   1841 N N   . MET   A 1 262 ? 8.209  -12.584 43.346  1.00 48.20  ? 955  MET   A N   1 
ATOM   1842 C CA  . MET   A 1 262 ? 6.999  -11.814 43.135  1.00 50.83  ? 955  MET   A CA  1 
ATOM   1843 C C   . MET   A 1 262 ? 5.836  -12.727 42.744  1.00 53.54  ? 955  MET   A C   1 
ATOM   1844 O O   . MET   A 1 262 ? 6.059  -13.751 42.115  1.00 53.75  ? 955  MET   A O   1 
ATOM   1845 C CB  . MET   A 1 262 ? 7.233  -10.733 42.093  1.00 51.63  ? 955  MET   A CB  1 
ATOM   1846 C CG  . MET   A 1 262 ? 8.145  -9.659  42.588  1.00 55.04  ? 955  MET   A CG  1 
ATOM   1847 S SD  . MET   A 1 262 ? 8.194  -8.376  41.347  1.00 65.80  ? 955  MET   A SD  1 
ATOM   1848 C CE  . MET   A 1 262 ? 9.363  -7.307  42.039  1.00 70.11  ? 955  MET   A CE  1 
ATOM   1849 N N   . ILE   A 1 263 ? 4.600  -12.374 43.132  1.00 55.59  ? 956  ILE   A N   1 
ATOM   1850 C CA  . ILE   A 1 263 ? 3.400  -13.142 42.800  1.00 58.00  ? 956  ILE   A CA  1 
ATOM   1851 C C   . ILE   A 1 263 ? 3.220  -13.150 41.284  1.00 60.93  ? 956  ILE   A C   1 
ATOM   1852 O O   . ILE   A 1 263 ? 3.048  -14.222 40.697  1.00 61.93  ? 956  ILE   A O   1 
ATOM   1853 C CB  . ILE   A 1 263 ? 2.148  -12.572 43.521  1.00 58.19  ? 956  ILE   A CB  1 
ATOM   1854 C CG1 . ILE   A 1 263 ? 2.287  -12.661 45.045  1.00 58.66  ? 956  ILE   A CG1 1 
ATOM   1855 C CG2 . ILE   A 1 263 ? 0.876  -13.262 43.042  1.00 58.68  ? 956  ILE   A CG2 1 
ATOM   1856 C CD1 . ILE   A 1 263 ? 2.475  -14.058 45.574  1.00 60.11  ? 956  ILE   A CD1 1 
ATOM   1857 N N   . ASP   A 1 264 ? 3.310  -11.966 40.646  1.00 62.20  ? 957  ASP   A N   1 
ATOM   1858 C CA  . ASP   A 1 264 ? 3.188  -11.848 39.191  1.00 64.01  ? 957  ASP   A CA  1 
ATOM   1859 C C   . ASP   A 1 264 ? 4.479  -12.335 38.544  1.00 64.50  ? 957  ASP   A C   1 
ATOM   1860 O O   . ASP   A 1 264 ? 5.529  -11.723 38.738  1.00 64.52  ? 957  ASP   A O   1 
ATOM   1861 C CB  . ASP   A 1 264 ? 2.895  -10.398 38.778  1.00 67.31  ? 957  ASP   A CB  1 
ATOM   1862 C CG  . ASP   A 1 264 ? 2.755  -10.211 37.277  1.00 75.76  ? 957  ASP   A CG  1 
ATOM   1863 O OD1 . ASP   A 1 264 ? 2.365  -11.186 36.586  1.00 77.85  ? 957  ASP   A OD1 1 
ATOM   1864 O OD2 . ASP   A 1 264 ? 3.027  -9.090  36.791  1.00 79.02  ? 957  ASP   A OD2 1 
ATOM   1865 N N   . ALA   A 1 265 ? 4.396  -13.443 37.787  1.00 64.64  ? 958  ALA   A N   1 
ATOM   1866 C CA  . ALA   A 1 265 ? 5.551  -14.062 37.140  1.00 65.40  ? 958  ALA   A CA  1 
ATOM   1867 C C   . ALA   A 1 265 ? 6.244  -13.147 36.136  1.00 66.38  ? 958  ALA   A C   1 
ATOM   1868 O O   . ALA   A 1 265 ? 7.473  -13.133 36.076  1.00 66.60  ? 958  ALA   A O   1 
ATOM   1869 C CB  . ALA   A 1 265 ? 5.146  -15.369 36.479  1.00 65.29  ? 958  ALA   A CB  1 
ATOM   1870 N N   . ASP   A 1 266 ? 5.463  -12.353 35.377  1.00 66.54  ? 959  ASP   A N   1 
ATOM   1871 C CA  . ASP   A 1 266 ? 6.009  -11.421 34.390  1.00 67.32  ? 959  ASP   A CA  1 
ATOM   1872 C C   . ASP   A 1 266 ? 6.748  -10.228 35.000  1.00 66.75  ? 959  ASP   A C   1 
ATOM   1873 O O   . ASP   A 1 266 ? 7.513  -9.571  34.297  1.00 67.51  ? 959  ASP   A O   1 
ATOM   1874 C CB  . ASP   A 1 266 ? 4.922  -10.951 33.419  1.00 70.66  ? 959  ASP   A CB  1 
ATOM   1875 C CG  . ASP   A 1 266 ? 4.448  -12.059 32.503  1.00 77.71  ? 959  ASP   A CG  1 
ATOM   1876 O OD1 . ASP   A 1 266 ? 5.273  -12.944 32.165  1.00 78.51  ? 959  ASP   A OD1 1 
ATOM   1877 O OD2 . ASP   A 1 266 ? 3.254  -12.044 32.122  1.00 81.45  ? 959  ASP   A OD2 1 
ATOM   1878 N N   . SER   A 1 267 ? 6.523  -9.937  36.287  1.00 65.14  ? 960  SER   A N   1 
ATOM   1879 C CA  . SER   A 1 267 ? 7.244  -8.864  36.966  1.00 64.01  ? 960  SER   A CA  1 
ATOM   1880 C C   . SER   A 1 267 ? 8.613  -9.333  37.512  1.00 62.16  ? 960  SER   A C   1 
ATOM   1881 O O   . SER   A 1 267 ? 9.456  -8.497  37.839  1.00 62.53  ? 960  SER   A O   1 
ATOM   1882 C CB  . SER   A 1 267 ? 6.397  -8.276  38.085  1.00 65.77  ? 960  SER   A CB  1 
ATOM   1883 O OG  . SER   A 1 267 ? 5.216  -7.712  37.535  1.00 68.54  ? 960  SER   A OG  1 
ATOM   1884 N N   . ARG   A 1 268 ? 8.837  -10.650 37.620  1.00 59.93  ? 961  ARG   A N   1 
ATOM   1885 C CA  . ARG   A 1 268 ? 10.121 -11.175 38.081  1.00 58.72  ? 961  ARG   A CA  1 
ATOM   1886 C C   . ARG   A 1 268 ? 11.208 -10.874 37.049  1.00 58.37  ? 961  ARG   A C   1 
ATOM   1887 O O   . ARG   A 1 268 ? 10.936 -10.862 35.849  1.00 58.95  ? 961  ARG   A O   1 
ATOM   1888 C CB  . ARG   A 1 268 ? 10.034 -12.692 38.297  1.00 57.74  ? 961  ARG   A CB  1 
ATOM   1889 C CG  . ARG   A 1 268 ? 9.083  -13.081 39.388  1.00 56.46  ? 961  ARG   A CG  1 
ATOM   1890 C CD  . ARG   A 1 268 ? 8.886  -14.573 39.417  1.00 55.93  ? 961  ARG   A CD  1 
ATOM   1891 N NE  . ARG   A 1 268 ? 7.667  -14.901 40.141  1.00 55.46  ? 961  ARG   A NE  1 
ATOM   1892 C CZ  . ARG   A 1 268 ? 6.914  -15.970 39.913  1.00 55.58  ? 961  ARG   A CZ  1 
ATOM   1893 N NH1 . ARG   A 1 268 ? 7.262  -16.850 38.985  1.00 53.96  ? 961  ARG   A NH1 1 
ATOM   1894 N NH2 . ARG   A 1 268 ? 5.801  -16.163 40.607  1.00 55.52  ? 961  ARG   A NH2 1 
ATOM   1895 N N   . PRO   A 1 269 ? 12.450 -10.641 37.489  1.00 57.52  ? 962  PRO   A N   1 
ATOM   1896 C CA  . PRO   A 1 269 ? 13.530 -10.395 36.525  1.00 56.99  ? 962  PRO   A CA  1 
ATOM   1897 C C   . PRO   A 1 269 ? 13.742 -11.559 35.558  1.00 55.72  ? 962  PRO   A C   1 
ATOM   1898 O O   . PRO   A 1 269 ? 13.352 -12.684 35.833  1.00 55.78  ? 962  PRO   A O   1 
ATOM   1899 C CB  . PRO   A 1 269 ? 14.764 -10.230 37.427  1.00 58.10  ? 962  PRO   A CB  1 
ATOM   1900 C CG  . PRO   A 1 269 ? 14.415 -10.971 38.689  1.00 58.66  ? 962  PRO   A CG  1 
ATOM   1901 C CD  . PRO   A 1 269 ? 12.961 -10.639 38.872  1.00 57.07  ? 962  PRO   A CD  1 
ATOM   1902 N N   . LYS   A 1 270 ? 14.350 -11.279 34.418  1.00 54.48  ? 963  LYS   A N   1 
ATOM   1903 C CA  . LYS   A 1 270 ? 14.679 -12.310 33.443  1.00 53.36  ? 963  LYS   A CA  1 
ATOM   1904 C C   . LYS   A 1 270 ? 16.116 -12.774 33.718  1.00 51.52  ? 963  LYS   A C   1 
ATOM   1905 O O   . LYS   A 1 270 ? 16.913 -12.011 34.274  1.00 51.44  ? 963  LYS   A O   1 
ATOM   1906 C CB  . LYS   A 1 270 ? 14.543 -11.755 32.024  1.00 55.54  ? 963  LYS   A CB  1 
ATOM   1907 C CG  . LYS   A 1 270 ? 13.178 -11.128 31.753  1.00 60.96  ? 963  LYS   A CG  1 
ATOM   1908 C CD  . LYS   A 1 270 ? 12.180 -12.137 31.180  1.00 65.90  ? 963  LYS   A CD  1 
ATOM   1909 N N   . PHE   A 1 271 ? 16.465 -14.001 33.319  1.00 49.98  ? 964  PHE   A N   1 
ATOM   1910 C CA  . PHE   A 1 271 ? 17.827 -14.508 33.517  1.00 49.44  ? 964  PHE   A CA  1 
ATOM   1911 C C   . PHE   A 1 271 ? 18.881 -13.623 32.858  1.00 50.53  ? 964  PHE   A C   1 
ATOM   1912 O O   . PHE   A 1 271 ? 19.949 -13.428 33.425  1.00 50.45  ? 964  PHE   A O   1 
ATOM   1913 C CB  . PHE   A 1 271 ? 17.966 -15.963 33.067  1.00 47.89  ? 964  PHE   A CB  1 
ATOM   1914 C CG  . PHE   A 1 271 ? 17.280 -16.941 33.987  1.00 47.12  ? 964  PHE   A CG  1 
ATOM   1915 C CD1 . PHE   A 1 271 ? 17.675 -17.070 35.305  1.00 47.60  ? 964  PHE   A CD1 1 
ATOM   1916 C CD2 . PHE   A 1 271 ? 16.258 -17.749 33.526  1.00 47.02  ? 964  PHE   A CD2 1 
ATOM   1917 C CE1 . PHE   A 1 271 ? 17.051 -17.980 36.144  1.00 48.10  ? 964  PHE   A CE1 1 
ATOM   1918 C CE2 . PHE   A 1 271 ? 15.646 -18.667 34.365  1.00 47.37  ? 964  PHE   A CE2 1 
ATOM   1919 C CZ  . PHE   A 1 271 ? 16.042 -18.772 35.667  1.00 47.42  ? 964  PHE   A CZ  1 
ATOM   1920 N N   . ARG   A 1 272 ? 18.540 -13.027 31.713  1.00 51.48  ? 965  ARG   A N   1 
ATOM   1921 C CA  . ARG   A 1 272 ? 19.383 -12.088 30.984  1.00 53.10  ? 965  ARG   A CA  1 
ATOM   1922 C C   . ARG   A 1 272 ? 19.723 -10.861 31.864  1.00 53.31  ? 965  ARG   A C   1 
ATOM   1923 O O   . ARG   A 1 272 ? 20.861 -10.393 31.846  1.00 53.72  ? 965  ARG   A O   1 
ATOM   1924 C CB  . ARG   A 1 272 ? 18.633 -11.625 29.735  1.00 56.40  ? 965  ARG   A CB  1 
ATOM   1925 C CG  . ARG   A 1 272 ? 19.520 -11.021 28.671  1.00 63.16  ? 965  ARG   A CG  1 
ATOM   1926 C CD  . ARG   A 1 272 ? 18.703 -10.127 27.752  1.00 70.74  ? 965  ARG   A CD  1 
ATOM   1927 N NE  . ARG   A 1 272 ? 19.128 -10.176 26.351  1.00 77.79  ? 965  ARG   A NE  1 
ATOM   1928 C CZ  . ARG   A 1 272 ? 20.153 -9.495  25.844  1.00 81.97  ? 965  ARG   A CZ  1 
ATOM   1929 N NH1 . ARG   A 1 272 ? 20.915 -8.740  26.631  1.00 82.82  ? 965  ARG   A NH1 1 
ATOM   1930 N NH2 . ARG   A 1 272 ? 20.452 -9.599  24.554  1.00 81.52  ? 965  ARG   A NH2 1 
ATOM   1931 N N   . GLU   A 1 273 ? 18.731 -10.350 32.632  1.00 52.68  ? 966  GLU   A N   1 
ATOM   1932 C CA  . GLU   A 1 273 ? 18.881 -9.208  33.536  1.00 52.26  ? 966  GLU   A CA  1 
ATOM   1933 C C   . GLU   A 1 273 ? 19.657 -9.605  34.790  1.00 50.94  ? 966  GLU   A C   1 
ATOM   1934 O O   . GLU   A 1 273 ? 20.509 -8.846  35.257  1.00 51.20  ? 966  GLU   A O   1 
ATOM   1935 C CB  . GLU   A 1 273 ? 17.505 -8.651  33.925  1.00 56.12  ? 966  GLU   A CB  1 
ATOM   1936 C CG  . GLU   A 1 273 ? 16.639 -8.283  32.728  1.00 64.90  ? 966  GLU   A CG  1 
ATOM   1937 C CD  . GLU   A 1 273 ? 15.198 -7.934  33.060  1.00 75.16  ? 966  GLU   A CD  1 
ATOM   1938 O OE1 . GLU   A 1 273 ? 14.778 -8.170  34.216  1.00 76.73  ? 966  GLU   A OE1 1 
ATOM   1939 O OE2 . GLU   A 1 273 ? 14.482 -7.440  32.159  1.00 79.51  ? 966  GLU   A OE2 1 
ATOM   1940 N N   . LEU   A 1 274 ? 19.367 -10.797 35.336  1.00 49.52  ? 967  LEU   A N   1 
ATOM   1941 C CA  . LEU   A 1 274 ? 20.072 -11.340 36.493  1.00 48.71  ? 967  LEU   A CA  1 
ATOM   1942 C C   . LEU   A 1 274 ? 21.575 -11.501 36.192  1.00 47.91  ? 967  LEU   A C   1 
ATOM   1943 O O   . LEU   A 1 274 ? 22.397 -11.296 37.081  1.00 48.02  ? 967  LEU   A O   1 
ATOM   1944 C CB  . LEU   A 1 274 ? 19.471 -12.685 36.894  1.00 48.64  ? 967  LEU   A CB  1 
ATOM   1945 C CG  . LEU   A 1 274 ? 18.062 -12.632 37.437  1.00 49.87  ? 967  LEU   A CG  1 
ATOM   1946 C CD1 . LEU   A 1 274 ? 17.434 -14.019 37.460  1.00 50.16  ? 967  LEU   A CD1 1 
ATOM   1947 C CD2 . LEU   A 1 274 ? 18.030 -11.963 38.817  1.00 50.18  ? 967  LEU   A CD2 1 
ATOM   1948 N N   . ILE   A 1 275 ? 21.940 -11.815 34.938  1.00 47.08  ? 968  ILE   A N   1 
ATOM   1949 C CA  . ILE   A 1 275 ? 23.349 -11.941 34.549  1.00 47.12  ? 968  ILE   A CA  1 
ATOM   1950 C C   . ILE   A 1 275 ? 24.014 -10.573 34.696  1.00 48.37  ? 968  ILE   A C   1 
ATOM   1951 O O   . ILE   A 1 275 ? 25.053 -10.466 35.331  1.00 48.72  ? 968  ILE   A O   1 
ATOM   1952 C CB  . ILE   A 1 275 ? 23.529 -12.501 33.105  1.00 46.19  ? 968  ILE   A CB  1 
ATOM   1953 C CG1 . ILE   A 1 275 ? 23.032 -13.960 32.971  1.00 45.75  ? 968  ILE   A CG1 1 
ATOM   1954 C CG2 . ILE   A 1 275 ? 24.979 -12.365 32.644  1.00 46.39  ? 968  ILE   A CG2 1 
ATOM   1955 C CD1 . ILE   A 1 275 ? 22.792 -14.407 31.566  1.00 45.80  ? 968  ILE   A CD1 1 
ATOM   1956 N N   . ILE   A 1 276 ? 23.374 -9.534  34.164  1.00 48.58  ? 969  ILE   A N   1 
ATOM   1957 C CA  . ILE   A 1 276 ? 23.868 -8.178  34.226  1.00 49.61  ? 969  ILE   A CA  1 
ATOM   1958 C C   . ILE   A 1 276 ? 23.999 -7.680  35.661  1.00 50.87  ? 969  ILE   A C   1 
ATOM   1959 O O   . ILE   A 1 276 ? 25.067 -7.182  36.019  1.00 51.50  ? 969  ILE   A O   1 
ATOM   1960 C CB  . ILE   A 1 276 ? 22.994 -7.258  33.339  1.00 50.27  ? 969  ILE   A CB  1 
ATOM   1961 C CG1 . ILE   A 1 276 ? 23.057 -7.720  31.863  1.00 51.18  ? 969  ILE   A CG1 1 
ATOM   1962 C CG2 . ILE   A 1 276 ? 23.366 -5.770  33.498  1.00 50.07  ? 969  ILE   A CG2 1 
ATOM   1963 C CD1 . ILE   A 1 276 ? 21.971 -7.114  30.964  1.00 52.51  ? 969  ILE   A CD1 1 
ATOM   1964 N N   . GLU   A 1 277 ? 22.950 -7.849  36.500  1.00 50.88  ? 970  GLU   A N   1 
ATOM   1965 C CA  . GLU   A 1 277 ? 22.996 -7.413  37.898  1.00 51.10  ? 970  GLU   A CA  1 
ATOM   1966 C C   . GLU   A 1 277 ? 24.111 -8.095  38.696  1.00 51.04  ? 970  GLU   A C   1 
ATOM   1967 O O   . GLU   A 1 277 ? 24.949 -7.408  39.273  1.00 51.60  ? 970  GLU   A O   1 
ATOM   1968 C CB  . GLU   A 1 277 ? 21.638 -7.616  38.584  1.00 53.61  ? 970  GLU   A CB  1 
ATOM   1969 C CG  . GLU   A 1 277 ? 20.534 -6.754  38.009  1.00 58.62  ? 970  GLU   A CG  1 
ATOM   1970 N N   . PHE   A 1 278 ? 24.142 -9.434  38.710  1.00 50.41  ? 971  PHE   A N   1 
ATOM   1971 C CA  . PHE   A 1 278 ? 25.178 -10.159 39.431  1.00 50.47  ? 971  PHE   A CA  1 
ATOM   1972 C C   . PHE   A 1 278 ? 26.575 -9.946  38.846  1.00 50.83  ? 971  PHE   A C   1 
ATOM   1973 O O   . PHE   A 1 278 ? 27.553 -10.049 39.578  1.00 51.45  ? 971  PHE   A O   1 
ATOM   1974 C CB  . PHE   A 1 278 ? 24.835 -11.646 39.559  1.00 50.12  ? 971  PHE   A CB  1 
ATOM   1975 C CG  . PHE   A 1 278 ? 23.831 -11.916 40.647  1.00 50.95  ? 971  PHE   A CG  1 
ATOM   1976 C CD1 . PHE   A 1 278 ? 24.209 -11.903 41.979  1.00 52.10  ? 971  PHE   A CD1 1 
ATOM   1977 C CD2 . PHE   A 1 278 ? 22.503 -12.161 40.342  1.00 51.44  ? 971  PHE   A CD2 1 
ATOM   1978 C CE1 . PHE   A 1 278 ? 23.279 -12.156 42.986  1.00 52.85  ? 971  PHE   A CE1 1 
ATOM   1979 C CE2 . PHE   A 1 278 ? 21.579 -12.420 41.343  1.00 52.13  ? 971  PHE   A CE2 1 
ATOM   1980 C CZ  . PHE   A 1 278 ? 21.968 -12.410 42.660  1.00 52.26  ? 971  PHE   A CZ  1 
ATOM   1981 N N   . SER   A 1 279 ? 26.680 -9.641  37.544  1.00 50.29  ? 972  SER   A N   1 
ATOM   1982 C CA  . SER   A 1 279 ? 27.973 -9.366  36.922  1.00 50.45  ? 972  SER   A CA  1 
ATOM   1983 C C   . SER   A 1 279 ? 28.528 -8.036  37.418  1.00 51.52  ? 972  SER   A C   1 
ATOM   1984 O O   . SER   A 1 279 ? 29.731 -7.924  37.602  1.00 51.99  ? 972  SER   A O   1 
ATOM   1985 C CB  . SER   A 1 279 ? 27.867 -9.348  35.402  1.00 50.42  ? 972  SER   A CB  1 
ATOM   1986 O OG  . SER   A 1 279 ? 27.786 -10.665 34.885  1.00 50.65  ? 972  SER   A OG  1 
ATOM   1987 N N   . LYS   A 1 280 ? 27.660 -7.038  37.632  1.00 51.63  ? 973  LYS   A N   1 
ATOM   1988 C CA  . LYS   A 1 280 ? 28.046 -5.742  38.165  1.00 52.59  ? 973  LYS   A CA  1 
ATOM   1989 C C   . LYS   A 1 280 ? 28.562 -5.920  39.603  1.00 53.74  ? 973  LYS   A C   1 
ATOM   1990 O O   . LYS   A 1 280 ? 29.607 -5.377  39.969  1.00 54.19  ? 973  LYS   A O   1 
ATOM   1991 C CB  . LYS   A 1 280 ? 26.848 -4.771  38.118  1.00 54.30  ? 973  LYS   A CB  1 
ATOM   1992 C CG  . LYS   A 1 280 ? 27.079 -3.451  38.854  1.00 58.36  ? 973  LYS   A CG  1 
ATOM   1993 N N   . MET   A 1 281 ? 27.849 -6.711  40.402  1.00 53.82  ? 974  MET   A N   1 
ATOM   1994 C CA  . MET   A 1 281 ? 28.232 -6.989  41.776  1.00 53.92  ? 974  MET   A CA  1 
ATOM   1995 C C   . MET   A 1 281 ? 29.517 -7.780  41.896  1.00 54.29  ? 974  MET   A C   1 
ATOM   1996 O O   . MET   A 1 281 ? 30.301 -7.517  42.804  1.00 54.46  ? 974  MET   A O   1 
ATOM   1997 C CB  . MET   A 1 281 ? 27.097 -7.687  42.507  1.00 54.17  ? 974  MET   A CB  1 
ATOM   1998 C CG  . MET   A 1 281 ? 25.887 -6.842  42.565  1.00 55.75  ? 974  MET   A CG  1 
ATOM   1999 S SD  . MET   A 1 281 ? 24.580 -7.591  43.521  1.00 59.68  ? 974  MET   A SD  1 
ATOM   2000 C CE  . MET   A 1 281 ? 23.544 -6.131  43.749  1.00 60.18  ? 974  MET   A CE  1 
ATOM   2001 N N   . ALA   A 1 282 ? 29.756 -8.720  40.978  1.00 54.36  ? 975  ALA   A N   1 
ATOM   2002 C CA  . ALA   A 1 282 ? 30.993 -9.504  40.994  1.00 55.33  ? 975  ALA   A CA  1 
ATOM   2003 C C   . ALA   A 1 282 ? 32.233 -8.643  40.664  1.00 56.83  ? 975  ALA   A C   1 
ATOM   2004 O O   . ALA   A 1 282 ? 33.340 -9.032  41.007  1.00 56.77  ? 975  ALA   A O   1 
ATOM   2005 C CB  . ALA   A 1 282 ? 30.890 -10.692 40.053  1.00 55.14  ? 975  ALA   A CB  1 
ATOM   2006 N N   . ARG   A 1 283 ? 32.052 -7.467  40.032  1.00 58.15  ? 976  ARG   A N   1 
ATOM   2007 C CA  . ARG   A 1 283 ? 33.157 -6.555  39.749  1.00 59.95  ? 976  ARG   A CA  1 
ATOM   2008 C C   . ARG   A 1 283 ? 33.651 -5.829  41.012  1.00 62.07  ? 976  ARG   A C   1 
ATOM   2009 O O   . ARG   A 1 283 ? 34.820 -5.440  41.070  1.00 62.94  ? 976  ARG   A O   1 
ATOM   2010 C CB  . ARG   A 1 283 ? 32.798 -5.582  38.629  1.00 60.81  ? 976  ARG   A CB  1 
ATOM   2011 C CG  . ARG   A 1 283 ? 32.692 -6.304  37.303  1.00 64.12  ? 976  ARG   A CG  1 
ATOM   2012 C CD  . ARG   A 1 283 ? 32.741 -5.355  36.119  1.00 67.78  ? 976  ARG   A CD  1 
ATOM   2013 N NE  . ARG   A 1 283 ? 31.480 -4.642  35.920  1.00 71.30  ? 976  ARG   A NE  1 
ATOM   2014 C CZ  . ARG   A 1 283 ? 30.432 -5.135  35.260  1.00 74.96  ? 976  ARG   A CZ  1 
ATOM   2015 N NH1 . ARG   A 1 283 ? 29.330 -4.412  35.120  1.00 75.34  ? 976  ARG   A NH1 1 
ATOM   2016 N NH2 . ARG   A 1 283 ? 30.477 -6.361  34.744  1.00 75.43  ? 976  ARG   A NH2 1 
ATOM   2017 N N   . ASP   A 1 284 ? 32.785 -5.677  42.033  1.00 62.61  ? 977  ASP   A N   1 
ATOM   2018 C CA  . ASP   A 1 284 ? 33.146 -5.080  43.329  1.00 63.38  ? 977  ASP   A CA  1 
ATOM   2019 C C   . ASP   A 1 284 ? 32.457 -5.924  44.426  1.00 63.79  ? 977  ASP   A C   1 
ATOM   2020 O O   . ASP   A 1 284 ? 31.463 -5.484  44.999  1.00 64.09  ? 977  ASP   A O   1 
ATOM   2021 C CB  . ASP   A 1 284 ? 32.659 -3.626  43.382  1.00 65.26  ? 977  ASP   A CB  1 
ATOM   2022 C CG  . ASP   A 1 284 ? 33.233 -2.798  44.518  1.00 71.46  ? 977  ASP   A CG  1 
ATOM   2023 O OD1 . ASP   A 1 284 ? 34.109 -3.318  45.257  1.00 72.42  ? 977  ASP   A OD1 1 
ATOM   2024 O OD2 . ASP   A 1 284 ? 32.817 -1.623  44.663  1.00 74.30  ? 977  ASP   A OD2 1 
ATOM   2025 N N   . PRO   A 1 285 ? 32.925 -7.165  44.692  1.00 63.59  ? 978  PRO   A N   1 
ATOM   2026 C CA  . PRO   A 1 285 ? 32.161 -8.058  45.584  1.00 63.67  ? 978  PRO   A CA  1 
ATOM   2027 C C   . PRO   A 1 285 ? 32.099 -7.683  47.068  1.00 63.73  ? 978  PRO   A C   1 
ATOM   2028 O O   . PRO   A 1 285 ? 31.103 -8.009  47.713  1.00 63.78  ? 978  PRO   A O   1 
ATOM   2029 C CB  . PRO   A 1 285 ? 32.816 -9.428  45.368  1.00 64.05  ? 978  PRO   A CB  1 
ATOM   2030 C CG  . PRO   A 1 285 ? 34.169 -9.132  44.880  1.00 64.32  ? 978  PRO   A CG  1 
ATOM   2031 C CD  . PRO   A 1 285 ? 34.060 -7.874  44.069  1.00 62.85  ? 978  PRO   A CD  1 
ATOM   2032 N N   . GLN   A 1 286 ? 33.124 -7.014  47.610  1.00 63.46  ? 979  GLN   A N   1 
ATOM   2033 C CA  . GLN   A 1 286 ? 33.111 -6.616  49.019  1.00 64.11  ? 979  GLN   A CA  1 
ATOM   2034 C C   . GLN   A 1 286 ? 32.067 -5.516  49.338  1.00 64.05  ? 979  GLN   A C   1 
ATOM   2035 O O   . GLN   A 1 286 ? 31.732 -5.305  50.500  1.00 64.27  ? 979  GLN   A O   1 
ATOM   2036 C CB  . GLN   A 1 286 ? 34.516 -6.196  49.486  1.00 66.22  ? 979  GLN   A CB  1 
ATOM   2037 C CG  . GLN   A 1 286 ? 35.494 -7.359  49.649  1.00 69.59  ? 979  GLN   A CG  1 
ATOM   2038 N N   . ARG   A 1 287 ? 31.558 -4.831  48.313  1.00 63.57  ? 980  ARG   A N   1 
ATOM   2039 C CA  . ARG   A 1 287 ? 30.527 -3.808  48.444  1.00 63.67  ? 980  ARG   A CA  1 
ATOM   2040 C C   . ARG   A 1 287 ? 29.116 -4.432  48.574  1.00 62.75  ? 980  ARG   A C   1 
ATOM   2041 O O   . ARG   A 1 287 ? 28.202 -3.781  49.072  1.00 63.24  ? 980  ARG   A O   1 
ATOM   2042 C CB  . ARG   A 1 287 ? 30.554 -2.910  47.192  1.00 65.83  ? 980  ARG   A CB  1 
ATOM   2043 C CG  . ARG   A 1 287 ? 29.949 -1.533  47.406  1.00 70.35  ? 980  ARG   A CG  1 
ATOM   2044 C CD  . ARG   A 1 287 ? 28.800 -1.251  46.466  1.00 74.90  ? 980  ARG   A CD  1 
ATOM   2045 N NE  . ARG   A 1 287 ? 29.216 -0.459  45.309  1.00 79.36  ? 980  ARG   A NE  1 
ATOM   2046 C CZ  . ARG   A 1 287 ? 28.577 0.626   44.877  1.00 82.39  ? 980  ARG   A CZ  1 
ATOM   2047 N NH1 . ARG   A 1 287 ? 27.484 1.056   45.499  1.00 81.68  ? 980  ARG   A NH1 1 
ATOM   2048 N NH2 . ARG   A 1 287 ? 29.020 1.283   43.813  1.00 82.94  ? 980  ARG   A NH2 1 
ATOM   2049 N N   . TYR   A 1 288 ? 28.931 -5.676  48.111  1.00 61.31  ? 981  TYR   A N   1 
ATOM   2050 C CA  . TYR   A 1 288 ? 27.626 -6.327  48.094  1.00 60.43  ? 981  TYR   A CA  1 
ATOM   2051 C C   . TYR   A 1 288 ? 27.488 -7.478  49.080  1.00 60.15  ? 981  TYR   A C   1 
ATOM   2052 O O   . TYR   A 1 288 ? 26.383 -7.744  49.547  1.00 59.96  ? 981  TYR   A O   1 
ATOM   2053 C CB  . TYR   A 1 288 ? 27.291 -6.766  46.667  1.00 59.72  ? 981  TYR   A CB  1 
ATOM   2054 C CG  . TYR   A 1 288 ? 27.237 -5.578  45.736  1.00 59.87  ? 981  TYR   A CG  1 
ATOM   2055 C CD1 . TYR   A 1 288 ? 26.171 -4.698  45.767  1.00 60.37  ? 981  TYR   A CD1 1 
ATOM   2056 C CD2 . TYR   A 1 288 ? 28.309 -5.264  44.917  1.00 60.45  ? 981  TYR   A CD2 1 
ATOM   2057 C CE1 . TYR   A 1 288 ? 26.130 -3.585  44.941  1.00 61.11  ? 981  TYR   A CE1 1 
ATOM   2058 C CE2 . TYR   A 1 288 ? 28.285 -4.149  44.092  1.00 61.14  ? 981  TYR   A CE2 1 
ATOM   2059 C CZ  . TYR   A 1 288 ? 27.186 -3.318  44.096  1.00 62.28  ? 981  TYR   A CZ  1 
ATOM   2060 O OH  . TYR   A 1 288 ? 27.157 -2.199  43.292  1.00 64.60  ? 981  TYR   A OH  1 
ATOM   2061 N N   . LEU   A 1 289 ? 28.595 -8.150  49.407  1.00 59.87  ? 982  LEU   A N   1 
ATOM   2062 C CA  . LEU   A 1 289 ? 28.572 -9.219  50.393  1.00 60.45  ? 982  LEU   A CA  1 
ATOM   2063 C C   . LEU   A 1 289 ? 29.600 -8.923  51.481  1.00 61.50  ? 982  LEU   A C   1 
ATOM   2064 O O   . LEU   A 1 289 ? 30.760 -8.634  51.179  1.00 61.80  ? 982  LEU   A O   1 
ATOM   2065 C CB  . LEU   A 1 289 ? 28.855 -10.586 49.756  1.00 60.18  ? 982  LEU   A CB  1 
ATOM   2066 C CG  . LEU   A 1 289 ? 27.841 -11.104 48.743  1.00 60.90  ? 982  LEU   A CG  1 
ATOM   2067 C CD1 . LEU   A 1 289 ? 28.255 -12.462 48.223  1.00 61.13  ? 982  LEU   A CD1 1 
ATOM   2068 C CD2 . LEU   A 1 289 ? 26.456 -11.192 49.345  1.00 61.29  ? 982  LEU   A CD2 1 
ATOM   2069 N N   . VAL   A 1 290 ? 29.175 -8.983  52.742  1.00 61.81  ? 983  VAL   A N   1 
ATOM   2070 C CA  . VAL   A 1 290 ? 30.052 -8.731  53.879  1.00 62.62  ? 983  VAL   A CA  1 
ATOM   2071 C C   . VAL   A 1 290 ? 30.389 -10.067 54.545  1.00 63.53  ? 983  VAL   A C   1 
ATOM   2072 O O   . VAL   A 1 290 ? 29.569 -10.619 55.280  1.00 63.82  ? 983  VAL   A O   1 
ATOM   2073 C CB  . VAL   A 1 290 ? 29.405 -7.738  54.874  1.00 63.11  ? 983  VAL   A CB  1 
ATOM   2074 C CG1 . VAL   A 1 290 ? 30.371 -7.404  56.009  1.00 63.45  ? 983  VAL   A CG1 1 
ATOM   2075 C CG2 . VAL   A 1 290 ? 28.931 -6.474  54.155  1.00 63.43  ? 983  VAL   A CG2 1 
ATOM   2076 N N   . ILE   A 1 291 ? 31.572 -10.610 54.251  1.00 63.72  ? 984  ILE   A N   1 
ATOM   2077 C CA  . ILE   A 1 291 ? 31.976 -11.904 54.782  1.00 64.97  ? 984  ILE   A CA  1 
ATOM   2078 C C   . ILE   A 1 291 ? 33.242 -11.785 55.631  1.00 67.09  ? 984  ILE   A C   1 
ATOM   2079 O O   . ILE   A 1 291 ? 34.192 -11.127 55.214  1.00 67.12  ? 984  ILE   A O   1 
ATOM   2080 C CB  . ILE   A 1 291 ? 32.170 -12.903 53.599  1.00 64.96  ? 984  ILE   A CB  1 
ATOM   2081 C CG1 . ILE   A 1 291 ? 30.853 -13.129 52.853  1.00 65.49  ? 984  ILE   A CG1 1 
ATOM   2082 C CG2 . ILE   A 1 291 ? 32.766 -14.227 54.063  1.00 65.27  ? 984  ILE   A CG2 1 
ATOM   2083 C CD1 . ILE   A 1 291 ? 30.973 -13.862 51.614  1.00 66.50  ? 984  ILE   A CD1 1 
ATOM   2084 N N   . GLN   A 1 292 ? 33.266 -12.410 56.820  1.00 68.71  ? 985  GLN   A N   1 
ATOM   2085 C CA  . GLN   A 1 292 ? 34.468 -12.402 57.666  1.00 70.93  ? 985  GLN   A CA  1 
ATOM   2086 C C   . GLN   A 1 292 ? 35.516 -13.280 56.953  1.00 72.98  ? 985  GLN   A C   1 
ATOM   2087 O O   . GLN   A 1 292 ? 35.211 -14.426 56.589  1.00 73.30  ? 985  GLN   A O   1 
ATOM   2088 C CB  . GLN   A 1 292 ? 34.150 -12.972 59.055  1.00 72.51  ? 985  GLN   A CB  1 
ATOM   2089 C CG  . GLN   A 1 292 ? 35.276 -12.783 60.045  1.00 76.95  ? 985  GLN   A CG  1 
ATOM   2090 C CD  . GLN   A 1 292 ? 35.108 -13.626 61.287  1.00 81.90  ? 985  GLN   A CD  1 
ATOM   2091 O OE1 . GLN   A 1 292 ? 34.437 -14.665 61.287  1.00 84.19  ? 985  GLN   A OE1 1 
ATOM   2092 N NE2 . GLN   A 1 292 ? 35.730 -13.203 62.370  1.00 82.32  ? 985  GLN   A NE2 1 
ATOM   2093 N N   . GLY   A 1 293 ? 36.691 -12.720 56.671  1.00 73.77  ? 986  GLY   A N   1 
ATOM   2094 C CA  . GLY   A 1 293 ? 37.705 -13.457 55.917  1.00 74.72  ? 986  GLY   A CA  1 
ATOM   2095 C C   . GLY   A 1 293 ? 38.039 -12.851 54.564  1.00 75.24  ? 986  GLY   A C   1 
ATOM   2096 O O   . GLY   A 1 293 ? 39.075 -13.168 53.972  1.00 75.61  ? 986  GLY   A O   1 
ATOM   2097 N N   . ASP   A 1 294 ? 37.160 -11.972 54.058  1.00 75.02  ? 987  ASP   A N   1 
ATOM   2098 C CA  . ASP   A 1 294 ? 37.424 -11.212 52.839  1.00 75.47  ? 987  ASP   A CA  1 
ATOM   2099 C C   . ASP   A 1 294 ? 38.304 -9.959  53.116  1.00 76.76  ? 987  ASP   A C   1 
ATOM   2100 O O   . ASP   A 1 294 ? 38.681 -9.268  52.173  1.00 77.21  ? 987  ASP   A O   1 
ATOM   2101 C CB  . ASP   A 1 294 ? 36.119 -10.787 52.167  1.00 75.83  ? 987  ASP   A CB  1 
ATOM   2102 C CG  . ASP   A 1 294 ? 35.603 -11.791 51.162  1.00 77.28  ? 987  ASP   A CG  1 
ATOM   2103 O OD1 . ASP   A 1 294 ? 36.427 -12.534 50.588  1.00 77.09  ? 987  ASP   A OD1 1 
ATOM   2104 O OD2 . ASP   A 1 294 ? 34.378 -11.828 50.942  1.00 78.56  ? 987  ASP   A OD2 1 
ATOM   2105 N N   . GLU   A 1 295 ? 38.641 -9.671  54.387  1.00 77.15  ? 988  GLU   A N   1 
ATOM   2106 C CA  . GLU   A 1 295 ? 39.482 -8.538  54.732  1.00 78.36  ? 988  GLU   A CA  1 
ATOM   2107 C C   . GLU   A 1 295 ? 40.963 -8.903  54.563  1.00 79.63  ? 988  GLU   A C   1 
ATOM   2108 O O   . GLU   A 1 295 ? 41.759 -8.741  55.497  1.00 79.85  ? 988  GLU   A O   1 
ATOM   2109 C CB  . GLU   A 1 295 ? 39.183 -8.053  56.164  1.00 80.17  ? 988  GLU   A CB  1 
ATOM   2110 N N   . ARG   A 1 296 ? 41.331 -9.380  53.356  1.00 80.07  ? 989  ARG   A N   1 
ATOM   2111 C CA  . ARG   A 1 296 ? 42.704 -9.760  53.027  1.00 81.07  ? 989  ARG   A CA  1 
ATOM   2112 C C   . ARG   A 1 296 ? 43.473 -8.582  52.424  1.00 81.42  ? 989  ARG   A C   1 
ATOM   2113 O O   . ARG   A 1 296 ? 44.694 -8.651  52.266  1.00 81.62  ? 989  ARG   A O   1 
ATOM   2114 C CB  . ARG   A 1 296 ? 42.711 -10.934 52.043  1.00 83.10  ? 989  ARG   A CB  1 
ATOM   2115 C CG  . ARG   A 1 296 ? 41.989 -12.172 52.549  1.00 86.77  ? 989  ARG   A CG  1 
ATOM   2116 C CD  . ARG   A 1 296 ? 41.917 -13.250 51.487  1.00 90.24  ? 989  ARG   A CD  1 
ATOM   2117 N NE  . ARG   A 1 296 ? 40.620 -13.247 50.814  1.00 94.13  ? 989  ARG   A NE  1 
ATOM   2118 C CZ  . ARG   A 1 296 ? 40.387 -12.694 49.628  1.00 96.76  ? 989  ARG   A CZ  1 
ATOM   2119 N NH1 . ARG   A 1 296 ? 39.170 -12.726 49.103  1.00 95.97  ? 989  ARG   A NH1 1 
ATOM   2120 N NH2 . ARG   A 1 296 ? 41.371 -12.104 48.957  1.00 97.14  ? 989  ARG   A NH2 1 
ATOM   2121 N N   . ALA   B 1 9   ? 23.224 -9.175  23.088  1.00 86.93  ? 702  ALA   B N   1 
ATOM   2122 C CA  . ALA   B 1 9   ? 23.608 -8.048  23.937  1.00 87.46  ? 702  ALA   B CA  1 
ATOM   2123 C C   . ALA   B 1 9   ? 23.412 -6.689  23.241  1.00 87.75  ? 702  ALA   B C   1 
ATOM   2124 O O   . ALA   B 1 9   ? 23.356 -6.622  22.010  1.00 88.26  ? 702  ALA   B O   1 
ATOM   2125 C CB  . ALA   B 1 9   ? 25.054 -8.203  24.387  1.00 87.68  ? 702  ALA   B CB  1 
ATOM   2126 N N   . LEU   B 1 10  ? 23.290 -5.603  24.030  1.00 87.06  ? 703  LEU   B N   1 
ATOM   2127 C CA  . LEU   B 1 10  ? 23.162 -4.262  23.462  1.00 86.40  ? 703  LEU   B CA  1 
ATOM   2128 C C   . LEU   B 1 10  ? 24.521 -3.814  22.900  1.00 85.66  ? 703  LEU   B C   1 
ATOM   2129 O O   . LEU   B 1 10  ? 25.584 -4.257  23.360  1.00 85.68  ? 703  LEU   B O   1 
ATOM   2130 C CB  . LEU   B 1 10  ? 22.664 -3.260  24.512  1.00 86.46  ? 703  LEU   B CB  1 
ATOM   2131 N N   . LEU   B 1 11  ? 24.484 -2.951  21.887  1.00 84.64  ? 704  LEU   B N   1 
ATOM   2132 C CA  . LEU   B 1 11  ? 25.700 -2.461  21.253  1.00 83.73  ? 704  LEU   B CA  1 
ATOM   2133 C C   . LEU   B 1 11  ? 26.139 -1.147  21.868  1.00 82.50  ? 704  LEU   B C   1 
ATOM   2134 O O   . LEU   B 1 11  ? 25.353 -0.202  21.948  1.00 82.85  ? 704  LEU   B O   1 
ATOM   2135 C CB  . LEU   B 1 11  ? 25.475 -2.305  19.747  1.00 83.79  ? 704  LEU   B CB  1 
ATOM   2136 C CG  . LEU   B 1 11  ? 26.602 -1.698  18.938  1.00 85.07  ? 704  LEU   B CG  1 
ATOM   2137 C CD1 . LEU   B 1 11  ? 27.736 -2.675  18.761  1.00 85.37  ? 704  LEU   B CD1 1 
ATOM   2138 C CD2 . LEU   B 1 11  ? 26.091 -1.191  17.604  1.00 85.83  ? 704  LEU   B CD2 1 
ATOM   2139 N N   . ARG   B 1 12  ? 27.393 -1.087  22.308  1.00 81.10  ? 705  ARG   B N   1 
ATOM   2140 C CA  . ARG   B 1 12  ? 27.932 0.126   22.888  1.00 80.31  ? 705  ARG   B CA  1 
ATOM   2141 C C   . ARG   B 1 12  ? 28.513 1.036   21.809  1.00 78.82  ? 705  ARG   B C   1 
ATOM   2142 O O   . ARG   B 1 12  ? 29.332 0.610   21.003  1.00 78.20  ? 705  ARG   B O   1 
ATOM   2143 C CB  . ARG   B 1 12  ? 28.975 -0.186  23.970  1.00 82.02  ? 705  ARG   B CB  1 
ATOM   2144 C CG  . ARG   B 1 12  ? 28.367 -0.512  25.324  1.00 86.38  ? 705  ARG   B CG  1 
ATOM   2145 C CD  . ARG   B 1 12  ? 29.066 -1.691  25.991  1.00 91.20  ? 705  ARG   B CD  1 
ATOM   2146 N NE  . ARG   B 1 12  ? 28.833 -2.945  25.265  1.00 94.70  ? 705  ARG   B NE  1 
ATOM   2147 C CZ  . ARG   B 1 12  ? 29.387 -4.111  25.578  1.00 96.65  ? 705  ARG   B CZ  1 
ATOM   2148 N NH1 . ARG   B 1 12  ? 30.228 -4.201  26.601  1.00 96.54  ? 705  ARG   B NH1 1 
ATOM   2149 N NH2 . ARG   B 1 12  ? 29.111 -5.194  24.865  1.00 96.48  ? 705  ARG   B NH2 1 
ATOM   2150 N N   . ILE   B 1 13  ? 28.066 2.293   21.789  1.00 78.06  ? 706  ILE   B N   1 
ATOM   2151 C CA  . ILE   B 1 13  ? 28.591 3.280   20.870  1.00 77.70  ? 706  ILE   B CA  1 
ATOM   2152 C C   . ILE   B 1 13  ? 29.673 4.023   21.644  1.00 77.49  ? 706  ILE   B C   1 
ATOM   2153 O O   . ILE   B 1 13  ? 29.385 4.707   22.620  1.00 77.92  ? 706  ILE   B O   1 
ATOM   2154 C CB  . ILE   B 1 13  ? 27.471 4.194   20.319  1.00 78.10  ? 706  ILE   B CB  1 
ATOM   2155 C CG1 . ILE   B 1 13  ? 26.519 3.389   19.404  1.00 79.17  ? 706  ILE   B CG1 1 
ATOM   2156 C CG2 . ILE   B 1 13  ? 28.065 5.375   19.572  1.00 78.25  ? 706  ILE   B CG2 1 
ATOM   2157 N N   . LEU   B 1 14  ? 30.927 3.805   21.274  1.00 77.09  ? 707  LEU   B N   1 
ATOM   2158 C CA  . LEU   B 1 14  ? 32.062 4.406   21.965  1.00 77.60  ? 707  LEU   B CA  1 
ATOM   2159 C C   . LEU   B 1 14  ? 32.461 5.759   21.360  1.00 78.17  ? 707  LEU   B C   1 
ATOM   2160 O O   . LEU   B 1 14  ? 32.139 6.061   20.213  1.00 78.07  ? 707  LEU   B O   1 
ATOM   2161 C CB  . LEU   B 1 14  ? 33.265 3.438   21.938  1.00 78.07  ? 707  LEU   B CB  1 
ATOM   2162 C CG  . LEU   B 1 14  ? 33.400 2.424   23.098  1.00 79.85  ? 707  LEU   B CG  1 
ATOM   2163 C CD1 . LEU   B 1 14  ? 32.224 1.484   23.161  1.00 80.44  ? 707  LEU   B CD1 1 
ATOM   2164 C CD2 . LEU   B 1 14  ? 34.655 1.593   22.956  1.00 80.49  ? 707  LEU   B CD2 1 
ATOM   2165 N N   . LYS   B 1 15  ? 33.149 6.580   22.152  1.00 78.59  ? 708  LYS   B N   1 
ATOM   2166 C CA  . LYS   B 1 15  ? 33.676 7.873   21.726  1.00 79.28  ? 708  LYS   B CA  1 
ATOM   2167 C C   . LYS   B 1 15  ? 35.205 7.749   21.631  1.00 80.14  ? 708  LYS   B C   1 
ATOM   2168 O O   . LYS   B 1 15  ? 35.799 6.934   22.333  1.00 79.91  ? 708  LYS   B O   1 
ATOM   2169 C CB  . LYS   B 1 15  ? 33.308 8.967   22.741  1.00 80.97  ? 708  LYS   B CB  1 
ATOM   2170 C CG  . LYS   B 1 15  ? 31.811 9.199   22.888  1.00 84.86  ? 708  LYS   B CG  1 
ATOM   2171 N N   . GLU   B 1 16  ? 35.850 8.572   20.802  1.00 81.20  ? 709  GLU   B N   1 
ATOM   2172 C CA  . GLU   B 1 16  ? 37.311 8.548   20.657  1.00 82.75  ? 709  GLU   B CA  1 
ATOM   2173 C C   . GLU   B 1 16  ? 38.047 8.843   21.979  1.00 83.73  ? 709  GLU   B C   1 
ATOM   2174 O O   . GLU   B 1 16  ? 39.159 8.353   22.186  1.00 84.22  ? 709  GLU   B O   1 
ATOM   2175 C CB  . GLU   B 1 16  ? 37.750 9.533   19.569  1.00 85.79  ? 709  GLU   B CB  1 
ATOM   2176 C CG  . GLU   B 1 16  ? 37.495 9.017   18.165  1.00 91.02  ? 709  GLU   B CG  1 
ATOM   2177 C CD  . GLU   B 1 16  ? 37.415 10.118  17.127  1.00 97.39  ? 709  GLU   B CD  1 
ATOM   2178 O OE1 . GLU   B 1 16  ? 36.736 11.136  17.392  1.00 97.89  ? 709  GLU   B OE1 1 
ATOM   2179 O OE2 . GLU   B 1 16  ? 38.023 9.957   16.044  1.00 100.10 ? 709  GLU   B OE2 1 
ATOM   2180 N N   . THR   B 1 17  ? 37.408 9.617   22.876  1.00 83.61  ? 710  THR   B N   1 
ATOM   2181 C CA  . THR   B 1 17  ? 37.933 9.953   24.197  1.00 84.15  ? 710  THR   B CA  1 
ATOM   2182 C C   . THR   B 1 17  ? 37.942 8.750   25.153  1.00 83.66  ? 710  THR   B C   1 
ATOM   2183 O O   . THR   B 1 17  ? 38.783 8.698   26.047  1.00 83.91  ? 710  THR   B O   1 
ATOM   2184 C CB  . THR   B 1 17  ? 37.091 11.072  24.816  1.00 86.46  ? 710  THR   B CB  1 
ATOM   2185 O OG1 . THR   B 1 17  ? 35.711 10.688  24.764  1.00 88.16  ? 710  THR   B OG1 1 
ATOM   2186 C CG2 . THR   B 1 17  ? 37.297 12.413  24.125  1.00 86.70  ? 710  THR   B CG2 1 
ATOM   2187 N N   . GLU   B 1 18  ? 36.996 7.802   24.980  1.00 82.81  ? 711  GLU   B N   1 
ATOM   2188 C CA  . GLU   B 1 18  ? 36.851 6.608   25.819  1.00 82.31  ? 711  GLU   B CA  1 
ATOM   2189 C C   . GLU   B 1 18  ? 38.003 5.637   25.700  1.00 81.70  ? 711  GLU   B C   1 
ATOM   2190 O O   . GLU   B 1 18  ? 38.286 4.902   26.646  1.00 81.89  ? 711  GLU   B O   1 
ATOM   2191 C CB  . GLU   B 1 18  ? 35.569 5.847   25.467  1.00 84.62  ? 711  GLU   B CB  1 
ATOM   2192 C CG  . GLU   B 1 18  ? 34.292 6.450   26.015  1.00 90.03  ? 711  GLU   B CG  1 
ATOM   2193 C CD  . GLU   B 1 18  ? 33.096 5.543   25.794  1.00 96.92  ? 711  GLU   B CD  1 
ATOM   2194 O OE1 . GLU   B 1 18  ? 33.159 4.361   26.209  1.00 98.24  ? 711  GLU   B OE1 1 
ATOM   2195 O OE2 . GLU   B 1 18  ? 32.103 6.011   25.191  1.00 98.74  ? 711  GLU   B OE2 1 
ATOM   2196 N N   . PHE   B 1 19  ? 38.624 5.576   24.528  1.00 81.01  ? 712  PHE   B N   1 
ATOM   2197 C CA  . PHE   B 1 19  ? 39.711 4.638   24.292  1.00 80.87  ? 712  PHE   B CA  1 
ATOM   2198 C C   . PHE   B 1 19  ? 40.922 5.300   23.659  1.00 80.62  ? 712  PHE   B C   1 
ATOM   2199 O O   . PHE   B 1 19  ? 40.805 6.328   22.991  1.00 80.78  ? 712  PHE   B O   1 
ATOM   2200 C CB  . PHE   B 1 19  ? 39.228 3.432   23.453  1.00 80.78  ? 712  PHE   B CB  1 
ATOM   2201 C CG  . PHE   B 1 19  ? 38.763 3.756   22.052  1.00 81.37  ? 712  PHE   B CG  1 
ATOM   2202 C CD1 . PHE   B 1 19  ? 37.448 4.103   21.804  1.00 82.19  ? 712  PHE   B CD1 1 
ATOM   2203 C CD2 . PHE   B 1 19  ? 39.633 3.678   20.979  1.00 82.22  ? 712  PHE   B CD2 1 
ATOM   2204 C CE1 . PHE   B 1 19  ? 37.024 4.413   20.514  1.00 82.91  ? 712  PHE   B CE1 1 
ATOM   2205 C CE2 . PHE   B 1 19  ? 39.205 3.985   19.692  1.00 82.93  ? 712  PHE   B CE2 1 
ATOM   2206 C CZ  . PHE   B 1 19  ? 37.903 4.348   19.468  1.00 82.67  ? 712  PHE   B CZ  1 
ATOM   2207 N N   . LYS   B 1 20  ? 42.087 4.697   23.858  1.00 80.14  ? 713  LYS   B N   1 
ATOM   2208 C CA  . LYS   B 1 20  ? 43.322 5.200   23.283  1.00 80.15  ? 713  LYS   B CA  1 
ATOM   2209 C C   . LYS   B 1 20  ? 44.001 4.104   22.463  1.00 80.21  ? 713  LYS   B C   1 
ATOM   2210 O O   . LYS   B 1 20  ? 43.929 2.930   22.819  1.00 80.15  ? 713  LYS   B O   1 
ATOM   2211 C CB  . LYS   B 1 20  ? 44.260 5.708   24.382  1.00 81.55  ? 713  LYS   B CB  1 
ATOM   2212 N N   . LYS   B 1 21  ? 44.647 4.482   21.355  1.00 80.22  ? 714  LYS   B N   1 
ATOM   2213 C CA  . LYS   B 1 21  ? 45.379 3.540   20.511  1.00 80.57  ? 714  LYS   B CA  1 
ATOM   2214 C C   . LYS   B 1 21  ? 46.846 3.569   20.954  1.00 81.08  ? 714  LYS   B C   1 
ATOM   2215 O O   . LYS   B 1 21  ? 47.430 4.648   21.043  1.00 81.53  ? 714  LYS   B O   1 
ATOM   2216 C CB  . LYS   B 1 21  ? 45.231 3.916   19.026  1.00 82.00  ? 714  LYS   B CB  1 
ATOM   2217 C CG  . LYS   B 1 21  ? 43.884 3.504   18.412  1.00 85.36  ? 714  LYS   B CG  1 
ATOM   2218 C CD  . LYS   B 1 21  ? 43.708 4.058   17.006  1.00 89.08  ? 714  LYS   B CD  1 
ATOM   2219 C CE  . LYS   B 1 21  ? 43.146 5.445   17.009  1.00 92.34  ? 714  LYS   B CE  1 
ATOM   2220 N N   . ILE   B 1 22  ? 47.424 2.408   21.297  1.00 80.87  ? 715  ILE   B N   1 
ATOM   2221 C CA  . ILE   B 1 22  ? 48.803 2.349   21.795  1.00 81.06  ? 715  ILE   B CA  1 
ATOM   2222 C C   . ILE   B 1 22  ? 49.815 2.005   20.689  1.00 80.61  ? 715  ILE   B C   1 
ATOM   2223 O O   . ILE   B 1 22  ? 50.728 2.791   20.447  1.00 81.10  ? 715  ILE   B O   1 
ATOM   2224 C CB  . ILE   B 1 22  ? 48.930 1.412   23.030  1.00 81.81  ? 715  ILE   B CB  1 
ATOM   2225 C CG1 . ILE   B 1 22  ? 47.914 1.789   24.118  1.00 82.89  ? 715  ILE   B CG1 1 
ATOM   2226 C CG2 . ILE   B 1 22  ? 50.341 1.433   23.587  1.00 82.31  ? 715  ILE   B CG2 1 
ATOM   2227 N N   . LYS   B 1 23  ? 49.660 0.858   20.016  1.00 79.78  ? 716  LYS   B N   1 
ATOM   2228 C CA  . LYS   B 1 23  ? 50.572 0.472   18.940  1.00 79.44  ? 716  LYS   B CA  1 
ATOM   2229 C C   . LYS   B 1 23  ? 49.857 -0.263  17.805  1.00 79.19  ? 716  LYS   B C   1 
ATOM   2230 O O   . LYS   B 1 23  ? 48.789 -0.825  18.008  1.00 79.01  ? 716  LYS   B O   1 
ATOM   2231 C CB  . LYS   B 1 23  ? 51.759 -0.354  19.478  1.00 80.73  ? 716  LYS   B CB  1 
ATOM   2232 C CG  . LYS   B 1 23  ? 51.435 -1.801  19.820  1.00 83.20  ? 716  LYS   B CG  1 
ATOM   2233 N N   . VAL   B 1 24  ? 50.444 -0.254  16.605  1.00 78.96  ? 717  VAL   B N   1 
ATOM   2234 C CA  . VAL   B 1 24  ? 49.869 -0.945  15.456  1.00 78.82  ? 717  VAL   B CA  1 
ATOM   2235 C C   . VAL   B 1 24  ? 50.215 -2.432  15.529  1.00 79.09  ? 717  VAL   B C   1 
ATOM   2236 O O   . VAL   B 1 24  ? 51.374 -2.783  15.736  1.00 79.36  ? 717  VAL   B O   1 
ATOM   2237 C CB  . VAL   B 1 24  ? 50.367 -0.329  14.128  1.00 78.97  ? 717  VAL   B CB  1 
ATOM   2238 C CG1 . VAL   B 1 24  ? 49.829 -1.102  12.934  1.00 79.44  ? 717  VAL   B CG1 1 
ATOM   2239 C CG2 . VAL   B 1 24  ? 49.989 1.142   14.031  1.00 79.17  ? 717  VAL   B CG2 1 
ATOM   2240 N N   . LEU   B 1 25  ? 49.218 -3.301  15.366  1.00 78.83  ? 718  LEU   B N   1 
ATOM   2241 C CA  . LEU   B 1 25  ? 49.400 -4.748  15.358  1.00 79.22  ? 718  LEU   B CA  1 
ATOM   2242 C C   . LEU   B 1 25  ? 49.566 -5.264  13.927  1.00 79.94  ? 718  LEU   B C   1 
ATOM   2243 O O   . LEU   B 1 25  ? 50.364 -6.166  13.684  1.00 80.09  ? 718  LEU   B O   1 
ATOM   2244 C CB  . LEU   B 1 25  ? 48.205 -5.448  16.026  1.00 79.19  ? 718  LEU   B CB  1 
ATOM   2245 C CG  . LEU   B 1 25  ? 47.981 -5.154  17.498  1.00 80.25  ? 718  LEU   B CG  1 
ATOM   2246 C CD1 . LEU   B 1 25  ? 46.734 -5.854  18.003  1.00 80.36  ? 718  LEU   B CD1 1 
ATOM   2247 C CD2 . LEU   B 1 25  ? 49.180 -5.563  18.317  1.00 80.97  ? 718  LEU   B CD2 1 
ATOM   2248 N N   . GLY   B 1 26  ? 48.798 -4.699  13.002  1.00 80.35  ? 719  GLY   B N   1 
ATOM   2249 C CA  . GLY   B 1 26  ? 48.839 -5.065  11.595  1.00 81.32  ? 719  GLY   B CA  1 
ATOM   2250 C C   . GLY   B 1 26  ? 48.227 -4.012  10.693  1.00 82.31  ? 719  GLY   B C   1 
ATOM   2251 O O   . GLY   B 1 26  ? 47.476 -3.155  11.153  1.00 82.09  ? 719  GLY   B O   1 
ATOM   2252 N N   . SER   B 1 27  ? 48.551 -4.067  9.397   1.00 83.17  ? 720  SER   B N   1 
ATOM   2253 C CA  . SER   B 1 27  ? 48.033 -3.141  8.387   1.00 84.20  ? 720  SER   B CA  1 
ATOM   2254 C C   . SER   B 1 27  ? 47.526 -3.914  7.140   1.00 85.02  ? 720  SER   B C   1 
ATOM   2255 O O   . SER   B 1 27  ? 47.651 -5.142  7.067   1.00 85.25  ? 720  SER   B O   1 
ATOM   2256 C CB  . SER   B 1 27  ? 49.109 -2.132  7.990   1.00 85.84  ? 720  SER   B CB  1 
ATOM   2257 O OG  . SER   B 1 27  ? 49.387 -1.206  9.027   1.00 88.86  ? 720  SER   B OG  1 
ATOM   2258 N N   . GLY   B 1 28  ? 46.939 -3.198  6.183   1.00 85.06  ? 721  GLY   B N   1 
ATOM   2259 C CA  . GLY   B 1 28  ? 46.439 -3.820  4.964   1.00 85.40  ? 721  GLY   B CA  1 
ATOM   2260 C C   . GLY   B 1 28  ? 45.608 -2.889  4.109   1.00 85.36  ? 721  GLY   B C   1 
ATOM   2261 O O   . GLY   B 1 28  ? 45.574 -1.678  4.349   1.00 85.61  ? 721  GLY   B O   1 
ATOM   2262 N N   . ALA   B 1 29  ? 44.953 -3.445  3.081   1.00 84.62  ? 722  ALA   B N   1 
ATOM   2263 C CA  . ALA   B 1 29  ? 44.071 -2.663  2.209   1.00 83.97  ? 722  ALA   B CA  1 
ATOM   2264 C C   . ALA   B 1 29  ? 42.758 -2.326  2.958   1.00 82.75  ? 722  ALA   B C   1 
ATOM   2265 O O   . ALA   B 1 29  ? 42.182 -1.258  2.736   1.00 82.66  ? 722  ALA   B O   1 
ATOM   2266 C CB  . ALA   B 1 29  ? 43.766 -3.447  0.941   1.00 84.19  ? 722  ALA   B CB  1 
ATOM   2267 N N   . PHE   B 1 30  ? 42.308 -3.249  3.856   1.00 81.36  ? 723  PHE   B N   1 
ATOM   2268 C CA  . PHE   B 1 30  ? 41.121 -3.142  4.711   1.00 80.35  ? 723  PHE   B CA  1 
ATOM   2269 C C   . PHE   B 1 30  ? 41.215 -1.958  5.695   1.00 77.95  ? 723  PHE   B C   1 
ATOM   2270 O O   . PHE   B 1 30  ? 40.193 -1.426  6.108   1.00 77.80  ? 723  PHE   B O   1 
ATOM   2271 C CB  . PHE   B 1 30  ? 40.929 -4.460  5.521   1.00 80.99  ? 723  PHE   B CB  1 
ATOM   2272 C CG  . PHE   B 1 30  ? 41.881 -4.612  6.695   1.00 82.54  ? 723  PHE   B CG  1 
ATOM   2273 C CD1 . PHE   B 1 30  ? 43.169 -5.087  6.507   1.00 83.82  ? 723  PHE   B CD1 1 
ATOM   2274 C CD2 . PHE   B 1 30  ? 41.516 -4.192  7.966   1.00 83.59  ? 723  PHE   B CD2 1 
ATOM   2275 C CE1 . PHE   B 1 30  ? 44.062 -5.161  7.571   1.00 84.77  ? 723  PHE   B CE1 1 
ATOM   2276 C CE2 . PHE   B 1 30  ? 42.421 -4.237  9.018   1.00 84.57  ? 723  PHE   B CE2 1 
ATOM   2277 C CZ  . PHE   B 1 30  ? 43.680 -4.743  8.821   1.00 84.54  ? 723  PHE   B CZ  1 
ATOM   2278 N N   . GLY   B 1 31  ? 42.427 -1.635  6.128   1.00 75.95  ? 724  GLY   B N   1 
ATOM   2279 C CA  . GLY   B 1 31  ? 42.660 -0.620  7.138   1.00 74.64  ? 724  GLY   B CA  1 
ATOM   2280 C C   . GLY   B 1 31  ? 43.749 -1.049  8.103   1.00 73.00  ? 724  GLY   B C   1 
ATOM   2281 O O   . GLY   B 1 31  ? 44.726 -1.665  7.684   1.00 73.39  ? 724  GLY   B O   1 
ATOM   2282 N N   . THR   B 1 32  ? 43.598 -0.740  9.403   1.00 70.91  ? 725  THR   B N   1 
ATOM   2283 C CA  . THR   B 1 32  ? 44.626 -1.045  10.399  1.00 69.21  ? 725  THR   B CA  1 
ATOM   2284 C C   . THR   B 1 32  ? 44.063 -1.637  11.706  1.00 66.95  ? 725  THR   B C   1 
ATOM   2285 O O   . THR   B 1 32  ? 42.952 -1.307  12.098  1.00 66.54  ? 725  THR   B O   1 
ATOM   2286 C CB  . THR   B 1 32  ? 45.414 0.247   10.697  1.00 70.47  ? 725  THR   B CB  1 
ATOM   2287 O OG1 . THR   B 1 32  ? 45.884 0.816   9.474   1.00 71.79  ? 725  THR   B OG1 1 
ATOM   2288 C CG2 . THR   B 1 32  ? 46.583 0.035   11.656  1.00 70.62  ? 725  THR   B CG2 1 
ATOM   2289 N N   . VAL   B 1 33  ? 44.842 -2.503  12.381  1.00 65.37  ? 726  VAL   B N   1 
ATOM   2290 C CA  . VAL   B 1 33  ? 44.482 -3.071  13.681  1.00 64.71  ? 726  VAL   B CA  1 
ATOM   2291 C C   . VAL   B 1 33  ? 45.425 -2.494  14.749  1.00 64.48  ? 726  VAL   B C   1 
ATOM   2292 O O   . VAL   B 1 33  ? 46.637 -2.514  14.577  1.00 64.42  ? 726  VAL   B O   1 
ATOM   2293 C CB  . VAL   B 1 33  ? 44.484 -4.617  13.675  1.00 64.39  ? 726  VAL   B CB  1 
ATOM   2294 C CG1 . VAL   B 1 33  ? 44.323 -5.175  15.083  1.00 64.43  ? 726  VAL   B CG1 1 
ATOM   2295 C CG2 . VAL   B 1 33  ? 43.398 -5.148  12.758  1.00 64.63  ? 726  VAL   B CG2 1 
ATOM   2296 N N   . TYR   B 1 34  ? 44.869 -1.944  15.825  1.00 64.31  ? 727  TYR   B N   1 
ATOM   2297 C CA  . TYR   B 1 34  ? 45.650 -1.337  16.891  1.00 64.70  ? 727  TYR   B CA  1 
ATOM   2298 C C   . TYR   B 1 34  ? 45.449 -2.059  18.210  1.00 64.75  ? 727  TYR   B C   1 
ATOM   2299 O O   . TYR   B 1 34  ? 44.367 -2.540  18.487  1.00 64.14  ? 727  TYR   B O   1 
ATOM   2300 C CB  . TYR   B 1 34  ? 45.197 0.114   17.090  1.00 64.85  ? 727  TYR   B CB  1 
ATOM   2301 C CG  . TYR   B 1 34  ? 45.354 0.998   15.877  1.00 66.17  ? 727  TYR   B CG  1 
ATOM   2302 C CD1 . TYR   B 1 34  ? 46.512 1.730   15.675  1.00 67.22  ? 727  TYR   B CD1 1 
ATOM   2303 C CD2 . TYR   B 1 34  ? 44.307 1.177   14.980  1.00 67.27  ? 727  TYR   B CD2 1 
ATOM   2304 C CE1 . TYR   B 1 34  ? 46.640 2.595   14.596  1.00 68.25  ? 727  TYR   B CE1 1 
ATOM   2305 C CE2 . TYR   B 1 34  ? 44.429 2.027   13.888  1.00 68.27  ? 727  TYR   B CE2 1 
ATOM   2306 C CZ  . TYR   B 1 34  ? 45.595 2.745   13.704  1.00 69.52  ? 727  TYR   B CZ  1 
ATOM   2307 O OH  . TYR   B 1 34  ? 45.719 3.610   12.631  1.00 71.48  ? 727  TYR   B OH  1 
ATOM   2308 N N   . LYS   B 1 35  ? 46.475 -2.081  19.048  1.00 65.62  ? 728  LYS   B N   1 
ATOM   2309 C CA  . LYS   B 1 35  ? 46.401 -2.609  20.408  1.00 66.81  ? 728  LYS   B CA  1 
ATOM   2310 C C   . LYS   B 1 35  ? 46.150 -1.358  21.229  1.00 68.33  ? 728  LYS   B C   1 
ATOM   2311 O O   . LYS   B 1 35  ? 46.929 -0.411  21.138  1.00 68.70  ? 728  LYS   B O   1 
ATOM   2312 C CB  . LYS   B 1 35  ? 47.742 -3.237  20.825  1.00 68.20  ? 728  LYS   B CB  1 
ATOM   2313 C CG  . LYS   B 1 35  ? 47.816 -3.631  22.291  1.00 71.53  ? 728  LYS   B CG  1 
ATOM   2314 N N   . GLY   B 1 36  ? 45.052 -1.321  21.968  1.00 69.01  ? 729  GLY   B N   1 
ATOM   2315 C CA  . GLY   B 1 36  ? 44.711 -0.136  22.741  1.00 69.82  ? 729  GLY   B CA  1 
ATOM   2316 C C   . GLY   B 1 36  ? 44.229 -0.378  24.150  1.00 70.64  ? 729  GLY   B C   1 
ATOM   2317 O O   . GLY   B 1 36  ? 44.332 -1.484  24.679  1.00 70.82  ? 729  GLY   B O   1 
ATOM   2318 N N   . LEU   B 1 37  ? 43.718 0.676   24.771  1.00 71.18  ? 730  LEU   B N   1 
ATOM   2319 C CA  . LEU   B 1 37  ? 43.209 0.607   26.129  1.00 72.41  ? 730  LEU   B CA  1 
ATOM   2320 C C   . LEU   B 1 37  ? 41.878 1.326   26.174  1.00 73.70  ? 730  LEU   B C   1 
ATOM   2321 O O   . LEU   B 1 37  ? 41.749 2.417   25.627  1.00 73.79  ? 730  LEU   B O   1 
ATOM   2322 C CB  . LEU   B 1 37  ? 44.202 1.265   27.107  1.00 72.58  ? 730  LEU   B CB  1 
ATOM   2323 C CG  . LEU   B 1 37  ? 44.267 0.634   28.494  1.00 74.03  ? 730  LEU   B CG  1 
ATOM   2324 C CD1 . LEU   B 1 37  ? 44.729 -0.816  28.426  1.00 74.14  ? 730  LEU   B CD1 1 
ATOM   2325 C CD2 . LEU   B 1 37  ? 45.166 1.429   29.404  1.00 75.02  ? 730  LEU   B CD2 1 
ATOM   2326 N N   . TRP   B 1 38  ? 40.890 0.723   26.820  1.00 74.71  ? 731  TRP   B N   1 
ATOM   2327 C CA  . TRP   B 1 38  ? 39.571 1.319   26.928  1.00 76.44  ? 731  TRP   B CA  1 
ATOM   2328 C C   . TRP   B 1 38  ? 39.200 1.586   28.386  1.00 79.37  ? 731  TRP   B C   1 
ATOM   2329 O O   . TRP   B 1 38  ? 39.373 0.719   29.244  1.00 79.47  ? 731  TRP   B O   1 
ATOM   2330 C CB  . TRP   B 1 38  ? 38.538 0.410   26.245  1.00 75.77  ? 731  TRP   B CB  1 
ATOM   2331 C CG  . TRP   B 1 38  ? 37.103 0.791   26.458  1.00 75.43  ? 731  TRP   B CG  1 
ATOM   2332 C CD1 . TRP   B 1 38  ? 36.564 2.041   26.391  1.00 76.06  ? 731  TRP   B CD1 1 
ATOM   2333 C CD2 . TRP   B 1 38  ? 36.006 -0.109  26.654  1.00 75.08  ? 731  TRP   B CD2 1 
ATOM   2334 N NE1 . TRP   B 1 38  ? 35.208 1.982   26.605  1.00 76.21  ? 731  TRP   B NE1 1 
ATOM   2335 C CE2 . TRP   B 1 38  ? 34.837 0.671   26.761  1.00 75.70  ? 731  TRP   B CE2 1 
ATOM   2336 C CE3 . TRP   B 1 38  ? 35.897 -1.501  26.758  1.00 75.41  ? 731  TRP   B CE3 1 
ATOM   2337 C CZ2 . TRP   B 1 38  ? 33.581 0.107   26.968  1.00 76.11  ? 731  TRP   B CZ2 1 
ATOM   2338 C CZ3 . TRP   B 1 38  ? 34.653 -2.057  26.974  1.00 76.03  ? 731  TRP   B CZ3 1 
ATOM   2339 C CH2 . TRP   B 1 38  ? 33.511 -1.259  27.065  1.00 76.14  ? 731  TRP   B CH2 1 
ATOM   2340 N N   . ILE   B 1 39  ? 38.699 2.799   28.651  1.00 81.56  ? 732  ILE   B N   1 
ATOM   2341 C CA  . ILE   B 1 39  ? 38.184 3.248   29.940  1.00 84.18  ? 732  ILE   B CA  1 
ATOM   2342 C C   . ILE   B 1 39  ? 36.678 3.449   29.735  1.00 86.54  ? 732  ILE   B C   1 
ATOM   2343 O O   . ILE   B 1 39  ? 36.263 4.422   29.091  1.00 86.56  ? 732  ILE   B O   1 
ATOM   2344 C CB  . ILE   B 1 39  ? 38.864 4.570   30.387  1.00 85.11  ? 732  ILE   B CB  1 
ATOM   2345 C CG1 . ILE   B 1 39  ? 40.344 4.344   30.740  1.00 86.22  ? 732  ILE   B CG1 1 
ATOM   2346 C CG2 . ILE   B 1 39  ? 38.109 5.218   31.558  1.00 85.63  ? 732  ILE   B CG2 1 
ATOM   2347 C CD1 . ILE   B 1 39  ? 41.117 5.631   31.002  1.00 87.52  ? 732  ILE   B CD1 1 
ATOM   2348 N N   . PRO   B 1 40  ? 35.844 2.501   30.196  1.00 88.16  ? 733  PRO   B N   1 
ATOM   2349 C CA  . PRO   B 1 40  ? 34.394 2.650   29.998  1.00 89.76  ? 733  PRO   B CA  1 
ATOM   2350 C C   . PRO   B 1 40  ? 33.859 3.878   30.731  1.00 92.22  ? 733  PRO   B C   1 
ATOM   2351 O O   . PRO   B 1 40  ? 34.293 4.144   31.855  1.00 92.41  ? 733  PRO   B O   1 
ATOM   2352 C CB  . PRO   B 1 40  ? 33.817 1.350   30.564  1.00 90.03  ? 733  PRO   B CB  1 
ATOM   2353 C CG  . PRO   B 1 40  ? 34.987 0.403   30.663  1.00 90.05  ? 733  PRO   B CG  1 
ATOM   2354 C CD  . PRO   B 1 40  ? 36.165 1.276   30.946  1.00 87.97  ? 733  PRO   B CD  1 
ATOM   2355 N N   . GLU   B 1 41  ? 32.957 4.637   30.056  1.00 93.66  ? 734  GLU   B N   1 
ATOM   2356 C CA  . GLU   B 1 41  ? 32.283 5.884   30.467  1.00 95.35  ? 734  GLU   B CA  1 
ATOM   2357 C C   . GLU   B 1 41  ? 32.443 6.276   31.963  1.00 96.29  ? 734  GLU   B C   1 
ATOM   2358 O O   . GLU   B 1 41  ? 32.977 7.349   32.256  1.00 96.68  ? 734  GLU   B O   1 
ATOM   2359 C CB  . GLU   B 1 41  ? 30.787 5.848   30.072  1.00 98.32  ? 734  GLU   B CB  1 
ATOM   2360 C CG  . GLU   B 1 41  ? 30.024 7.121   30.410  1.00 103.72 ? 734  GLU   B CG  1 
ATOM   2361 C CD  . GLU   B 1 41  ? 28.645 6.901   31.004  1.00 110.26 ? 734  GLU   B CD  1 
ATOM   2362 O OE1 . GLU   B 1 41  ? 27.848 7.866   31.026  1.00 112.06 ? 734  GLU   B OE1 1 
ATOM   2363 O OE2 . GLU   B 1 41  ? 28.362 5.766   31.452  1.00 112.05 ? 734  GLU   B OE2 1 
ATOM   2364 N N   . GLY   B 1 42  ? 31.972 5.433   32.880  1.00 96.35  ? 735  GLY   B N   1 
ATOM   2365 C CA  . GLY   B 1 42  ? 32.085 5.712   34.306  1.00 96.84  ? 735  GLY   B CA  1 
ATOM   2366 C C   . GLY   B 1 42  ? 32.382 4.493   35.155  1.00 97.21  ? 735  GLY   B C   1 
ATOM   2367 O O   . GLY   B 1 42  ? 32.224 4.533   36.376  1.00 97.51  ? 735  GLY   B O   1 
ATOM   2368 N N   . GLU   B 1 43  ? 32.823 3.401   34.525  1.00 97.00  ? 736  GLU   B N   1 
ATOM   2369 C CA  . GLU   B 1 43  ? 33.124 2.168   35.238  1.00 97.30  ? 736  GLU   B CA  1 
ATOM   2370 C C   . GLU   B 1 43  ? 34.471 2.199   35.971  1.00 97.43  ? 736  GLU   B C   1 
ATOM   2371 O O   . GLU   B 1 43  ? 34.679 1.363   36.858  1.00 97.95  ? 736  GLU   B O   1 
ATOM   2372 C CB  . GLU   B 1 43  ? 33.069 0.968   34.279  1.00 99.09  ? 736  GLU   B CB  1 
ATOM   2373 N N   . LYS   B 1 44  ? 35.383 3.139   35.596  1.00 96.55  ? 737  LYS   B N   1 
ATOM   2374 C CA  . LYS   B 1 44  ? 36.735 3.263   36.167  1.00 96.06  ? 737  LYS   B CA  1 
ATOM   2375 C C   . LYS   B 1 44  ? 37.529 1.943   36.023  1.00 95.11  ? 737  LYS   B C   1 
ATOM   2376 O O   . LYS   B 1 44  ? 37.824 1.269   37.019  1.00 95.41  ? 737  LYS   B O   1 
ATOM   2377 C CB  . LYS   B 1 44  ? 36.697 3.740   37.628  1.00 97.86  ? 737  LYS   B CB  1 
ATOM   2378 N N   . VAL   B 1 45  ? 37.828 1.560   34.770  1.00 93.45  ? 738  VAL   B N   1 
ATOM   2379 C CA  . VAL   B 1 45  ? 38.546 0.321   34.467  1.00 91.97  ? 738  VAL   B CA  1 
ATOM   2380 C C   . VAL   B 1 45  ? 39.493 0.485   33.280  1.00 89.74  ? 738  VAL   B C   1 
ATOM   2381 O O   . VAL   B 1 45  ? 39.294 1.354   32.431  1.00 89.84  ? 738  VAL   B O   1 
ATOM   2382 C CB  . VAL   B 1 45  ? 37.568 -0.846  34.216  1.00 92.70  ? 738  VAL   B CB  1 
ATOM   2383 N N   . LYS   B 1 46  ? 40.522 -0.361  33.216  1.00 87.39  ? 739  LYS   B N   1 
ATOM   2384 C CA  . LYS   B 1 46  ? 41.475 -0.329  32.118  1.00 85.42  ? 739  LYS   B CA  1 
ATOM   2385 C C   . LYS   B 1 46  ? 41.375 -1.656  31.381  1.00 82.88  ? 739  LYS   B C   1 
ATOM   2386 O O   . LYS   B 1 46  ? 41.923 -2.664  31.833  1.00 82.96  ? 739  LYS   B O   1 
ATOM   2387 C CB  . LYS   B 1 46  ? 42.899 -0.075  32.635  1.00 87.09  ? 739  LYS   B CB  1 
ATOM   2388 C CG  . LYS   B 1 46  ? 43.067 1.304   33.259  1.00 90.74  ? 739  LYS   B CG  1 
ATOM   2389 N N   . ILE   B 1 47  ? 40.621 -1.673  30.273  1.00 80.29  ? 740  ILE   B N   1 
ATOM   2390 C CA  . ILE   B 1 47  ? 40.429 -2.893  29.500  1.00 77.99  ? 740  ILE   B CA  1 
ATOM   2391 C C   . ILE   B 1 47  ? 41.339 -2.931  28.278  1.00 75.38  ? 740  ILE   B C   1 
ATOM   2392 O O   . ILE   B 1 47  ? 41.232 -2.089  27.393  1.00 75.21  ? 740  ILE   B O   1 
ATOM   2393 C CB  . ILE   B 1 47  ? 38.940 -3.081  29.118  1.00 78.23  ? 740  ILE   B CB  1 
ATOM   2394 C CG1 . ILE   B 1 47  ? 38.036 -2.995  30.358  1.00 79.05  ? 740  ILE   B CG1 1 
ATOM   2395 C CG2 . ILE   B 1 47  ? 38.727 -4.385  28.364  1.00 78.46  ? 740  ILE   B CG2 1 
ATOM   2396 N N   . PRO   B 1 48  ? 42.255 -3.909  28.221  1.00 73.25  ? 741  PRO   B N   1 
ATOM   2397 C CA  . PRO   B 1 48  ? 43.122 -4.032  27.041  1.00 71.43  ? 741  PRO   B CA  1 
ATOM   2398 C C   . PRO   B 1 48  ? 42.275 -4.451  25.846  1.00 68.65  ? 741  PRO   B C   1 
ATOM   2399 O O   . PRO   B 1 48  ? 41.669 -5.523  25.865  1.00 68.69  ? 741  PRO   B O   1 
ATOM   2400 C CB  . PRO   B 1 48  ? 44.109 -5.147  27.432  1.00 72.68  ? 741  PRO   B CB  1 
ATOM   2401 C CG  . PRO   B 1 48  ? 43.933 -5.349  28.914  1.00 73.74  ? 741  PRO   B CG  1 
ATOM   2402 C CD  . PRO   B 1 48  ? 42.507 -4.988  29.189  1.00 72.63  ? 741  PRO   B CD  1 
ATOM   2403 N N   . VAL   B 1 49  ? 42.183 -3.583  24.832  1.00 65.86  ? 742  VAL   B N   1 
ATOM   2404 C CA  . VAL   B 1 49  ? 41.357 -3.870  23.667  1.00 63.60  ? 742  VAL   B CA  1 
ATOM   2405 C C   . VAL   B 1 49  ? 42.162 -3.933  22.354  1.00 61.55  ? 742  VAL   B C   1 
ATOM   2406 O O   . VAL   B 1 49  ? 43.323 -3.550  22.318  1.00 61.90  ? 742  VAL   B O   1 
ATOM   2407 C CB  . VAL   B 1 49  ? 40.198 -2.840  23.576  1.00 63.58  ? 742  VAL   B CB  1 
ATOM   2408 C CG1 . VAL   B 1 49  ? 39.186 -3.038  24.695  1.00 63.89  ? 742  VAL   B CG1 1 
ATOM   2409 C CG2 . VAL   B 1 49  ? 40.736 -1.418  23.557  1.00 63.55  ? 742  VAL   B CG2 1 
ATOM   2410 N N   . ALA   B 1 50  ? 41.544 -4.456  21.299  1.00 59.50  ? 743  ALA   B N   1 
ATOM   2411 C CA  . ALA   B 1 50  ? 42.039 -4.465  19.936  1.00 58.56  ? 743  ALA   B CA  1 
ATOM   2412 C C   . ALA   B 1 50  ? 41.031 -3.609  19.150  1.00 57.59  ? 743  ALA   B C   1 
ATOM   2413 O O   . ALA   B 1 50  ? 39.819 -3.785  19.288  1.00 57.18  ? 743  ALA   B O   1 
ATOM   2414 C CB  . ALA   B 1 50  ? 42.065 -5.872  19.380  1.00 58.36  ? 743  ALA   B CB  1 
ATOM   2415 N N   . ILE   B 1 51  ? 41.529 -2.637  18.391  1.00 56.95  ? 744  ILE   B N   1 
ATOM   2416 C CA  . ILE   B 1 51  ? 40.685 -1.746  17.613  1.00 56.80  ? 744  ILE   B CA  1 
ATOM   2417 C C   . ILE   B 1 51  ? 40.926 -1.969  16.134  1.00 56.12  ? 744  ILE   B C   1 
ATOM   2418 O O   . ILE   B 1 51  ? 42.054 -1.809  15.678  1.00 56.25  ? 744  ILE   B O   1 
ATOM   2419 C CB  . ILE   B 1 51  ? 40.974 -0.272  17.990  1.00 57.51  ? 744  ILE   B CB  1 
ATOM   2420 C CG1 . ILE   B 1 51  ? 40.716 -0.015  19.483  1.00 58.45  ? 744  ILE   B CG1 1 
ATOM   2421 C CG2 . ILE   B 1 51  ? 40.172 0.680   17.112  1.00 58.07  ? 744  ILE   B CG2 1 
ATOM   2422 C CD1 . ILE   B 1 51  ? 41.859 0.608   20.202  1.00 59.96  ? 744  ILE   B CD1 1 
ATOM   2423 N N   . LYS   B 1 52  ? 39.877 -2.309  15.376  1.00 55.26  ? 745  LYS   B N   1 
ATOM   2424 C CA  . LYS   B 1 52  ? 40.010 -2.452  13.931  1.00 55.17  ? 745  LYS   B CA  1 
ATOM   2425 C C   . LYS   B 1 52  ? 39.465 -1.192  13.272  1.00 55.47  ? 745  LYS   B C   1 
ATOM   2426 O O   . LYS   B 1 52  ? 38.266 -0.959  13.307  1.00 55.00  ? 745  LYS   B O   1 
ATOM   2427 C CB  . LYS   B 1 52  ? 39.262 -3.694  13.431  1.00 56.02  ? 745  LYS   B CB  1 
ATOM   2428 C CG  . LYS   B 1 52  ? 39.559 -4.054  11.984  1.00 58.58  ? 745  LYS   B CG  1 
ATOM   2429 C CD  . LYS   B 1 52  ? 38.931 -5.393  11.650  1.00 61.60  ? 745  LYS   B CD  1 
ATOM   2430 C CE  . LYS   B 1 52  ? 39.667 -6.106  10.562  1.00 64.92  ? 745  LYS   B CE  1 
ATOM   2431 N NZ  . LYS   B 1 52  ? 39.591 -7.575  10.724  1.00 66.96  ? 745  LYS   B NZ  1 
ATOM   2432 N N   . GLU   B 1 53  ? 40.342 -0.356  12.720  1.00 56.53  ? 746  GLU   B N   1 
ATOM   2433 C CA  . GLU   B 1 53  ? 39.926 0.854   12.025  1.00 58.08  ? 746  GLU   B CA  1 
ATOM   2434 C C   . GLU   B 1 53  ? 39.843 0.557   10.533  1.00 59.56  ? 746  GLU   B C   1 
ATOM   2435 O O   . GLU   B 1 53  ? 40.866 0.348   9.896   1.00 59.55  ? 746  GLU   B O   1 
ATOM   2436 C CB  . GLU   B 1 53  ? 40.895 2.005   12.277  1.00 60.62  ? 746  GLU   B CB  1 
ATOM   2437 C CG  . GLU   B 1 53  ? 40.408 3.296   11.639  1.00 67.45  ? 746  GLU   B CG  1 
ATOM   2438 C CD  . GLU   B 1 53  ? 41.067 4.554   12.169  1.00 76.32  ? 746  GLU   B CD  1 
ATOM   2439 O OE1 . GLU   B 1 53  ? 42.272 4.502   12.510  1.00 79.03  ? 746  GLU   B OE1 1 
ATOM   2440 O OE2 . GLU   B 1 53  ? 40.373 5.595   12.242  1.00 79.39  ? 746  GLU   B OE2 1 
ATOM   2441 N N   . LEU   B 1 54  ? 38.630 0.502   9.979   1.00 60.65  ? 747  LEU   B N   1 
ATOM   2442 C CA  . LEU   B 1 54  ? 38.441 0.207   8.558   1.00 61.91  ? 747  LEU   B CA  1 
ATOM   2443 C C   . LEU   B 1 54  ? 38.758 1.431   7.721   1.00 63.56  ? 747  LEU   B C   1 
ATOM   2444 O O   . LEU   B 1 54  ? 38.518 2.553   8.147   1.00 63.96  ? 747  LEU   B O   1 
ATOM   2445 C CB  . LEU   B 1 54  ? 37.024 -0.328  8.288   1.00 61.90  ? 747  LEU   B CB  1 
ATOM   2446 C CG  . LEU   B 1 54  ? 36.593 -1.514  9.184   1.00 63.44  ? 747  LEU   B CG  1 
ATOM   2447 C CD1 . LEU   B 1 54  ? 35.150 -1.919  8.942   1.00 64.00  ? 747  LEU   B CD1 1 
ATOM   2448 C CD2 . LEU   B 1 54  ? 37.505 -2.701  9.015   1.00 63.92  ? 747  LEU   B CD2 1 
ATOM   2449 N N   . ARG   B 1 55  ? 39.405 1.243   6.577   1.00 64.70  ? 748  ARG   B N   1 
ATOM   2450 C CA  . ARG   B 1 55  ? 39.789 2.352   5.694   1.00 66.19  ? 748  ARG   B CA  1 
ATOM   2451 C C   . ARG   B 1 55  ? 38.535 3.133   5.257   1.00 66.03  ? 748  ARG   B C   1 
ATOM   2452 O O   . ARG   B 1 55  ? 37.511 2.508   4.977   1.00 65.59  ? 748  ARG   B O   1 
ATOM   2453 C CB  . ARG   B 1 55  ? 40.517 1.779   4.464   1.00 69.05  ? 748  ARG   B CB  1 
ATOM   2454 C CG  . ARG   B 1 55  ? 41.580 2.694   3.890   1.00 74.33  ? 748  ARG   B CG  1 
ATOM   2455 C CD  . ARG   B 1 55  ? 42.621 1.917   3.085   1.00 79.72  ? 748  ARG   B CD  1 
ATOM   2456 N NE  . ARG   B 1 55  ? 43.531 1.149   3.945   1.00 84.08  ? 748  ARG   B NE  1 
ATOM   2457 C CZ  . ARG   B 1 55  ? 44.603 1.661   4.548   1.00 87.42  ? 748  ARG   B CZ  1 
ATOM   2458 N NH1 . ARG   B 1 55  ? 44.920 2.944   4.384   1.00 87.57  ? 748  ARG   B NH1 1 
ATOM   2459 N NH2 . ARG   B 1 55  ? 45.368 0.897   5.319   1.00 87.07  ? 748  ARG   B NH2 1 
ATOM   2460 N N   . GLU   B 1 56  ? 38.589 4.467   5.241   1.00 66.52  ? 749  GLU   B N   1 
ATOM   2461 C CA  . GLU   B 1 56  ? 37.417 5.260   4.853   1.00 67.22  ? 749  GLU   B CA  1 
ATOM   2462 C C   . GLU   B 1 56  ? 36.832 4.875   3.476   1.00 68.17  ? 749  GLU   B C   1 
ATOM   2463 O O   . GLU   B 1 56  ? 37.577 4.512   2.564   1.00 67.92  ? 749  GLU   B O   1 
ATOM   2464 C CB  . GLU   B 1 56  ? 37.725 6.741   4.929   1.00 68.64  ? 749  GLU   B CB  1 
ATOM   2465 C CG  . GLU   B 1 56  ? 36.506 7.613   4.689   1.00 71.55  ? 749  GLU   B CG  1 
ATOM   2466 C CD  . GLU   B 1 56  ? 36.735 9.106   4.794   1.00 76.54  ? 749  GLU   B CD  1 
ATOM   2467 O OE1 . GLU   B 1 56  ? 37.914 9.511   4.892   1.00 78.54  ? 749  GLU   B OE1 1 
ATOM   2468 O OE2 . GLU   B 1 56  ? 35.747 9.877   4.763   1.00 77.72  ? 749  GLU   B OE2 1 
ATOM   2469 N N   . ALA   B 1 57  ? 35.489 4.904   3.362   1.00 69.05  ? 750  ALA   B N   1 
ATOM   2470 C CA  . ALA   B 1 57  ? 34.722 4.571   2.160   1.00 70.38  ? 750  ALA   B CA  1 
ATOM   2471 C C   . ALA   B 1 57  ? 34.969 3.138   1.647   1.00 71.96  ? 750  ALA   B C   1 
ATOM   2472 O O   . ALA   B 1 57  ? 34.940 2.889   0.442   1.00 72.47  ? 750  ALA   B O   1 
ATOM   2473 C CB  . ALA   B 1 57  ? 34.934 5.601   1.066   1.00 70.27  ? 750  ALA   B CB  1 
ATOM   2474 N N   . THR   B 1 58  ? 35.184 2.196   2.581   1.00 72.60  ? 751  THR   B N   1 
ATOM   2475 C CA  . THR   B 1 58  ? 35.375 0.781   2.252   1.00 73.94  ? 751  THR   B CA  1 
ATOM   2476 C C   . THR   B 1 58  ? 33.988 0.173   1.992   1.00 74.85  ? 751  THR   B C   1 
ATOM   2477 O O   . THR   B 1 58  ? 33.784 -0.484  0.976   1.00 75.96  ? 751  THR   B O   1 
ATOM   2478 C CB  . THR   B 1 58  ? 36.088 0.035   3.402   1.00 75.66  ? 751  THR   B CB  1 
ATOM   2479 O OG1 . THR   B 1 58  ? 37.350 0.635   3.678   1.00 76.84  ? 751  THR   B OG1 1 
ATOM   2480 C CG2 . THR   B 1 58  ? 36.305 -1.416  3.097   1.00 76.41  ? 751  THR   B CG2 1 
ATOM   2481 N N   . SER   B 1 59  ? 33.023 0.438   2.891   1.00 74.49  ? 752  SER   B N   1 
ATOM   2482 C CA  . SER   B 1 59  ? 31.646 -0.037  2.776   1.00 74.57  ? 752  SER   B CA  1 
ATOM   2483 C C   . SER   B 1 59  ? 30.770 0.988   2.057   1.00 74.45  ? 752  SER   B C   1 
ATOM   2484 O O   . SER   B 1 59  ? 30.849 2.182   2.347   1.00 74.68  ? 752  SER   B O   1 
ATOM   2485 C CB  . SER   B 1 59  ? 31.069 -0.302  4.165   1.00 75.89  ? 752  SER   B CB  1 
ATOM   2486 O OG  . SER   B 1 59  ? 29.670 -0.551  4.143   1.00 78.49  ? 752  SER   B OG  1 
ATOM   2487 N N   . PRO   B 1 60  ? 29.869 0.542   1.178   1.00 73.96  ? 753  PRO   B N   1 
ATOM   2488 C CA  . PRO   B 1 60  ? 28.954 1.492   0.526   1.00 73.82  ? 753  PRO   B CA  1 
ATOM   2489 C C   . PRO   B 1 60  ? 27.752 1.940   1.375   1.00 73.98  ? 753  PRO   B C   1 
ATOM   2490 O O   . PRO   B 1 60  ? 26.997 2.820   0.966   1.00 74.42  ? 753  PRO   B O   1 
ATOM   2491 C CB  . PRO   B 1 60  ? 28.502 0.734   -0.716  1.00 74.48  ? 753  PRO   B CB  1 
ATOM   2492 C CG  . PRO   B 1 60  ? 28.588 -0.704  -0.338  1.00 74.83  ? 753  PRO   B CG  1 
ATOM   2493 C CD  . PRO   B 1 60  ? 29.629 -0.846  0.737   1.00 73.27  ? 753  PRO   B CD  1 
ATOM   2494 N N   . LYS   B 1 61  ? 27.568 1.341   2.551   1.00 73.56  ? 754  LYS   B N   1 
ATOM   2495 C CA  . LYS   B 1 61  ? 26.451 1.637   3.445   1.00 73.42  ? 754  LYS   B CA  1 
ATOM   2496 C C   . LYS   B 1 61  ? 26.587 2.953   4.187   1.00 73.70  ? 754  LYS   B C   1 
ATOM   2497 O O   . LYS   B 1 61  ? 27.680 3.310   4.622   1.00 73.71  ? 754  LYS   B O   1 
ATOM   2498 C CB  . LYS   B 1 61  ? 26.332 0.528   4.502   1.00 73.93  ? 754  LYS   B CB  1 
ATOM   2499 C CG  . LYS   B 1 61  ? 26.071 -0.859  3.965   1.00 76.72  ? 754  LYS   B CG  1 
ATOM   2500 C CD  . LYS   B 1 61  ? 25.895 -1.833  5.085   1.00 79.85  ? 754  LYS   B CD  1 
ATOM   2501 C CE  . LYS   B 1 61  ? 25.626 -3.227  4.578   1.00 82.49  ? 754  LYS   B CE  1 
ATOM   2502 N NZ  . LYS   B 1 61  ? 24.300 -3.335  3.921   1.00 84.34  ? 754  LYS   B NZ  1 
ATOM   2503 N N   . ALA   B 1 62  ? 25.459 3.622   4.437   1.00 73.59  ? 755  ALA   B N   1 
ATOM   2504 C CA  . ALA   B 1 62  ? 25.458 4.828   5.272   1.00 73.87  ? 755  ALA   B CA  1 
ATOM   2505 C C   . ALA   B 1 62  ? 25.631 4.411   6.757   1.00 73.73  ? 755  ALA   B C   1 
ATOM   2506 O O   . ALA   B 1 62  ? 25.426 3.243   7.096   1.00 74.09  ? 755  ALA   B O   1 
ATOM   2507 C CB  . ALA   B 1 62  ? 24.149 5.588   5.095   1.00 74.13  ? 755  ALA   B CB  1 
ATOM   2508 N N   . ASN   B 1 63  ? 26.006 5.354   7.637   1.00 73.08  ? 756  ASN   B N   1 
ATOM   2509 C CA  . ASN   B 1 63  ? 26.229 5.070   9.056   1.00 72.67  ? 756  ASN   B CA  1 
ATOM   2510 C C   . ASN   B 1 63  ? 25.053 4.378   9.760   1.00 72.75  ? 756  ASN   B C   1 
ATOM   2511 O O   . ASN   B 1 63  ? 25.282 3.540   10.636  1.00 72.47  ? 756  ASN   B O   1 
ATOM   2512 C CB  . ASN   B 1 63  ? 26.645 6.327   9.804   1.00 73.00  ? 756  ASN   B CB  1 
ATOM   2513 C CG  . ASN   B 1 63  ? 28.112 6.673   9.723   1.00 74.66  ? 756  ASN   B CG  1 
ATOM   2514 O OD1 . ASN   B 1 63  ? 28.538 7.695   10.264  1.00 76.44  ? 756  ASN   B OD1 1 
ATOM   2515 N ND2 . ASN   B 1 63  ? 28.920 5.852   9.061   1.00 73.63  ? 756  ASN   B ND2 1 
ATOM   2516 N N   . LYS   B 1 64  ? 23.809 4.684   9.353   1.00 72.77  ? 757  LYS   B N   1 
ATOM   2517 C CA  . LYS   B 1 64  ? 22.629 4.048   9.935   1.00 73.03  ? 757  LYS   B CA  1 
ATOM   2518 C C   . LYS   B 1 64  ? 22.591 2.556   9.607   1.00 72.30  ? 757  LYS   B C   1 
ATOM   2519 O O   . LYS   B 1 64  ? 22.366 1.750   10.505  1.00 72.72  ? 757  LYS   B O   1 
ATOM   2520 C CB  . LYS   B 1 64  ? 21.342 4.749   9.467   1.00 75.68  ? 757  LYS   B CB  1 
ATOM   2521 C CG  . LYS   B 1 64  ? 20.070 4.135   10.050  1.00 80.13  ? 757  LYS   B CG  1 
ATOM   2522 N N   . GLU   B 1 65  ? 22.865 2.180   8.342   1.00 71.31  ? 758  GLU   B N   1 
ATOM   2523 C CA  . GLU   B 1 65  ? 22.883 0.772   7.924   1.00 70.83  ? 758  GLU   B CA  1 
ATOM   2524 C C   . GLU   B 1 65  ? 24.094 0.004   8.486   1.00 70.51  ? 758  GLU   B C   1 
ATOM   2525 O O   . GLU   B 1 65  ? 24.038 -1.220  8.625   1.00 70.41  ? 758  GLU   B O   1 
ATOM   2526 C CB  . GLU   B 1 65  ? 22.818 0.641   6.395   1.00 72.39  ? 758  GLU   B CB  1 
ATOM   2527 N N   . ILE   B 1 66  ? 25.194 0.716   8.771   1.00 70.10  ? 759  ILE   B N   1 
ATOM   2528 C CA  . ILE   B 1 66  ? 26.386 0.136   9.387   1.00 70.09  ? 759  ILE   B CA  1 
ATOM   2529 C C   . ILE   B 1 66  ? 26.020 -0.242  10.832  1.00 70.01  ? 759  ILE   B C   1 
ATOM   2530 O O   . ILE   B 1 66  ? 26.381 -1.323  11.288  1.00 70.26  ? 759  ILE   B O   1 
ATOM   2531 C CB  . ILE   B 1 66  ? 27.560 1.145   9.351   1.00 70.24  ? 759  ILE   B CB  1 
ATOM   2532 C CG1 . ILE   B 1 66  ? 28.110 1.308   7.938   1.00 70.45  ? 759  ILE   B CG1 1 
ATOM   2533 C CG2 . ILE   B 1 66  ? 28.678 0.778   10.341  1.00 70.47  ? 759  ILE   B CG2 1 
ATOM   2534 N N   . LEU   B 1 67  ? 25.277 0.638   11.534  1.00 69.75  ? 760  LEU   B N   1 
ATOM   2535 C CA  . LEU   B 1 67  ? 24.833 0.423   12.904  1.00 70.18  ? 760  LEU   B CA  1 
ATOM   2536 C C   . LEU   B 1 67  ? 23.934 -0.804  13.004  1.00 70.59  ? 760  LEU   B C   1 
ATOM   2537 O O   . LEU   B 1 67  ? 24.100 -1.591  13.932  1.00 70.94  ? 760  LEU   B O   1 
ATOM   2538 C CB  . LEU   B 1 67  ? 24.128 1.671   13.443  1.00 70.48  ? 760  LEU   B CB  1 
ATOM   2539 C CG  . LEU   B 1 67  ? 24.836 2.394   14.584  1.00 72.06  ? 760  LEU   B CG  1 
ATOM   2540 N N   . ASP   B 1 68  ? 23.045 -1.017  12.019  1.00 70.17  ? 761  ASP   B N   1 
ATOM   2541 C CA  . ASP   B 1 68  ? 22.181 -2.197  12.014  1.00 70.29  ? 761  ASP   B CA  1 
ATOM   2542 C C   . ASP   B 1 68  ? 23.003 -3.488  11.943  1.00 69.63  ? 761  ASP   B C   1 
ATOM   2543 O O   . ASP   B 1 68  ? 22.684 -4.441  12.642  1.00 69.71  ? 761  ASP   B O   1 
ATOM   2544 C CB  . ASP   B 1 68  ? 21.188 -2.145  10.845  1.00 72.36  ? 761  ASP   B CB  1 
ATOM   2545 C CG  . ASP   B 1 68  ? 20.325 -0.899  10.819  1.00 78.23  ? 761  ASP   B CG  1 
ATOM   2546 O OD1 . ASP   B 1 68  ? 20.219 -0.226  11.874  1.00 80.03  ? 761  ASP   B OD1 1 
ATOM   2547 O OD2 . ASP   B 1 68  ? 19.761 -0.586  9.739   1.00 79.89  ? 761  ASP   B OD2 1 
ATOM   2548 N N   . GLU   B 1 69  ? 24.057 -3.513  11.113  1.00 68.88  ? 762  GLU   B N   1 
ATOM   2549 C CA  . GLU   B 1 69  ? 24.934 -4.675  10.961  1.00 68.64  ? 762  GLU   B CA  1 
ATOM   2550 C C   . GLU   B 1 69  ? 25.710 -4.921  12.248  1.00 68.56  ? 762  GLU   B C   1 
ATOM   2551 O O   . GLU   B 1 69  ? 25.838 -6.067  12.676  1.00 68.80  ? 762  GLU   B O   1 
ATOM   2552 C CB  . GLU   B 1 69  ? 25.904 -4.487  9.788   1.00 70.24  ? 762  GLU   B CB  1 
ATOM   2553 C CG  . GLU   B 1 69  ? 25.509 -5.236  8.528   1.00 73.96  ? 762  GLU   B CG  1 
ATOM   2554 C CD  . GLU   B 1 69  ? 24.220 -4.798  7.868   1.00 79.42  ? 762  GLU   B CD  1 
ATOM   2555 N N   . ALA   B 1 70  ? 26.191 -3.846  12.890  1.00 68.03  ? 763  ALA   B N   1 
ATOM   2556 C CA  . ALA   B 1 70  ? 26.918 -3.918  14.155  1.00 67.79  ? 763  ALA   B CA  1 
ATOM   2557 C C   . ALA   B 1 70  ? 26.011 -4.420  15.292  1.00 67.19  ? 763  ALA   B C   1 
ATOM   2558 O O   . ALA   B 1 70  ? 26.491 -5.140  16.167  1.00 67.15  ? 763  ALA   B O   1 
ATOM   2559 C CB  . ALA   B 1 70  ? 27.508 -2.557  14.498  1.00 68.04  ? 763  ALA   B CB  1 
ATOM   2560 N N   . TYR   B 1 71  ? 24.700 -4.082  15.253  1.00 66.79  ? 764  TYR   B N   1 
ATOM   2561 C CA  . TYR   B 1 71  ? 23.711 -4.555  16.227  1.00 67.32  ? 764  TYR   B CA  1 
ATOM   2562 C C   . TYR   B 1 71  ? 23.591 -6.075  16.153  1.00 66.30  ? 764  TYR   B C   1 
ATOM   2563 O O   . TYR   B 1 71  ? 23.482 -6.724  17.193  1.00 66.36  ? 764  TYR   B O   1 
ATOM   2564 C CB  . TYR   B 1 71  ? 22.326 -3.925  15.998  1.00 68.53  ? 764  TYR   B CB  1 
ATOM   2565 C CG  . TYR   B 1 71  ? 22.170 -2.538  16.582  1.00 70.92  ? 764  TYR   B CG  1 
ATOM   2566 C CD1 . TYR   B 1 71  ? 22.576 -2.259  17.879  1.00 72.42  ? 764  TYR   B CD1 1 
ATOM   2567 C CD2 . TYR   B 1 71  ? 21.557 -1.521  15.860  1.00 72.37  ? 764  TYR   B CD2 1 
ATOM   2568 C CE1 . TYR   B 1 71  ? 22.445 -0.982  18.417  1.00 73.59  ? 764  TYR   B CE1 1 
ATOM   2569 C CE2 . TYR   B 1 71  ? 21.437 -0.238  16.380  1.00 73.58  ? 764  TYR   B CE2 1 
ATOM   2570 C CZ  . TYR   B 1 71  ? 21.878 0.027   17.664  1.00 74.92  ? 764  TYR   B CZ  1 
ATOM   2571 O OH  . TYR   B 1 71  ? 21.733 1.288   18.200  1.00 77.51  ? 764  TYR   B OH  1 
ATOM   2572 N N   . VAL   B 1 72  ? 23.632 -6.639  14.926  1.00 65.31  ? 765  VAL   B N   1 
ATOM   2573 C CA  . VAL   B 1 72  ? 23.592 -8.079  14.677  1.00 65.03  ? 765  VAL   B CA  1 
ATOM   2574 C C   . VAL   B 1 72  ? 24.869 -8.749  15.192  1.00 64.79  ? 765  VAL   B C   1 
ATOM   2575 O O   . VAL   B 1 72  ? 24.773 -9.758  15.885  1.00 65.39  ? 765  VAL   B O   1 
ATOM   2576 C CB  . VAL   B 1 72  ? 23.332 -8.394  13.182  1.00 65.28  ? 765  VAL   B CB  1 
ATOM   2577 C CG1 . VAL   B 1 72  ? 23.477 -9.885  12.894  1.00 65.45  ? 765  VAL   B CG1 1 
ATOM   2578 C CG2 . VAL   B 1 72  ? 21.962 -7.881  12.746  1.00 65.23  ? 765  VAL   B CG2 1 
ATOM   2579 N N   . MET   B 1 73  ? 26.051 -8.166  14.924  1.00 64.10  ? 766  MET   B N   1 
ATOM   2580 C CA  . MET   B 1 73  ? 27.321 -8.715  15.418  1.00 64.30  ? 766  MET   B CA  1 
ATOM   2581 C C   . MET   B 1 73  ? 27.333 -8.746  16.945  1.00 63.73  ? 766  MET   B C   1 
ATOM   2582 O O   . MET   B 1 73  ? 27.863 -9.689  17.528  1.00 64.10  ? 766  MET   B O   1 
ATOM   2583 C CB  . MET   B 1 73  ? 28.531 -7.893  14.937  1.00 65.66  ? 766  MET   B CB  1 
ATOM   2584 C CG  . MET   B 1 73  ? 28.743 -7.859  13.442  1.00 68.92  ? 766  MET   B CG  1 
ATOM   2585 S SD  . MET   B 1 73  ? 30.173 -6.795  13.036  1.00 76.30  ? 766  MET   B SD  1 
ATOM   2586 N N   . ALA   B 1 74  ? 26.753 -7.718  17.592  1.00 62.81  ? 767  ALA   B N   1 
ATOM   2587 C CA  . ALA   B 1 74  ? 26.690 -7.618  19.051  1.00 62.19  ? 767  ALA   B CA  1 
ATOM   2588 C C   . ALA   B 1 74  ? 25.653 -8.572  19.672  1.00 61.47  ? 767  ALA   B C   1 
ATOM   2589 O O   . ALA   B 1 74  ? 25.845 -9.032  20.797  1.00 62.43  ? 767  ALA   B O   1 
ATOM   2590 C CB  . ALA   B 1 74  ? 26.405 -6.183  19.468  1.00 62.13  ? 767  ALA   B CB  1 
ATOM   2591 N N   . SER   B 1 75  ? 24.574 -8.880  18.944  1.00 59.79  ? 768  SER   B N   1 
ATOM   2592 C CA  . SER   B 1 75  ? 23.524 -9.791  19.415  1.00 58.75  ? 768  SER   B CA  1 
ATOM   2593 C C   . SER   B 1 75  ? 24.016 -11.236 19.641  1.00 57.27  ? 768  SER   B C   1 
ATOM   2594 O O   . SER   B 1 75  ? 23.441 -11.965 20.449  1.00 56.85  ? 768  SER   B O   1 
ATOM   2595 C CB  . SER   B 1 75  ? 22.350 -9.788  18.443  1.00 59.83  ? 768  SER   B CB  1 
ATOM   2596 O OG  . SER   B 1 75  ? 22.677 -10.439 17.227  1.00 61.90  ? 768  SER   B OG  1 
ATOM   2597 N N   . VAL   B 1 76  ? 25.086 -11.623 18.931  1.00 56.62  ? 769  VAL   B N   1 
ATOM   2598 C CA  . VAL   B 1 76  ? 25.765 -12.914 18.999  1.00 56.53  ? 769  VAL   B CA  1 
ATOM   2599 C C   . VAL   B 1 76  ? 26.234 -13.221 20.441  1.00 56.78  ? 769  VAL   B C   1 
ATOM   2600 O O   . VAL   B 1 76  ? 26.282 -14.380 20.827  1.00 57.38  ? 769  VAL   B O   1 
ATOM   2601 C CB  . VAL   B 1 76  ? 26.912 -12.918 17.952  1.00 57.12  ? 769  VAL   B CB  1 
ATOM   2602 C CG1 . VAL   B 1 76  ? 27.812 -14.132 18.076  1.00 57.57  ? 769  VAL   B CG1 1 
ATOM   2603 C CG2 . VAL   B 1 76  ? 26.352 -12.806 16.542  1.00 57.75  ? 769  VAL   B CG2 1 
ATOM   2604 N N   . ASP   B 1 77  ? 26.502 -12.189 21.263  1.00 56.35  ? 770  ASP   B N   1 
ATOM   2605 C CA  . ASP   B 1 77  ? 26.865 -12.358 22.675  1.00 56.08  ? 770  ASP   B CA  1 
ATOM   2606 C C   . ASP   B 1 77  ? 25.742 -12.993 23.511  1.00 54.97  ? 770  ASP   B C   1 
ATOM   2607 O O   . ASP   B 1 77  ? 25.999 -13.400 24.643  1.00 55.48  ? 770  ASP   B O   1 
ATOM   2608 C CB  . ASP   B 1 77  ? 27.233 -11.000 23.305  1.00 58.47  ? 770  ASP   B CB  1 
ATOM   2609 C CG  . ASP   B 1 77  ? 28.499 -10.382 22.750  1.00 64.04  ? 770  ASP   B CG  1 
ATOM   2610 N N   . ASN   B 1 78  ? 24.517 -13.101 22.972  1.00 53.32  ? 771  ASN   B N   1 
ATOM   2611 C CA  . ASN   B 1 78  ? 23.400 -13.678 23.703  1.00 52.25  ? 771  ASN   B CA  1 
ATOM   2612 C C   . ASN   B 1 78  ? 22.769 -14.863 22.939  1.00 51.00  ? 771  ASN   B C   1 
ATOM   2613 O O   . ASN   B 1 78  ? 22.264 -14.680 21.832  1.00 51.04  ? 771  ASN   B O   1 
ATOM   2614 C CB  . ASN   B 1 78  ? 22.373 -12.590 23.971  1.00 53.77  ? 771  ASN   B CB  1 
ATOM   2615 C CG  . ASN   B 1 78  ? 21.165 -13.050 24.757  1.00 57.26  ? 771  ASN   B CG  1 
ATOM   2616 O OD1 . ASN   B 1 78  ? 21.213 -13.997 25.537  1.00 57.25  ? 771  ASN   B OD1 1 
ATOM   2617 N ND2 . ASN   B 1 78  ? 20.040 -12.386 24.562  1.00 59.36  ? 771  ASN   B ND2 1 
ATOM   2618 N N   . PRO   B 1 79  ? 22.784 -16.095 23.498  1.00 49.64  ? 772  PRO   B N   1 
ATOM   2619 C CA  . PRO   B 1 79  ? 23.349 -16.501 24.801  1.00 48.35  ? 772  PRO   B CA  1 
ATOM   2620 C C   . PRO   B 1 79  ? 24.878 -16.589 24.860  1.00 47.46  ? 772  PRO   B C   1 
ATOM   2621 O O   . PRO   B 1 79  ? 25.454 -16.593 25.937  1.00 48.13  ? 772  PRO   B O   1 
ATOM   2622 C CB  . PRO   B 1 79  ? 22.661 -17.842 25.063  1.00 48.94  ? 772  PRO   B CB  1 
ATOM   2623 C CG  . PRO   B 1 79  ? 22.469 -18.417 23.699  1.00 49.69  ? 772  PRO   B CG  1 
ATOM   2624 C CD  . PRO   B 1 79  ? 22.173 -17.243 22.797  1.00 48.74  ? 772  PRO   B CD  1 
ATOM   2625 N N   A GLY   B 1 80  ? 25.516 -16.668 23.704  0.50 46.87  ? 773  GLY   B N   1 
ATOM   2626 N N   B GLY   B 1 80  ? 25.516 -16.668 23.704  0.50 46.87  ? 773  GLY   B N   1 
ATOM   2627 C CA  A GLY   B 1 80  ? 26.968 -16.686 23.616  0.50 46.55  ? 773  GLY   B CA  1 
ATOM   2628 C CA  B GLY   B 1 80  ? 26.968 -16.686 23.616  0.50 46.55  ? 773  GLY   B CA  1 
ATOM   2629 C C   A GLY   B 1 80  ? 27.613 -18.044 23.447  0.50 45.72  ? 773  GLY   B C   1 
ATOM   2630 C C   B GLY   B 1 80  ? 27.613 -18.044 23.447  0.50 45.72  ? 773  GLY   B C   1 
ATOM   2631 O O   A GLY   B 1 80  ? 26.967 -19.086 23.592  0.50 46.07  ? 773  GLY   B O   1 
ATOM   2632 O O   B GLY   B 1 80  ? 26.967 -19.086 23.592  0.50 46.07  ? 773  GLY   B O   1 
ATOM   2633 N N   . ASN   B 1 81  ? 28.904 -18.024 23.124  1.00 44.29  ? 774  ASN   B N   1 
ATOM   2634 C CA  . ASN   B 1 81  ? 29.707 -19.213 22.964  1.00 42.50  ? 774  ASN   B CA  1 
ATOM   2635 C C   . ASN   B 1 81  ? 31.147 -18.806 23.237  1.00 41.29  ? 774  ASN   B C   1 
ATOM   2636 O O   . ASN   B 1 81  ? 31.602 -17.789 22.716  1.00 41.10  ? 774  ASN   B O   1 
ATOM   2637 C CB  . ASN   B 1 81  ? 29.603 -19.740 21.559  1.00 42.64  ? 774  ASN   B CB  1 
ATOM   2638 C CG  . ASN   B 1 81  ? 30.173 -21.105 21.393  1.00 43.30  ? 774  ASN   B CG  1 
ATOM   2639 O OD1 . ASN   B 1 81  ? 29.482 -22.105 21.579  1.00 44.52  ? 774  ASN   B OD1 1 
ATOM   2640 N ND2 . ASN   B 1 81  ? 31.439 -21.180 21.036  1.00 42.77  ? 774  ASN   B ND2 1 
ATOM   2641 N N   . PRO   B 1 82  ? 31.899 -19.603 24.013  1.00 40.11  ? 775  PRO   B N   1 
ATOM   2642 C CA  . PRO   B 1 82  ? 33.289 -19.222 24.313  1.00 39.48  ? 775  PRO   B CA  1 
ATOM   2643 C C   . PRO   B 1 82  ? 34.214 -19.139 23.113  1.00 39.37  ? 775  PRO   B C   1 
ATOM   2644 O O   . PRO   B 1 82  ? 35.271 -18.546 23.225  1.00 39.26  ? 775  PRO   B O   1 
ATOM   2645 C CB  . PRO   B 1 82  ? 33.768 -20.277 25.314  1.00 40.15  ? 775  PRO   B CB  1 
ATOM   2646 C CG  . PRO   B 1 82  ? 32.745 -21.353 25.309  1.00 40.70  ? 775  PRO   B CG  1 
ATOM   2647 C CD  . PRO   B 1 82  ? 31.481 -20.816 24.738  1.00 39.65  ? 775  PRO   B CD  1 
ATOM   2648 N N   . HIS   B 1 83  ? 33.828 -19.723 21.972  1.00 39.35  ? 776  HIS   B N   1 
ATOM   2649 C CA  . HIS   B 1 83  ? 34.690 -19.747 20.794  1.00 39.21  ? 776  HIS   B CA  1 
ATOM   2650 C C   . HIS   B 1 83  ? 34.268 -18.777 19.700  1.00 39.69  ? 776  HIS   B C   1 
ATOM   2651 O O   . HIS   B 1 83  ? 34.638 -18.939 18.555  1.00 38.88  ? 776  HIS   B O   1 
ATOM   2652 C CB  . HIS   B 1 83  ? 34.823 -21.172 20.277  1.00 38.83  ? 776  HIS   B CB  1 
ATOM   2653 C CG  . HIS   B 1 83  ? 35.290 -22.077 21.364  1.00 39.53  ? 776  HIS   B CG  1 
ATOM   2654 N ND1 . HIS   B 1 83  ? 34.452 -23.034 21.909  1.00 41.34  ? 776  HIS   B ND1 1 
ATOM   2655 C CD2 . HIS   B 1 83  ? 36.426 -22.021 22.092  1.00 39.55  ? 776  HIS   B CD2 1 
ATOM   2656 C CE1 . HIS   B 1 83  ? 35.135 -23.583 22.896  1.00 41.15  ? 776  HIS   B CE1 1 
ATOM   2657 N NE2 . HIS   B 1 83  ? 36.324 -22.998 23.051  1.00 40.94  ? 776  HIS   B NE2 1 
ATOM   2658 N N   . VAL   B 1 84  ? 33.588 -17.720 20.079  1.00 40.93  ? 777  VAL   B N   1 
ATOM   2659 C CA  . VAL   B 1 84  ? 33.147 -16.669 19.188  1.00 42.70  ? 777  VAL   B CA  1 
ATOM   2660 C C   . VAL   B 1 84  ? 33.504 -15.337 19.876  1.00 44.32  ? 777  VAL   B C   1 
ATOM   2661 O O   . VAL   B 1 84  ? 33.227 -15.171 21.058  1.00 44.63  ? 777  VAL   B O   1 
ATOM   2662 C CB  . VAL   B 1 84  ? 31.629 -16.829 18.927  1.00 43.21  ? 777  VAL   B CB  1 
ATOM   2663 C CG1 . VAL   B 1 84  ? 31.013 -15.550 18.443  1.00 43.93  ? 777  VAL   B CG1 1 
ATOM   2664 C CG2 . VAL   B 1 84  ? 31.352 -17.959 17.938  1.00 43.35  ? 777  VAL   B CG2 1 
ATOM   2665 N N   . CYS   B 1 85  ? 34.167 -14.420 19.161  1.00 45.53  ? 778  CYS   B N   1 
ATOM   2666 C CA  . CYS   B 1 85  ? 34.532 -13.119 19.726  1.00 47.50  ? 778  CYS   B CA  1 
ATOM   2667 C C   . CYS   B 1 85  ? 33.315 -12.266 20.077  1.00 48.63  ? 778  CYS   B C   1 
ATOM   2668 O O   . CYS   B 1 85  ? 32.197 -12.545 19.650  1.00 47.72  ? 778  CYS   B O   1 
ATOM   2669 C CB  . CYS   B 1 85  ? 35.517 -12.367 18.834  1.00 48.80  ? 778  CYS   B CB  1 
ATOM   2670 S SG  . CYS   B 1 85  ? 37.194 -13.046 18.864  1.00 56.17  ? 778  CYS   B SG  1 
ATOM   2671 N N   . ARG   B 1 86  ? 33.539 -11.243 20.897  1.00 50.27  ? 779  ARG   B N   1 
ATOM   2672 C CA  . ARG   B 1 86  ? 32.484 -10.379 21.380  1.00 52.02  ? 779  ARG   B CA  1 
ATOM   2673 C C   . ARG   B 1 86  ? 32.797 -8.945  20.998  1.00 52.84  ? 779  ARG   B C   1 
ATOM   2674 O O   . ARG   B 1 86  ? 33.839 -8.409  21.400  1.00 53.32  ? 779  ARG   B O   1 
ATOM   2675 C CB  . ARG   B 1 86  ? 32.372 -10.574 22.902  1.00 54.63  ? 779  ARG   B CB  1 
ATOM   2676 C CG  . ARG   B 1 86  ? 31.625 -9.517  23.681  1.00 61.05  ? 779  ARG   B CG  1 
ATOM   2677 C CD  . ARG   B 1 86  ? 31.600 -9.901  25.153  1.00 67.72  ? 779  ARG   B CD  1 
ATOM   2678 N NE  . ARG   B 1 86  ? 31.383 -8.739  26.019  1.00 73.92  ? 779  ARG   B NE  1 
ATOM   2679 C CZ  . ARG   B 1 86  ? 30.188 -8.318  26.423  1.00 78.43  ? 779  ARG   B CZ  1 
ATOM   2680 N NH1 . ARG   B 1 86  ? 29.086 -8.963  26.051  1.00 79.31  ? 779  ARG   B NH1 1 
ATOM   2681 N NH2 . ARG   B 1 86  ? 30.085 -7.252  27.206  1.00 78.61  ? 779  ARG   B NH2 1 
ATOM   2682 N N   . LEU   B 1 87  ? 31.922 -8.337  20.174  1.00 52.66  ? 780  LEU   B N   1 
ATOM   2683 C CA  . LEU   B 1 87  ? 32.082 -6.947  19.778  1.00 52.61  ? 780  LEU   B CA  1 
ATOM   2684 C C   . LEU   B 1 87  ? 31.703 -6.113  20.985  1.00 54.01  ? 780  LEU   B C   1 
ATOM   2685 O O   . LEU   B 1 87  ? 30.558 -6.173  21.434  1.00 54.56  ? 780  LEU   B O   1 
ATOM   2686 C CB  . LEU   B 1 87  ? 31.183 -6.580  18.588  1.00 51.89  ? 780  LEU   B CB  1 
ATOM   2687 C CG  . LEU   B 1 87  ? 31.430 -5.164  18.044  1.00 52.39  ? 780  LEU   B CG  1 
ATOM   2688 C CD1 . LEU   B 1 87  ? 32.819 -5.045  17.392  1.00 52.26  ? 780  LEU   B CD1 1 
ATOM   2689 C CD2 . LEU   B 1 87  ? 30.321 -4.726  17.101  1.00 52.55  ? 780  LEU   B CD2 1 
ATOM   2690 N N   . LEU   B 1 88  ? 32.675 -5.403  21.560  1.00 54.38  ? 781  LEU   B N   1 
ATOM   2691 C CA  . LEU   B 1 88  ? 32.440 -4.566  22.726  1.00 55.56  ? 781  LEU   B CA  1 
ATOM   2692 C C   . LEU   B 1 88  ? 31.813 -3.246  22.336  1.00 56.79  ? 781  LEU   B C   1 
ATOM   2693 O O   . LEU   B 1 88  ? 30.928 -2.753  23.040  1.00 57.50  ? 781  LEU   B O   1 
ATOM   2694 C CB  . LEU   B 1 88  ? 33.745 -4.303  23.499  1.00 55.78  ? 781  LEU   B CB  1 
ATOM   2695 C CG  . LEU   B 1 88  ? 34.466 -5.518  24.069  1.00 57.02  ? 781  LEU   B CG  1 
ATOM   2696 C CD1 . LEU   B 1 88  ? 35.686 -5.086  24.846  1.00 57.69  ? 781  LEU   B CD1 1 
ATOM   2697 C CD2 . LEU   B 1 88  ? 33.551 -6.337  24.962  1.00 57.50  ? 781  LEU   B CD2 1 
ATOM   2698 N N   . GLY   B 1 89  ? 32.295 -2.660  21.246  1.00 56.60  ? 782  GLY   B N   1 
ATOM   2699 C CA  . GLY   B 1 89  ? 31.766 -1.394  20.797  1.00 56.93  ? 782  GLY   B CA  1 
ATOM   2700 C C   . GLY   B 1 89  ? 32.111 -1.012  19.384  1.00 57.23  ? 782  GLY   B C   1 
ATOM   2701 O O   . GLY   B 1 89  ? 32.915 -1.659  18.716  1.00 56.69  ? 782  GLY   B O   1 
ATOM   2702 N N   . ILE   B 1 90  ? 31.491 0.063   18.936  1.00 57.95  ? 783  ILE   B N   1 
ATOM   2703 C CA  . ILE   B 1 90  ? 31.741 0.613   17.621  1.00 59.31  ? 783  ILE   B CA  1 
ATOM   2704 C C   . ILE   B 1 90  ? 31.873 2.120   17.728  1.00 60.29  ? 783  ILE   B C   1 
ATOM   2705 O O   . ILE   B 1 90  ? 31.126 2.761   18.461  1.00 59.83  ? 783  ILE   B O   1 
ATOM   2706 C CB  . ILE   B 1 90  ? 30.674 0.181   16.579  1.00 59.85  ? 783  ILE   B CB  1 
ATOM   2707 C CG1 . ILE   B 1 90  ? 31.038 0.672   15.158  1.00 60.72  ? 783  ILE   B CG1 1 
ATOM   2708 C CG2 . ILE   B 1 90  ? 29.263 0.630   16.989  1.00 60.22  ? 783  ILE   B CG2 1 
ATOM   2709 N N   . CYS   B 1 91  ? 32.862 2.683   17.043  1.00 61.71  ? 784  CYS   B N   1 
ATOM   2710 C CA  . CYS   B 1 91  ? 33.036 4.122   16.999  1.00 63.35  ? 784  CYS   B CA  1 
ATOM   2711 C C   . CYS   B 1 91  ? 32.905 4.573   15.553  1.00 64.73  ? 784  CYS   B C   1 
ATOM   2712 O O   . CYS   B 1 91  ? 33.759 4.249   14.733  1.00 64.72  ? 784  CYS   B O   1 
ATOM   2713 C CB  . CYS   B 1 91  ? 34.369 4.542   17.602  1.00 64.41  ? 784  CYS   B CB  1 
ATOM   2714 S SG  . CYS   B 1 91  ? 34.598 6.334   17.685  1.00 69.68  ? 784  CYS   B SG  1 
ATOM   2715 N N   . LEU   B 1 92  ? 31.825 5.295   15.231  1.00 65.89  ? 785  LEU   B N   1 
ATOM   2716 C CA  . LEU   B 1 92  ? 31.609 5.767   13.873  1.00 67.02  ? 785  LEU   B CA  1 
ATOM   2717 C C   . LEU   B 1 92  ? 31.910 7.229   13.680  1.00 68.41  ? 785  LEU   B C   1 
ATOM   2718 O O   . LEU   B 1 92  ? 31.149 8.088   14.124  1.00 69.50  ? 785  LEU   B O   1 
ATOM   2719 C CB  . LEU   B 1 92  ? 30.176 5.497   13.386  1.00 67.26  ? 785  LEU   B CB  1 
ATOM   2720 C CG  . LEU   B 1 92  ? 29.767 4.075   13.031  1.00 68.96  ? 785  LEU   B CG  1 
ATOM   2721 C CD1 . LEU   B 1 92  ? 28.498 4.091   12.218  1.00 69.52  ? 785  LEU   B CD1 1 
ATOM   2722 C CD2 . LEU   B 1 92  ? 30.814 3.351   12.208  1.00 69.95  ? 785  LEU   B CD2 1 
ATOM   2723 N N   . THR   B 1 93  ? 32.997 7.523   12.974  1.00 68.36  ? 786  THR   B N   1 
ATOM   2724 C CA  . THR   B 1 93  ? 33.342 8.878   12.552  1.00 68.87  ? 786  THR   B CA  1 
ATOM   2725 C C   . THR   B 1 93  ? 33.380 8.739   10.988  1.00 68.47  ? 786  THR   B C   1 
ATOM   2726 O O   . THR   B 1 93  ? 32.493 8.066   10.447  1.00 68.67  ? 786  THR   B O   1 
ATOM   2727 C CB  . THR   B 1 93  ? 34.606 9.369   13.297  1.00 70.75  ? 786  THR   B CB  1 
ATOM   2728 O OG1 . THR   B 1 93  ? 35.715 8.564   12.890  1.00 72.25  ? 786  THR   B OG1 1 
ATOM   2729 C CG2 . THR   B 1 93  ? 34.450 9.331   14.817  1.00 70.99  ? 786  THR   B CG2 1 
ATOM   2730 N N   . SER   B 1 94  ? 34.357 9.320   10.255  1.00 67.48  ? 787  SER   B N   1 
ATOM   2731 C CA  . SER   B 1 94  ? 34.467 9.057   8.810   1.00 66.44  ? 787  SER   B CA  1 
ATOM   2732 C C   . SER   B 1 94  ? 34.890 7.596   8.542   1.00 64.83  ? 787  SER   B C   1 
ATOM   2733 O O   . SER   B 1 94  ? 34.646 7.067   7.458   1.00 65.28  ? 787  SER   B O   1 
ATOM   2734 C CB  . SER   B 1 94  ? 35.441 10.019  8.162   1.00 67.61  ? 787  SER   B CB  1 
ATOM   2735 O OG  . SER   B 1 94  ? 34.910 11.329  8.306   1.00 69.65  ? 787  SER   B OG  1 
ATOM   2736 N N   . THR   B 1 95  ? 35.506 6.941   9.534   1.00 63.03  ? 788  THR   B N   1 
ATOM   2737 C CA  . THR   B 1 95  ? 35.878 5.528   9.469   1.00 62.03  ? 788  THR   B CA  1 
ATOM   2738 C C   . THR   B 1 95  ? 35.065 4.695   10.497  1.00 60.18  ? 788  THR   B C   1 
ATOM   2739 O O   . THR   B 1 95  ? 34.511 5.229   11.448  1.00 59.63  ? 788  THR   B O   1 
ATOM   2740 C CB  . THR   B 1 95  ? 37.393 5.342   9.720   1.00 63.40  ? 788  THR   B CB  1 
ATOM   2741 O OG1 . THR   B 1 95  ? 37.683 5.572   11.107  1.00 63.84  ? 788  THR   B OG1 1 
ATOM   2742 C CG2 . THR   B 1 95  ? 38.254 6.244   8.826   1.00 64.01  ? 788  THR   B CG2 1 
ATOM   2743 N N   . VAL   B 1 96  ? 35.015 3.394   10.297  1.00 59.48  ? 789  VAL   B N   1 
ATOM   2744 C CA  . VAL   B 1 96  ? 34.368 2.485   11.220  1.00 58.90  ? 789  VAL   B CA  1 
ATOM   2745 C C   . VAL   B 1 96  ? 35.454 1.954   12.131  1.00 57.73  ? 789  VAL   B C   1 
ATOM   2746 O O   . VAL   B 1 96  ? 36.492 1.516   11.641  1.00 58.06  ? 789  VAL   B O   1 
ATOM   2747 C CB  . VAL   B 1 96  ? 33.703 1.328   10.449  1.00 59.64  ? 789  VAL   B CB  1 
ATOM   2748 C CG1 . VAL   B 1 96  ? 33.045 0.343   11.403  1.00 59.93  ? 789  VAL   B CG1 1 
ATOM   2749 C CG2 . VAL   B 1 96  ? 32.708 1.864   9.419   1.00 60.27  ? 789  VAL   B CG2 1 
ATOM   2750 N N   . GLN   B 1 97  ? 35.245 2.012   13.446  1.00 56.36  ? 790  GLN   B N   1 
ATOM   2751 C CA  . GLN   B 1 97  ? 36.193 1.438   14.393  1.00 55.53  ? 790  GLN   B CA  1 
ATOM   2752 C C   . GLN   B 1 97  ? 35.480 0.370   15.188  1.00 53.69  ? 790  GLN   B C   1 
ATOM   2753 O O   . GLN   B 1 97  ? 34.421 0.631   15.733  1.00 53.28  ? 790  GLN   B O   1 
ATOM   2754 C CB  . GLN   B 1 97  ? 36.817 2.502   15.289  1.00 57.52  ? 790  GLN   B CB  1 
ATOM   2755 C CG  . GLN   B 1 97  ? 37.904 3.256   14.560  1.00 61.80  ? 790  GLN   B CG  1 
ATOM   2756 C CD  . GLN   B 1 97  ? 38.573 4.270   15.443  1.00 68.07  ? 790  GLN   B CD  1 
ATOM   2757 O OE1 . GLN   B 1 97  ? 39.678 4.042   15.959  1.00 70.92  ? 790  GLN   B OE1 1 
ATOM   2758 N NE2 . GLN   B 1 97  ? 37.923 5.420   15.628  1.00 68.63  ? 790  GLN   B NE2 1 
ATOM   2759 N N   . LEU   B 1 98  ? 35.989 -0.859  15.154  1.00 52.75  ? 791  LEU   B N   1 
ATOM   2760 C CA  . LEU   B 1 98  ? 35.385 -1.967  15.874  1.00 52.49  ? 791  LEU   B CA  1 
ATOM   2761 C C   . LEU   B 1 98  ? 36.266 -2.283  17.075  1.00 52.04  ? 791  LEU   B C   1 
ATOM   2762 O O   . LEU   B 1 98  ? 37.484 -2.384  16.933  1.00 51.89  ? 791  LEU   B O   1 
ATOM   2763 C CB  . LEU   B 1 98  ? 35.234 -3.189  14.957  1.00 52.82  ? 791  LEU   B CB  1 
ATOM   2764 C CG  . LEU   B 1 98  ? 34.448 -2.944  13.666  1.00 54.59  ? 791  LEU   B CG  1 
ATOM   2765 C CD1 . LEU   B 1 98  ? 34.485 -4.174  12.757  1.00 54.94  ? 791  LEU   B CD1 1 
ATOM   2766 C CD2 . LEU   B 1 98  ? 33.000 -2.553  13.976  1.00 55.26  ? 791  LEU   B CD2 1 
ATOM   2767 N N   . ILE   B 1 99  ? 35.667 -2.379  18.256  1.00 51.89  ? 792  ILE   B N   1 
ATOM   2768 C CA  . ILE   B 1 99  ? 36.424 -2.619  19.485  1.00 52.78  ? 792  ILE   B CA  1 
ATOM   2769 C C   . ILE   B 1 99  ? 36.125 -3.987  20.094  1.00 53.34  ? 792  ILE   B C   1 
ATOM   2770 O O   . ILE   B 1 99  ? 34.962 -4.327  20.254  1.00 53.89  ? 792  ILE   B O   1 
ATOM   2771 C CB  . ILE   B 1 99  ? 36.149 -1.478  20.506  1.00 53.40  ? 792  ILE   B CB  1 
ATOM   2772 C CG1 . ILE   B 1 99  ? 36.645 -0.116  19.987  1.00 53.85  ? 792  ILE   B CG1 1 
ATOM   2773 C CG2 . ILE   B 1 99  ? 36.754 -1.792  21.884  1.00 54.22  ? 792  ILE   B CG2 1 
ATOM   2774 C CD1 . ILE   B 1 99  ? 35.600 0.720   19.238  1.00 54.91  ? 792  ILE   B CD1 1 
ATOM   2775 N N   . THR   B 1 100 ? 37.159 -4.775  20.427  1.00 53.17  ? 793  THR   B N   1 
ATOM   2776 C CA  . THR   B 1 100 ? 37.000 -6.070  21.099  1.00 53.84  ? 793  THR   B CA  1 
ATOM   2777 C C   . THR   B 1 100 ? 38.066 -6.265  22.157  1.00 54.46  ? 793  THR   B C   1 
ATOM   2778 O O   . THR   B 1 100 ? 39.104 -5.642  22.086  1.00 54.28  ? 793  THR   B O   1 
ATOM   2779 C CB  . THR   B 1 100 ? 37.092 -7.260  20.120  1.00 55.45  ? 793  THR   B CB  1 
ATOM   2780 O OG1 . THR   B 1 100 ? 38.367 -7.285  19.471  1.00 55.96  ? 793  THR   B OG1 1 
ATOM   2781 C CG2 . THR   B 1 100 ? 35.995 -7.277  19.160  1.00 56.66  ? 793  THR   B CG2 1 
ATOM   2782 N N   . GLN   B 1 101 ? 37.875 -7.218  23.089  1.00 55.45  ? 794  GLN   B N   1 
ATOM   2783 C CA  . GLN   B 1 101 ? 38.892 -7.567  24.062  1.00 56.48  ? 794  GLN   B CA  1 
ATOM   2784 C C   . GLN   B 1 101 ? 40.145 -8.075  23.302  1.00 55.88  ? 794  GLN   B C   1 
ATOM   2785 O O   . GLN   B 1 101 ? 40.021 -8.807  22.320  1.00 55.16  ? 794  GLN   B O   1 
ATOM   2786 C CB  . GLN   B 1 101 ? 38.353 -8.659  24.989  1.00 59.39  ? 794  GLN   B CB  1 
ATOM   2787 C CG  . GLN   B 1 101 ? 39.188 -8.828  26.242  1.00 65.32  ? 794  GLN   B CG  1 
ATOM   2788 C CD  . GLN   B 1 101 ? 38.739 -10.025 27.029  1.00 72.66  ? 794  GLN   B CD  1 
ATOM   2789 O OE1 . GLN   B 1 101 ? 37.543 -10.351 27.081  1.00 75.65  ? 794  GLN   B OE1 1 
ATOM   2790 N NE2 . GLN   B 1 101 ? 39.687 -10.707 27.661  1.00 73.56  ? 794  GLN   B NE2 1 
ATOM   2791 N N   . LEU   B 1 102 ? 41.323 -7.595  23.698  1.00 55.82  ? 795  LEU   B N   1 
ATOM   2792 C CA  . LEU   B 1 102 ? 42.566 -8.001  23.058  1.00 55.92  ? 795  LEU   B CA  1 
ATOM   2793 C C   . LEU   B 1 102 ? 42.841 -9.480  23.306  1.00 56.00  ? 795  LEU   B C   1 
ATOM   2794 O O   . LEU   B 1 102 ? 42.756 -9.944  24.442  1.00 56.53  ? 795  LEU   B O   1 
ATOM   2795 C CB  . LEU   B 1 102 ? 43.736 -7.184  23.618  1.00 55.88  ? 795  LEU   B CB  1 
ATOM   2796 C CG  . LEU   B 1 102 ? 45.120 -7.543  23.080  1.00 57.36  ? 795  LEU   B CG  1 
ATOM   2797 C CD1 . LEU   B 1 102 ? 45.203 -7.279  21.590  1.00 57.88  ? 795  LEU   B CD1 1 
ATOM   2798 C CD2 . LEU   B 1 102 ? 46.216 -6.762  23.819  1.00 58.23  ? 795  LEU   B CD2 1 
ATOM   2799 N N   . MET   B 1 103 ? 43.185 -10.203 22.242  1.00 55.09  ? 796  MET   B N   1 
ATOM   2800 C CA  . MET   B 1 103 ? 43.611 -11.592 22.301  1.00 54.92  ? 796  MET   B CA  1 
ATOM   2801 C C   . MET   B 1 103 ? 45.140 -11.504 22.249  1.00 54.55  ? 796  MET   B C   1 
ATOM   2802 O O   . MET   B 1 103 ? 45.708 -11.067 21.248  1.00 54.98  ? 796  MET   B O   1 
ATOM   2803 C CB  . MET   B 1 103 ? 43.025 -12.352 21.118  1.00 55.49  ? 796  MET   B CB  1 
ATOM   2804 C CG  . MET   B 1 103 ? 41.504 -12.355 21.131  1.00 57.96  ? 796  MET   B CG  1 
ATOM   2805 S SD  . MET   B 1 103 ? 40.808 -13.444 22.399  1.00 61.94  ? 796  MET   B SD  1 
ATOM   2806 C CE  . MET   B 1 103 ? 40.046 -12.262 23.478  1.00 59.93  ? 796  MET   B CE  1 
ATOM   2807 N N   . PRO   B 1 104 ? 45.808 -11.748 23.385  1.00 53.62  ? 797  PRO   B N   1 
ATOM   2808 C CA  . PRO   B 1 104 ? 47.255 -11.471 23.465  1.00 53.27  ? 797  PRO   B CA  1 
ATOM   2809 C C   . PRO   B 1 104 ? 48.172 -12.319 22.593  1.00 52.71  ? 797  PRO   B C   1 
ATOM   2810 O O   . PRO   B 1 104 ? 49.298 -11.896 22.320  1.00 52.40  ? 797  PRO   B O   1 
ATOM   2811 C CB  . PRO   B 1 104 ? 47.572 -11.664 24.949  1.00 53.87  ? 797  PRO   B CB  1 
ATOM   2812 C CG  . PRO   B 1 104 ? 46.250 -11.671 25.648  1.00 54.06  ? 797  PRO   B CG  1 
ATOM   2813 C CD  . PRO   B 1 104 ? 45.270 -12.193 24.682  1.00 52.67  ? 797  PRO   B CD  1 
ATOM   2814 N N   . PHE   B 1 105 ? 47.713 -13.512 22.177  1.00 51.95  ? 798  PHE   B N   1 
ATOM   2815 C CA  . PHE   B 1 105 ? 48.542 -14.367 21.344  1.00 51.56  ? 798  PHE   B CA  1 
ATOM   2816 C C   . PHE   B 1 105 ? 48.286 -14.212 19.844  1.00 51.51  ? 798  PHE   B C   1 
ATOM   2817 O O   . PHE   B 1 105 ? 48.836 -14.986 19.073  1.00 52.69  ? 798  PHE   B O   1 
ATOM   2818 C CB  . PHE   B 1 105 ? 48.440 -15.827 21.768  1.00 51.15  ? 798  PHE   B CB  1 
ATOM   2819 C CG  . PHE   B 1 105 ? 48.883 -16.099 23.180  1.00 51.01  ? 798  PHE   B CG  1 
ATOM   2820 C CD1 . PHE   B 1 105 ? 47.986 -16.039 24.224  1.00 51.76  ? 798  PHE   B CD1 1 
ATOM   2821 C CD2 . PHE   B 1 105 ? 50.184 -16.484 23.454  1.00 51.43  ? 798  PHE   B CD2 1 
ATOM   2822 C CE1 . PHE   B 1 105 ? 48.390 -16.299 25.531  1.00 52.31  ? 798  PHE   B CE1 1 
ATOM   2823 C CE2 . PHE   B 1 105 ? 50.593 -16.719 24.761  1.00 52.01  ? 798  PHE   B CE2 1 
ATOM   2824 C CZ  . PHE   B 1 105 ? 49.692 -16.631 25.791  1.00 51.89  ? 798  PHE   B CZ  1 
ATOM   2825 N N   . GLY   B 1 106 ? 47.508 -13.212 19.434  1.00 50.13  ? 799  GLY   B N   1 
ATOM   2826 C CA  . GLY   B 1 106 ? 47.235 -12.971 18.026  1.00 49.67  ? 799  GLY   B CA  1 
ATOM   2827 C C   . GLY   B 1 106 ? 46.363 -14.032 17.382  1.00 49.51  ? 799  GLY   B C   1 
ATOM   2828 O O   . GLY   B 1 106 ? 45.600 -14.709 18.065  1.00 49.93  ? 799  GLY   B O   1 
ATOM   2829 N N   . CYS   B 1 107 ? 46.465 -14.187 16.067  1.00 48.74  ? 800  CYS   B N   1 
ATOM   2830 C CA  . CYS   B 1 107 ? 45.681 -15.165 15.343  1.00 48.45  ? 800  CYS   B CA  1 
ATOM   2831 C C   . CYS   B 1 107 ? 46.359 -16.532 15.297  1.00 47.38  ? 800  CYS   B C   1 
ATOM   2832 O O   . CYS   B 1 107 ? 47.581 -16.635 15.392  1.00 47.10  ? 800  CYS   B O   1 
ATOM   2833 C CB  . CYS   B 1 107 ? 45.349 -14.652 13.950  1.00 49.90  ? 800  CYS   B CB  1 
ATOM   2834 S SG  . CYS   B 1 107 ? 46.803 -14.368 12.915  1.00 55.38  ? 800  CYS   B SG  1 
ATOM   2835 N N   . LEU   B 1 108 ? 45.550 -17.579 15.146  1.00 46.82  ? 801  LEU   B N   1 
ATOM   2836 C CA  . LEU   B 1 108 ? 45.975 -18.966 15.107  1.00 47.42  ? 801  LEU   B CA  1 
ATOM   2837 C C   . LEU   B 1 108 ? 46.946 -19.254 13.968  1.00 48.39  ? 801  LEU   B C   1 
ATOM   2838 O O   . LEU   B 1 108 ? 47.873 -20.052 14.145  1.00 48.86  ? 801  LEU   B O   1 
ATOM   2839 C CB  . LEU   B 1 108 ? 44.749 -19.895 15.079  1.00 47.56  ? 801  LEU   B CB  1 
ATOM   2840 C CG  . LEU   B 1 108 ? 44.969 -21.369 15.476  1.00 49.05  ? 801  LEU   B CG  1 
ATOM   2841 C CD1 . LEU   B 1 108 ? 45.694 -21.511 16.823  1.00 49.35  ? 801  LEU   B CD1 1 
ATOM   2842 C CD2 . LEU   B 1 108 ? 43.652 -22.108 15.521  1.00 49.68  ? 801  LEU   B CD2 1 
ATOM   2843 N N   . LEU   B 1 109 ? 46.790 -18.555 12.836  1.00 48.79  ? 802  LEU   B N   1 
ATOM   2844 C CA  . LEU   B 1 109 ? 47.683 -18.700 11.690  1.00 49.87  ? 802  LEU   B CA  1 
ATOM   2845 C C   . LEU   B 1 109 ? 49.134 -18.337 12.044  1.00 50.88  ? 802  LEU   B C   1 
ATOM   2846 O O   . LEU   B 1 109 ? 50.039 -19.127 11.781  1.00 51.70  ? 802  LEU   B O   1 
ATOM   2847 C CB  . LEU   B 1 109 ? 47.193 -17.841 10.513  1.00 50.07  ? 802  LEU   B CB  1 
ATOM   2848 C CG  . LEU   B 1 109 ? 48.056 -17.919 9.260   1.00 51.48  ? 802  LEU   B CG  1 
ATOM   2849 C CD1 . LEU   B 1 109 ? 48.091 -19.336 8.708   1.00 51.90  ? 802  LEU   B CD1 1 
ATOM   2850 C CD2 . LEU   B 1 109 ? 47.595 -16.917 8.218   1.00 52.06  ? 802  LEU   B CD2 1 
ATOM   2851 N N   . ASP   B 1 110 ? 49.356 -17.155 12.627  1.00 50.81  ? 803  ASP   B N   1 
ATOM   2852 C CA  . ASP   B 1 110 ? 50.695 -16.738 13.025  1.00 51.71  ? 803  ASP   B CA  1 
ATOM   2853 C C   . ASP   B 1 110 ? 51.227 -17.624 14.143  1.00 51.87  ? 803  ASP   B C   1 
ATOM   2854 O O   . ASP   B 1 110 ? 52.409 -17.947 14.151  1.00 52.00  ? 803  ASP   B O   1 
ATOM   2855 C CB  . ASP   B 1 110 ? 50.695 -15.269 13.469  1.00 54.26  ? 803  ASP   B CB  1 
ATOM   2856 C CG  . ASP   B 1 110 ? 50.348 -14.269 12.376  1.00 61.07  ? 803  ASP   B CG  1 
ATOM   2857 O OD1 . ASP   B 1 110 ? 50.325 -14.666 11.187  1.00 62.08  ? 803  ASP   B OD1 1 
ATOM   2858 O OD2 . ASP   B 1 110 ? 50.107 -13.085 12.708  1.00 64.19  ? 803  ASP   B OD2 1 
ATOM   2859 N N   . TYR   B 1 111 ? 50.351 -18.024 15.074  1.00 51.81  ? 804  TYR   B N   1 
ATOM   2860 C CA  . TYR   B 1 111 ? 50.695 -18.867 16.209  1.00 52.23  ? 804  TYR   B CA  1 
ATOM   2861 C C   . TYR   B 1 111 ? 51.246 -20.234 15.783  1.00 52.47  ? 804  TYR   B C   1 
ATOM   2862 O O   . TYR   B 1 111 ? 52.262 -20.658 16.328  1.00 51.71  ? 804  TYR   B O   1 
ATOM   2863 C CB  . TYR   B 1 111 ? 49.486 -19.018 17.160  1.00 52.10  ? 804  TYR   B CB  1 
ATOM   2864 C CG  . TYR   B 1 111 ? 49.854 -19.696 18.461  1.00 52.22  ? 804  TYR   B CG  1 
ATOM   2865 C CD1 . TYR   B 1 111 ? 50.376 -18.969 19.523  1.00 52.71  ? 804  TYR   B CD1 1 
ATOM   2866 C CD2 . TYR   B 1 111 ? 49.728 -21.071 18.613  1.00 52.66  ? 804  TYR   B CD2 1 
ATOM   2867 C CE1 . TYR   B 1 111 ? 50.736 -19.589 20.713  1.00 53.50  ? 804  TYR   B CE1 1 
ATOM   2868 C CE2 . TYR   B 1 111 ? 50.126 -21.706 19.783  1.00 53.32  ? 804  TYR   B CE2 1 
ATOM   2869 C CZ  . TYR   B 1 111 ? 50.642 -20.960 20.826  1.00 54.48  ? 804  TYR   B CZ  1 
ATOM   2870 O OH  . TYR   B 1 111 ? 51.037 -21.558 21.992  1.00 56.49  ? 804  TYR   B OH  1 
ATOM   2871 N N   . VAL   B 1 112 ? 50.579 -20.928 14.824  1.00 53.14  ? 805  VAL   B N   1 
ATOM   2872 C CA  . VAL   B 1 112 ? 51.059 -22.245 14.374  1.00 54.09  ? 805  VAL   B CA  1 
ATOM   2873 C C   . VAL   B 1 112 ? 52.364 -22.131 13.577  1.00 55.13  ? 805  VAL   B C   1 
ATOM   2874 O O   . VAL   B 1 112 ? 53.204 -23.022 13.663  1.00 55.07  ? 805  VAL   B O   1 
ATOM   2875 C CB  . VAL   B 1 112 ? 50.007 -23.121 13.640  1.00 54.34  ? 805  VAL   B CB  1 
ATOM   2876 C CG1 . VAL   B 1 112 ? 48.829 -23.420 14.545  1.00 54.56  ? 805  VAL   B CG1 1 
ATOM   2877 C CG2 . VAL   B 1 112 ? 49.542 -22.479 12.341  1.00 55.03  ? 805  VAL   B CG2 1 
ATOM   2878 N N   . ARG   B 1 113 ? 52.550 -21.024 12.843  1.00 55.82  ? 806  ARG   B N   1 
ATOM   2879 C CA  . ARG   B 1 113 ? 53.782 -20.807 12.098  1.00 56.77  ? 806  ARG   B CA  1 
ATOM   2880 C C   . ARG   B 1 113 ? 54.926 -20.548 13.067  1.00 58.64  ? 806  ARG   B C   1 
ATOM   2881 O O   . ARG   B 1 113 ? 56.019 -21.058 12.863  1.00 59.61  ? 806  ARG   B O   1 
ATOM   2882 C CB  . ARG   B 1 113 ? 53.642 -19.604 11.155  1.00 56.92  ? 806  ARG   B CB  1 
ATOM   2883 C CG  . ARG   B 1 113 ? 52.769 -19.855 9.944   1.00 57.86  ? 806  ARG   B CG  1 
ATOM   2884 C CD  . ARG   B 1 113 ? 52.533 -18.557 9.220   1.00 58.80  ? 806  ARG   B CD  1 
ATOM   2885 N NE  . ARG   B 1 113 ? 51.778 -18.743 7.984   1.00 60.01  ? 806  ARG   B NE  1 
ATOM   2886 C CZ  . ARG   B 1 113 ? 51.267 -17.748 7.262   1.00 60.96  ? 806  ARG   B CZ  1 
ATOM   2887 N NH1 . ARG   B 1 113 ? 51.426 -16.488 7.649   1.00 60.08  ? 806  ARG   B NH1 1 
ATOM   2888 N NH2 . ARG   B 1 113 ? 50.600 -18.006 6.145   1.00 60.03  ? 806  ARG   B NH2 1 
ATOM   2889 N N   . GLU   B 1 114 ? 54.693 -19.745 14.111  1.00 59.32  ? 807  GLU   B N   1 
ATOM   2890 C CA  . GLU   B 1 114 ? 55.739 -19.413 15.074  1.00 60.46  ? 807  GLU   B CA  1 
ATOM   2891 C C   . GLU   B 1 114 ? 56.051 -20.558 16.050  1.00 62.41  ? 807  GLU   B C   1 
ATOM   2892 O O   . GLU   B 1 114 ? 57.178 -20.656 16.538  1.00 62.54  ? 807  GLU   B O   1 
ATOM   2893 C CB  . GLU   B 1 114 ? 55.414 -18.114 15.816  1.00 61.26  ? 807  GLU   B CB  1 
ATOM   2894 N N   . HIS   B 1 115 ? 55.080 -21.449 16.300  1.00 63.58  ? 808  HIS   B N   1 
ATOM   2895 C CA  . HIS   B 1 115 ? 55.290 -22.576 17.205  1.00 65.05  ? 808  HIS   B CA  1 
ATOM   2896 C C   . HIS   B 1 115 ? 55.272 -23.931 16.502  1.00 66.95  ? 808  HIS   B C   1 
ATOM   2897 O O   . HIS   B 1 115 ? 54.972 -24.925 17.152  1.00 66.99  ? 808  HIS   B O   1 
ATOM   2898 C CB  . HIS   B 1 115 ? 54.268 -22.542 18.345  1.00 65.49  ? 808  HIS   B CB  1 
ATOM   2899 C CG  . HIS   B 1 115 ? 54.337 -21.276 19.126  1.00 67.52  ? 808  HIS   B CG  1 
ATOM   2900 N ND1 . HIS   B 1 115 ? 53.559 -20.183 18.793  1.00 69.22  ? 808  HIS   B ND1 1 
ATOM   2901 C CD2 . HIS   B 1 115 ? 55.153 -20.939 20.153  1.00 68.48  ? 808  HIS   B CD2 1 
ATOM   2902 C CE1 . HIS   B 1 115 ? 53.918 -19.221 19.629  1.00 69.59  ? 808  HIS   B CE1 1 
ATOM   2903 N NE2 . HIS   B 1 115 ? 54.857 -19.637 20.480  1.00 69.57  ? 808  HIS   B NE2 1 
ATOM   2904 N N   . LYS   B 1 116 ? 55.623 -23.979 15.197  1.00 68.48  ? 809  LYS   B N   1 
ATOM   2905 C CA  . LYS   B 1 116 ? 55.671 -25.194 14.359  1.00 70.43  ? 809  LYS   B CA  1 
ATOM   2906 C C   . LYS   B 1 116 ? 56.171 -26.455 15.093  1.00 72.04  ? 809  LYS   B C   1 
ATOM   2907 O O   . LYS   B 1 116 ? 55.528 -27.504 15.030  1.00 72.43  ? 809  LYS   B O   1 
ATOM   2908 C CB  . LYS   B 1 116 ? 56.564 -24.955 13.117  1.00 72.59  ? 809  LYS   B CB  1 
ATOM   2909 C CG  . LYS   B 1 116 ? 55.870 -24.280 11.946  1.00 77.22  ? 809  LYS   B CG  1 
ATOM   2910 C CD  . LYS   B 1 116 ? 56.871 -23.630 10.974  1.00 81.66  ? 809  LYS   B CD  1 
ATOM   2911 C CE  . LYS   B 1 116 ? 56.166 -22.747 9.957   1.00 85.09  ? 809  LYS   B CE  1 
ATOM   2912 N NZ  . LYS   B 1 116 ? 56.988 -21.566 9.569   1.00 86.63  ? 809  LYS   B NZ  1 
ATOM   2913 N N   . ASP   B 1 117 ? 57.314 -26.331 15.795  1.00 72.57  ? 810  ASP   B N   1 
ATOM   2914 C CA  . ASP   B 1 117 ? 58.002 -27.417 16.498  1.00 73.32  ? 810  ASP   B CA  1 
ATOM   2915 C C   . ASP   B 1 117 ? 57.517 -27.669 17.928  1.00 72.91  ? 810  ASP   B C   1 
ATOM   2916 O O   . ASP   B 1 117 ? 58.107 -28.491 18.616  1.00 73.32  ? 810  ASP   B O   1 
ATOM   2917 C CB  . ASP   B 1 117 ? 59.525 -27.145 16.528  1.00 76.47  ? 810  ASP   B CB  1 
ATOM   2918 C CG  . ASP   B 1 117 ? 60.270 -27.475 15.257  1.00 83.11  ? 810  ASP   B CG  1 
ATOM   2919 O OD1 . ASP   B 1 117 ? 59.624 -27.510 14.184  1.00 84.12  ? 810  ASP   B OD1 1 
ATOM   2920 O OD2 . ASP   B 1 117 ? 61.505 -27.694 15.332  1.00 86.00  ? 810  ASP   B OD2 1 
ATOM   2921 N N   . ASN   B 1 118 ? 56.492 -26.958 18.396  1.00 71.89  ? 811  ASN   B N   1 
ATOM   2922 C CA  . ASN   B 1 118 ? 55.972 -27.138 19.756  1.00 71.01  ? 811  ASN   B CA  1 
ATOM   2923 C C   . ASN   B 1 118 ? 54.485 -27.516 19.788  1.00 68.74  ? 811  ASN   B C   1 
ATOM   2924 O O   . ASN   B 1 118 ? 53.882 -27.454 20.859  1.00 69.39  ? 811  ASN   B O   1 
ATOM   2925 C CB  . ASN   B 1 118 ? 56.178 -25.872 20.578  1.00 73.24  ? 811  ASN   B CB  1 
ATOM   2926 C CG  . ASN   B 1 118 ? 57.629 -25.548 20.791  1.00 79.42  ? 811  ASN   B CG  1 
ATOM   2927 O OD1 . ASN   B 1 118 ? 58.094 -24.432 20.509  1.00 81.51  ? 811  ASN   B OD1 1 
ATOM   2928 N ND2 . ASN   B 1 118 ? 58.384 -26.521 21.288  1.00 80.88  ? 811  ASN   B ND2 1 
ATOM   2929 N N   . ILE   B 1 119 ? 53.873 -27.863 18.640  1.00 65.60  ? 812  ILE   B N   1 
ATOM   2930 C CA  . ILE   B 1 119 ? 52.451 -28.196 18.618  1.00 63.24  ? 812  ILE   B CA  1 
ATOM   2931 C C   . ILE   B 1 119 ? 52.207 -29.674 18.371  1.00 60.95  ? 812  ILE   B C   1 
ATOM   2932 O O   . ILE   B 1 119 ? 52.569 -30.213 17.324  1.00 60.95  ? 812  ILE   B O   1 
ATOM   2933 C CB  . ILE   B 1 119 ? 51.665 -27.303 17.633  1.00 63.22  ? 812  ILE   B CB  1 
ATOM   2934 C CG1 . ILE   B 1 119 ? 51.883 -25.821 17.951  1.00 63.59  ? 812  ILE   B CG1 1 
ATOM   2935 C CG2 . ILE   B 1 119 ? 50.185 -27.657 17.656  1.00 63.47  ? 812  ILE   B CG2 1 
ATOM   2936 C CD1 . ILE   B 1 119 ? 51.397 -24.910 16.903  1.00 64.37  ? 812  ILE   B CD1 1 
ATOM   2937 N N   . GLY   B 1 120 ? 51.601 -30.322 19.348  1.00 58.99  ? 813  GLY   B N   1 
ATOM   2938 C CA  . GLY   B 1 120 ? 51.286 -31.741 19.256  1.00 57.47  ? 813  GLY   B CA  1 
ATOM   2939 C C   . GLY   B 1 120 ? 49.905 -32.003 18.695  1.00 55.36  ? 813  GLY   B C   1 
ATOM   2940 O O   . GLY   B 1 120 ? 49.158 -31.069 18.398  1.00 54.96  ? 813  GLY   B O   1 
ATOM   2941 N N   . SER   B 1 121 ? 49.555 -33.285 18.548  1.00 53.86  ? 814  SER   B N   1 
ATOM   2942 C CA  . SER   B 1 121 ? 48.262 -33.694 18.009  1.00 52.66  ? 814  SER   B CA  1 
ATOM   2943 C C   . SER   B 1 121 ? 47.078 -33.253 18.872  1.00 50.91  ? 814  SER   B C   1 
ATOM   2944 O O   . SER   B 1 121 ? 46.025 -32.942 18.338  1.00 50.96  ? 814  SER   B O   1 
ATOM   2945 C CB  . SER   B 1 121 ? 48.234 -35.208 17.811  1.00 54.05  ? 814  SER   B CB  1 
ATOM   2946 O OG  . SER   B 1 121 ? 48.566 -35.884 19.011  1.00 55.65  ? 814  SER   B OG  1 
ATOM   2947 N N   . GLN   B 1 122 ? 47.256 -33.222 20.192  1.00 49.70  ? 815  GLN   B N   1 
ATOM   2948 C CA  . GLN   B 1 122 ? 46.221 -32.835 21.139  1.00 49.16  ? 815  GLN   B CA  1 
ATOM   2949 C C   . GLN   B 1 122 ? 45.727 -31.418 20.897  1.00 48.38  ? 815  GLN   B C   1 
ATOM   2950 O O   . GLN   B 1 122 ? 44.516 -31.210 20.869  1.00 49.05  ? 815  GLN   B O   1 
ATOM   2951 C CB  . GLN   B 1 122 ? 46.714 -33.012 22.588  1.00 51.00  ? 815  GLN   B CB  1 
ATOM   2952 C CG  . GLN   B 1 122 ? 45.616 -32.983 23.641  1.00 55.14  ? 815  GLN   B CG  1 
ATOM   2953 C CD  . GLN   B 1 122 ? 44.716 -34.197 23.574  1.00 61.83  ? 815  GLN   B CD  1 
ATOM   2954 O OE1 . GLN   B 1 122 ? 45.019 -35.256 24.147  1.00 65.81  ? 815  GLN   B OE1 1 
ATOM   2955 N NE2 . GLN   B 1 122 ? 43.579 -34.070 22.901  1.00 61.21  ? 815  GLN   B NE2 1 
ATOM   2956 N N   . TYR   B 1 123 ? 46.632 -30.450 20.682  1.00 46.68  ? 816  TYR   B N   1 
ATOM   2957 C CA  . TYR   B 1 123 ? 46.215 -29.070 20.429  1.00 45.51  ? 816  TYR   B CA  1 
ATOM   2958 C C   . TYR   B 1 123 ? 45.578 -28.876 19.076  1.00 44.11  ? 816  TYR   B C   1 
ATOM   2959 O O   . TYR   B 1 123 ? 44.524 -28.244 18.989  1.00 44.09  ? 816  TYR   B O   1 
ATOM   2960 C CB  . TYR   B 1 123 ? 47.352 -28.072 20.643  1.00 45.76  ? 816  TYR   B CB  1 
ATOM   2961 C CG  . TYR   B 1 123 ? 47.508 -27.716 22.099  1.00 47.69  ? 816  TYR   B CG  1 
ATOM   2962 C CD1 . TYR   B 1 123 ? 47.943 -28.655 23.021  1.00 49.76  ? 816  TYR   B CD1 1 
ATOM   2963 C CD2 . TYR   B 1 123 ? 47.197 -26.448 22.562  1.00 49.06  ? 816  TYR   B CD2 1 
ATOM   2964 C CE1 . TYR   B 1 123 ? 48.086 -28.335 24.366  1.00 51.28  ? 816  TYR   B CE1 1 
ATOM   2965 C CE2 . TYR   B 1 123 ? 47.343 -26.111 23.903  1.00 50.38  ? 816  TYR   B CE2 1 
ATOM   2966 C CZ  . TYR   B 1 123 ? 47.796 -27.057 24.803  1.00 52.24  ? 816  TYR   B CZ  1 
ATOM   2967 O OH  . TYR   B 1 123 ? 47.933 -26.752 26.135  1.00 54.74  ? 816  TYR   B OH  1 
ATOM   2968 N N   . LEU   B 1 124 ? 46.171 -29.443 18.019  1.00 42.97  ? 817  LEU   B N   1 
ATOM   2969 C CA  . LEU   B 1 124 ? 45.603 -29.315 16.675  1.00 42.64  ? 817  LEU   B CA  1 
ATOM   2970 C C   . LEU   B 1 124 ? 44.154 -29.823 16.598  1.00 42.05  ? 817  LEU   B C   1 
ATOM   2971 O O   . LEU   B 1 124 ? 43.296 -29.143 16.032  1.00 41.72  ? 817  LEU   B O   1 
ATOM   2972 C CB  . LEU   B 1 124 ? 46.472 -30.057 15.653  1.00 42.71  ? 817  LEU   B CB  1 
ATOM   2973 C CG  . LEU   B 1 124 ? 47.816 -29.434 15.383  1.00 43.90  ? 817  LEU   B CG  1 
ATOM   2974 C CD1 . LEU   B 1 124 ? 48.682 -30.365 14.567  1.00 44.42  ? 817  LEU   B CD1 1 
ATOM   2975 C CD2 . LEU   B 1 124 ? 47.663 -28.091 14.706  1.00 44.75  ? 817  LEU   B CD2 1 
ATOM   2976 N N   . LEU   B 1 125 ? 43.874 -30.987 17.220  1.00 41.34  ? 818  LEU   B N   1 
ATOM   2977 C CA  . LEU   B 1 125 ? 42.517 -31.541 17.198  1.00 40.80  ? 818  LEU   B CA  1 
ATOM   2978 C C   . LEU   B 1 125 ? 41.547 -30.781 18.097  1.00 40.27  ? 818  LEU   B C   1 
ATOM   2979 O O   . LEU   B 1 125 ? 40.391 -30.622 17.730  1.00 40.23  ? 818  LEU   B O   1 
ATOM   2980 C CB  . LEU   B 1 125 ? 42.527 -33.036 17.510  1.00 40.34  ? 818  LEU   B CB  1 
ATOM   2981 C CG  . LEU   B 1 125 ? 43.158 -33.913 16.425  1.00 40.90  ? 818  LEU   B CG  1 
ATOM   2982 C CD1 . LEU   B 1 125 ? 43.475 -35.297 16.948  1.00 40.98  ? 818  LEU   B CD1 1 
ATOM   2983 C CD2 . LEU   B 1 125 ? 42.260 -34.016 15.219  1.00 41.26  ? 818  LEU   B CD2 1 
ATOM   2984 N N   . ASN   B 1 126 ? 42.020 -30.268 19.236  1.00 39.99  ? 819  ASN   B N   1 
ATOM   2985 C CA  . ASN   B 1 126 ? 41.192 -29.482 20.148  1.00 40.48  ? 819  ASN   B CA  1 
ATOM   2986 C C   . ASN   B 1 126 ? 40.799 -28.151 19.515  1.00 40.18  ? 819  ASN   B C   1 
ATOM   2987 O O   . ASN   B 1 126 ? 39.662 -27.714 19.687  1.00 39.92  ? 819  ASN   B O   1 
ATOM   2988 C CB  . ASN   B 1 126 ? 41.905 -29.242 21.473  1.00 42.17  ? 819  ASN   B CB  1 
ATOM   2989 C CG  . ASN   B 1 126 ? 41.958 -30.448 22.365  1.00 47.07  ? 819  ASN   B CG  1 
ATOM   2990 O OD1 . ASN   B 1 126 ? 41.230 -31.425 22.167  1.00 49.17  ? 819  ASN   B OD1 1 
ATOM   2991 N ND2 . ASN   B 1 126 ? 42.836 -30.411 23.367  1.00 48.35  ? 819  ASN   B ND2 1 
ATOM   2992 N N   . TRP   B 1 127 ? 41.720 -27.527 18.751  1.00 39.92  ? 820  TRP   B N   1 
ATOM   2993 C CA  . TRP   B 1 127 ? 41.417 -26.280 18.054  1.00 40.06  ? 820  TRP   B CA  1 
ATOM   2994 C C   . TRP   B 1 127 ? 40.376 -26.519 16.981  1.00 40.35  ? 820  TRP   B C   1 
ATOM   2995 O O   . TRP   B 1 127 ? 39.497 -25.686 16.830  1.00 40.96  ? 820  TRP   B O   1 
ATOM   2996 C CB  . TRP   B 1 127 ? 42.661 -25.668 17.432  1.00 39.83  ? 820  TRP   B CB  1 
ATOM   2997 C CG  . TRP   B 1 127 ? 43.664 -25.160 18.425  1.00 40.15  ? 820  TRP   B CG  1 
ATOM   2998 C CD1 . TRP   B 1 127 ? 43.413 -24.607 19.654  1.00 41.02  ? 820  TRP   B CD1 1 
ATOM   2999 C CD2 . TRP   B 1 127 ? 45.074 -25.062 18.221  1.00 39.99  ? 820  TRP   B CD2 1 
ATOM   3000 N NE1 . TRP   B 1 127 ? 44.591 -24.212 20.247  1.00 41.01  ? 820  TRP   B NE1 1 
ATOM   3001 C CE2 . TRP   B 1 127 ? 45.627 -24.478 19.387  1.00 40.85  ? 820  TRP   B CE2 1 
ATOM   3002 C CE3 . TRP   B 1 127 ? 45.930 -25.447 17.181  1.00 40.50  ? 820  TRP   B CE3 1 
ATOM   3003 C CZ2 . TRP   B 1 127 ? 46.997 -24.254 19.530  1.00 41.45  ? 820  TRP   B CZ2 1 
ATOM   3004 C CZ3 . TRP   B 1 127 ? 47.287 -25.233 17.328  1.00 41.67  ? 820  TRP   B CZ3 1 
ATOM   3005 C CH2 . TRP   B 1 127 ? 47.807 -24.635 18.487  1.00 41.71  ? 820  TRP   B CH2 1 
ATOM   3006 N N   . CYS   B 1 128 ? 40.441 -27.654 16.259  1.00 40.24  ? 821  CYS   B N   1 
ATOM   3007 C CA  . CYS   B 1 128 ? 39.441 -28.012 15.238  1.00 40.96  ? 821  CYS   B CA  1 
ATOM   3008 C C   . CYS   B 1 128 ? 38.052 -28.104 15.869  1.00 40.67  ? 821  CYS   B C   1 
ATOM   3009 O O   . CYS   B 1 128 ? 37.083 -27.651 15.270  1.00 41.60  ? 821  CYS   B O   1 
ATOM   3010 C CB  . CYS   B 1 128 ? 39.802 -29.324 14.544  1.00 42.78  ? 821  CYS   B CB  1 
ATOM   3011 S SG  . CYS   B 1 128 ? 41.282 -29.247 13.515  1.00 49.17  ? 821  CYS   B SG  1 
ATOM   3012 N N   . VAL   B 1 129 ? 37.958 -28.704 17.059  1.00 39.49  ? 822  VAL   B N   1 
ATOM   3013 C CA  . VAL   B 1 129 ? 36.711 -28.844 17.801  1.00 38.90  ? 822  VAL   B CA  1 
ATOM   3014 C C   . VAL   B 1 129 ? 36.171 -27.464 18.176  1.00 38.40  ? 822  VAL   B C   1 
ATOM   3015 O O   . VAL   B 1 129 ? 34.981 -27.198 18.001  1.00 39.30  ? 822  VAL   B O   1 
ATOM   3016 C CB  . VAL   B 1 129 ? 36.907 -29.698 19.082  1.00 39.09  ? 822  VAL   B CB  1 
ATOM   3017 C CG1 . VAL   B 1 129 ? 35.637 -29.696 19.932  1.00 39.48  ? 822  VAL   B CG1 1 
ATOM   3018 C CG2 . VAL   B 1 129 ? 37.317 -31.125 18.738  1.00 39.07  ? 822  VAL   B CG2 1 
ATOM   3019 N N   . GLN   B 1 130 ? 37.042 -26.601 18.715  1.00 36.56  ? 823  GLN   B N   1 
ATOM   3020 C CA  . GLN   B 1 130 ? 36.682 -25.273 19.149  1.00 34.95  ? 823  GLN   B CA  1 
ATOM   3021 C C   . GLN   B 1 130 ? 36.191 -24.416 18.000  1.00 34.50  ? 823  GLN   B C   1 
ATOM   3022 O O   . GLN   B 1 130 ? 35.145 -23.791 18.132  1.00 34.84  ? 823  GLN   B O   1 
ATOM   3023 C CB  . GLN   B 1 130 ? 37.840 -24.633 19.898  1.00 34.52  ? 823  GLN   B CB  1 
ATOM   3024 C CG  . GLN   B 1 130 ? 38.154 -25.362 21.201  1.00 34.09  ? 823  GLN   B CG  1 
ATOM   3025 C CD  . GLN   B 1 130 ? 39.196 -24.659 22.040  1.00 36.81  ? 823  GLN   B CD  1 
ATOM   3026 O OE1 . GLN   B 1 130 ? 39.595 -23.526 21.773  1.00 38.64  ? 823  GLN   B OE1 1 
ATOM   3027 N NE2 . GLN   B 1 130 ? 39.671 -25.310 23.083  1.00 36.81  ? 823  GLN   B NE2 1 
ATOM   3028 N N   . ILE   B 1 131 ? 36.874 -24.442 16.862  1.00 34.12  ? 824  ILE   B N   1 
ATOM   3029 C CA  . ILE   B 1 131 ? 36.425 -23.697 15.688  1.00 34.81  ? 824  ILE   B CA  1 
ATOM   3030 C C   . ILE   B 1 131 ? 35.061 -24.213 15.196  1.00 36.19  ? 824  ILE   B C   1 
ATOM   3031 O O   . ILE   B 1 131 ? 34.185 -23.403 14.887  1.00 36.83  ? 824  ILE   B O   1 
ATOM   3032 C CB  . ILE   B 1 131 ? 37.505 -23.693 14.583  1.00 34.41  ? 824  ILE   B CB  1 
ATOM   3033 C CG1 . ILE   B 1 131 ? 38.825 -23.075 15.124  1.00 34.67  ? 824  ILE   B CG1 1 
ATOM   3034 C CG2 . ILE   B 1 131 ? 37.001 -22.970 13.327  1.00 34.00  ? 824  ILE   B CG2 1 
ATOM   3035 C CD1 . ILE   B 1 131 ? 39.974 -23.330 14.296  1.00 35.26  ? 824  ILE   B CD1 1 
ATOM   3036 N N   . ALA   B 1 132 ? 34.842 -25.546 15.204  1.00 36.02  ? 825  ALA   B N   1 
ATOM   3037 C CA  . ALA   B 1 132 ? 33.544 -26.097 14.795  1.00 36.34  ? 825  ALA   B CA  1 
ATOM   3038 C C   . ALA   B 1 132 ? 32.444 -25.735 15.792  1.00 37.20  ? 825  ALA   B C   1 
ATOM   3039 O O   . ALA   B 1 132 ? 31.313 -25.535 15.390  1.00 38.10  ? 825  ALA   B O   1 
ATOM   3040 C CB  . ALA   B 1 132 ? 33.633 -27.604 14.614  1.00 36.22  ? 825  ALA   B CB  1 
ATOM   3041 N N   . LYS   B 1 133 ? 32.772 -25.603 17.085  1.00 37.10  ? 826  LYS   B N   1 
ATOM   3042 C CA  . LYS   B 1 133 ? 31.813 -25.202 18.106  1.00 37.27  ? 826  LYS   B CA  1 
ATOM   3043 C C   . LYS   B 1 133 ? 31.366 -23.756 17.919  1.00 38.36  ? 826  LYS   B C   1 
ATOM   3044 O O   . LYS   B 1 133 ? 30.180 -23.446 18.080  1.00 39.66  ? 826  LYS   B O   1 
ATOM   3045 C CB  . LYS   B 1 133 ? 32.377 -25.409 19.506  1.00 38.10  ? 826  LYS   B CB  1 
ATOM   3046 C CG  . LYS   B 1 133 ? 32.215 -26.823 19.970  1.00 41.80  ? 826  LYS   B CG  1 
ATOM   3047 C CD  . LYS   B 1 133 ? 32.943 -27.059 21.244  1.00 45.49  ? 826  LYS   B CD  1 
ATOM   3048 C CE  . LYS   B 1 133 ? 32.662 -28.460 21.719  1.00 49.69  ? 826  LYS   B CE  1 
ATOM   3049 N NZ  . LYS   B 1 133 ? 32.854 -28.575 23.186  1.00 53.23  ? 826  LYS   B NZ  1 
ATOM   3050 N N   . GLY   B 1 134 ? 32.303 -22.893 17.588  1.00 37.83  ? 827  GLY   B N   1 
ATOM   3051 C CA  . GLY   B 1 134 ? 31.996 -21.502 17.333  1.00 38.25  ? 827  GLY   B CA  1 
ATOM   3052 C C   . GLY   B 1 134 ? 31.216 -21.351 16.044  1.00 38.75  ? 827  GLY   B C   1 
ATOM   3053 O O   . GLY   B 1 134 ? 30.228 -20.624 16.004  1.00 39.53  ? 827  GLY   B O   1 
ATOM   3054 N N   . MET   B 1 135 ? 31.613 -22.077 14.990  1.00 38.46  ? 828  MET   B N   1 
ATOM   3055 C CA  . MET   B 1 135 ? 30.906 -22.029 13.713  1.00 38.65  ? 828  MET   B CA  1 
ATOM   3056 C C   . MET   B 1 135 ? 29.507 -22.578 13.811  1.00 38.85  ? 828  MET   B C   1 
ATOM   3057 O O   . MET   B 1 135 ? 28.575 -22.010 13.241  1.00 38.91  ? 828  MET   B O   1 
ATOM   3058 C CB  . MET   B 1 135 ? 31.698 -22.750 12.630  1.00 39.25  ? 828  MET   B CB  1 
ATOM   3059 C CG  . MET   B 1 135 ? 32.938 -22.005 12.200  1.00 41.79  ? 828  MET   B CG  1 
ATOM   3060 S SD  . MET   B 1 135 ? 32.598 -20.291 11.659  1.00 46.40  ? 828  MET   B SD  1 
ATOM   3061 C CE  . MET   B 1 135 ? 31.597 -20.625 10.217  1.00 38.24  ? 828  MET   B CE  1 
ATOM   3062 N N   . ASN   B 1 136 ? 29.344 -23.653 14.581  1.00 38.72  ? 829  ASN   B N   1 
ATOM   3063 C CA  . ASN   B 1 136 ? 28.044 -24.257 14.817  1.00 39.00  ? 829  ASN   B CA  1 
ATOM   3064 C C   . ASN   B 1 136 ? 27.122 -23.304 15.597  1.00 39.76  ? 829  ASN   B C   1 
ATOM   3065 O O   . ASN   B 1 136 ? 25.906 -23.349 15.424  1.00 39.65  ? 829  ASN   B O   1 
ATOM   3066 C CB  . ASN   B 1 136 ? 28.221 -25.563 15.571  1.00 39.23  ? 829  ASN   B CB  1 
ATOM   3067 C CG  . ASN   B 1 136 ? 26.941 -26.288 15.839  1.00 41.70  ? 829  ASN   B CG  1 
ATOM   3068 O OD1 . ASN   B 1 136 ? 26.209 -26.686 14.922  1.00 43.06  ? 829  ASN   B OD1 1 
ATOM   3069 N ND2 . ASN   B 1 136 ? 26.646 -26.444 17.109  1.00 41.89  ? 829  ASN   B ND2 1 
ATOM   3070 N N   . TYR   B 1 137 ? 27.701 -22.456 16.473  1.00 39.91  ? 830  TYR   B N   1 
ATOM   3071 C CA  . TYR   B 1 137 ? 26.949 -21.490 17.245  1.00 39.90  ? 830  TYR   B CA  1 
ATOM   3072 C C   . TYR   B 1 137 ? 26.468 -20.374 16.322  1.00 40.34  ? 830  TYR   B C   1 
ATOM   3073 O O   . TYR   B 1 137 ? 25.313 -19.963 16.421  1.00 41.05  ? 830  TYR   B O   1 
ATOM   3074 C CB  . TYR   B 1 137 ? 27.785 -20.942 18.421  1.00 39.88  ? 830  TYR   B CB  1 
ATOM   3075 C CG  . TYR   B 1 137 ? 27.087 -19.792 19.109  1.00 40.16  ? 830  TYR   B CG  1 
ATOM   3076 C CD1 . TYR   B 1 137 ? 25.885 -19.983 19.776  1.00 41.00  ? 830  TYR   B CD1 1 
ATOM   3077 C CD2 . TYR   B 1 137 ? 27.553 -18.494 18.975  1.00 40.27  ? 830  TYR   B CD2 1 
ATOM   3078 C CE1 . TYR   B 1 137 ? 25.209 -18.925 20.360  1.00 41.72  ? 830  TYR   B CE1 1 
ATOM   3079 C CE2 . TYR   B 1 137 ? 26.877 -17.426 19.538  1.00 40.98  ? 830  TYR   B CE2 1 
ATOM   3080 C CZ  . TYR   B 1 137 ? 25.714 -17.648 20.251  1.00 41.87  ? 830  TYR   B CZ  1 
ATOM   3081 O OH  . TYR   B 1 137 ? 25.021 -16.599 20.795  1.00 42.29  ? 830  TYR   B OH  1 
ATOM   3082 N N   . LEU   B 1 138 ? 27.329 -19.887 15.420  1.00 40.34  ? 831  LEU   B N   1 
ATOM   3083 C CA  . LEU   B 1 138 ? 26.947 -18.870 14.440  1.00 40.68  ? 831  LEU   B CA  1 
ATOM   3084 C C   . LEU   B 1 138 ? 25.837 -19.385 13.528  1.00 41.79  ? 831  LEU   B C   1 
ATOM   3085 O O   . LEU   B 1 138 ? 24.926 -18.633 13.213  1.00 41.97  ? 831  LEU   B O   1 
ATOM   3086 C CB  . LEU   B 1 138 ? 28.160 -18.418 13.620  1.00 40.61  ? 831  LEU   B CB  1 
ATOM   3087 C CG  . LEU   B 1 138 ? 29.202 -17.634 14.415  1.00 41.19  ? 831  LEU   B CG  1 
ATOM   3088 C CD1 . LEU   B 1 138 ? 30.473 -17.386 13.590  1.00 41.03  ? 831  LEU   B CD1 1 
ATOM   3089 C CD2 . LEU   B 1 138 ? 28.603 -16.352 14.994  1.00 40.73  ? 831  LEU   B CD2 1 
ATOM   3090 N N   . GLU   B 1 139 ? 25.863 -20.679 13.159  1.00 42.45  ? 832  GLU   B N   1 
ATOM   3091 C CA  . GLU   B 1 139 ? 24.811 -21.286 12.350  1.00 43.62  ? 832  GLU   B CA  1 
ATOM   3092 C C   . GLU   B 1 139 ? 23.483 -21.327 13.136  1.00 45.25  ? 832  GLU   B C   1 
ATOM   3093 O O   . GLU   B 1 139 ? 22.422 -21.111 12.560  1.00 45.94  ? 832  GLU   B O   1 
ATOM   3094 C CB  . GLU   B 1 139 ? 25.234 -22.688 11.883  1.00 45.79  ? 832  GLU   B CB  1 
ATOM   3095 C CG  . GLU   B 1 139 ? 24.134 -23.446 11.166  1.00 50.40  ? 832  GLU   B CG  1 
ATOM   3096 C CD  . GLU   B 1 139 ? 24.558 -24.704 10.440  1.00 58.47  ? 832  GLU   B CD  1 
ATOM   3097 O OE1 . GLU   B 1 139 ? 25.764 -25.041 10.490  1.00 60.47  ? 832  GLU   B OE1 1 
ATOM   3098 O OE2 . GLU   B 1 139 ? 23.685 -25.345 9.808   1.00 60.24  ? 832  GLU   B OE2 1 
ATOM   3099 N N   . ASP   B 1 140 ? 23.546 -21.553 14.454  1.00 46.06  ? 833  ASP   B N   1 
ATOM   3100 C CA  . ASP   B 1 140 ? 22.393 -21.539 15.359  1.00 47.20  ? 833  ASP   B CA  1 
ATOM   3101 C C   . ASP   B 1 140 ? 21.783 -20.120 15.421  1.00 48.25  ? 833  ASP   B C   1 
ATOM   3102 O O   . ASP   B 1 140 ? 20.565 -19.973 15.513  1.00 48.86  ? 833  ASP   B O   1 
ATOM   3103 C CB  . ASP   B 1 140 ? 22.827 -22.002 16.762  1.00 48.99  ? 833  ASP   B CB  1 
ATOM   3104 C CG  . ASP   B 1 140 ? 21.742 -21.927 17.810  1.00 54.47  ? 833  ASP   B CG  1 
ATOM   3105 O OD1 . ASP   B 1 140 ? 20.733 -22.656 17.670  1.00 55.30  ? 833  ASP   B OD1 1 
ATOM   3106 O OD2 . ASP   B 1 140 ? 21.899 -21.131 18.775  1.00 57.33  ? 833  ASP   B OD2 1 
ATOM   3107 N N   . ARG   B 1 141 ? 22.628 -19.084 15.370  1.00 48.09  ? 834  ARG   B N   1 
ATOM   3108 C CA  . ARG   B 1 141 ? 22.185 -17.695 15.345  1.00 48.61  ? 834  ARG   B CA  1 
ATOM   3109 C C   . ARG   B 1 141 ? 21.782 -17.221 13.942  1.00 49.76  ? 834  ARG   B C   1 
ATOM   3110 O O   . ARG   B 1 141 ? 21.492 -16.037 13.794  1.00 50.43  ? 834  ARG   B O   1 
ATOM   3111 C CB  . ARG   B 1 141 ? 23.293 -16.751 15.859  1.00 49.58  ? 834  ARG   B CB  1 
ATOM   3112 C CG  . ARG   B 1 141 ? 23.745 -16.881 17.326  1.00 51.68  ? 834  ARG   B CG  1 
ATOM   3113 C CD  . ARG   B 1 141 ? 22.825 -17.640 18.264  1.00 54.74  ? 834  ARG   B CD  1 
ATOM   3114 N NE  . ARG   B 1 141 ? 21.738 -16.827 18.793  1.00 57.17  ? 834  ARG   B NE  1 
ATOM   3115 C CZ  . ARG   B 1 141 ? 20.690 -17.322 19.445  1.00 58.61  ? 834  ARG   B CZ  1 
ATOM   3116 N NH1 . ARG   B 1 141 ? 19.748 -16.509 19.912  1.00 58.70  ? 834  ARG   B NH1 1 
ATOM   3117 N NH2 . ARG   B 1 141 ? 20.567 -18.634 19.624  1.00 57.09  ? 834  ARG   B NH2 1 
ATOM   3118 N N   . ARG   B 1 142 ? 21.773 -18.122 12.919  1.00 50.04  ? 835  ARG   B N   1 
ATOM   3119 C CA  . ARG   B 1 142 ? 21.437 -17.861 11.513  1.00 50.28  ? 835  ARG   B CA  1 
ATOM   3120 C C   . ARG   B 1 142 ? 22.408 -16.843 10.900  1.00 50.26  ? 835  ARG   B C   1 
ATOM   3121 O O   . ARG   B 1 142 ? 21.992 -15.966 10.155  1.00 50.51  ? 835  ARG   B O   1 
ATOM   3122 C CB  . ARG   B 1 142 ? 19.978 -17.391 11.370  1.00 51.45  ? 835  ARG   B CB  1 
ATOM   3123 C CG  . ARG   B 1 142 ? 18.964 -18.323 12.019  1.00 54.35  ? 835  ARG   B CG  1 
ATOM   3124 N N   . LEU   B 1 143 ? 23.694 -16.951 11.225  1.00 49.92  ? 836  LEU   B N   1 
ATOM   3125 C CA  . LEU   B 1 143 ? 24.695 -16.009 10.728  1.00 50.16  ? 836  LEU   B CA  1 
ATOM   3126 C C   . LEU   B 1 143 ? 25.741 -16.712 9.868   1.00 49.57  ? 836  LEU   B C   1 
ATOM   3127 O O   . LEU   B 1 143 ? 26.435 -17.608 10.344  1.00 50.32  ? 836  LEU   B O   1 
ATOM   3128 C CB  . LEU   B 1 143 ? 25.366 -15.278 11.912  1.00 50.78  ? 836  LEU   B CB  1 
ATOM   3129 C CG  . LEU   B 1 143 ? 26.113 -13.981 11.606  1.00 53.01  ? 836  LEU   B CG  1 
ATOM   3130 C CD1 . LEU   B 1 143 ? 26.014 -13.019 12.781  1.00 53.48  ? 836  LEU   B CD1 1 
ATOM   3131 C CD2 . LEU   B 1 143 ? 27.586 -14.247 11.305  1.00 54.19  ? 836  LEU   B CD2 1 
ATOM   3132 N N   . VAL   B 1 144 ? 25.862 -16.303 8.608   1.00 48.08  ? 837  VAL   B N   1 
ATOM   3133 C CA  . VAL   B 1 144 ? 26.862 -16.873 7.706   1.00 46.99  ? 837  VAL   B CA  1 
ATOM   3134 C C   . VAL   B 1 144 ? 28.110 -16.011 7.873   1.00 46.25  ? 837  VAL   B C   1 
ATOM   3135 O O   . VAL   B 1 144 ? 28.025 -14.794 7.749   1.00 46.00  ? 837  VAL   B O   1 
ATOM   3136 C CB  . VAL   B 1 144 ? 26.351 -16.908 6.228   1.00 46.54  ? 837  VAL   B CB  1 
ATOM   3137 C CG1 . VAL   B 1 144 ? 27.449 -17.371 5.269   1.00 47.20  ? 837  VAL   B CG1 1 
ATOM   3138 C CG2 . VAL   B 1 144 ? 25.115 -17.787 6.101   1.00 45.65  ? 837  VAL   B CG2 1 
ATOM   3139 N N   . HIS   B 1 145 ? 29.249 -16.623 8.203   1.00 45.64  ? 838  HIS   B N   1 
ATOM   3140 C CA  . HIS   B 1 145 ? 30.493 -15.879 8.416   1.00 45.60  ? 838  HIS   B CA  1 
ATOM   3141 C C   . HIS   B 1 145 ? 31.029 -15.228 7.130   1.00 46.94  ? 838  HIS   B C   1 
ATOM   3142 O O   . HIS   B 1 145 ? 31.319 -14.026 7.135   1.00 47.34  ? 838  HIS   B O   1 
ATOM   3143 C CB  . HIS   B 1 145 ? 31.548 -16.788 9.067   1.00 44.66  ? 838  HIS   B CB  1 
ATOM   3144 C CG  . HIS   B 1 145 ? 32.752 -16.072 9.587   1.00 43.64  ? 838  HIS   B CG  1 
ATOM   3145 N ND1 . HIS   B 1 145 ? 33.572 -15.342 8.756   1.00 45.06  ? 838  HIS   B ND1 1 
ATOM   3146 C CD2 . HIS   B 1 145 ? 33.271 -16.059 10.831  1.00 44.14  ? 838  HIS   B CD2 1 
ATOM   3147 C CE1 . HIS   B 1 145 ? 34.543 -14.879 9.524   1.00 45.35  ? 838  HIS   B CE1 1 
ATOM   3148 N NE2 . HIS   B 1 145 ? 34.411 -15.299 10.776  1.00 45.04  ? 838  HIS   B NE2 1 
ATOM   3149 N N   . ARG   B 1 146 ? 31.171 -16.026 6.047   1.00 47.60  ? 839  ARG   B N   1 
ATOM   3150 C CA  . ARG   B 1 146 ? 31.661 -15.642 4.721   1.00 48.88  ? 839  ARG   B CA  1 
ATOM   3151 C C   . ARG   B 1 146 ? 33.192 -15.529 4.608   1.00 50.10  ? 839  ARG   B C   1 
ATOM   3152 O O   . ARG   B 1 146 ? 33.704 -15.457 3.488   1.00 51.34  ? 839  ARG   B O   1 
ATOM   3153 C CB  . ARG   B 1 146 ? 31.005 -14.358 4.202   1.00 50.52  ? 839  ARG   B CB  1 
ATOM   3154 C CG  . ARG   B 1 146 ? 29.530 -14.461 3.871   1.00 54.46  ? 839  ARG   B CG  1 
ATOM   3155 C CD  . ARG   B 1 146 ? 29.040 -13.111 3.387   1.00 58.93  ? 839  ARG   B CD  1 
ATOM   3156 N NE  . ARG   B 1 146 ? 27.727 -13.177 2.747   1.00 64.70  ? 839  ARG   B NE  1 
ATOM   3157 C CZ  . ARG   B 1 146 ? 27.465 -12.706 1.523   1.00 69.56  ? 839  ARG   B CZ  1 
ATOM   3158 N NH1 . ARG   B 1 146 ? 26.243 -12.806 1.012   1.00 69.86  ? 839  ARG   B NH1 1 
ATOM   3159 N NH2 . ARG   B 1 146 ? 28.428 -12.148 0.797   1.00 70.30  ? 839  ARG   B NH2 1 
ATOM   3160 N N   . ASP   B 1 147 ? 33.921 -15.522 5.729   1.00 49.72  ? 840  ASP   B N   1 
ATOM   3161 C CA  . ASP   B 1 147 ? 35.373 -15.405 5.674   1.00 50.09  ? 840  ASP   B CA  1 
ATOM   3162 C C   . ASP   B 1 147 ? 36.087 -16.190 6.779   1.00 48.57  ? 840  ASP   B C   1 
ATOM   3163 O O   . ASP   B 1 147 ? 36.974 -15.649 7.432   1.00 49.16  ? 840  ASP   B O   1 
ATOM   3164 C CB  . ASP   B 1 147 ? 35.795 -13.922 5.658   1.00 54.05  ? 840  ASP   B CB  1 
ATOM   3165 C CG  . ASP   B 1 147 ? 37.250 -13.662 5.274   1.00 62.51  ? 840  ASP   B CG  1 
ATOM   3166 O OD1 . ASP   B 1 147 ? 37.871 -14.555 4.645   1.00 63.38  ? 840  ASP   B OD1 1 
ATOM   3167 O OD2 . ASP   B 1 147 ? 37.777 -12.576 5.632   1.00 66.55  ? 840  ASP   B OD2 1 
ATOM   3168 N N   . LEU   B 1 148 ? 35.706 -17.449 6.999   1.00 46.58  ? 841  LEU   B N   1 
ATOM   3169 C CA  . LEU   B 1 148 ? 36.392 -18.264 7.999   1.00 45.74  ? 841  LEU   B CA  1 
ATOM   3170 C C   . LEU   B 1 148 ? 37.762 -18.670 7.418   1.00 45.19  ? 841  LEU   B C   1 
ATOM   3171 O O   . LEU   B 1 148 ? 37.844 -19.155 6.291   1.00 45.59  ? 841  LEU   B O   1 
ATOM   3172 C CB  . LEU   B 1 148 ? 35.578 -19.500 8.385   1.00 45.88  ? 841  LEU   B CB  1 
ATOM   3173 C CG  . LEU   B 1 148 ? 36.279 -20.434 9.378   1.00 47.73  ? 841  LEU   B CG  1 
ATOM   3174 C CD1 . LEU   B 1 148 ? 36.582 -19.721 10.717  1.00 48.16  ? 841  LEU   B CD1 1 
ATOM   3175 C CD2 . LEU   B 1 148 ? 35.481 -21.672 9.607   1.00 48.07  ? 841  LEU   B CD2 1 
ATOM   3176 N N   . ALA   B 1 149 ? 38.829 -18.401 8.152   1.00 43.83  ? 842  ALA   B N   1 
ATOM   3177 C CA  . ALA   B 1 149 ? 40.206 -18.719 7.791   1.00 42.89  ? 842  ALA   B CA  1 
ATOM   3178 C C   . ALA   B 1 149 ? 41.033 -18.756 9.085   1.00 43.01  ? 842  ALA   B C   1 
ATOM   3179 O O   . ALA   B 1 149 ? 40.590 -18.209 10.094  1.00 42.71  ? 842  ALA   B O   1 
ATOM   3180 C CB  . ALA   B 1 149 ? 40.747 -17.680 6.836   1.00 42.24  ? 842  ALA   B CB  1 
ATOM   3181 N N   . ALA   B 1 150 ? 42.217 -19.391 9.084   1.00 43.36  ? 843  ALA   B N   1 
ATOM   3182 C CA  . ALA   B 1 150 ? 43.048 -19.439 10.302  1.00 43.94  ? 843  ALA   B CA  1 
ATOM   3183 C C   . ALA   B 1 150 ? 43.478 -18.027 10.761  1.00 44.41  ? 843  ALA   B C   1 
ATOM   3184 O O   . ALA   B 1 150 ? 43.716 -17.819 11.952  1.00 44.85  ? 843  ALA   B O   1 
ATOM   3185 C CB  . ALA   B 1 150 ? 44.250 -20.362 10.122  1.00 43.99  ? 843  ALA   B CB  1 
ATOM   3186 N N   . ARG   B 1 151 ? 43.509 -17.048 9.841   1.00 44.15  ? 844  ARG   B N   1 
ATOM   3187 C CA  . ARG   B 1 151 ? 43.806 -15.662 10.203  1.00 44.53  ? 844  ARG   B CA  1 
ATOM   3188 C C   . ARG   B 1 151 ? 42.628 -15.015 11.003  1.00 44.66  ? 844  ARG   B C   1 
ATOM   3189 O O   . ARG   B 1 151 ? 42.832 -14.028 11.707  1.00 45.78  ? 844  ARG   B O   1 
ATOM   3190 C CB  . ARG   B 1 151 ? 44.132 -14.832 8.954   1.00 45.60  ? 844  ARG   B CB  1 
ATOM   3191 C CG  . ARG   B 1 151 ? 42.925 -14.652 8.052   1.00 48.71  ? 844  ARG   B CG  1 
ATOM   3192 C CD  . ARG   B 1 151 ? 43.168 -13.745 6.848   1.00 52.94  ? 844  ARG   B CD  1 
ATOM   3193 N NE  . ARG   B 1 151 ? 42.037 -13.830 5.929   1.00 58.47  ? 844  ARG   B NE  1 
ATOM   3194 C CZ  . ARG   B 1 151 ? 41.916 -14.754 4.974   1.00 64.40  ? 844  ARG   B CZ  1 
ATOM   3195 N NH1 . ARG   B 1 151 ? 40.826 -14.797 4.219   1.00 65.34  ? 844  ARG   B NH1 1 
ATOM   3196 N NH2 . ARG   B 1 151 ? 42.883 -15.644 4.770   1.00 65.52  ? 844  ARG   B NH2 1 
ATOM   3197 N N   . ASN   B 1 152 ? 41.413 -15.569 10.891  1.00 43.57  ? 845  ASN   B N   1 
ATOM   3198 C CA  . ASN   B 1 152 ? 40.222 -15.094 11.589  1.00 43.16  ? 845  ASN   B CA  1 
ATOM   3199 C C   . ASN   B 1 152 ? 39.869 -15.909 12.824  1.00 42.68  ? 845  ASN   B C   1 
ATOM   3200 O O   . ASN   B 1 152 ? 38.732 -15.861 13.285  1.00 43.28  ? 845  ASN   B O   1 
ATOM   3201 C CB  . ASN   B 1 152 ? 39.025 -14.984 10.641  1.00 44.83  ? 845  ASN   B CB  1 
ATOM   3202 C CG  . ASN   B 1 152 ? 39.141 -13.813 9.686   1.00 48.49  ? 845  ASN   B CG  1 
ATOM   3203 O OD1 . ASN   B 1 152 ? 39.983 -12.919 9.854   1.00 50.43  ? 845  ASN   B OD1 1 
ATOM   3204 N ND2 . ASN   B 1 152 ? 38.296 -13.726 8.706   1.00 48.59  ? 845  ASN   B ND2 1 
ATOM   3205 N N   . VAL   B 1 153 ? 40.828 -16.681 13.340  1.00 41.23  ? 846  VAL   B N   1 
ATOM   3206 C CA  . VAL   B 1 153 ? 40.680 -17.428 14.565  1.00 40.55  ? 846  VAL   B CA  1 
ATOM   3207 C C   . VAL   B 1 153 ? 41.739 -16.836 15.475  1.00 40.78  ? 846  VAL   B C   1 
ATOM   3208 O O   . VAL   B 1 153 ? 42.909 -16.800 15.110  1.00 40.75  ? 846  VAL   B O   1 
ATOM   3209 C CB  . VAL   B 1 153 ? 40.896 -18.936 14.383  1.00 39.93  ? 846  VAL   B CB  1 
ATOM   3210 C CG1 . VAL   B 1 153 ? 40.778 -19.654 15.718  1.00 38.89  ? 846  VAL   B CG1 1 
ATOM   3211 C CG2 . VAL   B 1 153 ? 39.927 -19.505 13.353  1.00 40.18  ? 846  VAL   B CG2 1 
ATOM   3212 N N   . LEU   B 1 154 ? 41.331 -16.294 16.607  1.00 40.69  ? 847  LEU   B N   1 
ATOM   3213 C CA  . LEU   B 1 154 ? 42.245 -15.656 17.539  1.00 40.99  ? 847  LEU   B CA  1 
ATOM   3214 C C   . LEU   B 1 154 ? 42.543 -16.567 18.715  1.00 41.14  ? 847  LEU   B C   1 
ATOM   3215 O O   . LEU   B 1 154 ? 41.747 -17.428 19.075  1.00 40.75  ? 847  LEU   B O   1 
ATOM   3216 C CB  . LEU   B 1 154 ? 41.665 -14.328 18.011  1.00 41.48  ? 847  LEU   B CB  1 
ATOM   3217 C CG  . LEU   B 1 154 ? 41.170 -13.402 16.908  1.00 44.15  ? 847  LEU   B CG  1 
ATOM   3218 C CD1 . LEU   B 1 154 ? 40.540 -12.183 17.492  1.00 46.30  ? 847  LEU   B CD1 1 
ATOM   3219 C CD2 . LEU   B 1 154 ? 42.287 -13.005 15.966  1.00 44.56  ? 847  LEU   B CD2 1 
ATOM   3220 N N   . VAL   B 1 155 ? 43.698 -16.379 19.305  1.00 41.19  ? 848  VAL   B N   1 
ATOM   3221 C CA  . VAL   B 1 155 ? 44.163 -17.181 20.409  1.00 41.40  ? 848  VAL   B CA  1 
ATOM   3222 C C   . VAL   B 1 155 ? 44.077 -16.372 21.691  1.00 43.12  ? 848  VAL   B C   1 
ATOM   3223 O O   . VAL   B 1 155 ? 44.848 -15.436 21.887  1.00 43.07  ? 848  VAL   B O   1 
ATOM   3224 C CB  . VAL   B 1 155 ? 45.607 -17.651 20.116  1.00 40.98  ? 848  VAL   B CB  1 
ATOM   3225 C CG1 . VAL   B 1 155 ? 46.156 -18.501 21.242  1.00 41.19  ? 848  VAL   B CG1 1 
ATOM   3226 C CG2 . VAL   B 1 155 ? 45.676 -18.403 18.797  1.00 41.00  ? 848  VAL   B CG2 1 
ATOM   3227 N N   . LYS   B 1 156 ? 43.119 -16.717 22.558  1.00 44.54  ? 849  LYS   B N   1 
ATOM   3228 C CA  . LYS   B 1 156 ? 42.994 -16.078 23.865  1.00 45.77  ? 849  LYS   B CA  1 
ATOM   3229 C C   . LYS   B 1 156 ? 44.126 -16.664 24.705  1.00 46.69  ? 849  LYS   B C   1 
ATOM   3230 O O   . LYS   B 1 156 ? 44.946 -15.922 25.248  1.00 47.59  ? 849  LYS   B O   1 
ATOM   3231 C CB  . LYS   B 1 156 ? 41.613 -16.350 24.492  1.00 47.95  ? 849  LYS   B CB  1 
ATOM   3232 C CG  . LYS   B 1 156 ? 41.389 -15.567 25.777  1.00 51.67  ? 849  LYS   B CG  1 
ATOM   3233 C CD  . LYS   B 1 156 ? 39.970 -15.689 26.273  1.00 55.97  ? 849  LYS   B CD  1 
ATOM   3234 C CE  . LYS   B 1 156 ? 39.756 -14.884 27.529  1.00 59.47  ? 849  LYS   B CE  1 
ATOM   3235 N N   . THR   B 1 157 ? 44.206 -17.992 24.756  1.00 46.20  ? 850  THR   B N   1 
ATOM   3236 C CA  . THR   B 1 157 ? 45.270 -18.771 25.376  1.00 46.68  ? 850  THR   B CA  1 
ATOM   3237 C C   . THR   B 1 157 ? 45.518 -19.961 24.426  1.00 47.04  ? 850  THR   B C   1 
ATOM   3238 O O   . THR   B 1 157 ? 44.642 -20.301 23.617  1.00 47.10  ? 850  THR   B O   1 
ATOM   3239 C CB  . THR   B 1 157 ? 44.912 -19.220 26.821  1.00 47.45  ? 850  THR   B CB  1 
ATOM   3240 O OG1 . THR   B 1 157 ? 43.782 -20.086 26.820  1.00 47.90  ? 850  THR   B OG1 1 
ATOM   3241 C CG2 . THR   B 1 157 ? 44.691 -18.049 27.776  1.00 47.51  ? 850  THR   B CG2 1 
ATOM   3242 N N   . PRO   B 1 158 ? 46.686 -20.631 24.498  1.00 46.54  ? 851  PRO   B N   1 
ATOM   3243 C CA  . PRO   B 1 158 ? 46.924 -21.778 23.595  1.00 45.68  ? 851  PRO   B CA  1 
ATOM   3244 C C   . PRO   B 1 158 ? 45.827 -22.842 23.623  1.00 45.25  ? 851  PRO   B C   1 
ATOM   3245 O O   . PRO   B 1 158 ? 45.626 -23.530 22.625  1.00 45.62  ? 851  PRO   B O   1 
ATOM   3246 C CB  . PRO   B 1 158 ? 48.261 -22.344 24.072  1.00 46.02  ? 851  PRO   B CB  1 
ATOM   3247 C CG  . PRO   B 1 158 ? 48.929 -21.180 24.735  1.00 46.84  ? 851  PRO   B CG  1 
ATOM   3248 C CD  . PRO   B 1 158 ? 47.853 -20.360 25.361  1.00 45.61  ? 851  PRO   B CD  1 
ATOM   3249 N N   . GLN   B 1 159 ? 45.091 -22.952 24.739  1.00 44.19  ? 852  GLN   B N   1 
ATOM   3250 C CA  . GLN   B 1 159 ? 44.035 -23.946 24.829  1.00 43.59  ? 852  GLN   B CA  1 
ATOM   3251 C C   . GLN   B 1 159 ? 42.598 -23.340 24.669  1.00 43.06  ? 852  GLN   B C   1 
ATOM   3252 O O   . GLN   B 1 159 ? 41.602 -24.011 24.954  1.00 43.27  ? 852  GLN   B O   1 
ATOM   3253 C CB  . GLN   B 1 159 ? 44.191 -24.807 26.106  1.00 44.75  ? 852  GLN   B CB  1 
ATOM   3254 C CG  . GLN   B 1 159 ? 44.533 -24.081 27.384  1.00 48.50  ? 852  GLN   B CG  1 
ATOM   3255 C CD  . GLN   B 1 159 ? 45.992 -23.674 27.568  1.00 52.10  ? 852  GLN   B CD  1 
ATOM   3256 O OE1 . GLN   B 1 159 ? 46.280 -22.561 28.008  1.00 52.86  ? 852  GLN   B OE1 1 
ATOM   3257 N NE2 . GLN   B 1 159 ? 46.940 -24.549 27.252  1.00 51.49  ? 852  GLN   B NE2 1 
ATOM   3258 N N   . HIS   B 1 160 ? 42.492 -22.116 24.133  1.00 41.92  ? 853  HIS   B N   1 
ATOM   3259 C CA  . HIS   B 1 160 ? 41.205 -21.447 23.969  1.00 41.35  ? 853  HIS   B CA  1 
ATOM   3260 C C   . HIS   B 1 160 ? 41.236 -20.464 22.783  1.00 40.37  ? 853  HIS   B C   1 
ATOM   3261 O O   . HIS   B 1 160 ? 41.841 -19.389 22.861  1.00 40.07  ? 853  HIS   B O   1 
ATOM   3262 C CB  . HIS   B 1 160 ? 40.820 -20.766 25.301  1.00 42.29  ? 853  HIS   B CB  1 
ATOM   3263 C CG  . HIS   B 1 160 ? 39.546 -19.973 25.304  1.00 44.20  ? 853  HIS   B CG  1 
ATOM   3264 N ND1 . HIS   B 1 160 ? 38.686 -19.952 24.217  1.00 45.93  ? 853  HIS   B ND1 1 
ATOM   3265 C CD2 . HIS   B 1 160 ? 39.023 -19.204 26.284  1.00 45.00  ? 853  HIS   B CD2 1 
ATOM   3266 C CE1 . HIS   B 1 160 ? 37.687 -19.168 24.569  1.00 45.98  ? 853  HIS   B CE1 1 
ATOM   3267 N NE2 . HIS   B 1 160 ? 37.842 -18.706 25.809  1.00 46.18  ? 853  HIS   B NE2 1 
ATOM   3268 N N   . VAL   B 1 161 ? 40.602 -20.858 21.668  1.00 39.34  ? 854  VAL   B N   1 
ATOM   3269 C CA  . VAL   B 1 161 ? 40.568 -20.022 20.480  1.00 39.07  ? 854  VAL   B CA  1 
ATOM   3270 C C   . VAL   B 1 161 ? 39.145 -19.506 20.185  1.00 39.64  ? 854  VAL   B C   1 
ATOM   3271 O O   . VAL   B 1 161 ? 38.154 -20.104 20.600  1.00 39.81  ? 854  VAL   B O   1 
ATOM   3272 C CB  . VAL   B 1 161 ? 41.242 -20.679 19.245  1.00 38.98  ? 854  VAL   B CB  1 
ATOM   3273 C CG1 . VAL   B 1 161 ? 42.675 -21.101 19.563  1.00 38.73  ? 854  VAL   B CG1 1 
ATOM   3274 C CG2 . VAL   B 1 161 ? 40.419 -21.850 18.697  1.00 38.89  ? 854  VAL   B CG2 1 
ATOM   3275 N N   . LYS   B 1 162 ? 39.052 -18.373 19.500  1.00 39.80  ? 855  LYS   B N   1 
ATOM   3276 C CA  . LYS   B 1 162 ? 37.782 -17.728 19.202  1.00 40.78  ? 855  LYS   B CA  1 
ATOM   3277 C C   . LYS   B 1 162 ? 37.726 -17.266 17.755  1.00 41.54  ? 855  LYS   B C   1 
ATOM   3278 O O   . LYS   B 1 162 ? 38.701 -16.740 17.248  1.00 41.60  ? 855  LYS   B O   1 
ATOM   3279 C CB  . LYS   B 1 162 ? 37.649 -16.487 20.087  1.00 43.28  ? 855  LYS   B CB  1 
ATOM   3280 C CG  . LYS   B 1 162 ? 37.270 -16.759 21.517  1.00 47.64  ? 855  LYS   B CG  1 
ATOM   3281 C CD  . LYS   B 1 162 ? 37.588 -15.554 22.380  1.00 53.33  ? 855  LYS   B CD  1 
ATOM   3282 C CE  . LYS   B 1 162 ? 36.740 -15.480 23.624  1.00 58.42  ? 855  LYS   B CE  1 
ATOM   3283 N NZ  . LYS   B 1 162 ? 35.327 -15.139 23.295  1.00 61.40  ? 855  LYS   B NZ  1 
ATOM   3284 N N   . ILE   B 1 163 ? 36.571 -17.366 17.119  1.00 42.18  ? 856  ILE   B N   1 
ATOM   3285 C CA  . ILE   B 1 163 ? 36.381 -16.897 15.752  1.00 43.07  ? 856  ILE   B CA  1 
ATOM   3286 C C   . ILE   B 1 163 ? 36.023 -15.423 15.745  1.00 43.76  ? 856  ILE   B C   1 
ATOM   3287 O O   . ILE   B 1 163 ? 35.148 -14.991 16.493  1.00 43.87  ? 856  ILE   B O   1 
ATOM   3288 C CB  . ILE   B 1 163 ? 35.282 -17.731 15.081  1.00 43.88  ? 856  ILE   B CB  1 
ATOM   3289 C CG1 . ILE   B 1 163 ? 35.685 -19.195 15.048  1.00 44.71  ? 856  ILE   B CG1 1 
ATOM   3290 C CG2 . ILE   B 1 163 ? 34.939 -17.199 13.669  1.00 44.55  ? 856  ILE   B CG2 1 
ATOM   3291 C CD1 . ILE   B 1 163 ? 34.577 -20.010 14.907  1.00 46.43  ? 856  ILE   B CD1 1 
ATOM   3292 N N   . THR   B 1 164 ? 36.684 -14.656 14.887  1.00 44.41  ? 857  THR   B N   1 
ATOM   3293 C CA  . THR   B 1 164 ? 36.443 -13.221 14.746  1.00 45.48  ? 857  THR   B CA  1 
ATOM   3294 C C   . THR   B 1 164 ? 35.986 -12.877 13.317  1.00 46.58  ? 857  THR   B C   1 
ATOM   3295 O O   . THR   B 1 164 ? 35.950 -13.756 12.470  1.00 46.70  ? 857  THR   B O   1 
ATOM   3296 C CB  . THR   B 1 164 ? 37.718 -12.447 15.148  1.00 46.59  ? 857  THR   B CB  1 
ATOM   3297 O OG1 . THR   B 1 164 ? 37.401 -11.066 15.176  1.00 48.12  ? 857  THR   B OG1 1 
ATOM   3298 C CG2 . THR   B 1 164 ? 38.837 -12.627 14.160  1.00 46.80  ? 857  THR   B CG2 1 
ATOM   3299 N N   . ASP   B 1 165 ? 35.623 -11.598 13.056  1.00 47.52  ? 858  ASP   B N   1 
ATOM   3300 C CA  . ASP   B 1 165 ? 35.234 -11.039 11.757  1.00 48.28  ? 858  ASP   B CA  1 
ATOM   3301 C C   . ASP   B 1 165 ? 33.932 -11.578 11.200  1.00 48.45  ? 858  ASP   B C   1 
ATOM   3302 O O   . ASP   B 1 165 ? 33.717 -11.454 9.999   1.00 48.66  ? 858  ASP   B O   1 
ATOM   3303 C CB  . ASP   B 1 165 ? 36.355 -11.166 10.711  1.00 50.87  ? 858  ASP   B CB  1 
ATOM   3304 C CG  . ASP   B 1 165 ? 37.503 -10.193 10.902  1.00 58.32  ? 858  ASP   B CG  1 
ATOM   3305 O OD1 . ASP   B 1 165 ? 37.753 -9.779  12.062  1.00 59.10  ? 858  ASP   B OD1 1 
ATOM   3306 O OD2 . ASP   B 1 165 ? 38.165 -9.855  9.895   1.00 62.48  ? 858  ASP   B OD2 1 
ATOM   3307 N N   . PHE   B 1 166 ? 33.062 -12.155 12.042  1.00 48.62  ? 859  PHE   B N   1 
ATOM   3308 C CA  . PHE   B 1 166 ? 31.755 -12.596 11.560  1.00 49.55  ? 859  PHE   B CA  1 
ATOM   3309 C C   . PHE   B 1 166 ? 30.897 -11.340 11.316  1.00 50.57  ? 859  PHE   B C   1 
ATOM   3310 O O   . PHE   B 1 166 ? 30.969 -10.364 12.069  1.00 50.10  ? 859  PHE   B O   1 
ATOM   3311 C CB  . PHE   B 1 166 ? 31.076 -13.563 12.550  1.00 49.43  ? 859  PHE   B CB  1 
ATOM   3312 C CG  . PHE   B 1 166 ? 31.031 -13.082 13.990  1.00 49.66  ? 859  PHE   B CG  1 
ATOM   3313 C CD1 . PHE   B 1 166 ? 29.982 -12.289 14.447  1.00 50.22  ? 859  PHE   B CD1 1 
ATOM   3314 C CD2 . PHE   B 1 166 ? 32.004 -13.467 14.892  1.00 50.05  ? 859  PHE   B CD2 1 
ATOM   3315 C CE1 . PHE   B 1 166 ? 29.949 -11.840 15.753  1.00 51.01  ? 859  PHE   B CE1 1 
ATOM   3316 C CE2 . PHE   B 1 166 ? 31.967 -13.017 16.201  1.00 50.75  ? 859  PHE   B CE2 1 
ATOM   3317 C CZ  . PHE   B 1 166 ? 30.928 -12.227 16.629  1.00 50.91  ? 859  PHE   B CZ  1 
ATOM   3318 N N   . GLY   B 1 167 ? 30.129 -11.360 10.238  1.00 51.72  ? 860  GLY   B N   1 
ATOM   3319 C CA  . GLY   B 1 167 ? 29.275 -10.238 9.868   1.00 52.94  ? 860  GLY   B CA  1 
ATOM   3320 C C   . GLY   B 1 167 ? 29.983 -9.049  9.239   1.00 54.23  ? 860  GLY   B C   1 
ATOM   3321 O O   . GLY   B 1 167 ? 29.324 -8.118  8.763   1.00 54.15  ? 860  GLY   B O   1 
ATOM   3322 N N   . LEU   B 1 168 ? 31.329 -9.063  9.233   1.00 55.01  ? 861  LEU   B N   1 
ATOM   3323 C CA  . LEU   B 1 168 ? 32.146 -7.979  8.694   1.00 55.99  ? 861  LEU   B CA  1 
ATOM   3324 C C   . LEU   B 1 168 ? 31.991 -7.868  7.182   1.00 58.11  ? 861  LEU   B C   1 
ATOM   3325 O O   . LEU   B 1 168 ? 31.881 -6.757  6.668   1.00 58.41  ? 861  LEU   B O   1 
ATOM   3326 C CB  . LEU   B 1 168 ? 33.624 -8.175  9.074   1.00 55.31  ? 861  LEU   B CB  1 
ATOM   3327 C CG  . LEU   B 1 168 ? 34.570 -7.055  8.671   1.00 55.81  ? 861  LEU   B CG  1 
ATOM   3328 C CD1 . LEU   B 1 168 ? 34.144 -5.720  9.268   1.00 55.94  ? 861  LEU   B CD1 1 
ATOM   3329 C CD2 . LEU   B 1 168 ? 35.965 -7.369  9.081   1.00 56.21  ? 861  LEU   B CD2 1 
ATOM   3330 N N   . ALA   B 1 169 ? 31.944 -9.013  6.472   1.00 59.23  ? 862  ALA   B N   1 
ATOM   3331 C CA  . ALA   B 1 169 ? 31.750 -9.042  5.023   1.00 60.63  ? 862  ALA   B CA  1 
ATOM   3332 C C   . ALA   B 1 169 ? 30.419 -8.386  4.649   1.00 62.03  ? 862  ALA   B C   1 
ATOM   3333 O O   . ALA   B 1 169 ? 30.406 -7.535  3.773   1.00 62.43  ? 862  ALA   B O   1 
ATOM   3334 C CB  . ALA   B 1 169 ? 31.795 -10.477 4.511   1.00 60.82  ? 862  ALA   B CB  1 
ATOM   3335 N N   . LYS   B 1 170 ? 29.323 -8.704  5.371   1.00 62.87  ? 863  LYS   B N   1 
ATOM   3336 C CA  . LYS   B 1 170 ? 27.999 -8.115  5.132   1.00 63.85  ? 863  LYS   B CA  1 
ATOM   3337 C C   . LYS   B 1 170 ? 28.008 -6.609  5.385   1.00 64.63  ? 863  LYS   B C   1 
ATOM   3338 O O   . LYS   B 1 170 ? 27.369 -5.868  4.654   1.00 64.89  ? 863  LYS   B O   1 
ATOM   3339 C CB  . LYS   B 1 170 ? 26.924 -8.803  5.992   1.00 65.75  ? 863  LYS   B CB  1 
ATOM   3340 C CG  . LYS   B 1 170 ? 25.505 -8.583  5.478   1.00 70.10  ? 863  LYS   B CG  1 
ATOM   3341 C CD  . LYS   B 1 170 ? 24.453 -9.085  6.458   1.00 74.38  ? 863  LYS   B CD  1 
ATOM   3342 N N   . LEU   B 1 171 ? 28.756 -6.154  6.393   1.00 65.17  ? 864  LEU   B N   1 
ATOM   3343 C CA  . LEU   B 1 171 ? 28.915 -4.739  6.715   1.00 66.28  ? 864  LEU   B CA  1 
ATOM   3344 C C   . LEU   B 1 171 ? 29.674 -4.009  5.584   1.00 67.81  ? 864  LEU   B C   1 
ATOM   3345 O O   . LEU   B 1 171 ? 29.354 -2.864  5.277   1.00 67.88  ? 864  LEU   B O   1 
ATOM   3346 C CB  . LEU   B 1 171 ? 29.645 -4.616  8.062   1.00 66.63  ? 864  LEU   B CB  1 
ATOM   3347 C CG  . LEU   B 1 171 ? 30.303 -3.282  8.424   1.00 68.22  ? 864  LEU   B CG  1 
ATOM   3348 C CD1 . LEU   B 1 171 ? 29.274 -2.216  8.612   1.00 68.89  ? 864  LEU   B CD1 1 
ATOM   3349 C CD2 . LEU   B 1 171 ? 31.121 -3.415  9.680   1.00 68.82  ? 864  LEU   B CD2 1 
ATOM   3350 N N   . LEU   B 1 172 ? 30.619 -4.694  4.920   1.00 68.99  ? 865  LEU   B N   1 
ATOM   3351 C CA  . LEU   B 1 172 ? 31.405 -4.136  3.819   1.00 70.67  ? 865  LEU   B CA  1 
ATOM   3352 C C   . LEU   B 1 172 ? 30.760 -4.272  2.435   1.00 73.04  ? 865  LEU   B C   1 
ATOM   3353 O O   . LEU   B 1 172 ? 31.464 -4.275  1.427   1.00 73.15  ? 865  LEU   B O   1 
ATOM   3354 C CB  . LEU   B 1 172 ? 32.808 -4.748  3.817   1.00 70.57  ? 865  LEU   B CB  1 
ATOM   3355 C CG  . LEU   B 1 172 ? 33.599 -4.478  5.091   1.00 71.69  ? 865  LEU   B CG  1 
ATOM   3356 C CD1 . LEU   B 1 172 ? 34.842 -5.342  5.172   1.00 71.96  ? 865  LEU   B CD1 1 
ATOM   3357 C CD2 . LEU   B 1 172 ? 33.903 -2.999  5.243   1.00 72.08  ? 865  LEU   B CD2 1 
ATOM   3358 N N   . GLY   B 1 173 ? 29.438 -4.386  2.402   1.00 74.69  ? 866  GLY   B N   1 
ATOM   3359 C CA  . GLY   B 1 173 ? 28.668 -4.470  1.167   1.00 76.67  ? 866  GLY   B CA  1 
ATOM   3360 C C   . GLY   B 1 173 ? 28.807 -5.738  0.348   1.00 78.96  ? 866  GLY   B C   1 
ATOM   3361 O O   . GLY   B 1 173 ? 28.511 -5.723  -0.853  1.00 79.58  ? 866  GLY   B O   1 
ATOM   3362 N N   . ALA   B 1 174 ? 29.212 -6.858  0.976   1.00 80.03  ? 867  ALA   B N   1 
ATOM   3363 C CA  . ALA   B 1 174 ? 29.351 -8.120  0.241   1.00 81.51  ? 867  ALA   B CA  1 
ATOM   3364 C C   . ALA   B 1 174 ? 28.001 -8.675  -0.232  1.00 83.00  ? 867  ALA   B C   1 
ATOM   3365 O O   . ALA   B 1 174 ? 27.943 -9.302  -1.288  1.00 83.32  ? 867  ALA   B O   1 
ATOM   3366 C CB  . ALA   B 1 174 ? 30.104 -9.155  1.067   1.00 81.52  ? 867  ALA   B CB  1 
ATOM   3367 N N   . GLU   B 1 175 ? 26.916 -8.426  0.520   1.00 83.79  ? 868  GLU   B N   1 
ATOM   3368 C CA  . GLU   B 1 175 ? 25.587 -8.892  0.107   1.00 85.07  ? 868  GLU   B CA  1 
ATOM   3369 C C   . GLU   B 1 175 ? 24.837 -7.892  -0.802  1.00 86.43  ? 868  GLU   B C   1 
ATOM   3370 O O   . GLU   B 1 175 ? 23.724 -8.184  -1.236  1.00 86.88  ? 868  GLU   B O   1 
ATOM   3371 C CB  . GLU   B 1 175 ? 24.730 -9.287  1.319   1.00 87.06  ? 868  GLU   B CB  1 
ATOM   3372 N N   . GLU   B 1 176 ? 25.440 -6.729  -1.108  1.00 86.92  ? 869  GLU   B N   1 
ATOM   3373 C CA  . GLU   B 1 176 ? 24.814 -5.733  -1.970  1.00 87.87  ? 869  GLU   B CA  1 
ATOM   3374 C C   . GLU   B 1 176 ? 25.256 -5.927  -3.426  1.00 89.06  ? 869  GLU   B C   1 
ATOM   3375 O O   . GLU   B 1 176 ? 26.440 -6.149  -3.679  1.00 89.23  ? 869  GLU   B O   1 
ATOM   3376 C CB  . GLU   B 1 176 ? 25.161 -4.318  -1.483  1.00 89.67  ? 869  GLU   B CB  1 
ATOM   3377 N N   . LYS   B 1 177 ? 24.300 -5.842  -4.376  1.00 89.70  ? 870  LYS   B N   1 
ATOM   3378 C CA  . LYS   B 1 177 ? 24.512 -5.983  -5.825  1.00 90.47  ? 870  LYS   B CA  1 
ATOM   3379 C C   . LYS   B 1 177 ? 25.401 -7.176  -6.201  1.00 91.21  ? 870  LYS   B C   1 
ATOM   3380 O O   . LYS   B 1 177 ? 26.457 -7.003  -6.811  1.00 91.50  ? 870  LYS   B O   1 
ATOM   3381 C CB  . LYS   B 1 177 ? 25.038 -4.674  -6.444  1.00 92.00  ? 870  LYS   B CB  1 
ATOM   3382 N N   . GLY   B 1 184 ? 40.965 -4.120  -2.445  1.00 73.27  ? 877  GLY   B N   1 
ATOM   3383 C CA  . GLY   B 1 184 ? 40.246 -5.203  -1.786  1.00 73.84  ? 877  GLY   B CA  1 
ATOM   3384 C C   . GLY   B 1 184 ? 40.590 -6.573  -2.340  1.00 73.79  ? 877  GLY   B C   1 
ATOM   3385 O O   . GLY   B 1 184 ? 40.597 -6.762  -3.562  1.00 74.17  ? 877  GLY   B O   1 
ATOM   3386 N N   . LYS   B 1 185 ? 40.871 -7.543  -1.448  1.00 72.97  ? 878  LYS   B N   1 
ATOM   3387 C CA  . LYS   B 1 185 ? 41.233 -8.900  -1.863  1.00 72.67  ? 878  LYS   B CA  1 
ATOM   3388 C C   . LYS   B 1 185 ? 40.193 -9.959  -1.451  1.00 71.57  ? 878  LYS   B C   1 
ATOM   3389 O O   . LYS   B 1 185 ? 39.968 -10.178 -0.263  1.00 71.21  ? 878  LYS   B O   1 
ATOM   3390 C CB  . LYS   B 1 185 ? 42.622 -9.277  -1.326  1.00 74.68  ? 878  LYS   B CB  1 
ATOM   3391 N N   . VAL   B 1 186 ? 39.565 -10.612 -2.444  1.00 70.49  ? 879  VAL   B N   1 
ATOM   3392 C CA  . VAL   B 1 186 ? 38.560 -11.661 -2.226  1.00 69.61  ? 879  VAL   B CA  1 
ATOM   3393 C C   . VAL   B 1 186 ? 39.272 -12.975 -1.865  1.00 67.73  ? 879  VAL   B C   1 
ATOM   3394 O O   . VAL   B 1 186 ? 40.285 -13.313 -2.488  1.00 68.30  ? 879  VAL   B O   1 
ATOM   3395 C CB  . VAL   B 1 186 ? 37.621 -11.773 -3.464  1.00 70.82  ? 879  VAL   B CB  1 
ATOM   3396 C CG1 . VAL   B 1 186 ? 38.401 -11.864 -4.774  1.00 71.40  ? 879  VAL   B CG1 1 
ATOM   3397 C CG2 . VAL   B 1 186 ? 36.605 -12.896 -3.331  1.00 71.34  ? 879  VAL   B CG2 1 
ATOM   3398 N N   . PRO   B 1 187 ? 38.833 -13.694 -0.808  1.00 65.33  ? 880  PRO   B N   1 
ATOM   3399 C CA  . PRO   B 1 187 ? 39.566 -14.910 -0.401  1.00 63.45  ? 880  PRO   B CA  1 
ATOM   3400 C C   . PRO   B 1 187 ? 39.174 -16.168 -1.177  1.00 61.01  ? 880  PRO   B C   1 
ATOM   3401 O O   . PRO   B 1 187 ? 38.673 -17.123 -0.593  1.00 60.84  ? 880  PRO   B O   1 
ATOM   3402 C CB  . PRO   B 1 187 ? 39.244 -15.021 1.084   1.00 64.12  ? 880  PRO   B CB  1 
ATOM   3403 C CG  . PRO   B 1 187 ? 37.877 -14.403 1.213   1.00 64.92  ? 880  PRO   B CG  1 
ATOM   3404 C CD  . PRO   B 1 187 ? 37.680 -13.432 0.079   1.00 64.05  ? 880  PRO   B CD  1 
ATOM   3405 N N   . ILE   B 1 188 ? 39.431 -16.163 -2.490  1.00 59.03  ? 881  ILE   B N   1 
ATOM   3406 C CA  . ILE   B 1 188 ? 39.122 -17.238 -3.435  1.00 57.72  ? 881  ILE   B CA  1 
ATOM   3407 C C   . ILE   B 1 188 ? 39.599 -18.626 -2.976  1.00 55.50  ? 881  ILE   B C   1 
ATOM   3408 O O   . ILE   B 1 188 ? 38.857 -19.605 -3.098  1.00 55.43  ? 881  ILE   B O   1 
ATOM   3409 C CB  . ILE   B 1 188 ? 39.682 -16.876 -4.836  1.00 58.41  ? 881  ILE   B CB  1 
ATOM   3410 C CG1 . ILE   B 1 188 ? 39.203 -15.479 -5.299  1.00 59.25  ? 881  ILE   B CG1 1 
ATOM   3411 C CG2 . ILE   B 1 188 ? 39.349 -17.955 -5.868  1.00 58.97  ? 881  ILE   B CG2 1 
ATOM   3412 C CD1 . ILE   B 1 188 ? 37.720 -15.395 -5.692  1.00 60.49  ? 881  ILE   B CD1 1 
ATOM   3413 N N   . LYS   B 1 189 ? 40.812 -18.701 -2.406  1.00 53.19  ? 882  LYS   B N   1 
ATOM   3414 C CA  . LYS   B 1 189 ? 41.401 -19.965 -1.968  1.00 51.24  ? 882  LYS   B CA  1 
ATOM   3415 C C   . LYS   B 1 189 ? 40.768 -20.579 -0.704  1.00 49.47  ? 882  LYS   B C   1 
ATOM   3416 O O   . LYS   B 1 189 ? 41.139 -21.679 -0.312  1.00 49.59  ? 882  LYS   B O   1 
ATOM   3417 C CB  . LYS   B 1 189 ? 42.909 -19.812 -1.819  1.00 51.82  ? 882  LYS   B CB  1 
ATOM   3418 C CG  . LYS   B 1 189 ? 43.523 -19.518 -3.169  1.00 54.37  ? 882  LYS   B CG  1 
ATOM   3419 C CD  . LYS   B 1 189 ? 44.978 -19.167 -3.085  1.00 57.94  ? 882  LYS   B CD  1 
ATOM   3420 C CE  . LYS   B 1 189 ? 45.533 -18.972 -4.470  1.00 60.45  ? 882  LYS   B CE  1 
ATOM   3421 N NZ  . LYS   B 1 189 ? 47.012 -19.097 -4.474  1.00 62.71  ? 882  LYS   B NZ  1 
ATOM   3422 N N   . TRP   B 1 190 ? 39.788 -19.901 -0.104  1.00 47.78  ? 883  TRP   B N   1 
ATOM   3423 C CA  . TRP   B 1 190 ? 39.025 -20.396 1.047   1.00 46.43  ? 883  TRP   B CA  1 
ATOM   3424 C C   . TRP   B 1 190 ? 37.532 -20.595 0.716   1.00 46.25  ? 883  TRP   B C   1 
ATOM   3425 O O   . TRP   B 1 190 ? 36.812 -21.199 1.503   1.00 45.51  ? 883  TRP   B O   1 
ATOM   3426 C CB  . TRP   B 1 190 ? 39.134 -19.436 2.226   1.00 45.36  ? 883  TRP   B CB  1 
ATOM   3427 C CG  . TRP   B 1 190 ? 40.403 -19.570 3.005   1.00 44.63  ? 883  TRP   B CG  1 
ATOM   3428 C CD1 . TRP   B 1 190 ? 40.597 -20.285 4.153   1.00 44.71  ? 883  TRP   B CD1 1 
ATOM   3429 C CD2 . TRP   B 1 190 ? 41.664 -18.983 2.678   1.00 43.95  ? 883  TRP   B CD2 1 
ATOM   3430 N NE1 . TRP   B 1 190 ? 41.904 -20.181 4.555   1.00 44.66  ? 883  TRP   B NE1 1 
ATOM   3431 C CE2 . TRP   B 1 190 ? 42.585 -19.392 3.661   1.00 44.58  ? 883  TRP   B CE2 1 
ATOM   3432 C CE3 . TRP   B 1 190 ? 42.101 -18.139 1.658   1.00 44.49  ? 883  TRP   B CE3 1 
ATOM   3433 C CZ2 . TRP   B 1 190 ? 43.918 -18.981 3.647   1.00 45.34  ? 883  TRP   B CZ2 1 
ATOM   3434 C CZ3 . TRP   B 1 190 ? 43.431 -17.768 1.624   1.00 45.41  ? 883  TRP   B CZ3 1 
ATOM   3435 C CH2 . TRP   B 1 190 ? 44.320 -18.176 2.615   1.00 45.48  ? 883  TRP   B CH2 1 
ATOM   3436 N N   . MET   B 1 191 ? 37.071 -20.053 -0.423  1.00 46.86  ? 884  MET   B N   1 
ATOM   3437 C CA  . MET   B 1 191 ? 35.697 -20.092 -0.868  1.00 47.91  ? 884  MET   B CA  1 
ATOM   3438 C C   . MET   B 1 191 ? 35.292 -21.382 -1.559  1.00 48.75  ? 884  MET   B C   1 
ATOM   3439 O O   . MET   B 1 191 ? 36.055 -21.977 -2.326  1.00 48.71  ? 884  MET   B O   1 
ATOM   3440 C CB  . MET   B 1 191 ? 35.435 -18.922 -1.816  1.00 48.84  ? 884  MET   B CB  1 
ATOM   3441 C CG  . MET   B 1 191 ? 35.392 -17.588 -1.131  1.00 51.85  ? 884  MET   B CG  1 
ATOM   3442 S SD  . MET   B 1 191 ? 35.528 -16.179 -2.284  1.00 58.91  ? 884  MET   B SD  1 
ATOM   3443 C CE  . MET   B 1 191 ? 34.175 -16.460 -3.306  1.00 53.37  ? 884  MET   B CE  1 
ATOM   3444 N N   . ALA   B 1 192 ? 34.045 -21.777 -1.318  1.00 49.13  ? 885  ALA   B N   1 
ATOM   3445 C CA  . ALA   B 1 192 ? 33.434 -22.914 -1.965  1.00 49.66  ? 885  ALA   B CA  1 
ATOM   3446 C C   . ALA   B 1 192 ? 33.229 -22.578 -3.458  1.00 51.19  ? 885  ALA   B C   1 
ATOM   3447 O O   . ALA   B 1 192 ? 33.084 -21.408 -3.806  1.00 51.45  ? 885  ALA   B O   1 
ATOM   3448 C CB  . ALA   B 1 192 ? 32.106 -23.223 -1.294  1.00 49.12  ? 885  ALA   B CB  1 
ATOM   3449 N N   . LEU   B 1 193 ? 33.218 -23.591 -4.340  1.00 51.87  ? 886  LEU   B N   1 
ATOM   3450 C CA  . LEU   B 1 193 ? 33.048 -23.367 -5.771  1.00 53.37  ? 886  LEU   B CA  1 
ATOM   3451 C C   . LEU   B 1 193 ? 31.796 -22.539 -6.123  1.00 54.97  ? 886  LEU   B C   1 
ATOM   3452 O O   . LEU   B 1 193 ? 31.870 -21.682 -6.991  1.00 55.47  ? 886  LEU   B O   1 
ATOM   3453 C CB  . LEU   B 1 193 ? 33.050 -24.702 -6.524  1.00 53.64  ? 886  LEU   B CB  1 
ATOM   3454 C CG  . LEU   B 1 193 ? 32.993 -24.607 -8.042  1.00 54.88  ? 886  LEU   B CG  1 
ATOM   3455 C CD1 . LEU   B 1 193 ? 34.266 -24.013 -8.604  1.00 55.69  ? 886  LEU   B CD1 1 
ATOM   3456 C CD2 . LEU   B 1 193 ? 32.716 -25.944 -8.657  1.00 55.31  ? 886  LEU   B CD2 1 
ATOM   3457 N N   . GLU   B 1 194 ? 30.668 -22.753 -5.423  1.00 55.76  ? 887  GLU   B N   1 
ATOM   3458 C CA  . GLU   B 1 194 ? 29.429 -22.001 -5.684  1.00 56.36  ? 887  GLU   B CA  1 
ATOM   3459 C C   . GLU   B 1 194 ? 29.539 -20.523 -5.279  1.00 57.39  ? 887  GLU   B C   1 
ATOM   3460 O O   . GLU   B 1 194 ? 28.859 -19.685 -5.863  1.00 57.81  ? 887  GLU   B O   1 
ATOM   3461 C CB  . GLU   B 1 194 ? 28.190 -22.672 -5.040  1.00 57.13  ? 887  GLU   B CB  1 
ATOM   3462 C CG  . GLU   B 1 194 ? 28.054 -22.506 -3.531  1.00 59.65  ? 887  GLU   B CG  1 
ATOM   3463 C CD  . GLU   B 1 194 ? 28.745 -23.560 -2.679  1.00 61.47  ? 887  GLU   B CD  1 
ATOM   3464 O OE1 . GLU   B 1 194 ? 29.525 -24.354 -3.251  1.00 60.83  ? 887  GLU   B OE1 1 
ATOM   3465 O OE2 . GLU   B 1 194 ? 28.510 -23.591 -1.446  1.00 60.65  ? 887  GLU   B OE2 1 
ATOM   3466 N N   . SER   B 1 195 ? 30.405 -20.203 -4.316  1.00 57.71  ? 888  SER   B N   1 
ATOM   3467 C CA  . SER   B 1 195 ? 30.631 -18.816 -3.906  1.00 58.87  ? 888  SER   B CA  1 
ATOM   3468 C C   . SER   B 1 195 ? 31.506 -18.104 -4.937  1.00 60.10  ? 888  SER   B C   1 
ATOM   3469 O O   . SER   B 1 195 ? 31.294 -16.921 -5.190  1.00 60.41  ? 888  SER   B O   1 
ATOM   3470 C CB  . SER   B 1 195 ? 31.305 -18.752 -2.538  1.00 59.63  ? 888  SER   B CB  1 
ATOM   3471 O OG  . SER   B 1 195 ? 30.522 -19.389 -1.544  1.00 61.86  ? 888  SER   B OG  1 
ATOM   3472 N N   . ILE   B 1 196 ? 32.483 -18.808 -5.527  1.00 60.57  ? 889  ILE   B N   1 
ATOM   3473 C CA  . ILE   B 1 196 ? 33.355 -18.236 -6.547  1.00 61.56  ? 889  ILE   B CA  1 
ATOM   3474 C C   . ILE   B 1 196 ? 32.557 -17.932 -7.811  1.00 63.11  ? 889  ILE   B C   1 
ATOM   3475 O O   . ILE   B 1 196 ? 32.640 -16.826 -8.350  1.00 63.79  ? 889  ILE   B O   1 
ATOM   3476 C CB  . ILE   B 1 196 ? 34.547 -19.191 -6.854  1.00 61.50  ? 889  ILE   B CB  1 
ATOM   3477 C CG1 . ILE   B 1 196 ? 35.403 -19.460 -5.594  1.00 61.90  ? 889  ILE   B CG1 1 
ATOM   3478 C CG2 . ILE   B 1 196 ? 35.395 -18.656 -8.005  1.00 61.51  ? 889  ILE   B CG2 1 
ATOM   3479 C CD1 . ILE   B 1 196 ? 36.482 -20.518 -5.783  1.00 62.53  ? 889  ILE   B CD1 1 
ATOM   3480 N N   . LEU   B 1 197 ? 31.746 -18.896 -8.257  1.00 63.74  ? 890  LEU   B N   1 
ATOM   3481 C CA  . LEU   B 1 197 ? 30.983 -18.777 -9.489  1.00 64.77  ? 890  LEU   B CA  1 
ATOM   3482 C C   . LEU   B 1 197 ? 29.708 -17.964 -9.417  1.00 65.84  ? 890  LEU   B C   1 
ATOM   3483 O O   . LEU   B 1 197 ? 29.319 -17.387 -10.432 1.00 66.45  ? 890  LEU   B O   1 
ATOM   3484 C CB  . LEU   B 1 197 ? 30.650 -20.171 -10.037 1.00 65.22  ? 890  LEU   B CB  1 
ATOM   3485 C CG  . LEU   B 1 197 ? 31.820 -21.127 -10.222 1.00 67.02  ? 890  LEU   B CG  1 
ATOM   3486 C CD1 . LEU   B 1 197 ? 31.342 -22.462 -10.733 1.00 67.34  ? 890  LEU   B CD1 1 
ATOM   3487 C CD2 . LEU   B 1 197 ? 32.882 -20.540 -11.150 1.00 67.92  ? 890  LEU   B CD2 1 
ATOM   3488 N N   . HIS   B 1 198 ? 28.994 -17.985 -8.280  1.00 66.27  ? 891  HIS   B N   1 
ATOM   3489 C CA  . HIS   B 1 198 ? 27.700 -17.298 -8.198  1.00 67.08  ? 891  HIS   B CA  1 
ATOM   3490 C C   . HIS   B 1 198 ? 27.497 -16.408 -6.992  1.00 67.79  ? 891  HIS   B C   1 
ATOM   3491 O O   . HIS   B 1 198 ? 26.380 -15.940 -6.781  1.00 68.33  ? 891  HIS   B O   1 
ATOM   3492 C CB  . HIS   B 1 198 ? 26.559 -18.316 -8.261  1.00 68.16  ? 891  HIS   B CB  1 
ATOM   3493 C CG  . HIS   B 1 198 ? 26.631 -19.220 -9.450  1.00 70.91  ? 891  HIS   B CG  1 
ATOM   3494 N ND1 . HIS   B 1 198 ? 26.960 -20.560 -9.320  1.00 72.92  ? 891  HIS   B ND1 1 
ATOM   3495 C CD2 . HIS   B 1 198 ? 26.452 -18.938 -10.761 1.00 72.10  ? 891  HIS   B CD2 1 
ATOM   3496 C CE1 . HIS   B 1 198 ? 26.947 -21.053 -10.548 1.00 73.50  ? 891  HIS   B CE1 1 
ATOM   3497 N NE2 . HIS   B 1 198 ? 26.646 -20.115 -11.449 1.00 73.37  ? 891  HIS   B NE2 1 
ATOM   3498 N N   . ARG   B 1 199 ? 28.537 -16.200 -6.181  1.00 67.69  ? 892  ARG   B N   1 
ATOM   3499 C CA  . ARG   B 1 199 ? 28.439 -15.402 -4.968  1.00 68.12  ? 892  ARG   B CA  1 
ATOM   3500 C C   . ARG   B 1 199 ? 27.363 -15.937 -4.008  1.00 66.67  ? 892  ARG   B C   1 
ATOM   3501 O O   . ARG   B 1 199 ? 26.686 -15.163 -3.339  1.00 67.12  ? 892  ARG   B O   1 
ATOM   3502 C CB  . ARG   B 1 199 ? 28.267 -13.905 -5.284  1.00 71.20  ? 892  ARG   B CB  1 
ATOM   3503 C CG  . ARG   B 1 199 ? 29.540 -13.247 -5.813  1.00 77.16  ? 892  ARG   B CG  1 
ATOM   3504 C CD  . ARG   B 1 199 ? 30.640 -13.211 -4.751  1.00 83.52  ? 892  ARG   B CD  1 
ATOM   3505 N NE  . ARG   B 1 199 ? 31.906 -12.693 -5.273  1.00 89.03  ? 892  ARG   B NE  1 
ATOM   3506 C CZ  . ARG   B 1 199 ? 32.817 -13.431 -5.906  1.00 92.84  ? 892  ARG   B CZ  1 
ATOM   3507 N NH1 . ARG   B 1 199 ? 32.611 -14.726 -6.108  1.00 92.34  ? 892  ARG   B NH1 1 
ATOM   3508 N NH2 . ARG   B 1 199 ? 33.933 -12.874 -6.359  1.00 93.81  ? 892  ARG   B NH2 1 
ATOM   3509 N N   . ILE   B 1 200 ? 27.212 -17.267 -3.953  1.00 64.78  ? 893  ILE   B N   1 
ATOM   3510 C CA  . ILE   B 1 200 ? 26.269 -17.918 -3.055  1.00 63.58  ? 893  ILE   B CA  1 
ATOM   3511 C C   . ILE   B 1 200 ? 26.982 -18.235 -1.733  1.00 62.04  ? 893  ILE   B C   1 
ATOM   3512 O O   . ILE   B 1 200 ? 27.978 -18.956 -1.722  1.00 62.20  ? 893  ILE   B O   1 
ATOM   3513 C CB  . ILE   B 1 200 ? 25.676 -19.189 -3.704  1.00 64.26  ? 893  ILE   B CB  1 
ATOM   3514 C CG1 . ILE   B 1 200 ? 24.776 -18.839 -4.914  1.00 65.15  ? 893  ILE   B CG1 1 
ATOM   3515 C CG2 . ILE   B 1 200 ? 24.929 -20.054 -2.671  1.00 64.68  ? 893  ILE   B CG2 1 
ATOM   3516 N N   . TYR   B 1 201 ? 26.492 -17.674 -0.628  1.00 60.27  ? 894  TYR   B N   1 
ATOM   3517 C CA  . TYR   B 1 201 ? 27.084 -17.904 0.683   1.00 58.81  ? 894  TYR   B CA  1 
ATOM   3518 C C   . TYR   B 1 201 ? 26.059 -18.478 1.629   1.00 57.31  ? 894  TYR   B C   1 
ATOM   3519 O O   . TYR   B 1 201 ? 24.995 -17.897 1.834   1.00 57.64  ? 894  TYR   B O   1 
ATOM   3520 C CB  . TYR   B 1 201 ? 27.662 -16.622 1.265   1.00 58.81  ? 894  TYR   B CB  1 
ATOM   3521 C CG  . TYR   B 1 201 ? 28.852 -16.085 0.505   1.00 59.40  ? 894  TYR   B CG  1 
ATOM   3522 C CD1 . TYR   B 1 201 ? 28.685 -15.189 -0.545  1.00 60.39  ? 894  TYR   B CD1 1 
ATOM   3523 C CD2 . TYR   B 1 201 ? 30.145 -16.433 0.865   1.00 59.77  ? 894  TYR   B CD2 1 
ATOM   3524 C CE1 . TYR   B 1 201 ? 29.775 -14.653 -1.216  1.00 61.34  ? 894  TYR   B CE1 1 
ATOM   3525 C CE2 . TYR   B 1 201 ? 31.243 -15.900 0.205   1.00 60.92  ? 894  TYR   B CE2 1 
ATOM   3526 C CZ  . TYR   B 1 201 ? 31.054 -15.013 -0.841  1.00 62.43  ? 894  TYR   B CZ  1 
ATOM   3527 O OH  . TYR   B 1 201 ? 32.128 -14.482 -1.516  1.00 64.46  ? 894  TYR   B OH  1 
ATOM   3528 N N   . THR   B 1 202 ? 26.366 -19.650 2.178   1.00 55.54  ? 895  THR   B N   1 
ATOM   3529 C CA  . THR   B 1 202 ? 25.503 -20.398 3.089   1.00 54.42  ? 895  THR   B CA  1 
ATOM   3530 C C   . THR   B 1 202 ? 26.348 -20.951 4.257   1.00 53.09  ? 895  THR   B C   1 
ATOM   3531 O O   . THR   B 1 202 ? 27.575 -20.765 4.280   1.00 52.99  ? 895  THR   B O   1 
ATOM   3532 C CB  . THR   B 1 202 ? 24.825 -21.564 2.293   1.00 55.91  ? 895  THR   B CB  1 
ATOM   3533 O OG1 . THR   B 1 202 ? 25.808 -22.561 1.971   1.00 57.51  ? 895  THR   B OG1 1 
ATOM   3534 C CG2 . THR   B 1 202 ? 24.094 -21.104 1.038   1.00 55.22  ? 895  THR   B CG2 1 
ATOM   3535 N N   . HIS   B 1 203 ? 25.713 -21.645 5.222   1.00 51.81  ? 896  HIS   B N   1 
ATOM   3536 C CA  . HIS   B 1 203 ? 26.468 -22.312 6.269   1.00 50.87  ? 896  HIS   B CA  1 
ATOM   3537 C C   . HIS   B 1 203 ? 27.286 -23.468 5.667   1.00 49.66  ? 896  HIS   B C   1 
ATOM   3538 O O   . HIS   B 1 203 ? 28.336 -23.799 6.207   1.00 49.78  ? 896  HIS   B O   1 
ATOM   3539 C CB  . HIS   B 1 203 ? 25.546 -22.768 7.397   1.00 51.75  ? 896  HIS   B CB  1 
ATOM   3540 C CG  . HIS   B 1 203 ? 24.837 -21.620 8.052   1.00 53.17  ? 896  HIS   B CG  1 
ATOM   3541 N ND1 . HIS   B 1 203 ? 23.465 -21.461 7.944   1.00 54.37  ? 896  HIS   B ND1 1 
ATOM   3542 C CD2 . HIS   B 1 203 ? 25.346 -20.581 8.757   1.00 54.06  ? 896  HIS   B CD2 1 
ATOM   3543 C CE1 . HIS   B 1 203 ? 23.179 -20.353 8.605   1.00 54.55  ? 896  HIS   B CE1 1 
ATOM   3544 N NE2 . HIS   B 1 203 ? 24.279 -19.781 9.102   1.00 54.83  ? 896  HIS   B NE2 1 
ATOM   3545 N N   . GLN   B 1 204 ? 26.863 -24.025 4.500   1.00 48.56  ? 897  GLN   B N   1 
ATOM   3546 C CA  . GLN   B 1 204 ? 27.596 -25.093 3.835   1.00 47.88  ? 897  GLN   B CA  1 
ATOM   3547 C C   . GLN   B 1 204 ? 28.820 -24.579 3.090   1.00 47.62  ? 897  GLN   B C   1 
ATOM   3548 O O   . GLN   B 1 204 ? 29.819 -25.290 3.038   1.00 48.23  ? 897  GLN   B O   1 
ATOM   3549 C CB  . GLN   B 1 204 ? 26.680 -25.958 2.960   1.00 48.44  ? 897  GLN   B CB  1 
ATOM   3550 C CG  . GLN   B 1 204 ? 25.632 -26.707 3.782   1.00 50.44  ? 897  GLN   B CG  1 
ATOM   3551 C CD  . GLN   B 1 204 ? 26.226 -27.529 4.917   1.00 54.96  ? 897  GLN   B CD  1 
ATOM   3552 O OE1 . GLN   B 1 204 ? 26.886 -28.561 4.711   1.00 56.30  ? 897  GLN   B OE1 1 
ATOM   3553 N NE2 . GLN   B 1 204 ? 26.015 -27.078 6.150   1.00 55.49  ? 897  GLN   B NE2 1 
ATOM   3554 N N   . SER   B 1 205 ? 28.795 -23.338 2.591   1.00 47.12  ? 898  SER   B N   1 
ATOM   3555 C CA  . SER   B 1 205 ? 30.001 -22.749 1.996   1.00 46.93  ? 898  SER   B CA  1 
ATOM   3556 C C   . SER   B 1 205 ? 31.026 -22.382 3.112   1.00 46.43  ? 898  SER   B C   1 
ATOM   3557 O O   . SER   B 1 205 ? 32.231 -22.358 2.851   1.00 46.76  ? 898  SER   B O   1 
ATOM   3558 C CB  . SER   B 1 205 ? 29.669 -21.566 1.092   1.00 48.02  ? 898  SER   B CB  1 
ATOM   3559 O OG  . SER   B 1 205 ? 29.114 -20.486 1.819   1.00 49.96  ? 898  SER   B OG  1 
ATOM   3560 N N   . ASP   B 1 206 ? 30.551 -22.139 4.354   1.00 45.64  ? 899  ASP   B N   1 
ATOM   3561 C CA  . ASP   B 1 206 ? 31.408 -21.917 5.525   1.00 45.98  ? 899  ASP   B CA  1 
ATOM   3562 C C   . ASP   B 1 206 ? 32.108 -23.236 5.909   1.00 45.48  ? 899  ASP   B C   1 
ATOM   3563 O O   . ASP   B 1 206 ? 33.217 -23.203 6.441   1.00 45.75  ? 899  ASP   B O   1 
ATOM   3564 C CB  . ASP   B 1 206 ? 30.583 -21.433 6.733   1.00 48.21  ? 899  ASP   B CB  1 
ATOM   3565 C CG  . ASP   B 1 206 ? 30.290 -19.947 6.754   1.00 54.31  ? 899  ASP   B CG  1 
ATOM   3566 O OD1 . ASP   B 1 206 ? 31.031 -19.187 6.092   1.00 55.41  ? 899  ASP   B OD1 1 
ATOM   3567 O OD2 . ASP   B 1 206 ? 29.317 -19.539 7.438   1.00 56.99  ? 899  ASP   B OD2 1 
ATOM   3568 N N   . VAL   B 1 207 ? 31.440 -24.386 5.684   1.00 44.65  ? 900  VAL   B N   1 
ATOM   3569 C CA  . VAL   B 1 207 ? 31.984 -25.721 5.927   1.00 44.33  ? 900  VAL   B CA  1 
ATOM   3570 C C   . VAL   B 1 207 ? 33.190 -25.941 5.028   1.00 42.98  ? 900  VAL   B C   1 
ATOM   3571 O O   . VAL   B 1 207 ? 34.209 -26.438 5.509   1.00 42.96  ? 900  VAL   B O   1 
ATOM   3572 C CB  . VAL   B 1 207 ? 30.906 -26.820 5.786   1.00 45.24  ? 900  VAL   B CB  1 
ATOM   3573 C CG1 . VAL   B 1 207 ? 31.537 -28.205 5.669   1.00 46.19  ? 900  VAL   B CG1 1 
ATOM   3574 C CG2 . VAL   B 1 207 ? 29.957 -26.763 6.974   1.00 45.80  ? 900  VAL   B CG2 1 
ATOM   3575 N N   . TRP   B 1 208 ? 33.112 -25.492 3.749   1.00 41.55  ? 901  TRP   B N   1 
ATOM   3576 C CA  . TRP   B 1 208 ? 34.239 -25.537 2.825   1.00 41.02  ? 901  TRP   B CA  1 
ATOM   3577 C C   . TRP   B 1 208 ? 35.428 -24.750 3.407   1.00 40.65  ? 901  TRP   B C   1 
ATOM   3578 O O   . TRP   B 1 208 ? 36.508 -25.308 3.532   1.00 40.76  ? 901  TRP   B O   1 
ATOM   3579 C CB  . TRP   B 1 208 ? 33.847 -24.983 1.442   1.00 40.68  ? 901  TRP   B CB  1 
ATOM   3580 C CG  . TRP   B 1 208 ? 34.961 -25.048 0.435   1.00 41.05  ? 901  TRP   B CG  1 
ATOM   3581 C CD1 . TRP   B 1 208 ? 36.173 -24.418 0.501   1.00 41.76  ? 901  TRP   B CD1 1 
ATOM   3582 C CD2 . TRP   B 1 208 ? 34.962 -25.795 -0.792  1.00 41.07  ? 901  TRP   B CD2 1 
ATOM   3583 N NE1 . TRP   B 1 208 ? 36.935 -24.746 -0.595  1.00 42.15  ? 901  TRP   B NE1 1 
ATOM   3584 C CE2 . TRP   B 1 208 ? 36.209 -25.580 -1.413  1.00 41.64  ? 901  TRP   B CE2 1 
ATOM   3585 C CE3 . TRP   B 1 208 ? 33.995 -26.545 -1.469  1.00 42.05  ? 901  TRP   B CE3 1 
ATOM   3586 C CZ2 . TRP   B 1 208 ? 36.525 -26.121 -2.654  1.00 42.27  ? 901  TRP   B CZ2 1 
ATOM   3587 C CZ3 . TRP   B 1 208 ? 34.319 -27.113 -2.686  1.00 42.88  ? 901  TRP   B CZ3 1 
ATOM   3588 C CH2 . TRP   B 1 208 ? 35.571 -26.896 -3.268  1.00 42.91  ? 901  TRP   B CH2 1 
ATOM   3589 N N   . SER   B 1 209 ? 35.210 -23.493 3.822   1.00 41.01  ? 902  SER   B N   1 
ATOM   3590 C CA  . SER   B 1 209 ? 36.234 -22.627 4.446   1.00 41.45  ? 902  SER   B CA  1 
ATOM   3591 C C   . SER   B 1 209 ? 36.807 -23.235 5.723   1.00 40.71  ? 902  SER   B C   1 
ATOM   3592 O O   . SER   B 1 209 ? 37.970 -23.031 6.036   1.00 40.62  ? 902  SER   B O   1 
ATOM   3593 C CB  . SER   B 1 209 ? 35.660 -21.246 4.750   1.00 43.59  ? 902  SER   B CB  1 
ATOM   3594 O OG  . SER   B 1 209 ? 35.028 -20.703 3.599   1.00 48.21  ? 902  SER   B OG  1 
ATOM   3595 N N   . TYR   B 1 210 ? 35.989 -23.974 6.463   1.00 40.46  ? 903  TYR   B N   1 
ATOM   3596 C CA  . TYR   B 1 210 ? 36.415 -24.683 7.665   1.00 40.09  ? 903  TYR   B CA  1 
ATOM   3597 C C   . TYR   B 1 210 ? 37.424 -25.767 7.302   1.00 40.78  ? 903  TYR   B C   1 
ATOM   3598 O O   . TYR   B 1 210 ? 38.410 -25.926 8.027   1.00 41.33  ? 903  TYR   B O   1 
ATOM   3599 C CB  . TYR   B 1 210 ? 35.204 -25.272 8.395   1.00 39.56  ? 903  TYR   B CB  1 
ATOM   3600 C CG  . TYR   B 1 210 ? 35.584 -26.135 9.572   1.00 40.14  ? 903  TYR   B CG  1 
ATOM   3601 C CD1 . TYR   B 1 210 ? 35.944 -25.568 10.788  1.00 40.63  ? 903  TYR   B CD1 1 
ATOM   3602 C CD2 . TYR   B 1 210 ? 35.634 -27.517 9.459   1.00 40.48  ? 903  TYR   B CD2 1 
ATOM   3603 C CE1 . TYR   B 1 210 ? 36.331 -26.355 11.862  1.00 41.03  ? 903  TYR   B CE1 1 
ATOM   3604 C CE2 . TYR   B 1 210 ? 36.037 -28.310 10.521  1.00 41.18  ? 903  TYR   B CE2 1 
ATOM   3605 C CZ  . TYR   B 1 210 ? 36.369 -27.726 11.726  1.00 41.97  ? 903  TYR   B CZ  1 
ATOM   3606 O OH  . TYR   B 1 210 ? 36.725 -28.514 12.788  1.00 43.73  ? 903  TYR   B OH  1 
ATOM   3607 N N   . GLY   B 1 211 ? 37.189 -26.477 6.187   1.00 40.23  ? 904  GLY   B N   1 
ATOM   3608 C CA  . GLY   B 1 211 ? 38.093 -27.505 5.700   1.00 40.48  ? 904  GLY   B CA  1 
ATOM   3609 C C   . GLY   B 1 211 ? 39.445 -26.936 5.317   1.00 40.87  ? 904  GLY   B C   1 
ATOM   3610 O O   . GLY   B 1 211 ? 40.479 -27.546 5.600   1.00 41.10  ? 904  GLY   B O   1 
ATOM   3611 N N   . VAL   B 1 212 ? 39.448 -25.762 4.666   1.00 40.84  ? 905  VAL   B N   1 
ATOM   3612 C CA  . VAL   B 1 212 ? 40.674 -25.060 4.284   1.00 41.82  ? 905  VAL   B CA  1 
ATOM   3613 C C   . VAL   B 1 212 ? 41.415 -24.551 5.531   1.00 42.67  ? 905  VAL   B C   1 
ATOM   3614 O O   . VAL   B 1 212 ? 42.642 -24.590 5.559   1.00 43.22  ? 905  VAL   B O   1 
ATOM   3615 C CB  . VAL   B 1 212 ? 40.398 -23.921 3.263   1.00 43.05  ? 905  VAL   B CB  1 
ATOM   3616 C CG1 . VAL   B 1 212 ? 41.686 -23.179 2.898   1.00 43.36  ? 905  VAL   B CG1 1 
ATOM   3617 C CG2 . VAL   B 1 212 ? 39.732 -24.472 2.003   1.00 43.57  ? 905  VAL   B CG2 1 
ATOM   3618 N N   . THR   B 1 213 ? 40.671 -24.147 6.589   1.00 42.53  ? 906  THR   B N   1 
ATOM   3619 C CA  . THR   B 1 213 ? 41.222 -23.692 7.868   1.00 42.76  ? 906  THR   B CA  1 
ATOM   3620 C C   . THR   B 1 213 ? 41.894 -24.862 8.610   1.00 43.62  ? 906  THR   B C   1 
ATOM   3621 O O   . THR   B 1 213 ? 42.983 -24.696 9.154   1.00 43.63  ? 906  THR   B O   1 
ATOM   3622 C CB  . THR   B 1 213 ? 40.123 -23.008 8.704   1.00 43.02  ? 906  THR   B CB  1 
ATOM   3623 O OG1 . THR   B 1 213 ? 39.611 -21.896 7.965   1.00 43.69  ? 906  THR   B OG1 1 
ATOM   3624 C CG2 . THR   B 1 213 ? 40.616 -22.537 10.060  1.00 42.54  ? 906  THR   B CG2 1 
ATOM   3625 N N   . VAL   B 1 214 ? 41.262 -26.051 8.599   1.00 43.64  ? 907  VAL   B N   1 
ATOM   3626 C CA  . VAL   B 1 214 ? 41.830 -27.250 9.212   1.00 43.68  ? 907  VAL   B CA  1 
ATOM   3627 C C   . VAL   B 1 214 ? 43.110 -27.629 8.458   1.00 43.71  ? 907  VAL   B C   1 
ATOM   3628 O O   . VAL   B 1 214 ? 44.118 -27.928 9.093   1.00 43.83  ? 907  VAL   B O   1 
ATOM   3629 C CB  . VAL   B 1 214 ? 40.811 -28.418 9.245   1.00 44.13  ? 907  VAL   B CB  1 
ATOM   3630 C CG1 . VAL   B 1 214 ? 41.486 -29.739 9.618   1.00 44.56  ? 907  VAL   B CG1 1 
ATOM   3631 C CG2 . VAL   B 1 214 ? 39.672 -28.116 10.201  1.00 44.14  ? 907  VAL   B CG2 1 
ATOM   3632 N N   . TRP   B 1 215 ? 43.093 -27.529 7.113   1.00 43.18  ? 908  TRP   B N   1 
ATOM   3633 C CA  . TRP   B 1 215 ? 44.248 -27.798 6.259   1.00 43.21  ? 908  TRP   B CA  1 
ATOM   3634 C C   . TRP   B 1 215 ? 45.402 -26.844 6.587   1.00 44.55  ? 908  TRP   B C   1 
ATOM   3635 O O   . TRP   B 1 215 ? 46.555 -27.265 6.587   1.00 45.35  ? 908  TRP   B O   1 
ATOM   3636 C CB  . TRP   B 1 215 ? 43.871 -27.698 4.771   1.00 42.43  ? 908  TRP   B CB  1 
ATOM   3637 C CG  . TRP   B 1 215 ? 44.980 -28.110 3.853   1.00 42.41  ? 908  TRP   B CG  1 
ATOM   3638 C CD1 . TRP   B 1 215 ? 45.241 -29.366 3.395   1.00 43.19  ? 908  TRP   B CD1 1 
ATOM   3639 C CD2 . TRP   B 1 215 ? 46.023 -27.268 3.337   1.00 42.64  ? 908  TRP   B CD2 1 
ATOM   3640 N NE1 . TRP   B 1 215 ? 46.373 -29.360 2.615   1.00 43.35  ? 908  TRP   B NE1 1 
ATOM   3641 C CE2 . TRP   B 1 215 ? 46.882 -28.085 2.576   1.00 43.27  ? 908  TRP   B CE2 1 
ATOM   3642 C CE3 . TRP   B 1 215 ? 46.320 -25.900 3.456   1.00 42.78  ? 908  TRP   B CE3 1 
ATOM   3643 C CZ2 . TRP   B 1 215 ? 48.000 -27.576 1.918   1.00 43.62  ? 908  TRP   B CZ2 1 
ATOM   3644 C CZ3 . TRP   B 1 215 ? 47.447 -25.411 2.843   1.00 43.38  ? 908  TRP   B CZ3 1 
ATOM   3645 C CH2 . TRP   B 1 215 ? 48.260 -26.237 2.062   1.00 43.65  ? 908  TRP   B CH2 1 
ATOM   3646 N N   . GLU   B 1 216 ? 45.103 -25.567 6.864   1.00 44.53  ? 909  GLU   B N   1 
ATOM   3647 C CA  . GLU   B 1 216 ? 46.125 -24.597 7.248   1.00 44.77  ? 909  GLU   B CA  1 
ATOM   3648 C C   . GLU   B 1 216 ? 46.761 -25.008 8.571   1.00 45.39  ? 909  GLU   B C   1 
ATOM   3649 O O   . GLU   B 1 216 ? 47.957 -24.841 8.732   1.00 45.78  ? 909  GLU   B O   1 
ATOM   3650 C CB  . GLU   B 1 216 ? 45.520 -23.200 7.433   1.00 46.23  ? 909  GLU   B CB  1 
ATOM   3651 C CG  . GLU   B 1 216 ? 45.110 -22.470 6.169   1.00 49.19  ? 909  GLU   B CG  1 
ATOM   3652 C CD  . GLU   B 1 216 ? 44.512 -21.105 6.475   1.00 53.04  ? 909  GLU   B CD  1 
ATOM   3653 O OE1 . GLU   B 1 216 ? 43.287 -21.019 6.724   1.00 51.15  ? 909  GLU   B OE1 1 
ATOM   3654 O OE2 . GLU   B 1 216 ? 45.279 -20.116 6.476   1.00 55.44  ? 909  GLU   B OE2 1 
ATOM   3655 N N   . LEU   B 1 217 ? 45.968 -25.508 9.529   1.00 45.43  ? 910  LEU   B N   1 
ATOM   3656 C CA  . LEU   B 1 217 ? 46.480 -25.891 10.843  1.00 46.03  ? 910  LEU   B CA  1 
ATOM   3657 C C   . LEU   B 1 217 ? 47.326 -27.144 10.771  1.00 47.42  ? 910  LEU   B C   1 
ATOM   3658 O O   . LEU   B 1 217 ? 48.389 -27.195 11.391  1.00 47.36  ? 910  LEU   B O   1 
ATOM   3659 C CB  . LEU   B 1 217 ? 45.341 -26.103 11.852  1.00 45.76  ? 910  LEU   B CB  1 
ATOM   3660 C CG  . LEU   B 1 217 ? 44.380 -24.944 12.078  1.00 46.22  ? 910  LEU   B CG  1 
ATOM   3661 C CD1 . LEU   B 1 217 ? 43.289 -25.331 13.078  1.00 46.14  ? 910  LEU   B CD1 1 
ATOM   3662 C CD2 . LEU   B 1 217 ? 45.120 -23.692 12.513  1.00 46.41  ? 910  LEU   B CD2 1 
ATOM   3663 N N   . MET   B 1 218 ? 46.863 -28.152 10.004  1.00 48.44  ? 911  MET   B N   1 
ATOM   3664 C CA  . MET   B 1 218 ? 47.555 -29.426 9.819   1.00 49.57  ? 911  MET   B CA  1 
ATOM   3665 C C   . MET   B 1 218 ? 48.866 -29.279 9.065   1.00 50.38  ? 911  MET   B C   1 
ATOM   3666 O O   . MET   B 1 218 ? 49.740 -30.128 9.208   1.00 50.29  ? 911  MET   B O   1 
ATOM   3667 C CB  . MET   B 1 218 ? 46.649 -30.442 9.118   1.00 51.54  ? 911  MET   B CB  1 
ATOM   3668 C CG  . MET   B 1 218 ? 45.358 -30.728 9.852   1.00 55.59  ? 911  MET   B CG  1 
ATOM   3669 S SD  . MET   B 1 218 ? 45.550 -31.275 11.569  1.00 66.00  ? 911  MET   B SD  1 
ATOM   3670 C CE  . MET   B 1 218 ? 43.859 -31.813 11.916  1.00 64.01  ? 911  MET   B CE  1 
ATOM   3671 N N   . THR   B 1 219 ? 49.005 -28.223 8.238   1.00 51.22  ? 912  THR   B N   1 
ATOM   3672 C CA  . THR   B 1 219 ? 50.254 -27.931 7.525   1.00 52.17  ? 912  THR   B CA  1 
ATOM   3673 C C   . THR   B 1 219 ? 51.136 -26.898 8.268   1.00 53.60  ? 912  THR   B C   1 
ATOM   3674 O O   . THR   B 1 219 ? 52.173 -26.501 7.737   1.00 54.21  ? 912  THR   B O   1 
ATOM   3675 C CB  . THR   B 1 219 ? 49.971 -27.454 6.100   1.00 53.00  ? 912  THR   B CB  1 
ATOM   3676 O OG1 . THR   B 1 219 ? 49.123 -26.311 6.161   1.00 53.92  ? 912  THR   B OG1 1 
ATOM   3677 C CG2 . THR   B 1 219 ? 49.357 -28.538 5.232   1.00 53.26  ? 912  THR   B CG2 1 
ATOM   3678 N N   . PHE   B 1 220 ? 50.717 -26.459 9.473   1.00 54.07  ? 913  PHE   B N   1 
ATOM   3679 C CA  . PHE   B 1 220 ? 51.400 -25.501 10.344  1.00 54.87  ? 913  PHE   B CA  1 
ATOM   3680 C C   . PHE   B 1 220 ? 51.523 -24.114 9.723   1.00 56.12  ? 913  PHE   B C   1 
ATOM   3681 O O   . PHE   B 1 220 ? 52.525 -23.418 9.921   1.00 56.47  ? 913  PHE   B O   1 
ATOM   3682 C CB  . PHE   B 1 220 ? 52.753 -26.034 10.836  1.00 54.52  ? 913  PHE   B CB  1 
ATOM   3683 C CG  . PHE   B 1 220 ? 52.621 -27.295 11.656  1.00 54.83  ? 913  PHE   B CG  1 
ATOM   3684 C CD1 . PHE   B 1 220 ? 52.305 -27.236 13.000  1.00 55.67  ? 913  PHE   B CD1 1 
ATOM   3685 C CD2 . PHE   B 1 220 ? 52.771 -28.545 11.072  1.00 55.54  ? 913  PHE   B CD2 1 
ATOM   3686 C CE1 . PHE   B 1 220 ? 52.174 -28.405 13.754  1.00 56.14  ? 913  PHE   B CE1 1 
ATOM   3687 C CE2 . PHE   B 1 220 ? 52.623 -29.710 11.824  1.00 56.22  ? 913  PHE   B CE2 1 
ATOM   3688 C CZ  . PHE   B 1 220 ? 52.331 -29.633 13.161  1.00 55.85  ? 913  PHE   B CZ  1 
ATOM   3689 N N   . GLY   B 1 221 ? 50.482 -23.709 9.008   1.00 56.45  ? 914  GLY   B N   1 
ATOM   3690 C CA  . GLY   B 1 221 ? 50.409 -22.384 8.421   1.00 57.38  ? 914  GLY   B CA  1 
ATOM   3691 C C   . GLY   B 1 221 ? 50.800 -22.265 6.970   1.00 58.59  ? 914  GLY   B C   1 
ATOM   3692 O O   . GLY   B 1 221 ? 51.120 -21.163 6.528   1.00 59.50  ? 914  GLY   B O   1 
ATOM   3693 N N   . SER   B 1 222 ? 50.755 -23.367 6.205   1.00 58.84  ? 915  SER   B N   1 
ATOM   3694 C CA  . SER   B 1 222 ? 51.077 -23.304 4.776   1.00 59.59  ? 915  SER   B CA  1 
ATOM   3695 C C   . SER   B 1 222 ? 50.031 -22.499 4.006   1.00 60.06  ? 915  SER   B C   1 
ATOM   3696 O O   . SER   B 1 222 ? 48.870 -22.438 4.411   1.00 60.02  ? 915  SER   B O   1 
ATOM   3697 C CB  . SER   B 1 222 ? 51.199 -24.699 4.173   1.00 60.81  ? 915  SER   B CB  1 
ATOM   3698 O OG  . SER   B 1 222 ? 52.352 -25.357 4.666   1.00 63.13  ? 915  SER   B OG  1 
ATOM   3699 N N   . LYS   B 1 223 ? 50.438 -21.889 2.891   1.00 60.34  ? 916  LYS   B N   1 
ATOM   3700 C CA  . LYS   B 1 223 ? 49.522 -21.117 2.063   1.00 61.15  ? 916  LYS   B CA  1 
ATOM   3701 C C   . LYS   B 1 223 ? 48.810 -22.044 1.075   1.00 62.18  ? 916  LYS   B C   1 
ATOM   3702 O O   . LYS   B 1 223 ? 49.462 -22.781 0.332   1.00 62.52  ? 916  LYS   B O   1 
ATOM   3703 C CB  . LYS   B 1 223 ? 50.275 -19.992 1.343   1.00 62.62  ? 916  LYS   B CB  1 
ATOM   3704 C CG  . LYS   B 1 223 ? 50.982 -19.049 2.301   1.00 65.70  ? 916  LYS   B CG  1 
ATOM   3705 C CD  . LYS   B 1 223 ? 51.869 -18.053 1.566   1.00 69.74  ? 916  LYS   B CD  1 
ATOM   3706 N N   . PRO   B 1 224 ? 47.467 -22.058 1.095   1.00 62.62  ? 917  PRO   B N   1 
ATOM   3707 C CA  . PRO   B 1 224 ? 46.725 -22.960 0.196   1.00 63.34  ? 917  PRO   B CA  1 
ATOM   3708 C C   . PRO   B 1 224 ? 46.889 -22.645 -1.291  1.00 65.09  ? 917  PRO   B C   1 
ATOM   3709 O O   . PRO   B 1 224 ? 46.785 -21.477 -1.677  1.00 65.66  ? 917  PRO   B O   1 
ATOM   3710 C CB  . PRO   B 1 224 ? 45.272 -22.802 0.656   1.00 63.52  ? 917  PRO   B CB  1 
ATOM   3711 C CG  . PRO   B 1 224 ? 45.216 -21.483 1.308   1.00 63.70  ? 917  PRO   B CG  1 
ATOM   3712 C CD  . PRO   B 1 224 ? 46.559 -21.266 1.942   1.00 61.96  ? 917  PRO   B CD  1 
ATOM   3713 N N   . TYR   B 1 225 ? 47.143 -23.686 -2.124  1.00 65.72  ? 918  TYR   B N   1 
ATOM   3714 C CA  . TYR   B 1 225 ? 47.362 -23.567 -3.574  1.00 67.05  ? 918  TYR   B CA  1 
ATOM   3715 C C   . TYR   B 1 225 ? 48.466 -22.535 -3.871  1.00 69.90  ? 918  TYR   B C   1 
ATOM   3716 O O   . TYR   B 1 225 ? 48.261 -21.599 -4.650  1.00 70.25  ? 918  TYR   B O   1 
ATOM   3717 C CB  . TYR   B 1 225 ? 46.071 -23.207 -4.336  1.00 66.06  ? 918  TYR   B CB  1 
ATOM   3718 C CG  . TYR   B 1 225 ? 44.807 -23.899 -3.871  1.00 65.78  ? 918  TYR   B CG  1 
ATOM   3719 C CD1 . TYR   B 1 225 ? 44.467 -25.163 -4.340  1.00 66.02  ? 918  TYR   B CD1 1 
ATOM   3720 C CD2 . TYR   B 1 225 ? 43.895 -23.244 -3.055  1.00 66.01  ? 918  TYR   B CD2 1 
ATOM   3721 C CE1 . TYR   B 1 225 ? 43.280 -25.778 -3.962  1.00 66.39  ? 918  TYR   B CE1 1 
ATOM   3722 C CE2 . TYR   B 1 225 ? 42.710 -23.851 -2.665  1.00 66.74  ? 918  TYR   B CE2 1 
ATOM   3723 C CZ  . TYR   B 1 225 ? 42.397 -25.112 -3.136  1.00 67.47  ? 918  TYR   B CZ  1 
ATOM   3724 O OH  . TYR   B 1 225 ? 41.217 -25.703 -2.758  1.00 69.16  ? 918  TYR   B OH  1 
ATOM   3725 N N   . ASP   B 1 226 ? 49.619 -22.680 -3.205  1.00 71.62  ? 919  ASP   B N   1 
ATOM   3726 C CA  . ASP   B 1 226 ? 50.715 -21.728 -3.359  1.00 73.67  ? 919  ASP   B CA  1 
ATOM   3727 C C   . ASP   B 1 226 ? 51.283 -21.675 -4.765  1.00 75.22  ? 919  ASP   B C   1 
ATOM   3728 O O   . ASP   B 1 226 ? 51.667 -22.705 -5.315  1.00 75.68  ? 919  ASP   B O   1 
ATOM   3729 C CB  . ASP   B 1 226 ? 51.826 -21.995 -2.332  1.00 76.00  ? 919  ASP   B CB  1 
ATOM   3730 C CG  . ASP   B 1 226 ? 52.442 -20.727 -1.766  1.00 81.10  ? 919  ASP   B CG  1 
ATOM   3731 O OD1 . ASP   B 1 226 ? 52.362 -19.673 -2.439  1.00 81.93  ? 919  ASP   B OD1 1 
ATOM   3732 O OD2 . ASP   B 1 226 ? 53.001 -20.787 -0.652  1.00 83.51  ? 919  ASP   B OD2 1 
ATOM   3733 N N   . GLY   B 1 227 ? 51.324 -20.474 -5.333  1.00 75.97  ? 920  GLY   B N   1 
ATOM   3734 C CA  . GLY   B 1 227 ? 51.844 -20.262 -6.680  1.00 77.11  ? 920  GLY   B CA  1 
ATOM   3735 C C   . GLY   B 1 227 ? 50.767 -20.199 -7.745  1.00 77.77  ? 920  GLY   B C   1 
ATOM   3736 O O   . GLY   B 1 227 ? 50.949 -19.551 -8.780  1.00 78.33  ? 920  GLY   B O   1 
ATOM   3737 N N   . ILE   B 1 228 ? 49.643 -20.892 -7.505  1.00 77.38  ? 921  ILE   B N   1 
ATOM   3738 C CA  . ILE   B 1 228 ? 48.509 -20.914 -8.419  1.00 77.36  ? 921  ILE   B CA  1 
ATOM   3739 C C   . ILE   B 1 228 ? 47.779 -19.576 -8.321  1.00 77.56  ? 921  ILE   B C   1 
ATOM   3740 O O   . ILE   B 1 228 ? 47.431 -19.147 -7.221  1.00 77.63  ? 921  ILE   B O   1 
ATOM   3741 C CB  . ILE   B 1 228 ? 47.578 -22.093 -8.048  1.00 77.52  ? 921  ILE   B CB  1 
ATOM   3742 C CG1 . ILE   B 1 228 ? 48.332 -23.429 -8.099  1.00 78.22  ? 921  ILE   B CG1 1 
ATOM   3743 C CG2 . ILE   B 1 228 ? 46.337 -22.124 -8.924  1.00 77.85  ? 921  ILE   B CG2 1 
ATOM   3744 N N   . PRO   B 1 229 ? 47.579 -18.872 -9.446  1.00 77.45  ? 922  PRO   B N   1 
ATOM   3745 C CA  . PRO   B 1 229 ? 46.849 -17.592 -9.385  1.00 77.41  ? 922  PRO   B CA  1 
ATOM   3746 C C   . PRO   B 1 229 ? 45.385 -17.803 -8.986  1.00 77.33  ? 922  PRO   B C   1 
ATOM   3747 O O   . PRO   B 1 229 ? 44.806 -18.846 -9.293  1.00 77.50  ? 922  PRO   B O   1 
ATOM   3748 C CB  . PRO   B 1 229 ? 46.972 -17.033 -10.810 1.00 78.02  ? 922  PRO   B CB  1 
ATOM   3749 C CG  . PRO   B 1 229 ? 47.996 -17.891 -11.498 1.00 78.56  ? 922  PRO   B CG  1 
ATOM   3750 C CD  . PRO   B 1 229 ? 47.946 -19.223 -10.826 1.00 76.98  ? 922  PRO   B CD  1 
ATOM   3751 N N   . ALA   B 1 230 ? 44.788 -16.827 -8.291  1.00 76.91  ? 923  ALA   B N   1 
ATOM   3752 C CA  . ALA   B 1 230 ? 43.397 -16.935 -7.856  1.00 77.22  ? 923  ALA   B CA  1 
ATOM   3753 C C   . ALA   B 1 230 ? 42.417 -17.101 -9.017  1.00 77.11  ? 923  ALA   B C   1 
ATOM   3754 O O   . ALA   B 1 230 ? 41.379 -17.736 -8.852  1.00 77.09  ? 923  ALA   B O   1 
ATOM   3755 C CB  . ALA   B 1 230 ? 43.013 -15.736 -7.010  1.00 77.48  ? 923  ALA   B CB  1 
ATOM   3756 N N   . SER   B 1 231 ? 42.762 -16.571 -10.197 1.00 76.94  ? 924  SER   B N   1 
ATOM   3757 C CA  . SER   B 1 231 ? 41.937 -16.688 -11.396 1.00 77.05  ? 924  SER   B CA  1 
ATOM   3758 C C   . SER   B 1 231 ? 41.815 -18.135 -11.905 1.00 77.03  ? 924  SER   B C   1 
ATOM   3759 O O   . SER   B 1 231 ? 40.883 -18.437 -12.646 1.00 77.33  ? 924  SER   B O   1 
ATOM   3760 C CB  . SER   B 1 231 ? 42.493 -15.804 -12.506 1.00 78.20  ? 924  SER   B CB  1 
ATOM   3761 O OG  . SER   B 1 231 ? 43.793 -16.221 -12.888 1.00 80.11  ? 924  SER   B OG  1 
ATOM   3762 N N   . GLU   B 1 232 ? 42.746 -19.021 -11.522 1.00 76.51  ? 925  GLU   B N   1 
ATOM   3763 C CA  . GLU   B 1 232 ? 42.730 -20.410 -11.973 1.00 76.71  ? 925  GLU   B CA  1 
ATOM   3764 C C   . GLU   B 1 232 ? 42.124 -21.403 -10.978 1.00 75.64  ? 925  GLU   B C   1 
ATOM   3765 O O   . GLU   B 1 232 ? 41.986 -22.575 -11.316 1.00 76.06  ? 925  GLU   B O   1 
ATOM   3766 C CB  . GLU   B 1 232 ? 44.146 -20.860 -12.347 1.00 80.44  ? 925  GLU   B CB  1 
ATOM   3767 C CG  . GLU   B 1 232 ? 44.807 -19.974 -13.390 1.00 87.87  ? 925  GLU   B CG  1 
ATOM   3768 C CD  . GLU   B 1 232 ? 46.253 -20.314 -13.696 1.00 97.69  ? 925  GLU   B CD  1 
ATOM   3769 O OE1 . GLU   B 1 232 ? 46.726 -21.384 -13.247 1.00 99.48  ? 925  GLU   B OE1 1 
ATOM   3770 O OE2 . GLU   B 1 232 ? 46.919 -19.502 -14.380 1.00 101.35 ? 925  GLU   B OE2 1 
ATOM   3771 N N   . ILE   B 1 233 ? 41.765 -20.949 -9.772  1.00 74.21  ? 926  ILE   B N   1 
ATOM   3772 C CA  . ILE   B 1 233 ? 41.230 -21.800 -8.714  1.00 73.32  ? 926  ILE   B CA  1 
ATOM   3773 C C   . ILE   B 1 233 ? 39.925 -22.515 -9.105  1.00 72.81  ? 926  ILE   B C   1 
ATOM   3774 O O   . ILE   B 1 233 ? 39.831 -23.723 -8.913  1.00 73.11  ? 926  ILE   B O   1 
ATOM   3775 C CB  . ILE   B 1 233 ? 41.098 -20.998 -7.386  1.00 73.13  ? 926  ILE   B CB  1 
ATOM   3776 C CG1 . ILE   B 1 233 ? 42.482 -20.576 -6.870  1.00 73.82  ? 926  ILE   B CG1 1 
ATOM   3777 C CG2 . ILE   B 1 233 ? 40.339 -21.768 -6.313  1.00 73.22  ? 926  ILE   B CG2 1 
ATOM   3778 C CD1 . ILE   B 1 233 ? 43.430 -21.741 -6.603  1.00 74.92  ? 926  ILE   B CD1 1 
ATOM   3779 N N   . SER   B 1 234 ? 38.950 -21.799 -9.671  1.00 72.11  ? 927  SER   B N   1 
ATOM   3780 C CA  . SER   B 1 234 ? 37.670 -22.395 -10.049 1.00 72.12  ? 927  SER   B CA  1 
ATOM   3781 C C   . SER   B 1 234 ? 37.807 -23.544 -11.058 1.00 72.16  ? 927  SER   B C   1 
ATOM   3782 O O   . SER   B 1 234 ? 37.139 -24.562 -10.902 1.00 71.98  ? 927  SER   B O   1 
ATOM   3783 C CB  . SER   B 1 234 ? 36.698 -21.333 -10.557 1.00 73.27  ? 927  SER   B CB  1 
ATOM   3784 O OG  . SER   B 1 234 ? 37.096 -20.830 -11.822 1.00 75.66  ? 927  SER   B OG  1 
ATOM   3785 N N   . SER   B 1 235 ? 38.680 -23.399 -12.072 1.00 72.10  ? 928  SER   B N   1 
ATOM   3786 C CA  . SER   B 1 235 ? 38.883 -24.458 -13.057 1.00 72.33  ? 928  SER   B CA  1 
ATOM   3787 C C   . SER   B 1 235 ? 39.634 -25.654 -12.465 1.00 71.47  ? 928  SER   B C   1 
ATOM   3788 O O   . SER   B 1 235 ? 39.357 -26.794 -12.832 1.00 72.03  ? 928  SER   B O   1 
ATOM   3789 C CB  . SER   B 1 235 ? 39.593 -23.932 -14.300 1.00 74.91  ? 928  SER   B CB  1 
ATOM   3790 O OG  . SER   B 1 235 ? 40.803 -23.281 -13.949 1.00 78.98  ? 928  SER   B OG  1 
ATOM   3791 N N   . ILE   B 1 236 ? 40.552 -25.402 -11.530 1.00 70.01  ? 929  ILE   B N   1 
ATOM   3792 C CA  . ILE   B 1 236 ? 41.299 -26.455 -10.848 1.00 69.02  ? 929  ILE   B CA  1 
ATOM   3793 C C   . ILE   B 1 236 ? 40.340 -27.300 -9.973  1.00 67.67  ? 929  ILE   B C   1 
ATOM   3794 O O   . ILE   B 1 236 ? 40.457 -28.523 -9.935  1.00 67.84  ? 929  ILE   B O   1 
ATOM   3795 C CB  . ILE   B 1 236 ? 42.513 -25.827 -10.085 1.00 69.67  ? 929  ILE   B CB  1 
ATOM   3796 C CG1 . ILE   B 1 236 ? 43.821 -26.069 -10.848 1.00 70.87  ? 929  ILE   B CG1 1 
ATOM   3797 C CG2 . ILE   B 1 236 ? 42.635 -26.266 -8.620  1.00 70.16  ? 929  ILE   B CG2 1 
ATOM   3798 N N   . LEU   B 1 237 ? 39.364 -26.648 -9.328  1.00 66.34  ? 930  LEU   B N   1 
ATOM   3799 C CA  . LEU   B 1 237 ? 38.375 -27.331 -8.500  1.00 65.57  ? 930  LEU   B CA  1 
ATOM   3800 C C   . LEU   B 1 237 ? 37.425 -28.159 -9.351  1.00 65.80  ? 930  LEU   B C   1 
ATOM   3801 O O   . LEU   B 1 237 ? 37.034 -29.254 -8.942  1.00 65.95  ? 930  LEU   B O   1 
ATOM   3802 C CB  . LEU   B 1 237 ? 37.584 -26.328 -7.642  1.00 64.71  ? 930  LEU   B CB  1 
ATOM   3803 C CG  . LEU   B 1 237 ? 38.379 -25.574 -6.585  1.00 64.28  ? 930  LEU   B CG  1 
ATOM   3804 C CD1 . LEU   B 1 237 ? 37.513 -24.543 -5.906  1.00 64.23  ? 930  LEU   B CD1 1 
ATOM   3805 C CD2 . LEU   B 1 237 ? 39.002 -26.525 -5.581  1.00 64.16  ? 930  LEU   B CD2 1 
ATOM   3806 N N   . GLU   B 1 238 ? 37.070 -27.657 -10.541 1.00 65.83  ? 931  GLU   B N   1 
ATOM   3807 C CA  . GLU   B 1 238 ? 36.203 -28.389 -11.461 1.00 66.65  ? 931  GLU   B CA  1 
ATOM   3808 C C   . GLU   B 1 238 ? 36.882 -29.650 -12.030 1.00 66.29  ? 931  GLU   B C   1 
ATOM   3809 O O   . GLU   B 1 238 ? 36.187 -30.594 -12.383 1.00 66.72  ? 931  GLU   B O   1 
ATOM   3810 C CB  . GLU   B 1 238 ? 35.653 -27.472 -12.561 1.00 69.78  ? 931  GLU   B CB  1 
ATOM   3811 C CG  . GLU   B 1 238 ? 34.532 -26.585 -12.044 1.00 76.64  ? 931  GLU   B CG  1 
ATOM   3812 C CD  . GLU   B 1 238 ? 34.188 -25.387 -12.906 1.00 85.18  ? 931  GLU   B CD  1 
ATOM   3813 O OE1 . GLU   B 1 238 ? 35.085 -24.545 -13.142 1.00 86.42  ? 931  GLU   B OE1 1 
ATOM   3814 O OE2 . GLU   B 1 238 ? 33.015 -25.283 -13.335 1.00 88.42  ? 931  GLU   B OE2 1 
ATOM   3815 N N   . LYS   B 1 239 ? 38.227 -29.682 -12.075 1.00 65.50  ? 932  LYS   B N   1 
ATOM   3816 C CA  . LYS   B 1 239 ? 38.996 -30.855 -12.505 1.00 65.09  ? 932  LYS   B CA  1 
ATOM   3817 C C   . LYS   B 1 239 ? 39.132 -31.927 -11.388 1.00 64.71  ? 932  LYS   B C   1 
ATOM   3818 O O   . LYS   B 1 239 ? 39.694 -32.993 -11.639 1.00 65.34  ? 932  LYS   B O   1 
ATOM   3819 C CB  . LYS   B 1 239 ? 40.401 -30.454 -12.965 1.00 67.21  ? 932  LYS   B CB  1 
ATOM   3820 C CG  . LYS   B 1 239 ? 40.452 -29.568 -14.193 1.00 73.40  ? 932  LYS   B CG  1 
ATOM   3821 C CD  . LYS   B 1 239 ? 41.901 -29.311 -14.645 1.00 79.11  ? 932  LYS   B CD  1 
ATOM   3822 C CE  . LYS   B 1 239 ? 42.776 -28.644 -13.594 1.00 83.17  ? 932  LYS   B CE  1 
ATOM   3823 N NZ  . LYS   B 1 239 ? 43.466 -29.618 -12.693 1.00 85.32  ? 932  LYS   B NZ  1 
ATOM   3824 N N   . GLY   B 1 240 ? 38.676 -31.627 -10.171 1.00 63.42  ? 933  GLY   B N   1 
ATOM   3825 C CA  . GLY   B 1 240 ? 38.734 -32.565 -9.054  1.00 62.23  ? 933  GLY   B CA  1 
ATOM   3826 C C   . GLY   B 1 240 ? 39.966 -32.457 -8.182  1.00 60.54  ? 933  GLY   B C   1 
ATOM   3827 O O   . GLY   B 1 240 ? 40.193 -33.312 -7.324  1.00 60.40  ? 933  GLY   B O   1 
ATOM   3828 N N   . GLU   B 1 241 ? 40.777 -31.418 -8.412  1.00 59.00  ? 934  GLU   B N   1 
ATOM   3829 C CA  . GLU   B 1 241 ? 41.971 -31.173 -7.632  1.00 57.76  ? 934  GLU   B CA  1 
ATOM   3830 C C   . GLU   B 1 241 ? 41.577 -30.493 -6.349  1.00 56.19  ? 934  GLU   B C   1 
ATOM   3831 O O   . GLU   B 1 241 ? 40.760 -29.572 -6.340  1.00 56.13  ? 934  GLU   B O   1 
ATOM   3832 C CB  . GLU   B 1 241 ? 42.976 -30.312 -8.409  1.00 59.80  ? 934  GLU   B CB  1 
ATOM   3833 C CG  . GLU   B 1 241 ? 43.347 -30.911 -9.753  1.00 63.84  ? 934  GLU   B CG  1 
ATOM   3834 N N   . ARG   B 1 242 ? 42.128 -30.982 -5.252  1.00 54.87  ? 935  ARG   B N   1 
ATOM   3835 C CA  . ARG   B 1 242 ? 41.883 -30.433 -3.922  1.00 54.16  ? 935  ARG   B CA  1 
ATOM   3836 C C   . ARG   B 1 242 ? 43.217 -30.165 -3.203  1.00 54.54  ? 935  ARG   B C   1 
ATOM   3837 O O   . ARG   B 1 242 ? 44.273 -30.514 -3.727  1.00 55.22  ? 935  ARG   B O   1 
ATOM   3838 C CB  . ARG   B 1 242 ? 41.017 -31.407 -3.098  1.00 53.47  ? 935  ARG   B CB  1 
ATOM   3839 C CG  . ARG   B 1 242 ? 39.612 -31.597 -3.637  1.00 53.38  ? 935  ARG   B CG  1 
ATOM   3840 C CD  . ARG   B 1 242 ? 38.812 -30.313 -3.598  1.00 53.06  ? 935  ARG   B CD  1 
ATOM   3841 N NE  . ARG   B 1 242 ? 37.430 -30.528 -4.021  1.00 52.70  ? 935  ARG   B NE  1 
ATOM   3842 C CZ  . ARG   B 1 242 ? 37.000 -30.415 -5.275  1.00 51.67  ? 935  ARG   B CZ  1 
ATOM   3843 N NH1 . ARG   B 1 242 ? 35.726 -30.634 -5.567  1.00 51.00  ? 935  ARG   B NH1 1 
ATOM   3844 N NH2 . ARG   B 1 242 ? 37.841 -30.087 -6.244  1.00 50.12  ? 935  ARG   B NH2 1 
ATOM   3845 N N   . LEU   B 1 243 ? 43.188 -29.553 -2.005  1.00 54.14  ? 936  LEU   B N   1 
ATOM   3846 C CA  . LEU   B 1 243 ? 44.406 -29.335 -1.221  1.00 54.11  ? 936  LEU   B CA  1 
ATOM   3847 C C   . LEU   B 1 243 ? 45.021 -30.703 -0.859  1.00 54.52  ? 936  LEU   B C   1 
ATOM   3848 O O   . LEU   B 1 243 ? 44.290 -31.649 -0.545  1.00 54.47  ? 936  LEU   B O   1 
ATOM   3849 C CB  . LEU   B 1 243 ? 44.075 -28.540 0.038   1.00 53.65  ? 936  LEU   B CB  1 
ATOM   3850 C CG  . LEU   B 1 243 ? 43.717 -27.100 -0.233  1.00 54.45  ? 936  LEU   B CG  1 
ATOM   3851 C CD1 . LEU   B 1 243 ? 42.890 -26.518 0.884   1.00 54.68  ? 936  LEU   B CD1 1 
ATOM   3852 C CD2 . LEU   B 1 243 ? 44.956 -26.283 -0.528  1.00 54.83  ? 936  LEU   B CD2 1 
ATOM   3853 N N   . PRO   B 1 244 ? 46.343 -30.859 -1.013  1.00 54.60  ? 937  PRO   B N   1 
ATOM   3854 C CA  . PRO   B 1 244 ? 46.956 -32.181 -0.776  1.00 55.06  ? 937  PRO   B CA  1 
ATOM   3855 C C   . PRO   B 1 244 ? 46.853 -32.666 0.663   1.00 56.65  ? 937  PRO   B C   1 
ATOM   3856 O O   . PRO   B 1 244 ? 46.642 -31.865 1.574   1.00 57.04  ? 937  PRO   B O   1 
ATOM   3857 C CB  . PRO   B 1 244 ? 48.405 -31.980 -1.202  1.00 55.28  ? 937  PRO   B CB  1 
ATOM   3858 C CG  . PRO   B 1 244 ? 48.637 -30.498 -1.023  1.00 55.71  ? 937  PRO   B CG  1 
ATOM   3859 C CD  . PRO   B 1 244 ? 47.342 -29.850 -1.407  1.00 53.97  ? 937  PRO   B CD  1 
ATOM   3860 N N   . GLN   B 1 245 ? 46.976 -33.985 0.869   1.00 57.26  ? 938  GLN   B N   1 
ATOM   3861 C CA  . GLN   B 1 245 ? 46.915 -34.555 2.208   1.00 58.07  ? 938  GLN   B CA  1 
ATOM   3862 C C   . GLN   B 1 245 ? 48.149 -34.129 3.010   1.00 58.62  ? 938  GLN   B C   1 
ATOM   3863 O O   . GLN   B 1 245 ? 49.264 -34.446 2.595   1.00 59.21  ? 938  GLN   B O   1 
ATOM   3864 C CB  . GLN   B 1 245 ? 46.843 -36.087 2.127   1.00 59.29  ? 938  GLN   B CB  1 
ATOM   3865 C CG  . GLN   B 1 245 ? 46.788 -36.751 3.503   1.00 62.58  ? 938  GLN   B CG  1 
ATOM   3866 C CD  . GLN   B 1 245 ? 46.544 -38.245 3.479   1.00 66.97  ? 938  GLN   B CD  1 
ATOM   3867 O OE1 . GLN   B 1 245 ? 46.698 -38.934 4.491   1.00 69.16  ? 938  GLN   B OE1 1 
ATOM   3868 N NE2 . GLN   B 1 245 ? 46.154 -38.791 2.342   1.00 67.70  ? 938  GLN   B NE2 1 
ATOM   3869 N N   . PRO   B 1 246 ? 47.985 -33.406 4.139   1.00 58.26  ? 939  PRO   B N   1 
ATOM   3870 C CA  . PRO   B 1 246 ? 49.164 -33.004 4.929   1.00 58.48  ? 939  PRO   B CA  1 
ATOM   3871 C C   . PRO   B 1 246 ? 49.919 -34.223 5.478   1.00 58.94  ? 939  PRO   B C   1 
ATOM   3872 O O   . PRO   B 1 246 ? 49.309 -35.251 5.781   1.00 58.92  ? 939  PRO   B O   1 
ATOM   3873 C CB  . PRO   B 1 246 ? 48.576 -32.113 6.044   1.00 58.88  ? 939  PRO   B CB  1 
ATOM   3874 C CG  . PRO   B 1 246 ? 47.204 -31.739 5.564   1.00 59.25  ? 939  PRO   B CG  1 
ATOM   3875 C CD  . PRO   B 1 246 ? 46.738 -32.937 4.768   1.00 57.73  ? 939  PRO   B CD  1 
ATOM   3876 N N   . PRO   B 1 247 ? 51.261 -34.141 5.551   1.00 59.03  ? 940  PRO   B N   1 
ATOM   3877 C CA  . PRO   B 1 247 ? 52.048 -35.303 6.013   1.00 59.00  ? 940  PRO   B CA  1 
ATOM   3878 C C   . PRO   B 1 247 ? 51.634 -35.925 7.349   1.00 59.08  ? 940  PRO   B C   1 
ATOM   3879 O O   . PRO   B 1 247 ? 51.707 -37.146 7.491   1.00 59.43  ? 940  PRO   B O   1 
ATOM   3880 C CB  . PRO   B 1 247 ? 53.481 -34.767 6.084   1.00 59.82  ? 940  PRO   B CB  1 
ATOM   3881 C CG  . PRO   B 1 247 ? 53.500 -33.565 5.210   1.00 60.21  ? 940  PRO   B CG  1 
ATOM   3882 C CD  . PRO   B 1 247 ? 52.118 -32.989 5.199   1.00 58.51  ? 940  PRO   B CD  1 
ATOM   3883 N N   . ILE   B 1 248 ? 51.204 -35.106 8.326   1.00 58.57  ? 941  ILE   B N   1 
ATOM   3884 C CA  . ILE   B 1 248 ? 50.837 -35.608 9.647   1.00 58.68  ? 941  ILE   B CA  1 
ATOM   3885 C C   . ILE   B 1 248 ? 49.465 -36.284 9.704   1.00 59.39  ? 941  ILE   B C   1 
ATOM   3886 O O   . ILE   B 1 248 ? 49.184 -36.991 10.667  1.00 59.55  ? 941  ILE   B O   1 
ATOM   3887 C CB  . ILE   B 1 248 ? 50.946 -34.487 10.710  1.00 58.76  ? 941  ILE   B CB  1 
ATOM   3888 C CG1 . ILE   B 1 248 ? 49.846 -33.417 10.531  1.00 59.28  ? 941  ILE   B CG1 1 
ATOM   3889 C CG2 . ILE   B 1 248 ? 52.345 -33.857 10.719  1.00 58.97  ? 941  ILE   B CG2 1 
ATOM   3890 C CD1 . ILE   B 1 248 ? 49.679 -32.532 11.714  1.00 60.04  ? 941  ILE   B CD1 1 
ATOM   3891 N N   . CYS   B 1 249 ? 48.606 -36.068 8.704   1.00 59.56  ? 942  CYS   B N   1 
ATOM   3892 C CA  . CYS   B 1 249 ? 47.251 -36.611 8.730   1.00 59.79  ? 942  CYS   B CA  1 
ATOM   3893 C C   . CYS   B 1 249 ? 47.142 -38.037 8.320   1.00 60.06  ? 942  CYS   B C   1 
ATOM   3894 O O   . CYS   B 1 249 ? 47.698 -38.427 7.298   1.00 60.98  ? 942  CYS   B O   1 
ATOM   3895 C CB  . CYS   B 1 249 ? 46.316 -35.750 7.891   1.00 60.39  ? 942  CYS   B CB  1 
ATOM   3896 S SG  . CYS   B 1 249 ? 46.160 -34.049 8.470   1.00 62.21  ? 942  CYS   B SG  1 
ATOM   3897 N N   . THR   B 1 250 ? 46.319 -38.799 9.041   1.00 59.23  ? 943  THR   B N   1 
ATOM   3898 C CA  . THR   B 1 250 ? 45.981 -40.153 8.624   1.00 58.81  ? 943  THR   B CA  1 
ATOM   3899 C C   . THR   B 1 250 ? 44.860 -40.009 7.555   1.00 58.48  ? 943  THR   B C   1 
ATOM   3900 O O   . THR   B 1 250 ? 44.364 -38.895 7.322   1.00 58.26  ? 943  THR   B O   1 
ATOM   3901 C CB  . THR   B 1 250 ? 45.527 -40.991 9.837   1.00 59.66  ? 943  THR   B CB  1 
ATOM   3902 O OG1 . THR   B 1 250 ? 44.462 -40.314 10.504  1.00 60.52  ? 943  THR   B OG1 1 
ATOM   3903 C CG2 . THR   B 1 250 ? 46.667 -41.306 10.795  1.00 59.71  ? 943  THR   B CG2 1 
ATOM   3904 N N   . ILE   B 1 251 ? 44.454 -41.115 6.909   1.00 58.38  ? 944  ILE   B N   1 
ATOM   3905 C CA  . ILE   B 1 251 ? 43.392 -41.047 5.908   1.00 58.68  ? 944  ILE   B CA  1 
ATOM   3906 C C   . ILE   B 1 251 ? 42.045 -40.636 6.552   1.00 58.48  ? 944  ILE   B C   1 
ATOM   3907 O O   . ILE   B 1 251 ? 41.263 -39.948 5.902   1.00 58.69  ? 944  ILE   B O   1 
ATOM   3908 C CB  . ILE   B 1 251 ? 43.310 -42.339 5.049   1.00 59.46  ? 944  ILE   B CB  1 
ATOM   3909 C CG1 . ILE   B 1 251 ? 42.755 -42.037 3.659   1.00 60.57  ? 944  ILE   B CG1 1 
ATOM   3910 C CG2 . ILE   B 1 251 ? 42.523 -43.438 5.738   1.00 59.91  ? 944  ILE   B CG2 1 
ATOM   3911 N N   . ASP   B 1 252 ? 41.827 -40.963 7.844   1.00 57.93  ? 945  ASP   B N   1 
ATOM   3912 C CA  . ASP   B 1 252 ? 40.610 -40.631 8.595   1.00 58.16  ? 945  ASP   B CA  1 
ATOM   3913 C C   . ASP   B 1 252 ? 40.420 -39.131 8.739   1.00 57.13  ? 945  ASP   B C   1 
ATOM   3914 O O   . ASP   B 1 252 ? 39.290 -38.646 8.654   1.00 57.69  ? 945  ASP   B O   1 
ATOM   3915 C CB  . ASP   B 1 252 ? 40.644 -41.267 9.999   1.00 61.53  ? 945  ASP   B CB  1 
ATOM   3916 C CG  . ASP   B 1 252 ? 41.027 -42.732 10.000  1.00 68.81  ? 945  ASP   B CG  1 
ATOM   3917 O OD1 . ASP   B 1 252 ? 42.223 -43.038 9.766   1.00 70.23  ? 945  ASP   B OD1 1 
ATOM   3918 O OD2 . ASP   B 1 252 ? 40.136 -43.576 10.237  1.00 71.97  ? 945  ASP   B OD2 1 
ATOM   3919 N N   . VAL   B 1 253 ? 41.515 -38.396 8.989   1.00 55.31  ? 946  VAL   B N   1 
ATOM   3920 C CA  . VAL   B 1 253 ? 41.438 -36.954 9.134   1.00 54.13  ? 946  VAL   B CA  1 
ATOM   3921 C C   . VAL   B 1 253 ? 41.282 -36.306 7.764   1.00 53.53  ? 946  VAL   B C   1 
ATOM   3922 O O   . VAL   B 1 253 ? 40.429 -35.436 7.587   1.00 53.22  ? 946  VAL   B O   1 
ATOM   3923 C CB  . VAL   B 1 253 ? 42.657 -36.396 9.898   1.00 53.90  ? 946  VAL   B CB  1 
ATOM   3924 C CG1 . VAL   B 1 253 ? 42.589 -34.874 10.008  1.00 53.77  ? 946  VAL   B CG1 1 
ATOM   3925 C CG2 . VAL   B 1 253 ? 42.746 -37.032 11.273  1.00 54.17  ? 946  VAL   B CG2 1 
ATOM   3926 N N   . TYR   B 1 254 ? 42.077 -36.754 6.790   1.00 53.34  ? 947  TYR   B N   1 
ATOM   3927 C CA  . TYR   B 1 254 ? 42.015 -36.197 5.449   1.00 54.25  ? 947  TYR   B CA  1 
ATOM   3928 C C   . TYR   B 1 254 ? 40.650 -36.364 4.796   1.00 54.15  ? 947  TYR   B C   1 
ATOM   3929 O O   . TYR   B 1 254 ? 40.188 -35.445 4.119   1.00 54.31  ? 947  TYR   B O   1 
ATOM   3930 C CB  . TYR   B 1 254 ? 43.131 -36.725 4.540   1.00 54.71  ? 947  TYR   B CB  1 
ATOM   3931 C CG  . TYR   B 1 254 ? 43.141 -35.986 3.223   1.00 56.15  ? 947  TYR   B CG  1 
ATOM   3932 C CD1 . TYR   B 1 254 ? 43.331 -34.610 3.177   1.00 57.54  ? 947  TYR   B CD1 1 
ATOM   3933 C CD2 . TYR   B 1 254 ? 42.840 -36.638 2.037   1.00 57.18  ? 947  TYR   B CD2 1 
ATOM   3934 C CE1 . TYR   B 1 254 ? 43.271 -33.912 1.975   1.00 58.68  ? 947  TYR   B CE1 1 
ATOM   3935 C CE2 . TYR   B 1 254 ? 42.768 -35.950 0.831   1.00 58.26  ? 947  TYR   B CE2 1 
ATOM   3936 C CZ  . TYR   B 1 254 ? 42.994 -34.588 0.803   1.00 59.70  ? 947  TYR   B CZ  1 
ATOM   3937 O OH  . TYR   B 1 254 ? 42.933 -33.904 -0.388  1.00 62.06  ? 947  TYR   B OH  1 
ATOM   3938 N N   . MET   B 1 255 ? 39.985 -37.499 5.037   1.00 53.50  ? 948  MET   B N   1 
ATOM   3939 C CA  . MET   B 1 255 ? 38.671 -37.729 4.469   1.00 53.56  ? 948  MET   B CA  1 
ATOM   3940 C C   . MET   B 1 255 ? 37.637 -36.739 4.972   1.00 53.16  ? 948  MET   B C   1 
ATOM   3941 O O   . MET   B 1 255 ? 36.752 -36.375 4.213   1.00 53.83  ? 948  MET   B O   1 
ATOM   3942 C CB  . MET   B 1 255 ? 38.223 -39.177 4.642   1.00 54.67  ? 948  MET   B CB  1 
ATOM   3943 C CG  . MET   B 1 255 ? 38.863 -40.117 3.619   1.00 58.44  ? 948  MET   B CG  1 
ATOM   3944 S SD  . MET   B 1 255 ? 38.534 -39.687 1.873   1.00 68.15  ? 948  MET   B SD  1 
ATOM   3945 C CE  . MET   B 1 255 ? 40.051 -38.867 1.433   1.00 65.63  ? 948  MET   B CE  1 
ATOM   3946 N N   . ILE   B 1 256 ? 37.770 -36.261 6.208   1.00 52.17  ? 949  ILE   B N   1 
ATOM   3947 C CA  . ILE   B 1 256 ? 36.862 -35.268 6.770   1.00 51.97  ? 949  ILE   B CA  1 
ATOM   3948 C C   . ILE   B 1 256 ? 37.059 -33.929 6.054   1.00 51.54  ? 949  ILE   B C   1 
ATOM   3949 O O   . ILE   B 1 256 ? 36.073 -33.306 5.667   1.00 52.20  ? 949  ILE   B O   1 
ATOM   3950 C CB  . ILE   B 1 256 ? 37.063 -35.143 8.300   1.00 52.68  ? 949  ILE   B CB  1 
ATOM   3951 C CG1 . ILE   B 1 256 ? 36.616 -36.426 9.019   1.00 53.11  ? 949  ILE   B CG1 1 
ATOM   3952 C CG2 . ILE   B 1 256 ? 36.338 -33.921 8.851   1.00 53.72  ? 949  ILE   B CG2 1 
ATOM   3953 C CD1 . ILE   B 1 256 ? 36.929 -36.415 10.525  1.00 54.40  ? 949  ILE   B CD1 1 
ATOM   3954 N N   . MET   B 1 257 ? 38.328 -33.515 5.824   1.00 50.24  ? 950  MET   B N   1 
ATOM   3955 C CA  . MET   B 1 257 ? 38.657 -32.293 5.088   1.00 49.39  ? 950  MET   B CA  1 
ATOM   3956 C C   . MET   B 1 257 ? 38.107 -32.396 3.675   1.00 48.82  ? 950  MET   B C   1 
ATOM   3957 O O   . MET   B 1 257 ? 37.440 -31.493 3.204   1.00 49.26  ? 950  MET   B O   1 
ATOM   3958 C CB  . MET   B 1 257 ? 40.179 -32.099 5.017   1.00 50.25  ? 950  MET   B CB  1 
ATOM   3959 C CG  . MET   B 1 257 ? 40.788 -31.525 6.265   1.00 53.52  ? 950  MET   B CG  1 
ATOM   3960 S SD  . MET   B 1 257 ? 42.590 -31.385 6.100   1.00 57.73  ? 950  MET   B SD  1 
ATOM   3961 C CE  . MET   B 1 257 ? 43.068 -32.758 7.084   1.00 52.75  ? 950  MET   B CE  1 
ATOM   3962 N N   . ARG   B 1 258 ? 38.339 -33.528 3.029   1.00 48.30  ? 951  ARG   B N   1 
ATOM   3963 C CA  . ARG   B 1 258 ? 37.911 -33.856 1.685   1.00 48.39  ? 951  ARG   B CA  1 
ATOM   3964 C C   . ARG   B 1 258 ? 36.392 -33.762 1.533   1.00 47.76  ? 951  ARG   B C   1 
ATOM   3965 O O   . ARG   B 1 258 ? 35.935 -33.247 0.527   1.00 48.14  ? 951  ARG   B O   1 
ATOM   3966 C CB  . ARG   B 1 258 ? 38.447 -35.252 1.330   1.00 50.95  ? 951  ARG   B CB  1 
ATOM   3967 C CG  . ARG   B 1 258 ? 38.275 -35.708 -0.108  1.00 55.96  ? 951  ARG   B CG  1 
ATOM   3968 C CD  . ARG   B 1 258 ? 38.855 -34.739 -1.119  1.00 61.00  ? 951  ARG   B CD  1 
ATOM   3969 N NE  . ARG   B 1 258 ? 37.774 -33.977 -1.741  1.00 65.54  ? 951  ARG   B NE  1 
ATOM   3970 C CZ  . ARG   B 1 258 ? 37.264 -34.233 -2.934  1.00 69.30  ? 951  ARG   B CZ  1 
ATOM   3971 N NH1 . ARG   B 1 258 ? 37.779 -35.190 -3.692  1.00 71.68  ? 951  ARG   B NH1 1 
ATOM   3972 N NH2 . ARG   B 1 258 ? 36.263 -33.505 -3.401  1.00 69.60  ? 951  ARG   B NH2 1 
ATOM   3973 N N   . LYS   B 1 259 ? 35.606 -34.198 2.540   1.00 47.03  ? 952  LYS   B N   1 
ATOM   3974 C CA  . LYS   B 1 259 ? 34.143 -34.096 2.496   1.00 46.77  ? 952  LYS   B CA  1 
ATOM   3975 C C   . LYS   B 1 259 ? 33.660 -32.634 2.603   1.00 46.67  ? 952  LYS   B C   1 
ATOM   3976 O O   . LYS   B 1 259 ? 32.591 -32.310 2.104   1.00 46.63  ? 952  LYS   B O   1 
ATOM   3977 C CB  . LYS   B 1 259 ? 33.475 -34.988 3.550   1.00 48.25  ? 952  LYS   B CB  1 
ATOM   3978 C CG  . LYS   B 1 259 ? 33.627 -36.487 3.285   1.00 52.07  ? 952  LYS   B CG  1 
ATOM   3979 N N   . CYS   B 1 260 ? 34.444 -31.751 3.250   1.00 46.61  ? 953  CYS   B N   1 
ATOM   3980 C CA  . CYS   B 1 260 ? 34.151 -30.311 3.303   1.00 46.70  ? 953  CYS   B CA  1 
ATOM   3981 C C   . CYS   B 1 260 ? 34.240 -29.670 1.908   1.00 47.12  ? 953  CYS   B C   1 
ATOM   3982 O O   . CYS   B 1 260 ? 33.671 -28.605 1.696   1.00 47.36  ? 953  CYS   B O   1 
ATOM   3983 C CB  . CYS   B 1 260 ? 35.083 -29.594 4.276   1.00 46.70  ? 953  CYS   B CB  1 
ATOM   3984 S SG  . CYS   B 1 260 ? 34.854 -30.053 6.007   1.00 48.52  ? 953  CYS   B SG  1 
ATOM   3985 N N   . TRP   B 1 261 ? 34.980 -30.301 0.972   1.00 47.27  ? 954  TRP   B N   1 
ATOM   3986 C CA  . TRP   B 1 261 ? 35.234 -29.791 -0.361  1.00 47.37  ? 954  TRP   B CA  1 
ATOM   3987 C C   . TRP   B 1 261 ? 34.450 -30.490 -1.438  1.00 49.27  ? 954  TRP   B C   1 
ATOM   3988 O O   . TRP   B 1 261 ? 34.930 -30.624 -2.568  1.00 49.77  ? 954  TRP   B O   1 
ATOM   3989 C CB  . TRP   B 1 261 ? 36.731 -29.809 -0.671  1.00 46.44  ? 954  TRP   B CB  1 
ATOM   3990 C CG  . TRP   B 1 261 ? 37.576 -29.168 0.383   1.00 45.78  ? 954  TRP   B CG  1 
ATOM   3991 C CD1 . TRP   B 1 261 ? 37.283 -28.048 1.108   1.00 46.40  ? 954  TRP   B CD1 1 
ATOM   3992 C CD2 . TRP   B 1 261 ? 38.848 -29.628 0.848   1.00 45.36  ? 954  TRP   B CD2 1 
ATOM   3993 N NE1 . TRP   B 1 261 ? 38.298 -27.784 1.995   1.00 46.70  ? 954  TRP   B NE1 1 
ATOM   3994 C CE2 . TRP   B 1 261 ? 39.283 -28.729 1.842   1.00 46.09  ? 954  TRP   B CE2 1 
ATOM   3995 C CE3 . TRP   B 1 261 ? 39.680 -30.697 0.498   1.00 45.39  ? 954  TRP   B CE3 1 
ATOM   3996 C CZ2 . TRP   B 1 261 ? 40.507 -28.874 2.492   1.00 46.12  ? 954  TRP   B CZ2 1 
ATOM   3997 C CZ3 . TRP   B 1 261 ? 40.883 -30.848 1.155   1.00 45.68  ? 954  TRP   B CZ3 1 
ATOM   3998 C CH2 . TRP   B 1 261 ? 41.287 -29.942 2.137   1.00 45.98  ? 954  TRP   B CH2 1 
ATOM   3999 N N   . MET   B 1 262 ? 33.227 -30.886 -1.122  1.00 50.40  ? 955  MET   B N   1 
ATOM   4000 C CA  . MET   B 1 262 ? 32.361 -31.494 -2.111  1.00 52.61  ? 955  MET   B CA  1 
ATOM   4001 C C   . MET   B 1 262 ? 31.667 -30.425 -2.957  1.00 54.35  ? 955  MET   B C   1 
ATOM   4002 O O   . MET   B 1 262 ? 31.408 -29.342 -2.462  1.00 53.81  ? 955  MET   B O   1 
ATOM   4003 C CB  . MET   B 1 262 ? 31.355 -32.408 -1.435  1.00 54.13  ? 955  MET   B CB  1 
ATOM   4004 C CG  . MET   B 1 262 ? 32.001 -33.626 -0.868  1.00 58.89  ? 955  MET   B CG  1 
ATOM   4005 S SD  . MET   B 1 262 ? 30.718 -34.730 -0.343  1.00 74.47  ? 955  MET   B SD  1 
ATOM   4006 C CE  . MET   B 1 262 ? 31.661 -35.996 0.349   1.00 77.99  ? 955  MET   B CE  1 
ATOM   4007 N N   . ILE   B 1 263 ? 31.380 -30.724 -4.237  1.00 56.00  ? 956  ILE   B N   1 
ATOM   4008 C CA  . ILE   B 1 263 ? 30.699 -29.809 -5.140  1.00 58.28  ? 956  ILE   B CA  1 
ATOM   4009 C C   . ILE   B 1 263 ? 29.289 -29.544 -4.600  1.00 60.19  ? 956  ILE   B C   1 
ATOM   4010 O O   . ILE   B 1 263 ? 28.883 -28.388 -4.491  1.00 61.02  ? 956  ILE   B O   1 
ATOM   4011 C CB  . ILE   B 1 263 ? 30.654 -30.405 -6.587  1.00 59.64  ? 956  ILE   B CB  1 
ATOM   4012 C CG1 . ILE   B 1 263 ? 32.064 -30.572 -7.166  1.00 61.18  ? 956  ILE   B CG1 1 
ATOM   4013 C CG2 . ILE   B 1 263 ? 29.787 -29.559 -7.512  1.00 59.66  ? 956  ILE   B CG2 1 
ATOM   4014 C CD1 . ILE   B 1 263 ? 32.889 -29.291 -7.230  1.00 63.09  ? 956  ILE   B CD1 1 
ATOM   4015 N N   . ASP   B 1 264 ? 28.555 -30.613 -4.233  1.00 60.75  ? 957  ASP   B N   1 
ATOM   4016 C CA  . ASP   B 1 264 ? 27.209 -30.478 -3.674  1.00 61.33  ? 957  ASP   B CA  1 
ATOM   4017 C C   . ASP   B 1 264 ? 27.317 -30.017 -2.230  1.00 60.51  ? 957  ASP   B C   1 
ATOM   4018 O O   . ASP   B 1 264 ? 27.849 -30.742 -1.391  1.00 60.33  ? 957  ASP   B O   1 
ATOM   4019 C CB  . ASP   B 1 264 ? 26.437 -31.806 -3.763  1.00 64.21  ? 957  ASP   B CB  1 
ATOM   4020 C CG  . ASP   B 1 264 ? 25.029 -31.740 -3.195  1.00 71.46  ? 957  ASP   B CG  1 
ATOM   4021 O OD1 . ASP   B 1 264 ? 24.434 -30.639 -3.209  1.00 73.39  ? 957  ASP   B OD1 1 
ATOM   4022 O OD2 . ASP   B 1 264 ? 24.520 -32.789 -2.745  1.00 74.31  ? 957  ASP   B OD2 1 
ATOM   4023 N N   . ALA   B 1 265 ? 26.823 -28.804 -1.944  1.00 60.09  ? 958  ALA   B N   1 
ATOM   4024 C CA  . ALA   B 1 265 ? 26.895 -28.192 -0.614  1.00 59.58  ? 958  ALA   B CA  1 
ATOM   4025 C C   . ALA   B 1 265 ? 26.154 -28.995 0.455   1.00 59.66  ? 958  ALA   B C   1 
ATOM   4026 O O   . ALA   B 1 265 ? 26.643 -29.106 1.571   1.00 59.69  ? 958  ALA   B O   1 
ATOM   4027 C CB  . ALA   B 1 265 ? 26.377 -26.765 -0.664  1.00 59.04  ? 958  ALA   B CB  1 
ATOM   4028 N N   . ASP   B 1 266 ? 24.998 -29.583 0.107   1.00 59.62  ? 959  ASP   B N   1 
ATOM   4029 C CA  . ASP   B 1 266 ? 24.213 -30.393 1.038   1.00 59.93  ? 959  ASP   B CA  1 
ATOM   4030 C C   . ASP   B 1 266 ? 24.862 -31.727 1.404   1.00 58.79  ? 959  ASP   B C   1 
ATOM   4031 O O   . ASP   B 1 266 ? 24.473 -32.335 2.399   1.00 59.29  ? 959  ASP   B O   1 
ATOM   4032 C CB  . ASP   B 1 266 ? 22.786 -30.610 0.520   1.00 63.32  ? 959  ASP   B CB  1 
ATOM   4033 C CG  . ASP   B 1 266 ? 21.970 -29.331 0.519   1.00 71.21  ? 959  ASP   B CG  1 
ATOM   4034 O OD1 . ASP   B 1 266 ? 22.220 -28.465 1.394   1.00 72.51  ? 959  ASP   B OD1 1 
ATOM   4035 O OD2 . ASP   B 1 266 ? 21.082 -29.192 -0.358  1.00 74.79  ? 959  ASP   B OD2 1 
ATOM   4036 N N   . SER   B 1 267 ? 25.836 -32.194 0.610   1.00 57.13  ? 960  SER   B N   1 
ATOM   4037 C CA  . SER   B 1 267 ? 26.564 -33.428 0.921   1.00 55.49  ? 960  SER   B CA  1 
ATOM   4038 C C   . SER   B 1 267 ? 27.736 -33.183 1.883   1.00 53.62  ? 960  SER   B C   1 
ATOM   4039 O O   . SER   B 1 267 ? 28.239 -34.132 2.472   1.00 53.78  ? 960  SER   B O   1 
ATOM   4040 C CB  . SER   B 1 267 ? 27.053 -34.099 -0.353  1.00 56.52  ? 960  SER   B CB  1 
ATOM   4041 O OG  . SER   B 1 267 ? 25.941 -34.446 -1.157  1.00 59.50  ? 960  SER   B OG  1 
ATOM   4042 N N   . ARG   B 1 268 ? 28.168 -31.927 2.054   1.00 52.01  ? 961  ARG   B N   1 
ATOM   4043 C CA  . ARG   B 1 268 ? 29.233 -31.594 2.994   1.00 51.10  ? 961  ARG   B CA  1 
ATOM   4044 C C   . ARG   B 1 268 ? 28.753 -31.817 4.434   1.00 51.40  ? 961  ARG   B C   1 
ATOM   4045 O O   . ARG   B 1 268 ? 27.578 -31.606 4.740   1.00 51.72  ? 961  ARG   B O   1 
ATOM   4046 C CB  . ARG   B 1 268 ? 29.657 -30.128 2.828   1.00 50.26  ? 961  ARG   B CB  1 
ATOM   4047 C CG  . ARG   B 1 268 ? 30.258 -29.840 1.484   1.00 49.52  ? 961  ARG   B CG  1 
ATOM   4048 C CD  . ARG   B 1 268 ? 30.475 -28.360 1.307   1.00 49.35  ? 961  ARG   B CD  1 
ATOM   4049 N NE  . ARG   B 1 268 ? 30.618 -28.047 -0.110  1.00 49.04  ? 961  ARG   B NE  1 
ATOM   4050 C CZ  . ARG   B 1 268 ? 30.281 -26.893 -0.667  1.00 48.70  ? 961  ARG   B CZ  1 
ATOM   4051 N NH1 . ARG   B 1 268 ? 29.801 -25.904 0.076   1.00 48.24  ? 961  ARG   B NH1 1 
ATOM   4052 N NH2 . ARG   B 1 268 ? 30.417 -26.718 -1.974  1.00 47.01  ? 961  ARG   B NH2 1 
ATOM   4053 N N   . PRO   B 1 269 ? 29.650 -32.222 5.341   1.00 51.14  ? 962  PRO   B N   1 
ATOM   4054 C CA  . PRO   B 1 269 ? 29.245 -32.406 6.740   1.00 50.90  ? 962  PRO   B CA  1 
ATOM   4055 C C   . PRO   B 1 269 ? 28.716 -31.123 7.377   1.00 50.32  ? 962  PRO   B C   1 
ATOM   4056 O O   . PRO   B 1 269 ? 28.997 -30.027 6.905   1.00 50.98  ? 962  PRO   B O   1 
ATOM   4057 C CB  . PRO   B 1 269 ? 30.552 -32.829 7.422   1.00 51.93  ? 962  PRO   B CB  1 
ATOM   4058 C CG  . PRO   B 1 269 ? 31.639 -32.273 6.537   1.00 52.37  ? 962  PRO   B CG  1 
ATOM   4059 C CD  . PRO   B 1 269 ? 31.085 -32.498 5.163   1.00 50.97  ? 962  PRO   B CD  1 
ATOM   4060 N N   . LYS   B 1 270 ? 27.943 -31.259 8.447   1.00 48.71  ? 963  LYS   B N   1 
ATOM   4061 C CA  . LYS   B 1 270 ? 27.439 -30.108 9.183   1.00 47.38  ? 963  LYS   B CA  1 
ATOM   4062 C C   . LYS   B 1 270 ? 28.409 -29.825 10.333  1.00 46.02  ? 963  LYS   B C   1 
ATOM   4063 O O   . LYS   B 1 270 ? 29.100 -30.741 10.782  1.00 46.14  ? 963  LYS   B O   1 
ATOM   4064 C CB  . LYS   B 1 270 ? 26.027 -30.396 9.710   1.00 48.58  ? 963  LYS   B CB  1 
ATOM   4065 C CG  . LYS   B 1 270 ? 25.059 -30.846 8.618   1.00 51.16  ? 963  LYS   B CG  1 
ATOM   4066 C CD  . LYS   B 1 270 ? 24.306 -29.681 8.000   1.00 54.71  ? 963  LYS   B CD  1 
ATOM   4067 N N   . PHE   B 1 271 ? 28.456 -28.580 10.839  1.00 44.75  ? 964  PHE   B N   1 
ATOM   4068 C CA  . PHE   B 1 271 ? 29.342 -28.242 11.963  1.00 43.87  ? 964  PHE   B CA  1 
ATOM   4069 C C   . PHE   B 1 271 ? 29.064 -29.095 13.192  1.00 43.91  ? 964  PHE   B C   1 
ATOM   4070 O O   . PHE   B 1 271 ? 29.997 -29.480 13.880  1.00 43.97  ? 964  PHE   B O   1 
ATOM   4071 C CB  . PHE   B 1 271 ? 29.294 -26.759 12.311  1.00 43.02  ? 964  PHE   B CB  1 
ATOM   4072 C CG  . PHE   B 1 271 ? 29.970 -25.884 11.295  1.00 42.95  ? 964  PHE   B CG  1 
ATOM   4073 C CD1 . PHE   B 1 271 ? 31.324 -26.011 11.041  1.00 43.03  ? 964  PHE   B CD1 1 
ATOM   4074 C CD2 . PHE   B 1 271 ? 29.257 -24.919 10.604  1.00 43.18  ? 964  PHE   B CD2 1 
ATOM   4075 C CE1 . PHE   B 1 271 ? 31.942 -25.205 10.101  1.00 43.20  ? 964  PHE   B CE1 1 
ATOM   4076 C CE2 . PHE   B 1 271 ? 29.881 -24.109 9.676   1.00 43.08  ? 964  PHE   B CE2 1 
ATOM   4077 C CZ  . PHE   B 1 271 ? 31.217 -24.262 9.428   1.00 42.75  ? 964  PHE   B CZ  1 
ATOM   4078 N N   . ARG   B 1 272 ? 27.797 -29.455 13.409  1.00 44.11  ? 965  ARG   B N   1 
ATOM   4079 C CA  . ARG   B 1 272 ? 27.351 -30.331 14.482  1.00 45.33  ? 965  ARG   B CA  1 
ATOM   4080 C C   . ARG   B 1 272 ? 28.037 -31.709 14.379  1.00 45.37  ? 965  ARG   B C   1 
ATOM   4081 O O   . ARG   B 1 272 ? 28.435 -32.270 15.399  1.00 45.74  ? 965  ARG   B O   1 
ATOM   4082 C CB  . ARG   B 1 272 ? 25.833 -30.502 14.382  1.00 48.03  ? 965  ARG   B CB  1 
ATOM   4083 C CG  . ARG   B 1 272 ? 25.204 -31.036 15.638  1.00 54.45  ? 965  ARG   B CG  1 
ATOM   4084 C CD  . ARG   B 1 272 ? 23.816 -31.582 15.364  1.00 61.23  ? 965  ARG   B CD  1 
ATOM   4085 N NE  . ARG   B 1 272 ? 23.787 -32.721 14.440  1.00 66.12  ? 965  ARG   B NE  1 
ATOM   4086 C CZ  . ARG   B 1 272 ? 23.973 -33.989 14.802  1.00 68.16  ? 965  ARG   B CZ  1 
ATOM   4087 N NH1 . ARG   B 1 272 ? 23.896 -34.961 13.900  1.00 67.35  ? 965  ARG   B NH1 1 
ATOM   4088 N NH2 . ARG   B 1 272 ? 24.245 -34.293 16.066  1.00 67.83  ? 965  ARG   B NH2 1 
ATOM   4089 N N   . GLU   B 1 273 ? 28.163 -32.250 13.150  1.00 44.74  ? 966  GLU   B N   1 
ATOM   4090 C CA  . GLU   B 1 273 ? 28.806 -33.532 12.868  1.00 44.70  ? 966  GLU   B CA  1 
ATOM   4091 C C   . GLU   B 1 273 ? 30.323 -33.425 12.991  1.00 44.01  ? 966  GLU   B C   1 
ATOM   4092 O O   . GLU   B 1 273 ? 30.963 -34.312 13.550  1.00 43.80  ? 966  GLU   B O   1 
ATOM   4093 C CB  . GLU   B 1 273 ? 28.417 -34.028 11.466  1.00 47.47  ? 966  GLU   B CB  1 
ATOM   4094 C CG  . GLU   B 1 273 ? 26.915 -34.112 11.250  1.00 53.82  ? 966  GLU   B CG  1 
ATOM   4095 C CD  . GLU   B 1 273 ? 26.483 -34.379 9.817   1.00 63.31  ? 966  GLU   B CD  1 
ATOM   4096 O OE1 . GLU   B 1 273 ? 27.344 -34.304 8.909   1.00 65.00  ? 966  GLU   B OE1 1 
ATOM   4097 O OE2 . GLU   B 1 273 ? 25.276 -34.642 9.598   1.00 66.35  ? 966  GLU   B OE2 1 
ATOM   4098 N N   . LEU   B 1 274 ? 30.900 -32.332 12.475  1.00 43.76  ? 967  LEU   B N   1 
ATOM   4099 C CA  . LEU   B 1 274 ? 32.329 -32.056 12.580  1.00 43.61  ? 967  LEU   B CA  1 
ATOM   4100 C C   . LEU   B 1 274 ? 32.766 -31.970 14.061  1.00 43.88  ? 967  LEU   B C   1 
ATOM   4101 O O   . LEU   B 1 274 ? 33.869 -32.389 14.388  1.00 44.63  ? 967  LEU   B O   1 
ATOM   4102 C CB  . LEU   B 1 274 ? 32.664 -30.746 11.870  1.00 43.38  ? 967  LEU   B CB  1 
ATOM   4103 C CG  . LEU   B 1 274 ? 32.497 -30.757 10.363  1.00 43.82  ? 967  LEU   B CG  1 
ATOM   4104 C CD1 . LEU   B 1 274 ? 32.511 -29.351 9.811   1.00 43.52  ? 967  LEU   B CD1 1 
ATOM   4105 C CD2 . LEU   B 1 274 ? 33.560 -31.627 9.701   1.00 44.33  ? 967  LEU   B CD2 1 
ATOM   4106 N N   . ILE   B 1 275 ? 31.892 -31.472 14.962  1.00 42.91  ? 968  ILE   B N   1 
ATOM   4107 C CA  . ILE   B 1 275 ? 32.212 -31.406 16.392  1.00 42.56  ? 968  ILE   B CA  1 
ATOM   4108 C C   . ILE   B 1 275 ? 32.364 -32.827 16.919  1.00 43.41  ? 968  ILE   B C   1 
ATOM   4109 O O   . ILE   B 1 275 ? 33.355 -33.121 17.564  1.00 43.86  ? 968  ILE   B O   1 
ATOM   4110 C CB  . ILE   B 1 275 ? 31.145 -30.629 17.212  1.00 41.68  ? 968  ILE   B CB  1 
ATOM   4111 C CG1 . ILE   B 1 275 ? 31.106 -29.139 16.833  1.00 41.02  ? 968  ILE   B CG1 1 
ATOM   4112 C CG2 . ILE   B 1 275 ? 31.357 -30.812 18.721  1.00 41.49  ? 968  ILE   B CG2 1 
ATOM   4113 C CD1 . ILE   B 1 275 ? 29.886 -28.462 17.258  1.00 40.64  ? 968  ILE   B CD1 1 
ATOM   4114 N N   . ILE   B 1 276 ? 31.406 -33.708 16.590  1.00 43.32  ? 969  ILE   B N   1 
ATOM   4115 C CA  . ILE   B 1 276 ? 31.420 -35.095 17.003  1.00 43.65  ? 969  ILE   B CA  1 
ATOM   4116 C C   . ILE   B 1 276 ? 32.638 -35.837 16.471  1.00 44.83  ? 969  ILE   B C   1 
ATOM   4117 O O   . ILE   B 1 276 ? 33.331 -36.479 17.259  1.00 46.30  ? 969  ILE   B O   1 
ATOM   4118 C CB  . ILE   B 1 276 ? 30.081 -35.772 16.632  1.00 43.63  ? 969  ILE   B CB  1 
ATOM   4119 C CG1 . ILE   B 1 276 ? 28.906 -35.068 17.349  1.00 44.03  ? 969  ILE   B CG1 1 
ATOM   4120 C CG2 . ILE   B 1 276 ? 30.102 -37.286 16.922  1.00 43.13  ? 969  ILE   B CG2 1 
ATOM   4121 C CD1 . ILE   B 1 276 ? 27.529 -35.434 16.755  1.00 44.40  ? 969  ILE   B CD1 1 
ATOM   4122 N N   . GLU   B 1 277 ? 32.932 -35.724 15.168  1.00 44.54  ? 970  GLU   B N   1 
ATOM   4123 C CA  . GLU   B 1 277 ? 34.093 -36.386 14.570  1.00 44.73  ? 970  GLU   B CA  1 
ATOM   4124 C C   . GLU   B 1 277 ? 35.411 -35.944 15.198  1.00 44.83  ? 970  GLU   B C   1 
ATOM   4125 O O   . GLU   B 1 277 ? 36.157 -36.791 15.690  1.00 44.81  ? 970  GLU   B O   1 
ATOM   4126 C CB  . GLU   B 1 277 ? 34.130 -36.200 13.047  1.00 46.81  ? 970  GLU   B CB  1 
ATOM   4127 C CG  . GLU   B 1 277 ? 32.963 -36.865 12.341  1.00 53.44  ? 970  GLU   B CG  1 
ATOM   4128 N N   . PHE   B 1 278 ? 35.694 -34.634 15.210  1.00 44.79  ? 971  PHE   B N   1 
ATOM   4129 C CA  . PHE   B 1 278 ? 36.935 -34.139 15.796  1.00 45.44  ? 971  PHE   B CA  1 
ATOM   4130 C C   . PHE   B 1 278 ? 37.014 -34.356 17.300  1.00 45.61  ? 971  PHE   B C   1 
ATOM   4131 O O   . PHE   B 1 278 ? 38.119 -34.473 17.829  1.00 46.21  ? 971  PHE   B O   1 
ATOM   4132 C CB  . PHE   B 1 278 ? 37.191 -32.678 15.423  1.00 45.67  ? 971  PHE   B CB  1 
ATOM   4133 C CG  . PHE   B 1 278 ? 37.740 -32.520 14.029  1.00 46.58  ? 971  PHE   B CG  1 
ATOM   4134 C CD1 . PHE   B 1 278 ? 39.064 -32.796 13.754  1.00 47.73  ? 971  PHE   B CD1 1 
ATOM   4135 C CD2 . PHE   B 1 278 ? 36.928 -32.115 12.991  1.00 47.48  ? 971  PHE   B CD2 1 
ATOM   4136 C CE1 . PHE   B 1 278 ? 39.569 -32.648 12.466  1.00 48.71  ? 971  PHE   B CE1 1 
ATOM   4137 C CE2 . PHE   B 1 278 ? 37.436 -31.958 11.706  1.00 48.52  ? 971  PHE   B CE2 1 
ATOM   4138 C CZ  . PHE   B 1 278 ? 38.750 -32.231 11.447  1.00 48.38  ? 971  PHE   B CZ  1 
ATOM   4139 N N   . SER   B 1 279 ? 35.862 -34.433 17.994  1.00 44.98  ? 972  SER   B N   1 
ATOM   4140 C CA  . SER   B 1 279 ? 35.850 -34.698 19.432  1.00 45.04  ? 972  SER   B CA  1 
ATOM   4141 C C   . SER   B 1 279 ? 36.284 -36.123 19.710  1.00 45.51  ? 972  SER   B C   1 
ATOM   4142 O O   . SER   B 1 279 ? 36.975 -36.348 20.694  1.00 46.50  ? 972  SER   B O   1 
ATOM   4143 C CB  . SER   B 1 279 ? 34.472 -34.457 20.032  1.00 45.77  ? 972  SER   B CB  1 
ATOM   4144 O OG  . SER   B 1 279 ? 34.231 -33.069 20.178  1.00 47.70  ? 972  SER   B OG  1 
ATOM   4145 N N   . LYS   B 1 280 ? 35.879 -37.076 18.856  1.00 44.79  ? 973  LYS   B N   1 
ATOM   4146 C CA  . LYS   B 1 280 ? 36.265 -38.466 18.975  1.00 45.76  ? 973  LYS   B CA  1 
ATOM   4147 C C   . LYS   B 1 280 ? 37.777 -38.587 18.770  1.00 47.16  ? 973  LYS   B C   1 
ATOM   4148 O O   . LYS   B 1 280 ? 38.454 -39.259 19.542  1.00 47.70  ? 973  LYS   B O   1 
ATOM   4149 C CB  . LYS   B 1 280 ? 35.488 -39.325 17.949  1.00 46.72  ? 973  LYS   B CB  1 
ATOM   4150 C CG  . LYS   B 1 280 ? 35.971 -40.765 17.864  1.00 49.74  ? 973  LYS   B CG  1 
ATOM   4151 C CD  . LYS   B 1 280 ? 35.332 -41.505 16.717  1.00 54.55  ? 973  LYS   B CD  1 
ATOM   4152 N N   . MET   B 1 281 ? 38.303 -37.904 17.748  1.00 47.62  ? 974  MET   B N   1 
ATOM   4153 C CA  . MET   B 1 281 ? 39.721 -37.911 17.439  1.00 48.46  ? 974  MET   B CA  1 
ATOM   4154 C C   . MET   B 1 281 ? 40.567 -37.271 18.516  1.00 49.71  ? 974  MET   B C   1 
ATOM   4155 O O   . MET   B 1 281 ? 41.656 -37.761 18.791  1.00 49.87  ? 974  MET   B O   1 
ATOM   4156 C CB  . MET   B 1 281 ? 39.979 -37.268 16.087  1.00 48.80  ? 974  MET   B CB  1 
ATOM   4157 C CG  . MET   B 1 281 ? 39.299 -38.008 14.984  1.00 51.05  ? 974  MET   B CG  1 
ATOM   4158 S SD  . MET   B 1 281 ? 39.678 -37.335 13.357  1.00 56.95  ? 974  MET   B SD  1 
ATOM   4159 C CE  . MET   B 1 281 ? 39.119 -38.714 12.343  1.00 53.19  ? 974  MET   B CE  1 
ATOM   4160 N N   . ALA   B 1 282 ? 40.075 -36.198 19.145  1.00 50.40  ? 975  ALA   B N   1 
ATOM   4161 C CA  . ALA   B 1 282 ? 40.813 -35.549 20.229  1.00 51.54  ? 975  ALA   B CA  1 
ATOM   4162 C C   . ALA   B 1 282 ? 40.923 -36.426 21.483  1.00 52.25  ? 975  ALA   B C   1 
ATOM   4163 O O   . ALA   B 1 282 ? 41.805 -36.198 22.290  1.00 52.50  ? 975  ALA   B O   1 
ATOM   4164 C CB  . ALA   B 1 282 ? 40.181 -34.211 20.571  1.00 51.91  ? 975  ALA   B CB  1 
ATOM   4165 N N   . ARG   B 1 283 ? 40.050 -37.430 21.643  1.00 52.82  ? 976  ARG   B N   1 
ATOM   4166 C CA  . ARG   B 1 283 ? 40.132 -38.352 22.770  1.00 53.59  ? 976  ARG   B CA  1 
ATOM   4167 C C   . ARG   B 1 283 ? 41.298 -39.351 22.621  1.00 54.96  ? 976  ARG   B C   1 
ATOM   4168 O O   . ARG   B 1 283 ? 41.798 -39.849 23.625  1.00 55.52  ? 976  ARG   B O   1 
ATOM   4169 C CB  . ARG   B 1 283 ? 38.798 -39.060 22.990  1.00 54.10  ? 976  ARG   B CB  1 
ATOM   4170 C CG  . ARG   B 1 283 ? 37.747 -38.100 23.497  1.00 55.80  ? 976  ARG   B CG  1 
ATOM   4171 C CD  . ARG   B 1 283 ? 36.558 -38.814 24.102  1.00 57.33  ? 976  ARG   B CD  1 
ATOM   4172 N NE  . ARG   B 1 283 ? 35.670 -39.381 23.087  1.00 59.15  ? 976  ARG   B NE  1 
ATOM   4173 C CZ  . ARG   B 1 283 ? 34.717 -38.696 22.455  1.00 59.90  ? 976  ARG   B CZ  1 
ATOM   4174 N NH1 . ARG   B 1 283 ? 33.946 -39.296 21.558  1.00 59.20  ? 976  ARG   B NH1 1 
ATOM   4175 N NH2 . ARG   B 1 283 ? 34.535 -37.407 22.711  1.00 58.79  ? 976  ARG   B NH2 1 
ATOM   4176 N N   . ASP   B 1 284 ? 41.742 -39.629 21.378  1.00 55.50  ? 977  ASP   B N   1 
ATOM   4177 C CA  . ASP   B 1 284 ? 42.899 -40.488 21.089  1.00 56.80  ? 977  ASP   B CA  1 
ATOM   4178 C C   . ASP   B 1 284 ? 43.700 -39.820 19.954  1.00 56.70  ? 977  ASP   B C   1 
ATOM   4179 O O   . ASP   B 1 284 ? 43.644 -40.274 18.819  1.00 56.94  ? 977  ASP   B O   1 
ATOM   4180 C CB  . ASP   B 1 284 ? 42.415 -41.876 20.666  1.00 60.20  ? 977  ASP   B CB  1 
ATOM   4181 C CG  . ASP   B 1 284 ? 43.476 -42.953 20.657  1.00 67.22  ? 977  ASP   B CG  1 
ATOM   4182 O OD1 . ASP   B 1 284 ? 44.631 -42.663 21.075  1.00 67.74  ? 977  ASP   B OD1 1 
ATOM   4183 O OD2 . ASP   B 1 284 ? 43.154 -44.093 20.237  1.00 71.18  ? 977  ASP   B OD2 1 
ATOM   4184 N N   . PRO   B 1 285 ? 44.410 -38.704 20.229  1.00 56.45  ? 978  PRO   B N   1 
ATOM   4185 C CA  . PRO   B 1 285 ? 45.020 -37.937 19.133  1.00 56.72  ? 978  PRO   B CA  1 
ATOM   4186 C C   . PRO   B 1 285 ? 46.188 -38.586 18.387  1.00 57.28  ? 978  PRO   B C   1 
ATOM   4187 O O   . PRO   B 1 285 ? 46.352 -38.300 17.205  1.00 57.50  ? 978  PRO   B O   1 
ATOM   4188 C CB  . PRO   B 1 285 ? 45.427 -36.618 19.805  1.00 56.92  ? 978  PRO   B CB  1 
ATOM   4189 C CG  . PRO   B 1 285 ? 45.564 -36.940 21.225  1.00 57.18  ? 978  PRO   B CG  1 
ATOM   4190 C CD  . PRO   B 1 285 ? 44.542 -37.992 21.516  1.00 55.69  ? 978  PRO   B CD  1 
ATOM   4191 N N   . GLN   B 1 286 ? 46.983 -39.435 19.037  1.00 57.37  ? 979  GLN   B N   1 
ATOM   4192 C CA  . GLN   B 1 286 ? 48.110 -40.094 18.374  1.00 58.24  ? 979  GLN   B CA  1 
ATOM   4193 C C   . GLN   B 1 286 ? 47.672 -41.137 17.311  1.00 58.24  ? 979  GLN   B C   1 
ATOM   4194 O O   . GLN   B 1 286 ? 48.475 -41.536 16.466  1.00 58.53  ? 979  GLN   B O   1 
ATOM   4195 C CB  . GLN   B 1 286 ? 49.065 -40.719 19.405  1.00 60.75  ? 979  GLN   B CB  1 
ATOM   4196 C CG  . GLN   B 1 286 ? 49.943 -39.700 20.139  1.00 66.55  ? 979  GLN   B CG  1 
ATOM   4197 C CD  . GLN   B 1 286 ? 49.261 -38.957 21.275  1.00 74.00  ? 979  GLN   B CD  1 
ATOM   4198 O OE1 . GLN   B 1 286 ? 49.537 -37.769 21.530  1.00 75.69  ? 979  GLN   B OE1 1 
ATOM   4199 N NE2 . GLN   B 1 286 ? 48.361 -39.634 21.994  1.00 75.75  ? 979  GLN   B NE2 1 
ATOM   4200 N N   . ARG   B 1 287 ? 46.408 -41.569 17.358  1.00 57.63  ? 980  ARG   B N   1 
ATOM   4201 C CA  . ARG   B 1 287 ? 45.829 -42.501 16.400  1.00 57.74  ? 980  ARG   B CA  1 
ATOM   4202 C C   . ARG   B 1 287 ? 45.435 -41.783 15.070  1.00 57.54  ? 980  ARG   B C   1 
ATOM   4203 O O   . ARG   B 1 287 ? 45.298 -42.438 14.037  1.00 58.05  ? 980  ARG   B O   1 
ATOM   4204 C CB  . ARG   B 1 287 ? 44.568 -43.131 17.024  1.00 59.26  ? 980  ARG   B CB  1 
ATOM   4205 C CG  . ARG   B 1 287 ? 44.175 -44.463 16.419  1.00 63.67  ? 980  ARG   B CG  1 
ATOM   4206 C CD  . ARG   B 1 287 ? 42.772 -44.461 15.859  1.00 68.34  ? 980  ARG   B CD  1 
ATOM   4207 N NE  . ARG   B 1 287 ? 41.783 -45.014 16.790  1.00 72.98  ? 980  ARG   B NE  1 
ATOM   4208 C CZ  . ARG   B 1 287 ? 40.873 -45.933 16.464  1.00 77.49  ? 980  ARG   B CZ  1 
ATOM   4209 N NH1 . ARG   B 1 287 ? 40.824 -46.422 15.229  1.00 77.86  ? 980  ARG   B NH1 1 
ATOM   4210 N NH2 . ARG   B 1 287 ? 40.010 -46.373 17.372  1.00 77.95  ? 980  ARG   B NH2 1 
ATOM   4211 N N   . TYR   B 1 288 ? 45.216 -40.457 15.111  1.00 56.41  ? 981  TYR   B N   1 
ATOM   4212 C CA  . TYR   B 1 288 ? 44.752 -39.691 13.960  1.00 55.87  ? 981  TYR   B CA  1 
ATOM   4213 C C   . TYR   B 1 288 ? 45.783 -38.729 13.377  1.00 56.10  ? 981  TYR   B C   1 
ATOM   4214 O O   . TYR   B 1 288 ? 45.739 -38.445 12.182  1.00 55.72  ? 981  TYR   B O   1 
ATOM   4215 C CB  . TYR   B 1 288 ? 43.465 -38.965 14.328  1.00 55.33  ? 981  TYR   B CB  1 
ATOM   4216 C CG  . TYR   B 1 288 ? 42.386 -39.947 14.718  1.00 55.61  ? 981  TYR   B CG  1 
ATOM   4217 C CD1 . TYR   B 1 288 ? 41.747 -40.725 13.758  1.00 56.34  ? 981  TYR   B CD1 1 
ATOM   4218 C CD2 . TYR   B 1 288 ? 42.093 -40.192 16.053  1.00 56.03  ? 981  TYR   B CD2 1 
ATOM   4219 C CE1 . TYR   B 1 288 ? 40.777 -41.652 14.110  1.00 57.30  ? 981  TYR   B CE1 1 
ATOM   4220 C CE2 . TYR   B 1 288 ? 41.133 -41.121 16.422  1.00 57.00  ? 981  TYR   B CE2 1 
ATOM   4221 C CZ  . TYR   B 1 288 ? 40.458 -41.834 15.443  1.00 58.68  ? 981  TYR   B CZ  1 
ATOM   4222 O OH  . TYR   B 1 288 ? 39.507 -42.770 15.784  1.00 61.40  ? 981  TYR   B OH  1 
ATOM   4223 N N   . LEU   B 1 289 ? 46.714 -38.237 14.201  1.00 56.43  ? 982  LEU   B N   1 
ATOM   4224 C CA  . LEU   B 1 289 ? 47.777 -37.365 13.722  1.00 57.62  ? 982  LEU   B CA  1 
ATOM   4225 C C   . LEU   B 1 289 ? 49.118 -37.958 14.124  1.00 59.75  ? 982  LEU   B C   1 
ATOM   4226 O O   . LEU   B 1 289 ? 49.321 -38.302 15.289  1.00 59.85  ? 982  LEU   B O   1 
ATOM   4227 C CB  . LEU   B 1 289 ? 47.647 -35.938 14.271  1.00 57.48  ? 982  LEU   B CB  1 
ATOM   4228 C CG  . LEU   B 1 289 ? 46.418 -35.135 13.847  1.00 58.43  ? 982  LEU   B CG  1 
ATOM   4229 C CD1 . LEU   B 1 289 ? 46.446 -33.744 14.455  1.00 58.80  ? 982  LEU   B CD1 1 
ATOM   4230 C CD2 . LEU   B 1 289 ? 46.321 -35.030 12.341  1.00 58.94  ? 982  LEU   B CD2 1 
ATOM   4231 N N   . VAL   B 1 290 ? 50.031 -38.096 13.158  1.00 61.10  ? 983  VAL   B N   1 
ATOM   4232 C CA  . VAL   B 1 290 ? 51.356 -38.646 13.399  1.00 62.64  ? 983  VAL   B CA  1 
ATOM   4233 C C   . VAL   B 1 290 ? 52.363 -37.502 13.382  1.00 64.33  ? 983  VAL   B C   1 
ATOM   4234 O O   . VAL   B 1 290 ? 52.736 -37.018 12.319  1.00 64.31  ? 983  VAL   B O   1 
ATOM   4235 C CB  . VAL   B 1 290 ? 51.712 -39.745 12.378  1.00 63.55  ? 983  VAL   B CB  1 
ATOM   4236 C CG1 . VAL   B 1 290 ? 53.035 -40.411 12.736  1.00 64.14  ? 983  VAL   B CG1 1 
ATOM   4237 C CG2 . VAL   B 1 290 ? 50.601 -40.789 12.285  1.00 64.04  ? 983  VAL   B CG2 1 
ATOM   4238 N N   . ILE   B 1 291 ? 52.758 -37.031 14.564  1.00 65.87  ? 984  ILE   B N   1 
ATOM   4239 C CA  . ILE   B 1 291 ? 53.692 -35.922 14.683  1.00 68.17  ? 984  ILE   B CA  1 
ATOM   4240 C C   . ILE   B 1 291 ? 54.965 -36.375 15.391  1.00 71.34  ? 984  ILE   B C   1 
ATOM   4241 O O   . ILE   B 1 291 ? 54.883 -37.030 16.437  1.00 71.62  ? 984  ILE   B O   1 
ATOM   4242 C CB  . ILE   B 1 291 ? 53.000 -34.749 15.427  1.00 68.30  ? 984  ILE   B CB  1 
ATOM   4243 C CG1 . ILE   B 1 291 ? 51.791 -34.219 14.607  1.00 68.83  ? 984  ILE   B CG1 1 
ATOM   4244 C CG2 . ILE   B 1 291 ? 54.001 -33.640 15.768  1.00 68.67  ? 984  ILE   B CG2 1 
ATOM   4245 C CD1 . ILE   B 1 291 ? 50.926 -33.278 15.288  1.00 69.57  ? 984  ILE   B CD1 1 
ATOM   4246 N N   . GLN   B 1 292 ? 56.148 -36.050 14.821  1.00 73.53  ? 985  GLN   B N   1 
ATOM   4247 C CA  . GLN   B 1 292 ? 57.421 -36.393 15.453  1.00 76.22  ? 985  GLN   B CA  1 
ATOM   4248 C C   . GLN   B 1 292 ? 57.542 -35.537 16.720  1.00 78.78  ? 985  GLN   B C   1 
ATOM   4249 O O   . GLN   B 1 292 ? 57.364 -34.312 16.662  1.00 78.99  ? 985  GLN   B O   1 
ATOM   4250 C CB  . GLN   B 1 292 ? 58.595 -36.122 14.499  1.00 77.80  ? 985  GLN   B CB  1 
ATOM   4251 N N   . GLY   B 1 293 ? 57.725 -36.194 17.859  1.00 80.32  ? 986  GLY   B N   1 
ATOM   4252 C CA  . GLY   B 1 293 ? 57.788 -35.482 19.127  1.00 82.43  ? 986  GLY   B CA  1 
ATOM   4253 C C   . GLY   B 1 293 ? 56.704 -35.869 20.117  1.00 84.31  ? 986  GLY   B C   1 
ATOM   4254 O O   . GLY   B 1 293 ? 56.934 -35.760 21.327  1.00 84.94  ? 986  GLY   B O   1 
ATOM   4255 N N   . ASP   B 1 294 ? 55.519 -36.324 19.642  1.00 84.79  ? 987  ASP   B N   1 
ATOM   4256 C CA  . ASP   B 1 294 ? 54.458 -36.774 20.554  1.00 86.09  ? 987  ASP   B CA  1 
ATOM   4257 C C   . ASP   B 1 294 ? 54.951 -38.066 21.248  1.00 87.86  ? 987  ASP   B C   1 
ATOM   4258 O O   . ASP   B 1 294 ? 54.937 -38.174 22.479  1.00 88.28  ? 987  ASP   B O   1 
ATOM   4259 C CB  . ASP   B 1 294 ? 53.136 -37.045 19.796  1.00 87.16  ? 987  ASP   B CB  1 
ATOM   4260 C CG  . ASP   B 1 294 ? 52.429 -35.813 19.254  1.00 89.48  ? 987  ASP   B CG  1 
ATOM   4261 O OD1 . ASP   B 1 294 ? 52.973 -34.704 19.400  1.00 89.92  ? 987  ASP   B OD1 1 
ATOM   4262 O OD2 . ASP   B 1 294 ? 51.333 -35.966 18.683  1.00 90.44  ? 987  ASP   B OD2 1 
ATOM   4263 N N   . GLU   B 1 295 ? 55.444 -39.019 20.450  1.00 88.41  ? 988  GLU   B N   1 
ATOM   4264 C CA  . GLU   B 1 295 ? 55.995 -40.258 20.973  1.00 89.22  ? 988  GLU   B CA  1 
ATOM   4265 C C   . GLU   B 1 295 ? 57.525 -40.216 20.892  1.00 89.91  ? 988  GLU   B C   1 
ATOM   4266 O O   . GLU   B 1 295 ? 58.089 -39.463 20.093  1.00 90.17  ? 988  GLU   B O   1 
ATOM   4267 C CB  . GLU   B 1 295 ? 55.448 -41.463 20.195  1.00 91.38  ? 988  GLU   B CB  1 
HETATM 4268 C C3  . A1IUK C 2 .   ? 20.325 -36.108 34.879  0.87 46.26  ? 1101 A1IUK A C3  1 
HETATM 4269 C C4  . A1IUK C 2 .   ? 20.890 -34.012 32.049  0.87 47.89  ? 1101 A1IUK A C4  1 
HETATM 4270 C C5  . A1IUK C 2 .   ? 22.698 -36.773 35.758  0.87 46.54  ? 1101 A1IUK A C5  1 
HETATM 4271 C C6  . A1IUK C 2 .   ? 22.894 -36.286 37.046  0.87 46.78  ? 1101 A1IUK A C6  1 
HETATM 4272 C C7  . A1IUK C 2 .   ? 23.833 -36.847 37.906  0.87 47.15  ? 1101 A1IUK A C7  1 
HETATM 4273 C C8  . A1IUK C 2 .   ? 24.534 -37.951 37.445  0.87 46.34  ? 1101 A1IUK A C8  1 
HETATM 4274 C C9  . A1IUK C 2 .   ? 24.378 -38.470 36.186  0.87 46.31  ? 1101 A1IUK A C9  1 
HETATM 4275 C C10 . A1IUK C 2 .   ? 23.469 -37.854 35.364  0.87 46.49  ? 1101 A1IUK A C10 1 
HETATM 4276 C C11 . A1IUK C 2 .   ? 24.019 -36.288 39.253  0.87 48.27  ? 1101 A1IUK A C11 1 
HETATM 4277 C C12 . A1IUK C 2 .   ? 23.424 -35.699 41.230  0.87 49.83  ? 1101 A1IUK A C12 1 
HETATM 4278 O O   . A1IUK C 2 .   ? 22.709 -34.197 44.988  0.87 53.30  ? 1101 A1IUK A O   1 
HETATM 4279 N N1  . A1IUK C 2 .   ? 20.893 -34.895 33.237  0.87 47.06  ? 1101 A1IUK A N1  1 
HETATM 4280 C C20 . A1IUK C 2 .   ? 23.816 -34.343 44.483  0.87 52.61  ? 1101 A1IUK A C20 1 
HETATM 4281 C C21 . A1IUK C 2 .   ? 25.017 -33.784 45.169  0.87 52.71  ? 1101 A1IUK A C21 1 
HETATM 4282 C C22 . A1IUK C 2 .   ? 24.571 -32.920 46.318  0.87 52.82  ? 1101 A1IUK A C22 1 
HETATM 4283 N N3  . A1IUK C 2 .   ? 23.982 -34.974 43.302  0.87 51.39  ? 1101 A1IUK A N3  1 
HETATM 4284 C C13 . A1IUK C 2 .   ? 22.844 -35.441 42.528  0.87 50.71  ? 1101 A1IUK A C13 1 
HETATM 4285 C C14 . A1IUK C 2 .   ? 25.242 -35.283 42.630  0.87 50.22  ? 1101 A1IUK A C14 1 
HETATM 4286 C C15 . A1IUK C 2 .   ? 24.792 -35.697 41.258  0.87 49.49  ? 1101 A1IUK A C15 1 
HETATM 4287 N N2  . A1IUK C 2 .   ? 22.958 -36.030 39.993  0.87 49.08  ? 1101 A1IUK A N2  1 
HETATM 4288 N N4  . A1IUK C 2 .   ? 25.192 -36.068 39.966  0.87 48.46  ? 1101 A1IUK A N4  1 
HETATM 4289 C C16 . A1IUK C 2 .   ? 26.565 -36.120 39.502  0.87 48.03  ? 1101 A1IUK A C16 1 
HETATM 4290 N N6  . A1IUK C 2 .   ? 26.790 -35.718 38.251  0.87 48.04  ? 1101 A1IUK A N6  1 
HETATM 4291 C C19 . A1IUK C 2 .   ? 28.079 -35.614 37.912  0.87 47.47  ? 1101 A1IUK A C19 1 
HETATM 4292 N N5  . A1IUK C 2 .   ? 29.143 -35.875 38.662  0.87 47.08  ? 1101 A1IUK A N5  1 
HETATM 4293 C C18 . A1IUK C 2 .   ? 28.868 -36.297 39.893  0.87 47.21  ? 1101 A1IUK A C18 1 
HETATM 4294 C C17 . A1IUK C 2 .   ? 27.587 -36.446 40.382  0.87 47.72  ? 1101 A1IUK A C17 1 
HETATM 4295 F F2  . A1IUK C 2 .   ? 25.402 -38.563 38.276  0.87 45.76  ? 1101 A1IUK A F2  1 
HETATM 4296 F F3  . A1IUK C 2 .   ? 23.357 -38.299 34.095  0.87 46.82  ? 1101 A1IUK A F3  1 
HETATM 4297 C C2  . A1IUK C 2 .   ? 21.728 -36.101 34.856  0.87 46.33  ? 1101 A1IUK A C2  1 
HETATM 4298 N N   . A1IUK C 2 .   ? 19.803 -35.384 33.906  0.87 46.51  ? 1101 A1IUK A N   1 
HETATM 4299 F F1  . A1IUK C 2 .   ? 20.039 -34.459 31.104  0.87 48.32  ? 1101 A1IUK A F1  1 
HETATM 4300 F F   . A1IUK C 2 .   ? 20.496 -32.787 32.450  0.87 48.52  ? 1101 A1IUK A F   1 
HETATM 4301 C C1  . A1IUK C 2 .   ? 22.057 -35.299 33.791  0.87 46.54  ? 1101 A1IUK A C1  1 
HETATM 4302 C C   . A1IUK C 2 .   ? 23.401 -34.839 33.354  0.87 46.68  ? 1101 A1IUK A C   1 
HETATM 4303 C C3  . A1IUK D 2 .   ? 35.363 -7.491  13.673  0.93 50.40  ? 1101 A1IUK B C3  1 
HETATM 4304 C C4  . A1IUK D 2 .   ? 32.903 -9.304  15.549  0.93 52.64  ? 1101 A1IUK B C4  1 
HETATM 4305 C C5  . A1IUK D 2 .   ? 37.451 -7.212  15.221  0.93 49.90  ? 1101 A1IUK B C5  1 
HETATM 4306 C C6  . A1IUK D 2 .   ? 38.575 -7.871  14.724  0.93 49.96  ? 1101 A1IUK B C6  1 
HETATM 4307 C C7  . A1IUK D 2 .   ? 39.870 -7.500  15.090  0.93 50.53  ? 1101 A1IUK B C7  1 
HETATM 4308 C C8  . A1IUK D 2 .   ? 39.994 -6.423  15.946  0.93 49.55  ? 1101 A1IUK B C8  1 
HETATM 4309 C C9  . A1IUK D 2 .   ? 38.925 -5.751  16.476  0.93 49.32  ? 1101 A1IUK B C9  1 
HETATM 4310 C C10 . A1IUK D 2 .   ? 37.674 -6.165  16.103  0.93 49.51  ? 1101 A1IUK B C10 1 
HETATM 4311 C C11 . A1IUK D 2 .   ? 41.046 -8.221  14.571  0.93 52.47  ? 1101 A1IUK B C11 1 
HETATM 4312 C C12 . A1IUK D 2 .   ? 42.441 -8.958  13.106  0.93 54.34  ? 1101 A1IUK B C12 1 
HETATM 4313 O O   . A1IUK D 2 .   ? 45.006 -11.136 10.713  0.93 56.42  ? 1101 A1IUK B O   1 
HETATM 4314 N N1  . A1IUK D 2 .   ? 34.068 -8.552  14.983  0.93 51.51  ? 1101 A1IUK B N1  1 
HETATM 4315 C C20 . A1IUK D 2 .   ? 45.097 -11.018 11.931  0.93 55.99  ? 1101 A1IUK B C20 1 
HETATM 4316 C C21 . A1IUK D 2 .   ? 46.099 -11.823 12.724  0.93 55.78  ? 1101 A1IUK B C21 1 
HETATM 4317 C C22 . A1IUK D 2 .   ? 46.719 -12.932 11.904  0.93 55.62  ? 1101 A1IUK B C22 1 
HETATM 4318 N N3  . A1IUK D 2 .   ? 44.311 -10.169 12.627  0.93 55.34  ? 1101 A1IUK B N3  1 
HETATM 4319 C C13 . A1IUK D 2 .   ? 43.337 -9.298  11.990  0.93 55.11  ? 1101 A1IUK B C13 1 
HETATM 4320 C C14 . A1IUK D 2 .   ? 44.293 -9.988  14.075  0.93 54.58  ? 1101 A1IUK B C14 1 
HETATM 4321 C C15 . A1IUK D 2 .   ? 43.007 -9.254  14.314  0.93 53.97  ? 1101 A1IUK B C15 1 
HETATM 4322 N N2  . A1IUK D 2 .   ? 41.226 -8.351  13.270  0.93 53.59  ? 1101 A1IUK B N2  1 
HETATM 4323 N N4  . A1IUK D 2 .   ? 42.110 -8.770  15.278  0.93 52.98  ? 1101 A1IUK B N4  1 
HETATM 4324 C C16 . A1IUK D 2 .   ? 42.302 -8.867  16.720  0.93 52.55  ? 1101 A1IUK B C16 1 
HETATM 4325 N N6  . A1IUK D 2 .   ? 41.202 -8.989  17.473  0.93 52.52  ? 1101 A1IUK B N6  1 
HETATM 4326 C C19 . A1IUK D 2 .   ? 41.425 -9.171  18.780  0.93 52.09  ? 1101 A1IUK B C19 1 
HETATM 4327 N N5  . A1IUK D 2 .   ? 42.597 -9.245  19.404  0.93 52.02  ? 1101 A1IUK B N5  1 
HETATM 4328 C C18 . A1IUK D 2 .   ? 43.665 -9.111  18.616  0.93 52.05  ? 1101 A1IUK B C18 1 
HETATM 4329 C C17 . A1IUK D 2 .   ? 43.590 -8.908  17.252  0.93 52.15  ? 1101 A1IUK B C17 1 
HETATM 4330 F F2  . A1IUK D 2 .   ? 41.228 -5.968  16.224  0.93 49.61  ? 1101 A1IUK B F2  1 
HETATM 4331 F F3  . A1IUK D 2 .   ? 36.613 -5.545  16.666  0.93 49.38  ? 1101 A1IUK B F3  1 
HETATM 4332 C C2  . A1IUK D 2 .   ? 36.088 -7.683  14.860  0.93 50.38  ? 1101 A1IUK B C2  1 
HETATM 4333 N N   . A1IUK D 2 .   ? 34.144 -8.002  13.731  0.93 50.88  ? 1101 A1IUK B N   1 
HETATM 4334 F F1  . A1IUK D 2 .   ? 32.912 -10.530 14.987  0.93 53.42  ? 1101 A1IUK B F1  1 
HETATM 4335 F F   . A1IUK D 2 .   ? 31.698 -8.785  15.241  0.93 53.07  ? 1101 A1IUK B F   1 
HETATM 4336 C C1  . A1IUK D 2 .   ? 35.230 -8.401  15.682  0.93 50.88  ? 1101 A1IUK B C1  1 
HETATM 4337 C C   . A1IUK D 2 .   ? 35.527 -9.066  16.981  0.93 50.66  ? 1101 A1IUK B C   1 
HETATM 4338 O O   . HOH   E 3 .   ? 24.370 -29.824 27.618  1.00 45.04  ? 1201 HOH   A O   1 
HETATM 4339 O O   . HOH   E 3 .   ? 33.307 -50.100 24.345  1.00 65.46  ? 1202 HOH   A O   1 
HETATM 4340 O O   . HOH   E 3 .   ? 10.648 -16.930 49.544  1.00 37.27  ? 1203 HOH   A O   1 
HETATM 4341 O O   . HOH   E 3 .   ? 1.982  -16.466 41.089  1.00 55.00  ? 1204 HOH   A O   1 
HETATM 4342 O O   . HOH   E 3 .   ? 30.317 -30.929 47.180  1.00 66.51  ? 1205 HOH   A O   1 
HETATM 4343 O O   . HOH   E 3 .   ? 26.922 -22.055 22.393  1.00 38.54  ? 1206 HOH   A O   1 
HETATM 4344 O O   . HOH   E 3 .   ? 13.771 -15.566 32.529  1.00 40.51  ? 1207 HOH   A O   1 
HETATM 4345 O O   . HOH   E 3 .   ? 9.817  -23.958 36.816  1.00 48.16  ? 1208 HOH   A O   1 
HETATM 4346 O O   . HOH   E 3 .   ? 14.123 -31.411 36.316  1.00 52.16  ? 1209 HOH   A O   1 
HETATM 4347 O O   . HOH   E 3 .   ? 19.257 -26.124 51.190  1.00 45.10  ? 1210 HOH   A O   1 
HETATM 4348 O O   . HOH   E 3 .   ? 16.574 -14.381 29.938  1.00 46.03  ? 1211 HOH   A O   1 
HETATM 4349 O O   . HOH   E 3 .   ? 22.951 -32.738 27.254  1.00 51.16  ? 1212 HOH   A O   1 
HETATM 4350 O O   . HOH   E 3 .   ? 12.311 -30.867 33.667  1.00 46.54  ? 1213 HOH   A O   1 
HETATM 4351 O O   . HOH   E 3 .   ? 15.489 -33.340 39.462  1.00 62.33  ? 1214 HOH   A O   1 
HETATM 4352 O O   . HOH   E 3 .   ? -0.746 -23.735 52.571  1.00 70.07  ? 1215 HOH   A O   1 
HETATM 4353 O O   . HOH   E 3 .   ? 13.061 -24.668 38.739  1.00 46.24  ? 1216 HOH   A O   1 
HETATM 4354 O O   . HOH   E 3 .   ? 18.958 -27.802 47.180  1.00 46.75  ? 1217 HOH   A O   1 
HETATM 4355 O O   . HOH   E 3 .   ? -2.569 -17.239 53.619  1.00 60.49  ? 1218 HOH   A O   1 
HETATM 4356 O O   . HOH   E 3 .   ? 19.693 -49.341 32.822  1.00 53.43  ? 1219 HOH   A O   1 
HETATM 4357 O O   . HOH   E 3 .   ? 23.313 -17.395 28.806  1.00 51.73  ? 1220 HOH   A O   1 
HETATM 4358 O O   . HOH   E 3 .   ? 34.898 -37.029 32.590  1.00 70.66  ? 1221 HOH   A O   1 
HETATM 4359 O O   . HOH   E 3 .   ? 27.490 -28.913 19.979  1.00 51.57  ? 1222 HOH   A O   1 
HETATM 4360 O O   . HOH   E 3 .   ? 31.035 -36.386 42.533  1.00 59.33  ? 1223 HOH   A O   1 
HETATM 4361 O O   . HOH   E 3 .   ? 2.193  -25.455 50.110  1.00 51.81  ? 1224 HOH   A O   1 
HETATM 4362 O O   . HOH   E 3 .   ? 7.403  -48.490 33.736  1.00 63.32  ? 1225 HOH   A O   1 
HETATM 4363 O O   . HOH   E 3 .   ? 13.030 -26.983 42.707  1.00 59.74  ? 1226 HOH   A O   1 
HETATM 4364 O O   . HOH   E 3 .   ? 14.820 -22.519 32.055  1.00 66.24  ? 1227 HOH   A O   1 
HETATM 4365 O O   . HOH   E 3 .   ? 30.311 -53.755 32.153  1.00 71.84  ? 1228 HOH   A O   1 
HETATM 4366 O O   . HOH   E 3 .   ? 9.951  -16.015 30.608  1.00 62.45  ? 1229 HOH   A O   1 
HETATM 4367 O O   . HOH   E 3 .   ? 29.070 -45.088 22.528  1.00 61.18  ? 1230 HOH   A O   1 
HETATM 4368 O O   . HOH   E 3 .   ? 10.486 -8.382  34.396  1.00 67.65  ? 1231 HOH   A O   1 
HETATM 4369 O O   . HOH   E 3 .   ? 20.382 -49.222 26.411  1.00 71.08  ? 1232 HOH   A O   1 
HETATM 4370 O O   . HOH   E 3 .   ? 9.530  -21.033 47.704  1.00 50.32  ? 1233 HOH   A O   1 
HETATM 4371 O O   . HOH   E 3 .   ? 36.260 -12.154 47.676  1.00 61.07  ? 1234 HOH   A O   1 
HETATM 4372 O O   . HOH   E 3 .   ? 12.531 -36.036 21.007  1.00 57.21  ? 1235 HOH   A O   1 
HETATM 4373 O O   . HOH   E 3 .   ? 10.333 -27.278 28.525  1.00 52.30  ? 1236 HOH   A O   1 
HETATM 4374 O O   . HOH   E 3 .   ? 25.160 -54.883 27.116  1.00 67.31  ? 1237 HOH   A O   1 
HETATM 4375 O O   . HOH   E 3 .   ? 25.908 -31.490 52.831  1.00 64.95  ? 1238 HOH   A O   1 
HETATM 4376 O O   . HOH   E 3 .   ? 8.497  -23.600 40.038  1.00 60.25  ? 1239 HOH   A O   1 
HETATM 4377 O O   . HOH   E 3 .   ? -1.569 -26.512 55.661  1.00 67.52  ? 1240 HOH   A O   1 
HETATM 4378 O O   . HOH   E 3 .   ? 14.252 -19.891 56.039  1.00 62.63  ? 1241 HOH   A O   1 
HETATM 4379 O O   . HOH   E 3 .   ? 27.129 -51.865 33.588  1.00 56.15  ? 1242 HOH   A O   1 
HETATM 4380 O O   . HOH   E 3 .   ? 27.843 -18.460 28.828  1.00 65.64  ? 1243 HOH   A O   1 
HETATM 4381 O O   . HOH   E 3 .   ? 30.137 -48.776 46.455  1.00 69.98  ? 1244 HOH   A O   1 
HETATM 4382 O O   . HOH   E 3 .   ? 22.250 -52.118 36.428  1.00 57.19  ? 1245 HOH   A O   1 
HETATM 4383 O O   . HOH   E 3 .   ? 29.574 -50.329 43.058  1.00 70.69  ? 1246 HOH   A O   1 
HETATM 4384 O O   . HOH   E 3 .   ? 34.400 -7.963  54.760  1.00 66.35  ? 1247 HOH   A O   1 
HETATM 4385 O O   . HOH   E 3 .   ? 21.227 -9.234  57.133  1.00 54.38  ? 1248 HOH   A O   1 
HETATM 4386 O O   . HOH   E 3 .   ? 26.174 -27.744 27.147  1.00 40.14  ? 1249 HOH   A O   1 
HETATM 4387 O O   . HOH   E 3 .   ? 27.863 -10.910 58.038  1.00 60.00  ? 1250 HOH   A O   1 
HETATM 4388 O O   . HOH   E 3 .   ? 11.308 -20.987 59.080  1.00 79.30  ? 1251 HOH   A O   1 
HETATM 4389 O O   . HOH   E 3 .   ? 1.786  -15.432 37.604  1.00 68.91  ? 1252 HOH   A O   1 
HETATM 4390 O O   . HOH   E 3 .   ? 28.973 -2.846  52.133  1.00 78.28  ? 1253 HOH   A O   1 
HETATM 4391 O O   . HOH   E 3 .   ? 10.706 -28.748 49.778  1.00 64.52  ? 1254 HOH   A O   1 
HETATM 4392 O O   . HOH   E 3 .   ? 28.736 -27.369 26.043  1.00 58.20  ? 1255 HOH   A O   1 
HETATM 4393 O O   . HOH   E 3 .   ? 13.802 -10.502 56.232  1.00 68.30  ? 1256 HOH   A O   1 
HETATM 4394 O O   . HOH   E 3 .   ? 30.792 -35.369 20.712  1.00 74.19  ? 1257 HOH   A O   1 
HETATM 4395 O O   . HOH   E 3 .   ? 12.759 -33.686 28.572  1.00 68.83  ? 1258 HOH   A O   1 
HETATM 4396 O O   . HOH   E 3 .   ? 15.189 -40.401 20.289  1.00 74.94  ? 1259 HOH   A O   1 
HETATM 4397 O O   . HOH   E 3 .   ? 24.203 -37.852 45.427  1.00 61.16  ? 1260 HOH   A O   1 
HETATM 4398 O O   . HOH   E 3 .   ? 29.864 -23.715 24.877  1.00 57.74  ? 1261 HOH   A O   1 
HETATM 4399 O O   . HOH   F 3 .   ? 29.342 -9.989  19.383  1.00 42.56  ? 1201 HOH   B O   1 
HETATM 4400 O O   . HOH   F 3 .   ? 38.310 -22.219 -3.209  1.00 40.71  ? 1202 HOH   B O   1 
HETATM 4401 O O   . HOH   F 3 .   ? 50.969 -38.041 17.093  1.00 55.40  ? 1203 HOH   B O   1 
HETATM 4402 O O   . HOH   F 3 .   ? 32.801 -14.927 23.673  1.00 49.29  ? 1204 HOH   B O   1 
HETATM 4403 O O   . HOH   F 3 .   ? 33.522 -18.788 5.608   1.00 46.04  ? 1205 HOH   B O   1 
HETATM 4404 O O   . HOH   F 3 .   ? 35.099 -17.202 2.208   1.00 54.80  ? 1206 HOH   B O   1 
HETATM 4405 O O   . HOH   F 3 .   ? 23.814 -26.076 7.295   1.00 57.31  ? 1207 HOH   B O   1 
HETATM 4406 O O   . HOH   F 3 .   ? 47.524 -19.941 5.132   1.00 49.48  ? 1208 HOH   B O   1 
HETATM 4407 O O   . HOH   F 3 .   ? 32.962 -11.885 7.520   1.00 42.10  ? 1209 HOH   B O   1 
HETATM 4408 O O   . HOH   F 3 .   ? 41.877 -11.358 8.914   1.00 59.01  ? 1210 HOH   B O   1 
HETATM 4409 O O   . HOH   F 3 .   ? 26.967 -26.613 8.756   1.00 33.67  ? 1211 HOH   B O   1 
HETATM 4410 O O   . HOH   F 3 .   ? 35.854 6.151   13.935  1.00 52.61  ? 1212 HOH   B O   1 
HETATM 4411 O O   . HOH   F 3 .   ? 34.142 -31.264 -10.865 1.00 48.05  ? 1213 HOH   B O   1 
HETATM 4412 O O   . HOH   F 3 .   ? 37.088 -40.057 8.310   1.00 61.12  ? 1214 HOH   B O   1 
HETATM 4413 O O   . HOH   F 3 .   ? 28.473 -25.142 19.161  1.00 35.01  ? 1215 HOH   B O   1 
HETATM 4414 O O   . HOH   F 3 .   ? 37.882 -17.077 3.812   1.00 44.14  ? 1216 HOH   B O   1 
HETATM 4415 O O   . HOH   F 3 .   ? 40.606 -28.047 -1.667  1.00 39.73  ? 1217 HOH   B O   1 
HETATM 4416 O O   . HOH   F 3 .   ? 25.504 -27.504 12.493  1.00 47.29  ? 1218 HOH   B O   1 
HETATM 4417 O O   . HOH   F 3 .   ? 21.523 -14.030 19.362  1.00 61.49  ? 1219 HOH   B O   1 
HETATM 4418 O O   . HOH   F 3 .   ? 40.490 9.488   4.208   1.00 46.29  ? 1220 HOH   B O   1 
HETATM 4419 O O   . HOH   F 3 .   ? 29.769 -12.759 20.731  1.00 44.42  ? 1221 HOH   B O   1 
HETATM 4420 O O   . HOH   F 3 .   ? 39.553 -20.692 -13.206 1.00 62.10  ? 1222 HOH   B O   1 
HETATM 4421 O O   . HOH   F 3 .   ? 37.953 -34.944 -6.379  1.00 51.44  ? 1223 HOH   B O   1 
HETATM 4422 O O   . HOH   F 3 .   ? 42.465 -13.977 -4.004  1.00 66.82  ? 1224 HOH   B O   1 
HETATM 4423 O O   . HOH   F 3 .   ? 44.087 -17.694 7.025   1.00 44.92  ? 1225 HOH   B O   1 
HETATM 4424 O O   . HOH   F 3 .   ? 25.430 -20.434 25.442  1.00 45.94  ? 1226 HOH   B O   1 
HETATM 4425 O O   . HOH   F 3 .   ? 24.554 -31.673 5.162   1.00 56.16  ? 1227 HOH   B O   1 
HETATM 4426 O O   . HOH   F 3 .   ? 32.481 -37.419 19.810  1.00 57.78  ? 1228 HOH   B O   1 
HETATM 4427 O O   . HOH   F 3 .   ? 43.349 -21.458 29.305  1.00 61.76  ? 1229 HOH   B O   1 
HETATM 4428 O O   . HOH   F 3 .   ? 39.383 -23.622 -1.590  1.00 42.73  ? 1230 HOH   B O   1 
HETATM 4429 O O   . HOH   F 3 .   ? 24.407 -15.702 -0.904  1.00 58.24  ? 1231 HOH   B O   1 
HETATM 4430 O O   . HOH   F 3 .   ? 53.219 -22.142 2.148   1.00 58.59  ? 1232 HOH   B O   1 
HETATM 4431 O O   . HOH   F 3 .   ? 26.931 -35.531 -3.652  1.00 57.24  ? 1233 HOH   B O   1 
HETATM 4432 O O   . HOH   F 3 .   ? 51.988 -24.192 0.482   1.00 63.53  ? 1234 HOH   B O   1 
HETATM 4433 O O   . HOH   F 3 .   ? 30.283 6.801   17.210  1.00 68.86  ? 1235 HOH   B O   1 
HETATM 4434 O O   . HOH   F 3 .   ? 35.605 2.995   7.185   1.00 51.23  ? 1236 HOH   B O   1 
HETATM 4435 O O   . HOH   F 3 .   ? 31.286 -18.886 3.043   1.00 51.23  ? 1237 HOH   B O   1 
HETATM 4436 O O   . HOH   F 3 .   ? 37.445 -34.389 22.875  1.00 42.06  ? 1238 HOH   B O   1 
HETATM 4437 O O   . HOH   F 3 .   ? 34.106 9.949   18.786  1.00 66.29  ? 1239 HOH   B O   1 
HETATM 4438 O O   . HOH   F 3 .   ? 37.715 -26.711 -15.349 1.00 59.54  ? 1240 HOH   B O   1 
HETATM 4439 O O   . HOH   F 3 .   ? 47.562 1.914   7.227   1.00 66.57  ? 1241 HOH   B O   1 
HETATM 4440 O O   . HOH   F 3 .   ? 35.578 -10.635 6.383   1.00 52.54  ? 1242 HOH   B O   1 
HETATM 4441 O O   . HOH   F 3 .   ? 33.563 4.675   5.933   1.00 58.86  ? 1243 HOH   B O   1 
HETATM 4442 O O   . HOH   F 3 .   ? 45.904 -35.738 -1.395  1.00 61.08  ? 1244 HOH   B O   1 
HETATM 4443 O O   . HOH   F 3 .   ? 23.475 -23.700 4.807   1.00 68.26  ? 1245 HOH   B O   1 
HETATM 4444 O O   . HOH   F 3 .   ? 40.665 -20.771 -15.729 1.00 67.72  ? 1246 HOH   B O   1 
HETATM 4445 O O   . HOH   F 3 .   ? 59.505 -35.153 22.913  1.00 73.48  ? 1247 HOH   B O   1 
HETATM 4446 O O   . HOH   F 3 .   ? 26.494 -8.229  10.057  1.00 54.63  ? 1248 HOH   B O   1 
HETATM 4447 O O   . HOH   F 3 .   ? 26.017 -34.120 5.727   1.00 64.03  ? 1249 HOH   B O   1 
HETATM 4448 O O   . HOH   F 3 .   ? 27.582 -31.254 18.250  1.00 54.28  ? 1250 HOH   B O   1 
HETATM 4449 O O   . HOH   F 3 .   ? 23.783 7.625   8.237   1.00 59.11  ? 1251 HOH   B O   1 
HETATM 4450 O O   . HOH   F 3 .   ? 38.470 -12.438 30.070  1.00 53.52  ? 1252 HOH   B O   1 
HETATM 4451 O O   . HOH   F 3 .   ? 42.807 -16.180 -1.873  1.00 41.42  ? 1253 HOH   B O   1 
HETATM 4452 O O   . HOH   F 3 .   ? 24.746 -32.452 18.768  1.00 58.51  ? 1254 HOH   B O   1 
HETATM 4453 O O   . HOH   F 3 .   ? 34.905 -25.537 24.778  1.00 48.70  ? 1255 HOH   B O   1 
HETATM 4454 O O   . HOH   F 3 .   ? 47.211 -8.276  12.957  1.00 61.88  ? 1256 HOH   B O   1 
HETATM 4455 O O   . HOH   F 3 .   ? 35.446 -16.255 26.763  1.00 59.59  ? 1257 HOH   B O   1 
HETATM 4456 O O   . HOH   F 3 .   ? 22.489 -19.844 4.924   1.00 75.41  ? 1258 HOH   B O   1 
HETATM 4457 O O   . HOH   F 3 .   ? 42.923 -12.391 27.694  1.00 57.05  ? 1259 HOH   B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ALA   A 9   ? 0.9359 0.9114 0.8971 -0.0427 -0.1024 -0.0149 702  ALA   A N   
2    C CA  . ALA   A 9   ? 0.9678 0.9059 0.8825 -0.0446 -0.1015 -0.0201 702  ALA   A CA  
3    C C   . ALA   A 9   ? 0.9679 0.8921 0.8851 -0.0555 -0.0835 -0.0242 702  ALA   A C   
4    O O   . ALA   A 9   ? 0.9847 0.8924 0.8815 -0.0621 -0.0881 -0.0333 702  ALA   A O   
5    C CB  . ALA   A 9   ? 0.9929 0.9009 0.8700 -0.0361 -0.0934 -0.0134 702  ALA   A CB  
6    N N   . LEU   A 10  ? 0.9448 0.8763 0.8879 -0.0565 -0.0648 -0.0185 703  LEU   A N   
7    C CA  . LEU   A 10  ? 0.9394 0.8600 0.8890 -0.0636 -0.0483 -0.0219 703  LEU   A CA  
8    C C   . LEU   A 10  ? 0.8979 0.8455 0.8899 -0.0653 -0.0457 -0.0190 703  LEU   A C   
9    O O   . LEU   A 10  ? 0.8899 0.8500 0.9035 -0.0595 -0.0371 -0.0121 703  LEU   A O   
10   C CB  . LEU   A 10  ? 0.9577 0.8557 0.8940 -0.0615 -0.0263 -0.0201 703  LEU   A CB  
11   C CG  . LEU   A 10  ? 0.9859 0.8676 0.9237 -0.0660 -0.0079 -0.0249 703  LEU   A CG  
12   C CD1 . LEU   A 10  ? 0.9744 0.8748 0.9498 -0.0610 0.0047  -0.0203 703  LEU   A CD1 
13   C CD2 . LEU   A 10  ? 0.9997 0.8718 0.9293 -0.0744 -0.0143 -0.0328 703  LEU   A CD2 
14   N N   . LEU   A 11  ? 0.8714 0.8260 0.8734 -0.0735 -0.0533 -0.0251 704  LEU   A N   
15   C CA  . LEU   A 11  ? 0.8380 0.8099 0.8731 -0.0765 -0.0481 -0.0226 704  LEU   A CA  
16   C C   . LEU   A 11  ? 0.8271 0.7751 0.8562 -0.0821 -0.0325 -0.0261 704  LEU   A C   
17   O O   . LEU   A 11  ? 0.8394 0.7684 0.8492 -0.0909 -0.0342 -0.0356 704  LEU   A O   
18   C CB  . LEU   A 11  ? 0.8234 0.8175 0.8764 -0.0840 -0.0631 -0.0285 704  LEU   A CB  
19   C CG  . LEU   A 11  ? 0.8196 0.8281 0.9041 -0.0892 -0.0550 -0.0263 704  LEU   A CG  
20   C CD1 . LEU   A 11  ? 0.8136 0.8367 0.9145 -0.0778 -0.0490 -0.0140 704  LEU   A CD1 
21   C CD2 . LEU   A 11  ? 0.8106 0.8415 0.9158 -0.0997 -0.0674 -0.0357 704  LEU   A CD2 
22   N N   . ARG   A 12  ? 0.8065 0.7532 0.8490 -0.0752 -0.0184 -0.0193 705  ARG   A N   
23   C CA  . ARG   A 12  ? 0.8049 0.7273 0.8416 -0.0767 -0.0031 -0.0218 705  ARG   A CA  
24   C C   . ARG   A 12  ? 0.7866 0.7093 0.8381 -0.0827 0.0003  -0.0212 705  ARG   A C   
25   O O   . ARG   A 12  ? 0.7637 0.7031 0.8343 -0.0772 0.0003  -0.0134 705  ARG   A O   
26   C CB  . ARG   A 12  ? 0.8131 0.7331 0.8565 -0.0634 0.0096  -0.0161 705  ARG   A CB  
27   C CG  . ARG   A 12  ? 0.8483 0.7647 0.8796 -0.0594 0.0129  -0.0178 705  ARG   A CG  
28   C CD  . ARG   A 12  ? 0.8828 0.8043 0.9320 -0.0473 0.0250  -0.0149 705  ARG   A CD  
29   N NE  . ARG   A 12  ? 0.9146 0.8420 0.9645 -0.0440 0.0293  -0.0158 705  ARG   A NE  
30   C CZ  . ARG   A 12  ? 0.9245 0.8729 0.9861 -0.0409 0.0216  -0.0114 705  ARG   A CZ  
31   N NH1 . ARG   A 12  ? 0.9406 0.8895 1.0018 -0.0400 0.0291  -0.0136 705  ARG   A NH1 
32   N NH2 . ARG   A 12  ? 0.8933 0.8599 0.9660 -0.0396 0.0085  -0.0056 705  ARG   A NH2 
33   N N   . ILE   A 13  ? 0.7962 0.6971 0.8361 -0.0947 0.0045  -0.0299 706  ILE   A N   
34   C CA  . ILE   A 13  ? 0.8002 0.6935 0.8508 -0.1027 0.0125  -0.0303 706  ILE   A CA  
35   C C   . ILE   A 13  ? 0.8215 0.6865 0.8629 -0.0927 0.0303  -0.0253 706  ILE   A C   
36   O O   . ILE   A 13  ? 0.8349 0.6748 0.8572 -0.0928 0.0376  -0.0310 706  ILE   A O   
37   C CB  . ILE   A 13  ? 0.8048 0.6903 0.8509 -0.1225 0.0075  -0.0443 706  ILE   A CB  
38   C CG1 . ILE   A 13  ? 0.7959 0.7153 0.8563 -0.1286 -0.0132 -0.0497 706  ILE   A CG1 
39   C CG2 . ILE   A 13  ? 0.8102 0.6795 0.8648 -0.1326 0.0218  -0.0453 706  ILE   A CG2 
40   N N   . LEU   A 14  ? 0.8225 0.6912 0.8754 -0.0817 0.0365  -0.0147 707  LEU   A N   
41   C CA  . LEU   A 14  ? 0.8433 0.6878 0.8881 -0.0670 0.0500  -0.0091 707  LEU   A CA  
42   C C   . LEU   A 14  ? 0.8687 0.6781 0.9015 -0.0739 0.0644  -0.0099 707  LEU   A C   
43   O O   . LEU   A 14  ? 0.8707 0.6810 0.9097 -0.0861 0.0662  -0.0098 707  LEU   A O   
44   C CB  . LEU   A 14  ? 0.8336 0.6970 0.8917 -0.0486 0.0469  0.0025  707  LEU   A CB  
45   C CG  . LEU   A 14  ? 0.8404 0.7238 0.9072 -0.0344 0.0410  0.0035  707  LEU   A CG  
46   C CD1 . LEU   A 14  ? 0.8331 0.7404 0.9048 -0.0434 0.0295  -0.0007 707  LEU   A CD1 
47   C CD2 . LEU   A 14  ? 0.8432 0.7408 0.9215 -0.0164 0.0374  0.0128  707  LEU   A CD2 
48   N N   . LYS   A 15  ? 0.8909 0.6679 0.9071 -0.0660 0.0766  -0.0113 708  LYS   A N   
49   C CA  . LYS   A 15  ? 0.9214 0.6567 0.9209 -0.0691 0.0930  -0.0107 708  LYS   A CA  
50   C C   . LYS   A 15  ? 0.9388 0.6664 0.9365 -0.0463 0.0979  0.0033  708  LYS   A C   
51   O O   . LYS   A 15  ? 0.9297 0.6788 0.9373 -0.0267 0.0898  0.0084  708  LYS   A O   
52   C CB  . LYS   A 15  ? 0.9595 0.6596 0.9384 -0.0685 0.1039  -0.0188 708  LYS   A CB  
53   C CG  . LYS   A 15  ? 1.0073 0.7056 0.9787 -0.0904 0.0995  -0.0337 708  LYS   A CG  
54   N N   . GLU   A 16  ? 0.9659 0.6609 0.9491 -0.0484 0.1112  0.0087  709  GLU   A N   
55   C CA  . GLU   A 16  ? 0.9919 0.6726 0.9644 -0.0252 0.1152  0.0225  709  GLU   A CA  
56   C C   . GLU   A 16  ? 1.0092 0.6713 0.9701 0.0029  0.1170  0.0258  709  GLU   A C   
57   O O   . GLU   A 16  ? 1.0182 0.6790 0.9739 0.0272  0.1131  0.0359  709  GLU   A O   
58   C CB  . GLU   A 16  ? 1.0545 0.6965 1.0076 -0.0347 0.1326  0.0278  709  GLU   A CB  
59   C CG  . GLU   A 16  ? 1.1291 0.7955 1.0941 -0.0394 0.1287  0.0345  709  GLU   A CG  
60   C CD  . GLU   A 16  ? 1.2456 0.8787 1.1974 -0.0567 0.1492  0.0366  709  GLU   A CD  
61   O OE1 . GLU   A 16  ? 1.2767 0.8737 1.2163 -0.0728 0.1650  0.0293  709  GLU   A OE1 
62   O OE2 . GLU   A 16  ? 1.2750 0.9169 1.2288 -0.0552 0.1513  0.0445  709  GLU   A OE2 
63   N N   . THR   A 17  ? 1.0103 0.6600 0.9678 0.0008  0.1220  0.0164  710  THR   A N   
64   C CA  . THR   A 17  ? 1.0129 0.6500 0.9659 0.0273  0.1246  0.0170  710  THR   A CA  
65   C C   . THR   A 17  ? 0.9771 0.6637 0.9601 0.0399  0.1097  0.0139  710  THR   A C   
66   O O   . THR   A 17  ? 0.9775 0.6675 0.9675 0.0657  0.1079  0.0151  710  THR   A O   
67   C CB  . THR   A 17  ? 1.0482 0.6466 0.9830 0.0195  0.1399  0.0075  710  THR   A CB  
68   O OG1 . THR   A 17  ? 1.0482 0.6703 0.9953 0.0007  0.1351  -0.0045 710  THR   A OG1 
69   C CG2 . THR   A 17  ? 1.0806 0.6294 0.9877 0.0029  0.1561  0.0081  710  THR   A CG2 
70   N N   . GLU   A 18  ? 0.9416 0.6654 0.9429 0.0219  0.0996  0.0091  711  GLU   A N   
71   C CA  . GLU   A 18  ? 0.9091 0.6758 0.9366 0.0285  0.0884  0.0056  711  GLU   A CA  
72   C C   . GLU   A 18  ? 0.8909 0.6847 0.9343 0.0478  0.0758  0.0137  711  GLU   A C   
73   O O   . GLU   A 18  ? 0.8750 0.6973 0.9410 0.0609  0.0693  0.0102  711  GLU   A O   
74   C CB  . GLU   A 18  ? 0.9228 0.7133 0.9570 0.0048  0.0810  0.0002  711  GLU   A CB  
75   C CG  . GLU   A 18  ? 0.9894 0.7636 1.0107 -0.0108 0.0885  -0.0108 711  GLU   A CG  
76   C CD  . GLU   A 18  ? 1.0628 0.8599 1.0869 -0.0294 0.0778  -0.0155 711  GLU   A CD  
77   O OE1 . GLU   A 18  ? 1.0686 0.8941 1.1071 -0.0246 0.0710  -0.0155 711  GLU   A OE1 
78   O OE2 . GLU   A 18  ? 1.0930 0.8790 1.1048 -0.0482 0.0759  -0.0200 711  GLU   A OE2 
79   N N   . PHE   A 19  ? 0.8904 0.6765 0.9229 0.0478  0.0729  0.0232  712  PHE   A N   
80   C CA  . PHE   A 19  ? 0.8765 0.6851 0.9181 0.0651  0.0601  0.0305  712  PHE   A CA  
81   C C   . PHE   A 19  ? 0.9015 0.6753 0.9164 0.0828  0.0639  0.0413  712  PHE   A C   
82   O O   . PHE   A 19  ? 0.9265 0.6592 0.9158 0.0746  0.0784  0.0447  712  PHE   A O   
83   C CB  . PHE   A 19  ? 0.8547 0.6956 0.9092 0.0489  0.0503  0.0315  712  PHE   A CB  
84   C CG  . PHE   A 19  ? 0.8658 0.6902 0.9061 0.0298  0.0570  0.0356  712  PHE   A CG  
85   C CD1 . PHE   A 19  ? 0.8743 0.6897 0.9123 0.0062  0.0641  0.0284  712  PHE   A CD1 
86   C CD2 . PHE   A 19  ? 0.8765 0.6960 0.9070 0.0349  0.0563  0.0451  712  PHE   A CD2 
87   C CE1 . PHE   A 19  ? 0.8842 0.6903 0.9169 -0.0125 0.0700  0.0293  712  PHE   A CE1 
88   C CE2 . PHE   A 19  ? 0.8906 0.6974 0.9134 0.0159  0.0656  0.0472  712  PHE   A CE2 
89   C CZ  . PHE   A 19  ? 0.8861 0.6888 0.9135 -0.0081 0.0722  0.0386  712  PHE   A CZ  
90   N N   . LYS   A 20  ? 0.8994 0.6868 0.9174 0.1072  0.0512  0.0462  713  LYS   A N   
91   C CA  . LYS   A 20  ? 0.9342 0.6856 0.9199 0.1289  0.0524  0.0574  713  LYS   A CA  
92   C C   . LYS   A 20  ? 0.9396 0.7113 0.9243 0.1370  0.0384  0.0638  713  LYS   A C   
93   O O   . LYS   A 20  ? 0.9151 0.7321 0.9294 0.1383  0.0232  0.0579  713  LYS   A O   
94   C CB  . LYS   A 20  ? 0.9551 0.6928 0.9371 0.1605  0.0490  0.0559  713  LYS   A CB  
95   N N   . LYS   A 21  ? 0.9693 0.7042 0.9176 0.1415  0.0456  0.0754  714  LYS   A N   
96   C CA  . LYS   A 21  ? 0.9763 0.7218 0.9151 0.1506  0.0347  0.0821  714  LYS   A CA  
97   C C   . LYS   A 21  ? 1.0056 0.7346 0.9219 0.1886  0.0214  0.0867  714  LYS   A C   
98   O O   . LYS   A 21  ? 1.0405 0.7213 0.9232 0.2048  0.0307  0.0930  714  LYS   A O   
99   C CB  . LYS   A 21  ? 1.0055 0.7182 0.9156 0.1338  0.0526  0.0915  714  LYS   A CB  
100  C CG  . LYS   A 21  ? 1.0157 0.7586 0.9543 0.1000  0.0582  0.0857  714  LYS   A CG  
101  C CD  . LYS   A 21  ? 1.0757 0.7858 0.9918 0.0827  0.0793  0.0924  714  LYS   A CD  
102  C CE  . LYS   A 21  ? 1.1402 0.8088 1.0422 0.0688  0.1004  0.0910  714  LYS   A CE  
103  N N   . ILE   A 22  ? 0.9897 0.7578 0.9246 0.2038  -0.0012 0.0824  715  ILE   A N   
104  C CA  . ILE   A 22  ? 1.0064 0.7663 0.9247 0.2417  -0.0192 0.0837  715  ILE   A CA  
105  C C   . ILE   A 22  ? 1.0333 0.7661 0.9065 0.2562  -0.0245 0.0952  715  ILE   A C   
106  O O   . ILE   A 22  ? 1.0743 0.7544 0.8980 0.2793  -0.0205 0.1056  715  ILE   A O   
107  C CB  . ILE   A 22  ? 0.9781 0.7969 0.9473 0.2523  -0.0416 0.0683  715  ILE   A CB  
108  C CG1 . ILE   A 22  ? 0.9704 0.8092 0.9784 0.2369  -0.0314 0.0576  715  ILE   A CG1 
109  C CG2 . ILE   A 22  ? 0.9891 0.8036 0.9462 0.2934  -0.0631 0.0669  715  ILE   A CG2 
110  N N   . LYS   A 23  ? 1.0080 0.7712 0.8930 0.2438  -0.0320 0.0937  716  LYS   A N   
111  C CA  . LYS   A 23  ? 1.0306 0.7678 0.8713 0.2565  -0.0355 0.1037  716  LYS   A CA  
112  C C   . LYS   A 23  ? 1.0225 0.7744 0.8702 0.2281  -0.0250 0.1057  716  LYS   A C   
113  O O   . LYS   A 23  ? 0.9925 0.7865 0.8853 0.2035  -0.0241 0.0971  716  LYS   A O   
114  C CB  . LYS   A 23  ? 1.0410 0.7990 0.8802 0.2892  -0.0670 0.0978  716  LYS   A CB  
115  C CG  . LYS   A 23  ? 1.0493 0.8721 0.9389 0.2783  -0.0854 0.0839  716  LYS   A CG  
116  N N   . VAL   A 24  ? 1.0483 0.7635 0.8497 0.2327  -0.0164 0.1169  717  VAL   A N   
117  C CA  . VAL   A 24  ? 1.0486 0.7768 0.8563 0.2089  -0.0053 0.1186  717  VAL   A CA  
118  C C   . VAL   A 24  ? 1.0395 0.8101 0.8649 0.2160  -0.0292 0.1111  717  VAL   A C   
119  O O   . VAL   A 24  ? 1.0545 0.8158 0.8530 0.2439  -0.0480 0.1115  717  VAL   A O   
120  C CB  . VAL   A 24  ? 1.0927 0.7616 0.8440 0.2089  0.0190  0.1329  717  VAL   A CB  
121  C CG1 . VAL   A 24  ? 1.0878 0.7741 0.8503 0.1858  0.0312  0.1332  717  VAL   A CG1 
122  C CG2 . VAL   A 24  ? 1.1203 0.7436 0.8539 0.1992  0.0451  0.1391  717  VAL   A CG2 
123  N N   . LEU   A 25  ? 1.0149 0.8298 0.8832 0.1916  -0.0291 0.1036  718  LEU   A N   
124  C CA  . LEU   A 25  ? 1.0078 0.8607 0.8940 0.1937  -0.0480 0.0959  718  LEU   A CA  
125  C C   . LEU   A 25  ? 1.0379 0.8754 0.8971 0.1880  -0.0371 0.1030  718  LEU   A C   
126  O O   . LEU   A 25  ? 1.0441 0.8865 0.8879 0.2016  -0.0519 0.1009  718  LEU   A O   
127  C CB  . LEU   A 25  ? 0.9706 0.8750 0.9141 0.1722  -0.0530 0.0841  718  LEU   A CB  
128  C CG  . LEU   A 25  ? 0.9676 0.8933 0.9432 0.1760  -0.0626 0.0746  718  LEU   A CG  
129  C CD1 . LEU   A 25  ? 0.9473 0.9142 0.9694 0.1530  -0.0625 0.0648  718  LEU   A CD1 
130  C CD2 . LEU   A 25  ? 0.9709 0.9072 0.9453 0.2037  -0.0870 0.0675  718  LEU   A CD2 
131  N N   . GLY   A 26  ? 1.0556 0.8763 0.9116 0.1674  -0.0112 0.1096  719  GLY   A N   
132  C CA  . GLY   A 26  ? 1.0856 0.8933 0.9218 0.1598  0.0041  0.1155  719  GLY   A CA  
133  C C   . GLY   A 26  ? 1.1137 0.9001 0.9497 0.1377  0.0349  0.1213  719  GLY   A C   
134  O O   . GLY   A 26  ? 1.1007 0.8971 0.9652 0.1218  0.0412  0.1177  719  GLY   A O   
135  N N   . SER   A 27  ? 1.1503 0.9069 0.9546 0.1358  0.0554  0.1291  720  SER   A N   
136  C CA  . SER   A 27  ? 1.1796 0.9147 0.9846 0.1137  0.0880  0.1332  720  SER   A CA  
137  C C   . SER   A 27  ? 1.1833 0.9415 1.0087 0.0976  0.1012  0.1307  720  SER   A C   
138  O O   . SER   A 27  ? 1.1733 0.9589 1.0065 0.1050  0.0851  0.1270  720  SER   A O   
139  C CB  . SER   A 27  ? 1.2479 0.9129 0.9898 0.1266  0.1086  0.1457  720  SER   A CB  
140  O OG  . SER   A 27  ? 1.2991 0.9404 1.0249 0.1403  0.1002  0.1480  720  SER   A OG  
141  N N   . GLY   A 28  ? 1.1926 0.9410 1.0292 0.0755  0.1306  0.1312  721  GLY   A N   
142  C CA  . GLY   A 28  ? 1.1923 0.9635 1.0527 0.0607  0.1458  0.1277  721  GLY   A CA  
143  C C   . GLY   A 28  ? 1.1962 0.9675 1.0850 0.0328  0.1755  0.1239  721  GLY   A C   
144  O O   . GLY   A 28  ? 1.2135 0.9566 1.0942 0.0244  0.1880  0.1254  721  GLY   A O   
145  N N   . ALA   A 29  ? 1.1746 0.9777 1.0985 0.0183  0.1873  0.1177  722  ALA   A N   
146  C CA  . ALA   A 29  ? 1.1602 0.9746 1.1230 -0.0099 0.2138  0.1102  722  ALA   A CA  
147  C C   . ALA   A 29  ? 1.1248 0.9829 1.1410 -0.0260 0.1957  0.0981  722  ALA   A C   
148  O O   . ALA   A 29  ? 1.1228 0.9756 1.1587 -0.0472 0.2125  0.0922  722  ALA   A O   
149  C CB  . ALA   A 29  ? 1.1445 0.9859 1.1337 -0.0172 0.2288  0.1055  722  ALA   A CB  
150  N N   . PHE   A 30  ? 1.0941 0.9906 1.1290 -0.0159 0.1621  0.0943  723  PHE   A N   
151  C CA  . PHE   A 30  ? 1.0596 0.9934 1.1347 -0.0262 0.1412  0.0841  723  PHE   A CA  
152  C C   . PHE   A 30  ? 1.0546 0.9581 1.1127 -0.0292 0.1418  0.0854  723  PHE   A C   
153  O O   . PHE   A 30  ? 1.0425 0.9640 1.1311 -0.0460 0.1382  0.0758  723  PHE   A O   
154  C CB  . PHE   A 30  ? 1.0505 1.0160 1.1327 -0.0107 0.1095  0.0829  723  PHE   A CB  
155  C CG  . PHE   A 30  ? 1.0872 1.0268 1.1293 0.0112  0.0949  0.0908  723  PHE   A CG  
156  C CD1 . PHE   A 30  ? 1.1199 1.0361 1.1238 0.0299  0.0962  0.0990  723  PHE   A CD1 
157  C CD2 . PHE   A 30  ? 1.0990 1.0373 1.1418 0.0135  0.0801  0.0888  723  PHE   A CD2 
158  C CE1 . PHE   A 30  ? 1.1470 1.0429 1.1176 0.0509  0.0802  0.1040  723  PHE   A CE1 
159  C CE2 . PHE   A 30  ? 1.1248 1.0432 1.1369 0.0342  0.0671  0.0941  723  PHE   A CE2 
160  C CZ  . PHE   A 30  ? 1.1404 1.0398 1.1184 0.0530  0.0657  0.1011  723  PHE   A CZ  
161  N N   . GLY   A 31  ? 1.0601 0.9178 1.0682 -0.0110 0.1445  0.0966  724  GLY   A N   
162  C CA  . GLY   A 31  ? 1.0578 0.8824 1.0433 -0.0070 0.1435  0.0994  724  GLY   A CA  
163  C C   . GLY   A 31  ? 1.0476 0.8526 0.9946 0.0224  0.1251  0.1079  724  GLY   A C   
164  O O   . GLY   A 31  ? 1.0713 0.8582 0.9857 0.0393  0.1263  0.1157  724  GLY   A O   
165  N N   . THR   A 32  ? 1.0090 0.8180 0.9598 0.0295  0.1077  0.1051  725  THR   A N   
166  C CA  . THR   A 32  ? 0.9930 0.7873 0.9139 0.0577  0.0896  0.1106  725  THR   A CA  
167  C C   . THR   A 32  ? 0.9336 0.7671 0.8855 0.0615  0.0638  0.1020  725  THR   A C   
168  O O   . THR   A 32  ? 0.9180 0.7696 0.8993 0.0447  0.0637  0.0943  725  THR   A O   
169  C CB  . THR   A 32  ? 1.0425 0.7773 0.9184 0.0689  0.1039  0.1192  725  THR   A CB  
170  O OG1 . THR   A 32  ? 1.0802 0.7740 0.9254 0.0624  0.1324  0.1270  725  THR   A OG1 
171  C CG2 . THR   A 32  ? 1.0636 0.7806 0.9060 0.1019  0.0847  0.1246  725  THR   A CG2 
172  N N   . VAL   A 33  ? 0.8985 0.7431 0.8427 0.0832  0.0429  0.1023  726  VAL   A N   
173  C CA  . VAL   A 33  ? 0.8541 0.7331 0.8266 0.0877  0.0214  0.0936  726  VAL   A CA  
174  C C   . VAL   A 33  ? 0.8484 0.7051 0.8005 0.1107  0.0127  0.0953  726  VAL   A C   
175  O O   . VAL   A 33  ? 0.8684 0.6999 0.7856 0.1327  0.0084  0.1017  726  VAL   A O   
176  C CB  . VAL   A 33  ? 0.8332 0.7504 0.8241 0.0909  0.0040  0.0886  726  VAL   A CB  
177  C CG1 . VAL   A 33  ? 0.8131 0.7593 0.8292 0.0968  -0.0154 0.0794  726  VAL   A CG1 
178  C CG2 . VAL   A 33  ? 0.8207 0.7624 0.8364 0.0696  0.0110  0.0858  726  VAL   A CG2 
179  N N   . TYR   A 34  ? 0.8210 0.6852 0.7926 0.1070  0.0104  0.0892  727  TYR   A N   
180  C CA  . TYR   A 34  ? 0.8210 0.6678 0.7801 0.1288  0.0032  0.0891  727  TYR   A CA  
181  C C   . TYR   A 34  ? 0.7898 0.6782 0.7857 0.1338  -0.0154 0.0775  727  TYR   A C   
182  O O   . TYR   A 34  ? 0.7671 0.6861 0.7947 0.1148  -0.0159 0.0701  727  TYR   A O   
183  C CB  . TYR   A 34  ? 0.8312 0.6451 0.7810 0.1202  0.0212  0.0908  727  TYR   A CB  
184  C CG  . TYR   A 34  ? 0.8694 0.6369 0.7842 0.1126  0.0443  0.1008  727  TYR   A CG  
185  C CD1 . TYR   A 34  ? 0.8729 0.6477 0.8018 0.0845  0.0594  0.0994  727  TYR   A CD1 
186  C CD2 . TYR   A 34  ? 0.9152 0.6296 0.7835 0.1331  0.0524  0.1106  727  TYR   A CD2 
187  C CE1 . TYR   A 34  ? 0.9085 0.6423 0.8107 0.0745  0.0839  0.1065  727  TYR   A CE1 
188  C CE2 . TYR   A 34  ? 0.9538 0.6197 0.7877 0.1239  0.0781  0.1196  727  TYR   A CE2 
189  C CZ  . TYR   A 34  ? 0.9579 0.6351 0.8112 0.0932  0.0949  0.1169  727  TYR   A CZ  
190  O OH  . TYR   A 34  ? 1.0050 0.6367 0.8297 0.0813  0.1233  0.1238  727  TYR   A OH  
191  N N   . LYS   A 35  ? 0.7902 0.6778 0.7810 0.1596  -0.0298 0.0753  728  LYS   A N   
192  C CA  . LYS   A 35  ? 0.7656 0.6909 0.7943 0.1655  -0.0444 0.0626  728  LYS   A CA  
193  C C   . LYS   A 35  ? 0.7716 0.6772 0.8009 0.1675  -0.0338 0.0615  728  LYS   A C   
194  O O   . LYS   A 35  ? 0.8029 0.6694 0.7998 0.1854  -0.0296 0.0689  728  LYS   A O   
195  C CB  . LYS   A 35  ? 0.7837 0.7201 0.8093 0.1944  -0.0668 0.0587  728  LYS   A CB  
196  N N   . GLY   A 36  ? 0.7461 0.6723 0.8061 0.1496  -0.0278 0.0530  729  GLY   A N   
197  C CA  . GLY   A 36  ? 0.7498 0.6557 0.8093 0.1496  -0.0158 0.0509  729  GLY   A CA  
198  C C   . GLY   A 36  ? 0.7217 0.6580 0.8189 0.1474  -0.0179 0.0377  729  GLY   A C   
199  O O   . GLY   A 36  ? 0.6995 0.6744 0.8266 0.1498  -0.0301 0.0290  729  GLY   A O   
200  N N   . LEU   A 37  ? 0.7262 0.6430 0.8213 0.1411  -0.0037 0.0355  730  LEU   A N   
201  C CA  . LEU   A 37  ? 0.7137 0.6515 0.8396 0.1392  -0.0005 0.0232  730  LEU   A CA  
202  C C   . LEU   A 37  ? 0.7197 0.6389 0.8378 0.1153  0.0169  0.0215  730  LEU   A C   
203  O O   . LEU   A 37  ? 0.7372 0.6186 0.8267 0.1104  0.0275  0.0281  730  LEU   A O   
204  C CB  . LEU   A 37  ? 0.7227 0.6508 0.8509 0.1684  -0.0031 0.0202  730  LEU   A CB  
205  C CG  . LEU   A 37  ? 0.7162 0.6826 0.8887 0.1782  -0.0077 0.0052  730  LEU   A CG  
206  C CD1 . LEU   A 37  ? 0.6921 0.7064 0.8977 0.1717  -0.0213 -0.0027 730  LEU   A CD1 
207  C CD2 . LEU   A 37  ? 0.7281 0.6878 0.9020 0.2131  -0.0162 0.0033  730  LEU   A CD2 
208  N N   . TRP   A 38  ? 0.7049 0.6476 0.8457 0.1003  0.0201  0.0121  731  TRP   A N   
209  C CA  . TRP   A 38  ? 0.7180 0.6433 0.8478 0.0782  0.0338  0.0092  731  TRP   A CA  
210  C C   . TRP   A 38  ? 0.7269 0.6567 0.8727 0.0783  0.0441  -0.0021 731  TRP   A C   
211  O O   . TRP   A 38  ? 0.7071 0.6679 0.8821 0.0829  0.0411  -0.0099 731  TRP   A O   
212  C CB  . TRP   A 38  ? 0.7014 0.6416 0.8302 0.0561  0.0293  0.0106  731  TRP   A CB  
213  C CG  . TRP   A 38  ? 0.7051 0.6317 0.8221 0.0345  0.0384  0.0060  731  TRP   A CG  
214  C CD1 . TRP   A 38  ? 0.7301 0.6239 0.8256 0.0260  0.0488  0.0054  731  TRP   A CD1 
215  C CD2 . TRP   A 38  ? 0.6957 0.6384 0.8171 0.0188  0.0363  0.0013  731  TRP   A CD2 
216  N NE1 . TRP   A 38  ? 0.7354 0.6265 0.8229 0.0068  0.0515  -0.0007 731  TRP   A NE1 
217  C CE2 . TRP   A 38  ? 0.7180 0.6374 0.8190 0.0031  0.0438  -0.0024 731  TRP   A CE2 
218  C CE3 . TRP   A 38  ? 0.6886 0.6598 0.8260 0.0170  0.0289  -0.0003 731  TRP   A CE3 
219  C CZ2 . TRP   A 38  ? 0.7305 0.6536 0.8239 -0.0117 0.0424  -0.0071 731  TRP   A CZ2 
220  C CZ3 . TRP   A 38  ? 0.7032 0.6752 0.8325 0.0016  0.0300  -0.0039 731  TRP   A CZ3 
221  C CH2 . TRP   A 38  ? 0.7207 0.6686 0.8268 -0.0114 0.0359  -0.0070 731  TRP   A CH2 
222  N N   . ILE   A 39  ? 0.7549 0.6520 0.8813 0.0724  0.0581  -0.0039 732  ILE   A N   
223  C CA  . ILE   A 39  ? 0.7704 0.6629 0.9042 0.0707  0.0719  -0.0145 732  ILE   A CA  
224  C C   . ILE   A 39  ? 0.7994 0.6741 0.9104 0.0447  0.0795  -0.0170 732  ILE   A C   
225  O O   . ILE   A 39  ? 0.8177 0.6588 0.9020 0.0367  0.0856  -0.0152 732  ILE   A O   
226  C CB  . ILE   A 39  ? 0.7912 0.6545 0.9166 0.0892  0.0819  -0.0155 732  ILE   A CB  
227  C CG1 . ILE   A 39  ? 0.7975 0.6687 0.9333 0.1181  0.0703  -0.0104 732  ILE   A CG1 
228  C CG2 . ILE   A 39  ? 0.7949 0.6593 0.9343 0.0903  0.0973  -0.0278 732  ILE   A CG2 
229  N N   . PRO   A 40  ? 0.8002 0.6944 0.9188 0.0315  0.0787  -0.0218 733  PRO   A N   
230  C CA  . PRO   A 40  ? 0.8283 0.7041 0.9203 0.0098  0.0825  -0.0245 733  PRO   A CA  
231  C C   . PRO   A 40  ? 0.8743 0.7151 0.9451 0.0064  0.0989  -0.0318 733  PRO   A C   
232  O O   . PRO   A 40  ? 0.8731 0.7112 0.9562 0.0193  0.1110  -0.0372 733  PRO   A O   
233  C CB  . PRO   A 40  ? 0.8192 0.7185 0.9217 0.0025  0.0807  -0.0279 733  PRO   A CB  
234  C CG  . PRO   A 40  ? 0.7983 0.7320 0.9334 0.0157  0.0710  -0.0249 733  PRO   A CG  
235  C CD  . PRO   A 40  ? 0.7718 0.7028 0.9207 0.0358  0.0741  -0.0254 733  PRO   A CD  
236  N N   . GLU   A 41  ? 0.9124 0.7273 0.9530 -0.0104 0.0985  -0.0331 734  GLU   A N   
237  C CA  . GLU   A 41  ? 0.9580 0.7334 0.9707 -0.0170 0.1117  -0.0404 734  GLU   A CA  
238  C C   . GLU   A 41  ? 0.9819 0.7463 0.9938 -0.0105 0.1302  -0.0493 734  GLU   A C   
239  O O   . GLU   A 41  ? 0.9914 0.7373 1.0047 0.0019  0.1429  -0.0520 734  GLU   A O   
240  C CB  . GLU   A 41  ? 0.9985 0.7588 0.9824 -0.0392 0.1041  -0.0442 734  GLU   A CB  
241  C CG  . GLU   A 41  ? 1.0699 0.7876 1.0227 -0.0478 0.1155  -0.0532 734  GLU   A CG  
242  N N   . GLY   A 42  ? 0.9883 0.7611 0.9963 -0.0182 0.1335  -0.0539 735  GLY   A N   
243  C CA  . GLY   A 42  ? 1.0040 0.7647 1.0100 -0.0144 0.1548  -0.0631 735  GLY   A CA  
244  C C   . GLY   A 42  ? 0.9840 0.7807 1.0326 -0.0018 0.1607  -0.0645 735  GLY   A C   
245  O O   . GLY   A 42  ? 0.9876 0.7848 1.0381 -0.0053 0.1765  -0.0717 735  GLY   A O   
246  N N   . GLU   A 43  ? 0.9581 0.7841 1.0404 0.0125  0.1482  -0.0585 736  GLU   A N   
247  C CA  . GLU   A 43  ? 0.9258 0.7916 1.0538 0.0253  0.1485  -0.0613 736  GLU   A CA  
248  C C   . GLU   A 43  ? 0.9135 0.7899 1.0693 0.0495  0.1462  -0.0613 736  GLU   A C   
249  O O   . GLU   A 43  ? 0.9306 0.7869 1.0693 0.0564  0.1388  -0.0541 736  GLU   A O   
250  C CB  . GLU   A 43  ? 0.9251 0.8211 1.0653 0.0197  0.1298  -0.0546 736  GLU   A CB  
251  C CG  . GLU   A 43  ? 0.9846 0.8711 1.0979 -0.0003 0.1305  -0.0543 736  GLU   A CG  
252  C CD  . GLU   A 43  ? 1.0332 0.9515 1.1684 -0.0033 0.1225  -0.0528 736  GLU   A CD  
253  O OE1 . GLU   A 43  ? 1.0271 0.9650 1.1926 -0.0002 0.1345  -0.0608 736  GLU   A OE1 
254  O OE2 . GLU   A 43  ? 1.0514 0.9752 1.1752 -0.0093 0.1053  -0.0446 736  GLU   A OE2 
255  N N   . LYS   A 44  ? 0.8812 0.7885 1.0801 0.0629  0.1528  -0.0701 737  LYS   A N   
256  C CA  . LYS   A 44  ? 0.8606 0.7841 1.0909 0.0900  0.1479  -0.0722 737  LYS   A CA  
257  C C   . LYS   A 44  ? 0.8202 0.7926 1.0915 0.0981  0.1298  -0.0728 737  LYS   A C   
258  O O   . LYS   A 44  ? 0.7999 0.8070 1.1178 0.1101  0.1332  -0.0845 737  LYS   A O   
259  C CB  . LYS   A 44  ? 0.8729 0.7951 1.1249 0.1005  0.1710  -0.0858 737  LYS   A CB  
260  N N   . VAL   A 45  ? 0.8048 0.7808 1.0604 0.0904  0.1111  -0.0619 738  VAL   A N   
261  C CA  . VAL   A 45  ? 0.7692 0.7866 1.0565 0.0961  0.0931  -0.0623 738  VAL   A CA  
262  C C   . VAL   A 45  ? 0.7633 0.7737 1.0286 0.1025  0.0717  -0.0483 738  VAL   A C   
263  O O   . VAL   A 45  ? 0.7900 0.7716 1.0175 0.0890  0.0714  -0.0384 738  VAL   A O   
264  C CB  . VAL   A 45  ? 0.7684 0.8033 1.0645 0.0738  0.0985  -0.0671 738  VAL   A CB  
265  N N   . LYS   A 46  ? 0.7279 0.7650 1.0170 0.1228  0.0540  -0.0487 739  LYS   A N   
266  C CA  . LYS   A 46  ? 0.7248 0.7539 0.9913 0.1309  0.0352  -0.0358 739  LYS   A CA  
267  C C   . LYS   A 46  ? 0.6916 0.7478 0.9674 0.1180  0.0232  -0.0349 739  LYS   A C   
268  O O   . LYS   A 46  ? 0.6721 0.7653 0.9855 0.1200  0.0185  -0.0459 739  LYS   A O   
269  C CB  . LYS   A 46  ? 0.7436 0.7786 1.0206 0.1638  0.0213  -0.0361 739  LYS   A CB  
270  C CG  . LYS   A 46  ? 0.8245 0.8124 1.0641 0.1775  0.0270  -0.0264 739  LYS   A CG  
271  C CD  . LYS   A 46  ? 0.8786 0.8510 1.1247 0.1812  0.0464  -0.0345 739  LYS   A CD  
272  C CE  . LYS   A 46  ? 0.9067 0.8901 1.1767 0.2159  0.0399  -0.0414 739  LYS   A CE  
273  N N   . ILE   A 47  ? 0.6811 0.7192 0.9248 0.1041  0.0196  -0.0232 740  ILE   A N   
274  C CA  . ILE   A 47  ? 0.6541 0.7126 0.9018 0.0926  0.0095  -0.0213 740  ILE   A CA  
275  C C   . ILE   A 47  ? 0.6413 0.6941 0.8700 0.1030  -0.0061 -0.0103 740  ILE   A C   
276  O O   . ILE   A 47  ? 0.6632 0.6852 0.8602 0.1015  -0.0029 0.0003  740  ILE   A O   
277  C CB  . ILE   A 47  ? 0.6709 0.7162 0.8994 0.0665  0.0195  -0.0187 740  ILE   A CB  
278  C CG1 . ILE   A 47  ? 0.6806 0.7244 0.9194 0.0562  0.0372  -0.0292 740  ILE   A CG1 
279  C CG2 . ILE   A 47  ? 0.6666 0.7294 0.8962 0.0568  0.0090  -0.0158 740  ILE   A CG2 
280  C CD1 . ILE   A 47  ? 0.7136 0.7365 0.9242 0.0344  0.0457  -0.0266 740  ILE   A CD1 
281  N N   . PRO   A 48  ? 0.6029 0.6835 0.8494 0.1124  -0.0217 -0.0134 741  PRO   A N   
282  C CA  . PRO   A 48  ? 0.5920 0.6640 0.8154 0.1231  -0.0356 -0.0031 741  PRO   A CA  
283  C C   . PRO   A 48  ? 0.5660 0.6281 0.7679 0.1030  -0.0325 0.0059  741  PRO   A C   
284  O O   . PRO   A 48  ? 0.5538 0.6345 0.7684 0.0881  -0.0327 0.0017  741  PRO   A O   
285  C CB  . PRO   A 48  ? 0.5848 0.6925 0.8365 0.1363  -0.0532 -0.0128 741  PRO   A CB  
286  C CG  . PRO   A 48  ? 0.5714 0.7059 0.8655 0.1364  -0.0476 -0.0289 741  PRO   A CG  
287  C CD  . PRO   A 48  ? 0.5664 0.6858 0.8543 0.1132  -0.0264 -0.0279 741  PRO   A CD  
288  N N   . VAL   A 49  ? 0.5547 0.5864 0.7247 0.1025  -0.0283 0.0176  742  VAL   A N   
289  C CA  . VAL   A 49  ? 0.5347 0.5592 0.6889 0.0841  -0.0246 0.0247  742  VAL   A CA  
290  C C   . VAL   A 49  ? 0.5288 0.5410 0.6601 0.0923  -0.0300 0.0349  742  VAL   A C   
291  O O   . VAL   A 49  ? 0.5369 0.5358 0.6544 0.1128  -0.0353 0.0386  742  VAL   A O   
292  C CB  . VAL   A 49  ? 0.5439 0.5441 0.6846 0.0680  -0.0099 0.0265  742  VAL   A CB  
293  C CG1 . VAL   A 49  ? 0.5441 0.5534 0.7004 0.0568  -0.0033 0.0169  742  VAL   A CG1 
294  C CG2 . VAL   A 49  ? 0.5559 0.5224 0.6756 0.0790  -0.0023 0.0319  742  VAL   A CG2 
295  N N   . ALA   A 50  ? 0.5176 0.5329 0.6432 0.0776  -0.0284 0.0392  743  ALA   A N   
296  C CA  . ALA   A 50  ? 0.5305 0.5316 0.6338 0.0807  -0.0279 0.0487  743  ALA   A CA  
297  C C   . ALA   A 50  ? 0.5409 0.5244 0.6353 0.0620  -0.0134 0.0526  743  ALA   A C   
298  O O   . ALA   A 50  ? 0.5297 0.5265 0.6380 0.0449  -0.0117 0.0478  743  ALA   A O   
299  C CB  . ALA   A 50  ? 0.5165 0.5410 0.6273 0.0789  -0.0375 0.0478  743  ALA   A CB  
300  N N   . ILE   A 51  ? 0.5601 0.5116 0.6303 0.0654  -0.0029 0.0602  744  ILE   A N   
301  C CA  . ILE   A 51  ? 0.5812 0.5157 0.6460 0.0464  0.0120  0.0618  744  ILE   A CA  
302  C C   . ILE   A 51  ? 0.5974 0.5261 0.6517 0.0416  0.0190  0.0684  744  ILE   A C   
303  O O   . ILE   A 51  ? 0.6200 0.5258 0.6492 0.0562  0.0223  0.0763  744  ILE   A O   
304  C CB  . ILE   A 51  ? 0.6069 0.5028 0.6521 0.0503  0.0244  0.0639  744  ILE   A CB  
305  C CG1 . ILE   A 51  ? 0.6126 0.5144 0.6700 0.0551  0.0201  0.0562  744  ILE   A CG1 
306  C CG2 . ILE   A 51  ? 0.6197 0.4963 0.6599 0.0286  0.0410  0.0637  744  ILE   A CG2 
307  C CD1 . ILE   A 51  ? 0.6374 0.5160 0.6791 0.0784  0.0199  0.0590  744  ILE   A CD1 
308  N N   . LYS   A 52  ? 0.5868 0.5349 0.6588 0.0226  0.0214  0.0650  745  LYS   A N   
309  C CA  . LYS   A 52  ? 0.6002 0.5452 0.6680 0.0163  0.0314  0.0696  745  LYS   A CA  
310  C C   . LYS   A 52  ? 0.6185 0.5426 0.6855 -0.0020 0.0500  0.0680  745  LYS   A C   
311  O O   . LYS   A 52  ? 0.6048 0.5450 0.6934 -0.0195 0.0487  0.0593  745  LYS   A O   
312  C CB  . LYS   A 52  ? 0.6035 0.5860 0.6955 0.0089  0.0221  0.0654  745  LYS   A CB  
313  C CG  . LYS   A 52  ? 0.6472 0.6305 0.7370 0.0066  0.0320  0.0698  745  LYS   A CG  
314  C CD  . LYS   A 52  ? 0.6827 0.7022 0.7942 0.0050  0.0202  0.0658  745  LYS   A CD  
315  C CE  . LYS   A 52  ? 0.7319 0.7496 0.8333 0.0126  0.0263  0.0714  745  LYS   A CE  
316  N NZ  . LYS   A 52  ? 0.7416 0.7851 0.8523 0.0199  0.0114  0.0693  745  LYS   A NZ  
317  N N   . GLU   A 53  ? 0.6538 0.5392 0.6934 0.0021  0.0671  0.0756  746  GLU   A N   
318  C CA  . GLU   A 53  ? 0.6871 0.5481 0.7250 -0.0173 0.0884  0.0735  746  GLU   A CA  
319  C C   . GLU   A 53  ? 0.6999 0.5702 0.7490 -0.0299 0.1021  0.0737  746  GLU   A C   
320  O O   . GLU   A 53  ? 0.7311 0.5810 0.7555 -0.0187 0.1117  0.0831  746  GLU   A O   
321  C CB  . GLU   A 53  ? 0.7536 0.5596 0.7517 -0.0064 0.1034  0.0816  746  GLU   A CB  
322  C CG  . GLU   A 53  ? 0.8502 0.6272 0.8464 -0.0290 0.1275  0.0779  746  GLU   A CG  
323  C CD  . GLU   A 53  ? 0.9917 0.7119 0.9497 -0.0198 0.1409  0.0837  746  GLU   A CD  
324  O OE1 . GLU   A 53  ? 1.0363 0.7284 0.9587 0.0067  0.1384  0.0949  746  GLU   A OE1 
325  O OE2 . GLU   A 53  ? 1.0301 0.7328 0.9925 -0.0381 0.1531  0.0765  746  GLU   A OE2 
326  N N   . LEU   A 54  ? 0.6777 0.5797 0.7636 -0.0517 0.1021  0.0628  747  LEU   A N   
327  C CA  . LEU   A 54  ? 0.6724 0.5910 0.7786 -0.0643 0.1150  0.0603  747  LEU   A CA  
328  C C   . LEU   A 54  ? 0.7052 0.5864 0.8006 -0.0798 0.1460  0.0609  747  LEU   A C   
329  O O   . LEU   A 54  ? 0.7195 0.5721 0.8048 -0.0888 0.1547  0.0582  747  LEU   A O   
330  C CB  . LEU   A 54  ? 0.6360 0.6057 0.7885 -0.0794 0.1007  0.0467  747  LEU   A CB  
331  C CG  . LEU   A 54  ? 0.6364 0.6379 0.7966 -0.0661 0.0725  0.0458  747  LEU   A CG  
332  C CD1 . LEU   A 54  ? 0.6162 0.6604 0.8148 -0.0792 0.0586  0.0328  747  LEU   A CD1 
333  C CD2 . LEU   A 54  ? 0.6414 0.6475 0.7881 -0.0466 0.0675  0.0553  747  LEU   A CD2 
334  N N   . ARG   A 55  ? 0.7183 0.5994 0.8173 -0.0844 0.1646  0.0634  748  ARG   A N   
335  C CA  . ARG   A 55  ? 0.7557 0.6016 0.8467 -0.1014 0.1992  0.0634  748  ARG   A CA  
336  C C   . ARG   A 55  ? 0.7540 0.6208 0.8897 -0.1325 0.2068  0.0459  748  ARG   A C   
337  O O   . ARG   A 55  ? 0.7214 0.6425 0.9059 -0.1435 0.1934  0.0331  748  ARG   A O   
338  C CB  . ARG   A 55  ? 0.7721 0.6180 0.8598 -0.0988 0.2176  0.0688  748  ARG   A CB  
339  N N   . GLU   A 56  ? 0.7888 0.6105 0.9054 -0.1453 0.2271  0.0449  749  GLU   A N   
340  C CA  . GLU   A 56  ? 0.7992 0.6276 0.9490 -0.1758 0.2370  0.0277  749  GLU   A CA  
341  C C   . GLU   A 56  ? 0.7971 0.6629 0.9994 -0.2008 0.2529  0.0134  749  GLU   A C   
342  O O   . GLU   A 56  ? 0.8006 0.6572 0.9977 -0.1996 0.2754  0.0199  749  GLU   A O   
343  C CB  . GLU   A 56  ? 0.8556 0.6131 0.9626 -0.1821 0.2649  0.0331  749  GLU   A CB  
344  C CG  . GLU   A 56  ? 0.8963 0.6506 1.0299 -0.2135 0.2756  0.0150  749  GLU   A CG  
345  C CD  . GLU   A 56  ? 1.0231 0.7022 1.1075 -0.2155 0.2993  0.0215  749  GLU   A CD  
346  O OE1 . GLU   A 56  ? 1.0919 0.7196 1.1200 -0.1907 0.3080  0.0409  749  GLU   A OE1 
347  O OE2 . GLU   A 56  ? 1.0388 0.7088 1.1399 -0.2414 0.3088  0.0063  749  GLU   A OE2 
348  N N   . ALA   A 57  ? 0.7863 0.6955 1.0395 -0.2226 0.2401  -0.0073 750  ALA   A N   
349  C CA  . ALA   A 57  ? 0.7707 0.7263 1.0866 -0.2488 0.2492  -0.0270 750  ALA   A CA  
350  C C   . ALA   A 57  ? 0.7672 0.7667 1.1123 -0.2398 0.2478  -0.0256 750  ALA   A C   
351  O O   . ALA   A 57  ? 0.7504 0.7695 1.1358 -0.2590 0.2711  -0.0367 750  ALA   A O   
352  C CB  . ALA   A 57  ? 0.7822 0.6978 1.0995 -0.2772 0.2906  -0.0340 750  ALA   A CB  
353  N N   . THR   A 58  ? 0.7827 0.7984 1.1107 -0.2118 0.2220  -0.0137 751  THR   A N   
354  C CA  . THR   A 58  ? 0.7867 0.8426 1.1397 -0.2011 0.2185  -0.0125 751  THR   A CA  
355  C C   . THR   A 58  ? 0.7653 0.8913 1.1824 -0.2100 0.1928  -0.0328 751  THR   A C   
356  O O   . THR   A 58  ? 0.7381 0.9035 1.2037 -0.2197 0.2026  -0.0442 751  THR   A O   
357  C CB  . THR   A 58  ? 0.8191 0.8624 1.1275 -0.1685 0.2006  0.0067  751  THR   A CB  
358  N N   . SER   A 59  ? 0.7720 0.9113 1.1871 -0.2056 0.1603  -0.0377 752  SER   A N   
359  C CA  . SER   A 59  ? 0.7472 0.9441 1.2087 -0.2090 0.1298  -0.0553 752  SER   A CA  
360  C C   . SER   A 59  ? 0.7334 0.9455 1.2349 -0.2388 0.1335  -0.0783 752  SER   A C   
361  O O   . SER   A 59  ? 0.7556 0.9280 1.2334 -0.2521 0.1438  -0.0795 752  SER   A O   
362  C CB  . SER   A 59  ? 0.7778 0.9725 1.2080 -0.1890 0.0958  -0.0482 752  SER   A CB  
363  O OG  . SER   A 59  ? 0.7807 1.0200 1.2438 -0.1916 0.0656  -0.0647 752  SER   A OG  
364  N N   . PRO   A 60  ? 0.6917 0.9641 1.2549 -0.2478 0.1208  -0.0984 753  PRO   A N   
365  C CA  . PRO   A 60  ? 0.6690 0.9638 1.2757 -0.2760 0.1184  -0.1241 753  PRO   A CA  
366  C C   . PRO   A 60  ? 0.6734 0.9767 1.2693 -0.2727 0.0803  -0.1334 753  PRO   A C   
367  O O   . PRO   A 60  ? 0.6566 0.9752 1.2828 -0.2954 0.0748  -0.1557 753  PRO   A O   
368  C CB  . PRO   A 60  ? 0.6304 0.9905 1.3101 -0.2832 0.1186  -0.1424 753  PRO   A CB  
369  C CG  . PRO   A 60  ? 0.6326 1.0149 1.3031 -0.2515 0.0991  -0.1286 753  PRO   A CG  
370  C CD  . PRO   A 60  ? 0.6576 0.9813 1.2549 -0.2317 0.1068  -0.1001 753  PRO   A CD  
371  N N   . LYS   A 61  ? 0.6955 0.9876 1.2478 -0.2456 0.0550  -0.1177 754  LYS   A N   
372  C CA  . LYS   A 61  ? 0.7074 1.0005 1.2406 -0.2404 0.0217  -0.1243 754  LYS   A CA  
373  C C   . LYS   A 61  ? 0.7396 0.9819 1.2364 -0.2542 0.0326  -0.1242 754  LYS   A C   
374  O O   . LYS   A 61  ? 0.7730 0.9661 1.2304 -0.2507 0.0567  -0.1067 754  LYS   A O   
375  C CB  . LYS   A 61  ? 0.7473 1.0331 1.2397 -0.2098 -0.0001 -0.1061 754  LYS   A CB  
376  C CG  . LYS   A 61  ? 0.7765 1.1072 1.2949 -0.1915 -0.0164 -0.1052 754  LYS   A CG  
377  C CD  . LYS   A 61  ? 0.8513 1.1675 1.3244 -0.1646 -0.0378 -0.0892 754  LYS   A CD  
378  C CE  . LYS   A 61  ? 0.8847 1.2358 1.3759 -0.1448 -0.0504 -0.0857 754  LYS   A CE  
379  N NZ  . LYS   A 61  ? 0.9121 1.2613 1.4134 -0.1428 -0.0226 -0.0750 754  LYS   A NZ  
380  N N   . ALA   A 62  ? 0.7271 0.9797 1.2332 -0.2672 0.0124  -0.1439 755  ALA   A N   
381  C CA  . ALA   A 62  ? 0.7536 0.9582 1.2231 -0.2790 0.0189  -0.1460 755  ALA   A CA  
382  C C   . ALA   A 62  ? 0.7840 0.9560 1.1945 -0.2537 0.0054  -0.1269 755  ALA   A C   
383  O O   . ALA   A 62  ? 0.7777 0.9704 1.1815 -0.2311 -0.0143 -0.1176 755  ALA   A O   
384  C CB  . ALA   A 62  ? 0.7369 0.9653 1.2336 -0.2993 -0.0016 -0.1746 755  ALA   A CB  
385  N N   . ASN   A 63  ? 0.8120 0.9321 1.1812 -0.2577 0.0176  -0.1219 756  ASN   A N   
386  C CA  . ASN   A 63  ? 0.8424 0.9309 1.1606 -0.2363 0.0095  -0.1060 756  ASN   A CA  
387  C C   . ASN   A 63  ? 0.8325 0.9443 1.1418 -0.2234 -0.0251 -0.1115 756  ASN   A C   
388  O O   . ASN   A 63  ? 0.8503 0.9542 1.1314 -0.2015 -0.0326 -0.0962 756  ASN   A O   
389  C CB  . ASN   A 63  ? 0.8907 0.9235 1.1729 -0.2449 0.0275  -0.1050 756  ASN   A CB  
390  C CG  . ASN   A 63  ? 0.9579 0.9499 1.2213 -0.2416 0.0600  -0.0879 756  ASN   A CG  
391  O OD1 . ASN   A 63  ? 0.9962 0.9396 1.2290 -0.2455 0.0767  -0.0852 756  ASN   A OD1 
392  N ND2 . ASN   A 63  ? 0.9620 0.9687 1.2381 -0.2319 0.0694  -0.0754 756  ASN   A ND2 
393  N N   . LYS   A 64  ? 0.8043 0.9442 1.1370 -0.2363 -0.0461 -0.1337 757  LYS   A N   
394  C CA  . LYS   A 64  ? 0.7990 0.9572 1.1183 -0.2231 -0.0801 -0.1399 757  LYS   A CA  
395  C C   . LYS   A 64  ? 0.7757 0.9698 1.1097 -0.2021 -0.0937 -0.1300 757  LYS   A C   
396  O O   . LYS   A 64  ? 0.7961 0.9802 1.0960 -0.1820 -0.1071 -0.1190 757  LYS   A O   
397  C CB  . LYS   A 64  ? 0.8081 0.9901 1.1508 -0.2409 -0.1016 -0.1679 757  LYS   A CB  
398  C CG  . LYS   A 64  ? 0.8570 1.0519 1.1776 -0.2253 -0.1384 -0.1747 757  LYS   A CG  
399  N N   . GLU   A 65  ? 0.7326 0.9646 1.1153 -0.2066 -0.0871 -0.1332 758  GLU   A N   
400  C CA  . GLU   A 65  ? 0.7063 0.9711 1.1043 -0.1862 -0.0977 -0.1242 758  GLU   A CA  
401  C C   . GLU   A 65  ? 0.7159 0.9539 1.0835 -0.1689 -0.0804 -0.0986 758  GLU   A C   
402  O O   . GLU   A 65  ? 0.7130 0.9638 1.0738 -0.1487 -0.0921 -0.0888 758  GLU   A O   
403  C CB  . GLU   A 65  ? 0.6906 1.0043 1.1517 -0.1963 -0.0937 -0.1369 758  GLU   A CB  
404  N N   . ILE   A 66  ? 0.7220 0.9222 1.0712 -0.1762 -0.0533 -0.0887 759  ILE   A N   
405  C CA  . ILE   A 66  ? 0.7310 0.9043 1.0500 -0.1597 -0.0392 -0.0668 759  ILE   A CA  
406  C C   . ILE   A 66  ? 0.7418 0.8944 1.0192 -0.1448 -0.0545 -0.0602 759  ILE   A C   
407  O O   . ILE   A 66  ? 0.7474 0.9006 1.0102 -0.1266 -0.0589 -0.0474 759  ILE   A O   
408  C CB  . ILE   A 66  ? 0.7524 0.8875 1.0595 -0.1701 -0.0087 -0.0601 759  ILE   A CB  
409  C CG1 . ILE   A 66  ? 0.7453 0.8949 1.0877 -0.1828 0.0123  -0.0631 759  ILE   A CG1 
410  C CG2 . ILE   A 66  ? 0.7829 0.8847 1.0510 -0.1514 0.0003  -0.0402 759  ILE   A CG2 
411  C CD1 . ILE   A 66  ? 0.7756 0.8850 1.1064 -0.1980 0.0409  -0.0619 759  ILE   A CD1 
412  N N   . LEU   A 67  ? 0.7398 0.8732 0.9981 -0.1538 -0.0614 -0.0702 760  LEU   A N   
413  C CA  . LEU   A 67  ? 0.7514 0.8615 0.9692 -0.1427 -0.0724 -0.0664 760  LEU   A CA  
414  C C   . LEU   A 67  ? 0.7346 0.8669 0.9476 -0.1279 -0.0969 -0.0666 760  LEU   A C   
415  O O   . LEU   A 67  ? 0.7492 0.8660 0.9337 -0.1130 -0.0984 -0.0554 760  LEU   A O   
416  C CB  . LEU   A 67  ? 0.7668 0.8526 0.9668 -0.1571 -0.0740 -0.0799 760  LEU   A CB  
417  C CG  . LEU   A 67  ? 0.8092 0.8495 0.9763 -0.1568 -0.0549 -0.0724 760  LEU   A CG  
418  C CD1 . LEU   A 67  ? 0.8196 0.8476 0.9928 -0.1529 -0.0309 -0.0581 760  LEU   A CD1 
419  C CD2 . LEU   A 67  ? 0.8225 0.8405 0.9806 -0.1752 -0.0521 -0.0878 760  LEU   A CD2 
420  N N   . ASP   A 68  ? 0.7029 0.8713 0.9453 -0.1310 -0.1150 -0.0794 761  ASP   A N   
421  C CA  . ASP   A 68  ? 0.6933 0.8812 0.9298 -0.1140 -0.1394 -0.0794 761  ASP   A CA  
422  C C   . ASP   A 68  ? 0.6733 0.8672 0.9110 -0.0972 -0.1322 -0.0623 761  ASP   A C   
423  O O   . ASP   A 68  ? 0.6850 0.8683 0.8940 -0.0813 -0.1422 -0.0547 761  ASP   A O   
424  C CB  . ASP   A 68  ? 0.6948 0.9261 0.9708 -0.1188 -0.1605 -0.0977 761  ASP   A CB  
425  C CG  . ASP   A 68  ? 0.7903 1.0200 1.0690 -0.1366 -0.1709 -0.1180 761  ASP   A CG  
426  O OD1 . ASP   A 68  ? 0.8353 1.0253 1.0733 -0.1412 -0.1666 -0.1173 761  ASP   A OD1 
427  O OD2 . ASP   A 68  ? 0.8021 1.0712 1.1256 -0.1466 -0.1827 -0.1361 761  ASP   A OD2 
428  N N   . GLU   A 69  ? 0.6434 0.8504 0.9108 -0.1012 -0.1138 -0.0569 762  GLU   A N   
429  C CA  . GLU   A 69  ? 0.6351 0.8467 0.9035 -0.0865 -0.1060 -0.0422 762  GLU   A CA  
430  C C   . GLU   A 69  ? 0.6440 0.8197 0.8743 -0.0783 -0.0956 -0.0281 762  GLU   A C   
431  O O   . GLU   A 69  ? 0.6491 0.8219 0.8640 -0.0636 -0.1001 -0.0191 762  GLU   A O   
432  C CB  . GLU   A 69  ? 0.6505 0.8784 0.9540 -0.0942 -0.0865 -0.0408 762  GLU   A CB  
433  C CG  . GLU   A 69  ? 0.6850 0.9557 1.0285 -0.0903 -0.0947 -0.0476 762  GLU   A CG  
434  N N   . ALA   A 70  ? 0.6416 0.7902 0.8581 -0.0881 -0.0817 -0.0276 763  ALA   A N   
435  C CA  . ALA   A 70  ? 0.6546 0.7726 0.8412 -0.0810 -0.0717 -0.0173 763  ALA   A CA  
436  C C   . ALA   A 70  ? 0.6617 0.7659 0.8179 -0.0738 -0.0842 -0.0182 763  ALA   A C   
437  O O   . ALA   A 70  ? 0.6682 0.7593 0.8070 -0.0638 -0.0796 -0.0095 763  ALA   A O   
438  C CB  . ALA   A 70  ? 0.6640 0.7566 0.8441 -0.0919 -0.0554 -0.0187 763  ALA   A CB  
439  N N   . TYR   A 71  ? 0.6583 0.7645 0.8070 -0.0788 -0.0998 -0.0295 764  TYR   A N   
440  C CA  . TYR   A 71  ? 0.6790 0.7666 0.7916 -0.0715 -0.1114 -0.0305 764  TYR   A CA  
441  C C   . TYR   A 71  ? 0.6605 0.7572 0.7677 -0.0556 -0.1196 -0.0224 764  TYR   A C   
442  O O   . TYR   A 71  ? 0.6715 0.7453 0.7498 -0.0479 -0.1153 -0.0158 764  TYR   A O   
443  C CB  . TYR   A 71  ? 0.6953 0.7850 0.8004 -0.0784 -0.1300 -0.0455 764  TYR   A CB  
444  C CG  . TYR   A 71  ? 0.7523 0.8147 0.8104 -0.0701 -0.1411 -0.0464 764  TYR   A CG  
445  C CD1 . TYR   A 71  ? 0.7755 0.8445 0.8197 -0.0557 -0.1599 -0.0452 764  TYR   A CD1 
446  C CD2 . TYR   A 71  ? 0.7976 0.8235 0.8214 -0.0752 -0.1310 -0.0480 764  TYR   A CD2 
447  C CE1 . TYR   A 71  ? 0.8210 0.8569 0.8141 -0.0470 -0.1675 -0.0446 764  TYR   A CE1 
448  C CE2 . TYR   A 71  ? 0.8428 0.8382 0.8184 -0.0679 -0.1376 -0.0485 764  TYR   A CE2 
449  C CZ  . TYR   A 71  ? 0.8633 0.8619 0.8214 -0.0539 -0.1556 -0.0464 764  TYR   A CZ  
450  O OH  . TYR   A 71  ? 0.9242 0.8855 0.8272 -0.0460 -0.1606 -0.0461 764  TYR   A OH  
451  N N   . VAL   A 72  ? 0.6264 0.7551 0.7629 -0.0513 -0.1288 -0.0235 765  VAL   A N   
452  C CA  . VAL   A 72  ? 0.6146 0.7517 0.7480 -0.0357 -0.1359 -0.0163 765  VAL   A CA  
453  C C   . VAL   A 72  ? 0.6132 0.7391 0.7430 -0.0310 -0.1182 -0.0039 765  VAL   A C   
454  O O   . VAL   A 72  ? 0.6301 0.7394 0.7355 -0.0215 -0.1186 0.0020  765  VAL   A O   
455  C CB  . VAL   A 72  ? 0.5907 0.7670 0.7615 -0.0320 -0.1473 -0.0215 765  VAL   A CB  
456  C CG1 . VAL   A 72  ? 0.5899 0.7718 0.7573 -0.0148 -0.1513 -0.0130 765  VAL   A CG1 
457  C CG2 . VAL   A 72  ? 0.5860 0.7770 0.7613 -0.0341 -0.1698 -0.0361 765  VAL   A CG2 
458  N N   . MET   A 73  ? 0.5950 0.7262 0.7458 -0.0377 -0.1026 -0.0008 766  MET   A N   
459  C CA  . MET   A 73  ? 0.5949 0.7167 0.7424 -0.0323 -0.0888 0.0089  766  MET   A CA  
460  C C   . MET   A 73  ? 0.6003 0.6943 0.7202 -0.0319 -0.0828 0.0106  766  MET   A C   
461  O O   . MET   A 73  ? 0.6084 0.6960 0.7211 -0.0249 -0.0780 0.0160  766  MET   A O   
462  C CB  . MET   A 73  ? 0.6040 0.7293 0.7704 -0.0381 -0.0744 0.0113  766  MET   A CB  
463  C CG  . MET   A 73  ? 0.6340 0.7839 0.8285 -0.0397 -0.0734 0.0104  766  MET   A CG  
464  S SD  . MET   A 73  ? 0.7759 0.9156 0.9791 -0.0463 -0.0525 0.0147  766  MET   A SD  
465  C CE  . MET   A 73  ? 0.7527 0.9118 0.9856 -0.0618 -0.0508 0.0041  766  MET   A CE  
466  N N   . ALA   A 74  ? 0.5944 0.6719 0.7003 -0.0401 -0.0818 0.0045  767  ALA   A N   
467  C CA  . ALA   A 74  ? 0.6009 0.6514 0.6816 -0.0407 -0.0732 0.0045  767  ALA   A CA  
468  C C   . ALA   A 74  ? 0.6130 0.6475 0.6636 -0.0351 -0.0799 0.0045  767  ALA   A C   
469  O O   . ALA   A 74  ? 0.6329 0.6480 0.6670 -0.0337 -0.0690 0.0065  767  ALA   A O   
470  C CB  . ALA   A 74  ? 0.6055 0.6407 0.6785 -0.0508 -0.0685 -0.0023 767  ALA   A CB  
471  N N   . SER   A 75  ? 0.6009 0.6421 0.6437 -0.0314 -0.0971 0.0016  768  SER   A N   
472  C CA  . SER   A 75  ? 0.6168 0.6370 0.6235 -0.0234 -0.1052 0.0024  768  SER   A CA  
473  C C   . SER   A 75  ? 0.6113 0.6275 0.6147 -0.0147 -0.0986 0.0106  768  SER   A C   
474  O O   . SER   A 75  ? 0.6348 0.6226 0.6043 -0.0108 -0.0950 0.0127  768  SER   A O   
475  C CB  . SER   A 75  ? 0.6350 0.6675 0.6380 -0.0179 -0.1285 -0.0032 768  SER   A CB  
476  O OG  . SER   A 75  ? 0.6513 0.7153 0.6853 -0.0109 -0.1362 -0.0007 768  SER   A OG  
477  N N   . VAL   A 76  ? 0.5852 0.6261 0.6209 -0.0126 -0.0954 0.0147  769  VAL   A N   
478  C CA  . VAL   A 76  ? 0.5872 0.6275 0.6249 -0.0059 -0.0894 0.0207  769  VAL   A CA  
479  C C   . VAL   A 76  ? 0.6096 0.6270 0.6343 -0.0104 -0.0720 0.0213  769  VAL   A C   
480  O O   . VAL   A 76  ? 0.6275 0.6312 0.6391 -0.0067 -0.0669 0.0239  769  VAL   A O   
481  C CB  . VAL   A 76  ? 0.5708 0.6411 0.6448 -0.0043 -0.0888 0.0232  769  VAL   A CB  
482  C CG1 . VAL   A 76  ? 0.5777 0.6472 0.6545 0.0014  -0.0822 0.0278  769  VAL   A CG1 
483  C CG2 . VAL   A 76  ? 0.5588 0.6524 0.6484 -0.0002 -0.1030 0.0213  769  VAL   A CG2 
484  N N   . ASP   A 77  ? 0.6038 0.6154 0.6317 -0.0186 -0.0621 0.0176  770  ASP   A N   
485  C CA  . ASP   A 77  ? 0.6099 0.6027 0.6299 -0.0231 -0.0446 0.0157  770  ASP   A CA  
486  C C   . ASP   A 77  ? 0.6305 0.5872 0.6080 -0.0236 -0.0394 0.0151  770  ASP   A C   
487  O O   . ASP   A 77  ? 0.6414 0.5807 0.6119 -0.0284 -0.0219 0.0129  770  ASP   A O   
488  C CB  . ASP   A 77  ? 0.6343 0.6265 0.6639 -0.0295 -0.0359 0.0113  770  ASP   A CB  
489  C CG  . ASP   A 77  ? 0.6851 0.7024 0.7489 -0.0282 -0.0363 0.0124  770  ASP   A CG  
490  N N   . ASN   A 78  ? 0.6378 0.5822 0.5864 -0.0183 -0.0539 0.0163  771  ASN   A N   
491  C CA  . ASN   A 78  ? 0.6713 0.5746 0.5701 -0.0160 -0.0503 0.0169  771  ASN   A CA  
492  C C   . ASN   A 78  ? 0.6704 0.5658 0.5488 -0.0038 -0.0631 0.0223  771  ASN   A C   
493  O O   . ASN   A 78  ? 0.6622 0.5754 0.5453 0.0044  -0.0843 0.0223  771  ASN   A O   
494  C CB  . ASN   A 78  ? 0.7039 0.5905 0.5751 -0.0184 -0.0571 0.0119  771  ASN   A CB  
495  C CG  . ASN   A 78  ? 0.7875 0.6266 0.5982 -0.0141 -0.0555 0.0126  771  ASN   A CG  
496  O OD1 . ASN   A 78  ? 0.8262 0.6367 0.6128 -0.0132 -0.0402 0.0164  771  ASN   A OD1 
497  N ND2 . ASN   A 78  ? 0.8148 0.6419 0.5970 -0.0115 -0.0710 0.0083  771  ASN   A ND2 
498  N N   . PRO   A 79  ? 0.6800 0.5483 0.5366 -0.0023 -0.0499 0.0259  772  PRO   A N   
499  C CA  . PRO   A 79  ? 0.6793 0.5276 0.5339 -0.0131 -0.0229 0.0238  772  PRO   A CA  
500  C C   . PRO   A 79  ? 0.6419 0.5255 0.5499 -0.0197 -0.0142 0.0210  772  PRO   A C   
501  O O   . PRO   A 79  ? 0.6493 0.5277 0.5685 -0.0294 0.0060  0.0161  772  PRO   A O   
502  C CB  . PRO   A 79  ? 0.7151 0.5199 0.5238 -0.0078 -0.0155 0.0285  772  PRO   A CB  
503  C CG  . PRO   A 79  ? 0.7156 0.5365 0.5284 0.0065  -0.0376 0.0337  772  PRO   A CG  
504  C CD  . PRO   A 79  ? 0.6821 0.5357 0.5136 0.0112  -0.0607 0.0316  772  PRO   A CD  
505  N N   . GLY   A 80  ? 0.6018 0.5207 0.5420 -0.0138 -0.0292 0.0232  773  GLY   A N   
506  C CA  . GLY   A 80  ? 0.5692 0.5199 0.5541 -0.0170 -0.0251 0.0209  773  GLY   A CA  
507  C C   . GLY   A 80  ? 0.5629 0.5138 0.5547 -0.0154 -0.0208 0.0215  773  GLY   A C   
508  O O   . GLY   A 80  ? 0.5898 0.5097 0.5507 -0.0145 -0.0146 0.0234  773  GLY   A O   
509  N N   . ASN   A 81  ? 0.5297 0.5119 0.5587 -0.0148 -0.0240 0.0196  774  ASN   A N   
510  C CA  . ASN   A 81  ? 0.5195 0.5064 0.5599 -0.0139 -0.0216 0.0180  774  ASN   A CA  
511  C C   . ASN   A 81  ? 0.4996 0.5161 0.5792 -0.0169 -0.0201 0.0116  774  ASN   A C   
512  O O   . ASN   A 81  ? 0.4970 0.5348 0.5933 -0.0130 -0.0283 0.0134  774  ASN   A O   
513  C CB  . ASN   A 81  ? 0.5190 0.5141 0.5554 -0.0025 -0.0363 0.0243  774  ASN   A CB  
514  C CG  . ASN   A 81  ? 0.5233 0.5131 0.5601 -0.0009 -0.0333 0.0230  774  ASN   A CG  
515  O OD1 . ASN   A 81  ? 0.5672 0.5265 0.5754 0.0001  -0.0277 0.0246  774  ASN   A OD1 
516  N ND2 . ASN   A 81  ? 0.4737 0.4889 0.5384 0.0002  -0.0369 0.0198  774  ASN   A ND2 
517  N N   . PRO   A 82  ? 0.4765 0.4942 0.5708 -0.0230 -0.0106 0.0037  775  PRO   A N   
518  C CA  . PRO   A 82  ? 0.4479 0.4956 0.5794 -0.0230 -0.0130 -0.0039 775  PRO   A CA  
519  C C   . PRO   A 82  ? 0.4366 0.5066 0.5795 -0.0122 -0.0290 0.0000  775  PRO   A C   
520  O O   . PRO   A 82  ? 0.4231 0.5144 0.5890 -0.0084 -0.0339 -0.0039 775  PRO   A O   
521  C CB  . PRO   A 82  ? 0.4522 0.4968 0.5974 -0.0328 -0.0009 -0.0156 775  PRO   A CB  
522  C CG  . PRO   A 82  ? 0.4743 0.4835 0.5852 -0.0369 0.0079  -0.0118 775  PRO   A CG  
523  C CD  . PRO   A 82  ? 0.4755 0.4652 0.5524 -0.0307 0.0035  -0.0001 775  PRO   A CD  
524  N N   . HIS   A 83  ? 0.4435 0.5068 0.5687 -0.0059 -0.0363 0.0075  776  HIS   A N   
525  C CA  . HIS   A 83  ? 0.4376 0.5179 0.5702 0.0038  -0.0477 0.0111  776  HIS   A CA  
526  C C   . HIS   A 83  ? 0.4473 0.5340 0.5753 0.0099  -0.0544 0.0200  776  HIS   A C   
527  O O   . HIS   A 83  ? 0.4447 0.5397 0.5729 0.0174  -0.0605 0.0242  776  HIS   A O   
528  C CB  . HIS   A 83  ? 0.4460 0.5177 0.5684 0.0066  -0.0491 0.0104  776  HIS   A CB  
529  C CG  . HIS   A 83  ? 0.4530 0.5190 0.5835 -0.0023 -0.0412 -0.0007 776  HIS   A CG  
530  N ND1 . HIS   A 83  ? 0.4890 0.5280 0.6016 -0.0098 -0.0301 -0.0025 776  HIS   A ND1 
531  C CD2 . HIS   A 83  ? 0.4424 0.5262 0.5985 -0.0056 -0.0421 -0.0115 776  HIS   A CD2 
532  C CE1 . HIS   A 83  ? 0.4821 0.5243 0.6127 -0.0197 -0.0226 -0.0151 776  HIS   A CE1 
533  N NE2 . HIS   A 83  ? 0.4619 0.5338 0.6215 -0.0172 -0.0309 -0.0217 776  HIS   A NE2 
534  N N   . VAL   A 84  ? 0.4622 0.5458 0.5882 0.0058  -0.0520 0.0213  777  VAL   A N   
535  C CA  . VAL   A 84  ? 0.4861 0.5761 0.6115 0.0082  -0.0571 0.0269  777  VAL   A CA  
536  C C   . VAL   A 84  ? 0.5131 0.6061 0.6484 0.0042  -0.0529 0.0246  777  VAL   A C   
537  O O   . VAL   A 84  ? 0.5274 0.6110 0.6609 -0.0016 -0.0457 0.0199  777  VAL   A O   
538  C CB  . VAL   A 84  ? 0.5043 0.5816 0.6103 0.0075  -0.0603 0.0296  777  VAL   A CB  
539  C CG1 . VAL   A 84  ? 0.5164 0.6004 0.6252 0.0056  -0.0646 0.0310  777  VAL   A CG1 
540  C CG2 . VAL   A 84  ? 0.5056 0.5825 0.6039 0.0156  -0.0662 0.0329  777  VAL   A CG2 
541  N N   . CYS   A 85  ? 0.5174 0.6204 0.6617 0.0078  -0.0552 0.0277  778  CYS   A N   
542  C CA  . CYS   A 85  ? 0.5291 0.6306 0.6794 0.0061  -0.0508 0.0263  778  CYS   A CA  
543  C C   . CYS   A 85  ? 0.5389 0.6292 0.6798 -0.0020 -0.0478 0.0253  778  CYS   A C   
544  O O   . CYS   A 85  ? 0.5477 0.6341 0.6776 -0.0048 -0.0519 0.0264  778  CYS   A O   
545  C CB  . CYS   A 85  ? 0.5483 0.6550 0.7031 0.0123  -0.0520 0.0309  778  CYS   A CB  
546  S SG  . CYS   A 85  ? 0.6253 0.7395 0.7851 0.0242  -0.0564 0.0301  778  CYS   A SG  
547  N N   . ARG   A 86  ? 0.5368 0.6207 0.6806 -0.0042 -0.0414 0.0223  779  ARG   A N   
548  C CA  . ARG   A 86  ? 0.5471 0.6169 0.6794 -0.0118 -0.0372 0.0198  779  ARG   A CA  
549  C C   . ARG   A 86  ? 0.5446 0.6114 0.6799 -0.0129 -0.0351 0.0211  779  ARG   A C   
550  O O   . ARG   A 86  ? 0.5516 0.6173 0.6948 -0.0076 -0.0302 0.0208  779  ARG   A O   
551  C CB  . ARG   A 86  ? 0.5748 0.6345 0.7058 -0.0146 -0.0271 0.0137  779  ARG   A CB  
552  C CG  . ARG   A 86  ? 0.6520 0.7040 0.7719 -0.0178 -0.0247 0.0117  779  ARG   A CG  
553  C CD  . ARG   A 86  ? 0.7093 0.7663 0.8455 -0.0177 -0.0156 0.0054  779  ARG   A CD  
554  N NE  . ARG   A 86  ? 0.7695 0.8145 0.9050 -0.0231 -0.0014 -0.0011 779  ARG   A NE  
555  C CZ  . ARG   A 86  ? 0.8013 0.8415 0.9423 -0.0283 0.0118  -0.0083 779  ARG   A CZ  
556  N NH1 . ARG   A 86  ? 0.7739 0.8186 0.9202 -0.0300 0.0118  -0.0101 779  ARG   A NH1 
557  N NH2 . ARG   A 86  ? 0.8207 0.8500 0.9621 -0.0330 0.0270  -0.0146 779  ARG   A NH2 
558  N N   . LEU   A 87  ? 0.5348 0.5993 0.6640 -0.0194 -0.0388 0.0215  780  LEU   A N   
559  C CA  . LEU   A 87  ? 0.5323 0.5893 0.6628 -0.0237 -0.0341 0.0211  780  LEU   A CA  
560  C C   . LEU   A 87  ? 0.5466 0.5848 0.6665 -0.0276 -0.0265 0.0159  780  LEU   A C   
561  O O   . LEU   A 87  ? 0.5622 0.5912 0.6677 -0.0340 -0.0283 0.0114  780  LEU   A O   
562  C CB  . LEU   A 87  ? 0.5214 0.5844 0.6534 -0.0322 -0.0401 0.0195  780  LEU   A CB  
563  C CG  . LEU   A 87  ? 0.5271 0.5812 0.6628 -0.0393 -0.0327 0.0183  780  LEU   A CG  
564  C CD1 . LEU   A 87  ? 0.5222 0.5769 0.6651 -0.0325 -0.0256 0.0252  780  LEU   A CD1 
565  C CD2 . LEU   A 87  ? 0.5257 0.5883 0.6675 -0.0509 -0.0390 0.0122  780  LEU   A CD2 
566  N N   . LEU   A 88  ? 0.5405 0.5711 0.6651 -0.0220 -0.0182 0.0163  781  LEU   A N   
567  C CA  . LEU   A 88  ? 0.5575 0.5702 0.6745 -0.0236 -0.0087 0.0109  781  LEU   A CA  
568  C C   . LEU   A 88  ? 0.5813 0.5754 0.6860 -0.0332 -0.0051 0.0080  781  LEU   A C   
569  O O   . LEU   A 88  ? 0.5989 0.5756 0.6905 -0.0381 0.0010  0.0021  781  LEU   A O   
570  C CB  . LEU   A 88  ? 0.5551 0.5682 0.6841 -0.0110 -0.0026 0.0115  781  LEU   A CB  
571  C CG  . LEU   A 88  ? 0.5659 0.5984 0.7113 -0.0020 -0.0060 0.0106  781  LEU   A CG  
572  C CD1 . LEU   A 88  ? 0.5721 0.6065 0.7310 0.0116  -0.0025 0.0085  781  LEU   A CD1 
573  C CD2 . LEU   A 88  ? 0.5768 0.6103 0.7203 -0.0091 -0.0022 0.0048  781  LEU   A CD2 
574  N N   . GLY   A 89  ? 0.5789 0.5747 0.6878 -0.0364 -0.0068 0.0113  782  GLY   A N   
575  C CA  . GLY   A 89  ? 0.5925 0.5709 0.6933 -0.0478 -0.0022 0.0069  782  GLY   A CA  
576  C C   . GLY   A 89  ? 0.5933 0.5746 0.7027 -0.0524 -0.0004 0.0103  782  GLY   A C   
577  O O   . GLY   A 89  ? 0.5824 0.5762 0.7009 -0.0445 -0.0015 0.0175  782  GLY   A O   
578  N N   . ILE   A 90  ? 0.6067 0.5747 0.7124 -0.0663 0.0038  0.0041  783  ILE   A N   
579  C CA  . ILE   A 90  ? 0.6197 0.5873 0.7352 -0.0748 0.0101  0.0051  783  ILE   A CA  
580  C C   . ILE   A 90  ? 0.6394 0.5736 0.7428 -0.0832 0.0245  0.0015  783  ILE   A C   
581  O O   . ILE   A 90  ? 0.6411 0.5602 0.7329 -0.0901 0.0246  -0.0068 783  ILE   A O   
582  C CB  . ILE   A 90  ? 0.6185 0.6140 0.7520 -0.0871 -0.0014 -0.0017 783  ILE   A CB  
583  C CG1 . ILE   A 90  ? 0.6240 0.6226 0.7740 -0.0974 0.0088  -0.0019 783  ILE   A CG1 
584  C CG2 . ILE   A 90  ? 0.6288 0.6228 0.7557 -0.0987 -0.0112 -0.0143 783  ILE   A CG2 
585  C CD1 . ILE   A 90  ? 0.6216 0.6544 0.7976 -0.1064 -0.0018 -0.0090 783  ILE   A CD1 
586  N N   . CYS   A 91  ? 0.6600 0.5773 0.7611 -0.0814 0.0382  0.0082  784  CYS   A N   
587  C CA  . CYS   A 91  ? 0.7011 0.5808 0.7878 -0.0895 0.0547  0.0057  784  CYS   A CA  
588  C C   . CYS   A 91  ? 0.7156 0.5955 0.8150 -0.1074 0.0645  0.0026  784  CYS   A C   
589  O O   . CYS   A 91  ? 0.7133 0.5952 0.8157 -0.1020 0.0716  0.0114  784  CYS   A O   
590  C CB  . CYS   A 91  ? 0.7350 0.5840 0.8010 -0.0697 0.0655  0.0164  784  CYS   A CB  
591  S SG  . CYS   A 91  ? 0.8404 0.6336 0.8813 -0.0765 0.0872  0.0141  784  CYS   A SG  
592  N N   . LEU   A 92  ? 0.7291 0.6079 0.8367 -0.1292 0.0651  -0.0114 785  LEU   A N   
593  C CA  . LEU   A 92  ? 0.7404 0.6235 0.8677 -0.1497 0.0758  -0.0181 785  LEU   A CA  
594  C C   . LEU   A 92  ? 0.7702 0.6066 0.8813 -0.1626 0.0992  -0.0209 785  LEU   A C   
595  O O   . LEU   A 92  ? 0.7795 0.5979 0.8824 -0.1745 0.0996  -0.0323 785  LEU   A O   
596  C CB  . LEU   A 92  ? 0.7283 0.6496 0.8846 -0.1675 0.0588  -0.0349 785  LEU   A CB  
597  C CG  . LEU   A 92  ? 0.7315 0.7006 0.9092 -0.1588 0.0377  -0.0339 785  LEU   A CG  
598  C CD1 . LEU   A 92  ? 0.7154 0.7192 0.9242 -0.1768 0.0234  -0.0519 785  LEU   A CD1 
599  C CD2 . LEU   A 92  ? 0.7363 0.7163 0.9234 -0.1485 0.0465  -0.0211 785  LEU   A CD2 
600  N N   . THR   A 93  ? 0.7841 0.5968 0.8867 -0.1602 0.1199  -0.0107 786  THR   A N   
601  C CA  . THR   A 93  ? 0.8146 0.5771 0.8993 -0.1734 0.1469  -0.0120 786  THR   A CA  
602  C C   . THR   A 93  ? 0.7969 0.5739 0.9078 -0.1916 0.1619  -0.0149 786  THR   A C   
603  O O   . THR   A 93  ? 0.7680 0.5953 0.9185 -0.2044 0.1478  -0.0268 786  THR   A O   
604  C CB  . THR   A 93  ? 0.8710 0.5824 0.9116 -0.1484 0.1588  0.0045  786  THR   A CB  
605  O OG1 . THR   A 93  ? 0.8870 0.6037 0.9202 -0.1285 0.1595  0.0202  786  THR   A OG1 
606  C CG2 . THR   A 93  ? 0.8804 0.5891 0.9068 -0.1318 0.1436  0.0042  786  THR   A CG2 
607  N N   . SER   A 94  ? 0.8105 0.5448 0.8994 -0.1910 0.1902  -0.0044 787  SER   A N   
608  C CA  . SER   A 94  ? 0.7951 0.5411 0.9066 -0.2063 0.2083  -0.0058 787  SER   A CA  
609  C C   . SER   A 94  ? 0.7678 0.5594 0.8957 -0.1891 0.1921  0.0025  787  SER   A C   
610  O O   . SER   A 94  ? 0.7505 0.5734 0.9121 -0.2024 0.1982  -0.0036 787  SER   A O   
611  C CB  . SER   A 94  ? 0.8467 0.5272 0.9190 -0.2054 0.2435  0.0064  787  SER   A CB  
612  O OG  . SER   A 94  ? 0.9045 0.5314 0.9513 -0.2163 0.2606  0.0021  787  SER   A OG  
613  N N   . THR   A 95  ? 0.7634 0.5581 0.8688 -0.1598 0.1730  0.0154  788  THR   A N   
614  C CA  . THR   A 95  ? 0.7398 0.5728 0.8554 -0.1419 0.1562  0.0230  788  THR   A CA  
615  C C   . THR   A 95  ? 0.7014 0.5737 0.8315 -0.1331 0.1246  0.0179  788  THR   A C   
616  O O   . THR   A 95  ? 0.7077 0.5701 0.8302 -0.1351 0.1169  0.0119  788  THR   A O   
617  C CB  . THR   A 95  ? 0.7906 0.5870 0.8627 -0.1147 0.1635  0.0425  788  THR   A CB  
618  O OG1 . THR   A 95  ? 0.8224 0.5975 0.8680 -0.0960 0.1521  0.0474  788  THR   A OG1 
619  C CG2 . THR   A 95  ? 0.8212 0.5668 0.8660 -0.1202 0.1966  0.0499  788  THR   A CG2 
620  N N   . VAL   A 96  ? 0.6633 0.5756 0.8101 -0.1226 0.1084  0.0206  789  VAL   A N   
621  C CA  . VAL   A 96  ? 0.6366 0.5797 0.7908 -0.1121 0.0816  0.0181  789  VAL   A CA  
622  C C   . VAL   A 96  ? 0.6317 0.5592 0.7576 -0.0861 0.0764  0.0317  789  VAL   A C   
623  O O   . VAL   A 96  ? 0.6385 0.5582 0.7525 -0.0738 0.0832  0.0421  789  VAL   A O   
624  C CB  . VAL   A 96  ? 0.6152 0.6079 0.8025 -0.1146 0.0674  0.0129  789  VAL   A CB  
625  C CG1 . VAL   A 96  ? 0.6069 0.6234 0.7949 -0.1032 0.0421  0.0114  789  VAL   A CG1 
626  C CG2 . VAL   A 96  ? 0.6052 0.6191 0.8272 -0.1393 0.0715  -0.0027 789  VAL   A CG2 
627  N N   . GLN   A 97  ? 0.6176 0.5401 0.7329 -0.0776 0.0651  0.0305  790  GLN   A N   
628  C CA  . GLN   A 97  ? 0.6090 0.5249 0.7064 -0.0537 0.0578  0.0399  790  GLN   A CA  
629  C C   . GLN   A 97  ? 0.5757 0.5249 0.6871 -0.0494 0.0378  0.0353  790  GLN   A C   
630  O O   . GLN   A 97  ? 0.5663 0.5206 0.6831 -0.0593 0.0320  0.0263  790  GLN   A O   
631  C CB  . GLN   A 97  ? 0.6423 0.5179 0.7139 -0.0446 0.0670  0.0430  790  GLN   A CB  
632  C CG  . GLN   A 97  ? 0.7093 0.5456 0.7560 -0.0393 0.0860  0.0525  790  GLN   A CG  
633  C CD  . GLN   A 97  ? 0.7939 0.5870 0.8120 -0.0264 0.0941  0.0564  790  GLN   A CD  
634  O OE1 . GLN   A 97  ? 0.8327 0.6124 0.8314 -0.0018 0.0900  0.0651  790  GLN   A OE1 
635  N NE2 . GLN   A 97  ? 0.8011 0.5714 0.8156 -0.0413 0.1047  0.0492  790  GLN   A NE2 
636  N N   . LEU   A 98  ? 0.5553 0.5248 0.6706 -0.0360 0.0280  0.0407  791  LEU   A N   
637  C CA  . LEU   A 98  ? 0.5337 0.5302 0.6597 -0.0322 0.0118  0.0370  791  LEU   A CA  
638  C C   . LEU   A 98  ? 0.5385 0.5292 0.6552 -0.0144 0.0076  0.0404  791  LEU   A C   
639  O O   . LEU   A 98  ? 0.5450 0.5259 0.6517 -0.0003 0.0099  0.0474  791  LEU   A O   
640  C CB  . LEU   A 98  ? 0.5134 0.5379 0.6533 -0.0317 0.0043  0.0386  791  LEU   A CB  
641  C CG  . LEU   A 98  ? 0.5154 0.5528 0.6723 -0.0474 0.0080  0.0337  791  LEU   A CG  
642  C CD1 . LEU   A 98  ? 0.5075 0.5709 0.6778 -0.0429 0.0024  0.0359  791  LEU   A CD1 
643  C CD2 . LEU   A 98  ? 0.5146 0.5604 0.6806 -0.0613 0.0003  0.0227  791  LEU   A CD2 
644  N N   . ILE   A 99  ? 0.5315 0.5278 0.6512 -0.0144 0.0018  0.0346  792  ILE   A N   
645  C CA  . ILE   A 99  ? 0.5359 0.5313 0.6548 0.0007  -0.0006 0.0347  792  ILE   A CA  
646  C C   . ILE   A 99  ? 0.5355 0.5555 0.6663 0.0026  -0.0107 0.0313  792  ILE   A C   
647  O O   . ILE   A 99  ? 0.5351 0.5631 0.6677 -0.0084 -0.0140 0.0274  792  ILE   A O   
648  C CB  . ILE   A 99  ? 0.5501 0.5233 0.6614 -0.0001 0.0078  0.0302  792  ILE   A CB  
649  C CG1 . ILE   A 99  ? 0.5702 0.5120 0.6656 0.0015  0.0194  0.0347  792  ILE   A CG1 
650  C CG2 . ILE   A 99  ? 0.5533 0.5324 0.6721 0.0137  0.0058  0.0268  792  ILE   A CG2 
651  C CD1 . ILE   A 99  ? 0.5868 0.5136 0.6770 -0.0187 0.0276  0.0301  792  ILE   A CD1 
652  N N   . THR   A 100 ? 0.5372 0.5678 0.6742 0.0166  -0.0160 0.0325  793  THR   A N   
653  C CA  . THR   A 100 ? 0.5438 0.5951 0.6932 0.0182  -0.0232 0.0281  793  THR   A CA  
654  C C   . THR   A 100 ? 0.5394 0.5969 0.7001 0.0324  -0.0253 0.0239  793  THR   A C   
655  O O   . THR   A 100 ? 0.5394 0.5861 0.6952 0.0445  -0.0245 0.0265  793  THR   A O   
656  C CB  . THR   A 100 ? 0.5716 0.6378 0.7226 0.0194  -0.0311 0.0318  793  THR   A CB  
657  O OG1 . THR   A 100 ? 0.6021 0.6637 0.7461 0.0308  -0.0326 0.0380  793  THR   A OG1 
658  C CG2 . THR   A 100 ? 0.5840 0.6534 0.7322 0.0076  -0.0318 0.0329  793  THR   A CG2 
659  N N   . GLN   A 101 ? 0.5383 0.6130 0.7145 0.0315  -0.0281 0.0168  794  GLN   A N   
660  C CA  . GLN   A 101 ? 0.5422 0.6313 0.7379 0.0436  -0.0318 0.0097  794  GLN   A CA  
661  C C   . GLN   A 101 ? 0.5531 0.6489 0.7457 0.0579  -0.0441 0.0136  794  GLN   A C   
662  O O   . GLN   A 101 ? 0.5623 0.6593 0.7447 0.0542  -0.0482 0.0190  794  GLN   A O   
663  C CB  . GLN   A 101 ? 0.5489 0.6538 0.7621 0.0348  -0.0294 0.0004  794  GLN   A CB  
664  N N   . LEU   A 102 ? 0.5547 0.6524 0.7528 0.0753  -0.0499 0.0112  795  LEU   A N   
665  C CA  . LEU   A 102 ? 0.5758 0.6749 0.7640 0.0916  -0.0629 0.0146  795  LEU   A CA  
666  C C   . LEU   A 102 ? 0.5859 0.7107 0.7909 0.0909  -0.0740 0.0063  795  LEU   A C   
667  O O   . LEU   A 102 ? 0.5751 0.7215 0.8093 0.0888  -0.0754 -0.0062 795  LEU   A O   
668  C CB  . LEU   A 102 ? 0.5821 0.6753 0.7703 0.1131  -0.0682 0.0127  795  LEU   A CB  
669  C CG  . LEU   A 102 ? 0.6034 0.6932 0.7756 0.1353  -0.0839 0.0153  795  LEU   A CG  
670  C CD1 . LEU   A 102 ? 0.6309 0.6920 0.7643 0.1345  -0.0794 0.0297  795  LEU   A CD1 
671  C CD2 . LEU   A 102 ? 0.6123 0.6955 0.7850 0.1581  -0.0897 0.0128  795  LEU   A CD2 
672  N N   . MET   A 103 ? 0.6063 0.7275 0.7935 0.0911  -0.0795 0.0123  796  MET   A N   
673  C CA  . MET   A 103 ? 0.6101 0.7497 0.8064 0.0914  -0.0903 0.0051  796  MET   A CA  
674  C C   . MET   A 103 ? 0.6190 0.7586 0.8057 0.1140  -0.1062 0.0034  796  MET   A C   
675  O O   . MET   A 103 ? 0.6372 0.7546 0.7917 0.1243  -0.1074 0.0142  796  MET   A O   
676  C CB  . MET   A 103 ? 0.6298 0.7620 0.8090 0.0810  -0.0865 0.0126  796  MET   A CB  
677  C CG  . MET   A 103 ? 0.6580 0.7878 0.8419 0.0624  -0.0740 0.0146  796  MET   A CG  
678  S SD  . MET   A 103 ? 0.7365 0.8831 0.9463 0.0497  -0.0713 0.0014  796  MET   A SD  
679  C CE  . MET   A 103 ? 0.7112 0.8530 0.9315 0.0437  -0.0594 -0.0012 796  MET   A CE  
680  N N   . PRO   A 104 ? 0.6052 0.7682 0.8196 0.1229  -0.1177 -0.0108 797  PRO   A N   
681  C CA  . PRO   A 104 ? 0.6025 0.7655 0.8073 0.1485  -0.1362 -0.0137 797  PRO   A CA  
682  C C   . PRO   A 104 ? 0.5960 0.7536 0.7751 0.1582  -0.1506 -0.0126 797  PRO   A C   
683  O O   . PRO   A 104 ? 0.6060 0.7489 0.7585 0.1810  -0.1634 -0.0092 797  PRO   A O   
684  C CB  . PRO   A 104 ? 0.5907 0.7885 0.8419 0.1528  -0.1452 -0.0328 797  PRO   A CB  
685  C CG  . PRO   A 104 ? 0.5887 0.7952 0.8670 0.1300  -0.1255 -0.0364 797  PRO   A CG  
686  C CD  . PRO   A 104 ? 0.5821 0.7716 0.8381 0.1109  -0.1136 -0.0257 797  PRO   A CD  
687  N N   . PHE   A 105 ? 0.5778 0.7431 0.7603 0.1428  -0.1483 -0.0153 798  PHE   A N   
688  C CA  . PHE   A 105 ? 0.5810 0.7393 0.7375 0.1513  -0.1605 -0.0153 798  PHE   A CA  
689  C C   . PHE   A 105 ? 0.5861 0.7127 0.7010 0.1492  -0.1482 0.0022  798  PHE   A C   
690  O O   . PHE   A 105 ? 0.6020 0.7197 0.6929 0.1545  -0.1545 0.0029  798  PHE   A O   
691  C CB  . PHE   A 105 ? 0.5698 0.7530 0.7524 0.1390  -0.1670 -0.0308 798  PHE   A CB  
692  C CG  . PHE   A 105 ? 0.5564 0.7740 0.7839 0.1407  -0.1793 -0.0514 798  PHE   A CG  
693  C CD1 . PHE   A 105 ? 0.5694 0.8011 0.7997 0.1600  -0.2040 -0.0642 798  PHE   A CD1 
694  C CD2 . PHE   A 105 ? 0.5467 0.7827 0.8137 0.1229  -0.1659 -0.0593 798  PHE   A CD2 
695  C CE1 . PHE   A 105 ? 0.5528 0.8223 0.8326 0.1611  -0.2157 -0.0859 798  PHE   A CE1 
696  C CE2 . PHE   A 105 ? 0.5323 0.8024 0.8461 0.1226  -0.1739 -0.0800 798  PHE   A CE2 
697  C CZ  . PHE   A 105 ? 0.5263 0.8159 0.8501 0.1413  -0.1991 -0.0940 798  PHE   A CZ  
698  N N   . GLY   A 106 ? 0.5741 0.6839 0.6812 0.1417  -0.1306 0.0148  799  GLY   A N   
699  C CA  . GLY   A 106 ? 0.5866 0.6703 0.6619 0.1380  -0.1168 0.0293  799  GLY   A CA  
700  C C   . GLY   A 106 ? 0.5778 0.6699 0.6600 0.1216  -0.1096 0.0293  799  GLY   A C   
701  O O   . GLY   A 106 ? 0.5631 0.6759 0.6738 0.1087  -0.1101 0.0210  799  GLY   A O   
702  N N   . CYS   A 107 ? 0.5826 0.6565 0.6375 0.1227  -0.1015 0.0386  800  CYS   A N   
703  C CA  . CYS   A 107 ? 0.5708 0.6514 0.6310 0.1105  -0.0945 0.0390  800  CYS   A CA  
704  C C   . CYS   A 107 ? 0.5628 0.6483 0.6157 0.1163  -0.1066 0.0307  800  CYS   A C   
705  O O   . CYS   A 107 ? 0.5729 0.6504 0.6058 0.1319  -0.1191 0.0272  800  CYS   A O   
706  C CB  . CYS   A 107 ? 0.5874 0.6504 0.6297 0.1070  -0.0773 0.0511  800  CYS   A CB  
707  S SG  . CYS   A 107 ? 0.6602 0.6902 0.6544 0.1252  -0.0743 0.0591  800  CYS   A SG  
708  N N   . LEU   A 108 ? 0.5436 0.6396 0.6098 0.1047  -0.1032 0.0271  801  LEU   A N   
709  C CA  . LEU   A 108 ? 0.5490 0.6478 0.6102 0.1066  -0.1119 0.0182  801  LEU   A CA  
710  C C   . LEU   A 108 ? 0.5762 0.6542 0.5998 0.1197  -0.1120 0.0227  801  LEU   A C   
711  O O   . LEU   A 108 ? 0.5802 0.6562 0.5909 0.1280  -0.1255 0.0135  801  LEU   A O   
712  C CB  . LEU   A 108 ? 0.5380 0.6448 0.6161 0.0921  -0.1044 0.0161  801  LEU   A CB  
713  C CG  . LEU   A 108 ? 0.5420 0.6527 0.6237 0.0890  -0.1121 0.0037  801  LEU   A CG  
714  C CD1 . LEU   A 108 ? 0.5287 0.6543 0.6291 0.0893  -0.1264 -0.0112 801  LEU   A CD1 
715  C CD2 . LEU   A 108 ? 0.5386 0.6504 0.6327 0.0759  -0.1025 0.0039  801  LEU   A CD2 
716  N N   . LEU   A 109 ? 0.5925 0.6541 0.5980 0.1215  -0.0967 0.0357  802  LEU   A N   
717  C CA  . LEU   A 109 ? 0.6280 0.6648 0.5940 0.1336  -0.0915 0.0413  802  LEU   A CA  
718  C C   . LEU   A 109 ? 0.6609 0.6806 0.5953 0.1519  -0.1060 0.0392  802  LEU   A C   
719  O O   . LEU   A 109 ? 0.6830 0.6909 0.5897 0.1627  -0.1155 0.0340  802  LEU   A O   
720  C CB  . LEU   A 109 ? 0.6350 0.6587 0.5935 0.1295  -0.0688 0.0544  802  LEU   A CB  
721  C CG  . LEU   A 109 ? 0.6655 0.6598 0.5818 0.1403  -0.0571 0.0610  802  LEU   A CG  
722  C CD1 . LEU   A 109 ? 0.6701 0.6659 0.5798 0.1416  -0.0577 0.0554  802  LEU   A CD1 
723  C CD2 . LEU   A 109 ? 0.6758 0.6594 0.5918 0.1335  -0.0322 0.0720  802  LEU   A CD2 
724  N N   . ASP   A 110 ? 0.6626 0.6792 0.5988 0.1569  -0.1086 0.0428  803  ASP   A N   
725  C CA  . ASP   A 110 ? 0.6887 0.6886 0.5945 0.1777  -0.1247 0.0410  803  ASP   A CA  
726  C C   . ASP   A 110 ? 0.6765 0.7006 0.6005 0.1827  -0.1509 0.0233  803  ASP   A C   
727  O O   . ASP   A 110 ? 0.7026 0.7145 0.5959 0.2003  -0.1681 0.0176  803  ASP   A O   
728  C CB  . ASP   A 110 ? 0.7217 0.7126 0.6284 0.1823  -0.1209 0.0484  803  ASP   A CB  
729  C CG  . ASP   A 110 ? 0.8232 0.7860 0.7092 0.1773  -0.0945 0.0642  803  ASP   A CG  
730  O OD1 . ASP   A 110 ? 0.8538 0.8014 0.7196 0.1738  -0.0792 0.0701  803  ASP   A OD1 
731  O OD2 . ASP   A 110 ? 0.8553 0.8109 0.7468 0.1762  -0.0878 0.0698  803  ASP   A OD2 
732  N N   . TYR   A 111 ? 0.6412 0.6983 0.6138 0.1669  -0.1536 0.0136  804  TYR   A N   
733  C CA  . TYR   A 111 ? 0.6233 0.7076 0.6238 0.1662  -0.1741 -0.0054 804  TYR   A CA  
734  C C   . TYR   A 111 ? 0.6407 0.7208 0.6234 0.1680  -0.1833 -0.0149 804  TYR   A C   
735  O O   . TYR   A 111 ? 0.6423 0.7296 0.6212 0.1795  -0.2058 -0.0290 804  TYR   A O   
736  C CB  . TYR   A 111 ? 0.5935 0.7062 0.6449 0.1453  -0.1669 -0.0117 804  TYR   A CB  
737  C CG  . TYR   A 111 ? 0.5770 0.7192 0.6638 0.1427  -0.1842 -0.0325 804  TYR   A CG  
738  C CD1 . TYR   A 111 ? 0.5708 0.7308 0.6806 0.1516  -0.1964 -0.0405 804  TYR   A CD1 
739  C CD2 . TYR   A 111 ? 0.5803 0.7319 0.6785 0.1316  -0.1877 -0.0456 804  TYR   A CD2 
740  C CE1 . TYR   A 111 ? 0.5561 0.7478 0.7048 0.1486  -0.2115 -0.0622 804  TYR   A CE1 
741  C CE2 . TYR   A 111 ? 0.5688 0.7479 0.7023 0.1271  -0.2021 -0.0670 804  TYR   A CE2 
742  C CZ  . TYR   A 111 ? 0.5630 0.7646 0.7244 0.1351  -0.2139 -0.0759 804  TYR   A CZ  
743  O OH  . TYR   A 111 ? 0.5646 0.7982 0.7683 0.1291  -0.2269 -0.0995 804  TYR   A OH  
744  N N   . VAL   A 112 ? 0.6561 0.7253 0.6290 0.1576  -0.1671 -0.0087 805  VAL   A N   
745  C CA  . VAL   A 112 ? 0.6757 0.7369 0.6292 0.1590  -0.1734 -0.0178 805  VAL   A CA  
746  C C   . VAL   A 112 ? 0.7211 0.7522 0.6197 0.1802  -0.1813 -0.0145 805  VAL   A C   
747  O O   . VAL   A 112 ? 0.7365 0.7644 0.6182 0.1874  -0.1985 -0.0278 805  VAL   A O   
748  C CB  . VAL   A 112 ? 0.6810 0.7388 0.6402 0.1442  -0.1548 -0.0137 805  VAL   A CB  
749  C CG1 . VAL   A 112 ? 0.6666 0.7484 0.6718 0.1252  -0.1501 -0.0191 805  VAL   A CG1 
750  C CG2 . VAL   A 112 ? 0.6961 0.7345 0.6344 0.1460  -0.1329 0.0048  805  VAL   A CG2 
751  N N   . ARG   A 113 ? 0.7451 0.7514 0.6133 0.1903  -0.1690 0.0023  806  ARG   A N   
752  C CA  . ARG   A 113 ? 0.7868 0.7565 0.5946 0.2118  -0.1737 0.0072  806  ARG   A CA  
753  C C   . ARG   A 113 ? 0.8032 0.7771 0.6019 0.2307  -0.2040 -0.0040 806  ARG   A C   
754  O O   . ARG   A 113 ? 0.8263 0.7826 0.5849 0.2469  -0.2213 -0.0116 806  ARG   A O   
755  C CB  . ARG   A 113 ? 0.8108 0.7503 0.5904 0.2157  -0.1494 0.0277  806  ARG   A CB  
756  C CG  . ARG   A 113 ? 0.8326 0.7645 0.6134 0.2019  -0.1203 0.0376  806  ARG   A CG  
757  C CD  . ARG   A 113 ? 0.8715 0.7814 0.6384 0.2013  -0.0962 0.0546  806  ARG   A CD  
758  N NE  . ARG   A 113 ? 0.9023 0.8070 0.6723 0.1896  -0.0682 0.0624  806  ARG   A NE  
759  C CZ  . ARG   A 113 ? 0.9311 0.8259 0.7043 0.1820  -0.0430 0.0744  806  ARG   A CZ  
760  N NH1 . ARG   A 113 ? 0.9232 0.8070 0.6922 0.1843  -0.0411 0.0811  806  ARG   A NH1 
761  N NH2 . ARG   A 113 ? 0.9288 0.8248 0.7111 0.1720  -0.0191 0.0785  806  ARG   A NH2 
762  N N   . GLU   A 114 ? 0.7959 0.7934 0.6313 0.2298  -0.2115 -0.0062 807  GLU   A N   
763  C CA  . GLU   A 114 ? 0.8140 0.8202 0.6474 0.2500  -0.2410 -0.0176 807  GLU   A CA  
764  C C   . GLU   A 114 ? 0.7934 0.8377 0.6649 0.2454  -0.2666 -0.0431 807  GLU   A C   
765  O O   . GLU   A 114 ? 0.7916 0.8405 0.6516 0.2652  -0.2954 -0.0561 807  GLU   A O   
766  C CB  . GLU   A 114 ? 0.8521 0.8667 0.7090 0.2530  -0.2375 -0.0104 807  GLU   A CB  
767  C CG  . GLU   A 114 ? 0.9835 0.9510 0.7848 0.2708  -0.2257 0.0096  807  GLU   A CG  
768  C CD  . GLU   A 114 ? 1.0978 1.0503 0.9027 0.2542  -0.1915 0.0282  807  GLU   A CD  
769  O OE1 . GLU   A 114 ? 1.1128 1.0698 0.9378 0.2532  -0.1862 0.0333  807  GLU   A OE1 
770  O OE2 . GLU   A 114 ? 1.1342 1.0713 0.9234 0.2425  -0.1704 0.0365  807  GLU   A OE2 
771  N N   . HIS   A 115 ? 0.7772 0.8471 0.6926 0.2199  -0.2565 -0.0513 808  HIS   A N   
772  C CA  . HIS   A 115 ? 0.7619 0.8670 0.7180 0.2116  -0.2768 -0.0769 808  HIS   A CA  
773  C C   . HIS   A 115 ? 0.7825 0.8803 0.7267 0.2007  -0.2758 -0.0866 808  HIS   A C   
774  O O   . HIS   A 115 ? 0.7623 0.8877 0.7453 0.1871  -0.2855 -0.1073 808  HIS   A O   
775  C CB  . HIS   A 115 ? 0.7316 0.8742 0.7544 0.1914  -0.2683 -0.0833 808  HIS   A CB  
776  C CG  . HIS   A 115 ? 0.7437 0.8968 0.7822 0.2034  -0.2728 -0.0786 808  HIS   A CG  
777  N ND1 . HIS   A 115 ? 0.7641 0.9073 0.8060 0.1968  -0.2495 -0.0597 808  HIS   A ND1 
778  C CD2 . HIS   A 115 ? 0.7466 0.9158 0.7934 0.2238  -0.2988 -0.0904 808  HIS   A CD2 
779  C CE1 . HIS   A 115 ? 0.7656 0.9171 0.8173 0.2122  -0.2599 -0.0603 808  HIS   A CE1 
780  N NE2 . HIS   A 115 ? 0.7568 0.9246 0.8123 0.2298  -0.2898 -0.0782 808  HIS   A NE2 
781  N N   . LYS   A 116 ? 0.8192 0.8784 0.7093 0.2071  -0.2632 -0.0728 809  LYS   A N   
782  C CA  . LYS   A 116 ? 0.8433 0.8864 0.7114 0.2000  -0.2582 -0.0785 809  LYS   A CA  
783  C C   . LYS   A 116 ? 0.8436 0.9061 0.7294 0.1948  -0.2823 -0.1066 809  LYS   A C   
784  O O   . LYS   A 116 ? 0.8381 0.9095 0.7503 0.1742  -0.2723 -0.1151 809  LYS   A O   
785  C CB  . LYS   A 116 ? 0.9076 0.9047 0.7045 0.2186  -0.2517 -0.0647 809  LYS   A CB  
786  C CG  . LYS   A 116 ? 0.9786 0.9553 0.7513 0.2114  -0.2399 -0.0671 809  LYS   A CG  
787  C CD  . LYS   A 116 ? 1.0632 1.0137 0.7811 0.2289  -0.2601 -0.0789 809  LYS   A CD  
788  C CE  . LYS   A 116 ? 1.1109 1.0469 0.8152 0.2189  -0.2509 -0.0868 809  LYS   A CE  
789  N NZ  . LYS   A 116 ? 1.1447 1.0540 0.8263 0.2165  -0.2167 -0.0661 809  LYS   A NZ  
790  N N   . ASP   A 117 ? 0.8498 0.9168 0.7199 0.2136  -0.3141 -0.1220 810  ASP   A N   
791  C CA  . ASP   A 117 ? 0.8426 0.9292 0.7303 0.2081  -0.3386 -0.1514 810  ASP   A CA  
792  C C   . ASP   A 117 ? 0.7884 0.9254 0.7544 0.1884  -0.3454 -0.1721 810  ASP   A C   
793  O O   . ASP   A 117 ? 0.7788 0.9368 0.7682 0.1812  -0.3653 -0.1994 810  ASP   A O   
794  C CB  . ASP   A 117 ? 0.9014 0.9758 0.7433 0.2363  -0.3728 -0.1626 810  ASP   A CB  
795  C CG  . ASP   A 117 ? 1.0261 1.0513 0.7925 0.2475  -0.3702 -0.1575 810  ASP   A CG  
796  O OD1 . ASP   A 117 ? 1.0532 1.0503 0.7976 0.2387  -0.3381 -0.1384 810  ASP   A OD1 
797  O OD2 . ASP   A 117 ? 1.0736 1.0889 0.8034 0.2657  -0.4005 -0.1737 810  ASP   A OD2 
798  N N   . ASN   A 118 ? 0.7527 0.9081 0.7589 0.1788  -0.3282 -0.1606 811  ASN   A N   
799  C CA  . ASN   A 118 ? 0.7031 0.9023 0.7817 0.1592  -0.3286 -0.1784 811  ASN   A CA  
800  C C   . ASN   A 118 ? 0.6811 0.8791 0.7874 0.1322  -0.2953 -0.1686 811  ASN   A C   
801  O O   . ASN   A 118 ? 0.6642 0.8923 0.8260 0.1148  -0.2897 -0.1804 811  ASN   A O   
802  C CB  . ASN   A 118 ? 0.6982 0.9253 0.8055 0.1738  -0.3427 -0.1796 811  ASN   A CB  
803  C CG  . ASN   A 118 ? 0.7517 0.9865 0.8405 0.2008  -0.3808 -0.1953 811  ASN   A CG  
804  O OD1 . ASN   A 118 ? 0.7970 1.0177 0.8531 0.2272  -0.3913 -0.1823 811  ASN   A OD1 
805  N ND2 . ASN   A 118 ? 0.7376 0.9924 0.8440 0.1954  -0.4030 -0.2241 811  ASN   A ND2 
806  N N   . ILE   A 119 ? 0.6809 0.8438 0.7485 0.1297  -0.2730 -0.1477 812  ILE   A N   
807  C CA  . ILE   A 119 ? 0.6608 0.8184 0.7469 0.1082  -0.2442 -0.1377 812  ILE   A CA  
808  C C   . ILE   A 119 ? 0.6512 0.7952 0.7316 0.0932  -0.2388 -0.1502 812  ILE   A C   
809  O O   . ILE   A 119 ? 0.6663 0.7839 0.7027 0.1023  -0.2422 -0.1486 812  ILE   A O   
810  C CB  . ILE   A 119 ? 0.6782 0.8107 0.7330 0.1152  -0.2237 -0.1084 812  ILE   A CB  
811  C CG1 . ILE   A 119 ? 0.6822 0.8237 0.7403 0.1291  -0.2281 -0.0972 812  ILE   A CG1 
812  C CG2 . ILE   A 119 ? 0.6769 0.8043 0.7486 0.0957  -0.1980 -0.0994 812  ILE   A CG2 
813  C CD1 . ILE   A 119 ? 0.7144 0.8306 0.7393 0.1371  -0.2109 -0.0720 812  ILE   A CD1 
814  N N   . GLY   A 120 ? 0.6255 0.7848 0.7486 0.0704  -0.2294 -0.1635 813  GLY   A N   
815  C CA  . GLY   A 120 ? 0.6295 0.7725 0.7503 0.0530  -0.2203 -0.1758 813  GLY   A CA  
816  C C   . GLY   A 120 ? 0.6377 0.7546 0.7472 0.0426  -0.1909 -0.1569 813  GLY   A C   
817  O O   . GLY   A 120 ? 0.6344 0.7525 0.7470 0.0455  -0.1785 -0.1372 813  GLY   A O   
818  N N   . SER   A 121 ? 0.6442 0.7362 0.7395 0.0312  -0.1806 -0.1637 814  SER   A N   
819  C CA  . SER   A 121 ? 0.6646 0.7273 0.7435 0.0246  -0.1552 -0.1474 814  SER   A CA  
820  C C   . SER   A 121 ? 0.6469 0.7172 0.7561 0.0104  -0.1379 -0.1408 814  SER   A C   
821  O O   . SER   A 121 ? 0.6569 0.7108 0.7511 0.0137  -0.1224 -0.1206 814  SER   A O   
822  C CB  . SER   A 121 ? 0.7044 0.7383 0.7657 0.0142  -0.1487 -0.1604 814  SER   A CB  
823  O OG  . SER   A 121 ? 0.7273 0.7753 0.8235 -0.0061 -0.1529 -0.1867 814  SER   A OG  
824  N N   . GLN   A 122 ? 0.6206 0.7158 0.7725 -0.0049 -0.1405 -0.1588 815  GLN   A N   
825  C CA  . GLN   A 122 ? 0.6123 0.7128 0.7921 -0.0195 -0.1223 -0.1549 815  GLN   A CA  
826  C C   . GLN   A 122 ? 0.6048 0.7153 0.7826 -0.0067 -0.1208 -0.1330 815  GLN   A C   
827  O O   . GLN   A 122 ? 0.6122 0.7068 0.7828 -0.0110 -0.1031 -0.1181 815  GLN   A O   
828  C CB  . GLN   A 122 ? 0.6136 0.7445 0.8442 -0.0369 -0.1258 -0.1808 815  GLN   A CB  
829  C CG  . GLN   A 122 ? 0.6666 0.7928 0.9212 -0.0568 -0.1006 -0.1805 815  GLN   A CG  
830  C CD  . GLN   A 122 ? 0.7576 0.8403 0.9888 -0.0726 -0.0775 -0.1800 815  GLN   A CD  
831  O OE1 . GLN   A 122 ? 0.7779 0.8545 1.0234 -0.0908 -0.0722 -0.2017 815  GLN   A OE1 
832  N NE2 . GLN   A 122 ? 0.7847 0.8351 0.9797 -0.0657 -0.0632 -0.1559 815  GLN   A NE2 
833  N N   . TYR   A 123 ? 0.5887 0.7216 0.7685 0.0100  -0.1399 -0.1313 816  TYR   A N   
834  C CA  . TYR   A 123 ? 0.5838 0.7247 0.7602 0.0227  -0.1399 -0.1124 816  TYR   A CA  
835  C C   . TYR   A 123 ? 0.5772 0.6924 0.7163 0.0322  -0.1295 -0.0893 816  TYR   A C   
836  O O   . TYR   A 123 ? 0.5715 0.6839 0.7121 0.0308  -0.1176 -0.0747 816  TYR   A O   
837  C CB  . TYR   A 123 ? 0.5957 0.7580 0.7740 0.0403  -0.1630 -0.1171 816  TYR   A CB  
838  C CG  . TYR   A 123 ? 0.6060 0.8026 0.8299 0.0362  -0.1716 -0.1325 816  TYR   A CG  
839  C CD1 . TYR   A 123 ? 0.6196 0.8275 0.8606 0.0378  -0.1643 -0.1224 816  TYR   A CD1 
840  C CD2 . TYR   A 123 ? 0.6164 0.8355 0.8682 0.0314  -0.1873 -0.1588 816  TYR   A CD2 
841  C CE1 . TYR   A 123 ? 0.6141 0.8541 0.8986 0.0359  -0.1710 -0.1370 816  TYR   A CE1 
842  C CE2 . TYR   A 123 ? 0.6082 0.8639 0.9080 0.0293  -0.1957 -0.1747 816  TYR   A CE2 
843  C CZ  . TYR   A 123 ? 0.6147 0.8804 0.9306 0.0322  -0.1867 -0.1633 816  TYR   A CZ  
844  O OH  . TYR   A 123 ? 0.6164 0.9185 0.9815 0.0313  -0.1932 -0.1795 816  TYR   A OH  
845  N N   . LEU   A 124 ? 0.5769 0.6749 0.6837 0.0424  -0.1344 -0.0871 817  LEU   A N   
846  C CA  . LEU   A 124 ? 0.5814 0.6589 0.6573 0.0525  -0.1244 -0.0678 817  LEU   A CA  
847  C C   . LEU   A 124 ? 0.5772 0.6377 0.6518 0.0430  -0.1063 -0.0599 817  LEU   A C   
848  O O   . LEU   A 124 ? 0.5817 0.6397 0.6510 0.0481  -0.0982 -0.0434 817  LEU   A O   
849  C CB  . LEU   A 124 ? 0.5965 0.6571 0.6393 0.0638  -0.1309 -0.0707 817  LEU   A CB  
850  C CG  . LEU   A 124 ? 0.6106 0.6787 0.6390 0.0792  -0.1478 -0.0727 817  LEU   A CG  
851  C CD1 . LEU   A 124 ? 0.6353 0.6827 0.6281 0.0881  -0.1541 -0.0795 817  LEU   A CD1 
852  C CD2 . LEU   A 124 ? 0.6178 0.6863 0.6359 0.0908  -0.1421 -0.0531 817  LEU   A CD2 
853  N N   . LEU   A 125 ? 0.5683 0.6157 0.6471 0.0294  -0.1003 -0.0722 818  LEU   A N   
854  C CA  . LEU   A 125 ? 0.5770 0.6003 0.6465 0.0225  -0.0832 -0.0646 818  LEU   A CA  
855  C C   . LEU   A 125 ? 0.5631 0.5937 0.6517 0.0134  -0.0746 -0.0590 818  LEU   A C   
856  O O   . LEU   A 125 ? 0.5705 0.5867 0.6460 0.0164  -0.0651 -0.0452 818  LEU   A O   
857  C CB  . LEU   A 125 ? 0.5903 0.5884 0.6509 0.0111  -0.0765 -0.0787 818  LEU   A CB  
858  C CG  . LEU   A 125 ? 0.6186 0.5995 0.6508 0.0216  -0.0812 -0.0814 818  LEU   A CG  
859  C CD1 . LEU   A 125 ? 0.6343 0.5948 0.6631 0.0076  -0.0777 -0.1007 818  LEU   A CD1 
860  C CD2 . LEU   A 125 ? 0.6405 0.6010 0.6461 0.0356  -0.0718 -0.0632 818  LEU   A CD2 
861  N N   . ASN   A 126 ? 0.5414 0.5952 0.6603 0.0042  -0.0787 -0.0701 819  ASN   A N   
862  C CA  . ASN   A 126 ? 0.5317 0.5922 0.6682 -0.0043 -0.0695 -0.0662 819  ASN   A CA  
863  C C   . ASN   A 126 ? 0.5157 0.5862 0.6469 0.0083  -0.0730 -0.0486 819  ASN   A C   
864  O O   . ASN   A 126 ? 0.5234 0.5847 0.6501 0.0054  -0.0632 -0.0388 819  ASN   A O   
865  C CB  . ASN   A 126 ? 0.5443 0.6307 0.7187 -0.0155 -0.0729 -0.0840 819  ASN   A CB  
866  C CG  . ASN   A 126 ? 0.6236 0.6998 0.8110 -0.0346 -0.0629 -0.1030 819  ASN   A CG  
867  O OD1 . ASN   A 126 ? 0.6676 0.7101 0.8316 -0.0412 -0.0497 -0.1010 819  ASN   A OD1 
868  N ND2 . ASN   A 126 ? 0.6212 0.7259 0.8476 -0.0437 -0.0688 -0.1231 819  ASN   A ND2 
869  N N   . TRP   A 127 ? 0.4933 0.5787 0.6214 0.0221  -0.0859 -0.0448 820  TRP   A N   
870  C CA  . TRP   A 127 ? 0.4839 0.5761 0.6065 0.0324  -0.0870 -0.0290 820  TRP   A CA  
871  C C   . TRP   A 127 ? 0.4900 0.5647 0.5913 0.0374  -0.0791 -0.0156 820  TRP   A C   
872  O O   . TRP   A 127 ? 0.4898 0.5666 0.5924 0.0381  -0.0751 -0.0054 820  TRP   A O   
873  C CB  . TRP   A 127 ? 0.4770 0.5805 0.5939 0.0461  -0.0993 -0.0277 820  TRP   A CB  
874  C CG  . TRP   A 127 ? 0.4715 0.5948 0.6089 0.0467  -0.1106 -0.0390 820  TRP   A CG  
875  C CD1 . TRP   A 127 ? 0.4715 0.6096 0.6367 0.0382  -0.1086 -0.0453 820  TRP   A CD1 
876  C CD2 . TRP   A 127 ? 0.4741 0.6044 0.6041 0.0592  -0.1263 -0.0452 820  TRP   A CD2 
877  N NE1 . TRP   A 127 ? 0.4637 0.6212 0.6445 0.0451  -0.1230 -0.0561 820  TRP   A NE1 
878  C CE2 . TRP   A 127 ? 0.4699 0.6221 0.6275 0.0586  -0.1355 -0.0561 820  TRP   A CE2 
879  C CE3 . TRP   A 127 ? 0.4940 0.6122 0.5945 0.0717  -0.1335 -0.0437 820  TRP   A CE3 
880  C CZ2 . TRP   A 127 ? 0.4755 0.6388 0.6319 0.0719  -0.1546 -0.0654 820  TRP   A CZ2 
881  C CZ3 . TRP   A 127 ? 0.5065 0.6315 0.6005 0.0840  -0.1510 -0.0518 820  TRP   A CZ3 
882  C CH2 . TRP   A 127 ? 0.4917 0.6395 0.6133 0.0848  -0.1629 -0.0626 820  TRP   A CH2 
883  N N   . CYS   A 128 ? 0.4950 0.5531 0.5778 0.0415  -0.0776 -0.0169 821  CYS   A N   
884  C CA  . CYS   A 128 ? 0.5143 0.5571 0.5795 0.0486  -0.0710 -0.0059 821  CYS   A CA  
885  C C   . CYS   A 128 ? 0.5131 0.5425 0.5767 0.0413  -0.0629 -0.0023 821  CYS   A C   
886  O O   . CYS   A 128 ? 0.5192 0.5481 0.5778 0.0477  -0.0615 0.0084  821  CYS   A O   
887  C CB  . CYS   A 128 ? 0.5502 0.5742 0.5955 0.0542  -0.0697 -0.0102 821  CYS   A CB  
888  S SG  . CYS   A 128 ? 0.6291 0.6606 0.6638 0.0665  -0.0775 -0.0119 821  CYS   A SG  
889  N N   . VAL   A 129 ? 0.5077 0.5255 0.5749 0.0280  -0.0572 -0.0121 822  VAL   A N   
890  C CA  . VAL   A 129 ? 0.5149 0.5123 0.5737 0.0201  -0.0467 -0.0094 822  VAL   A CA  
891  C C   . VAL   A 129 ? 0.4997 0.5129 0.5703 0.0188  -0.0479 -0.0029 822  VAL   A C   
892  O O   . VAL   A 129 ? 0.5197 0.5209 0.5759 0.0224  -0.0454 0.0063  822  VAL   A O   
893  C CB  . VAL   A 129 ? 0.5292 0.5112 0.5927 0.0031  -0.0366 -0.0236 822  VAL   A CB  
894  C CG1 . VAL   A 129 ? 0.5503 0.5071 0.6011 -0.0057 -0.0225 -0.0202 822  VAL   A CG1 
895  C CG2 . VAL   A 129 ? 0.5467 0.5070 0.5951 0.0026  -0.0340 -0.0312 822  VAL   A CG2 
896  N N   . GLN   A 130 ? 0.4577 0.4964 0.5527 0.0148  -0.0528 -0.0084 823  GLN   A N   
897  C CA  . GLN   A 130 ? 0.4303 0.4827 0.5371 0.0129  -0.0530 -0.0040 823  GLN   A CA  
898  C C   . GLN   A 130 ? 0.4266 0.4862 0.5267 0.0239  -0.0587 0.0087  823  GLN   A C   
899  O O   . GLN   A 130 ? 0.4364 0.4912 0.5312 0.0225  -0.0563 0.0145  823  GLN   A O   
900  C CB  . GLN   A 130 ? 0.4247 0.5012 0.5582 0.0095  -0.0579 -0.0133 823  GLN   A CB  
901  C CG  . GLN   A 130 ? 0.4539 0.5286 0.6034 -0.0043 -0.0506 -0.0287 823  GLN   A CG  
902  C CD  . GLN   A 130 ? 0.4919 0.5949 0.6731 -0.0057 -0.0570 -0.0395 823  GLN   A CD  
903  O OE1 . GLN   A 130 ? 0.4935 0.6123 0.6807 0.0034  -0.0650 -0.0340 823  GLN   A OE1 
904  N NE2 . GLN   A 130 ? 0.4984 0.6083 0.7018 -0.0168 -0.0533 -0.0562 823  GLN   A NE2 
905  N N   . ILE   A 131 ? 0.4118 0.4812 0.5108 0.0342  -0.0650 0.0120  824  ILE   A N   
906  C CA  . ILE   A 131 ? 0.4032 0.4814 0.5008 0.0428  -0.0676 0.0221  824  ILE   A CA  
907  C C   . ILE   A 131 ? 0.4233 0.4878 0.5066 0.0472  -0.0662 0.0277  824  ILE   A C   
908  O O   . ILE   A 131 ? 0.4289 0.5000 0.5149 0.0487  -0.0684 0.0331  824  ILE   A O   
909  C CB  . ILE   A 131 ? 0.3950 0.4827 0.4924 0.0522  -0.0707 0.0238  824  ILE   A CB  
910  C CG1 . ILE   A 131 ? 0.3783 0.4761 0.4841 0.0513  -0.0749 0.0189  824  ILE   A CG1 
911  C CG2 . ILE   A 131 ? 0.3920 0.4897 0.4925 0.0590  -0.0695 0.0326  824  ILE   A CG2 
912  C CD1 . ILE   A 131 ? 0.3872 0.4848 0.4830 0.0606  -0.0778 0.0185  824  ILE   A CD1 
913  N N   . ALA   A 132 ? 0.4289 0.4723 0.4957 0.0492  -0.0631 0.0255  825  ALA   A N   
914  C CA  . ALA   A 132 ? 0.4385 0.4640 0.4868 0.0567  -0.0628 0.0309  825  ALA   A CA  
915  C C   . ALA   A 132 ? 0.4371 0.4474 0.4745 0.0498  -0.0604 0.0322  825  ALA   A C   
916  O O   . ALA   A 132 ? 0.4385 0.4435 0.4645 0.0575  -0.0651 0.0379  825  ALA   A O   
917  C CB  . ALA   A 132 ? 0.4567 0.4569 0.4855 0.0612  -0.0584 0.0283  825  ALA   A CB  
918  N N   . LYS   A 133 ? 0.4321 0.4361 0.4731 0.0360  -0.0532 0.0260  826  LYS   A N   
919  C CA  . LYS   A 133 ? 0.4336 0.4208 0.4625 0.0284  -0.0475 0.0266  826  LYS   A CA  
920  C C   . LYS   A 133 ? 0.4293 0.4367 0.4689 0.0295  -0.0547 0.0308  826  LYS   A C   
921  O O   . LYS   A 133 ? 0.4533 0.4465 0.4743 0.0315  -0.0564 0.0347  826  LYS   A O   
922  C CB  . LYS   A 133 ? 0.4285 0.4088 0.4659 0.0127  -0.0355 0.0170  826  LYS   A CB  
923  C CG  . LYS   A 133 ? 0.4451 0.3917 0.4622 0.0076  -0.0239 0.0125  826  LYS   A CG  
924  C CD  . LYS   A 133 ? 0.4470 0.3952 0.4833 -0.0096 -0.0119 -0.0004 826  LYS   A CD  
925  C CE  . LYS   A 133 ? 0.4998 0.4105 0.5153 -0.0176 0.0028  -0.0058 826  LYS   A CE  
926  N N   . GLY   A 134 ? 0.4017 0.4382 0.4675 0.0286  -0.0588 0.0296  827  GLY   A N   
927  C CA  . GLY   A 134 ? 0.4034 0.4573 0.4803 0.0284  -0.0640 0.0326  827  GLY   A CA  
928  C C   . GLY   A 134 ? 0.4136 0.4758 0.4883 0.0388  -0.0730 0.0381  827  GLY   A C   
929  O O   . GLY   A 134 ? 0.4213 0.4839 0.4915 0.0388  -0.0780 0.0397  827  GLY   A O   
930  N N   . MET   A 135 ? 0.4166 0.4856 0.4948 0.0481  -0.0753 0.0398  828  MET   A N   
931  C CA  . MET   A 135 ? 0.4251 0.5066 0.5077 0.0592  -0.0830 0.0432  828  MET   A CA  
932  C C   . MET   A 135 ? 0.4559 0.5178 0.5150 0.0669  -0.0892 0.0451  828  MET   A C   
933  O O   . MET   A 135 ? 0.4633 0.5374 0.5272 0.0725  -0.0992 0.0457  828  MET   A O   
934  C CB  . MET   A 135 ? 0.4319 0.5224 0.5222 0.0681  -0.0812 0.0439  828  MET   A CB  
935  C CG  . MET   A 135 ? 0.4597 0.5692 0.5690 0.0642  -0.0768 0.0435  828  MET   A CG  
936  S SD  . MET   A 135 ? 0.5357 0.6699 0.6683 0.0587  -0.0783 0.0445  828  MET   A SD  
937  C CE  . MET   A 135 ? 0.4707 0.6221 0.6159 0.0702  -0.0839 0.0447  828  MET   A CE  
938  N N   . ASN   A 136 ? 0.4721 0.5018 0.5043 0.0669  -0.0834 0.0452  829  ASN   A N   
939  C CA  . ASN   A 136 ? 0.5012 0.5010 0.5003 0.0754  -0.0872 0.0481  829  ASN   A CA  
940  C C   . ASN   A 136 ? 0.5153 0.5074 0.5021 0.0692  -0.0905 0.0479  829  ASN   A C   
941  O O   . ASN   A 136 ? 0.5374 0.5155 0.5009 0.0798  -0.1005 0.0503  829  ASN   A O   
942  C CB  . ASN   A 136 ? 0.5356 0.4972 0.5072 0.0731  -0.0752 0.0477  829  ASN   A CB  
943  C CG  . ASN   A 136 ? 0.5963 0.5167 0.5246 0.0831  -0.0763 0.0520  829  ASN   A CG  
944  O OD1 . ASN   A 136 ? 0.6114 0.5291 0.5286 0.1016  -0.0873 0.0559  829  ASN   A OD1 
945  N ND2 . ASN   A 136 ? 0.6235 0.5094 0.5253 0.0720  -0.0640 0.0511  829  ASN   A ND2 
946  N N   . TYR   A 137 ? 0.5037 0.5025 0.5033 0.0537  -0.0826 0.0446  830  TYR   A N   
947  C CA  . TYR   A 137 ? 0.5149 0.5055 0.5031 0.0468  -0.0834 0.0435  830  TYR   A CA  
948  C C   . TYR   A 137 ? 0.5031 0.5236 0.5105 0.0509  -0.0982 0.0428  830  TYR   A C   
949  O O   . TYR   A 137 ? 0.5162 0.5266 0.5041 0.0546  -0.1075 0.0424  830  TYR   A O   
950  C CB  . TYR   A 137 ? 0.5143 0.5057 0.5149 0.0307  -0.0696 0.0392  830  TYR   A CB  
951  C CG  . TYR   A 137 ? 0.5347 0.5211 0.5272 0.0240  -0.0698 0.0375  830  TYR   A CG  
952  C CD1 . TYR   A 137 ? 0.5717 0.5228 0.5241 0.0252  -0.0682 0.0386  830  TYR   A CD1 
953  C CD2 . TYR   A 137 ? 0.5285 0.5417 0.5484 0.0180  -0.0722 0.0350  830  TYR   A CD2 
954  C CE1 . TYR   A 137 ? 0.5877 0.5315 0.5285 0.0197  -0.0687 0.0364  830  TYR   A CE1 
955  C CE2 . TYR   A 137 ? 0.5464 0.5529 0.5571 0.0121  -0.0725 0.0327  830  TYR   A CE2 
956  C CZ  . TYR   A 137 ? 0.5825 0.5552 0.5541 0.0128  -0.0710 0.0330  830  TYR   A CZ  
957  O OH  . TYR   A 137 ? 0.6074 0.5709 0.5659 0.0073  -0.0716 0.0299  830  TYR   A OH  
958  N N   . LEU   A 138 ? 0.4859 0.5408 0.5293 0.0500  -0.0998 0.0418  831  LEU   A N   
959  C CA  . LEU   A 138 ? 0.4811 0.5658 0.5481 0.0514  -0.1106 0.0395  831  LEU   A CA  
960  C C   . LEU   A 138 ? 0.5002 0.5892 0.5609 0.0671  -0.1260 0.0394  831  LEU   A C   
961  O O   . LEU   A 138 ? 0.4939 0.5945 0.5586 0.0684  -0.1387 0.0353  831  LEU   A O   
962  C CB  . LEU   A 138 ? 0.4560 0.5696 0.5580 0.0476  -0.1046 0.0391  831  LEU   A CB  
963  C CG  . LEU   A 138 ? 0.4618 0.5742 0.5713 0.0350  -0.0935 0.0385  831  LEU   A CG  
964  C CD1 . LEU   A 138 ? 0.4504 0.5818 0.5830 0.0347  -0.0873 0.0397  831  LEU   A CD1 
965  C CD2 . LEU   A 138 ? 0.4636 0.5747 0.5723 0.0255  -0.0952 0.0353  831  LEU   A CD2 
966  N N   . GLU   A 139 ? 0.5232 0.6007 0.5720 0.0798  -0.1258 0.0429  832  GLU   A N   
967  C CA  . GLU   A 139 ? 0.5522 0.6304 0.5920 0.0987  -0.1409 0.0431  832  GLU   A CA  
968  C C   . GLU   A 139 ? 0.5981 0.6431 0.5946 0.1045  -0.1510 0.0438  832  GLU   A C   
969  O O   . GLU   A 139 ? 0.5978 0.6531 0.5926 0.1172  -0.1701 0.0406  832  GLU   A O   
970  C CB  . GLU   A 139 ? 0.5985 0.6649 0.6306 0.1111  -0.1355 0.0470  832  GLU   A CB  
971  C CG  . GLU   A 139 ? 0.6967 0.7576 0.7144 0.1342  -0.1507 0.0479  832  GLU   A CG  
972  C CD  . GLU   A 139 ? 0.8346 0.8899 0.8517 0.1484  -0.1456 0.0507  832  GLU   A CD  
973  O OE1 . GLU   A 139 ? 0.8677 0.9219 0.8935 0.1391  -0.1301 0.0516  832  GLU   A OE1 
974  O OE2 . GLU   A 139 ? 0.8816 0.9331 0.8885 0.1702  -0.1582 0.0514  832  GLU   A OE2 
975  N N   . ASP   A 140 ? 0.6343 0.6407 0.5970 0.0950  -0.1381 0.0467  833  ASP   A N   
976  C CA  . ASP   A 140 ? 0.6818 0.6488 0.5965 0.0980  -0.1423 0.0479  833  ASP   A CA  
977  C C   . ASP   A 140 ? 0.6761 0.6614 0.5998 0.0913  -0.1542 0.0418  833  ASP   A C   
978  O O   . ASP   A 140 ? 0.6919 0.6601 0.5841 0.1014  -0.1694 0.0405  833  ASP   A O   
979  C CB  . ASP   A 140 ? 0.7393 0.6657 0.6255 0.0847  -0.1196 0.0506  833  ASP   A CB  
980  C CG  . ASP   A 140 ? 0.8531 0.7333 0.6864 0.0846  -0.1174 0.0520  833  ASP   A CG  
981  O OD1 . ASP   A 140 ? 0.9040 0.7508 0.6938 0.1016  -0.1261 0.0561  833  ASP   A OD1 
982  O OD2 . ASP   A 140 ? 0.8855 0.7604 0.7182 0.0687  -0.1065 0.0489  833  ASP   A OD2 
983  N N   . ARG   A 141 ? 0.6556 0.6721 0.6188 0.0752  -0.1474 0.0378  834  ARG   A N   
984  C CA  . ARG   A 141 ? 0.6563 0.6908 0.6324 0.0666  -0.1564 0.0309  834  ARG   A CA  
985  C C   . ARG   A 141 ? 0.6558 0.7333 0.6681 0.0739  -0.1757 0.0243  834  ARG   A C   
986  O O   . ARG   A 141 ? 0.6542 0.7507 0.6841 0.0645  -0.1825 0.0167  834  ARG   A O   
987  C CB  . ARG   A 141 ? 0.6458 0.6928 0.6484 0.0472  -0.1398 0.0293  834  ARG   A CB  
988  C CG  . ARG   A 141 ? 0.6814 0.6963 0.6612 0.0368  -0.1204 0.0319  834  ARG   A CG  
989  C CD  . ARG   A 141 ? 0.7489 0.7171 0.6760 0.0421  -0.1176 0.0347  834  ARG   A CD  
990  N NE  . ARG   A 141 ? 0.7986 0.7477 0.6957 0.0406  -0.1249 0.0310  834  ARG   A NE  
991  C CZ  . ARG   A 141 ? 0.8588 0.7637 0.7016 0.0478  -0.1260 0.0332  834  ARG   A CZ  
992  N NH1 . ARG   A 141 ? 0.8805 0.7673 0.6937 0.0465  -0.1332 0.0289  834  ARG   A NH1 
993  N NH2 . ARG   A 141 ? 0.8736 0.7479 0.6873 0.0567  -0.1192 0.0396  834  ARG   A NH2 
994  N N   . ARG   A 142 ? 0.6540 0.7475 0.6803 0.0896  -0.1829 0.0259  835  ARG   A N   
995  C CA  . ARG   A 142 ? 0.6344 0.7729 0.7021 0.0979  -0.1989 0.0185  835  ARG   A CA  
996  C C   . ARG   A 142 ? 0.6106 0.7873 0.7298 0.0805  -0.1877 0.0138  835  ARG   A C   
997  O O   . ARG   A 142 ? 0.5982 0.8084 0.7502 0.0764  -0.1983 0.0038  835  ARG   A O   
998  C CB  . ARG   A 142 ? 0.6533 0.7952 0.7076 0.1073  -0.2250 0.0101  835  ARG   A CB  
999  C CG  . ARG   A 142 ? 0.7283 0.8237 0.7213 0.1263  -0.2359 0.0157  835  ARG   A CG  
1000 C CD  . ARG   A 142 ? 0.7861 0.8745 0.7534 0.1325  -0.2605 0.0075  835  ARG   A CD  
1001 N N   . LEU   A 143 ? 0.6046 0.7741 0.7290 0.0703  -0.1665 0.0201  836  LEU   A N   
1002 C CA  . LEU   A 143 ? 0.5863 0.7817 0.7490 0.0554  -0.1538 0.0176  836  LEU   A CA  
1003 C C   . LEU   A 143 ? 0.5714 0.7809 0.7553 0.0605  -0.1420 0.0218  836  LEU   A C   
1004 O O   . LEU   A 143 ? 0.5941 0.7816 0.7578 0.0642  -0.1327 0.0289  836  LEU   A O   
1005 C CB  . LEU   A 143 ? 0.6057 0.7789 0.7534 0.0396  -0.1399 0.0203  836  LEU   A CB  
1006 C CG  . LEU   A 143 ? 0.6159 0.8066 0.7930 0.0241  -0.1293 0.0170  836  LEU   A CG  
1007 C CD1 . LEU   A 143 ? 0.6384 0.8086 0.7979 0.0118  -0.1254 0.0153  836  LEU   A CD1 
1008 C CD2 . LEU   A 143 ? 0.6224 0.8150 0.8109 0.0227  -0.1124 0.0232  836  LEU   A CD2 
1009 N N   . VAL   A 144 ? 0.5294 0.7746 0.7540 0.0598  -0.1413 0.0162  837  VAL   A N   
1010 C CA  . VAL   A 144 ? 0.5066 0.7637 0.7499 0.0640  -0.1276 0.0196  837  VAL   A CA  
1011 C C   . VAL   A 144 ? 0.4978 0.7504 0.7473 0.0481  -0.1088 0.0223  837  VAL   A C   
1012 O O   . VAL   A 144 ? 0.4899 0.7536 0.7569 0.0347  -0.1062 0.0172  837  VAL   A O   
1013 C CB  . VAL   A 144 ? 0.4792 0.7760 0.7638 0.0720  -0.1332 0.0115  837  VAL   A CB  
1014 C CG1 . VAL   A 144 ? 0.4773 0.7841 0.7800 0.0747  -0.1146 0.0146  837  VAL   A CG1 
1015 C CG2 . VAL   A 144 ? 0.4735 0.7723 0.7481 0.0921  -0.1546 0.0090  837  VAL   A CG2 
1016 N N   . HIS   A 145 ? 0.5009 0.7343 0.7330 0.0500  -0.0968 0.0298  838  HIS   A N   
1017 C CA  . HIS   A 145 ? 0.4993 0.7239 0.7304 0.0391  -0.0815 0.0332  838  HIS   A CA  
1018 C C   . HIS   A 145 ? 0.4963 0.7414 0.7567 0.0341  -0.0681 0.0310  838  HIS   A C   
1019 O O   . HIS   A 145 ? 0.4990 0.7438 0.7676 0.0213  -0.0598 0.0295  838  HIS   A O   
1020 C CB  . HIS   A 145 ? 0.4999 0.7011 0.7054 0.0446  -0.0757 0.0395  838  HIS   A CB  
1021 C CG  . HIS   A 145 ? 0.4989 0.6872 0.6966 0.0370  -0.0653 0.0426  838  HIS   A CG  
1022 N ND1 . HIS   A 145 ? 0.5063 0.6998 0.7151 0.0331  -0.0525 0.0439  838  HIS   A ND1 
1023 C CD2 . HIS   A 145 ? 0.5130 0.6824 0.6921 0.0346  -0.0656 0.0442  838  HIS   A CD2 
1024 C CE1 . HIS   A 145 ? 0.5170 0.6926 0.7099 0.0304  -0.0478 0.0471  838  HIS   A CE1 
1025 N NE2 . HIS   A 145 ? 0.5218 0.6859 0.7001 0.0315  -0.0561 0.0467  838  HIS   A NE2 
1026 N N   . ARG   A 146 ? 0.4868 0.7462 0.7608 0.0441  -0.0637 0.0306  839  ARG   A N   
1027 C CA  . ARG   A 146 ? 0.4750 0.7531 0.7769 0.0408  -0.0472 0.0281  839  ARG   A CA  
1028 C C   . ARG   A 146 ? 0.4857 0.7413 0.7682 0.0389  -0.0277 0.0355  839  ARG   A C   
1029 O O   . ARG   A 146 ? 0.4889 0.7524 0.7856 0.0388  -0.0109 0.0349  839  ARG   A O   
1030 C CB  . ARG   A 146 ? 0.4757 0.7778 0.8123 0.0263  -0.0453 0.0191  839  ARG   A CB  
1031 C CG  . ARG   A 146 ? 0.5112 0.8440 0.8751 0.0304  -0.0648 0.0088  839  ARG   A CG  
1032 C CD  . ARG   A 146 ? 0.5583 0.9135 0.9566 0.0127  -0.0625 -0.0023 839  ARG   A CD  
1033 N NE  . ARG   A 146 ? 0.6043 0.9976 1.0383 0.0175  -0.0812 -0.0153 839  ARG   A NE  
1034 C CZ  . ARG   A 146 ? 0.6304 1.0625 1.1159 0.0106  -0.0746 -0.0278 839  ARG   A CZ  
1035 N NH1 . ARG   A 146 ? 0.6036 1.0733 1.1226 0.0176  -0.0960 -0.0413 839  ARG   A NH1 
1036 N NH2 . ARG   A 146 ? 0.6412 1.0742 1.1446 -0.0026 -0.0463 -0.0277 839  ARG   A NH2 
1037 N N   . ASP   A 147 ? 0.4875 0.7152 0.7378 0.0383  -0.0297 0.0415  840  ASP   A N   
1038 C CA  . ASP   A 147 ? 0.4956 0.7007 0.7236 0.0393  -0.0154 0.0478  840  ASP   A CA  
1039 C C   . ASP   A 147 ? 0.4893 0.6717 0.6851 0.0470  -0.0240 0.0518  840  ASP   A C   
1040 O O   . ASP   A 147 ? 0.5042 0.6680 0.6815 0.0451  -0.0216 0.0551  840  ASP   A O   
1041 C CB  . ASP   A 147 ? 0.5439 0.7402 0.7738 0.0265  -0.0030 0.0488  840  ASP   A CB  
1042 C CG  . ASP   A 147 ? 0.6618 0.8326 0.8672 0.0294  0.0146  0.0555  840  ASP   A CG  
1043 O OD1 . ASP   A 147 ? 0.6910 0.8572 0.8853 0.0394  0.0209  0.0578  840  ASP   A OD1 
1044 O OD2 . ASP   A 147 ? 0.7091 0.8608 0.9018 0.0231  0.0217  0.0586  840  ASP   A OD2 
1045 N N   . LEU   A 148 ? 0.4624 0.6459 0.6524 0.0560  -0.0340 0.0506  841  LEU   A N   
1046 C CA  . LEU   A 148 ? 0.4520 0.6159 0.6161 0.0611  -0.0406 0.0519  841  LEU   A CA  
1047 C C   . LEU   A 148 ? 0.4524 0.6029 0.5981 0.0685  -0.0313 0.0545  841  LEU   A C   
1048 O O   . LEU   A 148 ? 0.4513 0.6062 0.6003 0.0745  -0.0228 0.0548  841  LEU   A O   
1049 C CB  . LEU   A 148 ? 0.4400 0.6031 0.5999 0.0670  -0.0512 0.0495  841  LEU   A CB  
1050 C CG  . LEU   A 148 ? 0.4541 0.5975 0.5912 0.0696  -0.0558 0.0483  841  LEU   A CG  
1051 C CD1 . LEU   A 148 ? 0.4496 0.5862 0.5828 0.0611  -0.0597 0.0471  841  LEU   A CD1 
1052 C CD2 . LEU   A 148 ? 0.4646 0.6010 0.5944 0.0748  -0.0619 0.0464  841  LEU   A CD2 
1053 N N   . ALA   A 149 ? 0.4564 0.5903 0.5824 0.0689  -0.0328 0.0558  842  ALA   A N   
1054 C CA  . ALA   A 149 ? 0.4725 0.5885 0.5728 0.0775  -0.0275 0.0578  842  ALA   A CA  
1055 C C   . ALA   A 149 ? 0.4877 0.5920 0.5719 0.0795  -0.0394 0.0554  842  ALA   A C   
1056 O O   . ALA   A 149 ? 0.4853 0.5953 0.5809 0.0728  -0.0461 0.0537  842  ALA   A O   
1057 C CB  . ALA   A 149 ? 0.4761 0.5848 0.5718 0.0764  -0.0109 0.0630  842  ALA   A CB  
1058 N N   . ALA   A 150 ? 0.5012 0.5906 0.5603 0.0890  -0.0426 0.0538  843  ALA   A N   
1059 C CA  . ALA   A 150 ? 0.5120 0.5957 0.5614 0.0920  -0.0564 0.0487  843  ALA   A CA  
1060 C C   . ALA   A 150 ? 0.5252 0.6039 0.5727 0.0919  -0.0560 0.0525  843  ALA   A C   
1061 O O   . ALA   A 150 ? 0.5324 0.6154 0.5864 0.0917  -0.0671 0.0476  843  ALA   A O   
1062 C CB  . ALA   A 150 ? 0.5245 0.5934 0.5460 0.1032  -0.0620 0.0447  843  ALA   A CB  
1063 N N   . ARG   A 151 ? 0.5230 0.5924 0.5640 0.0914  -0.0415 0.0605  844  ARG   A N   
1064 C CA  . ARG   A 151 ? 0.5301 0.5894 0.5668 0.0907  -0.0383 0.0649  844  ARG   A CA  
1065 C C   . ARG   A 151 ? 0.5088 0.5852 0.5757 0.0780  -0.0405 0.0626  844  ARG   A C   
1066 O O   . ARG   A 151 ? 0.5092 0.5791 0.5754 0.0778  -0.0419 0.0635  844  ARG   A O   
1067 C CB  . ARG   A 151 ? 0.5615 0.6018 0.5818 0.0910  -0.0182 0.0734  844  ARG   A CB  
1068 C CG  . ARG   A 151 ? 0.5914 0.6488 0.6399 0.0778  -0.0044 0.0739  844  ARG   A CG  
1069 C CD  . ARG   A 151 ? 0.6558 0.6969 0.6951 0.0743  0.0190  0.0801  844  ARG   A CD  
1070 N NE  . ARG   A 151 ? 0.7089 0.7747 0.7830 0.0628  0.0295  0.0770  844  ARG   A NE  
1071 C CZ  . ARG   A 151 ? 0.7563 0.8316 0.8361 0.0661  0.0363  0.0754  844  ARG   A CZ  
1072 N NH1 . ARG   A 151 ? 0.7460 0.8486 0.8628 0.0573  0.0429  0.0711  844  ARG   A NH1 
1073 N NH2 . ARG   A 151 ? 0.7724 0.8305 0.8213 0.0792  0.0356  0.0771  844  ARG   A NH2 
1074 N N   . ASN   A 152 ? 0.4848 0.5797 0.5744 0.0690  -0.0409 0.0596  845  ASN   A N   
1075 C CA  . ASN   A 152 ? 0.4708 0.5784 0.5824 0.0579  -0.0438 0.0570  845  ASN   A CA  
1076 C C   . ASN   A 152 ? 0.4560 0.5708 0.5745 0.0566  -0.0557 0.0503  845  ASN   A C   
1077 O O   . ASN   A 152 ? 0.4493 0.5716 0.5808 0.0483  -0.0573 0.0480  845  ASN   A O   
1078 C CB  . ASN   A 152 ? 0.4770 0.5980 0.6067 0.0498  -0.0371 0.0576  845  ASN   A CB  
1079 C CG  . ASN   A 152 ? 0.5259 0.6428 0.6587 0.0448  -0.0225 0.0616  845  ASN   A CG  
1080 O OD1 . ASN   A 152 ? 0.5375 0.6668 0.6856 0.0408  -0.0149 0.0610  845  ASN   A OD1 
1081 N ND2 . ASN   A 152 ? 0.5451 0.6440 0.6644 0.0451  -0.0172 0.0650  845  ASN   A ND2 
1082 N N   . VAL   A 153 ? 0.4495 0.5604 0.5581 0.0642  -0.0634 0.0462  846  VAL   A N   
1083 C CA  . VAL   A 153 ? 0.4492 0.5660 0.5667 0.0612  -0.0718 0.0379  846  VAL   A CA  
1084 C C   . VAL   A 153 ? 0.4670 0.5825 0.5839 0.0671  -0.0781 0.0342  846  VAL   A C   
1085 O O   . VAL   A 153 ? 0.4807 0.5884 0.5812 0.0784  -0.0820 0.0353  846  VAL   A O   
1086 C CB  . VAL   A 153 ? 0.4537 0.5696 0.5649 0.0641  -0.0760 0.0331  846  VAL   A CB  
1087 C CG1 . VAL   A 153 ? 0.4491 0.5692 0.5714 0.0580  -0.0816 0.0230  846  VAL   A CG1 
1088 C CG2 . VAL   A 153 ? 0.4563 0.5723 0.5666 0.0625  -0.0700 0.0374  846  VAL   A CG2 
1089 N N   . LEU   A 154 ? 0.4681 0.5895 0.6006 0.0612  -0.0788 0.0301  847  LEU   A N   
1090 C CA  . LEU   A 154 ? 0.4841 0.6076 0.6214 0.0684  -0.0850 0.0255  847  LEU   A CA  
1091 C C   . LEU   A 154 ? 0.4811 0.6184 0.6361 0.0669  -0.0932 0.0123  847  LEU   A C   
1092 O O   . LEU   A 154 ? 0.4825 0.6238 0.6472 0.0560  -0.0897 0.0075  847  LEU   A O   
1093 C CB  . LEU   A 154 ? 0.4955 0.6158 0.6401 0.0637  -0.0780 0.0285  847  LEU   A CB  
1094 C CG  . LEU   A 154 ? 0.5399 0.6480 0.6728 0.0602  -0.0680 0.0390  847  LEU   A CG  
1095 C CD1 . LEU   A 154 ? 0.5503 0.6537 0.6899 0.0540  -0.0617 0.0396  847  LEU   A CD1 
1096 C CD2 . LEU   A 154 ? 0.5663 0.6594 0.6765 0.0721  -0.0666 0.0460  847  LEU   A CD2 
1097 N N   . VAL   A 155 ? 0.4768 0.6200 0.6353 0.0783  -0.1039 0.0057  848  VAL   A N   
1098 C CA  . VAL   A 155 ? 0.4717 0.6332 0.6535 0.0771  -0.1130 -0.0100 848  VAL   A CA  
1099 C C   . VAL   A 155 ? 0.4720 0.6458 0.6800 0.0758  -0.1112 -0.0165 848  VAL   A C   
1100 O O   . VAL   A 155 ? 0.4739 0.6463 0.6788 0.0893  -0.1167 -0.0145 848  VAL   A O   
1101 C CB  . VAL   A 155 ? 0.4774 0.6412 0.6475 0.0927  -0.1300 -0.0161 848  VAL   A CB  
1102 C CG1 . VAL   A 155 ? 0.4668 0.6539 0.6664 0.0898  -0.1411 -0.0358 848  VAL   A CG1 
1103 C CG2 . VAL   A 155 ? 0.4900 0.6373 0.6299 0.0949  -0.1287 -0.0087 848  VAL   A CG2 
1104 N N   . LYS   A 156 ? 0.4746 0.6559 0.7044 0.0604  -0.1012 -0.0234 849  LYS   A N   
1105 C CA  . LYS   A 156 ? 0.4782 0.6717 0.7354 0.0578  -0.0962 -0.0316 849  LYS   A CA  
1106 C C   . LYS   A 156 ? 0.4735 0.6928 0.7599 0.0642  -0.1095 -0.0496 849  LYS   A C   
1107 O O   . LYS   A 156 ? 0.4692 0.7011 0.7697 0.0783  -0.1187 -0.0548 849  LYS   A O   
1108 C CB  . LYS   A 156 ? 0.5036 0.6913 0.7682 0.0387  -0.0788 -0.0331 849  LYS   A CB  
1109 C CG  . LYS   A 156 ? 0.5469 0.7429 0.8361 0.0352  -0.0693 -0.0407 849  LYS   A CG  
1110 C CD  . LYS   A 156 ? 0.6086 0.7893 0.8923 0.0176  -0.0506 -0.0394 849  LYS   A CD  
1111 C CE  . LYS   A 156 ? 0.6475 0.8329 0.9522 0.0137  -0.0379 -0.0470 849  LYS   A CE  
1112 N NZ  . LYS   A 156 ? 0.6672 0.8800 1.0134 0.0128  -0.0383 -0.0657 849  LYS   A NZ  
1113 N N   . THR   A 157 ? 0.4718 0.6985 0.7674 0.0545  -0.1112 -0.0599 850  THR   A N   
1114 C CA  . THR   A 157 ? 0.4658 0.7174 0.7883 0.0573  -0.1255 -0.0793 850  THR   A CA  
1115 C C   . THR   A 157 ? 0.4803 0.7200 0.7776 0.0563  -0.1324 -0.0779 850  THR   A C   
1116 O O   . THR   A 157 ? 0.5008 0.7179 0.7727 0.0481  -0.1208 -0.0655 850  THR   A O   
1117 C CB  . THR   A 157 ? 0.4679 0.7405 0.8355 0.0402  -0.1141 -0.0983 850  THR   A CB  
1118 O OG1 . THR   A 157 ? 0.4918 0.7493 0.8525 0.0203  -0.0994 -0.0994 850  THR   A OG1 
1119 C CG2 . THR   A 157 ? 0.4683 0.7456 0.8553 0.0381  -0.1004 -0.0977 850  THR   A CG2 
1120 N N   . PRO   A 158 ? 0.4695 0.7236 0.7733 0.0647  -0.1515 -0.0916 851  PRO   A N   
1121 C CA  . PRO   A 158 ? 0.4803 0.7197 0.7572 0.0635  -0.1566 -0.0909 851  PRO   A CA  
1122 C C   . PRO   A 158 ? 0.4833 0.7095 0.7601 0.0422  -0.1388 -0.0919 851  PRO   A C   
1123 O O   . PRO   A 158 ? 0.5010 0.7064 0.7474 0.0422  -0.1373 -0.0843 851  PRO   A O   
1124 C CB  . PRO   A 158 ? 0.4746 0.7373 0.7693 0.0722  -0.1798 -0.1118 851  PRO   A CB  
1125 C CG  . PRO   A 158 ? 0.4642 0.7471 0.7785 0.0884  -0.1916 -0.1154 851  PRO   A CG  
1126 C CD  . PRO   A 158 ? 0.4389 0.7235 0.7736 0.0775  -0.1709 -0.1092 851  PRO   A CD  
1127 N N   . GLN   A 159 ? 0.4701 0.7048 0.7777 0.0250  -0.1240 -0.1009 852  GLN   A N   
1128 C CA  . GLN   A 159 ? 0.4809 0.6956 0.7820 0.0058  -0.1056 -0.1011 852  GLN   A CA  
1129 C C   . GLN   A 159 ? 0.4764 0.6692 0.7602 -0.0003 -0.0862 -0.0838 852  GLN   A C   
1130 O O   . GLN   A 159 ? 0.5005 0.6744 0.7782 -0.0151 -0.0694 -0.0838 852  GLN   A O   
1131 C CB  . GLN   A 159 ? 0.5019 0.7328 0.8420 -0.0118 -0.0999 -0.1253 852  GLN   A CB  
1132 C CG  . GLN   A 159 ? 0.5579 0.8219 0.9463 -0.0141 -0.0995 -0.1402 852  GLN   A CG  
1133 C CD  . GLN   A 159 ? 0.6279 0.9264 1.0402 0.0038  -0.1265 -0.1531 852  GLN   A CD  
1134 O OE1 . GLN   A 159 ? 0.6516 0.9689 1.0824 0.0155  -0.1318 -0.1528 852  GLN   A OE1 
1135 N NE2 . GLN   A 159 ? 0.6310 0.9362 1.0401 0.0079  -0.1451 -0.1650 852  GLN   A NE2 
1136 N N   . HIS   A 160 ? 0.4524 0.6433 0.7227 0.0116  -0.0891 -0.0688 853  HIS   A N   
1137 C CA  . HIS   A 160 ? 0.4475 0.6205 0.7018 0.0072  -0.0748 -0.0542 853  HIS   A CA  
1138 C C   . HIS   A 160 ? 0.4437 0.6095 0.6729 0.0212  -0.0816 -0.0370 853  HIS   A C   
1139 O O   . HIS   A 160 ? 0.4420 0.6175 0.6772 0.0311  -0.0878 -0.0348 853  HIS   A O   
1140 C CB  . HIS   A 160 ? 0.4405 0.6244 0.7216 0.0005  -0.0647 -0.0610 853  HIS   A CB  
1141 C CG  . HIS   A 160 ? 0.4680 0.6316 0.7326 -0.0063 -0.0491 -0.0499 853  HIS   A CG  
1142 N ND1 . HIS   A 160 ? 0.5009 0.6444 0.7325 -0.0029 -0.0491 -0.0337 853  HIS   A ND1 
1143 C CD2 . HIS   A 160 ? 0.4743 0.6363 0.7519 -0.0154 -0.0343 -0.0543 853  HIS   A CD2 
1144 C CE1 . HIS   A 160 ? 0.5122 0.6424 0.7361 -0.0095 -0.0370 -0.0293 853  HIS   A CE1 
1145 N NE2 . HIS   A 160 ? 0.5025 0.6405 0.7503 -0.0172 -0.0266 -0.0406 853  HIS   A NE2 
1146 N N   . VAL   A 161 ? 0.4381 0.5861 0.6404 0.0220  -0.0791 -0.0255 854  VAL   A N   
1147 C CA  . VAL   A 161 ? 0.4320 0.5744 0.6150 0.0322  -0.0822 -0.0111 854  VAL   A CA  
1148 C C   . VAL   A 161 ? 0.4248 0.5555 0.5980 0.0262  -0.0724 -0.0009 854  VAL   A C   
1149 O O   . VAL   A 161 ? 0.4225 0.5430 0.5932 0.0166  -0.0643 -0.0027 854  VAL   A O   
1150 C CB  . VAL   A 161 ? 0.4451 0.5817 0.6087 0.0412  -0.0889 -0.0073 854  VAL   A CB  
1151 C CG1 . VAL   A 161 ? 0.4494 0.5962 0.6181 0.0490  -0.1017 -0.0184 854  VAL   A CG1 
1152 C CG2 . VAL   A 161 ? 0.4537 0.5766 0.6053 0.0354  -0.0829 -0.0062 854  VAL   A CG2 
1153 N N   . LYS   A 162 ? 0.4213 0.5519 0.5882 0.0316  -0.0729 0.0086  855  LYS   A N   
1154 C CA  . LYS   A 162 ? 0.4207 0.5436 0.5807 0.0263  -0.0667 0.0161  855  LYS   A CA  
1155 C C   . LYS   A 162 ? 0.4245 0.5469 0.5745 0.0321  -0.0681 0.0257  855  LYS   A C   
1156 O O   . LYS   A 162 ? 0.4292 0.5541 0.5774 0.0396  -0.0703 0.0283  855  LYS   A O   
1157 C CB  . LYS   A 162 ? 0.4262 0.5505 0.5955 0.0230  -0.0627 0.0146  855  LYS   A CB  
1158 C CG  . LYS   A 162 ? 0.4793 0.6022 0.6594 0.0143  -0.0559 0.0056  855  LYS   A CG  
1159 C CD  . LYS   A 162 ? 0.5402 0.6684 0.7338 0.0153  -0.0529 0.0022  855  LYS   A CD  
1160 C CE  . LYS   A 162 ? 0.6043 0.7253 0.8027 0.0046  -0.0409 -0.0038 855  LYS   A CE  
1161 N NZ  . LYS   A 162 ? 0.6799 0.7824 0.8556 -0.0015 -0.0359 0.0034  855  LYS   A NZ  
1162 N N   . ILE   A 163 ? 0.4228 0.5416 0.5666 0.0290  -0.0662 0.0303  856  ILE   A N   
1163 C CA  . ILE   A 163 ? 0.4292 0.5523 0.5714 0.0325  -0.0658 0.0370  856  ILE   A CA  
1164 C C   . ILE   A 163 ? 0.4349 0.5591 0.5825 0.0274  -0.0626 0.0392  856  ILE   A C   
1165 O O   . ILE   A 163 ? 0.4313 0.5515 0.5791 0.0206  -0.0620 0.0369  856  ILE   A O   
1166 C CB  . ILE   A 163 ? 0.4395 0.5622 0.5771 0.0332  -0.0676 0.0386  856  ILE   A CB  
1167 C CG1 . ILE   A 163 ? 0.4557 0.5724 0.5850 0.0384  -0.0690 0.0364  856  ILE   A CG1 
1168 C CG2 . ILE   A 163 ? 0.4391 0.5725 0.5837 0.0355  -0.0667 0.0429  856  ILE   A CG2 
1169 C CD1 . ILE   A 163 ? 0.4861 0.5947 0.6064 0.0393  -0.0704 0.0370  856  ILE   A CD1 
1170 N N   . THR   A 164 ? 0.4496 0.5753 0.5980 0.0304  -0.0589 0.0434  857  THR   A N   
1171 C CA  . THR   A 164 ? 0.4752 0.5982 0.6274 0.0246  -0.0536 0.0451  857  THR   A CA  
1172 C C   . THR   A 164 ? 0.4979 0.6284 0.6573 0.0215  -0.0489 0.0478  857  THR   A C   
1173 O O   . THR   A 164 ? 0.4996 0.6379 0.6609 0.0260  -0.0497 0.0488  857  THR   A O   
1174 C CB  . THR   A 164 ? 0.4970 0.6096 0.6427 0.0302  -0.0504 0.0468  857  THR   A CB  
1175 O OG1 . THR   A 164 ? 0.5215 0.6265 0.6687 0.0236  -0.0440 0.0478  857  THR   A OG1 
1176 C CG2 . THR   A 164 ? 0.4980 0.6054 0.6328 0.0394  -0.0473 0.0517  857  THR   A CG2 
1177 N N   . ASP   A 165 ? 0.5136 0.6421 0.6790 0.0131  -0.0430 0.0476  858  ASP   A N   
1178 C CA  . ASP   A 165 ? 0.5347 0.6721 0.7133 0.0069  -0.0359 0.0475  858  ASP   A CA  
1179 C C   . ASP   A 165 ? 0.5478 0.7056 0.7424 0.0042  -0.0438 0.0428  858  ASP   A C   
1180 O O   . ASP   A 165 ? 0.5492 0.7213 0.7608 0.0017  -0.0387 0.0414  858  ASP   A O   
1181 C CB  . ASP   A 165 ? 0.5721 0.7043 0.7454 0.0129  -0.0248 0.0528  858  ASP   A CB  
1182 C CG  . ASP   A 165 ? 0.6707 0.7786 0.8262 0.0149  -0.0148 0.0577  858  ASP   A CG  
1183 O OD1 . ASP   A 165 ? 0.6880 0.7851 0.8342 0.0174  -0.0199 0.0574  858  ASP   A OD1 
1184 O OD2 . ASP   A 165 ? 0.7162 0.8140 0.8655 0.0153  -0.0010 0.0617  858  ASP   A OD2 
1185 N N   . PHE   A 166 ? 0.5577 0.7161 0.7468 0.0052  -0.0555 0.0400  859  PHE   A N   
1186 C CA  . PHE   A 166 ? 0.5744 0.7483 0.7732 0.0056  -0.0658 0.0355  859  PHE   A CA  
1187 C C   . PHE   A 166 ? 0.5979 0.7794 0.8104 -0.0063 -0.0671 0.0290  859  PHE   A C   
1188 O O   . PHE   A 166 ? 0.6084 0.7753 0.8128 -0.0141 -0.0631 0.0281  859  PHE   A O   
1189 C CB  . PHE   A 166 ? 0.5816 0.7448 0.7614 0.0112  -0.0761 0.0353  859  PHE   A CB  
1190 C CG  . PHE   A 166 ? 0.5952 0.7392 0.7587 0.0056  -0.0748 0.0344  859  PHE   A CG  
1191 C CD1 . PHE   A 166 ? 0.6025 0.7417 0.7613 -0.0017 -0.0793 0.0298  859  PHE   A CD1 
1192 C CD2 . PHE   A 166 ? 0.6106 0.7424 0.7649 0.0081  -0.0692 0.0367  859  PHE   A CD2 
1193 C CE1 . PHE   A 166 ? 0.6192 0.7395 0.7632 -0.0066 -0.0751 0.0285  859  PHE   A CE1 
1194 C CE2 . PHE   A 166 ? 0.6260 0.7437 0.7712 0.0033  -0.0660 0.0345  859  PHE   A CE2 
1195 C CZ  . PHE   A 166 ? 0.6248 0.7355 0.7638 -0.0039 -0.0677 0.0310  859  PHE   A CZ  
1196 N N   . GLY   A 167 ? 0.6023 0.8073 0.8383 -0.0080 -0.0713 0.0234  860  GLY   A N   
1197 C CA  . GLY   A 167 ? 0.6157 0.8318 0.8695 -0.0208 -0.0737 0.0143  860  GLY   A CA  
1198 C C   . GLY   A 167 ? 0.6373 0.8506 0.9048 -0.0334 -0.0556 0.0136  860  GLY   A C   
1199 O O   . GLY   A 167 ? 0.6263 0.8501 0.9133 -0.0464 -0.0550 0.0043  860  GLY   A O   
1200 N N   . LEU   A 168 ? 0.6678 0.8643 0.9230 -0.0295 -0.0407 0.0227  861  LEU   A N   
1201 C CA  . LEU   A 168 ? 0.6961 0.8804 0.9548 -0.0391 -0.0211 0.0241  861  LEU   A CA  
1202 C C   . LEU   A 168 ? 0.7159 0.9233 1.0069 -0.0461 -0.0101 0.0188  861  LEU   A C   
1203 O O   . LEU   A 168 ? 0.7150 0.9191 1.0193 -0.0609 0.0043  0.0141  861  LEU   A O   
1204 C CB  . LEU   A 168 ? 0.7087 0.8658 0.9393 -0.0293 -0.0111 0.0353  861  LEU   A CB  
1205 C CG  . LEU   A 168 ? 0.7327 0.8651 0.9537 -0.0357 0.0090  0.0392  861  LEU   A CG  
1206 C CD1 . LEU   A 168 ? 0.7458 0.8644 0.9650 -0.0480 0.0107  0.0343  861  LEU   A CD1 
1207 C CD2 . LEU   A 168 ? 0.7551 0.8624 0.9456 -0.0214 0.0134  0.0495  861  LEU   A CD2 
1208 N N   . ALA   A 169 ? 0.7275 0.9580 1.0327 -0.0361 -0.0155 0.0183  862  ALA   A N   
1209 C CA  . ALA   A 169 ? 0.7320 0.9896 1.0733 -0.0411 -0.0049 0.0117  862  ALA   A CA  
1210 C C   . ALA   A 169 ? 0.7377 1.0253 1.1164 -0.0545 -0.0145 -0.0038 862  ALA   A C   
1211 O O   . ALA   A 169 ? 0.7304 1.0281 1.1373 -0.0701 0.0016  -0.0117 862  ALA   A O   
1212 C CB  . ALA   A 169 ? 0.7260 1.0001 1.0720 -0.0246 -0.0104 0.0143  862  ALA   A CB  
1213 N N   . LYS   A 170 ? 0.7514 1.0495 1.1272 -0.0493 -0.0400 -0.0090 863  LYS   A N   
1214 C CA  . LYS   A 170 ? 0.7546 1.0798 1.1605 -0.0597 -0.0545 -0.0251 863  LYS   A CA  
1215 C C   . LYS   A 170 ? 0.7773 1.0864 1.1833 -0.0808 -0.0443 -0.0311 863  LYS   A C   
1216 O O   . LYS   A 170 ? 0.7646 1.0979 1.2069 -0.0960 -0.0446 -0.0463 863  LYS   A O   
1217 C CB  . LYS   A 170 ? 0.7886 1.1173 1.1772 -0.0468 -0.0839 -0.0272 863  LYS   A CB  
1218 C CG  . LYS   A 170 ? 0.8213 1.1839 1.2418 -0.0519 -0.1045 -0.0453 863  LYS   A CG  
1219 C CD  . LYS   A 170 ? 0.8842 1.2431 1.2783 -0.0361 -0.1334 -0.0462 863  LYS   A CD  
1220 N N   . LEU   A 171 ? 0.8114 1.0802 1.1787 -0.0816 -0.0352 -0.0203 864  LEU   A N   
1221 C CA  . LEU   A 171 ? 0.8349 1.0797 1.1947 -0.0990 -0.0232 -0.0238 864  LEU   A CA  
1222 C C   . LEU   A 171 ? 0.8438 1.0872 1.2260 -0.1139 0.0047  -0.0261 864  LEU   A C   
1223 O O   . LEU   A 171 ? 0.8463 1.0878 1.2450 -0.1338 0.0134  -0.0372 864  LEU   A O   
1224 C CB  . LEU   A 171 ? 0.8645 1.0678 1.1785 -0.0909 -0.0191 -0.0104 864  LEU   A CB  
1225 C CG  . LEU   A 171 ? 0.8955 1.0659 1.1942 -0.1041 -0.0041 -0.0108 864  LEU   A CG  
1226 C CD1 . LEU   A 171 ? 0.8984 1.0729 1.2032 -0.1170 -0.0168 -0.0247 864  LEU   A CD1 
1227 C CD2 . LEU   A 171 ? 0.9285 1.0638 1.1878 -0.0914 0.0002  0.0028  864  LEU   A CD2 
1228 N N   . LEU   A 172 ? 0.8493 1.0904 1.2297 -0.1051 0.0203  -0.0162 865  LEU   A N   
1229 C CA  . LEU   A 172 ? 0.8568 1.0899 1.2511 -0.1175 0.0507  -0.0164 865  LEU   A CA  
1230 C C   . LEU   A 172 ? 0.8337 1.1124 1.2856 -0.1299 0.0551  -0.0327 865  LEU   A C   
1231 O O   . LEU   A 172 ? 0.8300 1.1055 1.3033 -0.1491 0.0803  -0.0396 865  LEU   A O   
1232 C CB  . LEU   A 172 ? 0.8745 1.0826 1.2377 -0.1019 0.0659  0.0004  865  LEU   A CB  
1233 C CG  . LEU   A 172 ? 0.9183 1.0821 1.2296 -0.0904 0.0649  0.0147  865  LEU   A CG  
1234 C CD1 . LEU   A 172 ? 0.9401 1.0852 1.2228 -0.0732 0.0742  0.0285  865  LEU   A CD1 
1235 C CD2 . LEU   A 172 ? 0.9408 1.0684 1.2359 -0.1043 0.0819  0.0148  865  LEU   A CD2 
1236 N N   . GLY   A 173 ? 0.8149 1.1346 1.2920 -0.1184 0.0319  -0.0392 866  GLY   A N   
1237 C CA  . GLY   A 173 ? 0.7838 1.1541 1.3209 -0.1259 0.0319  -0.0562 866  GLY   A CA  
1238 C C   . GLY   A 173 ? 0.7778 1.1637 1.3272 -0.1120 0.0435  -0.0504 866  GLY   A C   
1239 O O   . GLY   A 173 ? 0.7948 1.1637 1.3087 -0.0914 0.0370  -0.0358 866  GLY   A O   
1240 N N   . LYS   A 185 ? 0.8284 0.8852 1.0335 -0.0439 0.2237  0.0620  878  LYS   A N   
1241 C CA  . LYS   A 185 ? 0.8326 0.8972 1.0279 -0.0266 0.2218  0.0647  878  LYS   A CA  
1242 C C   . LYS   A 185 ? 0.7971 0.9104 1.0258 -0.0174 0.1874  0.0579  878  LYS   A C   
1243 O O   . LYS   A 185 ? 0.8075 0.9194 1.0203 -0.0089 0.1586  0.0610  878  LYS   A O   
1244 C CB  . LYS   A 185 ? 0.9016 0.9114 1.0225 -0.0067 0.2228  0.0795  878  LYS   A CB  
1245 N N   . VAL   A 186 ? 0.7510 0.9056 1.0257 -0.0186 0.1921  0.0483  879  VAL   A N   
1246 C CA  . VAL   A 186 ? 0.7131 0.9102 1.0176 -0.0081 0.1627  0.0419  879  VAL   A CA  
1247 C C   . VAL   A 186 ? 0.7147 0.8911 0.9752 0.0141  0.1517  0.0507  879  VAL   A C   
1248 O O   . VAL   A 186 ? 0.7395 0.8888 0.9699 0.0211  0.1732  0.0563  879  VAL   A O   
1249 C CB  . VAL   A 186 ? 0.6822 0.9301 1.0522 -0.0150 0.1718  0.0277  879  VAL   A CB  
1250 N N   . PRO   A 187 ? 0.6860 0.8702 0.9382 0.0246  0.1199  0.0517  880  PRO   A N   
1251 C CA  . PRO   A 187 ? 0.6856 0.8487 0.8970 0.0430  0.1096  0.0580  880  PRO   A CA  
1252 C C   . PRO   A 187 ? 0.6492 0.8350 0.8792 0.0545  0.1093  0.0532  880  PRO   A C   
1253 O O   . PRO   A 187 ? 0.6471 0.8434 0.8771 0.0644  0.0865  0.0517  880  PRO   A O   
1254 C CB  . PRO   A 187 ? 0.6977 0.8588 0.8967 0.0457  0.0799  0.0596  880  PRO   A CB  
1255 C CG  . PRO   A 187 ? 0.6832 0.8781 0.9267 0.0337  0.0696  0.0517  880  PRO   A CG  
1256 C CD  . PRO   A 187 ? 0.6559 0.8647 0.9326 0.0191  0.0936  0.0463  880  PRO   A CD  
1257 N N   . ILE   A 188 ? 0.6154 0.8050 0.8588 0.0533  0.1371  0.0508  881  ILE   A N   
1258 C CA  . ILE   A 188 ? 0.5833 0.7940 0.8477 0.0644  0.1435  0.0454  881  ILE   A CA  
1259 C C   . ILE   A 188 ? 0.5763 0.7664 0.8007 0.0832  0.1288  0.0497  881  ILE   A C   
1260 O O   . ILE   A 188 ? 0.5561 0.7684 0.8004 0.0937  0.1166  0.0448  881  ILE   A O   
1261 C CB  . ILE   A 188 ? 0.5868 0.7920 0.8599 0.0589  0.1828  0.0437  881  ILE   A CB  
1262 C CG1 . ILE   A 188 ? 0.5743 0.8003 0.8912 0.0371  0.1992  0.0372  881  ILE   A CG1 
1263 C CG2 . ILE   A 188 ? 0.5771 0.8064 0.8763 0.0711  0.1922  0.0370  881  ILE   A CG2 
1264 N N   . LYS   A 189 ? 0.5868 0.7336 0.7546 0.0879  0.1286  0.0579  882  LYS   A N   
1265 C CA  . LYS   A 189 ? 0.5887 0.7135 0.7170 0.1034  0.1156  0.0599  882  LYS   A CA  
1266 C C   . LYS   A 189 ? 0.5543 0.6885 0.6845 0.1065  0.0832  0.0582  882  LYS   A C   
1267 O O   . LYS   A 189 ? 0.5662 0.6842 0.6688 0.1172  0.0724  0.0579  882  LYS   A O   
1268 C CB  . LYS   A 189 ? 0.6555 0.7329 0.7239 0.1081  0.1244  0.0670  882  LYS   A CB  
1269 C CG  . LYS   A 189 ? 0.7266 0.7876 0.7845 0.1082  0.1597  0.0686  882  LYS   A CG  
1270 C CD  . LYS   A 189 ? 0.8328 0.8418 0.8264 0.1130  0.1705  0.0767  882  LYS   A CD  
1271 C CE  . LYS   A 189 ? 0.8873 0.8752 0.8664 0.1131  0.2094  0.0784  882  LYS   A CE  
1272 N NZ  . LYS   A 189 ? 0.9614 0.8912 0.8635 0.1250  0.2170  0.0858  882  LYS   A NZ  
1273 N N   . TRP   A 190 ? 0.5143 0.6725 0.6761 0.0966  0.0697  0.0562  883  TRP   A N   
1274 C CA  . TRP   A 190 ? 0.4957 0.6622 0.6611 0.0981  0.0428  0.0544  883  TRP   A CA  
1275 C C   . TRP   A 190 ? 0.4741 0.6764 0.6830 0.0990  0.0344  0.0485  883  TRP   A C   
1276 O O   . TRP   A 190 ? 0.4713 0.6763 0.6790 0.1030  0.0147  0.0472  883  TRP   A O   
1277 C CB  . TRP   A 190 ? 0.4849 0.6435 0.6421 0.0877  0.0316  0.0571  883  TRP   A CB  
1278 C CG  . TRP   A 190 ? 0.4931 0.6195 0.6071 0.0918  0.0272  0.0612  883  TRP   A CG  
1279 C CD1 . TRP   A 190 ? 0.5029 0.6194 0.5988 0.0957  0.0086  0.0597  883  TRP   A CD1 
1280 C CD2 . TRP   A 190 ? 0.5018 0.6013 0.5851 0.0932  0.0415  0.0662  883  TRP   A CD2 
1281 N NE1 . TRP   A 190 ? 0.5250 0.6154 0.5854 0.1000  0.0078  0.0619  883  TRP   A NE1 
1282 C CE2 . TRP   A 190 ? 0.5294 0.6065 0.5775 0.1002  0.0269  0.0668  883  TRP   A CE2 
1283 C CE3 . TRP   A 190 ? 0.5061 0.5963 0.5869 0.0894  0.0661  0.0697  883  TRP   A CE3 
1284 C CZ2 . TRP   A 190 ? 0.5599 0.6056 0.5677 0.1063  0.0326  0.0713  883  TRP   A CZ2 
1285 C CZ3 . TRP   A 190 ? 0.5454 0.5985 0.5810 0.0948  0.0754  0.0756  883  TRP   A CZ3 
1286 C CH2 . TRP   A 190 ? 0.5654 0.5966 0.5638 0.1045  0.0569  0.0766  883  TRP   A CH2 
1287 N N   . MET   A 191 ? 0.4609 0.6898 0.7078 0.0951  0.0491  0.0441  884  MET   A N   
1288 C CA  . MET   A 191 ? 0.4536 0.7213 0.7465 0.0969  0.0401  0.0364  884  MET   A CA  
1289 C C   . MET   A 191 ? 0.4591 0.7370 0.7604 0.1150  0.0387  0.0330  884  MET   A C   
1290 O O   . MET   A 191 ? 0.4648 0.7303 0.7533 0.1228  0.0565  0.0341  884  MET   A O   
1291 C CB  . MET   A 191 ? 0.4464 0.7421 0.7828 0.0835  0.0571  0.0302  884  MET   A CB  
1292 C CG  . MET   A 191 ? 0.4955 0.7872 0.8327 0.0658  0.0541  0.0311  884  MET   A CG  
1293 S SD  . MET   A 191 ? 0.6105 0.9191 0.9862 0.0464  0.0835  0.0248  884  MET   A SD  
1294 C CE  . MET   A 191 ? 0.5342 0.9007 0.9776 0.0501  0.0782  0.0099  884  MET   A CE  
1295 N N   . ALA   A 192 ? 0.4552 0.7538 0.7763 0.1227  0.0178  0.0287  885  ALA   A N   
1296 C CA  . ALA   A 192 ? 0.4639 0.7746 0.7970 0.1422  0.0137  0.0249  885  ALA   A CA  
1297 C C   . ALA   A 192 ? 0.4547 0.8037 0.8390 0.1436  0.0320  0.0162  885  ALA   A C   
1298 O O   . ALA   A 192 ? 0.4420 0.8153 0.8602 0.1280  0.0401  0.0112  885  ALA   A O   
1299 C CB  . ALA   A 192 ? 0.4588 0.7790 0.7968 0.1505  -0.0141 0.0228  885  ALA   A CB  
1300 N N   . LEU   A 193 ? 0.4586 0.8131 0.8506 0.1615  0.0403  0.0134  886  LEU   A N   
1301 C CA  . LEU   A 193 ? 0.4400 0.8330 0.8845 0.1641  0.0602  0.0037  886  LEU   A CA  
1302 C C   . LEU   A 193 ? 0.4177 0.8644 0.9251 0.1592  0.0472  -0.0082 886  LEU   A C   
1303 O O   . LEU   A 193 ? 0.3987 0.8753 0.9508 0.1459  0.0668  -0.0165 886  LEU   A O   
1304 C CB  . LEU   A 193 ? 0.4428 0.8331 0.8848 0.1881  0.0666  0.0019  886  LEU   A CB  
1305 C CG  . LEU   A 193 ? 0.4255 0.8543 0.9219 0.1926  0.0916  -0.0088 886  LEU   A CG  
1306 C CD1 . LEU   A 193 ? 0.4418 0.8521 0.9261 0.1765  0.1276  -0.0061 886  LEU   A CD1 
1307 C CD2 . LEU   A 193 ? 0.4259 0.8553 0.9233 0.2199  0.0920  -0.0115 886  LEU   A CD2 
1308 N N   . GLU   A 194 ? 0.4214 0.8772 0.9297 0.1684  0.0148  -0.0097 887  GLU   A N   
1309 C CA  . GLU   A 194 ? 0.3994 0.9048 0.9627 0.1658  -0.0031 -0.0223 887  GLU   A CA  
1310 C C   . GLU   A 194 ? 0.4054 0.9169 0.9801 0.1377  0.0000  -0.0245 887  GLU   A C   
1311 O O   . GLU   A 194 ? 0.3745 0.9311 1.0052 0.1286  -0.0022 -0.0382 887  GLU   A O   
1312 C CB  . GLU   A 194 ? 0.4262 0.9326 0.9775 0.1862  -0.0391 -0.0227 887  GLU   A CB  
1313 C CG  . GLU   A 194 ? 0.5245 0.9917 1.0230 0.1784  -0.0579 -0.0127 887  GLU   A CG  
1314 C CD  . GLU   A 194 ? 0.6463 1.0580 1.0801 0.1859  -0.0556 0.0010  887  GLU   A CD  
1315 O OE1 . GLU   A 194 ? 0.6766 1.0747 1.1002 0.1945  -0.0372 0.0038  887  GLU   A OE1 
1316 O OE2 . GLU   A 194 ? 0.6763 1.0577 1.0702 0.1824  -0.0712 0.0076  887  GLU   A OE2 
1317 N N   . SER   A 195 ? 0.4427 0.9096 0.9665 0.1242  0.0055  -0.0124 888  SER   A N   
1318 C CA  . SER   A 195 ? 0.4525 0.9173 0.9803 0.0990  0.0112  -0.0130 888  SER   A CA  
1319 C C   . SER   A 195 ? 0.4526 0.9242 1.0046 0.0836  0.0470  -0.0163 888  SER   A C   
1320 O O   . SER   A 195 ? 0.4383 0.9297 1.0235 0.0639  0.0546  -0.0243 888  SER   A O   
1321 C CB  . SER   A 195 ? 0.5067 0.9220 0.9731 0.0931  0.0054  0.0005  888  SER   A CB  
1322 O OG  . SER   A 195 ? 0.5446 0.9484 0.9857 0.1051  -0.0230 0.0037  888  SER   A OG  
1323 N N   . ILE   A 196 ? 0.4719 0.9234 1.0044 0.0919  0.0704  -0.0106 889  ILE   A N   
1324 C CA  . ILE   A 196 ? 0.4818 0.9322 1.0292 0.0792  0.1083  -0.0127 889  ILE   A CA  
1325 C C   . ILE   A 196 ? 0.4495 0.9583 1.0747 0.0764  0.1187  -0.0302 889  ILE   A C   
1326 O O   . ILE   A 196 ? 0.4374 0.9621 1.0973 0.0550  0.1401  -0.0381 889  ILE   A O   
1327 C CB  . ILE   A 196 ? 0.5171 0.9281 1.0177 0.0918  0.1288  -0.0027 889  ILE   A CB  
1328 C CG1 . ILE   A 196 ? 0.5710 0.9279 0.9991 0.0937  0.1175  0.0121  889  ILE   A CG1 
1329 C CG2 . ILE   A 196 ? 0.5194 0.9262 1.0323 0.0805  0.1710  -0.0050 889  ILE   A CG2 
1330 C CD1 . ILE   A 196 ? 0.6121 0.9308 0.9914 0.1080  0.1303  0.0198  889  ILE   A CD1 
1331 N N   . LEU   A 197 ? 0.4336 0.9748 1.0881 0.0980  0.1030  -0.0375 890  LEU   A N   
1332 C CA  . LEU   A 197 ? 0.3986 1.0006 1.1318 0.0999  0.1105  -0.0560 890  LEU   A CA  
1333 C C   . LEU   A 197 ? 0.3854 1.0379 1.1751 0.0911  0.0852  -0.0717 890  LEU   A C   
1334 O O   . LEU   A 197 ? 0.3558 1.0582 1.2163 0.0806  0.0993  -0.0894 890  LEU   A O   
1335 C CB  . LEU   A 197 ? 0.3865 1.0028 1.1288 0.1304  0.1040  -0.0583 890  LEU   A CB  
1336 C CG  . LEU   A 197 ? 0.4272 0.9963 1.1161 0.1421  0.1273  -0.0456 890  LEU   A CG  
1337 C CD1 . LEU   A 197 ? 0.4195 1.0032 1.1194 0.1728  0.1181  -0.0492 890  LEU   A CD1 
1338 C CD2 . LEU   A 197 ? 0.4310 0.9904 1.1268 0.1250  0.1734  -0.0466 890  LEU   A CD2 
1339 N N   . HIS   A 198 ? 0.4042 1.0467 1.1663 0.0965  0.0479  -0.0674 891  HIS   A N   
1340 C CA  . HIS   A 198 ? 0.3853 1.0742 1.1957 0.0916  0.0196  -0.0834 891  HIS   A CA  
1341 C C   . HIS   A 198 ? 0.4059 1.0705 1.1834 0.0748  0.0016  -0.0787 891  HIS   A C   
1342 O O   . HIS   A 198 ? 0.3870 1.0833 1.1933 0.0735  -0.0264 -0.0912 891  HIS   A O   
1343 C CB  . HIS   A 198 ? 0.3927 1.1094 1.2178 0.1230  -0.0147 -0.0893 891  HIS   A CB  
1344 C CG  . HIS   A 198 ? 0.4186 1.1632 1.2808 0.1430  0.0004  -0.0957 891  HIS   A CG  
1345 N ND1 . HIS   A 198 ? 0.4756 1.1867 1.2923 0.1686  -0.0001 -0.0829 891  HIS   A ND1 
1346 C CD2 . HIS   A 198 ? 0.3930 1.1936 1.3330 0.1392  0.0194  -0.1142 891  HIS   A CD2 
1347 C CE1 . HIS   A 198 ? 0.4545 1.2012 1.3205 0.1817  0.0171  -0.0933 891  HIS   A CE1 
1348 N NE2 . HIS   A 198 ? 0.4090 1.2117 1.3518 0.1648  0.0299  -0.1124 891  HIS   A NE2 
1349 N N   . ARG   A 199 ? 0.4415 1.0500 1.1580 0.0638  0.0159  -0.0617 892  ARG   A N   
1350 C CA  . ARG   A 199 ? 0.4627 1.0433 1.1436 0.0493  0.0015  -0.0559 892  ARG   A CA  
1351 C C   . ARG   A 199 ? 0.4632 1.0412 1.1206 0.0662  -0.0388 -0.0546 892  ARG   A C   
1352 O O   . ARG   A 199 ? 0.4711 1.0518 1.1274 0.0559  -0.0577 -0.0595 892  ARG   A O   
1353 C CB  . ARG   A 199 ? 0.4621 1.0652 1.1851 0.0207  0.0127  -0.0691 892  ARG   A CB  
1354 C CG  . ARG   A 199 ? 0.5093 1.0885 1.2273 0.0010  0.0555  -0.0642 892  ARG   A CG  
1355 N N   . ILE   A 200 ? 0.4553 1.0238 1.0901 0.0923  -0.0503 -0.0479 893  ILE   A N   
1356 C CA  . ILE   A 200 ? 0.4565 1.0125 1.0594 0.1106  -0.0843 -0.0445 893  ILE   A CA  
1357 C C   . ILE   A 200 ? 0.4834 0.9798 1.0152 0.1081  -0.0830 -0.0267 893  ILE   A C   
1358 O O   . ILE   A 200 ? 0.5040 0.9713 1.0060 0.1133  -0.0661 -0.0159 893  ILE   A O   
1359 C CB  . ILE   A 200 ? 0.4548 1.0288 1.0704 0.1409  -0.0964 -0.0474 893  ILE   A CB  
1360 C CG1 . ILE   A 200 ? 0.4218 1.0626 1.1148 0.1456  -0.1041 -0.0682 893  ILE   A CG1 
1361 C CG2 . ILE   A 200 ? 0.4884 1.0312 1.0529 0.1612  -0.1257 -0.0394 893  ILE   A CG2 
1362 N N   . TYR   A 201 ? 0.4802 0.9595 0.9864 0.0996  -0.1003 -0.0250 894  TYR   A N   
1363 C CA  . TYR   A 201 ? 0.5056 0.9336 0.9516 0.0963  -0.0994 -0.0106 894  TYR   A CA  
1364 C C   . TYR   A 201 ? 0.5081 0.9176 0.9198 0.1106  -0.1264 -0.0080 894  TYR   A C   
1365 O O   . TYR   A 201 ? 0.5018 0.9262 0.9230 0.1095  -0.1467 -0.0162 894  TYR   A O   
1366 C CB  . TYR   A 201 ? 0.5120 0.9265 0.9513 0.0716  -0.0882 -0.0091 894  TYR   A CB  
1367 C CG  . TYR   A 201 ? 0.5195 0.9362 0.9758 0.0582  -0.0580 -0.0080 894  TYR   A CG  
1368 C CD1 . TYR   A 201 ? 0.5564 0.9378 0.9762 0.0592  -0.0406 0.0042  894  TYR   A CD1 
1369 C CD2 . TYR   A 201 ? 0.5070 0.9578 1.0133 0.0437  -0.0464 -0.0199 894  TYR   A CD2 
1370 C CE1 . TYR   A 201 ? 0.5696 0.9456 0.9956 0.0487  -0.0129 0.0062  894  TYR   A CE1 
1371 C CE2 . TYR   A 201 ? 0.5195 0.9642 1.0346 0.0305  -0.0152 -0.0180 894  TYR   A CE2 
1372 C CZ  . TYR   A 201 ? 0.5598 0.9650 1.0314 0.0343  0.0014  -0.0040 894  TYR   A CZ  
1373 O OH  . TYR   A 201 ? 0.5893 0.9823 1.0615 0.0235  0.0321  -0.0014 894  TYR   A OH  
1374 N N   . THR   A 202 ? 0.5164 0.8909 0.8860 0.1244  -0.1260 0.0026  895  THR   A N   
1375 C CA  . THR   A 202 ? 0.5270 0.8728 0.8549 0.1388  -0.1461 0.0071  895  THR   A CA  
1376 C C   . THR   A 202 ? 0.5447 0.8415 0.8220 0.1333  -0.1353 0.0192  895  THR   A C   
1377 O O   . THR   A 202 ? 0.5458 0.8353 0.8228 0.1213  -0.1161 0.0232  895  THR   A O   
1378 C CB  . THR   A 202 ? 0.5340 0.8903 0.8685 0.1664  -0.1571 0.0049  895  THR   A CB  
1379 O OG1 . THR   A 202 ? 0.5584 0.8975 0.8812 0.1732  -0.1385 0.0117  895  THR   A OG1 
1380 C CG2 . THR   A 202 ? 0.4951 0.9071 0.8889 0.1732  -0.1668 -0.0093 895  THR   A CG2 
1381 N N   . HIS   A 203 ? 0.5591 0.8214 0.7932 0.1424  -0.1472 0.0242  896  HIS   A N   
1382 C CA  . HIS   A 203 ? 0.5806 0.7998 0.7729 0.1375  -0.1363 0.0330  896  HIS   A CA  
1383 C C   . HIS   A 203 ? 0.5691 0.7795 0.7572 0.1483  -0.1241 0.0364  896  HIS   A C   
1384 O O   . HIS   A 203 ? 0.5854 0.7731 0.7547 0.1399  -0.1109 0.0407  896  HIS   A O   
1385 C CB  . HIS   A 203 ? 0.6229 0.8052 0.7706 0.1430  -0.1481 0.0366  896  HIS   A CB  
1386 C CG  . HIS   A 203 ? 0.6478 0.8338 0.7938 0.1320  -0.1584 0.0330  896  HIS   A CG  
1387 N ND1 . HIS   A 203 ? 0.6697 0.8601 0.8092 0.1440  -0.1797 0.0287  896  HIS   A ND1 
1388 C CD2 . HIS   A 203 ? 0.6599 0.8453 0.8093 0.1115  -0.1505 0.0325  896  HIS   A CD2 
1389 C CE1 . HIS   A 203 ? 0.6794 0.8704 0.8169 0.1289  -0.1833 0.0253  896  HIS   A CE1 
1390 N NE2 . HIS   A 203 ? 0.6755 0.8636 0.8198 0.1091  -0.1652 0.0277  896  HIS   A NE2 
1391 N N   . GLN   A 204 ? 0.5365 0.7680 0.7458 0.1667  -0.1282 0.0330  897  GLN   A N   
1392 C CA  . GLN   A 204 ? 0.5289 0.7523 0.7350 0.1778  -0.1154 0.0351  897  GLN   A CA  
1393 C C   . GLN   A 204 ? 0.5033 0.7473 0.7367 0.1662  -0.0959 0.0335  897  GLN   A C   
1394 O O   . GLN   A 204 ? 0.5309 0.7542 0.7461 0.1671  -0.0823 0.0369  897  GLN   A O   
1395 C CB  . GLN   A 204 ? 0.5305 0.7636 0.7447 0.2043  -0.1260 0.0324  897  GLN   A CB  
1396 C CG  . GLN   A 204 ? 0.5846 0.7798 0.7540 0.2187  -0.1420 0.0368  897  GLN   A CG  
1397 C CD  . GLN   A 204 ? 0.6808 0.8220 0.7993 0.2114  -0.1314 0.0444  897  GLN   A CD  
1398 O OE1 . GLN   A 204 ? 0.7179 0.8375 0.8208 0.2177  -0.1195 0.0467  897  GLN   A OE1 
1399 N NE2 . GLN   A 204 ? 0.6955 0.8145 0.7888 0.1970  -0.1344 0.0471  897  GLN   A NE2 
1400 N N   . SER   A 205 ? 0.4545 0.7332 0.7259 0.1541  -0.0936 0.0282  898  SER   A N   
1401 C CA  . SER   A 205 ? 0.4317 0.7205 0.7201 0.1415  -0.0723 0.0281  898  SER   A CA  
1402 C C   . SER   A 205 ? 0.4284 0.6864 0.6845 0.1255  -0.0654 0.0345  898  SER   A C   
1403 O O   . SER   A 205 ? 0.4289 0.6774 0.6775 0.1208  -0.0492 0.0371  898  SER   A O   
1404 C CB  . SER   A 205 ? 0.4279 0.7595 0.7665 0.1324  -0.0686 0.0197  898  SER   A CB  
1405 O OG  . SER   A 205 ? 0.4674 0.8037 0.8094 0.1181  -0.0796 0.0175  898  SER   A OG  
1406 N N   . ASP   A 206 ? 0.4268 0.6679 0.6617 0.1189  -0.0780 0.0365  899  ASP   A N   
1407 C CA  . ASP   A 206 ? 0.4355 0.6495 0.6426 0.1066  -0.0740 0.0410  899  ASP   A CA  
1408 C C   . ASP   A 206 ? 0.4503 0.6343 0.6257 0.1139  -0.0700 0.0442  899  ASP   A C   
1409 O O   . ASP   A 206 ? 0.4685 0.6369 0.6284 0.1063  -0.0631 0.0458  899  ASP   A O   
1410 C CB  . ASP   A 206 ? 0.4662 0.6702 0.6606 0.0993  -0.0868 0.0409  899  ASP   A CB  
1411 C CG  . ASP   A 206 ? 0.5229 0.7462 0.7392 0.0856  -0.0880 0.0377  899  ASP   A CG  
1412 O OD1 . ASP   A 206 ? 0.5219 0.7597 0.7586 0.0779  -0.0757 0.0368  899  ASP   A OD1 
1413 O OD2 . ASP   A 206 ? 0.5477 0.7677 0.7574 0.0824  -0.1001 0.0358  899  ASP   A OD2 
1414 N N   . VAL   A 207 ? 0.4468 0.6211 0.6114 0.1290  -0.0756 0.0441  900  VAL   A N   
1415 C CA  . VAL   A 207 ? 0.4620 0.6062 0.5973 0.1361  -0.0711 0.0455  900  VAL   A CA  
1416 C C   . VAL   A 207 ? 0.4554 0.6033 0.5948 0.1383  -0.0570 0.0449  900  VAL   A C   
1417 O O   . VAL   A 207 ? 0.4788 0.6042 0.5950 0.1342  -0.0518 0.0449  900  VAL   A O   
1418 C CB  . VAL   A 207 ? 0.4799 0.6092 0.6005 0.1535  -0.0792 0.0461  900  VAL   A CB  
1419 C CG1 . VAL   A 207 ? 0.5033 0.6039 0.5986 0.1621  -0.0710 0.0462  900  VAL   A CG1 
1420 C CG2 . VAL   A 207 ? 0.4984 0.6070 0.5969 0.1495  -0.0901 0.0478  900  VAL   A CG2 
1421 N N   . TRP   A 208 ? 0.4193 0.5958 0.5887 0.1435  -0.0501 0.0432  901  TRP   A N   
1422 C CA  . TRP   A 208 ? 0.4103 0.5886 0.5819 0.1447  -0.0331 0.0429  901  TRP   A CA  
1423 C C   . TRP   A 208 ? 0.4179 0.5854 0.5759 0.1301  -0.0271 0.0452  901  TRP   A C   
1424 O O   . TRP   A 208 ? 0.4452 0.5901 0.5765 0.1315  -0.0214 0.0456  901  TRP   A O   
1425 C CB  . TRP   A 208 ? 0.3790 0.5926 0.5910 0.1491  -0.0240 0.0396  901  TRP   A CB  
1426 C CG  . TRP   A 208 ? 0.3748 0.5859 0.5857 0.1508  -0.0024 0.0395  901  TRP   A CG  
1427 C CD1 . TRP   A 208 ? 0.3891 0.5865 0.5838 0.1401  0.0102  0.0424  901  TRP   A CD1 
1428 C CD2 . TRP   A 208 ? 0.3662 0.5853 0.5887 0.1656  0.0101  0.0364  901  TRP   A CD2 
1429 N NE1 . TRP   A 208 ? 0.3956 0.5885 0.5867 0.1467  0.0304  0.0417  901  TRP   A NE1 
1430 C CE2 . TRP   A 208 ? 0.3841 0.5917 0.5944 0.1616  0.0318  0.0376  901  TRP   A CE2 
1431 C CE3 . TRP   A 208 ? 0.3582 0.5938 0.6014 0.1830  0.0055  0.0323  901  TRP   A CE3 
1432 C CZ2 . TRP   A 208 ? 0.3914 0.6021 0.6087 0.1730  0.0511  0.0348  901  TRP   A CZ2 
1433 C CZ3 . TRP   A 208 ? 0.3646 0.6056 0.6178 0.1954  0.0233  0.0291  901  TRP   A CZ3 
1434 C CH2 . TRP   A 208 ? 0.3774 0.6063 0.6182 0.1894  0.0469  0.0302  901  TRP   A CH2 
1435 N N   . SER   A 209 ? 0.3984 0.5795 0.5717 0.1174  -0.0303 0.0459  902  SER   A N   
1436 C CA  . SER   A 209 ? 0.4044 0.5744 0.5649 0.1056  -0.0263 0.0484  902  SER   A CA  
1437 C C   . SER   A 209 ? 0.4083 0.5530 0.5390 0.1038  -0.0351 0.0483  902  SER   A C   
1438 O O   . SER   A 209 ? 0.4202 0.5515 0.5335 0.1010  -0.0319 0.0491  902  SER   A O   
1439 C CB  . SER   A 209 ? 0.4114 0.5982 0.5934 0.0933  -0.0295 0.0483  902  SER   A CB  
1440 O OG  . SER   A 209 ? 0.4377 0.6522 0.6535 0.0931  -0.0227 0.0454  902  SER   A OG  
1441 N N   . TYR   A 210 ? 0.4014 0.5388 0.5262 0.1054  -0.0459 0.0468  903  TYR   A N   
1442 C CA  . TYR   A 210 ? 0.4207 0.5353 0.5224 0.1019  -0.0518 0.0444  903  TYR   A CA  
1443 C C   . TYR   A 210 ? 0.4479 0.5447 0.5282 0.1091  -0.0470 0.0418  903  TYR   A C   
1444 O O   . TYR   A 210 ? 0.4692 0.5535 0.5345 0.1046  -0.0496 0.0383  903  TYR   A O   
1445 C CB  . TYR   A 210 ? 0.4194 0.5248 0.5162 0.1023  -0.0600 0.0437  903  TYR   A CB  
1446 C CG  . TYR   A 210 ? 0.4294 0.5099 0.5049 0.0969  -0.0620 0.0397  903  TYR   A CG  
1447 C CD1 . TYR   A 210 ? 0.4241 0.5033 0.5008 0.0846  -0.0647 0.0371  903  TYR   A CD1 
1448 C CD2 . TYR   A 210 ? 0.4470 0.5056 0.5035 0.1037  -0.0599 0.0370  903  TYR   A CD2 
1449 C CE1 . TYR   A 210 ? 0.4415 0.5023 0.5059 0.0779  -0.0650 0.0309  903  TYR   A CE1 
1450 C CE2 . TYR   A 210 ? 0.4658 0.5020 0.5062 0.0959  -0.0599 0.0311  903  TYR   A CE2 
1451 C CZ  . TYR   A 210 ? 0.4664 0.5059 0.5132 0.0824  -0.0623 0.0275  903  TYR   A CZ  
1452 O OH  . TYR   A 210 ? 0.4986 0.5197 0.5360 0.0732  -0.0610 0.0194  903  TYR   A OH  
1453 N N   . GLY   A 211 ? 0.4445 0.5414 0.5247 0.1209  -0.0406 0.0422  904  GLY   A N   
1454 C CA  . GLY   A 211 ? 0.4607 0.5385 0.5183 0.1289  -0.0343 0.0393  904  GLY   A CA  
1455 C C   . GLY   A 211 ? 0.4806 0.5561 0.5277 0.1276  -0.0274 0.0396  904  GLY   A C   
1456 O O   . GLY   A 211 ? 0.5004 0.5561 0.5217 0.1287  -0.0291 0.0353  904  GLY   A O   
1457 N N   . VAL   A 212 ? 0.4643 0.5578 0.5292 0.1252  -0.0194 0.0442  905  VAL   A N   
1458 C CA  . VAL   A 212 ? 0.4663 0.5522 0.5164 0.1245  -0.0105 0.0465  905  VAL   A CA  
1459 C C   . VAL   A 212 ? 0.4910 0.5680 0.5277 0.1174  -0.0224 0.0454  905  VAL   A C   
1460 O O   . VAL   A 212 ? 0.5182 0.5775 0.5275 0.1214  -0.0224 0.0444  905  VAL   A O   
1461 C CB  . VAL   A 212 ? 0.4495 0.5535 0.5228 0.1220  0.0045  0.0510  905  VAL   A CB  
1462 C CG1 . VAL   A 212 ? 0.4661 0.5526 0.5154 0.1216  0.0164  0.0546  905  VAL   A CG1 
1463 C CG2 . VAL   A 212 ? 0.4384 0.5559 0.5307 0.1304  0.0163  0.0496  905  VAL   A CG2 
1464 N N   . THR   A 213 ? 0.4823 0.5704 0.5366 0.1084  -0.0331 0.0447  906  THR   A N   
1465 C CA  . THR   A 213 ? 0.4903 0.5747 0.5395 0.1020  -0.0441 0.0422  906  THR   A CA  
1466 C C   . THR   A 213 ? 0.5111 0.5808 0.5419 0.1037  -0.0538 0.0338  906  THR   A C   
1467 O O   . THR   A 213 ? 0.5283 0.5912 0.5455 0.1049  -0.0610 0.0300  906  THR   A O   
1468 C CB  . THR   A 213 ? 0.4887 0.5877 0.5616 0.0921  -0.0496 0.0431  906  THR   A CB  
1469 O OG1 . THR   A 213 ? 0.4925 0.6052 0.5824 0.0895  -0.0414 0.0487  906  THR   A OG1 
1470 C CG2 . THR   A 213 ? 0.4875 0.5849 0.5598 0.0858  -0.0589 0.0397  906  THR   A CG2 
1471 N N   . VAL   A 214 ? 0.5132 0.5767 0.5428 0.1046  -0.0543 0.0301  907  VAL   A N   
1472 C CA  . VAL   A 214 ? 0.5225 0.5698 0.5356 0.1041  -0.0610 0.0203  907  VAL   A CA  
1473 C C   . VAL   A 214 ? 0.5352 0.5681 0.5210 0.1137  -0.0593 0.0176  907  VAL   A C   
1474 O O   . VAL   A 214 ? 0.5442 0.5696 0.5166 0.1130  -0.0695 0.0090  907  VAL   A O   
1475 C CB  . VAL   A 214 ? 0.5348 0.5714 0.5475 0.1038  -0.0584 0.0182  907  VAL   A CB  
1476 C CG1 . VAL   A 214 ? 0.5534 0.5687 0.5462 0.1029  -0.0616 0.0072  907  VAL   A CG1 
1477 C CG2 . VAL   A 214 ? 0.5315 0.5747 0.5616 0.0944  -0.0612 0.0197  907  VAL   A CG2 
1478 N N   . TRP   A 215 ? 0.5384 0.5683 0.5165 0.1229  -0.0464 0.0243  908  TRP   A N   
1479 C CA  . TRP   A 215 ? 0.5562 0.5679 0.5030 0.1330  -0.0406 0.0233  908  TRP   A CA  
1480 C C   . TRP   A 215 ? 0.5830 0.5908 0.5142 0.1344  -0.0467 0.0243  908  TRP   A C   
1481 O O   . TRP   A 215 ? 0.6111 0.6002 0.5104 0.1413  -0.0529 0.0185  908  TRP   A O   
1482 C CB  . TRP   A 215 ? 0.5432 0.5559 0.4918 0.1410  -0.0212 0.0306  908  TRP   A CB  
1483 C CG  . TRP   A 215 ? 0.5545 0.5430 0.4661 0.1517  -0.0116 0.0294  908  TRP   A CG  
1484 C CD1 . TRP   A 215 ? 0.5729 0.5415 0.4615 0.1594  -0.0084 0.0232  908  TRP   A CD1 
1485 C CD2 . TRP   A 215 ? 0.5644 0.5401 0.4511 0.1564  -0.0036 0.0342  908  TRP   A CD2 
1486 N NE1 . TRP   A 215 ? 0.5948 0.5402 0.4457 0.1686  0.0009  0.0235  908  TRP   A NE1 
1487 C CE2 . TRP   A 215 ? 0.5922 0.5400 0.4394 0.1672  0.0040  0.0306  908  TRP   A CE2 
1488 C CE3 . TRP   A 215 ? 0.5667 0.5469 0.4564 0.1530  -0.0012 0.0413  908  TRP   A CE3 
1489 C CZ2 . TRP   A 215 ? 0.6237 0.5470 0.4318 0.1752  0.0141  0.0345  908  TRP   A CZ2 
1490 C CZ3 . TRP   A 215 ? 0.6000 0.5547 0.4512 0.1609  0.0087  0.0454  908  TRP   A CZ3 
1491 C CH2 . TRP   A 215 ? 0.6264 0.5524 0.4361 0.1721  0.0165  0.0424  908  TRP   A CH2 
1492 N N   . GLU   A 216 ? 0.5790 0.6016 0.5292 0.1292  -0.0457 0.0312  909  GLU   A N   
1493 C CA  . GLU   A 216 ? 0.5971 0.6132 0.5315 0.1323  -0.0518 0.0330  909  GLU   A CA  
1494 C C   . GLU   A 216 ? 0.6117 0.6292 0.5439 0.1311  -0.0733 0.0217  909  GLU   A C   
1495 O O   . GLU   A 216 ? 0.6383 0.6429 0.5437 0.1400  -0.0830 0.0184  909  GLU   A O   
1496 C CB  . GLU   A 216 ? 0.6061 0.6373 0.5649 0.1252  -0.0467 0.0412  909  GLU   A CB  
1497 C CG  . GLU   A 216 ? 0.6705 0.7017 0.6337 0.1250  -0.0255 0.0507  909  GLU   A CG  
1498 C CD  . GLU   A 216 ? 0.7558 0.8006 0.7433 0.1159  -0.0223 0.0563  909  GLU   A CD  
1499 O OE1 . GLU   A 216 ? 0.7406 0.8073 0.7613 0.1068  -0.0238 0.0555  909  GLU   A OE1 
1500 O OE2 . GLU   A 216 ? 0.7941 0.8243 0.7635 0.1186  -0.0187 0.0611  909  GLU   A OE2 
1501 N N   . LEU   A 217 ? 0.5973 0.6301 0.5574 0.1204  -0.0806 0.0151  910  LEU   A N   
1502 C CA  . LEU   A 217 ? 0.6020 0.6411 0.5695 0.1162  -0.0983 0.0021  910  LEU   A CA  
1503 C C   . LEU   A 217 ? 0.6302 0.6544 0.5741 0.1207  -0.1067 -0.0102 910  LEU   A C   
1504 O O   . LEU   A 217 ? 0.6405 0.6649 0.5754 0.1249  -0.1232 -0.0206 910  LEU   A O   
1505 C CB  . LEU   A 217 ? 0.5830 0.6377 0.5844 0.1017  -0.0985 -0.0016 910  LEU   A CB  
1506 C CG  . LEU   A 217 ? 0.5794 0.6482 0.6039 0.0957  -0.0920 0.0081  910  LEU   A CG  
1507 C CD1 . LEU   A 217 ? 0.5660 0.6426 0.6146 0.0825  -0.0914 0.0035  910  LEU   A CD1 
1508 C CD2 . LEU   A 217 ? 0.5880 0.6631 0.6138 0.0998  -0.0986 0.0100  910  LEU   A CD2 
1509 N N   . MET   A 218 ? 0.6457 0.6568 0.5794 0.1209  -0.0964 -0.0101 911  MET   A N   
1510 C CA  . MET   A 218 ? 0.6710 0.6633 0.5794 0.1243  -0.1017 -0.0220 911  MET   A CA  
1511 C C   . MET   A 218 ? 0.7050 0.6783 0.5721 0.1392  -0.1052 -0.0220 911  MET   A C   
1512 O O   . MET   A 218 ? 0.7252 0.6852 0.5696 0.1425  -0.1171 -0.0353 911  MET   A O   
1513 C CB  . MET   A 218 ? 0.6857 0.6655 0.5918 0.1230  -0.0873 -0.0200 911  MET   A CB  
1514 C CG  . MET   A 218 ? 0.7172 0.7067 0.6534 0.1105  -0.0842 -0.0203 911  MET   A CG  
1515 S SD  . MET   A 218 ? 0.8327 0.8294 0.7887 0.0943  -0.0984 -0.0381 911  MET   A SD  
1516 C CE  . MET   A 218 ? 0.7943 0.7855 0.7680 0.0835  -0.0854 -0.0336 911  MET   A CE  
1517 N N   . THR   A 219 ? 0.7182 0.6868 0.5724 0.1478  -0.0941 -0.0078 912  THR   A N   
1518 C CA  . THR   A 219 ? 0.7556 0.6994 0.5632 0.1630  -0.0947 -0.0056 912  THR   A CA  
1519 C C   . THR   A 219 ? 0.7729 0.7199 0.5731 0.1693  -0.1113 -0.0059 912  THR   A C   
1520 O O   . THR   A 219 ? 0.8086 0.7307 0.5647 0.1839  -0.1125 -0.0025 912  THR   A O   
1521 C CB  . THR   A 219 ? 0.7800 0.7102 0.5728 0.1688  -0.0687 0.0092  912  THR   A CB  
1522 O OG1 . THR   A 219 ? 0.7719 0.7226 0.5986 0.1614  -0.0593 0.0204  912  THR   A OG1 
1523 C CG2 . THR   A 219 ? 0.7847 0.7078 0.5770 0.1685  -0.0534 0.0081  912  THR   A CG2 
1524 N N   . PHE   A 220 ? 0.7529 0.7275 0.5931 0.1599  -0.1228 -0.0097 913  PHE   A N   
1525 C CA  . PHE   A 220 ? 0.7588 0.7418 0.6016 0.1661  -0.1393 -0.0113 913  PHE   A CA  
1526 C C   . PHE   A 220 ? 0.7744 0.7440 0.5999 0.1741  -0.1261 0.0059  913  PHE   A C   
1527 O O   . PHE   A 220 ? 0.7908 0.7474 0.5897 0.1879  -0.1370 0.0072  913  PHE   A O   
1528 C CB  . PHE   A 220 ? 0.7727 0.7479 0.5888 0.1780  -0.1650 -0.0270 913  PHE   A CB  
1529 C CG  . PHE   A 220 ? 0.7759 0.7686 0.6186 0.1660  -0.1784 -0.0469 913  PHE   A CG  
1530 C CD1 . PHE   A 220 ? 0.7651 0.7899 0.6555 0.1547  -0.1903 -0.0581 913  PHE   A CD1 
1531 C CD2 . PHE   A 220 ? 0.7985 0.7736 0.6190 0.1648  -0.1760 -0.0550 913  PHE   A CD2 
1532 C CE1 . PHE   A 220 ? 0.7627 0.8012 0.6787 0.1410  -0.1986 -0.0772 913  PHE   A CE1 
1533 C CE2 . PHE   A 220 ? 0.7978 0.7850 0.6420 0.1517  -0.1857 -0.0738 913  PHE   A CE2 
1534 C CZ  . PHE   A 220 ? 0.7720 0.7907 0.6642 0.1391  -0.1964 -0.0850 913  PHE   A CZ  
1535 N N   . GLY   A 221 ? 0.7689 0.7417 0.6107 0.1653  -0.1031 0.0181  914  GLY   A N   
1536 C CA  . GLY   A 221 ? 0.7832 0.7453 0.6164 0.1680  -0.0869 0.0330  914  GLY   A CA  
1537 C C   . GLY   A 221 ? 0.8116 0.7429 0.6053 0.1758  -0.0650 0.0429  914  GLY   A C   
1538 O O   . GLY   A 221 ? 0.8306 0.7432 0.6045 0.1805  -0.0525 0.0537  914  GLY   A O   
1539 N N   . SER   A 222 ? 0.8169 0.7403 0.5983 0.1769  -0.0576 0.0392  915  SER   A N   
1540 C CA  . SER   A 222 ? 0.8451 0.7399 0.5915 0.1837  -0.0328 0.0476  915  SER   A CA  
1541 C C   . SER   A 222 ? 0.8422 0.7503 0.6209 0.1727  -0.0067 0.0581  915  SER   A C   
1542 O O   . SER   A 222 ? 0.8114 0.7523 0.6396 0.1601  -0.0087 0.0569  915  SER   A O   
1543 C CB  . SER   A 222 ? 0.8675 0.7521 0.5966 0.1876  -0.0302 0.0399  915  SER   A CB  
1544 O OG  . SER   A 222 ? 0.9248 0.7897 0.6138 0.1990  -0.0520 0.0295  915  SER   A OG  
1545 N N   . LYS   A 223 ? 0.8734 0.7549 0.6231 0.1772  0.0183  0.0674  916  LYS   A N   
1546 C CA  . LYS   A 223 ? 0.8770 0.7718 0.6594 0.1656  0.0450  0.0749  916  LYS   A CA  
1547 C C   . LYS   A 223 ? 0.8826 0.7911 0.6857 0.1632  0.0608  0.0716  916  LYS   A C   
1548 O O   . LYS   A 223 ? 0.9053 0.7887 0.6718 0.1733  0.0705  0.0700  916  LYS   A O   
1549 C CB  . LYS   A 223 ? 0.9216 0.7796 0.6656 0.1695  0.0683  0.0855  916  LYS   A CB  
1550 C CG  . LYS   A 223 ? 0.9839 0.8245 0.7039 0.1753  0.0523  0.0894  916  LYS   A CG  
1551 C CD  . LYS   A 223 ? 1.0698 0.8618 0.7374 0.1826  0.0753  0.1005  916  LYS   A CD  
1552 N N   . PRO   A 224 ? 0.8613 0.8087 0.7214 0.1516  0.0620  0.0697  917  PRO   A N   
1553 C CA  . PRO   A 224 ? 0.8608 0.8240 0.7441 0.1523  0.0744  0.0659  917  PRO   A CA  
1554 C C   . PRO   A 224 ? 0.8871 0.8391 0.7648 0.1537  0.1086  0.0698  917  PRO   A C   
1555 O O   . PRO   A 224 ? 0.8837 0.8373 0.7735 0.1453  0.1258  0.0752  917  PRO   A O   
1556 C CB  . PRO   A 224 ? 0.8324 0.8377 0.7743 0.1413  0.0646  0.0636  917  PRO   A CB  
1557 C CG  . PRO   A 224 ? 0.8288 0.8391 0.7811 0.1318  0.0604  0.0681  917  PRO   A CG  
1558 C CD  . PRO   A 224 ? 0.8321 0.8089 0.7350 0.1394  0.0509  0.0704  917  PRO   A CD  
1559 N N   . TYR   A 225 ? 0.9143 0.8541 0.7744 0.1635  0.1202  0.0663  918  TYR   A N   
1560 C CA  . TYR   A 225 ? 0.9471 0.8744 0.8000 0.1661  0.1557  0.0684  918  TYR   A CA  
1561 C C   . TYR   A 225 ? 1.0126 0.8990 0.8178 0.1664  0.1742  0.0767  918  TYR   A C   
1562 O O   . TYR   A 225 ? 1.0132 0.9021 0.8362 0.1574  0.2024  0.0807  918  TYR   A O   
1563 C CB  . TYR   A 225 ? 0.9053 0.8769 0.8266 0.1564  0.1724  0.0662  918  TYR   A CB  
1564 C CG  . TYR   A 225 ? 0.8797 0.8923 0.8499 0.1560  0.1506  0.0600  918  TYR   A CG  
1565 C CD1 . TYR   A 225 ? 0.8836 0.9018 0.8597 0.1671  0.1515  0.0542  918  TYR   A CD1 
1566 C CD2 . TYR   A 225 ? 0.8621 0.9054 0.8717 0.1451  0.1323  0.0600  918  TYR   A CD2 
1567 C CE1 . TYR   A 225 ? 0.8675 0.9171 0.8827 0.1688  0.1329  0.0496  918  TYR   A CE1 
1568 C CE2 . TYR   A 225 ? 0.8492 0.9243 0.8970 0.1460  0.1136  0.0551  918  TYR   A CE2 
1569 C CZ  . TYR   A 225 ? 0.8569 0.9343 0.9066 0.1584  0.1140  0.0503  918  TYR   A CZ  
1570 O OH  . TYR   A 225 ? 0.8529 0.9555 0.9339 0.1614  0.0961  0.0465  918  TYR   A OH  
1571 N N   . ASP   A 226 ? 1.0655 0.9136 0.8102 0.1766  0.1577  0.0785  919  ASP   A N   
1572 C CA  . ASP   A 226 ? 1.1229 0.9254 0.8127 0.1807  0.1710  0.0872  919  ASP   A CA  
1573 C C   . ASP   A 226 ? 1.1630 0.9290 0.8160 0.1852  0.2112  0.0912  919  ASP   A C   
1574 O O   . ASP   A 226 ? 1.1847 0.9333 0.8088 0.1960  0.2169  0.0867  919  ASP   A O   
1575 C CB  . ASP   A 226 ? 1.1852 0.9575 0.8190 0.1942  0.1397  0.0864  919  ASP   A CB  
1576 C CG  . ASP   A 226 ? 1.2829 1.0322 0.8907 0.1951  0.1354  0.0949  919  ASP   A CG  
1577 O OD1 . ASP   A 226 ? 1.2985 1.0354 0.9085 0.1872  0.1651  0.1033  919  ASP   A OD1 
1578 O OD2 . ASP   A 226 ? 1.3288 1.0723 0.9152 0.2039  0.1032  0.0923  919  ASP   A OD2 
1579 N N   . GLY   A 227 ? 1.1714 0.9237 0.8251 0.1761  0.2408  0.0988  920  GLY   A N   
1580 C CA  . GLY   A 227 ? 1.2039 0.9193 0.8248 0.1773  0.2853  0.1029  920  GLY   A CA  
1581 C C   . GLY   A 227 ? 1.1722 0.9296 0.8639 0.1630  0.3167  0.0976  920  GLY   A C   
1582 O O   . GLY   A 227 ? 1.1838 0.9211 0.8697 0.1560  0.3591  0.1008  920  GLY   A O   
1583 N N   . ILE   A 228 ? 1.1271 0.9424 0.8859 0.1594  0.2966  0.0887  921  ILE   A N   
1584 C CA  . ILE   A 228 ? 1.0836 0.9481 0.9178 0.1487  0.3182  0.0815  921  ILE   A CA  
1585 C C   . ILE   A 228 ? 1.0558 0.9487 0.9417 0.1286  0.3247  0.0825  921  ILE   A C   
1586 O O   . ILE   A 228 ? 1.0450 0.9528 0.9435 0.1239  0.2944  0.0840  921  ILE   A O   
1587 C CB  . ILE   A 228 ? 1.0572 0.9671 0.9357 0.1551  0.2895  0.0726  921  ILE   A CB  
1588 C CG1 . ILE   A 228 ? 1.0954 0.9733 0.9204 0.1738  0.2828  0.0704  921  ILE   A CG1 
1589 C CG2 . ILE   A 228 ? 1.0174 0.9828 0.9773 0.1474  0.3056  0.0642  921  ILE   A CG2 
1590 N N   . PRO   A 229 ? 1.0435 0.9415 0.9580 0.1156  0.3659  0.0807  922  PRO   A N   
1591 C CA  . PRO   A 229 ? 1.0154 0.9407 0.9816 0.0943  0.3728  0.0792  922  PRO   A CA  
1592 C C   . PRO   A 229 ? 0.9658 0.9624 1.0143 0.0880  0.3442  0.0690  922  PRO   A C   
1593 O O   . PRO   A 229 ? 0.9491 0.9786 1.0288 0.0977  0.3351  0.0615  922  PRO   A O   
1594 C CB  . PRO   A 229 ? 1.0205 0.9375 1.0026 0.0819  0.4265  0.0764  922  PRO   A CB  
1595 C CG  . PRO   A 229 ? 1.0613 0.9317 0.9807 0.0988  0.4488  0.0800  922  PRO   A CG  
1596 C CD  . PRO   A 229 ? 1.0446 0.9265 0.9508 0.1184  0.4093  0.0780  922  PRO   A CD  
1597 N N   . ALA   A 230 ? 0.9427 0.9591 1.0215 0.0734  0.3293  0.0687  923  ALA   A N   
1598 C CA  . ALA   A 230 ? 0.8992 0.9779 1.0484 0.0679  0.3007  0.0593  923  ALA   A CA  
1599 C C   . ALA   A 230 ? 0.8551 0.9871 1.0796 0.0618  0.3190  0.0459  923  ALA   A C   
1600 O O   . ALA   A 230 ? 0.8256 1.0048 1.0971 0.0676  0.2941  0.0379  923  ALA   A O   
1601 C CB  . ALA   A 230 ? 0.8952 0.9791 1.0578 0.0523  0.2867  0.0609  923  ALA   A CB  
1602 N N   . SER   A 231 ? 0.8509 0.9740 1.0856 0.0514  0.3632  0.0431  924  SER   A N   
1603 C CA  . SER   A 231 ? 0.8077 0.9833 1.1185 0.0453  0.3851  0.0283  924  SER   A CA  
1604 C C   . SER   A 231 ? 0.7954 0.9867 1.1119 0.0673  0.3816  0.0242  924  SER   A C   
1605 O O   . SER   A 231 ? 0.7549 1.0013 1.1422 0.0683  0.3854  0.0107  924  SER   A O   
1606 C CB  . SER   A 231 ? 0.8337 0.9881 1.1474 0.0278  0.4383  0.0265  924  SER   A CB  
1607 O OG  . SER   A 231 ? 0.9165 1.0065 1.1524 0.0391  0.4649  0.0376  924  SER   A OG  
1608 N N   . GLU   A 232 ? 0.8284 0.9718 1.0717 0.0856  0.3738  0.0344  925  GLU   A N   
1609 C CA  . GLU   A 232 ? 0.8293 0.9783 1.0689 0.1066  0.3720  0.0308  925  GLU   A CA  
1610 C C   . GLU   A 232 ? 0.8076 0.9728 1.0457 0.1220  0.3253  0.0309  925  GLU   A C   
1611 O O   . GLU   A 232 ? 0.8045 0.9747 1.0421 0.1396  0.3221  0.0273  925  GLU   A O   
1612 C CB  . GLU   A 232 ? 0.9249 1.0085 1.0839 0.1170  0.3978  0.0393  925  GLU   A CB  
1613 C CG  . GLU   A 232 ? 1.0325 1.0896 1.1823 0.1034  0.4493  0.0403  925  GLU   A CG  
1614 C CD  . GLU   A 232 ? 1.2134 1.1963 1.2707 0.1145  0.4739  0.0500  925  GLU   A CD  
1615 O OE1 . GLU   A 232 ? 1.2603 1.2181 1.2671 0.1339  0.4518  0.0535  925  GLU   A OE1 
1616 O OE2 . GLU   A 232 ? 1.2763 1.2232 1.3089 0.1035  0.5158  0.0538  925  GLU   A OE2 
1617 N N   . ILE   A 233 ? 0.7916 0.9611 1.0267 0.1155  0.2918  0.0350  926  ILE   A N   
1618 C CA  . ILE   A 233 ? 0.7821 0.9605 1.0108 0.1272  0.2502  0.0358  926  ILE   A CA  
1619 C C   . ILE   A 233 ? 0.7382 0.9688 1.0284 0.1372  0.2373  0.0253  926  ILE   A C   
1620 O O   . ILE   A 233 ? 0.7444 0.9674 1.0166 0.1548  0.2232  0.0252  926  ILE   A O   
1621 C CB  . ILE   A 233 ? 0.7888 0.9628 1.0072 0.1157  0.2228  0.0412  926  ILE   A CB  
1622 C CG1 . ILE   A 233 ? 0.8405 0.9578 0.9884 0.1135  0.2289  0.0520  926  ILE   A CG1 
1623 C CG2 . ILE   A 233 ? 0.7866 0.9748 1.0083 0.1246  0.1832  0.0404  926  ILE   A CG2 
1624 N N   . SER   A 234 ? 0.6928 0.9743 1.0537 0.1270  0.2422  0.0157  927  SER   A N   
1625 C CA  . SER   A 234 ? 0.6574 0.9915 1.0788 0.1387  0.2267  0.0046  927  SER   A CA  
1626 C C   . SER   A 234 ? 0.6547 0.9910 1.0810 0.1585  0.2448  0.0000  927  SER   A C   
1627 O O   . SER   A 234 ? 0.6502 0.9986 1.0831 0.1777  0.2230  -0.0025 927  SER   A O   
1628 C CB  . SER   A 234 ? 0.6339 1.0233 1.1317 0.1231  0.2305  -0.0074 927  SER   A CB  
1629 O OG  . SER   A 234 ? 0.6543 1.0545 1.1830 0.1129  0.2727  -0.0143 927  SER   A OG  
1630 N N   . SER   A 235 ? 0.6585 0.9781 1.0768 0.1546  0.2857  -0.0008 928  SER   A N   
1631 C CA  . SER   A 235 ? 0.6585 0.9764 1.0784 0.1733  0.3072  -0.0056 928  SER   A CA  
1632 C C   . SER   A 235 ? 0.6939 0.9580 1.0372 0.1905  0.2952  0.0035  928  SER   A C   
1633 O O   . SER   A 235 ? 0.7014 0.9696 1.0481 0.2110  0.2928  -0.0007 928  SER   A O   
1634 C CB  . SER   A 235 ? 0.6807 0.9920 1.1104 0.1631  0.3578  -0.0094 928  SER   A CB  
1635 O OG  . SER   A 235 ? 0.7571 1.0122 1.1211 0.1492  0.3734  0.0023  928  SER   A OG  
1636 N N   . ILE   A 236 ? 0.7132 0.9281 0.9897 0.1828  0.2863  0.0147  929  ILE   A N   
1637 C CA  . ILE   A 236 ? 0.7432 0.9085 0.9484 0.1959  0.2718  0.0213  929  ILE   A CA  
1638 C C   . ILE   A 236 ? 0.7185 0.9000 0.9347 0.2073  0.2329  0.0198  929  ILE   A C   
1639 O O   . ILE   A 236 ? 0.7382 0.8979 0.9254 0.2239  0.2270  0.0189  929  ILE   A O   
1640 C CB  . ILE   A 236 ? 0.7925 0.9080 0.9314 0.1846  0.2705  0.0316  929  ILE   A CB  
1641 C CG1 . ILE   A 236 ? 0.8467 0.9124 0.9277 0.1897  0.3037  0.0345  929  ILE   A CG1 
1642 C CG2 . ILE   A 236 ? 0.8158 0.9101 0.9151 0.1870  0.2314  0.0365  929  ILE   A CG2 
1643 C CD1 . ILE   A 236 ? 0.8555 0.9345 0.9698 0.1848  0.3497  0.0298  929  ILE   A CD1 
1644 N N   . LEU   A 237 ? 0.6735 0.8901 0.9297 0.1984  0.2084  0.0190  930  LEU   A N   
1645 C CA  . LEU   A 237 ? 0.6541 0.8826 0.9180 0.2084  0.1737  0.0182  930  LEU   A CA  
1646 C C   . LEU   A 237 ? 0.6315 0.8916 0.9381 0.2284  0.1749  0.0098  930  LEU   A C   
1647 O O   . LEU   A 237 ? 0.6444 0.8900 0.9313 0.2447  0.1570  0.0103  930  LEU   A O   
1648 C CB  . LEU   A 237 ? 0.6281 0.8828 0.9199 0.1939  0.1500  0.0192  930  LEU   A CB  
1649 C CG  . LEU   A 237 ? 0.6540 0.8780 0.9043 0.1772  0.1427  0.0274  930  LEU   A CG  
1650 C CD1 . LEU   A 237 ? 0.6324 0.8853 0.9161 0.1632  0.1238  0.0268  930  LEU   A CD1 
1651 C CD2 . LEU   A 237 ? 0.6908 0.8715 0.8816 0.1840  0.1257  0.0326  930  LEU   A CD2 
1652 N N   . GLU   A 238 ? 0.5942 0.8960 0.9591 0.2278  0.1972  0.0012  931  GLU   A N   
1653 C CA  . GLU   A 238 ? 0.5710 0.9085 0.9835 0.2490  0.1996  -0.0085 931  GLU   A CA  
1654 C C   . GLU   A 238 ? 0.6023 0.9036 0.9758 0.2682  0.2185  -0.0082 931  GLU   A C   
1655 O O   . GLU   A 238 ? 0.5963 0.9097 0.9867 0.2911  0.2112  -0.0132 931  GLU   A O   
1656 C CB  . GLU   A 238 ? 0.5468 0.9437 1.0392 0.2413  0.2187  -0.0204 931  GLU   A CB  
1657 N N   . LYS   A 239 ? 0.6359 0.8891 0.9524 0.2606  0.2409  -0.0023 932  LYS   A N   
1658 C CA  . LYS   A 239 ? 0.6680 0.8785 0.9361 0.2770  0.2577  -0.0021 932  LYS   A CA  
1659 C C   . LYS   A 239 ? 0.6940 0.8598 0.9015 0.2856  0.2291  0.0035  932  LYS   A C   
1660 O O   . LYS   A 239 ? 0.7234 0.8510 0.8879 0.2991  0.2387  0.0025  932  LYS   A O   
1661 C CB  . LYS   A 239 ? 0.7274 0.8993 0.9511 0.2661  0.2919  0.0014  932  LYS   A CB  
1662 C CG  . LYS   A 239 ? 0.7638 0.9681 1.0383 0.2570  0.3294  -0.0046 932  LYS   A CG  
1663 C CD  . LYS   A 239 ? 0.8623 1.0161 1.0790 0.2488  0.3653  0.0003  932  LYS   A CD  
1664 N N   . GLY   A 240 ? 0.6811 0.8495 0.8844 0.2762  0.1970  0.0082  933  GLY   A N   
1665 C CA  . GLY   A 240 ? 0.7037 0.8330 0.8567 0.2806  0.1718  0.0121  933  GLY   A CA  
1666 C C   . GLY   A 240 ? 0.7260 0.8101 0.8171 0.2663  0.1682  0.0173  933  GLY   A C   
1667 O O   . GLY   A 240 ? 0.7547 0.8042 0.8032 0.2687  0.1513  0.0180  933  GLY   A O   
1668 N N   . GLU   A 241 ? 0.7093 0.7924 0.7950 0.2519  0.1843  0.0203  934  GLU   A N   
1669 C CA  . GLU   A 241 ? 0.7296 0.7716 0.7571 0.2410  0.1798  0.0250  934  GLU   A CA  
1670 C C   . GLU   A 241 ? 0.7050 0.7584 0.7403 0.2266  0.1517  0.0291  934  GLU   A C   
1671 O O   . GLU   A 241 ? 0.6839 0.7743 0.7652 0.2175  0.1492  0.0305  934  GLU   A O   
1672 C CB  . GLU   A 241 ? 0.7643 0.7936 0.7760 0.2344  0.2103  0.0274  934  GLU   A CB  
1673 N N   . ARG   A 242 ? 0.7055 0.7285 0.6986 0.2240  0.1308  0.0297  935  ARG   A N   
1674 C CA  . ARG   A 242 ? 0.6832 0.7134 0.6803 0.2108  0.1052  0.0326  935  ARG   A CA  
1675 C C   . ARG   A 242 ? 0.7021 0.6995 0.6501 0.2030  0.0993  0.0342  935  ARG   A C   
1676 O O   . ARG   A 242 ? 0.7328 0.6993 0.6395 0.2091  0.1127  0.0328  935  ARG   A O   
1677 C CB  . ARG   A 242 ? 0.6779 0.7062 0.6778 0.2153  0.0833  0.0299  935  ARG   A CB  
1678 C CG  . ARG   A 242 ? 0.6547 0.7147 0.7003 0.2254  0.0827  0.0289  935  ARG   A CG  
1679 C CD  . ARG   A 242 ? 0.6413 0.7432 0.7347 0.2157  0.0778  0.0315  935  ARG   A CD  
1680 N NE  . ARG   A 242 ? 0.6196 0.7526 0.7550 0.2273  0.0714  0.0290  935  ARG   A NE  
1681 C CZ  . ARG   A 242 ? 0.5935 0.7568 0.7684 0.2373  0.0868  0.0250  935  ARG   A CZ  
1682 N NH1 . ARG   A 242 ? 0.5699 0.7626 0.7825 0.2501  0.0761  0.0216  935  ARG   A NH1 
1683 N NH2 . ARG   A 242 ? 0.5676 0.7314 0.7444 0.2351  0.1135  0.0236  935  ARG   A NH2 
1684 N N   . LEU   A 243 ? 0.6871 0.6903 0.6378 0.1911  0.0787  0.0363  936  LEU   A N   
1685 C CA  . LEU   A 243 ? 0.7081 0.6845 0.6167 0.1862  0.0683  0.0362  936  LEU   A CA  
1686 C C   . LEU   A 243 ? 0.7441 0.6887 0.6123 0.1930  0.0587  0.0282  936  LEU   A C   
1687 O O   . LEU   A 243 ? 0.7445 0.6905 0.6227 0.1952  0.0507  0.0237  936  LEU   A O   
1688 C CB  . LEU   A 243 ? 0.6823 0.6757 0.6099 0.1735  0.0478  0.0383  936  LEU   A CB  
1689 C CG  . LEU   A 243 ? 0.6650 0.6818 0.6225 0.1653  0.0567  0.0451  936  LEU   A CG  
1690 C CD1 . LEU   A 243 ? 0.6498 0.6893 0.6368 0.1543  0.0378  0.0460  936  LEU   A CD1 
1691 C CD2 . LEU   A 243 ? 0.6857 0.6795 0.6095 0.1652  0.0682  0.0494  936  LEU   A CD2 
1692 N N   . PRO   A 244 ? 0.7737 0.6860 0.5929 0.1974  0.0611  0.0258  937  PRO   A N   
1693 C CA  . PRO   A 244 ? 0.8033 0.6847 0.5833 0.2033  0.0523  0.0157  937  PRO   A CA  
1694 C C   . PRO   A 244 ? 0.8102 0.6937 0.5946 0.1940  0.0253  0.0080  937  PRO   A C   
1695 O O   . PRO   A 244 ? 0.7976 0.7016 0.6049 0.1840  0.0118  0.0106  937  PRO   A O   
1696 C CB  . PRO   A 244 ? 0.8388 0.6871 0.5647 0.2099  0.0579  0.0151  937  PRO   A CB  
1697 C CG  . PRO   A 244 ? 0.8325 0.6936 0.5680 0.2041  0.0590  0.0245  937  PRO   A CG  
1698 C CD  . PRO   A 244 ? 0.7801 0.6783 0.5728 0.1980  0.0718  0.0315  937  PRO   A CD  
1699 N N   . GLN   A 245 ? 0.8289 0.6903 0.5925 0.1965  0.0195  -0.0023 938  GLN   A N   
1700 C CA  . GLN   A 245 ? 0.8376 0.6981 0.6055 0.1856  -0.0024 -0.0120 938  GLN   A CA  
1701 C C   . GLN   A 245 ? 0.8559 0.7110 0.6014 0.1811  -0.0211 -0.0187 938  GLN   A C   
1702 O O   . GLN   A 245 ? 0.8836 0.7123 0.5854 0.1892  -0.0217 -0.0246 938  GLN   A O   
1703 C CB  . GLN   A 245 ? 0.8713 0.7039 0.6184 0.1888  -0.0010 -0.0227 938  GLN   A CB  
1704 C CG  . GLN   A 245 ? 0.9106 0.7389 0.6625 0.1748  -0.0199 -0.0348 938  GLN   A CG  
1705 C CD  . GLN   A 245 ? 0.9771 0.7749 0.7108 0.1757  -0.0157 -0.0449 938  GLN   A CD  
1706 O OE1 . GLN   A 245 ? 0.9973 0.7850 0.7293 0.1632  -0.0278 -0.0575 938  GLN   A OE1 
1707 N NE2 . GLN   A 245 ? 0.9934 0.7751 0.7146 0.1901  0.0026  -0.0407 938  GLN   A NE2 
1708 N N   . PRO   A 246 ? 0.8374 0.7162 0.6105 0.1700  -0.0368 -0.0185 939  PRO   A N   
1709 C CA  . PRO   A 246 ? 0.8420 0.7191 0.5978 0.1684  -0.0567 -0.0260 939  PRO   A CA  
1710 C C   . PRO   A 246 ? 0.8606 0.7180 0.5918 0.1662  -0.0724 -0.0449 939  PRO   A C   
1711 O O   . PRO   A 246 ? 0.8577 0.7097 0.5994 0.1587  -0.0713 -0.0528 939  PRO   A O   
1712 C CB  . PRO   A 246 ? 0.8201 0.7292 0.6188 0.1566  -0.0672 -0.0227 939  PRO   A CB  
1713 C CG  . PRO   A 246 ? 0.8106 0.7360 0.6415 0.1542  -0.0505 -0.0099 939  PRO   A CG  
1714 C CD  . PRO   A 246 ? 0.8028 0.7099 0.6221 0.1600  -0.0378 -0.0122 939  PRO   A CD  
1715 N N   . PRO   A 247 ? 0.8802 0.7232 0.5748 0.1736  -0.0869 -0.0529 940  PRO   A N   
1716 C CA  . PRO   A 247 ? 0.8960 0.7211 0.5664 0.1715  -0.1041 -0.0739 940  PRO   A CA  
1717 C C   . PRO   A 247 ? 0.8805 0.7239 0.5889 0.1533  -0.1186 -0.0892 940  PRO   A C   
1718 O O   . PRO   A 247 ? 0.8920 0.7175 0.5898 0.1472  -0.1209 -0.1043 940  PRO   A O   
1719 C CB  . PRO   A 247 ? 0.9183 0.7345 0.5515 0.1833  -0.1229 -0.0786 940  PRO   A CB  
1720 C CG  . PRO   A 247 ? 0.9276 0.7399 0.5474 0.1947  -0.1061 -0.0580 940  PRO   A CG  
1721 C CD  . PRO   A 247 ? 0.8819 0.7210 0.5522 0.1851  -0.0885 -0.0437 940  PRO   A CD  
1722 N N   . ILE   A 248 ? 0.8514 0.7274 0.6026 0.1438  -0.1263 -0.0860 941  ILE   A N   
1723 C CA  . ILE   A 248 ? 0.8342 0.7278 0.6233 0.1253  -0.1368 -0.1006 941  ILE   A CA  
1724 C C   . ILE   A 248 ? 0.8392 0.7272 0.6496 0.1139  -0.1184 -0.0964 941  ILE   A C   
1725 O O   . ILE   A 248 ? 0.8320 0.7218 0.6628 0.0978  -0.1221 -0.1104 941  ILE   A O   
1726 C CB  . ILE   A 248 ? 0.8106 0.7392 0.6357 0.1204  -0.1506 -0.0999 941  ILE   A CB  
1727 C CG1 . ILE   A 248 ? 0.8041 0.7481 0.6540 0.1200  -0.1345 -0.0783 941  ILE   A CG1 
1728 C CG2 . ILE   A 248 ? 0.8203 0.7509 0.6207 0.1346  -0.1715 -0.1050 941  ILE   A CG2 
1729 C CD1 . ILE   A 248 ? 0.7871 0.7624 0.6776 0.1108  -0.1438 -0.0795 941  ILE   A CD1 
1730 N N   . CYS   A 249 ? 0.8497 0.7305 0.6556 0.1224  -0.0985 -0.0781 942  CYS   A N   
1731 C CA  . CYS   A 249 ? 0.8546 0.7290 0.6772 0.1160  -0.0832 -0.0726 942  CYS   A CA  
1732 C C   . CYS   A 249 ? 0.8809 0.7207 0.6778 0.1168  -0.0748 -0.0813 942  CYS   A C   
1733 O O   . CYS   A 249 ? 0.9041 0.7232 0.6672 0.1297  -0.0696 -0.0816 942  CYS   A O   
1734 C CB  . CYS   A 249 ? 0.8608 0.7468 0.6952 0.1255  -0.0686 -0.0516 942  CYS   A CB  
1735 S SG  . CYS   A 249 ? 0.9068 0.8302 0.7741 0.1218  -0.0755 -0.0407 942  CYS   A SG  
1736 N N   . THR   A 250 ? 0.8805 0.7099 0.6908 0.1040  -0.0696 -0.0867 943  THR   A N   
1737 C CA  . THR   A 250 ? 0.9049 0.6960 0.6903 0.1056  -0.0576 -0.0923 943  THR   A CA  
1738 C C   . THR   A 250 ? 0.9086 0.6946 0.6925 0.1219  -0.0403 -0.0726 943  THR   A C   
1739 O O   . THR   A 250 ? 0.8954 0.7097 0.7014 0.1273  -0.0394 -0.0578 943  THR   A O   
1740 C CB  . THR   A 250 ? 0.9190 0.6964 0.7169 0.0850  -0.0568 -0.1056 943  THR   A CB  
1741 O OG1 . THR   A 250 ? 0.9110 0.7068 0.7396 0.0782  -0.0528 -0.0944 943  THR   A OG1 
1742 C CG2 . THR   A 250 ? 0.9180 0.7022 0.7215 0.0689  -0.0739 -0.1297 943  THR   A CG2 
1743 N N   . ILE   A 251 ? 0.9239 0.6751 0.6835 0.1302  -0.0272 -0.0736 944  ILE   A N   
1744 C CA  . ILE   A 251 ? 0.9276 0.6770 0.6894 0.1479  -0.0130 -0.0572 944  ILE   A CA  
1745 C C   . ILE   A 251 ? 0.9108 0.6727 0.6999 0.1432  -0.0121 -0.0466 944  ILE   A C   
1746 O O   . ILE   A 251 ? 0.9016 0.6836 0.7072 0.1558  -0.0081 -0.0322 944  ILE   A O   
1747 C CB  . ILE   A 251 ? 0.9627 0.6706 0.6910 0.1611  0.0007  -0.0610 944  ILE   A CB  
1748 C CG1 . ILE   A 251 ? 0.9680 0.6852 0.7002 0.1848  0.0138  -0.0464 944  ILE   A CG1 
1749 C CG2 . ILE   A 251 ? 0.9852 0.6570 0.7035 0.1533  0.0063  -0.0664 944  ILE   A CG2 
1750 C CD1 . ILE   A 251 ? 0.9606 0.7129 0.7061 0.1914  0.0135  -0.0388 944  ILE   A CD1 
1751 N N   . ASP   A 252 ? 0.9043 0.6567 0.6994 0.1242  -0.0162 -0.0548 945  ASP   A N   
1752 C CA  . ASP   A 252 ? 0.8961 0.6525 0.7091 0.1180  -0.0144 -0.0463 945  ASP   A CA  
1753 C C   . ASP   A 252 ? 0.8621 0.6634 0.7071 0.1171  -0.0227 -0.0358 945  ASP   A C   
1754 O O   . ASP   A 252 ? 0.8589 0.6686 0.7155 0.1232  -0.0205 -0.0234 945  ASP   A O   
1755 C CB  . ASP   A 252 ? 0.9365 0.6719 0.7485 0.0948  -0.0137 -0.0601 945  ASP   A CB  
1756 C CG  . ASP   A 252 ? 1.0451 0.7349 0.8263 0.0905  -0.0058 -0.0744 945  ASP   A CG  
1757 O OD1 . ASP   A 252 ? 1.0697 0.7603 0.8419 0.0877  -0.0125 -0.0880 945  ASP   A OD1 
1758 O OD2 . ASP   A 252 ? 1.0929 0.7427 0.8552 0.0905  0.0070  -0.0723 945  ASP   A OD2 
1759 N N   . VAL   A 253 ? 0.8336 0.6613 0.6906 0.1101  -0.0332 -0.0416 946  VAL   A N   
1760 C CA  . VAL   A 253 ? 0.8017 0.6678 0.6859 0.1092  -0.0401 -0.0324 946  VAL   A CA  
1761 C C   . VAL   A 253 ? 0.7849 0.6665 0.6710 0.1274  -0.0351 -0.0194 946  VAL   A C   
1762 O O   . VAL   A 253 ? 0.7790 0.6821 0.6861 0.1309  -0.0343 -0.0080 946  VAL   A O   
1763 C CB  . VAL   A 253 ? 0.7993 0.6849 0.6935 0.0979  -0.0532 -0.0429 946  VAL   A CB  
1764 C CG1 . VAL   A 253 ? 0.7806 0.7010 0.6995 0.0986  -0.0586 -0.0325 946  VAL   A CG1 
1765 C CG2 . VAL   A 253 ? 0.8071 0.6836 0.7092 0.0782  -0.0567 -0.0580 946  VAL   A CG2 
1766 N N   . TYR   A 254 ? 0.7807 0.6504 0.6451 0.1384  -0.0305 -0.0223 947  TYR   A N   
1767 C CA  . TYR   A 254 ? 0.7713 0.6542 0.6386 0.1545  -0.0214 -0.0120 947  TYR   A CA  
1768 C C   . TYR   A 254 ? 0.7644 0.6497 0.6444 0.1666  -0.0129 -0.0024 947  TYR   A C   
1769 O O   . TYR   A 254 ? 0.7485 0.6615 0.6519 0.1734  -0.0096 0.0068  947  TYR   A O   
1770 C CB  . TYR   A 254 ? 0.7864 0.6502 0.6227 0.1641  -0.0151 -0.0178 947  TYR   A CB  
1771 C CG  . TYR   A 254 ? 0.7853 0.6651 0.6281 0.1778  -0.0026 -0.0077 947  TYR   A CG  
1772 C CD1 . TYR   A 254 ? 0.7752 0.6832 0.6372 0.1745  -0.0041 -0.0001 947  TYR   A CD1 
1773 C CD2 . TYR   A 254 ? 0.8033 0.6706 0.6370 0.1937  0.0129  -0.0059 947  TYR   A CD2 
1774 C CE1 . TYR   A 254 ? 0.7798 0.7022 0.6515 0.1842  0.0107  0.0081  947  TYR   A CE1 
1775 C CE2 . TYR   A 254 ? 0.8052 0.6908 0.6521 0.2047  0.0273  0.0019  947  TYR   A CE2 
1776 C CZ  . TYR   A 254 ? 0.8004 0.7134 0.6666 0.1987  0.0268  0.0086  947  TYR   A CZ  
1777 O OH  . TYR   A 254 ? 0.8116 0.7415 0.6927 0.2067  0.0442  0.0149  947  TYR   A OH  
1778 N N   . MET   A 255 ? 0.7762 0.6324 0.6417 0.1691  -0.0100 -0.0054 948  MET   A N   
1779 C CA  . MET   A 255 ? 0.7835 0.6383 0.6566 0.1842  -0.0049 0.0031  948  MET   A CA  
1780 C C   . MET   A 255 ? 0.7670 0.6483 0.6679 0.1802  -0.0127 0.0117  948  MET   A C   
1781 O O   . MET   A 255 ? 0.7556 0.6550 0.6741 0.1943  -0.0117 0.0193  948  MET   A O   
1782 C CB  . MET   A 255 ? 0.8272 0.6366 0.6709 0.1891  0.0005  -0.0014 948  MET   A CB  
1783 C CG  . MET   A 255 ? 0.8891 0.6744 0.7081 0.2029  0.0115  -0.0068 948  MET   A CG  
1784 S SD  . MET   A 255 ? 0.9914 0.8046 0.8311 0.2290  0.0216  0.0021  948  MET   A SD  
1785 C CE  . MET   A 255 ? 0.9167 0.7511 0.7574 0.2217  0.0253  -0.0014 948  MET   A CE  
1786 N N   . ILE   A 256 ? 0.7611 0.6473 0.6678 0.1613  -0.0208 0.0093  949  ILE   A N   
1787 C CA  . ILE   A 256 ? 0.7453 0.6538 0.6746 0.1560  -0.0277 0.0164  949  ILE   A CA  
1788 C C   . ILE   A 256 ? 0.7141 0.6639 0.6720 0.1589  -0.0293 0.0222  949  ILE   A C   
1789 O O   . ILE   A 256 ? 0.7054 0.6753 0.6830 0.1663  -0.0317 0.0290  949  ILE   A O   
1790 C CB  . ILE   A 256 ? 0.7587 0.6598 0.6868 0.1350  -0.0328 0.0109  949  ILE   A CB  
1791 C CG1 . ILE   A 256 ? 0.7956 0.6531 0.6972 0.1306  -0.0274 0.0056  949  ILE   A CG1 
1792 C CG2 . ILE   A 256 ? 0.7508 0.6768 0.7014 0.1291  -0.0391 0.0178  949  ILE   A CG2 
1793 C CD1 . ILE   A 256 ? 0.8144 0.6646 0.7184 0.1078  -0.0285 -0.0031 949  ILE   A CD1 
1794 N N   . MET   A 257 ? 0.6924 0.6525 0.6505 0.1536  -0.0280 0.0189  950  MET   A N   
1795 C CA  . MET   A 257 ? 0.6683 0.6600 0.6484 0.1555  -0.0253 0.0244  950  MET   A CA  
1796 C C   . MET   A 257 ? 0.6518 0.6537 0.6426 0.1726  -0.0151 0.0283  950  MET   A C   
1797 O O   . MET   A 257 ? 0.6346 0.6660 0.6544 0.1748  -0.0140 0.0331  950  MET   A O   
1798 C CB  . MET   A 257 ? 0.6822 0.6725 0.6493 0.1510  -0.0238 0.0208  950  MET   A CB  
1799 C CG  . MET   A 257 ? 0.7256 0.7087 0.6840 0.1373  -0.0349 0.0141  950  MET   A CG  
1800 S SD  . MET   A 257 ? 0.8312 0.8091 0.7671 0.1389  -0.0357 0.0099  950  MET   A SD  
1801 C CE  . MET   A 257 ? 0.8100 0.7582 0.7178 0.1360  -0.0424 -0.0045 950  MET   A CE  
1802 N N   . ARG   A 258 ? 0.6562 0.6344 0.6256 0.1843  -0.0072 0.0246  951  ARG   A N   
1803 C CA  . ARG   A 258 ? 0.6527 0.6379 0.6316 0.2026  0.0042  0.0263  951  ARG   A CA  
1804 C C   . ARG   A 258 ? 0.6309 0.6335 0.6350 0.2129  -0.0022 0.0306  951  ARG   A C   
1805 O O   . ARG   A 258 ? 0.6182 0.6507 0.6528 0.2231  0.0031  0.0323  951  ARG   A O   
1806 C CB  . ARG   A 258 ? 0.7035 0.6517 0.6479 0.2123  0.0124  0.0204  951  ARG   A CB  
1807 C CG  . ARG   A 258 ? 0.7583 0.7092 0.7081 0.2325  0.0274  0.0204  951  ARG   A CG  
1808 C CD  . ARG   A 258 ? 0.7965 0.7752 0.7665 0.2331  0.0407  0.0223  951  ARG   A CD  
1809 N NE  . ARG   A 258 ? 0.8132 0.8331 0.8302 0.2395  0.0412  0.0262  951  ARG   A NE  
1810 C CZ  . ARG   A 258 ? 0.8127 0.8491 0.8529 0.2570  0.0529  0.0249  951  ARG   A CZ  
1811 N NH1 . ARG   A 258 ? 0.8183 0.8310 0.8363 0.2702  0.0682  0.0211  951  ARG   A NH1 
1812 N NH2 . ARG   A 258 ? 0.7768 0.8550 0.8641 0.2614  0.0498  0.0261  951  ARG   A NH2 
1813 N N   . LYS   A 259 ? 0.6213 0.6056 0.6132 0.2098  -0.0134 0.0316  952  LYS   A N   
1814 C CA  . LYS   A 259 ? 0.6031 0.5982 0.6101 0.2210  -0.0225 0.0359  952  LYS   A CA  
1815 C C   . LYS   A 259 ? 0.5728 0.6089 0.6153 0.2123  -0.0308 0.0390  952  LYS   A C   
1816 O O   . LYS   A 259 ? 0.5663 0.6257 0.6326 0.2242  -0.0377 0.0405  952  LYS   A O   
1817 C CB  . LYS   A 259 ? 0.6380 0.5928 0.6128 0.2206  -0.0291 0.0368  952  LYS   A CB  
1818 C CG  . LYS   A 259 ? 0.6995 0.6117 0.6406 0.2325  -0.0205 0.0336  952  LYS   A CG  
1819 C CD  . LYS   A 259 ? 0.7766 0.6423 0.6821 0.2274  -0.0228 0.0338  952  LYS   A CD  
1820 C CE  . LYS   A 259 ? 0.8486 0.6686 0.7200 0.2419  -0.0135 0.0312  952  LYS   A CE  
1821 N N   . CYS   A 260 ? 0.5490 0.5935 0.5949 0.1927  -0.0311 0.0388  953  CYS   A N   
1822 C CA  . CYS   A 260 ? 0.5183 0.5978 0.5954 0.1830  -0.0360 0.0409  953  CYS   A CA  
1823 C C   . CYS   A 260 ? 0.4901 0.6044 0.6012 0.1896  -0.0262 0.0401  953  CYS   A C   
1824 O O   . CYS   A 260 ? 0.4674 0.6135 0.6103 0.1850  -0.0302 0.0403  953  CYS   A O   
1825 C CB  . CYS   A 260 ? 0.5261 0.6018 0.5955 0.1632  -0.0369 0.0407  953  CYS   A CB  
1826 S SG  . CYS   A 260 ? 0.5854 0.6315 0.6294 0.1512  -0.0467 0.0397  953  CYS   A SG  
1827 N N   . TRP   A 261 ? 0.4923 0.5991 0.5963 0.1987  -0.0117 0.0380  954  TRP   A N   
1828 C CA  . TRP   A 261 ? 0.4779 0.6124 0.6109 0.2035  0.0035  0.0364  954  TRP   A CA  
1829 C C   . TRP   A 261 ? 0.4929 0.6410 0.6461 0.2250  0.0072  0.0333  954  TRP   A C   
1830 O O   . TRP   A 261 ? 0.4897 0.6460 0.6538 0.2326  0.0253  0.0305  954  TRP   A O   
1831 C CB  . TRP   A 261 ? 0.4780 0.5939 0.5871 0.1982  0.0200  0.0361  954  TRP   A CB  
1832 C CG  . TRP   A 261 ? 0.4861 0.5886 0.5746 0.1809  0.0143  0.0383  954  TRP   A CG  
1833 C CD1 . TRP   A 261 ? 0.4831 0.6017 0.5875 0.1672  0.0051  0.0407  954  TRP   A CD1 
1834 C CD2 . TRP   A 261 ? 0.5046 0.5751 0.5531 0.1772  0.0161  0.0369  954  TRP   A CD2 
1835 N NE1 . TRP   A 261 ? 0.4993 0.5988 0.5778 0.1564  0.0016  0.0415  954  TRP   A NE1 
1836 C CE2 . TRP   A 261 ? 0.5138 0.5853 0.5587 0.1625  0.0072  0.0387  954  TRP   A CE2 
1837 C CE3 . TRP   A 261 ? 0.5291 0.5703 0.5441 0.1856  0.0238  0.0332  954  TRP   A CE3 
1838 C CZ2 . TRP   A 261 ? 0.5325 0.5804 0.5447 0.1574  0.0037  0.0365  954  TRP   A CZ2 
1839 C CZ3 . TRP   A 261 ? 0.5586 0.5746 0.5386 0.1789  0.0196  0.0305  954  TRP   A CZ3 
1840 C CH2 . TRP   A 261 ? 0.5517 0.5730 0.5321 0.1656  0.0087  0.0320  954  TRP   A CH2 
1841 N N   . MET   A 262 ? 0.5080 0.6579 0.6655 0.2360  -0.0092 0.0336  955  MET   A N   
1842 C CA  . MET   A 262 ? 0.5286 0.6945 0.7081 0.2598  -0.0097 0.0303  955  MET   A CA  
1843 C C   . MET   A 262 ? 0.5246 0.7464 0.7631 0.2606  -0.0112 0.0254  955  MET   A C   
1844 O O   . MET   A 262 ? 0.5155 0.7565 0.7703 0.2447  -0.0202 0.0257  955  MET   A O   
1845 C CB  . MET   A 262 ? 0.5566 0.6953 0.7097 0.2742  -0.0272 0.0329  955  MET   A CB  
1846 C CG  . MET   A 262 ? 0.6351 0.7198 0.7361 0.2752  -0.0213 0.0349  955  MET   A CG  
1847 S SD  . MET   A 262 ? 0.7938 0.8427 0.8634 0.2946  -0.0373 0.0384  955  MET   A SD  
1848 C CE  . MET   A 262 ? 0.8880 0.8747 0.9011 0.2879  -0.0261 0.0384  955  MET   A CE  
1849 N N   . ILE   A 263 ? 0.5302 0.7790 0.8029 0.2783  -0.0016 0.0193  956  ILE   A N   
1850 C CA  . ILE   A 263 ? 0.5200 0.8270 0.8569 0.2796  -0.0020 0.0113  956  ILE   A CA  
1851 C C   . ILE   A 263 ? 0.5465 0.8715 0.8972 0.2868  -0.0320 0.0098  956  ILE   A C   
1852 O O   . ILE   A 263 ? 0.5376 0.8953 0.9203 0.2721  -0.0402 0.0060  956  ILE   A O   
1853 C CB  . ILE   A 263 ? 0.5028 0.8340 0.8742 0.3003  0.0149  0.0036  956  ILE   A CB  
1854 C CG1 . ILE   A 263 ? 0.5214 0.8322 0.8751 0.2924  0.0469  0.0048  956  ILE   A CG1 
1855 C CG2 . ILE   A 263 ? 0.4622 0.8594 0.9079 0.3027  0.0115  -0.0078 956  ILE   A CG2 
1856 C CD1 . ILE   A 263 ? 0.5310 0.8546 0.8981 0.2655  0.0631  0.0050  956  ILE   A CD1 
1857 N N   . ASP   A 264 ? 0.5819 0.8793 0.9020 0.3088  -0.0481 0.0130  957  ASP   A N   
1858 C CA  . ASP   A 264 ? 0.6030 0.9064 0.9225 0.3192  -0.0774 0.0128  957  ASP   A CA  
1859 C C   . ASP   A 264 ? 0.6333 0.9048 0.9126 0.2974  -0.0864 0.0204  957  ASP   A C   
1860 O O   . ASP   A 264 ? 0.6677 0.8886 0.8952 0.2930  -0.0814 0.0279  957  ASP   A O   
1861 C CB  . ASP   A 264 ? 0.6635 0.9389 0.9551 0.3518  -0.0887 0.0150  957  ASP   A CB  
1862 C CG  . ASP   A 264 ? 0.7742 1.0486 1.0558 0.3665  -0.1196 0.0156  957  ASP   A CG  
1863 O OD1 . ASP   A 264 ? 0.7737 1.0910 1.0932 0.3583  -0.1343 0.0092  957  ASP   A OD1 
1864 O OD2 . ASP   A 264 ? 0.8474 1.0748 1.0801 0.3862  -0.1287 0.0221  957  ASP   A OD2 
1865 N N   . ALA   A 265 ? 0.6160 0.9183 0.9219 0.2828  -0.0986 0.0169  958  ALA   A N   
1866 C CA  . ALA   A 265 ? 0.6439 0.9221 0.9188 0.2616  -0.1058 0.0226  958  ALA   A CA  
1867 C C   . ALA   A 265 ? 0.6902 0.9209 0.9110 0.2725  -0.1216 0.0296  958  ALA   A C   
1868 O O   . ALA   A 265 ? 0.7194 0.9111 0.9001 0.2571  -0.1167 0.0361  958  ALA   A O   
1869 C CB  . ALA   A 265 ? 0.6148 0.9357 0.9304 0.2474  -0.1161 0.0158  958  ALA   A CB  
1870 N N   . ASP   A 266 ? 0.6923 0.9246 0.9113 0.2999  -0.1394 0.0278  959  ASP   A N   
1871 C CA  . ASP   A 266 ? 0.7385 0.9191 0.9002 0.3135  -0.1529 0.0351  959  ASP   A CA  
1872 C C   . ASP   A 266 ? 0.7664 0.8906 0.8793 0.3182  -0.1370 0.0423  959  ASP   A C   
1873 O O   . ASP   A 266 ? 0.8109 0.8833 0.8708 0.3200  -0.1407 0.0490  959  ASP   A O   
1874 C CB  . ASP   A 266 ? 0.7728 0.9690 0.9428 0.3447  -0.1783 0.0310  959  ASP   A CB  
1875 C CG  . ASP   A 266 ? 0.8366 1.0760 1.0400 0.3380  -0.1991 0.0234  959  ASP   A CG  
1876 O OD1 . ASP   A 266 ? 0.8527 1.0848 1.0453 0.3118  -0.1971 0.0255  959  ASP   A OD1 
1877 O OD2 . ASP   A 266 ? 0.8571 1.1387 1.0989 0.3593  -0.2178 0.0140  959  ASP   A OD2 
1878 N N   . SER   A 267 ? 0.7384 0.8697 0.8669 0.3193  -0.1181 0.0401  960  SER   A N   
1879 C CA  . SER   A 267 ? 0.7565 0.8353 0.8404 0.3208  -0.1024 0.0447  960  SER   A CA  
1880 C C   . SER   A 267 ? 0.7467 0.8043 0.8108 0.2896  -0.0887 0.0468  960  SER   A C   
1881 O O   . SER   A 267 ? 0.7809 0.7910 0.8038 0.2859  -0.0791 0.0493  960  SER   A O   
1882 C CB  . SER   A 267 ? 0.7679 0.8594 0.8718 0.3378  -0.0888 0.0405  960  SER   A CB  
1883 O OG  . SER   A 267 ? 0.7921 0.8998 0.9122 0.3698  -0.1024 0.0379  960  SER   A OG  
1884 N N   . ARG   A 268 ? 0.6972 0.7889 0.7908 0.2678  -0.0881 0.0448  961  ARG   A N   
1885 C CA  . ARG   A 268 ? 0.6927 0.7680 0.7704 0.2412  -0.0783 0.0462  961  ARG   A CA  
1886 C C   . ARG   A 268 ? 0.7148 0.7502 0.7527 0.2325  -0.0852 0.0502  961  ARG   A C   
1887 O O   . ARG   A 268 ? 0.7255 0.7581 0.7562 0.2407  -0.0994 0.0524  961  ARG   A O   
1888 C CB  . ARG   A 268 ? 0.6531 0.7712 0.7694 0.2231  -0.0770 0.0438  961  ARG   A CB  
1889 C CG  . ARG   A 268 ? 0.6134 0.7658 0.7661 0.2270  -0.0645 0.0396  961  ARG   A CG  
1890 C CD  . ARG   A 268 ? 0.5817 0.7723 0.7709 0.2099  -0.0629 0.0373  961  ARG   A CD  
1891 N NE  . ARG   A 268 ? 0.5492 0.7774 0.7805 0.2164  -0.0516 0.0320  961  ARG   A NE  
1892 C CZ  . ARG   A 268 ? 0.5216 0.7923 0.7977 0.2088  -0.0521 0.0270  961  ARG   A CZ  
1893 N NH1 . ARG   A 268 ? 0.4962 0.7760 0.7781 0.1950  -0.0647 0.0269  961  ARG   A NH1 
1894 N NH2 . ARG   A 268 ? 0.4964 0.8002 0.8128 0.2142  -0.0383 0.0208  961  ARG   A NH2 
1895 N N   . PRO   A 269 ? 0.7231 0.7273 0.7349 0.2158  -0.0749 0.0502  962  PRO   A N   
1896 C CA  . PRO   A 269 ? 0.7398 0.7073 0.7181 0.2047  -0.0772 0.0526  962  PRO   A CA  
1897 C C   . PRO   A 269 ? 0.7119 0.7007 0.7044 0.1925  -0.0869 0.0538  962  PRO   A C   
1898 O O   . PRO   A 269 ? 0.6867 0.7172 0.7153 0.1861  -0.0896 0.0519  962  PRO   A O   
1899 C CB  . PRO   A 269 ? 0.7646 0.7125 0.7304 0.1857  -0.0643 0.0486  962  PRO   A CB  
1900 C CG  . PRO   A 269 ? 0.7493 0.7334 0.7459 0.1826  -0.0596 0.0455  962  PRO   A CG  
1901 C CD  . PRO   A 269 ? 0.7182 0.7199 0.7304 0.2056  -0.0611 0.0466  962  PRO   A CD  
1902 N N   . LYS   A 270 ? 0.7176 0.6737 0.6788 0.1891  -0.0903 0.0567  963  LYS   A N   
1903 C CA  . LYS   A 270 ? 0.6973 0.6657 0.6644 0.1769  -0.0978 0.0573  963  LYS   A CA  
1904 C C   . LYS   A 270 ? 0.6775 0.6373 0.6429 0.1514  -0.0863 0.0546  963  LYS   A C   
1905 O O   . LYS   A 270 ? 0.6910 0.6239 0.6396 0.1449  -0.0749 0.0523  963  LYS   A O   
1906 C CB  . LYS   A 270 ? 0.7491 0.6829 0.6781 0.1888  -0.1069 0.0618  963  LYS   A CB  
1907 C CG  . LYS   A 270 ? 0.8170 0.7553 0.7438 0.2184  -0.1207 0.0637  963  LYS   A CG  
1908 C CD  . LYS   A 270 ? 0.8528 0.8379 0.8132 0.2252  -0.1397 0.0608  963  LYS   A CD  
1909 N N   . PHE   A 271 ? 0.6443 0.6267 0.6279 0.1373  -0.0896 0.0536  964  PHE   A N   
1910 C CA  . PHE   A 271 ? 0.6382 0.6162 0.6241 0.1156  -0.0802 0.0502  964  PHE   A CA  
1911 C C   . PHE   A 271 ? 0.6793 0.6109 0.6296 0.1080  -0.0706 0.0496  964  PHE   A C   
1912 O O   . PHE   A 271 ? 0.6808 0.6037 0.6325 0.0941  -0.0602 0.0441  964  PHE   A O   
1913 C CB  . PHE   A 271 ? 0.6019 0.6077 0.6101 0.1043  -0.0850 0.0495  964  PHE   A CB  
1914 C CG  . PHE   A 271 ? 0.5661 0.6136 0.6108 0.1046  -0.0877 0.0485  964  PHE   A CG  
1915 C CD1 . PHE   A 271 ? 0.5651 0.6216 0.6217 0.0999  -0.0800 0.0461  964  PHE   A CD1 
1916 C CD2 . PHE   A 271 ? 0.5488 0.6239 0.6139 0.1091  -0.0972 0.0489  964  PHE   A CD2 
1917 C CE1 . PHE   A 271 ? 0.5522 0.6396 0.6356 0.1001  -0.0791 0.0461  964  PHE   A CE1 
1918 C CE2 . PHE   A 271 ? 0.5307 0.6403 0.6289 0.1068  -0.0954 0.0474  964  PHE   A CE2 
1919 C CZ  . PHE   A 271 ? 0.5280 0.6410 0.6328 0.1026  -0.0851 0.0468  964  PHE   A CZ  
1920 N N   . ARG   A 272 ? 0.7128 0.6131 0.6300 0.1182  -0.0738 0.0543  965  ARG   A N   
1921 C CA  . ARG   A 272 ? 0.7649 0.6121 0.6406 0.1127  -0.0616 0.0550  965  ARG   A CA  
1922 C C   . ARG   A 272 ? 0.7805 0.6013 0.6437 0.1128  -0.0498 0.0518  965  ARG   A C   
1923 O O   . ARG   A 272 ? 0.7992 0.5922 0.6499 0.0962  -0.0346 0.0467  965  ARG   A O   
1924 C CB  . ARG   A 272 ? 0.8300 0.6462 0.6665 0.1310  -0.0700 0.0623  965  ARG   A CB  
1925 C CG  . ARG   A 272 ? 0.9509 0.7094 0.7394 0.1231  -0.0560 0.0643  965  ARG   A CG  
1926 C CD  . ARG   A 272 ? 1.0789 0.7928 0.8162 0.1476  -0.0631 0.0725  965  ARG   A CD  
1927 N NE  . ARG   A 272 ? 1.1974 0.8689 0.8893 0.1450  -0.0588 0.0765  965  ARG   A NE  
1928 C CZ  . ARG   A 272 ? 1.2825 0.8977 0.9343 0.1318  -0.0358 0.0770  965  ARG   A CZ  
1929 N NH1 . ARG   A 272 ? 1.2978 0.8955 0.9536 0.1184  -0.0163 0.0721  965  ARG   A NH1 
1930 N NH2 . ARG   A 272 ? 1.3048 0.8802 0.9123 0.1307  -0.0310 0.0810  965  ARG   A NH2 
1931 N N   . GLU   A 273 ? 0.7678 0.5978 0.6360 0.1309  -0.0559 0.0534  966  GLU   A N   
1932 C CA  . GLU   A 273 ? 0.7750 0.5805 0.6303 0.1336  -0.0461 0.0500  966  GLU   A CA  
1933 C C   . GLU   A 273 ? 0.7397 0.5710 0.6248 0.1165  -0.0408 0.0409  966  GLU   A C   
1934 O O   . GLU   A 273 ? 0.7553 0.5610 0.6289 0.1052  -0.0294 0.0338  966  GLU   A O   
1935 C CB  . GLU   A 273 ? 0.8226 0.6334 0.6763 0.1604  -0.0544 0.0543  966  GLU   A CB  
1936 C CG  . GLU   A 273 ? 0.9504 0.7396 0.7758 0.1823  -0.0645 0.0625  966  GLU   A CG  
1937 C CD  . GLU   A 273 ? 1.0712 0.8782 0.9065 0.2108  -0.0758 0.0651  966  GLU   A CD  
1938 O OE1 . GLU   A 273 ? 1.0679 0.9104 0.9371 0.2121  -0.0747 0.0611  966  GLU   A OE1 
1939 O OE2 . GLU   A 273 ? 1.1423 0.9277 0.9510 0.2330  -0.0858 0.0708  966  GLU   A OE2 
1940 N N   . LEU   A 274 ? 0.6933 0.5733 0.6150 0.1148  -0.0494 0.0404  967  LEU   A N   
1941 C CA  . LEU   A 274 ? 0.6667 0.5710 0.6129 0.1017  -0.0472 0.0328  967  LEU   A CA  
1942 C C   . LEU   A 274 ? 0.6594 0.5540 0.6070 0.0794  -0.0402 0.0252  967  LEU   A C   
1943 O O   . LEU   A 274 ? 0.6581 0.5536 0.6129 0.0692  -0.0365 0.0157  967  LEU   A O   
1944 C CB  . LEU   A 274 ? 0.6396 0.5902 0.6181 0.1042  -0.0559 0.0356  967  LEU   A CB  
1945 C CG  . LEU   A 274 ? 0.6463 0.6146 0.6340 0.1230  -0.0598 0.0398  967  LEU   A CG  
1946 C CD1 . LEU   A 274 ? 0.6256 0.6355 0.6447 0.1225  -0.0659 0.0426  967  LEU   A CD1 
1947 C CD2 . LEU   A 274 ? 0.6542 0.6157 0.6366 0.1276  -0.0535 0.0353  967  LEU   A CD2 
1948 N N   . ILE   A 275 ? 0.6547 0.5389 0.5951 0.0725  -0.0380 0.0281  968  ILE   A N   
1949 C CA  . ILE   A 275 ? 0.6569 0.5321 0.6014 0.0514  -0.0282 0.0200  968  ILE   A CA  
1950 C C   . ILE   A 275 ? 0.6937 0.5281 0.6161 0.0434  -0.0144 0.0126  968  ILE   A C   
1951 O O   . ILE   A 275 ? 0.6904 0.5311 0.6297 0.0281  -0.0094 0.0003  968  ILE   A O   
1952 C CB  . ILE   A 275 ? 0.6512 0.5174 0.5864 0.0466  -0.0257 0.0250  968  ILE   A CB  
1953 C CG1 . ILE   A 275 ? 0.6235 0.5307 0.5840 0.0502  -0.0382 0.0295  968  ILE   A CG1 
1954 C CG2 . ILE   A 275 ? 0.6590 0.5083 0.5954 0.0250  -0.0100 0.0158  968  ILE   A CG2 
1955 C CD1 . ILE   A 275 ? 0.6336 0.5292 0.5775 0.0515  -0.0396 0.0356  968  ILE   A CD1 
1956 N N   . ILE   A 276 ? 0.7227 0.5156 0.6078 0.0551  -0.0094 0.0192  969  ILE   A N   
1957 C CA  . ILE   A 276 ? 0.7607 0.5061 0.6181 0.0486  0.0059  0.0134  969  ILE   A CA  
1958 C C   . ILE   A 276 ? 0.7696 0.5240 0.6393 0.0472  0.0045  0.0036  969  ILE   A C   
1959 O O   . ILE   A 276 ? 0.7801 0.5221 0.6546 0.0285  0.0148  -0.0098 969  ILE   A O   
1960 C CB  . ILE   A 276 ? 0.8014 0.4977 0.6108 0.0669  0.0094  0.0250  969  ILE   A CB  
1961 C CG1 . ILE   A 276 ? 0.8245 0.5053 0.6147 0.0662  0.0113  0.0328  969  ILE   A CG1 
1962 C CG2 . ILE   A 276 ? 0.8294 0.4688 0.6041 0.0626  0.0268  0.0200  969  ILE   A CG2 
1963 C CD1 . ILE   A 276 ? 0.8695 0.5120 0.6135 0.0913  0.0062  0.0459  969  ILE   A CD1 
1964 N N   . GLU   A 277 ? 0.7598 0.5372 0.6364 0.0658  -0.0077 0.0085  970  GLU   A N   
1965 C CA  . GLU   A 277 ? 0.7587 0.5417 0.6411 0.0666  -0.0090 -0.0004 970  GLU   A CA  
1966 C C   . GLU   A 277 ? 0.7366 0.5518 0.6508 0.0485  -0.0131 -0.0137 970  GLU   A C   
1967 O O   . GLU   A 277 ? 0.7491 0.5497 0.6617 0.0355  -0.0076 -0.0275 970  GLU   A O   
1968 C CB  . GLU   A 277 ? 0.7827 0.5861 0.6681 0.0898  -0.0187 0.0078  970  GLU   A CB  
1969 C CG  . GLU   A 277 ? 0.8664 0.6388 0.7224 0.1111  -0.0164 0.0178  970  GLU   A CG  
1970 N N   . PHE   A 278 ? 0.7052 0.5627 0.6476 0.0480  -0.0233 -0.0105 971  PHE   A N   
1971 C CA  . PHE   A 278 ? 0.6863 0.5743 0.6571 0.0351  -0.0295 -0.0222 971  PHE   A CA  
1972 C C   . PHE   A 278 ? 0.6899 0.5694 0.6720 0.0127  -0.0206 -0.0348 971  PHE   A C   
1973 O O   . PHE   A 278 ? 0.6852 0.5815 0.6881 0.0015  -0.0248 -0.0498 971  PHE   A O   
1974 C CB  . PHE   A 278 ? 0.6605 0.5895 0.6543 0.0416  -0.0407 -0.0148 971  PHE   A CB  
1975 C CG  . PHE   A 278 ? 0.6673 0.6104 0.6582 0.0581  -0.0478 -0.0093 971  PHE   A CG  
1976 C CD1 . PHE   A 278 ? 0.6791 0.6298 0.6709 0.0586  -0.0534 -0.0185 971  PHE   A CD1 
1977 C CD2 . PHE   A 278 ? 0.6734 0.6212 0.6599 0.0733  -0.0483 0.0037  971  PHE   A CD2 
1978 C CE1 . PHE   A 278 ? 0.6883 0.6470 0.6726 0.0736  -0.0564 -0.0131 971  PHE   A CE1 
1979 C CE2 . PHE   A 278 ? 0.6775 0.6387 0.6644 0.0869  -0.0509 0.0076  971  PHE   A CE2 
1980 C CZ  . PHE   A 278 ? 0.6794 0.6434 0.6628 0.0869  -0.0533 -0.0001 971  PHE   A CZ  
1981 N N   . SER   A 279 ? 0.6964 0.5495 0.6648 0.0066  -0.0080 -0.0298 972  SER   A N   
1982 C CA  . SER   A 279 ? 0.6992 0.5401 0.6776 -0.0160 0.0059  -0.0420 972  SER   A CA  
1983 C C   . SER   A 279 ? 0.7271 0.5364 0.6941 -0.0279 0.0168  -0.0563 972  SER   A C   
1984 O O   . SER   A 279 ? 0.7217 0.5399 0.7140 -0.0481 0.0223  -0.0740 972  SER   A O   
1985 C CB  . SER   A 279 ? 0.7153 0.5279 0.6726 -0.0183 0.0191  -0.0319 972  SER   A CB  
1986 O OG  . SER   A 279 ? 0.7011 0.5459 0.6773 -0.0154 0.0111  -0.0250 972  SER   A OG  
1987 N N   . LYS   A 280 ? 0.7523 0.5256 0.6837 -0.0155 0.0201  -0.0500 973  LYS   A N   
1988 C CA  . LYS   A 280 ? 0.7816 0.5195 0.6969 -0.0250 0.0306  -0.0630 973  LYS   A CA  
1989 C C   . LYS   A 280 ? 0.7760 0.5477 0.7183 -0.0296 0.0164  -0.0796 973  LYS   A C   
1990 O O   . LYS   A 280 ? 0.7785 0.5457 0.7346 -0.0496 0.0219  -0.0997 973  LYS   A O   
1991 C CB  . LYS   A 280 ? 0.8332 0.5270 0.7029 -0.0050 0.0351  -0.0503 973  LYS   A CB  
1992 C CG  . LYS   A 280 ? 0.9042 0.5597 0.7534 -0.0113 0.0445  -0.0631 973  LYS   A CG  
1993 N N   . MET   A 281 ? 0.7635 0.5685 0.7127 -0.0115 -0.0017 -0.0721 974  MET   A N   
1994 C CA  . MET   A 281 ? 0.7498 0.5833 0.7158 -0.0114 -0.0170 -0.0854 974  MET   A CA  
1995 C C   . MET   A 281 ? 0.7277 0.6001 0.7350 -0.0271 -0.0254 -0.1005 974  MET   A C   
1996 O O   . MET   A 281 ? 0.7219 0.6050 0.7425 -0.0359 -0.0336 -0.1199 974  MET   A O   
1997 C CB  . MET   A 281 ? 0.7489 0.6022 0.7070 0.0122  -0.0301 -0.0717 974  MET   A CB  
1998 C CG  . MET   A 281 ? 0.7916 0.6115 0.7151 0.0286  -0.0228 -0.0609 974  MET   A CG  
1999 S SD  . MET   A 281 ? 0.8346 0.6790 0.7539 0.0539  -0.0337 -0.0479 974  MET   A SD  
2000 C CE  . MET   A 281 ? 0.8695 0.6674 0.7498 0.0690  -0.0221 -0.0441 974  MET   A CE  
2001 N N   . ALA   A 282 ? 0.7149 0.6081 0.7426 -0.0302 -0.0239 -0.0932 975  ALA   A N   
2002 C CA  . ALA   A 282 ? 0.7005 0.6315 0.7703 -0.0434 -0.0306 -0.1075 975  ALA   A CA  
2003 C C   . ALA   A 282 ? 0.7171 0.6364 0.8059 -0.0695 -0.0166 -0.1294 975  ALA   A C   
2004 O O   . ALA   A 282 ? 0.6919 0.6452 0.8200 -0.0806 -0.0247 -0.1480 975  ALA   A O   
2005 C CB  . ALA   A 282 ? 0.6866 0.6380 0.7705 -0.0397 -0.0298 -0.0941 975  ALA   A CB  
2006 N N   . ARG   A 283 ? 0.7592 0.6299 0.8204 -0.0788 0.0046  -0.1282 976  ARG   A N   
2007 C CA  . ARG   A 283 ? 0.7833 0.6356 0.8589 -0.1058 0.0225  -0.1495 976  ARG   A CA  
2008 C C   . ARG   A 283 ? 0.8060 0.6623 0.8902 -0.1136 0.0125  -0.1725 976  ARG   A C   
2009 O O   . ARG   A 283 ? 0.8029 0.6684 0.9200 -0.1374 0.0187  -0.1971 976  ARG   A O   
2010 C CB  . ARG   A 283 ? 0.8276 0.6190 0.8639 -0.1124 0.0505  -0.1394 976  ARG   A CB  
2011 C CG  . ARG   A 283 ? 0.8711 0.6606 0.9047 -0.1107 0.0611  -0.1236 976  ARG   A CG  
2012 C CD  . ARG   A 283 ? 0.9499 0.6776 0.9477 -0.1226 0.0916  -0.1189 976  ARG   A CD  
2013 N NE  . ARG   A 283 ? 1.0299 0.7087 0.9706 -0.1023 0.0939  -0.0996 976  ARG   A NE  
2014 C CZ  . ARG   A 283 ? 1.0874 0.7597 1.0009 -0.0802 0.0875  -0.0767 976  ARG   A CZ  
2015 N NH1 . ARG   A 283 ? 1.1223 0.7525 0.9879 -0.0607 0.0884  -0.0619 976  ARG   A NH1 
2016 N NH2 . ARG   A 283 ? 1.0740 0.7829 1.0093 -0.0766 0.0792  -0.0697 976  ARG   A NH2 
2017 N N   . ASP   A 284 ? 0.8237 0.6747 0.8804 -0.0941 -0.0029 -0.1662 977  ASP   A N   
2018 C CA  . ASP   A 284 ? 0.8321 0.6859 0.8900 -0.0978 -0.0159 -0.1872 977  ASP   A CA  
2019 C C   . ASP   A 284 ? 0.8314 0.7128 0.8795 -0.0719 -0.0417 -0.1779 977  ASP   A C   
2020 O O   . ASP   A 284 ? 0.8565 0.7123 0.8662 -0.0558 -0.0428 -0.1680 977  ASP   A O   
2021 C CB  . ASP   A 284 ? 0.8899 0.6840 0.9056 -0.1017 0.0015  -0.1883 977  ASP   A CB  
2022 C CG  . ASP   A 284 ? 0.9699 0.7581 0.9871 -0.1132 -0.0062 -0.2149 977  ASP   A CG  
2023 O OD1 . ASP   A 284 ? 0.9549 0.7881 1.0087 -0.1190 -0.0270 -0.2348 977  ASP   A OD1 
2024 O OD2 . ASP   A 284 ? 1.0351 0.7722 1.0157 -0.1155 0.0077  -0.2166 977  ASP   A OD2 
2025 N N   . PRO   A 285 ? 0.8019 0.7324 0.8818 -0.0661 -0.0604 -0.1797 978  PRO   A N   
2026 C CA  . PRO   A 285 ? 0.8023 0.7509 0.8659 -0.0406 -0.0800 -0.1665 978  PRO   A CA  
2027 C C   . PRO   A 285 ? 0.8115 0.7560 0.8539 -0.0317 -0.0970 -0.1789 978  PRO   A C   
2028 O O   . PRO   A 285 ? 0.8249 0.7623 0.8362 -0.0106 -0.1027 -0.1639 978  PRO   A O   
2029 C CB  . PRO   A 285 ? 0.7789 0.7742 0.8803 -0.0386 -0.0927 -0.1665 978  PRO   A CB  
2030 C CG  . PRO   A 285 ? 0.7631 0.7742 0.9068 -0.0628 -0.0880 -0.1896 978  PRO   A CG  
2031 C CD  . PRO   A 285 ? 0.7638 0.7313 0.8928 -0.0805 -0.0612 -0.1906 978  PRO   A CD  
2032 N N   . GLN   A 286 ? 0.8016 0.7497 0.8599 -0.0478 -0.1044 -0.2068 979  GLN   A N   
2033 C CA  . GLN   A 286 ? 0.8204 0.7613 0.8543 -0.0398 -0.1220 -0.2209 979  GLN   A CA  
2034 C C   . GLN   A 286 ? 0.8534 0.7429 0.8374 -0.0334 -0.1077 -0.2130 979  GLN   A C   
2035 O O   . GLN   A 286 ? 0.8705 0.7484 0.8231 -0.0208 -0.1195 -0.2178 979  GLN   A O   
2036 C CB  . GLN   A 286 ? 0.8288 0.7904 0.8969 -0.0599 -0.1358 -0.2561 979  GLN   A CB  
2037 C CG  . GLN   A 286 ? 0.8383 0.8553 0.9504 -0.0570 -0.1594 -0.2669 979  GLN   A CG  
2038 N N   . ARG   A 287 ? 0.8616 0.7184 0.8354 -0.0401 -0.0823 -0.2009 980  ARG   A N   
2039 C CA  . ARG   A 287 ? 0.8946 0.7017 0.8230 -0.0315 -0.0670 -0.1914 980  ARG   A CA  
2040 C C   . ARG   A 287 ? 0.8918 0.6982 0.7942 -0.0033 -0.0666 -0.1637 980  ARG   A C   
2041 O O   . ARG   A 287 ? 0.9209 0.6955 0.7864 0.0101  -0.0598 -0.1576 980  ARG   A O   
2042 C CB  . ARG   A 287 ? 0.9349 0.7056 0.8609 -0.0471 -0.0405 -0.1879 980  ARG   A CB  
2043 C CG  . ARG   A 287 ? 1.0257 0.7388 0.9084 -0.0453 -0.0248 -0.1892 980  ARG   A CG  
2044 C CD  . ARG   A 287 ? 1.1037 0.7836 0.9586 -0.0303 -0.0062 -0.1631 980  ARG   A CD  
2045 N NE  . ARG   A 287 ? 1.1736 0.8165 1.0253 -0.0487 0.0166  -0.1648 980  ARG   A NE  
2046 C CZ  . ARG   A 287 ? 1.2446 0.8298 1.0562 -0.0433 0.0361  -0.1566 980  ARG   A CZ  
2047 N NH1 . ARG   A 287 ? 1.2548 0.8173 1.0312 -0.0198 0.0352  -0.1471 980  ARG   A NH1 
2048 N NH2 . ARG   A 287 ? 1.2665 0.8139 1.0710 -0.0602 0.0581  -0.1577 980  ARG   A NH2 
2049 N N   . TYR   A 288 ? 0.8552 0.6960 0.7783 0.0049  -0.0723 -0.1483 981  TYR   A N   
2050 C CA  . TYR   A 288 ? 0.8485 0.6923 0.7551 0.0277  -0.0697 -0.1236 981  TYR   A CA  
2051 C C   . TYR   A 288 ? 0.8355 0.7084 0.7414 0.0426  -0.0868 -0.1202 981  TYR   A C   
2052 O O   . TYR   A 288 ? 0.8427 0.7095 0.7259 0.0611  -0.0834 -0.1057 981  TYR   A O   
2053 C CB  . TYR   A 288 ? 0.8317 0.6822 0.7550 0.0263  -0.0585 -0.1063 981  TYR   A CB  
2054 C CG  . TYR   A 288 ? 0.8512 0.6617 0.7617 0.0165  -0.0396 -0.1063 981  TYR   A CG  
2055 C CD1 . TYR   A 288 ? 0.8814 0.6548 0.7577 0.0302  -0.0283 -0.0969 981  TYR   A CD1 
2056 C CD2 . TYR   A 288 ? 0.8534 0.6596 0.7837 -0.0064 -0.0318 -0.1178 981  TYR   A CD2 
2057 C CE1 . TYR   A 288 ? 0.9115 0.6414 0.7692 0.0236  -0.0109 -0.0963 981  TYR   A CE1 
2058 C CE2 . TYR   A 288 ? 0.8834 0.6447 0.7948 -0.0156 -0.0118 -0.1176 981  TYR   A CE2 
2059 C CZ  . TYR   A 288 ? 0.9241 0.6454 0.7967 0.0003  -0.0021 -0.1060 981  TYR   A CZ  
2060 O OH  . TYR   A 288 ? 0.9790 0.6492 0.8265 -0.0064 0.0179  -0.1050 981  TYR   A OH  
2061 N N   . LEU   A 289 ? 0.8141 0.7170 0.7437 0.0353  -0.1042 -0.1337 982  LEU   A N   
2062 C CA  . LEU   A 289 ? 0.8171 0.7408 0.7389 0.0507  -0.1215 -0.1313 982  LEU   A CA  
2063 C C   . LEU   A 289 ? 0.8308 0.7580 0.7480 0.0469  -0.1417 -0.1564 982  LEU   A C   
2064 O O   . LEU   A 289 ? 0.8191 0.7615 0.7677 0.0290  -0.1489 -0.1763 982  LEU   A O   
2065 C CB  . LEU   A 289 ? 0.7916 0.7507 0.7443 0.0520  -0.1271 -0.1212 982  LEU   A CB  
2066 C CG  . LEU   A 289 ? 0.7986 0.7592 0.7561 0.0573  -0.1114 -0.0972 982  LEU   A CG  
2067 C CD1 . LEU   A 289 ? 0.7813 0.7743 0.7670 0.0574  -0.1183 -0.0907 982  LEU   A CD1 
2068 C CD2 . LEU   A 289 ? 0.8195 0.7641 0.7450 0.0759  -0.1037 -0.0814 982  LEU   A CD2 
2069 N N   . VAL   A 290 ? 0.8525 0.7654 0.7307 0.0633  -0.1506 -0.1570 983  VAL   A N   
2070 C CA  . VAL   A 290 ? 0.8669 0.7800 0.7322 0.0633  -0.1731 -0.1811 983  VAL   A CA  
2071 C C   . VAL   A 290 ? 0.8718 0.8091 0.7332 0.0797  -0.1948 -0.1784 983  VAL   A C   
2072 O O   . VAL   A 290 ? 0.8935 0.8156 0.7158 0.0995  -0.1933 -0.1637 983  VAL   A O   
2073 C CB  . VAL   A 290 ? 0.9038 0.7752 0.7188 0.0709  -0.1680 -0.1861 983  VAL   A CB  
2074 C CG1 . VAL   A 290 ? 0.9134 0.7835 0.7139 0.0692  -0.1935 -0.2143 983  VAL   A CG1 
2075 C CG2 . VAL   A 290 ? 0.9180 0.7599 0.7321 0.0586  -0.1440 -0.1847 983  VAL   A CG2 
2076 N N   . ILE   A 291 ? 0.8485 0.8219 0.7505 0.0720  -0.2127 -0.1920 984  ILE   A N   
2077 C CA  . ILE   A 291 ? 0.8578 0.8534 0.7575 0.0892  -0.2341 -0.1894 984  ILE   A CA  
2078 C C   . ILE   A 291 ? 0.8765 0.8896 0.7830 0.0897  -0.2663 -0.2190 984  ILE   A C   
2079 O O   . ILE   A 291 ? 0.8559 0.8893 0.8050 0.0693  -0.2715 -0.2420 984  ILE   A O   
2080 C CB  . ILE   A 291 ? 0.8325 0.8592 0.7766 0.0848  -0.2273 -0.1761 984  ILE   A CB  
2081 C CG1 . ILE   A 291 ? 0.8480 0.8587 0.7818 0.0873  -0.1998 -0.1476 984  ILE   A CG1 
2082 C CG2 . ILE   A 291 ? 0.8276 0.8779 0.7746 0.1018  -0.2503 -0.1761 984  ILE   A CG2 
2083 C CD1 . ILE   A 291 ? 0.8395 0.8741 0.8130 0.0798  -0.1907 -0.1366 984  ILE   A CD1 
2084 N N   . GLN   A 292 ? 0.9140 0.9186 0.7783 0.1129  -0.2878 -0.2198 985  GLN   A N   
2085 C CA  . GLN   A 292 ? 0.9344 0.9578 0.8028 0.1177  -0.3238 -0.2487 985  GLN   A CA  
2086 C C   . GLN   A 292 ? 0.9235 0.9968 0.8524 0.1148  -0.3381 -0.2555 985  GLN   A C   
2087 O O   . GLN   A 292 ? 0.9251 1.0052 0.8545 0.1277  -0.3330 -0.2337 985  GLN   A O   
2088 C CB  . GLN   A 292 ? 0.9865 0.9825 0.7862 0.1472  -0.3423 -0.2438 985  GLN   A CB  
2089 C CG  . GLN   A 292 ? 1.0402 1.0496 0.8342 0.1546  -0.3824 -0.2754 985  GLN   A CG  
2090 C CD  . GLN   A 292 ? 1.1339 1.1182 0.8597 0.1878  -0.4036 -0.2684 985  GLN   A CD  
2091 O OE1 . GLN   A 292 ? 1.1778 1.1462 0.8750 0.2053  -0.3917 -0.2407 985  GLN   A OE1 
2092 N NE2 . GLN   A 292 ? 1.1514 1.1288 0.8474 0.1969  -0.4355 -0.2941 985  GLN   A NE2 
2093 N N   . GLY   A 293 ? 0.9044 1.0115 0.8870 0.0960  -0.3517 -0.2853 986  GLY   A N   
2094 C CA  . GLY   A 293 ? 0.8783 1.0352 0.9254 0.0914  -0.3615 -0.2937 986  GLY   A CA  
2095 C C   . GLY   A 293 ? 0.8584 1.0338 0.9666 0.0598  -0.3359 -0.2992 986  GLY   A C   
2096 O O   . GLY   A 293 ? 0.8282 1.0470 0.9976 0.0503  -0.3429 -0.3146 986  GLY   A O   
2097 N N   . ASP   A 294 ? 0.8732 1.0138 0.9636 0.0445  -0.3050 -0.2867 987  ASP   A N   
2098 C CA  . ASP   A 294 ? 0.8622 1.0078 0.9976 0.0145  -0.2789 -0.2925 987  ASP   A CA  
2099 C C   . ASP   A 294 ? 0.8685 1.0189 1.0291 -0.0092 -0.2851 -0.3283 987  ASP   A C   
2100 O O   . ASP   A 294 ? 0.8608 1.0133 1.0594 -0.0363 -0.2631 -0.3373 987  ASP   A O   
2101 C CB  . ASP   A 294 ? 0.8915 0.9953 0.9943 0.0108  -0.2452 -0.2645 987  ASP   A CB  
2102 C CG  . ASP   A 294 ? 0.9039 1.0154 1.0171 0.0167  -0.2291 -0.2369 987  ASP   A CG  
2103 O OD1 . ASP   A 294 ? 0.8743 1.0224 1.0326 0.0133  -0.2348 -0.2423 987  ASP   A OD1 
2104 O OD2 . ASP   A 294 ? 0.9417 1.0236 1.0196 0.0246  -0.2109 -0.2114 987  ASP   A OD2 
2105 N N   . GLU   A 295 ? 0.8812 1.0308 1.0194 0.0001  -0.3141 -0.3495 988  GLU   A N   
2106 C CA  . GLU   A 295 ? 0.8866 1.0421 1.0488 -0.0225 -0.3228 -0.3862 988  GLU   A CA  
2107 C C   . GLU   A 295 ? 0.8570 1.0742 1.0942 -0.0325 -0.3448 -0.4172 988  GLU   A C   
2108 O O   . GLU   A 295 ? 0.8486 1.0888 1.0963 -0.0293 -0.3782 -0.4480 988  GLU   A O   
2109 C CB  . GLU   A 295 ? 0.9389 1.0652 1.0418 -0.0080 -0.3451 -0.3971 988  GLU   A CB  
2110 N N   . ARG   A 296 ? 0.8358 1.0805 1.1262 -0.0444 -0.3260 -0.4103 989  ARG   A N   
2111 C CA  . ARG   A 296 ? 0.8017 1.1075 1.1709 -0.0548 -0.3407 -0.4383 989  ARG   A CA  
2112 C C   . ARG   A 296 ? 0.7857 1.0993 1.2085 -0.0950 -0.3204 -0.4681 989  ARG   A C   
2113 O O   . ARG   A 296 ? 0.7469 1.1128 1.2415 -0.1089 -0.3317 -0.4993 989  ARG   A O   
2114 C CB  . ARG   A 296 ? 0.8105 1.1395 1.2074 -0.0461 -0.3285 -0.4158 989  ARG   A CB  
2115 C CG  . ARG   A 296 ? 0.8768 1.1963 1.2240 -0.0088 -0.3444 -0.3862 989  ARG   A CG  
2116 C CD  . ARG   A 296 ? 0.9074 1.2425 1.2788 -0.0039 -0.3277 -0.3635 989  ARG   A CD  
2117 N NE  . ARG   A 296 ? 0.9868 1.2761 1.3135 -0.0045 -0.2954 -0.3278 989  ARG   A NE  
2118 C CZ  . ARG   A 296 ? 1.0201 1.2939 1.3624 -0.0286 -0.2605 -0.3201 989  ARG   A CZ  
2119 N NH1 . ARG   A 296 ? 1.0375 1.2718 1.3369 -0.0249 -0.2367 -0.2886 989  ARG   A NH1 
2120 N NH2 . ARG   A 296 ? 0.9979 1.2948 1.3982 -0.0562 -0.2488 -0.3445 989  ARG   A NH2 
2121 N N   . ALA   B 9   ? 1.1709 1.0152 1.1170 0.1774  0.0705  -0.0015 702  ALA   B N   
2122 C CA  . ALA   B 9   ? 1.2157 1.0027 1.1048 0.1833  0.0827  -0.0071 702  ALA   B CA  
2123 C C   . ALA   B 9   ? 1.2341 0.9918 1.1083 0.2009  0.0766  -0.0064 702  ALA   B C   
2124 O O   . ALA   B 9   ? 1.2274 1.0025 1.1234 0.2026  0.0573  -0.0015 702  ALA   B O   
2125 C CB  . ALA   B 9   ? 1.2450 1.0009 1.0853 0.1584  0.0737  -0.0113 702  ALA   B CB  
2126 N N   . LEU   B 10  ? 1.2556 0.9641 1.0882 0.2145  0.0932  -0.0112 703  LEU   B N   
2127 C CA  . LEU   B 10  ? 1.2672 0.9381 1.0776 0.2314  0.0887  -0.0107 703  LEU   B CA  
2128 C C   . LEU   B 10  ? 1.2846 0.9194 1.0506 0.2098  0.0680  -0.0119 703  LEU   B C   
2129 O O   . LEU   B 10  ? 1.2958 0.9223 1.0373 0.1845  0.0627  -0.0156 703  LEU   B O   
2130 C CB  . LEU   B 10  ? 1.2955 0.9192 1.0704 0.2520  0.1143  -0.0164 703  LEU   B CB  
2131 N N   . LEU   B 11  ? 1.2814 0.8957 1.0389 0.2196  0.0562  -0.0081 704  LEU   B N   
2132 C CA  . LEU   B 11  ? 1.2944 0.8743 1.0125 0.1995  0.0392  -0.0083 704  LEU   B CA  
2133 C C   . LEU   B 11  ? 1.3236 0.8318 0.9791 0.2011  0.0476  -0.0142 704  LEU   B C   
2134 O O   . LEU   B 11  ? 1.3419 0.8203 0.9858 0.2267  0.0573  -0.0138 704  LEU   B O   
2135 C CB  . LEU   B 11  ? 1.2830 0.8783 1.0223 0.2059  0.0206  0.0001  704  LEU   B CB  
2136 C CG  . LEU   B 11  ? 1.3254 0.8824 1.0243 0.1881  0.0062  0.0016  704  LEU   B CG  
2137 C CD1 . LEU   B 11  ? 1.3202 0.9004 1.0231 0.1566  -0.0035 0.0001  704  LEU   B CD1 
2138 C CD2 . LEU   B 11  ? 1.3329 0.8882 1.0399 0.2038  -0.0074 0.0102  704  LEU   B CD2 
2139 N N   . ARG   B 12  ? 1.3285 0.8085 0.9444 0.1740  0.0431  -0.0199 705  ARG   B N   
2140 C CA  . ARG   B 12  ? 1.3631 0.7722 0.9163 0.1699  0.0482  -0.0265 705  ARG   B CA  
2141 C C   . ARG   B 12  ? 1.3634 0.7385 0.8930 0.1634  0.0347  -0.0225 705  ARG   B C   
2142 O O   . ARG   B 12  ? 1.3446 0.7406 0.8861 0.1423  0.0193  -0.0186 705  ARG   B O   
2143 C CB  . ARG   B 12  ? 1.4010 0.7936 0.9218 0.1429  0.0475  -0.0347 705  ARG   B CB  
2144 C CG  . ARG   B 12  ? 1.4599 0.8499 0.9721 0.1532  0.0667  -0.0407 705  ARG   B CG  
2145 C CD  . ARG   B 12  ? 1.5081 0.9287 1.0286 0.1300  0.0607  -0.0426 705  ARG   B CD  
2146 N NE  . ARG   B 12  ? 1.5082 0.9988 1.0912 0.1285  0.0534  -0.0349 705  ARG   B NE  
2147 C CZ  . ARG   B 12  ? 1.5157 1.0406 1.1160 0.1105  0.0463  -0.0343 705  ARG   B CZ  
2148 N NH1 . ARG   B 12  ? 1.5357 1.0348 1.0977 0.0926  0.0434  -0.0403 705  ARG   B NH1 
2149 N NH2 . ARG   B 12  ? 1.4763 1.0592 1.1305 0.1102  0.0405  -0.0278 705  ARG   B NH2 
2150 N N   . ILE   B 13  ? 1.3835 0.7040 0.8784 0.1825  0.0422  -0.0231 706  ILE   B N   
2151 C CA  . ILE   B 13  ? 1.4045 0.6805 0.8673 0.1768  0.0319  -0.0191 706  ILE   B CA  
2152 C C   . ILE   B 13  ? 1.4420 0.6573 0.8452 0.1520  0.0333  -0.0282 706  ILE   B C   
2153 O O   . ILE   B 13  ? 1.4753 0.6444 0.8408 0.1619  0.0469  -0.0361 706  ILE   B O   
2154 C CB  . ILE   B 13  ? 1.4196 0.6689 0.8787 0.2127  0.0373  -0.0135 706  ILE   B CB  
2155 C CG1 . ILE   B 13  ? 1.3900 0.7053 0.9129 0.2330  0.0299  -0.0038 706  ILE   B CG1 
2156 C CG2 . ILE   B 13  ? 1.4588 0.6451 0.8694 0.2059  0.0295  -0.0101 706  ILE   B CG2 
2157 N N   . LEU   B 14  ? 1.4378 0.6563 0.8349 0.1188  0.0195  -0.0279 707  LEU   B N   
2158 C CA  . LEU   B 14  ? 1.4768 0.6461 0.8254 0.0903  0.0168  -0.0363 707  LEU   B CA  
2159 C C   . LEU   B 14  ? 1.5226 0.6238 0.8238 0.0843  0.0148  -0.0348 707  LEU   B C   
2160 O O   . LEU   B 14  ? 1.5191 0.6190 0.8283 0.0952  0.0116  -0.0253 707  LEU   B O   
2161 C CB  . LEU   B 14  ? 1.4597 0.6734 0.8334 0.0562  0.0032  -0.0369 707  LEU   B CB  
2162 C CG  . LEU   B 14  ? 1.4662 0.7135 0.8544 0.0489  0.0037  -0.0433 707  LEU   B CG  
2163 C CD1 . LEU   B 14  ? 1.4427 0.7402 0.8736 0.0755  0.0131  -0.0397 707  LEU   B CD1 
2164 C CD2 . LEU   B 14  ? 1.4526 0.7399 0.8658 0.0172  -0.0114 -0.0426 707  LEU   B CD2 
2165 N N   . LYS   B 15  ? 1.5658 0.6062 0.8139 0.0666  0.0160  -0.0441 708  LYS   B N   
2166 C CA  . LYS   B 15  ? 1.6152 0.5841 0.8128 0.0547  0.0144  -0.0440 708  LYS   B CA  
2167 C C   . LYS   B 15  ? 1.6256 0.5988 0.8208 0.0096  0.0008  -0.0462 708  LYS   B C   
2168 O O   . LYS   B 15  ? 1.6042 0.6139 0.8181 -0.0091 -0.0061 -0.0518 708  LYS   B O   
2169 C CB  . LYS   B 15  ? 1.6835 0.5737 0.8194 0.0667  0.0262  -0.0541 708  LYS   B CB  
2170 C CG  . LYS   B 15  ? 1.7343 0.6168 0.8732 0.1129  0.0425  -0.0524 708  LYS   B CG  
2171 N N   . GLU   B 16  ? 1.6594 0.5943 0.8316 -0.0079 -0.0028 -0.0415 709  GLU   B N   
2172 C CA  . GLU   B 16  ? 1.6770 0.6162 0.8511 -0.0516 -0.0137 -0.0431 709  GLU   B CA  
2173 C C   . GLU   B 16  ? 1.7110 0.6179 0.8525 -0.0764 -0.0196 -0.0566 709  GLU   B C   
2174 O O   . GLU   B 16  ? 1.6997 0.6378 0.8626 -0.1094 -0.0318 -0.0593 709  GLU   B O   
2175 C CB  . GLU   B 16  ? 1.7406 0.6320 0.8871 -0.0643 -0.0122 -0.0356 709  GLU   B CB  
2176 C CG  . GLU   B 16  ? 1.7812 0.7139 0.9631 -0.0527 -0.0115 -0.0219 709  GLU   B CG  
2177 C CD  . GLU   B 16  ? 1.8962 0.7667 1.0374 -0.0504 -0.0066 -0.0131 709  GLU   B CD  
2178 O OE1 . GLU   B 16  ? 1.9406 0.7442 1.0346 -0.0300 -0.0005 -0.0146 709  GLU   B OE1 
2179 O OE2 . GLU   B 16  ? 1.9212 0.8070 1.0753 -0.0681 -0.0077 -0.0044 709  GLU   B OE2 
2180 N N   . THR   B 17  ? 1.7474 0.5920 0.8373 -0.0595 -0.0116 -0.0652 710  THR   B N   
2181 C CA  . THR   B 17  ? 1.7824 0.5855 0.8296 -0.0785 -0.0169 -0.0791 710  THR   B CA  
2182 C C   . THR   B 17  ? 1.7474 0.6073 0.8241 -0.0788 -0.0227 -0.0843 710  THR   B C   
2183 O O   . THR   B 17  ? 1.7602 0.6093 0.8186 -0.1062 -0.0356 -0.0933 710  THR   B O   
2184 C CB  . THR   B 17  ? 1.8617 0.5803 0.8432 -0.0539 -0.0027 -0.0864 710  THR   B CB  
2185 O OG1 . THR   B 17  ? 1.8677 0.6116 0.8705 -0.0093 0.0126  -0.0819 710  THR   B OG1 
2186 C CG2 . THR   B 17  ? 1.9047 0.5483 0.8411 -0.0605 0.0004  -0.0838 710  THR   B CG2 
2187 N N   . GLU   B 18  ? 1.7030 0.6204 0.8231 -0.0487 -0.0142 -0.0783 711  GLU   B N   
2188 C CA  . GLU   B 18  ? 1.6696 0.6400 0.8179 -0.0450 -0.0166 -0.0813 711  GLU   B CA  
2189 C C   . GLU   B 18  ? 1.6270 0.6578 0.8193 -0.0760 -0.0351 -0.0790 711  GLU   B C   
2190 O O   . GLU   B 18  ? 1.6204 0.6740 0.8172 -0.0838 -0.0427 -0.0840 711  GLU   B O   
2191 C CB  . GLU   B 18  ? 1.6684 0.6879 0.8588 -0.0079 -0.0027 -0.0738 711  GLU   B CB  
2192 C CG  . GLU   B 18  ? 1.7625 0.7383 0.9199 0.0277  0.0177  -0.0777 711  GLU   B CG  
2193 C CD  . GLU   B 18  ? 1.8129 0.8480 1.0216 0.0602  0.0298  -0.0708 711  GLU   B CD  
2194 O OE1 . GLU   B 18  ? 1.7999 0.8900 1.0426 0.0553  0.0269  -0.0706 711  GLU   B OE1 
2195 O OE2 . GLU   B 18  ? 1.8363 0.8630 1.0523 0.0902  0.0412  -0.0654 711  GLU   B OE2 
2196 N N   . PHE   B 19  ? 1.5981 0.6562 0.8236 -0.0912 -0.0410 -0.0706 712  PHE   B N   
2197 C CA  . PHE   B 19  ? 1.5597 0.6793 0.8337 -0.1178 -0.0559 -0.0676 712  PHE   B CA  
2198 C C   . PHE   B 19  ? 1.5627 0.6658 0.8347 -0.1520 -0.0647 -0.0663 712  PHE   B C   
2199 O O   . PHE   B 19  ? 1.5904 0.6452 0.8336 -0.1519 -0.0571 -0.0637 712  PHE   B O   
2200 C CB  . PHE   B 19  ? 1.5136 0.7071 0.8487 -0.0999 -0.0516 -0.0575 712  PHE   B CB  
2201 C CG  . PHE   B 19  ? 1.5170 0.7109 0.8639 -0.0866 -0.0428 -0.0477 712  PHE   B CG  
2202 C CD1 . PHE   B 19  ? 1.5387 0.7120 0.8721 -0.0526 -0.0301 -0.0447 712  PHE   B CD1 
2203 C CD2 . PHE   B 19  ? 1.5115 0.7282 0.8842 -0.1072 -0.0470 -0.0410 712  PHE   B CD2 
2204 C CE1 . PHE   B 19  ? 1.5462 0.7173 0.8869 -0.0399 -0.0254 -0.0351 712  PHE   B CE1 
2205 C CE2 . PHE   B 19  ? 1.5215 0.7325 0.8969 -0.0950 -0.0394 -0.0317 712  PHE   B CE2 
2206 C CZ  . PHE   B 19  ? 1.5317 0.7193 0.8899 -0.0615 -0.0304 -0.0286 712  PHE   B CZ  
2207 N N   . LYS   B 20  ? 1.5321 0.6763 0.8367 -0.1811 -0.0801 -0.0674 713  LYS   B N   
2208 C CA  . LYS   B 20  ? 1.5302 0.6704 0.8446 -0.2164 -0.0877 -0.0658 713  LYS   B CA  
2209 C C   . LYS   B 20  ? 1.4814 0.7008 0.8654 -0.2260 -0.0908 -0.0575 713  LYS   B C   
2210 O O   . LYS   B 20  ? 1.4503 0.7245 0.8706 -0.2170 -0.0964 -0.0569 713  LYS   B O   
2211 C CB  . LYS   B 20  ? 1.5685 0.6759 0.8542 -0.2478 -0.1055 -0.0767 713  LYS   B CB  
2212 N N   . LYS   B 21  ? 1.4754 0.6973 0.8752 -0.2435 -0.0853 -0.0509 714  LYS   B N   
2213 C CA  . LYS   B 21  ? 1.4360 0.7270 0.8983 -0.2541 -0.0849 -0.0435 714  LYS   B CA  
2214 C C   . LYS   B 21  ? 1.4282 0.7374 0.9152 -0.2931 -0.1001 -0.0477 714  LYS   B C   
2215 O O   . LYS   B 21  ? 1.4593 0.7212 0.9174 -0.3185 -0.1027 -0.0512 714  LYS   B O   
2216 C CB  . LYS   B 21  ? 1.4571 0.7387 0.9198 -0.2504 -0.0680 -0.0335 714  LYS   B CB  
2217 C CG  . LYS   B 21  ? 1.4984 0.7869 0.9578 -0.2116 -0.0572 -0.0274 714  LYS   B CG  
2218 C CD  . LYS   B 21  ? 1.5592 0.8222 1.0034 -0.2080 -0.0434 -0.0179 714  LYS   B CD  
2219 C CE  . LYS   B 21  ? 1.6480 0.8307 1.0300 -0.2004 -0.0382 -0.0185 714  LYS   B CE  
2220 N N   . ILE   B 22  ? 1.3860 0.7613 0.9254 -0.2978 -0.1115 -0.0476 715  ILE   B N   
2221 C CA  . ILE   B 22  ? 1.3697 0.7700 0.9400 -0.3325 -0.1293 -0.0513 715  ILE   B CA  
2222 C C   . ILE   B 22  ? 1.3271 0.7785 0.9571 -0.3515 -0.1214 -0.0436 715  ILE   B C   
2223 O O   . ILE   B 22  ? 1.3370 0.7734 0.9710 -0.3832 -0.1220 -0.0441 715  ILE   B O   
2224 C CB  . ILE   B 22  ? 1.3633 0.7966 0.9486 -0.3279 -0.1504 -0.0567 715  ILE   B CB  
2225 C CG1 . ILE   B 22  ? 1.4170 0.7947 0.9378 -0.3090 -0.1539 -0.0644 715  ILE   B CG1 
2226 C CG2 . ILE   B 22  ? 1.3516 0.8083 0.9676 -0.3633 -0.1733 -0.0606 715  ILE   B CG2 
2227 N N   . LYS   B 23  ? 1.2827 0.7912 0.9573 -0.3333 -0.1124 -0.0369 716  LYS   B N   
2228 C CA  . LYS   B 23  ? 1.2445 0.8003 0.9734 -0.3479 -0.1011 -0.0299 716  LYS   B CA  
2229 C C   . LYS   B 23  ? 1.2305 0.8082 0.9703 -0.3208 -0.0813 -0.0220 716  LYS   B C   
2230 O O   . LYS   B 23  ? 1.2336 0.8107 0.9575 -0.2912 -0.0816 -0.0222 716  LYS   B O   
2231 C CB  . LYS   B 23  ? 1.2183 0.8385 1.0107 -0.3653 -0.1180 -0.0314 716  LYS   B CB  
2232 C CG  . LYS   B 23  ? 1.2215 0.8939 1.0460 -0.3398 -0.1247 -0.0303 716  LYS   B CG  
2233 N N   . VAL   B 24  ? 1.2129 0.8087 0.9786 -0.3320 -0.0638 -0.0153 717  VAL   B N   
2234 C CA  . VAL   B 24  ? 1.2028 0.8165 0.9754 -0.3092 -0.0459 -0.0083 717  VAL   B CA  
2235 C C   . VAL   B 24  ? 1.1633 0.8476 0.9941 -0.2994 -0.0496 -0.0078 717  VAL   B C   
2236 O O   . VAL   B 24  ? 1.1358 0.8629 1.0165 -0.3190 -0.0539 -0.0083 717  VAL   B O   
2237 C CB  . VAL   B 24  ? 1.2125 0.8084 0.9797 -0.3250 -0.0235 -0.0013 717  VAL   B CB  
2238 C CG1 . VAL   B 24  ? 1.2117 0.8245 0.9823 -0.3025 -0.0067 0.0054  717  VAL   B CG1 
2239 C CG2 . VAL   B 24  ? 1.2611 0.7809 0.9661 -0.3331 -0.0196 -0.0009 717  VAL   B CG2 
2240 N N   . LEU   B 25  ? 1.1575 0.8539 0.9836 -0.2693 -0.0485 -0.0066 718  LEU   B N   
2241 C CA  . LEU   B 25  ? 1.1269 0.8825 1.0008 -0.2569 -0.0504 -0.0058 718  LEU   B CA  
2242 C C   . LEU   B 25  ? 1.1237 0.8987 1.0150 -0.2522 -0.0291 0.0002  718  LEU   B C   
2243 O O   . LEU   B 25  ? 1.0929 0.9169 1.0333 -0.2555 -0.0250 0.0013  718  LEU   B O   
2244 C CB  . LEU   B 25  ? 1.1316 0.8875 0.9898 -0.2287 -0.0603 -0.0081 718  LEU   B CB  
2245 C CG  . LEU   B 25  ? 1.1575 0.8956 0.9960 -0.2298 -0.0795 -0.0143 718  LEU   B CG  
2246 C CD1 . LEU   B 25  ? 1.1644 0.9018 0.9871 -0.2016 -0.0831 -0.0154 718  LEU   B CD1 
2247 C CD2 . LEU   B 25  ? 1.1408 0.9159 1.0198 -0.2482 -0.0956 -0.0170 718  LEU   B CD2 
2248 N N   . GLY   B 26  ? 1.1567 0.8909 1.0052 -0.2431 -0.0162 0.0041  719  GLY   B N   
2249 C CA  . GLY   B 26  ? 1.1666 0.9066 1.0166 -0.2382 0.0038  0.0098  719  GLY   B CA  
2250 C C   . GLY   B 26  ? 1.2173 0.8990 1.0113 -0.2361 0.0150  0.0147  719  GLY   B C   
2251 O O   . GLY   B 26  ? 1.2422 0.8809 0.9959 -0.2298 0.0063  0.0136  719  GLY   B O   
2252 N N   . SER   B 27  ? 1.2314 0.9087 1.0200 -0.2405 0.0350  0.0203  720  SER   B N   
2253 C CA  . SER   B 27  ? 1.2824 0.9024 1.0145 -0.2381 0.0465  0.0266  720  SER   B CA  
2254 C C   . SER   B 27  ? 1.2956 0.9195 1.0151 -0.2200 0.0574  0.0309  720  SER   B C   
2255 O O   . SER   B 27  ? 1.2710 0.9412 1.0271 -0.2116 0.0581  0.0284  720  SER   B O   
2256 C CB  . SER   B 27  ? 1.3136 0.9091 1.0388 -0.2690 0.0625  0.0302  720  SER   B CB  
2257 O OG  . SER   B 27  ? 1.3599 0.9354 1.0810 -0.2858 0.0507  0.0264  720  SER   B OG  
2258 N N   . GLY   B 28  ? 1.3318 0.9036 0.9963 -0.2136 0.0644  0.0374  721  GLY   B N   
2259 C CA  . GLY   B 28  ? 1.3451 0.9118 0.9878 -0.1979 0.0723  0.0414  721  GLY   B CA  
2260 C C   . GLY   B 28  ? 1.3884 0.8909 0.9640 -0.1879 0.0726  0.0489  721  GLY   B C   
2261 O O   . GLY   B 28  ? 1.4167 0.8747 0.9615 -0.1961 0.0719  0.0519  721  GLY   B O   
2262 N N   . ALA   B 29  ? 1.3903 0.8845 0.9403 -0.1702 0.0728  0.0522  722  ALA   B N   
2263 C CA  . ALA   B 29  ? 1.4239 0.8580 0.9087 -0.1570 0.0689  0.0601  722  ALA   B CA  
2264 C C   . ALA   B 29  ? 1.4145 0.8383 0.8912 -0.1335 0.0438  0.0589  722  ALA   B C   
2265 O O   . ALA   B 29  ? 1.4468 0.8173 0.8768 -0.1262 0.0389  0.0649  722  ALA   B O   
2266 C CB  . ALA   B 29  ? 1.4358 0.8665 0.8967 -0.1457 0.0735  0.0631  722  ALA   B CB  
2267 N N   . PHE   B 30  ? 1.3648 0.8391 0.8874 -0.1213 0.0297  0.0513  723  PHE   B N   
2268 C CA  . PHE   B 30  ? 1.3492 0.8268 0.8772 -0.0995 0.0094  0.0487  723  PHE   B CA  
2269 C C   . PHE   B 30  ? 1.3322 0.7801 0.8494 -0.1062 0.0076  0.0476  723  PHE   B C   
2270 O O   . PHE   B 30  ? 1.3432 0.7694 0.8436 -0.0871 -0.0045 0.0482  723  PHE   B O   
2271 C CB  . PHE   B 30  ? 1.3180 0.8580 0.9011 -0.0924 0.0007  0.0407  723  PHE   B CB  
2272 C CG  . PHE   B 30  ? 1.3139 0.8849 0.9373 -0.1103 0.0044  0.0343  723  PHE   B CG  
2273 C CD1 . PHE   B 30  ? 1.3128 0.9094 0.9627 -0.1312 0.0184  0.0328  723  PHE   B CD1 
2274 C CD2 . PHE   B 30  ? 1.3247 0.8951 0.9564 -0.1064 -0.0058 0.0300  723  PHE   B CD2 
2275 C CE1 . PHE   B 30  ? 1.3030 0.9275 0.9905 -0.1477 0.0184  0.0277  723  PHE   B CE1 
2276 C CE2 . PHE   B 30  ? 1.3200 0.9120 0.9812 -0.1241 -0.0051 0.0245  723  PHE   B CE2 
2277 C CZ  . PHE   B 30  ? 1.3001 0.9211 0.9910 -0.1445 0.0052  0.0236  723  PHE   B CZ  
2278 N N   . GLY   B 31  ? 1.3011 0.7521 0.8324 -0.1328 0.0190  0.0451  724  GLY   B N   
2279 C CA  . GLY   B 31  ? 1.2960 0.7210 0.8191 -0.1436 0.0165  0.0422  724  GLY   B CA  
2280 C C   . GLY   B 31  ? 1.2453 0.7125 0.8158 -0.1659 0.0181  0.0348  724  GLY   B C   
2281 O O   . GLY   B 31  ? 1.2300 0.7291 0.8295 -0.1824 0.0292  0.0350  724  GLY   B O   
2282 N N   . THR   B 32  ? 1.2163 0.6835 0.7946 -0.1658 0.0068  0.0283  725  THR   B N   
2283 C CA  . THR   B 32  ? 1.1698 0.6718 0.7881 -0.1874 0.0039  0.0215  725  THR   B CA  
2284 C C   . THR   B 32  ? 1.1250 0.6544 0.7645 -0.1734 -0.0119 0.0141  725  THR   B C   
2285 O O   . THR   B 32  ? 1.1365 0.6411 0.7506 -0.1524 -0.0186 0.0131  725  THR   B O   
2286 C CB  . THR   B 32  ? 1.2080 0.6667 0.8030 -0.2141 0.0079  0.0210  725  THR   B CB  
2287 O OG1 . THR   B 32  ? 1.2418 0.6717 0.8141 -0.2274 0.0249  0.0288  725  THR   B OG1 
2288 C CG2 . THR   B 32  ? 1.1845 0.6776 0.8210 -0.2399 0.0022  0.0144  725  THR   B CG2 
2289 N N   . VAL   B 33  ? 1.0731 0.6522 0.7586 -0.1846 -0.0168 0.0094  726  VAL   B N   
2290 C CA  . VAL   B 33  ? 1.0515 0.6534 0.7538 -0.1751 -0.0311 0.0029  726  VAL   B CA  
2291 C C   . VAL   B 33  ? 1.0500 0.6443 0.7557 -0.1997 -0.0394 -0.0028 726  VAL   B C   
2292 O O   . VAL   B 33  ? 1.0332 0.6480 0.7665 -0.2239 -0.0369 -0.0024 726  VAL   B O   
2293 C CB  . VAL   B 33  ? 1.0127 0.6738 0.7601 -0.1647 -0.0337 0.0024  726  VAL   B CB  
2294 C CG1 . VAL   B 33  ? 1.0011 0.6830 0.7641 -0.1598 -0.0476 -0.0035 726  VAL   B CG1 
2295 C CG2 . VAL   B 33  ? 1.0178 0.6811 0.7567 -0.1403 -0.0294 0.0065  726  VAL   B CG2 
2296 N N   . TYR   B 34  ? 1.0677 0.6311 0.7446 -0.1938 -0.0490 -0.0081 727  TYR   B N   
2297 C CA  . TYR   B 34  ? 1.0802 0.6276 0.7504 -0.2165 -0.0598 -0.0145 727  TYR   B CA  
2298 C C   . TYR   B 34  ? 1.0697 0.6395 0.7510 -0.2087 -0.0745 -0.0206 727  TYR   B C   
2299 O O   . TYR   B 34  ? 1.0641 0.6361 0.7368 -0.1832 -0.0740 -0.0209 727  TYR   B O   
2300 C CB  . TYR   B 34  ? 1.1254 0.6012 0.7375 -0.2179 -0.0578 -0.0166 727  TYR   B CB  
2301 C CG  . TYR   B 34  ? 1.1615 0.6016 0.7510 -0.2262 -0.0438 -0.0100 727  TYR   B CG  
2302 C CD1 . TYR   B 34  ? 1.1803 0.6043 0.7697 -0.2591 -0.0411 -0.0098 727  TYR   B CD1 
2303 C CD2 . TYR   B 34  ? 1.1914 0.6090 0.7557 -0.2014 -0.0342 -0.0037 727  TYR   B CD2 
2304 C CE1 . TYR   B 34  ? 1.2158 0.5997 0.7778 -0.2677 -0.0265 -0.0031 727  TYR   B CE1 
2305 C CE2 . TYR   B 34  ? 1.2270 0.6045 0.7625 -0.2082 -0.0223 0.0032  727  TYR   B CE2 
2306 C CZ  . TYR   B 34  ? 1.2504 0.6088 0.7824 -0.2416 -0.0172 0.0037  727  TYR   B CZ  
2307 O OH  . TYR   B 34  ? 1.3014 0.6147 0.7999 -0.2494 -0.0035 0.0113  727  TYR   B OH  
2308 N N   . LYS   B 35  ? 1.0709 0.6540 0.7686 -0.2313 -0.0881 -0.0252 728  LYS   B N   
2309 C CA  . LYS   B 35  ? 1.0825 0.6759 0.7799 -0.2273 -0.1045 -0.0311 728  LYS   B CA  
2310 C C   . LYS   B 35  ? 1.1427 0.6709 0.7828 -0.2339 -0.1095 -0.0379 728  LYS   B C   
2311 O O   . LYS   B 35  ? 1.1607 0.6612 0.7885 -0.2591 -0.1120 -0.0398 728  LYS   B O   
2312 C CB  . LYS   B 35  ? 1.0691 0.7089 0.8134 -0.2495 -0.1196 -0.0321 728  LYS   B CB  
2313 C CG  . LYS   B 35  ? 1.1131 0.7554 0.8493 -0.2491 -0.1402 -0.0379 728  LYS   B CG  
2314 N N   . GLY   B 36  ? 1.1722 0.6734 0.7767 -0.2117 -0.1088 -0.0415 729  GLY   B N   
2315 C CA  . GLY   B 36  ? 1.2248 0.6585 0.7695 -0.2141 -0.1106 -0.0487 729  GLY   B CA  
2316 C C   . GLY   B 36  ? 1.2503 0.6678 0.7660 -0.2038 -0.1192 -0.0558 729  GLY   B C   
2317 O O   . GLY   B 36  ? 1.2297 0.6892 0.7721 -0.1993 -0.1277 -0.0552 729  GLY   B O   
2318 N N   . LEU   B 37  ? 1.2988 0.6506 0.7554 -0.2001 -0.1162 -0.0625 730  LEU   B N   
2319 C CA  . LEU   B 37  ? 1.3368 0.6607 0.7536 -0.1900 -0.1207 -0.0701 730  LEU   B CA  
2320 C C   . LEU   B 37  ? 1.3853 0.6582 0.7569 -0.1626 -0.1013 -0.0720 730  LEU   B C   
2321 O O   . LEU   B 37  ? 1.4099 0.6387 0.7552 -0.1640 -0.0934 -0.0721 730  LEU   B O   
2322 C CB  . LEU   B 37  ? 1.3628 0.6495 0.7456 -0.2199 -0.1411 -0.0793 730  LEU   B CB  
2323 C CG  . LEU   B 37  ? 1.3877 0.6744 0.7508 -0.2190 -0.1557 -0.0851 730  LEU   B CG  
2324 C CD1 . LEU   B 37  ? 1.3437 0.7057 0.7673 -0.2183 -0.1658 -0.0783 730  LEU   B CD1 
2325 C CD2 . LEU   B 37  ? 1.4296 0.6703 0.7507 -0.2485 -0.1776 -0.0950 730  LEU   B CD2 
2326 N N   . TRP   B 38  ? 1.3987 0.6775 0.7626 -0.1371 -0.0927 -0.0728 731  TRP   B N   
2327 C CA  . TRP   B 38  ? 1.4458 0.6837 0.7748 -0.1081 -0.0726 -0.0744 731  TRP   B CA  
2328 C C   . TRP   B 38  ? 1.5178 0.7074 0.7903 -0.1024 -0.0707 -0.0844 731  TRP   B C   
2329 O O   . TRP   B 38  ? 1.5111 0.7221 0.7866 -0.1059 -0.0789 -0.0863 731  TRP   B O   
2330 C CB  . TRP   B 38  ? 1.4051 0.6944 0.7794 -0.0798 -0.0589 -0.0658 731  TRP   B CB  
2331 C CG  . TRP   B 38  ? 1.4174 0.6793 0.7692 -0.0470 -0.0384 -0.0666 731  TRP   B CG  
2332 C CD1 . TRP   B 38  ? 1.4598 0.6613 0.7687 -0.0350 -0.0274 -0.0698 731  TRP   B CD1 
2333 C CD2 . TRP   B 38  ? 1.3920 0.6904 0.7703 -0.0210 -0.0256 -0.0631 731  TRP   B CD2 
2334 N NE1 . TRP   B 38  ? 1.4626 0.6622 0.7709 -0.0017 -0.0084 -0.0689 731  TRP   B NE1 
2335 C CE2 . TRP   B 38  ? 1.4212 0.6816 0.7736 0.0063  -0.0067 -0.0648 731  TRP   B CE2 
2336 C CE3 . TRP   B 38  ? 1.3614 0.7200 0.7837 -0.0185 -0.0277 -0.0587 731  TRP   B CE3 
2337 C CZ2 . TRP   B 38  ? 1.4106 0.6963 0.7848 0.0347  0.0103  -0.0621 731  TRP   B CZ2 
2338 C CZ3 . TRP   B 38  ? 1.3569 0.7359 0.7958 0.0079  -0.0110 -0.0562 731  TRP   B CZ3 
2339 C CH2 . TRP   B 38  ? 1.3764 0.7221 0.7944 0.0337  0.0078  -0.0578 731  TRP   B CH2 
2340 N N   . ILE   B 39  ? 1.5870 0.7075 0.8045 -0.0930 -0.0592 -0.0906 732  ILE   B N   
2341 C CA  . ILE   B 39  ? 1.6607 0.7228 0.8149 -0.0830 -0.0513 -0.1008 732  ILE   B CA  
2342 C C   . ILE   B 39  ? 1.6950 0.7466 0.8466 -0.0437 -0.0234 -0.0982 732  ILE   B C   
2343 O O   . ILE   B 39  ? 1.7116 0.7282 0.8490 -0.0323 -0.0134 -0.0972 732  ILE   B O   
2344 C CB  . ILE   B 39  ? 1.7203 0.7039 0.8097 -0.1057 -0.0609 -0.1113 732  ILE   B CB  
2345 C CG1 . ILE   B 39  ? 1.7276 0.7253 0.8232 -0.1455 -0.0908 -0.1145 732  ILE   B CG1 
2346 C CG2 . ILE   B 39  ? 1.7760 0.6865 0.7911 -0.0892 -0.0466 -0.1224 732  ILE   B CG2 
2347 C CD1 . ILE   B 39  ? 1.7856 0.7127 0.8272 -0.1735 -0.1034 -0.1240 732  ILE   B CD1 
2348 N N   . PRO   B 40  ? 1.6972 0.7838 0.8686 -0.0224 -0.0109 -0.0959 733  PRO   B N   
2349 C CA  . PRO   B 40  ? 1.7155 0.8006 0.8945 0.0148  0.0157  -0.0930 733  PRO   B CA  
2350 C C   . PRO   B 40  ? 1.7979 0.7998 0.9064 0.0288  0.0320  -0.1030 733  PRO   B C   
2351 O O   . PRO   B 40  ? 1.8356 0.7891 0.8865 0.0156  0.0280  -0.1132 733  PRO   B O   
2352 C CB  . PRO   B 40  ? 1.6919 0.8275 0.9013 0.0267  0.0241  -0.0899 733  PRO   B CB  
2353 C CG  . PRO   B 40  ? 1.6711 0.8471 0.9033 -0.0025 -0.0005 -0.0879 733  PRO   B CG  
2354 C CD  . PRO   B 40  ? 1.6764 0.8027 0.8632 -0.0312 -0.0199 -0.0955 733  PRO   B CD  
2355 N N   . GLU   B 41  ? 1.8212 0.8046 0.9328 0.0557  0.0489  -0.0999 734  GLU   B N   
2356 C CA  . GLU   B 41  ? 1.8882 0.7938 0.9410 0.0766  0.0681  -0.1075 734  GLU   B CA  
2357 C C   . GLU   B 41  ? 1.9482 0.7863 0.9241 0.0701  0.0742  -0.1217 734  GLU   B C   
2358 O O   . GLU   B 41  ? 1.9984 0.7629 0.9120 0.0557  0.0680  -0.1307 734  GLU   B O   
2359 C CB  . GLU   B 41  ? 1.9065 0.8349 0.9943 0.1194  0.0936  -0.1011 734  GLU   B CB  
2360 C CG  . GLU   B 41  ? 2.0183 0.8700 1.0527 0.1459  0.1151  -0.1077 734  GLU   B CG  
2361 C CD  . GLU   B 41  ? 2.0932 0.9554 1.1407 0.1849  0.1463  -0.1081 734  GLU   B CD  
2362 O OE1 . GLU   B 41  ? 2.1384 0.9552 1.1642 0.2146  0.1654  -0.1099 734  GLU   B OE1 
2363 O OE2 . GLU   B 41  ? 2.0872 1.0026 1.1677 0.1859  0.1525  -0.1061 734  GLU   B OE2 
2364 N N   . GLY   B 42  ? 1.9418 0.8006 0.9184 0.0798  0.0864  -0.1236 735  GLY   B N   
2365 C CA  . GLY   B 42  ? 1.9953 0.7894 0.8947 0.0744  0.0929  -0.1365 735  GLY   B CA  
2366 C C   . GLY   B 42  ? 1.9862 0.8164 0.8910 0.0617  0.0859  -0.1363 735  GLY   B C   
2367 O O   . GLY   B 42  ? 2.0262 0.8090 0.8696 0.0638  0.0966  -0.1454 735  GLY   B O   
2368 N N   . GLU   B 43  ? 1.9341 0.8439 0.9077 0.0487  0.0684  -0.1258 736  GLU   B N   
2369 C CA  . GLU   B 43  ? 1.9221 0.8693 0.9057 0.0374  0.0602  -0.1237 736  GLU   B CA  
2370 C C   . GLU   B 43  ? 1.9501 0.8656 0.8861 0.0021  0.0295  -0.1310 736  GLU   B C   
2371 O O   . GLU   B 43  ? 1.9589 0.8830 0.8798 -0.0050 0.0237  -0.1314 736  GLU   B O   
2372 C CB  . GLU   B 43  ? 1.8834 0.9244 0.9573 0.0382  0.0533  -0.1102 736  GLU   B CB  
2373 N N   . LYS   B 44  ? 1.9583 0.8380 0.8723 -0.0205 0.0089  -0.1361 737  LYS   B N   
2374 C CA  . LYS   B 44  ? 1.9727 0.8267 0.8503 -0.0570 -0.0243 -0.1428 737  LYS   B CA  
2375 C C   . LYS   B 44  ? 1.9157 0.8462 0.8519 -0.0750 -0.0488 -0.1340 737  LYS   B C   
2376 O O   . LYS   B 44  ? 1.9285 0.8569 0.8395 -0.0826 -0.0595 -0.1359 737  LYS   B O   
2377 C CB  . LYS   B 44  ? 2.0546 0.8270 0.8367 -0.0594 -0.0215 -0.1563 737  LYS   B CB  
2378 N N   . VAL   B 45  ? 1.8476 0.8431 0.8599 -0.0794 -0.0560 -0.1238 738  VAL   B N   
2379 C CA  . VAL   B 45  ? 1.7835 0.8535 0.8575 -0.0932 -0.0761 -0.1149 738  VAL   B CA  
2380 C C   . VAL   B 45  ? 1.7253 0.8326 0.8519 -0.1143 -0.0941 -0.1098 738  VAL   B C   
2381 O O   . VAL   B 45  ? 1.7321 0.8206 0.8607 -0.1118 -0.0853 -0.1096 738  VAL   B O   
2382 C CB  . VAL   B 45  ? 1.7570 0.8852 0.8802 -0.0673 -0.0563 -0.1052 738  VAL   B CB  
2383 N N   . LYS   B 46  ? 1.6647 0.8230 0.8326 -0.1345 -0.1184 -0.1051 739  LYS   B N   
2384 C CA  . LYS   B 46  ? 1.6077 0.8074 0.8303 -0.1550 -0.1333 -0.0998 739  LYS   B CA  
2385 C C   . LYS   B 46  ? 1.5246 0.8041 0.8205 -0.1445 -0.1303 -0.0884 739  LYS   B C   
2386 O O   . LYS   B 46  ? 1.5064 0.8221 0.8236 -0.1516 -0.1460 -0.0855 739  LYS   B O   
2387 C CB  . LYS   B 46  ? 1.6363 0.8258 0.8471 -0.1902 -0.1658 -0.1052 739  LYS   B CB  
2388 C CG  . LYS   B 46  ? 1.7347 0.8413 0.8718 -0.2048 -0.1710 -0.1174 739  LYS   B CG  
2389 N N   . ILE   B 47  ? 1.4722 0.7757 0.8028 -0.1261 -0.1104 -0.0819 740  ILE   B N   
2390 C CA  . ILE   B 47  ? 1.3979 0.7717 0.7937 -0.1155 -0.1063 -0.0719 740  ILE   B CA  
2391 C C   . ILE   B 47  ? 1.3348 0.7479 0.7812 -0.1324 -0.1156 -0.0663 740  ILE   B C   
2392 O O   . ILE   B 47  ? 1.3385 0.7350 0.7840 -0.1329 -0.1074 -0.0653 740  ILE   B O   
2393 C CB  . ILE   B 47  ? 1.3959 0.7762 0.8002 -0.0835 -0.0800 -0.0679 740  ILE   B CB  
2394 C CG1 . ILE   B 47  ? 1.4363 0.7766 0.7907 -0.0667 -0.0663 -0.0736 740  ILE   B CG1 
2395 C CG2 . ILE   B 47  ? 1.3545 0.8039 0.8225 -0.0746 -0.0774 -0.0585 740  ILE   B CG2 
2396 N N   . PRO   B 48  ? 1.2767 0.7404 0.7662 -0.1457 -0.1317 -0.0623 741  PRO   B N   
2397 C CA  . PRO   B 48  ? 1.2228 0.7273 0.7639 -0.1602 -0.1366 -0.0569 741  PRO   B CA  
2398 C C   . PRO   B 48  ? 1.1669 0.7008 0.7408 -0.1395 -0.1174 -0.0496 741  PRO   B C   
2399 O O   . PRO   B 48  ? 1.1489 0.7157 0.7453 -0.1222 -0.1115 -0.0455 741  PRO   B O   
2400 C CB  . PRO   B 48  ? 1.2099 0.7624 0.7890 -0.1721 -0.1562 -0.0543 741  PRO   B CB  
2401 C CG  . PRO   B 48  ? 1.2472 0.7718 0.7829 -0.1695 -0.1666 -0.0594 741  PRO   B CG  
2402 C CD  . PRO   B 48  ? 1.2601 0.7458 0.7538 -0.1456 -0.1443 -0.0618 741  PRO   B CD  
2403 N N   . VAL   B 49  ? 1.1379 0.6551 0.7096 -0.1413 -0.1082 -0.0479 742  VAL   B N   
2404 C CA  . VAL   B 49  ? 1.0940 0.6325 0.6899 -0.1220 -0.0927 -0.0411 742  VAL   B CA  
2405 C C   . VAL   B 49  ? 1.0466 0.6132 0.6786 -0.1357 -0.0926 -0.0355 742  VAL   B C   
2406 O O   . VAL   B 49  ? 1.0498 0.6148 0.6873 -0.1606 -0.1016 -0.0369 742  VAL   B O   
2407 C CB  . VAL   B 49  ? 1.1240 0.6128 0.6790 -0.1030 -0.0784 -0.0426 742  VAL   B CB  
2408 C CG1 . VAL   B 49  ? 1.1417 0.6142 0.6715 -0.0830 -0.0717 -0.0467 742  VAL   B CG1 
2409 C CG2 . VAL   B 49  ? 1.1556 0.5888 0.6704 -0.1199 -0.0807 -0.0469 742  VAL   B CG2 
2410 N N   . ALA   B 50  ? 1.0036 0.5966 0.6606 -0.1199 -0.0822 -0.0292 743  ALA   B N   
2411 C CA  . ALA   B 50  ? 0.9778 0.5885 0.6586 -0.1276 -0.0773 -0.0235 743  ALA   B CA  
2412 C C   . ALA   B 50  ? 0.9872 0.5616 0.6394 -0.1111 -0.0658 -0.0205 743  ALA   B C   
2413 O O   . ALA   B 50  ? 0.9854 0.5567 0.6306 -0.0869 -0.0609 -0.0199 743  ALA   B O   
2414 C CB  . ALA   B 50  ? 0.9411 0.6079 0.6682 -0.1205 -0.0763 -0.0190 743  ALA   B CB  
2415 N N   . ILE   B 51  ? 0.9948 0.5395 0.6296 -0.1243 -0.0620 -0.0183 744  ILE   B N   
2416 C CA  . ILE   B 51  ? 1.0166 0.5213 0.6201 -0.1094 -0.0531 -0.0144 744  ILE   B CA  
2417 C C   . ILE   B 51  ? 0.9973 0.5182 0.6167 -0.1117 -0.0470 -0.0067 744  ILE   B C   
2418 O O   . ILE   B 51  ? 0.9948 0.5195 0.6229 -0.1354 -0.0452 -0.0053 744  ILE   B O   
2419 C CB  . ILE   B 51  ? 1.0629 0.5036 0.6188 -0.1217 -0.0525 -0.0180 744  ILE   B CB  
2420 C CG1 . ILE   B 51  ? 1.0908 0.5079 0.6222 -0.1191 -0.0579 -0.0267 744  ILE   B CG1 
2421 C CG2 . ILE   B 51  ? 1.0962 0.4920 0.6183 -0.1056 -0.0437 -0.0126 744  ILE   B CG2 
2422 C CD1 . ILE   B 51  ? 1.1242 0.5160 0.6380 -0.1491 -0.0669 -0.0331 744  ILE   B CD1 
2423 N N   . LYS   B 52  ? 0.9828 0.5118 0.6049 -0.0879 -0.0436 -0.0017 745  LYS   B N   
2424 C CA  . LYS   B 52  ? 0.9785 0.5134 0.6045 -0.0886 -0.0385 0.0055  745  LYS   B CA  
2425 C C   . LYS   B 52  ? 1.0164 0.4944 0.5970 -0.0798 -0.0344 0.0104  745  LYS   B C   
2426 O O   . LYS   B 52  ? 1.0196 0.4830 0.5870 -0.0545 -0.0364 0.0118  745  LYS   B O   
2427 C CB  . LYS   B 52  ? 0.9643 0.5436 0.6206 -0.0700 -0.0406 0.0079  745  LYS   B CB  
2428 C CG  . LYS   B 52  ? 0.9922 0.5811 0.6525 -0.0736 -0.0359 0.0139  745  LYS   B CG  
2429 C CD  . LYS   B 52  ? 1.0050 0.6389 0.6968 -0.0591 -0.0399 0.0143  745  LYS   B CD  
2430 C CE  . LYS   B 52  ? 1.0363 0.6901 0.7405 -0.0695 -0.0342 0.0169  745  LYS   B CE  
2431 N NZ  . LYS   B 52  ? 1.0332 0.7356 0.7754 -0.0639 -0.0376 0.0143  745  LYS   B NZ  
2432 N N   . GLU   B 53  ? 1.0486 0.4933 0.6061 -0.1005 -0.0283 0.0132  746  GLU   B N   
2433 C CA  . GLU   B 53  ? 1.1041 0.4888 0.6137 -0.0938 -0.0239 0.0191  746  GLU   B CA  
2434 C C   . GLU   B 53  ? 1.1229 0.5117 0.6286 -0.0893 -0.0196 0.0279  746  GLU   B C   
2435 O O   . GLU   B 53  ? 1.1164 0.5158 0.6306 -0.1110 -0.0116 0.0301  746  GLU   B O   
2436 C CB  . GLU   B 53  ? 1.1618 0.4995 0.6418 -0.1206 -0.0188 0.0175  746  GLU   B CB  
2437 C CG  . GLU   B 53  ? 1.2901 0.5579 0.7150 -0.1119 -0.0143 0.0239  746  GLU   B CG  
2438 C CD  . GLU   B 53  ? 1.4339 0.6440 0.8221 -0.1337 -0.0110 0.0206  746  GLU   B CD  
2439 O OE1 . GLU   B 53  ? 1.4576 0.6817 0.8635 -0.1656 -0.0095 0.0164  746  GLU   B OE1 
2440 O OE2 . GLU   B 53  ? 1.5079 0.6582 0.8505 -0.1186 -0.0105 0.0220  746  GLU   B OE2 
2441 N N   . LEU   B 54  ? 1.1427 0.5246 0.6370 -0.0610 -0.0251 0.0328  747  LEU   B N   
2442 C CA  . LEU   B 54  ? 1.1626 0.5437 0.6461 -0.0548 -0.0242 0.0410  747  LEU   B CA  
2443 C C   . LEU   B 54  ? 1.2227 0.5391 0.6530 -0.0629 -0.0168 0.0488  747  LEU   B C   
2444 O O   . LEU   B 54  ? 1.2551 0.5223 0.6528 -0.0592 -0.0168 0.0492  747  LEU   B O   
2445 C CB  . LEU   B 54  ? 1.1528 0.5527 0.6463 -0.0227 -0.0365 0.0434  747  LEU   B CB  
2446 C CG  . LEU   B 54  ? 1.1353 0.5954 0.6799 -0.0143 -0.0425 0.0361  747  LEU   B CG  
2447 C CD1 . LEU   B 54  ? 1.1325 0.6097 0.6894 0.0155  -0.0542 0.0387  747  LEU   B CD1 
2448 C CD2 . LEU   B 54  ? 1.1144 0.6214 0.6931 -0.0328 -0.0386 0.0330  747  LEU   B CD2 
2449 N N   . ARG   B 55  ? 1.2424 0.5548 0.6611 -0.0767 -0.0081 0.0546  748  ARG   B N   
2450 C CA  . ARG   B 55  ? 1.3006 0.5489 0.6652 -0.0873 0.0018  0.0632  748  ARG   B CA  
2451 C C   . ARG   B 55  ? 1.3300 0.5288 0.6502 -0.0577 -0.0091 0.0707  748  ARG   B C   
2452 O O   . ARG   B 55  ? 1.3121 0.5353 0.6448 -0.0319 -0.0224 0.0721  748  ARG   B O   
2453 C CB  . ARG   B 55  ? 1.3346 0.5932 0.6956 -0.1017 0.0138  0.0683  748  ARG   B CB  
2454 C CG  . ARG   B 55  ? 1.4297 0.6403 0.7544 -0.1292 0.0326  0.0742  748  ARG   B CG  
2455 C CD  . ARG   B 55  ? 1.4822 0.7223 0.8246 -0.1501 0.0501  0.0752  748  ARG   B CD  
2456 N NE  . ARG   B 55  ? 1.4957 0.7975 0.9013 -0.1686 0.0545  0.0658  748  ARG   B NE  
2457 C CZ  . ARG   B 55  ? 1.5325 0.8342 0.9549 -0.1970 0.0641  0.0627  748  ARG   B CZ  
2458 N NH1 . ARG   B 55  ? 1.5688 0.8100 0.9485 -0.2125 0.0725  0.0678  748  ARG   B NH1 
2459 N NH2 . ARG   B 55  ? 1.4886 0.8494 0.9703 -0.2107 0.0641  0.0548  748  ARG   B NH2 
2460 N N   . GLU   B 56  ? 1.3750 0.5060 0.6466 -0.0606 -0.0047 0.0754  749  GLU   B N   
2461 C CA  . GLU   B 56  ? 1.4142 0.4959 0.6441 -0.0300 -0.0156 0.0833  749  GLU   B CA  
2462 C C   . GLU   B 56  ? 1.4343 0.5125 0.6434 -0.0131 -0.0239 0.0933  749  GLU   B C   
2463 O O   . GLU   B 56  ? 1.4345 0.5139 0.6322 -0.0315 -0.0141 0.0971  749  GLU   B O   
2464 C CB  . GLU   B 56  ? 1.4768 0.4794 0.6519 -0.0387 -0.0075 0.0876  749  GLU   B CB  
2465 C CG  . GLU   B 56  ? 1.5443 0.4951 0.6793 -0.0038 -0.0193 0.0952  749  GLU   B CG  
2466 C CD  . GLU   B 56  ? 1.6554 0.5208 0.7321 -0.0092 -0.0117 0.0993  749  GLU   B CD  
2467 O OE1 . GLU   B 56  ? 1.6932 0.5354 0.7558 -0.0445 0.0035  0.0975  749  GLU   B OE1 
2468 O OE2 . GLU   B 56  ? 1.6954 0.5163 0.7412 0.0214  -0.0208 0.1047  749  GLU   B OE2 
2469 N N   . ALA   B 57  ? 1.4467 0.5233 0.6536 0.0221  -0.0423 0.0970  750  ALA   B N   
2470 C CA  . ALA   B 57  ? 1.4712 0.5441 0.6588 0.0424  -0.0569 0.1062  750  ALA   B CA  
2471 C C   . ALA   B 57  ? 1.4589 0.5932 0.6822 0.0341  -0.0589 0.1023  750  ALA   B C   
2472 O O   . ALA   B 57  ? 1.4802 0.6001 0.6731 0.0352  -0.0630 0.1094  750  ALA   B O   
2473 C CB  . ALA   B 57  ? 1.5203 0.5154 0.6343 0.0390  -0.0526 0.1191  750  ALA   B CB  
2474 N N   . THR   B 58  ? 1.4255 0.6239 0.7090 0.0263  -0.0561 0.0910  751  THR   B N   
2475 C CA  . THR   B 58  ? 1.4106 0.6676 0.7313 0.0198  -0.0578 0.0862  751  THR   B CA  
2476 C C   . THR   B 58  ? 1.4062 0.6915 0.7463 0.0494  -0.0813 0.0875  751  THR   B C   
2477 O O   . THR   B 58  ? 1.4207 0.7142 0.7511 0.0522  -0.0899 0.0905  751  THR   B O   
2478 C CB  . THR   B 58  ? 1.3957 0.7071 0.7720 0.0019  -0.0476 0.0747  751  THR   B CB  
2479 O OG1 . THR   B 58  ? 1.4224 0.7109 0.7862 -0.0260 -0.0288 0.0734  751  THR   B OG1 
2480 C CG2 . THR   B 58  ? 1.3749 0.7414 0.7871 -0.0043 -0.0480 0.0699  751  THR   B CG2 
2481 N N   . SER   B 59  ? 1.3887 0.6868 0.7547 0.0711  -0.0915 0.0852  752  SER   B N   
2482 C CA  . SER   B 59  ? 1.3703 0.6993 0.7636 0.0996  -0.1134 0.0866  752  SER   B CA  
2483 C C   . SER   B 59  ? 1.4003 0.6780 0.7505 0.1246  -0.1286 0.0979  752  SER   B C   
2484 O O   . SER   B 59  ? 1.4307 0.6580 0.7488 0.1295  -0.1220 0.1017  752  SER   B O   
2485 C CB  . SER   B 59  ? 1.3551 0.7263 0.8020 0.1105  -0.1129 0.0785  752  SER   B CB  
2486 O OG  . SER   B 59  ? 1.3703 0.7669 0.8452 0.1397  -0.1320 0.0809  752  SER   B OG  
2487 N N   . PRO   B 60  ? 1.3900 0.6796 0.7406 0.1425  -0.1512 0.1033  753  PRO   B N   
2488 C CA  . PRO   B 60  ? 1.4163 0.6594 0.7290 0.1697  -0.1696 0.1150  753  PRO   B CA  
2489 C C   . PRO   B 60  ? 1.4008 0.6597 0.7505 0.2011  -0.1800 0.1152  753  PRO   B C   
2490 O O   . PRO   B 60  ? 1.4283 0.6485 0.7509 0.2265  -0.1944 0.1250  753  PRO   B O   
2491 C CB  . PRO   B 60  ? 1.4251 0.6788 0.7260 0.1743  -0.1919 0.1197  753  PRO   B CB  
2492 C CG  . PRO   B 60  ? 1.3866 0.7112 0.7452 0.1614  -0.1906 0.1086  753  PRO   B CG  
2493 C CD  . PRO   B 60  ? 1.3527 0.6954 0.7359 0.1386  -0.1626 0.0990  753  PRO   B CD  
2494 N N   . LYS   B 61  ? 1.3569 0.6708 0.7673 0.2006  -0.1719 0.1049  754  LYS   B N   
2495 C CA  . LYS   B 61  ? 1.3339 0.6699 0.7860 0.2292  -0.1768 0.1037  754  LYS   B CA  
2496 C C   . LYS   B 61  ? 1.3642 0.6480 0.7880 0.2376  -0.1614 0.1043  754  LYS   B C   
2497 O O   . LYS   B 61  ? 1.3831 0.6378 0.7797 0.2133  -0.1414 0.0997  754  LYS   B O   
2498 C CB  . LYS   B 61  ? 1.2937 0.7014 0.8140 0.2221  -0.1689 0.0922  754  LYS   B CB  
2499 C CG  . LYS   B 61  ? 1.2973 0.7620 0.8557 0.2174  -0.1846 0.0903  754  LYS   B CG  
2500 C CD  . LYS   B 61  ? 1.2963 0.8225 0.9153 0.2091  -0.1737 0.0798  754  LYS   B CD  
2501 C CE  . LYS   B 61  ? 1.3019 0.8787 0.9536 0.1995  -0.1870 0.0770  754  LYS   B CE  
2502 N NZ  . LYS   B 61  ? 1.3109 0.9083 0.9852 0.2231  -0.2143 0.0832  754  LYS   B NZ  
2503 N N   . ALA   B 62  ? 1.3610 0.6375 0.7976 0.2718  -0.1700 0.1086  755  ALA   B N   
2504 C CA  . ALA   B 62  ? 1.3887 0.6162 0.8016 0.2832  -0.1541 0.1075  755  ALA   B CA  
2505 C C   . ALA   B 62  ? 1.3601 0.6261 0.8154 0.2737  -0.1336 0.0939  755  ALA   B C   
2506 O O   . ALA   B 62  ? 1.3240 0.6575 0.8336 0.2675  -0.1351 0.0878  755  ALA   B O   
2507 C CB  . ALA   B 62  ? 1.3957 0.6072 0.8138 0.3260  -0.1688 0.1162  755  ALA   B CB  
2508 N N   . ASN   B 63  ? 1.3770 0.5962 0.8034 0.2720  -0.1149 0.0893  756  ASN   B N   
2509 C CA  . ASN   B 63  ? 1.3548 0.5982 0.8081 0.2624  -0.0958 0.0766  756  ASN   B CA  
2510 C C   . ASN   B 63  ? 1.3120 0.6198 0.8323 0.2861  -0.0965 0.0727  756  ASN   B C   
2511 O O   . ASN   B 63  ? 1.2823 0.6343 0.8367 0.2712  -0.0860 0.0634  756  ASN   B O   
2512 C CB  . ASN   B 63  ? 1.3986 0.5720 0.8032 0.2621  -0.0791 0.0729  756  ASN   B CB  
2513 C CG  . ASN   B 63  ? 1.4505 0.5798 0.8065 0.2243  -0.0700 0.0704  756  ASN   B CG  
2514 O OD1 . ASN   B 63  ? 1.5078 0.5761 0.8203 0.2194  -0.0583 0.0672  756  ASN   B OD1 
2515 N ND2 . ASN   B 63  ? 1.4259 0.5832 0.7883 0.1966  -0.0745 0.0714  756  ASN   B ND2 
2516 N N   . LYS   B 64  ? 1.3030 0.6179 0.8439 0.3221  -0.1091 0.0804  757  LYS   B N   
2517 C CA  . LYS   B 64  ? 1.2617 0.6410 0.8720 0.3450  -0.1093 0.0779  757  LYS   B CA  
2518 C C   . LYS   B 64  ? 1.2114 0.6640 0.8718 0.3279  -0.1206 0.0761  757  LYS   B C   
2519 O O   . LYS   B 64  ? 1.1848 0.6873 0.8912 0.3229  -0.1092 0.0684  757  LYS   B O   
2520 C CB  . LYS   B 64  ? 1.2928 0.6652 0.9177 0.3876  -0.1229 0.0877  757  LYS   B CB  
2521 C CG  . LYS   B 64  ? 1.2995 0.7419 1.0033 0.4121  -0.1211 0.0856  757  LYS   B CG  
2522 N N   . GLU   B 65  ? 1.2033 0.6570 0.8491 0.3173  -0.1414 0.0829  758  GLU   B N   
2523 C CA  . GLU   B 65  ? 1.1634 0.6787 0.8490 0.3001  -0.1530 0.0808  758  GLU   B CA  
2524 C C   . GLU   B 65  ? 1.1572 0.6843 0.8375 0.2637  -0.1367 0.0713  758  GLU   B C   
2525 O O   . GLU   B 65  ? 1.1234 0.7059 0.8459 0.2513  -0.1388 0.0667  758  GLU   B O   
2526 C CB  . GLU   B 65  ? 1.1935 0.6995 0.8576 0.3009  -0.1800 0.0904  758  GLU   B CB  
2527 N N   . ILE   B 66  ? 1.1866 0.6611 0.8158 0.2464  -0.1219 0.0687  759  ILE   B N   
2528 C CA  . ILE   B 66  ? 1.1849 0.6682 0.8100 0.2136  -0.1071 0.0600  759  ILE   B CA  
2529 C C   . ILE   B 66  ? 1.1599 0.6765 0.8238 0.2174  -0.0919 0.0511  759  ILE   B C   
2530 O O   . ILE   B 66  ? 1.1390 0.6984 0.8323 0.1996  -0.0876 0.0451  759  ILE   B O   
2531 C CB  . ILE   B 66  ? 1.2294 0.6465 0.7929 0.1955  -0.0965 0.0600  759  ILE   B CB  
2532 C CG1 . ILE   B 66  ? 1.2551 0.6424 0.7794 0.1850  -0.1071 0.0683  759  ILE   B CG1 
2533 C CG2 . ILE   B 66  ? 1.2294 0.6541 0.7939 0.1662  -0.0804 0.0500  759  ILE   B CG2 
2534 N N   . LEU   B 67  ? 1.1648 0.6591 0.8263 0.2421  -0.0830 0.0507  760  LEU   B N   
2535 C CA  . LEU   B 67  ? 1.1533 0.6698 0.8435 0.2494  -0.0657 0.0428  760  LEU   B CA  
2536 C C   . LEU   B 67  ? 1.1117 0.7016 0.8689 0.2565  -0.0703 0.0425  760  LEU   B C   
2537 O O   . LEU   B 67  ? 1.0980 0.7189 0.8784 0.2441  -0.0582 0.0355  760  LEU   B O   
2538 C CB  . LEU   B 67  ? 1.1773 0.6512 0.8492 0.2787  -0.0553 0.0434  760  LEU   B CB  
2539 C CG  . LEU   B 67  ? 1.2292 0.6520 0.8566 0.2686  -0.0353 0.0348  760  LEU   B CG  
2540 N N   . ASP   B 68  ? 1.0876 0.7044 0.8740 0.2737  -0.0894 0.0503  761  ASP   B N   
2541 C CA  . ASP   B 68  ? 1.0438 0.7308 0.8960 0.2779  -0.0963 0.0503  761  ASP   B CA  
2542 C C   . ASP   B 68  ? 1.0217 0.7404 0.8834 0.2460  -0.0983 0.0456  761  ASP   B C   
2543 O O   . ASP   B 68  ? 0.9931 0.7578 0.8976 0.2408  -0.0905 0.0412  761  ASP   B O   
2544 C CB  . ASP   B 68  ? 1.0560 0.7612 0.9322 0.2992  -0.1218 0.0597  761  ASP   B CB  
2545 C CG  . ASP   B 68  ? 1.1418 0.8179 1.0127 0.3344  -0.1225 0.0657  761  ASP   B CG  
2546 O OD1 . ASP   B 68  ? 1.1749 0.8284 1.0377 0.3458  -0.0997 0.0613  761  ASP   B OD1 
2547 O OD2 . ASP   B 68  ? 1.1638 0.8363 1.0354 0.3514  -0.1465 0.0748  761  ASP   B OD2 
2548 N N   . GLU   B 69  ? 1.0346 0.7267 0.8559 0.2254  -0.1069 0.0469  762  GLU   B N   
2549 C CA  . GLU   B 69  ? 1.0217 0.7383 0.8480 0.1967  -0.1080 0.0427  762  GLU   B CA  
2550 C C   . GLU   B 69  ? 1.0217 0.7382 0.8449 0.1799  -0.0875 0.0345  762  GLU   B C   
2551 O O   . GLU   B 69  ? 1.0015 0.7577 0.8550 0.1668  -0.0842 0.0303  762  GLU   B O   
2552 C CB  . GLU   B 69  ? 1.0687 0.7511 0.8491 0.1810  -0.1178 0.0463  762  GLU   B CB  
2553 C CG  . GLU   B 69  ? 1.1038 0.8099 0.8966 0.1810  -0.1393 0.0507  762  GLU   B CG  
2554 C CD  . GLU   B 69  ? 1.1676 0.8767 0.9732 0.2085  -0.1587 0.0584  762  GLU   B CD  
2555 N N   . ALA   B 70  ? 1.0435 0.7130 0.8282 0.1805  -0.0749 0.0323  763  ALA   B N   
2556 C CA  . ALA   B 70  ? 1.0468 0.7081 0.8207 0.1657  -0.0581 0.0245  763  ALA   B CA  
2557 C C   . ALA   B 70  ? 1.0151 0.7104 0.8275 0.1781  -0.0459 0.0207  763  ALA   B C   
2558 O O   . ALA   B 70  ? 1.0067 0.7183 0.8262 0.1626  -0.0370 0.0152  763  ALA   B O   
2559 C CB  . ALA   B 70  ? 1.0886 0.6867 0.8098 0.1652  -0.0498 0.0230  763  ALA   B CB  
2560 N N   . TYR   B 71  ? 0.9972 0.7046 0.8360 0.2061  -0.0453 0.0243  764  TYR   B N   
2561 C CA  . TYR   B 71  ? 0.9779 0.7210 0.8589 0.2197  -0.0312 0.0217  764  TYR   B CA  
2562 C C   . TYR   B 71  ? 0.9305 0.7314 0.8573 0.2055  -0.0362 0.0213  764  TYR   B C   
2563 O O   . TYR   B 71  ? 0.9186 0.7398 0.8628 0.2004  -0.0211 0.0171  764  TYR   B O   
2564 C CB  . TYR   B 71  ? 0.9808 0.7326 0.8903 0.2531  -0.0319 0.0269  764  TYR   B CB  
2565 C CG  . TYR   B 71  ? 1.0409 0.7395 0.9141 0.2731  -0.0173 0.0254  764  TYR   B CG  
2566 C CD1 . TYR   B 71  ? 1.0792 0.7490 0.9233 0.2678  0.0051  0.0175  764  TYR   B CD1 
2567 C CD2 . TYR   B 71  ? 1.0695 0.7443 0.9357 0.2988  -0.0263 0.0319  764  TYR   B CD2 
2568 C CE1 . TYR   B 71  ? 1.1252 0.7403 0.9306 0.2857  0.0191  0.0150  764  TYR   B CE1 
2569 C CE2 . TYR   B 71  ? 1.1154 0.7357 0.9446 0.3179  -0.0122 0.0303  764  TYR   B CE2 
2570 C CZ  . TYR   B 71  ? 1.1526 0.7427 0.9513 0.3110  0.0112  0.0213  764  TYR   B CZ  
2571 O OH  . TYR   B 71  ? 1.2182 0.7500 0.9768 0.3302  0.0260  0.0187  764  TYR   B OH  
2572 N N   . VAL   B 72  ? 0.9060 0.7284 0.8471 0.1989  -0.0570 0.0256  765  VAL   B N   
2573 C CA  . VAL   B 72  ? 0.8739 0.7445 0.8525 0.1839  -0.0644 0.0250  765  VAL   B CA  
2574 C C   . VAL   B 72  ? 0.8802 0.7443 0.8373 0.1573  -0.0574 0.0197  765  VAL   B C   
2575 O O   . VAL   B 72  ? 0.8691 0.7633 0.8522 0.1488  -0.0495 0.0169  765  VAL   B O   
2576 C CB  . VAL   B 72  ? 0.8687 0.7539 0.8578 0.1842  -0.0895 0.0302  765  VAL   B CB  
2577 C CG1 . VAL   B 72  ? 0.8484 0.7732 0.8654 0.1651  -0.0969 0.0281  765  VAL   B CG1 
2578 C CG2 . VAL   B 72  ? 0.8522 0.7534 0.8730 0.2115  -0.0997 0.0360  765  VAL   B CG2 
2579 N N   . MET   B 73  ? 0.9001 0.7245 0.8109 0.1446  -0.0594 0.0187  766  MET   B N   
2580 C CA  . MET   B 73  ? 0.9102 0.7295 0.8036 0.1205  -0.0543 0.0141  766  MET   B CA  
2581 C C   . MET   B 73  ? 0.9050 0.7206 0.7959 0.1198  -0.0370 0.0092  766  MET   B C   
2582 O O   . MET   B 73  ? 0.9015 0.7339 0.7999 0.1047  -0.0337 0.0063  766  MET   B O   
2583 C CB  . MET   B 73  ? 0.9568 0.7336 0.8044 0.1080  -0.0576 0.0141  766  MET   B CB  
2584 C CG  . MET   B 73  ? 1.0019 0.7753 0.8414 0.1048  -0.0718 0.0188  766  MET   B CG  
2585 S SD  . MET   B 73  ? 1.1310 0.8516 0.9166 0.0884  -0.0699 0.0192  766  MET   B SD  
2586 N N   . ALA   B 74  ? 0.9066 0.6966 0.7834 0.1371  -0.0259 0.0083  767  ALA   B N   
2587 C CA  . ALA   B 74  ? 0.9066 0.6844 0.7719 0.1386  -0.0078 0.0032  767  ALA   B CA  
2588 C C   . ALA   B 74  ? 0.8686 0.6890 0.7781 0.1468  0.0030  0.0037  767  ALA   B C   
2589 O O   . ALA   B 74  ? 0.8834 0.7028 0.7857 0.1398  0.0160  0.0001  767  ALA   B O   
2590 C CB  . ALA   B 74  ? 0.9333 0.6637 0.7639 0.1550  0.0020  0.0015  767  ALA   B CB  
2591 N N   . SER   B 75  ? 0.8202 0.6770 0.7744 0.1603  -0.0029 0.0084  768  SER   B N   
2592 C CA  . SER   B 75  ? 0.7756 0.6772 0.7792 0.1663  0.0071  0.0095  768  SER   B CA  
2593 C C   . SER   B 75  ? 0.7431 0.6718 0.7611 0.1442  0.0053  0.0084  768  SER   B C   
2594 O O   . SER   B 75  ? 0.7222 0.6735 0.7642 0.1439  0.0199  0.0081  768  SER   B O   
2595 C CB  . SER   B 75  ? 0.7621 0.6983 0.8129 0.1830  -0.0042 0.0149  768  SER   B CB  
2596 O OG  . SER   B 75  ? 0.7789 0.7331 0.8399 0.1705  -0.0274 0.0173  768  SER   B OG  
2597 N N   . VAL   B 76  ? 0.7420 0.6657 0.7436 0.1264  -0.0108 0.0081  769  VAL   B N   
2598 C CA  . VAL   B 76  ? 0.7323 0.6745 0.7412 0.1061  -0.0149 0.0071  769  VAL   B CA  
2599 C C   . VAL   B 76  ? 0.7470 0.6753 0.7353 0.0982  0.0009  0.0040  769  VAL   B C   
2600 O O   . VAL   B 76  ? 0.7422 0.6913 0.7468 0.0880  0.0037  0.0044  769  VAL   B O   
2601 C CB  . VAL   B 76  ? 0.7511 0.6807 0.7386 0.0926  -0.0319 0.0070  769  VAL   B CB  
2602 C CG1 . VAL   B 76  ? 0.7518 0.6939 0.7415 0.0733  -0.0350 0.0055  769  VAL   B CG1 
2603 C CG2 . VAL   B 76  ? 0.7490 0.6916 0.7537 0.0998  -0.0477 0.0105  769  VAL   B CG2 
2604 N N   . ASP   B 77  ? 0.7670 0.6571 0.7171 0.1036  0.0110  0.0010  770  ASP   B N   
2605 C CA  . ASP   B 77  ? 0.7792 0.6495 0.7020 0.0977  0.0250  -0.0022 770  ASP   B CA  
2606 C C   . ASP   B 77  ? 0.7493 0.6413 0.6981 0.1060  0.0446  -0.0008 770  ASP   B C   
2607 O O   . ASP   B 77  ? 0.7676 0.6460 0.6945 0.0995  0.0561  -0.0024 770  ASP   B O   
2608 C CB  . ASP   B 77  ? 0.8425 0.6628 0.7162 0.1033  0.0315  -0.0066 770  ASP   B CB  
2609 C CG  . ASP   B 77  ? 0.9324 0.7259 0.7748 0.0901  0.0153  -0.0084 770  ASP   B CG  
2610 N N   . ASN   B 78  ? 0.7018 0.6272 0.6969 0.1194  0.0483  0.0025  771  ASN   B N   
2611 C CA  . ASN   B 78  ? 0.6693 0.6195 0.6962 0.1264  0.0689  0.0043  771  ASN   B CA  
2612 C C   . ASN   B 78  ? 0.6175 0.6188 0.7015 0.1201  0.0604  0.0084  771  ASN   B C   
2613 O O   . ASN   B 78  ? 0.5996 0.6240 0.7158 0.1272  0.0460  0.0105  771  ASN   B O   
2614 C CB  . ASN   B 78  ? 0.6886 0.6317 0.7228 0.1506  0.0857  0.0039  771  ASN   B CB  
2615 C CG  . ASN   B 78  ? 0.7122 0.6814 0.7819 0.1597  0.1118  0.0057  771  ASN   B CG  
2616 O OD1 . ASN   B 78  ? 0.7106 0.6857 0.7791 0.1473  0.1238  0.0063  771  ASN   B OD1 
2617 N ND2 . ASN   B 78  ? 0.7218 0.7076 0.8258 0.1819  0.1220  0.0073  771  ASN   B ND2 
2618 N N   . PRO   B 79  ? 0.5916 0.6080 0.6864 0.1063  0.0677  0.0098  772  PRO   B N   
2619 C CA  . PRO   B 79  ? 0.5971 0.5868 0.6534 0.0970  0.0825  0.0086  772  PRO   B CA  
2620 C C   . PRO   B 79  ? 0.6109 0.5708 0.6215 0.0825  0.0663  0.0063  772  PRO   B C   
2621 O O   . PRO   B 79  ? 0.6432 0.5729 0.6128 0.0774  0.0743  0.0048  772  PRO   B O   
2622 C CB  . PRO   B 79  ? 0.5810 0.6034 0.6753 0.0883  0.0928  0.0126  772  PRO   B CB  
2623 C CG  . PRO   B 79  ? 0.5637 0.6225 0.7018 0.0827  0.0712  0.0142  772  PRO   B CG  
2624 C CD  . PRO   B 79  ? 0.5480 0.6090 0.6949 0.0982  0.0597  0.0131  772  PRO   B CD  
2625 N N   A GLY   B 80  ? 0.5978 0.5668 0.6162 0.0759  0.0437  0.0062  773  GLY   B N   
2626 N N   B GLY   B 80  ? 0.5978 0.5668 0.6162 0.0759  0.0437  0.0062  773  GLY   B N   
2627 C CA  A GLY   B 80  ? 0.6126 0.5594 0.5968 0.0631  0.0285  0.0042  773  GLY   B CA  
2628 C CA  B GLY   B 80  ? 0.6126 0.5594 0.5968 0.0631  0.0285  0.0042  773  GLY   B CA  
2629 C C   A GLY   B 80  ? 0.5938 0.5557 0.5878 0.0477  0.0191  0.0060  773  GLY   B C   
2630 C C   B GLY   B 80  ? 0.5938 0.5557 0.5878 0.0477  0.0191  0.0060  773  GLY   B C   
2631 O O   A GLY   B 80  ? 0.5818 0.5659 0.6027 0.0447  0.0257  0.0088  773  GLY   B O   
2632 O O   B GLY   B 80  ? 0.5818 0.5659 0.6027 0.0447  0.0257  0.0088  773  GLY   B O   
2633 N N   . ASN   B 81  ? 0.5868 0.5359 0.5601 0.0380  0.0042  0.0045  774  ASN   B N   
2634 C CA  . ASN   B 81  ? 0.5589 0.5179 0.5380 0.0255  -0.0052 0.0060  774  ASN   B CA  
2635 C C   . ASN   B 81  ? 0.5618 0.4980 0.5089 0.0178  -0.0155 0.0040  774  ASN   B C   
2636 O O   . ASN   B 81  ? 0.5672 0.4919 0.5025 0.0183  -0.0220 0.0015  774  ASN   B O   
2637 C CB  . ASN   B 81  ? 0.5422 0.5262 0.5519 0.0230  -0.0166 0.0063  774  ASN   B CB  
2638 C CG  . ASN   B 81  ? 0.5435 0.5383 0.5634 0.0127  -0.0226 0.0076  774  ASN   B CG  
2639 O OD1 . ASN   B 81  ? 0.5474 0.5566 0.5874 0.0106  -0.0168 0.0098  774  ASN   B OD1 
2640 N ND2 . ASN   B 81  ? 0.5432 0.5309 0.5509 0.0061  -0.0332 0.0064  774  ASN   B ND2 
2641 N N   . PRO   B 82  ? 0.5533 0.4832 0.4876 0.0098  -0.0184 0.0055  775  PRO   B N   
2642 C CA  . PRO   B 82  ? 0.5594 0.4719 0.4688 0.0019  -0.0306 0.0038  775  PRO   B CA  
2643 C C   . PRO   B 82  ? 0.5487 0.4738 0.4734 -0.0040 -0.0436 0.0026  775  PRO   B C   
2644 O O   . PRO   B 82  ? 0.5564 0.4696 0.4658 -0.0107 -0.0524 0.0008  775  PRO   B O   
2645 C CB  . PRO   B 82  ? 0.5731 0.4807 0.4717 -0.0032 -0.0327 0.0070  775  PRO   B CB  
2646 C CG  . PRO   B 82  ? 0.5673 0.4911 0.4880 -0.0001 -0.0217 0.0106  775  PRO   B CG  
2647 C CD  . PRO   B 82  ? 0.5436 0.4792 0.4837 0.0080  -0.0105 0.0093  775  PRO   B CD  
2648 N N   . HIS   B 83  ? 0.5312 0.4791 0.4849 -0.0025 -0.0443 0.0034  776  HIS   B N   
2649 C CA  . HIS   B 83  ? 0.5225 0.4799 0.4875 -0.0078 -0.0535 0.0024  776  HIS   B CA  
2650 C C   . HIS   B 83  ? 0.5291 0.4843 0.4948 -0.0037 -0.0535 0.0009  776  HIS   B C   
2651 O O   . HIS   B 83  ? 0.5128 0.4763 0.4881 -0.0064 -0.0581 0.0005  776  HIS   B O   
2652 C CB  . HIS   B 83  ? 0.5035 0.4804 0.4915 -0.0102 -0.0559 0.0039  776  HIS   B CB  
2653 C CG  . HIS   B 83  ? 0.5146 0.4890 0.4982 -0.0130 -0.0568 0.0064  776  HIS   B CG  
2654 N ND1 . HIS   B 83  ? 0.5344 0.5121 0.5241 -0.0108 -0.0500 0.0092  776  HIS   B ND1 
2655 C CD2 . HIS   B 83  ? 0.5219 0.4879 0.4927 -0.0175 -0.0641 0.0071  776  HIS   B CD2 
2656 C CE1 . HIS   B 83  ? 0.5395 0.5078 0.5163 -0.0133 -0.0531 0.0119  776  HIS   B CE1 
2657 N NE2 . HIS   B 83  ? 0.5426 0.5046 0.5084 -0.0168 -0.0630 0.0107  776  HIS   B NE2 
2658 N N   . VAL   B 84  ? 0.5548 0.4945 0.5058 0.0033  -0.0482 0.0002  777  VAL   B N   
2659 C CA  . VAL   B 84  ? 0.5815 0.5129 0.5279 0.0095  -0.0488 -0.0003 777  VAL   B CA  
2660 C C   . VAL   B 84  ? 0.6231 0.5233 0.5376 0.0094  -0.0465 -0.0024 777  VAL   B C   
2661 O O   . VAL   B 84  ? 0.6361 0.5236 0.5361 0.0124  -0.0400 -0.0034 777  VAL   B O   
2662 C CB  . VAL   B 84  ? 0.5765 0.5223 0.5431 0.0218  -0.0441 0.0012  777  VAL   B CB  
2663 C CG1 . VAL   B 84  ? 0.5937 0.5248 0.5506 0.0327  -0.0438 0.0014  777  VAL   B CG1 
2664 C CG2 . VAL   B 84  ? 0.5606 0.5321 0.5545 0.0193  -0.0503 0.0023  777  VAL   B CG2 
2665 N N   . CYS   B 85  ? 0.6485 0.5329 0.5487 0.0047  -0.0511 -0.0031 778  CYS   B N   
2666 C CA  . CYS   B 85  ? 0.6956 0.5459 0.5633 0.0026  -0.0497 -0.0055 778  CYS   B CA  
2667 C C   . CYS   B 85  ? 0.7204 0.5521 0.5751 0.0187  -0.0410 -0.0059 778  CYS   B C   
2668 O O   . CYS   B 85  ? 0.6964 0.5450 0.5719 0.0317  -0.0376 -0.0036 778  CYS   B O   
2669 C CB  . CYS   B 85  ? 0.7202 0.5570 0.5769 -0.0079 -0.0551 -0.0055 778  CYS   B CB  
2670 S SG  . CYS   B 85  ? 0.8041 0.6572 0.6730 -0.0278 -0.0626 -0.0062 778  CYS   B SG  
2671 N N   . ARG   B 86  ? 0.7640 0.5607 0.5852 0.0179  -0.0377 -0.0092 779  ARG   B N   
2672 C CA  . ARG   B 86  ? 0.7994 0.5730 0.6040 0.0343  -0.0269 -0.0104 779  ARG   B CA  
2673 C C   . ARG   B 86  ? 0.8335 0.5676 0.6065 0.0342  -0.0286 -0.0119 779  ARG   B C   
2674 O O   . ARG   B 86  ? 0.8572 0.5657 0.6030 0.0190  -0.0333 -0.0152 779  ARG   B O   
2675 C CB  . ARG   B 86  ? 0.8435 0.6036 0.6287 0.0345  -0.0186 -0.0138 779  ARG   B CB  
2676 C CG  . ARG   B 86  ? 0.9472 0.6708 0.7017 0.0486  -0.0051 -0.0172 779  ARG   B CG  
2677 C CD  . ARG   B 86  ? 1.0435 0.7540 0.7755 0.0467  0.0035  -0.0203 779  ARG   B CD  
2678 N NE  . ARG   B 86  ? 1.1542 0.8149 0.8394 0.0538  0.0138  -0.0259 779  ARG   B NE  
2679 C CZ  . ARG   B 86  ? 1.2165 0.8658 0.8976 0.0742  0.0332  -0.0268 779  ARG   B CZ  
2680 N NH1 . ARG   B 86  ? 1.1997 0.8883 0.9256 0.0884  0.0432  -0.0220 779  ARG   B NH1 
2681 N NH2 . ARG   B 86  ? 1.2517 0.8503 0.8850 0.0805  0.0432  -0.0327 779  ARG   B NH2 
2682 N N   . LEU   B 87  ? 0.8314 0.5605 0.6090 0.0501  -0.0262 -0.0089 780  LEU   B N   
2683 C CA  . LEU   B 87  ? 0.8560 0.5424 0.6005 0.0526  -0.0267 -0.0092 780  LEU   B CA  
2684 C C   . LEU   B 87  ? 0.8974 0.5457 0.6092 0.0614  -0.0155 -0.0142 780  LEU   B C   
2685 O O   . LEU   B 87  ? 0.8987 0.5534 0.6211 0.0811  -0.0044 -0.0141 780  LEU   B O   
2686 C CB  . LEU   B 87  ? 0.8415 0.5317 0.5985 0.0698  -0.0291 -0.0036 780  LEU   B CB  
2687 C CG  . LEU   B 87  ? 0.8767 0.5181 0.5958 0.0717  -0.0304 -0.0025 780  LEU   B CG  
2688 C CD1 . LEU   B 87  ? 0.8836 0.5143 0.5878 0.0471  -0.0380 -0.0019 780  LEU   B CD1 
2689 C CD2 . LEU   B 87  ? 0.8761 0.5166 0.6039 0.0947  -0.0329 0.0035  780  LEU   B CD2 
2690 N N   . LEU   B 88  ? 0.9278 0.5376 0.6009 0.0459  -0.0178 -0.0191 781  LEU   B N   
2691 C CA  . LEU   B 88  ? 0.9714 0.5360 0.6034 0.0519  -0.0080 -0.0253 781  LEU   B CA  
2692 C C   . LEU   B 88  ? 1.0096 0.5321 0.6162 0.0688  -0.0014 -0.0250 781  LEU   B C   
2693 O O   . LEU   B 88  ? 1.0320 0.5308 0.6218 0.0879  0.0125  -0.0280 781  LEU   B O   
2694 C CB  . LEU   B 88  ? 0.9947 0.5318 0.5929 0.0269  -0.0164 -0.0313 781  LEU   B CB  
2695 C CG  . LEU   B 88  ? 0.9927 0.5641 0.6094 0.0114  -0.0244 -0.0318 781  LEU   B CG  
2696 C CD1 . LEU   B 88  ? 1.0229 0.5639 0.6051 -0.0116 -0.0355 -0.0377 781  LEU   B CD1 
2697 C CD2 . LEU   B 88  ? 0.9906 0.5783 0.6157 0.0261  -0.0127 -0.0321 781  LEU   B CD2 
2698 N N   . GLY   B 89  ? 1.0134 0.5229 0.6144 0.0621  -0.0100 -0.0213 782  GLY   B N   
2699 C CA  . GLY   B 89  ? 1.0416 0.5065 0.6151 0.0780  -0.0054 -0.0197 782  GLY   B CA  
2700 C C   . GLY   B 89  ? 1.0468 0.5067 0.6211 0.0733  -0.0148 -0.0128 782  GLY   B C   
2701 O O   . GLY   B 89  ? 1.0244 0.5124 0.6174 0.0544  -0.0239 -0.0101 782  GLY   B O   
2702 N N   . ILE   B 90  ? 1.0766 0.4974 0.6279 0.0918  -0.0114 -0.0098 783  ILE   B N   
2703 C CA  . ILE   B 90  ? 1.1035 0.5063 0.6436 0.0894  -0.0191 -0.0025 783  ILE   B CA  
2704 C C   . ILE   B 90  ? 1.1586 0.4881 0.6442 0.0921  -0.0144 -0.0038 783  ILE   B C   
2705 O O   . ILE   B 90  ? 1.1693 0.4681 0.6360 0.1125  -0.0047 -0.0075 783  ILE   B O   
2706 C CB  . ILE   B 90  ? 1.0873 0.5248 0.6618 0.1128  -0.0248 0.0061  783  ILE   B CB  
2707 C CG1 . ILE   B 90  ? 1.1119 0.5275 0.6676 0.1078  -0.0340 0.0143  783  ILE   B CG1 
2708 C CG2 . ILE   B 90  ? 1.0921 0.5227 0.6732 0.1472  -0.0171 0.0067  783  ILE   B CG2 
2709 N N   . CYS   B 91  ? 1.1957 0.4946 0.6545 0.0702  -0.0193 -0.0014 784  CYS   B N   
2710 C CA  . CYS   B 91  ? 1.2593 0.4840 0.6638 0.0699  -0.0154 -0.0016 784  CYS   B CA  
2711 C C   . CYS   B 91  ? 1.2860 0.4934 0.6799 0.0763  -0.0205 0.0095  784  CYS   B C   
2712 O O   . CYS   B 91  ? 1.2794 0.5008 0.6790 0.0541  -0.0254 0.0137  784  CYS   B O   
2713 C CB  . CYS   B 91  ? 1.2928 0.4865 0.6679 0.0349  -0.0157 -0.0088 784  CYS   B CB  
2714 S SG  . CYS   B 91  ? 1.4164 0.5112 0.7197 0.0312  -0.0103 -0.0107 784  CYS   B SG  
2715 N N   . LEU   B 92  ? 1.3159 0.4930 0.6945 0.1080  -0.0191 0.0146  785  LEU   B N   
2716 C CA  . LEU   B 92  ? 1.3433 0.4977 0.7054 0.1173  -0.0259 0.0261  785  LEU   B CA  
2717 C C   . LEU   B 92  ? 1.4098 0.4797 0.7098 0.1152  -0.0215 0.0284  785  LEU   B C   
2718 O O   . LEU   B 92  ? 1.4462 0.4729 0.7218 0.1398  -0.0159 0.0270  785  LEU   B O   
2719 C CB  . LEU   B 92  ? 1.3269 0.5098 0.7189 0.1555  -0.0324 0.0332  785  LEU   B CB  
2720 C CG  . LEU   B 92  ? 1.3021 0.5648 0.7535 0.1588  -0.0409 0.0349  785  LEU   B CG  
2721 C CD1 . LEU   B 92  ? 1.2991 0.5743 0.7678 0.1915  -0.0522 0.0444  785  LEU   B CD1 
2722 C CD2 . LEU   B 92  ? 1.3039 0.5920 0.7621 0.1282  -0.0467 0.0368  785  LEU   B CD2 
2723 N N   . THR   B 93  ? 1.4263 0.4708 0.7003 0.0864  -0.0226 0.0324  786  THR   B N   
2724 C CA  . THR   B 93  ? 1.4805 0.4426 0.6935 0.0807  -0.0188 0.0370  786  THR   B CA  
2725 C C   . THR   B 93  ? 1.4765 0.4408 0.6841 0.0813  -0.0259 0.0506  786  THR   B C   
2726 O O   . THR   B 93  ? 1.4548 0.4610 0.6932 0.1060  -0.0352 0.0563  786  THR   B O   
2727 C CB  . THR   B 93  ? 1.5244 0.4527 0.7109 0.0426  -0.0117 0.0279  786  THR   B CB  
2728 O OG1 . THR   B 93  ? 1.5194 0.4923 0.7333 0.0090  -0.0135 0.0283  786  THR   B OG1 
2729 C CG2 . THR   B 93  ? 1.5250 0.4562 0.7163 0.0450  -0.0075 0.0144  786  THR   B CG2 
2730 N N   . SER   B 94  ? 1.4913 0.4121 0.6606 0.0543  -0.0218 0.0560  787  SER   B N   
2731 C CA  . SER   B 94  ? 1.4792 0.4041 0.6410 0.0525  -0.0265 0.0682  787  SER   B CA  
2732 C C   . SER   B 94  ? 1.4138 0.4201 0.6294 0.0378  -0.0294 0.0659  787  SER   B C   
2733 O O   . SER   B 94  ? 1.4116 0.4370 0.6319 0.0450  -0.0360 0.0741  787  SER   B O   
2734 C CB  . SER   B 94  ? 1.5352 0.3919 0.6418 0.0259  -0.0174 0.0745  787  SER   B CB  
2735 O OG  . SER   B 94  ? 1.6045 0.3828 0.6590 0.0442  -0.0162 0.0778  787  SER   B OG  
2736 N N   . THR   B 95  ? 1.3638 0.4145 0.6168 0.0182  -0.0254 0.0547  788  THR   B N   
2737 C CA  . THR   B 95  ? 1.3078 0.4351 0.6141 0.0068  -0.0279 0.0514  788  THR   B CA  
2738 C C   . THR   B 95  ? 1.2509 0.4321 0.6035 0.0260  -0.0334 0.0433  788  THR   B C   
2739 O O   . THR   B 95  ? 1.2539 0.4139 0.5978 0.0403  -0.0317 0.0381  788  THR   B O   
2740 C CB  . THR   B 95  ? 1.3184 0.4570 0.6338 -0.0343 -0.0189 0.0462  788  THR   B CB  
2741 O OG1 . THR   B 95  ? 1.3229 0.4586 0.6442 -0.0443 -0.0176 0.0354  788  THR   B OG1 
2742 C CG2 . THR   B 95  ? 1.3593 0.4426 0.6301 -0.0570 -0.0095 0.0537  788  THR   B CG2 
2743 N N   . VAL   B 96  ? 1.2048 0.4518 0.6035 0.0257  -0.0381 0.0423  789  VAL   B N   
2744 C CA  . VAL   B 96  ? 1.1647 0.4647 0.6083 0.0390  -0.0415 0.0354  789  VAL   B CA  
2745 C C   . VAL   B 96  ? 1.1345 0.4607 0.5983 0.0107  -0.0366 0.0265  789  VAL   B C   
2746 O O   . VAL   B 96  ? 1.1299 0.4732 0.6029 -0.0137 -0.0345 0.0273  789  VAL   B O   
2747 C CB  . VAL   B 96  ? 1.1435 0.4979 0.6247 0.0530  -0.0507 0.0395  789  VAL   B CB  
2748 C CG1 . VAL   B 96  ? 1.1132 0.5221 0.6419 0.0641  -0.0524 0.0328  789  VAL   B CG1 
2749 C CG2 . VAL   B 96  ? 1.1671 0.4956 0.6272 0.0793  -0.0597 0.0493  789  VAL   B CG2 
2750 N N   . GLN   B 97  ? 1.1148 0.4424 0.5841 0.0143  -0.0345 0.0182  790  GLN   B N   
2751 C CA  . GLN   B 97  ? 1.0890 0.4433 0.5778 -0.0100 -0.0336 0.0100  790  GLN   B CA  
2752 C C   . GLN   B 97  ? 1.0361 0.4406 0.5633 0.0051  -0.0357 0.0057  790  GLN   B C   
2753 O O   . GLN   B 97  ? 1.0358 0.4302 0.5585 0.0292  -0.0331 0.0042  790  GLN   B O   
2754 C CB  . GLN   B 97  ? 1.1441 0.4462 0.5950 -0.0261 -0.0302 0.0035  790  GLN   B CB  
2755 C CG  . GLN   B 97  ? 1.2186 0.4857 0.6440 -0.0532 -0.0277 0.0070  790  GLN   B CG  
2756 C CD  . GLN   B 97  ? 1.3271 0.5428 0.7165 -0.0730 -0.0263 -0.0001 790  GLN   B CD  
2757 O OE1 . GLN   B 97  ? 1.3538 0.5847 0.7562 -0.1022 -0.0295 -0.0054 790  GLN   B OE1 
2758 N NE2 . GLN   B 97  ? 1.3708 0.5231 0.7139 -0.0574 -0.0225 -0.0003 790  GLN   B NE2 
2759 N N   . LEU   B 98  ? 0.9931 0.4518 0.5594 -0.0071 -0.0390 0.0046  791  LEU   B N   
2760 C CA  . LEU   B 98  ? 0.9622 0.4677 0.5644 0.0043  -0.0404 0.0013  791  LEU   B CA  
2761 C C   . LEU   B 98  ? 0.9524 0.4664 0.5583 -0.0153 -0.0412 -0.0062 791  LEU   B C   
2762 O O   . LEU   B 98  ? 0.9472 0.4672 0.5573 -0.0402 -0.0443 -0.0070 791  LEU   B O   
2763 C CB  . LEU   B 98  ? 0.9364 0.4933 0.5772 0.0071  -0.0449 0.0059  791  LEU   B CB  
2764 C CG  . LEU   B 98  ? 0.9637 0.5122 0.5982 0.0239  -0.0481 0.0136  791  LEU   B CG  
2765 C CD1 . LEU   B 98  ? 0.9424 0.5364 0.6086 0.0218  -0.0534 0.0166  791  LEU   B CD1 
2766 C CD2 . LEU   B 98  ? 0.9755 0.5150 0.6093 0.0537  -0.0482 0.0148  791  LEU   B CD2 
2767 N N   . ILE   B 99  ? 0.9525 0.4643 0.5549 -0.0042 -0.0384 -0.0115 792  ILE   B N   
2768 C CA  . ILE   B 99  ? 0.9651 0.4777 0.5625 -0.0212 -0.0413 -0.0186 792  ILE   B CA  
2769 C C   . ILE   B 99  ? 0.9443 0.5059 0.5764 -0.0155 -0.0422 -0.0194 792  ILE   B C   
2770 O O   . ILE   B 99  ? 0.9433 0.5175 0.5867 0.0066  -0.0357 -0.0182 792  ILE   B O   
2771 C CB  . ILE   B 99  ? 1.0080 0.4632 0.5577 -0.0169 -0.0363 -0.0251 792  ILE   B CB  
2772 C CG1 . ILE   B 99  ? 1.0448 0.4453 0.5560 -0.0275 -0.0362 -0.0247 792  ILE   B CG1 
2773 C CG2 . ILE   B 99  ? 1.0224 0.4761 0.5615 -0.0315 -0.0411 -0.0328 792  ILE   B CG2 
2774 C CD1 . ILE   B 99  ? 1.0752 0.4434 0.5676 -0.0024 -0.0287 -0.0197 792  ILE   B CD1 
2775 N N   . THR   B 100 ? 0.9267 0.5162 0.5774 -0.0350 -0.0502 -0.0210 793  THR   B N   
2776 C CA  . THR   B 100 ? 0.9127 0.5422 0.5907 -0.0317 -0.0519 -0.0215 793  THR   B CA  
2777 C C   . THR   B 100 ? 0.9244 0.5513 0.5935 -0.0513 -0.0614 -0.0263 793  THR   B C   
2778 O O   . THR   B 100 ? 0.9317 0.5415 0.5890 -0.0710 -0.0687 -0.0282 793  THR   B O   
2779 C CB  . THR   B 100 ? 0.9015 0.5814 0.6240 -0.0312 -0.0543 -0.0161 793  THR   B CB  
2780 O OG1 . THR   B 100 ? 0.9010 0.5908 0.6345 -0.0518 -0.0605 -0.0149 793  THR   B OG1 
2781 C CG2 . THR   B 100 ? 0.9110 0.5978 0.6440 -0.0123 -0.0488 -0.0116 793  THR   B CG2 
2782 N N   . GLN   B 101 ? 0.9274 0.5742 0.6053 -0.0473 -0.0628 -0.0274 794  GLN   B N   
2783 C CA  . GLN   B 101 ? 0.9420 0.5902 0.6136 -0.0645 -0.0755 -0.0306 794  GLN   B CA  
2784 C C   . GLN   B 101 ? 0.9104 0.5941 0.6189 -0.0826 -0.0864 -0.0275 794  GLN   B C   
2785 O O   . GLN   B 101 ? 0.8779 0.5966 0.6215 -0.0771 -0.0824 -0.0226 794  GLN   B O   
2786 C CB  . GLN   B 101 ? 0.9714 0.6370 0.6480 -0.0542 -0.0734 -0.0300 794  GLN   B CB  
2787 C CG  . GLN   B 101 ? 1.0586 0.7108 0.7124 -0.0681 -0.0870 -0.0338 794  GLN   B CG  
2788 C CD  . GLN   B 101 ? 1.1441 0.8138 0.8030 -0.0588 -0.0848 -0.0315 794  GLN   B CD  
2789 O OE1 . GLN   B 101 ? 1.1802 0.8531 0.8412 -0.0409 -0.0686 -0.0297 794  GLN   B OE1 
2790 N NE2 . GLN   B 101 ? 1.1506 0.8318 0.8127 -0.0710 -0.1013 -0.0308 794  GLN   B NE2 
2791 N N   . LEU   B 102 ? 0.9164 0.5885 0.6160 -0.1041 -0.0991 -0.0307 795  LEU   B N   
2792 C CA  . LEU   B 102 ? 0.8932 0.6000 0.6313 -0.1215 -0.1077 -0.0280 795  LEU   B CA  
2793 C C   . LEU   B 102 ? 0.8669 0.6194 0.6414 -0.1177 -0.1141 -0.0248 795  LEU   B C   
2794 O O   . LEU   B 102 ? 0.8793 0.6280 0.6406 -0.1149 -0.1221 -0.0264 795  LEU   B O   
2795 C CB  . LEU   B 102 ? 0.9043 0.5908 0.6280 -0.1464 -0.1221 -0.0325 795  LEU   B CB  
2796 C CG  . LEU   B 102 ? 0.8950 0.6204 0.6640 -0.1663 -0.1311 -0.0299 795  LEU   B CG  
2797 C CD1 . LEU   B 102 ? 0.8916 0.6270 0.6805 -0.1680 -0.1165 -0.0256 795  LEU   B CD1 
2798 C CD2 . LEU   B 102 ? 0.9163 0.6232 0.6730 -0.1921 -0.1487 -0.0349 795  LEU   B CD2 
2799 N N   . MET   B 103 ? 0.8288 0.6198 0.6447 -0.1173 -0.1101 -0.0202 796  MET   B N   
2800 C CA  . MET   B 103 ? 0.8001 0.6334 0.6533 -0.1145 -0.1156 -0.0170 796  MET   B CA  
2801 C C   . MET   B 103 ? 0.7798 0.6329 0.6600 -0.1350 -0.1275 -0.0170 796  MET   B C   
2802 O O   . MET   B 103 ? 0.7770 0.6378 0.6743 -0.1450 -0.1210 -0.0160 796  MET   B O   
2803 C CB  . MET   B 103 ? 0.7908 0.6485 0.6689 -0.1013 -0.1025 -0.0130 796  MET   B CB  
2804 C CG  . MET   B 103 ? 0.8343 0.6761 0.6919 -0.0826 -0.0923 -0.0128 796  MET   B CG  
2805 S SD  . MET   B 103 ? 0.8842 0.7319 0.7373 -0.0706 -0.0950 -0.0124 796  MET   B SD  
2806 C CE  . MET   B 103 ? 0.8917 0.6913 0.6939 -0.0671 -0.0921 -0.0170 796  MET   B CE  
2807 N N   . PRO   B 104 ? 0.7671 0.6236 0.6467 -0.1428 -0.1456 -0.0185 797  PRO   B N   
2808 C CA  . PRO   B 104 ? 0.7481 0.6221 0.6539 -0.1643 -0.1603 -0.0191 797  PRO   B CA  
2809 C C   . PRO   B 104 ? 0.7046 0.6291 0.6691 -0.1667 -0.1577 -0.0146 797  PRO   B C   
2810 O O   . PRO   B 104 ? 0.6858 0.6269 0.6781 -0.1852 -0.1629 -0.0148 797  PRO   B O   
2811 C CB  . PRO   B 104 ? 0.7651 0.6294 0.6524 -0.1682 -0.1828 -0.0212 797  PRO   B CB  
2812 C CG  . PRO   B 104 ? 0.7957 0.6241 0.6344 -0.1516 -0.1757 -0.0229 797  PRO   B CG  
2813 C CD  . PRO   B 104 ? 0.7697 0.6105 0.6211 -0.1336 -0.1542 -0.0195 797  PRO   B CD  
2814 N N   . PHE   B 105 ? 0.6805 0.6288 0.6645 -0.1488 -0.1489 -0.0109 798  PHE   B N   
2815 C CA  . PHE   B 105 ? 0.6436 0.6358 0.6797 -0.1483 -0.1440 -0.0073 798  PHE   B CA  
2816 C C   . PHE   B 105 ? 0.6395 0.6345 0.6833 -0.1458 -0.1213 -0.0063 798  PHE   B C   
2817 O O   . PHE   B 105 ? 0.6313 0.6582 0.7127 -0.1428 -0.1131 -0.0038 798  PHE   B O   
2818 C CB  . PHE   B 105 ? 0.6247 0.6401 0.6788 -0.1323 -0.1497 -0.0040 798  PHE   B CB  
2819 C CG  . PHE   B 105 ? 0.6249 0.6398 0.6736 -0.1349 -0.1738 -0.0036 798  PHE   B CG  
2820 C CD1 . PHE   B 105 ? 0.6609 0.6424 0.6631 -0.1281 -0.1799 -0.0048 798  PHE   B CD1 
2821 C CD2 . PHE   B 105 ? 0.6049 0.6536 0.6957 -0.1426 -0.1900 -0.0014 798  PHE   B CD2 
2822 C CE1 . PHE   B 105 ? 0.6742 0.6496 0.6635 -0.1304 -0.2026 -0.0041 798  PHE   B CE1 
2823 C CE2 . PHE   B 105 ? 0.6162 0.6618 0.6983 -0.1447 -0.2158 -0.0005 798  PHE   B CE2 
2824 C CZ  . PHE   B 105 ? 0.6458 0.6523 0.6735 -0.1388 -0.2221 -0.0018 798  PHE   B CZ  
2825 N N   . GLY   B 106 ? 0.6459 0.6058 0.6530 -0.1466 -0.1114 -0.0080 799  GLY   B N   
2826 C CA  . GLY   B 106 ? 0.6417 0.5975 0.6479 -0.1444 -0.0922 -0.0064 799  GLY   B CA  
2827 C C   . GLY   B 106 ? 0.6353 0.6013 0.6446 -0.1247 -0.0827 -0.0046 799  GLY   B C   
2828 O O   . GLY   B 106 ? 0.6434 0.6089 0.6448 -0.1117 -0.0887 -0.0048 799  GLY   B O   
2829 N N   . CYS   B 107 ? 0.6202 0.5930 0.6387 -0.1234 -0.0675 -0.0030 800  CYS   B N   
2830 C CA  . CYS   B 107 ? 0.6143 0.5935 0.6331 -0.1071 -0.0596 -0.0021 800  CYS   B CA  
2831 C C   . CYS   B 107 ? 0.5760 0.5909 0.6333 -0.1021 -0.0592 -0.0014 800  CYS   B C   
2832 O O   . CYS   B 107 ? 0.5539 0.5924 0.6433 -0.1115 -0.0599 -0.0008 800  CYS   B O   
2833 C CB  . CYS   B 107 ? 0.6454 0.6061 0.6447 -0.1068 -0.0450 -0.0010 800  CYS   B CB  
2834 S SG  . CYS   B 107 ? 0.7029 0.6767 0.7247 -0.1230 -0.0293 0.0005  800  CYS   B SG  
2835 N N   . LEU   B 108 ? 0.5683 0.5867 0.6238 -0.0871 -0.0580 -0.0015 801  LEU   B N   
2836 C CA  . LEU   B 108 ? 0.5576 0.6019 0.6424 -0.0792 -0.0572 -0.0010 801  LEU   B CA  
2837 C C   . LEU   B 108 ? 0.5566 0.6172 0.6648 -0.0824 -0.0423 -0.0010 801  LEU   B C   
2838 O O   . LEU   B 108 ? 0.5418 0.6294 0.6852 -0.0805 -0.0423 -0.0003 801  LEU   B O   
2839 C CB  . LEU   B 108 ? 0.5663 0.6033 0.6376 -0.0649 -0.0578 -0.0014 801  LEU   B CB  
2840 C CG  . LEU   B 108 ? 0.5714 0.6269 0.6653 -0.0556 -0.0614 -0.0006 801  LEU   B CG  
2841 C CD1 . LEU   B 108 ? 0.5656 0.6339 0.6754 -0.0581 -0.0757 0.0017  801  LEU   B CD1 
2842 C CD2 . LEU   B 108 ? 0.5887 0.6328 0.6662 -0.0454 -0.0622 -0.0010 801  LEU   B CD2 
2843 N N   . LEU   B 109 ? 0.5742 0.6173 0.6624 -0.0871 -0.0289 -0.0014 802  LEU   B N   
2844 C CA  . LEU   B 109 ? 0.5795 0.6323 0.6829 -0.0912 -0.0105 -0.0014 802  LEU   B CA  
2845 C C   . LEU   B 109 ? 0.5702 0.6498 0.7130 -0.1045 -0.0088 -0.0001 802  LEU   B C   
2846 O O   . LEU   B 109 ? 0.5592 0.6666 0.7387 -0.1016 -0.0003 0.0001  802  LEU   B O   
2847 C CB  . LEU   B 109 ? 0.6052 0.6266 0.6705 -0.0952 0.0019  -0.0012 802  LEU   B CB  
2848 C CG  . LEU   B 109 ? 0.6202 0.6443 0.6917 -0.1000 0.0245  -0.0010 802  LEU   B CG  
2849 C CD1 . LEU   B 109 ? 0.6180 0.6535 0.7004 -0.0866 0.0327  -0.0036 802  LEU   B CD1 
2850 C CD2 . LEU   B 109 ? 0.6548 0.6417 0.6815 -0.1053 0.0345  0.0005  802  LEU   B CD2 
2851 N N   . ASP   B 110 ? 0.5742 0.6455 0.7110 -0.1191 -0.0171 0.0008  803  ASP   B N   
2852 C CA  . ASP   B 110 ? 0.5637 0.6612 0.7399 -0.1348 -0.0189 0.0019  803  ASP   B CA  
2853 C C   . ASP   B 110 ? 0.5422 0.6724 0.7563 -0.1289 -0.0366 0.0023  803  ASP   B C   
2854 O O   . ASP   B 110 ? 0.5160 0.6815 0.7781 -0.1334 -0.0344 0.0036  803  ASP   B O   
2855 C CB  . ASP   B 110 ? 0.6110 0.6852 0.7653 -0.1527 -0.0264 0.0019  803  ASP   B CB  
2856 C CG  . ASP   B 110 ? 0.7212 0.7608 0.8385 -0.1600 -0.0092 0.0028  803  ASP   B CG  
2857 O OD1 . ASP   B 110 ? 0.7362 0.7736 0.8488 -0.1541 0.0101  0.0036  803  ASP   B OD1 
2858 O OD2 . ASP   B 110 ? 0.7796 0.7903 0.8689 -0.1713 -0.0152 0.0026  803  ASP   B OD2 
2859 N N   . TYR   B 111 ? 0.5526 0.6706 0.7453 -0.1183 -0.0536 0.0018  804  TYR   B N   
2860 C CA  . TYR   B 111 ? 0.5427 0.6824 0.7595 -0.1114 -0.0723 0.0032  804  TYR   B CA  
2861 C C   . TYR   B 111 ? 0.5235 0.6924 0.7777 -0.0976 -0.0645 0.0045  804  TYR   B C   
2862 O O   . TYR   B 111 ? 0.4894 0.6898 0.7857 -0.0977 -0.0744 0.0067  804  TYR   B O   
2863 C CB  . TYR   B 111 ? 0.5628 0.6762 0.7405 -0.1025 -0.0863 0.0027  804  TYR   B CB  
2864 C CG  . TYR   B 111 ? 0.5549 0.6821 0.7470 -0.0979 -0.1074 0.0048  804  TYR   B CG  
2865 C CD1 . TYR   B 111 ? 0.5620 0.6879 0.7527 -0.1105 -0.1269 0.0048  804  TYR   B CD1 
2866 C CD2 . TYR   B 111 ? 0.5525 0.6910 0.7572 -0.0816 -0.1089 0.0070  804  TYR   B CD2 
2867 C CE1 . TYR   B 111 ? 0.5661 0.7015 0.7653 -0.1062 -0.1485 0.0073  804  TYR   B CE1 
2868 C CE2 . TYR   B 111 ? 0.5540 0.7024 0.7695 -0.0767 -0.1289 0.0102  804  TYR   B CE2 
2869 C CZ  . TYR   B 111 ? 0.5700 0.7175 0.7826 -0.0888 -0.1493 0.0106  804  TYR   B CZ  
2870 O OH  . TYR   B 111 ? 0.5916 0.7452 0.8094 -0.0840 -0.1717 0.0142  804  TYR   B OH  
2871 N N   . VAL   B 112 ? 0.5412 0.6984 0.7797 -0.0852 -0.0481 0.0032  805  VAL   B N   
2872 C CA  . VAL   B 112 ? 0.5364 0.7143 0.8044 -0.0710 -0.0388 0.0035  805  VAL   B CA  
2873 C C   . VAL   B 112 ? 0.5258 0.7324 0.8364 -0.0767 -0.0213 0.0038  805  VAL   B C   
2874 O O   . VAL   B 112 ? 0.5013 0.7372 0.8541 -0.0672 -0.0199 0.0053  805  VAL   B O   
2875 C CB  . VAL   B 112 ? 0.5573 0.7122 0.7951 -0.0570 -0.0282 0.0011  805  VAL   B CB  
2876 C CG1 . VAL   B 112 ? 0.5766 0.7116 0.7849 -0.0509 -0.0446 0.0016  805  VAL   B CG1 
2877 C CG2 . VAL   B 112 ? 0.5836 0.7158 0.7914 -0.0623 -0.0097 -0.0016 805  VAL   B CG2 
2878 N N   . ARG   B 113 ? 0.5407 0.7387 0.8416 -0.0918 -0.0075 0.0030  806  ARG   B N   
2879 C CA  . ARG   B 113 ? 0.5302 0.7550 0.8717 -0.1001 0.0122  0.0038  806  ARG   B CA  
2880 C C   . ARG   B 113 ? 0.5230 0.7870 0.9179 -0.1101 -0.0042 0.0066  806  ARG   B C   
2881 O O   . ARG   B 113 ? 0.5045 0.8068 0.9537 -0.1071 0.0047  0.0080  806  ARG   B O   
2882 C CB  . ARG   B 113 ? 0.5505 0.7502 0.8620 -0.1161 0.0301  0.0032  806  ARG   B CB  
2883 C CG  . ARG   B 113 ? 0.5898 0.7546 0.8540 -0.1071 0.0488  0.0009  806  ARG   B CG  
2884 C CD  . ARG   B 113 ? 0.6242 0.7583 0.8515 -0.1226 0.0603  0.0017  806  ARG   B CD  
2885 N NE  . ARG   B 113 ? 0.6667 0.7664 0.8472 -0.1148 0.0770  0.0001  806  ARG   B NE  
2886 C CZ  . ARG   B 113 ? 0.7064 0.7690 0.8406 -0.1232 0.0845  0.0013  806  ARG   B CZ  
2887 N NH1 . ARG   B 113 ? 0.7003 0.7538 0.8288 -0.1400 0.0789  0.0039  806  ARG   B NH1 
2888 N NH2 . ARG   B 113 ? 0.7197 0.7509 0.8103 -0.1150 0.0965  -0.0001 806  ARG   B NH2 
2889 N N   . GLU   B 114 ? 0.5398 0.7942 0.9200 -0.1221 -0.0282 0.0071  807  GLU   B N   
2890 C CA  . GLU   B 114 ? 0.5282 0.8157 0.9535 -0.1343 -0.0484 0.0092  807  GLU   B CA  
2891 C C   . GLU   B 114 ? 0.5343 0.8474 0.9897 -0.1180 -0.0701 0.0118  807  GLU   B C   
2892 O O   . GLU   B 114 ? 0.5040 0.8575 1.0146 -0.1224 -0.0822 0.0144  807  GLU   B O   
2893 C CB  . GLU   B 114 ? 0.5578 0.8196 0.9502 -0.1537 -0.0662 0.0080  807  GLU   B CB  
2894 N N   . HIS   B 115 ? 0.5680 0.8582 0.9894 -0.0992 -0.0749 0.0115  808  HIS   B N   
2895 C CA  . HIS   B 115 ? 0.5747 0.8808 1.0160 -0.0827 -0.0944 0.0148  808  HIS   B CA  
2896 C C   . HIS   B 115 ? 0.5922 0.9047 1.0469 -0.0604 -0.0773 0.0152  808  HIS   B C   
2897 O O   . HIS   B 115 ? 0.5967 0.9036 1.0450 -0.0445 -0.0905 0.0176  808  HIS   B O   
2898 C CB  . HIS   B 115 ? 0.6082 0.8808 0.9994 -0.0807 -0.1172 0.0152  808  HIS   B CB  
2899 C CG  . HIS   B 115 ? 0.6428 0.9051 1.0177 -0.1010 -0.1352 0.0141  808  HIS   B CG  
2900 N ND1 . HIS   B 115 ? 0.6897 0.9190 1.0213 -0.1134 -0.1260 0.0104  808  HIS   B ND1 
2901 C CD2 . HIS   B 115 ? 0.6417 0.9217 1.0386 -0.1109 -0.1617 0.0160  808  HIS   B CD2 
2902 C CE1 . HIS   B 115 ? 0.6975 0.9227 1.0241 -0.1306 -0.1453 0.0097  808  HIS   B CE1 
2903 N NE2 . HIS   B 115 ? 0.6750 0.9296 1.0386 -0.1306 -0.1682 0.0127  808  HIS   B NE2 
2904 N N   . LYS   B 116 ? 0.6036 0.9243 1.0740 -0.0594 -0.0475 0.0129  809  LYS   B N   
2905 C CA  . LYS   B 116 ? 0.6249 0.9470 1.1044 -0.0392 -0.0269 0.0117  809  LYS   B CA  
2906 C C   . LYS   B 116 ? 0.6264 0.9700 1.1406 -0.0194 -0.0416 0.0157  809  LYS   B C   
2907 O O   . LYS   B 116 ? 0.6469 0.9681 1.1368 -0.0025 -0.0405 0.0152  809  LYS   B O   
2908 C CB  . LYS   B 116 ? 0.6345 0.9772 1.1465 -0.0434 0.0047  0.0099  809  LYS   B CB  
2909 C CG  . LYS   B 116 ? 0.7207 1.0288 1.1846 -0.0533 0.0280  0.0057  809  LYS   B CG  
2910 C CD  . LYS   B 116 ? 0.7597 1.0882 1.2546 -0.0651 0.0562  0.0055  809  LYS   B CD  
2911 C CE  . LYS   B 116 ? 0.8352 1.1234 1.2744 -0.0772 0.0749  0.0027  809  LYS   B CE  
2912 N NZ  . LYS   B 116 ? 0.8435 1.1451 1.3029 -0.0998 0.0879  0.0046  809  LYS   B NZ  
2913 N N   . ASP   B 117 ? 0.6002 0.9860 1.1710 -0.0221 -0.0570 0.0200  810  ASP   B N   
2914 C CA  . ASP   B 117 ? 0.5867 0.9991 1.1998 -0.0032 -0.0735 0.0252  810  ASP   B CA  
2915 C C   . ASP   B 117 ? 0.5962 0.9916 1.1823 0.0001  -0.1091 0.0295  810  ASP   B C   
2916 O O   . ASP   B 117 ? 0.5845 0.9993 1.2020 0.0150  -0.1272 0.0350  810  ASP   B O   
2917 C CB  . ASP   B 117 ? 0.5809 1.0512 1.2733 -0.0082 -0.0756 0.0283  810  ASP   B CB  
2918 C CG  . ASP   B 117 ? 0.6418 1.1380 1.3779 -0.0010 -0.0392 0.0261  810  ASP   B CG  
2919 O OD1 . ASP   B 117 ? 0.6782 1.1432 1.3748 0.0001  -0.0099 0.0209  810  ASP   B OD1 
2920 O OD2 . ASP   B 117 ? 0.6367 1.1843 1.4467 0.0037  -0.0399 0.0297  810  ASP   B OD2 
2921 N N   . ASN   B 118 ? 0.6144 0.9737 1.1432 -0.0131 -0.1190 0.0275  811  ASN   B N   
2922 C CA  . ASN   B 118 ? 0.6215 0.9593 1.1172 -0.0111 -0.1492 0.0314  811  ASN   B CA  
2923 C C   . ASN   B 118 ? 0.6306 0.9199 1.0614 -0.0055 -0.1429 0.0294  811  ASN   B C   
2924 O O   . ASN   B 118 ? 0.6589 0.9243 1.0532 -0.0071 -0.1628 0.0319  811  ASN   B O   
2925 C CB  . ASN   B 118 ? 0.6517 0.9914 1.1398 -0.0332 -0.1709 0.0311  811  ASN   B CB  
2926 C CG  . ASN   B 118 ? 0.6915 1.0804 1.2456 -0.0410 -0.1845 0.0337  811  ASN   B CG  
2927 O OD1 . ASN   B 118 ? 0.7077 1.1110 1.2782 -0.0621 -0.1809 0.0308  811  ASN   B OD1 
2928 N ND2 . ASN   B 118 ? 0.6875 1.1033 1.2823 -0.0242 -0.2007 0.0397  811  ASN   B ND2 
2929 N N   . ILE   B 119 ? 0.6014 0.8750 1.0163 -0.0002 -0.1157 0.0250  812  ILE   B N   
2930 C CA  . ILE   B 119 ? 0.6037 0.8359 0.9635 0.0030  -0.1107 0.0229  812  ILE   B CA  
2931 C C   . ILE   B 119 ? 0.5793 0.7997 0.9370 0.0228  -0.1031 0.0241  812  ILE   B C   
2932 O O   . ILE   B 119 ? 0.5701 0.7983 0.9473 0.0313  -0.0829 0.0212  812  ILE   B O   
2933 C CB  . ILE   B 119 ? 0.6191 0.8335 0.9496 -0.0093 -0.0917 0.0168  812  ILE   B CB  
2934 C CG1 . ILE   B 119 ? 0.6232 0.8424 0.9506 -0.0288 -0.0999 0.0159  812  ILE   B CG1 
2935 C CG2 . ILE   B 119 ? 0.6510 0.8282 0.9322 -0.0059 -0.0888 0.0151  812  ILE   B CG2 
2936 C CD1 . ILE   B 119 ? 0.6448 0.8500 0.9510 -0.0398 -0.0813 0.0112  812  ILE   B CD1 
2937 N N   . GLY   B 120 ? 0.5710 0.7688 0.9016 0.0295  -0.1182 0.0283  813  GLY   B N   
2938 C CA  . GLY   B 120 ? 0.5605 0.7401 0.8830 0.0466  -0.1130 0.0301  813  GLY   B CA  
2939 C C   . GLY   B 120 ? 0.5596 0.7049 0.8390 0.0438  -0.0987 0.0254  813  GLY   B C   
2940 O O   . GLY   B 120 ? 0.5652 0.7018 0.8213 0.0302  -0.0938 0.0214  813  GLY   B O   
2941 N N   . SER   B 121 ? 0.5507 0.6756 0.8202 0.0568  -0.0929 0.0261  814  SER   B N   
2942 C CA  . SER   B 121 ? 0.5583 0.6516 0.7911 0.0537  -0.0811 0.0216  814  SER   B CA  
2943 C C   . SER   B 121 ? 0.5546 0.6283 0.7516 0.0428  -0.0906 0.0237  814  SER   B C   
2944 O O   . SER   B 121 ? 0.5672 0.6274 0.7418 0.0342  -0.0817 0.0190  814  SER   B O   
2945 C CB  . SER   B 121 ? 0.5836 0.6565 0.8135 0.0688  -0.0753 0.0225  814  SER   B CB  
2946 O OG  . SER   B 121 ? 0.6051 0.6726 0.8369 0.0785  -0.0920 0.0313  814  SER   B OG  
2947 N N   . GLN   B 122 ? 0.5417 0.6135 0.7331 0.0438  -0.1083 0.0309  815  GLN   B N   
2948 C CA  . GLN   B 122 ? 0.5534 0.6049 0.7095 0.0350  -0.1152 0.0334  815  GLN   B CA  
2949 C C   . GLN   B 122 ? 0.5447 0.6023 0.6911 0.0209  -0.1118 0.0284  815  GLN   B C   
2950 O O   . GLN   B 122 ? 0.5672 0.6081 0.6885 0.0147  -0.1051 0.0264  815  GLN   B O   
2951 C CB  . GLN   B 122 ? 0.5810 0.6273 0.7295 0.0393  -0.1356 0.0420  815  GLN   B CB  
2952 C CG  . GLN   B 122 ? 0.6575 0.6742 0.7633 0.0334  -0.1389 0.0457  815  GLN   B CG  
2953 C CD  . GLN   B 122 ? 0.7573 0.7472 0.8447 0.0376  -0.1280 0.0475  815  GLN   B CD  
2954 O OE1 . GLN   B 122 ? 0.8150 0.7888 0.8966 0.0477  -0.1342 0.0543  815  GLN   B OE1 
2955 N NE2 . GLN   B 122 ? 0.7551 0.7382 0.8324 0.0293  -0.1128 0.0419  815  GLN   B NE2 
2956 N N   . TYR   B 123 ? 0.5082 0.5894 0.6761 0.0158  -0.1157 0.0266  816  TYR   B N   
2957 C CA  . TYR   B 123 ? 0.4969 0.5793 0.6531 0.0027  -0.1123 0.0222  816  TYR   B CA  
2958 C C   . TYR   B 123 ? 0.4813 0.5608 0.6340 -0.0001 -0.0945 0.0159  816  TYR   B C   
2959 O O   . TYR   B 123 ? 0.4933 0.5595 0.6225 -0.0066 -0.0906 0.0135  816  TYR   B O   
2960 C CB  . TYR   B 123 ? 0.4855 0.5900 0.6631 -0.0046 -0.1221 0.0223  816  TYR   B CB  
2961 C CG  . TYR   B 123 ? 0.5179 0.6147 0.6794 -0.0081 -0.1426 0.0267  816  TYR   B CG  
2962 C CD1 . TYR   B 123 ? 0.5441 0.6386 0.7080 0.0015  -0.1573 0.0332  816  TYR   B CD1 
2963 C CD2 . TYR   B 123 ? 0.5465 0.6329 0.6847 -0.0204 -0.1475 0.0244  816  TYR   B CD2 
2964 C CE1 . TYR   B 123 ? 0.5747 0.6572 0.7166 -0.0019 -0.1776 0.0374  816  TYR   B CE1 
2965 C CE2 . TYR   B 123 ? 0.5746 0.6484 0.6912 -0.0241 -0.1663 0.0275  816  TYR   B CE2 
2966 C CZ  . TYR   B 123 ? 0.5985 0.6704 0.7159 -0.0153 -0.1819 0.0340  816  TYR   B CZ  
2967 O OH  . TYR   B 123 ? 0.6453 0.7000 0.7345 -0.0189 -0.2020 0.0373  816  TYR   B OH  
2968 N N   . LEU   B 124 ? 0.4562 0.5461 0.6304 0.0057  -0.0836 0.0133  817  LEU   B N   
2969 C CA  . LEU   B 124 ? 0.4577 0.5401 0.6224 0.0032  -0.0678 0.0072  817  LEU   B CA  
2970 C C   . LEU   B 124 ? 0.4672 0.5262 0.6043 0.0031  -0.0657 0.0057  817  LEU   B C   
2971 O O   . LEU   B 124 ? 0.4710 0.5225 0.5915 -0.0033 -0.0614 0.0023  817  LEU   B O   
2972 C CB  . LEU   B 124 ? 0.4483 0.5396 0.6349 0.0115  -0.0551 0.0045  817  LEU   B CB  
2973 C CG  . LEU   B 124 ? 0.4437 0.5619 0.6624 0.0094  -0.0514 0.0048  817  LEU   B CG  
2974 C CD1 . LEU   B 124 ? 0.4392 0.5663 0.6823 0.0211  -0.0372 0.0029  817  LEU   B CD1 
2975 C CD2 . LEU   B 124 ? 0.4582 0.5763 0.6658 -0.0037 -0.0442 0.0016  817  LEU   B CD2 
2976 N N   . LEU   B 125 ? 0.4632 0.5110 0.5966 0.0099  -0.0695 0.0089  818  LEU   B N   
2977 C CA  . LEU   B 125 ? 0.4701 0.4979 0.5823 0.0077  -0.0671 0.0079  818  LEU   B CA  
2978 C C   . LEU   B 125 ? 0.4706 0.4934 0.5659 0.0007  -0.0724 0.0104  818  LEU   B C   
2979 O O   . LEU   B 125 ? 0.4763 0.4920 0.5604 -0.0041 -0.0683 0.0078  818  LEU   B O   
2980 C CB  . LEU   B 125 ? 0.4693 0.4825 0.5811 0.0157  -0.0672 0.0106  818  LEU   B CB  
2981 C CG  . LEU   B 125 ? 0.4738 0.4841 0.5961 0.0237  -0.0580 0.0062  818  LEU   B CG  
2982 C CD1 . LEU   B 125 ? 0.4793 0.4746 0.6032 0.0342  -0.0600 0.0104  818  LEU   B CD1 
2983 C CD2 . LEU   B 125 ? 0.4878 0.4850 0.5950 0.0179  -0.0493 -0.0013 818  LEU   B CD2 
2984 N N   . ASN   B 126 ? 0.4665 0.4930 0.5601 0.0003  -0.0816 0.0151  819  ASN   B N   
2985 C CA  . ASN   B 126 ? 0.4820 0.5003 0.5557 -0.0052 -0.0846 0.0170  819  ASN   B CA  
2986 C C   . ASN   B 126 ? 0.4779 0.5012 0.5476 -0.0115 -0.0807 0.0123  819  ASN   B C   
2987 O O   . ASN   B 126 ? 0.4817 0.4972 0.5379 -0.0141 -0.0771 0.0117  819  ASN   B O   
2988 C CB  . ASN   B 126 ? 0.5065 0.5226 0.5732 -0.0045 -0.0969 0.0222  819  ASN   B CB  
2989 C CG  . ASN   B 126 ? 0.5757 0.5782 0.6348 0.0019  -0.1019 0.0286  819  ASN   B CG  
2990 O OD1 . ASN   B 126 ? 0.6073 0.5983 0.6625 0.0040  -0.0943 0.0294  819  ASN   B OD1 
2991 N ND2 . ASN   B 126 ? 0.5934 0.5949 0.6488 0.0044  -0.1161 0.0336  819  ASN   B ND2 
2992 N N   . TRP   B 127 ? 0.4661 0.5020 0.5488 -0.0134 -0.0803 0.0095  820  TRP   B N   
2993 C CA  . TRP   B 127 ? 0.4701 0.5061 0.5459 -0.0192 -0.0761 0.0059  820  TRP   B CA  
2994 C C   . TRP   B 127 ? 0.4775 0.5078 0.5477 -0.0182 -0.0685 0.0024  820  TRP   B C   
2995 O O   . TRP   B 127 ? 0.4913 0.5158 0.5493 -0.0204 -0.0675 0.0013  820  TRP   B O   
2996 C CB  . TRP   B 127 ? 0.4580 0.5068 0.5487 -0.0229 -0.0750 0.0043  820  TRP   B CB  
2997 C CG  . TRP   B 127 ? 0.4568 0.5136 0.5552 -0.0269 -0.0855 0.0071  820  TRP   B CG  
2998 C CD1 . TRP   B 127 ? 0.4771 0.5236 0.5579 -0.0300 -0.0953 0.0091  820  TRP   B CD1 
2999 C CD2 . TRP   B 127 ? 0.4392 0.5157 0.5645 -0.0294 -0.0875 0.0075  820  TRP   B CD2 
3000 N NE1 . TRP   B 127 ? 0.4694 0.5263 0.5623 -0.0351 -0.1064 0.0106  820  TRP   B NE1 
3001 C CE2 . TRP   B 127 ? 0.4497 0.5284 0.5742 -0.0350 -0.1021 0.0100  820  TRP   B CE2 
3002 C CE3 . TRP   B 127 ? 0.4317 0.5245 0.5826 -0.0273 -0.0778 0.0060  820  TRP   B CE3 
3003 C CZ2 . TRP   B 127 ? 0.4403 0.5408 0.5938 -0.0398 -0.1096 0.0112  820  TRP   B CZ2 
3004 C CZ3 . TRP   B 127 ? 0.4286 0.5443 0.6102 -0.0307 -0.0817 0.0075  820  TRP   B CZ3 
3005 C CH2 . TRP   B 127 ? 0.4260 0.5475 0.6114 -0.0374 -0.0987 0.0102  820  TRP   B CH2 
3006 N N   . CYS   B 128 ? 0.4737 0.5038 0.5515 -0.0146 -0.0644 0.0007  821  CYS   B N   
3007 C CA  . CYS   B 128 ? 0.4879 0.5102 0.5582 -0.0150 -0.0603 -0.0032 821  CYS   B CA  
3008 C C   . CYS   B 128 ? 0.4878 0.5055 0.5520 -0.0163 -0.0629 -0.0015 821  CYS   B C   
3009 O O   . CYS   B 128 ? 0.5018 0.5180 0.5607 -0.0182 -0.0631 -0.0037 821  CYS   B O   
3010 C CB  . CYS   B 128 ? 0.5108 0.5283 0.5864 -0.0112 -0.0560 -0.0058 821  CYS   B CB  
3011 S SG  . CYS   B 128 ? 0.5869 0.6103 0.6712 -0.0084 -0.0472 -0.0089 821  CYS   B SG  
3012 N N   . VAL   B 129 ? 0.4733 0.4884 0.5386 -0.0151 -0.0645 0.0028  822  VAL   B N   
3013 C CA  . VAL   B 129 ? 0.4686 0.4797 0.5297 -0.0169 -0.0633 0.0052  822  VAL   B CA  
3014 C C   . VAL   B 129 ? 0.4640 0.4773 0.5176 -0.0176 -0.0629 0.0055  822  VAL   B C   
3015 O O   . VAL   B 129 ? 0.4739 0.4897 0.5297 -0.0181 -0.0604 0.0047  822  VAL   B O   
3016 C CB  . VAL   B 129 ? 0.4752 0.4778 0.5322 -0.0155 -0.0636 0.0108  822  VAL   B CB  
3017 C CG1 . VAL   B 129 ? 0.4838 0.4816 0.5348 -0.0182 -0.0583 0.0138  822  VAL   B CG1 
3018 C CG2 . VAL   B 129 ? 0.4753 0.4711 0.5380 -0.0133 -0.0633 0.0109  822  VAL   B CG2 
3019 N N   . GLN   B 130 ? 0.4436 0.4557 0.4896 -0.0173 -0.0659 0.0065  823  GLN   B N   
3020 C CA  . GLN   B 130 ? 0.4288 0.4366 0.4626 -0.0176 -0.0654 0.0064  823  GLN   B CA  
3021 C C   . GLN   B 130 ? 0.4221 0.4323 0.4565 -0.0173 -0.0642 0.0030  823  GLN   B C   
3022 O O   . GLN   B 130 ? 0.4283 0.4364 0.4589 -0.0146 -0.0615 0.0030  823  GLN   B O   
3023 C CB  . GLN   B 130 ? 0.4280 0.4313 0.4524 -0.0198 -0.0711 0.0075  823  GLN   B CB  
3024 C CG  . GLN   B 130 ? 0.4273 0.4237 0.4443 -0.0189 -0.0748 0.0118  823  GLN   B CG  
3025 C CD  . GLN   B 130 ? 0.4675 0.4583 0.4728 -0.0220 -0.0842 0.0127  823  GLN   B CD  
3026 O OE1 . GLN   B 130 ? 0.4922 0.4824 0.4937 -0.0262 -0.0864 0.0098  823  GLN   B OE1 
3027 N NE2 . GLN   B 130 ? 0.4724 0.4565 0.4699 -0.0209 -0.0913 0.0168  823  GLN   B NE2 
3028 N N   . ILE   B 131 ? 0.4149 0.4282 0.4533 -0.0189 -0.0655 0.0005  824  ILE   B N   
3029 C CA  . ILE   B 131 ? 0.4263 0.4370 0.4592 -0.0184 -0.0653 -0.0019 824  ILE   B CA  
3030 C C   . ILE   B 131 ? 0.4405 0.4548 0.4798 -0.0159 -0.0666 -0.0028 824  ILE   B C   
3031 O O   . ILE   B 131 ? 0.4502 0.4632 0.4861 -0.0127 -0.0684 -0.0028 824  ILE   B O   
3032 C CB  . ILE   B 131 ? 0.4219 0.4318 0.4536 -0.0212 -0.0637 -0.0042 824  ILE   B CB  
3033 C CG1 . ILE   B 131 ? 0.4244 0.4357 0.4571 -0.0255 -0.0632 -0.0030 824  ILE   B CG1 
3034 C CG2 . ILE   B 131 ? 0.4241 0.4252 0.4425 -0.0207 -0.0641 -0.0059 824  ILE   B CG2 
3035 C CD1 . ILE   B 131 ? 0.4275 0.4440 0.4680 -0.0281 -0.0586 -0.0044 824  ILE   B CD1 
3036 N N   . ALA   B 132 ? 0.4333 0.4519 0.4833 -0.0174 -0.0665 -0.0032 825  ALA   B N   
3037 C CA  . ALA   B 132 ? 0.4324 0.4561 0.4922 -0.0179 -0.0691 -0.0043 825  ALA   B CA  
3038 C C   . ALA   B 132 ? 0.4379 0.4687 0.5067 -0.0157 -0.0659 -0.0011 825  ALA   B C   
3039 O O   . ALA   B 132 ? 0.4428 0.4821 0.5226 -0.0144 -0.0689 -0.0015 825  ALA   B O   
3040 C CB  . ALA   B 132 ? 0.4293 0.4512 0.4958 -0.0218 -0.0690 -0.0058 825  ALA   B CB  
3041 N N   . LYS   B 133 ? 0.4397 0.4667 0.5033 -0.0148 -0.0600 0.0020  826  LYS   B N   
3042 C CA  . LYS   B 133 ? 0.4399 0.4694 0.5067 -0.0118 -0.0530 0.0048  826  LYS   B CA  
3043 C C   . LYS   B 133 ? 0.4558 0.4843 0.5174 -0.0053 -0.0531 0.0041  826  LYS   B C   
3044 O O   . LYS   B 133 ? 0.4650 0.5024 0.5396 -0.0006 -0.0490 0.0051  826  LYS   B O   
3045 C CB  . LYS   B 133 ? 0.4588 0.4772 0.5116 -0.0125 -0.0474 0.0081  826  LYS   B CB  
3046 C CG  . LYS   B 133 ? 0.5037 0.5215 0.5631 -0.0169 -0.0440 0.0108  826  LYS   B CG  
3047 C CD  . LYS   B 133 ? 0.5618 0.5646 0.6018 -0.0168 -0.0418 0.0147  826  LYS   B CD  
3048 C CE  . LYS   B 133 ? 0.6157 0.6133 0.6589 -0.0207 -0.0373 0.0185  826  LYS   B CE  
3049 N NZ  . LYS   B 133 ? 0.6746 0.6539 0.6940 -0.0199 -0.0327 0.0238  826  LYS   B NZ  
3050 N N   . GLY   B 134 ? 0.4584 0.4761 0.5028 -0.0048 -0.0569 0.0028  827  GLY   B N   
3051 C CA  . GLY   B 134 ? 0.4696 0.4798 0.5038 0.0013  -0.0573 0.0023  827  GLY   B CA  
3052 C C   . GLY   B 134 ? 0.4699 0.4880 0.5145 0.0048  -0.0642 0.0014  827  GLY   B C   
3053 O O   . GLY   B 134 ? 0.4769 0.4978 0.5272 0.0130  -0.0640 0.0025  827  GLY   B O   
3054 N N   . MET   B 135 ? 0.4647 0.4854 0.5111 -0.0004 -0.0708 -0.0005 828  MET   B N   
3055 C CA  . MET   B 135 ? 0.4647 0.4889 0.5150 0.0019  -0.0803 -0.0016 828  MET   B CA  
3056 C C   . MET   B 135 ? 0.4517 0.4952 0.5292 0.0038  -0.0833 -0.0009 828  MET   B C   
3057 O O   . MET   B 135 ? 0.4476 0.4974 0.5334 0.0104  -0.0909 0.0000  828  MET   B O   
3058 C CB  . MET   B 135 ? 0.4780 0.4954 0.5179 -0.0047 -0.0848 -0.0046 828  MET   B CB  
3059 C CG  . MET   B 135 ? 0.5235 0.5243 0.5399 -0.0063 -0.0816 -0.0050 828  MET   B CG  
3060 S SD  . MET   B 135 ? 0.5942 0.5788 0.5901 0.0007  -0.0853 -0.0026 828  MET   B SD  
3061 C CE  . MET   B 135 ? 0.4916 0.4762 0.4852 0.0037  -0.0991 -0.0035 828  MET   B CE  
3062 N N   . ASN   B 136 ? 0.4416 0.4948 0.5348 -0.0018 -0.0773 -0.0006 829  ASN   B N   
3063 C CA  . ASN   B 136 ? 0.4283 0.5018 0.5518 -0.0028 -0.0772 0.0005  829  ASN   B CA  
3064 C C   . ASN   B 136 ? 0.4302 0.5135 0.5671 0.0071  -0.0693 0.0036  829  ASN   B C   
3065 O O   . ASN   B 136 ? 0.4119 0.5161 0.5785 0.0099  -0.0721 0.0046  829  ASN   B O   
3066 C CB  . ASN   B 136 ? 0.4284 0.5032 0.5591 -0.0118 -0.0695 0.0010  829  ASN   B CB  
3067 C CG  . ASN   B 136 ? 0.4421 0.5370 0.6052 -0.0164 -0.0671 0.0023  829  ASN   B CG  
3068 O OD1 . ASN   B 136 ? 0.4492 0.5565 0.6306 -0.0205 -0.0787 0.0002  829  ASN   B OD1 
3069 N ND2 . ASN   B 136 ? 0.4416 0.5389 0.6110 -0.0165 -0.0521 0.0059  829  ASN   B ND2 
3070 N N   . TYR   B 137 ? 0.4442 0.5121 0.5602 0.0124  -0.0594 0.0048  830  TYR   B N   
3071 C CA  . TYR   B 137 ? 0.4417 0.5114 0.5628 0.0233  -0.0494 0.0068  830  TYR   B CA  
3072 C C   . TYR   B 137 ? 0.4471 0.5167 0.5690 0.0343  -0.0592 0.0070  830  TYR   B C   
3073 O O   . TYR   B 137 ? 0.4425 0.5281 0.5891 0.0443  -0.0569 0.0088  830  TYR   B O   
3074 C CB  . TYR   B 137 ? 0.4593 0.5058 0.5501 0.0242  -0.0380 0.0070  830  TYR   B CB  
3075 C CG  . TYR   B 137 ? 0.4661 0.5063 0.5535 0.0370  -0.0272 0.0079  830  TYR   B CG  
3076 C CD1 . TYR   B 137 ? 0.4624 0.5196 0.5757 0.0427  -0.0139 0.0098  830  TYR   B CD1 
3077 C CD2 . TYR   B 137 ? 0.4841 0.5015 0.5446 0.0438  -0.0294 0.0066  830  TYR   B CD2 
3078 C CE1 . TYR   B 137 ? 0.4743 0.5254 0.5856 0.0568  -0.0017 0.0102  830  TYR   B CE1 
3079 C CE2 . TYR   B 137 ? 0.4980 0.5056 0.5533 0.0572  -0.0191 0.0069  830  TYR   B CE2 
3080 C CZ  . TYR   B 137 ? 0.4953 0.5197 0.5758 0.0647  -0.0046 0.0085  830  TYR   B CZ  
3081 O OH  . TYR   B 137 ? 0.5053 0.5198 0.5819 0.0802  0.0080  0.0085  830  TYR   B OH  
3082 N N   . LEU   B 138 ? 0.4617 0.5132 0.5577 0.0330  -0.0694 0.0056  831  LEU   B N   
3083 C CA  . LEU   B 138 ? 0.4703 0.5154 0.5599 0.0430  -0.0802 0.0067  831  LEU   B CA  
3084 C C   . LEU   B 138 ? 0.4662 0.5354 0.5860 0.0449  -0.0942 0.0073  831  LEU   B C   
3085 O O   . LEU   B 138 ? 0.4617 0.5382 0.5947 0.0576  -0.1005 0.0098  831  LEU   B O   
3086 C CB  . LEU   B 138 ? 0.4901 0.5091 0.5438 0.0381  -0.0862 0.0055  831  LEU   B CB  
3087 C CG  . LEU   B 138 ? 0.5146 0.5098 0.5404 0.0362  -0.0758 0.0051  831  LEU   B CG  
3088 C CD1 . LEU   B 138 ? 0.5286 0.5038 0.5266 0.0277  -0.0798 0.0041  831  LEU   B CD1 
3089 C CD2 . LEU   B 138 ? 0.5153 0.4980 0.5341 0.0495  -0.0698 0.0068  831  LEU   B CD2 
3090 N N   . GLU   B 139 ? 0.4663 0.5480 0.5987 0.0326  -0.0999 0.0051  832  GLU   B N   
3091 C CA  . GLU   B 139 ? 0.4639 0.5681 0.6253 0.0310  -0.1152 0.0048  832  GLU   B CA  
3092 C C   . GLU   B 139 ? 0.4586 0.5945 0.6662 0.0369  -0.1085 0.0075  832  GLU   B C   
3093 O O   . GLU   B 139 ? 0.4508 0.6077 0.6869 0.0435  -0.1217 0.0091  832  GLU   B O   
3094 C CB  . GLU   B 139 ? 0.4924 0.5961 0.6515 0.0151  -0.1205 0.0009  832  GLU   B CB  
3095 C CG  . GLU   B 139 ? 0.5332 0.6592 0.7226 0.0096  -0.1370 -0.0004 832  GLU   B CG  
3096 C CD  . GLU   B 139 ? 0.6427 0.7589 0.8201 -0.0053 -0.1454 -0.0054 832  GLU   B CD  
3097 O OE1 . GLU   B 139 ? 0.6856 0.7791 0.8328 -0.0100 -0.1367 -0.0076 832  GLU   B OE1 
3098 O OE2 . GLU   B 139 ? 0.6530 0.7840 0.8519 -0.0121 -0.1611 -0.0074 832  GLU   B OE2 
3099 N N   . ASP   B 140 ? 0.4655 0.6045 0.6800 0.0353  -0.0877 0.0084  833  ASP   B N   
3100 C CA  . ASP   B 140 ? 0.4578 0.6234 0.7122 0.0411  -0.0743 0.0112  833  ASP   B CA  
3101 C C   . ASP   B 140 ? 0.4690 0.6357 0.7288 0.0615  -0.0722 0.0138  833  ASP   B C   
3102 O O   . ASP   B 140 ? 0.4521 0.6488 0.7555 0.0702  -0.0709 0.0162  833  ASP   B O   
3103 C CB  . ASP   B 140 ? 0.4869 0.6433 0.7311 0.0350  -0.0511 0.0117  833  ASP   B CB  
3104 C CG  . ASP   B 140 ? 0.5383 0.7158 0.8157 0.0411  -0.0312 0.0146  833  ASP   B CG  
3105 O OD1 . ASP   B 140 ? 0.5229 0.7326 0.8457 0.0354  -0.0322 0.0159  833  ASP   B OD1 
3106 O OD2 . ASP   B 140 ? 0.5866 0.7475 0.8442 0.0509  -0.0138 0.0154  833  ASP   B OD2 
3107 N N   . ARG   B 141 ? 0.4919 0.6259 0.7093 0.0691  -0.0716 0.0134  834  ARG   B N   
3108 C CA  . ARG   B 141 ? 0.5026 0.6282 0.7162 0.0888  -0.0706 0.0156  834  ARG   B CA  
3109 C C   . ARG   B 141 ? 0.5150 0.6433 0.7322 0.0968  -0.0953 0.0175  834  ARG   B C   
3110 O O   . ARG   B 141 ? 0.5305 0.6462 0.7392 0.1142  -0.0970 0.0201  834  ARG   B O   
3111 C CB  . ARG   B 141 ? 0.5459 0.6297 0.7084 0.0914  -0.0607 0.0143  834  ARG   B CB  
3112 C CG  . ARG   B 141 ? 0.5818 0.6530 0.7287 0.0867  -0.0382 0.0126  834  ARG   B CG  
3113 C CD  . ARG   B 141 ? 0.5994 0.6979 0.7826 0.0862  -0.0218 0.0137  834  ARG   B CD  
3114 N NE  . ARG   B 141 ? 0.6199 0.7277 0.8247 0.1049  -0.0079 0.0155  834  ARG   B NE  
3115 C CZ  . ARG   B 141 ? 0.6145 0.7520 0.8605 0.1076  0.0078  0.0173  834  ARG   B CZ  
3116 N NH1 . ARG   B 141 ? 0.6062 0.7516 0.8725 0.1268  0.0227  0.0188  834  ARG   B NH1 
3117 N NH2 . ARG   B 141 ? 0.5807 0.7395 0.8490 0.0912  0.0101  0.0178  834  ARG   B NH2 
3118 N N   . ARG   B 142 ? 0.5122 0.6521 0.7370 0.0847  -0.1147 0.0163  835  ARG   B N   
3119 C CA  . ARG   B 142 ? 0.5167 0.6556 0.7382 0.0894  -0.1412 0.0177  835  ARG   B CA  
3120 C C   . ARG   B 142 ? 0.5494 0.6448 0.7152 0.0944  -0.1456 0.0185  835  ARG   B C   
3121 O O   . ARG   B 142 ? 0.5585 0.6443 0.7161 0.1083  -0.1600 0.0222  835  ARG   B O   
3122 C CB  . ARG   B 142 ? 0.5048 0.6759 0.7741 0.1064  -0.1509 0.0219  835  ARG   B CB  
3123 C CG  . ARG   B 142 ? 0.5058 0.7232 0.8362 0.1004  -0.1437 0.0217  835  ARG   B CG  
3124 N N   . LEU   B 143 ? 0.5662 0.6353 0.6952 0.0831  -0.1334 0.0157  836  LEU   B N   
3125 C CA  . LEU   B 143 ? 0.5995 0.6282 0.6783 0.0845  -0.1341 0.0164  836  LEU   B CA  
3126 C C   . LEU   B 143 ? 0.6068 0.6199 0.6565 0.0683  -0.1400 0.0134  836  LEU   B C   
3127 O O   . LEU   B 143 ? 0.6142 0.6322 0.6657 0.0550  -0.1301 0.0098  836  LEU   B O   
3128 C CB  . LEU   B 143 ? 0.6199 0.6290 0.6804 0.0864  -0.1131 0.0158  836  LEU   B CB  
3129 C CG  . LEU   B 143 ? 0.6768 0.6447 0.6924 0.0911  -0.1119 0.0176  836  LEU   B CG  
3130 C CD1 . LEU   B 143 ? 0.6894 0.6434 0.6994 0.1013  -0.0959 0.0177  836  LEU   B CD1 
3131 C CD2 . LEU   B 143 ? 0.7100 0.6567 0.6923 0.0735  -0.1085 0.0149  836  LEU   B CD2 
3132 N N   . VAL   B 144 ? 0.6047 0.5966 0.6255 0.0704  -0.1550 0.0151  837  VAL   B N   
3133 C CA  . VAL   B 144 ? 0.6082 0.5807 0.5965 0.0567  -0.1577 0.0122  837  VAL   B CA  
3134 C C   . VAL   B 144 ? 0.6221 0.5623 0.5729 0.0536  -0.1432 0.0130  837  VAL   B C   
3135 O O   . VAL   B 144 ? 0.6332 0.5511 0.5636 0.0636  -0.1440 0.0172  837  VAL   B O   
3136 C CB  . VAL   B 144 ? 0.6121 0.5739 0.5822 0.0593  -0.1810 0.0135  837  VAL   B CB  
3137 C CG1 . VAL   B 144 ? 0.6437 0.5780 0.5718 0.0464  -0.1794 0.0103  837  VAL   B CG1 
3138 C CG2 . VAL   B 144 ? 0.5753 0.5720 0.5872 0.0598  -0.1977 0.0122  837  VAL   B CG2 
3139 N N   . HIS   B 145 ? 0.6173 0.5554 0.5615 0.0399  -0.1302 0.0092  838  HIS   B N   
3140 C CA  . HIS   B 145 ? 0.6345 0.5476 0.5506 0.0341  -0.1168 0.0097  838  HIS   B CA  
3141 C C   . HIS   B 145 ? 0.6769 0.5561 0.5505 0.0323  -0.1202 0.0121  838  HIS   B C   
3142 O O   . HIS   B 145 ? 0.6987 0.5518 0.5481 0.0355  -0.1159 0.0157  838  HIS   B O   
3143 C CB  . HIS   B 145 ? 0.6151 0.5400 0.5419 0.0209  -0.1044 0.0056  838  HIS   B CB  
3144 C CG  . HIS   B 145 ? 0.6129 0.5215 0.5235 0.0140  -0.0918 0.0058  838  HIS   B CG  
3145 N ND1 . HIS   B 145 ? 0.6505 0.5320 0.5294 0.0090  -0.0884 0.0075  838  HIS   B ND1 
3146 C CD2 . HIS   B 145 ? 0.6129 0.5289 0.5351 0.0097  -0.0829 0.0045  838  HIS   B CD2 
3147 C CE1 . HIS   B 145 ? 0.6567 0.5329 0.5336 0.0011  -0.0780 0.0069  838  HIS   B CE1 
3148 N NE2 . HIS   B 145 ? 0.6379 0.5340 0.5393 0.0015  -0.0759 0.0050  838  HIS   B NE2 
3149 N N   . ARG   B 146 ? 0.6906 0.5664 0.5514 0.0266  -0.1266 0.0101  839  ARG   B N   
3150 C CA  . ARG   B 146 ? 0.7332 0.5750 0.5490 0.0238  -0.1286 0.0120  839  ARG   B CA  
3151 C C   . ARG   B 146 ? 0.7610 0.5862 0.5565 0.0108  -0.1088 0.0108  839  ARG   B C   
3152 O O   . ARG   B 146 ? 0.7976 0.5964 0.5567 0.0062  -0.1059 0.0114  839  ARG   B O   
3153 C CB  . ARG   B 146 ? 0.7718 0.5869 0.5609 0.0361  -0.1396 0.0187  839  ARG   B CB  
3154 C CG  . ARG   B 146 ? 0.8118 0.6405 0.6167 0.0497  -0.1628 0.0207  839  ARG   B CG  
3155 C CD  . ARG   B 146 ? 0.8881 0.6867 0.6644 0.0637  -0.1726 0.0283  839  ARG   B CD  
3156 N NE  . ARG   B 146 ? 0.9556 0.7624 0.7401 0.0771  -0.1988 0.0313  839  ARG   B NE  
3157 C CZ  . ARG   B 146 ? 1.0422 0.8163 0.7844 0.0833  -0.2157 0.0364  839  ARG   B CZ  
3158 N NH1 . ARG   B 146 ? 1.0375 0.8239 0.7930 0.0956  -0.2428 0.0391  839  ARG   B NH1 
3159 N NH2 . ARG   B 146 ? 1.0852 0.8141 0.7717 0.0765  -0.2060 0.0390  839  ARG   B NH2 
3160 N N   . ASP   B 147 ? 0.7436 0.5838 0.5617 0.0047  -0.0955 0.0092  840  ASP   B N   
3161 C CA  . ASP   B 147 ? 0.7548 0.5858 0.5627 -0.0080 -0.0782 0.0083  840  ASP   B CA  
3162 C C   . ASP   B 147 ? 0.7136 0.5743 0.5575 -0.0150 -0.0694 0.0043  840  ASP   B C   
3163 O O   . ASP   B 147 ? 0.7198 0.5799 0.5683 -0.0223 -0.0599 0.0049  840  ASP   B O   
3164 C CB  . ASP   B 147 ? 0.8237 0.6249 0.6049 -0.0101 -0.0720 0.0131  840  ASP   B CB  
3165 C CG  . ASP   B 147 ? 0.9403 0.7278 0.7069 -0.0249 -0.0542 0.0134  840  ASP   B CG  
3166 O OD1 . ASP   B 147 ? 0.9488 0.7431 0.7163 -0.0309 -0.0463 0.0105  840  ASP   B OD1 
3167 O OD2 . ASP   B 147 ? 1.0007 0.7711 0.7568 -0.0311 -0.0472 0.0161  840  ASP   B OD2 
3168 N N   . LEU   B 148 ? 0.6725 0.5569 0.5404 -0.0132 -0.0739 0.0006  841  LEU   B N   
3169 C CA  . LEU   B 148 ? 0.6437 0.5525 0.5419 -0.0185 -0.0668 -0.0022 841  LEU   B CA  
3170 C C   . LEU   B 148 ? 0.6390 0.5452 0.5330 -0.0274 -0.0533 -0.0041 841  LEU   B C   
3171 O O   . LEU   B 148 ? 0.6537 0.5485 0.5301 -0.0279 -0.0509 -0.0060 841  LEU   B O   
3172 C CB  . LEU   B 148 ? 0.6301 0.5605 0.5526 -0.0144 -0.0743 -0.0049 841  LEU   B CB  
3173 C CG  . LEU   B 148 ? 0.6380 0.5887 0.5869 -0.0187 -0.0678 -0.0068 841  LEU   B CG  
3174 C CD1 . LEU   B 148 ? 0.6382 0.5946 0.5973 -0.0197 -0.0653 -0.0045 841  LEU   B CD1 
3175 C CD2 . LEU   B 148 ? 0.6313 0.5966 0.5984 -0.0162 -0.0739 -0.0090 841  LEU   B CD2 
3176 N N   . ALA   B 149 ? 0.6138 0.5290 0.5225 -0.0345 -0.0445 -0.0035 842  ALA   B N   
3177 C CA  . ALA   B 149 ? 0.5978 0.5181 0.5137 -0.0426 -0.0304 -0.0048 842  ALA   B CA  
3178 C C   . ALA   B 149 ? 0.5814 0.5242 0.5287 -0.0477 -0.0293 -0.0045 842  ALA   B C   
3179 O O   . ALA   B 149 ? 0.5762 0.5201 0.5266 -0.0467 -0.0376 -0.0032 842  ALA   B O   
3180 C CB  . ALA   B 149 ? 0.6074 0.5028 0.4949 -0.0493 -0.0203 -0.0022 842  ALA   B CB  
3181 N N   . ALA   B 150 ? 0.5727 0.5325 0.5424 -0.0523 -0.0198 -0.0057 843  ALA   B N   
3182 C CA  . ALA   B 150 ? 0.5625 0.5445 0.5627 -0.0570 -0.0224 -0.0050 843  ALA   B CA  
3183 C C   . ALA   B 150 ? 0.5735 0.5467 0.5673 -0.0675 -0.0235 -0.0027 843  ALA   B C   
3184 O O   . ALA   B 150 ? 0.5715 0.5541 0.5785 -0.0706 -0.0323 -0.0023 843  ALA   B O   
3185 C CB  . ALA   B 150 ? 0.5461 0.5500 0.5754 -0.0582 -0.0125 -0.0062 843  ALA   B CB  
3186 N N   . ARG   B 151 ? 0.5865 0.5366 0.5546 -0.0730 -0.0156 -0.0012 844  ARG   B N   
3187 C CA  . ARG   B 151 ? 0.6006 0.5347 0.5565 -0.0836 -0.0162 0.0009  844  ARG   B CA  
3188 C C   . ARG   B 151 ? 0.6147 0.5313 0.5506 -0.0765 -0.0294 0.0012  844  ARG   B C   
3189 O O   . ARG   B 151 ? 0.6355 0.5400 0.5640 -0.0839 -0.0330 0.0017  844  ARG   B O   
3190 C CB  . ARG   B 151 ? 0.6316 0.5402 0.5609 -0.0911 -0.0026 0.0033  844  ARG   B CB  
3191 C CG  . ARG   B 151 ? 0.6932 0.5735 0.5841 -0.0801 -0.0053 0.0046  844  ARG   B CG  
3192 C CD  . ARG   B 151 ? 0.7700 0.6167 0.6247 -0.0867 0.0066  0.0082  844  ARG   B CD  
3193 N NE  . ARG   B 151 ? 0.8596 0.6825 0.6795 -0.0743 0.0006  0.0094  844  ARG   B NE  
3194 C CZ  . ARG   B 151 ? 0.9376 0.7605 0.7487 -0.0691 0.0047  0.0075  844  ARG   B CZ  
3195 N NH1 . ARG   B 151 ? 0.9672 0.7687 0.7468 -0.0585 -0.0055 0.0084  844  ARG   B NH1 
3196 N NH2 . ARG   B 151 ? 0.9372 0.7810 0.7712 -0.0739 0.0183  0.0045  844  ARG   B NH2 
3197 N N   . ASN   B 152 ? 0.6040 0.5191 0.5323 -0.0627 -0.0358 0.0007  845  ASN   B N   
3198 C CA  . ASN   B 152 ? 0.6069 0.5105 0.5226 -0.0535 -0.0453 0.0011  845  ASN   B CA  
3199 C C   . ASN   B 152 ? 0.5869 0.5111 0.5238 -0.0483 -0.0522 -0.0006 845  ASN   B C   
3200 O O   . ASN   B 152 ? 0.5975 0.5179 0.5292 -0.0383 -0.0572 -0.0005 845  ASN   B O   
3201 C CB  . ASN   B 152 ? 0.6400 0.5283 0.5351 -0.0421 -0.0483 0.0026  845  ASN   B CB  
3202 C CG  . ASN   B 152 ? 0.7080 0.5642 0.5704 -0.0452 -0.0440 0.0057  845  ASN   B CG  
3203 O OD1 . ASN   B 152 ? 0.7401 0.5823 0.5937 -0.0564 -0.0381 0.0067  845  ASN   B OD1 
3204 N ND2 . ASN   B 152 ? 0.7213 0.5621 0.5628 -0.0361 -0.0481 0.0077  845  ASN   B ND2 
3205 N N   . VAL   B 153 ? 0.5532 0.4990 0.5143 -0.0542 -0.0519 -0.0016 846  VAL   B N   
3206 C CA  . VAL   B 153 ? 0.5347 0.4953 0.5109 -0.0506 -0.0586 -0.0022 846  VAL   B CA  
3207 C C   . VAL   B 153 ? 0.5362 0.4971 0.5163 -0.0617 -0.0625 -0.0024 846  VAL   B C   
3208 O O   . VAL   B 153 ? 0.5273 0.4987 0.5223 -0.0714 -0.0594 -0.0022 846  VAL   B O   
3209 C CB  . VAL   B 153 ? 0.5116 0.4945 0.5111 -0.0467 -0.0577 -0.0027 846  VAL   B CB  
3210 C CG1 . VAL   B 153 ? 0.4915 0.4844 0.5016 -0.0436 -0.0647 -0.0020 846  VAL   B CG1 
3211 C CG2 . VAL   B 153 ? 0.5177 0.4977 0.5112 -0.0388 -0.0553 -0.0035 846  VAL   B CG2 
3212 N N   . LEU   B 154 ? 0.5441 0.4921 0.5097 -0.0610 -0.0687 -0.0030 847  LEU   B N   
3213 C CA  . LEU   B 154 ? 0.5506 0.4934 0.5134 -0.0726 -0.0757 -0.0039 847  LEU   B CA  
3214 C C   . LEU   B 154 ? 0.5433 0.5010 0.5187 -0.0711 -0.0851 -0.0036 847  LEU   B C   
3215 O O   . LEU   B 154 ? 0.5368 0.4988 0.5127 -0.0604 -0.0848 -0.0026 847  LEU   B O   
3216 C CB  . LEU   B 154 ? 0.5793 0.4885 0.5083 -0.0734 -0.0764 -0.0055 847  LEU   B CB  
3217 C CG  . LEU   B 154 ? 0.6263 0.5145 0.5368 -0.0713 -0.0683 -0.0047 847  LEU   B CG  
3218 C CD1 . LEU   B 154 ? 0.6763 0.5295 0.5536 -0.0690 -0.0688 -0.0062 847  LEU   B CD1 
3219 C CD2 . LEU   B 154 ? 0.6280 0.5186 0.5464 -0.0851 -0.0634 -0.0037 847  LEU   B CD2 
3220 N N   . VAL   B 155 ? 0.5384 0.5030 0.5237 -0.0826 -0.0943 -0.0038 848  VAL   B N   
3221 C CA  . VAL   B 155 ? 0.5335 0.5104 0.5290 -0.0819 -0.1066 -0.0027 848  VAL   B CA  
3222 C C   . VAL   B 155 ? 0.5745 0.5252 0.5385 -0.0876 -0.1173 -0.0047 848  VAL   B C   
3223 O O   . VAL   B 155 ? 0.5785 0.5206 0.5375 -0.1016 -0.1243 -0.0068 848  VAL   B O   
3224 C CB  . VAL   B 155 ? 0.5048 0.5127 0.5396 -0.0898 -0.1118 -0.0012 848  VAL   B CB  
3225 C CG1 . VAL   B 155 ? 0.4993 0.5201 0.5457 -0.0875 -0.1276 0.0011  848  VAL   B CG1 
3226 C CG2 . VAL   B 155 ? 0.4903 0.5179 0.5499 -0.0836 -0.0978 -0.0001 848  VAL   B CG2 
3227 N N   . LYS   B 156 ? 0.6057 0.5408 0.5459 -0.0775 -0.1172 -0.0044 849  LYS   B N   
3228 C CA  . LYS   B 156 ? 0.6433 0.5489 0.5469 -0.0812 -0.1259 -0.0068 849  LYS   B CA  
3229 C C   . LYS   B 156 ? 0.6467 0.5655 0.5618 -0.0883 -0.1449 -0.0050 849  LYS   B C   
3230 O O   . LYS   B 156 ? 0.6647 0.5735 0.5701 -0.1017 -0.1589 -0.0075 849  LYS   B O   
3231 C CB  . LYS   B 156 ? 0.6862 0.5728 0.5630 -0.0674 -0.1162 -0.0064 849  LYS   B CB  
3232 C CG  . LYS   B 156 ? 0.7613 0.6099 0.5920 -0.0699 -0.1205 -0.0098 849  LYS   B CG  
3233 C CD  . LYS   B 156 ? 0.8296 0.6602 0.6369 -0.0557 -0.1051 -0.0096 849  LYS   B CD  
3234 C CE  . LYS   B 156 ? 0.9049 0.6932 0.6615 -0.0571 -0.1062 -0.0136 849  LYS   B CE  
3235 N N   . THR   B 157 ? 0.6256 0.5668 0.5629 -0.0796 -0.1466 -0.0005 850  THR   B N   
3236 C CA  . THR   B 157 ? 0.6195 0.5786 0.5755 -0.0819 -0.1647 0.0029  850  THR   B CA  
3237 C C   . THR   B 157 ? 0.5984 0.5914 0.5975 -0.0733 -0.1574 0.0066  850  THR   B C   
3238 O O   . THR   B 157 ? 0.5979 0.5921 0.5997 -0.0651 -0.1405 0.0064  850  THR   B O   
3239 C CB  . THR   B 157 ? 0.6497 0.5844 0.5690 -0.0768 -0.1749 0.0051  850  THR   B CB  
3240 O OG1 . THR   B 157 ? 0.6599 0.5894 0.5708 -0.0632 -0.1599 0.0080  850  THR   B OG1 
3241 C CG2 . THR   B 157 ? 0.6797 0.5754 0.5501 -0.0849 -0.1809 0.0004  850  THR   B CG2 
3242 N N   . PRO   B 158 ? 0.5717 0.5917 0.6050 -0.0743 -0.1703 0.0097  851  PRO   B N   
3243 C CA  . PRO   B 158 ? 0.5390 0.5866 0.6101 -0.0643 -0.1613 0.0126  851  PRO   B CA  
3244 C C   . PRO   B 158 ? 0.5422 0.5785 0.5988 -0.0505 -0.1510 0.0150  851  PRO   B C   
3245 O O   . PRO   B 158 ? 0.5359 0.5849 0.6125 -0.0437 -0.1380 0.0149  851  PRO   B O   
3246 C CB  . PRO   B 158 ? 0.5240 0.5968 0.6278 -0.0646 -0.1801 0.0165  851  PRO   B CB  
3247 C CG  . PRO   B 158 ? 0.5387 0.6066 0.6345 -0.0806 -0.1970 0.0141  851  PRO   B CG  
3248 C CD  . PRO   B 158 ? 0.5551 0.5820 0.5959 -0.0841 -0.1942 0.0107  851  PRO   B CD  
3249 N N   . GLN   B 159 ? 0.5497 0.5598 0.5695 -0.0475 -0.1555 0.0167  852  GLN   B N   
3250 C CA  . GLN   B 159 ? 0.5497 0.5490 0.5573 -0.0369 -0.1448 0.0194  852  GLN   B CA  
3251 C C   . GLN   B 159 ? 0.5580 0.5380 0.5399 -0.0365 -0.1285 0.0161  852  GLN   B C   
3252 O O   . GLN   B 159 ? 0.5684 0.5378 0.5379 -0.0301 -0.1195 0.0183  852  GLN   B O   
3253 C CB  . GLN   B 159 ? 0.5753 0.5606 0.5643 -0.0317 -0.1577 0.0254  852  GLN   B CB  
3254 C CG  . GLN   B 159 ? 0.6413 0.6051 0.5965 -0.0382 -0.1742 0.0257  852  GLN   B CG  
3255 C CD  . GLN   B 159 ? 0.6740 0.6555 0.6502 -0.0458 -0.1966 0.0257  852  GLN   B CD  
3256 O OE1 . GLN   B 159 ? 0.6934 0.6635 0.6516 -0.0569 -0.2063 0.0218  852  GLN   B OE1 
3257 N NE2 . GLN   B 159 ? 0.6436 0.6531 0.6597 -0.0402 -0.2055 0.0298  852  GLN   B NE2 
3258 N N   . HIS   B 160 ? 0.5459 0.5231 0.5237 -0.0429 -0.1239 0.0113  853  HIS   B N   
3259 C CA  . HIS   B 160 ? 0.5512 0.5118 0.5083 -0.0404 -0.1102 0.0086  853  HIS   B CA  
3260 C C   . HIS   B 160 ? 0.5338 0.4997 0.5005 -0.0446 -0.1039 0.0047  853  HIS   B C   
3261 O O   . HIS   B 160 ? 0.5355 0.4933 0.4936 -0.0532 -0.1093 0.0021  853  HIS   B O   
3262 C CB  . HIS   B 160 ? 0.5866 0.5171 0.5030 -0.0419 -0.1132 0.0079  853  HIS   B CB  
3263 C CG  . HIS   B 160 ? 0.6240 0.5361 0.5191 -0.0375 -0.0985 0.0050  853  HIS   B CG  
3264 N ND1 . HIS   B 160 ? 0.6360 0.5600 0.5493 -0.0320 -0.0860 0.0042  853  HIS   B ND1 
3265 C CD2 . HIS   B 160 ? 0.6568 0.5390 0.5142 -0.0368 -0.0951 0.0029  853  HIS   B CD2 
3266 C CE1 . HIS   B 160 ? 0.6502 0.5552 0.5417 -0.0273 -0.0760 0.0022  853  HIS   B CE1 
3267 N NE2 . HIS   B 160 ? 0.6729 0.5516 0.5300 -0.0295 -0.0792 0.0012  853  HIS   B NE2 
3268 N N   . VAL   B 161 ? 0.5118 0.4887 0.4942 -0.0392 -0.0933 0.0043  854  VAL   B N   
3269 C CA  . VAL   B 161 ? 0.5067 0.4847 0.4932 -0.0419 -0.0873 0.0017  854  VAL   B CA  
3270 C C   . VAL   B 161 ? 0.5230 0.4883 0.4948 -0.0350 -0.0783 0.0006  854  VAL   B C   
3271 O O   . VAL   B 161 ? 0.5257 0.4907 0.4961 -0.0279 -0.0740 0.0018  854  VAL   B O   
3272 C CB  . VAL   B 161 ? 0.4894 0.4883 0.5032 -0.0427 -0.0842 0.0017  854  VAL   B CB  
3273 C CG1 . VAL   B 161 ? 0.4739 0.4890 0.5085 -0.0480 -0.0924 0.0030  854  VAL   B CG1 
3274 C CG2 . VAL   B 161 ? 0.4827 0.4889 0.5060 -0.0343 -0.0783 0.0023  854  VAL   B CG2 
3275 N N   . LYS   B 162 ? 0.5318 0.4864 0.4939 -0.0370 -0.0755 -0.0013 855  LYS   B N   
3276 C CA  . LYS   B 162 ? 0.5526 0.4948 0.5022 -0.0288 -0.0690 -0.0018 855  LYS   B CA  
3277 C C   . LYS   B 162 ? 0.5614 0.5034 0.5134 -0.0286 -0.0667 -0.0021 855  LYS   B C   
3278 O O   . LYS   B 162 ? 0.5644 0.5024 0.5139 -0.0373 -0.0676 -0.0025 855  LYS   B O   
3279 C CB  . LYS   B 162 ? 0.6027 0.5180 0.5237 -0.0295 -0.0688 -0.0036 855  LYS   B CB  
3280 C CG  . LYS   B 162 ? 0.6655 0.5717 0.5727 -0.0264 -0.0681 -0.0036 855  LYS   B CG  
3281 C CD  . LYS   B 162 ? 0.7589 0.6344 0.6330 -0.0312 -0.0706 -0.0066 855  LYS   B CD  
3282 C CE  . LYS   B 162 ? 0.8381 0.6940 0.6876 -0.0236 -0.0637 -0.0074 855  LYS   B CE  
3283 N NZ  . LYS   B 162 ? 0.8762 0.7294 0.7275 -0.0095 -0.0504 -0.0072 855  LYS   B NZ  
3284 N N   . ILE   B 163 ? 0.5678 0.5119 0.5227 -0.0193 -0.0639 -0.0014 856  ILE   B N   
3285 C CA  . ILE   B 163 ? 0.5826 0.5213 0.5327 -0.0176 -0.0638 -0.0011 856  ILE   B CA  
3286 C C   . ILE   B 163 ? 0.6079 0.5208 0.5341 -0.0142 -0.0627 -0.0007 856  ILE   B C   
3287 O O   . ILE   B 163 ? 0.6142 0.5188 0.5340 -0.0056 -0.0608 -0.0007 856  ILE   B O   
3288 C CB  . ILE   B 163 ? 0.5833 0.5361 0.5478 -0.0095 -0.0653 -0.0005 856  ILE   B CB  
3289 C CG1 . ILE   B 163 ? 0.5809 0.5530 0.5647 -0.0135 -0.0657 -0.0013 856  ILE   B CG1 
3290 C CG2 . ILE   B 163 ? 0.5988 0.5417 0.5522 -0.0062 -0.0681 0.0003  856  ILE   B CG2 
3291 C CD1 . ILE   B 163 ? 0.5940 0.5781 0.5920 -0.0080 -0.0673 -0.0012 856  ILE   B CD1 
3292 N N   . THR   B 164 ? 0.6261 0.5237 0.5377 -0.0203 -0.0621 -0.0001 857  THR   B N   
3293 C CA  . THR   B 164 ? 0.6589 0.5258 0.5435 -0.0178 -0.0610 0.0009  857  THR   B CA  
3294 C C   . THR   B 164 ? 0.6801 0.5362 0.5533 -0.0121 -0.0623 0.0038  857  THR   B C   
3295 O O   . THR   B 164 ? 0.6725 0.5446 0.5572 -0.0120 -0.0640 0.0041  857  THR   B O   
3296 C CB  . THR   B 164 ? 0.6828 0.5334 0.5539 -0.0331 -0.0595 -0.0004 857  THR   B CB  
3297 O OG1 . THR   B 164 ? 0.7238 0.5392 0.5653 -0.0304 -0.0580 0.0000  857  THR   B OG1 
3298 C CG2 . THR   B 164 ? 0.6816 0.5382 0.5584 -0.0456 -0.0566 0.0006  857  THR   B CG2 
3299 N N   . ASP   B 165 ? 0.7114 0.5363 0.5580 -0.0067 -0.0621 0.0058  858  ASP   B N   
3300 C CA  . ASP   B 165 ? 0.7343 0.5395 0.5606 -0.0007 -0.0648 0.0098  858  ASP   B CA  
3301 C C   . ASP   B 165 ? 0.7273 0.5474 0.5663 0.0150  -0.0732 0.0116  858  ASP   B C   
3302 O O   . ASP   B 165 ? 0.7387 0.5476 0.5626 0.0182  -0.0785 0.0147  858  ASP   B O   
3303 C CB  . ASP   B 165 ? 0.7726 0.5719 0.5885 -0.0150 -0.0604 0.0109  858  ASP   B CB  
3304 C CG  . ASP   B 165 ? 0.8809 0.6564 0.6786 -0.0304 -0.0529 0.0110  858  ASP   B CG  
3305 O OD1 . ASP   B 165 ? 0.8910 0.6633 0.6912 -0.0347 -0.0524 0.0084  858  ASP   B OD1 
3306 O OD2 . ASP   B 165 ? 0.9452 0.7038 0.7248 -0.0393 -0.0471 0.0137  858  ASP   B OD2 
3307 N N   . PHE   B 166 ? 0.7126 0.5567 0.5779 0.0240  -0.0747 0.0099  859  PHE   B N   
3308 C CA  . PHE   B 166 ? 0.7127 0.5741 0.5959 0.0379  -0.0836 0.0117  859  PHE   B CA  
3309 C C   . PHE   B 166 ? 0.7392 0.5765 0.6057 0.0542  -0.0875 0.0157  859  PHE   B C   
3310 O O   . PHE   B 166 ? 0.7459 0.5608 0.5971 0.0579  -0.0805 0.0155  859  PHE   B O   
3311 C CB  . PHE   B 166 ? 0.6883 0.5828 0.6070 0.0411  -0.0813 0.0093  859  PHE   B CB  
3312 C CG  . PHE   B 166 ? 0.6932 0.5820 0.6115 0.0439  -0.0711 0.0077  859  PHE   B CG  
3313 C CD1 . PHE   B 166 ? 0.7023 0.5839 0.6220 0.0603  -0.0682 0.0091  859  PHE   B CD1 
3314 C CD2 . PHE   B 166 ? 0.6987 0.5885 0.6145 0.0314  -0.0647 0.0047  859  PHE   B CD2 
3315 C CE1 . PHE   B 166 ? 0.7185 0.5889 0.6308 0.0632  -0.0570 0.0068  859  PHE   B CE1 
3316 C CE2 . PHE   B 166 ? 0.7140 0.5928 0.6215 0.0334  -0.0567 0.0029  859  PHE   B CE2 
3317 C CZ  . PHE   B 166 ? 0.7208 0.5886 0.6247 0.0490  -0.0518 0.0035  859  PHE   B CZ  
3318 N N   . GLY   B 167 ? 0.7533 0.5920 0.6198 0.0639  -0.0999 0.0192  860  GLY   B N   
3319 C CA  . GLY   B 167 ? 0.7810 0.5975 0.6331 0.0819  -0.1067 0.0242  860  GLY   B CA  
3320 C C   . GLY   B 167 ? 0.8291 0.5979 0.6336 0.0791  -0.1051 0.0278  860  GLY   B C   
3321 O O   . GLY   B 167 ? 0.8423 0.5865 0.6285 0.0945  -0.1125 0.0330  860  GLY   B O   
3322 N N   . LEU   B 168 ? 0.8499 0.6050 0.6353 0.0594  -0.0951 0.0255  861  LEU   B N   
3323 C CA  . LEU   B 168 ? 0.8918 0.6020 0.6336 0.0518  -0.0902 0.0288  861  LEU   B CA  
3324 C C   . LEU   B 168 ? 0.9343 0.6251 0.6487 0.0546  -0.0998 0.0343  861  LEU   B C   
3325 O O   . LEU   B 168 ? 0.9642 0.6135 0.6416 0.0608  -0.1017 0.0400  861  LEU   B O   
3326 C CB  . LEU   B 168 ? 0.8843 0.5943 0.6231 0.0284  -0.0774 0.0248  861  LEU   B CB  
3327 C CG  . LEU   B 168 ? 0.9184 0.5845 0.6175 0.0164  -0.0695 0.0277  861  LEU   B CG  
3328 C CD1 . LEU   B 168 ? 0.9403 0.5692 0.6160 0.0261  -0.0685 0.0294  861  LEU   B CD1 
3329 C CD2 . LEU   B 168 ? 0.9170 0.5935 0.6252 -0.0067 -0.0586 0.0237  861  LEU   B CD2 
3330 N N   . ALA   B 169 ? 0.9352 0.6517 0.6635 0.0508  -0.1065 0.0328  862  ALA   B N   
3331 C CA  . ALA   B 169 ? 0.9697 0.6662 0.6677 0.0535  -0.1174 0.0373  862  ALA   B CA  
3332 C C   . ALA   B 169 ? 0.9930 0.6784 0.6853 0.0765  -0.1356 0.0433  862  ALA   B C   
3333 O O   . ALA   B 169 ? 1.0261 0.6704 0.6756 0.0819  -0.1412 0.0499  862  ALA   B O   
3334 C CB  . ALA   B 169 ? 0.9561 0.6827 0.6721 0.0464  -0.1221 0.0329  862  ALA   B CB  
3335 N N   . LYS   B 170 ? 0.9773 0.6980 0.7134 0.0904  -0.1432 0.0416  863  LYS   B N   
3336 C CA  . LYS   B 170 ? 0.9886 0.7067 0.7307 0.1144  -0.1602 0.0473  863  LYS   B CA  
3337 C C   . LYS   B 170 ? 1.0232 0.6979 0.7346 0.1255  -0.1540 0.0523  863  LYS   B C   
3338 O O   . LYS   B 170 ? 1.0421 0.6914 0.7320 0.1426  -0.1680 0.0596  863  LYS   B O   
3339 C CB  . LYS   B 170 ? 0.9756 0.7450 0.7777 0.1252  -0.1650 0.0441  863  LYS   B CB  
3340 C CG  . LYS   B 170 ? 1.0223 0.7999 0.8411 0.1495  -0.1859 0.0501  863  LYS   B CG  
3341 C CD  . LYS   B 170 ? 1.0368 0.8690 0.9204 0.1582  -0.1881 0.0471  863  LYS   B CD  
3342 N N   . LEU   B 171 ? 1.0358 0.6983 0.7419 0.1156  -0.1344 0.0485  864  LEU   B N   
3343 C CA  . LEU   B 171 ? 1.0770 0.6922 0.7491 0.1222  -0.1263 0.0518  864  LEU   B CA  
3344 C C   . LEU   B 171 ? 1.1333 0.6957 0.7476 0.1144  -0.1274 0.0584  864  LEU   B C   
3345 O O   . LEU   B 171 ? 1.1599 0.6786 0.7408 0.1282  -0.1310 0.0650  864  LEU   B O   
3346 C CB  . LEU   B 171 ? 1.0791 0.6951 0.7573 0.1072  -0.1069 0.0448  864  LEU   B CB  
3347 C CG  . LEU   B 171 ? 1.1303 0.6930 0.7689 0.1073  -0.0968 0.0461  864  LEU   B CG  
3348 C CD1 . LEU   B 171 ? 1.1417 0.6919 0.7841 0.1356  -0.1004 0.0487  864  LEU   B CD1 
3349 C CD2 . LEU   B 171 ? 1.1368 0.7004 0.7777 0.0868  -0.0815 0.0386  864  LEU   B CD2 
3350 N N   . LEU   B 172 ? 1.1517 0.7166 0.7531 0.0937  -0.1235 0.0571  865  LEU   B N   
3351 C CA  . LEU   B 172 ? 1.2075 0.7239 0.7538 0.0831  -0.1200 0.0631  865  LEU   B CA  
3352 C C   . LEU   B 172 ? 1.2517 0.7528 0.7707 0.0947  -0.1392 0.0701  865  LEU   B C   
3353 O O   . LEU   B 172 ? 1.2771 0.7482 0.7541 0.0822  -0.1351 0.0735  865  LEU   B O   
3354 C CB  . LEU   B 172 ? 1.2034 0.7285 0.7495 0.0548  -0.1021 0.0580  865  LEU   B CB  
3355 C CG  . LEU   B 172 ? 1.2086 0.7416 0.7739 0.0410  -0.0858 0.0520  865  LEU   B CG  
3356 C CD1 . LEU   B 172 ? 1.1975 0.7563 0.7803 0.0166  -0.0723 0.0465  865  LEU   B CD1 
3357 C CD2 . LEU   B 172 ? 1.2449 0.7233 0.7705 0.0397  -0.0785 0.0563  865  LEU   B CD2 
3358 N N   . GLY   B 173 ? 1.2581 0.7792 0.8007 0.1180  -0.1599 0.0724  866  GLY   B N   
3359 C CA  . GLY   B 173 ? 1.2951 0.8033 0.8147 0.1314  -0.1840 0.0793  866  GLY   B CA  
3360 C C   . GLY   B 173 ? 1.3160 0.8467 0.8373 0.1194  -0.1922 0.0755  866  GLY   B C   
3361 O O   . GLY   B 173 ? 1.3460 0.8498 0.8277 0.1243  -0.2092 0.0812  866  GLY   B O   
3362 N N   . ALA   B 174 ? 1.3000 0.8769 0.8638 0.1048  -0.1816 0.0660  867  ALA   B N   
3363 C CA  . ALA   B 174 ? 1.3120 0.9078 0.8771 0.0937  -0.1880 0.0613  867  ALA   B CA  
3364 C C   . ALA   B 174 ? 1.3157 0.9361 0.9020 0.1091  -0.2185 0.0623  867  ALA   B C   
3365 O O   . ALA   B 174 ? 1.3308 0.9427 0.8923 0.1042  -0.2315 0.0617  867  ALA   B O   
3366 C CB  . ALA   B 174 ? 1.2855 0.9215 0.8906 0.0761  -0.1696 0.0516  867  ALA   B CB  
3367 N N   . GLU   B 175 ? 1.3010 0.9504 0.9323 0.1275  -0.2297 0.0639  868  GLU   B N   
3368 C CA  . GLU   B 175 ? 1.2977 0.9762 0.9584 0.1420  -0.2598 0.0654  868  GLU   B CA  
3369 C C   . GLU   B 175 ? 1.3389 0.9811 0.9640 0.1632  -0.2847 0.0762  868  GLU   B C   
3370 O O   . GLU   B 175 ? 1.3291 0.9942 0.9776 0.1762  -0.3137 0.0785  868  GLU   B O   
3371 C CB  . GLU   B 175 ? 1.2786 1.0149 1.0145 0.1503  -0.2586 0.0613  868  GLU   B CB  
3372 N N   . GLU   B 176 ? 1.3828 0.9681 0.9516 0.1663  -0.2751 0.0833  869  GLU   B N   
3373 C CA  . GLU   B 176 ? 1.4226 0.9658 0.9504 0.1872  -0.2981 0.0948  869  GLU   B CA  
3374 C C   . GLU   B 176 ? 1.4768 0.9734 0.9335 0.1772  -0.3092 0.0985  869  GLU   B C   
3375 O O   . GLU   B 176 ? 1.4999 0.9714 0.9192 0.1555  -0.2859 0.0951  869  GLU   B O   
3376 C CB  . GLU   B 176 ? 1.4680 0.9686 0.9703 0.1974  -0.2815 0.1012  869  GLU   B CB  
3377 N N   . LYS   B 177 ? 1.4949 0.9802 0.9331 0.1933  -0.3447 0.1054  870  LYS   B N   
3378 C CA  . LYS   B 177 ? 1.5460 0.9818 0.9097 0.1873  -0.3607 0.1098  870  LYS   B CA  
3379 C C   . LYS   B 177 ? 1.5596 0.9995 0.9066 0.1595  -0.3447 0.0994  870  LYS   B C   
3380 O O   . LYS   B 177 ? 1.6030 0.9913 0.8825 0.1458  -0.3279 0.1012  870  LYS   B O   
3381 C CB  . LYS   B 177 ? 1.6176 0.9759 0.9022 0.1932  -0.3534 0.1217  870  LYS   B CB  
3382 N N   . GLY   B 184 ? 1.3775 0.7165 0.6899 -0.0894 0.0424  0.0778  877  GLY   B N   
3383 C CA  . GLY   B 184 ? 1.3509 0.7433 0.7113 -0.0738 0.0222  0.0696  877  GLY   B CA  
3384 C C   . GLY   B 184 ? 1.3346 0.7583 0.7108 -0.0765 0.0302  0.0633  877  GLY   B C   
3385 O O   . GLY   B 184 ? 1.3661 0.7578 0.6941 -0.0763 0.0367  0.0665  877  GLY   B O   
3386 N N   . LYS   B 185 ? 1.2835 0.7659 0.7231 -0.0783 0.0297  0.0544  878  LYS   B N   
3387 C CA  . LYS   B 185 ? 1.2630 0.7761 0.7220 -0.0798 0.0378  0.0476  878  LYS   B CA  
3388 C C   . LYS   B 185 ? 1.2272 0.7761 0.7162 -0.0629 0.0133  0.0413  878  LYS   B C   
3389 O O   . LYS   B 185 ? 1.1934 0.7807 0.7317 -0.0597 0.0039  0.0373  878  LYS   B O   
3390 C CB  . LYS   B 185 ? 1.2600 0.8100 0.7674 -0.0980 0.0621  0.0431  878  LYS   B CB  
3391 N N   . VAL   B 186 ? 1.2295 0.7630 0.6860 -0.0533 0.0032  0.0405  879  VAL   B N   
3392 C CA  . VAL   B 186 ? 1.2001 0.7636 0.6813 -0.0399 -0.0199 0.0346  879  VAL   B CA  
3393 C C   . VAL   B 186 ? 1.1478 0.7532 0.6726 -0.0465 -0.0068 0.0257  879  VAL   B C   
3394 O O   . VAL   B 186 ? 1.1622 0.7589 0.6739 -0.0566 0.0168  0.0240  879  VAL   B O   
3395 C CB  . VAL   B 186 ? 1.2461 0.7727 0.6720 -0.0289 -0.0387 0.0373  879  VAL   B CB  
3396 C CG1 . VAL   B 186 ? 1.2867 0.7713 0.6550 -0.0379 -0.0184 0.0386  879  VAL   B CG1 
3397 C CG2 . VAL   B 186 ? 1.2337 0.7910 0.6857 -0.0182 -0.0627 0.0308  879  VAL   B CG2 
3398 N N   . PRO   B 187 ? 1.0847 0.7350 0.6627 -0.0411 -0.0192 0.0204  880  PRO   B N   
3399 C CA  . PRO   B 187 ? 1.0351 0.7220 0.6537 -0.0465 -0.0068 0.0129  880  PRO   B CA  
3400 C C   . PRO   B 187 ? 1.0094 0.6943 0.6142 -0.0413 -0.0125 0.0069  880  PRO   B C   
3401 O O   . PRO   B 187 ? 0.9858 0.7010 0.6249 -0.0364 -0.0244 0.0017  880  PRO   B O   
3402 C CB  . PRO   B 187 ? 1.0120 0.7395 0.6849 -0.0433 -0.0175 0.0111  880  PRO   B CB  
3403 C CG  . PRO   B 187 ? 1.0296 0.7465 0.6907 -0.0311 -0.0413 0.0149  880  PRO   B CG  
3404 C CD  . PRO   B 187 ? 1.0541 0.7223 0.6572 -0.0294 -0.0427 0.0214  880  PRO   B CD  
3405 N N   . ILE   B 188 ? 1.0154 0.6609 0.5665 -0.0437 -0.0029 0.0075  881  ILE   B N   
3406 C CA  . ILE   B 188 ? 1.0138 0.6437 0.5357 -0.0403 -0.0070 0.0013  881  ILE   B CA  
3407 C C   . ILE   B 188 ? 0.9604 0.6243 0.5241 -0.0413 0.0023  -0.0075 881  ILE   B C   
3408 O O   . ILE   B 188 ? 0.9578 0.6261 0.5223 -0.0362 -0.0139 -0.0134 881  ILE   B O   
3409 C CB  . ILE   B 188 ? 1.0628 0.6403 0.5164 -0.0451 0.0108  0.0038  881  ILE   B CB  
3410 C CG1 . ILE   B 188 ? 1.1020 0.6400 0.5092 -0.0432 0.0006  0.0139  881  ILE   B CG1 
3411 C CG2 . ILE   B 188 ? 1.0915 0.6446 0.5047 -0.0418 0.0058  -0.0034 881  ILE   B CG2 
3412 C CD1 . ILE   B 188 ? 1.1322 0.6537 0.5127 -0.0309 -0.0364 0.0158  881  ILE   B CD1 
3413 N N   . LYS   B 189 ? 0.9105 0.5991 0.5112 -0.0480 0.0267  -0.0081 882  LYS   B N   
3414 C CA  . LYS   B 189 ? 0.8625 0.5815 0.5030 -0.0473 0.0372  -0.0154 882  LYS   B CA  
3415 C C   . LYS   B 189 ? 0.8094 0.5685 0.5019 -0.0422 0.0175  -0.0176 882  LYS   B C   
3416 O O   . LYS   B 189 ? 0.7936 0.5744 0.5162 -0.0404 0.0231  -0.0230 882  LYS   B O   
3417 C CB  . LYS   B 189 ? 0.8566 0.5902 0.5219 -0.0550 0.0683  -0.0144 882  LYS   B CB  
3418 C CG  . LYS   B 189 ? 0.9203 0.6130 0.5326 -0.0596 0.0924  -0.0138 882  LYS   B CG  
3419 C CD  . LYS   B 189 ? 0.9521 0.6594 0.5902 -0.0692 0.1246  -0.0113 882  LYS   B CD  
3420 C CE  . LYS   B 189 ? 1.0170 0.6809 0.5990 -0.0735 0.1519  -0.0108 882  LYS   B CE  
3421 N NZ  . LYS   B 189 ? 1.0264 0.7124 0.6439 -0.0809 0.1880  -0.0109 882  LYS   B NZ  
3422 N N   . TRP   B 190 ? 0.7834 0.5489 0.4833 -0.0391 -0.0044 -0.0134 883  TRP   B N   
3423 C CA  . TRP   B 190 ? 0.7409 0.5396 0.4836 -0.0343 -0.0223 -0.0148 883  TRP   B CA  
3424 C C   . TRP   B 190 ? 0.7469 0.5367 0.4737 -0.0278 -0.0485 -0.0155 883  TRP   B C   
3425 O O   . TRP   B 190 ? 0.7181 0.5333 0.4780 -0.0246 -0.0618 -0.0174 883  TRP   B O   
3426 C CB  . TRP   B 190 ? 0.7106 0.5294 0.4834 -0.0358 -0.0240 -0.0095 883  TRP   B CB  
3427 C CG  . TRP   B 190 ? 0.6812 0.5246 0.4899 -0.0421 -0.0068 -0.0099 883  TRP   B CG  
3428 C CD1 . TRP   B 190 ? 0.6566 0.5330 0.5091 -0.0409 -0.0093 -0.0119 883  TRP   B CD1 
3429 C CD2 . TRP   B 190 ? 0.6760 0.5133 0.4808 -0.0509 0.0145  -0.0078 883  TRP   B CD2 
3430 N NE1 . TRP   B 190 ? 0.6425 0.5349 0.5195 -0.0474 0.0065  -0.0112 883  TRP   B NE1 
3431 C CE2 . TRP   B 190 ? 0.6569 0.5283 0.5087 -0.0544 0.0220  -0.0089 883  TRP   B CE2 
3432 C CE3 . TRP   B 190 ? 0.7062 0.5119 0.4723 -0.0569 0.0281  -0.0045 883  TRP   B CE3 
3433 C CZ2 . TRP   B 190 ? 0.6584 0.5384 0.5260 -0.0640 0.0414  -0.0072 883  TRP   B CZ2 
3434 C CZ3 . TRP   B 190 ? 0.7113 0.5233 0.4909 -0.0674 0.0508  -0.0029 883  TRP   B CZ3 
3435 C CH2 . TRP   B 190 ? 0.6812 0.5324 0.5142 -0.0710 0.0567  -0.0044 883  TRP   B CH2 
3436 N N   . MET   B 191 ? 0.7830 0.5370 0.4603 -0.0261 -0.0562 -0.0134 884  MET   B N   
3437 C CA  . MET   B 191 ? 0.8049 0.5496 0.4659 -0.0199 -0.0836 -0.0132 884  MET   B CA  
3438 C C   . MET   B 191 ? 0.8230 0.5595 0.4698 -0.0211 -0.0929 -0.0210 884  MET   B C   
3439 O O   . MET   B 191 ? 0.8396 0.5538 0.4574 -0.0251 -0.0773 -0.0260 884  MET   B O   
3440 C CB  . MET   B 191 ? 0.8469 0.5525 0.4563 -0.0171 -0.0900 -0.0066 884  MET   B CB  
3441 C CG  . MET   B 191 ? 0.8797 0.5894 0.5009 -0.0139 -0.0896 0.0013  884  MET   B CG  
3442 S SD  . MET   B 191 ? 1.0105 0.6645 0.5634 -0.0126 -0.0880 0.0101  884  MET   B SD  
3443 C CE  . MET   B 191 ? 0.9592 0.5919 0.4767 -0.0033 -0.1203 0.0101  884  MET   B CE  
3444 N N   . ALA   B 192 ? 0.8160 0.5686 0.4822 -0.0177 -0.1183 -0.0223 885  ALA   B N   
3445 C CA  . ALA   B 192 ? 0.8303 0.5738 0.4829 -0.0204 -0.1333 -0.0296 885  ALA   B CA  
3446 C C   . ALA   B 192 ? 0.8882 0.5838 0.4728 -0.0200 -0.1437 -0.0297 885  ALA   B C   
3447 O O   . ALA   B 192 ? 0.9058 0.5840 0.4652 -0.0153 -0.1485 -0.0221 885  ALA   B O   
3448 C CB  . ALA   B 192 ? 0.7983 0.5742 0.4937 -0.0183 -0.1582 -0.0294 885  ALA   B CB  
3449 N N   . LEU   B 193 ? 0.9170 0.5868 0.4672 -0.0248 -0.1475 -0.0381 886  LEU   B N   
3450 C CA  . LEU   B 193 ? 0.9772 0.5959 0.4549 -0.0251 -0.1578 -0.0389 886  LEU   B CA  
3451 C C   . LEU   B 193 ? 1.0029 0.6171 0.4688 -0.0191 -0.1927 -0.0322 886  LEU   B C   
3452 O O   . LEU   B 193 ? 1.0402 0.6158 0.4517 -0.0156 -0.1956 -0.0267 886  LEU   B O   
3453 C CB  . LEU   B 193 ? 0.9997 0.5927 0.4455 -0.0315 -0.1604 -0.0506 886  LEU   B CB  
3454 C CG  . LEU   B 193 ? 1.0640 0.5964 0.4247 -0.0328 -0.1685 -0.0531 886  LEU   B CG  
3455 C CD1 . LEU   B 193 ? 1.1007 0.5990 0.4162 -0.0321 -0.1336 -0.0503 886  LEU   B CD1 
3456 C CD2 . LEU   B 193 ? 1.0865 0.5953 0.4197 -0.0396 -0.1785 -0.0656 886  LEU   B CD2 
3457 N N   . GLU   B 194 ? 0.9822 0.6360 0.5005 -0.0170 -0.2176 -0.0317 887  GLU   B N   
3458 C CA  . GLU   B 194 ? 0.9886 0.6458 0.5072 -0.0092 -0.2517 -0.0250 887  GLU   B CA  
3459 C C   . GLU   B 194 ? 0.9987 0.6589 0.5230 0.0015  -0.2451 -0.0135 887  GLU   B C   
3460 O O   . GLU   B 194 ? 1.0189 0.6607 0.5169 0.0101  -0.2676 -0.0066 887  GLU   B O   
3461 C CB  . GLU   B 194 ? 0.9625 0.6656 0.5426 -0.0105 -0.2773 -0.0276 887  GLU   B CB  
3462 C CG  . GLU   B 194 ? 0.9519 0.7079 0.6067 -0.0071 -0.2651 -0.0241 887  GLU   B CG  
3463 C CD  . GLU   B 194 ? 0.9572 0.7336 0.6448 -0.0159 -0.2407 -0.0308 887  GLU   B CD  
3464 O OE1 . GLU   B 194 ? 0.9702 0.7186 0.6226 -0.0234 -0.2280 -0.0381 887  GLU   B OE1 
3465 O OE2 . GLU   B 194 ? 0.9137 0.7312 0.6594 -0.0144 -0.2340 -0.0285 887  GLU   B OE2 
3466 N N   . SER   B 195 ? 0.9861 0.6655 0.5410 0.0009  -0.2157 -0.0115 888  SER   B N   
3467 C CA  . SER   B 195 ? 1.0013 0.6780 0.5576 0.0087  -0.2068 -0.0019 888  SER   B CA  
3468 C C   . SER   B 195 ? 1.0581 0.6811 0.5442 0.0069  -0.1921 0.0020  888  SER   B C   
3469 O O   . SER   B 195 ? 1.0778 0.6787 0.5389 0.0147  -0.1983 0.0110  888  SER   B O   
3470 C CB  . SER   B 195 ? 0.9815 0.6938 0.5904 0.0064  -0.1820 -0.0020 888  SER   B CB  
3471 O OG  . SER   B 195 ? 0.9743 0.7324 0.6437 0.0076  -0.1921 -0.0049 888  SER   B OG  
3472 N N   . ILE   B 196 ? 1.0826 0.6827 0.5362 -0.0028 -0.1710 -0.0043 889  ILE   B N   
3473 C CA  . ILE   B 196 ? 1.1351 0.6831 0.5207 -0.0061 -0.1526 -0.0011 889  ILE   B CA  
3474 C C   . ILE   B 196 ? 1.1924 0.6940 0.5116 -0.0009 -0.1801 0.0022  889  ILE   B C   
3475 O O   . ILE   B 196 ? 1.2290 0.6928 0.5019 0.0032  -0.1797 0.0112  889  ILE   B O   
3476 C CB  . ILE   B 196 ? 1.1418 0.6804 0.5144 -0.0162 -0.1215 -0.0097 889  ILE   B CB  
3477 C CG1 . ILE   B 196 ? 1.1095 0.6942 0.5483 -0.0203 -0.0964 -0.0118 889  ILE   B CG1 
3478 C CG2 . ILE   B 196 ? 1.1854 0.6677 0.4842 -0.0202 -0.1001 -0.0066 889  ILE   B CG2 
3479 C CD1 . ILE   B 196 ? 1.1179 0.7015 0.5563 -0.0271 -0.0686 -0.0203 889  ILE   B CD1 
3480 N N   . LEU   B 197 ? 1.2016 0.7045 0.5157 -0.0015 -0.2061 -0.0049 890  LEU   B N   
3481 C CA  . LEU   B 197 ? 1.2510 0.7095 0.5003 0.0021  -0.2364 -0.0032 890  LEU   B CA  
3482 C C   . LEU   B 197 ? 1.2563 0.7256 0.5198 0.0149  -0.2742 0.0058  890  LEU   B C   
3483 O O   . LEU   B 197 ? 1.3004 0.7238 0.5007 0.0206  -0.2944 0.0118  890  LEU   B O   
3484 C CB  . LEU   B 197 ? 1.2640 0.7158 0.4984 -0.0057 -0.2510 -0.0154 890  LEU   B CB  
3485 C CG  . LEU   B 197 ? 1.2974 0.7346 0.5146 -0.0160 -0.2157 -0.0256 890  LEU   B CG  
3486 C CD1 . LEU   B 197 ? 1.3106 0.7371 0.5111 -0.0229 -0.2341 -0.0379 890  LEU   B CD1 
3487 C CD2 . LEU   B 197 ? 1.3524 0.7331 0.4952 -0.0178 -0.1859 -0.0223 890  LEU   B CD2 
3488 N N   . HIS   B 198 ? 1.2155 0.7433 0.5590 0.0202  -0.2854 0.0066  891  HIS   B N   
3489 C CA  . HIS   B 198 ? 1.2132 0.7570 0.5787 0.0342  -0.3215 0.0145  891  HIS   B CA  
3490 C C   . HIS   B 198 ? 1.1893 0.7715 0.6151 0.0448  -0.3135 0.0218  891  HIS   B C   
3491 O O   . HIS   B 198 ? 1.1782 0.7826 0.6354 0.0580  -0.3410 0.0274  891  HIS   B O   
3492 C CB  . HIS   B 198 ? 1.2050 0.7798 0.6048 0.0318  -0.3560 0.0078  891  HIS   B CB  
3493 C CG  . HIS   B 198 ? 1.2742 0.8080 0.6119 0.0211  -0.3684 -0.0006 891  HIS   B CG  
3494 N ND1 . HIS   B 198 ? 1.2915 0.8364 0.6427 0.0068  -0.3572 -0.0131 891  HIS   B ND1 
3495 C CD2 . HIS   B 198 ? 1.3352 0.8121 0.5922 0.0231  -0.3894 0.0020  891  HIS   B CD2 
3496 C CE1 . HIS   B 198 ? 1.3394 0.8343 0.6189 0.0005  -0.3716 -0.0187 891  HIS   B CE1 
3497 N NE2 . HIS   B 198 ? 1.3718 0.8244 0.5914 0.0095  -0.3915 -0.0100 891  HIS   B NE2 
3498 N N   . ARG   B 199 ? 1.1786 0.7701 0.6230 0.0394  -0.2770 0.0212  892  ARG   B N   
3499 C CA  . ARG   B 199 ? 1.1560 0.7795 0.6526 0.0476  -0.2668 0.0265  892  ARG   B CA  
3500 C C   . ARG   B 199 ? 1.0922 0.7752 0.6659 0.0527  -0.2832 0.0236  892  ARG   B C   
3501 O O   . ARG   B 199 ? 1.0791 0.7832 0.6882 0.0660  -0.2904 0.0297  892  ARG   B O   
3502 C CB  . ARG   B 199 ? 1.2187 0.8069 0.6795 0.0611  -0.2729 0.0384  892  ARG   B CB  
3503 C CG  . ARG   B 199 ? 1.3320 0.8687 0.7310 0.0531  -0.2448 0.0421  892  ARG   B CG  
3504 C CD  . ARG   B 199 ? 1.3936 0.9522 0.8275 0.0426  -0.2087 0.0387  892  ARG   B CD  
3505 N NE  . ARG   B 199 ? 1.4950 1.0102 0.8775 0.0319  -0.1802 0.0415  892  ARG   B NE  
3506 C CZ  . ARG   B 199 ? 1.5581 1.0574 0.9120 0.0186  -0.1610 0.0357  892  ARG   B CZ  
3507 N NH1 . ARG   B 199 ? 1.5413 1.0596 0.9078 0.0147  -0.1684 0.0265  892  ARG   B NH1 
3508 N NH2 . ARG   B 199 ? 1.5966 1.0592 0.9086 0.0091  -0.1331 0.0391  892  ARG   B NH2 
3509 N N   . ILE   B 200 ? 1.0520 0.7594 0.6501 0.0419  -0.2872 0.0142  893  ILE   B N   
3510 C CA  . ILE   B 200 ? 0.9942 0.7568 0.6648 0.0429  -0.2987 0.0110  893  ILE   B CA  
3511 C C   . ILE   B 200 ? 0.9497 0.7428 0.6647 0.0367  -0.2675 0.0076  893  ILE   B C   
3512 O O   . ILE   B 200 ? 0.9588 0.7436 0.6611 0.0245  -0.2469 0.0014  893  ILE   B O   
3513 C CB  . ILE   B 200 ? 1.0007 0.7694 0.6716 0.0329  -0.3215 0.0030  893  ILE   B CB  
3514 C CG1 . ILE   B 200 ? 1.0332 0.7764 0.6657 0.0401  -0.3595 0.0069  893  ILE   B CG1 
3515 C CG2 . ILE   B 200 ? 0.9614 0.7871 0.7091 0.0288  -0.3254 -0.0013 893  ILE   B CG2 
3516 N N   . TYR   B 201 ? 0.8999 0.7258 0.6643 0.0461  -0.2638 0.0118  894  TYR   B N   
3517 C CA  . TYR   B 201 ? 0.8599 0.7119 0.6626 0.0411  -0.2372 0.0093  894  TYR   B CA  
3518 C C   . TYR   B 201 ? 0.8027 0.7039 0.6708 0.0431  -0.2441 0.0077  894  TYR   B C   
3519 O O   . TYR   B 201 ? 0.7912 0.7113 0.6875 0.0560  -0.2586 0.0127  894  TYR   B O   
3520 C CB  . TYR   B 201 ? 0.8678 0.7059 0.6610 0.0484  -0.2194 0.0153  894  TYR   B CB  
3521 C CG  . TYR   B 201 ? 0.9102 0.7024 0.6444 0.0427  -0.2055 0.0169  894  TYR   B CG  
3522 C CD1 . TYR   B 201 ? 0.9527 0.7048 0.6368 0.0501  -0.2178 0.0232  894  TYR   B CD1 
3523 C CD2 . TYR   B 201 ? 0.9173 0.7064 0.6473 0.0302  -0.1794 0.0128  894  TYR   B CD2 
3524 C CE1 . TYR   B 201 ? 0.9976 0.7060 0.6271 0.0437  -0.2017 0.0254  894  TYR   B CE1 
3525 C CE2 . TYR   B 201 ? 0.9604 0.7115 0.6427 0.0241  -0.1637 0.0147  894  TYR   B CE2 
3526 C CZ  . TYR   B 201 ? 1.0105 0.7202 0.6414 0.0300  -0.1736 0.0210  894  TYR   B CZ  
3527 O OH  . TYR   B 201 ? 1.0658 0.7357 0.6478 0.0225  -0.1556 0.0235  894  TYR   B OH  
3528 N N   . THR   B 202 ? 0.7656 0.6866 0.6580 0.0306  -0.2330 0.0011  895  THR   B N   
3529 C CA  . THR   B 202 ? 0.7172 0.6818 0.6687 0.0284  -0.2354 -0.0008 895  THR   B CA  
3530 C C   . THR   B 202 ? 0.6903 0.6667 0.6602 0.0206  -0.2084 -0.0038 895  THR   B C   
3531 O O   . THR   B 202 ? 0.7065 0.6602 0.6467 0.0170  -0.1909 -0.0046 895  THR   B O   
3532 C CB  . THR   B 202 ? 0.7324 0.7034 0.6887 0.0183  -0.2577 -0.0064 895  THR   B CB  
3533 O OG1 . THR   B 202 ? 0.7693 0.7189 0.6969 0.0046  -0.2462 -0.0136 895  THR   B OG1 
3534 C CG2 . THR   B 202 ? 0.7377 0.6923 0.6681 0.0246  -0.2883 -0.0039 895  THR   B CG2 
3535 N N   . HIS   B 203 ? 0.6462 0.6575 0.6649 0.0174  -0.2049 -0.0050 896  HIS   B N   
3536 C CA  . HIS   B 203 ? 0.6275 0.6463 0.6589 0.0096  -0.1827 -0.0074 896  HIS   B CA  
3537 C C   . HIS   B 203 ? 0.6262 0.6271 0.6338 -0.0033 -0.1803 -0.0139 896  HIS   B C   
3538 O O   . HIS   B 203 ? 0.6320 0.6265 0.6331 -0.0075 -0.1619 -0.0154 896  HIS   B O   
3539 C CB  . HIS   B 203 ? 0.6091 0.6644 0.6927 0.0091  -0.1786 -0.0063 896  HIS   B CB  
3540 C CG  . HIS   B 203 ? 0.6148 0.6851 0.7202 0.0236  -0.1761 -0.0005 896  HIS   B CG  
3541 N ND1 . HIS   B 203 ? 0.6082 0.7061 0.7513 0.0305  -0.1906 0.0021  896  HIS   B ND1 
3542 C CD2 . HIS   B 203 ? 0.6338 0.6932 0.7272 0.0326  -0.1612 0.0027  896  HIS   B CD2 
3543 C CE1 . HIS   B 203 ? 0.6057 0.7082 0.7585 0.0453  -0.1819 0.0068  896  HIS   B CE1 
3544 N NE2 . HIS   B 203 ? 0.6286 0.7057 0.7490 0.0465  -0.1645 0.0070  896  HIS   B NE2 
3545 N N   . GLN   B 204 ? 0.6216 0.6111 0.6124 -0.0085 -0.1992 -0.0178 897  GLN   B N   
3546 C CA  . GLN   B 204 ? 0.6302 0.5966 0.5924 -0.0192 -0.1964 -0.0249 897  GLN   B CA  
3547 C C   . GLN   B 204 ? 0.6555 0.5865 0.5675 -0.0170 -0.1854 -0.0254 897  GLN   B C   
3548 O O   . GLN   B 204 ? 0.6726 0.5899 0.5698 -0.0227 -0.1702 -0.0298 897  GLN   B O   
3549 C CB  . GLN   B 204 ? 0.6384 0.6028 0.5992 -0.0274 -0.2203 -0.0301 897  GLN   B CB  
3550 C CG  . GLN   B 204 ? 0.6334 0.6341 0.6489 -0.0341 -0.2258 -0.0303 897  GLN   B CG  
3551 C CD  . GLN   B 204 ? 0.6813 0.6905 0.7165 -0.0399 -0.2027 -0.0314 897  GLN   B CD  
3552 O OE1 . GLN   B 204 ? 0.7109 0.7006 0.7276 -0.0483 -0.1960 -0.0372 897  GLN   B OE1 
3553 N NE2 . GLN   B 204 ? 0.6675 0.7030 0.7377 -0.0343 -0.1900 -0.0257 897  GLN   B NE2 
3554 N N   . SER   B 205 ? 0.6618 0.5784 0.5499 -0.0085 -0.1905 -0.0203 898  SER   B N   
3555 C CA  . SER   B 205 ? 0.6854 0.5693 0.5285 -0.0078 -0.1757 -0.0195 898  SER   B CA  
3556 C C   . SER   B 205 ? 0.6694 0.5644 0.5304 -0.0075 -0.1511 -0.0171 898  SER   B C   
3557 O O   . SER   B 205 ? 0.6871 0.5645 0.5253 -0.0111 -0.1339 -0.0184 898  SER   B O   
3558 C CB  . SER   B 205 ? 0.7195 0.5788 0.5265 0.0000  -0.1887 -0.0142 898  SER   B CB  
3559 O OG  . SER   B 205 ? 0.7306 0.6061 0.5614 0.0102  -0.1915 -0.0072 898  SER   B OG  
3560 N N   . ASP   B 206 ? 0.6359 0.5602 0.5378 -0.0037 -0.1493 -0.0139 899  ASP   B N   
3561 C CA  . ASP   B 206 ? 0.6309 0.5661 0.5501 -0.0044 -0.1301 -0.0122 899  ASP   B CA  
3562 C C   . ASP   B 206 ? 0.6177 0.5606 0.5497 -0.0122 -0.1193 -0.0171 899  ASP   B C   
3563 O O   . ASP   B 206 ? 0.6205 0.5636 0.5543 -0.0143 -0.1038 -0.0168 899  ASP   B O   
3564 C CB  . ASP   B 206 ? 0.6393 0.5992 0.5934 0.0019  -0.1315 -0.0083 899  ASP   B CB  
3565 C CG  . ASP   B 206 ? 0.7234 0.6736 0.6665 0.0117  -0.1341 -0.0029 899  ASP   B CG  
3566 O OD1 . ASP   B 206 ? 0.7577 0.6813 0.6662 0.0115  -0.1302 -0.0013 899  ASP   B OD1 
3567 O OD2 . ASP   B 206 ? 0.7430 0.7107 0.7117 0.0198  -0.1383 -0.0001 899  ASP   B OD2 
3568 N N   . VAL   B 207 ? 0.6016 0.5508 0.5442 -0.0165 -0.1287 -0.0213 900  VAL   B N   
3569 C CA  . VAL   B 207 ? 0.5944 0.5448 0.5449 -0.0229 -0.1203 -0.0260 900  VAL   B CA  
3570 C C   . VAL   B 207 ? 0.5969 0.5218 0.5142 -0.0247 -0.1091 -0.0298 900  VAL   B C   
3571 O O   . VAL   B 207 ? 0.5932 0.5207 0.5185 -0.0255 -0.0940 -0.0308 900  VAL   B O   
3572 C CB  . VAL   B 207 ? 0.5984 0.5564 0.5642 -0.0286 -0.1340 -0.0298 900  VAL   B CB  
3573 C CG1 . VAL   B 207 ? 0.6167 0.5623 0.5761 -0.0350 -0.1263 -0.0358 900  VAL   B CG1 
3574 C CG2 . VAL   B 207 ? 0.5816 0.5697 0.5889 -0.0278 -0.1360 -0.0256 900  VAL   B CG2 
3575 N N   . TRP   B 208 ? 0.5998 0.4996 0.4794 -0.0242 -0.1156 -0.0312 901  TRP   B N   
3576 C CA  . TRP   B 208 ? 0.6141 0.4868 0.4578 -0.0254 -0.1015 -0.0342 901  TRP   B CA  
3577 C C   . TRP   B 208 ? 0.6042 0.4838 0.4564 -0.0240 -0.0822 -0.0298 901  TRP   B C   
3578 O O   . TRP   B 208 ? 0.6036 0.4841 0.4612 -0.0252 -0.0655 -0.0322 901  TRP   B O   
3579 C CB  . TRP   B 208 ? 0.6358 0.4773 0.4326 -0.0249 -0.1125 -0.0347 901  TRP   B CB  
3580 C CG  . TRP   B 208 ? 0.6652 0.4746 0.4199 -0.0266 -0.0949 -0.0379 901  TRP   B CG  
3581 C CD1 . TRP   B 208 ? 0.6767 0.4829 0.4271 -0.0264 -0.0725 -0.0349 901  TRP   B CD1 
3582 C CD2 . TRP   B 208 ? 0.6914 0.4668 0.4023 -0.0293 -0.0969 -0.0451 901  TRP   B CD2 
3583 N NE1 . TRP   B 208 ? 0.7055 0.4804 0.4157 -0.0282 -0.0576 -0.0393 901  TRP   B NE1 
3584 C CE2 . TRP   B 208 ? 0.7160 0.4686 0.3974 -0.0294 -0.0720 -0.0459 901  TRP   B CE2 
3585 C CE3 . TRP   B 208 ? 0.7156 0.4754 0.4068 -0.0325 -0.1182 -0.0509 901  TRP   B CE3 
3586 C CZ2 . TRP   B 208 ? 0.7546 0.4671 0.3843 -0.0311 -0.0651 -0.0525 901  TRP   B CZ2 
3587 C CZ3 . TRP   B 208 ? 0.7575 0.4759 0.3957 -0.0352 -0.1142 -0.0581 901  TRP   B CZ3 
3588 C CH2 . TRP   B 208 ? 0.7770 0.4706 0.3829 -0.0337 -0.0868 -0.0589 901  TRP   B CH2 
3589 N N   . SER   B 209 ? 0.6053 0.4909 0.4617 -0.0212 -0.0853 -0.0236 902  SER   B N   
3590 C CA  . SER   B 209 ? 0.6062 0.4977 0.4711 -0.0221 -0.0703 -0.0194 902  SER   B CA  
3591 C C   . SER   B 209 ? 0.5752 0.4930 0.4784 -0.0233 -0.0625 -0.0197 902  SER   B C   
3592 O O   . SER   B 209 ? 0.5698 0.4926 0.4811 -0.0260 -0.0488 -0.0187 902  SER   B O   
3593 C CB  . SER   B 209 ? 0.6351 0.5246 0.4963 -0.0185 -0.0780 -0.0135 902  SER   B CB  
3594 O OG  . SER   B 209 ? 0.7143 0.5782 0.5394 -0.0155 -0.0886 -0.0121 902  SER   B OG  
3595 N N   . TYR   B 210 ? 0.5585 0.4931 0.4855 -0.0217 -0.0719 -0.0205 903  TYR   B N   
3596 C CA  . TYR   B 210 ? 0.5371 0.4916 0.4946 -0.0221 -0.0665 -0.0202 903  TYR   B CA  
3597 C C   . TYR   B 210 ? 0.5470 0.4975 0.5048 -0.0232 -0.0555 -0.0242 903  TYR   B C   
3598 O O   . TYR   B 210 ? 0.5437 0.5065 0.5203 -0.0228 -0.0466 -0.0227 903  TYR   B O   
3599 C CB  . TYR   B 210 ? 0.5191 0.4873 0.4967 -0.0211 -0.0772 -0.0198 903  TYR   B CB  
3600 C CG  . TYR   B 210 ? 0.5137 0.4959 0.5154 -0.0216 -0.0720 -0.0189 903  TYR   B CG  
3601 C CD1 . TYR   B 210 ? 0.5119 0.5053 0.5266 -0.0205 -0.0685 -0.0146 903  TYR   B CD1 
3602 C CD2 . TYR   B 210 ? 0.5174 0.4967 0.5238 -0.0232 -0.0710 -0.0223 903  TYR   B CD2 
3603 C CE1 . TYR   B 210 ? 0.5085 0.5107 0.5397 -0.0204 -0.0655 -0.0131 903  TYR   B CE1 
3604 C CE2 . TYR   B 210 ? 0.5175 0.5051 0.5420 -0.0226 -0.0666 -0.0204 903  TYR   B CE2 
3605 C CZ  . TYR   B 210 ? 0.5195 0.5190 0.5560 -0.0210 -0.0645 -0.0154 903  TYR   B CZ  
3606 O OH  . TYR   B 210 ? 0.5360 0.5402 0.5854 -0.0199 -0.0623 -0.0128 903  TYR   B OH  
3607 N N   . GLY   B 211 ? 0.5535 0.4856 0.4896 -0.0238 -0.0566 -0.0295 904  GLY   B N   
3608 C CA  . GLY   B 211 ? 0.5615 0.4839 0.4926 -0.0229 -0.0442 -0.0343 904  GLY   B CA  
3609 C C   . GLY   B 211 ? 0.5689 0.4889 0.4951 -0.0225 -0.0264 -0.0333 904  GLY   B C   
3610 O O   . GLY   B 211 ? 0.5628 0.4916 0.5073 -0.0197 -0.0137 -0.0342 904  GLY   B O   
3611 N N   . VAL   B 212 ? 0.5801 0.4882 0.4832 -0.0251 -0.0250 -0.0311 905  VAL   B N   
3612 C CA  . VAL   B 212 ? 0.5950 0.5005 0.4936 -0.0274 -0.0068 -0.0293 905  VAL   B CA  
3613 C C   . VAL   B 212 ? 0.5836 0.5177 0.5201 -0.0293 -0.0040 -0.0244 905  VAL   B C   
3614 O O   . VAL   B 212 ? 0.5812 0.5260 0.5349 -0.0305 0.0113  -0.0241 905  VAL   B O   
3615 C CB  . VAL   B 212 ? 0.6328 0.5120 0.4910 -0.0307 -0.0068 -0.0272 905  VAL   B CB  
3616 C CG1 . VAL   B 212 ? 0.6387 0.5149 0.4938 -0.0357 0.0146  -0.0247 905  VAL   B CG1 
3617 C CG2 . VAL   B 212 ? 0.6638 0.5117 0.4798 -0.0292 -0.0117 -0.0323 905  VAL   B CG2 
3618 N N   . THR   B 213 ? 0.5727 0.5196 0.5237 -0.0292 -0.0188 -0.0210 906  THR   B N   
3619 C CA  . THR   B 213 ? 0.5585 0.5274 0.5387 -0.0313 -0.0200 -0.0170 906  THR   B CA  
3620 C C   . THR   B 213 ? 0.5528 0.5410 0.5637 -0.0276 -0.0175 -0.0179 906  THR   B C   
3621 O O   . THR   B 213 ? 0.5394 0.5445 0.5739 -0.0295 -0.0121 -0.0158 906  THR   B O   
3622 C CB  . THR   B 213 ? 0.5617 0.5321 0.5408 -0.0306 -0.0345 -0.0140 906  THR   B CB  
3623 O OG1 . THR   B 213 ? 0.5859 0.5369 0.5370 -0.0319 -0.0366 -0.0126 906  THR   B OG1 
3624 C CG2 . THR   B 213 ? 0.5430 0.5296 0.5436 -0.0331 -0.0369 -0.0108 906  THR   B CG2 
3625 N N   . VAL   B 214 ? 0.5544 0.5389 0.5650 -0.0226 -0.0222 -0.0207 907  VAL   B N   
3626 C CA  . VAL   B 214 ? 0.5432 0.5391 0.5773 -0.0174 -0.0200 -0.0211 907  VAL   B CA  
3627 C C   . VAL   B 214 ? 0.5411 0.5380 0.5819 -0.0145 -0.0031 -0.0236 907  VAL   B C   
3628 O O   . VAL   B 214 ? 0.5263 0.5425 0.5967 -0.0111 0.0008  -0.0214 907  VAL   B O   
3629 C CB  . VAL   B 214 ? 0.5547 0.5401 0.5821 -0.0145 -0.0275 -0.0239 907  VAL   B CB  
3630 C CG1 . VAL   B 214 ? 0.5533 0.5418 0.5979 -0.0079 -0.0227 -0.0246 907  VAL   B CG1 
3631 C CG2 . VAL   B 214 ? 0.5516 0.5428 0.5826 -0.0168 -0.0409 -0.0204 907  VAL   B CG2 
3632 N N   . TRP   B 215 ? 0.5503 0.5267 0.5635 -0.0156 0.0073  -0.0279 908  TRP   B N   
3633 C CA  . TRP   B 215 ? 0.5512 0.5249 0.5658 -0.0128 0.0281  -0.0307 908  TRP   B CA  
3634 C C   . TRP   B 215 ? 0.5516 0.5484 0.5928 -0.0177 0.0372  -0.0261 908  TRP   B C   
3635 O O   . TRP   B 215 ? 0.5468 0.5601 0.6160 -0.0135 0.0510  -0.0262 908  TRP   B O   
3636 C CB  . TRP   B 215 ? 0.5674 0.5080 0.5367 -0.0146 0.0366  -0.0357 908  TRP   B CB  
3637 C CG  . TRP   B 215 ? 0.5709 0.5039 0.5367 -0.0106 0.0616  -0.0394 908  TRP   B CG  
3638 C CD1 . TRP   B 215 ? 0.5869 0.5067 0.5475 -0.0019 0.0721  -0.0455 908  TRP   B CD1 
3639 C CD2 . TRP   B 215 ? 0.5707 0.5090 0.5404 -0.0151 0.0819  -0.0372 908  TRP   B CD2 
3640 N NE1 . TRP   B 215 ? 0.5895 0.5069 0.5509 0.0011  0.0987  -0.0474 908  TRP   B NE1 
3641 C CE2 . TRP   B 215 ? 0.5814 0.5122 0.5506 -0.0077 0.1057  -0.0421 908  TRP   B CE2 
3642 C CE3 . TRP   B 215 ? 0.5681 0.5154 0.5417 -0.0251 0.0834  -0.0316 908  TRP   B CE3 
3643 C CZ2 . TRP   B 215 ? 0.5823 0.5174 0.5575 -0.0103 0.1322  -0.0412 908  TRP   B CZ2 
3644 C CZ3 . TRP   B 215 ? 0.5724 0.5234 0.5524 -0.0294 0.1080  -0.0305 908  TRP   B CZ3 
3645 C CH2 . TRP   B 215 ? 0.5769 0.5231 0.5583 -0.0222 0.1328  -0.0351 908  TRP   B CH2 
3646 N N   . GLU   B 216 ? 0.5532 0.5511 0.5875 -0.0265 0.0297  -0.0222 909  GLU   B N   
3647 C CA  . GLU   B 216 ? 0.5418 0.5593 0.6001 -0.0343 0.0356  -0.0181 909  GLU   B CA  
3648 C C   . GLU   B 216 ? 0.5246 0.5733 0.6267 -0.0316 0.0265  -0.0152 909  GLU   B C   
3649 O O   . GLU   B 216 ? 0.5109 0.5827 0.6459 -0.0342 0.0349  -0.0135 909  GLU   B O   
3650 C CB  . GLU   B 216 ? 0.5709 0.5773 0.6085 -0.0436 0.0261  -0.0148 909  GLU   B CB  
3651 C CG  . GLU   B 216 ? 0.6328 0.6084 0.6277 -0.0477 0.0345  -0.0154 909  GLU   B CG  
3652 C CD  . GLU   B 216 ? 0.6917 0.6551 0.6683 -0.0545 0.0239  -0.0115 909  GLU   B CD  
3653 O OE1 . GLU   B 216 ? 0.6770 0.6297 0.6367 -0.0498 0.0081  -0.0114 909  GLU   B OE1 
3654 O OE2 . GLU   B 216 ? 0.7204 0.6848 0.7012 -0.0645 0.0322  -0.0085 909  GLU   B OE2 
3655 N N   . LEU   B 217 ? 0.5247 0.5742 0.6275 -0.0269 0.0090  -0.0143 910  LEU   B N   
3656 C CA  . LEU   B 217 ? 0.5134 0.5863 0.6491 -0.0239 -0.0023 -0.0108 910  LEU   B CA  
3657 C C   . LEU   B 217 ? 0.5177 0.6036 0.6804 -0.0130 0.0053  -0.0116 910  LEU   B C   
3658 O O   . LEU   B 217 ? 0.4959 0.6080 0.6954 -0.0117 0.0034  -0.0085 910  LEU   B O   
3659 C CB  . LEU   B 217 ? 0.5171 0.5817 0.6399 -0.0219 -0.0199 -0.0092 910  LEU   B CB  
3660 C CG  . LEU   B 217 ? 0.5354 0.5872 0.6336 -0.0293 -0.0279 -0.0083 910  LEU   B CG  
3661 C CD1 . LEU   B 217 ? 0.5390 0.5851 0.6290 -0.0257 -0.0409 -0.0068 910  LEU   B CD1 
3662 C CD2 . LEU   B 217 ? 0.5318 0.5929 0.6389 -0.0391 -0.0299 -0.0058 910  LEU   B CD2 
3663 N N   . MET   B 218 ? 0.5430 0.6098 0.6878 -0.0049 0.0131  -0.0160 911  MET   B N   
3664 C CA  . MET   B 218 ? 0.5495 0.6206 0.7134 0.0078  0.0224  -0.0177 911  MET   B CA  
3665 C C   . MET   B 218 ? 0.5462 0.6333 0.7345 0.0097  0.0435  -0.0188 911  MET   B C   
3666 O O   . MET   B 218 ? 0.5297 0.6320 0.7491 0.0214  0.0501  -0.0184 911  MET   B O   
3667 C CB  . MET   B 218 ? 0.5957 0.6355 0.7272 0.0135  0.0255  -0.0233 911  MET   B CB  
3668 C CG  . MET   B 218 ? 0.6568 0.6842 0.7712 0.0112  0.0070  -0.0220 911  MET   B CG  
3669 S SD  . MET   B 218 ? 0.7735 0.8181 0.9160 0.0168  -0.0092 -0.0148 911  MET   B SD  
3670 C CE  . MET   B 218 ? 0.7661 0.7866 0.8793 0.0130  -0.0213 -0.0154 911  MET   B CE  
3671 N N   . THR   B 219 ? 0.5630 0.6457 0.7373 -0.0008 0.0555  -0.0199 912  THR   B N   
3672 C CA  . THR   B 219 ? 0.5616 0.6607 0.7600 -0.0020 0.0787  -0.0202 912  THR   B CA  
3673 C C   . THR   B 219 ? 0.5547 0.6885 0.7933 -0.0129 0.0732  -0.0145 912  THR   B C   
3674 O O   . THR   B 219 ? 0.5478 0.6997 0.8121 -0.0172 0.0923  -0.0140 912  THR   B O   
3675 C CB  . THR   B 219 ? 0.5967 0.6654 0.7519 -0.0079 0.0981  -0.0244 912  THR   B CB  
3676 O OG1 . THR   B 219 ? 0.6234 0.6772 0.7481 -0.0205 0.0854  -0.0223 912  THR   B OG1 
3677 C CG2 . THR   B 219 ? 0.6237 0.6584 0.7415 0.0024  0.1058  -0.0312 912  THR   B CG2 
3678 N N   . PHE   B 220 ? 0.5569 0.6981 0.7992 -0.0185 0.0481  -0.0107 913  PHE   B N   
3679 C CA  . PHE   B 220 ? 0.5479 0.7160 0.8210 -0.0302 0.0367  -0.0061 913  PHE   B CA  
3680 C C   . PHE   B 220 ? 0.5712 0.7315 0.8295 -0.0474 0.0472  -0.0059 913  PHE   B C   
3681 O O   . PHE   B 220 ? 0.5558 0.7414 0.8483 -0.0585 0.0501  -0.0033 913  PHE   B O   
3682 C CB  . PHE   B 220 ? 0.5097 0.7187 0.8432 -0.0240 0.0372  -0.0032 913  PHE   B CB  
3683 C CG  . PHE   B 220 ? 0.5083 0.7215 0.8535 -0.0071 0.0223  -0.0017 913  PHE   B CG  
3684 C CD1 . PHE   B 220 ? 0.5177 0.7343 0.8632 -0.0084 -0.0050 0.0023  913  PHE   B CD1 
3685 C CD2 . PHE   B 220 ? 0.5178 0.7253 0.8671 0.0100  0.0364  -0.0043 913  PHE   B CD2 
3686 C CE1 . PHE   B 220 ? 0.5222 0.7376 0.8734 0.0068  -0.0180 0.0048  913  PHE   B CE1 
3687 C CE2 . PHE   B 220 ? 0.5248 0.7305 0.8807 0.0254  0.0229  -0.0023 913  PHE   B CE2 
3688 C CZ  . PHE   B 220 ? 0.5184 0.7283 0.8754 0.0235  -0.0042 0.0028  913  PHE   B CZ  
3689 N N   . GLY   B 221 ? 0.6043 0.7287 0.8117 -0.0501 0.0509  -0.0082 914  GLY   B N   
3690 C CA  . GLY   B 221 ? 0.6300 0.7374 0.8127 -0.0649 0.0589  -0.0073 914  GLY   B CA  
3691 C C   . GLY   B 221 ? 0.6560 0.7485 0.8217 -0.0671 0.0870  -0.0090 914  GLY   B C   
3692 O O   . GLY   B 221 ? 0.6737 0.7578 0.8293 -0.0811 0.0973  -0.0069 914  GLY   B O   
3693 N N   . SER   B 222 ? 0.6648 0.7488 0.8220 -0.0540 0.1005  -0.0130 915  SER   B N   
3694 C CA  . SER   B 222 ? 0.6899 0.7526 0.8215 -0.0553 0.1291  -0.0154 915  SER   B CA  
3695 C C   . SER   B 222 ? 0.7318 0.7502 0.7999 -0.0615 0.1267  -0.0155 915  SER   B C   
3696 O O   . SER   B 222 ? 0.7449 0.7477 0.7879 -0.0587 0.1041  -0.0157 915  SER   B O   
3697 C CB  . SER   B 222 ? 0.7078 0.7649 0.8378 -0.0390 0.1429  -0.0208 915  SER   B CB  
3698 O OG  . SER   B 222 ? 0.7037 0.8009 0.8940 -0.0318 0.1510  -0.0200 915  SER   B OG  
3699 N N   . LYS   B 223 ? 0.7508 0.7487 0.7933 -0.0694 0.1504  -0.0148 916  LYS   B N   
3700 C CA  . LYS   B 223 ? 0.7976 0.7498 0.7761 -0.0742 0.1483  -0.0139 916  LYS   B CA  
3701 C C   . LYS   B 223 ? 0.8371 0.7559 0.7696 -0.0624 0.1518  -0.0196 916  LYS   B C   
3702 O O   . LYS   B 223 ? 0.8426 0.7581 0.7747 -0.0570 0.1755  -0.0235 916  LYS   B O   
3703 C CB  . LYS   B 223 ? 0.8248 0.7642 0.7905 -0.0893 0.1718  -0.0095 916  LYS   B CB  
3704 C CG  . LYS   B 223 ? 0.8392 0.8085 0.8486 -0.1039 0.1667  -0.0045 916  LYS   B CG  
3705 C CD  . LYS   B 223 ? 0.8963 0.8549 0.8987 -0.1209 0.1936  -0.0002 916  LYS   B CD  
3706 N N   . PRO   B 224 ? 0.8629 0.7578 0.7585 -0.0582 0.1278  -0.0206 917  PRO   B N   
3707 C CA  . PRO   B 224 ? 0.8974 0.7602 0.7492 -0.0490 0.1263  -0.0267 917  PRO   B CA  
3708 C C   . PRO   B 224 ? 0.9531 0.7727 0.7475 -0.0521 0.1478  -0.0277 917  PRO   B C   
3709 O O   . PRO   B 224 ? 0.9768 0.7758 0.7421 -0.0610 0.1497  -0.0222 917  PRO   B O   
3710 C CB  . PRO   B 224 ? 0.9084 0.7622 0.7428 -0.0466 0.0940  -0.0259 917  PRO   B CB  
3711 C CG  . PRO   B 224 ? 0.9047 0.7669 0.7487 -0.0550 0.0854  -0.0190 917  PRO   B CG  
3712 C CD  . PRO   B 224 ? 0.8547 0.7510 0.7484 -0.0615 0.1011  -0.0166 917  PRO   B CD  
3713 N N   . TYR   B 225 ? 0.9741 0.7754 0.7477 -0.0445 0.1645  -0.0346 918  TYR   B N   
3714 C CA  . TYR   B 225 ? 1.0264 0.7818 0.7393 -0.0462 0.1881  -0.0368 918  TYR   B CA  
3715 C C   . TYR   B 225 ? 1.0585 0.8181 0.7794 -0.0573 0.2173  -0.0305 918  TYR   B C   
3716 O O   . TYR   B 225 ? 1.0926 0.8150 0.7618 -0.0652 0.2225  -0.0262 918  TYR   B O   
3717 C CB  . TYR   B 225 ? 1.0535 0.7608 0.6956 -0.0470 0.1662  -0.0369 918  TYR   B CB  
3718 C CG  . TYR   B 225 ? 1.0490 0.7588 0.6914 -0.0404 0.1313  -0.0408 918  TYR   B CG  
3719 C CD1 . TYR   B 225 ? 1.0655 0.7564 0.6865 -0.0330 0.1288  -0.0500 918  TYR   B CD1 
3720 C CD2 . TYR   B 225 ? 1.0412 0.7669 0.6998 -0.0422 0.1019  -0.0356 918  TYR   B CD2 
3721 C CE1 . TYR   B 225 ? 1.0694 0.7618 0.6911 -0.0298 0.0973  -0.0533 918  TYR   B CE1 
3722 C CE2 . TYR   B 225 ? 1.0482 0.7778 0.7097 -0.0373 0.0723  -0.0387 918  TYR   B CE2 
3723 C CZ  . TYR   B 225 ? 1.0689 0.7823 0.7124 -0.0321 0.0696  -0.0474 918  TYR   B CZ  
3724 O OH  . TYR   B 225 ? 1.0869 0.8051 0.7359 -0.0298 0.0407  -0.0502 918  TYR   B OH  
3725 N N   . ASP   B 226 ? 1.0425 0.8483 0.8303 -0.0586 0.2346  -0.0293 919  ASP   B N   
3726 C CA  . ASP   B 226 ? 1.0577 0.8758 0.8657 -0.0716 0.2615  -0.0232 919  ASP   B CA  
3727 C C   . ASP   B 226 ? 1.1060 0.8858 0.8663 -0.0740 0.2997  -0.0245 919  ASP   B C   
3728 O O   . ASP   B 226 ? 1.1151 0.8889 0.8713 -0.0632 0.3205  -0.0313 919  ASP   B O   
3729 C CB  . ASP   B 226 ? 1.0370 0.9175 0.9331 -0.0722 0.2682  -0.0219 919  ASP   B CB  
3730 C CG  . ASP   B 226 ? 1.0822 0.9869 1.0124 -0.0900 0.2693  -0.0140 919  ASP   B CG  
3731 O OD1 . ASP   B 226 ? 1.1188 0.9893 1.0046 -0.1026 0.2789  -0.0093 919  ASP   B OD1 
3732 O OD2 . ASP   B 226 ? 1.0735 1.0279 1.0717 -0.0919 0.2595  -0.0123 919  ASP   B OD2 
3733 N N   . GLY   B 227 ? 1.1385 0.8885 0.8594 -0.0878 0.3096  -0.0178 920  GLY   B N   
3734 C CA  . GLY   B 227 ? 1.1852 0.8924 0.8522 -0.0924 0.3475  -0.0173 920  GLY   B CA  
3735 C C   . GLY   B 227 ? 1.2492 0.8872 0.8184 -0.0886 0.3365  -0.0188 920  GLY   B C   
3736 O O   . GLY   B 227 ? 1.2920 0.8834 0.8008 -0.0966 0.3590  -0.0148 920  GLY   B O   
3737 N N   . ILE   B 228 ? 1.2524 0.8826 0.8050 -0.0769 0.3016  -0.0243 921  ILE   B N   
3738 C CA  . ILE   B 228 ? 1.3010 0.8710 0.7673 -0.0728 0.2828  -0.0262 921  ILE   B CA  
3739 C C   . ILE   B 228 ? 1.3191 0.8701 0.7575 -0.0811 0.2591  -0.0166 921  ILE   B C   
3740 O O   . ILE   B 228 ? 1.2917 0.8793 0.7786 -0.0827 0.2344  -0.0129 921  ILE   B O   
3741 C CB  . ILE   B 228 ? 1.2987 0.8759 0.7707 -0.0599 0.2517  -0.0350 921  ILE   B CB  
3742 C CG1 . ILE   B 228 ? 1.2938 0.8858 0.7924 -0.0502 0.2757  -0.0446 921  ILE   B CG1 
3743 C CG2 . ILE   B 228 ? 1.3490 0.8698 0.7391 -0.0568 0.2259  -0.0371 921  ILE   B CG2 
3744 N N   . PRO   B 229 ? 1.3644 0.8556 0.7229 -0.0860 0.2677  -0.0119 922  PRO   B N   
3745 C CA  . PRO   B 229 ? 1.3817 0.8497 0.7099 -0.0915 0.2441  -0.0021 922  PRO   B CA  
3746 C C   . PRO   B 229 ? 1.3827 0.8514 0.7041 -0.0808 0.1958  -0.0039 922  PRO   B C   
3747 O O   . PRO   B 229 ? 1.3930 0.8539 0.6976 -0.0714 0.1820  -0.0123 922  PRO   B O   
3748 C CB  . PRO   B 229 ? 1.4439 0.8411 0.6795 -0.0967 0.2654  0.0026  922  PRO   B CB  
3749 C CG  . PRO   B 229 ? 1.4551 0.8460 0.6836 -0.0966 0.3079  -0.0044 922  PRO   B CG  
3750 C CD  . PRO   B 229 ? 1.4007 0.8375 0.6868 -0.0853 0.2979  -0.0153 922  PRO   B CD  
3751 N N   . ALA   B 230 ? 1.3692 0.8474 0.7058 -0.0825 0.1711  0.0036  923  ALA   B N   
3752 C CA  . ALA   B 230 ? 1.3707 0.8545 0.7087 -0.0721 0.1274  0.0028  923  ALA   B CA  
3753 C C   . ALA   B 230 ? 1.4143 0.8431 0.6723 -0.0650 0.1077  0.0020  923  ALA   B C   
3754 O O   . ALA   B 230 ? 1.4096 0.8472 0.6724 -0.0561 0.0757  -0.0027 923  ALA   B O   
3755 C CB  . ALA   B 230 ? 1.3619 0.8586 0.7235 -0.0743 0.1102  0.0115  923  ALA   B CB  
3756 N N   . SER   B 231 ? 1.4560 0.8274 0.6399 -0.0697 0.1269  0.0064  924  SER   B N   
3757 C CA  . SER   B 231 ? 1.5060 0.8177 0.6038 -0.0638 0.1089  0.0060  924  SER   B CA  
3758 C C   . SER   B 231 ? 1.5132 0.8186 0.5948 -0.0589 0.1083  -0.0068 924  SER   B C   
3759 O O   . SER   B 231 ? 1.5488 0.8163 0.5732 -0.0533 0.0813  -0.0095 924  SER   B O   
3760 C CB  . SER   B 231 ? 1.5679 0.8162 0.5870 -0.0711 0.1346  0.0143  924  SER   B CB  
3761 O OG  . SER   B 231 ? 1.5921 0.8389 0.6127 -0.0796 0.1823  0.0105  924  SER   B OG  
3762 N N   . GLU   B 232 ? 1.4788 0.8190 0.6092 -0.0608 0.1365  -0.0148 925  GLU   B N   
3763 C CA  . GLU   B 232 ? 1.4896 0.8204 0.6045 -0.0558 0.1398  -0.0275 925  GLU   B CA  
3764 C C   . GLU   B 232 ? 1.4372 0.8186 0.6183 -0.0497 0.1136  -0.0351 925  GLU   B C   
3765 O O   . GLU   B 232 ? 1.4506 0.8214 0.6179 -0.0458 0.1122  -0.0458 925  GLU   B O   
3766 C CB  . GLU   B 232 ? 1.5375 0.8647 0.6541 -0.0592 0.1909  -0.0319 925  GLU   B CB  
3767 C CG  . GLU   B 232 ? 1.6719 0.9463 0.7206 -0.0667 0.2228  -0.0247 925  GLU   B CG  
3768 C CD  . GLU   B 232 ? 1.7908 1.0691 0.8520 -0.0706 0.2775  -0.0278 925  GLU   B CD  
3769 O OE1 . GLU   B 232 ? 1.7836 1.0989 0.8974 -0.0648 0.2899  -0.0371 925  GLU   B OE1 
3770 O OE2 . GLU   B 232 ? 1.8623 1.1066 0.8821 -0.0792 0.3089  -0.0206 925  GLU   B OE2 
3771 N N   . ILE   B 233 ? 1.3799 0.8116 0.6282 -0.0492 0.0942  -0.0297 926  ILE   B N   
3772 C CA  . ILE   B 233 ? 1.3306 0.8114 0.6440 -0.0445 0.0721  -0.0352 926  ILE   B CA  
3773 C C   . ILE   B 233 ? 1.3405 0.8023 0.6235 -0.0401 0.0356  -0.0414 926  ILE   B C   
3774 O O   . ILE   B 233 ? 1.3345 0.8078 0.6357 -0.0380 0.0330  -0.0509 926  ILE   B O   
3775 C CB  . ILE   B 233 ? 1.2891 0.8197 0.6699 -0.0454 0.0604  -0.0273 926  ILE   B CB  
3776 C CG1 . ILE   B 233 ? 1.2751 0.8321 0.6975 -0.0517 0.0951  -0.0236 926  ILE   B CG1 
3777 C CG2 . ILE   B 233 ? 1.2560 0.8310 0.6949 -0.0406 0.0347  -0.0315 926  ILE   B CG2 
3778 C CD1 . ILE   B 233 ? 1.2669 0.8506 0.7292 -0.0501 0.1197  -0.0316 926  ILE   B CD1 
3779 N N   . SER   B 234 ? 1.3571 0.7888 0.5940 -0.0388 0.0073  -0.0360 927  SER   B N   
3780 C CA  . SER   B 234 ? 1.3703 0.7875 0.5826 -0.0359 -0.0313 -0.0410 927  SER   B CA  
3781 C C   . SER   B 234 ? 1.4036 0.7781 0.5599 -0.0376 -0.0249 -0.0528 927  SER   B C   
3782 O O   . SER   B 234 ? 1.3933 0.7776 0.5641 -0.0376 -0.0460 -0.0614 927  SER   B O   
3783 C CB  . SER   B 234 ? 1.4083 0.7978 0.5780 -0.0328 -0.0615 -0.0318 927  SER   B CB  
3784 O OG  . SER   B 234 ? 1.4888 0.8144 0.5717 -0.0346 -0.0482 -0.0291 927  SER   B OG  
3785 N N   . SER   B 235 ? 1.4409 0.7661 0.5326 -0.0396 0.0057  -0.0536 928  SER   B N   
3786 C CA  . SER   B 235 ? 1.4799 0.7576 0.5108 -0.0404 0.0162  -0.0656 928  SER   B CA  
3787 C C   . SER   B 235 ? 1.4416 0.7499 0.5239 -0.0389 0.0411  -0.0756 928  SER   B C   
3788 O O   . SER   B 235 ? 1.4636 0.7506 0.5227 -0.0386 0.0337  -0.0872 928  SER   B O   
3789 C CB  . SER   B 235 ? 1.5626 0.7765 0.5071 -0.0424 0.0454  -0.0632 928  SER   B CB  
3790 O OG  . SER   B 235 ? 1.5963 0.8313 0.5735 -0.0443 0.0862  -0.0560 928  SER   B OG  
3791 N N   . ILE   B 236 ? 1.3837 0.7408 0.5357 -0.0379 0.0680  -0.0709 929  ILE   B N   
3792 C CA  . ILE   B 236 ? 1.3407 0.7323 0.5495 -0.0343 0.0898  -0.0782 929  ILE   B CA  
3793 C C   . ILE   B 236 ? 1.2962 0.7216 0.5531 -0.0331 0.0556  -0.0829 929  ILE   B C   
3794 O O   . ILE   B 236 ? 1.2976 0.7194 0.5606 -0.0306 0.0606  -0.0931 929  ILE   B O   
3795 C CB  . ILE   B 236 ? 1.3131 0.7495 0.5844 -0.0345 0.1225  -0.0704 929  ILE   B CB  
3796 C CG1 . ILE   B 236 ? 1.3456 0.7569 0.5902 -0.0332 0.1707  -0.0739 929  ILE   B CG1 
3797 C CG2 . ILE   B 236 ? 1.2665 0.7687 0.6307 -0.0315 0.1162  -0.0700 929  ILE   B CG2 
3798 N N   . LEU   B 237 ? 1.2600 0.7138 0.5469 -0.0349 0.0220  -0.0756 930  LEU   B N   
3799 C CA  . LEU   B 237 ? 1.2239 0.7105 0.5569 -0.0353 -0.0093 -0.0786 930  LEU   B CA  
3800 C C   . LEU   B 237 ? 1.2579 0.7040 0.5383 -0.0385 -0.0356 -0.0882 930  LEU   B C   
3801 O O   . LEU   B 237 ? 1.2474 0.7054 0.5531 -0.0401 -0.0466 -0.0958 930  LEU   B O   
3802 C CB  . LEU   B 237 ? 1.1852 0.7111 0.5623 -0.0353 -0.0348 -0.0680 930  LEU   B CB  
3803 C CG  . LEU   B 237 ? 1.1456 0.7153 0.5814 -0.0338 -0.0151 -0.0596 930  LEU   B CG  
3804 C CD1 . LEU   B 237 ? 1.1269 0.7227 0.5908 -0.0330 -0.0401 -0.0502 930  LEU   B CD1 
3805 C CD2 . LEU   B 237 ? 1.1111 0.7193 0.6076 -0.0319 -0.0005 -0.0638 930  LEU   B CD2 
3806 N N   . GLU   B 238 ? 1.3007 0.6956 0.5048 -0.0404 -0.0463 -0.0878 931  GLU   B N   
3807 C CA  . GLU   B 238 ? 1.3457 0.6959 0.4909 -0.0449 -0.0738 -0.0972 931  GLU   B CA  
3808 C C   . GLU   B 238 ? 1.3665 0.6781 0.4741 -0.0453 -0.0496 -0.1111 931  GLU   B C   
3809 O O   . GLU   B 238 ? 1.3880 0.6761 0.4709 -0.0503 -0.0723 -0.1213 931  GLU   B O   
3810 C CB  . GLU   B 238 ? 1.4260 0.7293 0.4961 -0.0458 -0.0941 -0.0921 931  GLU   B CB  
3811 C CG  . GLU   B 238 ? 1.4885 0.8272 0.5963 -0.0446 -0.1322 -0.0816 931  GLU   B CG  
3812 C CD  . GLU   B 238 ? 1.6295 0.9306 0.6762 -0.0419 -0.1470 -0.0721 931  GLU   B CD  
3813 O OE1 . GLU   B 238 ? 1.6595 0.9426 0.6813 -0.0394 -0.1165 -0.0652 931  GLU   B OE1 
3814 O OE2 . GLU   B 238 ? 1.6812 0.9713 0.7069 -0.0424 -0.1897 -0.0711 931  GLU   B OE2 
3815 N N   . LYS   B 239 ? 1.3579 0.6651 0.4658 -0.0399 -0.0038 -0.1117 932  LYS   B N   
3816 C CA  . LYS   B 239 ? 1.3721 0.6474 0.4535 -0.0369 0.0249  -0.1244 932  LYS   B CA  
3817 C C   . LYS   B 239 ? 1.3277 0.6469 0.4839 -0.0340 0.0276  -0.1291 932  LYS   B C   
3818 O O   . LYS   B 239 ? 1.3491 0.6437 0.4897 -0.0298 0.0491  -0.1397 932  LYS   B O   
3819 C CB  . LYS   B 239 ? 1.4117 0.6700 0.4719 -0.0310 0.0752  -0.1225 932  LYS   B CB  
3820 C CG  . LYS   B 239 ? 1.5370 0.7401 0.5117 -0.0338 0.0816  -0.1187 932  LYS   B CG  
3821 C CD  . LYS   B 239 ? 1.6200 0.8076 0.5783 -0.0291 0.1372  -0.1176 932  LYS   B CD  
3822 C CE  . LYS   B 239 ? 1.6192 0.8739 0.6669 -0.0269 0.1607  -0.1070 932  LYS   B CE  
3823 N NZ  . LYS   B 239 ? 1.6077 0.9059 0.7283 -0.0195 0.1801  -0.1126 932  LYS   B NZ  
3824 N N   . GLY   B 240 ? 1.2653 0.6454 0.4988 -0.0351 0.0088  -0.1209 933  GLY   B N   
3825 C CA  . GLY   B 240 ? 1.2143 0.6344 0.5157 -0.0329 0.0092  -0.1234 933  GLY   B CA  
3826 C C   . GLY   B 240 ? 1.1588 0.6206 0.5208 -0.0240 0.0432  -0.1179 933  GLY   B C   
3827 O O   . GLY   B 240 ? 1.1322 0.6198 0.5430 -0.0200 0.0477  -0.1201 933  GLY   B O   
3828 N N   . GLU   B 241 ? 1.1389 0.6058 0.4970 -0.0216 0.0665  -0.1104 934  GLU   B N   
3829 C CA  . GLU   B 241 ? 1.0891 0.5985 0.5070 -0.0152 0.0966  -0.1045 934  GLU   B CA  
3830 C C   . GLU   B 241 ? 1.0277 0.5942 0.5131 -0.0178 0.0765  -0.0940 934  GLU   B C   
3831 O O   . GLU   B 241 ? 1.0287 0.5986 0.5053 -0.0236 0.0530  -0.0877 934  GLU   B O   
3832 C CB  . GLU   B 241 ? 1.1312 0.6225 0.5185 -0.0144 0.1301  -0.1007 934  GLU   B CB  
3833 C CG  . GLU   B 241 ? 1.2285 0.6572 0.5401 -0.0115 0.1536  -0.1111 934  GLU   B CG  
3834 N N   . ARG   B 242 ? 0.9753 0.5838 0.5257 -0.0125 0.0849  -0.0924 935  ARG   B N   
3835 C CA  . ARG   B 242 ? 0.9275 0.5887 0.5417 -0.0142 0.0692  -0.0831 935  ARG   B CA  
3836 C C   . ARG   B 242 ? 0.9016 0.6012 0.5695 -0.0091 0.0953  -0.0776 935  ARG   B C   
3837 O O   . ARG   B 242 ? 0.9159 0.6047 0.5774 -0.0034 0.1255  -0.0812 935  ARG   B O   
3838 C CB  . ARG   B 242 ? 0.9043 0.5801 0.5471 -0.0144 0.0452  -0.0860 935  ARG   B CB  
3839 C CG  . ARG   B 242 ? 0.9249 0.5741 0.5292 -0.0218 0.0146  -0.0903 935  ARG   B CG  
3840 C CD  . ARG   B 242 ? 0.9180 0.5786 0.5195 -0.0270 -0.0064 -0.0822 935  ARG   B CD  
3841 N NE  . ARG   B 242 ? 0.9278 0.5709 0.5035 -0.0334 -0.0387 -0.0856 935  ARG   B NE  
3842 C CZ  . ARG   B 242 ? 0.9509 0.5496 0.4629 -0.0367 -0.0485 -0.0901 935  ARG   B CZ  
3843 N NH1 . ARG   B 242 ? 0.9506 0.5397 0.4476 -0.0430 -0.0815 -0.0928 935  ARG   B NH1 
3844 N NH2 . ARG   B 242 ? 0.9594 0.5230 0.4221 -0.0342 -0.0257 -0.0916 935  ARG   B NH2 
3845 N N   . LEU   B 243 ? 0.8640 0.6080 0.5851 -0.0111 0.0840  -0.0692 936  LEU   B N   
3846 C CA  . LEU   B 243 ? 0.8323 0.6156 0.6082 -0.0076 0.1029  -0.0641 936  LEU   B CA  
3847 C C   . LEU   B 243 ? 0.8252 0.6168 0.6293 0.0032  0.1143  -0.0692 936  LEU   B C   
3848 O O   . LEU   B 243 ? 0.8279 0.6115 0.6301 0.0057  0.0979  -0.0733 936  LEU   B O   
3849 C CB  . LEU   B 243 ? 0.7992 0.6212 0.6182 -0.0122 0.0833  -0.0555 936  LEU   B CB  
3850 C CG  . LEU   B 243 ? 0.8184 0.6342 0.6162 -0.0207 0.0770  -0.0495 936  LEU   B CG  
3851 C CD1 . LEU   B 243 ? 0.8041 0.6447 0.6288 -0.0238 0.0518  -0.0437 936  LEU   B CD1 
3852 C CD2 . LEU   B 243 ? 0.8184 0.6409 0.6241 -0.0244 0.1035  -0.0457 936  LEU   B CD2 
3853 N N   . PRO   B 244 ? 0.8145 0.6183 0.6418 0.0100  0.1435  -0.0693 937  PRO   B N   
3854 C CA  . PRO   B 244 ? 0.8110 0.6185 0.6623 0.0234  0.1557  -0.0742 937  PRO   B CA  
3855 C C   . PRO   B 244 ? 0.8017 0.6447 0.7060 0.0277  0.1364  -0.0695 937  PRO   B C   
3856 O O   . PRO   B 244 ? 0.7868 0.6606 0.7201 0.0208  0.1196  -0.0618 937  PRO   B O   
3857 C CB  . PRO   B 244 ? 0.8017 0.6233 0.6754 0.0293  0.1910  -0.0734 937  PRO   B CB  
3858 C CG  . PRO   B 244 ? 0.7943 0.6400 0.6825 0.0168  0.1904  -0.0649 937  PRO   B CG  
3859 C CD  . PRO   B 244 ? 0.8001 0.6153 0.6353 0.0059  0.1676  -0.0648 937  PRO   B CD  
3860 N N   . GLN   B 245 ? 0.8100 0.6437 0.7219 0.0392  0.1388  -0.0742 938  GLN   B N   
3861 C CA  . GLN   B 245 ? 0.7966 0.6573 0.7526 0.0444  0.1220  -0.0692 938  GLN   B CA  
3862 C C   . GLN   B 245 ? 0.7673 0.6759 0.7842 0.0503  0.1307  -0.0614 938  GLN   B C   
3863 O O   . GLN   B 245 ? 0.7664 0.6815 0.8018 0.0611  0.1557  -0.0632 938  GLN   B O   
3864 C CB  . GLN   B 245 ? 0.8252 0.6577 0.7698 0.0560  0.1251  -0.0760 938  GLN   B CB  
3865 C CG  . GLN   B 245 ? 0.8460 0.7005 0.8312 0.0622  0.1088  -0.0699 938  GLN   B CG  
3866 C CD  . GLN   B 245 ? 0.9188 0.7389 0.8870 0.0714  0.1087  -0.0758 938  GLN   B CD  
3867 O OE1 . GLN   B 245 ? 0.9334 0.7644 0.9301 0.0791  0.0997  -0.0709 938  GLN   B OE1 
3868 N NE2 . GLN   B 245 ? 0.9602 0.7340 0.8779 0.0704  0.1177  -0.0865 938  GLN   B NE2 
3869 N N   . PRO   B 246 ? 0.7409 0.6831 0.7898 0.0433  0.1109  -0.0530 939  PRO   B N   
3870 C CA  . PRO   B 246 ? 0.7094 0.6967 0.8159 0.0472  0.1153  -0.0458 939  PRO   B CA  
3871 C C   . PRO   B 246 ? 0.6996 0.6983 0.8417 0.0652  0.1194  -0.0451 939  PRO   B C   
3872 O O   . PRO   B 246 ? 0.7117 0.6883 0.8388 0.0717  0.1091  -0.0472 939  PRO   B O   
3873 C CB  . PRO   B 246 ? 0.7032 0.7118 0.8222 0.0356  0.0893  -0.0386 939  PRO   B CB  
3874 C CG  . PRO   B 246 ? 0.7347 0.7125 0.8041 0.0250  0.0780  -0.0417 939  PRO   B CG  
3875 C CD  . PRO   B 246 ? 0.7393 0.6798 0.7743 0.0319  0.0840  -0.0498 939  PRO   B CD  
3876 N N   . PRO   B 247 ? 0.6737 0.7056 0.8636 0.0737  0.1356  -0.0422 940  PRO   B N   
3877 C CA  . PRO   B 247 ? 0.6573 0.7005 0.8838 0.0941  0.1400  -0.0410 940  PRO   B CA  
3878 C C   . PRO   B 247 ? 0.6521 0.7004 0.8922 0.0991  0.1119  -0.0350 940  PRO   B C   
3879 O O   . PRO   B 247 ? 0.6626 0.6934 0.9022 0.1150  0.1131  -0.0364 940  PRO   B O   
3880 C CB  . PRO   B 247 ? 0.6319 0.7228 0.9183 0.0981  0.1552  -0.0364 940  PRO   B CB  
3881 C CG  . PRO   B 247 ? 0.6433 0.7333 0.9111 0.0812  0.1704  -0.0384 940  PRO   B CG  
3882 C CD  . PRO   B 247 ? 0.6493 0.7100 0.8639 0.0650  0.1507  -0.0395 940  PRO   B CD  
3883 N N   . ILE   B 248 ? 0.6366 0.7042 0.8847 0.0861  0.0880  -0.0284 941  ILE   B N   
3884 C CA  . ILE   B 248 ? 0.6339 0.7046 0.8910 0.0897  0.0627  -0.0219 941  ILE   B CA  
3885 C C   . ILE   B 248 ? 0.6723 0.7018 0.8823 0.0860  0.0521  -0.0250 941  ILE   B C   
3886 O O   . ILE   B 248 ? 0.6757 0.6988 0.8881 0.0917  0.0369  -0.0202 941  ILE   B O   
3887 C CB  . ILE   B 248 ? 0.6163 0.7200 0.8965 0.0775  0.0426  -0.0142 941  ILE   B CB  
3888 C CG1 . ILE   B 248 ? 0.6397 0.7299 0.8827 0.0580  0.0358  -0.0161 941  ILE   B CG1 
3889 C CG2 . ILE   B 248 ? 0.5868 0.7342 0.9196 0.0790  0.0506  -0.0109 941  ILE   B CG2 
3890 C CD1 . ILE   B 248 ? 0.6399 0.7486 0.8926 0.0478  0.0139  -0.0095 941  ILE   B CD1 
3891 N N   . CYS   B 249 ? 0.6980 0.6994 0.8655 0.0757  0.0590  -0.0323 942  CYS   B N   
3892 C CA  . CYS   B 249 ? 0.7256 0.6927 0.8535 0.0691  0.0473  -0.0354 942  CYS   B CA  
3893 C C   . CYS   B 249 ? 0.7470 0.6789 0.8562 0.0802  0.0551  -0.0410 942  CYS   B C   
3894 O O   . CYS   B 249 ? 0.7668 0.6835 0.8668 0.0886  0.0755  -0.0479 942  CYS   B O   
3895 C CB  . CYS   B 249 ? 0.7497 0.7028 0.8419 0.0534  0.0466  -0.0403 942  CYS   B CB  
3896 S SG  . CYS   B 249 ? 0.7575 0.7428 0.8633 0.0393  0.0350  -0.0337 942  CYS   B SG  
3897 N N   . THR   B 250 ? 0.7468 0.6600 0.8438 0.0786  0.0403  -0.0387 943  THR   B N   
3898 C CA  . THR   B 250 ? 0.7643 0.6354 0.8348 0.0850  0.0456  -0.0449 943  THR   B CA  
3899 C C   . THR   B 250 ? 0.7852 0.6262 0.8105 0.0696  0.0454  -0.0544 943  THR   B C   
3900 O O   . THR   B 250 ? 0.7794 0.6352 0.7989 0.0566  0.0395  -0.0542 943  THR   B O   
3901 C CB  . THR   B 250 ? 0.7771 0.6383 0.8515 0.0870  0.0302  -0.0378 943  THR   B CB  
3902 O OG1 . THR   B 250 ? 0.7864 0.6579 0.8553 0.0700  0.0132  -0.0333 943  THR   B OG1 
3903 C CG2 . THR   B 250 ? 0.7577 0.6408 0.8704 0.1049  0.0287  -0.0287 943  THR   B CG2 
3904 N N   . ILE   B 251 ? 0.8096 0.6066 0.8019 0.0711  0.0502  -0.0627 944  ILE   B N   
3905 C CA  . ILE   B 251 ? 0.8378 0.6050 0.7868 0.0559  0.0460  -0.0719 944  ILE   B CA  
3906 C C   . ILE   B 251 ? 0.8321 0.6093 0.7806 0.0377  0.0231  -0.0676 944  ILE   B C   
3907 O O   . ILE   B 251 ? 0.8420 0.6174 0.7706 0.0248  0.0157  -0.0714 944  ILE   B O   
3908 C CB  . ILE   B 251 ? 0.8781 0.5922 0.7888 0.0605  0.0557  -0.0829 944  ILE   B CB  
3909 C CG1 . ILE   B 251 ? 0.9175 0.6027 0.7812 0.0495  0.0579  -0.0940 944  ILE   B CG1 
3910 C CG2 . ILE   B 251 ? 0.8944 0.5837 0.7984 0.0555  0.0426  -0.0817 944  ILE   B CG2 
3911 N N   . ASP   B 252 ? 0.8131 0.6030 0.7850 0.0380  0.0128  -0.0588 945  ASP   B N   
3912 C CA  . ASP   B 252 ? 0.8107 0.6120 0.7870 0.0226  -0.0047 -0.0537 945  ASP   B CA  
3913 C C   . ASP   B 252 ? 0.7809 0.6184 0.7713 0.0161  -0.0108 -0.0494 945  ASP   B C   
3914 O O   . ASP   B 252 ? 0.7891 0.6305 0.7723 0.0025  -0.0223 -0.0500 945  ASP   B O   
3915 C CB  . ASP   B 252 ? 0.8460 0.6506 0.8414 0.0269  -0.0100 -0.0441 945  ASP   B CB  
3916 C CG  . ASP   B 252 ? 0.9544 0.7220 0.9380 0.0370  -0.0030 -0.0463 945  ASP   B CG  
3917 O OD1 . ASP   B 252 ? 0.9703 0.7361 0.9619 0.0549  0.0092  -0.0471 945  ASP   B OD1 
3918 O OD2 . ASP   B 252 ? 1.0087 0.7491 0.9766 0.0270  -0.0090 -0.0472 945  ASP   B OD2 
3919 N N   . VAL   B 253 ? 0.7416 0.6059 0.7541 0.0256  -0.0037 -0.0449 946  VAL   B N   
3920 C CA  . VAL   B 253 ? 0.7132 0.6072 0.7365 0.0194  -0.0084 -0.0411 946  VAL   B CA  
3921 C C   . VAL   B 253 ? 0.7172 0.6012 0.7154 0.0142  -0.0031 -0.0484 946  VAL   B C   
3922 O O   . VAL   B 253 ? 0.7142 0.6042 0.7036 0.0041  -0.0128 -0.0481 946  VAL   B O   
3923 C CB  . VAL   B 253 ? 0.6893 0.6139 0.7447 0.0285  -0.0045 -0.0339 946  VAL   B CB  
3924 C CG1 . VAL   B 253 ? 0.6772 0.6267 0.7393 0.0207  -0.0086 -0.0309 946  VAL   B CG1 
3925 C CG2 . VAL   B 253 ? 0.6850 0.6150 0.7582 0.0336  -0.0130 -0.0259 946  VAL   B CG2 
3926 N N   . TYR   B 254 ? 0.7256 0.5913 0.7099 0.0220  0.0128  -0.0549 947  TYR   B N   
3927 C CA  . TYR   B 254 ? 0.7530 0.6025 0.7058 0.0177  0.0199  -0.0617 947  TYR   B CA  
3928 C C   . TYR   B 254 ? 0.7720 0.5956 0.6900 0.0056  0.0054  -0.0676 947  TYR   B C   
3929 O O   . TYR   B 254 ? 0.7809 0.6032 0.6796 -0.0016 0.0002  -0.0687 947  TYR   B O   
3930 C CB  . TYR   B 254 ? 0.7688 0.5999 0.7101 0.0292  0.0431  -0.0680 947  TYR   B CB  
3931 C CG  . TYR   B 254 ? 0.8046 0.6187 0.7101 0.0243  0.0524  -0.0735 947  TYR   B CG  
3932 C CD1 . TYR   B 254 ? 0.8121 0.6491 0.7252 0.0189  0.0530  -0.0682 947  TYR   B CD1 
3933 C CD2 . TYR   B 254 ? 0.8483 0.6181 0.7060 0.0235  0.0582  -0.0839 947  TYR   B CD2 
3934 C CE1 . TYR   B 254 ? 0.8462 0.6626 0.7208 0.0138  0.0606  -0.0721 947  TYR   B CE1 
3935 C CE2 . TYR   B 254 ? 0.8827 0.6313 0.6995 0.0184  0.0648  -0.0883 947  TYR   B CE2 
3936 C CZ  . TYR   B 254 ? 0.8902 0.6623 0.7157 0.0140  0.0664  -0.0819 947  TYR   B CZ  
3937 O OH  . TYR   B 254 ? 0.9435 0.6904 0.7241 0.0092  0.0733  -0.0852 947  TYR   B OH  
3938 N N   . MET   B 255 ? 0.7724 0.5762 0.6840 0.0026  -0.0027 -0.0706 948  MET   B N   
3939 C CA  . MET   B 255 ? 0.7892 0.5718 0.6740 -0.0108 -0.0189 -0.0763 948  MET   B CA  
3940 C C   . MET   B 255 ? 0.7694 0.5800 0.6704 -0.0209 -0.0366 -0.0701 948  MET   B C   
3941 O O   . MET   B 255 ? 0.7881 0.5895 0.6679 -0.0299 -0.0493 -0.0739 948  MET   B O   
3942 C CB  . MET   B 255 ? 0.8153 0.5699 0.6920 -0.0139 -0.0226 -0.0808 948  MET   B CB  
3943 C CG  . MET   B 255 ? 0.8895 0.6007 0.7304 -0.0069 -0.0082 -0.0913 948  MET   B CG  
3944 S SD  . MET   B 255 ? 1.0425 0.7196 0.8271 -0.0141 -0.0102 -0.1026 948  MET   B SD  
3945 C CE  . MET   B 255 ? 1.0063 0.6952 0.7923 0.0013  0.0166  -0.1007 948  MET   B CE  
3946 N N   . ILE   B 256 ? 0.7342 0.5775 0.6706 -0.0184 -0.0376 -0.0607 949  ILE   B N   
3947 C CA  . ILE   B 256 ? 0.7175 0.5869 0.6701 -0.0254 -0.0508 -0.0548 949  ILE   B CA  
3948 C C   . ILE   B 256 ? 0.7140 0.5901 0.6542 -0.0246 -0.0501 -0.0545 949  ILE   B C   
3949 O O   . ILE   B 256 ? 0.7249 0.6025 0.6561 -0.0311 -0.0634 -0.0548 949  ILE   B O   
3950 C CB  . ILE   B 256 ? 0.7066 0.6023 0.6928 -0.0220 -0.0497 -0.0455 949  ILE   B CB  
3951 C CG1 . ILE   B 256 ? 0.7131 0.5980 0.7069 -0.0248 -0.0520 -0.0445 949  ILE   B CG1 
3952 C CG2 . ILE   B 256 ? 0.7067 0.6277 0.7066 -0.0262 -0.0586 -0.0397 949  ILE   B CG2 
3953 C CD1 . ILE   B 256 ? 0.7151 0.6184 0.7335 -0.0203 -0.0501 -0.0350 949  ILE   B CD1 
3954 N N   . MET   B 257 ? 0.6969 0.5755 0.6363 -0.0166 -0.0345 -0.0537 950  MET   B N   
3955 C CA  . MET   B 257 ? 0.6910 0.5706 0.6150 -0.0168 -0.0302 -0.0531 950  MET   B CA  
3956 C C   . MET   B 257 ? 0.7090 0.5564 0.5897 -0.0211 -0.0347 -0.0605 950  MET   B C   
3957 O O   . MET   B 257 ? 0.7203 0.5659 0.5852 -0.0254 -0.0455 -0.0592 950  MET   B O   
3958 C CB  . MET   B 257 ? 0.6968 0.5826 0.6297 -0.0091 -0.0095 -0.0519 950  MET   B CB  
3959 C CG  . MET   B 257 ? 0.7146 0.6335 0.6856 -0.0066 -0.0085 -0.0439 950  MET   B CG  
3960 S SD  . MET   B 257 ? 0.7575 0.6888 0.7474 0.0011  0.0142  -0.0429 950  MET   B SD  
3961 C CE  . MET   B 257 ? 0.6822 0.6210 0.7010 0.0110  0.0145  -0.0417 950  MET   B CE  
3962 N N   . ARG   B 258 ? 0.7190 0.5382 0.5782 -0.0196 -0.0280 -0.0683 951  ARG   B N   
3963 C CA  . ARG   B 258 ? 0.7488 0.5298 0.5600 -0.0238 -0.0319 -0.0771 951  ARG   B CA  
3964 C C   . ARG   B 258 ? 0.7440 0.5230 0.5475 -0.0344 -0.0589 -0.0780 951  ARG   B C   
3965 O O   . ARG   B 258 ? 0.7671 0.5267 0.5351 -0.0381 -0.0685 -0.0808 951  ARG   B O   
3966 C CB  . ARG   B 258 ? 0.7964 0.5477 0.5917 -0.0193 -0.0192 -0.0854 951  ARG   B CB  
3967 C CG  . ARG   B 258 ? 0.8952 0.5984 0.6327 -0.0224 -0.0184 -0.0962 951  ARG   B CG  
3968 C CD  . ARG   B 258 ? 0.9750 0.6643 0.6785 -0.0197 -0.0057 -0.0965 951  ARG   B CD  
3969 N NE  . ARG   B 258 ? 1.0451 0.7251 0.7201 -0.0290 -0.0288 -0.0961 951  ARG   B NE  
3970 C CZ  . ARG   B 258 ? 1.1256 0.7628 0.7446 -0.0344 -0.0383 -0.1043 951  ARG   B CZ  
3971 N NH1 . ARG   B 258 ? 1.1826 0.7781 0.7627 -0.0317 -0.0236 -0.1145 951  ARG   B NH1 
3972 N NH2 . ARG   B 258 ? 1.1375 0.7707 0.7364 -0.0416 -0.0628 -0.1023 951  ARG   B NH2 
3973 N N   . LYS   B 259 ? 0.7163 0.5165 0.5540 -0.0391 -0.0713 -0.0748 952  LYS   B N   
3974 C CA  . LYS   B 259 ? 0.7093 0.5161 0.5515 -0.0493 -0.0959 -0.0748 952  LYS   B CA  
3975 C C   . LYS   B 259 ? 0.6965 0.5277 0.5492 -0.0480 -0.1056 -0.0674 952  LYS   B C   
3976 O O   . LYS   B 259 ? 0.6988 0.5293 0.5437 -0.0536 -0.1260 -0.0682 952  LYS   B O   
3977 C CB  . LYS   B 259 ? 0.7114 0.5334 0.5883 -0.0555 -0.1020 -0.0731 952  LYS   B CB  
3978 C CG  . LYS   B 259 ? 0.7763 0.5660 0.6361 -0.0594 -0.0981 -0.0812 952  LYS   B CG  
3979 N N   . CYS   B 260 ? 0.6831 0.5345 0.5534 -0.0404 -0.0922 -0.0604 953  CYS   B N   
3980 C CA  . CYS   B 260 ? 0.6780 0.5448 0.5517 -0.0379 -0.0982 -0.0539 953  CYS   B CA  
3981 C C   . CYS   B 260 ? 0.7084 0.5465 0.5354 -0.0375 -0.1012 -0.0565 953  CYS   B C   
3982 O O   . CYS   B 260 ? 0.7119 0.5542 0.5333 -0.0362 -0.1126 -0.0519 953  CYS   B O   
3983 C CB  . CYS   B 260 ? 0.6627 0.5512 0.5605 -0.0320 -0.0827 -0.0471 953  CYS   B CB  
3984 S SG  . CYS   B 260 ? 0.6596 0.5791 0.6049 -0.0319 -0.0820 -0.0420 953  CYS   B SG  
3985 N N   . TRP   B 261 ? 0.7330 0.5390 0.5238 -0.0374 -0.0895 -0.0635 954  TRP   B N   
3986 C CA  . TRP   B 261 ? 0.7632 0.5350 0.5018 -0.0369 -0.0874 -0.0662 954  TRP   B CA  
3987 C C   . TRP   B 261 ? 0.8121 0.5502 0.5097 -0.0429 -0.1050 -0.0745 954  TRP   B C   
3988 O O   . TRP   B 261 ? 0.8489 0.5475 0.4947 -0.0426 -0.0968 -0.0801 954  TRP   B O   
3989 C CB  . TRP   B 261 ? 0.7607 0.5191 0.4848 -0.0319 -0.0575 -0.0676 954  TRP   B CB  
3990 C CG  . TRP   B 261 ? 0.7270 0.5192 0.4931 -0.0278 -0.0423 -0.0600 954  TRP   B CG  
3991 C CD1 . TRP   B 261 ? 0.7185 0.5359 0.5084 -0.0278 -0.0497 -0.0518 954  TRP   B CD1 
3992 C CD2 . TRP   B 261 ? 0.7101 0.5137 0.4995 -0.0231 -0.0189 -0.0603 954  TRP   B CD2 
3993 N NE1 . TRP   B 261 ? 0.7030 0.5447 0.5264 -0.0252 -0.0335 -0.0475 954  TRP   B NE1 
3994 C CE2 . TRP   B 261 ? 0.6963 0.5324 0.5224 -0.0221 -0.0152 -0.0522 954  TRP   B CE2 
3995 C CE3 . TRP   B 261 ? 0.7180 0.5062 0.5004 -0.0186 -0.0008 -0.0668 954  TRP   B CE3 
3996 C CZ2 . TRP   B 261 ? 0.6792 0.5358 0.5375 -0.0181 0.0029  -0.0500 954  TRP   B CZ2 
3997 C CZ3 . TRP   B 261 ? 0.7025 0.5130 0.5203 -0.0125 0.0187  -0.0641 954  TRP   B CZ3 
3998 C CH2 . TRP   B 261 ? 0.6816 0.5275 0.5379 -0.0128 0.0191  -0.0556 954  TRP   B CH2 
3999 N N   . MET   B 262 ? 0.8147 0.5669 0.5334 -0.0491 -0.1293 -0.0752 955  MET   B N   
4000 C CA  . MET   B 262 ? 0.8643 0.5872 0.5476 -0.0572 -0.1517 -0.0830 955  MET   B CA  
4001 C C   . MET   B 262 ? 0.8998 0.6120 0.5531 -0.0564 -0.1730 -0.0795 955  MET   B C   
4002 O O   . MET   B 262 ? 0.8756 0.6149 0.5542 -0.0510 -0.1771 -0.0704 955  MET   B O   
4003 C CB  . MET   B 262 ? 0.8636 0.6074 0.5858 -0.0662 -0.1688 -0.0852 955  MET   B CB  
4004 C CG  . MET   B 262 ? 0.9211 0.6601 0.6565 -0.0674 -0.1503 -0.0899 955  MET   B CG  
4005 S SD  . MET   B 262 ? 1.1029 0.8550 0.8715 -0.0818 -0.1718 -0.0932 955  MET   B SD  
4006 C CE  . MET   B 262 ? 1.1485 0.8889 0.9260 -0.0797 -0.1470 -0.0965 955  MET   B CE  
4007 N N   . ILE   B 263 ? 0.9545 0.6234 0.5498 -0.0612 -0.1871 -0.0867 956  ILE   B N   
4008 C CA  . ILE   B 263 ? 1.0012 0.6532 0.5601 -0.0601 -0.2110 -0.0834 956  ILE   B CA  
4009 C C   . ILE   B 263 ? 0.9955 0.6878 0.6038 -0.0627 -0.2428 -0.0784 956  ILE   B C   
4010 O O   . ILE   B 263 ? 0.9966 0.7057 0.6162 -0.0551 -0.2529 -0.0693 956  ILE   B O   
4011 C CB  . ILE   B 263 ? 1.0635 0.6564 0.5462 -0.0662 -0.2218 -0.0937 956  ILE   B CB  
4012 C CG1 . ILE   B 263 ? 1.1129 0.6654 0.5460 -0.0617 -0.1859 -0.0982 956  ILE   B CG1 
4013 C CG2 . ILE   B 263 ? 1.0828 0.6572 0.5269 -0.0655 -0.2537 -0.0899 956  ILE   B CG2 
4014 C CD1 . ILE   B 263 ? 1.1414 0.6933 0.5624 -0.0525 -0.1645 -0.0887 956  ILE   B CD1 
4015 N N   . ASP   B 264 ? 0.9868 0.6947 0.6268 -0.0731 -0.2565 -0.0841 957  ASP   B N   
4016 C CA  . ASP   B 264 ? 0.9614 0.7125 0.6565 -0.0769 -0.2835 -0.0798 957  ASP   B CA  
4017 C C   . ASP   B 264 ? 0.9132 0.7131 0.6729 -0.0700 -0.2654 -0.0709 957  ASP   B C   
4018 O O   . ASP   B 264 ? 0.8991 0.7095 0.6837 -0.0727 -0.2443 -0.0727 957  ASP   B O   
4019 C CB  . ASP   B 264 ? 0.9944 0.7438 0.7014 -0.0932 -0.3021 -0.0889 957  ASP   B CB  
4020 C CG  . ASP   B 264 ? 1.0492 0.8468 0.8193 -0.0991 -0.3285 -0.0846 957  ASP   B CG  
4021 O OD1 . ASP   B 264 ? 1.0604 0.8809 0.8472 -0.0899 -0.3439 -0.0763 957  ASP   B OD1 
4022 O OD2 . ASP   B 264 ? 1.0693 0.8812 0.8729 -0.1127 -0.3329 -0.0892 957  ASP   B OD2 
4023 N N   . ALA   B 265 ? 0.8918 0.7173 0.6741 -0.0602 -0.2737 -0.0614 958  ALA   B N   
4024 C CA  . ALA   B 265 ? 0.8540 0.7204 0.6894 -0.0524 -0.2573 -0.0531 958  ALA   B CA  
4025 C C   . ALA   B 265 ? 0.8218 0.7270 0.7182 -0.0602 -0.2585 -0.0534 958  ALA   B C   
4026 O O   . ALA   B 265 ? 0.8064 0.7300 0.7317 -0.0582 -0.2360 -0.0505 958  ALA   B O   
4027 C CB  . ALA   B 265 ? 0.8409 0.7200 0.6824 -0.0400 -0.2691 -0.0439 958  ALA   B CB  
4028 N N   . ASP   B 266 ? 0.8118 0.7276 0.7258 -0.0703 -0.2849 -0.0569 959  ASP   B N   
4029 C CA  . ASP   B 266 ? 0.7847 0.7359 0.7565 -0.0805 -0.2860 -0.0572 959  ASP   B CA  
4030 C C   . ASP   B 266 ? 0.7783 0.7121 0.7435 -0.0916 -0.2682 -0.0638 959  ASP   B C   
4031 O O   . ASP   B 266 ? 0.7612 0.7206 0.7709 -0.0985 -0.2602 -0.0622 959  ASP   B O   
4032 C CB  . ASP   B 266 ? 0.8129 0.7831 0.8099 -0.0898 -0.3206 -0.0588 959  ASP   B CB  
4033 C CG  . ASP   B 266 ? 0.8935 0.8941 0.9180 -0.0764 -0.3365 -0.0500 959  ASP   B CG  
4034 O OD1 . ASP   B 266 ? 0.8959 0.9165 0.9426 -0.0629 -0.3169 -0.0423 959  ASP   B OD1 
4035 O OD2 . ASP   B 266 ? 0.9387 0.9414 0.9613 -0.0788 -0.3695 -0.0509 959  ASP   B OD2 
4036 N N   . SER   B 267 ? 0.7911 0.6795 0.7002 -0.0926 -0.2606 -0.0710 960  SER   B N   
4037 C CA  . SER   B 267 ? 0.7805 0.6479 0.6799 -0.0995 -0.2420 -0.0771 960  SER   B CA  
4038 C C   . SER   B 267 ? 0.7514 0.6258 0.6602 -0.0881 -0.2104 -0.0717 960  SER   B C   
4039 O O   . SER   B 267 ? 0.7532 0.6210 0.6690 -0.0914 -0.1947 -0.0738 960  SER   B O   
4040 C CB  . SER   B 267 ? 0.8323 0.6468 0.6685 -0.1044 -0.2465 -0.0879 960  SER   B CB  
4041 O OG  . SER   B 267 ? 0.8754 0.6821 0.7032 -0.1175 -0.2785 -0.0936 960  SER   B OG  
4042 N N   . ARG   B 268 ? 0.7271 0.6133 0.6357 -0.0752 -0.2024 -0.0647 961  ARG   B N   
4043 C CA  . ARG   B 268 ? 0.7084 0.6043 0.6288 -0.0660 -0.1763 -0.0594 961  ARG   B CA  
4044 C C   . ARG   B 268 ? 0.6832 0.6141 0.6555 -0.0678 -0.1704 -0.0537 961  ARG   B C   
4045 O O   . ARG   B 268 ? 0.6679 0.6249 0.6725 -0.0716 -0.1841 -0.0507 961  ARG   B O   
4046 C CB  . ARG   B 268 ? 0.7008 0.5998 0.6089 -0.0545 -0.1720 -0.0533 961  ARG   B CB  
4047 C CG  . ARG   B 268 ? 0.7223 0.5837 0.5753 -0.0523 -0.1726 -0.0575 961  ARG   B CG  
4048 C CD  . ARG   B 268 ? 0.7237 0.5866 0.5649 -0.0430 -0.1711 -0.0506 961  ARG   B CD  
4049 N NE  . ARG   B 268 ? 0.7509 0.5760 0.5363 -0.0427 -0.1788 -0.0537 961  ARG   B NE  
4050 C CZ  . ARG   B 268 ? 0.7562 0.5734 0.5209 -0.0369 -0.1903 -0.0485 961  ARG   B CZ  
4051 N NH1 . ARG   B 268 ? 0.7300 0.5754 0.5275 -0.0300 -0.1943 -0.0403 961  ARG   B NH1 
4052 N NH2 . ARG   B 268 ? 0.7672 0.5445 0.4746 -0.0373 -0.1972 -0.0512 961  ARG   B NH2 
4053 N N   . PRO   B 269 ? 0.6768 0.6086 0.6577 -0.0647 -0.1498 -0.0517 962  PRO   B N   
4054 C CA  . PRO   B 269 ? 0.6509 0.6101 0.6730 -0.0661 -0.1428 -0.0456 962  PRO   B CA  
4055 C C   . PRO   B 269 ? 0.6255 0.6142 0.6722 -0.0589 -0.1440 -0.0381 962  PRO   B C   
4056 O O   . PRO   B 269 ? 0.6401 0.6262 0.6708 -0.0508 -0.1460 -0.0364 962  PRO   B O   
4057 C CB  . PRO   B 269 ? 0.6694 0.6184 0.6852 -0.0604 -0.1224 -0.0442 962  PRO   B CB  
4058 C CG  . PRO   B 269 ? 0.6922 0.6226 0.6750 -0.0527 -0.1165 -0.0469 962  PRO   B CG  
4059 C CD  . PRO   B 269 ? 0.6910 0.5998 0.6457 -0.0586 -0.1317 -0.0541 962  PRO   B CD  
4060 N N   . LYS   B 270 ? 0.5846 0.5982 0.6680 -0.0619 -0.1411 -0.0334 963  LYS   B N   
4061 C CA  . LYS   B 270 ? 0.5514 0.5907 0.6580 -0.0538 -0.1385 -0.0267 963  LYS   B CA  
4062 C C   . LYS   B 270 ? 0.5354 0.5736 0.6394 -0.0471 -0.1193 -0.0221 963  LYS   B C   
4063 O O   . LYS   B 270 ? 0.5428 0.5693 0.6410 -0.0504 -0.1098 -0.0228 963  LYS   B O   
4064 C CB  . LYS   B 270 ? 0.5433 0.6107 0.6920 -0.0605 -0.1436 -0.0243 963  LYS   B CB  
4065 C CG  . LYS   B 270 ? 0.5724 0.6430 0.7284 -0.0701 -0.1660 -0.0292 963  LYS   B CG  
4066 C CD  . LYS   B 270 ? 0.6091 0.6958 0.7737 -0.0616 -0.1826 -0.0271 963  LYS   B CD  
4067 N N   . PHE   B 271 ? 0.5148 0.5633 0.6222 -0.0375 -0.1147 -0.0174 964  PHE   B N   
4068 C CA  . PHE   B 271 ? 0.5059 0.5521 0.6087 -0.0324 -0.0994 -0.0135 964  PHE   B CA  
4069 C C   . PHE   B 271 ? 0.4982 0.5513 0.6191 -0.0372 -0.0895 -0.0104 964  PHE   B C   
4070 O O   . PHE   B 271 ? 0.5058 0.5484 0.6164 -0.0365 -0.0805 -0.0089 964  PHE   B O   
4071 C CB  . PHE   B 271 ? 0.4939 0.5460 0.5949 -0.0228 -0.0971 -0.0098 964  PHE   B CB  
4072 C CG  . PHE   B 271 ? 0.5068 0.5439 0.5813 -0.0184 -0.1023 -0.0115 964  PHE   B CG  
4073 C CD1 . PHE   B 271 ? 0.5203 0.5414 0.5734 -0.0197 -0.0961 -0.0132 964  PHE   B CD1 
4074 C CD2 . PHE   B 271 ? 0.5099 0.5488 0.5818 -0.0126 -0.1125 -0.0106 964  PHE   B CD2 
4075 C CE1 . PHE   B 271 ? 0.5356 0.5419 0.5641 -0.0172 -0.0978 -0.0142 964  PHE   B CE1 
4076 C CE2 . PHE   B 271 ? 0.5247 0.5448 0.5673 -0.0092 -0.1160 -0.0111 964  PHE   B CE2 
4077 C CZ  . PHE   B 271 ? 0.5335 0.5370 0.5540 -0.0125 -0.1074 -0.0130 964  PHE   B CZ  
4078 N N   . ARG   B 272 ? 0.4860 0.5560 0.6340 -0.0425 -0.0916 -0.0093 965  ARG   B N   
4079 C CA  . ARG   B 272 ? 0.4941 0.5690 0.6591 -0.0494 -0.0809 -0.0060 965  ARG   B CA  
4080 C C   . ARG   B 272 ? 0.5064 0.5600 0.6575 -0.0572 -0.0796 -0.0083 965  ARG   B C   
4081 O O   . ARG   B 272 ? 0.5156 0.5601 0.6622 -0.0581 -0.0684 -0.0043 965  ARG   B O   
4082 C CB  . ARG   B 272 ? 0.5082 0.6075 0.7092 -0.0561 -0.0853 -0.0055 965  ARG   B CB  
4083 C CG  . ARG   B 272 ? 0.5795 0.6879 0.8014 -0.0618 -0.0694 -0.0003 965  ARG   B CG  
4084 C CD  . ARG   B 272 ? 0.6441 0.7764 0.9057 -0.0733 -0.0745 -0.0008 965  ARG   B CD  
4085 N NE  . ARG   B 272 ? 0.7110 0.8318 0.9697 -0.0871 -0.0880 -0.0063 965  ARG   B NE  
4086 C CZ  . ARG   B 272 ? 0.7448 0.8476 0.9974 -0.0991 -0.0811 -0.0061 965  ARG   B CZ  
4087 N NH1 . ARG   B 272 ? 0.7408 0.8299 0.9884 -0.1115 -0.0940 -0.0121 965  ARG   B NH1 
4088 N NH2 . ARG   B 272 ? 0.7454 0.8394 0.9925 -0.0987 -0.0617 0.0000  965  ARG   B NH2 
4089 N N   . GLU   B 273 ? 0.5056 0.5478 0.6464 -0.0621 -0.0912 -0.0146 966  GLU   B N   
4090 C CA  . GLU   B 273 ? 0.5188 0.5364 0.6433 -0.0678 -0.0903 -0.0182 966  GLU   B CA  
4091 C C   . GLU   B 273 ? 0.5234 0.5247 0.6239 -0.0578 -0.0831 -0.0178 966  GLU   B C   
4092 O O   . GLU   B 273 ? 0.5281 0.5144 0.6219 -0.0576 -0.0758 -0.0161 966  GLU   B O   
4093 C CB  . GLU   B 273 ? 0.5599 0.5673 0.6763 -0.0755 -0.1050 -0.0262 966  GLU   B CB  
4094 C CG  . GLU   B 273 ? 0.6240 0.6516 0.7692 -0.0865 -0.1163 -0.0269 966  GLU   B CG  
4095 C CD  . GLU   B 273 ? 0.7512 0.7692 0.8853 -0.0940 -0.1358 -0.0349 966  GLU   B CD  
4096 O OE1 . GLU   B 273 ? 0.7920 0.7863 0.8913 -0.0887 -0.1390 -0.0400 966  GLU   B OE1 
4097 O OE2 . GLU   B 273 ? 0.7756 0.8097 0.9357 -0.1055 -0.1481 -0.0361 966  GLU   B OE2 
4098 N N   . LEU   B 274 ? 0.5229 0.5274 0.6123 -0.0496 -0.0853 -0.0189 967  LEU   B N   
4099 C CA  . LEU   B 274 ? 0.5292 0.5247 0.6030 -0.0412 -0.0784 -0.0182 967  LEU   B CA  
4100 C C   . LEU   B 274 ? 0.5287 0.5292 0.6091 -0.0373 -0.0700 -0.0112 967  LEU   B C   
4101 O O   . LEU   B 274 ? 0.5436 0.5350 0.6171 -0.0328 -0.0655 -0.0100 967  LEU   B O   
4102 C CB  . LEU   B 274 ? 0.5284 0.5280 0.5917 -0.0358 -0.0814 -0.0194 967  LEU   B CB  
4103 C CG  . LEU   B 274 ? 0.5436 0.5314 0.5899 -0.0380 -0.0896 -0.0257 967  LEU   B CG  
4104 C CD1 . LEU   B 274 ? 0.5421 0.5334 0.5782 -0.0333 -0.0932 -0.0248 967  LEU   B CD1 
4105 C CD2 . LEU   B 274 ? 0.5634 0.5298 0.5911 -0.0371 -0.0836 -0.0307 967  LEU   B CD2 
4106 N N   . ILE   B 275 ? 0.5079 0.5217 0.6008 -0.0385 -0.0678 -0.0067 968  ILE   B N   
4107 C CA  . ILE   B 275 ? 0.5042 0.5171 0.5957 -0.0356 -0.0600 -0.0003 968  ILE   B CA  
4108 C C   . ILE   B 275 ? 0.5207 0.5187 0.6101 -0.0393 -0.0561 0.0021  968  ILE   B C   
4109 O O   . ILE   B 275 ? 0.5332 0.5210 0.6124 -0.0342 -0.0540 0.0054  968  ILE   B O   
4110 C CB  . ILE   B 275 ? 0.4852 0.5114 0.5871 -0.0357 -0.0552 0.0034  968  ILE   B CB  
4111 C CG1 . ILE   B 275 ? 0.4744 0.5100 0.5741 -0.0294 -0.0585 0.0019  968  ILE   B CG1 
4112 C CG2 . ILE   B 275 ? 0.4883 0.5062 0.5817 -0.0344 -0.0460 0.0097  968  ILE   B CG2 
4113 C CD1 . ILE   B 275 ? 0.4601 0.5095 0.5743 -0.0280 -0.0544 0.0039  968  ILE   B CD1 
4114 N N   . ILE   B 276 ? 0.5170 0.5128 0.6163 -0.0485 -0.0565 0.0004  969  ILE   B N   
4115 C CA  . ILE   B 276 ? 0.5288 0.5057 0.6241 -0.0538 -0.0523 0.0026  969  ILE   B CA  
4116 C C   . ILE   B 276 ? 0.5554 0.5124 0.6356 -0.0480 -0.0546 -0.0004 969  ILE   B C   
4117 O O   . ILE   B 276 ? 0.5821 0.5239 0.6531 -0.0434 -0.0508 0.0046  969  ILE   B O   
4118 C CB  . ILE   B 276 ? 0.5221 0.5020 0.6337 -0.0675 -0.0534 0.0004  969  ILE   B CB  
4119 C CG1 . ILE   B 276 ? 0.5123 0.5155 0.6450 -0.0712 -0.0475 0.0047  969  ILE   B CG1 
4120 C CG2 . ILE   B 276 ? 0.5269 0.4809 0.6310 -0.0751 -0.0491 0.0020  969  ILE   B CG2 
4121 C CD1 . ILE   B 276 ? 0.5032 0.5212 0.6627 -0.0846 -0.0520 0.0016  969  ILE   B CD1 
4122 N N   . GLU   B 277 ? 0.5535 0.5092 0.6296 -0.0469 -0.0603 -0.0079 970  GLU   B N   
4123 C CA  . GLU   B 277 ? 0.5664 0.5039 0.6293 -0.0398 -0.0592 -0.0115 970  GLU   B CA  
4124 C C   . GLU   B 277 ? 0.5664 0.5088 0.6282 -0.0276 -0.0561 -0.0070 970  GLU   B C   
4125 O O   . GLU   B 277 ? 0.5720 0.5004 0.6301 -0.0214 -0.0534 -0.0037 970  GLU   B O   
4126 C CB  . GLU   B 277 ? 0.5972 0.5305 0.6509 -0.0409 -0.0636 -0.0206 970  GLU   B CB  
4127 C CG  . GLU   B 277 ? 0.6851 0.6084 0.7371 -0.0537 -0.0703 -0.0262 970  GLU   B CG  
4128 N N   . PHE   B 278 ? 0.5583 0.5198 0.6239 -0.0244 -0.0576 -0.0063 971  PHE   B N   
4129 C CA  . PHE   B 278 ? 0.5633 0.5321 0.6311 -0.0155 -0.0569 -0.0024 971  PHE   B CA  
4130 C C   . PHE   B 278 ? 0.5667 0.5327 0.6334 -0.0137 -0.0575 0.0059  971  PHE   B C   
4131 O O   . PHE   B 278 ? 0.5740 0.5398 0.6420 -0.0058 -0.0596 0.0095  971  PHE   B O   
4132 C CB  . PHE   B 278 ? 0.5601 0.5456 0.6295 -0.0151 -0.0583 -0.0040 971  PHE   B CB  
4133 C CG  . PHE   B 278 ? 0.5735 0.5572 0.6389 -0.0134 -0.0558 -0.0106 971  PHE   B CG  
4134 C CD1 . PHE   B 278 ? 0.5868 0.5704 0.6565 -0.0062 -0.0509 -0.0113 971  PHE   B CD1 
4135 C CD2 . PHE   B 278 ? 0.5885 0.5699 0.6454 -0.0186 -0.0580 -0.0156 971  PHE   B CD2 
4136 C CE1 . PHE   B 278 ? 0.6027 0.5822 0.6660 -0.0049 -0.0448 -0.0173 971  PHE   B CE1 
4137 C CE2 . PHE   B 278 ? 0.6079 0.5820 0.6535 -0.0173 -0.0547 -0.0213 971  PHE   B CE2 
4138 C CZ  . PHE   B 278 ? 0.6062 0.5784 0.6538 -0.0108 -0.0464 -0.0223 971  PHE   B CZ  
4139 N N   . SER   B 279 ? 0.5603 0.5238 0.6249 -0.0206 -0.0557 0.0091  972  SER   B N   
4140 C CA  . SER   B 279 ? 0.5670 0.5215 0.6230 -0.0196 -0.0543 0.0173  972  SER   B CA  
4141 C C   . SER   B 279 ? 0.5827 0.5146 0.6318 -0.0163 -0.0537 0.0208  972  SER   B C   
4142 O O   . SER   B 279 ? 0.6015 0.5241 0.6411 -0.0099 -0.0566 0.0276  972  SER   B O   
4143 C CB  . SER   B 279 ? 0.5755 0.5322 0.6314 -0.0279 -0.0481 0.0197  972  SER   B CB  
4144 O OG  . SER   B 279 ? 0.5940 0.5668 0.6516 -0.0270 -0.0483 0.0188  972  SER   B OG  
4145 N N   . LYS   B 280 ? 0.5769 0.4970 0.6280 -0.0206 -0.0512 0.0162  973  LYS   B N   
4146 C CA  . LYS   B 280 ? 0.6009 0.4943 0.6433 -0.0171 -0.0498 0.0186  973  LYS   B CA  
4147 C C   . LYS   B 280 ? 0.6177 0.5113 0.6627 -0.0021 -0.0536 0.0185  973  LYS   B C   
4148 O O   . LYS   B 280 ? 0.6317 0.5104 0.6703 0.0068  -0.0560 0.0253  973  LYS   B O   
4149 C CB  . LYS   B 280 ? 0.6179 0.4972 0.6601 -0.0266 -0.0471 0.0115  973  LYS   B CB  
4150 C CG  . LYS   B 280 ? 0.6711 0.5175 0.7014 -0.0221 -0.0450 0.0120  973  LYS   B CG  
4151 C CD  . LYS   B 280 ? 0.7388 0.5687 0.7652 -0.0325 -0.0439 0.0031  973  LYS   B CD  
4152 N N   . MET   B 281 ? 0.6143 0.5254 0.6697 0.0011  -0.0540 0.0115  974  MET   B N   
4153 C CA  . MET   B 281 ? 0.6195 0.5372 0.6846 0.0144  -0.0548 0.0109  974  MET   B CA  
4154 C C   . MET   B 281 ? 0.6277 0.5609 0.7000 0.0210  -0.0624 0.0183  974  MET   B C   
4155 O O   . MET   B 281 ? 0.6273 0.5596 0.7080 0.0332  -0.0658 0.0220  974  MET   B O   
4156 C CB  . MET   B 281 ? 0.6173 0.5481 0.6888 0.0137  -0.0505 0.0019  974  MET   B CB  
4157 C CG  . MET   B 281 ? 0.6566 0.5670 0.7159 0.0082  -0.0456 -0.0060 974  MET   B CG  
4158 S SD  . MET   B 281 ? 0.7299 0.6473 0.7867 0.0085  -0.0399 -0.0161 974  MET   B SD  
4159 C CE  . MET   B 281 ? 0.7018 0.5822 0.7369 0.0050  -0.0359 -0.0248 974  MET   B CE  
4160 N N   . ALA   B 282 ? 0.6335 0.5793 0.7023 0.0136  -0.0659 0.0205  975  ALA   B N   
4161 C CA  . ALA   B 282 ? 0.6442 0.6001 0.7139 0.0177  -0.0751 0.0269  975  ALA   B CA  
4162 C C   . ALA   B 282 ? 0.6654 0.5999 0.7201 0.0230  -0.0809 0.0363  975  ALA   B C   
4163 O O   . ALA   B 282 ? 0.6666 0.6059 0.7222 0.0296  -0.0918 0.0418  975  ALA   B O   
4164 C CB  . ALA   B 282 ? 0.6472 0.6146 0.7105 0.0087  -0.0759 0.0260  975  ALA   B CB  
4165 N N   . ARG   B 283 ? 0.6858 0.5953 0.7257 0.0194  -0.0745 0.0384  976  ARG   B N   
4166 C CA  . ARG   B 283 ? 0.7110 0.5937 0.7314 0.0243  -0.0783 0.0481  976  ARG   B CA  
4167 C C   . ARG   B 283 ? 0.7288 0.6021 0.7574 0.0399  -0.0841 0.0510  976  ARG   B C   
4168 O O   . ARG   B 283 ? 0.7456 0.6026 0.7613 0.0484  -0.0932 0.0603  976  ARG   B O   
4169 C CB  . ARG   B 283 ? 0.7315 0.5898 0.7343 0.0132  -0.0676 0.0499  976  ARG   B CB  
4170 C CG  . ARG   B 283 ? 0.7524 0.6199 0.7481 0.0013  -0.0621 0.0499  976  ARG   B CG  
4171 C CD  . ARG   B 283 ? 0.7851 0.6289 0.7640 -0.0090 -0.0509 0.0548  976  ARG   B CD  
4172 N NE  . ARG   B 283 ? 0.8035 0.6474 0.7964 -0.0191 -0.0428 0.0483  976  ARG   B NE  
4173 C CZ  . ARG   B 283 ? 0.8001 0.6661 0.8096 -0.0290 -0.0378 0.0417  976  ARG   B CZ  
4174 N NH1 . ARG   B 283 ? 0.7880 0.6522 0.8091 -0.0389 -0.0339 0.0360  976  ARG   B NH1 
4175 N NH2 . ARG   B 283 ? 0.7772 0.6654 0.7910 -0.0290 -0.0381 0.0406  976  ARG   B NH2 
4176 N N   . ASP   B 284 ? 0.7263 0.6081 0.7745 0.0450  -0.0787 0.0433  977  ASP   B N   
4177 C CA  . ASP   B 284 ? 0.7399 0.6167 0.8014 0.0622  -0.0811 0.0446  977  ASP   B CA  
4178 C C   . ASP   B 284 ? 0.7186 0.6266 0.8091 0.0664  -0.0770 0.0361  977  ASP   B C   
4179 O O   . ASP   B 284 ? 0.7229 0.6241 0.8165 0.0677  -0.0657 0.0282  977  ASP   B O   
4180 C CB  . ASP   B 284 ? 0.8003 0.6405 0.8466 0.0637  -0.0721 0.0433  977  ASP   B CB  
4181 C CG  . ASP   B 284 ? 0.8925 0.7165 0.9450 0.0840  -0.0742 0.0470  977  ASP   B CG  
4182 O OD1 . ASP   B 284 ? 0.8853 0.7305 0.9582 0.0981  -0.0846 0.0519  977  ASP   B OD1 
4183 O OD2 . ASP   B 284 ? 0.9590 0.7487 0.9969 0.0859  -0.0663 0.0451  977  ASP   B OD2 
4184 N N   . PRO   B 285 ? 0.6987 0.6385 0.8075 0.0665  -0.0850 0.0372  978  PRO   B N   
4185 C CA  . PRO   B 285 ? 0.6844 0.6525 0.8180 0.0663  -0.0781 0.0293  978  PRO   B CA  
4186 C C   . PRO   B 285 ? 0.6804 0.6561 0.8401 0.0825  -0.0715 0.0271  978  PRO   B C   
4187 O O   . PRO   B 285 ? 0.6769 0.6620 0.8459 0.0810  -0.0583 0.0188  978  PRO   B O   
4188 C CB  . PRO   B 285 ? 0.6745 0.6699 0.8183 0.0602  -0.0894 0.0322  978  PRO   B CB  
4189 C CG  . PRO   B 285 ? 0.6856 0.6697 0.8174 0.0647  -0.1050 0.0422  978  PRO   B CG  
4190 C CD  . PRO   B 285 ? 0.6888 0.6363 0.7909 0.0636  -0.0998 0.0448  978  PRO   B CD  
4191 N N   . GLN   B 286 ? 0.6797 0.6502 0.8499 0.0985  -0.0795 0.0344  979  GLN   B N   
4192 C CA  . GLN   B 286 ? 0.6785 0.6571 0.8774 0.1170  -0.0718 0.0327  979  GLN   B CA  
4193 C C   . GLN   B 286 ? 0.6953 0.6410 0.8765 0.1213  -0.0536 0.0249  979  GLN   B C   
4194 O O   . GLN   B 286 ? 0.6909 0.6415 0.8915 0.1346  -0.0408 0.0202  979  GLN   B O   
4195 C CB  . GLN   B 286 ? 0.7036 0.6850 0.9195 0.1352  -0.0879 0.0437  979  GLN   B CB  
4196 C CG  . GLN   B 286 ? 0.7536 0.7754 0.9995 0.1342  -0.1056 0.0492  979  GLN   B CG  
4197 C CD  . GLN   B 286 ? 0.8591 0.8754 1.0772 0.1189  -0.1221 0.0543  979  GLN   B CD  
4198 O OE1 . GLN   B 286 ? 0.8670 0.9112 1.0977 0.1085  -0.1307 0.0537  979  GLN   B OE1 
4199 N NE2 . GLN   B 286 ? 0.9077 0.8851 1.0855 0.1169  -0.1256 0.0593  979  GLN   B NE2 
4200 N N   . ARG   B 287 ? 0.7109 0.6230 0.8556 0.1094  -0.0520 0.0233  980  ARG   B N   
4201 C CA  . ARG   B 287 ? 0.7315 0.6085 0.8539 0.1087  -0.0380 0.0151  980  ARG   B CA  
4202 C C   . ARG   B 287 ? 0.7275 0.6134 0.8455 0.0968  -0.0257 0.0032  980  ARG   B C   
4203 O O   . ARG   B 287 ? 0.7472 0.6083 0.8503 0.0989  -0.0130 -0.0055 980  ARG   B O   
4204 C CB  . ARG   B 287 ? 0.7736 0.6154 0.8625 0.0966  -0.0429 0.0184  980  ARG   B CB  
4205 C CG  . ARG   B 287 ? 0.8523 0.6489 0.9179 0.0994  -0.0332 0.0133  980  ARG   B CG  
4206 C CD  . ARG   B 287 ? 0.9259 0.7043 0.9665 0.0774  -0.0295 0.0058  980  ARG   B CD  
4207 N NE  . ARG   B 287 ? 0.9998 0.7531 1.0202 0.0660  -0.0352 0.0128  980  ARG   B NE  
4208 C CZ  . ARG   B 287 ? 1.0773 0.7932 1.0740 0.0548  -0.0307 0.0087  980  ARG   B CZ  
4209 N NH1 . ARG   B 287 ? 1.0921 0.7879 1.0782 0.0540  -0.0226 -0.0030 980  ARG   B NH1 
4210 N NH2 . ARG   B 287 ? 1.0945 0.7908 1.0763 0.0432  -0.0339 0.0161  980  ARG   B NH2 
4211 N N   . TYR   B 288 ? 0.7007 0.6163 0.8262 0.0842  -0.0300 0.0029  981  TYR   B N   
4212 C CA  . TYR   B 288 ? 0.6953 0.6161 0.8116 0.0724  -0.0212 -0.0066 981  TYR   B CA  
4213 C C   . TYR   B 288 ? 0.6791 0.6321 0.8203 0.0760  -0.0136 -0.0088 981  TYR   B C   
4214 O O   . TYR   B 288 ? 0.6792 0.6278 0.8103 0.0725  -0.0011 -0.0171 981  TYR   B O   
4215 C CB  . TYR   B 288 ? 0.6933 0.6156 0.7932 0.0540  -0.0301 -0.0057 981  TYR   B CB  
4216 C CG  . TYR   B 288 ? 0.7149 0.6057 0.7924 0.0477  -0.0336 -0.0045 981  TYR   B CG  
4217 C CD1 . TYR   B 288 ? 0.7408 0.6022 0.7974 0.0429  -0.0270 -0.0129 981  TYR   B CD1 
4218 C CD2 . TYR   B 288 ? 0.7223 0.6089 0.7976 0.0468  -0.0428 0.0050  981  TYR   B CD2 
4219 C CE1 . TYR   B 288 ? 0.7686 0.6012 0.8074 0.0348  -0.0300 -0.0118 981  TYR   B CE1 
4220 C CE2 . TYR   B 288 ? 0.7511 0.6078 0.8067 0.0397  -0.0434 0.0069  981  TYR   B CE2 
4221 C CZ  . TYR   B 288 ? 0.7860 0.6175 0.8259 0.0327  -0.0371 -0.0016 981  TYR   B CZ  
4222 O OH  . TYR   B 288 ? 0.8361 0.6379 0.8588 0.0231  -0.0375 0.0001  981  TYR   B OH  
4223 N N   . LEU   B 289 ? 0.6628 0.6464 0.8347 0.0821  -0.0215 -0.0014 982  LEU   B N   
4224 C CA  . LEU   B 289 ? 0.6570 0.6738 0.8586 0.0841  -0.0140 -0.0028 982  LEU   B CA  
4225 C C   . LEU   B 289 ? 0.6653 0.7002 0.9049 0.1030  -0.0142 0.0023  982  LEU   B C   
4226 O O   . LEU   B 289 ? 0.6623 0.7006 0.9112 0.1093  -0.0308 0.0109  982  LEU   B O   
4227 C CB  . LEU   B 289 ? 0.6446 0.6869 0.8525 0.0698  -0.0250 0.0005  982  LEU   B CB  
4228 C CG  . LEU   B 289 ? 0.6709 0.7015 0.8478 0.0530  -0.0247 -0.0040 982  LEU   B CG  
4229 C CD1 . LEU   B 289 ? 0.6656 0.7189 0.8498 0.0418  -0.0346 -0.0004 982  LEU   B CD1 
4230 C CD2 . LEU   B 289 ? 0.6854 0.7053 0.8485 0.0507  -0.0072 -0.0129 982  LEU   B CD2 
4231 N N   . VAL   B 290 ? 0.6718 0.7172 0.9325 0.1130  0.0047  -0.0025 983  VAL   B N   
4232 C CA  . VAL   B 290 ? 0.6692 0.7368 0.9738 0.1332  0.0072  0.0019  983  VAL   B CA  
4233 C C   . VAL   B 290 ? 0.6597 0.7759 1.0087 0.1285  0.0083  0.0040  983  VAL   B C   
4234 O O   . VAL   B 290 ? 0.6535 0.7797 1.0102 0.1251  0.0293  -0.0022 983  VAL   B O   
4235 C CB  . VAL   B 290 ? 0.6901 0.7339 0.9906 0.1504  0.0303  -0.0049 983  VAL   B CB  
4236 C CG1 . VAL   B 290 ? 0.6738 0.7402 1.0229 0.1749  0.0317  0.0008  983  VAL   B CG1 
4237 C CG2 . VAL   B 290 ? 0.7305 0.7213 0.9815 0.1498  0.0293  -0.0086 983  VAL   B CG2 
4238 N N   . ILE   B 291 ? 0.6617 0.8052 1.0357 0.1262  -0.0147 0.0127  984  ILE   B N   
4239 C CA  . ILE   B 291 ? 0.6612 0.8506 1.0783 0.1186  -0.0177 0.0150  984  ILE   B CA  
4240 C C   . ILE   B 291 ? 0.6714 0.8952 1.1440 0.1361  -0.0297 0.0228  984  ILE   B C   
4241 O O   . ILE   B 291 ? 0.6801 0.8936 1.1475 0.1455  -0.0515 0.0301  984  ILE   B O   
4242 C CB  . ILE   B 291 ? 0.6696 0.8606 1.0648 0.0967  -0.0367 0.0172  984  ILE   B CB  
4243 C CG1 . ILE   B 291 ? 0.7019 0.8641 1.0493 0.0812  -0.0241 0.0097  984  ILE   B CG1 
4244 C CG2 . ILE   B 291 ? 0.6448 0.8804 1.0839 0.0875  -0.0454 0.0204  984  ILE   B CG2 
4245 C CD1 . ILE   B 291 ? 0.7229 0.8778 1.0428 0.0640  -0.0398 0.0113  984  ILE   B CD1 
4246 N N   . GLN   B 292 ? 0.6678 0.9321 1.1941 0.1408  -0.0152 0.0218  985  GLN   B N   
4247 C CA  . GLN   B 292 ? 0.6670 0.9725 1.2564 0.1574  -0.0276 0.0294  985  GLN   B CA  
4248 C C   . GLN   B 292 ? 0.6883 1.0165 1.2885 0.1432  -0.0618 0.0367  985  GLN   B C   
4249 O O   . GLN   B 292 ? 0.6890 1.0286 1.2837 0.1201  -0.0634 0.0342  985  GLN   B O   
4250 C CB  . GLN   B 292 ? 0.6537 1.0011 1.3013 0.1623  -0.0013 0.0262  985  GLN   B CB  
4251 N N   . GLY   B 293 ? 0.7070 1.0328 1.3120 0.1564  -0.0894 0.0454  986  GLY   B N   
4252 C CA  . GLY   B 293 ? 0.7295 1.0681 1.3343 0.1438  -0.1239 0.0521  986  GLY   B CA  
4253 C C   . GLY   B 293 ? 0.7901 1.0814 1.3318 0.1420  -0.1437 0.0563  986  GLY   B C   
4254 O O   . GLY   B 293 ? 0.7970 1.0924 1.3379 0.1415  -0.1748 0.0641  986  GLY   B O   
4255 N N   . ASP   B 294 ? 0.8294 1.0749 1.3172 0.1401  -0.1265 0.0513  987  ASP   B N   
4256 C CA  . ASP   B 294 ? 0.8799 1.0806 1.3105 0.1383  -0.1413 0.0556  987  ASP   B CA  
4257 C C   . ASP   B 294 ? 0.9033 1.0926 1.3423 0.1631  -0.1558 0.0650  987  ASP   B C   
4258 O O   . ASP   B 294 ? 0.9179 1.0963 1.3398 0.1647  -0.1829 0.0738  987  ASP   B O   
4259 C CB  . ASP   B 294 ? 0.9237 1.0833 1.3047 0.1310  -0.1189 0.0481  987  ASP   B CB  
4260 C CG  . ASP   B 294 ? 0.9593 1.1204 1.3202 0.1077  -0.1087 0.0405  987  ASP   B CG  
4261 O OD1 . ASP   B 294 ? 0.9474 1.1389 1.3305 0.0959  -0.1163 0.0403  987  ASP   B OD1 
4262 O OD2 . ASP   B 294 ? 0.9940 1.1250 1.3174 0.1012  -0.0943 0.0348  987  ASP   B OD2 
4263 N N   . GLU   B 295 ? 0.9014 1.0919 1.3658 0.1834  -0.1378 0.0632  988  GLU   B N   
4264 C CA  . GLU   B 295 ? 0.9112 1.0908 1.3879 0.2101  -0.1489 0.0719  988  GLU   B CA  
4265 C C   . GLU   B 295 ? 0.8762 1.1107 1.4293 0.2269  -0.1542 0.0754  988  GLU   B C   
4266 O O   . GLU   B 295 ? 0.8524 1.1269 1.4468 0.2193  -0.1382 0.0689  988  GLU   B O   
4267 C CB  . GLU   B 295 ? 0.9630 1.0983 1.4108 0.2231  -0.1246 0.0673  988  GLU   B CB  
4268 C C3  . A1IUK C .   ? 0.5013 0.5931 0.6631 -0.0088 -0.0212 0.0458  1101 A1IUK A C3  
4269 C C4  . A1IUK C .   ? 0.5152 0.6263 0.6781 -0.0125 -0.0478 0.0343  1101 A1IUK A C4  
4270 C C5  . A1IUK C .   ? 0.5231 0.5863 0.6592 0.0116  -0.0207 0.0512  1101 A1IUK A C5  
4271 C C6  . A1IUK C .   ? 0.5295 0.5917 0.6562 0.0242  -0.0224 0.0559  1101 A1IUK A C6  
4272 C C7  . A1IUK C .   ? 0.5454 0.5905 0.6555 0.0383  -0.0225 0.0594  1101 A1IUK A C7  
4273 C C8  . A1IUK C .   ? 0.5420 0.5713 0.6476 0.0399  -0.0192 0.0586  1101 A1IUK A C8  
4274 C C9  . A1IUK C .   ? 0.5385 0.5673 0.6537 0.0269  -0.0150 0.0542  1101 A1IUK A C9  
4275 C C10 . A1IUK C .   ? 0.5305 0.5762 0.6598 0.0126  -0.0166 0.0503  1101 A1IUK A C10 
4276 C C11 . A1IUK C .   ? 0.5654 0.6077 0.6610 0.0524  -0.0267 0.0633  1101 A1IUK A C11 
4277 C C12 . A1IUK C .   ? 0.5987 0.6285 0.6661 0.0664  -0.0239 0.0709  1101 A1IUK A C12 
4278 O O   . A1IUK C .   ? 0.6769 0.6745 0.6738 0.0983  -0.0215 0.0811  1101 A1IUK A O   
4279 N N1  . A1IUK C .   ? 0.5065 0.6110 0.6706 -0.0102 -0.0377 0.0388  1101 A1IUK A N1  
4280 C C20 . A1IUK C .   ? 0.6625 0.6680 0.6686 0.1026  -0.0355 0.0764  1101 A1IUK A C20 
4281 C C21 . A1IUK C .   ? 0.6669 0.6746 0.6611 0.1195  -0.0553 0.0707  1101 A1IUK A C21 
4282 C C22 . A1IUK C .   ? 0.6789 0.6786 0.6495 0.1270  -0.0559 0.0717  1101 A1IUK A C22 
4283 N N3  . A1IUK C .   ? 0.6367 0.6505 0.6654 0.0920  -0.0335 0.0744  1101 A1IUK A N3  
4284 C C13 . A1IUK C .   ? 0.6221 0.6383 0.6665 0.0743  -0.0178 0.0765  1101 A1IUK A C13 
4285 C C14 . A1IUK C .   ? 0.6148 0.6369 0.6564 0.0962  -0.0456 0.0685  1101 A1IUK A C14 
4286 C C15 . A1IUK C .   ? 0.5945 0.6258 0.6601 0.0784  -0.0372 0.0669  1101 A1IUK A C15 
4287 N N2  . A1IUK C .   ? 0.5790 0.6185 0.6674 0.0506  -0.0191 0.0678  1101 A1IUK A N2  
4288 N N4  . A1IUK C .   ? 0.5717 0.6120 0.6577 0.0690  -0.0376 0.0620  1101 A1IUK A N4  
4289 C C16 . A1IUK C .   ? 0.5596 0.6084 0.6569 0.0757  -0.0478 0.0551  1101 A1IUK A C16 
4290 N N6  . A1IUK C .   ? 0.5467 0.6121 0.6664 0.0638  -0.0487 0.0485  1101 A1IUK A N6  
4291 C C19 . A1IUK C .   ? 0.5315 0.6073 0.6649 0.0694  -0.0559 0.0407  1101 A1IUK A C19 
4292 N N5  . A1IUK C .   ? 0.5270 0.6030 0.6587 0.0864  -0.0649 0.0377  1101 A1IUK A N5  
4293 C C18 . A1IUK C .   ? 0.5432 0.6014 0.6490 0.0999  -0.0670 0.0449  1101 A1IUK A C18 
4294 C C17 . A1IUK C .   ? 0.5624 0.6035 0.6474 0.0950  -0.0570 0.0545  1101 A1IUK A C17 
4295 F F2  . A1IUK C .   ? 0.5462 0.5579 0.6346 0.0566  -0.0206 0.0620  1101 A1IUK A F2  
4296 F F3  . A1IUK C .   ? 0.5335 0.5775 0.6681 0.0009  -0.0151 0.0447  1101 A1IUK A F3  
4297 C C2  . A1IUK C .   ? 0.5095 0.5909 0.6600 0.0000  -0.0249 0.0467  1101 A1IUK A C2  
4298 N N   . A1IUK C .   ? 0.4953 0.6039 0.6680 -0.0143 -0.0306 0.0404  1101 A1IUK A N   
4299 F F1  . A1IUK C .   ? 0.5182 0.6325 0.6853 -0.0221 -0.0509 0.0290  1101 A1IUK A F1  
4300 F F   . A1IUK C .   ? 0.5183 0.6415 0.6839 -0.0061 -0.0535 0.0361  1101 A1IUK A F   
4301 C C1  . A1IUK C .   ? 0.5074 0.5986 0.6623 -0.0026 -0.0340 0.0416  1101 A1IUK A C1  
4302 C C   . A1IUK C .   ? 0.5112 0.5999 0.6624 0.0024  -0.0382 0.0389  1101 A1IUK A C   
4303 C C3  . A1IUK D .   ? 0.8166 0.5261 0.5722 0.0009  -0.0557 0.0083  1101 A1IUK B C3  
4304 C C4  . A1IUK D .   ? 0.8017 0.5781 0.6202 0.0341  -0.0550 0.0043  1101 A1IUK B C4  
4305 C C5  . A1IUK D .   ? 0.8148 0.5163 0.5647 -0.0339 -0.0524 0.0008  1101 A1IUK B C5  
4306 C C6  . A1IUK D .   ? 0.8011 0.5265 0.5707 -0.0509 -0.0523 0.0012  1101 A1IUK B C6  
4307 C C7  . A1IUK D .   ? 0.8106 0.5303 0.5789 -0.0727 -0.0522 -0.0009 1101 A1IUK B C7  
4308 C C8  . A1IUK D .   ? 0.8193 0.5033 0.5599 -0.0786 -0.0537 -0.0041 1101 A1IUK B C8  
4309 C C9  . A1IUK D .   ? 0.8352 0.4893 0.5495 -0.0622 -0.0530 -0.0054 1101 A1IUK B C9  
4310 C C10 . A1IUK D .   ? 0.8312 0.4967 0.5531 -0.0393 -0.0515 -0.0027 1101 A1IUK B C10 
4311 C C11 . A1IUK D .   ? 0.8158 0.5657 0.6121 -0.0884 -0.0502 -0.0001 1101 A1IUK B C11 
4312 C C12 . A1IUK D .   ? 0.8196 0.5998 0.6452 -0.1053 -0.0398 0.0033  1101 A1IUK B C12 
4313 O O   . A1IUK D .   ? 0.7966 0.6523 0.6948 -0.1257 -0.0113 0.0065  1101 A1IUK B O   
4314 N N1  . A1IUK D .   ? 0.8058 0.5541 0.5972 0.0188  -0.0558 0.0049  1101 A1IUK B N1  
4315 C C20 . A1IUK D .   ? 0.7850 0.6481 0.6944 -0.1290 -0.0228 0.0040  1101 A1IUK B C20 
4316 C C21 . A1IUK D .   ? 0.7541 0.6572 0.7080 -0.1366 -0.0281 0.0019  1101 A1IUK B C21 
4317 C C22 . A1IUK D .   ? 0.7312 0.6661 0.7160 -0.1339 -0.0170 0.0026  1101 A1IUK B C22 
4318 N N3  . A1IUK D .   ? 0.7961 0.6299 0.6768 -0.1248 -0.0317 0.0032  1101 A1IUK B N3  
4319 C C13 . A1IUK D .   ? 0.8203 0.6141 0.6596 -0.1157 -0.0289 0.0058  1101 A1IUK B C13 
4320 C C14 . A1IUK D .   ? 0.7854 0.6196 0.6687 -0.1269 -0.0447 -0.0003 1101 A1IUK B C14 
4321 C C15 . A1IUK D .   ? 0.8021 0.6007 0.6477 -0.1130 -0.0478 -0.0005 1101 A1IUK B C15 
4322 N N2  . A1IUK D .   ? 0.8291 0.5810 0.6260 -0.0897 -0.0432 0.0038  1101 A1IUK B N2  
4323 N N4  . A1IUK D .   ? 0.8045 0.5809 0.6274 -0.1029 -0.0545 -0.0029 1101 A1IUK B N4  
4324 C C16 . A1IUK D .   ? 0.7971 0.5769 0.6226 -0.1066 -0.0643 -0.0071 1101 A1IUK B C16 
4325 N N6  . A1IUK D .   ? 0.8041 0.5754 0.6161 -0.0901 -0.0666 -0.0088 1101 A1IUK B N6  
4326 C C19 . A1IUK D .   ? 0.7987 0.5713 0.6090 -0.0938 -0.0748 -0.0124 1101 A1IUK B C19 
4327 N N5  . A1IUK D .   ? 0.7909 0.5733 0.6123 -0.1114 -0.0841 -0.0145 1101 A1IUK B N5  
4328 C C18 . A1IUK D .   ? 0.7802 0.5758 0.6217 -0.1273 -0.0826 -0.0128 1101 A1IUK B C18 
4329 C C17 . A1IUK D .   ? 0.7812 0.5754 0.6249 -0.1262 -0.0708 -0.0091 1101 A1IUK B C17 
4330 F F2  . A1IUK D .   ? 0.8230 0.4996 0.5623 -0.1018 -0.0555 -0.0062 1101 A1IUK B F2  
4331 F F3  . A1IUK D .   ? 0.8442 0.4852 0.5467 -0.0215 -0.0491 -0.0038 1101 A1IUK B F3  
4332 C C2  . A1IUK D .   ? 0.8122 0.5283 0.5738 -0.0116 -0.0536 0.0033  1101 A1IUK B C2  
4333 N N   . A1IUK D .   ? 0.8096 0.5394 0.5841 0.0194  -0.0588 0.0092  1101 A1IUK B N   
4334 F F1  . A1IUK D .   ? 0.7907 0.6020 0.6370 0.0305  -0.0596 0.0053  1101 A1IUK B F1  
4335 F F   . A1IUK D .   ? 0.8094 0.5789 0.6282 0.0539  -0.0557 0.0072  1101 A1IUK B F   
4336 C C1  . A1IUK D .   ? 0.8039 0.5435 0.5858 0.0009  -0.0538 0.0013  1101 A1IUK B C1  
4337 C C   . A1IUK D .   ? 0.7915 0.5477 0.5854 -0.0049 -0.0531 -0.0029 1101 A1IUK B C   
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