data_9ETR
# 
_entry.id   9ETR 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.400 
_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   9ETR         pdb_00009etr 10.2210/pdb9etr/pdb 
WWPDB D_1292137580 ?            ?                   
# 
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 2024-12-04 
2 'Structure model' 1 1 2024-12-18 
3 'Structure model' 1 2 2025-01-08 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' '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 
3 3 'Structure model' citation        
4 3 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.pdbx_database_id_DOI'    
7  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
8  2 'Structure model' '_citation.title'                   
9  2 'Structure model' '_citation.year'                    
10 3 'Structure model' '_citation.journal_volume'          
11 3 'Structure model' '_citation.page_first'              
12 3 'Structure model' '_citation.page_last'               
13 3 '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                        9ETR 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-26 
_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                 1 
_pdbx_contact_author.email              marianne.schimpl@astrazeneca.com 
_pdbx_contact_author.name_first         Marianne 
_pdbx_contact_author.name_last          Schimpl 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2284-5250 
# 
_audit_author.name               'Schimpl, M.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0003-2284-5250 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            67 
_citation.language                  ? 
_citation.page_first                21717 
_citation.page_last                 21728 
_citation.title                     
;Discovery of 6-Fluoro-5-{4-[(5-fluoro-2-methyl-3-oxo-3,4-dihydroquinoxalin-6-yl)methyl]piperazin-1-yl}- N -methylpyridine-2-carboxamide (AZD9574): A CNS-Penetrant, PARP1-Selective Inhibitor.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c01725 
_citation.pdbx_database_id_PubMed   39655996 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Johannes, J.W.'     1  ? 
primary 'Balazs, A.Y.S.'     2  ? 
primary 'Barratt, D.'        3  ? 
primary 'Bista, M.'          4  ? 
primary 'Chuba, M.D.'        5  ? 
primary 'Cosulich, S.'       6  ? 
primary 'Critchlow, S.E.'    7  ? 
primary 'Degorce, S.L.'      8  ? 
primary 'Di Fruscia, P.'     9  ? 
primary 'Edmondson, S.D.'    10 ? 
primary 'Embrey, K.J.'       11 ? 
primary 'Fawell, S.'         12 ? 
primary 'Ghosh, A.'          13 ? 
primary 'Gill, S.J.'         14 ? 
primary 'Gunnarsson, A.'     15 ? 
primary 'Hande, S.M.'        16 ? 
primary 'Heightman, T.D.'    17 ? 
primary 'Hemsley, P.'        18 ? 
primary 'Illuzzi, G.'        19 ? 
primary 'Lane, J.'           20 ? 
primary 'Larner, C.J.B.'     21 ? 
primary 'Leo, E.'            22 ? 
primary 'Liu, L.'            23 ? 
primary 'Madin, A.'          24 ? 
primary 'McWilliams, L.'     25 ? 
primary 
;O'Connor, M.J.
;
26 ? 
primary 'Orme, J.P.'         27 ? 
primary 'Pachl, F.'          28 ? 
primary 'Packer, M.J.'       29 ? 
primary 'Pei, X.'            30 ? 
primary 'Pike, A.'           31 ? 
primary 'Schimpl, M.'        32 ? 
primary 'She, H.'            33 ? 
primary 'Staniszewska, A.D.' 34 ? 
primary 'Talbot, V.'         35 ? 
primary 'Underwood, E.'      36 ? 
primary 'Varnes, J.G.'       37 ? 
primary 'Xue, L.'            38 ? 
primary 'Yao, T.'            39 ? 
primary 'Zhang, K.'          40 ? 
primary 'Zhang, A.X.'        41 ? 
primary 'Zheng, X.'          42 ? 
# 
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 'Poly [ADP-ribose] polymerase 1, processed C-terminus' 39580.262 2   ? ? ? ? 
2 non-polymer syn 
;6-fluoranyl-5-[4-[(5-fluoranyl-2-methyl-3-oxidanylidene-4~{H}-quinoxalin-6-yl)methyl]piperazin-1-yl]-~{N}-methyl-pyridine-2-carboxamide
;
428.435   2   ? ? ? ? 
3 non-polymer syn 'SULFATE ION' 96.063    2   ? ? ? ? 
4 water       nat water 18.015    108 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Poly [ADP-ribose] polymerase 1,89-kDa form' 
# 
_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       
;GPLGSKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSSDSQILDLSNRF
YTLIPHDFGMKKPPLLNNADSVQAKAEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRK
YVKNTHATTHNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIY
FADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSANISLDGVDVPLGTGIS
SGVNDTSLLYNEYIVYDIAQVNLKYLLKLKFNFKT
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPLGSKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSSDSQILDLSNRF
YTLIPHDFGMKKPPLLNNADSVQAKAEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRK
YVKNTHATTHNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIY
FADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSANISLDGVDVPLGTGIS
SGVNDTSLLYNEYIVYDIAQVNLKYLLKLKFNFKT
;
_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 
;6-fluoranyl-5-[4-[(5-fluoranyl-2-methyl-3-oxidanylidene-4~{H}-quinoxalin-6-yl)methyl]piperazin-1-yl]-~{N}-methyl-pyridine-2-carboxamide
;
A1H64 
3 'SULFATE ION' SO4   
4 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   PRO n 
1 3   LEU n 
1 4   GLY n 
1 5   SER n 
1 6   LYS n 
1 7   SER n 
1 8   LYS n 
1 9   LEU n 
1 10  PRO n 
1 11  LYS n 
1 12  PRO n 
1 13  VAL n 
1 14  GLN n 
1 15  ASP n 
1 16  LEU n 
1 17  ILE n 
1 18  LYS n 
1 19  MET n 
1 20  ILE n 
1 21  PHE n 
1 22  ASP n 
1 23  VAL n 
1 24  GLU n 
1 25  SER n 
1 26  MET n 
1 27  LYS n 
1 28  LYS n 
1 29  ALA n 
1 30  MET n 
1 31  VAL n 
1 32  GLU n 
1 33  TYR n 
1 34  GLU n 
1 35  ILE n 
1 36  ASP n 
1 37  LEU n 
1 38  GLN n 
1 39  LYS n 
1 40  MET n 
1 41  PRO n 
1 42  LEU n 
1 43  GLY n 
1 44  LYS n 
1 45  LEU n 
1 46  SER n 
1 47  LYS n 
1 48  ARG n 
1 49  GLN n 
1 50  ILE n 
1 51  GLN n 
1 52  ALA n 
1 53  ALA n 
1 54  TYR n 
1 55  SER n 
1 56  ILE n 
1 57  LEU n 
1 58  SER n 
1 59  GLU n 
1 60  VAL n 
1 61  GLN n 
1 62  GLN n 
1 63  ALA n 
1 64  VAL n 
1 65  SER n 
1 66  GLN n 
1 67  GLY n 
1 68  SER n 
1 69  SER n 
1 70  ASP n 
1 71  SER n 
1 72  GLN n 
1 73  ILE n 
1 74  LEU n 
1 75  ASP n 
1 76  LEU n 
1 77  SER n 
1 78  ASN n 
1 79  ARG n 
1 80  PHE n 
1 81  TYR n 
1 82  THR n 
1 83  LEU n 
1 84  ILE n 
1 85  PRO n 
1 86  HIS n 
1 87  ASP n 
1 88  PHE n 
1 89  GLY n 
1 90  MET n 
1 91  LYS n 
1 92  LYS n 
1 93  PRO n 
1 94  PRO n 
1 95  LEU n 
1 96  LEU n 
1 97  ASN n 
1 98  ASN n 
1 99  ALA n 
1 100 ASP n 
1 101 SER n 
1 102 VAL n 
1 103 GLN n 
1 104 ALA n 
1 105 LYS n 
1 106 ALA n 
1 107 GLU n 
1 108 MET n 
1 109 LEU n 
1 110 ASP n 
1 111 ASN n 
1 112 LEU n 
1 113 LEU n 
1 114 ASP n 
1 115 ILE n 
1 116 GLU n 
1 117 VAL n 
1 118 ALA n 
1 119 TYR n 
1 120 SER n 
1 121 LEU n 
1 122 LEU n 
1 123 ARG n 
1 124 GLY n 
1 125 GLY n 
1 126 SER n 
1 127 ASP n 
1 128 ASP n 
1 129 SER n 
1 130 SER n 
1 131 LYS n 
1 132 ASP n 
1 133 PRO n 
1 134 ILE n 
1 135 ASP n 
1 136 VAL n 
1 137 ASN n 
1 138 TYR n 
1 139 GLU n 
1 140 LYS n 
1 141 LEU n 
1 142 LYS n 
1 143 THR n 
1 144 ASP n 
1 145 ILE n 
1 146 LYS n 
1 147 VAL n 
1 148 VAL n 
1 149 ASP n 
1 150 ARG n 
1 151 ASP n 
1 152 SER n 
1 153 GLU n 
1 154 GLU n 
1 155 ALA n 
1 156 GLU n 
1 157 ILE n 
1 158 ILE n 
1 159 ARG n 
1 160 LYS n 
1 161 TYR n 
1 162 VAL n 
1 163 LYS n 
1 164 ASN n 
1 165 THR n 
1 166 HIS n 
1 167 ALA n 
1 168 THR n 
1 169 THR n 
1 170 HIS n 
1 171 ASN n 
1 172 ALA n 
1 173 TYR n 
1 174 ASP n 
1 175 LEU n 
1 176 GLU n 
1 177 VAL n 
1 178 ILE n 
1 179 ASP n 
1 180 ILE n 
1 181 PHE n 
1 182 LYS n 
1 183 ILE n 
1 184 GLU n 
1 185 ARG n 
1 186 GLU n 
1 187 GLY n 
1 188 GLU n 
1 189 CYS n 
1 190 GLN n 
1 191 ARG n 
1 192 TYR n 
1 193 LYS n 
1 194 PRO n 
1 195 PHE n 
1 196 LYS n 
1 197 GLN n 
1 198 LEU n 
1 199 HIS n 
1 200 ASN n 
1 201 ARG n 
1 202 ARG n 
1 203 LEU n 
1 204 LEU n 
1 205 TRP n 
1 206 HIS n 
1 207 GLY n 
1 208 SER n 
1 209 ARG n 
1 210 THR n 
1 211 THR n 
1 212 ASN n 
1 213 PHE n 
1 214 ALA n 
1 215 GLY n 
1 216 ILE n 
1 217 LEU n 
1 218 SER n 
1 219 GLN n 
1 220 GLY n 
1 221 LEU n 
1 222 ARG n 
1 223 ILE n 
1 224 ALA n 
1 225 PRO n 
1 226 PRO n 
1 227 GLU n 
1 228 ALA n 
1 229 PRO n 
1 230 VAL n 
1 231 THR n 
1 232 GLY n 
1 233 TYR n 
1 234 MET n 
1 235 PHE n 
1 236 GLY n 
1 237 LYS n 
1 238 GLY n 
1 239 ILE n 
1 240 TYR n 
1 241 PHE n 
1 242 ALA n 
1 243 ASP n 
1 244 MET n 
1 245 VAL n 
1 246 SER n 
1 247 LYS n 
1 248 SER n 
1 249 ALA n 
1 250 ASN n 
1 251 TYR n 
1 252 CYS n 
1 253 HIS n 
1 254 THR n 
1 255 SER n 
1 256 GLN n 
1 257 GLY n 
1 258 ASP n 
1 259 PRO n 
1 260 ILE n 
1 261 GLY n 
1 262 LEU n 
1 263 ILE n 
1 264 LEU n 
1 265 LEU n 
1 266 GLY n 
1 267 GLU n 
1 268 VAL n 
1 269 ALA n 
1 270 LEU n 
1 271 GLY n 
1 272 ASN n 
1 273 MET n 
1 274 TYR n 
1 275 GLU n 
1 276 LEU n 
1 277 LYS n 
1 278 HIS n 
1 279 ALA n 
1 280 SER n 
1 281 HIS n 
1 282 ILE n 
1 283 SER n 
1 284 LYS n 
1 285 LEU n 
1 286 PRO n 
1 287 LYS n 
1 288 GLY n 
1 289 LYS n 
1 290 HIS n 
1 291 SER n 
1 292 VAL n 
1 293 LYS n 
1 294 GLY n 
1 295 LEU n 
1 296 GLY n 
1 297 LYS n 
1 298 THR n 
1 299 THR n 
1 300 PRO n 
1 301 ASP n 
1 302 PRO n 
1 303 SER n 
1 304 ALA n 
1 305 ASN n 
1 306 ILE n 
1 307 SER n 
1 308 LEU n 
1 309 ASP n 
1 310 GLY n 
1 311 VAL n 
1 312 ASP n 
1 313 VAL n 
1 314 PRO n 
1 315 LEU n 
1 316 GLY n 
1 317 THR n 
1 318 GLY n 
1 319 ILE n 
1 320 SER n 
1 321 SER n 
1 322 GLY n 
1 323 VAL n 
1 324 ASN n 
1 325 ASP n 
1 326 THR n 
1 327 SER n 
1 328 LEU n 
1 329 LEU n 
1 330 TYR n 
1 331 ASN n 
1 332 GLU n 
1 333 TYR n 
1 334 ILE n 
1 335 VAL n 
1 336 TYR n 
1 337 ASP n 
1 338 ILE n 
1 339 ALA n 
1 340 GLN n 
1 341 VAL n 
1 342 ASN n 
1 343 LEU n 
1 344 LYS n 
1 345 TYR n 
1 346 LEU n 
1 347 LEU n 
1 348 LYS n 
1 349 LEU n 
1 350 LYS n 
1 351 PHE n 
1 352 ASN n 
1 353 PHE n 
1 354 LYS n 
1 355 THR 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                   355 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'PARP1, ADPRT, PPOL' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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 
A1H64 non-polymer         . 
;6-fluoranyl-5-[4-[(5-fluoranyl-2-methyl-3-oxidanylidene-4~{H}-quinoxalin-6-yl)methyl]piperazin-1-yl]-~{N}-methyl-pyridine-2-carboxamide
;
? 'C21 H22 F2 N6 O2' 428.435 
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 
SO4   non-polymer         . 'SULFATE ION' ? 'O4 S -2'          96.063  
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   657  ?    ?   ?   A . n 
A 1 2   PRO 2   658  ?    ?   ?   A . n 
A 1 3   LEU 3   659  ?    ?   ?   A . n 
A 1 4   GLY 4   660  ?    ?   ?   A . n 
A 1 5   SER 5   661  ?    ?   ?   A . n 
A 1 6   LYS 6   662  662  LYS LYS A . n 
A 1 7   SER 7   663  663  SER SER A . n 
A 1 8   LYS 8   664  664  LYS LYS A . n 
A 1 9   LEU 9   665  665  LEU LEU A . n 
A 1 10  PRO 10  666  666  PRO PRO A . n 
A 1 11  LYS 11  667  667  LYS LYS A . n 
A 1 12  PRO 12  668  668  PRO PRO A . n 
A 1 13  VAL 13  669  669  VAL VAL A . n 
A 1 14  GLN 14  670  670  GLN GLN A . n 
A 1 15  ASP 15  671  671  ASP ASP A . n 
A 1 16  LEU 16  672  672  LEU LEU A . n 
A 1 17  ILE 17  673  673  ILE ILE A . n 
A 1 18  LYS 18  674  674  LYS LYS A . n 
A 1 19  MET 19  675  675  MET MET A . n 
A 1 20  ILE 20  676  676  ILE ILE A . n 
A 1 21  PHE 21  677  677  PHE PHE A . n 
A 1 22  ASP 22  678  678  ASP ASP A . n 
A 1 23  VAL 23  679  679  VAL VAL A . n 
A 1 24  GLU 24  680  680  GLU GLU A . n 
A 1 25  SER 25  681  681  SER SER A . n 
A 1 26  MET 26  682  682  MET MET A . n 
A 1 27  LYS 27  683  683  LYS LYS A . n 
A 1 28  LYS 28  684  684  LYS LYS A . n 
A 1 29  ALA 29  685  685  ALA ALA A . n 
A 1 30  MET 30  686  686  MET MET A . n 
A 1 31  VAL 31  687  687  VAL VAL A . n 
A 1 32  GLU 32  688  688  GLU GLU A . n 
A 1 33  TYR 33  689  689  TYR TYR A . n 
A 1 34  GLU 34  690  690  GLU GLU A . n 
A 1 35  ILE 35  691  691  ILE ILE A . n 
A 1 36  ASP 36  692  692  ASP ASP A . n 
A 1 37  LEU 37  693  693  LEU LEU A . n 
A 1 38  GLN 38  694  694  GLN GLN A . n 
A 1 39  LYS 39  695  695  LYS LYS A . n 
A 1 40  MET 40  696  696  MET MET A . n 
A 1 41  PRO 41  697  697  PRO PRO A . n 
A 1 42  LEU 42  698  698  LEU LEU A . n 
A 1 43  GLY 43  699  699  GLY GLY A . n 
A 1 44  LYS 44  700  700  LYS LYS A . n 
A 1 45  LEU 45  701  701  LEU LEU A . n 
A 1 46  SER 46  702  702  SER SER A . n 
A 1 47  LYS 47  703  703  LYS LYS A . n 
A 1 48  ARG 48  704  704  ARG ARG A . n 
A 1 49  GLN 49  705  705  GLN GLN A . n 
A 1 50  ILE 50  706  706  ILE ILE A . n 
A 1 51  GLN 51  707  707  GLN GLN A . n 
A 1 52  ALA 52  708  708  ALA ALA A . n 
A 1 53  ALA 53  709  709  ALA ALA A . n 
A 1 54  TYR 54  710  710  TYR TYR A . n 
A 1 55  SER 55  711  711  SER SER A . n 
A 1 56  ILE 56  712  712  ILE ILE A . n 
A 1 57  LEU 57  713  713  LEU LEU A . n 
A 1 58  SER 58  714  714  SER SER A . n 
A 1 59  GLU 59  715  715  GLU GLU A . n 
A 1 60  VAL 60  716  716  VAL VAL A . n 
A 1 61  GLN 61  717  717  GLN GLN A . n 
A 1 62  GLN 62  718  718  GLN GLN A . n 
A 1 63  ALA 63  719  719  ALA ALA A . n 
A 1 64  VAL 64  720  720  VAL VAL A . n 
A 1 65  SER 65  721  721  SER SER A . n 
A 1 66  GLN 66  722  722  GLN GLN A . n 
A 1 67  GLY 67  723  723  GLY GLY A . n 
A 1 68  SER 68  724  724  SER SER A . n 
A 1 69  SER 69  725  725  SER SER A . n 
A 1 70  ASP 70  726  726  ASP ASP A . n 
A 1 71  SER 71  727  727  SER SER A . n 
A 1 72  GLN 72  728  728  GLN GLN A . n 
A 1 73  ILE 73  729  729  ILE ILE A . n 
A 1 74  LEU 74  730  730  LEU LEU A . n 
A 1 75  ASP 75  731  731  ASP ASP A . n 
A 1 76  LEU 76  732  732  LEU LEU A . n 
A 1 77  SER 77  733  733  SER SER A . n 
A 1 78  ASN 78  734  734  ASN ASN A . n 
A 1 79  ARG 79  735  735  ARG ARG A . n 
A 1 80  PHE 80  736  736  PHE PHE A . n 
A 1 81  TYR 81  737  737  TYR TYR A . n 
A 1 82  THR 82  738  738  THR THR A . n 
A 1 83  LEU 83  739  739  LEU LEU A . n 
A 1 84  ILE 84  740  740  ILE ILE A . n 
A 1 85  PRO 85  741  741  PRO PRO A . n 
A 1 86  HIS 86  742  742  HIS HIS A . n 
A 1 87  ASP 87  743  743  ASP ASP A . n 
A 1 88  PHE 88  744  744  PHE PHE A . n 
A 1 89  GLY 89  745  745  GLY GLY A . n 
A 1 90  MET 90  746  746  MET MET A . n 
A 1 91  LYS 91  747  747  LYS LYS A . n 
A 1 92  LYS 92  748  748  LYS LYS A . n 
A 1 93  PRO 93  749  749  PRO PRO A . n 
A 1 94  PRO 94  750  750  PRO PRO A . n 
A 1 95  LEU 95  751  751  LEU LEU A . n 
A 1 96  LEU 96  752  752  LEU LEU A . n 
A 1 97  ASN 97  753  753  ASN ASN A . n 
A 1 98  ASN 98  754  754  ASN ASN A . n 
A 1 99  ALA 99  755  755  ALA ALA A . n 
A 1 100 ASP 100 756  756  ASP ASP A . n 
A 1 101 SER 101 757  757  SER SER A . n 
A 1 102 VAL 102 758  758  VAL VAL A . n 
A 1 103 GLN 103 759  759  GLN GLN A . n 
A 1 104 ALA 104 760  760  ALA ALA A . n 
A 1 105 LYS 105 761  761  LYS LYS A . n 
A 1 106 ALA 106 762  762  ALA ALA A . n 
A 1 107 GLU 107 763  763  GLU GLU A . n 
A 1 108 MET 108 764  764  MET MET A . n 
A 1 109 LEU 109 765  765  LEU LEU A . n 
A 1 110 ASP 110 766  766  ASP ASP A . n 
A 1 111 ASN 111 767  767  ASN ASN A . n 
A 1 112 LEU 112 768  768  LEU LEU A . n 
A 1 113 LEU 113 769  769  LEU LEU A . n 
A 1 114 ASP 114 770  770  ASP ASP A . n 
A 1 115 ILE 115 771  771  ILE ILE A . n 
A 1 116 GLU 116 772  772  GLU GLU A . n 
A 1 117 VAL 117 773  773  VAL VAL A . n 
A 1 118 ALA 118 774  774  ALA ALA A . n 
A 1 119 TYR 119 775  775  TYR TYR A . n 
A 1 120 SER 120 776  776  SER SER A . n 
A 1 121 LEU 121 777  777  LEU LEU A . n 
A 1 122 LEU 122 778  778  LEU LEU A . n 
A 1 123 ARG 123 779  779  ARG ARG A . n 
A 1 124 GLY 124 780  780  GLY GLY A . n 
A 1 125 GLY 125 781  781  GLY GLY A . n 
A 1 126 SER 126 782  782  SER SER A . n 
A 1 127 ASP 127 783  783  ASP ASP A . n 
A 1 128 ASP 128 784  784  ASP ASP A . n 
A 1 129 SER 129 785  785  SER SER A . n 
A 1 130 SER 130 786  786  SER SER A . n 
A 1 131 LYS 131 787  787  LYS LYS A . n 
A 1 132 ASP 132 788  788  ASP ASP A . n 
A 1 133 PRO 133 789  789  PRO PRO A . n 
A 1 134 ILE 134 790  790  ILE ILE A . n 
A 1 135 ASP 135 791  791  ASP ASP A . n 
A 1 136 VAL 136 792  792  VAL VAL A . n 
A 1 137 ASN 137 793  793  ASN ASN A . n 
A 1 138 TYR 138 794  794  TYR TYR A . n 
A 1 139 GLU 139 795  795  GLU GLU A . n 
A 1 140 LYS 140 796  796  LYS LYS A . n 
A 1 141 LEU 141 797  797  LEU LEU A . n 
A 1 142 LYS 142 798  798  LYS LYS A . n 
A 1 143 THR 143 799  799  THR THR A . n 
A 1 144 ASP 144 800  800  ASP ASP A . n 
A 1 145 ILE 145 801  801  ILE ILE A . n 
A 1 146 LYS 146 802  802  LYS LYS A . n 
A 1 147 VAL 147 803  803  VAL VAL A . n 
A 1 148 VAL 148 804  804  VAL VAL A . n 
A 1 149 ASP 149 805  805  ASP ASP A . n 
A 1 150 ARG 150 806  806  ARG ARG A . n 
A 1 151 ASP 151 807  807  ASP ASP A . n 
A 1 152 SER 152 808  808  SER SER A . n 
A 1 153 GLU 153 809  809  GLU GLU A . n 
A 1 154 GLU 154 810  810  GLU GLU A . n 
A 1 155 ALA 155 811  811  ALA ALA A . n 
A 1 156 GLU 156 812  812  GLU GLU A . n 
A 1 157 ILE 157 813  813  ILE ILE A . n 
A 1 158 ILE 158 814  814  ILE ILE A . n 
A 1 159 ARG 159 815  815  ARG ARG A . n 
A 1 160 LYS 160 816  816  LYS LYS A . n 
A 1 161 TYR 161 817  817  TYR TYR A . n 
A 1 162 VAL 162 818  818  VAL VAL A . n 
A 1 163 LYS 163 819  819  LYS LYS A . n 
A 1 164 ASN 164 820  820  ASN ASN A . n 
A 1 165 THR 165 821  821  THR THR A . n 
A 1 166 HIS 166 822  822  HIS HIS A . n 
A 1 167 ALA 167 823  823  ALA ALA A . n 
A 1 168 THR 168 824  824  THR THR A . n 
A 1 169 THR 169 825  825  THR THR A . n 
A 1 170 HIS 170 826  826  HIS HIS A . n 
A 1 171 ASN 171 827  827  ASN ASN A . n 
A 1 172 ALA 172 828  828  ALA ALA A . n 
A 1 173 TYR 173 829  829  TYR TYR A . n 
A 1 174 ASP 174 830  830  ASP ASP A . n 
A 1 175 LEU 175 831  831  LEU LEU A . n 
A 1 176 GLU 176 832  832  GLU GLU A . n 
A 1 177 VAL 177 833  833  VAL VAL A . n 
A 1 178 ILE 178 834  834  ILE ILE A . n 
A 1 179 ASP 179 835  835  ASP ASP A . n 
A 1 180 ILE 180 836  836  ILE ILE A . n 
A 1 181 PHE 181 837  837  PHE PHE A . n 
A 1 182 LYS 182 838  838  LYS LYS A . n 
A 1 183 ILE 183 839  839  ILE ILE A . n 
A 1 184 GLU 184 840  840  GLU GLU A . n 
A 1 185 ARG 185 841  841  ARG ARG A . n 
A 1 186 GLU 186 842  842  GLU GLU A . n 
A 1 187 GLY 187 843  843  GLY GLY A . n 
A 1 188 GLU 188 844  844  GLU GLU A . n 
A 1 189 CYS 189 845  845  CYS CYS A . n 
A 1 190 GLN 190 846  846  GLN GLN A . n 
A 1 191 ARG 191 847  847  ARG ARG A . n 
A 1 192 TYR 192 848  848  TYR TYR A . n 
A 1 193 LYS 193 849  849  LYS LYS A . n 
A 1 194 PRO 194 850  850  PRO PRO A . n 
A 1 195 PHE 195 851  851  PHE PHE A . n 
A 1 196 LYS 196 852  852  LYS LYS A . n 
A 1 197 GLN 197 853  853  GLN GLN A . n 
A 1 198 LEU 198 854  854  LEU LEU A . n 
A 1 199 HIS 199 855  855  HIS HIS A . n 
A 1 200 ASN 200 856  856  ASN ASN A . n 
A 1 201 ARG 201 857  857  ARG ARG A . n 
A 1 202 ARG 202 858  858  ARG ARG A . n 
A 1 203 LEU 203 859  859  LEU LEU A . n 
A 1 204 LEU 204 860  860  LEU LEU A . n 
A 1 205 TRP 205 861  861  TRP TRP A . n 
A 1 206 HIS 206 862  862  HIS HIS A . n 
A 1 207 GLY 207 863  863  GLY GLY A . n 
A 1 208 SER 208 864  864  SER SER A . n 
A 1 209 ARG 209 865  865  ARG ARG A . n 
A 1 210 THR 210 866  866  THR THR A . n 
A 1 211 THR 211 867  867  THR THR A . n 
A 1 212 ASN 212 868  868  ASN ASN A . n 
A 1 213 PHE 213 869  869  PHE PHE A . n 
A 1 214 ALA 214 870  870  ALA ALA A . n 
A 1 215 GLY 215 871  871  GLY GLY A . n 
A 1 216 ILE 216 872  872  ILE ILE A . n 
A 1 217 LEU 217 873  873  LEU LEU A . n 
A 1 218 SER 218 874  874  SER SER A . n 
A 1 219 GLN 219 875  875  GLN GLN A . n 
A 1 220 GLY 220 876  876  GLY GLY A . n 
A 1 221 LEU 221 877  877  LEU LEU A . n 
A 1 222 ARG 222 878  878  ARG ARG A . n 
A 1 223 ILE 223 879  879  ILE ILE A . n 
A 1 224 ALA 224 880  880  ALA ALA A . n 
A 1 225 PRO 225 881  881  PRO PRO A . n 
A 1 226 PRO 226 882  882  PRO PRO A . n 
A 1 227 GLU 227 883  883  GLU GLU A . n 
A 1 228 ALA 228 884  884  ALA ALA A . n 
A 1 229 PRO 229 885  885  PRO PRO A . n 
A 1 230 VAL 230 886  886  VAL VAL A . n 
A 1 231 THR 231 887  887  THR THR A . n 
A 1 232 GLY 232 888  888  GLY GLY A . n 
A 1 233 TYR 233 889  889  TYR TYR A . n 
A 1 234 MET 234 890  890  MET MET A . n 
A 1 235 PHE 235 891  891  PHE PHE A . n 
A 1 236 GLY 236 892  892  GLY GLY A . n 
A 1 237 LYS 237 893  893  LYS LYS A . n 
A 1 238 GLY 238 894  894  GLY GLY A . n 
A 1 239 ILE 239 895  895  ILE ILE A . n 
A 1 240 TYR 240 896  896  TYR TYR A . n 
A 1 241 PHE 241 897  897  PHE PHE A . n 
A 1 242 ALA 242 898  898  ALA ALA A . n 
A 1 243 ASP 243 899  899  ASP ASP A . n 
A 1 244 MET 244 900  900  MET MET A . n 
A 1 245 VAL 245 901  901  VAL VAL A . n 
A 1 246 SER 246 902  902  SER SER A . n 
A 1 247 LYS 247 903  903  LYS LYS A . n 
A 1 248 SER 248 904  904  SER SER A . n 
A 1 249 ALA 249 905  905  ALA ALA A . n 
A 1 250 ASN 250 906  906  ASN ASN A . n 
A 1 251 TYR 251 907  907  TYR TYR A . n 
A 1 252 CYS 252 908  908  CYS CYS A . n 
A 1 253 HIS 253 909  909  HIS HIS A . n 
A 1 254 THR 254 910  910  THR THR A . n 
A 1 255 SER 255 911  911  SER SER A . n 
A 1 256 GLN 256 912  912  GLN GLN A . n 
A 1 257 GLY 257 913  913  GLY GLY A . n 
A 1 258 ASP 258 914  914  ASP ASP A . n 
A 1 259 PRO 259 915  915  PRO PRO A . n 
A 1 260 ILE 260 916  916  ILE ILE A . n 
A 1 261 GLY 261 917  917  GLY GLY A . n 
A 1 262 LEU 262 918  918  LEU LEU A . n 
A 1 263 ILE 263 919  919  ILE ILE A . n 
A 1 264 LEU 264 920  920  LEU LEU A . n 
A 1 265 LEU 265 921  921  LEU LEU A . n 
A 1 266 GLY 266 922  922  GLY GLY A . n 
A 1 267 GLU 267 923  923  GLU GLU A . n 
A 1 268 VAL 268 924  924  VAL VAL A . n 
A 1 269 ALA 269 925  925  ALA ALA A . n 
A 1 270 LEU 270 926  926  LEU LEU A . n 
A 1 271 GLY 271 927  927  GLY GLY A . n 
A 1 272 ASN 272 928  928  ASN ASN A . n 
A 1 273 MET 273 929  929  MET MET A . n 
A 1 274 TYR 274 930  930  TYR TYR A . n 
A 1 275 GLU 275 931  931  GLU GLU A . n 
A 1 276 LEU 276 932  932  LEU LEU A . n 
A 1 277 LYS 277 933  933  LYS LYS A . n 
A 1 278 HIS 278 934  934  HIS HIS A . n 
A 1 279 ALA 279 935  935  ALA ALA A . n 
A 1 280 SER 280 936  936  SER SER A . n 
A 1 281 HIS 281 937  937  HIS HIS A . n 
A 1 282 ILE 282 938  938  ILE ILE A . n 
A 1 283 SER 283 939  939  SER SER A . n 
A 1 284 LYS 284 940  940  LYS LYS A . n 
A 1 285 LEU 285 941  941  LEU LEU A . n 
A 1 286 PRO 286 942  942  PRO PRO A . n 
A 1 287 LYS 287 943  943  LYS LYS A . n 
A 1 288 GLY 288 944  944  GLY GLY A . n 
A 1 289 LYS 289 945  945  LYS LYS A . n 
A 1 290 HIS 290 946  946  HIS HIS A . n 
A 1 291 SER 291 947  947  SER SER A . n 
A 1 292 VAL 292 948  948  VAL VAL A . n 
A 1 293 LYS 293 949  949  LYS LYS A . n 
A 1 294 GLY 294 950  950  GLY GLY A . n 
A 1 295 LEU 295 951  951  LEU LEU A . n 
A 1 296 GLY 296 952  952  GLY GLY A . n 
A 1 297 LYS 297 953  953  LYS LYS A . n 
A 1 298 THR 298 954  954  THR THR A . n 
A 1 299 THR 299 955  955  THR THR A . n 
A 1 300 PRO 300 956  956  PRO PRO A . n 
A 1 301 ASP 301 957  957  ASP ASP A . n 
A 1 302 PRO 302 958  958  PRO PRO A . n 
A 1 303 SER 303 959  959  SER SER A . n 
A 1 304 ALA 304 960  960  ALA ALA A . n 
A 1 305 ASN 305 961  961  ASN ASN A . n 
A 1 306 ILE 306 962  962  ILE ILE A . n 
A 1 307 SER 307 963  963  SER SER A . n 
A 1 308 LEU 308 964  964  LEU LEU A . n 
A 1 309 ASP 309 965  965  ASP ASP A . n 
A 1 310 GLY 310 966  966  GLY GLY A . n 
A 1 311 VAL 311 967  967  VAL VAL A . n 
A 1 312 ASP 312 968  968  ASP ASP A . n 
A 1 313 VAL 313 969  969  VAL VAL A . n 
A 1 314 PRO 314 970  970  PRO PRO A . n 
A 1 315 LEU 315 971  971  LEU LEU A . n 
A 1 316 GLY 316 972  972  GLY GLY A . n 
A 1 317 THR 317 973  973  THR THR A . n 
A 1 318 GLY 318 974  974  GLY GLY A . n 
A 1 319 ILE 319 975  975  ILE ILE A . n 
A 1 320 SER 320 976  976  SER SER A . n 
A 1 321 SER 321 977  977  SER SER A . n 
A 1 322 GLY 322 978  978  GLY GLY A . n 
A 1 323 VAL 323 979  979  VAL VAL A . n 
A 1 324 ASN 324 980  980  ASN ASN A . n 
A 1 325 ASP 325 981  981  ASP ASP A . n 
A 1 326 THR 326 982  982  THR THR A . n 
A 1 327 SER 327 983  983  SER SER A . n 
A 1 328 LEU 328 984  984  LEU LEU A . n 
A 1 329 LEU 329 985  985  LEU LEU A . n 
A 1 330 TYR 330 986  986  TYR TYR A . n 
A 1 331 ASN 331 987  987  ASN ASN A . n 
A 1 332 GLU 332 988  988  GLU GLU A . n 
A 1 333 TYR 333 989  989  TYR TYR A . n 
A 1 334 ILE 334 990  990  ILE ILE A . n 
A 1 335 VAL 335 991  991  VAL VAL A . n 
A 1 336 TYR 336 992  992  TYR TYR A . n 
A 1 337 ASP 337 993  993  ASP ASP A . n 
A 1 338 ILE 338 994  994  ILE ILE A . n 
A 1 339 ALA 339 995  995  ALA ALA A . n 
A 1 340 GLN 340 996  996  GLN GLN A . n 
A 1 341 VAL 341 997  997  VAL VAL A . n 
A 1 342 ASN 342 998  998  ASN ASN A . n 
A 1 343 LEU 343 999  999  LEU LEU A . n 
A 1 344 LYS 344 1000 1000 LYS LYS A . n 
A 1 345 TYR 345 1001 1001 TYR TYR A . n 
A 1 346 LEU 346 1002 1002 LEU LEU A . n 
A 1 347 LEU 347 1003 1003 LEU LEU A . n 
A 1 348 LYS 348 1004 1004 LYS LYS A . n 
A 1 349 LEU 349 1005 1005 LEU LEU A . n 
A 1 350 LYS 350 1006 1006 LYS LYS A . n 
A 1 351 PHE 351 1007 1007 PHE PHE A . n 
A 1 352 ASN 352 1008 1008 ASN ASN A . n 
A 1 353 PHE 353 1009 1009 PHE PHE A . n 
A 1 354 LYS 354 1010 1010 LYS LYS A . n 
A 1 355 THR 355 1011 1011 THR THR A . n 
B 1 1   GLY 1   657  ?    ?   ?   B . n 
B 1 2   PRO 2   658  ?    ?   ?   B . n 
B 1 3   LEU 3   659  ?    ?   ?   B . n 
B 1 4   GLY 4   660  ?    ?   ?   B . n 
B 1 5   SER 5   661  ?    ?   ?   B . n 
B 1 6   LYS 6   662  662  LYS LYS B . n 
B 1 7   SER 7   663  663  SER SER B . n 
B 1 8   LYS 8   664  664  LYS LYS B . n 
B 1 9   LEU 9   665  665  LEU LEU B . n 
B 1 10  PRO 10  666  666  PRO PRO B . n 
B 1 11  LYS 11  667  667  LYS LYS B . n 
B 1 12  PRO 12  668  668  PRO PRO B . n 
B 1 13  VAL 13  669  669  VAL VAL B . n 
B 1 14  GLN 14  670  670  GLN GLN B . n 
B 1 15  ASP 15  671  671  ASP ASP B . n 
B 1 16  LEU 16  672  672  LEU LEU B . n 
B 1 17  ILE 17  673  673  ILE ILE B . n 
B 1 18  LYS 18  674  674  LYS LYS B . n 
B 1 19  MET 19  675  675  MET MET B . n 
B 1 20  ILE 20  676  676  ILE ILE B . n 
B 1 21  PHE 21  677  677  PHE PHE B . n 
B 1 22  ASP 22  678  678  ASP ASP B . n 
B 1 23  VAL 23  679  679  VAL VAL B . n 
B 1 24  GLU 24  680  680  GLU GLU B . n 
B 1 25  SER 25  681  681  SER SER B . n 
B 1 26  MET 26  682  682  MET MET B . n 
B 1 27  LYS 27  683  683  LYS LYS B . n 
B 1 28  LYS 28  684  684  LYS LYS B . n 
B 1 29  ALA 29  685  685  ALA ALA B . n 
B 1 30  MET 30  686  686  MET MET B . n 
B 1 31  VAL 31  687  687  VAL VAL B . n 
B 1 32  GLU 32  688  688  GLU GLU B . n 
B 1 33  TYR 33  689  689  TYR TYR B . n 
B 1 34  GLU 34  690  690  GLU GLU B . n 
B 1 35  ILE 35  691  691  ILE ILE B . n 
B 1 36  ASP 36  692  692  ASP ASP B . n 
B 1 37  LEU 37  693  693  LEU LEU B . n 
B 1 38  GLN 38  694  694  GLN GLN B . n 
B 1 39  LYS 39  695  695  LYS LYS B . n 
B 1 40  MET 40  696  696  MET MET B . n 
B 1 41  PRO 41  697  697  PRO PRO B . n 
B 1 42  LEU 42  698  698  LEU LEU B . n 
B 1 43  GLY 43  699  699  GLY GLY B . n 
B 1 44  LYS 44  700  700  LYS LYS B . n 
B 1 45  LEU 45  701  701  LEU LEU B . n 
B 1 46  SER 46  702  702  SER SER B . n 
B 1 47  LYS 47  703  703  LYS LYS B . n 
B 1 48  ARG 48  704  704  ARG ARG B . n 
B 1 49  GLN 49  705  705  GLN GLN B . n 
B 1 50  ILE 50  706  706  ILE ILE B . n 
B 1 51  GLN 51  707  707  GLN GLN B . n 
B 1 52  ALA 52  708  708  ALA ALA B . n 
B 1 53  ALA 53  709  709  ALA ALA B . n 
B 1 54  TYR 54  710  710  TYR TYR B . n 
B 1 55  SER 55  711  711  SER SER B . n 
B 1 56  ILE 56  712  712  ILE ILE B . n 
B 1 57  LEU 57  713  713  LEU LEU B . n 
B 1 58  SER 58  714  714  SER SER B . n 
B 1 59  GLU 59  715  715  GLU GLU B . n 
B 1 60  VAL 60  716  716  VAL VAL B . n 
B 1 61  GLN 61  717  717  GLN GLN B . n 
B 1 62  GLN 62  718  718  GLN GLN B . n 
B 1 63  ALA 63  719  719  ALA ALA B . n 
B 1 64  VAL 64  720  720  VAL VAL B . n 
B 1 65  SER 65  721  721  SER SER B . n 
B 1 66  GLN 66  722  722  GLN GLN B . n 
B 1 67  GLY 67  723  723  GLY GLY B . n 
B 1 68  SER 68  724  724  SER SER B . n 
B 1 69  SER 69  725  725  SER SER B . n 
B 1 70  ASP 70  726  726  ASP ASP B . n 
B 1 71  SER 71  727  727  SER SER B . n 
B 1 72  GLN 72  728  728  GLN GLN B . n 
B 1 73  ILE 73  729  729  ILE ILE B . n 
B 1 74  LEU 74  730  730  LEU LEU B . n 
B 1 75  ASP 75  731  731  ASP ASP B . n 
B 1 76  LEU 76  732  732  LEU LEU B . n 
B 1 77  SER 77  733  733  SER SER B . n 
B 1 78  ASN 78  734  734  ASN ASN B . n 
B 1 79  ARG 79  735  735  ARG ARG B . n 
B 1 80  PHE 80  736  736  PHE PHE B . n 
B 1 81  TYR 81  737  737  TYR TYR B . n 
B 1 82  THR 82  738  738  THR THR B . n 
B 1 83  LEU 83  739  739  LEU LEU B . n 
B 1 84  ILE 84  740  740  ILE ILE B . n 
B 1 85  PRO 85  741  741  PRO PRO B . n 
B 1 86  HIS 86  742  742  HIS HIS B . n 
B 1 87  ASP 87  743  743  ASP ASP B . n 
B 1 88  PHE 88  744  744  PHE PHE B . n 
B 1 89  GLY 89  745  745  GLY GLY B . n 
B 1 90  MET 90  746  746  MET MET B . n 
B 1 91  LYS 91  747  747  LYS LYS B . n 
B 1 92  LYS 92  748  748  LYS LYS B . n 
B 1 93  PRO 93  749  749  PRO PRO B . n 
B 1 94  PRO 94  750  750  PRO PRO B . n 
B 1 95  LEU 95  751  751  LEU LEU B . n 
B 1 96  LEU 96  752  752  LEU LEU B . n 
B 1 97  ASN 97  753  753  ASN ASN B . n 
B 1 98  ASN 98  754  754  ASN ASN B . n 
B 1 99  ALA 99  755  755  ALA ALA B . n 
B 1 100 ASP 100 756  756  ASP ASP B . n 
B 1 101 SER 101 757  757  SER SER B . n 
B 1 102 VAL 102 758  758  VAL VAL B . n 
B 1 103 GLN 103 759  759  GLN GLN B . n 
B 1 104 ALA 104 760  760  ALA ALA B . n 
B 1 105 LYS 105 761  761  LYS LYS B . n 
B 1 106 ALA 106 762  762  ALA ALA B . n 
B 1 107 GLU 107 763  763  GLU GLU B . n 
B 1 108 MET 108 764  764  MET MET B . n 
B 1 109 LEU 109 765  765  LEU LEU B . n 
B 1 110 ASP 110 766  766  ASP ASP B . n 
B 1 111 ASN 111 767  767  ASN ASN B . n 
B 1 112 LEU 112 768  768  LEU LEU B . n 
B 1 113 LEU 113 769  769  LEU LEU B . n 
B 1 114 ASP 114 770  770  ASP ASP B . n 
B 1 115 ILE 115 771  771  ILE ILE B . n 
B 1 116 GLU 116 772  772  GLU GLU B . n 
B 1 117 VAL 117 773  773  VAL VAL B . n 
B 1 118 ALA 118 774  774  ALA ALA B . n 
B 1 119 TYR 119 775  775  TYR TYR B . n 
B 1 120 SER 120 776  776  SER SER B . n 
B 1 121 LEU 121 777  777  LEU LEU B . n 
B 1 122 LEU 122 778  778  LEU LEU B . n 
B 1 123 ARG 123 779  779  ARG ARG B . n 
B 1 124 GLY 124 780  780  GLY GLY B . n 
B 1 125 GLY 125 781  781  GLY GLY B . n 
B 1 126 SER 126 782  782  SER SER B . n 
B 1 127 ASP 127 783  783  ASP ASP B . n 
B 1 128 ASP 128 784  784  ASP ASP B . n 
B 1 129 SER 129 785  785  SER SER B . n 
B 1 130 SER 130 786  786  SER SER B . n 
B 1 131 LYS 131 787  787  LYS LYS B . n 
B 1 132 ASP 132 788  788  ASP ASP B . n 
B 1 133 PRO 133 789  789  PRO PRO B . n 
B 1 134 ILE 134 790  790  ILE ILE B . n 
B 1 135 ASP 135 791  791  ASP ASP B . n 
B 1 136 VAL 136 792  792  VAL VAL B . n 
B 1 137 ASN 137 793  793  ASN ASN B . n 
B 1 138 TYR 138 794  794  TYR TYR B . n 
B 1 139 GLU 139 795  795  GLU GLU B . n 
B 1 140 LYS 140 796  796  LYS LYS B . n 
B 1 141 LEU 141 797  797  LEU LEU B . n 
B 1 142 LYS 142 798  798  LYS LYS B . n 
B 1 143 THR 143 799  799  THR THR B . n 
B 1 144 ASP 144 800  800  ASP ASP B . n 
B 1 145 ILE 145 801  801  ILE ILE B . n 
B 1 146 LYS 146 802  802  LYS LYS B . n 
B 1 147 VAL 147 803  803  VAL VAL B . n 
B 1 148 VAL 148 804  804  VAL VAL B . n 
B 1 149 ASP 149 805  805  ASP ASP B . n 
B 1 150 ARG 150 806  806  ARG ARG B . n 
B 1 151 ASP 151 807  807  ASP ASP B . n 
B 1 152 SER 152 808  808  SER SER B . n 
B 1 153 GLU 153 809  809  GLU GLU B . n 
B 1 154 GLU 154 810  810  GLU GLU B . n 
B 1 155 ALA 155 811  811  ALA ALA B . n 
B 1 156 GLU 156 812  812  GLU GLU B . n 
B 1 157 ILE 157 813  813  ILE ILE B . n 
B 1 158 ILE 158 814  814  ILE ILE B . n 
B 1 159 ARG 159 815  815  ARG ARG B . n 
B 1 160 LYS 160 816  816  LYS LYS B . n 
B 1 161 TYR 161 817  817  TYR TYR B . n 
B 1 162 VAL 162 818  818  VAL VAL B . n 
B 1 163 LYS 163 819  819  LYS LYS B . n 
B 1 164 ASN 164 820  820  ASN ASN B . n 
B 1 165 THR 165 821  821  THR THR B . n 
B 1 166 HIS 166 822  822  HIS HIS B . n 
B 1 167 ALA 167 823  823  ALA ALA B . n 
B 1 168 THR 168 824  824  THR THR B . n 
B 1 169 THR 169 825  825  THR THR B . n 
B 1 170 HIS 170 826  826  HIS HIS B . n 
B 1 171 ASN 171 827  827  ASN ASN B . n 
B 1 172 ALA 172 828  828  ALA ALA B . n 
B 1 173 TYR 173 829  829  TYR TYR B . n 
B 1 174 ASP 174 830  830  ASP ASP B . n 
B 1 175 LEU 175 831  831  LEU LEU B . n 
B 1 176 GLU 176 832  832  GLU GLU B . n 
B 1 177 VAL 177 833  833  VAL VAL B . n 
B 1 178 ILE 178 834  834  ILE ILE B . n 
B 1 179 ASP 179 835  835  ASP ASP B . n 
B 1 180 ILE 180 836  836  ILE ILE B . n 
B 1 181 PHE 181 837  837  PHE PHE B . n 
B 1 182 LYS 182 838  838  LYS LYS B . n 
B 1 183 ILE 183 839  839  ILE ILE B . n 
B 1 184 GLU 184 840  840  GLU GLU B . n 
B 1 185 ARG 185 841  841  ARG ARG B . n 
B 1 186 GLU 186 842  842  GLU GLU B . n 
B 1 187 GLY 187 843  843  GLY GLY B . n 
B 1 188 GLU 188 844  844  GLU GLU B . n 
B 1 189 CYS 189 845  845  CYS CYS B . n 
B 1 190 GLN 190 846  846  GLN GLN B . n 
B 1 191 ARG 191 847  847  ARG ARG B . n 
B 1 192 TYR 192 848  848  TYR TYR B . n 
B 1 193 LYS 193 849  849  LYS LYS B . n 
B 1 194 PRO 194 850  850  PRO PRO B . n 
B 1 195 PHE 195 851  851  PHE PHE B . n 
B 1 196 LYS 196 852  852  LYS LYS B . n 
B 1 197 GLN 197 853  853  GLN GLN B . n 
B 1 198 LEU 198 854  854  LEU LEU B . n 
B 1 199 HIS 199 855  855  HIS HIS B . n 
B 1 200 ASN 200 856  856  ASN ASN B . n 
B 1 201 ARG 201 857  857  ARG ARG B . n 
B 1 202 ARG 202 858  858  ARG ARG B . n 
B 1 203 LEU 203 859  859  LEU LEU B . n 
B 1 204 LEU 204 860  860  LEU LEU B . n 
B 1 205 TRP 205 861  861  TRP TRP B . n 
B 1 206 HIS 206 862  862  HIS HIS B . n 
B 1 207 GLY 207 863  863  GLY GLY B . n 
B 1 208 SER 208 864  864  SER SER B . n 
B 1 209 ARG 209 865  865  ARG ARG B . n 
B 1 210 THR 210 866  866  THR THR B . n 
B 1 211 THR 211 867  867  THR THR B . n 
B 1 212 ASN 212 868  868  ASN ASN B . n 
B 1 213 PHE 213 869  869  PHE PHE B . n 
B 1 214 ALA 214 870  870  ALA ALA B . n 
B 1 215 GLY 215 871  871  GLY GLY B . n 
B 1 216 ILE 216 872  872  ILE ILE B . n 
B 1 217 LEU 217 873  873  LEU LEU B . n 
B 1 218 SER 218 874  874  SER SER B . n 
B 1 219 GLN 219 875  875  GLN GLN B . n 
B 1 220 GLY 220 876  876  GLY GLY B . n 
B 1 221 LEU 221 877  877  LEU LEU B . n 
B 1 222 ARG 222 878  878  ARG ARG B . n 
B 1 223 ILE 223 879  879  ILE ILE B . n 
B 1 224 ALA 224 880  880  ALA ALA B . n 
B 1 225 PRO 225 881  881  PRO PRO B . n 
B 1 226 PRO 226 882  882  PRO PRO B . n 
B 1 227 GLU 227 883  883  GLU GLU B . n 
B 1 228 ALA 228 884  884  ALA ALA B . n 
B 1 229 PRO 229 885  885  PRO PRO B . n 
B 1 230 VAL 230 886  886  VAL VAL B . n 
B 1 231 THR 231 887  887  THR THR B . n 
B 1 232 GLY 232 888  888  GLY GLY B . n 
B 1 233 TYR 233 889  889  TYR TYR B . n 
B 1 234 MET 234 890  890  MET MET B . n 
B 1 235 PHE 235 891  891  PHE PHE B . n 
B 1 236 GLY 236 892  892  GLY GLY B . n 
B 1 237 LYS 237 893  893  LYS LYS B . n 
B 1 238 GLY 238 894  894  GLY GLY B . n 
B 1 239 ILE 239 895  895  ILE ILE B . n 
B 1 240 TYR 240 896  896  TYR TYR B . n 
B 1 241 PHE 241 897  897  PHE PHE B . n 
B 1 242 ALA 242 898  898  ALA ALA B . n 
B 1 243 ASP 243 899  899  ASP ASP B . n 
B 1 244 MET 244 900  900  MET MET B . n 
B 1 245 VAL 245 901  901  VAL VAL B . n 
B 1 246 SER 246 902  902  SER SER B . n 
B 1 247 LYS 247 903  903  LYS LYS B . n 
B 1 248 SER 248 904  904  SER SER B . n 
B 1 249 ALA 249 905  905  ALA ALA B . n 
B 1 250 ASN 250 906  906  ASN ASN B . n 
B 1 251 TYR 251 907  907  TYR TYR B . n 
B 1 252 CYS 252 908  908  CYS CYS B . n 
B 1 253 HIS 253 909  909  HIS HIS B . n 
B 1 254 THR 254 910  910  THR THR B . n 
B 1 255 SER 255 911  911  SER SER B . n 
B 1 256 GLN 256 912  912  GLN GLN B . n 
B 1 257 GLY 257 913  913  GLY GLY B . n 
B 1 258 ASP 258 914  914  ASP ASP B . n 
B 1 259 PRO 259 915  915  PRO PRO B . n 
B 1 260 ILE 260 916  916  ILE ILE B . n 
B 1 261 GLY 261 917  917  GLY GLY B . n 
B 1 262 LEU 262 918  918  LEU LEU B . n 
B 1 263 ILE 263 919  919  ILE ILE B . n 
B 1 264 LEU 264 920  920  LEU LEU B . n 
B 1 265 LEU 265 921  921  LEU LEU B . n 
B 1 266 GLY 266 922  922  GLY GLY B . n 
B 1 267 GLU 267 923  923  GLU GLU B . n 
B 1 268 VAL 268 924  924  VAL VAL B . n 
B 1 269 ALA 269 925  925  ALA ALA B . n 
B 1 270 LEU 270 926  926  LEU LEU B . n 
B 1 271 GLY 271 927  927  GLY GLY B . n 
B 1 272 ASN 272 928  928  ASN ASN B . n 
B 1 273 MET 273 929  929  MET MET B . n 
B 1 274 TYR 274 930  930  TYR TYR B . n 
B 1 275 GLU 275 931  931  GLU GLU B . n 
B 1 276 LEU 276 932  932  LEU LEU B . n 
B 1 277 LYS 277 933  933  LYS LYS B . n 
B 1 278 HIS 278 934  934  HIS HIS B . n 
B 1 279 ALA 279 935  935  ALA ALA B . n 
B 1 280 SER 280 936  936  SER SER B . n 
B 1 281 HIS 281 937  937  HIS HIS B . n 
B 1 282 ILE 282 938  938  ILE ILE B . n 
B 1 283 SER 283 939  939  SER SER B . n 
B 1 284 LYS 284 940  940  LYS LYS B . n 
B 1 285 LEU 285 941  941  LEU LEU B . n 
B 1 286 PRO 286 942  942  PRO PRO B . n 
B 1 287 LYS 287 943  943  LYS LYS B . n 
B 1 288 GLY 288 944  944  GLY GLY B . n 
B 1 289 LYS 289 945  945  LYS LYS B . n 
B 1 290 HIS 290 946  946  HIS HIS B . n 
B 1 291 SER 291 947  947  SER SER B . n 
B 1 292 VAL 292 948  948  VAL VAL B . n 
B 1 293 LYS 293 949  949  LYS LYS B . n 
B 1 294 GLY 294 950  950  GLY GLY B . n 
B 1 295 LEU 295 951  951  LEU LEU B . n 
B 1 296 GLY 296 952  952  GLY GLY B . n 
B 1 297 LYS 297 953  953  LYS LYS B . n 
B 1 298 THR 298 954  954  THR THR B . n 
B 1 299 THR 299 955  955  THR THR B . n 
B 1 300 PRO 300 956  956  PRO PRO B . n 
B 1 301 ASP 301 957  957  ASP ASP B . n 
B 1 302 PRO 302 958  958  PRO PRO B . n 
B 1 303 SER 303 959  959  SER SER B . n 
B 1 304 ALA 304 960  960  ALA ALA B . n 
B 1 305 ASN 305 961  961  ASN ASN B . n 
B 1 306 ILE 306 962  962  ILE ILE B . n 
B 1 307 SER 307 963  963  SER SER B . n 
B 1 308 LEU 308 964  964  LEU LEU B . n 
B 1 309 ASP 309 965  965  ASP ASP B . n 
B 1 310 GLY 310 966  966  GLY GLY B . n 
B 1 311 VAL 311 967  967  VAL VAL B . n 
B 1 312 ASP 312 968  968  ASP ASP B . n 
B 1 313 VAL 313 969  969  VAL VAL B . n 
B 1 314 PRO 314 970  970  PRO PRO B . n 
B 1 315 LEU 315 971  971  LEU LEU B . n 
B 1 316 GLY 316 972  972  GLY GLY B . n 
B 1 317 THR 317 973  973  THR THR B . n 
B 1 318 GLY 318 974  974  GLY GLY B . n 
B 1 319 ILE 319 975  975  ILE ILE B . n 
B 1 320 SER 320 976  976  SER SER B . n 
B 1 321 SER 321 977  977  SER SER B . n 
B 1 322 GLY 322 978  978  GLY GLY B . n 
B 1 323 VAL 323 979  979  VAL VAL B . n 
B 1 324 ASN 324 980  980  ASN ASN B . n 
B 1 325 ASP 325 981  981  ASP ASP B . n 
B 1 326 THR 326 982  982  THR THR B . n 
B 1 327 SER 327 983  983  SER SER B . n 
B 1 328 LEU 328 984  984  LEU LEU B . n 
B 1 329 LEU 329 985  985  LEU LEU B . n 
B 1 330 TYR 330 986  986  TYR TYR B . n 
B 1 331 ASN 331 987  987  ASN ASN B . n 
B 1 332 GLU 332 988  988  GLU GLU B . n 
B 1 333 TYR 333 989  989  TYR TYR B . n 
B 1 334 ILE 334 990  990  ILE ILE B . n 
B 1 335 VAL 335 991  991  VAL VAL B . n 
B 1 336 TYR 336 992  992  TYR TYR B . n 
B 1 337 ASP 337 993  993  ASP ASP B . n 
B 1 338 ILE 338 994  994  ILE ILE B . n 
B 1 339 ALA 339 995  995  ALA ALA B . n 
B 1 340 GLN 340 996  996  GLN GLN B . n 
B 1 341 VAL 341 997  997  VAL VAL B . n 
B 1 342 ASN 342 998  998  ASN ASN B . n 
B 1 343 LEU 343 999  999  LEU LEU B . n 
B 1 344 LYS 344 1000 1000 LYS LYS B . n 
B 1 345 TYR 345 1001 1001 TYR TYR B . n 
B 1 346 LEU 346 1002 1002 LEU LEU B . n 
B 1 347 LEU 347 1003 1003 LEU LEU B . n 
B 1 348 LYS 348 1004 1004 LYS LYS B . n 
B 1 349 LEU 349 1005 1005 LEU LEU B . n 
B 1 350 LYS 350 1006 1006 LYS LYS B . n 
B 1 351 PHE 351 1007 1007 PHE PHE B . n 
B 1 352 ASN 352 1008 1008 ASN ASN B . n 
B 1 353 PHE 353 1009 1009 PHE PHE B . n 
B 1 354 LYS 354 1010 1010 LYS LYS B . n 
B 1 355 THR 355 1011 1011 THR THR B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1H64 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H64 
_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 A1H64 1  1101 1   A1H64 INH A . 
D 3 SO4   1  1102 1   SO4   SO4 A . 
E 2 A1H64 1  1101 2   A1H64 INH B . 
F 3 SO4   1  1102 2   SO4   SO4 B . 
G 4 HOH   1  1201 87  HOH   HOH A . 
G 4 HOH   2  1202 38  HOH   HOH A . 
G 4 HOH   3  1203 99  HOH   HOH A . 
G 4 HOH   4  1204 11  HOH   HOH A . 
G 4 HOH   5  1205 77  HOH   HOH A . 
G 4 HOH   6  1206 35  HOH   HOH A . 
G 4 HOH   7  1207 46  HOH   HOH A . 
G 4 HOH   8  1208 58  HOH   HOH A . 
G 4 HOH   9  1209 79  HOH   HOH A . 
G 4 HOH   10 1210 7   HOH   HOH A . 
G 4 HOH   11 1211 10  HOH   HOH A . 
G 4 HOH   12 1212 31  HOH   HOH A . 
G 4 HOH   13 1213 89  HOH   HOH A . 
G 4 HOH   14 1214 14  HOH   HOH A . 
G 4 HOH   15 1215 24  HOH   HOH A . 
G 4 HOH   16 1216 71  HOH   HOH A . 
G 4 HOH   17 1217 107 HOH   HOH A . 
G 4 HOH   18 1218 28  HOH   HOH A . 
G 4 HOH   19 1219 3   HOH   HOH A . 
G 4 HOH   20 1220 23  HOH   HOH A . 
G 4 HOH   21 1221 93  HOH   HOH A . 
G 4 HOH   22 1222 105 HOH   HOH A . 
G 4 HOH   23 1223 1   HOH   HOH A . 
G 4 HOH   24 1224 39  HOH   HOH A . 
G 4 HOH   25 1225 59  HOH   HOH A . 
G 4 HOH   26 1226 51  HOH   HOH A . 
G 4 HOH   27 1227 80  HOH   HOH A . 
G 4 HOH   28 1228 88  HOH   HOH A . 
G 4 HOH   29 1229 92  HOH   HOH A . 
G 4 HOH   30 1230 55  HOH   HOH A . 
G 4 HOH   31 1231 21  HOH   HOH A . 
G 4 HOH   32 1232 29  HOH   HOH A . 
G 4 HOH   33 1233 91  HOH   HOH A . 
G 4 HOH   34 1234 17  HOH   HOH A . 
G 4 HOH   35 1235 108 HOH   HOH A . 
G 4 HOH   36 1236 50  HOH   HOH A . 
G 4 HOH   37 1237 26  HOH   HOH A . 
G 4 HOH   38 1238 4   HOH   HOH A . 
G 4 HOH   39 1239 90  HOH   HOH A . 
G 4 HOH   40 1240 64  HOH   HOH A . 
G 4 HOH   41 1241 70  HOH   HOH A . 
G 4 HOH   42 1242 57  HOH   HOH A . 
G 4 HOH   43 1243 40  HOH   HOH A . 
G 4 HOH   44 1244 47  HOH   HOH A . 
G 4 HOH   45 1245 54  HOH   HOH A . 
G 4 HOH   46 1246 33  HOH   HOH A . 
G 4 HOH   47 1247 73  HOH   HOH A . 
G 4 HOH   48 1248 61  HOH   HOH A . 
G 4 HOH   49 1249 32  HOH   HOH A . 
G 4 HOH   50 1250 36  HOH   HOH A . 
G 4 HOH   51 1251 15  HOH   HOH A . 
G 4 HOH   52 1252 78  HOH   HOH A . 
H 4 HOH   1  1201 100 HOH   HOH B . 
H 4 HOH   2  1202 37  HOH   HOH B . 
H 4 HOH   3  1203 101 HOH   HOH B . 
H 4 HOH   4  1204 44  HOH   HOH B . 
H 4 HOH   5  1205 84  HOH   HOH B . 
H 4 HOH   6  1206 13  HOH   HOH B . 
H 4 HOH   7  1207 6   HOH   HOH B . 
H 4 HOH   8  1208 42  HOH   HOH B . 
H 4 HOH   9  1209 106 HOH   HOH B . 
H 4 HOH   10 1210 53  HOH   HOH B . 
H 4 HOH   11 1211 69  HOH   HOH B . 
H 4 HOH   12 1212 103 HOH   HOH B . 
H 4 HOH   13 1213 86  HOH   HOH B . 
H 4 HOH   14 1214 12  HOH   HOH B . 
H 4 HOH   15 1215 96  HOH   HOH B . 
H 4 HOH   16 1216 75  HOH   HOH B . 
H 4 HOH   17 1217 98  HOH   HOH B . 
H 4 HOH   18 1218 65  HOH   HOH B . 
H 4 HOH   19 1219 43  HOH   HOH B . 
H 4 HOH   20 1220 68  HOH   HOH B . 
H 4 HOH   21 1221 97  HOH   HOH B . 
H 4 HOH   22 1222 22  HOH   HOH B . 
H 4 HOH   23 1223 85  HOH   HOH B . 
H 4 HOH   24 1224 81  HOH   HOH B . 
H 4 HOH   25 1225 56  HOH   HOH B . 
H 4 HOH   26 1226 25  HOH   HOH B . 
H 4 HOH   27 1227 95  HOH   HOH B . 
H 4 HOH   28 1228 18  HOH   HOH B . 
H 4 HOH   29 1229 5   HOH   HOH B . 
H 4 HOH   30 1230 94  HOH   HOH B . 
H 4 HOH   31 1231 52  HOH   HOH B . 
H 4 HOH   32 1232 45  HOH   HOH B . 
H 4 HOH   33 1233 66  HOH   HOH B . 
H 4 HOH   34 1234 82  HOH   HOH B . 
H 4 HOH   35 1235 67  HOH   HOH B . 
H 4 HOH   36 1236 49  HOH   HOH B . 
H 4 HOH   37 1237 48  HOH   HOH B . 
H 4 HOH   38 1238 60  HOH   HOH B . 
H 4 HOH   39 1239 74  HOH   HOH B . 
H 4 HOH   40 1240 8   HOH   HOH B . 
H 4 HOH   41 1241 9   HOH   HOH B . 
H 4 HOH   42 1242 72  HOH   HOH B . 
H 4 HOH   43 1243 30  HOH   HOH B . 
H 4 HOH   44 1244 16  HOH   HOH B . 
H 4 HOH   45 1245 41  HOH   HOH B . 
H 4 HOH   46 1246 19  HOH   HOH B . 
H 4 HOH   47 1247 63  HOH   HOH B . 
H 4 HOH   48 1248 2   HOH   HOH B . 
H 4 HOH   49 1249 83  HOH   HOH B . 
H 4 HOH   50 1250 62  HOH   HOH B . 
H 4 HOH   51 1251 104 HOH   HOH B . 
H 4 HOH   52 1252 20  HOH   HOH B . 
H 4 HOH   53 1253 34  HOH   HOH B . 
H 4 HOH   54 1254 76  HOH   HOH B . 
H 4 HOH   55 1255 27  HOH   HOH B . 
H 4 HOH   56 1256 102 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 LYS 662 ? CG  ? A LYS 6   CG  
2  1 Y 1 A LYS 662 ? CD  ? A LYS 6   CD  
3  1 Y 1 A LYS 662 ? CE  ? A LYS 6   CE  
4  1 Y 1 A LYS 662 ? NZ  ? A LYS 6   NZ  
5  1 Y 1 A LYS 664 ? CG  ? A LYS 8   CG  
6  1 Y 1 A LYS 664 ? CD  ? A LYS 8   CD  
7  1 Y 1 A LYS 664 ? CE  ? A LYS 8   CE  
8  1 Y 1 A LYS 664 ? NZ  ? A LYS 8   NZ  
9  1 Y 1 A GLN 728 ? CG  ? A GLN 72  CG  
10 1 Y 1 A GLN 728 ? CD  ? A GLN 72  CD  
11 1 Y 1 A GLN 728 ? OE1 ? A GLN 72  OE1 
12 1 Y 1 A GLN 728 ? NE2 ? A GLN 72  NE2 
13 1 Y 1 A GLU 809 ? CG  ? A GLU 153 CG  
14 1 Y 1 A GLU 809 ? CD  ? A GLU 153 CD  
15 1 Y 1 A GLU 809 ? OE1 ? A GLU 153 OE1 
16 1 Y 1 A GLU 809 ? OE2 ? A GLU 153 OE2 
17 1 Y 1 A GLN 846 ? CG  ? A GLN 190 CG  
18 1 Y 1 A GLN 846 ? CD  ? A GLN 190 CD  
19 1 Y 1 A GLN 846 ? OE1 ? A GLN 190 OE1 
20 1 Y 1 A GLN 846 ? NE2 ? A GLN 190 NE2 
21 1 Y 1 B LYS 684 ? CD  ? B LYS 28  CD  
22 1 Y 1 B LYS 684 ? CE  ? B LYS 28  CE  
23 1 Y 1 B LYS 684 ? NZ  ? B LYS 28  NZ  
24 1 Y 1 B GLN 694 ? OE1 ? B GLN 38  OE1 
25 1 Y 1 B GLN 694 ? NE2 ? B GLN 38  NE2 
26 1 Y 1 B LYS 849 ? CE  ? B LYS 193 CE  
27 1 Y 1 B LYS 849 ? NZ  ? B LYS 193 NZ  
28 1 Y 1 B LYS 852 ? CG  ? B LYS 196 CG  
29 1 Y 1 B LYS 852 ? CD  ? B LYS 196 CD  
30 1 Y 1 B LYS 852 ? CE  ? B LYS 196 CE  
31 1 Y 1 B LYS 852 ? NZ  ? B LYS 196 NZ  
32 1 Y 1 B GLN 853 ? CG  ? B GLN 197 CG  
33 1 Y 1 B GLN 853 ? CD  ? B GLN 197 CD  
34 1 Y 1 B GLN 853 ? OE1 ? B GLN 197 OE1 
35 1 Y 1 B GLN 853 ? NE2 ? B GLN 197 NE2 
36 1 Y 1 B ASP 914 ? CG  ? B ASP 258 CG  
37 1 Y 1 B ASP 914 ? OD1 ? B ASP 258 OD1 
38 1 Y 1 B ASP 914 ? OD2 ? B ASP 258 OD2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER    ? ? ? 2.11.7 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? STARANISO ? ? ? .      2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? AMoRE     ? ? ? .      4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9ETR 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.272 
_cell.length_a_esd                 ? 
_cell.length_b                     92.583 
_cell.length_b_esd                 ? 
_cell.length_c                     165.252 
_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                         9ETR 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9ETR 
_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             2.33 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.23 
_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' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.5 
_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    '2.4-2.9 M ammonium sulfate, 0.1 M Tris pH 8.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-01-31 
_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   0.97622 
_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 I03' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97622 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9ETR 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.822 
_reflns.d_resolution_low                               82.626 
_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                                     42562 
_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                           63.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.152 
_reflns.pdbx_Rpim_I_all                                0.059 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.139 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.822 
_reflns_shell.d_res_low                                     2.003 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           12674 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2126 
_reflns_shell.percent_possible_obs                          13.0 
_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                               6.0 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.8 
_reflns_shell.pdbx_Rrim_I_all                               1.140 
_reflns_shell.pdbx_Rpim_I_all                               0.449 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.044 
_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]                            -5.56990 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.00000 
_refine.aniso_B[2][2]                            0.83670 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            4.73320 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               34.57 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.903 
_refine.correlation_coeff_Fo_to_Fc_free          0.874 
_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                                 9ETR 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.822 
_refine.ls_d_res_low                             26.40 
_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                     42562 
_refine.ls_number_reflns_R_free                  2046 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    61.9 
_refine.ls_percent_reflns_R_free                 4.810 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.215 
_refine.ls_R_factor_R_free                       0.252 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.213 
_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   0.194 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.191 
_refine.pdbx_overall_SU_R_Blow_DPI               0.237 
_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             0.240 
_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                        9ETR 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.35 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.822 
_refine_hist.d_res_low                        26.40 
_refine_hist.number_atoms_solvent             108 
_refine_hist.number_atoms_total               5644 
_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        5464 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         72 
_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' ? 0.010 ? 5644 ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 1.16  ? 7632 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 2006 ? 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' ? ?     ? 938  ? t_gen_planes              5.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 5644 ? t_it                      20.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 3.06  ? ?    ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 18.85 ? ?    ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 732  ? 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' ? ?     ? 6356 ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.822 
_refine_ls_shell.d_res_low                        1.91 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             ? 
_refine_ls_shell.number_reflns_R_work             817 
_refine_ls_shell.percent_reflns_obs               8.45 
_refine_ls_shell.percent_reflns_R_free            4.11 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.1966 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   ? 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.2587 
# 
_struct.entry_id                     9ETR 
_struct.title                        'Crystal structure of PARP1 catalytic domain bound to AZD9574' 
_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        9ETR 
_struct_keywords.text            'PARP1 INHIBITOR, PARYLATION, PARP TRAPPING, SELECTIVITY, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PARP1_HUMAN 
_struct_ref.pdbx_db_accession          P09874 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;KSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSSDSQILDLSNRFYTLIP
HDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNT
HATTHNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMV
SKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSANISLDGVDVPLGTGISSGVND
TSLLYNEYIVYDIAQVNLKYLLKLKFNFKT
;
_struct_ref.pdbx_align_begin           662 
# 
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 9ETR A 6 ? 355 ? P09874 662 ? 1011 ? 662 1011 
2 1 9ETR B 6 ? 355 ? P09874 662 ? 1011 ? 662 1011 
# 
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 9ETR GLY A 1   ? UNP P09874 ?   ?   'expression tag'      657 1  
1 9ETR PRO A 2   ? UNP P09874 ?   ?   'expression tag'      658 2  
1 9ETR LEU A 3   ? UNP P09874 ?   ?   'expression tag'      659 3  
1 9ETR GLY A 4   ? UNP P09874 ?   ?   'expression tag'      660 4  
1 9ETR SER A 5   ? UNP P09874 ?   ?   'expression tag'      661 5  
1 9ETR ALA A 106 ? UNP P09874 VAL 762 'engineered mutation' 762 6  
2 9ETR GLY B 1   ? UNP P09874 ?   ?   'expression tag'      657 7  
2 9ETR PRO B 2   ? UNP P09874 ?   ?   'expression tag'      658 8  
2 9ETR LEU B 3   ? UNP P09874 ?   ?   'expression tag'      659 9  
2 9ETR GLY B 4   ? UNP P09874 ?   ?   'expression tag'      660 10 
2 9ETR SER B 5   ? UNP P09874 ?   ?   'expression tag'      661 11 
2 9ETR ALA B 106 ? UNP P09874 VAL 762 'engineered mutation' 762 12 
# 
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,D,G 
2 1 B,E,F,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 10  ? PHE A 21  ? PRO A 666 PHE A 677 1 ? 12 
HELX_P HELX_P2  AA2 ASP A 22  ? TYR A 33  ? ASP A 678 TYR A 689 1 ? 12 
HELX_P HELX_P3  AA3 PRO A 41  ? LEU A 45  ? PRO A 697 LEU A 701 5 ? 5  
HELX_P HELX_P4  AA4 SER A 46  ? GLN A 66  ? SER A 702 GLN A 722 1 ? 21 
HELX_P HELX_P5  AA5 SER A 69  ? ILE A 84  ? SER A 725 ILE A 740 1 ? 16 
HELX_P HELX_P6  AA6 ASN A 98  ? GLY A 124 ? ASN A 754 GLY A 780 1 ? 27 
HELX_P HELX_P7  AA7 ASP A 132 ? LEU A 141 ? ASP A 788 LEU A 797 1 ? 10 
HELX_P HELX_P8  AA8 SER A 152 ? THR A 165 ? SER A 808 THR A 821 1 ? 14 
HELX_P HELX_P9  AA9 ALA A 167 ? ASN A 171 ? ALA A 823 ASN A 827 5 ? 5  
HELX_P HELX_P10 AB1 GLY A 187 ? LYS A 193 ? GLY A 843 LYS A 849 1 ? 7  
HELX_P HELX_P11 AB2 PRO A 194 ? LYS A 196 ? PRO A 850 LYS A 852 5 ? 3  
HELX_P HELX_P12 AB3 ARG A 209 ? THR A 211 ? ARG A 865 THR A 867 5 ? 3  
HELX_P HELX_P13 AB4 ASN A 212 ? GLY A 220 ? ASN A 868 GLY A 876 1 ? 9  
HELX_P HELX_P14 AB5 PRO A 229 ? TYR A 233 ? PRO A 885 TYR A 889 5 ? 5  
HELX_P HELX_P15 AB6 MET A 244 ? ASN A 250 ? MET A 900 ASN A 906 1 ? 7  
HELX_P HELX_P16 AB7 TYR A 251 ? HIS A 253 ? TYR A 907 HIS A 909 5 ? 3  
HELX_P HELX_P17 AB8 PRO A 302 ? ASN A 305 ? PRO A 958 ASN A 961 5 ? 4  
HELX_P HELX_P18 AB9 ASP A 337 ? ALA A 339 ? ASP A 993 ALA A 995 5 ? 3  
HELX_P HELX_P19 AC1 PRO B 10  ? PHE B 21  ? PRO B 666 PHE B 677 1 ? 12 
HELX_P HELX_P20 AC2 ASP B 22  ? TYR B 33  ? ASP B 678 TYR B 689 1 ? 12 
HELX_P HELX_P21 AC3 PRO B 41  ? LEU B 45  ? PRO B 697 LEU B 701 5 ? 5  
HELX_P HELX_P22 AC4 SER B 46  ? GLY B 67  ? SER B 702 GLY B 723 1 ? 22 
HELX_P HELX_P23 AC5 SER B 69  ? ILE B 84  ? SER B 725 ILE B 740 1 ? 16 
HELX_P HELX_P24 AC6 ASN B 98  ? GLY B 124 ? ASN B 754 GLY B 780 1 ? 27 
HELX_P HELX_P25 AC7 ASP B 132 ? LEU B 141 ? ASP B 788 LEU B 797 1 ? 10 
HELX_P HELX_P26 AC8 SER B 152 ? THR B 165 ? SER B 808 THR B 821 1 ? 14 
HELX_P HELX_P27 AC9 ALA B 167 ? ASN B 171 ? ALA B 823 ASN B 827 5 ? 5  
HELX_P HELX_P28 AD1 GLY B 187 ? LYS B 193 ? GLY B 843 LYS B 849 1 ? 7  
HELX_P HELX_P29 AD2 PRO B 194 ? LYS B 196 ? PRO B 850 LYS B 852 5 ? 3  
HELX_P HELX_P30 AD3 ARG B 209 ? THR B 211 ? ARG B 865 THR B 867 5 ? 3  
HELX_P HELX_P31 AD4 ASN B 212 ? GLY B 220 ? ASN B 868 GLY B 876 1 ? 9  
HELX_P HELX_P32 AD5 PRO B 229 ? TYR B 233 ? PRO B 885 TYR B 889 5 ? 5  
HELX_P HELX_P33 AD6 MET B 244 ? ASN B 250 ? MET B 900 ASN B 906 1 ? 7  
HELX_P HELX_P34 AD7 TYR B 251 ? HIS B 253 ? TYR B 907 HIS B 909 5 ? 3  
HELX_P HELX_P35 AD8 PRO B 302 ? ASN B 305 ? PRO B 958 ASN B 961 5 ? 4  
HELX_P HELX_P36 AD9 ASP B 337 ? ALA B 339 ? ASP B 993 ALA B 995 5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 4 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 5 ? 
AA6 ? 4 ? 
AA7 ? 2 ? 
AA8 ? 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 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? parallel      
AA7 1 2 ? anti-parallel 
AA8 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 THR A 143 ? VAL A 147 ? THR A 799 VAL A 803  
AA1 2 TYR A 173 ? ARG A 185 ? TYR A 829 ARG A 841  
AA1 3 VAL A 341 ? PHE A 353 ? VAL A 997 PHE A 1009 
AA1 4 ILE A 260 ? ALA A 269 ? ILE A 916 ALA A 925  
AA1 5 ARG A 201 ? SER A 208 ? ARG A 857 SER A 864  
AA2 1 ILE A 239 ? PHE A 241 ? ILE A 895 PHE A 897  
AA2 2 GLU A 332 ? VAL A 335 ? GLU A 988 VAL A 991  
AA2 3 SER A 291 ? GLY A 294 ? SER A 947 GLY A 950  
AA2 4 MET A 273 ? LEU A 276 ? MET A 929 LEU A 932  
AA3 1 THR A 298 ? PRO A 300 ? THR A 954 PRO A 956  
AA3 2 GLY A 318 ? SER A 320 ? GLY A 974 SER A 976  
AA4 1 ILE A 306 ? LEU A 308 ? ILE A 962 LEU A 964  
AA4 2 VAL A 311 ? VAL A 313 ? VAL A 967 VAL A 969  
AA5 1 THR B 143 ? VAL B 147 ? THR B 799 VAL B 803  
AA5 2 TYR B 173 ? ARG B 185 ? TYR B 829 ARG B 841  
AA5 3 VAL B 341 ? PHE B 353 ? VAL B 997 PHE B 1009 
AA5 4 ILE B 260 ? ALA B 269 ? ILE B 916 ALA B 925  
AA5 5 ARG B 201 ? SER B 208 ? ARG B 857 SER B 864  
AA6 1 ILE B 239 ? PHE B 241 ? ILE B 895 PHE B 897  
AA6 2 GLU B 332 ? VAL B 335 ? GLU B 988 VAL B 991  
AA6 3 SER B 291 ? GLY B 294 ? SER B 947 GLY B 950  
AA6 4 MET B 273 ? LEU B 276 ? MET B 929 LEU B 932  
AA7 1 THR B 298 ? PRO B 300 ? THR B 954 PRO B 956  
AA7 2 GLY B 318 ? SER B 320 ? GLY B 974 SER B 976  
AA8 1 ILE B 306 ? LEU B 308 ? ILE B 962 LEU B 964  
AA8 2 VAL B 311 ? VAL B 313 ? VAL B 967 VAL B 969  
# 
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 LYS A 146 ? N LYS A 802 O LYS A 182 ? O LYS A 838  
AA1 2 3 N GLU A 176 ? N GLU A 832 O LYS A 350 ? O LYS A 1006 
AA1 3 4 O ASN A 342 ? O ASN A 998 N GLU A 267 ? N GLU A 923  
AA1 4 5 O LEU A 264 ? O LEU A 920 N HIS A 206 ? N HIS A 862  
AA2 1 2 N ILE A 239 ? N ILE A 895 O VAL A 335 ? O VAL A 991  
AA2 2 3 O GLU A 332 ? O GLU A 988 N GLY A 294 ? N GLY A 950  
AA2 3 4 O LYS A 293 ? O LYS A 949 N TYR A 274 ? N TYR A 930  
AA3 1 2 N THR A 299 ? N THR A 955 O ILE A 319 ? O ILE A 975  
AA4 1 2 N ILE A 306 ? N ILE A 962 O VAL A 313 ? O VAL A 969  
AA5 1 2 N LYS B 146 ? N LYS B 802 O LYS B 182 ? O LYS B 838  
AA5 2 3 N GLU B 176 ? N GLU B 832 O LYS B 350 ? O LYS B 1006 
AA5 3 4 O ASN B 342 ? O ASN B 998 N GLU B 267 ? N GLU B 923  
AA5 4 5 O LEU B 264 ? O LEU B 920 N HIS B 206 ? N HIS B 862  
AA6 1 2 N ILE B 239 ? N ILE B 895 O VAL B 335 ? O VAL B 991  
AA6 2 3 O GLU B 332 ? O GLU B 988 N GLY B 294 ? N GLY B 950  
AA6 3 4 O LYS B 293 ? O LYS B 949 N TYR B 274 ? N TYR B 930  
AA7 1 2 N THR B 299 ? N THR B 955 O ILE B 319 ? O ILE B 975  
AA8 1 2 N ILE B 306 ? N ILE B 962 O VAL B 313 ? O VAL B 969  
# 
_pdbx_entry_details.entry_id                   9ETR 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 914 ? ? -161.57 76.69   
2 1 MET B 696 ? ? -155.99 88.66   
3 1 ASP B 914 ? ? -158.62 77.59   
4 1 ILE B 962 ? ? -124.58 -167.58 
# 
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 9.3278  43.2940 5.3823  -0.1950 ? 0.0423  ? -0.0097 ? -0.0911 ? -0.0341 ? -0.0323 ? 1.2687 ? 
0.2217 ? -0.1030 ? 0.5725 ? -0.0799 ? 1.0905 ? 0.0106 ? 0.0025  ? 0.0888  ? -0.0407 ? -0.0442 ? -0.0216 ? -0.0518 ? -0.0891 ? 
0.0336  ? 
2 'X-RAY DIFFRACTION' ? refined 30.3417 26.0172 38.2130 -0.2704 ? -0.0032 ? -0.0233 ? -0.1760 ? 0.0172  ? -0.0289 ? 1.1164 ? 
0.0958 ? -0.0527 ? 0.9834 ? -0.9062 ? 3.1799 ? 0.0544 ? -0.0087 ? -0.1311 ? 0.0110  ? 0.0432  ? 0.0803  ? -0.0487 ? -0.0694 ? 
-0.0975 ? 
# 
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 657 ? A GLY 1 
2  1 Y 1 A PRO 658 ? A PRO 2 
3  1 Y 1 A LEU 659 ? A LEU 3 
4  1 Y 1 A GLY 660 ? A GLY 4 
5  1 Y 1 A SER 661 ? A SER 5 
6  1 Y 1 B GLY 657 ? B GLY 1 
7  1 Y 1 B PRO 658 ? B PRO 2 
8  1 Y 1 B LEU 659 ? B LEU 3 
9  1 Y 1 B GLY 660 ? B GLY 4 
10 1 Y 1 B SER 661 ? B SER 5 
# 
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 
A1H64 C1   C N N 1   
A1H64 C2   C Y N 2   
A1H64 C3   C Y N 3   
A1H64 C7   C N N 4   
A1H64 C8   C N N 5   
A1H64 C9   C Y N 6   
A1H64 C10  C Y N 7   
A1H64 C11  C Y N 8   
A1H64 C12  C Y N 9   
A1H64 C13  C N N 10  
A1H64 C14  C N N 11  
A1H64 C15  C N N 12  
A1H64 C16  C Y N 13  
A1H64 C19  C N N 14  
A1H64 C20  C Y N 15  
A1H64 F1   F N N 16  
A1H64 N5   N Y N 17  
A1H64 O    O N N 18  
A1H64 N    N N N 19  
A1H64 C    C N N 20  
A1H64 C5   C Y N 21  
A1H64 C4   C Y N 22  
A1H64 N1   N N N 23  
A1H64 C18  C N N 24  
A1H64 N2   N N N 25  
A1H64 C6   C N N 26  
A1H64 C17  C Y N 27  
A1H64 F    F N N 28  
A1H64 N4   N N N 29  
A1H64 O1   O N N 30  
A1H64 N3   N N N 31  
A1H64 H1   H N N 32  
A1H64 H2   H N N 33  
A1H64 H3   H N N 34  
A1H64 H4   H N N 35  
A1H64 H5   H N N 36  
A1H64 H6   H N N 37  
A1H64 H7   H N N 38  
A1H64 H8   H N N 39  
A1H64 H9   H N N 40  
A1H64 H10  H N N 41  
A1H64 H11  H N N 42  
A1H64 H12  H N N 43  
A1H64 H13  H N N 44  
A1H64 H14  H N N 45  
A1H64 H15  H N N 46  
A1H64 H16  H N N 47  
A1H64 H17  H N N 48  
A1H64 H18  H N N 49  
A1H64 H19  H N N 50  
A1H64 H21  H N N 51  
A1H64 H22  H N N 52  
A1H64 H23  H N N 53  
ALA   N    N N N 54  
ALA   CA   C N S 55  
ALA   C    C N N 56  
ALA   O    O N N 57  
ALA   CB   C N N 58  
ALA   OXT  O N N 59  
ALA   H    H N N 60  
ALA   H2   H N N 61  
ALA   HA   H N N 62  
ALA   HB1  H N N 63  
ALA   HB2  H N N 64  
ALA   HB3  H N N 65  
ALA   HXT  H N N 66  
ARG   N    N N N 67  
ARG   CA   C N S 68  
ARG   C    C N N 69  
ARG   O    O N N 70  
ARG   CB   C N N 71  
ARG   CG   C N N 72  
ARG   CD   C N N 73  
ARG   NE   N N N 74  
ARG   CZ   C N N 75  
ARG   NH1  N N N 76  
ARG   NH2  N N N 77  
ARG   OXT  O N N 78  
ARG   H    H N N 79  
ARG   H2   H N N 80  
ARG   HA   H N N 81  
ARG   HB2  H N N 82  
ARG   HB3  H N N 83  
ARG   HG2  H N N 84  
ARG   HG3  H N N 85  
ARG   HD2  H N N 86  
ARG   HD3  H N N 87  
ARG   HE   H N N 88  
ARG   HH11 H N N 89  
ARG   HH12 H N N 90  
ARG   HH21 H N N 91  
ARG   HH22 H N N 92  
ARG   HXT  H N N 93  
ASN   N    N N N 94  
ASN   CA   C N S 95  
ASN   C    C N N 96  
ASN   O    O N N 97  
ASN   CB   C N N 98  
ASN   CG   C N N 99  
ASN   OD1  O N N 100 
ASN   ND2  N N N 101 
ASN   OXT  O N N 102 
ASN   H    H N N 103 
ASN   H2   H N N 104 
ASN   HA   H N N 105 
ASN   HB2  H N N 106 
ASN   HB3  H N N 107 
ASN   HD21 H N N 108 
ASN   HD22 H N N 109 
ASN   HXT  H N N 110 
ASP   N    N N N 111 
ASP   CA   C N S 112 
ASP   C    C N N 113 
ASP   O    O N N 114 
ASP   CB   C N N 115 
ASP   CG   C N N 116 
ASP   OD1  O N N 117 
ASP   OD2  O N N 118 
ASP   OXT  O N N 119 
ASP   H    H N N 120 
ASP   H2   H N N 121 
ASP   HA   H N N 122 
ASP   HB2  H N N 123 
ASP   HB3  H N N 124 
ASP   HD2  H N N 125 
ASP   HXT  H N N 126 
CYS   N    N N N 127 
CYS   CA   C N R 128 
CYS   C    C N N 129 
CYS   O    O N N 130 
CYS   CB   C N N 131 
CYS   SG   S N N 132 
CYS   OXT  O N N 133 
CYS   H    H N N 134 
CYS   H2   H N N 135 
CYS   HA   H N N 136 
CYS   HB2  H N N 137 
CYS   HB3  H N N 138 
CYS   HG   H N N 139 
CYS   HXT  H N N 140 
GLN   N    N N N 141 
GLN   CA   C N S 142 
GLN   C    C N N 143 
GLN   O    O N N 144 
GLN   CB   C N N 145 
GLN   CG   C N N 146 
GLN   CD   C N N 147 
GLN   OE1  O N N 148 
GLN   NE2  N N N 149 
GLN   OXT  O N N 150 
GLN   H    H N N 151 
GLN   H2   H N N 152 
GLN   HA   H N N 153 
GLN   HB2  H N N 154 
GLN   HB3  H N N 155 
GLN   HG2  H N N 156 
GLN   HG3  H N N 157 
GLN   HE21 H N N 158 
GLN   HE22 H N N 159 
GLN   HXT  H N N 160 
GLU   N    N N N 161 
GLU   CA   C N S 162 
GLU   C    C N N 163 
GLU   O    O N N 164 
GLU   CB   C N N 165 
GLU   CG   C N N 166 
GLU   CD   C N N 167 
GLU   OE1  O N N 168 
GLU   OE2  O N N 169 
GLU   OXT  O N N 170 
GLU   H    H N N 171 
GLU   H2   H N N 172 
GLU   HA   H N N 173 
GLU   HB2  H N N 174 
GLU   HB3  H N N 175 
GLU   HG2  H N N 176 
GLU   HG3  H N N 177 
GLU   HE2  H N N 178 
GLU   HXT  H N N 179 
GLY   N    N N N 180 
GLY   CA   C N N 181 
GLY   C    C N N 182 
GLY   O    O N N 183 
GLY   OXT  O N N 184 
GLY   H    H N N 185 
GLY   H2   H N N 186 
GLY   HA2  H N N 187 
GLY   HA3  H N N 188 
GLY   HXT  H N N 189 
HIS   N    N N N 190 
HIS   CA   C N S 191 
HIS   C    C N N 192 
HIS   O    O N N 193 
HIS   CB   C N N 194 
HIS   CG   C Y N 195 
HIS   ND1  N Y N 196 
HIS   CD2  C Y N 197 
HIS   CE1  C Y N 198 
HIS   NE2  N Y N 199 
HIS   OXT  O N N 200 
HIS   H    H N N 201 
HIS   H2   H N N 202 
HIS   HA   H N N 203 
HIS   HB2  H N N 204 
HIS   HB3  H N N 205 
HIS   HD1  H N N 206 
HIS   HD2  H N N 207 
HIS   HE1  H N N 208 
HIS   HE2  H N N 209 
HIS   HXT  H N N 210 
HOH   O    O N N 211 
HOH   H1   H N N 212 
HOH   H2   H N N 213 
ILE   N    N N N 214 
ILE   CA   C N S 215 
ILE   C    C N N 216 
ILE   O    O N N 217 
ILE   CB   C N S 218 
ILE   CG1  C N N 219 
ILE   CG2  C N N 220 
ILE   CD1  C N N 221 
ILE   OXT  O N N 222 
ILE   H    H N N 223 
ILE   H2   H N N 224 
ILE   HA   H N N 225 
ILE   HB   H N N 226 
ILE   HG12 H N N 227 
ILE   HG13 H N N 228 
ILE   HG21 H N N 229 
ILE   HG22 H N N 230 
ILE   HG23 H N N 231 
ILE   HD11 H N N 232 
ILE   HD12 H N N 233 
ILE   HD13 H N N 234 
ILE   HXT  H N N 235 
LEU   N    N N N 236 
LEU   CA   C N S 237 
LEU   C    C N N 238 
LEU   O    O N N 239 
LEU   CB   C N N 240 
LEU   CG   C N N 241 
LEU   CD1  C N N 242 
LEU   CD2  C N N 243 
LEU   OXT  O N N 244 
LEU   H    H N N 245 
LEU   H2   H N N 246 
LEU   HA   H N N 247 
LEU   HB2  H N N 248 
LEU   HB3  H N N 249 
LEU   HG   H N N 250 
LEU   HD11 H N N 251 
LEU   HD12 H N N 252 
LEU   HD13 H N N 253 
LEU   HD21 H N N 254 
LEU   HD22 H N N 255 
LEU   HD23 H N N 256 
LEU   HXT  H N N 257 
LYS   N    N N N 258 
LYS   CA   C N S 259 
LYS   C    C N N 260 
LYS   O    O N N 261 
LYS   CB   C N N 262 
LYS   CG   C N N 263 
LYS   CD   C N N 264 
LYS   CE   C N N 265 
LYS   NZ   N N N 266 
LYS   OXT  O N N 267 
LYS   H    H N N 268 
LYS   H2   H N N 269 
LYS   HA   H N N 270 
LYS   HB2  H N N 271 
LYS   HB3  H N N 272 
LYS   HG2  H N N 273 
LYS   HG3  H N N 274 
LYS   HD2  H N N 275 
LYS   HD3  H N N 276 
LYS   HE2  H N N 277 
LYS   HE3  H N N 278 
LYS   HZ1  H N N 279 
LYS   HZ2  H N N 280 
LYS   HZ3  H N N 281 
LYS   HXT  H N N 282 
MET   N    N N N 283 
MET   CA   C N S 284 
MET   C    C N N 285 
MET   O    O N N 286 
MET   CB   C N N 287 
MET   CG   C N N 288 
MET   SD   S N N 289 
MET   CE   C N N 290 
MET   OXT  O N N 291 
MET   H    H N N 292 
MET   H2   H N N 293 
MET   HA   H N N 294 
MET   HB2  H N N 295 
MET   HB3  H N N 296 
MET   HG2  H N N 297 
MET   HG3  H N N 298 
MET   HE1  H N N 299 
MET   HE2  H N N 300 
MET   HE3  H N N 301 
MET   HXT  H N N 302 
PHE   N    N N N 303 
PHE   CA   C N S 304 
PHE   C    C N N 305 
PHE   O    O N N 306 
PHE   CB   C N N 307 
PHE   CG   C Y N 308 
PHE   CD1  C Y N 309 
PHE   CD2  C Y N 310 
PHE   CE1  C Y N 311 
PHE   CE2  C Y N 312 
PHE   CZ   C Y N 313 
PHE   OXT  O N N 314 
PHE   H    H N N 315 
PHE   H2   H N N 316 
PHE   HA   H N N 317 
PHE   HB2  H N N 318 
PHE   HB3  H N N 319 
PHE   HD1  H N N 320 
PHE   HD2  H N N 321 
PHE   HE1  H N N 322 
PHE   HE2  H N N 323 
PHE   HZ   H N N 324 
PHE   HXT  H N N 325 
PRO   N    N N N 326 
PRO   CA   C N S 327 
PRO   C    C N N 328 
PRO   O    O N N 329 
PRO   CB   C N N 330 
PRO   CG   C N N 331 
PRO   CD   C N N 332 
PRO   OXT  O N N 333 
PRO   H    H N N 334 
PRO   HA   H N N 335 
PRO   HB2  H N N 336 
PRO   HB3  H N N 337 
PRO   HG2  H N N 338 
PRO   HG3  H N N 339 
PRO   HD2  H N N 340 
PRO   HD3  H N N 341 
PRO   HXT  H N N 342 
SER   N    N N N 343 
SER   CA   C N S 344 
SER   C    C N N 345 
SER   O    O N N 346 
SER   CB   C N N 347 
SER   OG   O N N 348 
SER   OXT  O N N 349 
SER   H    H N N 350 
SER   H2   H N N 351 
SER   HA   H N N 352 
SER   HB2  H N N 353 
SER   HB3  H N N 354 
SER   HG   H N N 355 
SER   HXT  H N N 356 
SO4   S    S N N 357 
SO4   O1   O N N 358 
SO4   O2   O N N 359 
SO4   O3   O N N 360 
SO4   O4   O N N 361 
THR   N    N N N 362 
THR   CA   C N S 363 
THR   C    C N N 364 
THR   O    O N N 365 
THR   CB   C N R 366 
THR   OG1  O N N 367 
THR   CG2  C N N 368 
THR   OXT  O N N 369 
THR   H    H N N 370 
THR   H2   H N N 371 
THR   HA   H N N 372 
THR   HB   H N N 373 
THR   HG1  H N N 374 
THR   HG21 H N N 375 
THR   HG22 H N N 376 
THR   HG23 H N N 377 
THR   HXT  H N N 378 
TRP   N    N N N 379 
TRP   CA   C N S 380 
TRP   C    C N N 381 
TRP   O    O N N 382 
TRP   CB   C N N 383 
TRP   CG   C Y N 384 
TRP   CD1  C Y N 385 
TRP   CD2  C Y N 386 
TRP   NE1  N Y N 387 
TRP   CE2  C Y N 388 
TRP   CE3  C Y N 389 
TRP   CZ2  C Y N 390 
TRP   CZ3  C Y N 391 
TRP   CH2  C Y N 392 
TRP   OXT  O N N 393 
TRP   H    H N N 394 
TRP   H2   H N N 395 
TRP   HA   H N N 396 
TRP   HB2  H N N 397 
TRP   HB3  H N N 398 
TRP   HD1  H N N 399 
TRP   HE1  H N N 400 
TRP   HE3  H N N 401 
TRP   HZ2  H N N 402 
TRP   HZ3  H N N 403 
TRP   HH2  H N N 404 
TRP   HXT  H N N 405 
TYR   N    N N N 406 
TYR   CA   C N S 407 
TYR   C    C N N 408 
TYR   O    O N N 409 
TYR   CB   C N N 410 
TYR   CG   C Y N 411 
TYR   CD1  C Y N 412 
TYR   CD2  C Y N 413 
TYR   CE1  C Y N 414 
TYR   CE2  C Y N 415 
TYR   CZ   C Y N 416 
TYR   OH   O N N 417 
TYR   OXT  O N N 418 
TYR   H    H N N 419 
TYR   H2   H N N 420 
TYR   HA   H N N 421 
TYR   HB2  H N N 422 
TYR   HB3  H N N 423 
TYR   HD1  H N N 424 
TYR   HD2  H N N 425 
TYR   HE1  H N N 426 
TYR   HE2  H N N 427 
TYR   HH   H N N 428 
TYR   HXT  H N N 429 
VAL   N    N N N 430 
VAL   CA   C N S 431 
VAL   C    C N N 432 
VAL   O    O N N 433 
VAL   CB   C N N 434 
VAL   CG1  C N N 435 
VAL   CG2  C N N 436 
VAL   OXT  O N N 437 
VAL   H    H N N 438 
VAL   H2   H N N 439 
VAL   HA   H N N 440 
VAL   HB   H N N 441 
VAL   HG11 H N N 442 
VAL   HG12 H N N 443 
VAL   HG13 H N N 444 
VAL   HG21 H N N 445 
VAL   HG22 H N N 446 
VAL   HG23 H N N 447 
VAL   HXT  H N N 448 
# 
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 
A1H64 O1  C15  doub N N 1   
A1H64 F   C17  sing N N 2   
A1H64 N4  C15  sing N N 3   
A1H64 N4  C16  sing N N 4   
A1H64 C15 C13  sing N N 5   
A1H64 C17 C16  doub Y N 6   
A1H64 C17 C9   sing Y N 7   
A1H64 C16 C12  sing Y N 8   
A1H64 C13 C14  sing N N 9   
A1H64 C13 N3   doub N N 10  
A1H64 C8  C9   sing N N 11  
A1H64 C8  N2   sing N N 12  
A1H64 C18 N2   sing N N 13  
A1H64 C18 C19  sing N N 14  
A1H64 C9  C10  doub Y N 15  
A1H64 N2  C7   sing N N 16  
A1H64 C19 N1   sing N N 17  
A1H64 C12 N3   sing N N 18  
A1H64 C12 C11  doub Y N 19  
A1H64 C10 C11  sing Y N 20  
A1H64 C7  C6   sing N N 21  
A1H64 N1  C6   sing N N 22  
A1H64 N1  C5   sing N N 23  
A1H64 C4  C5   doub Y N 24  
A1H64 C4  C3   sing Y N 25  
A1H64 C5  C20  sing Y N 26  
A1H64 C3  C2   doub Y N 27  
A1H64 C20 F1   sing N N 28  
A1H64 C20 N5   doub Y N 29  
A1H64 C2  N5   sing Y N 30  
A1H64 C2  C1   sing N N 31  
A1H64 O   C1   doub N N 32  
A1H64 C1  N    sing N N 33  
A1H64 N   C    sing N N 34  
A1H64 C3  H1   sing N N 35  
A1H64 C7  H2   sing N N 36  
A1H64 C7  H3   sing N N 37  
A1H64 C8  H4   sing N N 38  
A1H64 C8  H5   sing N N 39  
A1H64 C10 H6   sing N N 40  
A1H64 C11 H7   sing N N 41  
A1H64 C14 H8   sing N N 42  
A1H64 C14 H9   sing N N 43  
A1H64 C14 H10  sing N N 44  
A1H64 C19 H11  sing N N 45  
A1H64 C19 H12  sing N N 46  
A1H64 N   H13  sing N N 47  
A1H64 C   H14  sing N N 48  
A1H64 C   H15  sing N N 49  
A1H64 C   H16  sing N N 50  
A1H64 C4  H17  sing N N 51  
A1H64 C18 H18  sing N N 52  
A1H64 C18 H19  sing N N 53  
A1H64 C6  H21  sing N N 54  
A1H64 C6  H22  sing N N 55  
A1H64 N4  H23  sing N N 56  
ALA   N   CA   sing N N 57  
ALA   N   H    sing N N 58  
ALA   N   H2   sing N N 59  
ALA   CA  C    sing N N 60  
ALA   CA  CB   sing N N 61  
ALA   CA  HA   sing N N 62  
ALA   C   O    doub N N 63  
ALA   C   OXT  sing N N 64  
ALA   CB  HB1  sing N N 65  
ALA   CB  HB2  sing N N 66  
ALA   CB  HB3  sing N N 67  
ALA   OXT HXT  sing N N 68  
ARG   N   CA   sing N N 69  
ARG   N   H    sing N N 70  
ARG   N   H2   sing N N 71  
ARG   CA  C    sing N N 72  
ARG   CA  CB   sing N N 73  
ARG   CA  HA   sing N N 74  
ARG   C   O    doub N N 75  
ARG   C   OXT  sing N N 76  
ARG   CB  CG   sing N N 77  
ARG   CB  HB2  sing N N 78  
ARG   CB  HB3  sing N N 79  
ARG   CG  CD   sing N N 80  
ARG   CG  HG2  sing N N 81  
ARG   CG  HG3  sing N N 82  
ARG   CD  NE   sing N N 83  
ARG   CD  HD2  sing N N 84  
ARG   CD  HD3  sing N N 85  
ARG   NE  CZ   sing N N 86  
ARG   NE  HE   sing N N 87  
ARG   CZ  NH1  sing N N 88  
ARG   CZ  NH2  doub N N 89  
ARG   NH1 HH11 sing N N 90  
ARG   NH1 HH12 sing N N 91  
ARG   NH2 HH21 sing N N 92  
ARG   NH2 HH22 sing N N 93  
ARG   OXT HXT  sing N N 94  
ASN   N   CA   sing N N 95  
ASN   N   H    sing N N 96  
ASN   N   H2   sing N N 97  
ASN   CA  C    sing N N 98  
ASN   CA  CB   sing N N 99  
ASN   CA  HA   sing N N 100 
ASN   C   O    doub N N 101 
ASN   C   OXT  sing N N 102 
ASN   CB  CG   sing N N 103 
ASN   CB  HB2  sing N N 104 
ASN   CB  HB3  sing N N 105 
ASN   CG  OD1  doub N N 106 
ASN   CG  ND2  sing N N 107 
ASN   ND2 HD21 sing N N 108 
ASN   ND2 HD22 sing N N 109 
ASN   OXT HXT  sing N N 110 
ASP   N   CA   sing N N 111 
ASP   N   H    sing N N 112 
ASP   N   H2   sing N N 113 
ASP   CA  C    sing N N 114 
ASP   CA  CB   sing N N 115 
ASP   CA  HA   sing N N 116 
ASP   C   O    doub N N 117 
ASP   C   OXT  sing N N 118 
ASP   CB  CG   sing N N 119 
ASP   CB  HB2  sing N N 120 
ASP   CB  HB3  sing N N 121 
ASP   CG  OD1  doub N N 122 
ASP   CG  OD2  sing N N 123 
ASP   OD2 HD2  sing N N 124 
ASP   OXT HXT  sing N N 125 
CYS   N   CA   sing N N 126 
CYS   N   H    sing N N 127 
CYS   N   H2   sing N N 128 
CYS   CA  C    sing N N 129 
CYS   CA  CB   sing N N 130 
CYS   CA  HA   sing N N 131 
CYS   C   O    doub N N 132 
CYS   C   OXT  sing N N 133 
CYS   CB  SG   sing N N 134 
CYS   CB  HB2  sing N N 135 
CYS   CB  HB3  sing N N 136 
CYS   SG  HG   sing N N 137 
CYS   OXT HXT  sing N N 138 
GLN   N   CA   sing N N 139 
GLN   N   H    sing N N 140 
GLN   N   H2   sing N N 141 
GLN   CA  C    sing N N 142 
GLN   CA  CB   sing N N 143 
GLN   CA  HA   sing N N 144 
GLN   C   O    doub N N 145 
GLN   C   OXT  sing N N 146 
GLN   CB  CG   sing N N 147 
GLN   CB  HB2  sing N N 148 
GLN   CB  HB3  sing N N 149 
GLN   CG  CD   sing N N 150 
GLN   CG  HG2  sing N N 151 
GLN   CG  HG3  sing N N 152 
GLN   CD  OE1  doub N N 153 
GLN   CD  NE2  sing N N 154 
GLN   NE2 HE21 sing N N 155 
GLN   NE2 HE22 sing N N 156 
GLN   OXT HXT  sing N N 157 
GLU   N   CA   sing N N 158 
GLU   N   H    sing N N 159 
GLU   N   H2   sing N N 160 
GLU   CA  C    sing N N 161 
GLU   CA  CB   sing N N 162 
GLU   CA  HA   sing N N 163 
GLU   C   O    doub N N 164 
GLU   C   OXT  sing N N 165 
GLU   CB  CG   sing N N 166 
GLU   CB  HB2  sing N N 167 
GLU   CB  HB3  sing N N 168 
GLU   CG  CD   sing N N 169 
GLU   CG  HG2  sing N N 170 
GLU   CG  HG3  sing N N 171 
GLU   CD  OE1  doub N N 172 
GLU   CD  OE2  sing N N 173 
GLU   OE2 HE2  sing N N 174 
GLU   OXT HXT  sing N N 175 
GLY   N   CA   sing N N 176 
GLY   N   H    sing N N 177 
GLY   N   H2   sing N N 178 
GLY   CA  C    sing N N 179 
GLY   CA  HA2  sing N N 180 
GLY   CA  HA3  sing N N 181 
GLY   C   O    doub N N 182 
GLY   C   OXT  sing N N 183 
GLY   OXT HXT  sing N N 184 
HIS   N   CA   sing N N 185 
HIS   N   H    sing N N 186 
HIS   N   H2   sing N N 187 
HIS   CA  C    sing N N 188 
HIS   CA  CB   sing N N 189 
HIS   CA  HA   sing N N 190 
HIS   C   O    doub N N 191 
HIS   C   OXT  sing N N 192 
HIS   CB  CG   sing N N 193 
HIS   CB  HB2  sing N N 194 
HIS   CB  HB3  sing N N 195 
HIS   CG  ND1  sing Y N 196 
HIS   CG  CD2  doub Y N 197 
HIS   ND1 CE1  doub Y N 198 
HIS   ND1 HD1  sing N N 199 
HIS   CD2 NE2  sing Y N 200 
HIS   CD2 HD2  sing N N 201 
HIS   CE1 NE2  sing Y N 202 
HIS   CE1 HE1  sing N N 203 
HIS   NE2 HE2  sing N N 204 
HIS   OXT HXT  sing N N 205 
HOH   O   H1   sing N N 206 
HOH   O   H2   sing N N 207 
ILE   N   CA   sing N N 208 
ILE   N   H    sing N N 209 
ILE   N   H2   sing N N 210 
ILE   CA  C    sing N N 211 
ILE   CA  CB   sing N N 212 
ILE   CA  HA   sing N N 213 
ILE   C   O    doub N N 214 
ILE   C   OXT  sing N N 215 
ILE   CB  CG1  sing N N 216 
ILE   CB  CG2  sing N N 217 
ILE   CB  HB   sing N N 218 
ILE   CG1 CD1  sing N N 219 
ILE   CG1 HG12 sing N N 220 
ILE   CG1 HG13 sing N N 221 
ILE   CG2 HG21 sing N N 222 
ILE   CG2 HG22 sing N N 223 
ILE   CG2 HG23 sing N N 224 
ILE   CD1 HD11 sing N N 225 
ILE   CD1 HD12 sing N N 226 
ILE   CD1 HD13 sing N N 227 
ILE   OXT HXT  sing N N 228 
LEU   N   CA   sing N N 229 
LEU   N   H    sing N N 230 
LEU   N   H2   sing N N 231 
LEU   CA  C    sing N N 232 
LEU   CA  CB   sing N N 233 
LEU   CA  HA   sing N N 234 
LEU   C   O    doub N N 235 
LEU   C   OXT  sing N N 236 
LEU   CB  CG   sing N N 237 
LEU   CB  HB2  sing N N 238 
LEU   CB  HB3  sing N N 239 
LEU   CG  CD1  sing N N 240 
LEU   CG  CD2  sing N N 241 
LEU   CG  HG   sing N N 242 
LEU   CD1 HD11 sing N N 243 
LEU   CD1 HD12 sing N N 244 
LEU   CD1 HD13 sing N N 245 
LEU   CD2 HD21 sing N N 246 
LEU   CD2 HD22 sing N N 247 
LEU   CD2 HD23 sing N N 248 
LEU   OXT HXT  sing N N 249 
LYS   N   CA   sing N N 250 
LYS   N   H    sing N N 251 
LYS   N   H2   sing N N 252 
LYS   CA  C    sing N N 253 
LYS   CA  CB   sing N N 254 
LYS   CA  HA   sing N N 255 
LYS   C   O    doub N N 256 
LYS   C   OXT  sing N N 257 
LYS   CB  CG   sing N N 258 
LYS   CB  HB2  sing N N 259 
LYS   CB  HB3  sing N N 260 
LYS   CG  CD   sing N N 261 
LYS   CG  HG2  sing N N 262 
LYS   CG  HG3  sing N N 263 
LYS   CD  CE   sing N N 264 
LYS   CD  HD2  sing N N 265 
LYS   CD  HD3  sing N N 266 
LYS   CE  NZ   sing N N 267 
LYS   CE  HE2  sing N N 268 
LYS   CE  HE3  sing N N 269 
LYS   NZ  HZ1  sing N N 270 
LYS   NZ  HZ2  sing N N 271 
LYS   NZ  HZ3  sing N N 272 
LYS   OXT HXT  sing N N 273 
MET   N   CA   sing N N 274 
MET   N   H    sing N N 275 
MET   N   H2   sing N N 276 
MET   CA  C    sing N N 277 
MET   CA  CB   sing N N 278 
MET   CA  HA   sing N N 279 
MET   C   O    doub N N 280 
MET   C   OXT  sing N N 281 
MET   CB  CG   sing N N 282 
MET   CB  HB2  sing N N 283 
MET   CB  HB3  sing N N 284 
MET   CG  SD   sing N N 285 
MET   CG  HG2  sing N N 286 
MET   CG  HG3  sing N N 287 
MET   SD  CE   sing N N 288 
MET   CE  HE1  sing N N 289 
MET   CE  HE2  sing N N 290 
MET   CE  HE3  sing N N 291 
MET   OXT HXT  sing N N 292 
PHE   N   CA   sing N N 293 
PHE   N   H    sing N N 294 
PHE   N   H2   sing N N 295 
PHE   CA  C    sing N N 296 
PHE   CA  CB   sing N N 297 
PHE   CA  HA   sing N N 298 
PHE   C   O    doub N N 299 
PHE   C   OXT  sing N N 300 
PHE   CB  CG   sing N N 301 
PHE   CB  HB2  sing N N 302 
PHE   CB  HB3  sing N N 303 
PHE   CG  CD1  doub Y N 304 
PHE   CG  CD2  sing Y N 305 
PHE   CD1 CE1  sing Y N 306 
PHE   CD1 HD1  sing N N 307 
PHE   CD2 CE2  doub Y N 308 
PHE   CD2 HD2  sing N N 309 
PHE   CE1 CZ   doub Y N 310 
PHE   CE1 HE1  sing N N 311 
PHE   CE2 CZ   sing Y N 312 
PHE   CE2 HE2  sing N N 313 
PHE   CZ  HZ   sing N N 314 
PHE   OXT HXT  sing N N 315 
PRO   N   CA   sing N N 316 
PRO   N   CD   sing N N 317 
PRO   N   H    sing N N 318 
PRO   CA  C    sing N N 319 
PRO   CA  CB   sing N N 320 
PRO   CA  HA   sing N N 321 
PRO   C   O    doub N N 322 
PRO   C   OXT  sing N N 323 
PRO   CB  CG   sing N N 324 
PRO   CB  HB2  sing N N 325 
PRO   CB  HB3  sing N N 326 
PRO   CG  CD   sing N N 327 
PRO   CG  HG2  sing N N 328 
PRO   CG  HG3  sing N N 329 
PRO   CD  HD2  sing N N 330 
PRO   CD  HD3  sing N N 331 
PRO   OXT HXT  sing N N 332 
SER   N   CA   sing N N 333 
SER   N   H    sing N N 334 
SER   N   H2   sing N N 335 
SER   CA  C    sing N N 336 
SER   CA  CB   sing N N 337 
SER   CA  HA   sing N N 338 
SER   C   O    doub N N 339 
SER   C   OXT  sing N N 340 
SER   CB  OG   sing N N 341 
SER   CB  HB2  sing N N 342 
SER   CB  HB3  sing N N 343 
SER   OG  HG   sing N N 344 
SER   OXT HXT  sing N N 345 
SO4   S   O1   doub N N 346 
SO4   S   O2   doub N N 347 
SO4   S   O3   sing N N 348 
SO4   S   O4   sing N N 349 
THR   N   CA   sing N N 350 
THR   N   H    sing N N 351 
THR   N   H2   sing N N 352 
THR   CA  C    sing N N 353 
THR   CA  CB   sing N N 354 
THR   CA  HA   sing N N 355 
THR   C   O    doub N N 356 
THR   C   OXT  sing N N 357 
THR   CB  OG1  sing N N 358 
THR   CB  CG2  sing N N 359 
THR   CB  HB   sing N N 360 
THR   OG1 HG1  sing N N 361 
THR   CG2 HG21 sing N N 362 
THR   CG2 HG22 sing N N 363 
THR   CG2 HG23 sing N N 364 
THR   OXT HXT  sing N N 365 
TRP   N   CA   sing N N 366 
TRP   N   H    sing N N 367 
TRP   N   H2   sing N N 368 
TRP   CA  C    sing N N 369 
TRP   CA  CB   sing N N 370 
TRP   CA  HA   sing N N 371 
TRP   C   O    doub N N 372 
TRP   C   OXT  sing N N 373 
TRP   CB  CG   sing N N 374 
TRP   CB  HB2  sing N N 375 
TRP   CB  HB3  sing N N 376 
TRP   CG  CD1  doub Y N 377 
TRP   CG  CD2  sing Y N 378 
TRP   CD1 NE1  sing Y N 379 
TRP   CD1 HD1  sing N N 380 
TRP   CD2 CE2  doub Y N 381 
TRP   CD2 CE3  sing Y N 382 
TRP   NE1 CE2  sing Y N 383 
TRP   NE1 HE1  sing N N 384 
TRP   CE2 CZ2  sing Y N 385 
TRP   CE3 CZ3  doub Y N 386 
TRP   CE3 HE3  sing N N 387 
TRP   CZ2 CH2  doub Y N 388 
TRP   CZ2 HZ2  sing N N 389 
TRP   CZ3 CH2  sing Y N 390 
TRP   CZ3 HZ3  sing N N 391 
TRP   CH2 HH2  sing N N 392 
TRP   OXT HXT  sing N N 393 
TYR   N   CA   sing N N 394 
TYR   N   H    sing N N 395 
TYR   N   H2   sing N N 396 
TYR   CA  C    sing N N 397 
TYR   CA  CB   sing N N 398 
TYR   CA  HA   sing N N 399 
TYR   C   O    doub N N 400 
TYR   C   OXT  sing N N 401 
TYR   CB  CG   sing N N 402 
TYR   CB  HB2  sing N N 403 
TYR   CB  HB3  sing N N 404 
TYR   CG  CD1  doub Y N 405 
TYR   CG  CD2  sing Y N 406 
TYR   CD1 CE1  sing Y N 407 
TYR   CD1 HD1  sing N N 408 
TYR   CD2 CE2  doub Y N 409 
TYR   CD2 HD2  sing N N 410 
TYR   CE1 CZ   doub Y N 411 
TYR   CE1 HE1  sing N N 412 
TYR   CE2 CZ   sing Y N 413 
TYR   CE2 HE2  sing N N 414 
TYR   CZ  OH   sing N N 415 
TYR   OH  HH   sing N N 416 
TYR   OXT HXT  sing N N 417 
VAL   N   CA   sing N N 418 
VAL   N   H    sing N N 419 
VAL   N   H2   sing N N 420 
VAL   CA  C    sing N N 421 
VAL   CA  CB   sing N N 422 
VAL   CA  HA   sing N N 423 
VAL   C   O    doub N N 424 
VAL   C   OXT  sing N N 425 
VAL   CB  CG1  sing N N 426 
VAL   CB  CG2  sing N N 427 
VAL   CB  HB   sing N N 428 
VAL   CG1 HG11 sing N N 429 
VAL   CG1 HG12 sing N N 430 
VAL   CG1 HG13 sing N N 431 
VAL   CG2 HG21 sing N N 432 
VAL   CG2 HG22 sing N N 433 
VAL   CG2 HG23 sing N N 434 
VAL   OXT HXT  sing N N 435 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9ETR 
_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]   0.020716 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010801 
_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]   0.006051 
_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   . LYS   A 1 6   ? -12.166 54.396 -17.188 1.00 41.78  ? 662  LYS   A N   1 
ATOM   2    C CA  . LYS   A 1 6   ? -10.775 54.028 -16.925 1.00 42.49  ? 662  LYS   A CA  1 
ATOM   3    C C   . LYS   A 1 6   ? -10.044 55.083 -16.066 1.00 46.71  ? 662  LYS   A C   1 
ATOM   4    O O   . LYS   A 1 6   ? -10.238 56.294 -16.236 1.00 47.66  ? 662  LYS   A O   1 
ATOM   5    C CB  . LYS   A 1 6   ? -10.003 53.738 -18.227 1.00 44.38  ? 662  LYS   A CB  1 
ATOM   6    N N   . SER   A 1 7   ? -9.213  54.596 -15.147 1.00 41.37  ? 663  SER   A N   1 
ATOM   7    C CA  . SER   A 1 7   ? -8.394  55.343 -14.193 1.00 39.41  ? 663  SER   A CA  1 
ATOM   8    C C   . SER   A 1 7   ? -7.495  56.468 -14.790 1.00 42.43  ? 663  SER   A C   1 
ATOM   9    O O   . SER   A 1 7   ? -6.769  56.266 -15.783 1.00 41.30  ? 663  SER   A O   1 
ATOM   10   C CB  . SER   A 1 7   ? -7.537  54.363 -13.396 1.00 39.53  ? 663  SER   A CB  1 
ATOM   11   O OG  . SER   A 1 7   ? -6.703  55.019 -12.456 1.00 40.31  ? 663  SER   A OG  1 
ATOM   12   N N   . LYS   A 1 8   ? -7.515  57.638 -14.111 1.00 37.77  ? 664  LYS   A N   1 
ATOM   13   C CA  . LYS   A 1 8   ? -6.701  58.818 -14.407 1.00 37.20  ? 664  LYS   A CA  1 
ATOM   14   C C   . LYS   A 1 8   ? -5.347  58.732 -13.684 1.00 41.41  ? 664  LYS   A C   1 
ATOM   15   O O   . LYS   A 1 8   ? -4.493  59.605 -13.870 1.00 42.23  ? 664  LYS   A O   1 
ATOM   16   C CB  . LYS   A 1 8   ? -7.436  60.105 -13.994 1.00 39.02  ? 664  LYS   A CB  1 
ATOM   17   N N   . LEU   A 1 9   ? -5.151  57.685 -12.855 1.00 35.95  ? 665  LEU   A N   1 
ATOM   18   C CA  . LEU   A 1 9   ? -3.904  57.473 -12.121 1.00 34.79  ? 665  LEU   A CA  1 
ATOM   19   C C   . LEU   A 1 9   ? -2.701  57.285 -13.064 1.00 37.80  ? 665  LEU   A C   1 
ATOM   20   O O   . LEU   A 1 9   ? -2.861  56.699 -14.136 1.00 37.34  ? 665  LEU   A O   1 
ATOM   21   C CB  . LEU   A 1 9   ? -4.007  56.239 -11.209 1.00 34.17  ? 665  LEU   A CB  1 
ATOM   22   C CG  . LEU   A 1 9   ? -4.728  56.407 -9.885  1.00 37.16  ? 665  LEU   A CG  1 
ATOM   23   C CD1 . LEU   A 1 9   ? -5.086  55.063 -9.312  1.00 35.86  ? 665  LEU   A CD1 1 
ATOM   24   C CD2 . LEU   A 1 9   ? -3.873  57.188 -8.886  1.00 37.25  ? 665  LEU   A CD2 1 
ATOM   25   N N   . PRO   A 1 10  ? -1.494  57.740 -12.677 1.00 33.66  ? 666  PRO   A N   1 
ATOM   26   C CA  . PRO   A 1 10  ? -0.321  57.507 -13.534 1.00 33.72  ? 666  PRO   A CA  1 
ATOM   27   C C   . PRO   A 1 10  ? -0.151  56.014 -13.810 1.00 37.93  ? 666  PRO   A C   1 
ATOM   28   O O   . PRO   A 1 10  ? -0.430  55.198 -12.926 1.00 37.77  ? 666  PRO   A O   1 
ATOM   29   C CB  . PRO   A 1 10  ? 0.843   58.041 -12.688 1.00 35.24  ? 666  PRO   A CB  1 
ATOM   30   C CG  . PRO   A 1 10  ? 0.214   59.001 -11.747 1.00 39.63  ? 666  PRO   A CG  1 
ATOM   31   C CD  . PRO   A 1 10  ? -1.118  58.428 -11.426 1.00 35.11  ? 666  PRO   A CD  1 
ATOM   32   N N   . LYS   A 1 11  ? 0.268   55.653 -15.039 1.00 33.28  ? 667  LYS   A N   1 
ATOM   33   C CA  . LYS   A 1 11  ? 0.481   54.255 -15.423 1.00 32.19  ? 667  LYS   A CA  1 
ATOM   34   C C   . LYS   A 1 11  ? 1.397   53.503 -14.423 1.00 33.54  ? 667  LYS   A C   1 
ATOM   35   O O   . LYS   A 1 11  ? 1.007   52.400 -14.013 1.00 31.01  ? 667  LYS   A O   1 
ATOM   36   C CB  . LYS   A 1 11  ? 0.964   54.128 -16.876 1.00 35.24  ? 667  LYS   A CB  1 
ATOM   37   C CG  . LYS   A 1 11  ? 0.461   52.868 -17.567 1.00 49.85  ? 667  LYS   A CG  1 
ATOM   38   C CD  . LYS   A 1 11  ? 1.611   52.040 -18.124 1.00 59.76  ? 667  LYS   A CD  1 
ATOM   39   C CE  . LYS   A 1 11  ? 1.144   50.804 -18.859 1.00 69.89  ? 667  LYS   A CE  1 
ATOM   40   N NZ  . LYS   A 1 11  ? 0.648   49.748 -17.934 1.00 81.31  ? 667  LYS   A NZ  1 
ATOM   41   N N   . PRO   A 1 12  ? 2.532   54.082 -13.923 1.00 29.64  ? 668  PRO   A N   1 
ATOM   42   C CA  . PRO   A 1 12  ? 3.340   53.348 -12.938 1.00 28.94  ? 668  PRO   A CA  1 
ATOM   43   C C   . PRO   A 1 12  ? 2.598   53.023 -11.641 1.00 30.92  ? 668  PRO   A C   1 
ATOM   44   O O   . PRO   A 1 12  ? 2.849   51.963 -11.060 1.00 29.03  ? 668  PRO   A O   1 
ATOM   45   C CB  . PRO   A 1 12  ? 4.536   54.272 -12.709 1.00 30.92  ? 668  PRO   A CB  1 
ATOM   46   C CG  . PRO   A 1 12  ? 4.594   55.137 -13.914 1.00 35.49  ? 668  PRO   A CG  1 
ATOM   47   C CD  . PRO   A 1 12  ? 3.174   55.374 -14.251 1.00 31.06  ? 668  PRO   A CD  1 
ATOM   48   N N   . VAL   A 1 13  ? 1.667   53.912 -11.202 1.00 27.10  ? 669  VAL   A N   1 
ATOM   49   C CA  . VAL   A 1 13  ? 0.847   53.719 -9.990  1.00 26.25  ? 669  VAL   A CA  1 
ATOM   50   C C   . VAL   A 1 13  ? -0.163  52.588 -10.226 1.00 31.74  ? 669  VAL   A C   1 
ATOM   51   O O   . VAL   A 1 13  ? -0.366  51.753 -9.348  1.00 32.79  ? 669  VAL   A O   1 
ATOM   52   C CB  . VAL   A 1 13  ? 0.190   55.041 -9.516  1.00 29.68  ? 669  VAL   A CB  1 
ATOM   53   C CG1 . VAL   A 1 13  ? -0.899  54.803 -8.473  1.00 29.98  ? 669  VAL   A CG1 1 
ATOM   54   C CG2 . VAL   A 1 13  ? 1.228   56.017 -8.978  1.00 28.88  ? 669  VAL   A CG2 1 
ATOM   55   N N   . GLN   A 1 14  ? -0.760  52.548 -11.432 1.00 28.61  ? 670  GLN   A N   1 
ATOM   56   C CA  . GLN   A 1 14  ? -1.731  51.529 -11.866 1.00 28.65  ? 670  GLN   A CA  1 
ATOM   57   C C   . GLN   A 1 14  ? -1.110  50.131 -11.871 1.00 33.18  ? 670  GLN   A C   1 
ATOM   58   O O   . GLN   A 1 14  ? -1.724  49.175 -11.376 1.00 33.64  ? 670  GLN   A O   1 
ATOM   59   C CB  . GLN   A 1 14  ? -2.270  51.856 -13.270 1.00 29.15  ? 670  GLN   A CB  1 
ATOM   60   C CG  . GLN   A 1 14  ? -3.093  53.136 -13.343 1.00 36.65  ? 670  GLN   A CG  1 
ATOM   61   C CD  . GLN   A 1 14  ? -3.934  53.208 -14.591 1.00 47.30  ? 670  GLN   A CD  1 
ATOM   62   O OE1 . GLN   A 1 14  ? -4.330  52.187 -15.179 1.00 41.64  ? 670  GLN   A OE1 1 
ATOM   63   N NE2 . GLN   A 1 14  ? -4.242  54.422 -15.010 1.00 35.95  ? 670  GLN   A NE2 1 
ATOM   64   N N   . ASP   A 1 15  ? 0.127   50.030 -12.409 1.00 28.42  ? 671  ASP   A N   1 
ATOM   65   C CA  . ASP   A 1 15  ? 0.875   48.782 -12.494 1.00 27.77  ? 671  ASP   A CA  1 
ATOM   66   C C   . ASP   A 1 15  ? 1.257   48.302 -11.117 1.00 29.11  ? 671  ASP   A C   1 
ATOM   67   O O   . ASP   A 1 15  ? 1.261   47.098 -10.891 1.00 28.76  ? 671  ASP   A O   1 
ATOM   68   C CB  . ASP   A 1 15  ? 2.118   48.936 -13.387 1.00 30.30  ? 671  ASP   A CB  1 
ATOM   69   C CG  . ASP   A 1 15  ? 1.836   49.185 -14.861 1.00 43.31  ? 671  ASP   A CG  1 
ATOM   70   O OD1 . ASP   A 1 15  ? 0.872   48.580 -15.401 1.00 41.75  ? 671  ASP   A OD1 1 
ATOM   71   O OD2 . ASP   A 1 15  ? 2.591   49.957 -15.482 1.00 55.38  ? 671  ASP   A OD2 1 
ATOM   72   N N   . LEU   A 1 16  ? 1.553   49.243 -10.188 1.00 23.14  ? 672  LEU   A N   1 
ATOM   73   C CA  . LEU   A 1 16  ? 1.885   48.937 -8.802  1.00 20.37  ? 672  LEU   A CA  1 
ATOM   74   C C   . LEU   A 1 16  ? 0.702   48.294 -8.075  1.00 21.80  ? 672  LEU   A C   1 
ATOM   75   O O   . LEU   A 1 16  ? 0.893   47.295 -7.389  1.00 18.90  ? 672  LEU   A O   1 
ATOM   76   C CB  . LEU   A 1 16  ? 2.384   50.184 -8.039  1.00 19.58  ? 672  LEU   A CB  1 
ATOM   77   C CG  . LEU   A 1 16  ? 2.638   49.972 -6.526  1.00 23.69  ? 672  LEU   A CG  1 
ATOM   78   C CD1 . LEU   A 1 16  ? 3.935   49.264 -6.285  1.00 23.26  ? 672  LEU   A CD1 1 
ATOM   79   C CD2 . LEU   A 1 16  ? 2.525   51.269 -5.726  1.00 26.10  ? 672  LEU   A CD2 1 
ATOM   80   N N   . ILE   A 1 17  ? -0.503  48.880 -8.211  1.00 20.46  ? 673  ILE   A N   1 
ATOM   81   C CA  . ILE   A 1 17  ? -1.743  48.394 -7.595  1.00 21.23  ? 673  ILE   A CA  1 
ATOM   82   C C   . ILE   A 1 17  ? -2.057  46.972 -8.094  1.00 23.86  ? 673  ILE   A C   1 
ATOM   83   O O   . ILE   A 1 17  ? -2.443  46.113 -7.290  1.00 23.74  ? 673  ILE   A O   1 
ATOM   84   C CB  . ILE   A 1 17  ? -2.922  49.397 -7.866  1.00 25.78  ? 673  ILE   A CB  1 
ATOM   85   C CG1 . ILE   A 1 17  ? -2.655  50.818 -7.282  1.00 26.27  ? 673  ILE   A CG1 1 
ATOM   86   C CG2 . ILE   A 1 17  ? -4.305  48.860 -7.415  1.00 26.59  ? 673  ILE   A CG2 1 
ATOM   87   C CD1 . ILE   A 1 17  ? -2.199  50.939 -5.833  1.00 31.24  ? 673  ILE   A CD1 1 
ATOM   88   N N   . LYS   A 1 18  ? -1.892  46.732 -9.408  1.00 19.99  ? 674  LYS   A N   1 
ATOM   89   C CA  . LYS   A 1 18  ? -2.189  45.443 -10.043 1.00 20.85  ? 674  LYS   A CA  1 
ATOM   90   C C   . LYS   A 1 18  ? -1.271  44.345 -9.506  1.00 26.14  ? 674  LYS   A C   1 
ATOM   91   O O   . LYS   A 1 18  ? -1.714  43.229 -9.220  1.00 26.42  ? 674  LYS   A O   1 
ATOM   92   C CB  . LYS   A 1 18  ? -2.040  45.536 -11.568 1.00 25.42  ? 674  LYS   A CB  1 
ATOM   93   C CG  . LYS   A 1 18  ? -3.175  46.236 -12.298 1.00 36.13  ? 674  LYS   A CG  1 
ATOM   94   C CD  . LYS   A 1 18  ? -3.123  45.952 -13.795 1.00 39.36  ? 674  LYS   A CD  1 
ATOM   95   C CE  . LYS   A 1 18  ? -2.439  47.045 -14.598 1.00 54.98  ? 674  LYS   A CE  1 
ATOM   96   N NZ  . LYS   A 1 18  ? -2.384  46.721 -16.051 1.00 63.77  ? 674  LYS   A NZ  1 
ATOM   97   N N   . MET   A 1 19  ? 0.004   44.693 -9.352  1.00 24.15  ? 675  MET   A N   1 
ATOM   98   C CA  . MET   A 1 19  ? 1.077   43.876 -8.842  1.00 24.33  ? 675  MET   A CA  1 
ATOM   99   C C   . MET   A 1 19  ? 0.768   43.412 -7.426  1.00 25.01  ? 675  MET   A C   1 
ATOM   100  O O   . MET   A 1 19  ? 0.778   42.213 -7.171  1.00 23.64  ? 675  MET   A O   1 
ATOM   101  C CB  . MET   A 1 19  ? 2.337   44.736 -8.830  1.00 28.26  ? 675  MET   A CB  1 
ATOM   102  C CG  . MET   A 1 19  ? 3.623   43.974 -8.854  1.00 34.12  ? 675  MET   A CG  1 
ATOM   103  S SD  . MET   A 1 19  ? 4.971   45.163 -8.823  1.00 39.49  ? 675  MET   A SD  1 
ATOM   104  C CE  . MET   A 1 19  ? 6.289   44.073 -8.506  1.00 36.36  ? 675  MET   A CE  1 
ATOM   105  N N   . ILE   A 1 20  ? 0.479   44.360 -6.514  1.00 21.54  ? 676  ILE   A N   1 
ATOM   106  C CA  . ILE   A 1 20  ? 0.247   44.092 -5.099  1.00 21.09  ? 676  ILE   A CA  1 
ATOM   107  C C   . ILE   A 1 20  ? -1.111  43.451 -4.812  1.00 24.82  ? 676  ILE   A C   1 
ATOM   108  O O   . ILE   A 1 20  ? -1.222  42.783 -3.794  1.00 24.59  ? 676  ILE   A O   1 
ATOM   109  C CB  . ILE   A 1 20  ? 0.513   45.329 -4.185  1.00 23.75  ? 676  ILE   A CB  1 
ATOM   110  C CG1 . ILE   A 1 20  ? -0.541  46.426 -4.330  1.00 23.90  ? 676  ILE   A CG1 1 
ATOM   111  C CG2 . ILE   A 1 20  ? 1.899   45.878 -4.425  1.00 22.64  ? 676  ILE   A CG2 1 
ATOM   112  C CD1 . ILE   A 1 20  ? -0.683  47.230 -3.171  1.00 30.80  ? 676  ILE   A CD1 1 
ATOM   113  N N   . PHE   A 1 21  ? -2.132  43.633 -5.665  1.00 22.82  ? 677  PHE   A N   1 
ATOM   114  C CA  . PHE   A 1 21  ? -3.440  42.996 -5.420  1.00 22.56  ? 677  PHE   A CA  1 
ATOM   115  C C   . PHE   A 1 21  ? -3.637  41.672 -6.218  1.00 27.31  ? 677  PHE   A C   1 
ATOM   116  O O   . PHE   A 1 21  ? -4.750  41.135 -6.244  1.00 24.41  ? 677  PHE   A O   1 
ATOM   117  C CB  . PHE   A 1 21  ? -4.625  43.997 -5.641  1.00 23.75  ? 677  PHE   A CB  1 
ATOM   118  C CG  . PHE   A 1 21  ? -4.826  44.917 -4.447  1.00 24.18  ? 677  PHE   A CG  1 
ATOM   119  C CD1 . PHE   A 1 21  ? -5.352  44.432 -3.259  1.00 27.04  ? 677  PHE   A CD1 1 
ATOM   120  C CD2 . PHE   A 1 21  ? -4.395  46.238 -4.482  1.00 24.94  ? 677  PHE   A CD2 1 
ATOM   121  C CE1 . PHE   A 1 21  ? -5.514  45.269 -2.151  1.00 28.41  ? 677  PHE   A CE1 1 
ATOM   122  C CE2 . PHE   A 1 21  ? -4.567  47.078 -3.375  1.00 28.91  ? 677  PHE   A CE2 1 
ATOM   123  C CZ  . PHE   A 1 21  ? -5.134  46.590 -2.219  1.00 27.13  ? 677  PHE   A CZ  1 
ATOM   124  N N   . ASP   A 1 22  ? -2.541  41.126 -6.806  1.00 25.88  ? 678  ASP   A N   1 
ATOM   125  C CA  . ASP   A 1 22  ? -2.526  39.874 -7.580  1.00 26.02  ? 678  ASP   A CA  1 
ATOM   126  C C   . ASP   A 1 22  ? -2.828  38.673 -6.670  1.00 27.99  ? 678  ASP   A C   1 
ATOM   127  O O   . ASP   A 1 22  ? -2.029  38.355 -5.791  1.00 27.61  ? 678  ASP   A O   1 
ATOM   128  C CB  . ASP   A 1 22  ? -1.160  39.695 -8.293  1.00 28.56  ? 678  ASP   A CB  1 
ATOM   129  C CG  . ASP   A 1 22  ? -1.205  38.798 -9.528  1.00 40.75  ? 678  ASP   A CG  1 
ATOM   130  O OD1 . ASP   A 1 22  ? -1.239  37.558 -9.365  1.00 40.69  ? 678  ASP   A OD1 1 
ATOM   131  O OD2 . ASP   A 1 22  ? -1.195  39.339 -10.657 1.00 50.73  ? 678  ASP   A OD2 1 
ATOM   132  N N   . VAL   A 1 23  ? -3.994  38.034 -6.880  1.00 23.99  ? 679  VAL   A N   1 
ATOM   133  C CA  . VAL   A 1 23  ? -4.506  36.878 -6.121  1.00 24.05  ? 679  VAL   A CA  1 
ATOM   134  C C   . VAL   A 1 23  ? -3.677  35.617 -6.380  1.00 29.72  ? 679  VAL   A C   1 
ATOM   135  O O   . VAL   A 1 23  ? -3.460  34.830 -5.455  1.00 30.19  ? 679  VAL   A O   1 
ATOM   136  C CB  . VAL   A 1 23  ? -6.017  36.652 -6.393  1.00 27.30  ? 679  VAL   A CB  1 
ATOM   137  C CG1 . VAL   A 1 23  ? -6.492  35.279 -5.916  1.00 27.84  ? 679  VAL   A CG1 1 
ATOM   138  C CG2 . VAL   A 1 23  ? -6.853  37.756 -5.769  1.00 26.59  ? 679  VAL   A CG2 1 
ATOM   139  N N   . GLU   A 1 24  ? -3.246  35.414 -7.644  1.00 25.06  ? 680  GLU   A N   1 
ATOM   140  C CA  . GLU   A 1 24  ? -2.439  34.271 -8.032  1.00 24.39  ? 680  GLU   A CA  1 
ATOM   141  C C   . GLU   A 1 24  ? -1.019  34.355 -7.448  1.00 26.01  ? 680  GLU   A C   1 
ATOM   142  O O   . GLU   A 1 24  ? -0.399  33.314 -7.214  1.00 23.66  ? 680  GLU   A O   1 
ATOM   143  C CB  . GLU   A 1 24  ? -2.425  34.078 -9.557  1.00 25.78  ? 680  GLU   A CB  1 
ATOM   144  C CG  . GLU   A 1 24  ? -3.786  33.802 -10.181 1.00 38.73  ? 680  GLU   A CG  1 
ATOM   145  C CD  . GLU   A 1 24  ? -4.653  32.709 -9.584  1.00 55.31  ? 680  GLU   A CD  1 
ATOM   146  O OE1 . GLU   A 1 24  ? -4.133  31.591 -9.355  1.00 53.09  ? 680  GLU   A OE1 1 
ATOM   147  O OE2 . GLU   A 1 24  ? -5.861  32.968 -9.364  1.00 35.55  ? 680  GLU   A OE2 1 
ATOM   148  N N   . SER   A 1 25  ? -0.522  35.584 -7.162  1.00 25.20  ? 681  SER   A N   1 
ATOM   149  C CA  . SER   A 1 25  ? 0.792   35.771 -6.518  1.00 25.45  ? 681  SER   A CA  1 
ATOM   150  C C   . SER   A 1 25  ? 0.667   35.371 -5.043  1.00 27.03  ? 681  SER   A C   1 
ATOM   151  O O   . SER   A 1 25  ? 1.571   34.745 -4.497  1.00 27.95  ? 681  SER   A O   1 
ATOM   152  C CB  . SER   A 1 25  ? 1.262   37.222 -6.641  1.00 29.53  ? 681  SER   A CB  1 
ATOM   153  O OG  . SER   A 1 25  ? 1.456   37.591 -7.995  1.00 38.75  ? 681  SER   A OG  1 
ATOM   154  N N   . MET   A 1 26  ? -0.471  35.712 -4.422  1.00 23.10  ? 682  MET   A N   1 
ATOM   155  C CA  . MET   A 1 26  ? -0.813  35.386 -3.031  1.00 23.76  ? 682  MET   A CA  1 
ATOM   156  C C   . MET   A 1 26  ? -0.888  33.886 -2.871  1.00 27.11  ? 682  MET   A C   1 
ATOM   157  O O   . MET   A 1 26  ? -0.346  33.352 -1.910  1.00 26.15  ? 682  MET   A O   1 
ATOM   158  C CB  . MET   A 1 26  ? -2.149  36.018 -2.605  1.00 26.12  ? 682  MET   A CB  1 
ATOM   159  C CG  . MET   A 1 26  ? -2.132  37.508 -2.520  1.00 30.25  ? 682  MET   A CG  1 
ATOM   160  S SD  . MET   A 1 26  ? -3.798  38.082 -2.117  1.00 35.91  ? 682  MET   A SD  1 
ATOM   161  C CE  . MET   A 1 26  ? -3.768  39.675 -2.871  1.00 32.64  ? 682  MET   A CE  1 
ATOM   162  N N   . LYS   A 1 27  ? -1.504  33.210 -3.848  1.00 25.42  ? 683  LYS   A N   1 
ATOM   163  C CA  . LYS   A 1 27  ? -1.620  31.748 -3.906  1.00 25.71  ? 683  LYS   A CA  1 
ATOM   164  C C   . LYS   A 1 27  ? -0.241  31.096 -4.146  1.00 28.15  ? 683  LYS   A C   1 
ATOM   165  O O   . LYS   A 1 27  ? 0.094   30.136 -3.459  1.00 27.79  ? 683  LYS   A O   1 
ATOM   166  C CB  . LYS   A 1 27  ? -2.625  31.317 -4.994  1.00 27.48  ? 683  LYS   A CB  1 
ATOM   167  C CG  . LYS   A 1 27  ? -4.067  31.653 -4.672  1.00 34.64  ? 683  LYS   A CG  1 
ATOM   168  C CD  . LYS   A 1 27  ? -4.985  31.286 -5.839  1.00 43.30  ? 683  LYS   A CD  1 
ATOM   169  C CE  . LYS   A 1 27  ? -6.447  31.473 -5.509  1.00 47.56  ? 683  LYS   A CE  1 
ATOM   170  N NZ  . LYS   A 1 27  ? -7.335  30.804 -6.498  1.00 51.78  ? 683  LYS   A NZ  1 
ATOM   171  N N   . LYS   A 1 28  ? 0.556   31.626 -5.104  1.00 25.55  ? 684  LYS   A N   1 
ATOM   172  C CA  . LYS   A 1 28  ? 1.911   31.137 -5.411  1.00 25.50  ? 684  LYS   A CA  1 
ATOM   173  C C   . LYS   A 1 28  ? 2.799   31.228 -4.170  1.00 29.62  ? 684  LYS   A C   1 
ATOM   174  O O   . LYS   A 1 28  ? 3.654   30.365 -3.972  1.00 30.35  ? 684  LYS   A O   1 
ATOM   175  C CB  . LYS   A 1 28  ? 2.536   31.933 -6.581  1.00 28.50  ? 684  LYS   A CB  1 
ATOM   176  C CG  . LYS   A 1 28  ? 3.715   31.228 -7.255  1.00 39.92  ? 684  LYS   A CG  1 
ATOM   177  C CD  . LYS   A 1 28  ? 4.457   32.125 -8.237  1.00 49.40  ? 684  LYS   A CD  1 
ATOM   178  C CE  . LYS   A 1 28  ? 5.784   32.622 -7.718  1.00 60.16  ? 684  LYS   A CE  1 
ATOM   179  N NZ  . LYS   A 1 28  ? 6.773   32.785 -8.822  1.00 68.00  ? 684  LYS   A NZ  1 
ATOM   180  N N   . ALA   A 1 29  ? 2.587   32.272 -3.331  1.00 25.97  ? 685  ALA   A N   1 
ATOM   181  C CA  . ALA   A 1 29  ? 3.334   32.462 -2.105  1.00 25.65  ? 685  ALA   A CA  1 
ATOM   182  C C   . ALA   A 1 29  ? 2.930   31.408 -1.056  1.00 31.25  ? 685  ALA   A C   1 
ATOM   183  O O   . ALA   A 1 29  ? 3.793   30.908 -0.345  1.00 31.15  ? 685  ALA   A O   1 
ATOM   184  C CB  . ALA   A 1 29  ? 3.130   33.874 -1.573  1.00 25.93  ? 685  ALA   A CB  1 
ATOM   185  N N   . MET   A 1 30  ? 1.647   31.039 -0.991  1.00 28.66  ? 686  MET   A N   1 
ATOM   186  C CA  . MET   A 1 30  ? 1.174   30.024 -0.043  1.00 29.37  ? 686  MET   A CA  1 
ATOM   187  C C   . MET   A 1 30  ? 1.693   28.641 -0.408  1.00 32.52  ? 686  MET   A C   1 
ATOM   188  O O   . MET   A 1 30  ? 2.110   27.901 0.483   1.00 30.87  ? 686  MET   A O   1 
ATOM   189  C CB  . MET   A 1 30  ? -0.349  30.067 0.128   1.00 32.19  ? 686  MET   A CB  1 
ATOM   190  C CG  . MET   A 1 30  ? -0.810  31.322 0.874   1.00 36.62  ? 686  MET   A CG  1 
ATOM   191  S SD  . MET   A 1 30  ? -2.595  31.567 0.971   1.00 42.44  ? 686  MET   A SD  1 
ATOM   192  C CE  . MET   A 1 30  ? -3.074  30.282 2.219   1.00 39.06  ? 686  MET   A CE  1 
ATOM   193  N N   . VAL   A 1 31  ? 1.726   28.329 -1.724  1.00 30.18  ? 687  VAL   A N   1 
ATOM   194  C CA  . VAL   A 1 31  ? 2.242   27.079 -2.311  1.00 30.39  ? 687  VAL   A CA  1 
ATOM   195  C C   . VAL   A 1 31  ? 3.753   26.908 -1.995  1.00 36.29  ? 687  VAL   A C   1 
ATOM   196  O O   . VAL   A 1 31  ? 4.197   25.802 -1.687  1.00 35.01  ? 687  VAL   A O   1 
ATOM   197  C CB  . VAL   A 1 31  ? 1.919   27.009 -3.832  1.00 34.05  ? 687  VAL   A CB  1 
ATOM   198  C CG1 . VAL   A 1 31  ? 2.791   25.988 -4.575  1.00 34.43  ? 687  VAL   A CG1 1 
ATOM   199  C CG2 . VAL   A 1 31  ? 0.446   26.721 -4.061  1.00 33.38  ? 687  VAL   A CG2 1 
ATOM   200  N N   . GLU   A 1 32  ? 4.511   28.025 -2.011  1.00 36.07  ? 688  GLU   A N   1 
ATOM   201  C CA  . GLU   A 1 32  ? 5.945   28.093 -1.700  1.00 36.68  ? 688  GLU   A CA  1 
ATOM   202  C C   . GLU   A 1 32  ? 6.227   27.633 -0.258  1.00 43.03  ? 688  GLU   A C   1 
ATOM   203  O O   . GLU   A 1 32  ? 7.302   27.091 0.029   1.00 41.53  ? 688  GLU   A O   1 
ATOM   204  C CB  . GLU   A 1 32  ? 6.442   29.532 -1.903  1.00 37.45  ? 688  GLU   A CB  1 
ATOM   205  C CG  . GLU   A 1 32  ? 7.895   29.630 -2.312  1.00 44.12  ? 688  GLU   A CG  1 
ATOM   206  C CD  . GLU   A 1 32  ? 8.308   30.982 -2.860  1.00 61.13  ? 688  GLU   A CD  1 
ATOM   207  O OE1 . GLU   A 1 32  ? 9.427   31.430 -2.516  1.00 41.33  ? 688  GLU   A OE1 1 
ATOM   208  O OE2 . GLU   A 1 32  ? 7.527   31.593 -3.628  1.00 52.17  ? 688  GLU   A OE2 1 
ATOM   209  N N   . TYR   A 1 33  ? 5.245   27.853 0.641   1.00 40.60  ? 689  TYR   A N   1 
ATOM   210  C CA  . TYR   A 1 33  ? 5.313   27.479 2.053   1.00 40.61  ? 689  TYR   A CA  1 
ATOM   211  C C   . TYR   A 1 33  ? 4.848   26.052 2.300   1.00 45.38  ? 689  TYR   A C   1 
ATOM   212  O O   . TYR   A 1 33  ? 4.849   25.593 3.447   1.00 45.27  ? 689  TYR   A O   1 
ATOM   213  C CB  . TYR   A 1 33  ? 4.472   28.455 2.886   1.00 41.45  ? 689  TYR   A CB  1 
ATOM   214  C CG  . TYR   A 1 33  ? 5.099   29.818 3.010   1.00 42.73  ? 689  TYR   A CG  1 
ATOM   215  C CD1 . TYR   A 1 33  ? 6.388   29.970 3.515   1.00 45.20  ? 689  TYR   A CD1 1 
ATOM   216  C CD2 . TYR   A 1 33  ? 4.383   30.966 2.688   1.00 42.69  ? 689  TYR   A CD2 1 
ATOM   217  C CE1 . TYR   A 1 33  ? 6.970   31.226 3.639   1.00 46.90  ? 689  TYR   A CE1 1 
ATOM   218  C CE2 . TYR   A 1 33  ? 4.952   32.229 2.817   1.00 42.95  ? 689  TYR   A CE2 1 
ATOM   219  C CZ  . TYR   A 1 33  ? 6.246   32.352 3.297   1.00 48.00  ? 689  TYR   A CZ  1 
ATOM   220  O OH  . TYR   A 1 33  ? 6.838   33.571 3.434   1.00 44.11  ? 689  TYR   A OH  1 
ATOM   221  N N   . GLU   A 1 34  ? 4.445   25.360 1.216   1.00 41.87  ? 690  GLU   A N   1 
ATOM   222  C CA  . GLU   A 1 34  ? 3.933   23.990 1.187   1.00 41.70  ? 690  GLU   A CA  1 
ATOM   223  C C   . GLU   A 1 34  ? 2.579   23.862 1.920   1.00 43.05  ? 690  GLU   A C   1 
ATOM   224  O O   . GLU   A 1 34  ? 2.265   22.806 2.440   1.00 43.33  ? 690  GLU   A O   1 
ATOM   225  C CB  . GLU   A 1 34  ? 4.983   22.960 1.670   1.00 43.66  ? 690  GLU   A CB  1 
ATOM   226  C CG  . GLU   A 1 34  ? 6.283   23.012 0.877   1.00 59.45  ? 690  GLU   A CG  1 
ATOM   227  C CD  . GLU   A 1 34  ? 7.141   21.760 0.889   1.00 88.67  ? 690  GLU   A CD  1 
ATOM   228  O OE1 . GLU   A 1 34  ? 7.506   21.283 -0.209  1.00 95.17  ? 690  GLU   A OE1 1 
ATOM   229  O OE2 . GLU   A 1 34  ? 7.444   21.252 1.993   1.00 84.03  ? 690  GLU   A OE2 1 
ATOM   230  N N   . ILE   A 1 35  ? 1.764   24.926 1.912   1.00 37.48  ? 691  ILE   A N   1 
ATOM   231  C CA  . ILE   A 1 35  ? 0.435   24.930 2.528   1.00 37.28  ? 691  ILE   A CA  1 
ATOM   232  C C   . ILE   A 1 35  ? -0.539  24.202 1.582   1.00 42.99  ? 691  ILE   A C   1 
ATOM   233  O O   . ILE   A 1 35  ? -0.506  24.427 0.363   1.00 43.22  ? 691  ILE   A O   1 
ATOM   234  C CB  . ILE   A 1 35  ? -0.049  26.389 2.846   1.00 39.85  ? 691  ILE   A CB  1 
ATOM   235  C CG1 . ILE   A 1 35  ? 0.884   27.120 3.819   1.00 39.51  ? 691  ILE   A CG1 1 
ATOM   236  C CG2 . ILE   A 1 35  ? -1.498  26.440 3.360   1.00 40.96  ? 691  ILE   A CG2 1 
ATOM   237  C CD1 . ILE   A 1 35  ? 0.881   28.640 3.629   1.00 40.39  ? 691  ILE   A CD1 1 
ATOM   238  N N   . ASP   A 1 36  ? -1.409  23.355 2.152   1.00 39.86  ? 692  ASP   A N   1 
ATOM   239  C CA  . ASP   A 1 36  ? -2.436  22.648 1.401   1.00 40.46  ? 692  ASP   A CA  1 
ATOM   240  C C   . ASP   A 1 36  ? -3.588  23.645 1.174   1.00 44.91  ? 692  ASP   A C   1 
ATOM   241  O O   . ASP   A 1 36  ? -4.307  23.981 2.124   1.00 43.96  ? 692  ASP   A O   1 
ATOM   242  C CB  . ASP   A 1 36  ? -2.905  21.402 2.178   1.00 42.74  ? 692  ASP   A CB  1 
ATOM   243  C CG  . ASP   A 1 36  ? -3.627  20.363 1.339   1.00 56.14  ? 692  ASP   A CG  1 
ATOM   244  O OD1 . ASP   A 1 36  ? -4.768  20.638 0.903   1.00 56.04  ? 692  ASP   A OD1 1 
ATOM   245  O OD2 . ASP   A 1 36  ? -3.062  19.263 1.138   1.00 63.98  ? 692  ASP   A OD2 1 
ATOM   246  N N   . LEU   A 1 37  ? -3.741  24.154 -0.081  1.00 42.35  ? 693  LEU   A N   1 
ATOM   247  C CA  . LEU   A 1 37  ? -4.771  25.143 -0.457  1.00 41.48  ? 693  LEU   A CA  1 
ATOM   248  C C   . LEU   A 1 37  ? -6.151  24.543 -0.557  1.00 47.42  ? 693  LEU   A C   1 
ATOM   249  O O   . LEU   A 1 37  ? -7.144  25.274 -0.534  1.00 47.54  ? 693  LEU   A O   1 
ATOM   250  C CB  . LEU   A 1 37  ? -4.418  25.920 -1.736  1.00 41.18  ? 693  LEU   A CB  1 
ATOM   251  C CG  . LEU   A 1 37  ? -3.439  27.094 -1.586  1.00 46.08  ? 693  LEU   A CG  1 
ATOM   252  C CD1 . LEU   A 1 37  ? -2.922  27.526 -2.927  1.00 47.02  ? 693  LEU   A CD1 1 
ATOM   253  C CD2 . LEU   A 1 37  ? -4.082  28.294 -0.910  1.00 46.65  ? 693  LEU   A CD2 1 
ATOM   254  N N   . GLN   A 1 38  ? -6.223  23.214 -0.684  1.00 44.67  ? 694  GLN   A N   1 
ATOM   255  C CA  . GLN   A 1 38  ? -7.489  22.503 -0.710  1.00 44.82  ? 694  GLN   A CA  1 
ATOM   256  C C   . GLN   A 1 38  ? -8.018  22.428 0.724   1.00 49.09  ? 694  GLN   A C   1 
ATOM   257  O O   . GLN   A 1 38  ? -9.169  22.786 0.966   1.00 48.07  ? 694  GLN   A O   1 
ATOM   258  C CB  . GLN   A 1 38  ? -7.321  21.106 -1.331  1.00 46.00  ? 694  GLN   A CB  1 
ATOM   259  C CG  . GLN   A 1 38  ? -7.537  21.096 -2.839  1.00 49.36  ? 694  GLN   A CG  1 
ATOM   260  C CD  . GLN   A 1 38  ? -8.992  20.917 -3.199  1.00 72.50  ? 694  GLN   A CD  1 
ATOM   261  O OE1 . GLN   A 1 38  ? -9.778  21.874 -3.228  1.00 66.60  ? 694  GLN   A OE1 1 
ATOM   262  N NE2 . GLN   A 1 38  ? -9.384  19.678 -3.474  1.00 67.28  ? 694  GLN   A NE2 1 
ATOM   263  N N   . LYS   A 1 39  ? -7.143  22.017 1.680   1.00 46.46  ? 695  LYS   A N   1 
ATOM   264  C CA  . LYS   A 1 39  ? -7.437  21.905 3.119   1.00 45.83  ? 695  LYS   A CA  1 
ATOM   265  C C   . LYS   A 1 39  ? -7.623  23.284 3.749   1.00 48.35  ? 695  LYS   A C   1 
ATOM   266  O O   . LYS   A 1 39  ? -8.293  23.399 4.774   1.00 48.99  ? 695  LYS   A O   1 
ATOM   267  C CB  . LYS   A 1 39  ? -6.316  21.150 3.853   1.00 48.30  ? 695  LYS   A CB  1 
ATOM   268  C CG  . LYS   A 1 39  ? -6.365  19.632 3.719   1.00 63.12  ? 695  LYS   A CG  1 
ATOM   269  C CD  . LYS   A 1 39  ? -5.179  18.997 4.450   1.00 73.12  ? 695  LYS   A CD  1 
ATOM   270  C CE  . LYS   A 1 39  ? -5.347  17.514 4.690   1.00 83.85  ? 695  LYS   A CE  1 
ATOM   271  N NZ  . LYS   A 1 39  ? -4.917  16.706 3.520   1.00 91.43  ? 695  LYS   A NZ  1 
ATOM   272  N N   . MET   A 1 40  ? -7.006  24.324 3.153   1.00 43.41  ? 696  MET   A N   1 
ATOM   273  C CA  . MET   A 1 40  ? -7.117  25.696 3.626   1.00 42.21  ? 696  MET   A CA  1 
ATOM   274  C C   . MET   A 1 40  ? -6.780  26.757 2.563   1.00 39.31  ? 696  MET   A C   1 
ATOM   275  O O   . MET   A 1 40  ? -5.641  27.244 2.504   1.00 38.67  ? 696  MET   A O   1 
ATOM   276  C CB  . MET   A 1 40  ? -6.314  25.943 4.909   1.00 45.44  ? 696  MET   A CB  1 
ATOM   277  C CG  . MET   A 1 40  ? -6.889  27.088 5.715   1.00 49.93  ? 696  MET   A CG  1 
ATOM   278  S SD  . MET   A 1 40  ? -5.690  28.183 6.481   1.00 55.44  ? 696  MET   A SD  1 
ATOM   279  C CE  . MET   A 1 40  ? -4.326  28.147 5.250   1.00 52.31  ? 696  MET   A CE  1 
ATOM   280  N N   . PRO   A 1 41  ? -7.788  27.244 1.815   1.00 30.86  ? 697  PRO   A N   1 
ATOM   281  C CA  . PRO   A 1 41  ? -7.514  28.295 0.826   1.00 29.58  ? 697  PRO   A CA  1 
ATOM   282  C C   . PRO   A 1 41  ? -7.264  29.692 1.424   1.00 32.47  ? 697  PRO   A C   1 
ATOM   283  O O   . PRO   A 1 41  ? -7.369  29.899 2.647   1.00 32.31  ? 697  PRO   A O   1 
ATOM   284  C CB  . PRO   A 1 41  ? -8.758  28.256 -0.071  1.00 31.14  ? 697  PRO   A CB  1 
ATOM   285  C CG  . PRO   A 1 41  ? -9.843  27.757 0.805   1.00 35.77  ? 697  PRO   A CG  1 
ATOM   286  C CD  . PRO   A 1 41  ? -9.195  26.797 1.753   1.00 32.05  ? 697  PRO   A CD  1 
ATOM   287  N N   . LEU   A 1 42  ? -6.936  30.655 0.528   1.00 27.22  ? 698  LEU   A N   1 
ATOM   288  C CA  . LEU   A 1 42  ? -6.694  32.069 0.795   1.00 26.57  ? 698  LEU   A CA  1 
ATOM   289  C C   . LEU   A 1 42  ? -7.819  32.687 1.604   1.00 27.34  ? 698  LEU   A C   1 
ATOM   290  O O   . LEU   A 1 42  ? -7.553  33.529 2.462   1.00 25.01  ? 698  LEU   A O   1 
ATOM   291  C CB  . LEU   A 1 42  ? -6.602  32.843 -0.540  1.00 27.32  ? 698  LEU   A CB  1 
ATOM   292  C CG  . LEU   A 1 42  ? -5.253  33.393 -0.983  1.00 33.21  ? 698  LEU   A CG  1 
ATOM   293  C CD1 . LEU   A 1 42  ? -5.400  34.140 -2.275  1.00 34.04  ? 698  LEU   A CD1 1 
ATOM   294  C CD2 . LEU   A 1 42  ? -4.667  34.333 0.042   1.00 36.33  ? 698  LEU   A CD2 1 
ATOM   295  N N   . GLY   A 1 43  ? -9.062  32.286 1.288   1.00 24.21  ? 699  GLY   A N   1 
ATOM   296  C CA  . GLY   A 1 43  ? -10.261 32.812 1.924   1.00 24.03  ? 699  GLY   A CA  1 
ATOM   297  C C   . GLY   A 1 43  ? -10.526 32.273 3.312   1.00 29.74  ? 699  GLY   A C   1 
ATOM   298  O O   . GLY   A 1 43  ? -11.339 32.843 4.047   1.00 28.80  ? 699  GLY   A O   1 
ATOM   299  N N   . LYS   A 1 44  ? -9.864  31.150 3.669   1.00 27.77  ? 700  LYS   A N   1 
ATOM   300  C CA  . LYS   A 1 44  ? -10.000 30.531 4.991   1.00 27.17  ? 700  LYS   A CA  1 
ATOM   301  C C   . LYS   A 1 44  ? -8.964  31.075 5.986   1.00 29.32  ? 700  LYS   A C   1 
ATOM   302  O O   . LYS   A 1 44  ? -9.088  30.852 7.193   1.00 27.95  ? 700  LYS   A O   1 
ATOM   303  C CB  . LYS   A 1 44  ? -9.980  29.002 4.905   1.00 29.93  ? 700  LYS   A CB  1 
ATOM   304  C CG  . LYS   A 1 44  ? -11.335 28.414 4.481   1.00 51.96  ? 700  LYS   A CG  1 
ATOM   305  C CD  . LYS   A 1 44  ? -11.336 26.892 4.565   1.00 68.13  ? 700  LYS   A CD  1 
ATOM   306  C CE  . LYS   A 1 44  ? -12.376 26.250 3.673   1.00 79.35  ? 700  LYS   A CE  1 
ATOM   307  N NZ  . LYS   A 1 44  ? -12.191 24.770 3.606   1.00 82.75  ? 700  LYS   A NZ  1 
ATOM   308  N N   . LEU   A 1 45  ? -7.973  31.829 5.473   1.00 25.56  ? 701  LEU   A N   1 
ATOM   309  C CA  . LEU   A 1 45  ? -6.914  32.448 6.264   1.00 25.81  ? 701  LEU   A CA  1 
ATOM   310  C C   . LEU   A 1 45  ? -7.532  33.477 7.226   1.00 27.90  ? 701  LEU   A C   1 
ATOM   311  O O   . LEU   A 1 45  ? -8.325  34.310 6.794   1.00 26.04  ? 701  LEU   A O   1 
ATOM   312  C CB  . LEU   A 1 45  ? -5.914  33.103 5.283   1.00 26.37  ? 701  LEU   A CB  1 
ATOM   313  C CG  . LEU   A 1 45  ? -4.398  32.928 5.446   1.00 30.26  ? 701  LEU   A CG  1 
ATOM   314  C CD1 . LEU   A 1 45  ? -3.972  31.501 5.774   1.00 30.18  ? 701  LEU   A CD1 1 
ATOM   315  C CD2 . LEU   A 1 45  ? -3.655  33.451 4.221   1.00 29.40  ? 701  LEU   A CD2 1 
ATOM   316  N N   . SER   A 1 46  ? -7.231  33.364 8.533   1.00 23.89  ? 702  SER   A N   1 
ATOM   317  C CA  . SER   A 1 46  ? -7.724  34.270 9.578   1.00 22.86  ? 702  SER   A CA  1 
ATOM   318  C C   . SER   A 1 46  ? -6.661  34.527 10.635  1.00 27.06  ? 702  SER   A C   1 
ATOM   319  O O   . SER   A 1 46  ? -5.806  33.667 10.854  1.00 29.27  ? 702  SER   A O   1 
ATOM   320  C CB  . SER   A 1 46  ? -8.990  33.705 10.220  1.00 24.91  ? 702  SER   A CB  1 
ATOM   321  O OG  . SER   A 1 46  ? -8.682  32.732 11.203  1.00 24.37  ? 702  SER   A OG  1 
ATOM   322  N N   . LYS   A 1 47  ? -6.715  35.694 11.299  1.00 23.42  ? 703  LYS   A N   1 
ATOM   323  C CA  . LYS   A 1 47  ? -5.762  36.144 12.347  1.00 23.17  ? 703  LYS   A CA  1 
ATOM   324  C C   . LYS   A 1 47  ? -5.733  35.157 13.513  1.00 27.66  ? 703  LYS   A C   1 
ATOM   325  O O   . LYS   A 1 47  ? -4.671  34.710 13.914  1.00 26.36  ? 703  LYS   A O   1 
ATOM   326  C CB  . LYS   A 1 47  ? -6.112  37.564 12.841  1.00 24.69  ? 703  LYS   A CB  1 
ATOM   327  C CG  . LYS   A 1 47  ? -5.934  38.663 11.782  1.00 28.75  ? 703  LYS   A CG  1 
ATOM   328  C CD  . LYS   A 1 47  ? -6.910  39.827 11.989  1.00 44.64  ? 703  LYS   A CD  1 
ATOM   329  C CE  . LYS   A 1 47  ? -6.382  40.951 12.845  1.00 54.75  ? 703  LYS   A CE  1 
ATOM   330  N NZ  . LYS   A 1 47  ? -7.456  41.934 13.152  1.00 63.51  ? 703  LYS   A NZ  1 
ATOM   331  N N   . ARG   A 1 48  ? -6.928  34.801 14.002  1.00 24.41  ? 704  ARG   A N   1 
ATOM   332  C CA  . ARG   A 1 48  ? -7.282  33.820 15.013  1.00 23.52  ? 704  ARG   A CA  1 
ATOM   333  C C   . ARG   A 1 48  ? -6.483  32.502 14.812  1.00 24.68  ? 704  ARG   A C   1 
ATOM   334  O O   . ARG   A 1 48  ? -5.933  31.960 15.762  1.00 24.10  ? 704  ARG   A O   1 
ATOM   335  C CB  . ARG   A 1 48  ? -8.792  33.568 14.812  1.00 24.82  ? 704  ARG   A CB  1 
ATOM   336  C CG  . ARG   A 1 48  ? -9.505  32.720 15.838  1.00 31.97  ? 704  ARG   A CG  1 
ATOM   337  C CD  . ARG   A 1 48  ? -10.967 32.612 15.508  1.00 24.70  ? 704  ARG   A CD  1 
ATOM   338  N NE  . ARG   A 1 48  ? -11.637 33.918 15.562  1.00 29.32  ? 704  ARG   A NE  1 
ATOM   339  C CZ  . ARG   A 1 48  ? -12.112 34.575 14.506  1.00 36.47  ? 704  ARG   A CZ  1 
ATOM   340  N NH1 . ARG   A 1 48  ? -12.651 35.773 14.654  1.00 25.60  ? 704  ARG   A NH1 1 
ATOM   341  N NH2 . ARG   A 1 48  ? -12.032 34.044 13.290  1.00 20.01  ? 704  ARG   A NH2 1 
ATOM   342  N N   . GLN   A 1 49  ? -6.492  31.968 13.593  1.00 21.32  ? 705  GLN   A N   1 
ATOM   343  C CA  . GLN   A 1 49  ? -5.813  30.716 13.233  1.00 21.31  ? 705  GLN   A CA  1 
ATOM   344  C C   . GLN   A 1 49  ? -4.307  30.917 13.228  1.00 24.29  ? 705  GLN   A C   1 
ATOM   345  O O   . GLN   A 1 49  ? -3.593  30.076 13.775  1.00 24.36  ? 705  GLN   A O   1 
ATOM   346  C CB  . GLN   A 1 49  ? -6.311  30.170 11.864  1.00 21.90  ? 705  GLN   A CB  1 
ATOM   347  C CG  . GLN   A 1 49  ? -7.705  29.545 11.951  1.00 27.95  ? 705  GLN   A CG  1 
ATOM   348  C CD  . GLN   A 1 49  ? -8.223  29.026 10.632  1.00 44.56  ? 705  GLN   A CD  1 
ATOM   349  O OE1 . GLN   A 1 49  ? -8.427  27.823 10.443  1.00 43.66  ? 705  GLN   A OE1 1 
ATOM   350  N NE2 . GLN   A 1 49  ? -8.486  29.919 9.703   1.00 35.92  ? 705  GLN   A NE2 1 
ATOM   351  N N   . ILE   A 1 50  ? -3.837  32.038 12.610  1.00 21.69  ? 706  ILE   A N   1 
ATOM   352  C CA  . ILE   A 1 50  ? -2.420  32.422 12.525  1.00 21.77  ? 706  ILE   A CA  1 
ATOM   353  C C   . ILE   A 1 50  ? -1.855  32.590 13.932  1.00 25.08  ? 706  ILE   A C   1 
ATOM   354  O O   . ILE   A 1 50  ? -0.828  31.991 14.220  1.00 25.68  ? 706  ILE   A O   1 
ATOM   355  C CB  . ILE   A 1 50  ? -2.120  33.637 11.574  1.00 24.24  ? 706  ILE   A CB  1 
ATOM   356  C CG1 . ILE   A 1 50  ? -2.592  33.341 10.128  1.00 24.33  ? 706  ILE   A CG1 1 
ATOM   357  C CG2 . ILE   A 1 50  ? -0.589  33.973 11.578  1.00 21.04  ? 706  ILE   A CG2 1 
ATOM   358  C CD1 . ILE   A 1 50  ? -2.907  34.567 9.216   1.00 25.10  ? 706  ILE   A CD1 1 
ATOM   359  N N   . GLN   A 1 51  ? -2.577  33.310 14.824  1.00 20.09  ? 707  GLN   A N   1 
ATOM   360  C CA  . GLN   A 1 51  ? -2.173  33.534 16.221  1.00 19.42  ? 707  GLN   A CA  1 
ATOM   361  C C   . GLN   A 1 51  ? -2.083  32.209 17.028  1.00 21.07  ? 707  GLN   A C   1 
ATOM   362  O O   . GLN   A 1 51  ? -1.181  32.060 17.831  1.00 18.41  ? 707  GLN   A O   1 
ATOM   363  C CB  . GLN   A 1 51  ? -3.121  34.540 16.903  1.00 20.83  ? 707  GLN   A CB  1 
ATOM   364  C CG  . GLN   A 1 51  ? -2.900  35.989 16.447  1.00 35.79  ? 707  GLN   A CG  1 
ATOM   365  C CD  . GLN   A 1 51  ? -4.117  36.902 16.589  1.00 45.33  ? 707  GLN   A CD  1 
ATOM   366  O OE1 . GLN   A 1 51  ? -5.168  36.539 17.143  1.00 31.08  ? 707  GLN   A OE1 1 
ATOM   367  N NE2 . GLN   A 1 51  ? -3.997  38.128 16.082  1.00 37.70  ? 707  GLN   A NE2 1 
ATOM   368  N N   . ALA   A 1 52  ? -3.021  31.251 16.792  1.00 18.67  ? 708  ALA   A N   1 
ATOM   369  C CA  . ALA   A 1 52  ? -3.030  29.929 17.426  1.00 17.78  ? 708  ALA   A CA  1 
ATOM   370  C C   . ALA   A 1 52  ? -1.803  29.142 16.945  1.00 21.47  ? 708  ALA   A C   1 
ATOM   371  O O   . ALA   A 1 52  ? -1.200  28.412 17.738  1.00 21.01  ? 708  ALA   A O   1 
ATOM   372  C CB  . ALA   A 1 52  ? -4.318  29.175 17.073  1.00 17.44  ? 708  ALA   A CB  1 
ATOM   373  N N   . ALA   A 1 53  ? -1.455  29.287 15.646  1.00 17.33  ? 709  ALA   A N   1 
ATOM   374  C CA  . ALA   A 1 53  ? -0.261  28.668 15.027  1.00 16.84  ? 709  ALA   A CA  1 
ATOM   375  C C   . ALA   A 1 53  ? 1.039   29.221 15.655  1.00 20.40  ? 709  ALA   A C   1 
ATOM   376  O O   . ALA   A 1 53  ? 1.980   28.462 15.868  1.00 20.49  ? 709  ALA   A O   1 
ATOM   377  C CB  . ALA   A 1 53  ? -0.247  28.907 13.526  1.00 17.02  ? 709  ALA   A CB  1 
ATOM   378  N N   . TYR   A 1 54  ? 1.096   30.533 15.918  1.00 17.62  ? 710  TYR   A N   1 
ATOM   379  C CA  . TYR   A 1 54  ? 2.247   31.172 16.577  1.00 17.53  ? 710  TYR   A CA  1 
ATOM   380  C C   . TYR   A 1 54  ? 2.432   30.618 17.981  1.00 22.73  ? 710  TYR   A C   1 
ATOM   381  O O   . TYR   A 1 54  ? 3.561   30.404 18.413  1.00 22.53  ? 710  TYR   A O   1 
ATOM   382  C CB  . TYR   A 1 54  ? 2.013   32.675 16.755  1.00 16.88  ? 710  TYR   A CB  1 
ATOM   383  C CG  . TYR   A 1 54  ? 2.407   33.563 15.610  1.00 17.65  ? 710  TYR   A CG  1 
ATOM   384  C CD1 . TYR   A 1 54  ? 3.718   33.583 15.130  1.00 20.16  ? 710  TYR   A CD1 1 
ATOM   385  C CD2 . TYR   A 1 54  ? 1.496   34.450 15.054  1.00 18.66  ? 710  TYR   A CD2 1 
ATOM   386  C CE1 . TYR   A 1 54  ? 4.108   34.477 14.131  1.00 22.00  ? 710  TYR   A CE1 1 
ATOM   387  C CE2 . TYR   A 1 54  ? 1.856   35.299 14.017  1.00 19.40  ? 710  TYR   A CE2 1 
ATOM   388  C CZ  . TYR   A 1 54  ? 3.173   35.360 13.605  1.00 26.44  ? 710  TYR   A CZ  1 
ATOM   389  O OH  . TYR   A 1 54  ? 3.492   36.234 12.603  1.00 28.19  ? 710  TYR   A OH  1 
ATOM   390  N N   . SER   A 1 55  ? 1.320   30.517 18.716  1.00 19.15  ? 711  SER   A N   1 
ATOM   391  C CA  . SER   A 1 55  ? 1.257   30.072 20.091  1.00 18.90  ? 711  SER   A CA  1 
ATOM   392  C C   . SER   A 1 55  ? 1.778   28.623 20.223  1.00 24.03  ? 711  SER   A C   1 
ATOM   393  O O   . SER   A 1 55  ? 2.554   28.339 21.145  1.00 22.76  ? 711  SER   A O   1 
ATOM   394  C CB  . SER   A 1 55  ? -0.167  30.240 20.619  1.00 21.39  ? 711  SER   A CB  1 
ATOM   395  O OG  . SER   A 1 55  ? -0.209  30.005 22.014  1.00 35.39  ? 711  SER   A OG  1 
ATOM   396  N N   . ILE   A 1 56  ? 1.392   27.727 19.275  1.00 21.25  ? 712  ILE   A N   1 
ATOM   397  C CA  . ILE   A 1 56  ? 1.875   26.340 19.258  1.00 20.92  ? 712  ILE   A CA  1 
ATOM   398  C C   . ILE   A 1 56  ? 3.389   26.308 18.954  1.00 24.91  ? 712  ILE   A C   1 
ATOM   399  O O   . ILE   A 1 56  ? 4.116   25.515 19.561  1.00 23.81  ? 712  ILE   A O   1 
ATOM   400  C CB  . ILE   A 1 56  ? 1.019   25.409 18.342  1.00 23.80  ? 712  ILE   A CB  1 
ATOM   401  C CG1 . ILE   A 1 56  ? -0.415  25.201 18.904  1.00 24.64  ? 712  ILE   A CG1 1 
ATOM   402  C CG2 . ILE   A 1 56  ? 1.703   24.052 18.059  1.00 24.36  ? 712  ILE   A CG2 1 
ATOM   403  C CD1 . ILE   A 1 56  ? -0.615  24.447 20.282  1.00 33.79  ? 712  ILE   A CD1 1 
ATOM   404  N N   . LEU   A 1 57  ? 3.864   27.206 18.056  1.00 22.86  ? 713  LEU   A N   1 
ATOM   405  C CA  . LEU   A 1 57  ? 5.284   27.363 17.701  1.00 23.69  ? 713  LEU   A CA  1 
ATOM   406  C C   . LEU   A 1 57  ? 6.090   27.794 18.924  1.00 28.67  ? 713  LEU   A C   1 
ATOM   407  O O   . LEU   A 1 57  ? 7.263   27.411 19.054  1.00 29.39  ? 713  LEU   A O   1 
ATOM   408  C CB  . LEU   A 1 57  ? 5.408   28.428 16.632  1.00 24.46  ? 713  LEU   A CB  1 
ATOM   409  C CG  . LEU   A 1 57  ? 6.203   28.138 15.372  1.00 29.57  ? 713  LEU   A CG  1 
ATOM   410  C CD1 . LEU   A 1 57  ? 6.050   26.683 14.917  1.00 29.30  ? 713  LEU   A CD1 1 
ATOM   411  C CD2 . LEU   A 1 57  ? 5.761   29.091 14.276  1.00 30.06  ? 713  LEU   A CD2 1 
ATOM   412  N N   . SER   A 1 58  ? 5.464   28.595 19.814  1.00 24.47  ? 714  SER   A N   1 
ATOM   413  C CA  . SER   A 1 58  ? 6.067   29.024 21.074  1.00 24.71  ? 714  SER   A CA  1 
ATOM   414  C C   . SER   A 1 58  ? 6.157   27.831 22.011  1.00 31.15  ? 714  SER   A C   1 
ATOM   415  O O   . SER   A 1 58  ? 7.152   27.698 22.729  1.00 31.24  ? 714  SER   A O   1 
ATOM   416  C CB  . SER   A 1 58  ? 5.270   30.148 21.717  1.00 23.66  ? 714  SER   A CB  1 
ATOM   417  O OG  . SER   A 1 58  ? 5.384   31.312 20.925  1.00 25.66  ? 714  SER   A OG  1 
ATOM   418  N N   . GLU   A 1 59  ? 5.144   26.946 21.988  1.00 29.21  ? 715  GLU   A N   1 
ATOM   419  C CA  . GLU   A 1 59  ? 5.190   25.732 22.808  1.00 30.20  ? 715  GLU   A CA  1 
ATOM   420  C C   . GLU   A 1 59  ? 6.282   24.779 22.281  1.00 33.67  ? 715  GLU   A C   1 
ATOM   421  O O   . GLU   A 1 59  ? 6.976   24.168 23.090  1.00 35.01  ? 715  GLU   A O   1 
ATOM   422  C CB  . GLU   A 1 59  ? 3.837   25.039 22.873  1.00 32.05  ? 715  GLU   A CB  1 
ATOM   423  C CG  . GLU   A 1 59  ? 3.645   24.350 24.209  1.00 48.08  ? 715  GLU   A CG  1 
ATOM   424  C CD  . GLU   A 1 59  ? 2.555   23.300 24.262  1.00 74.23  ? 715  GLU   A CD  1 
ATOM   425  O OE1 . GLU   A 1 59  ? 1.727   23.234 23.322  1.00 73.08  ? 715  GLU   A OE1 1 
ATOM   426  O OE2 . GLU   A 1 59  ? 2.539   22.532 25.249  1.00 66.69  ? 715  GLU   A OE2 1 
ATOM   427  N N   . VAL   A 1 60  ? 6.448   24.685 20.940  1.00 27.85  ? 716  VAL   A N   1 
ATOM   428  C CA  . VAL   A 1 60  ? 7.489   23.867 20.290  1.00 27.88  ? 716  VAL   A CA  1 
ATOM   429  C C   . VAL   A 1 60  ? 8.853   24.414 20.747  1.00 31.15  ? 716  VAL   A C   1 
ATOM   430  O O   . VAL   A 1 60  ? 9.688   23.640 21.218  1.00 28.95  ? 716  VAL   A O   1 
ATOM   431  C CB  . VAL   A 1 60  ? 7.356   23.839 18.731  1.00 31.41  ? 716  VAL   A CB  1 
ATOM   432  C CG1 . VAL   A 1 60  ? 8.547   23.134 18.074  1.00 30.43  ? 716  VAL   A CG1 1 
ATOM   433  C CG2 . VAL   A 1 60  ? 6.035   23.199 18.291  1.00 31.14  ? 716  VAL   A CG2 1 
ATOM   434  N N   . GLN   A 1 61  ? 9.036   25.757 20.649  1.00 28.94  ? 717  GLN   A N   1 
ATOM   435  C CA  . GLN   A 1 61  ? 10.218  26.529 21.057  1.00 30.00  ? 717  GLN   A CA  1 
ATOM   436  C C   . GLN   A 1 61  ? 10.625  26.207 22.510  1.00 35.68  ? 717  GLN   A C   1 
ATOM   437  O O   . GLN   A 1 61  ? 11.810  26.051 22.786  1.00 37.01  ? 717  GLN   A O   1 
ATOM   438  C CB  . GLN   A 1 61  ? 9.923   28.037 20.863  1.00 31.57  ? 717  GLN   A CB  1 
ATOM   439  C CG  . GLN   A 1 61  ? 10.706  29.015 21.754  1.00 53.73  ? 717  GLN   A CG  1 
ATOM   440  C CD  . GLN   A 1 61  ? 9.952   30.305 22.069  1.00 62.54  ? 717  GLN   A CD  1 
ATOM   441  O OE1 . GLN   A 1 61  ? 10.343  31.407 21.650  1.00 49.36  ? 717  GLN   A OE1 1 
ATOM   442  N NE2 . GLN   A 1 61  ? 8.875   30.203 22.849  1.00 50.60  ? 717  GLN   A NE2 1 
ATOM   443  N N   . GLN   A 1 62  ? 9.644   26.096 23.422  1.00 32.78  ? 718  GLN   A N   1 
ATOM   444  C CA  . GLN   A 1 62  ? 9.864   25.793 24.831  1.00 33.43  ? 718  GLN   A CA  1 
ATOM   445  C C   . GLN   A 1 62  ? 10.365  24.375 24.999  1.00 39.84  ? 718  GLN   A C   1 
ATOM   446  O O   . GLN   A 1 62  ? 11.298  24.154 25.765  1.00 38.59  ? 718  GLN   A O   1 
ATOM   447  C CB  . GLN   A 1 62  ? 8.591   26.005 25.646  1.00 34.62  ? 718  GLN   A CB  1 
ATOM   448  C CG  . GLN   A 1 62  ? 8.671   27.219 26.550  1.00 58.36  ? 718  GLN   A CG  1 
ATOM   449  C CD  . GLN   A 1 62  ? 8.216   26.902 27.953  1.00 81.34  ? 718  GLN   A CD  1 
ATOM   450  O OE1 . GLN   A 1 62  ? 7.070   26.489 28.191  1.00 71.03  ? 718  GLN   A OE1 1 
ATOM   451  N NE2 . GLN   A 1 62  ? 9.111   27.097 28.918  1.00 79.61  ? 718  GLN   A NE2 1 
ATOM   452  N N   . ALA   A 1 63  ? 9.786   23.433 24.242  1.00 38.88  ? 719  ALA   A N   1 
ATOM   453  C CA  . ALA   A 1 63  ? 10.174  22.031 24.233  1.00 40.53  ? 719  ALA   A CA  1 
ATOM   454  C C   . ALA   A 1 63  ? 11.581  21.833 23.645  1.00 49.12  ? 719  ALA   A C   1 
ATOM   455  O O   . ALA   A 1 63  ? 12.321  21.000 24.156  1.00 49.78  ? 719  ALA   A O   1 
ATOM   456  C CB  . ALA   A 1 63  ? 9.161   21.216 23.452  1.00 41.23  ? 719  ALA   A CB  1 
ATOM   457  N N   . VAL   A 1 64  ? 11.970  22.609 22.610  1.00 48.63  ? 720  VAL   A N   1 
ATOM   458  C CA  . VAL   A 1 64  ? 13.299  22.453 21.999  1.00 49.78  ? 720  VAL   A CA  1 
ATOM   459  C C   . VAL   A 1 64  ? 14.395  23.021 22.914  1.00 54.61  ? 720  VAL   A C   1 
ATOM   460  O O   . VAL   A 1 64  ? 15.396  22.340 23.143  1.00 54.27  ? 720  VAL   A O   1 
ATOM   461  C CB  . VAL   A 1 64  ? 13.426  22.947 20.521  1.00 54.32  ? 720  VAL   A CB  1 
ATOM   462  C CG1 . VAL   A 1 64  ? 12.313  22.381 19.644  1.00 53.86  ? 720  VAL   A CG1 1 
ATOM   463  C CG2 . VAL   A 1 64  ? 13.484  24.468 20.408  1.00 54.57  ? 720  VAL   A CG2 1 
ATOM   464  N N   . SER   A 1 65  ? 14.174  24.233 23.474  1.00 52.08  ? 721  SER   A N   1 
ATOM   465  C CA  . SER   A 1 65  ? 15.120  24.918 24.360  1.00 51.74  ? 721  SER   A CA  1 
ATOM   466  C C   . SER   A 1 65  ? 15.342  24.169 25.673  1.00 56.90  ? 721  SER   A C   1 
ATOM   467  O O   . SER   A 1 65  ? 16.461  24.176 26.200  1.00 57.46  ? 721  SER   A O   1 
ATOM   468  C CB  . SER   A 1 65  ? 14.691  26.362 24.605  1.00 54.42  ? 721  SER   A CB  1 
ATOM   469  O OG  . SER   A 1 65  ? 13.695  26.488 25.606  1.00 61.16  ? 721  SER   A OG  1 
ATOM   470  N N   . GLN   A 1 66  ? 14.295  23.481 26.166  1.00 53.27  ? 722  GLN   A N   1 
ATOM   471  C CA  . GLN   A 1 66  ? 14.347  22.694 27.399  1.00 53.22  ? 722  GLN   A CA  1 
ATOM   472  C C   . GLN   A 1 66  ? 14.812  21.249 27.151  1.00 58.08  ? 722  GLN   A C   1 
ATOM   473  O O   . GLN   A 1 66  ? 14.837  20.425 28.077  1.00 57.04  ? 722  GLN   A O   1 
ATOM   474  C CB  . GLN   A 1 66  ? 13.012  22.766 28.149  1.00 54.41  ? 722  GLN   A CB  1 
ATOM   475  C CG  . GLN   A 1 66  ? 12.677  24.191 28.586  1.00 71.21  ? 722  GLN   A CG  1 
ATOM   476  C CD  . GLN   A 1 66  ? 12.739  24.383 30.070  1.00 92.70  ? 722  GLN   A CD  1 
ATOM   477  O OE1 . GLN   A 1 66  ? 11.960  23.793 30.818  1.00 91.41  ? 722  GLN   A OE1 1 
ATOM   478  N NE2 . GLN   A 1 66  ? 13.652  25.229 30.524  1.00 81.61  ? 722  GLN   A NE2 1 
ATOM   479  N N   . GLY   A 1 67  ? 15.213  20.986 25.907  1.00 55.24  ? 723  GLY   A N   1 
ATOM   480  C CA  . GLY   A 1 67  ? 15.748  19.710 25.458  1.00 55.45  ? 723  GLY   A CA  1 
ATOM   481  C C   . GLY   A 1 67  ? 14.840  18.513 25.630  1.00 59.83  ? 723  GLY   A C   1 
ATOM   482  O O   . GLY   A 1 67  ? 15.198  17.565 26.335  1.00 60.68  ? 723  GLY   A O   1 
ATOM   483  N N   . SER   A 1 68  ? 13.666  18.541 24.985  1.00 55.29  ? 724  SER   A N   1 
ATOM   484  C CA  . SER   A 1 68  ? 12.748  17.404 25.008  1.00 55.08  ? 724  SER   A CA  1 
ATOM   485  C C   . SER   A 1 68  ? 13.176  16.443 23.889  1.00 59.27  ? 724  SER   A C   1 
ATOM   486  O O   . SER   A 1 68  ? 13.882  16.859 22.968  1.00 58.59  ? 724  SER   A O   1 
ATOM   487  C CB  . SER   A 1 68  ? 11.303  17.862 24.809  1.00 58.43  ? 724  SER   A CB  1 
ATOM   488  O OG  . SER   A 1 68  ? 10.828  18.594 25.927  1.00 65.21  ? 724  SER   A OG  1 
ATOM   489  N N   . SER   A 1 69  ? 12.782  15.164 23.980  1.00 56.72  ? 725  SER   A N   1 
ATOM   490  C CA  . SER   A 1 69  ? 13.107  14.156 22.964  1.00 56.89  ? 725  SER   A CA  1 
ATOM   491  C C   . SER   A 1 69  ? 12.210  14.346 21.727  1.00 61.54  ? 725  SER   A C   1 
ATOM   492  O O   . SER   A 1 69  ? 11.129  14.920 21.850  1.00 60.87  ? 725  SER   A O   1 
ATOM   493  C CB  . SER   A 1 69  ? 12.914  12.750 23.531  1.00 60.35  ? 725  SER   A CB  1 
ATOM   494  O OG  . SER   A 1 69  ? 11.549  12.459 23.793  1.00 67.92  ? 725  SER   A OG  1 
ATOM   495  N N   . ASP   A 1 70  ? 12.639  13.829 20.553  1.00 58.10  ? 726  ASP   A N   1 
ATOM   496  C CA  . ASP   A 1 70  ? 11.890  13.872 19.287  1.00 57.40  ? 726  ASP   A CA  1 
ATOM   497  C C   . ASP   A 1 70  ? 10.538  13.151 19.387  1.00 59.20  ? 726  ASP   A C   1 
ATOM   498  O O   . ASP   A 1 70  ? 9.604   13.483 18.653  1.00 57.66  ? 726  ASP   A O   1 
ATOM   499  C CB  . ASP   A 1 70  ? 12.736  13.287 18.144  1.00 59.77  ? 726  ASP   A CB  1 
ATOM   500  C CG  . ASP   A 1 70  ? 13.975  14.101 17.775  1.00 73.48  ? 726  ASP   A CG  1 
ATOM   501  O OD1 . ASP   A 1 70  ? 14.357  15.010 18.564  1.00 74.34  ? 726  ASP   A OD1 1 
ATOM   502  O OD2 . ASP   A 1 70  ? 14.566  13.830 16.700  1.00 78.53  ? 726  ASP   A OD2 1 
ATOM   503  N N   . SER   A 1 71  ? 10.438  12.175 20.310  1.00 55.94  ? 727  SER   A N   1 
ATOM   504  C CA  . SER   A 1 71  ? 9.203   11.435 20.596  1.00 55.41  ? 727  SER   A CA  1 
ATOM   505  C C   . SER   A 1 71  ? 8.244   12.331 21.400  1.00 56.41  ? 727  SER   A C   1 
ATOM   506  O O   . SER   A 1 71  ? 7.035   12.323 21.147  1.00 55.87  ? 727  SER   A O   1 
ATOM   507  C CB  . SER   A 1 71  ? 9.511   10.152 21.362  1.00 59.95  ? 727  SER   A CB  1 
ATOM   508  O OG  . SER   A 1 71  ? 10.532  10.359 22.326  1.00 70.26  ? 727  SER   A OG  1 
ATOM   509  N N   . GLN   A 1 72  ? 8.806   13.133 22.341  1.00 50.33  ? 728  GLN   A N   1 
ATOM   510  C CA  . GLN   A 1 72  ? 8.081   14.081 23.190  1.00 48.63  ? 728  GLN   A CA  1 
ATOM   511  C C   . GLN   A 1 72  ? 7.568   15.310 22.410  1.00 48.29  ? 728  GLN   A C   1 
ATOM   512  O O   . GLN   A 1 72  ? 6.413   15.695 22.597  1.00 47.62  ? 728  GLN   A O   1 
ATOM   513  C CB  . GLN   A 1 72  ? 8.950   14.505 24.389  1.00 49.95  ? 728  GLN   A CB  1 
ATOM   514  N N   . ILE   A 1 73  ? 8.412   15.910 21.542  1.00 42.83  ? 729  ILE   A N   1 
ATOM   515  C CA  . ILE   A 1 73  ? 8.055   17.089 20.738  1.00 42.99  ? 729  ILE   A CA  1 
ATOM   516  C C   . ILE   A 1 73  ? 7.098   16.743 19.602  1.00 45.37  ? 729  ILE   A C   1 
ATOM   517  O O   . ILE   A 1 73  ? 6.365   17.630 19.169  1.00 45.10  ? 729  ILE   A O   1 
ATOM   518  C CB  . ILE   A 1 73  ? 9.250   17.956 20.203  1.00 46.91  ? 729  ILE   A CB  1 
ATOM   519  C CG1 . ILE   A 1 73  ? 10.541  17.819 21.052  1.00 48.39  ? 729  ILE   A CG1 1 
ATOM   520  C CG2 . ILE   A 1 73  ? 8.834   19.439 20.070  1.00 46.75  ? 729  ILE   A CG2 1 
ATOM   521  C CD1 . ILE   A 1 73  ? 11.881  18.054 20.279  1.00 58.56  ? 729  ILE   A CD1 1 
ATOM   522  N N   . LEU   A 1 74  ? 7.095   15.474 19.119  1.00 41.40  ? 730  LEU   A N   1 
ATOM   523  C CA  . LEU   A 1 74  ? 6.251   15.007 18.009  1.00 40.94  ? 730  LEU   A CA  1 
ATOM   524  C C   . LEU   A 1 74  ? 4.829   15.543 18.086  1.00 44.57  ? 730  LEU   A C   1 
ATOM   525  O O   . LEU   A 1 74  ? 4.318   16.086 17.101  1.00 44.53  ? 730  LEU   A O   1 
ATOM   526  C CB  . LEU   A 1 74  ? 6.276   13.467 17.866  1.00 40.70  ? 730  LEU   A CB  1 
ATOM   527  C CG  . LEU   A 1 74  ? 5.299   12.808 16.888  1.00 43.87  ? 730  LEU   A CG  1 
ATOM   528  C CD1 . LEU   A 1 74  ? 5.567   13.237 15.442  1.00 43.72  ? 730  LEU   A CD1 1 
ATOM   529  C CD2 . LEU   A 1 74  ? 5.313   11.306 17.026  1.00 42.33  ? 730  LEU   A CD2 1 
ATOM   530  N N   . ASP   A 1 75  ? 4.233   15.444 19.279  1.00 41.58  ? 731  ASP   A N   1 
ATOM   531  C CA  . ASP   A 1 75  ? 2.894   15.902 19.606  1.00 41.57  ? 731  ASP   A CA  1 
ATOM   532  C C   . ASP   A 1 75  ? 2.696   17.393 19.332  1.00 41.60  ? 731  ASP   A C   1 
ATOM   533  O O   . ASP   A 1 75  ? 1.691   17.747 18.717  1.00 42.69  ? 731  ASP   A O   1 
ATOM   534  C CB  . ASP   A 1 75  ? 2.547   15.538 21.055  1.00 44.61  ? 731  ASP   A CB  1 
ATOM   535  C CG  . ASP   A 1 75  ? 2.615   14.042 21.301  1.00 60.46  ? 731  ASP   A CG  1 
ATOM   536  O OD1 . ASP   A 1 75  ? 1.592   13.354 21.061  1.00 60.80  ? 731  ASP   A OD1 1 
ATOM   537  O OD2 . ASP   A 1 75  ? 3.702   13.555 21.711  1.00 67.35  ? 731  ASP   A OD2 1 
ATOM   538  N N   . LEU   A 1 76  ? 3.661   18.242 19.735  1.00 33.99  ? 732  LEU   A N   1 
ATOM   539  C CA  . LEU   A 1 76  ? 3.625   19.699 19.538  1.00 32.29  ? 732  LEU   A CA  1 
ATOM   540  C C   . LEU   A 1 76  ? 3.856   20.112 18.086  1.00 35.79  ? 732  LEU   A C   1 
ATOM   541  O O   . LEU   A 1 76  ? 3.322   21.139 17.648  1.00 35.00  ? 732  LEU   A O   1 
ATOM   542  C CB  . LEU   A 1 76  ? 4.650   20.420 20.421  1.00 31.63  ? 732  LEU   A CB  1 
ATOM   543  C CG  . LEU   A 1 76  ? 4.719   20.128 21.917  1.00 35.42  ? 732  LEU   A CG  1 
ATOM   544  C CD1 . LEU   A 1 76  ? 5.641   21.099 22.574  1.00 34.66  ? 732  LEU   A CD1 1 
ATOM   545  C CD2 . LEU   A 1 76  ? 3.367   20.224 22.586  1.00 37.67  ? 732  LEU   A CD2 1 
ATOM   546  N N   . SER   A 1 77  ? 4.698   19.349 17.355  1.00 31.83  ? 733  SER   A N   1 
ATOM   547  C CA  . SER   A 1 77  ? 4.979   19.601 15.941  1.00 31.17  ? 733  SER   A CA  1 
ATOM   548  C C   . SER   A 1 77  ? 3.728   19.344 15.109  1.00 33.84  ? 733  SER   A C   1 
ATOM   549  O O   . SER   A 1 77  ? 3.444   20.127 14.201  1.00 32.78  ? 733  SER   A O   1 
ATOM   550  C CB  . SER   A 1 77  ? 6.126   18.724 15.442  1.00 32.79  ? 733  SER   A CB  1 
ATOM   551  O OG  . SER   A 1 77  ? 6.442   19.001 14.086  1.00 33.87  ? 733  SER   A OG  1 
ATOM   552  N N   . ASN   A 1 78  ? 2.981   18.255 15.431  1.00 30.27  ? 734  ASN   A N   1 
ATOM   553  C CA  . ASN   A 1 78  ? 1.758   17.861 14.712  1.00 30.23  ? 734  ASN   A CA  1 
ATOM   554  C C   . ASN   A 1 78  ? 0.639   18.873 14.922  1.00 33.52  ? 734  ASN   A C   1 
ATOM   555  O O   . ASN   A 1 78  ? -0.148  19.098 14.001  1.00 31.84  ? 734  ASN   A O   1 
ATOM   556  C CB  . ASN   A 1 78  ? 1.273   16.469 15.135  1.00 32.76  ? 734  ASN   A CB  1 
ATOM   557  C CG  . ASN   A 1 78  ? 2.116   15.289 14.702  1.00 58.04  ? 734  ASN   A CG  1 
ATOM   558  O OD1 . ASN   A 1 78  ? 2.879   15.348 13.736  1.00 51.91  ? 734  ASN   A OD1 1 
ATOM   559  N ND2 . ASN   A 1 78  ? 1.967   14.166 15.406  1.00 50.62  ? 734  ASN   A ND2 1 
ATOM   560  N N   . ARG   A 1 79  ? 0.589   19.492 16.134  1.00 30.42  ? 735  ARG   A N   1 
ATOM   561  C CA  . ARG   A 1 79  ? -0.402  20.489 16.557  1.00 29.79  ? 735  ARG   A CA  1 
ATOM   562  C C   . ARG   A 1 79  ? -0.365  21.733 15.685  1.00 31.97  ? 735  ARG   A C   1 
ATOM   563  O O   . ARG   A 1 79  ? -1.399  22.374 15.508  1.00 32.44  ? 735  ARG   A O   1 
ATOM   564  C CB  . ARG   A 1 79  ? -0.194  20.867 18.036  1.00 31.74  ? 735  ARG   A CB  1 
ATOM   565  C CG  . ARG   A 1 79  ? -1.256  20.304 18.972  1.00 41.99  ? 735  ARG   A CG  1 
ATOM   566  C CD  . ARG   A 1 79  ? -0.672  19.416 20.072  1.00 50.39  ? 735  ARG   A CD  1 
ATOM   567  N NE  . ARG   A 1 79  ? -0.379  20.173 21.290  1.00 48.88  ? 735  ARG   A NE  1 
ATOM   568  C CZ  . ARG   A 1 79  ? -0.178  19.639 22.491  1.00 55.49  ? 735  ARG   A CZ  1 
ATOM   569  N NH1 . ARG   A 1 79  ? 0.056   20.417 23.538  1.00 44.48  ? 735  ARG   A NH1 1 
ATOM   570  N NH2 . ARG   A 1 79  ? -0.221  18.324 22.658  1.00 38.28  ? 735  ARG   A NH2 1 
ATOM   571  N N   . PHE   A 1 80  ? 0.829   22.079 15.162  1.00 27.49  ? 736  PHE   A N   1 
ATOM   572  C CA  . PHE   A 1 80  ? 1.047   23.228 14.286  1.00 26.52  ? 736  PHE   A CA  1 
ATOM   573  C C   . PHE   A 1 80  ? 0.468   22.920 12.918  1.00 29.05  ? 736  PHE   A C   1 
ATOM   574  O O   . PHE   A 1 80  ? -0.247  23.756 12.361  1.00 27.63  ? 736  PHE   A O   1 
ATOM   575  C CB  . PHE   A 1 80  ? 2.563   23.562 14.165  1.00 28.03  ? 736  PHE   A CB  1 
ATOM   576  C CG  . PHE   A 1 80  ? 2.856   24.663 13.169  1.00 29.54  ? 736  PHE   A CG  1 
ATOM   577  C CD1 . PHE   A 1 80  ? 2.840   26.001 13.558  1.00 31.88  ? 736  PHE   A CD1 1 
ATOM   578  C CD2 . PHE   A 1 80  ? 3.086   24.370 11.828  1.00 30.97  ? 736  PHE   A CD2 1 
ATOM   579  C CE1 . PHE   A 1 80  ? 3.069   27.021 12.626  1.00 31.36  ? 736  PHE   A CE1 1 
ATOM   580  C CE2 . PHE   A 1 80  ? 3.291   25.394 10.896  1.00 32.21  ? 736  PHE   A CE2 1 
ATOM   581  C CZ  . PHE   A 1 80  ? 3.303   26.706 11.308  1.00 29.53  ? 736  PHE   A CZ  1 
ATOM   582  N N   . TYR   A 1 81  ? 0.801   21.720 12.375  1.00 25.68  ? 737  TYR   A N   1 
ATOM   583  C CA  . TYR   A 1 81  ? 0.366   21.220 11.075  1.00 25.87  ? 737  TYR   A CA  1 
ATOM   584  C C   . TYR   A 1 81  ? -1.142  21.026 11.014  1.00 34.12  ? 737  TYR   A C   1 
ATOM   585  O O   . TYR   A 1 81  ? -1.722  20.936 9.915   1.00 35.79  ? 737  TYR   A O   1 
ATOM   586  C CB  . TYR   A 1 81  ? 1.104   19.917 10.720  1.00 26.66  ? 737  TYR   A CB  1 
ATOM   587  C CG  . TYR   A 1 81  ? 2.574   20.095 10.397  1.00 27.44  ? 737  TYR   A CG  1 
ATOM   588  C CD1 . TYR   A 1 81  ? 2.984   20.868 9.312   1.00 29.01  ? 737  TYR   A CD1 1 
ATOM   589  C CD2 . TYR   A 1 81  ? 3.557   19.458 11.153  1.00 27.70  ? 737  TYR   A CD2 1 
ATOM   590  C CE1 . TYR   A 1 81  ? 4.337   21.038 9.016   1.00 29.02  ? 737  TYR   A CE1 1 
ATOM   591  C CE2 . TYR   A 1 81  ? 4.911   19.611 10.858  1.00 27.63  ? 737  TYR   A CE2 1 
ATOM   592  C CZ  . TYR   A 1 81  ? 5.295   20.395 9.785   1.00 32.71  ? 737  TYR   A CZ  1 
ATOM   593  O OH  . TYR   A 1 81  ? 6.629   20.539 9.493   1.00 33.23  ? 737  TYR   A OH  1 
ATOM   594  N N   . THR   A 1 82  ? -1.774  20.986 12.202  1.00 30.81  ? 738  THR   A N   1 
ATOM   595  C CA  . THR   A 1 82  ? -3.217  20.871 12.401  1.00 31.12  ? 738  THR   A CA  1 
ATOM   596  C C   . THR   A 1 82  ? -3.861  22.260 12.216  1.00 34.95  ? 738  THR   A C   1 
ATOM   597  O O   . THR   A 1 82  ? -4.980  22.360 11.715  1.00 34.98  ? 738  THR   A O   1 
ATOM   598  C CB  . THR   A 1 82  ? -3.489  20.258 13.799  1.00 38.52  ? 738  THR   A CB  1 
ATOM   599  O OG1 . THR   A 1 82  ? -2.866  18.972 13.863  1.00 38.48  ? 738  THR   A OG1 1 
ATOM   600  C CG2 . THR   A 1 82  ? -4.982  20.128 14.127  1.00 36.41  ? 738  THR   A CG2 1 
ATOM   601  N N   . LEU   A 1 83  ? -3.149  23.323 12.634  1.00 30.24  ? 739  LEU   A N   1 
ATOM   602  C CA  . LEU   A 1 83  ? -3.635  24.705 12.562  1.00 28.21  ? 739  LEU   A CA  1 
ATOM   603  C C   . LEU   A 1 83  ? -3.293  25.330 11.215  1.00 26.52  ? 739  LEU   A C   1 
ATOM   604  O O   . LEU   A 1 83  ? -4.072  26.119 10.684  1.00 22.95  ? 739  LEU   A O   1 
ATOM   605  C CB  . LEU   A 1 83  ? -3.068  25.536 13.729  1.00 27.80  ? 739  LEU   A CB  1 
ATOM   606  C CG  . LEU   A 1 83  ? -3.454  25.068 15.122  1.00 31.91  ? 739  LEU   A CG  1 
ATOM   607  C CD1 . LEU   A 1 83  ? -2.481  25.575 16.126  1.00 32.17  ? 739  LEU   A CD1 1 
ATOM   608  C CD2 . LEU   A 1 83  ? -4.861  25.499 15.483  1.00 32.85  ? 739  LEU   A CD2 1 
ATOM   609  N N   . ILE   A 1 84  ? -2.137  24.967 10.666  1.00 23.58  ? 740  ILE   A N   1 
ATOM   610  C CA  . ILE   A 1 84  ? -1.722  25.428 9.347   1.00 24.67  ? 740  ILE   A CA  1 
ATOM   611  C C   . ILE   A 1 84  ? -1.503  24.188 8.471   1.00 29.49  ? 740  ILE   A C   1 
ATOM   612  O O   . ILE   A 1 84  ? -0.416  23.634 8.493   1.00 28.45  ? 740  ILE   A O   1 
ATOM   613  C CB  . ILE   A 1 84  ? -0.527  26.453 9.335   1.00 27.78  ? 740  ILE   A CB  1 
ATOM   614  C CG1 . ILE   A 1 84  ? -0.732  27.637 10.313  1.00 27.86  ? 740  ILE   A CG1 1 
ATOM   615  C CG2 . ILE   A 1 84  ? -0.246  26.973 7.918   1.00 29.50  ? 740  ILE   A CG2 1 
ATOM   616  C CD1 . ILE   A 1 84  ? -1.914  28.712 10.000  1.00 33.77  ? 740  ILE   A CD1 1 
ATOM   617  N N   . PRO   A 1 85  ? -2.548  23.711 7.744   1.00 28.00  ? 741  PRO   A N   1 
ATOM   618  C CA  . PRO   A 1 85  ? -2.379  22.499 6.891   1.00 28.27  ? 741  PRO   A CA  1 
ATOM   619  C C   . PRO   A 1 85  ? -1.335  22.594 5.778   1.00 32.32  ? 741  PRO   A C   1 
ATOM   620  O O   . PRO   A 1 85  ? -1.310  23.561 5.019   1.00 31.69  ? 741  PRO   A O   1 
ATOM   621  C CB  . PRO   A 1 85  ? -3.782  22.249 6.308   1.00 29.68  ? 741  PRO   A CB  1 
ATOM   622  C CG  . PRO   A 1 85  ? -4.709  23.118 7.100   1.00 33.85  ? 741  PRO   A CG  1 
ATOM   623  C CD  . PRO   A 1 85  ? -3.925  24.251 7.664   1.00 28.95  ? 741  PRO   A CD  1 
ATOM   624  N N   . HIS   A 1 86  ? -0.474  21.575 5.687   1.00 29.53  ? 742  HIS   A N   1 
ATOM   625  C CA  . HIS   A 1 86  ? 0.585   21.501 4.688   1.00 29.00  ? 742  HIS   A CA  1 
ATOM   626  C C   . HIS   A 1 86  ? 0.320   20.379 3.644   1.00 32.97  ? 742  HIS   A C   1 
ATOM   627  O O   . HIS   A 1 86  ? -0.508  19.497 3.868   1.00 29.00  ? 742  HIS   A O   1 
ATOM   628  C CB  . HIS   A 1 86  ? 1.973   21.399 5.355   1.00 29.39  ? 742  HIS   A CB  1 
ATOM   629  C CG  . HIS   A 1 86  ? 2.470   22.687 5.964   1.00 32.35  ? 742  HIS   A CG  1 
ATOM   630  N ND1 . HIS   A 1 86  ? 1.833   23.271 7.048   1.00 33.83  ? 742  HIS   A ND1 1 
ATOM   631  C CD2 . HIS   A 1 86  ? 3.556   23.431 5.657   1.00 33.38  ? 742  HIS   A CD2 1 
ATOM   632  C CE1 . HIS   A 1 86  ? 2.522   24.366 7.338   1.00 32.49  ? 742  HIS   A CE1 1 
ATOM   633  N NE2 . HIS   A 1 86  ? 3.558   24.514 6.525   1.00 32.94  ? 742  HIS   A NE2 1 
ATOM   634  N N   . ASP   A 1 87  ? 0.976   20.468 2.477   1.00 34.32  ? 743  ASP   A N   1 
ATOM   635  C CA  . ASP   A 1 87  ? 0.779   19.541 1.365   1.00 35.61  ? 743  ASP   A CA  1 
ATOM   636  C C   . ASP   A 1 87  ? 1.853   18.500 1.317   1.00 41.95  ? 743  ASP   A C   1 
ATOM   637  O O   . ASP   A 1 87  ? 2.920   18.718 0.730   1.00 43.01  ? 743  ASP   A O   1 
ATOM   638  C CB  . ASP   A 1 87  ? 0.678   20.284 0.021   1.00 38.13  ? 743  ASP   A CB  1 
ATOM   639  C CG  . ASP   A 1 87  ? -0.013  19.516 -1.095  1.00 52.96  ? 743  ASP   A CG  1 
ATOM   640  O OD1 . ASP   A 1 87  ? -0.771  18.556 -0.786  1.00 52.48  ? 743  ASP   A OD1 1 
ATOM   641  O OD2 . ASP   A 1 87  ? 0.184   19.885 -2.276  1.00 62.53  ? 743  ASP   A OD2 1 
ATOM   642  N N   . PHE   A 1 88  ? 1.574   17.359 1.963   1.00 38.64  ? 744  PHE   A N   1 
ATOM   643  C CA  . PHE   A 1 88  ? 2.477   16.216 2.008   1.00 37.94  ? 744  PHE   A CA  1 
ATOM   644  C C   . PHE   A 1 88  ? 1.776   14.928 1.612   1.00 40.42  ? 744  PHE   A C   1 
ATOM   645  O O   . PHE   A 1 88  ? 2.419   13.888 1.506   1.00 42.09  ? 744  PHE   A O   1 
ATOM   646  C CB  . PHE   A 1 88  ? 3.159   16.119 3.381   1.00 39.56  ? 744  PHE   A CB  1 
ATOM   647  C CG  . PHE   A 1 88  ? 4.117   17.256 3.644   1.00 40.89  ? 744  PHE   A CG  1 
ATOM   648  C CD1 . PHE   A 1 88  ? 5.333   17.338 2.964   1.00 44.15  ? 744  PHE   A CD1 1 
ATOM   649  C CD2 . PHE   A 1 88  ? 3.809   18.249 4.568   1.00 43.03  ? 744  PHE   A CD2 1 
ATOM   650  C CE1 . PHE   A 1 88  ? 6.224   18.396 3.205   1.00 44.31  ? 744  PHE   A CE1 1 
ATOM   651  C CE2 . PHE   A 1 88  ? 4.710   19.295 4.822   1.00 45.92  ? 744  PHE   A CE2 1 
ATOM   652  C CZ  . PHE   A 1 88  ? 5.904   19.367 4.127   1.00 43.66  ? 744  PHE   A CZ  1 
ATOM   653  N N   . GLY   A 1 89  ? 0.480   15.028 1.332   1.00 34.86  ? 745  GLY   A N   1 
ATOM   654  C CA  . GLY   A 1 89  ? -0.372  13.908 0.962   1.00 33.23  ? 745  GLY   A CA  1 
ATOM   655  C C   . GLY   A 1 89  ? -0.577  13.012 2.157   1.00 37.83  ? 745  GLY   A C   1 
ATOM   656  O O   . GLY   A 1 89  ? -0.916  13.488 3.244   1.00 36.78  ? 745  GLY   A O   1 
ATOM   657  N N   . MET   A 1 90  ? -0.296  11.710 1.969   1.00 36.83  ? 746  MET   A N   1 
ATOM   658  C CA  . MET   A 1 90  ? -0.412  10.666 2.993   1.00 37.54  ? 746  MET   A CA  1 
ATOM   659  C C   . MET   A 1 90  ? 0.895   10.397 3.734   1.00 40.39  ? 746  MET   A C   1 
ATOM   660  O O   . MET   A 1 90  ? 0.972   9.441  4.509   1.00 38.96  ? 746  MET   A O   1 
ATOM   661  C CB  . MET   A 1 90  ? -0.971  9.372  2.392   1.00 40.39  ? 746  MET   A CB  1 
ATOM   662  C CG  . MET   A 1 90  ? -2.341  9.550  1.790   1.00 45.39  ? 746  MET   A CG  1 
ATOM   663  S SD  . MET   A 1 90  ? -3.588  10.192 2.947   1.00 50.54  ? 746  MET   A SD  1 
ATOM   664  C CE  . MET   A 1 90  ? -4.001  11.793 2.125   1.00 47.30  ? 746  MET   A CE  1 
ATOM   665  N N   . LYS   A 1 91  ? 1.913   11.245 3.499   1.00 36.96  ? 747  LYS   A N   1 
ATOM   666  C CA  . LYS   A 1 91  ? 3.233   11.163 4.136   1.00 37.32  ? 747  LYS   A CA  1 
ATOM   667  C C   . LYS   A 1 91  ? 3.207   11.935 5.446   1.00 40.53  ? 747  LYS   A C   1 
ATOM   668  O O   . LYS   A 1 91  ? 2.504   12.946 5.545   1.00 40.02  ? 747  LYS   A O   1 
ATOM   669  C CB  . LYS   A 1 91  ? 4.336   11.783 3.237   1.00 40.27  ? 747  LYS   A CB  1 
ATOM   670  C CG  . LYS   A 1 91  ? 4.440   11.212 1.822   1.00 56.11  ? 747  LYS   A CG  1 
ATOM   671  C CD  . LYS   A 1 91  ? 5.336   12.061 0.910   1.00 66.49  ? 747  LYS   A CD  1 
ATOM   672  C CE  . LYS   A 1 91  ? 6.699   11.441 0.729   1.00 76.16  ? 747  LYS   A CE  1 
ATOM   673  N NZ  . LYS   A 1 91  ? 7.578   12.275 -0.134  1.00 81.05  ? 747  LYS   A NZ  1 
ATOM   674  N N   . LYS   A 1 92  ? 4.019   11.492 6.427   1.00 36.40  ? 748  LYS   A N   1 
ATOM   675  C CA  . LYS   A 1 92  ? 4.198   12.167 7.711   1.00 35.76  ? 748  LYS   A CA  1 
ATOM   676  C C   . LYS   A 1 92  ? 4.909   13.522 7.460   1.00 41.23  ? 748  LYS   A C   1 
ATOM   677  O O   . LYS   A 1 92  ? 5.859   13.574 6.669   1.00 40.35  ? 748  LYS   A O   1 
ATOM   678  C CB  . LYS   A 1 92  ? 5.045   11.312 8.670   1.00 36.74  ? 748  LYS   A CB  1 
ATOM   679  C CG  . LYS   A 1 92  ? 4.315   10.124 9.264   1.00 36.78  ? 748  LYS   A CG  1 
ATOM   680  C CD  . LYS   A 1 92  ? 5.176   9.387  10.278  1.00 41.50  ? 748  LYS   A CD  1 
ATOM   681  C CE  . LYS   A 1 92  ? 4.520   8.125  10.786  1.00 47.15  ? 748  LYS   A CE  1 
ATOM   682  N NZ  . LYS   A 1 92  ? 5.506   7.167  11.351  1.00 56.16  ? 748  LYS   A NZ  1 
ATOM   683  N N   . PRO   A 1 93  ? 4.443   14.634 8.081   1.00 40.41  ? 749  PRO   A N   1 
ATOM   684  C CA  . PRO   A 1 93  ? 5.114   15.930 7.860   1.00 40.62  ? 749  PRO   A CA  1 
ATOM   685  C C   . PRO   A 1 93  ? 6.506   15.973 8.509   1.00 43.66  ? 749  PRO   A C   1 
ATOM   686  O O   . PRO   A 1 93  ? 6.748   15.218 9.454   1.00 42.41  ? 749  PRO   A O   1 
ATOM   687  C CB  . PRO   A 1 93  ? 4.164   16.958 8.505   1.00 42.33  ? 749  PRO   A CB  1 
ATOM   688  C CG  . PRO   A 1 93  ? 2.985   16.206 9.002   1.00 47.22  ? 749  PRO   A CG  1 
ATOM   689  C CD  . PRO   A 1 93  ? 3.337   14.756 9.054   1.00 42.66  ? 749  PRO   A CD  1 
ATOM   690  N N   . PRO   A 1 94  ? 7.441   16.837 8.052   1.00 40.99  ? 750  PRO   A N   1 
ATOM   691  C CA  . PRO   A 1 94  ? 8.745   16.903 8.742   1.00 40.83  ? 750  PRO   A CA  1 
ATOM   692  C C   . PRO   A 1 94  ? 8.613   17.409 10.194  1.00 42.97  ? 750  PRO   A C   1 
ATOM   693  O O   . PRO   A 1 94  ? 7.941   18.406 10.444  1.00 42.30  ? 750  PRO   A O   1 
ATOM   694  C CB  . PRO   A 1 94  ? 9.573   17.863 7.877   1.00 42.60  ? 750  PRO   A CB  1 
ATOM   695  C CG  . PRO   A 1 94  ? 8.591   18.624 7.084   1.00 46.72  ? 750  PRO   A CG  1 
ATOM   696  C CD  . PRO   A 1 94  ? 7.365   17.791 6.925   1.00 41.97  ? 750  PRO   A CD  1 
ATOM   697  N N   . LEU   A 1 95  ? 9.257   16.720 11.149  1.00 38.53  ? 751  LEU   A N   1 
ATOM   698  C CA  . LEU   A 1 95  ? 9.249   17.073 12.577  1.00 37.68  ? 751  LEU   A CA  1 
ATOM   699  C C   . LEU   A 1 95  ? 9.906   18.430 12.849  1.00 39.31  ? 751  LEU   A C   1 
ATOM   700  O O   . LEU   A 1 95  ? 11.027  18.667 12.401  1.00 39.05  ? 751  LEU   A O   1 
ATOM   701  C CB  . LEU   A 1 95  ? 10.006  15.993 13.390  1.00 37.57  ? 751  LEU   A CB  1 
ATOM   702  C CG  . LEU   A 1 95  ? 9.412   15.462 14.717  1.00 41.92  ? 751  LEU   A CG  1 
ATOM   703  C CD1 . LEU   A 1 95  ? 10.435  14.626 15.451  1.00 41.99  ? 751  LEU   A CD1 1 
ATOM   704  C CD2 . LEU   A 1 95  ? 8.982   16.564 15.664  1.00 44.08  ? 751  LEU   A CD2 1 
ATOM   705  N N   . LEU   A 1 96  ? 9.222   19.303 13.616  1.00 34.89  ? 752  LEU   A N   1 
ATOM   706  C CA  . LEU   A 1 96  ? 9.781   20.594 14.031  1.00 34.56  ? 752  LEU   A CA  1 
ATOM   707  C C   . LEU   A 1 96  ? 10.414  20.369 15.425  1.00 39.95  ? 752  LEU   A C   1 
ATOM   708  O O   . LEU   A 1 96  ? 9.730   20.430 16.455  1.00 39.95  ? 752  LEU   A O   1 
ATOM   709  C CB  . LEU   A 1 96  ? 8.726   21.731 14.051  1.00 34.40  ? 752  LEU   A CB  1 
ATOM   710  C CG  . LEU   A 1 96  ? 7.771   21.890 12.841  1.00 38.95  ? 752  LEU   A CG  1 
ATOM   711  C CD1 . LEU   A 1 96  ? 6.575   22.743 13.202  1.00 37.74  ? 752  LEU   A CD1 1 
ATOM   712  C CD2 . LEU   A 1 96  ? 8.482   22.505 11.633  1.00 42.88  ? 752  LEU   A CD2 1 
ATOM   713  N N   . ASN   A 1 97  ? 11.713  20.027 15.439  1.00 37.73  ? 753  ASN   A N   1 
ATOM   714  C CA  . ASN   A 1 97  ? 12.479  19.742 16.660  1.00 37.80  ? 753  ASN   A CA  1 
ATOM   715  C C   . ASN   A 1 97  ? 13.680  20.692 16.861  1.00 41.51  ? 753  ASN   A C   1 
ATOM   716  O O   . ASN   A 1 97  ? 14.477  20.488 17.781  1.00 43.41  ? 753  ASN   A O   1 
ATOM   717  C CB  . ASN   A 1 97  ? 12.947  18.275 16.631  1.00 39.33  ? 753  ASN   A CB  1 
ATOM   718  C CG  . ASN   A 1 97  ? 13.934  17.960 15.520  1.00 56.09  ? 753  ASN   A CG  1 
ATOM   719  O OD1 . ASN   A 1 97  ? 13.845  18.465 14.389  1.00 51.34  ? 753  ASN   A OD1 1 
ATOM   720  N ND2 . ASN   A 1 97  ? 14.903  17.124 15.828  1.00 43.48  ? 753  ASN   A ND2 1 
ATOM   721  N N   . ASN   A 1 98  ? 13.800  21.735 16.026  1.00 35.83  ? 754  ASN   A N   1 
ATOM   722  C CA  . ASN   A 1 98  ? 14.929  22.676 16.088  1.00 34.81  ? 754  ASN   A CA  1 
ATOM   723  C C   . ASN   A 1 98  ? 14.494  24.145 15.965  1.00 38.28  ? 754  ASN   A C   1 
ATOM   724  O O   . ASN   A 1 98  ? 13.346  24.426 15.590  1.00 37.17  ? 754  ASN   A O   1 
ATOM   725  C CB  . ASN   A 1 98  ? 16.000  22.312 15.042  1.00 33.16  ? 754  ASN   A CB  1 
ATOM   726  C CG  . ASN   A 1 98  ? 15.496  22.234 13.619  1.00 63.06  ? 754  ASN   A CG  1 
ATOM   727  O OD1 . ASN   A 1 98  ? 15.638  23.166 12.827  1.00 54.46  ? 754  ASN   A OD1 1 
ATOM   728  N ND2 . ASN   A 1 98  ? 14.890  21.116 13.254  1.00 62.02  ? 754  ASN   A ND2 1 
ATOM   729  N N   . ALA   A 1 99  ? 15.405  25.072 16.313  1.00 33.80  ? 755  ALA   A N   1 
ATOM   730  C CA  . ALA   A 1 99  ? 15.165  26.512 16.265  1.00 33.18  ? 755  ALA   A CA  1 
ATOM   731  C C   . ALA   A 1 99  ? 15.041  27.026 14.842  1.00 35.19  ? 755  ALA   A C   1 
ATOM   732  O O   . ALA   A 1 99  ? 14.288  27.967 14.606  1.00 33.93  ? 755  ALA   A O   1 
ATOM   733  C CB  . ALA   A 1 99  ? 16.272  27.254 16.998  1.00 34.19  ? 755  ALA   A CB  1 
ATOM   734  N N   . ASP   A 1 100 ? 15.780  26.423 13.888  1.00 32.52  ? 756  ASP   A N   1 
ATOM   735  C CA  . ASP   A 1 100 ? 15.741  26.818 12.469  1.00 31.60  ? 756  ASP   A CA  1 
ATOM   736  C C   . ASP   A 1 100 ? 14.358  26.602 11.885  1.00 33.47  ? 756  ASP   A C   1 
ATOM   737  O O   . ASP   A 1 100 ? 13.867  27.431 11.126  1.00 31.20  ? 756  ASP   A O   1 
ATOM   738  C CB  . ASP   A 1 100 ? 16.808  26.064 11.649  1.00 33.33  ? 756  ASP   A CB  1 
ATOM   739  C CG  . ASP   A 1 100 ? 18.233  26.558 11.863  1.00 46.05  ? 756  ASP   A CG  1 
ATOM   740  O OD1 . ASP   A 1 100 ? 18.443  27.790 11.866  1.00 50.34  ? 756  ASP   A OD1 1 
ATOM   741  O OD2 . ASP   A 1 100 ? 19.140  25.712 12.009  1.00 48.82  ? 756  ASP   A OD2 1 
ATOM   742  N N   . SER   A 1 101 ? 13.716  25.505 12.305  1.00 32.86  ? 757  SER   A N   1 
ATOM   743  C CA  . SER   A 1 101 ? 12.379  25.064 11.909  1.00 33.45  ? 757  SER   A CA  1 
ATOM   744  C C   . SER   A 1 101 ? 11.312  26.009 12.449  1.00 38.73  ? 757  SER   A C   1 
ATOM   745  O O   . SER   A 1 101 ? 10.371  26.353 11.733  1.00 38.97  ? 757  SER   A O   1 
ATOM   746  C CB  . SER   A 1 101 ? 12.135  23.641 12.405  1.00 36.30  ? 757  SER   A CB  1 
ATOM   747  O OG  . SER   A 1 101 ? 13.107  22.764 11.861  1.00 41.50  ? 757  SER   A OG  1 
ATOM   748  N N   . VAL   A 1 102 ? 11.474  26.443 13.702  1.00 35.00  ? 758  VAL   A N   1 
ATOM   749  C CA  . VAL   A 1 102 ? 10.544  27.359 14.363  1.00 33.97  ? 758  VAL   A CA  1 
ATOM   750  C C   . VAL   A 1 102 ? 10.702  28.753 13.728  1.00 33.89  ? 758  VAL   A C   1 
ATOM   751  O O   . VAL   A 1 102 ? 9.699   29.417 13.485  1.00 31.47  ? 758  VAL   A O   1 
ATOM   752  C CB  . VAL   A 1 102 ? 10.726  27.316 15.921  1.00 37.54  ? 758  VAL   A CB  1 
ATOM   753  C CG1 . VAL   A 1 102 ? 10.097  28.528 16.618  1.00 36.90  ? 758  VAL   A CG1 1 
ATOM   754  C CG2 . VAL   A 1 102 ? 10.149  26.023 16.495  1.00 37.28  ? 758  VAL   A CG2 1 
ATOM   755  N N   . GLN   A 1 103 ? 11.955  29.159 13.418  1.00 29.57  ? 759  GLN   A N   1 
ATOM   756  C CA  . GLN   A 1 103 ? 12.297  30.439 12.773  1.00 29.08  ? 759  GLN   A CA  1 
ATOM   757  C C   . GLN   A 1 103 ? 11.602  30.496 11.415  1.00 32.18  ? 759  GLN   A C   1 
ATOM   758  O O   . GLN   A 1 103 ? 10.854  31.437 11.153  1.00 32.49  ? 759  GLN   A O   1 
ATOM   759  C CB  . GLN   A 1 103 ? 13.822  30.570 12.592  1.00 30.35  ? 759  GLN   A CB  1 
ATOM   760  C CG  . GLN   A 1 103 ? 14.303  31.950 12.167  1.00 41.93  ? 759  GLN   A CG  1 
ATOM   761  C CD  . GLN   A 1 103 ? 15.696  31.985 11.568  1.00 55.79  ? 759  GLN   A CD  1 
ATOM   762  O OE1 . GLN   A 1 103 ? 16.538  31.101 11.782  1.00 51.27  ? 759  GLN   A OE1 1 
ATOM   763  N NE2 . GLN   A 1 103 ? 15.976  33.032 10.806  1.00 42.23  ? 759  GLN   A NE2 1 
ATOM   764  N N   . ALA   A 1 104 ? 11.817  29.453 10.578  1.00 27.62  ? 760  ALA   A N   1 
ATOM   765  C CA  . ALA   A 1 104 ? 11.214  29.321 9.256   1.00 26.59  ? 760  ALA   A CA  1 
ATOM   766  C C   . ALA   A 1 104 ? 9.674   29.411 9.331   1.00 29.01  ? 760  ALA   A C   1 
ATOM   767  O O   . ALA   A 1 104 ? 9.084   30.147 8.549   1.00 29.00  ? 760  ALA   A O   1 
ATOM   768  C CB  . ALA   A 1 104 ? 11.642  28.016 8.614   1.00 26.96  ? 760  ALA   A CB  1 
ATOM   769  N N   . LYS   A 1 105 ? 9.034   28.698 10.284  1.00 25.44  ? 761  LYS   A N   1 
ATOM   770  C CA  . LYS   A 1 105 ? 7.571   28.737 10.455  1.00 25.14  ? 761  LYS   A CA  1 
ATOM   771  C C   . LYS   A 1 105 ? 7.056   30.082 11.003  1.00 28.50  ? 761  LYS   A C   1 
ATOM   772  O O   . LYS   A 1 105 ? 5.986   30.521 10.576  1.00 30.57  ? 761  LYS   A O   1 
ATOM   773  C CB  . LYS   A 1 105 ? 7.055   27.558 11.293  1.00 27.04  ? 761  LYS   A CB  1 
ATOM   774  C CG  . LYS   A 1 105 ? 7.275   26.196 10.655  1.00 31.94  ? 761  LYS   A CG  1 
ATOM   775  C CD  . LYS   A 1 105 ? 6.460   25.993 9.386   1.00 33.21  ? 761  LYS   A CD  1 
ATOM   776  C CE  . LYS   A 1 105 ? 6.626   24.626 8.813   1.00 24.39  ? 761  LYS   A CE  1 
ATOM   777  N NZ  . LYS   A 1 105 ? 7.213   24.706 7.459   1.00 42.32  ? 761  LYS   A NZ  1 
ATOM   778  N N   . ALA   A 1 106 ? 7.812   30.737 11.920  1.00 22.42  ? 762  ALA   A N   1 
ATOM   779  C CA  . ALA   A 1 106 ? 7.469   32.057 12.478  1.00 21.51  ? 762  ALA   A CA  1 
ATOM   780  C C   . ALA   A 1 106 ? 7.464   33.095 11.341  1.00 25.36  ? 762  ALA   A C   1 
ATOM   781  O O   . ALA   A 1 106 ? 6.546   33.920 11.287  1.00 21.58  ? 762  ALA   A O   1 
ATOM   782  C CB  . ALA   A 1 106 ? 8.462   32.468 13.564  1.00 21.76  ? 762  ALA   A CB  1 
ATOM   783  N N   . GLU   A 1 107 ? 8.468   32.994 10.404  1.00 23.77  ? 763  GLU   A N   1 
ATOM   784  C CA  . GLU   A 1 107 ? 8.638   33.851 9.210   1.00 23.15  ? 763  GLU   A CA  1 
ATOM   785  C C   . GLU   A 1 107 ? 7.478   33.688 8.232   1.00 23.19  ? 763  GLU   A C   1 
ATOM   786  O O   . GLU   A 1 107 ? 7.001   34.682 7.696   1.00 23.95  ? 763  GLU   A O   1 
ATOM   787  C CB  . GLU   A 1 107 ? 9.972   33.572 8.484   1.00 24.94  ? 763  GLU   A CB  1 
ATOM   788  C CG  . GLU   A 1 107 ? 11.209  34.034 9.233   1.00 36.89  ? 763  GLU   A CG  1 
ATOM   789  C CD  . GLU   A 1 107 ? 12.535  33.430 8.797   1.00 63.12  ? 763  GLU   A CD  1 
ATOM   790  O OE1 . GLU   A 1 107 ? 12.572  32.689 7.786   1.00 57.26  ? 763  GLU   A OE1 1 
ATOM   791  O OE2 . GLU   A 1 107 ? 13.548  33.709 9.477   1.00 56.16  ? 763  GLU   A OE2 1 
ATOM   792  N N   . MET   A 1 108 ? 7.047   32.443 7.977   1.00 16.82  ? 764  MET   A N   1 
ATOM   793  C CA  . MET   A 1 108 ? 5.917   32.153 7.106   1.00 16.52  ? 764  MET   A CA  1 
ATOM   794  C C   . MET   A 1 108 ? 4.650   32.814 7.657   1.00 20.21  ? 764  MET   A C   1 
ATOM   795  O O   . MET   A 1 108 ? 3.934   33.482 6.909   1.00 18.54  ? 764  MET   A O   1 
ATOM   796  C CB  . MET   A 1 108 ? 5.690   30.646 7.002   1.00 19.48  ? 764  MET   A CB  1 
ATOM   797  C CG  . MET   A 1 108 ? 4.357   30.306 6.344   1.00 24.53  ? 764  MET   A CG  1 
ATOM   798  S SD  . MET   A 1 108 ? 3.757   28.658 6.666   1.00 30.44  ? 764  MET   A SD  1 
ATOM   799  C CE  . MET   A 1 108 ? 3.345   28.788 8.370   1.00 26.49  ? 764  MET   A CE  1 
ATOM   800  N N   . LEU   A 1 109 ? 4.414   32.655 8.982   1.00 17.47  ? 765  LEU   A N   1 
ATOM   801  C CA  . LEU   A 1 109 ? 3.248   33.216 9.659   1.00 17.98  ? 765  LEU   A CA  1 
ATOM   802  C C   . LEU   A 1 109 ? 3.181   34.730 9.564   1.00 19.89  ? 765  LEU   A C   1 
ATOM   803  O O   . LEU   A 1 109 ? 2.114   35.246 9.264   1.00 18.55  ? 765  LEU   A O   1 
ATOM   804  C CB  . LEU   A 1 109 ? 3.125   32.729 11.111  1.00 18.60  ? 765  LEU   A CB  1 
ATOM   805  C CG  . LEU   A 1 109 ? 2.846   31.233 11.308  1.00 23.97  ? 765  LEU   A CG  1 
ATOM   806  C CD1 . LEU   A 1 109 ? 2.900   30.864 12.769  1.00 23.45  ? 765  LEU   A CD1 1 
ATOM   807  C CD2 . LEU   A 1 109 ? 1.486   30.834 10.730  1.00 27.69  ? 765  LEU   A CD2 1 
ATOM   808  N N   . ASP   A 1 110 ? 4.326   35.429 9.743   1.00 18.42  ? 766  ASP   A N   1 
ATOM   809  C CA  . ASP   A 1 110 ? 4.457   36.895 9.604   1.00 17.01  ? 766  ASP   A CA  1 
ATOM   810  C C   . ASP   A 1 110 ? 3.951   37.316 8.234   1.00 17.65  ? 766  ASP   A C   1 
ATOM   811  O O   . ASP   A 1 110 ? 3.176   38.259 8.140   1.00 18.50  ? 766  ASP   A O   1 
ATOM   812  C CB  . ASP   A 1 110 ? 5.938   37.330 9.709   1.00 17.40  ? 766  ASP   A CB  1 
ATOM   813  C CG  . ASP   A 1 110 ? 6.599   37.363 11.062  1.00 23.42  ? 766  ASP   A CG  1 
ATOM   814  O OD1 . ASP   A 1 110 ? 6.000   36.858 12.032  1.00 26.10  ? 766  ASP   A OD1 1 
ATOM   815  O OD2 . ASP   A 1 110 ? 7.737   37.851 11.144  1.00 24.88  ? 766  ASP   A OD2 1 
ATOM   816  N N   . ASN   A 1 111 ? 4.405   36.607 7.174   1.00 13.75  ? 767  ASN   A N   1 
ATOM   817  C CA  . ASN   A 1 111 ? 4.023   36.850 5.783   1.00 14.83  ? 767  ASN   A CA  1 
ATOM   818  C C   . ASN   A 1 111 ? 2.549   36.605 5.557   1.00 20.73  ? 767  ASN   A C   1 
ATOM   819  O O   . ASN   A 1 111 ? 1.915   37.415 4.874   1.00 20.44  ? 767  ASN   A O   1 
ATOM   820  C CB  . ASN   A 1 111 ? 4.867   36.002 4.835   1.00 18.94  ? 767  ASN   A CB  1 
ATOM   821  C CG  . ASN   A 1 111 ? 6.267   36.553 4.687   1.00 16.10  ? 767  ASN   A CG  1 
ATOM   822  O OD1 . ASN   A 1 111 ? 6.463   37.727 4.416   1.00 15.58  ? 767  ASN   A OD1 1 
ATOM   823  N ND2 . ASN   A 1 111 ? 7.269   35.739 4.905   1.00 15.79  ? 767  ASN   A ND2 1 
ATOM   824  N N   . LEU   A 1 112 ? 1.988   35.508 6.162   1.00 17.58  ? 768  LEU   A N   1 
ATOM   825  C CA  . LEU   A 1 112 ? 0.556   35.165 6.077   1.00 16.38  ? 768  LEU   A CA  1 
ATOM   826  C C   . LEU   A 1 112 ? -0.282  36.263 6.707   1.00 22.57  ? 768  LEU   A C   1 
ATOM   827  O O   . LEU   A 1 112 ? -1.371  36.524 6.212   1.00 22.75  ? 768  LEU   A O   1 
ATOM   828  C CB  . LEU   A 1 112 ? 0.220   33.814 6.718   1.00 15.62  ? 768  LEU   A CB  1 
ATOM   829  C CG  . LEU   A 1 112 ? 0.715   32.536 6.046   1.00 19.38  ? 768  LEU   A CG  1 
ATOM   830  C CD1 . LEU   A 1 112 ? 0.180   31.318 6.802   1.00 19.42  ? 768  LEU   A CD1 1 
ATOM   831  C CD2 . LEU   A 1 112 ? 0.285   32.443 4.594   1.00 19.18  ? 768  LEU   A CD2 1 
ATOM   832  N N   . LEU   A 1 113 ? 0.241   36.952 7.760   1.00 20.14  ? 769  LEU   A N   1 
ATOM   833  C CA  . LEU   A 1 113 ? -0.452  38.087 8.385   1.00 19.40  ? 769  LEU   A CA  1 
ATOM   834  C C   . LEU   A 1 113 ? -0.626  39.269 7.422   1.00 23.23  ? 769  LEU   A C   1 
ATOM   835  O O   . LEU   A 1 113 ? -1.620  39.971 7.524   1.00 22.84  ? 769  LEU   A O   1 
ATOM   836  C CB  . LEU   A 1 113 ? 0.243   38.546 9.667   1.00 18.87  ? 769  LEU   A CB  1 
ATOM   837  C CG  . LEU   A 1 113 ? 0.006   37.713 10.924  1.00 22.25  ? 769  LEU   A CG  1 
ATOM   838  C CD1 . LEU   A 1 113 ? 0.780   38.290 12.084  1.00 22.64  ? 769  LEU   A CD1 1 
ATOM   839  C CD2 . LEU   A 1 113 ? -1.487  37.637 11.290  1.00 23.05  ? 769  LEU   A CD2 1 
ATOM   840  N N   . ASP   A 1 114 ? 0.329   39.494 6.494   1.00 18.78  ? 770  ASP   A N   1 
ATOM   841  C CA  . ASP   A 1 114 ? 0.193   40.558 5.493   1.00 18.06  ? 770  ASP   A CA  1 
ATOM   842  C C   . ASP   A 1 114 ? -0.717  40.119 4.352   1.00 20.72  ? 770  ASP   A C   1 
ATOM   843  O O   . ASP   A 1 114 ? -1.475  40.935 3.861   1.00 19.79  ? 770  ASP   A O   1 
ATOM   844  C CB  . ASP   A 1 114 ? 1.552   41.017 4.926   1.00 19.29  ? 770  ASP   A CB  1 
ATOM   845  C CG  . ASP   A 1 114 ? 2.254   42.104 5.711   1.00 25.55  ? 770  ASP   A CG  1 
ATOM   846  O OD1 . ASP   A 1 114 ? 1.569   42.843 6.457   1.00 28.09  ? 770  ASP   A OD1 1 
ATOM   847  O OD2 . ASP   A 1 114 ? 3.485   42.211 5.591   1.00 27.14  ? 770  ASP   A OD2 1 
ATOM   848  N N   . ILE   A 1 115 ? -0.609  38.849 3.913   1.00 17.42  ? 771  ILE   A N   1 
ATOM   849  C CA  . ILE   A 1 115 ? -1.424  38.242 2.849   1.00 16.64  ? 771  ILE   A CA  1 
ATOM   850  C C   . ILE   A 1 115 ? -2.923  38.268 3.204   1.00 21.30  ? 771  ILE   A C   1 
ATOM   851  O O   . ILE   A 1 115 ? -3.735  38.569 2.331   1.00 20.73  ? 771  ILE   A O   1 
ATOM   852  C CB  . ILE   A 1 115 ? -0.920  36.827 2.467   1.00 19.42  ? 771  ILE   A CB  1 
ATOM   853  C CG1 . ILE   A 1 115 ? 0.403   36.905 1.662   1.00 20.02  ? 771  ILE   A CG1 1 
ATOM   854  C CG2 . ILE   A 1 115 ? -1.996  36.049 1.680   1.00 19.88  ? 771  ILE   A CG2 1 
ATOM   855  C CD1 . ILE   A 1 115 ? 1.199   35.549 1.542   1.00 19.72  ? 771  ILE   A CD1 1 
ATOM   856  N N   . GLU   A 1 116 ? -3.265  37.976 4.482   1.00 19.45  ? 772  GLU   A N   1 
ATOM   857  C CA  . GLU   A 1 116 ? -4.615  37.988 5.045   1.00 20.71  ? 772  GLU   A CA  1 
ATOM   858  C C   . GLU   A 1 116 ? -5.189  39.411 4.949   1.00 26.26  ? 772  GLU   A C   1 
ATOM   859  O O   . GLU   A 1 116 ? -6.359  39.541 4.628   1.00 25.23  ? 772  GLU   A O   1 
ATOM   860  C CB  . GLU   A 1 116 ? -4.591  37.484 6.501   1.00 22.43  ? 772  GLU   A CB  1 
ATOM   861  C CG  . GLU   A 1 116 ? -5.943  37.175 7.140   1.00 34.20  ? 772  GLU   A CG  1 
ATOM   862  C CD  . GLU   A 1 116 ? -6.755  38.353 7.654   1.00 56.84  ? 772  GLU   A CD  1 
ATOM   863  O OE1 . GLU   A 1 116 ? -6.160  39.297 8.223   1.00 43.51  ? 772  GLU   A OE1 1 
ATOM   864  O OE2 . GLU   A 1 116 ? -7.995  38.332 7.482   1.00 48.06  ? 772  GLU   A OE2 1 
ATOM   865  N N   . VAL   A 1 117 ? -4.367  40.472 5.200   1.00 22.83  ? 773  VAL   A N   1 
ATOM   866  C CA  . VAL   A 1 117 ? -4.830  41.864 5.107   1.00 22.37  ? 773  VAL   A CA  1 
ATOM   867  C C   . VAL   A 1 117 ? -5.190  42.205 3.667   1.00 24.76  ? 773  VAL   A C   1 
ATOM   868  O O   . VAL   A 1 117 ? -6.262  42.777 3.421   1.00 22.97  ? 773  VAL   A O   1 
ATOM   869  C CB  . VAL   A 1 117 ? -3.843  42.872 5.736   1.00 26.44  ? 773  VAL   A CB  1 
ATOM   870  C CG1 . VAL   A 1 117 ? -4.300  44.294 5.496   1.00 25.95  ? 773  VAL   A CG1 1 
ATOM   871  C CG2 . VAL   A 1 117 ? -3.700  42.635 7.239   1.00 26.44  ? 773  VAL   A CG2 1 
ATOM   872  N N   . ALA   A 1 118 ? -4.305  41.823 2.722   1.00 19.78  ? 774  ALA   A N   1 
ATOM   873  C CA  . ALA   A 1 118 ? -4.464  42.021 1.279   1.00 19.40  ? 774  ALA   A CA  1 
ATOM   874  C C   . ALA   A 1 118 ? -5.775  41.388 0.763   1.00 25.79  ? 774  ALA   A C   1 
ATOM   875  O O   . ALA   A 1 118 ? -6.551  42.049 0.058   1.00 25.10  ? 774  ALA   A O   1 
ATOM   876  C CB  . ALA   A 1 118 ? -3.289  41.395 0.546   1.00 19.91  ? 774  ALA   A CB  1 
ATOM   877  N N   . TYR   A 1 119 ? -6.006  40.108 1.118   1.00 23.36  ? 775  TYR   A N   1 
ATOM   878  C CA  . TYR   A 1 119 ? -7.179  39.363 0.678   1.00 25.97  ? 775  TYR   A CA  1 
ATOM   879  C C   . TYR   A 1 119 ? -8.464  39.880 1.322   1.00 27.72  ? 775  TYR   A C   1 
ATOM   880  O O   . TYR   A 1 119 ? -9.476  39.942 0.641   1.00 26.89  ? 775  TYR   A O   1 
ATOM   881  C CB  . TYR   A 1 119 ? -6.997  37.850 0.859   1.00 29.17  ? 775  TYR   A CB  1 
ATOM   882  C CG  . TYR   A 1 119 ? -7.940  37.036 0.008   1.00 33.25  ? 775  TYR   A CG  1 
ATOM   883  C CD1 . TYR   A 1 119 ? -7.745  36.913 -1.366  1.00 36.32  ? 775  TYR   A CD1 1 
ATOM   884  C CD2 . TYR   A 1 119 ? -9.041  36.408 0.568   1.00 34.38  ? 775  TYR   A CD2 1 
ATOM   885  C CE1 . TYR   A 1 119 ? -8.634  36.199 -2.161  1.00 37.63  ? 775  TYR   A CE1 1 
ATOM   886  C CE2 . TYR   A 1 119 ? -9.924  35.670 -0.214  1.00 35.60  ? 775  TYR   A CE2 1 
ATOM   887  C CZ  . TYR   A 1 119 ? -9.715  35.565 -1.579  1.00 43.85  ? 775  TYR   A CZ  1 
ATOM   888  O OH  . TYR   A 1 119 ? -10.562 34.809 -2.357  1.00 45.16  ? 775  TYR   A OH  1 
ATOM   889  N N   . SER   A 1 120 ? -8.392  40.313 2.606   1.00 22.64  ? 776  SER   A N   1 
ATOM   890  C CA  . SER   A 1 120 ? -9.491  40.909 3.377   1.00 22.69  ? 776  SER   A CA  1 
ATOM   891  C C   . SER   A 1 120 ? -9.959  42.236 2.721   1.00 25.19  ? 776  SER   A C   1 
ATOM   892  O O   . SER   A 1 120 ? -11.155 42.493 2.603   1.00 22.99  ? 776  SER   A O   1 
ATOM   893  C CB  . SER   A 1 120 ? -9.041  41.159 4.820   1.00 27.36  ? 776  SER   A CB  1 
ATOM   894  O OG  . SER   A 1 120 ? -9.938  41.931 5.604   1.00 39.95  ? 776  SER   A OG  1 
ATOM   895  N N   . LEU   A 1 121 ? -9.001  43.057 2.293   1.00 23.40  ? 777  LEU   A N   1 
ATOM   896  C CA  . LEU   A 1 121 ? -9.200  44.356 1.652   1.00 24.01  ? 777  LEU   A CA  1 
ATOM   897  C C   . LEU   A 1 121 ? -9.938  44.177 0.314   1.00 27.48  ? 777  LEU   A C   1 
ATOM   898  O O   . LEU   A 1 121 ? -11.020 44.747 0.099   1.00 26.39  ? 777  LEU   A O   1 
ATOM   899  C CB  . LEU   A 1 121 ? -7.792  44.977 1.465   1.00 24.08  ? 777  LEU   A CB  1 
ATOM   900  C CG  . LEU   A 1 121 ? -7.559  46.455 1.773   1.00 29.68  ? 777  LEU   A CG  1 
ATOM   901  C CD1 . LEU   A 1 121 ? -8.244  46.920 3.052   1.00 30.51  ? 777  LEU   A CD1 1 
ATOM   902  C CD2 . LEU   A 1 121 ? -6.065  46.763 1.843   1.00 29.42  ? 777  LEU   A CD2 1 
ATOM   903  N N   . LEU   A 1 122 ? -9.421  43.269 -0.513  1.00 23.78  ? 778  LEU   A N   1 
ATOM   904  C CA  . LEU   A 1 122 ? -9.967  42.887 -1.810  1.00 25.47  ? 778  LEU   A CA  1 
ATOM   905  C C   . LEU   A 1 122 ? -11.403 42.268 -1.723  1.00 31.61  ? 778  LEU   A C   1 
ATOM   906  O O   . LEU   A 1 122 ? -12.270 42.612 -2.530  1.00 31.94  ? 778  LEU   A O   1 
ATOM   907  C CB  . LEU   A 1 122 ? -8.969  41.903 -2.456  1.00 26.49  ? 778  LEU   A CB  1 
ATOM   908  C CG  . LEU   A 1 122 ? -8.885  41.870 -3.975  1.00 31.60  ? 778  LEU   A CG  1 
ATOM   909  C CD1 . LEU   A 1 122 ? -8.459  43.214 -4.555  1.00 30.96  ? 778  LEU   A CD1 1 
ATOM   910  C CD2 . LEU   A 1 122 ? -7.894  40.851 -4.402  1.00 33.32  ? 778  LEU   A CD2 1 
ATOM   911  N N   . ARG   A 1 123 ? -11.656 41.388 -0.728  1.00 28.91  ? 779  ARG   A N   1 
ATOM   912  C CA  . ARG   A 1 123 ? -12.943 40.717 -0.524  1.00 28.51  ? 779  ARG   A CA  1 
ATOM   913  C C   . ARG   A 1 123 ? -13.936 41.521 0.351   1.00 33.59  ? 779  ARG   A C   1 
ATOM   914  O O   . ARG   A 1 123 ? -15.147 41.212 0.390   1.00 31.41  ? 779  ARG   A O   1 
ATOM   915  C CB  . ARG   A 1 123 ? -12.749 39.290 0.004   1.00 30.35  ? 779  ARG   A CB  1 
ATOM   916  C CG  . ARG   A 1 123 ? -12.284 38.279 -1.082  1.00 41.80  ? 779  ARG   A CG  1 
ATOM   917  C CD  . ARG   A 1 123 ? -13.132 38.282 -2.360  1.00 59.23  ? 779  ARG   A CD  1 
ATOM   918  N NE  . ARG   A 1 123 ? -12.597 37.455 -3.448  1.00 72.18  ? 779  ARG   A NE  1 
ATOM   919  C CZ  . ARG   A 1 123 ? -11.655 37.839 -4.311  1.00 90.70  ? 779  ARG   A CZ  1 
ATOM   920  N NH1 . ARG   A 1 123 ? -11.062 39.019 -4.179  1.00 82.89  ? 779  ARG   A NH1 1 
ATOM   921  N NH2 . ARG   A 1 123 ? -11.271 37.027 -5.286  1.00 77.12  ? 779  ARG   A NH2 1 
ATOM   922  N N   . GLY   A 1 124 ? -13.429 42.564 1.009   1.00 29.37  ? 780  GLY   A N   1 
ATOM   923  C CA  . GLY   A 1 124 ? -14.248 43.501 1.773   1.00 29.60  ? 780  GLY   A CA  1 
ATOM   924  C C   . GLY   A 1 124 ? -14.687 44.640 0.858   1.00 34.42  ? 780  GLY   A C   1 
ATOM   925  O O   . GLY   A 1 124 ? -14.363 44.660 -0.339  1.00 36.76  ? 780  GLY   A O   1 
ATOM   926  N N   . GLY   A 1 125 ? -15.432 45.584 1.367   1.00 27.11  ? 781  GLY   A N   1 
ATOM   927  C CA  . GLY   A 1 125 ? -15.834 46.660 0.473   1.00 27.56  ? 781  GLY   A CA  1 
ATOM   928  C C   . GLY   A 1 125 ? -17.003 46.414 -0.462  1.00 32.19  ? 781  GLY   A C   1 
ATOM   929  O O   . GLY   A 1 125 ? -17.795 45.467 -0.301  1.00 31.87  ? 781  GLY   A O   1 
ATOM   930  N N   . SER   A 1 126 ? -17.105 47.316 -1.444  1.00 29.45  ? 782  SER   A N   1 
ATOM   931  C CA  . SER   A 1 126 ? -18.198 47.404 -2.396  1.00 29.36  ? 782  SER   A CA  1 
ATOM   932  C C   . SER   A 1 126 ? -17.806 47.028 -3.832  1.00 36.08  ? 782  SER   A C   1 
ATOM   933  O O   . SER   A 1 126 ? -16.654 47.225 -4.251  1.00 34.97  ? 782  SER   A O   1 
ATOM   934  C CB  . SER   A 1 126 ? -18.766 48.823 -2.374  1.00 32.33  ? 782  SER   A CB  1 
ATOM   935  O OG  . SER   A 1 126 ? -19.184 49.210 -1.076  1.00 40.76  ? 782  SER   A OG  1 
ATOM   936  N N   . ASP   A 1 127 ? -18.788 46.528 -4.589  1.00 34.04  ? 783  ASP   A N   1 
ATOM   937  C CA  . ASP   A 1 127 ? -18.665 46.193 -6.000  1.00 36.08  ? 783  ASP   A CA  1 
ATOM   938  C C   . ASP   A 1 127 ? -19.454 47.185 -6.881  1.00 39.23  ? 783  ASP   A C   1 
ATOM   939  O O   . ASP   A 1 127 ? -20.666 47.358 -6.730  1.00 38.49  ? 783  ASP   A O   1 
ATOM   940  C CB  . ASP   A 1 127 ? -19.091 44.741 -6.281  1.00 39.56  ? 783  ASP   A CB  1 
ATOM   941  C CG  . ASP   A 1 127 ? -18.553 44.191 -7.588  1.00 57.52  ? 783  ASP   A CG  1 
ATOM   942  O OD1 . ASP   A 1 127 ? -17.314 44.069 -7.712  1.00 61.09  ? 783  ASP   A OD1 1 
ATOM   943  O OD2 . ASP   A 1 127 ? -19.376 43.885 -8.494  1.00 63.95  ? 783  ASP   A OD2 1 
ATOM   944  N N   . ASP   A 1 128 ? -18.737 47.836 -7.797  1.00 37.18  ? 784  ASP   A N   1 
ATOM   945  C CA  . ASP   A 1 128 ? -19.268 48.831 -8.722  1.00 37.69  ? 784  ASP   A CA  1 
ATOM   946  C C   . ASP   A 1 128 ? -18.556 48.645 -10.055 1.00 43.11  ? 784  ASP   A C   1 
ATOM   947  O O   . ASP   A 1 128 ? -17.364 48.946 -10.166 1.00 42.42  ? 784  ASP   A O   1 
ATOM   948  C CB  . ASP   A 1 128 ? -19.046 50.244 -8.128  1.00 39.66  ? 784  ASP   A CB  1 
ATOM   949  C CG  . ASP   A 1 128 ? -19.631 51.432 -8.870  1.00 47.23  ? 784  ASP   A CG  1 
ATOM   950  O OD1 . ASP   A 1 128 ? -20.237 51.229 -9.952  1.00 45.89  ? 784  ASP   A OD1 1 
ATOM   951  O OD2 . ASP   A 1 128 ? -19.485 52.565 -8.369  1.00 55.61  ? 784  ASP   A OD2 1 
ATOM   952  N N   . SER   A 1 129 ? -19.284 48.130 -11.062 1.00 42.91  ? 785  SER   A N   1 
ATOM   953  C CA  . SER   A 1 129 ? -18.770 47.870 -12.419 1.00 44.25  ? 785  SER   A CA  1 
ATOM   954  C C   . SER   A 1 129 ? -18.262 49.136 -13.103 1.00 47.87  ? 785  SER   A C   1 
ATOM   955  O O   . SER   A 1 129 ? -17.226 49.084 -13.759 1.00 48.91  ? 785  SER   A O   1 
ATOM   956  C CB  . SER   A 1 129 ? -19.849 47.239 -13.300 1.00 50.58  ? 785  SER   A CB  1 
ATOM   957  O OG  . SER   A 1 129 ? -20.442 46.089 -12.722 1.00 64.85  ? 785  SER   A OG  1 
ATOM   958  N N   . SER   A 1 130 ? -18.987 50.266 -12.924 1.00 43.48  ? 786  SER   A N   1 
ATOM   959  C CA  . SER   A 1 130 ? -18.697 51.578 -13.510 1.00 42.44  ? 786  SER   A CA  1 
ATOM   960  C C   . SER   A 1 130 ? -17.344 52.158 -13.111 1.00 44.23  ? 786  SER   A C   1 
ATOM   961  O O   . SER   A 1 130 ? -16.827 53.036 -13.813 1.00 43.80  ? 786  SER   A O   1 
ATOM   962  C CB  . SER   A 1 130 ? -19.812 52.566 -13.191 1.00 44.80  ? 786  SER   A CB  1 
ATOM   963  O OG  . SER   A 1 130 ? -19.721 53.040 -11.859 1.00 52.75  ? 786  SER   A OG  1 
ATOM   964  N N   . LYS   A 1 131 ? -16.771 51.675 -11.985 1.00 39.15  ? 787  LYS   A N   1 
ATOM   965  C CA  . LYS   A 1 131 ? -15.466 52.122 -11.477 1.00 37.31  ? 787  LYS   A CA  1 
ATOM   966  C C   . LYS   A 1 131 ? -14.343 51.172 -11.851 1.00 38.44  ? 787  LYS   A C   1 
ATOM   967  O O   . LYS   A 1 131 ? -14.509 49.951 -11.746 1.00 37.14  ? 787  LYS   A O   1 
ATOM   968  C CB  . LYS   A 1 131 ? -15.497 52.352 -9.957  1.00 39.02  ? 787  LYS   A CB  1 
ATOM   969  C CG  . LYS   A 1 131 ? -16.460 53.478 -9.545  1.00 57.24  ? 787  LYS   A CG  1 
ATOM   970  C CD  . LYS   A 1 131 ? -16.306 53.879 -8.078  1.00 65.25  ? 787  LYS   A CD  1 
ATOM   971  C CE  . LYS   A 1 131 ? -17.017 55.181 -7.782  1.00 73.78  ? 787  LYS   A CE  1 
ATOM   972  N NZ  . LYS   A 1 131 ? -16.861 55.604 -6.369  1.00 78.60  ? 787  LYS   A NZ  1 
ATOM   973  N N   . ASP   A 1 132 ? -13.201 51.729 -12.306 1.00 33.48  ? 788  ASP   A N   1 
ATOM   974  C CA  . ASP   A 1 132 ? -12.015 50.948 -12.666 1.00 32.85  ? 788  ASP   A CA  1 
ATOM   975  C C   . ASP   A 1 132 ? -11.530 50.235 -11.392 1.00 35.19  ? 788  ASP   A C   1 
ATOM   976  O O   . ASP   A 1 132 ? -11.308 50.919 -10.393 1.00 34.54  ? 788  ASP   A O   1 
ATOM   977  C CB  . ASP   A 1 132 ? -10.926 51.905 -13.197 1.00 34.91  ? 788  ASP   A CB  1 
ATOM   978  C CG  . ASP   A 1 132 ? -9.699  51.262 -13.818 1.00 36.33  ? 788  ASP   A CG  1 
ATOM   979  O OD1 . ASP   A 1 132 ? -9.220  50.251 -13.275 1.00 35.29  ? 788  ASP   A OD1 1 
ATOM   980  O OD2 . ASP   A 1 132 ? -9.210  51.787 -14.834 1.00 42.65  ? 788  ASP   A OD2 1 
ATOM   981  N N   . PRO   A 1 133 ? -11.366 48.882 -11.399 1.00 32.95  ? 789  PRO   A N   1 
ATOM   982  C CA  . PRO   A 1 133 ? -10.882 48.176 -10.183 1.00 31.98  ? 789  PRO   A CA  1 
ATOM   983  C C   . PRO   A 1 133 ? -9.539  48.657 -9.624  1.00 33.05  ? 789  PRO   A C   1 
ATOM   984  O O   . PRO   A 1 133 ? -9.281  48.466 -8.447  1.00 31.40  ? 789  PRO   A O   1 
ATOM   985  C CB  . PRO   A 1 133 ? -10.817 46.704 -10.617 1.00 33.74  ? 789  PRO   A CB  1 
ATOM   986  C CG  . PRO   A 1 133 ? -11.704 46.610 -11.820 1.00 38.93  ? 789  PRO   A CG  1 
ATOM   987  C CD  . PRO   A 1 133 ? -11.601 47.930 -12.510 1.00 34.83  ? 789  PRO   A CD  1 
ATOM   988  N N   . ILE   A 1 134 ? -8.701  49.293 -10.460 1.00 30.72  ? 790  ILE   A N   1 
ATOM   989  C CA  . ILE   A 1 134 ? -7.411  49.880 -10.061 1.00 30.03  ? 790  ILE   A CA  1 
ATOM   990  C C   . ILE   A 1 134 ? -7.692  51.088 -9.127  1.00 34.32  ? 790  ILE   A C   1 
ATOM   991  O O   . ILE   A 1 134 ? -7.055  51.208 -8.078  1.00 34.50  ? 790  ILE   A O   1 
ATOM   992  C CB  . ILE   A 1 134 ? -6.576  50.258 -11.312 1.00 32.64  ? 790  ILE   A CB  1 
ATOM   993  C CG1 . ILE   A 1 134 ? -6.216  48.986 -12.127 1.00 33.22  ? 790  ILE   A CG1 1 
ATOM   994  C CG2 . ILE   A 1 134 ? -5.320  51.048 -10.920 1.00 32.59  ? 790  ILE   A CG2 1 
ATOM   995  C CD1 . ILE   A 1 134 ? -5.909  49.184 -13.617 1.00 38.92  ? 790  ILE   A CD1 1 
ATOM   996  N N   . ASP   A 1 135 ? -8.661  51.949 -9.505  1.00 30.48  ? 791  ASP   A N   1 
ATOM   997  C CA  . ASP   A 1 135 ? -9.109  53.097 -8.714  1.00 31.22  ? 791  ASP   A CA  1 
ATOM   998  C C   . ASP   A 1 135 ? -9.715  52.622 -7.378  1.00 34.48  ? 791  ASP   A C   1 
ATOM   999  O O   . ASP   A 1 135 ? -9.345  53.154 -6.325  1.00 34.31  ? 791  ASP   A O   1 
ATOM   1000 C CB  . ASP   A 1 135 ? -10.140 53.934 -9.508  1.00 33.39  ? 791  ASP   A CB  1 
ATOM   1001 C CG  . ASP   A 1 135 ? -9.529  54.938 -10.467 1.00 44.87  ? 791  ASP   A CG  1 
ATOM   1002 O OD1 . ASP   A 1 135 ? -8.325  55.246 -10.316 1.00 45.73  ? 791  ASP   A OD1 1 
ATOM   1003 O OD2 . ASP   A 1 135 ? -10.265 55.444 -11.349 1.00 49.06  ? 791  ASP   A OD2 1 
ATOM   1004 N N   . VAL   A 1 136 ? -10.604 51.583 -7.436  1.00 28.45  ? 792  VAL   A N   1 
ATOM   1005 C CA  . VAL   A 1 136 ? -11.251 50.958 -6.285  1.00 27.62  ? 792  VAL   A CA  1 
ATOM   1006 C C   . VAL   A 1 136 ? -10.151 50.441 -5.326  1.00 33.71  ? 792  VAL   A C   1 
ATOM   1007 O O   . VAL   A 1 136 ? -10.086 50.880 -4.181  1.00 34.50  ? 792  VAL   A O   1 
ATOM   1008 C CB  . VAL   A 1 136 ? -12.207 49.818 -6.724  1.00 30.60  ? 792  VAL   A CB  1 
ATOM   1009 C CG1 . VAL   A 1 136 ? -12.764 49.060 -5.519  1.00 30.23  ? 792  VAL   A CG1 1 
ATOM   1010 C CG2 . VAL   A 1 136 ? -13.348 50.342 -7.605  1.00 30.38  ? 792  VAL   A CG2 1 
ATOM   1011 N N   . ASN   A 1 137 ? -9.249  49.575 -5.827  1.00 30.03  ? 793  ASN   A N   1 
ATOM   1012 C CA  . ASN   A 1 137 ? -8.187  48.992 -5.015  1.00 29.47  ? 793  ASN   A CA  1 
ATOM   1013 C C   . ASN   A 1 137 ? -7.153  50.012 -4.519  1.00 34.48  ? 793  ASN   A C   1 
ATOM   1014 O O   . ASN   A 1 137 ? -6.575  49.794 -3.453  1.00 35.80  ? 793  ASN   A O   1 
ATOM   1015 C CB  . ASN   A 1 137 ? -7.536  47.819 -5.733  1.00 28.36  ? 793  ASN   A CB  1 
ATOM   1016 C CG  . ASN   A 1 137 ? -8.449  46.628 -5.912  1.00 48.08  ? 793  ASN   A CG  1 
ATOM   1017 O OD1 . ASN   A 1 137 ? -9.439  46.440 -5.188  1.00 45.44  ? 793  ASN   A OD1 1 
ATOM   1018 N ND2 . ASN   A 1 137 ? -8.129  45.785 -6.881  1.00 41.47  ? 793  ASN   A ND2 1 
ATOM   1019 N N   . TYR   A 1 138 ? -6.950  51.136 -5.238  1.00 30.44  ? 794  TYR   A N   1 
ATOM   1020 C CA  . TYR   A 1 138 ? -6.021  52.181 -4.781  1.00 30.41  ? 794  TYR   A CA  1 
ATOM   1021 C C   . TYR   A 1 138 ? -6.551  52.848 -3.500  1.00 33.03  ? 794  TYR   A C   1 
ATOM   1022 O O   . TYR   A 1 138 ? -5.769  53.064 -2.575  1.00 31.61  ? 794  TYR   A O   1 
ATOM   1023 C CB  . TYR   A 1 138 ? -5.762  53.225 -5.898  1.00 30.68  ? 794  TYR   A CB  1 
ATOM   1024 C CG  . TYR   A 1 138 ? -4.974  54.445 -5.468  1.00 31.18  ? 794  TYR   A CG  1 
ATOM   1025 C CD1 . TYR   A 1 138 ? -3.583  54.417 -5.418  1.00 33.44  ? 794  TYR   A CD1 1 
ATOM   1026 C CD2 . TYR   A 1 138 ? -5.616  55.641 -5.154  1.00 31.67  ? 794  TYR   A CD2 1 
ATOM   1027 C CE1 . TYR   A 1 138 ? -2.851  55.541 -5.040  1.00 33.18  ? 794  TYR   A CE1 1 
ATOM   1028 C CE2 . TYR   A 1 138 ? -4.895  56.769 -4.762  1.00 32.74  ? 794  TYR   A CE2 1 
ATOM   1029 C CZ  . TYR   A 1 138 ? -3.511  56.715 -4.716  1.00 38.85  ? 794  TYR   A CZ  1 
ATOM   1030 O OH  . TYR   A 1 138 ? -2.783  57.820 -4.345  1.00 43.83  ? 794  TYR   A OH  1 
ATOM   1031 N N   . GLU   A 1 139 ? -7.870  53.158 -3.457  1.00 29.66  ? 795  GLU   A N   1 
ATOM   1032 C CA  . GLU   A 1 139 ? -8.513  53.834 -2.324  1.00 29.04  ? 795  GLU   A CA  1 
ATOM   1033 C C   . GLU   A 1 139 ? -8.492  52.981 -1.069  1.00 31.71  ? 795  GLU   A C   1 
ATOM   1034 O O   . GLU   A 1 139 ? -8.455  53.532 0.031   1.00 29.00  ? 795  GLU   A O   1 
ATOM   1035 C CB  . GLU   A 1 139 ? -9.941  54.240 -2.645  1.00 30.48  ? 795  GLU   A CB  1 
ATOM   1036 C CG  . GLU   A 1 139 ? -10.095 55.155 -3.849  1.00 45.07  ? 795  GLU   A CG  1 
ATOM   1037 C CD  . GLU   A 1 139 ? -11.538 55.580 -4.013  1.00 67.71  ? 795  GLU   A CD  1 
ATOM   1038 O OE1 . GLU   A 1 139 ? -11.971 55.755 -5.175  1.00 67.61  ? 795  GLU   A OE1 1 
ATOM   1039 O OE2 . GLU   A 1 139 ? -12.249 55.726 -2.990  1.00 58.97  ? 795  GLU   A OE2 1 
ATOM   1040 N N   . LYS   A 1 140 ? -8.481  51.636 -1.230  1.00 28.79  ? 796  LYS   A N   1 
ATOM   1041 C CA  . LYS   A 1 140 ? -8.461  50.674 -0.123  1.00 27.62  ? 796  LYS   A CA  1 
ATOM   1042 C C   . LYS   A 1 140 ? -7.220  50.832 0.725   1.00 32.02  ? 796  LYS   A C   1 
ATOM   1043 O O   . LYS   A 1 140 ? -7.282  50.584 1.919   1.00 34.07  ? 796  LYS   A O   1 
ATOM   1044 C CB  . LYS   A 1 140 ? -8.548  49.227 -0.631  1.00 28.53  ? 796  LYS   A CB  1 
ATOM   1045 C CG  . LYS   A 1 140 ? -9.760  48.953 -1.484  1.00 34.93  ? 796  LYS   A CG  1 
ATOM   1046 C CD  . LYS   A 1 140 ? -10.245 47.521 -1.368  1.00 37.55  ? 796  LYS   A CD  1 
ATOM   1047 C CE  . LYS   A 1 140 ? -11.492 47.259 -2.176  1.00 33.15  ? 796  LYS   A CE  1 
ATOM   1048 N NZ  . LYS   A 1 140 ? -12.531 48.317 -1.990  1.00 40.76  ? 796  LYS   A NZ  1 
ATOM   1049 N N   . LEU   A 1 141 ? -6.100  51.249 0.108   1.00 27.73  ? 797  LEU   A N   1 
ATOM   1050 C CA  . LEU   A 1 141 ? -4.802  51.414 0.739   1.00 27.95  ? 797  LEU   A CA  1 
ATOM   1051 C C   . LEU   A 1 141 ? -4.671  52.585 1.691   1.00 33.88  ? 797  LEU   A C   1 
ATOM   1052 O O   . LEU   A 1 141 ? -3.760  52.562 2.535   1.00 33.86  ? 797  LEU   A O   1 
ATOM   1053 C CB  . LEU   A 1 141 ? -3.695  51.496 -0.322  1.00 28.03  ? 797  LEU   A CB  1 
ATOM   1054 C CG  . LEU   A 1 141 ? -3.528  50.264 -1.209  1.00 33.33  ? 797  LEU   A CG  1 
ATOM   1055 C CD1 . LEU   A 1 141 ? -2.455  50.496 -2.232  1.00 33.26  ? 797  LEU   A CD1 1 
ATOM   1056 C CD2 . LEU   A 1 141 ? -3.242  49.004 -0.382  1.00 36.74  ? 797  LEU   A CD2 1 
ATOM   1057 N N   . LYS   A 1 142 ? -5.554  53.622 1.553   1.00 29.66  ? 798  LYS   A N   1 
ATOM   1058 C CA  . LYS   A 1 142 ? -5.531  54.847 2.369   1.00 29.38  ? 798  LYS   A CA  1 
ATOM   1059 C C   . LYS   A 1 142 ? -4.092  55.440 2.441   1.00 33.63  ? 798  LYS   A C   1 
ATOM   1060 O O   . LYS   A 1 142 ? -3.616  55.838 3.507   1.00 33.40  ? 798  LYS   A O   1 
ATOM   1061 C CB  . LYS   A 1 142 ? -6.159  54.612 3.760   1.00 31.39  ? 798  LYS   A CB  1 
ATOM   1062 C CG  . LYS   A 1 142 ? -7.601  54.110 3.673   1.00 42.12  ? 798  LYS   A CG  1 
ATOM   1063 C CD  . LYS   A 1 142 ? -8.038  53.405 4.905   1.00 46.54  ? 798  LYS   A CD  1 
ATOM   1064 C CE  . LYS   A 1 142 ? -9.438  52.859 4.730   1.00 35.01  ? 798  LYS   A CE  1 
ATOM   1065 N NZ  . LYS   A 1 142 ? -10.051 52.483 6.036   1.00 39.91  ? 798  LYS   A NZ  1 
ATOM   1066 N N   . THR   A 1 143 ? -3.401  55.447 1.276   1.00 29.91  ? 799  THR   A N   1 
ATOM   1067 C CA  . THR   A 1 143 ? -2.033  55.919 1.043   1.00 29.13  ? 799  THR   A CA  1 
ATOM   1068 C C   . THR   A 1 143 ? -2.022  56.814 -0.204  1.00 33.30  ? 799  THR   A C   1 
ATOM   1069 O O   . THR   A 1 143 ? -2.589  56.444 -1.235  1.00 33.43  ? 799  THR   A O   1 
ATOM   1070 C CB  . THR   A 1 143 ? -1.048  54.699 0.900   1.00 30.25  ? 799  THR   A CB  1 
ATOM   1071 O OG1 . THR   A 1 143 ? -1.108  53.903 2.076   1.00 29.70  ? 799  THR   A OG1 1 
ATOM   1072 C CG2 . THR   A 1 143 ? 0.413   55.108 0.680   1.00 26.64  ? 799  THR   A CG2 1 
ATOM   1073 N N   . ASP   A 1 144 ? -1.388  57.992 -0.104  1.00 30.05  ? 800  ASP   A N   1 
ATOM   1074 C CA  . ASP   A 1 144 ? -1.201  58.880 -1.249  1.00 29.98  ? 800  ASP   A CA  1 
ATOM   1075 C C   . ASP   A 1 144 ? 0.072   58.345 -1.918  1.00 33.59  ? 800  ASP   A C   1 
ATOM   1076 O O   . ASP   A 1 144 ? 1.097   58.217 -1.253  1.00 33.27  ? 800  ASP   A O   1 
ATOM   1077 C CB  . ASP   A 1 144 ? -1.020  60.350 -0.808  1.00 32.15  ? 800  ASP   A CB  1 
ATOM   1078 C CG  . ASP   A 1 144 ? -0.686  61.325 -1.933  1.00 47.28  ? 800  ASP   A CG  1 
ATOM   1079 O OD1 . ASP   A 1 144 ? -1.468  61.406 -2.908  1.00 50.27  ? 800  ASP   A OD1 1 
ATOM   1080 O OD2 . ASP   A 1 144 ? 0.333   62.029 -1.823  1.00 53.18  ? 800  ASP   A OD2 1 
ATOM   1081 N N   . ILE   A 1 145 ? -0.029  57.908 -3.176  1.00 29.64  ? 801  ILE   A N   1 
ATOM   1082 C CA  . ILE   A 1 145 ? 1.104   57.363 -3.910  1.00 29.55  ? 801  ILE   A CA  1 
ATOM   1083 C C   . ILE   A 1 145 ? 1.348   58.272 -5.100  1.00 34.88  ? 801  ILE   A C   1 
ATOM   1084 O O   . ILE   A 1 145 ? 0.470   58.432 -5.948  1.00 35.29  ? 801  ILE   A O   1 
ATOM   1085 C CB  . ILE   A 1 145 ? 0.920   55.868 -4.324  1.00 32.88  ? 801  ILE   A CB  1 
ATOM   1086 C CG1 . ILE   A 1 145 ? 0.573   54.965 -3.111  1.00 33.76  ? 801  ILE   A CG1 1 
ATOM   1087 C CG2 . ILE   A 1 145 ? 2.161   55.331 -5.077  1.00 33.36  ? 801  ILE   A CG2 1 
ATOM   1088 C CD1 . ILE   A 1 145 ? -0.046  53.607 -3.458  1.00 40.55  ? 801  ILE   A CD1 1 
ATOM   1089 N N   . LYS   A 1 146 ? 2.520   58.902 -5.139  1.00 30.29  ? 802  LYS   A N   1 
ATOM   1090 C CA  . LYS   A 1 146 ? 2.897   59.791 -6.241  1.00 30.11  ? 802  LYS   A CA  1 
ATOM   1091 C C   . LYS   A 1 146 ? 4.192   59.285 -6.887  1.00 34.66  ? 802  LYS   A C   1 
ATOM   1092 O O   . LYS   A 1 146 ? 4.987   58.644 -6.214  1.00 32.99  ? 802  LYS   A O   1 
ATOM   1093 C CB  . LYS   A 1 146 ? 3.032   61.257 -5.765  1.00 31.96  ? 802  LYS   A CB  1 
ATOM   1094 C CG  . LYS   A 1 146 ? 1.681   61.868 -5.397  1.00 47.38  ? 802  LYS   A CG  1 
ATOM   1095 C CD  . LYS   A 1 146 ? 1.676   63.388 -5.372  1.00 56.55  ? 802  LYS   A CD  1 
ATOM   1096 C CE  . LYS   A 1 146 ? 0.268   63.910 -5.157  1.00 54.56  ? 802  LYS   A CE  1 
ATOM   1097 N NZ  . LYS   A 1 146 ? 0.218   65.392 -5.220  1.00 65.15  ? 802  LYS   A NZ  1 
ATOM   1098 N N   . VAL   A 1 147 ? 4.373   59.533 -8.190  1.00 32.69  ? 803  VAL   A N   1 
ATOM   1099 C CA  . VAL   A 1 147 ? 5.565   59.125 -8.941  1.00 33.13  ? 803  VAL   A CA  1 
ATOM   1100 C C   . VAL   A 1 147 ? 6.628   60.220 -8.783  1.00 38.07  ? 803  VAL   A C   1 
ATOM   1101 O O   . VAL   A 1 147 ? 6.339   61.399 -9.004  1.00 39.36  ? 803  VAL   A O   1 
ATOM   1102 C CB  . VAL   A 1 147 ? 5.260   58.813 -10.443 1.00 36.89  ? 803  VAL   A CB  1 
ATOM   1103 C CG1 . VAL   A 1 147 ? 6.461   58.175 -11.140 1.00 36.72  ? 803  VAL   A CG1 1 
ATOM   1104 C CG2 . VAL   A 1 147 ? 4.051   57.903 -10.579 1.00 36.51  ? 803  VAL   A CG2 1 
ATOM   1105 N N   . VAL   A 1 148 ? 7.835   59.843 -8.373  1.00 33.71  ? 804  VAL   A N   1 
ATOM   1106 C CA  . VAL   A 1 148 ? 8.929   60.802 -8.219  1.00 33.83  ? 804  VAL   A CA  1 
ATOM   1107 C C   . VAL   A 1 148 ? 9.564   61.061 -9.611  1.00 43.25  ? 804  VAL   A C   1 
ATOM   1108 O O   . VAL   A 1 148 ? 9.893   60.106 -10.334 1.00 42.74  ? 804  VAL   A O   1 
ATOM   1109 C CB  . VAL   A 1 148 ? 9.957   60.354 -7.137  1.00 36.07  ? 804  VAL   A CB  1 
ATOM   1110 C CG1 . VAL   A 1 148 ? 11.221  61.202 -7.171  1.00 35.65  ? 804  VAL   A CG1 1 
ATOM   1111 C CG2 . VAL   A 1 148 ? 9.341   60.389 -5.741  1.00 35.25  ? 804  VAL   A CG2 1 
ATOM   1112 N N   . ASP   A 1 149 ? 9.701   62.353 -9.983  1.00 43.99  ? 805  ASP   A N   1 
ATOM   1113 C CA  . ASP   A 1 149 ? 10.291  62.785 -11.249 1.00 46.10  ? 805  ASP   A CA  1 
ATOM   1114 C C   . ASP   A 1 149 ? 11.749  62.324 -11.325 1.00 51.94  ? 805  ASP   A C   1 
ATOM   1115 O O   . ASP   A 1 149 ? 12.518  62.551 -10.389 1.00 51.28  ? 805  ASP   A O   1 
ATOM   1116 C CB  . ASP   A 1 149 ? 10.170  64.320 -11.410 1.00 48.96  ? 805  ASP   A CB  1 
ATOM   1117 C CG  . ASP   A 1 149 ? 10.685  64.888 -12.723 1.00 67.04  ? 805  ASP   A CG  1 
ATOM   1118 O OD1 . ASP   A 1 149 ? 10.591  64.183 -13.760 1.00 68.53  ? 805  ASP   A OD1 1 
ATOM   1119 O OD2 . ASP   A 1 149 ? 11.170  66.044 -12.718 1.00 75.39  ? 805  ASP   A OD2 1 
ATOM   1120 N N   . ARG   A 1 150 ? 12.104  61.656 -12.442 1.00 50.00  ? 806  ARG   A N   1 
ATOM   1121 C CA  . ARG   A 1 150 ? 13.422  61.080 -12.727 1.00 50.43  ? 806  ARG   A CA  1 
ATOM   1122 C C   . ARG   A 1 150 ? 14.589  62.044 -12.539 1.00 56.18  ? 806  ARG   A C   1 
ATOM   1123 O O   . ARG   A 1 150 ? 15.655  61.626 -12.086 1.00 55.63  ? 806  ARG   A O   1 
ATOM   1124 C CB  . ARG   A 1 150 ? 13.462  60.508 -14.156 1.00 50.33  ? 806  ARG   A CB  1 
ATOM   1125 C CG  . ARG   A 1 150 ? 13.844  59.037 -14.207 1.00 59.91  ? 806  ARG   A CG  1 
ATOM   1126 C CD  . ARG   A 1 150 ? 14.491  58.650 -15.525 1.00 67.48  ? 806  ARG   A CD  1 
ATOM   1127 N NE  . ARG   A 1 150 ? 15.953  58.778 -15.492 1.00 73.48  ? 806  ARG   A NE  1 
ATOM   1128 C CZ  . ARG   A 1 150 ? 16.791  57.816 -15.103 1.00 80.26  ? 806  ARG   A CZ  1 
ATOM   1129 N NH1 . ARG   A 1 150 ? 16.322  56.649 -14.675 1.00 63.10  ? 806  ARG   A NH1 1 
ATOM   1130 N NH2 . ARG   A 1 150 ? 18.103  58.024 -15.114 1.00 58.67  ? 806  ARG   A NH2 1 
ATOM   1131 N N   . ASP   A 1 151 ? 14.394  63.319 -12.895 1.00 53.91  ? 807  ASP   A N   1 
ATOM   1132 C CA  . ASP   A 1 151 ? 15.437  64.336 -12.843 1.00 55.04  ? 807  ASP   A CA  1 
ATOM   1133 C C   . ASP   A 1 151 ? 15.465  65.159 -11.535 1.00 59.39  ? 807  ASP   A C   1 
ATOM   1134 O O   . ASP   A 1 151 ? 16.304  66.063 -11.410 1.00 60.20  ? 807  ASP   A O   1 
ATOM   1135 C CB  . ASP   A 1 151 ? 15.351  65.253 -14.085 1.00 57.83  ? 807  ASP   A CB  1 
ATOM   1136 C CG  . ASP   A 1 151 ? 15.575  64.516 -15.393 1.00 75.29  ? 807  ASP   A CG  1 
ATOM   1137 O OD1 . ASP   A 1 151 ? 16.739  64.135 -15.671 1.00 77.69  ? 807  ASP   A OD1 1 
ATOM   1138 O OD2 . ASP   A 1 151 ? 14.589  64.310 -16.133 1.00 81.48  ? 807  ASP   A OD2 1 
ATOM   1139 N N   . SER   A 1 152 ? 14.604  64.825 -10.548 1.00 53.98  ? 808  SER   A N   1 
ATOM   1140 C CA  . SER   A 1 152 ? 14.562  65.544 -9.274  1.00 52.77  ? 808  SER   A CA  1 
ATOM   1141 C C   . SER   A 1 152 ? 15.765  65.223 -8.375  1.00 56.79  ? 808  SER   A C   1 
ATOM   1142 O O   . SER   A 1 152 ? 16.478  64.240 -8.622  1.00 57.12  ? 808  SER   A O   1 
ATOM   1143 C CB  . SER   A 1 152 ? 13.246  65.292 -8.547  1.00 55.10  ? 808  SER   A CB  1 
ATOM   1144 O OG  . SER   A 1 152 ? 13.116  63.947 -8.118  1.00 61.20  ? 808  SER   A OG  1 
ATOM   1145 N N   . GLU   A 1 153 ? 16.001  66.071 -7.344  1.00 52.24  ? 809  GLU   A N   1 
ATOM   1146 C CA  . GLU   A 1 153 ? 17.095  65.899 -6.385  1.00 51.44  ? 809  GLU   A CA  1 
ATOM   1147 C C   . GLU   A 1 153 ? 16.900  64.644 -5.527  1.00 50.94  ? 809  GLU   A C   1 
ATOM   1148 O O   . GLU   A 1 153 ? 17.850  63.874 -5.369  1.00 51.12  ? 809  GLU   A O   1 
ATOM   1149 C CB  . GLU   A 1 153 ? 17.274  67.153 -5.514  1.00 53.28  ? 809  GLU   A CB  1 
ATOM   1150 N N   . GLU   A 1 154 ? 15.669  64.419 -5.015  1.00 43.61  ? 810  GLU   A N   1 
ATOM   1151 C CA  . GLU   A 1 154 ? 15.323  63.241 -4.205  1.00 42.02  ? 810  GLU   A CA  1 
ATOM   1152 C C   . GLU   A 1 154 ? 15.556  61.928 -4.967  1.00 41.35  ? 810  GLU   A C   1 
ATOM   1153 O O   . GLU   A 1 154 ? 16.077  60.991 -4.378  1.00 40.68  ? 810  GLU   A O   1 
ATOM   1154 C CB  . GLU   A 1 154 ? 13.902  63.327 -3.605  1.00 43.28  ? 810  GLU   A CB  1 
ATOM   1155 C CG  . GLU   A 1 154 ? 12.788  63.543 -4.618  1.00 53.86  ? 810  GLU   A CG  1 
ATOM   1156 C CD  . GLU   A 1 154 ? 11.414  63.914 -4.082  1.00 67.01  ? 810  GLU   A CD  1 
ATOM   1157 O OE1 . GLU   A 1 154 ? 11.248  64.006 -2.845  1.00 44.89  ? 810  GLU   A OE1 1 
ATOM   1158 O OE2 . GLU   A 1 154 ? 10.497  64.114 -4.911  1.00 65.03  ? 810  GLU   A OE2 1 
ATOM   1159 N N   . ALA   A 1 155 ? 15.250  61.905 -6.285  1.00 35.21  ? 811  ALA   A N   1 
ATOM   1160 C CA  . ALA   A 1 155 ? 15.447  60.767 -7.191  1.00 34.14  ? 811  ALA   A CA  1 
ATOM   1161 C C   . ALA   A 1 155 ? 16.931  60.458 -7.394  1.00 36.24  ? 811  ALA   A C   1 
ATOM   1162 O O   . ALA   A 1 155 ? 17.305  59.297 -7.494  1.00 33.22  ? 811  ALA   A O   1 
ATOM   1163 C CB  . ALA   A 1 155 ? 14.796  61.051 -8.540  1.00 34.66  ? 811  ALA   A CB  1 
ATOM   1164 N N   . GLU   A 1 156 ? 17.766  61.519 -7.480  1.00 35.45  ? 812  GLU   A N   1 
ATOM   1165 C CA  . GLU   A 1 156 ? 19.225  61.440 -7.635  1.00 35.75  ? 812  GLU   A CA  1 
ATOM   1166 C C   . GLU   A 1 156 ? 19.854  60.813 -6.392  1.00 35.98  ? 812  GLU   A C   1 
ATOM   1167 O O   . GLU   A 1 156 ? 20.694  59.927 -6.530  1.00 34.94  ? 812  GLU   A O   1 
ATOM   1168 C CB  . GLU   A 1 156 ? 19.826  62.837 -7.898  1.00 37.86  ? 812  GLU   A CB  1 
ATOM   1169 C CG  . GLU   A 1 156 ? 19.644  63.331 -9.329  1.00 52.30  ? 812  GLU   A CG  1 
ATOM   1170 C CD  . GLU   A 1 156 ? 19.976  64.789 -9.601  1.00 81.23  ? 812  GLU   A CD  1 
ATOM   1171 O OE1 . GLU   A 1 156 ? 20.850  65.356 -8.902  1.00 76.02  ? 812  GLU   A OE1 1 
ATOM   1172 O OE2 . GLU   A 1 156 ? 19.363  65.364 -10.531 1.00 79.59  ? 812  GLU   A OE2 1 
ATOM   1173 N N   . ILE   A 1 157 ? 19.415  61.255 -5.189  1.00 30.77  ? 813  ILE   A N   1 
ATOM   1174 C CA  . ILE   A 1 157 ? 19.868  60.764 -3.880  1.00 28.80  ? 813  ILE   A CA  1 
ATOM   1175 C C   . ILE   A 1 157 ? 19.486  59.285 -3.697  1.00 29.67  ? 813  ILE   A C   1 
ATOM   1176 O O   . ILE   A 1 157 ? 20.310  58.488 -3.225  1.00 28.38  ? 813  ILE   A O   1 
ATOM   1177 C CB  . ILE   A 1 157 ? 19.307  61.674 -2.732  1.00 30.69  ? 813  ILE   A CB  1 
ATOM   1178 C CG1 . ILE   A 1 157 ? 20.124  62.975 -2.618  1.00 30.22  ? 813  ILE   A CG1 1 
ATOM   1179 C CG2 . ILE   A 1 157 ? 19.232  60.937 -1.373  1.00 30.07  ? 813  ILE   A CG2 1 
ATOM   1180 C CD1 . ILE   A 1 157 ? 19.355  64.146 -2.055  1.00 39.46  ? 813  ILE   A CD1 1 
ATOM   1181 N N   . ILE   A 1 158 ? 18.236  58.935 -4.066  1.00 24.21  ? 814  ILE   A N   1 
ATOM   1182 C CA  . ILE   A 1 158 ? 17.681  57.573 -3.964  1.00 23.79  ? 814  ILE   A CA  1 
ATOM   1183 C C   . ILE   A 1 158 ? 18.465  56.614 -4.866  1.00 26.82  ? 814  ILE   A C   1 
ATOM   1184 O O   . ILE   A 1 158 ? 18.799  55.508 -4.435  1.00 25.53  ? 814  ILE   A O   1 
ATOM   1185 C CB  . ILE   A 1 158 ? 16.151  57.572 -4.234  1.00 27.12  ? 814  ILE   A CB  1 
ATOM   1186 C CG1 . ILE   A 1 158 ? 15.387  58.276 -3.084  1.00 27.20  ? 814  ILE   A CG1 1 
ATOM   1187 C CG2 . ILE   A 1 158 ? 15.614  56.156 -4.450  1.00 28.22  ? 814  ILE   A CG2 1 
ATOM   1188 C CD1 . ILE   A 1 158 ? 13.986  58.624 -3.414  1.00 35.00  ? 814  ILE   A CD1 1 
ATOM   1189 N N   . ARG   A 1 159 ? 18.759  57.054 -6.115  1.00 24.47  ? 815  ARG   A N   1 
ATOM   1190 C CA  . ARG   A 1 159 ? 19.514  56.276 -7.106  1.00 24.36  ? 815  ARG   A CA  1 
ATOM   1191 C C   . ARG   A 1 159 ? 20.954  56.070 -6.675  1.00 24.63  ? 815  ARG   A C   1 
ATOM   1192 O O   . ARG   A 1 159 ? 21.548  55.066 -7.047  1.00 24.61  ? 815  ARG   A O   1 
ATOM   1193 C CB  . ARG   A 1 159 ? 19.459  56.940 -8.490  1.00 25.84  ? 815  ARG   A CB  1 
ATOM   1194 C CG  . ARG   A 1 159 ? 18.191  56.630 -9.293  1.00 37.68  ? 815  ARG   A CG  1 
ATOM   1195 C CD  . ARG   A 1 159 ? 18.349  57.032 -10.761 1.00 48.49  ? 815  ARG   A CD  1 
ATOM   1196 N NE  . ARG   A 1 159 ? 18.681  58.456 -10.900 1.00 55.31  ? 815  ARG   A NE  1 
ATOM   1197 C CZ  . ARG   A 1 159 ? 17.800  59.398 -11.224 1.00 70.32  ? 815  ARG   A CZ  1 
ATOM   1198 N NH1 . ARG   A 1 159 ? 16.543  59.075 -11.500 1.00 60.33  ? 815  ARG   A NH1 1 
ATOM   1199 N NH2 . ARG   A 1 159 ? 18.171  60.671 -11.280 1.00 55.69  ? 815  ARG   A NH2 1 
ATOM   1200 N N   . LYS   A 1 160 ? 21.530  57.023 -5.906  1.00 20.74  ? 816  LYS   A N   1 
ATOM   1201 C CA  . LYS   A 1 160 ? 22.910  56.922 -5.411  1.00 20.92  ? 816  LYS   A CA  1 
ATOM   1202 C C   . LYS   A 1 160 ? 22.985  55.906 -4.243  1.00 22.72  ? 816  LYS   A C   1 
ATOM   1203 O O   . LYS   A 1 160 ? 23.930  55.129 -4.176  1.00 21.18  ? 816  LYS   A O   1 
ATOM   1204 C CB  . LYS   A 1 160 ? 23.456  58.301 -5.013  1.00 22.42  ? 816  LYS   A CB  1 
ATOM   1205 C CG  . LYS   A 1 160 ? 24.965  58.371 -4.991  1.00 21.86  ? 816  LYS   A CG  1 
ATOM   1206 C CD  . LYS   A 1 160 ? 25.443  59.795 -4.870  1.00 29.34  ? 816  LYS   A CD  1 
ATOM   1207 C CE  . LYS   A 1 160 ? 26.959  59.877 -4.857  1.00 35.06  ? 816  LYS   A CE  1 
ATOM   1208 N NZ  . LYS   A 1 160 ? 27.438  61.207 -4.425  1.00 37.34  ? 816  LYS   A NZ  1 
ATOM   1209 N N   . TYR   A 1 161 ? 21.946  55.885 -3.384  1.00 19.63  ? 817  TYR   A N   1 
ATOM   1210 C CA  . TYR   A 1 161 ? 21.787  54.969 -2.253  1.00 18.68  ? 817  TYR   A CA  1 
ATOM   1211 C C   . TYR   A 1 161 ? 21.742  53.520 -2.762  1.00 21.79  ? 817  TYR   A C   1 
ATOM   1212 O O   . TYR   A 1 161 ? 22.481  52.683 -2.253  1.00 20.02  ? 817  TYR   A O   1 
ATOM   1213 C CB  . TYR   A 1 161 ? 20.505  55.332 -1.492  1.00 19.30  ? 817  TYR   A CB  1 
ATOM   1214 C CG  . TYR   A 1 161 ? 20.396  54.910 -0.034  1.00 21.10  ? 817  TYR   A CG  1 
ATOM   1215 C CD1 . TYR   A 1 161 ? 21.389  54.137 0.574   1.00 22.67  ? 817  TYR   A CD1 1 
ATOM   1216 C CD2 . TYR   A 1 161 ? 19.300  55.285 0.738   1.00 21.77  ? 817  TYR   A CD2 1 
ATOM   1217 C CE1 . TYR   A 1 161 ? 21.279  53.737 1.907   1.00 23.09  ? 817  TYR   A CE1 1 
ATOM   1218 C CE2 . TYR   A 1 161 ? 19.183  54.894 2.070   1.00 22.82  ? 817  TYR   A CE2 1 
ATOM   1219 C CZ  . TYR   A 1 161 ? 20.170  54.117 2.650   1.00 25.33  ? 817  TYR   A CZ  1 
ATOM   1220 O OH  . TYR   A 1 161 ? 20.020  53.750 3.964   1.00 20.45  ? 817  TYR   A OH  1 
ATOM   1221 N N   . VAL   A 1 162 ? 20.935  53.253 -3.821  1.00 19.73  ? 818  VAL   A N   1 
ATOM   1222 C CA  . VAL   A 1 162 ? 20.825  51.956 -4.497  1.00 19.65  ? 818  VAL   A CA  1 
ATOM   1223 C C   . VAL   A 1 162 ? 22.187  51.581 -5.097  1.00 26.22  ? 818  VAL   A C   1 
ATOM   1224 O O   . VAL   A 1 162 ? 22.724  50.516 -4.783  1.00 27.83  ? 818  VAL   A O   1 
ATOM   1225 C CB  . VAL   A 1 162 ? 19.707  51.960 -5.579  1.00 22.31  ? 818  VAL   A CB  1 
ATOM   1226 C CG1 . VAL   A 1 162 ? 19.649  50.627 -6.333  1.00 21.20  ? 818  VAL   A CG1 1 
ATOM   1227 C CG2 . VAL   A 1 162 ? 18.346  52.274 -4.969  1.00 22.48  ? 818  VAL   A CG2 1 
ATOM   1228 N N   . LYS   A 1 163 ? 22.755  52.492 -5.919  1.00 23.47  ? 819  LYS   A N   1 
ATOM   1229 C CA  . LYS   A 1 163 ? 24.046  52.341 -6.597  1.00 23.56  ? 819  LYS   A CA  1 
ATOM   1230 C C   . LYS   A 1 163 ? 25.240  52.029 -5.645  1.00 28.46  ? 819  LYS   A C   1 
ATOM   1231 O O   . LYS   A 1 163 ? 26.013  51.123 -5.932  1.00 29.38  ? 819  LYS   A O   1 
ATOM   1232 C CB  . LYS   A 1 163 ? 24.313  53.592 -7.457  1.00 25.67  ? 819  LYS   A CB  1 
ATOM   1233 C CG  . LYS   A 1 163 ? 25.556  53.557 -8.338  1.00 39.83  ? 819  LYS   A CG  1 
ATOM   1234 C CD  . LYS   A 1 163 ? 25.644  54.844 -9.168  1.00 43.52  ? 819  LYS   A CD  1 
ATOM   1235 C CE  . LYS   A 1 163 ? 26.964  55.605 -9.111  1.00 50.19  ? 819  LYS   A CE  1 
ATOM   1236 N NZ  . LYS   A 1 163 ? 28.072  54.885 -9.801  1.00 44.80  ? 819  LYS   A NZ  1 
ATOM   1237 N N   . ASN   A 1 164 ? 25.384  52.777 -4.539  1.00 23.90  ? 820  ASN   A N   1 
ATOM   1238 C CA  . ASN   A 1 164 ? 26.519  52.658 -3.631  1.00 23.05  ? 820  ASN   A CA  1 
ATOM   1239 C C   . ASN   A 1 164 ? 26.441  51.629 -2.505  1.00 24.67  ? 820  ASN   A C   1 
ATOM   1240 O O   . ASN   A 1 164 ? 27.490  51.325 -1.941  1.00 23.83  ? 820  ASN   A O   1 
ATOM   1241 C CB  . ASN   A 1 164 ? 26.824  54.012 -2.995  1.00 25.11  ? 820  ASN   A CB  1 
ATOM   1242 C CG  . ASN   A 1 164 ? 27.317  55.104 -3.919  1.00 38.40  ? 820  ASN   A CG  1 
ATOM   1243 O OD1 . ASN   A 1 164 ? 27.733  54.886 -5.071  1.00 33.42  ? 820  ASN   A OD1 1 
ATOM   1244 N ND2 . ASN   A 1 164 ? 27.306  56.311 -3.400  1.00 26.25  ? 820  ASN   A ND2 1 
ATOM   1245 N N   . THR   A 1 165 ? 25.245  51.135 -2.134  1.00 19.38  ? 821  THR   A N   1 
ATOM   1246 C CA  . THR   A 1 165 ? 25.137  50.233 -0.986  1.00 18.30  ? 821  THR   A CA  1 
ATOM   1247 C C   . THR   A 1 165 ? 24.751  48.785 -1.383  1.00 21.25  ? 821  THR   A C   1 
ATOM   1248 O O   . THR   A 1 165 ? 24.177  48.043 -0.586  1.00 20.33  ? 821  THR   A O   1 
ATOM   1249 C CB  . THR   A 1 165 ? 24.206  50.844 0.123   1.00 26.66  ? 821  THR   A CB  1 
ATOM   1250 O OG1 . THR   A 1 165 ? 22.845  50.844 -0.307  1.00 22.41  ? 821  THR   A OG1 1 
ATOM   1251 C CG2 . THR   A 1 165 ? 24.644  52.257 0.582   1.00 19.72  ? 821  THR   A CG2 1 
ATOM   1252 N N   . HIS   A 1 166 ? 25.110  48.367 -2.589  1.00 20.12  ? 822  HIS   A N   1 
ATOM   1253 C CA  . HIS   A 1 166 ? 24.898  46.984 -3.017  1.00 19.47  ? 822  HIS   A CA  1 
ATOM   1254 C C   . HIS   A 1 166 ? 26.183  46.227 -2.644  1.00 20.18  ? 822  HIS   A C   1 
ATOM   1255 O O   . HIS   A 1 166 ? 27.237  46.545 -3.161  1.00 17.14  ? 822  HIS   A O   1 
ATOM   1256 C CB  . HIS   A 1 166 ? 24.598  46.892 -4.528  1.00 20.34  ? 822  HIS   A CB  1 
ATOM   1257 C CG  . HIS   A 1 166 ? 24.171  45.519 -4.985  1.00 24.17  ? 822  HIS   A CG  1 
ATOM   1258 N ND1 . HIS   A 1 166 ? 23.080  45.346 -5.810  1.00 26.33  ? 822  HIS   A ND1 1 
ATOM   1259 C CD2 . HIS   A 1 166 ? 24.736  44.304 -4.754  1.00 25.70  ? 822  HIS   A CD2 1 
ATOM   1260 C CE1 . HIS   A 1 166 ? 23.004  44.042 -6.035  1.00 25.71  ? 822  HIS   A CE1 1 
ATOM   1261 N NE2 . HIS   A 1 166 ? 23.981  43.378 -5.417  1.00 25.58  ? 822  HIS   A NE2 1 
ATOM   1262 N N   . ALA   A 1 167 ? 26.091  45.256 -1.725  1.00 15.77  ? 823  ALA   A N   1 
ATOM   1263 C CA  . ALA   A 1 167 ? 27.224  44.481 -1.227  1.00 14.20  ? 823  ALA   A CA  1 
ATOM   1264 C C   . ALA   A 1 167 ? 27.806  43.485 -2.236  1.00 19.78  ? 823  ALA   A C   1 
ATOM   1265 O O   . ALA   A 1 167 ? 27.079  42.866 -3.013  1.00 18.07  ? 823  ALA   A O   1 
ATOM   1266 C CB  . ALA   A 1 167 ? 26.837  43.769 0.043   1.00 14.71  ? 823  ALA   A CB  1 
ATOM   1267 N N   . THR   A 1 168 ? 29.130  43.333 -2.213  1.00 19.87  ? 824  THR   A N   1 
ATOM   1268 C CA  . THR   A 1 168 ? 29.879  42.396 -3.062  1.00 20.23  ? 824  THR   A CA  1 
ATOM   1269 C C   . THR   A 1 168 ? 29.383  40.965 -2.845  1.00 25.26  ? 824  THR   A C   1 
ATOM   1270 O O   . THR   A 1 168 ? 29.219  40.243 -3.830  1.00 26.13  ? 824  THR   A O   1 
ATOM   1271 C CB  . THR   A 1 168 ? 31.398  42.508 -2.784  1.00 26.34  ? 824  THR   A CB  1 
ATOM   1272 O OG1 . THR   A 1 168 ? 31.822  43.836 -3.064  1.00 27.69  ? 824  THR   A OG1 1 
ATOM   1273 C CG2 . THR   A 1 168 ? 32.248  41.481 -3.583  1.00 16.31  ? 824  THR   A CG2 1 
ATOM   1274 N N   . THR   A 1 169 ? 29.083  40.571 -1.578  1.00 20.67  ? 825  THR   A N   1 
ATOM   1275 C CA  . THR   A 1 169 ? 28.611  39.204 -1.299  1.00 20.41  ? 825  THR   A CA  1 
ATOM   1276 C C   . THR   A 1 169 ? 27.212  38.923 -1.900  1.00 24.96  ? 825  THR   A C   1 
ATOM   1277 O O   . THR   A 1 169 ? 26.797  37.772 -1.945  1.00 26.63  ? 825  THR   A O   1 
ATOM   1278 C CB  . THR   A 1 169 ? 28.693  38.850 0.189   1.00 26.05  ? 825  THR   A CB  1 
ATOM   1279 O OG1 . THR   A 1 169 ? 27.649  39.514 0.896   1.00 32.10  ? 825  THR   A OG1 1 
ATOM   1280 C CG2 . THR   A 1 169 ? 30.058  39.167 0.809   1.00 22.79  ? 825  THR   A CG2 1 
ATOM   1281 N N   . HIS   A 1 170 ? 26.512  39.962 -2.385  1.00 20.78  ? 826  HIS   A N   1 
ATOM   1282 C CA  . HIS   A 1 170 ? 25.166  39.879 -2.994  1.00 19.43  ? 826  HIS   A CA  1 
ATOM   1283 C C   . HIS   A 1 170 ? 25.223  40.127 -4.522  1.00 27.31  ? 826  HIS   A C   1 
ATOM   1284 O O   . HIS   A 1 170 ? 24.213  40.522 -5.112  1.00 27.75  ? 826  HIS   A O   1 
ATOM   1285 C CB  . HIS   A 1 170 ? 24.212  40.885 -2.298  1.00 18.05  ? 826  HIS   A CB  1 
ATOM   1286 C CG  . HIS   A 1 170 ? 24.048  40.668 -0.814  1.00 19.92  ? 826  HIS   A CG  1 
ATOM   1287 N ND1 . HIS   A 1 170 ? 23.697  41.710 0.034   1.00 21.10  ? 826  HIS   A ND1 1 
ATOM   1288 C CD2 . HIS   A 1 170 ? 24.229  39.548 -0.069  1.00 19.80  ? 826  HIS   A CD2 1 
ATOM   1289 C CE1 . HIS   A 1 170 ? 23.657  41.191 1.253   1.00 19.60  ? 826  HIS   A CE1 1 
ATOM   1290 N NE2 . HIS   A 1 170 ? 23.978  39.895 1.243   1.00 19.37  ? 826  HIS   A NE2 1 
ATOM   1291 N N   . ASN   A 1 171 ? 26.397  39.850 -5.154  1.00 25.82  ? 827  ASN   A N   1 
ATOM   1292 C CA  . ASN   A 1 171 ? 26.686  40.099 -6.574  1.00 26.56  ? 827  ASN   A CA  1 
ATOM   1293 C C   . ASN   A 1 171 ? 26.058  39.110 -7.596  1.00 29.27  ? 827  ASN   A C   1 
ATOM   1294 O O   . ASN   A 1 171 ? 26.184  39.365 -8.791  1.00 27.89  ? 827  ASN   A O   1 
ATOM   1295 C CB  . ASN   A 1 171 ? 28.209  40.217 -6.823  1.00 31.07  ? 827  ASN   A CB  1 
ATOM   1296 C CG  . ASN   A 1 171 ? 28.999  38.944 -6.692  1.00 37.88  ? 827  ASN   A CG  1 
ATOM   1297 O OD1 . ASN   A 1 171 ? 28.581  37.966 -6.070  1.00 36.27  ? 827  ASN   A OD1 1 
ATOM   1298 N ND2 . ASN   A 1 171 ? 30.173  38.942 -7.277  1.00 34.55  ? 827  ASN   A ND2 1 
ATOM   1299 N N   . ALA   A 1 172 ? 25.332  38.061 -7.152  1.00 25.81  ? 828  ALA   A N   1 
ATOM   1300 C CA  . ALA   A 1 172 ? 24.630  37.119 -8.047  1.00 25.39  ? 828  ALA   A CA  1 
ATOM   1301 C C   . ALA   A 1 172 ? 23.496  37.845 -8.839  1.00 29.35  ? 828  ALA   A C   1 
ATOM   1302 O O   . ALA   A 1 172 ? 22.828  37.238 -9.688  1.00 29.97  ? 828  ALA   A O   1 
ATOM   1303 C CB  . ALA   A 1 172 ? 24.034  35.975 -7.227  1.00 26.19  ? 828  ALA   A CB  1 
ATOM   1304 N N   . TYR   A 1 173 ? 23.254  39.127 -8.514  1.00 24.15  ? 829  TYR   A N   1 
ATOM   1305 C CA  . TYR   A 1 173 ? 22.260  39.986 -9.166  1.00 22.65  ? 829  TYR   A CA  1 
ATOM   1306 C C   . TYR   A 1 173 ? 22.672  41.445 -9.071  1.00 26.67  ? 829  TYR   A C   1 
ATOM   1307 O O   . TYR   A 1 173 ? 23.399  41.824 -8.157  1.00 26.27  ? 829  TYR   A O   1 
ATOM   1308 C CB  . TYR   A 1 173 ? 20.825  39.778 -8.597  1.00 21.09  ? 829  TYR   A CB  1 
ATOM   1309 C CG  . TYR   A 1 173 ? 20.620  40.279 -7.180  1.00 19.20  ? 829  TYR   A CG  1 
ATOM   1310 C CD1 . TYR   A 1 173 ? 20.227  41.598 -6.933  1.00 20.46  ? 829  TYR   A CD1 1 
ATOM   1311 C CD2 . TYR   A 1 173 ? 20.797  39.429 -6.084  1.00 19.35  ? 829  TYR   A CD2 1 
ATOM   1312 C CE1 . TYR   A 1 173 ? 20.033  42.067 -5.634  1.00 17.94  ? 829  TYR   A CE1 1 
ATOM   1313 C CE2 . TYR   A 1 173 ? 20.610  39.889 -4.778  1.00 20.87  ? 829  TYR   A CE2 1 
ATOM   1314 C CZ  . TYR   A 1 173 ? 20.222  41.209 -4.562  1.00 24.22  ? 829  TYR   A CZ  1 
ATOM   1315 O OH  . TYR   A 1 173 ? 20.030  41.674 -3.295  1.00 15.63  ? 829  TYR   A OH  1 
ATOM   1316 N N   . ASP   A 1 174 ? 22.148  42.269 -9.977  1.00 25.32  ? 830  ASP   A N   1 
ATOM   1317 C CA  . ASP   A 1 174 ? 22.313  43.717 -9.969  1.00 24.92  ? 830  ASP   A CA  1 
ATOM   1318 C C   . ASP   A 1 174 ? 20.920  44.281 -9.861  1.00 25.34  ? 830  ASP   A C   1 
ATOM   1319 O O   . ASP   A 1 174 ? 19.947  43.542 -9.960  1.00 24.64  ? 830  ASP   A O   1 
ATOM   1320 C CB  . ASP   A 1 174 ? 23.087  44.258 -11.190 1.00 27.98  ? 830  ASP   A CB  1 
ATOM   1321 C CG  . ASP   A 1 174 ? 22.458  43.964 -12.523 1.00 50.23  ? 830  ASP   A CG  1 
ATOM   1322 O OD1 . ASP   A 1 174 ? 21.569  44.746 -12.947 1.00 54.32  ? 830  ASP   A OD1 1 
ATOM   1323 O OD2 . ASP   A 1 174 ? 22.857  42.960 -13.154 1.00 62.05  ? 830  ASP   A OD2 1 
ATOM   1324 N N   . LEU   A 1 175 ? 20.824  45.547 -9.559  1.00 20.84  ? 831  LEU   A N   1 
ATOM   1325 C CA  . LEU   A 1 175 ? 19.548  46.202 -9.360  1.00 21.79  ? 831  LEU   A CA  1 
ATOM   1326 C C   . LEU   A 1 175 ? 19.360  47.342 -10.316 1.00 28.51  ? 831  LEU   A C   1 
ATOM   1327 O O   . LEU   A 1 175 ? 20.265  48.164 -10.507 1.00 28.68  ? 831  LEU   A O   1 
ATOM   1328 C CB  . LEU   A 1 175 ? 19.454  46.730 -7.920  1.00 21.72  ? 831  LEU   A CB  1 
ATOM   1329 C CG  . LEU   A 1 175 ? 19.289  45.708 -6.807  1.00 23.65  ? 831  LEU   A CG  1 
ATOM   1330 C CD1 . LEU   A 1 175 ? 19.480  46.361 -5.472  1.00 22.56  ? 831  LEU   A CD1 1 
ATOM   1331 C CD2 . LEU   A 1 175 ? 17.932  45.011 -6.893  1.00 22.51  ? 831  LEU   A CD2 1 
ATOM   1332 N N   . GLU   A 1 176 ? 18.172  47.406 -10.903 1.00 27.50  ? 832  GLU   A N   1 
ATOM   1333 C CA  . GLU   A 1 176 ? 17.768  48.477 -11.803 1.00 28.76  ? 832  GLU   A CA  1 
ATOM   1334 C C   . GLU   A 1 176 ? 16.481  49.099 -11.249 1.00 32.39  ? 832  GLU   A C   1 
ATOM   1335 O O   . GLU   A 1 176 ? 15.479  48.402 -11.100 1.00 31.26  ? 832  GLU   A O   1 
ATOM   1336 C CB  . GLU   A 1 176 ? 17.540  47.935 -13.224 1.00 30.56  ? 832  GLU   A CB  1 
ATOM   1337 C CG  . GLU   A 1 176 ? 17.461  49.012 -14.295 1.00 37.07  ? 832  GLU   A CG  1 
ATOM   1338 C CD  . GLU   A 1 176 ? 16.835  48.551 -15.596 1.00 55.00  ? 832  GLU   A CD  1 
ATOM   1339 O OE1 . GLU   A 1 176 ? 15.951  49.276 -16.105 1.00 51.75  ? 832  GLU   A OE1 1 
ATOM   1340 O OE2 . GLU   A 1 176 ? 17.208  47.466 -16.100 1.00 53.94  ? 832  GLU   A OE2 1 
ATOM   1341 N N   . VAL   A 1 177 ? 16.523  50.396 -10.926 1.00 30.22  ? 833  VAL   A N   1 
ATOM   1342 C CA  . VAL   A 1 177 ? 15.364  51.127 -10.404 1.00 29.94  ? 833  VAL   A CA  1 
ATOM   1343 C C   . VAL   A 1 177 ? 14.409  51.391 -11.552 1.00 34.00  ? 833  VAL   A C   1 
ATOM   1344 O O   . VAL   A 1 177 ? 14.785  52.085 -12.495 1.00 34.09  ? 833  VAL   A O   1 
ATOM   1345 C CB  . VAL   A 1 177 ? 15.723  52.450 -9.661  1.00 32.92  ? 833  VAL   A CB  1 
ATOM   1346 C CG1 . VAL   A 1 177 ? 14.516  52.980 -8.886  1.00 32.37  ? 833  VAL   A CG1 1 
ATOM   1347 C CG2 . VAL   A 1 177 ? 16.935  52.287 -8.741  1.00 32.40  ? 833  VAL   A CG2 1 
ATOM   1348 N N   . ILE   A 1 178 ? 13.194  50.826 -11.489 1.00 31.36  ? 834  ILE   A N   1 
ATOM   1349 C CA  . ILE   A 1 178 ? 12.182  51.042 -12.529 1.00 30.90  ? 834  ILE   A CA  1 
ATOM   1350 C C   . ILE   A 1 178 ? 11.369  52.313 -12.198 1.00 33.31  ? 834  ILE   A C   1 
ATOM   1351 O O   . ILE   A 1 178 ? 11.270  53.232 -13.026 1.00 31.95  ? 834  ILE   A O   1 
ATOM   1352 C CB  . ILE   A 1 178 ? 11.271  49.799 -12.749 1.00 34.24  ? 834  ILE   A CB  1 
ATOM   1353 C CG1 . ILE   A 1 178 ? 12.081  48.512 -13.091 1.00 34.59  ? 834  ILE   A CG1 1 
ATOM   1354 C CG2 . ILE   A 1 178 ? 10.170  50.090 -13.801 1.00 35.19  ? 834  ILE   A CG2 1 
ATOM   1355 C CD1 . ILE   A 1 178 ? 12.752  48.347 -14.628 1.00 39.61  ? 834  ILE   A CD1 1 
ATOM   1356 N N   . ASP   A 1 179 ? 10.792  52.349 -10.988 1.00 28.44  ? 835  ASP   A N   1 
ATOM   1357 C CA  . ASP   A 1 179 ? 9.978   53.466 -10.531 1.00 27.77  ? 835  ASP   A CA  1 
ATOM   1358 C C   . ASP   A 1 179 ? 10.295  53.854 -9.096  1.00 29.50  ? 835  ASP   A C   1 
ATOM   1359 O O   . ASP   A 1 179 ? 10.650  52.998 -8.278  1.00 29.78  ? 835  ASP   A O   1 
ATOM   1360 C CB  . ASP   A 1 179 ? 8.494   53.083 -10.614 1.00 30.06  ? 835  ASP   A CB  1 
ATOM   1361 C CG  . ASP   A 1 179 ? 7.933   52.910 -12.014 1.00 46.00  ? 835  ASP   A CG  1 
ATOM   1362 O OD1 . ASP   A 1 179 ? 7.991   53.884 -12.806 1.00 47.48  ? 835  ASP   A OD1 1 
ATOM   1363 O OD2 . ASP   A 1 179 ? 7.391   51.819 -12.304 1.00 54.32  ? 835  ASP   A OD2 1 
ATOM   1364 N N   . ILE   A 1 180 ? 10.141  55.146 -8.794  1.00 24.59  ? 836  ILE   A N   1 
ATOM   1365 C CA  . ILE   A 1 180 ? 10.280  55.695 -7.450  1.00 24.67  ? 836  ILE   A CA  1 
ATOM   1366 C C   . ILE   A 1 180 ? 8.941   56.312 -7.077  1.00 28.43  ? 836  ILE   A C   1 
ATOM   1367 O O   . ILE   A 1 180 ? 8.436   57.178 -7.802  1.00 29.36  ? 836  ILE   A O   1 
ATOM   1368 C CB  . ILE   A 1 180 ? 11.446  56.710 -7.281  1.00 28.73  ? 836  ILE   A CB  1 
ATOM   1369 C CG1 . ILE   A 1 180 ? 12.816  56.102 -7.712  1.00 29.17  ? 836  ILE   A CG1 1 
ATOM   1370 C CG2 . ILE   A 1 180 ? 11.486  57.197 -5.818  1.00 31.20  ? 836  ILE   A CG2 1 
ATOM   1371 C CD1 . ILE   A 1 180 ? 14.006  57.125 -7.844  1.00 33.87  ? 836  ILE   A CD1 1 
ATOM   1372 N N   . PHE   A 1 181 ? 8.346   55.856 -5.969  1.00 23.74  ? 837  PHE   A N   1 
ATOM   1373 C CA  . PHE   A 1 181 ? 7.083   56.414 -5.489  1.00 22.83  ? 837  PHE   A CA  1 
ATOM   1374 C C   . PHE   A 1 181 ? 7.279   57.152 -4.185  1.00 29.68  ? 837  PHE   A C   1 
ATOM   1375 O O   . PHE   A 1 181 ? 7.992   56.664 -3.306  1.00 29.30  ? 837  PHE   A O   1 
ATOM   1376 C CB  . PHE   A 1 181 ? 6.012   55.327 -5.312  1.00 23.62  ? 837  PHE   A CB  1 
ATOM   1377 C CG  . PHE   A 1 181 ? 5.739   54.519 -6.556  1.00 24.61  ? 837  PHE   A CG  1 
ATOM   1378 C CD1 . PHE   A 1 181 ? 4.927   55.018 -7.566  1.00 28.22  ? 837  PHE   A CD1 1 
ATOM   1379 C CD2 . PHE   A 1 181 ? 6.301   53.263 -6.722  1.00 26.23  ? 837  PHE   A CD2 1 
ATOM   1380 C CE1 . PHE   A 1 181 ? 4.695   54.272 -8.728  1.00 29.98  ? 837  PHE   A CE1 1 
ATOM   1381 C CE2 . PHE   A 1 181 ? 6.068   52.521 -7.884  1.00 30.05  ? 837  PHE   A CE2 1 
ATOM   1382 C CZ  . PHE   A 1 181 ? 5.259   53.023 -8.874  1.00 28.98  ? 837  PHE   A CZ  1 
ATOM   1383 N N   . LYS   A 1 182 ? 6.666   58.331 -4.057  1.00 28.66  ? 838  LYS   A N   1 
ATOM   1384 C CA  . LYS   A 1 182 ? 6.687   59.070 -2.799  1.00 29.22  ? 838  LYS   A CA  1 
ATOM   1385 C C   . LYS   A 1 182 ? 5.395   58.634 -2.129  1.00 32.67  ? 838  LYS   A C   1 
ATOM   1386 O O   . LYS   A 1 182 ? 4.334   58.768 -2.734  1.00 33.10  ? 838  LYS   A O   1 
ATOM   1387 C CB  . LYS   A 1 182 ? 6.726   60.592 -3.013  1.00 32.06  ? 838  LYS   A CB  1 
ATOM   1388 C CG  . LYS   A 1 182 ? 7.199   61.351 -1.778  1.00 42.54  ? 838  LYS   A CG  1 
ATOM   1389 C CD  . LYS   A 1 182 ? 6.763   62.809 -1.817  1.00 52.97  ? 838  LYS   A CD  1 
ATOM   1390 C CE  . LYS   A 1 182 ? 7.515   63.659 -0.822  1.00 64.92  ? 838  LYS   A CE  1 
ATOM   1391 N NZ  . LYS   A 1 182 ? 8.800   64.150 -1.382  1.00 74.34  ? 838  LYS   A NZ  1 
ATOM   1392 N N   . ILE   A 1 183 ? 5.484   58.007 -0.944  1.00 29.90  ? 839  ILE   A N   1 
ATOM   1393 C CA  . ILE   A 1 183 ? 4.295   57.473 -0.270  1.00 30.08  ? 839  ILE   A CA  1 
ATOM   1394 C C   . ILE   A 1 183 ? 3.988   58.186 1.062   1.00 35.48  ? 839  ILE   A C   1 
ATOM   1395 O O   . ILE   A 1 183 ? 4.901   58.555 1.812   1.00 35.92  ? 839  ILE   A O   1 
ATOM   1396 C CB  . ILE   A 1 183 ? 4.329   55.920 -0.124  1.00 32.67  ? 839  ILE   A CB  1 
ATOM   1397 C CG1 . ILE   A 1 183 ? 5.513   55.435 0.748   1.00 32.46  ? 839  ILE   A CG1 1 
ATOM   1398 C CG2 . ILE   A 1 183 ? 4.308   55.243 -1.514  1.00 33.00  ? 839  ILE   A CG2 1 
ATOM   1399 C CD1 . ILE   A 1 183 ? 5.428   53.987 1.207   1.00 35.51  ? 839  ILE   A CD1 1 
ATOM   1400 N N   . GLU   A 1 184 ? 2.681   58.391 1.317   1.00 31.53  ? 840  GLU   A N   1 
ATOM   1401 C CA  . GLU   A 1 184 ? 2.130   59.035 2.498   1.00 31.57  ? 840  GLU   A CA  1 
ATOM   1402 C C   . GLU   A 1 184 ? 0.932   58.233 3.013   1.00 35.20  ? 840  GLU   A C   1 
ATOM   1403 O O   . GLU   A 1 184 ? -0.177  58.354 2.485   1.00 35.92  ? 840  GLU   A O   1 
ATOM   1404 C CB  . GLU   A 1 184 ? 1.739   60.499 2.191   1.00 33.21  ? 840  GLU   A CB  1 
ATOM   1405 C CG  . GLU   A 1 184 ? 1.424   61.311 3.442   1.00 48.05  ? 840  GLU   A CG  1 
ATOM   1406 C CD  . GLU   A 1 184 ? 1.142   62.790 3.238   1.00 77.54  ? 840  GLU   A CD  1 
ATOM   1407 O OE1 . GLU   A 1 184 ? 1.955   63.470 2.570   1.00 75.65  ? 840  GLU   A OE1 1 
ATOM   1408 O OE2 . GLU   A 1 184 ? 0.119   63.275 3.774   1.00 70.21  ? 840  GLU   A OE2 1 
ATOM   1409 N N   . ARG   A 1 185 ? 1.160   57.407 4.043   1.00 29.89  ? 841  ARG   A N   1 
ATOM   1410 C CA  . ARG   A 1 185 ? 0.102   56.608 4.656   1.00 28.54  ? 841  ARG   A CA  1 
ATOM   1411 C C   . ARG   A 1 185 ? -0.742  57.517 5.522   1.00 32.04  ? 841  ARG   A C   1 
ATOM   1412 O O   . ARG   A 1 185 ? -0.205  58.354 6.259   1.00 32.02  ? 841  ARG   A O   1 
ATOM   1413 C CB  . ARG   A 1 185 ? 0.679   55.492 5.524   1.00 28.59  ? 841  ARG   A CB  1 
ATOM   1414 C CG  . ARG   A 1 185 ? 1.245   54.282 4.777   1.00 30.19  ? 841  ARG   A CG  1 
ATOM   1415 C CD  . ARG   A 1 185 ? 1.554   53.148 5.753   1.00 24.85  ? 841  ARG   A CD  1 
ATOM   1416 N NE  . ARG   A 1 185 ? 0.329   52.630 6.366   1.00 31.15  ? 841  ARG   A NE  1 
ATOM   1417 C CZ  . ARG   A 1 185 ? -0.056  52.850 7.619   1.00 35.47  ? 841  ARG   A CZ  1 
ATOM   1418 N NH1 . ARG   A 1 185 ? -1.215  52.387 8.051   1.00 22.87  ? 841  ARG   A NH1 1 
ATOM   1419 N NH2 . ARG   A 1 185 ? 0.719   53.535 8.451   1.00 24.86  ? 841  ARG   A NH2 1 
ATOM   1420 N N   . GLU   A 1 186 ? -2.067  57.367 5.418   1.00 28.53  ? 842  GLU   A N   1 
ATOM   1421 C CA  . GLU   A 1 186 ? -3.017  58.135 6.206   1.00 28.72  ? 842  GLU   A CA  1 
ATOM   1422 C C   . GLU   A 1 186 ? -2.789  57.855 7.712   1.00 32.81  ? 842  GLU   A C   1 
ATOM   1423 O O   . GLU   A 1 186 ? -2.667  56.689 8.124   1.00 32.24  ? 842  GLU   A O   1 
ATOM   1424 C CB  . GLU   A 1 186 ? -4.446  57.769 5.775   1.00 30.39  ? 842  GLU   A CB  1 
ATOM   1425 C CG  . GLU   A 1 186 ? -5.551  58.638 6.327   1.00 43.84  ? 842  GLU   A CG  1 
ATOM   1426 C CD  . GLU   A 1 186 ? -6.915  58.095 5.956   1.00 62.33  ? 842  GLU   A CD  1 
ATOM   1427 O OE1 . GLU   A 1 186 ? -7.461  58.522 4.914   1.00 59.01  ? 842  GLU   A OE1 1 
ATOM   1428 O OE2 . GLU   A 1 186 ? -7.427  57.222 6.693   1.00 49.66  ? 842  GLU   A OE2 1 
ATOM   1429 N N   . GLY   A 1 187 ? -2.646  58.937 8.481   1.00 28.16  ? 843  GLY   A N   1 
ATOM   1430 C CA  . GLY   A 1 187 ? -2.462  58.887 9.930   1.00 27.44  ? 843  GLY   A CA  1 
ATOM   1431 C C   . GLY   A 1 187 ? -1.045  58.666 10.427  1.00 28.96  ? 843  GLY   A C   1 
ATOM   1432 O O   . GLY   A 1 187 ? -0.738  58.941 11.590  1.00 24.82  ? 843  GLY   A O   1 
ATOM   1433 N N   . GLU   A 1 188 ? -0.175  58.167 9.552   1.00 28.43  ? 844  GLU   A N   1 
ATOM   1434 C CA  . GLU   A 1 188 ? 1.195   57.837 9.892   1.00 28.56  ? 844  GLU   A CA  1 
ATOM   1435 C C   . GLU   A 1 188 ? 2.011   59.047 10.357  1.00 36.46  ? 844  GLU   A C   1 
ATOM   1436 O O   . GLU   A 1 188 ? 2.719   58.942 11.359  1.00 35.64  ? 844  GLU   A O   1 
ATOM   1437 C CB  . GLU   A 1 188 ? 1.864   57.103 8.732   1.00 29.24  ? 844  GLU   A CB  1 
ATOM   1438 C CG  . GLU   A 1 188 ? 3.109   56.360 9.162   1.00 39.24  ? 844  GLU   A CG  1 
ATOM   1439 C CD  . GLU   A 1 188 ? 3.781   55.607 8.035   1.00 49.22  ? 844  GLU   A CD  1 
ATOM   1440 O OE1 . GLU   A 1 188 ? 4.371   56.254 7.137   1.00 35.54  ? 844  GLU   A OE1 1 
ATOM   1441 O OE2 . GLU   A 1 188 ? 3.714   54.359 8.057   1.00 37.00  ? 844  GLU   A OE2 1 
ATOM   1442 N N   . CYS   A 1 189 ? 1.875   60.187 9.662   1.00 36.58  ? 845  CYS   A N   1 
ATOM   1443 C CA  . CYS   A 1 189 ? 2.592   61.416 9.979   1.00 38.99  ? 845  CYS   A CA  1 
ATOM   1444 C C   . CYS   A 1 189 ? 2.260   61.949 11.384  1.00 41.98  ? 845  CYS   A C   1 
ATOM   1445 O O   . CYS   A 1 189 ? 3.157   62.433 12.080  1.00 43.33  ? 845  CYS   A O   1 
ATOM   1446 C CB  . CYS   A 1 189 ? 2.350   62.469 8.905   1.00 41.56  ? 845  CYS   A CB  1 
ATOM   1447 S SG  . CYS   A 1 189 ? 3.362   63.962 9.096   1.00 46.74  ? 845  CYS   A SG  1 
ATOM   1448 N N   . GLN   A 1 190 ? 0.987   61.831 11.804  1.00 35.22  ? 846  GLN   A N   1 
ATOM   1449 C CA  . GLN   A 1 190 ? 0.527   62.250 13.128  1.00 33.07  ? 846  GLN   A CA  1 
ATOM   1450 C C   . GLN   A 1 190 ? 1.035   61.262 14.201  1.00 30.92  ? 846  GLN   A C   1 
ATOM   1451 O O   . GLN   A 1 190 ? 1.408   61.693 15.296  1.00 29.84  ? 846  GLN   A O   1 
ATOM   1452 C CB  . GLN   A 1 190 ? -1.002  62.359 13.153  1.00 33.93  ? 846  GLN   A CB  1 
ATOM   1453 N N   . ARG   A 1 191 ? 1.065   59.950 13.869  1.00 22.47  ? 847  ARG   A N   1 
ATOM   1454 C CA  . ARG   A 1 191 ? 1.574   58.883 14.743  1.00 21.71  ? 847  ARG   A CA  1 
ATOM   1455 C C   . ARG   A 1 191 ? 3.076   59.104 15.055  1.00 23.54  ? 847  ARG   A C   1 
ATOM   1456 O O   . ARG   A 1 191 ? 3.511   58.883 16.184  1.00 22.43  ? 847  ARG   A O   1 
ATOM   1457 C CB  . ARG   A 1 191 ? 1.399   57.517 14.064  1.00 18.48  ? 847  ARG   A CB  1 
ATOM   1458 C CG  . ARG   A 1 191 ? 1.560   56.326 14.991  1.00 16.83  ? 847  ARG   A CG  1 
ATOM   1459 C CD  . ARG   A 1 191 ? 1.331   55.000 14.270  1.00 22.34  ? 847  ARG   A CD  1 
ATOM   1460 N NE  . ARG   A 1 191 ? 2.379   54.726 13.287  1.00 32.85  ? 847  ARG   A NE  1 
ATOM   1461 C CZ  . ARG   A 1 191 ? 2.391   53.703 12.434  1.00 52.90  ? 847  ARG   A CZ  1 
ATOM   1462 N NH1 . ARG   A 1 191 ? 1.405   52.819 12.433  1.00 46.40  ? 847  ARG   A NH1 1 
ATOM   1463 N NH2 . ARG   A 1 191 ? 3.397   53.554 11.583  1.00 44.90  ? 847  ARG   A NH2 1 
ATOM   1464 N N   . TYR   A 1 192 ? 3.836   59.547 14.046  1.00 18.80  ? 848  TYR   A N   1 
ATOM   1465 C CA  . TYR   A 1 192 ? 5.275   59.758 14.086  1.00 18.80  ? 848  TYR   A CA  1 
ATOM   1466 C C   . TYR   A 1 192 ? 5.708   60.996 14.859  1.00 25.38  ? 848  TYR   A C   1 
ATOM   1467 O O   . TYR   A 1 192 ? 6.824   61.015 15.368  1.00 25.27  ? 848  TYR   A O   1 
ATOM   1468 C CB  . TYR   A 1 192 ? 5.842   59.764 12.638  1.00 20.12  ? 848  TYR   A CB  1 
ATOM   1469 C CG  . TYR   A 1 192 ? 7.356   59.794 12.565  1.00 22.31  ? 848  TYR   A CG  1 
ATOM   1470 C CD1 . TYR   A 1 192 ? 8.111   58.665 12.864  1.00 23.64  ? 848  TYR   A CD1 1 
ATOM   1471 C CD2 . TYR   A 1 192 ? 8.037   60.961 12.209  1.00 23.29  ? 848  TYR   A CD2 1 
ATOM   1472 C CE1 . TYR   A 1 192 ? 9.506   58.687 12.803  1.00 25.67  ? 848  TYR   A CE1 1 
ATOM   1473 C CE2 . TYR   A 1 192 ? 9.433   60.988 12.122  1.00 23.74  ? 848  TYR   A CE2 1 
ATOM   1474 C CZ  . TYR   A 1 192 ? 10.162  59.848 12.428  1.00 26.62  ? 848  TYR   A CZ  1 
ATOM   1475 O OH  . TYR   A 1 192 ? 11.529  59.859 12.379  1.00 26.93  ? 848  TYR   A OH  1 
ATOM   1476 N N   . LYS   A 1 193 ? 4.833   62.026 14.963  1.00 27.68  ? 849  LYS   A N   1 
ATOM   1477 C CA  . LYS   A 1 193 ? 5.077   63.323 15.626  1.00 28.08  ? 849  LYS   A CA  1 
ATOM   1478 C C   . LYS   A 1 193 ? 5.932   63.246 16.934  1.00 32.05  ? 849  LYS   A C   1 
ATOM   1479 O O   . LYS   A 1 193 ? 6.908   63.999 16.994  1.00 32.72  ? 849  LYS   A O   1 
ATOM   1480 C CB  . LYS   A 1 193 ? 3.774   64.105 15.871  1.00 30.83  ? 849  LYS   A CB  1 
ATOM   1481 C CG  . LYS   A 1 193 ? 4.009   65.614 15.929  1.00 57.93  ? 849  LYS   A CG  1 
ATOM   1482 C CD  . LYS   A 1 193 ? 2.734   66.426 16.155  1.00 74.71  ? 849  LYS   A CD  1 
ATOM   1483 C CE  . LYS   A 1 193 ? 3.035   67.895 16.395  1.00 83.08  ? 849  LYS   A CE  1 
ATOM   1484 N NZ  . LYS   A 1 193 ? 1.807   68.739 16.356  1.00 93.30  ? 849  LYS   A NZ  1 
ATOM   1485 N N   . PRO   A 1 194 ? 5.670   62.373 17.957  1.00 26.70  ? 850  PRO   A N   1 
ATOM   1486 C CA  . PRO   A 1 194 ? 6.545   62.389 19.162  1.00 25.92  ? 850  PRO   A CA  1 
ATOM   1487 C C   . PRO   A 1 194 ? 8.023   62.030 18.917  1.00 28.01  ? 850  PRO   A C   1 
ATOM   1488 O O   . PRO   A 1 194 ? 8.869   62.255 19.774  1.00 27.16  ? 850  PRO   A O   1 
ATOM   1489 C CB  . PRO   A 1 194 ? 5.870   61.386 20.118  1.00 27.16  ? 850  PRO   A CB  1 
ATOM   1490 C CG  . PRO   A 1 194 ? 4.471   61.215 19.600  1.00 31.20  ? 850  PRO   A CG  1 
ATOM   1491 C CD  . PRO   A 1 194 ? 4.559   61.403 18.118  1.00 26.78  ? 850  PRO   A CD  1 
ATOM   1492 N N   . PHE   A 1 195 ? 8.324   61.495 17.737  1.00 24.06  ? 851  PHE   A N   1 
ATOM   1493 C CA  . PHE   A 1 195 ? 9.644   61.019 17.330  1.00 23.45  ? 851  PHE   A CA  1 
ATOM   1494 C C   . PHE   A 1 195 ? 10.245  61.845 16.185  1.00 27.78  ? 851  PHE   A C   1 
ATOM   1495 O O   . PHE   A 1 195 ? 11.388  61.593 15.806  1.00 26.52  ? 851  PHE   A O   1 
ATOM   1496 C CB  . PHE   A 1 195 ? 9.541   59.524 16.913  1.00 24.27  ? 851  PHE   A CB  1 
ATOM   1497 C CG  . PHE   A 1 195 ? 8.930   58.619 17.958  1.00 24.61  ? 851  PHE   A CG  1 
ATOM   1498 C CD1 . PHE   A 1 195 ? 9.702   58.104 18.994  1.00 28.09  ? 851  PHE   A CD1 1 
ATOM   1499 C CD2 . PHE   A 1 195 ? 7.579   58.298 17.918  1.00 26.63  ? 851  PHE   A CD2 1 
ATOM   1500 C CE1 . PHE   A 1 195 ? 9.130   57.294 19.981  1.00 29.02  ? 851  PHE   A CE1 1 
ATOM   1501 C CE2 . PHE   A 1 195 ? 7.002   57.506 18.914  1.00 30.10  ? 851  PHE   A CE2 1 
ATOM   1502 C CZ  . PHE   A 1 195 ? 7.784   56.990 19.926  1.00 28.49  ? 851  PHE   A CZ  1 
ATOM   1503 N N   . LYS   A 1 196 ? 9.480   62.827 15.653  1.00 26.55  ? 852  LYS   A N   1 
ATOM   1504 C CA  . LYS   A 1 196 ? 9.840   63.664 14.506  1.00 27.72  ? 852  LYS   A CA  1 
ATOM   1505 C C   . LYS   A 1 196 ? 11.135  64.473 14.681  1.00 33.82  ? 852  LYS   A C   1 
ATOM   1506 O O   . LYS   A 1 196 ? 11.825  64.692 13.687  1.00 34.07  ? 852  LYS   A O   1 
ATOM   1507 C CB  . LYS   A 1 196 ? 8.662   64.576 14.069  1.00 30.15  ? 852  LYS   A CB  1 
ATOM   1508 C CG  . LYS   A 1 196 ? 8.435   65.870 14.842  1.00 40.71  ? 852  LYS   A CG  1 
ATOM   1509 C CD  . LYS   A 1 196 ? 7.269   66.652 14.252  1.00 48.84  ? 852  LYS   A CD  1 
ATOM   1510 C CE  . LYS   A 1 196 ? 6.951   67.905 15.034  1.00 51.82  ? 852  LYS   A CE  1 
ATOM   1511 N NZ  . LYS   A 1 196 ? 5.760   68.607 14.483  1.00 55.39  ? 852  LYS   A NZ  1 
ATOM   1512 N N   . GLN   A 1 197 ? 11.464  64.914 15.908  1.00 31.42  ? 853  GLN   A N   1 
ATOM   1513 C CA  . GLN   A 1 197 ? 12.689  65.683 16.165  1.00 31.40  ? 853  GLN   A CA  1 
ATOM   1514 C C   . GLN   A 1 197 ? 13.751  64.892 16.977  1.00 33.90  ? 853  GLN   A C   1 
ATOM   1515 O O   . GLN   A 1 197 ? 14.770  65.468 17.392  1.00 33.18  ? 853  GLN   A O   1 
ATOM   1516 C CB  . GLN   A 1 197 ? 12.373  67.043 16.814  1.00 33.20  ? 853  GLN   A CB  1 
ATOM   1517 C CG  . GLN   A 1 197 ? 11.708  68.038 15.865  1.00 50.51  ? 853  GLN   A CG  1 
ATOM   1518 C CD  . GLN   A 1 197 ? 11.090  69.196 16.608  1.00 77.26  ? 853  GLN   A CD  1 
ATOM   1519 O OE1 . GLN   A 1 197 ? 9.862   69.323 16.695  1.00 77.13  ? 853  GLN   A OE1 1 
ATOM   1520 N NE2 . GLN   A 1 197 ? 11.923  70.073 17.160  1.00 68.66  ? 853  GLN   A NE2 1 
ATOM   1521 N N   . LEU   A 1 198 ? 13.527  63.570 17.163  1.00 28.64  ? 854  LEU   A N   1 
ATOM   1522 C CA  . LEU   A 1 198 ? 14.447  62.684 17.881  1.00 28.11  ? 854  LEU   A CA  1 
ATOM   1523 C C   . LEU   A 1 198 ? 15.814  62.652 17.189  1.00 32.23  ? 854  LEU   A C   1 
ATOM   1524 O O   . LEU   A 1 198 ? 15.903  62.930 15.992  1.00 31.65  ? 854  LEU   A O   1 
ATOM   1525 C CB  . LEU   A 1 198 ? 13.874  61.257 17.978  1.00 27.32  ? 854  LEU   A CB  1 
ATOM   1526 C CG  . LEU   A 1 198 ? 14.247  60.431 19.211  1.00 30.54  ? 854  LEU   A CG  1 
ATOM   1527 C CD1 . LEU   A 1 198 ? 13.543  60.964 20.468  1.00 31.01  ? 854  LEU   A CD1 1 
ATOM   1528 C CD2 . LEU   A 1 198 ? 13.873  58.958 19.004  1.00 29.55  ? 854  LEU   A CD2 1 
ATOM   1529 N N   . HIS   A 1 199 ? 16.881  62.376 17.948  1.00 29.41  ? 855  HIS   A N   1 
ATOM   1530 C CA  . HIS   A 1 199 ? 18.219  62.282 17.364  1.00 29.89  ? 855  HIS   A CA  1 
ATOM   1531 C C   . HIS   A 1 199 ? 18.345  60.928 16.686  1.00 33.11  ? 855  HIS   A C   1 
ATOM   1532 O O   . HIS   A 1 199 ? 17.503  60.063 16.928  1.00 33.35  ? 855  HIS   A O   1 
ATOM   1533 C CB  . HIS   A 1 199 ? 19.322  62.516 18.412  1.00 31.11  ? 855  HIS   A CB  1 
ATOM   1534 C CG  . HIS   A 1 199 ? 19.459  61.439 19.442  1.00 35.04  ? 855  HIS   A CG  1 
ATOM   1535 N ND1 . HIS   A 1 199 ? 18.444  61.163 20.357  1.00 37.55  ? 855  HIS   A ND1 1 
ATOM   1536 C CD2 . HIS   A 1 199 ? 20.510  60.631 19.701  1.00 37.32  ? 855  HIS   A CD2 1 
ATOM   1537 C CE1 . HIS   A 1 199 ? 18.903  60.176 21.110  1.00 37.19  ? 855  HIS   A CE1 1 
ATOM   1538 N NE2 . HIS   A 1 199 ? 20.142  59.826 20.754  1.00 37.49  ? 855  HIS   A NE2 1 
ATOM   1539 N N   . ASN   A 1 200 ? 19.352  60.734 15.810  1.00 27.77  ? 856  ASN   A N   1 
ATOM   1540 C CA  . ASN   A 1 200 ? 19.545  59.482 15.079  1.00 26.71  ? 856  ASN   A CA  1 
ATOM   1541 C C   . ASN   A 1 200 ? 18.329  59.140 14.179  1.00 30.28  ? 856  ASN   A C   1 
ATOM   1542 O O   . ASN   A 1 200 ? 17.801  58.028 14.263  1.00 28.64  ? 856  ASN   A O   1 
ATOM   1543 C CB  . ASN   A 1 200 ? 19.829  58.301 16.035  1.00 29.84  ? 856  ASN   A CB  1 
ATOM   1544 C CG  . ASN   A 1 200 ? 21.258  57.995 16.363  1.00 56.77  ? 856  ASN   A CG  1 
ATOM   1545 O OD1 . ASN   A 1 200 ? 21.792  58.399 17.404  1.00 42.68  ? 856  ASN   A OD1 1 
ATOM   1546 N ND2 . ASN   A 1 200 ? 21.880  57.202 15.516  1.00 57.51  ? 856  ASN   A ND2 1 
ATOM   1547 N N   . ARG   A 1 201 ? 17.882  60.075 13.324  1.00 26.81  ? 857  ARG   A N   1 
ATOM   1548 C CA  . ARG   A 1 201 ? 16.810  59.739 12.379  1.00 25.56  ? 857  ARG   A CA  1 
ATOM   1549 C C   . ARG   A 1 201 ? 17.464  59.405 11.050  1.00 29.83  ? 857  ARG   A C   1 
ATOM   1550 O O   . ARG   A 1 201 ? 18.171  60.245 10.471  1.00 29.22  ? 857  ARG   A O   1 
ATOM   1551 C CB  . ARG   A 1 201 ? 15.743  60.831 12.236  1.00 21.38  ? 857  ARG   A CB  1 
ATOM   1552 C CG  . ARG   A 1 201 ? 14.872  60.982 13.480  1.00 20.85  ? 857  ARG   A CG  1 
ATOM   1553 C CD  . ARG   A 1 201 ? 13.999  62.214 13.415  1.00 15.95  ? 857  ARG   A CD  1 
ATOM   1554 N NE  . ARG   A 1 201 ? 14.794  63.453 13.392  1.00 28.62  ? 857  ARG   A NE  1 
ATOM   1555 C CZ  . ARG   A 1 201 ? 14.776  64.342 12.398  1.00 44.11  ? 857  ARG   A CZ  1 
ATOM   1556 N NH1 . ARG   A 1 201 ? 13.984  64.159 11.346  1.00 31.59  ? 857  ARG   A NH1 1 
ATOM   1557 N NH2 . ARG   A 1 201 ? 15.526  65.432 12.462  1.00 36.48  ? 857  ARG   A NH2 1 
ATOM   1558 N N   . ARG   A 1 202 ? 17.288  58.147 10.610  1.00 25.64  ? 858  ARG   A N   1 
ATOM   1559 C CA  . ARG   A 1 202 ? 17.915  57.635 9.394   1.00 24.86  ? 858  ARG   A CA  1 
ATOM   1560 C C   . ARG   A 1 202 ? 16.940  57.121 8.370   1.00 24.92  ? 858  ARG   A C   1 
ATOM   1561 O O   . ARG   A 1 202 ? 15.918  56.560 8.739   1.00 23.29  ? 858  ARG   A O   1 
ATOM   1562 C CB  . ARG   A 1 202 ? 18.937  56.541 9.731   1.00 24.44  ? 858  ARG   A CB  1 
ATOM   1563 C CG  . ARG   A 1 202 ? 20.243  57.097 10.229  1.00 33.19  ? 858  ARG   A CG  1 
ATOM   1564 C CD  . ARG   A 1 202 ? 21.249  56.022 10.555  1.00 39.99  ? 858  ARG   A CD  1 
ATOM   1565 N NE  . ARG   A 1 202 ? 22.023  56.400 11.740  1.00 48.86  ? 858  ARG   A NE  1 
ATOM   1566 C CZ  . ARG   A 1 202 ? 23.008  55.682 12.262  1.00 64.18  ? 858  ARG   A CZ  1 
ATOM   1567 N NH1 . ARG   A 1 202 ? 23.383  54.544 11.694  1.00 52.83  ? 858  ARG   A NH1 1 
ATOM   1568 N NH2 . ARG   A 1 202 ? 23.636  56.103 13.349  1.00 56.50  ? 858  ARG   A NH2 1 
ATOM   1569 N N   . LEU   A 1 203 ? 17.281  57.297 7.084   1.00 19.82  ? 859  LEU   A N   1 
ATOM   1570 C CA  . LEU   A 1 203 ? 16.477  56.799 5.981   1.00 20.25  ? 859  LEU   A CA  1 
ATOM   1571 C C   . LEU   A 1 203 ? 17.043  55.422 5.656   1.00 22.82  ? 859  LEU   A C   1 
ATOM   1572 O O   . LEU   A 1 203 ? 18.180  55.310 5.212   1.00 21.02  ? 859  LEU   A O   1 
ATOM   1573 C CB  . LEU   A 1 203 ? 16.491  57.755 4.780   1.00 20.55  ? 859  LEU   A CB  1 
ATOM   1574 C CG  . LEU   A 1 203 ? 15.465  57.466 3.703   1.00 25.02  ? 859  LEU   A CG  1 
ATOM   1575 C CD1 . LEU   A 1 203 ? 14.068  57.976 4.089   1.00 24.82  ? 859  LEU   A CD1 1 
ATOM   1576 C CD2 . LEU   A 1 203 ? 15.929  58.024 2.358   1.00 28.95  ? 859  LEU   A CD2 1 
ATOM   1577 N N   . LEU   A 1 204 ? 16.278  54.375 5.992   1.00 18.90  ? 860  LEU   A N   1 
ATOM   1578 C CA  . LEU   A 1 204 ? 16.708  52.989 5.872   1.00 18.34  ? 860  LEU   A CA  1 
ATOM   1579 C C   . LEU   A 1 204 ? 15.800  52.161 4.987   1.00 21.23  ? 860  LEU   A C   1 
ATOM   1580 O O   . LEU   A 1 204 ? 14.649  52.535 4.753   1.00 21.12  ? 860  LEU   A O   1 
ATOM   1581 C CB  . LEU   A 1 204 ? 16.826  52.341 7.265   1.00 18.68  ? 860  LEU   A CB  1 
ATOM   1582 C CG  . LEU   A 1 204 ? 17.816  52.966 8.266   1.00 23.68  ? 860  LEU   A CG  1 
ATOM   1583 C CD1 . LEU   A 1 204 ? 17.494  52.563 9.674   1.00 23.39  ? 860  LEU   A CD1 1 
ATOM   1584 C CD2 . LEU   A 1 204 ? 19.277  52.666 7.906   1.00 25.81  ? 860  LEU   A CD2 1 
ATOM   1585 N N   . TRP   A 1 205 ? 16.336  51.028 4.510   1.00 15.99  ? 861  TRP   A N   1 
ATOM   1586 C CA  . TRP   A 1 205 ? 15.673  50.075 3.634   1.00 15.64  ? 861  TRP   A CA  1 
ATOM   1587 C C   . TRP   A 1 205 ? 14.874  49.031 4.394   1.00 19.38  ? 861  TRP   A C   1 
ATOM   1588 O O   . TRP   A 1 205 ? 15.293  48.545 5.447   1.00 17.60  ? 861  TRP   A O   1 
ATOM   1589 C CB  . TRP   A 1 205 ? 16.708  49.312 2.790   1.00 14.34  ? 861  TRP   A CB  1 
ATOM   1590 C CG  . TRP   A 1 205 ? 17.601  50.159 1.941   1.00 15.82  ? 861  TRP   A CG  1 
ATOM   1591 C CD1 . TRP   A 1 205 ? 18.922  50.424 2.151   1.00 18.64  ? 861  TRP   A CD1 1 
ATOM   1592 C CD2 . TRP   A 1 205 ? 17.242  50.832 0.726   1.00 15.59  ? 861  TRP   A CD2 1 
ATOM   1593 N NE1 . TRP   A 1 205 ? 19.415  51.199 1.128   1.00 18.36  ? 861  TRP   A NE1 1 
ATOM   1594 C CE2 . TRP   A 1 205 ? 18.395  51.502 0.263   1.00 19.45  ? 861  TRP   A CE2 1 
ATOM   1595 C CE3 . TRP   A 1 205 ? 16.056  50.918 -0.029  1.00 16.24  ? 861  TRP   A CE3 1 
ATOM   1596 C CZ2 . TRP   A 1 205 ? 18.403  52.244 -0.923  1.00 19.03  ? 861  TRP   A CZ2 1 
ATOM   1597 C CZ3 . TRP   A 1 205 ? 16.064  51.669 -1.193  1.00 17.21  ? 861  TRP   A CZ3 1 
ATOM   1598 C CH2 . TRP   A 1 205 ? 17.222  52.338 -1.619  1.00 17.80  ? 861  TRP   A CH2 1 
ATOM   1599 N N   . HIS   A 1 206 ? 13.762  48.616 3.785   1.00 16.19  ? 862  HIS   A N   1 
ATOM   1600 C CA  . HIS   A 1 206 ? 12.941  47.510 4.224   1.00 15.14  ? 862  HIS   A CA  1 
ATOM   1601 C C   . HIS   A 1 206 ? 12.340  46.875 2.970   1.00 18.42  ? 862  HIS   A C   1 
ATOM   1602 O O   . HIS   A 1 206 ? 11.417  47.429 2.366   1.00 16.93  ? 862  HIS   A O   1 
ATOM   1603 C CB  . HIS   A 1 206 ? 11.840  47.888 5.230   1.00 15.19  ? 862  HIS   A CB  1 
ATOM   1604 C CG  . HIS   A 1 206 ? 11.117  46.668 5.741   1.00 17.24  ? 862  HIS   A CG  1 
ATOM   1605 N ND1 . HIS   A 1 206 ? 11.489  46.058 6.918   1.00 18.42  ? 862  HIS   A ND1 1 
ATOM   1606 C CD2 . HIS   A 1 206 ? 10.125  45.939 5.172   1.00 16.97  ? 862  HIS   A CD2 1 
ATOM   1607 C CE1 . HIS   A 1 206 ? 10.690  45.011 7.059   1.00 16.34  ? 862  HIS   A CE1 1 
ATOM   1608 N NE2 . HIS   A 1 206 ? 9.860   44.890 6.031   1.00 16.16  ? 862  HIS   A NE2 1 
ATOM   1609 N N   . GLY   A 1 207 ? 12.924  45.753 2.579   1.00 15.29  ? 863  GLY   A N   1 
ATOM   1610 C CA  . GLY   A 1 207 ? 12.460  44.942 1.468   1.00 15.11  ? 863  GLY   A CA  1 
ATOM   1611 C C   . GLY   A 1 207 ? 11.462  43.934 1.982   1.00 18.80  ? 863  GLY   A C   1 
ATOM   1612 O O   . GLY   A 1 207 ? 11.517  43.524 3.143   1.00 18.14  ? 863  GLY   A O   1 
ATOM   1613 N N   . SER   A 1 208 ? 10.530  43.539 1.128   1.00 17.53  ? 864  SER   A N   1 
ATOM   1614 C CA  . SER   A 1 208 ? 9.518   42.530 1.432   1.00 16.93  ? 864  SER   A CA  1 
ATOM   1615 C C   . SER   A 1 208 ? 8.994   41.953 0.123   1.00 19.01  ? 864  SER   A C   1 
ATOM   1616 O O   . SER   A 1 208 ? 9.280   42.497 -0.950  1.00 18.44  ? 864  SER   A O   1 
ATOM   1617 C CB  . SER   A 1 208 ? 8.383   43.127 2.268   1.00 20.43  ? 864  SER   A CB  1 
ATOM   1618 O OG  . SER   A 1 208 ? 7.839   42.132 3.121   1.00 25.95  ? 864  SER   A OG  1 
ATOM   1619 N N   . ARG   A 1 209 ? 8.287   40.836 0.203   1.00 15.33  ? 865  ARG   A N   1 
ATOM   1620 C CA  . ARG   A 1 209 ? 7.674   40.234 -0.966  1.00 16.88  ? 865  ARG   A CA  1 
ATOM   1621 C C   . ARG   A 1 209 ? 6.519   41.112 -1.487  1.00 21.14  ? 865  ARG   A C   1 
ATOM   1622 O O   . ARG   A 1 209 ? 5.906   41.886 -0.738  1.00 22.34  ? 865  ARG   A O   1 
ATOM   1623 C CB  . ARG   A 1 209 ? 7.201   38.809 -0.662  1.00 21.31  ? 865  ARG   A CB  1 
ATOM   1624 C CG  . ARG   A 1 209 ? 8.355   37.821 -0.408  1.00 30.93  ? 865  ARG   A CG  1 
ATOM   1625 C CD  . ARG   A 1 209 ? 7.980   36.875 0.725   1.00 35.25  ? 865  ARG   A CD  1 
ATOM   1626 N NE  . ARG   A 1 209 ? 8.913   35.757 0.904   1.00 36.89  ? 865  ARG   A NE  1 
ATOM   1627 C CZ  . ARG   A 1 209 ? 8.802   34.582 0.292   1.00 53.93  ? 865  ARG   A CZ  1 
ATOM   1628 N NH1 . ARG   A 1 209 ? 7.843   34.378 -0.605  1.00 51.16  ? 865  ARG   A NH1 1 
ATOM   1629 N NH2 . ARG   A 1 209 ? 9.656   33.608 0.558   1.00 42.61  ? 865  ARG   A NH2 1 
ATOM   1630 N N   . THR   A 1 210 ? 6.239   41.005 -2.775  1.00 17.35  ? 866  THR   A N   1 
ATOM   1631 C CA  . THR   A 1 210 ? 5.207   41.789 -3.439  1.00 18.94  ? 866  THR   A CA  1 
ATOM   1632 C C   . THR   A 1 210 ? 3.865   41.590 -2.751  1.00 22.97  ? 866  THR   A C   1 
ATOM   1633 O O   . THR   A 1 210 ? 3.128   42.561 -2.611  1.00 23.20  ? 866  THR   A O   1 
ATOM   1634 C CB  . THR   A 1 210 ? 5.227   41.508 -4.946  1.00 24.89  ? 866  THR   A CB  1 
ATOM   1635 O OG1 . THR   A 1 210 ? 6.381   42.181 -5.436  1.00 28.31  ? 866  THR   A OG1 1 
ATOM   1636 C CG2 . THR   A 1 210 ? 4.077   42.085 -5.659  1.00 29.69  ? 866  THR   A CG2 1 
ATOM   1637 N N   . THR   A 1 211 ? 3.619   40.369 -2.231  1.00 20.97  ? 867  THR   A N   1 
ATOM   1638 C CA  . THR   A 1 211 ? 2.390   39.945 -1.542  1.00 21.19  ? 867  THR   A CA  1 
ATOM   1639 C C   . THR   A 1 211 ? 2.222   40.555 -0.135  1.00 24.61  ? 867  THR   A C   1 
ATOM   1640 O O   . THR   A 1 211 ? 1.183   40.361 0.478   1.00 22.81  ? 867  THR   A O   1 
ATOM   1641 C CB  . THR   A 1 211 ? 2.322   38.410 -1.506  1.00 31.94  ? 867  THR   A CB  1 
ATOM   1642 O OG1 . THR   A 1 211 ? 3.581   37.900 -1.073  1.00 30.59  ? 867  THR   A OG1 1 
ATOM   1643 C CG2 . THR   A 1 211 ? 1.985   37.820 -2.852  1.00 32.07  ? 867  THR   A CG2 1 
ATOM   1644 N N   . ASN   A 1 212 ? 3.239   41.278 0.378   1.00 21.30  ? 868  ASN   A N   1 
ATOM   1645 C CA  . ASN   A 1 212 ? 3.186   41.917 1.687   1.00 19.73  ? 868  ASN   A CA  1 
ATOM   1646 C C   . ASN   A 1 212 ? 2.729   43.361 1.611   1.00 20.78  ? 868  ASN   A C   1 
ATOM   1647 O O   . ASN   A 1 212 ? 2.214   43.903 2.595   1.00 18.71  ? 868  ASN   A O   1 
ATOM   1648 C CB  . ASN   A 1 212 ? 4.583   41.918 2.318   1.00 16.72  ? 868  ASN   A CB  1 
ATOM   1649 C CG  . ASN   A 1 212 ? 5.064   40.586 2.835   1.00 30.32  ? 868  ASN   A CG  1 
ATOM   1650 O OD1 . ASN   A 1 212 ? 5.603   39.772 2.087   1.00 24.60  ? 868  ASN   A OD1 1 
ATOM   1651 N ND2 . ASN   A 1 212 ? 4.931   40.356 4.144   1.00 13.03  ? 868  ASN   A ND2 1 
ATOM   1652 N N   . PHE   A 1 213 ? 2.982   43.999 0.453   1.00 18.96  ? 869  PHE   A N   1 
ATOM   1653 C CA  . PHE   A 1 213 ? 2.827   45.434 0.234   1.00 19.02  ? 869  PHE   A CA  1 
ATOM   1654 C C   . PHE   A 1 213 ? 1.408   45.965 0.287   1.00 22.84  ? 869  PHE   A C   1 
ATOM   1655 O O   . PHE   A 1 213 ? 1.250   47.126 0.683   1.00 23.64  ? 869  PHE   A O   1 
ATOM   1656 C CB  . PHE   A 1 213 ? 3.566   45.883 -1.034  1.00 20.54  ? 869  PHE   A CB  1 
ATOM   1657 C CG  . PHE   A 1 213 ? 5.044   45.973 -0.718  1.00 21.48  ? 869  PHE   A CG  1 
ATOM   1658 C CD1 . PHE   A 1 213 ? 5.897   44.912 -0.989  1.00 23.20  ? 869  PHE   A CD1 1 
ATOM   1659 C CD2 . PHE   A 1 213 ? 5.561   47.075 -0.047  1.00 23.85  ? 869  PHE   A CD2 1 
ATOM   1660 C CE1 . PHE   A 1 213 ? 7.251   44.980 -0.656  1.00 23.79  ? 869  PHE   A CE1 1 
ATOM   1661 C CE2 . PHE   A 1 213 ? 6.921   47.142 0.276   1.00 25.32  ? 869  PHE   A CE2 1 
ATOM   1662 C CZ  . PHE   A 1 213 ? 7.752   46.095 -0.023  1.00 22.57  ? 869  PHE   A CZ  1 
ATOM   1663 N N   . ALA   A 1 214 ? 0.380   45.142 0.044   1.00 19.75  ? 870  ALA   A N   1 
ATOM   1664 C CA  . ALA   A 1 214 ? -0.992  45.636 0.233   1.00 18.43  ? 870  ALA   A CA  1 
ATOM   1665 C C   . ALA   A 1 214 ? -1.211  45.825 1.751   1.00 21.65  ? 870  ALA   A C   1 
ATOM   1666 O O   . ALA   A 1 214 ? -1.738  46.848 2.158   1.00 22.67  ? 870  ALA   A O   1 
ATOM   1667 C CB  . ALA   A 1 214 ? -2.007  44.670 -0.366  1.00 19.15  ? 870  ALA   A CB  1 
ATOM   1668 N N   . GLY   A 1 215 ? -0.685  44.905 2.570   1.00 17.89  ? 871  GLY   A N   1 
ATOM   1669 C CA  . GLY   A 1 215 ? -0.752  44.970 4.031   1.00 17.08  ? 871  GLY   A CA  1 
ATOM   1670 C C   . GLY   A 1 215 ? 0.095   46.096 4.592   1.00 20.53  ? 871  GLY   A C   1 
ATOM   1671 O O   . GLY   A 1 215 ? -0.339  46.827 5.491   1.00 19.88  ? 871  GLY   A O   1 
ATOM   1672 N N   . ILE   A 1 216 ? 1.308   46.253 4.042   1.00 17.76  ? 872  ILE   A N   1 
ATOM   1673 C CA  . ILE   A 1 216 ? 2.263   47.300 4.449   1.00 16.96  ? 872  ILE   A CA  1 
ATOM   1674 C C   . ILE   A 1 216 ? 1.697   48.683 4.163   1.00 20.08  ? 872  ILE   A C   1 
ATOM   1675 O O   . ILE   A 1 216 ? 1.777   49.554 5.012   1.00 19.03  ? 872  ILE   A O   1 
ATOM   1676 C CB  . ILE   A 1 216 ? 3.696   47.127 3.838   1.00 18.97  ? 872  ILE   A CB  1 
ATOM   1677 C CG1 . ILE   A 1 216 ? 4.378   45.839 4.375   1.00 18.47  ? 872  ILE   A CG1 1 
ATOM   1678 C CG2 . ILE   A 1 216 ? 4.575   48.387 4.145   1.00 15.89  ? 872  ILE   A CG2 1 
ATOM   1679 C CD1 . ILE   A 1 216 ? 5.568   45.325 3.563   1.00 11.05  ? 872  ILE   A CD1 1 
ATOM   1680 N N   . LEU   A 1 217 ? 1.155   48.904 2.973   1.00 18.81  ? 873  LEU   A N   1 
ATOM   1681 C CA  . LEU   A 1 217 ? 0.616   50.227 2.673   1.00 19.87  ? 873  LEU   A CA  1 
ATOM   1682 C C   . LEU   A 1 217 ? -0.648  50.561 3.465   1.00 24.94  ? 873  LEU   A C   1 
ATOM   1683 O O   . LEU   A 1 217 ? -0.823  51.712 3.844   1.00 25.40  ? 873  LEU   A O   1 
ATOM   1684 C CB  . LEU   A 1 217 ? 0.402   50.433 1.165   1.00 19.84  ? 873  LEU   A CB  1 
ATOM   1685 C CG  . LEU   A 1 217 ? 1.669   50.380 0.304   1.00 24.04  ? 873  LEU   A CG  1 
ATOM   1686 C CD1 . LEU   A 1 217 ? 1.324   50.432 -1.184  1.00 23.58  ? 873  LEU   A CD1 1 
ATOM   1687 C CD2 . LEU   A 1 217 ? 2.669   51.479 0.697   1.00 26.70  ? 873  LEU   A CD2 1 
ATOM   1688 N N   . SER   A 1 218 ? -1.505  49.583 3.743   1.00 21.75  ? 874  SER   A N   1 
ATOM   1689 C CA  . SER   A 1 218 ? -2.732  49.886 4.481   1.00 22.31  ? 874  SER   A CA  1 
ATOM   1690 C C   . SER   A 1 218 ? -2.559  49.904 6.015   1.00 25.25  ? 874  SER   A C   1 
ATOM   1691 O O   . SER   A 1 218 ? -3.190  50.734 6.673   1.00 26.07  ? 874  SER   A O   1 
ATOM   1692 C CB  . SER   A 1 218 ? -3.888  48.970 4.065   1.00 27.73  ? 874  SER   A CB  1 
ATOM   1693 O OG  . SER   A 1 218 ? -3.827  47.684 4.643   1.00 39.29  ? 874  SER   A OG  1 
ATOM   1694 N N   . GLN   A 1 219 ? -1.715  49.010 6.577   1.00 18.40  ? 875  GLN   A N   1 
ATOM   1695 C CA  . GLN   A 1 219 ? -1.533  48.872 8.028   1.00 17.35  ? 875  GLN   A CA  1 
ATOM   1696 C C   . GLN   A 1 219 ? -0.176  49.321 8.512   1.00 22.20  ? 875  GLN   A C   1 
ATOM   1697 O O   . GLN   A 1 219 ? 0.022   49.444 9.719   1.00 22.05  ? 875  GLN   A O   1 
ATOM   1698 C CB  . GLN   A 1 219 ? -1.724  47.412 8.461   1.00 17.99  ? 875  GLN   A CB  1 
ATOM   1699 C CG  . GLN   A 1 219 ? -3.004  46.758 7.900   1.00 31.98  ? 875  GLN   A CG  1 
ATOM   1700 C CD  . GLN   A 1 219 ? -4.267  46.965 8.695   1.00 60.38  ? 875  GLN   A CD  1 
ATOM   1701 O OE1 . GLN   A 1 219 ? -5.004  46.007 8.961   1.00 66.75  ? 875  GLN   A OE1 1 
ATOM   1702 N NE2 . GLN   A 1 219 ? -4.571  48.204 9.067   1.00 42.97  ? 875  GLN   A NE2 1 
ATOM   1703 N N   . GLY   A 1 220 ? 0.755   49.504 7.582   1.00 19.27  ? 876  GLY   A N   1 
ATOM   1704 C CA  . GLY   A 1 220 ? 2.114   49.915 7.892   1.00 18.78  ? 876  GLY   A CA  1 
ATOM   1705 C C   . GLY   A 1 220 ? 2.946   48.720 8.273   1.00 23.63  ? 876  GLY   A C   1 
ATOM   1706 O O   . GLY   A 1 220 ? 2.434   47.596 8.327   1.00 24.59  ? 876  GLY   A O   1 
ATOM   1707 N N   . LEU   A 1 221 ? 4.264   48.952 8.467   1.00 20.17  ? 877  LEU   A N   1 
ATOM   1708 C CA  . LEU   A 1 221 ? 5.196   47.950 8.967   1.00 18.21  ? 877  LEU   A CA  1 
ATOM   1709 C C   . LEU   A 1 221 ? 4.764   47.667 10.392  1.00 21.56  ? 877  LEU   A C   1 
ATOM   1710 O O   . LEU   A 1 221 ? 4.419   48.577 11.148  1.00 22.18  ? 877  LEU   A O   1 
ATOM   1711 C CB  . LEU   A 1 221 ? 6.657   48.434 8.896   1.00 17.48  ? 877  LEU   A CB  1 
ATOM   1712 C CG  . LEU   A 1 221 ? 7.325   48.414 7.504   1.00 20.35  ? 877  LEU   A CG  1 
ATOM   1713 C CD1 . LEU   A 1 221 ? 8.760   48.925 7.576   1.00 20.10  ? 877  LEU   A CD1 1 
ATOM   1714 C CD2 . LEU   A 1 221 ? 7.281   47.031 6.889   1.00 17.73  ? 877  LEU   A CD2 1 
ATOM   1715 N N   . ARG   A 1 222 ? 4.654   46.401 10.713  1.00 18.12  ? 878  ARG   A N   1 
ATOM   1716 C CA  . ARG   A 1 222 ? 4.112   45.955 11.980  1.00 16.53  ? 878  ARG   A CA  1 
ATOM   1717 C C   . ARG   A 1 222 ? 5.032   44.944 12.574  1.00 19.62  ? 878  ARG   A C   1 
ATOM   1718 O O   . ARG   A 1 222 ? 5.809   44.330 11.857  1.00 18.06  ? 878  ARG   A O   1 
ATOM   1719 C CB  . ARG   A 1 222 ? 2.724   45.331 11.747  1.00 10.98  ? 878  ARG   A CB  1 
ATOM   1720 C CG  . ARG   A 1 222 ? 1.636   46.345 11.424  1.00 15.95  ? 878  ARG   A CG  1 
ATOM   1721 C CD  . ARG   A 1 222 ? 0.296   45.659 11.200  1.00 24.01  ? 878  ARG   A CD  1 
ATOM   1722 N NE  . ARG   A 1 222 ? 0.321   44.824 9.988   1.00 38.80  ? 878  ARG   A NE  1 
ATOM   1723 C CZ  . ARG   A 1 222 ? -0.685  44.069 9.560   1.00 42.69  ? 878  ARG   A CZ  1 
ATOM   1724 N NH1 . ARG   A 1 222 ? -1.816  43.997 10.256  1.00 31.54  ? 878  ARG   A NH1 1 
ATOM   1725 N NH2 . ARG   A 1 222 ? -0.559  43.357 8.452   1.00 25.81  ? 878  ARG   A NH2 1 
ATOM   1726 N N   . ILE   A 1 223 ? 4.955   44.791 13.897  1.00 19.08  ? 879  ILE   A N   1 
ATOM   1727 C CA  . ILE   A 1 223 ? 5.752   43.860 14.685  1.00 19.56  ? 879  ILE   A CA  1 
ATOM   1728 C C   . ILE   A 1 223 ? 4.929   42.585 14.789  1.00 24.01  ? 879  ILE   A C   1 
ATOM   1729 O O   . ILE   A 1 223 ? 3.693   42.675 14.870  1.00 25.89  ? 879  ILE   A O   1 
ATOM   1730 C CB  . ILE   A 1 223 ? 6.027   44.480 16.092  1.00 22.77  ? 879  ILE   A CB  1 
ATOM   1731 C CG1 . ILE   A 1 223 ? 6.839   45.781 16.003  1.00 23.19  ? 879  ILE   A CG1 1 
ATOM   1732 C CG2 . ILE   A 1 223 ? 6.676   43.459 17.054  1.00 22.36  ? 879  ILE   A CG2 1 
ATOM   1733 C CD1 . ILE   A 1 223 ? 6.642   46.741 17.162  1.00 29.48  ? 879  ILE   A CD1 1 
ATOM   1734 N N   . ALA   A 1 224 ? 5.602   41.402 14.823  1.00 20.76  ? 880  ALA   A N   1 
ATOM   1735 C CA  . ALA   A 1 224 ? 4.948   40.098 14.980  1.00 20.84  ? 880  ALA   A CA  1 
ATOM   1736 C C   . ALA   A 1 224 ? 4.059   40.142 16.266  1.00 24.81  ? 880  ALA   A C   1 
ATOM   1737 O O   . ALA   A 1 224 ? 4.441   40.824 17.227  1.00 23.68  ? 880  ALA   A O   1 
ATOM   1738 C CB  . ALA   A 1 224 ? 5.996   38.995 15.073  1.00 21.55  ? 880  ALA   A CB  1 
ATOM   1739 N N   . PRO   A 1 225 ? 2.877   39.468 16.296  1.00 22.29  ? 881  PRO   A N   1 
ATOM   1740 C CA  . PRO   A 1 225 ? 1.967   39.591 17.464  1.00 21.89  ? 881  PRO   A CA  1 
ATOM   1741 C C   . PRO   A 1 225 ? 2.479   38.984 18.768  1.00 25.78  ? 881  PRO   A C   1 
ATOM   1742 O O   . PRO   A 1 225 ? 3.463   38.258 18.707  1.00 24.09  ? 881  PRO   A O   1 
ATOM   1743 C CB  . PRO   A 1 225 ? 0.682   38.908 16.985  1.00 23.40  ? 881  PRO   A CB  1 
ATOM   1744 C CG  . PRO   A 1 225 ? 1.122   37.983 15.940  1.00 27.30  ? 881  PRO   A CG  1 
ATOM   1745 C CD  . PRO   A 1 225 ? 2.278   38.631 15.244  1.00 23.10  ? 881  PRO   A CD  1 
ATOM   1746 N N   . PRO   A 1 226 ? 1.841   39.237 19.947  1.00 23.36  ? 882  PRO   A N   1 
ATOM   1747 C CA  . PRO   A 1 226 ? 2.367   38.672 21.212  1.00 22.77  ? 882  PRO   A CA  1 
ATOM   1748 C C   . PRO   A 1 226 ? 2.497   37.145 21.268  1.00 25.57  ? 882  PRO   A C   1 
ATOM   1749 O O   . PRO   A 1 226 ? 3.336   36.646 22.001  1.00 25.12  ? 882  PRO   A O   1 
ATOM   1750 C CB  . PRO   A 1 226 ? 1.386   39.186 22.269  1.00 24.75  ? 882  PRO   A CB  1 
ATOM   1751 C CG  . PRO   A 1 226 ? 0.789   40.399 21.668  1.00 30.06  ? 882  PRO   A CG  1 
ATOM   1752 C CD  . PRO   A 1 226 ? 0.672   40.101 20.205  1.00 25.26  ? 882  PRO   A CD  1 
ATOM   1753 N N   . GLU   A 1 227 ? 1.685   36.413 20.496  1.00 22.59  ? 883  GLU   A N   1 
ATOM   1754 C CA  . GLU   A 1 227 ? 1.689   34.943 20.450  1.00 22.21  ? 883  GLU   A CA  1 
ATOM   1755 C C   . GLU   A 1 227 ? 2.982   34.400 19.841  1.00 26.27  ? 883  GLU   A C   1 
ATOM   1756 O O   . GLU   A 1 227 ? 3.404   33.293 20.195  1.00 26.65  ? 883  GLU   A O   1 
ATOM   1757 C CB  . GLU   A 1 227 ? 0.471   34.409 19.670  1.00 23.05  ? 883  GLU   A CB  1 
ATOM   1758 C CG  . GLU   A 1 227 ? -0.851  34.518 20.427  1.00 28.13  ? 883  GLU   A CG  1 
ATOM   1759 C CD  . GLU   A 1 227 ? -1.509  35.888 20.449  1.00 46.53  ? 883  GLU   A CD  1 
ATOM   1760 O OE1 . GLU   A 1 227 ? -2.365  36.115 21.334  1.00 35.02  ? 883  GLU   A OE1 1 
ATOM   1761 O OE2 . GLU   A 1 227 ? -1.169  36.737 19.592  1.00 42.48  ? 883  GLU   A OE2 1 
ATOM   1762 N N   . ALA   A 1 228 ? 3.601   35.179 18.922  1.00 20.81  ? 884  ALA   A N   1 
ATOM   1763 C CA  . ALA   A 1 228 ? 4.852   34.871 18.212  1.00 20.34  ? 884  ALA   A CA  1 
ATOM   1764 C C   . ALA   A 1 228 ? 6.041   34.591 19.122  1.00 22.74  ? 884  ALA   A C   1 
ATOM   1765 O O   . ALA   A 1 228 ? 6.215   35.302 20.120  1.00 20.87  ? 884  ALA   A O   1 
ATOM   1766 C CB  . ALA   A 1 228 ? 5.192   35.975 17.236  1.00 20.61  ? 884  ALA   A CB  1 
ATOM   1767 N N   . PRO   A 1 229 ? 6.833   33.530 18.802  1.00 21.12  ? 885  PRO   A N   1 
ATOM   1768 C CA  . PRO   A 1 229 ? 8.020   33.207 19.625  1.00 22.40  ? 885  PRO   A CA  1 
ATOM   1769 C C   . PRO   A 1 229 ? 9.125   34.250 19.448  1.00 28.86  ? 885  PRO   A C   1 
ATOM   1770 O O   . PRO   A 1 229 ? 9.610   34.432 18.326  1.00 29.60  ? 885  PRO   A O   1 
ATOM   1771 C CB  . PRO   A 1 229 ? 8.465   31.832 19.094  1.00 24.29  ? 885  PRO   A CB  1 
ATOM   1772 C CG  . PRO   A 1 229 ? 7.959   31.772 17.699  1.00 28.11  ? 885  PRO   A CG  1 
ATOM   1773 C CD  . PRO   A 1 229 ? 6.698   32.605 17.654  1.00 23.09  ? 885  PRO   A CD  1 
ATOM   1774 N N   . VAL   A 1 230 ? 9.491   34.956 20.539  1.00 26.30  ? 886  VAL   A N   1 
ATOM   1775 C CA  . VAL   A 1 230 ? 10.509  36.018 20.553  1.00 26.97  ? 886  VAL   A CA  1 
ATOM   1776 C C   . VAL   A 1 230 ? 11.873  35.469 20.053  1.00 29.15  ? 886  VAL   A C   1 
ATOM   1777 O O   . VAL   A 1 230 ? 12.617  36.207 19.399  1.00 27.27  ? 886  VAL   A O   1 
ATOM   1778 C CB  . VAL   A 1 230 ? 10.558  36.761 21.926  1.00 32.49  ? 886  VAL   A CB  1 
ATOM   1779 C CG1 . VAL   A 1 230 ? 10.603  35.784 23.086  1.00 33.25  ? 886  VAL   A CG1 1 
ATOM   1780 C CG2 . VAL   A 1 230 ? 11.690  37.797 22.016  1.00 32.80  ? 886  VAL   A CG2 1 
ATOM   1781 N N   . THR   A 1 231 ? 12.104  34.144 20.212  1.00 24.69  ? 887  THR   A N   1 
ATOM   1782 C CA  . THR   A 1 231 ? 13.333  33.479 19.782  1.00 24.79  ? 887  THR   A CA  1 
ATOM   1783 C C   . THR   A 1 231 ? 13.385  33.175 18.273  1.00 28.69  ? 887  THR   A C   1 
ATOM   1784 O O   . THR   A 1 231 ? 14.458  32.834 17.756  1.00 25.75  ? 887  THR   A O   1 
ATOM   1785 C CB  . THR   A 1 231 ? 13.645  32.234 20.617  1.00 29.61  ? 887  THR   A CB  1 
ATOM   1786 O OG1 . THR   A 1 231 ? 12.708  31.216 20.336  1.00 27.05  ? 887  THR   A OG1 1 
ATOM   1787 C CG2 . THR   A 1 231 ? 13.725  32.520 22.112  1.00 27.50  ? 887  THR   A CG2 1 
ATOM   1788 N N   . GLY   A 1 232 ? 12.268  33.369 17.573  1.00 25.99  ? 888  GLY   A N   1 
ATOM   1789 C CA  . GLY   A 1 232 ? 12.203  33.141 16.135  1.00 25.72  ? 888  GLY   A CA  1 
ATOM   1790 C C   . GLY   A 1 232 ? 12.808  34.255 15.299  1.00 29.14  ? 888  GLY   A C   1 
ATOM   1791 O O   . GLY   A 1 232 ? 12.823  34.159 14.072  1.00 29.35  ? 888  GLY   A O   1 
ATOM   1792 N N   . TYR   A 1 233 ? 13.278  35.335 15.959  1.00 24.45  ? 889  TYR   A N   1 
ATOM   1793 C CA  . TYR   A 1 233 ? 13.834  36.560 15.363  1.00 22.24  ? 889  TYR   A CA  1 
ATOM   1794 C C   . TYR   A 1 233 ? 15.102  36.930 16.090  1.00 23.25  ? 889  TYR   A C   1 
ATOM   1795 O O   . TYR   A 1 233 ? 15.112  36.970 17.323  1.00 22.33  ? 889  TYR   A O   1 
ATOM   1796 C CB  . TYR   A 1 233 ? 12.805  37.711 15.446  1.00 22.82  ? 889  TYR   A CB  1 
ATOM   1797 C CG  . TYR   A 1 233 ? 11.368  37.281 15.170  1.00 24.94  ? 889  TYR   A CG  1 
ATOM   1798 C CD1 . TYR   A 1 233 ? 10.559  36.778 16.190  1.00 26.42  ? 889  TYR   A CD1 1 
ATOM   1799 C CD2 . TYR   A 1 233 ? 10.840  37.316 13.880  1.00 25.41  ? 889  TYR   A CD2 1 
ATOM   1800 C CE1 . TYR   A 1 233 ? 9.259   36.334 15.937  1.00 26.42  ? 889  TYR   A CE1 1 
ATOM   1801 C CE2 . TYR   A 1 233 ? 9.525   36.914 13.625  1.00 26.03  ? 889  TYR   A CE2 1 
ATOM   1802 C CZ  . TYR   A 1 233 ? 8.732   36.438 14.661  1.00 28.56  ? 889  TYR   A CZ  1 
ATOM   1803 O OH  . TYR   A 1 233 ? 7.448   36.011 14.428  1.00 28.38  ? 889  TYR   A OH  1 
ATOM   1804 N N   . MET   A 1 234 ? 16.166  37.223 15.335  1.00 18.55  ? 890  MET   A N   1 
ATOM   1805 C CA  . MET   A 1 234 ? 17.506  37.500 15.853  1.00 18.32  ? 890  MET   A CA  1 
ATOM   1806 C C   . MET   A 1 234 ? 17.566  38.500 17.040  1.00 22.30  ? 890  MET   A C   1 
ATOM   1807 O O   . MET   A 1 234 ? 18.252  38.227 18.015  1.00 20.11  ? 890  MET   A O   1 
ATOM   1808 C CB  . MET   A 1 234 ? 18.467  37.931 14.737  1.00 20.10  ? 890  MET   A CB  1 
ATOM   1809 C CG  . MET   A 1 234 ? 19.920  37.772 15.153  1.00 23.58  ? 890  MET   A CG  1 
ATOM   1810 S SD  . MET   A 1 234 ? 21.026  38.270 13.860  1.00 27.78  ? 890  MET   A SD  1 
ATOM   1811 C CE  . MET   A 1 234 ? 22.597  38.528 14.824  1.00 24.09  ? 890  MET   A CE  1 
ATOM   1812 N N   . PHE   A 1 235 ? 16.854  39.628 16.944  1.00 19.76  ? 891  PHE   A N   1 
ATOM   1813 C CA  . PHE   A 1 235 ? 16.827  40.667 17.975  1.00 18.58  ? 891  PHE   A CA  1 
ATOM   1814 C C   . PHE   A 1 235 ? 15.418  40.841 18.565  1.00 23.46  ? 891  PHE   A C   1 
ATOM   1815 O O   . PHE   A 1 235 ? 15.024  41.934 18.992  1.00 22.72  ? 891  PHE   A O   1 
ATOM   1816 C CB  . PHE   A 1 235 ? 17.410  41.985 17.419  1.00 20.07  ? 891  PHE   A CB  1 
ATOM   1817 C CG  . PHE   A 1 235 ? 18.886  41.895 17.101  1.00 22.98  ? 891  PHE   A CG  1 
ATOM   1818 C CD1 . PHE   A 1 235 ? 19.830  41.797 18.119  1.00 26.19  ? 891  PHE   A CD1 1 
ATOM   1819 C CD2 . PHE   A 1 235 ? 19.328  41.866 15.787  1.00 25.31  ? 891  PHE   A CD2 1 
ATOM   1820 C CE1 . PHE   A 1 235 ? 21.190  41.705 17.827  1.00 26.75  ? 891  PHE   A CE1 1 
ATOM   1821 C CE2 . PHE   A 1 235 ? 20.687  41.790 15.496  1.00 27.81  ? 891  PHE   A CE2 1 
ATOM   1822 C CZ  . PHE   A 1 235 ? 21.610  41.706 16.517  1.00 25.95  ? 891  PHE   A CZ  1 
ATOM   1823 N N   . GLY   A 1 236 ? 14.680  39.740 18.617  1.00 19.75  ? 892  GLY   A N   1 
ATOM   1824 C CA  . GLY   A 1 236 ? 13.329  39.745 19.154  1.00 18.23  ? 892  GLY   A CA  1 
ATOM   1825 C C   . GLY   A 1 236 ? 12.327  40.338 18.195  1.00 23.16  ? 892  GLY   A C   1 
ATOM   1826 O O   . GLY   A 1 236 ? 12.594  40.482 16.999  1.00 22.92  ? 892  GLY   A O   1 
ATOM   1827 N N   . LYS   A 1 237 ? 11.187  40.728 18.736  1.00 20.77  ? 893  LYS   A N   1 
ATOM   1828 C CA  . LYS   A 1 237 ? 10.048  41.213 17.964  1.00 19.50  ? 893  LYS   A CA  1 
ATOM   1829 C C   . LYS   A 1 237 ? 10.005  42.736 17.811  1.00 22.07  ? 893  LYS   A C   1 
ATOM   1830 O O   . LYS   A 1 237 ? 9.473   43.444 18.662  1.00 21.73  ? 893  LYS   A O   1 
ATOM   1831 C CB  . LYS   A 1 237 ? 8.752   40.647 18.550  1.00 22.02  ? 893  LYS   A CB  1 
ATOM   1832 C CG  . LYS   A 1 237 ? 8.608   39.133 18.344  1.00 23.92  ? 893  LYS   A CG  1 
ATOM   1833 C CD  . LYS   A 1 237 ? 7.270   38.605 18.839  1.00 34.64  ? 893  LYS   A CD  1 
ATOM   1834 C CE  . LYS   A 1 237 ? 7.211   38.458 20.345  1.00 34.87  ? 893  LYS   A CE  1 
ATOM   1835 N NZ  . LYS   A 1 237 ? 5.892   37.974 20.813  1.00 25.57  ? 893  LYS   A NZ  1 
ATOM   1836 N N   . GLY   A 1 238 ? 10.548  43.202 16.692  1.00 18.42  ? 894  GLY   A N   1 
ATOM   1837 C CA  . GLY   A 1 238 ? 10.584  44.604 16.306  1.00 18.77  ? 894  GLY   A CA  1 
ATOM   1838 C C   . GLY   A 1 238 ? 10.421  44.759 14.808  1.00 23.36  ? 894  GLY   A C   1 
ATOM   1839 O O   . GLY   A 1 238 ? 10.016  43.798 14.142  1.00 23.91  ? 894  GLY   A O   1 
ATOM   1840 N N   . ILE   A 1 239 ? 10.732  45.959 14.260  1.00 18.43  ? 895  ILE   A N   1 
ATOM   1841 C CA  . ILE   A 1 239 ? 10.686  46.219 12.808  1.00 16.64  ? 895  ILE   A CA  1 
ATOM   1842 C C   . ILE   A 1 239 ? 12.130  46.365 12.370  1.00 19.15  ? 895  ILE   A C   1 
ATOM   1843 O O   . ILE   A 1 239 ? 12.858  47.212 12.901  1.00 15.68  ? 895  ILE   A O   1 
ATOM   1844 C CB  . ILE   A 1 239 ? 9.789   47.412 12.343  1.00 18.16  ? 895  ILE   A CB  1 
ATOM   1845 C CG1 . ILE   A 1 239 ? 8.370   47.357 12.957  1.00 15.97  ? 895  ILE   A CG1 1 
ATOM   1846 C CG2 . ILE   A 1 239 ? 9.700   47.412 10.826  1.00 18.62  ? 895  ILE   A CG2 1 
ATOM   1847 C CD1 . ILE   A 1 239 ? 7.601   48.681 12.911  1.00 18.76  ? 895  ILE   A CD1 1 
ATOM   1848 N N   . TYR   A 1 240 ? 12.565  45.496 11.435  1.00 18.06  ? 896  TYR   A N   1 
ATOM   1849 C CA  . TYR   A 1 240 ? 13.961  45.420 10.987  1.00 16.47  ? 896  TYR   A CA  1 
ATOM   1850 C C   . TYR   A 1 240 ? 14.230  46.217 9.724   1.00 20.76  ? 896  TYR   A C   1 
ATOM   1851 O O   . TYR   A 1 240 ? 13.466  46.138 8.770   1.00 20.73  ? 896  TYR   A O   1 
ATOM   1852 C CB  . TYR   A 1 240 ? 14.390  43.960 10.786  1.00 17.09  ? 896  TYR   A CB  1 
ATOM   1853 C CG  . TYR   A 1 240 ? 14.488  43.114 12.043  1.00 18.20  ? 896  TYR   A CG  1 
ATOM   1854 C CD1 . TYR   A 1 240 ? 13.357  42.827 12.808  1.00 19.49  ? 896  TYR   A CD1 1 
ATOM   1855 C CD2 . TYR   A 1 240 ? 15.682  42.493 12.392  1.00 18.31  ? 896  TYR   A CD2 1 
ATOM   1856 C CE1 . TYR   A 1 240 ? 13.439  42.021 13.938  1.00 19.17  ? 896  TYR   A CE1 1 
ATOM   1857 C CE2 . TYR   A 1 240 ? 15.778  41.700 13.530  1.00 18.50  ? 896  TYR   A CE2 1 
ATOM   1858 C CZ  . TYR   A 1 240 ? 14.654  41.460 14.292  1.00 19.85  ? 896  TYR   A CZ  1 
ATOM   1859 O OH  . TYR   A 1 240 ? 14.742  40.660 15.390  1.00 19.32  ? 896  TYR   A OH  1 
ATOM   1860 N N   . PHE   A 1 241 ? 15.334  46.979 9.720   1.00 16.64  ? 897  PHE   A N   1 
ATOM   1861 C CA  . PHE   A 1 241 ? 15.779  47.829 8.608   1.00 15.79  ? 897  PHE   A CA  1 
ATOM   1862 C C   . PHE   A 1 241 ? 17.266  47.607 8.323   1.00 19.64  ? 897  PHE   A C   1 
ATOM   1863 O O   . PHE   A 1 241 ? 18.004  47.190 9.211   1.00 19.50  ? 897  PHE   A O   1 
ATOM   1864 C CB  . PHE   A 1 241 ? 15.576  49.314 8.965   1.00 16.79  ? 897  PHE   A CB  1 
ATOM   1865 C CG  . PHE   A 1 241 ? 14.141  49.710 9.156   1.00 16.80  ? 897  PHE   A CG  1 
ATOM   1866 C CD1 . PHE   A 1 241 ? 13.378  50.158 8.084   1.00 18.84  ? 897  PHE   A CD1 1 
ATOM   1867 C CD2 . PHE   A 1 241 ? 13.541  49.618 10.401  1.00 17.81  ? 897  PHE   A CD2 1 
ATOM   1868 C CE1 . PHE   A 1 241 ? 12.032  50.487 8.249   1.00 17.97  ? 897  PHE   A CE1 1 
ATOM   1869 C CE2 . PHE   A 1 241 ? 12.199  49.961 10.570  1.00 19.61  ? 897  PHE   A CE2 1 
ATOM   1870 C CZ  . PHE   A 1 241 ? 11.451  50.380 9.482   1.00 16.76  ? 897  PHE   A CZ  1 
ATOM   1871 N N   . ALA   A 1 242 ? 17.705  47.934 7.095   1.00 14.95  ? 898  ALA   A N   1 
ATOM   1872 C CA  . ALA   A 1 242 ? 19.089  47.810 6.652   1.00 12.54  ? 898  ALA   A CA  1 
ATOM   1873 C C   . ALA   A 1 242 ? 19.589  49.102 6.003   1.00 16.97  ? 898  ALA   A C   1 
ATOM   1874 O O   . ALA   A 1 242 ? 18.807  49.845 5.430   1.00 17.90  ? 898  ALA   A O   1 
ATOM   1875 C CB  . ALA   A 1 242 ? 19.219  46.639 5.666   1.00 12.36  ? 898  ALA   A CB  1 
ATOM   1876 N N   . ASP   A 1 243 ? 20.901  49.349 6.053   1.00 15.41  ? 899  ASP   A N   1 
ATOM   1877 C CA  . ASP   A 1 243 ? 21.535  50.502 5.404   1.00 15.10  ? 899  ASP   A CA  1 
ATOM   1878 C C   . ASP   A 1 243 ? 22.204  50.086 4.078   1.00 20.38  ? 899  ASP   A C   1 
ATOM   1879 O O   . ASP   A 1 243 ? 22.698  50.945 3.364   1.00 22.37  ? 899  ASP   A O   1 
ATOM   1880 C CB  . ASP   A 1 243 ? 22.478  51.271 6.365   1.00 15.89  ? 899  ASP   A CB  1 
ATOM   1881 C CG  . ASP   A 1 243 ? 23.627  50.505 7.010   1.00 24.38  ? 899  ASP   A CG  1 
ATOM   1882 O OD1 . ASP   A 1 243 ? 24.051  49.458 6.450   1.00 25.69  ? 899  ASP   A OD1 1 
ATOM   1883 O OD2 . ASP   A 1 243 ? 24.146  50.982 8.031   1.00 25.58  ? 899  ASP   A OD2 1 
ATOM   1884 N N   . MET   A 1 244 ? 22.228  48.758 3.777   1.00 16.99  ? 900  MET   A N   1 
ATOM   1885 C CA  . MET   A 1 244 ? 22.751  48.177 2.531   1.00 17.14  ? 900  MET   A CA  1 
ATOM   1886 C C   . MET   A 1 244 ? 21.534  47.708 1.734   1.00 20.03  ? 900  MET   A C   1 
ATOM   1887 O O   . MET   A 1 244 ? 20.864  46.773 2.177   1.00 19.52  ? 900  MET   A O   1 
ATOM   1888 C CB  . MET   A 1 244 ? 23.705  46.972 2.775   1.00 18.95  ? 900  MET   A CB  1 
ATOM   1889 C CG  . MET   A 1 244 ? 25.029  47.316 3.460   1.00 22.81  ? 900  MET   A CG  1 
ATOM   1890 S SD  . MET   A 1 244 ? 26.148  48.439 2.572   1.00 26.68  ? 900  MET   A SD  1 
ATOM   1891 C CE  . MET   A 1 244 ? 27.047  47.315 1.602   1.00 22.24  ? 900  MET   A CE  1 
ATOM   1892 N N   . VAL   A 1 245 ? 21.239  48.359 0.575   1.00 14.78  ? 901  VAL   A N   1 
ATOM   1893 C CA  . VAL   A 1 245 ? 20.105  48.046 -0.300  1.00 14.33  ? 901  VAL   A CA  1 
ATOM   1894 C C   . VAL   A 1 245 ? 19.960  46.551 -0.607  1.00 18.38  ? 901  VAL   A C   1 
ATOM   1895 O O   . VAL   A 1 245 ? 18.845  46.044 -0.554  1.00 19.37  ? 901  VAL   A O   1 
ATOM   1896 C CB  . VAL   A 1 245 ? 20.065  48.902 -1.612  1.00 18.93  ? 901  VAL   A CB  1 
ATOM   1897 C CG1 . VAL   A 1 245 ? 21.145  48.494 -2.608  1.00 18.27  ? 901  VAL   A CG1 1 
ATOM   1898 C CG2 . VAL   A 1 245 ? 18.661  48.862 -2.263  1.00 18.19  ? 901  VAL   A CG2 1 
ATOM   1899 N N   . SER   A 1 246 ? 21.080  45.861 -0.927  1.00 14.67  ? 902  SER   A N   1 
ATOM   1900 C CA  . SER   A 1 246 ? 21.131  44.450 -1.277  1.00 13.60  ? 902  SER   A CA  1 
ATOM   1901 C C   . SER   A 1 246 ? 20.726  43.575 -0.082  1.00 19.30  ? 902  SER   A C   1 
ATOM   1902 O O   . SER   A 1 246 ? 20.069  42.571 -0.295  1.00 19.72  ? 902  SER   A O   1 
ATOM   1903 C CB  . SER   A 1 246 ? 22.523  44.105 -1.816  1.00 16.66  ? 902  SER   A CB  1 
ATOM   1904 O OG  . SER   A 1 246 ? 23.569  44.362 -0.880  1.00 16.78  ? 902  SER   A OG  1 
ATOM   1905 N N   . LYS   A 1 247 ? 21.051  43.978 1.183   1.00 17.09  ? 903  LYS   A N   1 
ATOM   1906 C CA  . LYS   A 1 247 ? 20.636  43.224 2.374   1.00 16.61  ? 903  LYS   A CA  1 
ATOM   1907 C C   . LYS   A 1 247 ? 19.092  43.143 2.476   1.00 21.47  ? 903  LYS   A C   1 
ATOM   1908 O O   . LYS   A 1 247 ? 18.539  42.088 2.844   1.00 20.49  ? 903  LYS   A O   1 
ATOM   1909 C CB  . LYS   A 1 247 ? 21.245  43.780 3.664   1.00 17.83  ? 903  LYS   A CB  1 
ATOM   1910 C CG  . LYS   A 1 247 ? 20.971  42.897 4.896   1.00 15.19  ? 903  LYS   A CG  1 
ATOM   1911 C CD  . LYS   A 1 247 ? 21.700  43.357 6.145   1.00 17.10  ? 903  LYS   A CD  1 
ATOM   1912 C CE  . LYS   A 1 247 ? 21.024  42.723 7.354   1.00 30.11  ? 903  LYS   A CE  1 
ATOM   1913 N NZ  . LYS   A 1 247 ? 21.922  42.641 8.551   1.00 24.50  ? 903  LYS   A NZ  1 
ATOM   1914 N N   . SER   A 1 248 ? 18.413  44.268 2.154   1.00 18.21  ? 904  SER   A N   1 
ATOM   1915 C CA  . SER   A 1 248 ? 16.950  44.364 2.165   1.00 16.87  ? 904  SER   A CA  1 
ATOM   1916 C C   . SER   A 1 248 ? 16.335  43.764 0.925   1.00 20.55  ? 904  SER   A C   1 
ATOM   1917 O O   . SER   A 1 248 ? 15.316  43.092 1.038   1.00 20.07  ? 904  SER   A O   1 
ATOM   1918 C CB  . SER   A 1 248 ? 16.503  45.813 2.319   1.00 17.04  ? 904  SER   A CB  1 
ATOM   1919 O OG  . SER   A 1 248 ? 16.607  46.222 3.668   1.00 21.58  ? 904  SER   A OG  1 
ATOM   1920 N N   . ALA   A 1 249 ? 16.958  43.986 -0.262  1.00 17.17  ? 905  ALA   A N   1 
ATOM   1921 C CA  . ALA   A 1 249 ? 16.464  43.455 -1.538  1.00 17.47  ? 905  ALA   A CA  1 
ATOM   1922 C C   . ALA   A 1 249 ? 16.438  41.913 -1.551  1.00 21.20  ? 905  ALA   A C   1 
ATOM   1923 O O   . ALA   A 1 249 ? 15.657  41.326 -2.299  1.00 19.25  ? 905  ALA   A O   1 
ATOM   1924 C CB  . ALA   A 1 249 ? 17.268  44.008 -2.696  1.00 18.44  ? 905  ALA   A CB  1 
ATOM   1925 N N   . ASN   A 1 250 ? 17.246  41.266 -0.664  1.00 17.73  ? 906  ASN   A N   1 
ATOM   1926 C CA  . ASN   A 1 250 ? 17.246  39.807 -0.480  1.00 17.45  ? 906  ASN   A CA  1 
ATOM   1927 C C   . ASN   A 1 250 ? 15.909  39.350 0.123   1.00 19.36  ? 906  ASN   A C   1 
ATOM   1928 O O   . ASN   A 1 250 ? 15.501  38.210 -0.096  1.00 19.54  ? 906  ASN   A O   1 
ATOM   1929 C CB  . ASN   A 1 250 ? 18.416  39.341 0.393   1.00 15.44  ? 906  ASN   A CB  1 
ATOM   1930 C CG  . ASN   A 1 250 ? 19.790  39.339 -0.243  1.00 30.31  ? 906  ASN   A CG  1 
ATOM   1931 O OD1 . ASN   A 1 250 ? 20.804  39.156 0.442   1.00 31.26  ? 906  ASN   A OD1 1 
ATOM   1932 N ND2 . ASN   A 1 250 ? 19.875  39.523 -1.548  1.00 15.16  ? 906  ASN   A ND2 1 
ATOM   1933 N N   . TYR   A 1 251 ? 15.215  40.246 0.839   1.00 16.41  ? 907  TYR   A N   1 
ATOM   1934 C CA  . TYR   A 1 251 ? 13.880  39.993 1.398   1.00 15.81  ? 907  TYR   A CA  1 
ATOM   1935 C C   . TYR   A 1 251 ? 12.735  40.085 0.361   1.00 20.59  ? 907  TYR   A C   1 
ATOM   1936 O O   . TYR   A 1 251 ? 11.594  39.776 0.698   1.00 20.00  ? 907  TYR   A O   1 
ATOM   1937 C CB  . TYR   A 1 251 ? 13.600  40.893 2.602   1.00 15.40  ? 907  TYR   A CB  1 
ATOM   1938 C CG  . TYR   A 1 251 ? 14.274  40.398 3.851   1.00 15.78  ? 907  TYR   A CG  1 
ATOM   1939 C CD1 . TYR   A 1 251 ? 13.727  39.357 4.594   1.00 17.96  ? 907  TYR   A CD1 1 
ATOM   1940 C CD2 . TYR   A 1 251 ? 15.492  40.926 4.261   1.00 15.70  ? 907  TYR   A CD2 1 
ATOM   1941 C CE1 . TYR   A 1 251 ? 14.354  38.887 5.741   1.00 20.61  ? 907  TYR   A CE1 1 
ATOM   1942 C CE2 . TYR   A 1 251 ? 16.120  40.475 5.412   1.00 15.87  ? 907  TYR   A CE2 1 
ATOM   1943 C CZ  . TYR   A 1 251 ? 15.560  39.443 6.140   1.00 19.16  ? 907  TYR   A CZ  1 
ATOM   1944 O OH  . TYR   A 1 251 ? 16.213  38.972 7.252   1.00 22.18  ? 907  TYR   A OH  1 
ATOM   1945 N N   . CYS   A 1 252 ? 13.040  40.485 -0.889  1.00 17.86  ? 908  CYS   A N   1 
ATOM   1946 C CA  . CYS   A 1 252 ? 12.069  40.547 -1.987  1.00 18.71  ? 908  CYS   A CA  1 
ATOM   1947 C C   . CYS   A 1 252 ? 11.736  39.146 -2.509  1.00 25.09  ? 908  CYS   A C   1 
ATOM   1948 O O   . CYS   A 1 252 ? 10.633  38.940 -3.026  1.00 26.91  ? 908  CYS   A O   1 
ATOM   1949 C CB  . CYS   A 1 252 ? 12.556  41.446 -3.115  1.00 18.44  ? 908  CYS   A CB  1 
ATOM   1950 S SG  . CYS   A 1 252 ? 12.817  43.163 -2.627  1.00 23.19  ? 908  CYS   A SG  1 
ATOM   1951 N N   . HIS   A 1 253 ? 12.680  38.197 -2.364  1.00 23.29  ? 909  HIS   A N   1 
ATOM   1952 C CA  . HIS   A 1 253 ? 12.593  36.791 -2.776  1.00 24.63  ? 909  HIS   A CA  1 
ATOM   1953 C C   . HIS   A 1 253 ? 12.182  36.660 -4.259  1.00 28.21  ? 909  HIS   A C   1 
ATOM   1954 O O   . HIS   A 1 253 ? 11.267  35.903 -4.625  1.00 29.75  ? 909  HIS   A O   1 
ATOM   1955 C CB  . HIS   A 1 253 ? 11.698  35.974 -1.818  1.00 26.94  ? 909  HIS   A CB  1 
ATOM   1956 C CG  . HIS   A 1 253 ? 12.296  35.796 -0.450  1.00 31.50  ? 909  HIS   A CG  1 
ATOM   1957 N ND1 . HIS   A 1 253 ? 13.130  34.731 -0.159  1.00 33.64  ? 909  HIS   A ND1 1 
ATOM   1958 C CD2 . HIS   A 1 253 ? 12.171  36.564 0.661   1.00 33.84  ? 909  HIS   A CD2 1 
ATOM   1959 C CE1 . HIS   A 1 253 ? 13.481  34.885 1.109   1.00 33.24  ? 909  HIS   A CE1 1 
ATOM   1960 N NE2 . HIS   A 1 253 ? 12.932  35.977 1.642   1.00 33.62  ? 909  HIS   A NE2 1 
ATOM   1961 N N   . THR   A 1 254 ? 12.843  37.456 -5.106  1.00 21.27  ? 910  THR   A N   1 
ATOM   1962 C CA  . THR   A 1 254 ? 12.655  37.462 -6.548  1.00 20.63  ? 910  THR   A CA  1 
ATOM   1963 C C   . THR   A 1 254 ? 13.458  36.290 -7.133  1.00 24.42  ? 910  THR   A C   1 
ATOM   1964 O O   . THR   A 1 254 ? 14.257  35.670 -6.425  1.00 25.01  ? 910  THR   A O   1 
ATOM   1965 C CB  . THR   A 1 254 ? 13.094  38.821 -7.142  1.00 23.95  ? 910  THR   A CB  1 
ATOM   1966 O OG1 . THR   A 1 254 ? 14.424  39.109 -6.724  1.00 24.79  ? 910  THR   A OG1 1 
ATOM   1967 C CG2 . THR   A 1 254 ? 12.147  39.974 -6.783  1.00 18.98  ? 910  THR   A CG2 1 
ATOM   1968 N N   . SER   A 1 255 ? 13.249  35.983 -8.418  1.00 21.00  ? 911  SER   A N   1 
ATOM   1969 C CA  . SER   A 1 255 ? 13.972  34.908 -9.122  1.00 20.52  ? 911  SER   A CA  1 
ATOM   1970 C C   . SER   A 1 255 ? 13.974  35.223 -10.596 1.00 26.04  ? 911  SER   A C   1 
ATOM   1971 O O   . SER   A 1 255 ? 13.488  36.274 -10.993 1.00 27.07  ? 911  SER   A O   1 
ATOM   1972 C CB  . SER   A 1 255 ? 13.328  33.544 -8.861  1.00 25.44  ? 911  SER   A CB  1 
ATOM   1973 O OG  . SER   A 1 255 ? 11.939  33.547 -9.172  1.00 34.99  ? 911  SER   A OG  1 
ATOM   1974 N N   . GLN   A 1 256 ? 14.527  34.331 -11.413 1.00 24.87  ? 912  GLN   A N   1 
ATOM   1975 C CA  . GLN   A 1 256 ? 14.566  34.442 -12.869 1.00 26.08  ? 912  GLN   A CA  1 
ATOM   1976 C C   . GLN   A 1 256 ? 13.132  34.414 -13.429 1.00 32.43  ? 912  GLN   A C   1 
ATOM   1977 O O   . GLN   A 1 256 ? 12.855  35.035 -14.447 1.00 31.23  ? 912  GLN   A O   1 
ATOM   1978 C CB  . GLN   A 1 256 ? 15.386  33.281 -13.451 1.00 27.70  ? 912  GLN   A CB  1 
ATOM   1979 C CG  . GLN   A 1 256 ? 16.889  33.550 -13.520 1.00 41.90  ? 912  GLN   A CG  1 
ATOM   1980 C CD  . GLN   A 1 256 ? 17.685  33.144 -12.295 1.00 48.71  ? 912  GLN   A CD  1 
ATOM   1981 O OE1 . GLN   A 1 256 ? 17.144  33.035 -11.182 1.00 40.68  ? 912  GLN   A OE1 1 
ATOM   1982 N NE2 . GLN   A 1 256 ? 18.986  32.957 -12.445 1.00 34.03  ? 912  GLN   A NE2 1 
ATOM   1983 N N   . GLY   A 1 257 ? 12.245  33.706 -12.727 1.00 32.82  ? 913  GLY   A N   1 
ATOM   1984 C CA  . GLY   A 1 257 ? 10.833  33.545 -13.053 1.00 33.88  ? 913  GLY   A CA  1 
ATOM   1985 C C   . GLY   A 1 257 ? 9.917   34.646 -12.543 1.00 38.81  ? 913  GLY   A C   1 
ATOM   1986 O O   . GLY   A 1 257 ? 8.721   34.607 -12.826 1.00 38.68  ? 913  GLY   A O   1 
ATOM   1987 N N   . ASP   A 1 258 ? 10.454  35.598 -11.741 1.00 34.82  ? 914  ASP   A N   1 
ATOM   1988 C CA  . ASP   A 1 258 ? 9.751   36.776 -11.183 1.00 33.40  ? 914  ASP   A CA  1 
ATOM   1989 C C   . ASP   A 1 258 ? 10.831  37.801 -10.741 1.00 31.89  ? 914  ASP   A C   1 
ATOM   1990 O O   . ASP   A 1 258 ? 11.153  37.853 -9.556  1.00 30.38  ? 914  ASP   A O   1 
ATOM   1991 C CB  . ASP   A 1 258 ? 8.821   36.383 -10.013 1.00 36.07  ? 914  ASP   A CB  1 
ATOM   1992 C CG  . ASP   A 1 258 ? 8.029   37.532 -9.392  1.00 54.87  ? 914  ASP   A CG  1 
ATOM   1993 O OD1 . ASP   A 1 258 ? 7.834   38.573 -10.079 1.00 56.38  ? 914  ASP   A OD1 1 
ATOM   1994 O OD2 . ASP   A 1 258 ? 7.599   37.391 -8.223  1.00 64.03  ? 914  ASP   A OD2 1 
ATOM   1995 N N   . PRO   A 1 259 ? 11.472  38.559 -11.681 1.00 26.15  ? 915  PRO   A N   1 
ATOM   1996 C CA  . PRO   A 1 259 ? 12.588  39.438 -11.275 1.00 24.89  ? 915  PRO   A CA  1 
ATOM   1997 C C   . PRO   A 1 259 ? 12.211  40.844 -10.811 1.00 28.14  ? 915  PRO   A C   1 
ATOM   1998 O O   . PRO   A 1 259 ? 13.093  41.673 -10.643 1.00 28.41  ? 915  PRO   A O   1 
ATOM   1999 C CB  . PRO   A 1 259 ? 13.465  39.463 -12.528 1.00 26.41  ? 915  PRO   A CB  1 
ATOM   2000 C CG  . PRO   A 1 259 ? 12.493  39.292 -13.664 1.00 30.02  ? 915  PRO   A CG  1 
ATOM   2001 C CD  . PRO   A 1 259 ? 11.269  38.594 -13.150 1.00 25.92  ? 915  PRO   A CD  1 
ATOM   2002 N N   . ILE   A 1 260 ? 10.914  41.119 -10.613 1.00 24.91  ? 916  ILE   A N   1 
ATOM   2003 C CA  . ILE   A 1 260 ? 10.443  42.440 -10.192 1.00 23.81  ? 916  ILE   A CA  1 
ATOM   2004 C C   . ILE   A 1 260 ? 10.141  42.437 -8.696  1.00 25.96  ? 916  ILE   A C   1 
ATOM   2005 O O   . ILE   A 1 260 ? 9.321   41.650 -8.233  1.00 21.83  ? 916  ILE   A O   1 
ATOM   2006 C CB  . ILE   A 1 260 ? 9.241   42.984 -11.050 1.00 26.75  ? 916  ILE   A CB  1 
ATOM   2007 C CG1 . ILE   A 1 260 ? 9.294   42.554 -12.556 1.00 27.26  ? 916  ILE   A CG1 1 
ATOM   2008 C CG2 . ILE   A 1 260 ? 9.107   44.511 -10.913 1.00 25.41  ? 916  ILE   A CG2 1 
ATOM   2009 C CD1 . ILE   A 1 260 ? 10.524  42.993 -13.405 1.00 33.60  ? 916  ILE   A CD1 1 
ATOM   2010 N N   . GLY   A 1 261 ? 10.834  43.302 -7.961  1.00 25.32  ? 917  GLY   A N   1 
ATOM   2011 C CA  . GLY   A 1 261 ? 10.673  43.434 -6.514  1.00 24.76  ? 917  GLY   A CA  1 
ATOM   2012 C C   . GLY   A 1 261 ? 10.274  44.828 -6.076  1.00 25.25  ? 917  GLY   A C   1 
ATOM   2013 O O   . GLY   A 1 261 ? 10.305  45.776 -6.871  1.00 24.36  ? 917  GLY   A O   1 
ATOM   2014 N N   . LEU   A 1 262 ? 9.906   44.951 -4.798  1.00 19.35  ? 918  LEU   A N   1 
ATOM   2015 C CA  . LEU   A 1 262 ? 9.513   46.214 -4.158  1.00 17.49  ? 918  LEU   A CA  1 
ATOM   2016 C C   . LEU   A 1 262 ? 10.292  46.434 -2.857  1.00 20.55  ? 918  LEU   A C   1 
ATOM   2017 O O   . LEU   A 1 262 ? 10.434  45.523 -2.040  1.00 21.04  ? 918  LEU   A O   1 
ATOM   2018 C CB  . LEU   A 1 262 ? 7.983   46.267 -3.892  1.00 16.16  ? 918  LEU   A CB  1 
ATOM   2019 C CG  . LEU   A 1 262 ? 7.028   46.356 -5.097  1.00 18.57  ? 918  LEU   A CG  1 
ATOM   2020 C CD1 . LEU   A 1 262 ? 5.565   46.099 -4.656  1.00 15.87  ? 918  LEU   A CD1 1 
ATOM   2021 C CD2 . LEU   A 1 262 ? 7.152   47.697 -5.802  1.00 20.30  ? 918  LEU   A CD2 1 
ATOM   2022 N N   . ILE   A 1 263 ? 10.799  47.637 -2.667  1.00 17.32  ? 919  ILE   A N   1 
ATOM   2023 C CA  . ILE   A 1 263 ? 11.583  47.958 -1.472  1.00 17.70  ? 919  ILE   A CA  1 
ATOM   2024 C C   . ILE   A 1 263 ? 11.202  49.313 -0.914  1.00 22.46  ? 919  ILE   A C   1 
ATOM   2025 O O   . ILE   A 1 263 ? 10.946  50.255 -1.686  1.00 23.67  ? 919  ILE   A O   1 
ATOM   2026 C CB  . ILE   A 1 263 ? 13.117  47.809 -1.762  1.00 20.60  ? 919  ILE   A CB  1 
ATOM   2027 C CG1 . ILE   A 1 263 ? 13.970  47.837 -0.468  1.00 19.43  ? 919  ILE   A CG1 1 
ATOM   2028 C CG2 . ILE   A 1 263 ? 13.605  48.841 -2.792  1.00 23.79  ? 919  ILE   A CG2 1 
ATOM   2029 C CD1 . ILE   A 1 263 ? 15.362  47.357 -0.641  1.00 28.80  ? 919  ILE   A CD1 1 
ATOM   2030 N N   . LEU   A 1 264 ? 11.118  49.412 0.419   1.00 18.20  ? 920  LEU   A N   1 
ATOM   2031 C CA  . LEU   A 1 264 ? 10.740  50.700 1.033   1.00 17.72  ? 920  LEU   A CA  1 
ATOM   2032 C C   . LEU   A 1 264 ? 11.959  51.452 1.503   1.00 21.54  ? 920  LEU   A C   1 
ATOM   2033 O O   . LEU   A 1 264 ? 12.995  50.843 1.793   1.00 19.92  ? 920  LEU   A O   1 
ATOM   2034 C CB  . LEU   A 1 264 ? 9.830   50.499 2.264   1.00 17.18  ? 920  LEU   A CB  1 
ATOM   2035 C CG  . LEU   A 1 264 ? 8.505   49.823 2.064   1.00 22.17  ? 920  LEU   A CG  1 
ATOM   2036 C CD1 . LEU   A 1 264 ? 8.055   49.171 3.359   1.00 21.39  ? 920  LEU   A CD1 1 
ATOM   2037 C CD2 . LEU   A 1 264 ? 7.478   50.812 1.515   1.00 23.35  ? 920  LEU   A CD2 1 
ATOM   2038 N N   . LEU   A 1 265 ? 11.795  52.768 1.633   1.00 19.15  ? 921  LEU   A N   1 
ATOM   2039 C CA  . LEU   A 1 265 ? 12.707  53.721 2.254   1.00 19.63  ? 921  LEU   A CA  1 
ATOM   2040 C C   . LEU   A 1 265 ? 11.898  54.403 3.348   1.00 23.70  ? 921  LEU   A C   1 
ATOM   2041 O O   . LEU   A 1 265 ? 10.904  55.083 3.053   1.00 22.34  ? 921  LEU   A O   1 
ATOM   2042 C CB  . LEU   A 1 265 ? 13.265  54.756 1.267   1.00 19.85  ? 921  LEU   A CB  1 
ATOM   2043 C CG  . LEU   A 1 265 ? 14.556  54.384 0.563   1.00 23.90  ? 921  LEU   A CG  1 
ATOM   2044 C CD1 . LEU   A 1 265 ? 14.920  55.432 -0.499  1.00 24.21  ? 921  LEU   A CD1 1 
ATOM   2045 C CD2 . LEU   A 1 265 ? 15.718  54.197 1.567   1.00 24.54  ? 921  LEU   A CD2 1 
ATOM   2046 N N   . GLY   A 1 266 ? 12.261  54.133 4.602   1.00 20.15  ? 922  GLY   A N   1 
ATOM   2047 C CA  . GLY   A 1 266 ? 11.540  54.699 5.735   1.00 19.40  ? 922  GLY   A CA  1 
ATOM   2048 C C   . GLY   A 1 266 ? 12.402  55.565 6.622   1.00 25.14  ? 922  GLY   A C   1 
ATOM   2049 O O   . GLY   A 1 266 ? 13.597  55.302 6.794   1.00 24.62  ? 922  GLY   A O   1 
ATOM   2050 N N   . GLU   A 1 267 ? 11.809  56.611 7.192   1.00 22.31  ? 923  GLU   A N   1 
ATOM   2051 C CA  . GLU   A 1 267 ? 12.512  57.450 8.137   1.00 21.47  ? 923  GLU   A CA  1 
ATOM   2052 C C   . GLU   A 1 267 ? 12.273  56.792 9.483   1.00 25.24  ? 923  GLU   A C   1 
ATOM   2053 O O   . GLU   A 1 267 ? 11.123  56.635 9.918   1.00 24.32  ? 923  GLU   A O   1 
ATOM   2054 C CB  . GLU   A 1 267 ? 12.027  58.893 8.126   1.00 23.45  ? 923  GLU   A CB  1 
ATOM   2055 C CG  . GLU   A 1 267 ? 12.683  59.722 9.225   1.00 31.92  ? 923  GLU   A CG  1 
ATOM   2056 C CD  . GLU   A 1 267 ? 12.133  61.113 9.454   1.00 42.37  ? 923  GLU   A CD  1 
ATOM   2057 O OE1 . GLU   A 1 267 ? 11.468  61.644 8.540   1.00 28.71  ? 923  GLU   A OE1 1 
ATOM   2058 O OE2 . GLU   A 1 267 ? 12.396  61.685 10.536  1.00 37.66  ? 923  GLU   A OE2 1 
ATOM   2059 N N   . VAL   A 1 268 ? 13.376  56.358 10.118  1.00 20.98  ? 924  VAL   A N   1 
ATOM   2060 C CA  . VAL   A 1 268 ? 13.342  55.625 11.372  1.00 19.92  ? 924  VAL   A CA  1 
ATOM   2061 C C   . VAL   A 1 268 ? 13.986  56.463 12.478  1.00 25.30  ? 924  VAL   A C   1 
ATOM   2062 O O   . VAL   A 1 268 ? 15.148  56.886 12.367  1.00 22.43  ? 924  VAL   A O   1 
ATOM   2063 C CB  . VAL   A 1 268 ? 14.027  54.236 11.194  1.00 22.22  ? 924  VAL   A CB  1 
ATOM   2064 C CG1 . VAL   A 1 268 ? 13.896  53.375 12.434  1.00 21.01  ? 924  VAL   A CG1 1 
ATOM   2065 C CG2 . VAL   A 1 268 ? 13.498  53.495 9.960   1.00 21.56  ? 924  VAL   A CG2 1 
ATOM   2066 N N   . ALA   A 1 269 ? 13.209  56.710 13.545  1.00 23.32  ? 925  ALA   A N   1 
ATOM   2067 C CA  . ALA   A 1 269 ? 13.667  57.449 14.719  1.00 22.25  ? 925  ALA   A CA  1 
ATOM   2068 C C   . ALA   A 1 269 ? 14.408  56.439 15.602  1.00 25.27  ? 925  ALA   A C   1 
ATOM   2069 O O   . ALA   A 1 269 ? 13.781  55.670 16.351  1.00 24.76  ? 925  ALA   A O   1 
ATOM   2070 C CB  . ALA   A 1 269 ? 12.478  58.037 15.456  1.00 22.73  ? 925  ALA   A CB  1 
ATOM   2071 N N   . LEU   A 1 270 ? 15.747  56.388 15.438  1.00 20.10  ? 926  LEU   A N   1 
ATOM   2072 C CA  . LEU   A 1 270 ? 16.594  55.438 16.141  1.00 19.54  ? 926  LEU   A CA  1 
ATOM   2073 C C   . LEU   A 1 270 ? 16.935  55.859 17.559  1.00 24.57  ? 926  LEU   A C   1 
ATOM   2074 O O   . LEU   A 1 270 ? 17.077  55.001 18.430  1.00 23.18  ? 926  LEU   A O   1 
ATOM   2075 C CB  . LEU   A 1 270 ? 17.871  55.111 15.335  1.00 19.30  ? 926  LEU   A CB  1 
ATOM   2076 C CG  . LEU   A 1 270 ? 17.675  54.464 13.963  1.00 23.21  ? 926  LEU   A CG  1 
ATOM   2077 C CD1 . LEU   A 1 270 ? 18.988  54.495 13.157  1.00 22.52  ? 926  LEU   A CD1 1 
ATOM   2078 C CD2 . LEU   A 1 270 ? 17.140  53.025 14.097  1.00 23.78  ? 926  LEU   A CD2 1 
ATOM   2079 N N   . GLY   A 1 271 ? 17.050  57.165 17.791  1.00 23.95  ? 927  GLY   A N   1 
ATOM   2080 C CA  . GLY   A 1 271 ? 17.414  57.683 19.101  1.00 25.00  ? 927  GLY   A CA  1 
ATOM   2081 C C   . GLY   A 1 271 ? 18.701  57.038 19.584  1.00 31.34  ? 927  GLY   A C   1 
ATOM   2082 O O   . GLY   A 1 271 ? 19.599  56.750 18.784  1.00 30.23  ? 927  GLY   A O   1 
ATOM   2083 N N   . ASN   A 1 272 ? 18.741  56.703 20.884  1.00 29.87  ? 928  ASN   A N   1 
ATOM   2084 C CA  . ASN   A 1 272 ? 19.877  56.048 21.542  1.00 29.90  ? 928  ASN   A CA  1 
ATOM   2085 C C   . ASN   A 1 272 ? 19.856  54.560 21.176  1.00 30.04  ? 928  ASN   A C   1 
ATOM   2086 O O   . ASN   A 1 272 ? 18.932  53.834 21.573  1.00 29.26  ? 928  ASN   A O   1 
ATOM   2087 C CB  . ASN   A 1 272 ? 19.779  56.262 23.067  1.00 35.44  ? 928  ASN   A CB  1 
ATOM   2088 C CG  . ASN   A 1 272 ? 21.065  56.110 23.843  1.00 66.48  ? 928  ASN   A CG  1 
ATOM   2089 O OD1 . ASN   A 1 272 ? 21.915  55.254 23.564  1.00 59.04  ? 928  ASN   A OD1 1 
ATOM   2090 N ND2 . ASN   A 1 272 ? 21.217  56.930 24.865  1.00 64.18  ? 928  ASN   A ND2 1 
ATOM   2091 N N   . MET   A 1 273 ? 20.846  54.129 20.363  1.00 24.00  ? 929  MET   A N   1 
ATOM   2092 C CA  . MET   A 1 273 ? 20.962  52.753 19.864  1.00 22.13  ? 929  MET   A CA  1 
ATOM   2093 C C   . MET   A 1 273 ? 21.638  51.808 20.858  1.00 24.85  ? 929  MET   A C   1 
ATOM   2094 O O   . MET   A 1 273 ? 22.685  52.129 21.398  1.00 24.62  ? 929  MET   A O   1 
ATOM   2095 C CB  . MET   A 1 273 ? 21.720  52.704 18.525  1.00 23.88  ? 929  MET   A CB  1 
ATOM   2096 C CG  . MET   A 1 273 ? 21.095  53.538 17.419  1.00 27.57  ? 929  MET   A CG  1 
ATOM   2097 S SD  . MET   A 1 273 ? 21.964  53.525 15.823  1.00 31.71  ? 929  MET   A SD  1 
ATOM   2098 C CE  . MET   A 1 273 ? 23.593  54.229 16.324  1.00 28.88  ? 929  MET   A CE  1 
ATOM   2099 N N   . TYR   A 1 274 ? 21.054  50.633 21.055  1.00 21.66  ? 930  TYR   A N   1 
ATOM   2100 C CA  . TYR   A 1 274 ? 21.596  49.566 21.885  1.00 22.21  ? 930  TYR   A CA  1 
ATOM   2101 C C   . TYR   A 1 274 ? 22.354  48.657 20.891  1.00 24.18  ? 930  TYR   A C   1 
ATOM   2102 O O   . TYR   A 1 274 ? 21.749  48.001 20.037  1.00 21.90  ? 930  TYR   A O   1 
ATOM   2103 C CB  . TYR   A 1 274 ? 20.450  48.846 22.630  1.00 24.60  ? 930  TYR   A CB  1 
ATOM   2104 C CG  . TYR   A 1 274 ? 20.861  47.683 23.506  1.00 26.25  ? 930  TYR   A CG  1 
ATOM   2105 C CD1 . TYR   A 1 274 ? 21.997  47.752 24.304  1.00 28.13  ? 930  TYR   A CD1 1 
ATOM   2106 C CD2 . TYR   A 1 274 ? 20.069  46.544 23.597  1.00 27.36  ? 930  TYR   A CD2 1 
ATOM   2107 C CE1 . TYR   A 1 274 ? 22.388  46.674 25.098  1.00 29.13  ? 930  TYR   A CE1 1 
ATOM   2108 C CE2 . TYR   A 1 274 ? 20.437  45.466 24.403  1.00 28.55  ? 930  TYR   A CE2 1 
ATOM   2109 C CZ  . TYR   A 1 274 ? 21.583  45.545 25.171  1.00 33.80  ? 930  TYR   A CZ  1 
ATOM   2110 O OH  . TYR   A 1 274 ? 21.919  44.475 25.964  1.00 33.92  ? 930  TYR   A OH  1 
ATOM   2111 N N   . GLU   A 1 275 ? 23.682  48.751 20.926  1.00 21.60  ? 931  GLU   A N   1 
ATOM   2112 C CA  . GLU   A 1 275 ? 24.609  48.113 19.989  1.00 22.85  ? 931  GLU   A CA  1 
ATOM   2113 C C   . GLU   A 1 275 ? 24.948  46.677 20.366  1.00 29.32  ? 931  GLU   A C   1 
ATOM   2114 O O   . GLU   A 1 275 ? 25.489  46.420 21.452  1.00 31.24  ? 931  GLU   A O   1 
ATOM   2115 C CB  . GLU   A 1 275 ? 25.875  48.973 19.800  1.00 24.14  ? 931  GLU   A CB  1 
ATOM   2116 C CG  . GLU   A 1 275 ? 25.592  50.332 19.171  1.00 32.04  ? 931  GLU   A CG  1 
ATOM   2117 C CD  . GLU   A 1 275 ? 26.766  51.165 18.680  1.00 57.59  ? 931  GLU   A CD  1 
ATOM   2118 O OE1 . GLU   A 1 275 ? 27.934  50.781 18.921  1.00 51.85  ? 931  GLU   A OE1 1 
ATOM   2119 O OE2 . GLU   A 1 275 ? 26.512  52.214 18.047  1.00 60.59  ? 931  GLU   A OE2 1 
ATOM   2120 N N   . LEU   A 1 276 ? 24.600  45.731 19.463  1.00 22.81  ? 932  LEU   A N   1 
ATOM   2121 C CA  . LEU   A 1 276 ? 24.805  44.303 19.679  1.00 20.72  ? 932  LEU   A CA  1 
ATOM   2122 C C   . LEU   A 1 276 ? 25.471  43.649 18.478  1.00 25.21  ? 932  LEU   A C   1 
ATOM   2123 O O   . LEU   A 1 276 ? 25.226  44.047 17.342  1.00 24.37  ? 932  LEU   A O   1 
ATOM   2124 C CB  . LEU   A 1 276 ? 23.455  43.610 19.992  1.00 20.32  ? 932  LEU   A CB  1 
ATOM   2125 C CG  . LEU   A 1 276 ? 22.676  44.096 21.230  1.00 22.66  ? 932  LEU   A CG  1 
ATOM   2126 C CD1 . LEU   A 1 276 ? 21.216  43.699 21.150  1.00 22.46  ? 932  LEU   A CD1 1 
ATOM   2127 C CD2 . LEU   A 1 276 ? 23.307  43.588 22.507  1.00 21.81  ? 932  LEU   A CD2 1 
ATOM   2128 N N   . LYS   A 1 277 ? 26.291  42.627 18.734  1.00 23.48  ? 933  LYS   A N   1 
ATOM   2129 C CA  . LYS   A 1 277 ? 27.028  41.870 17.705  1.00 23.81  ? 933  LYS   A CA  1 
ATOM   2130 C C   . LYS   A 1 277 ? 26.412  40.479 17.445  1.00 30.62  ? 933  LYS   A C   1 
ATOM   2131 O O   . LYS   A 1 277 ? 26.758  39.841 16.444  1.00 32.12  ? 933  LYS   A O   1 
ATOM   2132 C CB  . LYS   A 1 277 ? 28.479  41.664 18.151  1.00 23.48  ? 933  LYS   A CB  1 
ATOM   2133 C CG  . LYS   A 1 277 ? 29.315  42.918 18.305  1.00 33.41  ? 933  LYS   A CG  1 
ATOM   2134 C CD  . LYS   A 1 277 ? 30.729  42.550 18.768  1.00 45.42  ? 933  LYS   A CD  1 
ATOM   2135 C CE  . LYS   A 1 277 ? 31.578  43.769 19.043  1.00 62.87  ? 933  LYS   A CE  1 
ATOM   2136 N NZ  . LYS   A 1 277 ? 32.966  43.407 19.440  1.00 74.42  ? 933  LYS   A NZ  1 
ATOM   2137 N N   . HIS   A 1 278 ? 25.595  39.965 18.411  1.00 26.33  ? 934  HIS   A N   1 
ATOM   2138 C CA  . HIS   A 1 278 ? 25.021  38.608 18.375  1.00 25.45  ? 934  HIS   A CA  1 
ATOM   2139 C C   . HIS   A 1 278 ? 23.568  38.602 18.801  1.00 27.44  ? 934  HIS   A C   1 
ATOM   2140 O O   . HIS   A 1 278 ? 23.110  39.564 19.428  1.00 25.90  ? 934  HIS   A O   1 
ATOM   2141 C CB  . HIS   A 1 278 ? 25.840  37.641 19.266  1.00 26.01  ? 934  HIS   A CB  1 
ATOM   2142 C CG  . HIS   A 1 278 ? 27.318  37.853 19.192  1.00 28.81  ? 934  HIS   A CG  1 
ATOM   2143 N ND1 . HIS   A 1 278 ? 28.072  37.377 18.138  1.00 30.48  ? 934  HIS   A ND1 1 
ATOM   2144 C CD2 . HIS   A 1 278 ? 28.107  38.614 19.988  1.00 29.92  ? 934  HIS   A CD2 1 
ATOM   2145 C CE1 . HIS   A 1 278 ? 29.313  37.802 18.366  1.00 29.49  ? 934  HIS   A CE1 1 
ATOM   2146 N NE2 . HIS   A 1 278 ? 29.377  38.559 19.461  1.00 29.59  ? 934  HIS   A NE2 1 
ATOM   2147 N N   . ALA   A 1 279 ? 22.847  37.513 18.476  1.00 23.03  ? 935  ALA   A N   1 
ATOM   2148 C CA  . ALA   A 1 279 ? 21.422  37.351 18.783  1.00 22.75  ? 935  ALA   A CA  1 
ATOM   2149 C C   . ALA   A 1 279 ? 21.098  37.646 20.238  1.00 27.63  ? 935  ALA   A C   1 
ATOM   2150 O O   . ALA   A 1 279 ? 21.805  37.218 21.159  1.00 27.03  ? 935  ALA   A O   1 
ATOM   2151 C CB  . ALA   A 1 279 ? 20.942  35.958 18.417  1.00 22.83  ? 935  ALA   A CB  1 
ATOM   2152 N N   . SER   A 1 280 ? 20.062  38.446 20.417  1.00 24.40  ? 936  SER   A N   1 
ATOM   2153 C CA  . SER   A 1 280 ? 19.542  38.853 21.705  1.00 24.98  ? 936  SER   A CA  1 
ATOM   2154 C C   . SER   A 1 280 ? 18.011  38.903 21.548  1.00 26.63  ? 936  SER   A C   1 
ATOM   2155 O O   . SER   A 1 280 ? 17.478  39.846 20.994  1.00 25.34  ? 936  SER   A O   1 
ATOM   2156 C CB  . SER   A 1 280 ? 20.150  40.192 22.116  1.00 30.97  ? 936  SER   A CB  1 
ATOM   2157 O OG  . SER   A 1 280 ? 19.590  40.678 23.323  1.00 43.26  ? 936  SER   A OG  1 
ATOM   2158 N N   . HIS   A 1 281 ? 17.335  37.827 21.952  1.00 23.36  ? 937  HIS   A N   1 
ATOM   2159 C CA  . HIS   A 1 281 ? 15.880  37.638 21.844  1.00 23.59  ? 937  HIS   A CA  1 
ATOM   2160 C C   . HIS   A 1 281 ? 15.142  38.410 22.929  1.00 31.57  ? 937  HIS   A C   1 
ATOM   2161 O O   . HIS   A 1 281 ? 14.652  37.813 23.885  1.00 31.23  ? 937  HIS   A O   1 
ATOM   2162 C CB  . HIS   A 1 281 ? 15.541  36.130 21.827  1.00 22.60  ? 937  HIS   A CB  1 
ATOM   2163 C CG  . HIS   A 1 281 ? 16.322  35.373 20.802  1.00 24.71  ? 937  HIS   A CG  1 
ATOM   2164 N ND1 . HIS   A 1 281 ? 16.107  35.562 19.451  1.00 25.78  ? 937  HIS   A ND1 1 
ATOM   2165 C CD2 . HIS   A 1 281 ? 17.335  34.493 20.964  1.00 25.96  ? 937  HIS   A CD2 1 
ATOM   2166 C CE1 . HIS   A 1 281 ? 16.982  34.784 18.831  1.00 25.33  ? 937  HIS   A CE1 1 
ATOM   2167 N NE2 . HIS   A 1 281 ? 17.743  34.122 19.699  1.00 25.79  ? 937  HIS   A NE2 1 
ATOM   2168 N N   . ILE   A 1 282 ? 15.087  39.757 22.773  1.00 31.69  ? 938  ILE   A N   1 
ATOM   2169 C CA  . ILE   A 1 282 ? 14.509  40.712 23.736  1.00 33.01  ? 938  ILE   A CA  1 
ATOM   2170 C C   . ILE   A 1 282 ? 13.060  41.075 23.464  1.00 39.51  ? 938  ILE   A C   1 
ATOM   2171 O O   . ILE   A 1 282 ? 12.643  41.162 22.313  1.00 36.72  ? 938  ILE   A O   1 
ATOM   2172 C CB  . ILE   A 1 282 ? 15.365  42.002 23.891  1.00 36.15  ? 938  ILE   A CB  1 
ATOM   2173 C CG1 . ILE   A 1 282 ? 15.560  42.752 22.545  1.00 36.08  ? 938  ILE   A CG1 1 
ATOM   2174 C CG2 . ILE   A 1 282 ? 16.685  41.711 24.578  1.00 38.54  ? 938  ILE   A CG2 1 
ATOM   2175 C CD1 . ILE   A 1 282 ? 15.553  44.257 22.662  1.00 37.43  ? 938  ILE   A CD1 1 
ATOM   2176 N N   . SER   A 1 283 ? 12.318  41.352 24.549  1.00 41.38  ? 939  SER   A N   1 
ATOM   2177 C CA  . SER   A 1 283 ? 10.909  41.741 24.558  1.00 43.02  ? 939  SER   A CA  1 
ATOM   2178 C C   . SER   A 1 283 ? 10.771  43.270 24.754  1.00 47.41  ? 939  SER   A C   1 
ATOM   2179 O O   . SER   A 1 283 ? 9.868   43.894 24.188  1.00 47.83  ? 939  SER   A O   1 
ATOM   2180 C CB  . SER   A 1 283 ? 10.161  41.010 25.682  1.00 48.64  ? 939  SER   A CB  1 
ATOM   2181 O OG  . SER   A 1 283 ? 10.318  39.596 25.661  1.00 59.67  ? 939  SER   A OG  1 
ATOM   2182 N N   . LYS   A 1 284 ? 11.657  43.851 25.572  1.00 42.25  ? 940  LYS   A N   1 
ATOM   2183 C CA  . LYS   A 1 284 ? 11.676  45.276 25.900  1.00 40.87  ? 940  LYS   A CA  1 
ATOM   2184 C C   . LYS   A 1 284 ? 13.124  45.777 25.886  1.00 40.98  ? 940  LYS   A C   1 
ATOM   2185 O O   . LYS   A 1 284 ? 14.031  45.049 26.314  1.00 40.82  ? 940  LYS   A O   1 
ATOM   2186 C CB  . LYS   A 1 284 ? 11.013  45.478 27.287  1.00 44.23  ? 940  LYS   A CB  1 
ATOM   2187 C CG  . LYS   A 1 284 ? 11.012  46.907 27.842  1.00 65.52  ? 940  LYS   A CG  1 
ATOM   2188 C CD  . LYS   A 1 284 ? 10.234  47.003 29.168  1.00 76.17  ? 940  LYS   A CD  1 
ATOM   2189 C CE  . LYS   A 1 284 ? 8.876   47.620 28.992  1.00 80.25  ? 940  LYS   A CE  1 
ATOM   2190 N NZ  . LYS   A 1 284 ? 8.194   47.774 30.302  1.00 86.16  ? 940  LYS   A NZ  1 
ATOM   2191 N N   . LEU   A 1 285 ? 13.341  47.010 25.380  1.00 33.92  ? 941  LEU   A N   1 
ATOM   2192 C CA  . LEU   A 1 285 ? 14.669  47.648 25.359  1.00 32.86  ? 941  LEU   A CA  1 
ATOM   2193 C C   . LEU   A 1 285 ? 15.063  48.100 26.763  1.00 39.67  ? 941  LEU   A C   1 
ATOM   2194 O O   . LEU   A 1 285 ? 14.176  48.490 27.534  1.00 41.85  ? 941  LEU   A O   1 
ATOM   2195 C CB  . LEU   A 1 285 ? 14.665  48.903 24.474  1.00 31.47  ? 941  LEU   A CB  1 
ATOM   2196 C CG  . LEU   A 1 285 ? 14.753  48.716 22.987  1.00 34.86  ? 941  LEU   A CG  1 
ATOM   2197 C CD1 . LEU   A 1 285 ? 14.241  49.930 22.299  1.00 34.80  ? 941  LEU   A CD1 1 
ATOM   2198 C CD2 . LEU   A 1 285 ? 16.168  48.471 22.560  1.00 36.37  ? 941  LEU   A CD2 1 
ATOM   2199 N N   . PRO   A 1 286 ? 16.371  48.158 27.099  1.00 35.64  ? 942  PRO   A N   1 
ATOM   2200 C CA  . PRO   A 1 286 ? 16.762  48.739 28.402  1.00 35.48  ? 942  PRO   A CA  1 
ATOM   2201 C C   . PRO   A 1 286 ? 16.414  50.239 28.444  1.00 38.49  ? 942  PRO   A C   1 
ATOM   2202 O O   . PRO   A 1 286 ? 16.379  50.889 27.397  1.00 37.33  ? 942  PRO   A O   1 
ATOM   2203 C CB  . PRO   A 1 286 ? 18.295  48.540 28.455  1.00 36.45  ? 942  PRO   A CB  1 
ATOM   2204 C CG  . PRO   A 1 286 ? 18.640  47.675 27.321  1.00 40.68  ? 942  PRO   A CG  1 
ATOM   2205 C CD  . PRO   A 1 286 ? 17.555  47.782 26.298  1.00 36.52  ? 942  PRO   A CD  1 
ATOM   2206 N N   . LYS   A 1 287 ? 16.156  50.771 29.651  1.00 35.52  ? 943  LYS   A N   1 
ATOM   2207 C CA  . LYS   A 1 287 ? 15.827  52.176 29.920  1.00 35.00  ? 943  LYS   A CA  1 
ATOM   2208 C C   . LYS   A 1 287 ? 16.843  53.130 29.253  1.00 38.68  ? 943  LYS   A C   1 
ATOM   2209 O O   . LYS   A 1 287 ? 18.054  52.936 29.376  1.00 37.69  ? 943  LYS   A O   1 
ATOM   2210 C CB  . LYS   A 1 287 ? 15.792  52.416 31.439  1.00 36.45  ? 943  LYS   A CB  1 
ATOM   2211 C CG  . LYS   A 1 287 ? 14.403  52.530 32.036  1.00 45.01  ? 943  LYS   A CG  1 
ATOM   2212 C CD  . LYS   A 1 287 ? 14.472  52.767 33.544  1.00 58.97  ? 943  LYS   A CD  1 
ATOM   2213 C CE  . LYS   A 1 287 ? 14.829  54.195 33.932  1.00 65.39  ? 943  LYS   A CE  1 
ATOM   2214 N NZ  . LYS   A 1 287 ? 14.719  54.421 35.404  1.00 65.59  ? 943  LYS   A NZ  1 
ATOM   2215 N N   . GLY   A 1 288 ? 16.324  54.122 28.535  1.00 36.09  ? 944  GLY   A N   1 
ATOM   2216 C CA  . GLY   A 1 288 ? 17.134  55.107 27.830  1.00 35.57  ? 944  GLY   A CA  1 
ATOM   2217 C C   . GLY   A 1 288 ? 17.404  54.801 26.370  1.00 38.97  ? 944  GLY   A C   1 
ATOM   2218 O O   . GLY   A 1 288 ? 17.789  55.709 25.626  1.00 39.59  ? 944  GLY   A O   1 
ATOM   2219 N N   . LYS   A 1 289 ? 17.251  53.517 25.958  1.00 33.77  ? 945  LYS   A N   1 
ATOM   2220 C CA  . LYS   A 1 289 ? 17.436  53.050 24.574  1.00 32.68  ? 945  LYS   A CA  1 
ATOM   2221 C C   . LYS   A 1 289 ? 16.137  53.155 23.785  1.00 35.72  ? 945  LYS   A C   1 
ATOM   2222 O O   . LYS   A 1 289 ? 15.063  52.965 24.363  1.00 35.65  ? 945  LYS   A O   1 
ATOM   2223 C CB  . LYS   A 1 289 ? 17.961  51.604 24.534  1.00 33.27  ? 945  LYS   A CB  1 
ATOM   2224 C CG  . LYS   A 1 289 ? 19.314  51.404 25.206  1.00 28.97  ? 945  LYS   A CG  1 
ATOM   2225 C CD  . LYS   A 1 289 ? 20.453  52.173 24.516  1.00 28.61  ? 945  LYS   A CD  1 
ATOM   2226 C CE  . LYS   A 1 289 ? 21.752  51.976 25.225  1.00 25.56  ? 945  LYS   A CE  1 
ATOM   2227 N NZ  . LYS   A 1 289 ? 22.857  52.562 24.455  1.00 26.38  ? 945  LYS   A NZ  1 
ATOM   2228 N N   . HIS   A 1 290 ? 16.233  53.480 22.474  1.00 30.63  ? 946  HIS   A N   1 
ATOM   2229 C CA  . HIS   A 1 290 ? 15.069  53.642 21.579  1.00 29.84  ? 946  HIS   A CA  1 
ATOM   2230 C C   . HIS   A 1 290 ? 15.101  52.645 20.421  1.00 28.01  ? 946  HIS   A C   1 
ATOM   2231 O O   . HIS   A 1 290 ? 14.110  52.493 19.705  1.00 25.54  ? 946  HIS   A O   1 
ATOM   2232 C CB  . HIS   A 1 290 ? 15.020  55.068 20.997  1.00 31.28  ? 946  HIS   A CB  1 
ATOM   2233 C CG  . HIS   A 1 290 ? 15.115  56.159 22.012  1.00 35.45  ? 946  HIS   A CG  1 
ATOM   2234 N ND1 . HIS   A 1 290 ? 16.341  56.571 22.520  1.00 37.33  ? 946  HIS   A ND1 1 
ATOM   2235 C CD2 . HIS   A 1 290 ? 14.138  56.910 22.564  1.00 37.74  ? 946  HIS   A CD2 1 
ATOM   2236 C CE1 . HIS   A 1 290 ? 16.067  57.541 23.374  1.00 37.10  ? 946  HIS   A CE1 1 
ATOM   2237 N NE2 . HIS   A 1 290 ? 14.755  57.780 23.438  1.00 37.66  ? 946  HIS   A NE2 1 
ATOM   2238 N N   . SER   A 1 291 ? 16.255  52.001 20.208  1.00 23.48  ? 947  SER   A N   1 
ATOM   2239 C CA  . SER   A 1 291 ? 16.449  51.037 19.123  1.00 22.33  ? 947  SER   A CA  1 
ATOM   2240 C C   . SER   A 1 291 ? 17.595  50.111 19.428  1.00 25.10  ? 947  SER   A C   1 
ATOM   2241 O O   . SER   A 1 291 ? 18.341  50.317 20.391  1.00 25.36  ? 947  SER   A O   1 
ATOM   2242 C CB  . SER   A 1 291 ? 16.702  51.752 17.793  1.00 24.33  ? 947  SER   A CB  1 
ATOM   2243 O OG  . SER   A 1 291 ? 17.894  52.525 17.843  1.00 31.91  ? 947  SER   A OG  1 
ATOM   2244 N N   . VAL   A 1 292 ? 17.715  49.073 18.610  1.00 21.05  ? 948  VAL   A N   1 
ATOM   2245 C CA  . VAL   A 1 292 ? 18.803  48.128 18.648  1.00 21.00  ? 948  VAL   A CA  1 
ATOM   2246 C C   . VAL   A 1 292 ? 19.554  48.297 17.326  1.00 24.63  ? 948  VAL   A C   1 
ATOM   2247 O O   . VAL   A 1 292 ? 18.934  48.411 16.256  1.00 23.13  ? 948  VAL   A O   1 
ATOM   2248 C CB  . VAL   A 1 292 ? 18.350  46.659 18.895  1.00 23.98  ? 948  VAL   A CB  1 
ATOM   2249 C CG1 . VAL   A 1 292 ? 19.439  45.656 18.477  1.00 24.09  ? 948  VAL   A CG1 1 
ATOM   2250 C CG2 . VAL   A 1 292 ? 17.999  46.446 20.354  1.00 23.22  ? 948  VAL   A CG2 1 
ATOM   2251 N N   . LYS   A 1 293 ? 20.879  48.344 17.406  1.00 20.89  ? 949  LYS   A N   1 
ATOM   2252 C CA  . LYS   A 1 293 ? 21.669  48.351 16.207  1.00 20.36  ? 949  LYS   A CA  1 
ATOM   2253 C C   . LYS   A 1 293 ? 22.506  47.060 16.210  1.00 25.08  ? 949  LYS   A C   1 
ATOM   2254 O O   . LYS   A 1 293 ? 23.330  46.857 17.100  1.00 23.84  ? 949  LYS   A O   1 
ATOM   2255 C CB  . LYS   A 1 293 ? 22.536  49.627 16.051  1.00 21.10  ? 949  LYS   A CB  1 
ATOM   2256 C CG  . LYS   A 1 293 ? 23.344  49.592 14.747  1.00 13.08  ? 949  LYS   A CG  1 
ATOM   2257 C CD  . LYS   A 1 293 ? 24.297  50.739 14.584  1.00 18.25  ? 949  LYS   A CD  1 
ATOM   2258 C CE  . LYS   A 1 293 ? 25.046  50.631 13.282  1.00 18.86  ? 949  LYS   A CE  1 
ATOM   2259 N NZ  . LYS   A 1 293 ? 26.021  51.741 13.117  1.00 23.13  ? 949  LYS   A NZ  1 
ATOM   2260 N N   . GLY   A 1 294 ? 22.248  46.197 15.230  1.00 22.79  ? 950  GLY   A N   1 
ATOM   2261 C CA  . GLY   A 1 294 ? 23.042  45.003 14.984  1.00 22.28  ? 950  GLY   A CA  1 
ATOM   2262 C C   . GLY   A 1 294 ? 24.307  45.445 14.263  1.00 24.37  ? 950  GLY   A C   1 
ATOM   2263 O O   . GLY   A 1 294 ? 24.230  45.933 13.141  1.00 23.39  ? 950  GLY   A O   1 
ATOM   2264 N N   . LEU   A 1 295 ? 25.467  45.350 14.907  1.00 22.42  ? 951  LEU   A N   1 
ATOM   2265 C CA  . LEU   A 1 295 ? 26.732  45.859 14.329  1.00 20.88  ? 951  LEU   A CA  1 
ATOM   2266 C C   . LEU   A 1 295 ? 27.359  44.942 13.286  1.00 24.42  ? 951  LEU   A C   1 
ATOM   2267 O O   . LEU   A 1 295 ? 27.816  43.869 13.633  1.00 26.30  ? 951  LEU   A O   1 
ATOM   2268 C CB  . LEU   A 1 295 ? 27.759  46.204 15.410  1.00 20.46  ? 951  LEU   A CB  1 
ATOM   2269 C CG  . LEU   A 1 295 ? 27.359  47.094 16.603  1.00 24.12  ? 951  LEU   A CG  1 
ATOM   2270 C CD1 . LEU   A 1 295 ? 28.494  47.130 17.647  1.00 23.28  ? 951  LEU   A CD1 1 
ATOM   2271 C CD2 . LEU   A 1 295 ? 27.029  48.510 16.154  1.00 26.10  ? 951  LEU   A CD2 1 
ATOM   2272 N N   . GLY   A 1 296 ? 27.373  45.377 12.027  1.00 18.18  ? 952  GLY   A N   1 
ATOM   2273 C CA  . GLY   A 1 296 ? 27.961  44.637 10.936  1.00 18.28  ? 952  GLY   A CA  1 
ATOM   2274 C C   . GLY   A 1 296 ? 29.442  44.910 10.789  1.00 24.72  ? 952  GLY   A C   1 
ATOM   2275 O O   . GLY   A 1 296 ? 29.937  45.933 11.293  1.00 25.35  ? 952  GLY   A O   1 
ATOM   2276 N N   . LYS   A 1 297 ? 30.177  43.960 10.132  1.00 21.59  ? 953  LYS   A N   1 
ATOM   2277 C CA  . LYS   A 1 297 ? 31.620  44.077 9.830   1.00 22.40  ? 953  LYS   A CA  1 
ATOM   2278 C C   . LYS   A 1 297 ? 31.803  45.208 8.842   1.00 26.06  ? 953  LYS   A C   1 
ATOM   2279 O O   . LYS   A 1 297 ? 32.804  45.904 8.876   1.00 24.36  ? 953  LYS   A O   1 
ATOM   2280 C CB  . LYS   A 1 297 ? 32.188  42.782 9.194   1.00 26.60  ? 953  LYS   A CB  1 
ATOM   2281 C CG  . LYS   A 1 297 ? 31.950  41.506 9.985   1.00 49.77  ? 953  LYS   A CG  1 
ATOM   2282 C CD  . LYS   A 1 297 ? 33.213  41.035 10.683  1.00 71.40  ? 953  LYS   A CD  1 
ATOM   2283 C CE  . LYS   A 1 297 ? 32.982  39.711 11.365  1.00 85.40  ? 953  LYS   A CE  1 
ATOM   2284 N NZ  . LYS   A 1 297 ? 34.234  39.144 11.919  1.00 92.31  ? 953  LYS   A NZ  1 
ATOM   2285 N N   . THR   A 1 298 ? 30.820  45.377 7.942   1.00 23.32  ? 954  THR   A N   1 
ATOM   2286 C CA  . THR   A 1 298 ? 30.858  46.406 6.922   1.00 20.93  ? 954  THR   A CA  1 
ATOM   2287 C C   . THR   A 1 298 ? 29.787  47.437 7.220   1.00 20.34  ? 954  THR   A C   1 
ATOM   2288 O O   . THR   A 1 298 ? 28.694  47.096 7.671   1.00 17.72  ? 954  THR   A O   1 
ATOM   2289 C CB  . THR   A 1 298 ? 30.789  45.748 5.529   1.00 22.01  ? 954  THR   A CB  1 
ATOM   2290 O OG1 . THR   A 1 298 ? 31.996  45.038 5.300   1.00 25.04  ? 954  THR   A OG1 1 
ATOM   2291 C CG2 . THR   A 1 298 ? 30.540  46.726 4.395   1.00 18.61  ? 954  THR   A CG2 1 
ATOM   2292 N N   . THR   A 1 299 ? 30.108  48.703 6.906   1.00 17.13  ? 955  THR   A N   1 
ATOM   2293 C CA  . THR   A 1 299 ? 29.220  49.845 7.034   1.00 16.44  ? 955  THR   A CA  1 
ATOM   2294 C C   . THR   A 1 299 ? 29.378  50.803 5.851   1.00 22.82  ? 955  THR   A C   1 
ATOM   2295 O O   . THR   A 1 299 ? 30.515  51.023 5.420   1.00 22.41  ? 955  THR   A O   1 
ATOM   2296 C CB  . THR   A 1 299 ? 29.429  50.575 8.389   1.00 22.82  ? 955  THR   A CB  1 
ATOM   2297 O OG1 . THR   A 1 299 ? 28.442  51.597 8.508   1.00 25.37  ? 955  THR   A OG1 1 
ATOM   2298 C CG2 . THR   A 1 299 ? 30.828  51.243 8.538   1.00 18.96  ? 955  THR   A CG2 1 
ATOM   2299 N N   . PRO   A 1 300 ? 28.291  51.455 5.354   1.00 21.21  ? 956  PRO   A N   1 
ATOM   2300 C CA  . PRO   A 1 300 ? 28.474  52.521 4.362   1.00 21.10  ? 956  PRO   A CA  1 
ATOM   2301 C C   . PRO   A 1 300 ? 29.364  53.602 4.997   1.00 28.69  ? 956  PRO   A C   1 
ATOM   2302 O O   . PRO   A 1 300 ? 29.226  53.859 6.203   1.00 30.15  ? 956  PRO   A O   1 
ATOM   2303 C CB  . PRO   A 1 300 ? 27.053  53.050 4.154   1.00 21.69  ? 956  PRO   A CB  1 
ATOM   2304 C CG  . PRO   A 1 300 ? 26.159  51.936 4.567   1.00 26.65  ? 956  PRO   A CG  1 
ATOM   2305 C CD  . PRO   A 1 300 ? 26.865  51.343 5.738   1.00 23.09  ? 956  PRO   A CD  1 
ATOM   2306 N N   . ASP   A 1 301 ? 30.325  54.166 4.232   1.00 26.03  ? 957  ASP   A N   1 
ATOM   2307 C CA  . ASP   A 1 301 ? 31.259  55.180 4.724   1.00 26.74  ? 957  ASP   A CA  1 
ATOM   2308 C C   . ASP   A 1 301 ? 30.530  56.339 5.461   1.00 37.29  ? 957  ASP   A C   1 
ATOM   2309 O O   . ASP   A 1 301 ? 29.792  57.087 4.811   1.00 36.46  ? 957  ASP   A O   1 
ATOM   2310 C CB  . ASP   A 1 301 ? 32.125  55.711 3.568   1.00 28.32  ? 957  ASP   A CB  1 
ATOM   2311 C CG  . ASP   A 1 301 ? 33.317  56.567 3.984   1.00 34.27  ? 957  ASP   A CG  1 
ATOM   2312 O OD1 . ASP   A 1 301 ? 33.626  56.618 5.196   1.00 34.67  ? 957  ASP   A OD1 1 
ATOM   2313 O OD2 . ASP   A 1 301 ? 33.936  57.178 3.100   1.00 34.95  ? 957  ASP   A OD2 1 
ATOM   2314 N N   . PRO   A 1 302 ? 30.710  56.475 6.812   1.00 37.46  ? 958  PRO   A N   1 
ATOM   2315 C CA  . PRO   A 1 302 ? 30.014  57.545 7.567   1.00 37.66  ? 958  PRO   A CA  1 
ATOM   2316 C C   . PRO   A 1 302 ? 30.308  58.986 7.141   1.00 44.34  ? 958  PRO   A C   1 
ATOM   2317 O O   . PRO   A 1 302 ? 29.471  59.856 7.371   1.00 45.29  ? 958  PRO   A O   1 
ATOM   2318 C CB  . PRO   A 1 302 ? 30.458  57.305 9.016   1.00 39.18  ? 958  PRO   A CB  1 
ATOM   2319 C CG  . PRO   A 1 302 ? 30.939  55.903 9.051   1.00 43.52  ? 958  PRO   A CG  1 
ATOM   2320 C CD  . PRO   A 1 302 ? 31.551  55.664 7.716   1.00 39.03  ? 958  PRO   A CD  1 
ATOM   2321 N N   . SER   A 1 303 ? 31.477  59.252 6.532   1.00 40.79  ? 959  SER   A N   1 
ATOM   2322 C CA  . SER   A 1 303 ? 31.803  60.597 6.067   1.00 40.74  ? 959  SER   A CA  1 
ATOM   2323 C C   . SER   A 1 303 ? 31.076  60.955 4.749   1.00 43.10  ? 959  SER   A C   1 
ATOM   2324 O O   . SER   A 1 303 ? 31.067  62.122 4.337   1.00 42.88  ? 959  SER   A O   1 
ATOM   2325 C CB  . SER   A 1 303 ? 33.312  60.790 5.963   1.00 45.89  ? 959  SER   A CB  1 
ATOM   2326 O OG  . SER   A 1 303 ? 33.951  59.725 5.278   1.00 58.72  ? 959  SER   A OG  1 
ATOM   2327 N N   . ALA   A 1 304 ? 30.425  59.952 4.122   1.00 37.48  ? 960  ALA   A N   1 
ATOM   2328 C CA  . ALA   A 1 304 ? 29.674  60.110 2.881   1.00 36.17  ? 960  ALA   A CA  1 
ATOM   2329 C C   . ALA   A 1 304 ? 28.156  60.307 3.101   1.00 38.08  ? 960  ALA   A C   1 
ATOM   2330 O O   . ALA   A 1 304 ? 27.413  60.429 2.127   1.00 35.28  ? 960  ALA   A O   1 
ATOM   2331 C CB  . ALA   A 1 304 ? 29.944  58.939 1.961   1.00 36.71  ? 960  ALA   A CB  1 
ATOM   2332 N N   . ASN   A 1 305 ? 27.712  60.397 4.381   1.00 35.83  ? 961  ASN   A N   1 
ATOM   2333 C CA  . ASN   A 1 305 ? 26.314  60.643 4.763   1.00 36.40  ? 961  ASN   A CA  1 
ATOM   2334 C C   . ASN   A 1 305 ? 25.836  61.988 4.217   1.00 41.14  ? 961  ASN   A C   1 
ATOM   2335 O O   . ASN   A 1 305 ? 26.563  62.980 4.294   1.00 40.54  ? 961  ASN   A O   1 
ATOM   2336 C CB  . ASN   A 1 305 ? 26.139  60.591 6.286   1.00 35.61  ? 961  ASN   A CB  1 
ATOM   2337 C CG  . ASN   A 1 305 ? 25.658  59.260 6.813   1.00 51.33  ? 961  ASN   A CG  1 
ATOM   2338 O OD1 . ASN   A 1 305 ? 24.492  59.098 7.177   1.00 55.92  ? 961  ASN   A OD1 1 
ATOM   2339 N ND2 . ASN   A 1 305 ? 26.532  58.273 6.871   1.00 31.20  ? 961  ASN   A ND2 1 
ATOM   2340 N N   . ILE   A 1 306 ? 24.643  61.985 3.603   1.00 38.55  ? 962  ILE   A N   1 
ATOM   2341 C CA  . ILE   A 1 306 ? 23.955  63.114 2.964   1.00 38.88  ? 962  ILE   A CA  1 
ATOM   2342 C C   . ILE   A 1 306 ? 22.615  63.337 3.703   1.00 43.40  ? 962  ILE   A C   1 
ATOM   2343 O O   . ILE   A 1 306 ? 22.175  62.439 4.406   1.00 42.44  ? 962  ILE   A O   1 
ATOM   2344 C CB  . ILE   A 1 306 ? 23.800  62.795 1.431   1.00 42.36  ? 962  ILE   A CB  1 
ATOM   2345 C CG1 . ILE   A 1 306 ? 24.432  63.890 0.544   1.00 42.79  ? 962  ILE   A CG1 1 
ATOM   2346 C CG2 . ILE   A 1 306 ? 22.363  62.476 0.982   1.00 43.97  ? 962  ILE   A CG2 1 
ATOM   2347 C CD1 . ILE   A 1 306 ? 25.807  63.533 -0.048  1.00 37.83  ? 962  ILE   A CD1 1 
ATOM   2348 N N   . SER   A 1 307 ? 21.983  64.516 3.568   1.00 41.89  ? 963  SER   A N   1 
ATOM   2349 C CA  . SER   A 1 307 ? 20.711  64.836 4.221   1.00 41.85  ? 963  SER   A CA  1 
ATOM   2350 C C   . SER   A 1 307 ? 19.586  65.086 3.195   1.00 47.24  ? 963  SER   A C   1 
ATOM   2351 O O   . SER   A 1 307 ? 19.770  65.846 2.237   1.00 47.76  ? 963  SER   A O   1 
ATOM   2352 C CB  . SER   A 1 307 ? 20.872  66.035 5.154   1.00 45.13  ? 963  SER   A CB  1 
ATOM   2353 O OG  . SER   A 1 307 ? 19.715  66.220 5.955   1.00 57.10  ? 963  SER   A OG  1 
ATOM   2354 N N   . LEU   A 1 308 ? 18.441  64.413 3.384   1.00 43.72  ? 964  LEU   A N   1 
ATOM   2355 C CA  . LEU   A 1 308 ? 17.245  64.532 2.548   1.00 44.06  ? 964  LEU   A CA  1 
ATOM   2356 C C   . LEU   A 1 308 ? 16.063  64.786 3.493   1.00 48.48  ? 964  LEU   A C   1 
ATOM   2357 O O   . LEU   A 1 308 ? 15.590  63.863 4.166   1.00 48.22  ? 964  LEU   A O   1 
ATOM   2358 C CB  . LEU   A 1 308 ? 17.036  63.285 1.634   1.00 44.10  ? 964  LEU   A CB  1 
ATOM   2359 C CG  . LEU   A 1 308 ? 15.732  63.171 0.801   1.00 48.42  ? 964  LEU   A CG  1 
ATOM   2360 C CD1 . LEU   A 1 308 ? 15.566  64.328 -0.175  1.00 48.72  ? 964  LEU   A CD1 1 
ATOM   2361 C CD2 . LEU   A 1 308 ? 15.684  61.858 0.033   1.00 50.24  ? 964  LEU   A CD2 1 
ATOM   2362 N N   . ASP   A 1 309 ? 15.655  66.068 3.586   1.00 45.71  ? 965  ASP   A N   1 
ATOM   2363 C CA  . ASP   A 1 309 ? 14.585  66.600 4.445   1.00 45.93  ? 965  ASP   A CA  1 
ATOM   2364 C C   . ASP   A 1 309 ? 14.942  66.494 5.943   1.00 48.67  ? 965  ASP   A C   1 
ATOM   2365 O O   . ASP   A 1 309 ? 14.084  66.176 6.772   1.00 48.27  ? 965  ASP   A O   1 
ATOM   2366 C CB  . ASP   A 1 309 ? 13.203  65.991 4.109   1.00 48.42  ? 965  ASP   A CB  1 
ATOM   2367 C CG  . ASP   A 1 309 ? 12.614  66.514 2.807   1.00 65.40  ? 965  ASP   A CG  1 
ATOM   2368 O OD1 . ASP   A 1 309 ? 13.080  66.084 1.726   1.00 66.98  ? 965  ASP   A OD1 1 
ATOM   2369 O OD2 . ASP   A 1 309 ? 11.685  67.351 2.869   1.00 73.63  ? 965  ASP   A OD2 1 
ATOM   2370 N N   . GLY   A 1 310 ? 16.210  66.775 6.260   1.00 44.24  ? 966  GLY   A N   1 
ATOM   2371 C CA  . GLY   A 1 310 ? 16.745  66.742 7.620   1.00 43.74  ? 966  GLY   A CA  1 
ATOM   2372 C C   . GLY   A 1 310 ? 17.010  65.359 8.189   1.00 46.72  ? 966  GLY   A C   1 
ATOM   2373 O O   . GLY   A 1 310 ? 17.394  65.229 9.359   1.00 48.23  ? 966  GLY   A O   1 
ATOM   2374 N N   . VAL   A 1 311 ? 16.826  64.320 7.366   1.00 39.96  ? 967  VAL   A N   1 
ATOM   2375 C CA  . VAL   A 1 311 ? 17.029  62.915 7.745   1.00 37.89  ? 967  VAL   A CA  1 
ATOM   2376 C C   . VAL   A 1 311 ? 18.372  62.450 7.186   1.00 38.64  ? 967  VAL   A C   1 
ATOM   2377 O O   . VAL   A 1 311 ? 18.685  62.761 6.037   1.00 36.68  ? 967  VAL   A O   1 
ATOM   2378 C CB  . VAL   A 1 311 ? 15.868  62.030 7.224   1.00 40.53  ? 967  VAL   A CB  1 
ATOM   2379 C CG1 . VAL   A 1 311 ? 15.928  60.624 7.826   1.00 39.91  ? 967  VAL   A CG1 1 
ATOM   2380 C CG2 . VAL   A 1 311 ? 14.517  62.685 7.493   1.00 39.99  ? 967  VAL   A CG2 1 
ATOM   2381 N N   . ASP   A 1 312 ? 19.166  61.716 7.993   1.00 34.57  ? 968  ASP   A N   1 
ATOM   2382 C CA  . ASP   A 1 312 ? 20.463  61.207 7.545   1.00 33.67  ? 968  ASP   A CA  1 
ATOM   2383 C C   . ASP   A 1 312 ? 20.316  60.065 6.543   1.00 32.07  ? 968  ASP   A C   1 
ATOM   2384 O O   . ASP   A 1 312 ? 19.527  59.141 6.757   1.00 31.03  ? 968  ASP   A O   1 
ATOM   2385 C CB  . ASP   A 1 312 ? 21.360  60.832 8.731   1.00 37.12  ? 968  ASP   A CB  1 
ATOM   2386 C CG  . ASP   A 1 312 ? 22.303  61.963 9.122   1.00 56.82  ? 968  ASP   A CG  1 
ATOM   2387 O OD1 . ASP   A 1 312 ? 23.162  62.338 8.289   1.00 59.27  ? 968  ASP   A OD1 1 
ATOM   2388 O OD2 . ASP   A 1 312 ? 22.185  62.472 10.262  1.00 66.13  ? 968  ASP   A OD2 1 
ATOM   2389 N N   . VAL   A 1 313 ? 20.999  60.178 5.409   1.00 25.14  ? 969  VAL   A N   1 
ATOM   2390 C CA  . VAL   A 1 313 ? 20.938  59.169 4.347   1.00 25.19  ? 969  VAL   A CA  1 
ATOM   2391 C C   . VAL   A 1 313 ? 22.307  58.475 4.222   1.00 26.57  ? 969  VAL   A C   1 
ATOM   2392 O O   . VAL   A 1 313 ? 23.224  59.084 3.682   1.00 25.36  ? 969  VAL   A O   1 
ATOM   2393 C CB  . VAL   A 1 313 ? 20.394  59.737 2.997   1.00 29.11  ? 969  VAL   A CB  1 
ATOM   2394 C CG1 . VAL   A 1 313 ? 20.326  58.637 1.927   1.00 29.20  ? 969  VAL   A CG1 1 
ATOM   2395 C CG2 . VAL   A 1 313 ? 19.019  60.378 3.194   1.00 28.08  ? 969  VAL   A CG2 1 
ATOM   2396 N N   . PRO   A 1 314 ? 22.488  57.235 4.748   1.00 23.88  ? 970  PRO   A N   1 
ATOM   2397 C CA  . PRO   A 1 314 ? 23.833  56.606 4.686   1.00 24.39  ? 970  PRO   A CA  1 
ATOM   2398 C C   . PRO   A 1 314 ? 24.140  55.980 3.321   1.00 29.30  ? 970  PRO   A C   1 
ATOM   2399 O O   . PRO   A 1 314 ? 24.243  54.753 3.203   1.00 28.50  ? 970  PRO   A O   1 
ATOM   2400 C CB  . PRO   A 1 314 ? 23.801  55.565 5.831   1.00 25.28  ? 970  PRO   A CB  1 
ATOM   2401 C CG  . PRO   A 1 314 ? 22.357  55.213 5.980   1.00 28.80  ? 970  PRO   A CG  1 
ATOM   2402 C CD  . PRO   A 1 314 ? 21.520  56.369 5.460   1.00 23.83  ? 970  PRO   A CD  1 
ATOM   2403 N N   . LEU   A 1 315 ? 24.321  56.830 2.290   1.00 26.71  ? 971  LEU   A N   1 
ATOM   2404 C CA  . LEU   A 1 315 ? 24.557  56.359 0.923   1.00 25.97  ? 971  LEU   A CA  1 
ATOM   2405 C C   . LEU   A 1 315 ? 26.031  56.143 0.558   1.00 30.42  ? 971  LEU   A C   1 
ATOM   2406 O O   . LEU   A 1 315 ? 26.331  55.937 -0.620  1.00 29.90  ? 971  LEU   A O   1 
ATOM   2407 C CB  . LEU   A 1 315 ? 23.859  57.235 -0.137  1.00 25.35  ? 971  LEU   A CB  1 
ATOM   2408 C CG  . LEU   A 1 315 ? 23.924  58.753 -0.056  1.00 30.45  ? 971  LEU   A CG  1 
ATOM   2409 C CD1 . LEU   A 1 315 ? 25.364  59.298 -0.254  1.00 30.95  ? 971  LEU   A CD1 1 
ATOM   2410 C CD2 . LEU   A 1 315 ? 23.015  59.356 -1.108  1.00 32.64  ? 971  LEU   A CD2 1 
ATOM   2411 N N   . GLY   A 1 316 ? 26.928  56.181 1.545   1.00 27.73  ? 972  GLY   A N   1 
ATOM   2412 C CA  . GLY   A 1 316 ? 28.353  55.940 1.318   1.00 27.29  ? 972  GLY   A CA  1 
ATOM   2413 C C   . GLY   A 1 316 ? 28.628  54.523 0.853   1.00 29.77  ? 972  GLY   A C   1 
ATOM   2414 O O   . GLY   A 1 316 ? 27.761  53.654 1.017   1.00 29.02  ? 972  GLY   A O   1 
ATOM   2415 N N   . THR   A 1 317 ? 29.811  54.278 0.232   1.00 26.16  ? 973  THR   A N   1 
ATOM   2416 C CA  . THR   A 1 317 ? 30.143  52.917 -0.217  1.00 25.82  ? 973  THR   A CA  1 
ATOM   2417 C C   . THR   A 1 317 ? 30.574  52.102 0.989   1.00 27.92  ? 973  THR   A C   1 
ATOM   2418 O O   . THR   A 1 317 ? 31.046  52.683 1.969   1.00 26.80  ? 973  THR   A O   1 
ATOM   2419 C CB  . THR   A 1 317 ? 31.194  52.882 -1.346  1.00 37.50  ? 973  THR   A CB  1 
ATOM   2420 O OG1 . THR   A 1 317 ? 32.417  53.469 -0.901  1.00 32.20  ? 973  THR   A OG1 1 
ATOM   2421 C CG2 . THR   A 1 317 ? 30.704  53.521 -2.634  1.00 41.62  ? 973  THR   A CG2 1 
ATOM   2422 N N   . GLY   A 1 318 ? 30.390  50.784 0.912   1.00 24.15  ? 974  GLY   A N   1 
ATOM   2423 C CA  . GLY   A 1 318 ? 30.766  49.852 1.971   1.00 24.47  ? 974  GLY   A CA  1 
ATOM   2424 C C   . GLY   A 1 318 ? 32.250  49.842 2.331   1.00 27.85  ? 974  GLY   A C   1 
ATOM   2425 O O   . GLY   A 1 318 ? 33.119  49.595 1.481   1.00 26.01  ? 974  GLY   A O   1 
ATOM   2426 N N   . ILE   A 1 319 ? 32.541  50.155 3.605   1.00 24.42  ? 975  ILE   A N   1 
ATOM   2427 C CA  . ILE   A 1 319 ? 33.883  50.160 4.207   1.00 23.89  ? 975  ILE   A CA  1 
ATOM   2428 C C   . ILE   A 1 319 ? 33.812  49.316 5.513   1.00 27.48  ? 975  ILE   A C   1 
ATOM   2429 O O   . ILE   A 1 319 ? 32.712  49.027 6.001   1.00 25.86  ? 975  ILE   A O   1 
ATOM   2430 C CB  . ILE   A 1 319 ? 34.448  51.607 4.458   1.00 25.98  ? 975  ILE   A CB  1 
ATOM   2431 C CG1 . ILE   A 1 319 ? 33.716  52.330 5.619   1.00 24.58  ? 975  ILE   A CG1 1 
ATOM   2432 C CG2 . ILE   A 1 319 ? 34.461  52.456 3.172   1.00 26.61  ? 975  ILE   A CG2 1 
ATOM   2433 C CD1 . ILE   A 1 319 ? 34.524  53.285 6.378   1.00 17.17  ? 975  ILE   A CD1 1 
ATOM   2434 N N   . SER   A 1 320 ? 34.973  48.942 6.066   1.00 22.13  ? 976  SER   A N   1 
ATOM   2435 C CA  . SER   A 1 320 ? 35.066  48.202 7.327   1.00 22.43  ? 976  SER   A CA  1 
ATOM   2436 C C   . SER   A 1 320 ? 34.577  49.094 8.491   1.00 27.36  ? 976  SER   A C   1 
ATOM   2437 O O   . SER   A 1 320 ? 34.967  50.264 8.584   1.00 26.91  ? 976  SER   A O   1 
ATOM   2438 C CB  . SER   A 1 320 ? 36.515  47.782 7.570   1.00 24.83  ? 976  SER   A CB  1 
ATOM   2439 O OG  . SER   A 1 320 ? 36.696  47.230 8.864   1.00 34.41  ? 976  SER   A OG  1 
ATOM   2440 N N   . SER   A 1 321 ? 33.707  48.551 9.360   1.00 24.69  ? 977  SER   A N   1 
ATOM   2441 C CA  . SER   A 1 321 ? 33.208  49.280 10.534  1.00 24.24  ? 977  SER   A CA  1 
ATOM   2442 C C   . SER   A 1 321 ? 34.279  49.379 11.649  1.00 28.03  ? 977  SER   A C   1 
ATOM   2443 O O   . SER   A 1 321 ? 34.290  50.331 12.420  1.00 27.88  ? 977  SER   A O   1 
ATOM   2444 C CB  . SER   A 1 321 ? 31.953  48.611 11.086  1.00 25.95  ? 977  SER   A CB  1 
ATOM   2445 O OG  . SER   A 1 321 ? 32.216  47.287 11.509  1.00 23.24  ? 977  SER   A OG  1 
ATOM   2446 N N   . GLY   A 1 322 ? 35.149  48.381 11.713  1.00 24.80  ? 978  GLY   A N   1 
ATOM   2447 C CA  . GLY   A 1 322 ? 36.178  48.267 12.738  1.00 24.87  ? 978  GLY   A CA  1 
ATOM   2448 C C   . GLY   A 1 322 ? 35.730  47.272 13.786  1.00 29.78  ? 978  GLY   A C   1 
ATOM   2449 O O   . GLY   A 1 322 ? 36.526  46.870 14.639  1.00 30.39  ? 978  GLY   A O   1 
ATOM   2450 N N   . VAL   A 1 323 ? 34.449  46.840 13.697  1.00 25.17  ? 979  VAL   A N   1 
ATOM   2451 C CA  . VAL   A 1 323 ? 33.831  45.878 14.609  1.00 25.52  ? 979  VAL   A CA  1 
ATOM   2452 C C   . VAL   A 1 323 ? 34.385  44.442 14.385  1.00 32.42  ? 979  VAL   A C   1 
ATOM   2453 O O   . VAL   A 1 323 ? 34.362  43.902 13.276  1.00 32.86  ? 979  VAL   A O   1 
ATOM   2454 C CB  . VAL   A 1 323 ? 32.272  45.953 14.575  1.00 28.58  ? 979  VAL   A CB  1 
ATOM   2455 C CG1 . VAL   A 1 323 ? 31.637  44.857 15.426  1.00 28.86  ? 979  VAL   A CG1 1 
ATOM   2456 C CG2 . VAL   A 1 323 ? 31.788  47.324 15.048  1.00 27.89  ? 979  VAL   A CG2 1 
ATOM   2457 N N   . ASN   A 1 324 ? 34.890  43.852 15.461  1.00 30.36  ? 980  ASN   A N   1 
ATOM   2458 C CA  . ASN   A 1 324 ? 35.456  42.501 15.478  1.00 30.65  ? 980  ASN   A CA  1 
ATOM   2459 C C   . ASN   A 1 324 ? 34.490  41.473 16.102  1.00 33.92  ? 980  ASN   A C   1 
ATOM   2460 O O   . ASN   A 1 324 ? 33.700  41.817 16.986  1.00 31.12  ? 980  ASN   A O   1 
ATOM   2461 C CB  . ASN   A 1 324 ? 36.760  42.505 16.271  1.00 30.31  ? 980  ASN   A CB  1 
ATOM   2462 C CG  . ASN   A 1 324 ? 37.842  43.391 15.699  1.00 56.73  ? 980  ASN   A CG  1 
ATOM   2463 O OD1 . ASN   A 1 324 ? 38.085  43.428 14.486  1.00 51.06  ? 980  ASN   A OD1 1 
ATOM   2464 N ND2 . ASN   A 1 324 ? 38.522  44.122 16.570  1.00 52.22  ? 980  ASN   A ND2 1 
ATOM   2465 N N   . ASP   A 1 325 ? 34.621  40.198 15.667  1.00 31.56  ? 981  ASP   A N   1 
ATOM   2466 C CA  . ASP   A 1 325 ? 33.885  39.019 16.153  1.00 30.90  ? 981  ASP   A CA  1 
ATOM   2467 C C   . ASP   A 1 325 ? 32.374  39.232 16.249  1.00 32.04  ? 981  ASP   A C   1 
ATOM   2468 O O   . ASP   A 1 325 ? 31.768  38.903 17.265  1.00 31.30  ? 981  ASP   A O   1 
ATOM   2469 C CB  . ASP   A 1 325 ? 34.474  38.523 17.499  1.00 32.35  ? 981  ASP   A CB  1 
ATOM   2470 C CG  . ASP   A 1 325 ? 35.952  38.175 17.481  1.00 41.25  ? 981  ASP   A CG  1 
ATOM   2471 O OD1 . ASP   A 1 325 ? 36.563  38.230 16.391  1.00 39.87  ? 981  ASP   A OD1 1 
ATOM   2472 O OD2 . ASP   A 1 325 ? 36.493  37.827 18.559  1.00 49.85  ? 981  ASP   A OD2 1 
ATOM   2473 N N   . THR   A 1 326 ? 31.780  39.813 15.193  1.00 27.16  ? 982  THR   A N   1 
ATOM   2474 C CA  . THR   A 1 326 ? 30.351  40.046 15.133  1.00 27.11  ? 982  THR   A CA  1 
ATOM   2475 C C   . THR   A 1 326 ? 29.700  38.971 14.258  1.00 29.63  ? 982  THR   A C   1 
ATOM   2476 O O   . THR   A 1 326 ? 30.333  38.490 13.319  1.00 28.65  ? 982  THR   A O   1 
ATOM   2477 C CB  . THR   A 1 326 ? 30.003  41.492 14.715  1.00 33.65  ? 982  THR   A CB  1 
ATOM   2478 O OG1 . THR   A 1 326 ? 28.584  41.575 14.578  1.00 29.12  ? 982  THR   A OG1 1 
ATOM   2479 C CG2 . THR   A 1 326 ? 30.679  41.934 13.413  1.00 31.12  ? 982  THR   A CG2 1 
ATOM   2480 N N   . SER   A 1 327 ? 28.446  38.607 14.564  1.00 24.96  ? 983  SER   A N   1 
ATOM   2481 C CA  . SER   A 1 327 ? 27.702  37.593 13.807  1.00 24.94  ? 983  SER   A CA  1 
ATOM   2482 C C   . SER   A 1 327 ? 27.051  38.184 12.530  1.00 26.13  ? 983  SER   A C   1 
ATOM   2483 O O   . SER   A 1 327 ? 26.327  37.479 11.817  1.00 26.07  ? 983  SER   A O   1 
ATOM   2484 C CB  . SER   A 1 327 ? 26.630  36.952 14.692  1.00 28.33  ? 983  SER   A CB  1 
ATOM   2485 O OG  . SER   A 1 327 ? 27.154  36.115 15.712  1.00 41.13  ? 983  SER   A OG  1 
ATOM   2486 N N   . LEU   A 1 328 ? 27.303  39.478 12.251  1.00 18.78  ? 984  LEU   A N   1 
ATOM   2487 C CA  . LEU   A 1 328 ? 26.702  40.141 11.111  1.00 17.90  ? 984  LEU   A CA  1 
ATOM   2488 C C   . LEU   A 1 328 ? 27.694  40.711 10.168  1.00 19.53  ? 984  LEU   A C   1 
ATOM   2489 O O   . LEU   A 1 328 ? 28.584  41.436 10.564  1.00 16.89  ? 984  LEU   A O   1 
ATOM   2490 C CB  . LEU   A 1 328 ? 25.729  41.253 11.543  1.00 17.80  ? 984  LEU   A CB  1 
ATOM   2491 C CG  . LEU   A 1 328 ? 24.560  40.836 12.388  1.00 23.24  ? 984  LEU   A CG  1 
ATOM   2492 C CD1 . LEU   A 1 328 ? 24.152  41.962 13.289  1.00 24.73  ? 984  LEU   A CD1 1 
ATOM   2493 C CD2 . LEU   A 1 328 ? 23.381  40.372 11.524  1.00 28.79  ? 984  LEU   A CD2 1 
ATOM   2494 N N   . LEU   A 1 329 ? 27.446  40.473 8.892   1.00 19.09  ? 985  LEU   A N   1 
ATOM   2495 C CA  . LEU   A 1 329 ? 28.225  41.023 7.811   1.00 19.65  ? 985  LEU   A CA  1 
ATOM   2496 C C   . LEU   A 1 329 ? 27.867  42.479 7.653   1.00 20.01  ? 985  LEU   A C   1 
ATOM   2497 O O   . LEU   A 1 329 ? 28.729  43.273 7.337   1.00 18.95  ? 985  LEU   A O   1 
ATOM   2498 C CB  . LEU   A 1 329 ? 27.873  40.266 6.518   1.00 20.08  ? 985  LEU   A CB  1 
ATOM   2499 C CG  . LEU   A 1 329 ? 28.429  38.866 6.365   1.00 24.49  ? 985  LEU   A CG  1 
ATOM   2500 C CD1 . LEU   A 1 329 ? 27.965  38.253 5.032   1.00 24.01  ? 985  LEU   A CD1 1 
ATOM   2501 C CD2 . LEU   A 1 329 ? 29.944  38.891 6.455   1.00 28.91  ? 985  LEU   A CD2 1 
ATOM   2502 N N   . TYR   A 1 330 ? 26.587  42.820 7.857   1.00 17.95  ? 986  TYR   A N   1 
ATOM   2503 C CA  . TYR   A 1 330 ? 26.083  44.179 7.670   1.00 18.39  ? 986  TYR   A CA  1 
ATOM   2504 C C   . TYR   A 1 330 ? 25.230  44.592 8.805   1.00 21.24  ? 986  TYR   A C   1 
ATOM   2505 O O   . TYR   A 1 330 ? 24.679  43.751 9.516   1.00 21.62  ? 986  TYR   A O   1 
ATOM   2506 C CB  . TYR   A 1 330 ? 25.307  44.335 6.314   1.00 19.24  ? 986  TYR   A CB  1 
ATOM   2507 C CG  . TYR   A 1 330 ? 26.060  43.731 5.151   1.00 20.49  ? 986  TYR   A CG  1 
ATOM   2508 C CD1 . TYR   A 1 330 ? 27.250  44.299 4.694   1.00 21.10  ? 986  TYR   A CD1 1 
ATOM   2509 C CD2 . TYR   A 1 330 ? 25.675  42.511 4.609   1.00 21.56  ? 986  TYR   A CD2 1 
ATOM   2510 C CE1 . TYR   A 1 330 ? 28.019  43.681 3.713   1.00 19.67  ? 986  TYR   A CE1 1 
ATOM   2511 C CE2 . TYR   A 1 330 ? 26.413  41.907 3.595   1.00 22.78  ? 986  TYR   A CE2 1 
ATOM   2512 C CZ  . TYR   A 1 330 ? 27.599  42.484 3.170   1.00 28.11  ? 986  TYR   A CZ  1 
ATOM   2513 O OH  . TYR   A 1 330 ? 28.336  41.877 2.184   1.00 28.03  ? 986  TYR   A OH  1 
ATOM   2514 N N   . ASN   A 1 331 ? 25.139  45.900 8.995   1.00 17.71  ? 987  ASN   A N   1 
ATOM   2515 C CA  . ASN   A 1 331 ? 24.289  46.498 10.017  1.00 19.74  ? 987  ASN   A CA  1 
ATOM   2516 C C   . ASN   A 1 331 ? 22.814  46.169 9.828   1.00 22.05  ? 987  ASN   A C   1 
ATOM   2517 O O   . ASN   A 1 331 ? 22.350  45.883 8.717   1.00 20.37  ? 987  ASN   A O   1 
ATOM   2518 C CB  . ASN   A 1 331 ? 24.412  48.012 9.970   1.00 23.83  ? 987  ASN   A CB  1 
ATOM   2519 C CG  . ASN   A 1 331 ? 25.777  48.515 10.285  1.00 26.38  ? 987  ASN   A CG  1 
ATOM   2520 O OD1 . ASN   A 1 331 ? 26.425  48.018 11.185  1.00 16.44  ? 987  ASN   A OD1 1 
ATOM   2521 N ND2 . ASN   A 1 331 ? 26.224  49.524 9.539   1.00 19.89  ? 987  ASN   A ND2 1 
ATOM   2522 N N   . GLU   A 1 332 ? 22.083  46.236 10.936  1.00 20.50  ? 988  GLU   A N   1 
ATOM   2523 C CA  . GLU   A 1 332 ? 20.640  46.147 10.975  1.00 19.44  ? 988  GLU   A CA  1 
ATOM   2524 C C   . GLU   A 1 332 ? 20.131  46.981 12.111  1.00 22.60  ? 988  GLU   A C   1 
ATOM   2525 O O   . GLU   A 1 332 ? 20.833  47.179 13.099  1.00 22.62  ? 988  GLU   A O   1 
ATOM   2526 C CB  . GLU   A 1 332 ? 20.065  44.724 10.929  1.00 20.87  ? 988  GLU   A CB  1 
ATOM   2527 C CG  . GLU   A 1 332 ? 20.399  43.779 12.068  1.00 18.72  ? 988  GLU   A CG  1 
ATOM   2528 C CD  . GLU   A 1 332 ? 19.905  42.391 11.714  1.00 35.03  ? 988  GLU   A CD  1 
ATOM   2529 O OE1 . GLU   A 1 332 ? 18.910  41.943 12.324  1.00 19.16  ? 988  GLU   A OE1 1 
ATOM   2530 O OE2 . GLU   A 1 332 ? 20.472  41.774 10.786  1.00 26.15  ? 988  GLU   A OE2 1 
ATOM   2531 N N   . TYR   A 1 333 ? 18.966  47.573 11.906  1.00 18.93  ? 989  TYR   A N   1 
ATOM   2532 C CA  . TYR   A 1 333 ? 18.344  48.490 12.855  1.00 18.62  ? 989  TYR   A CA  1 
ATOM   2533 C C   . TYR   A 1 333 ? 16.951  47.982 13.209  1.00 23.12  ? 989  TYR   A C   1 
ATOM   2534 O O   . TYR   A 1 333 ? 16.168  47.677 12.314  1.00 22.63  ? 989  TYR   A O   1 
ATOM   2535 C CB  . TYR   A 1 333 ? 18.279  49.889 12.232  1.00 18.52  ? 989  TYR   A CB  1 
ATOM   2536 C CG  . TYR   A 1 333 ? 19.624  50.393 11.740  1.00 18.47  ? 989  TYR   A CG  1 
ATOM   2537 C CD1 . TYR   A 1 333 ? 20.102  50.049 10.476  1.00 20.08  ? 989  TYR   A CD1 1 
ATOM   2538 C CD2 . TYR   A 1 333 ? 20.409  51.229 12.533  1.00 18.24  ? 989  TYR   A CD2 1 
ATOM   2539 C CE1 . TYR   A 1 333 ? 21.345  50.501 10.027  1.00 21.29  ? 989  TYR   A CE1 1 
ATOM   2540 C CE2 . TYR   A 1 333 ? 21.637  51.715 12.082  1.00 19.29  ? 989  TYR   A CE2 1 
ATOM   2541 C CZ  . TYR   A 1 333 ? 22.093  51.360 10.824  1.00 29.69  ? 989  TYR   A CZ  1 
ATOM   2542 O OH  . TYR   A 1 333 ? 23.298  51.859 10.393  1.00 30.65  ? 989  TYR   A OH  1 
ATOM   2543 N N   . ILE   A 1 334 ? 16.665  47.855 14.516  1.00 19.23  ? 990  ILE   A N   1 
ATOM   2544 C CA  . ILE   A 1 334 ? 15.385  47.335 14.992  1.00 19.14  ? 990  ILE   A CA  1 
ATOM   2545 C C   . ILE   A 1 334 ? 14.739  48.332 15.959  1.00 23.47  ? 990  ILE   A C   1 
ATOM   2546 O O   . ILE   A 1 334 ? 15.385  48.795 16.898  1.00 22.53  ? 990  ILE   A O   1 
ATOM   2547 C CB  . ILE   A 1 334 ? 15.509  45.898 15.613  1.00 21.58  ? 990  ILE   A CB  1 
ATOM   2548 C CG1 . ILE   A 1 334 ? 16.418  44.955 14.788  1.00 22.33  ? 990  ILE   A CG1 1 
ATOM   2549 C CG2 . ILE   A 1 334 ? 14.141  45.249 15.831  1.00 20.22  ? 990  ILE   A CG2 1 
ATOM   2550 C CD1 . ILE   A 1 334 ? 17.921  45.006 15.078  1.00 23.07  ? 990  ILE   A CD1 1 
ATOM   2551 N N   . VAL   A 1 335 ? 13.467  48.681 15.685  1.00 20.21  ? 991  VAL   A N   1 
ATOM   2552 C CA  . VAL   A 1 335 ? 12.615  49.540 16.522  1.00 18.74  ? 991  VAL   A CA  1 
ATOM   2553 C C   . VAL   A 1 335 ? 11.478  48.656 17.086  1.00 22.49  ? 991  VAL   A C   1 
ATOM   2554 O O   . VAL   A 1 335 ? 11.023  47.721 16.422  1.00 20.45  ? 991  VAL   A O   1 
ATOM   2555 C CB  . VAL   A 1 335 ? 12.132  50.848 15.850  1.00 21.13  ? 991  VAL   A CB  1 
ATOM   2556 C CG1 . VAL   A 1 335 ? 13.287  51.810 15.612  1.00 20.41  ? 991  VAL   A CG1 1 
ATOM   2557 C CG2 . VAL   A 1 335 ? 11.345  50.586 14.565  1.00 20.89  ? 991  VAL   A CG2 1 
ATOM   2558 N N   . TYR   A 1 336 ? 11.094  48.895 18.329  1.00 20.44  ? 992  TYR   A N   1 
ATOM   2559 C CA  . TYR   A 1 336 ? 10.118  48.060 19.034  1.00 19.87  ? 992  TYR   A CA  1 
ATOM   2560 C C   . TYR   A 1 336 ? 8.798   48.794 19.282  1.00 25.07  ? 992  TYR   A C   1 
ATOM   2561 O O   . TYR   A 1 336 ? 7.904   48.269 19.970  1.00 26.35  ? 992  TYR   A O   1 
ATOM   2562 C CB  . TYR   A 1 336 ? 10.752  47.483 20.323  1.00 20.18  ? 992  TYR   A CB  1 
ATOM   2563 C CG  . TYR   A 1 336 ? 12.032  46.705 20.040  1.00 21.57  ? 992  TYR   A CG  1 
ATOM   2564 C CD1 . TYR   A 1 336 ? 13.248  47.365 19.860  1.00 23.21  ? 992  TYR   A CD1 1 
ATOM   2565 C CD2 . TYR   A 1 336 ? 12.011  45.321 19.892  1.00 21.17  ? 992  TYR   A CD2 1 
ATOM   2566 C CE1 . TYR   A 1 336 ? 14.414  46.664 19.552  1.00 24.78  ? 992  TYR   A CE1 1 
ATOM   2567 C CE2 . TYR   A 1 336 ? 13.168  44.609 19.586  1.00 21.59  ? 992  TYR   A CE2 1 
ATOM   2568 C CZ  . TYR   A 1 336 ? 14.368  45.286 19.420  1.00 26.70  ? 992  TYR   A CZ  1 
ATOM   2569 O OH  . TYR   A 1 336 ? 15.506  44.591 19.136  1.00 18.17  ? 992  TYR   A OH  1 
ATOM   2570 N N   . ASP   A 1 337 ? 8.643   49.979 18.637  1.00 20.73  ? 993  ASP   A N   1 
ATOM   2571 C CA  . ASP   A 1 337 ? 7.405   50.766 18.646  1.00 20.30  ? 993  ASP   A CA  1 
ATOM   2572 C C   . ASP   A 1 337 ? 7.101   51.117 17.188  1.00 24.93  ? 993  ASP   A C   1 
ATOM   2573 O O   . ASP   A 1 337 ? 7.923   51.746 16.526  1.00 23.89  ? 993  ASP   A O   1 
ATOM   2574 C CB  . ASP   A 1 337 ? 7.561   52.031 19.519  1.00 20.76  ? 993  ASP   A CB  1 
ATOM   2575 C CG  . ASP   A 1 337 ? 6.319   52.874 19.737  1.00 25.14  ? 993  ASP   A CG  1 
ATOM   2576 O OD1 . ASP   A 1 337 ? 5.382   52.804 18.897  1.00 25.37  ? 993  ASP   A OD1 1 
ATOM   2577 O OD2 . ASP   A 1 337 ? 6.285   53.616 20.727  1.00 34.36  ? 993  ASP   A OD2 1 
ATOM   2578 N N   . ILE   A 1 338 ? 5.913   50.728 16.696  1.00 22.77  ? 994  ILE   A N   1 
ATOM   2579 C CA  . ILE   A 1 338 ? 5.482   50.978 15.309  1.00 22.40  ? 994  ILE   A CA  1 
ATOM   2580 C C   . ILE   A 1 338 ? 5.443   52.480 14.962  1.00 25.77  ? 994  ILE   A C   1 
ATOM   2581 O O   . ILE   A 1 338 ? 5.633   52.826 13.790  1.00 25.77  ? 994  ILE   A O   1 
ATOM   2582 C CB  . ILE   A 1 338 ? 4.146   50.256 14.946  1.00 25.41  ? 994  ILE   A CB  1 
ATOM   2583 C CG1 . ILE   A 1 338 ? 2.950   50.745 15.818  1.00 25.09  ? 994  ILE   A CG1 1 
ATOM   2584 C CG2 . ILE   A 1 338 ? 4.330   48.726 14.991  1.00 26.99  ? 994  ILE   A CG2 1 
ATOM   2585 C CD1 . ILE   A 1 338 ? 1.541   50.359 15.303  1.00 30.97  ? 994  ILE   A CD1 1 
ATOM   2586 N N   . ALA   A 1 339 ? 5.238   53.356 15.979  1.00 22.29  ? 995  ALA   A N   1 
ATOM   2587 C CA  . ALA   A 1 339 ? 5.185   54.814 15.785  1.00 23.65  ? 995  ALA   A CA  1 
ATOM   2588 C C   . ALA   A 1 339 ? 6.519   55.464 15.335  1.00 25.48  ? 995  ALA   A C   1 
ATOM   2589 O O   . ALA   A 1 339 ? 6.496   56.537 14.722  1.00 24.26  ? 995  ALA   A O   1 
ATOM   2590 C CB  . ALA   A 1 339 ? 4.659   55.493 17.036  1.00 24.80  ? 995  ALA   A CB  1 
ATOM   2591 N N   . GLN   A 1 340 ? 7.657   54.788 15.614  1.00 21.93  ? 996  GLN   A N   1 
ATOM   2592 C CA  . GLN   A 1 340 ? 9.042   55.188 15.288  1.00 21.38  ? 996  GLN   A CA  1 
ATOM   2593 C C   . GLN   A 1 340 ? 9.405   55.078 13.773  1.00 26.02  ? 996  GLN   A C   1 
ATOM   2594 O O   . GLN   A 1 340 ? 10.542  55.388 13.377  1.00 26.40  ? 996  GLN   A O   1 
ATOM   2595 C CB  . GLN   A 1 340 ? 10.022  54.350 16.135  1.00 22.11  ? 996  GLN   A CB  1 
ATOM   2596 C CG  . GLN   A 1 340 ? 10.071  54.759 17.609  1.00 31.87  ? 996  GLN   A CG  1 
ATOM   2597 C CD  . GLN   A 1 340 ? 11.061  53.952 18.423  1.00 43.47  ? 996  GLN   A CD  1 
ATOM   2598 O OE1 . GLN   A 1 340 ? 10.678  53.062 19.192  1.00 28.80  ? 996  GLN   A OE1 1 
ATOM   2599 N NE2 . GLN   A 1 340 ? 12.351  54.258 18.286  1.00 23.03  ? 996  GLN   A NE2 1 
ATOM   2600 N N   . VAL   A 1 341 ? 8.438   54.640 12.941  1.00 22.83  ? 997  VAL   A N   1 
ATOM   2601 C CA  . VAL   A 1 341 ? 8.599   54.469 11.490  1.00 21.65  ? 997  VAL   A CA  1 
ATOM   2602 C C   . VAL   A 1 341 ? 7.664   55.400 10.706  1.00 24.92  ? 997  VAL   A C   1 
ATOM   2603 O O   . VAL   A 1 341 ? 6.449   55.386 10.927  1.00 23.08  ? 997  VAL   A O   1 
ATOM   2604 C CB  . VAL   A 1 341 ? 8.401   52.992 11.030  1.00 24.42  ? 997  VAL   A CB  1 
ATOM   2605 C CG1 . VAL   A 1 341 ? 8.689   52.832 9.531   1.00 23.83  ? 997  VAL   A CG1 1 
ATOM   2606 C CG2 . VAL   A 1 341 ? 9.246   52.017 11.860  1.00 23.45  ? 997  VAL   A CG2 1 
ATOM   2607 N N   . ASN   A 1 342 ? 8.242   56.193 9.779   1.00 20.21  ? 998  ASN   A N   1 
ATOM   2608 C CA  . ASN   A 1 342 ? 7.472   57.020 8.864   1.00 20.10  ? 998  ASN   A CA  1 
ATOM   2609 C C   . ASN   A 1 342 ? 7.908   56.649 7.441   1.00 24.58  ? 998  ASN   A C   1 
ATOM   2610 O O   . ASN   A 1 342 ? 9.012   57.008 7.018   1.00 24.66  ? 998  ASN   A O   1 
ATOM   2611 C CB  . ASN   A 1 342 ? 7.618   58.523 9.156   1.00 21.25  ? 998  ASN   A CB  1 
ATOM   2612 C CG  . ASN   A 1 342 ? 6.654   59.428 8.397   1.00 35.73  ? 998  ASN   A CG  1 
ATOM   2613 O OD1 . ASN   A 1 342 ? 6.922   60.603 8.196   1.00 30.35  ? 998  ASN   A OD1 1 
ATOM   2614 N ND2 . ASN   A 1 342 ? 5.511   58.925 7.958   1.00 25.94  ? 998  ASN   A ND2 1 
ATOM   2615 N N   . LEU   A 1 343 ? 7.067   55.871 6.732   1.00 23.09  ? 999  LEU   A N   1 
ATOM   2616 C CA  . LEU   A 1 343 ? 7.362   55.416 5.365   1.00 23.50  ? 999  LEU   A CA  1 
ATOM   2617 C C   . LEU   A 1 343 ? 7.458   56.595 4.418   1.00 25.48  ? 999  LEU   A C   1 
ATOM   2618 O O   . LEU   A 1 343 ? 6.578   57.462 4.434   1.00 24.01  ? 999  LEU   A O   1 
ATOM   2619 C CB  . LEU   A 1 343 ? 6.342   54.384 4.856   1.00 23.67  ? 999  LEU   A CB  1 
ATOM   2620 C CG  . LEU   A 1 343 ? 6.232   53.062 5.621   1.00 28.35  ? 999  LEU   A CG  1 
ATOM   2621 C CD1 . LEU   A 1 343 ? 5.220   52.143 4.948   1.00 28.18  ? 999  LEU   A CD1 1 
ATOM   2622 C CD2 . LEU   A 1 343 ? 7.598   52.370 5.781   1.00 28.30  ? 999  LEU   A CD2 1 
ATOM   2623 N N   . LYS   A 1 344 ? 8.549   56.651 3.625   1.00 21.57  ? 1000 LYS   A N   1 
ATOM   2624 C CA  . LYS   A 1 344 ? 8.781   57.801 2.757   1.00 21.37  ? 1000 LYS   A CA  1 
ATOM   2625 C C   . LYS   A 1 344 ? 8.720   57.473 1.285   1.00 25.40  ? 1000 LYS   A C   1 
ATOM   2626 O O   . LYS   A 1 344 ? 8.073   58.201 0.531   1.00 25.09  ? 1000 LYS   A O   1 
ATOM   2627 C CB  . LYS   A 1 344 ? 10.082  58.525 3.127   1.00 22.54  ? 1000 LYS   A CB  1 
ATOM   2628 C CG  . LYS   A 1 344 ? 9.959   59.307 4.436   1.00 32.24  ? 1000 LYS   A CG  1 
ATOM   2629 C CD  . LYS   A 1 344 ? 9.366   60.697 4.202   1.00 46.25  ? 1000 LYS   A CD  1 
ATOM   2630 C CE  . LYS   A 1 344 ? 8.475   61.143 5.330   1.00 63.43  ? 1000 LYS   A CE  1 
ATOM   2631 N NZ  . LYS   A 1 344 ? 7.487   62.158 4.880   1.00 78.48  ? 1000 LYS   A NZ  1 
ATOM   2632 N N   . TYR   A 1 345 ? 9.343   56.378 0.878   1.00 22.78  ? 1001 TYR   A N   1 
ATOM   2633 C CA  . TYR   A 1 345 ? 9.363   55.962 -0.518  1.00 22.81  ? 1001 TYR   A CA  1 
ATOM   2634 C C   . TYR   A 1 345 ? 9.131   54.486 -0.674  1.00 26.36  ? 1001 TYR   A C   1 
ATOM   2635 O O   . TYR   A 1 345 ? 9.318   53.706 0.269   1.00 26.40  ? 1001 TYR   A O   1 
ATOM   2636 C CB  . TYR   A 1 345 ? 10.694  56.349 -1.205  1.00 24.03  ? 1001 TYR   A CB  1 
ATOM   2637 C CG  . TYR   A 1 345 ? 11.008  57.828 -1.123  1.00 26.28  ? 1001 TYR   A CG  1 
ATOM   2638 C CD1 . TYR   A 1 345 ? 10.453  58.729 -2.027  1.00 27.33  ? 1001 TYR   A CD1 1 
ATOM   2639 C CD2 . TYR   A 1 345 ? 11.859  58.327 -0.143  1.00 26.86  ? 1001 TYR   A CD2 1 
ATOM   2640 C CE1 . TYR   A 1 345 ? 10.722  60.093 -1.945  1.00 27.04  ? 1001 TYR   A CE1 1 
ATOM   2641 C CE2 . TYR   A 1 345 ? 12.129  59.689 -0.049  1.00 28.16  ? 1001 TYR   A CE2 1 
ATOM   2642 C CZ  . TYR   A 1 345 ? 11.557  60.568 -0.950  1.00 35.08  ? 1001 TYR   A CZ  1 
ATOM   2643 O OH  . TYR   A 1 345 ? 11.827  61.909 -0.856  1.00 37.66  ? 1001 TYR   A OH  1 
ATOM   2644 N N   . LEU   A 1 346 ? 8.731   54.116 -1.885  1.00 21.50  ? 1002 LEU   A N   1 
ATOM   2645 C CA  . LEU   A 1 346 ? 8.536   52.756 -2.350  1.00 20.72  ? 1002 LEU   A CA  1 
ATOM   2646 C C   . LEU   A 1 346 ? 9.204   52.692 -3.713  1.00 25.92  ? 1002 LEU   A C   1 
ATOM   2647 O O   . LEU   A 1 346 ? 8.941   53.546 -4.571  1.00 27.86  ? 1002 LEU   A O   1 
ATOM   2648 C CB  . LEU   A 1 346 ? 7.042   52.410 -2.457  1.00 20.62  ? 1002 LEU   A CB  1 
ATOM   2649 C CG  . LEU   A 1 346 ? 6.671   50.989 -2.941  1.00 25.20  ? 1002 LEU   A CG  1 
ATOM   2650 C CD1 . LEU   A 1 346 ? 7.407   49.906 -2.156  1.00 26.76  ? 1002 LEU   A CD1 1 
ATOM   2651 C CD2 . LEU   A 1 346 ? 5.187   50.754 -2.832  1.00 23.94  ? 1002 LEU   A CD2 1 
ATOM   2652 N N   . LEU   A 1 347 ? 10.100  51.718 -3.906  1.00 21.48  ? 1003 LEU   A N   1 
ATOM   2653 C CA  . LEU   A 1 347 ? 10.795  51.551 -5.183  1.00 20.51  ? 1003 LEU   A CA  1 
ATOM   2654 C C   . LEU   A 1 347 ? 10.427  50.232 -5.826  1.00 23.89  ? 1003 LEU   A C   1 
ATOM   2655 O O   . LEU   A 1 347 ? 10.347  49.217 -5.135  1.00 22.29  ? 1003 LEU   A O   1 
ATOM   2656 C CB  . LEU   A 1 347 ? 12.304  51.577 -4.969  1.00 20.46  ? 1003 LEU   A CB  1 
ATOM   2657 C CG  . LEU   A 1 347 ? 13.046  52.928 -4.940  1.00 24.46  ? 1003 LEU   A CG  1 
ATOM   2658 C CD1 . LEU   A 1 347 ? 12.774  53.686 -3.651  1.00 25.05  ? 1003 LEU   A CD1 1 
ATOM   2659 C CD2 . LEU   A 1 347 ? 14.548  52.700 -5.052  1.00 23.23  ? 1003 LEU   A CD2 1 
ATOM   2660 N N   . LYS   A 1 348 ? 10.191  50.260 -7.146  1.00 22.12  ? 1004 LYS   A N   1 
ATOM   2661 C CA  . LYS   A 1 348 ? 9.967   49.071 -7.966  1.00 23.01  ? 1004 LYS   A CA  1 
ATOM   2662 C C   . LYS   A 1 348 ? 11.314  48.810 -8.610  1.00 29.09  ? 1004 LYS   A C   1 
ATOM   2663 O O   . LYS   A 1 348 ? 11.865  49.703 -9.261  1.00 30.28  ? 1004 LYS   A O   1 
ATOM   2664 C CB  . LYS   A 1 348 ? 8.903   49.309 -9.042  1.00 25.94  ? 1004 LYS   A CB  1 
ATOM   2665 C CG  . LYS   A 1 348 ? 8.603   48.091 -9.899  1.00 26.51  ? 1004 LYS   A CG  1 
ATOM   2666 C CD  . LYS   A 1 348 ? 7.231   48.222 -10.563 1.00 31.02  ? 1004 LYS   A CD  1 
ATOM   2667 C CE  . LYS   A 1 348 ? 7.331   48.210 -12.070 1.00 38.31  ? 1004 LYS   A CE  1 
ATOM   2668 N NZ  . LYS   A 1 348 ? 6.054   48.623 -12.708 1.00 38.71  ? 1004 LYS   A NZ  1 
ATOM   2669 N N   . LEU   A 1 349 ? 11.873  47.617 -8.381  1.00 25.51  ? 1005 LEU   A N   1 
ATOM   2670 C CA  . LEU   A 1 349 ? 13.195  47.271 -8.915  1.00 24.74  ? 1005 LEU   A CA  1 
ATOM   2671 C C   . LEU   A 1 349 ? 13.172  46.033 -9.811  1.00 25.05  ? 1005 LEU   A C   1 
ATOM   2672 O O   . LEU   A 1 349 ? 12.463  45.061 -9.538  1.00 21.39  ? 1005 LEU   A O   1 
ATOM   2673 C CB  . LEU   A 1 349 ? 14.203  47.018 -7.773  1.00 25.05  ? 1005 LEU   A CB  1 
ATOM   2674 C CG  . LEU   A 1 349 ? 14.432  48.088 -6.700  1.00 30.11  ? 1005 LEU   A CG  1 
ATOM   2675 C CD1 . LEU   A 1 349 ? 15.256  47.519 -5.585  1.00 31.19  ? 1005 LEU   A CD1 1 
ATOM   2676 C CD2 . LEU   A 1 349 ? 15.198  49.261 -7.237  1.00 32.14  ? 1005 LEU   A CD2 1 
ATOM   2677 N N   . LYS   A 1 350 ? 13.997  46.054 -10.862 1.00 22.30  ? 1006 LYS   A N   1 
ATOM   2678 C CA  . LYS   A 1 350 ? 14.196  44.899 -11.728 1.00 21.07  ? 1006 LYS   A CA  1 
ATOM   2679 C C   . LYS   A 1 350 ? 15.552  44.295 -11.279 1.00 23.41  ? 1006 LYS   A C   1 
ATOM   2680 O O   . LYS   A 1 350 ? 16.569  44.990 -11.277 1.00 23.09  ? 1006 LYS   A O   1 
ATOM   2681 C CB  . LYS   A 1 350 ? 14.209  45.314 -13.208 1.00 22.23  ? 1006 LYS   A CB  1 
ATOM   2682 C CG  . LYS   A 1 350 ? 14.879  44.312 -14.170 1.00 38.23  ? 1006 LYS   A CG  1 
ATOM   2683 C CD  . LYS   A 1 350 ? 13.880  43.518 -15.002 1.00 43.68  ? 1006 LYS   A CD  1 
ATOM   2684 C CE  . LYS   A 1 350 ? 14.560  42.478 -15.864 1.00 45.04  ? 1006 LYS   A CE  1 
ATOM   2685 N NZ  . LYS   A 1 350 ? 13.599  41.780 -16.763 1.00 46.14  ? 1006 LYS   A NZ  1 
ATOM   2686 N N   . PHE   A 1 351 ? 15.532  43.030 -10.861 1.00 19.30  ? 1007 PHE   A N   1 
ATOM   2687 C CA  . PHE   A 1 351 ? 16.697  42.255 -10.427 1.00 19.41  ? 1007 PHE   A CA  1 
ATOM   2688 C C   . PHE   A 1 351 ? 17.262  41.567 -11.672 1.00 25.12  ? 1007 PHE   A C   1 
ATOM   2689 O O   . PHE   A 1 351 ? 16.552  40.789 -12.315 1.00 26.70  ? 1007 PHE   A O   1 
ATOM   2690 C CB  . PHE   A 1 351 ? 16.273  41.190 -9.393  1.00 20.00  ? 1007 PHE   A CB  1 
ATOM   2691 C CG  . PHE   A 1 351 ? 15.893  41.728 -8.040  1.00 19.30  ? 1007 PHE   A CG  1 
ATOM   2692 C CD1 . PHE   A 1 351 ? 14.722  42.460 -7.867  1.00 18.95  ? 1007 PHE   A CD1 1 
ATOM   2693 C CD2 . PHE   A 1 351 ? 16.686  41.467 -6.924  1.00 19.36  ? 1007 PHE   A CD2 1 
ATOM   2694 C CE1 . PHE   A 1 351 ? 14.383  42.976 -6.615  1.00 19.26  ? 1007 PHE   A CE1 1 
ATOM   2695 C CE2 . PHE   A 1 351 ? 16.341  41.966 -5.671  1.00 20.65  ? 1007 PHE   A CE2 1 
ATOM   2696 C CZ  . PHE   A 1 351 ? 15.196  42.730 -5.525  1.00 18.46  ? 1007 PHE   A CZ  1 
ATOM   2697 N N   . ASN   A 1 352 ? 18.488  41.902 -12.056 1.00 21.32  ? 1008 ASN   A N   1 
ATOM   2698 C CA  . ASN   A 1 352 ? 19.141  41.267 -13.195 1.00 21.82  ? 1008 ASN   A CA  1 
ATOM   2699 C C   . ASN   A 1 352 ? 20.151  40.240 -12.674 1.00 26.64  ? 1008 ASN   A C   1 
ATOM   2700 O O   . ASN   A 1 352 ? 21.270  40.575 -12.281 1.00 25.52  ? 1008 ASN   A O   1 
ATOM   2701 C CB  . ASN   A 1 352 ? 19.759  42.295 -14.157 1.00 27.05  ? 1008 ASN   A CB  1 
ATOM   2702 C CG  . ASN   A 1 352 ? 20.689  41.758 -15.250 1.00 50.64  ? 1008 ASN   A CG  1 
ATOM   2703 O OD1 . ASN   A 1 352 ? 20.551  40.638 -15.776 1.00 32.24  ? 1008 ASN   A OD1 1 
ATOM   2704 N ND2 . ASN   A 1 352 ? 21.648  42.585 -15.650 1.00 49.85  ? 1008 ASN   A ND2 1 
ATOM   2705 N N   . PHE   A 1 353 ? 19.716  38.983 -12.652 1.00 24.29  ? 1009 PHE   A N   1 
ATOM   2706 C CA  . PHE   A 1 353 ? 20.505  37.848 -12.181 1.00 24.97  ? 1009 PHE   A CA  1 
ATOM   2707 C C   . PHE   A 1 353 ? 21.685  37.506 -13.104 1.00 29.11  ? 1009 PHE   A C   1 
ATOM   2708 O O   . PHE   A 1 353 ? 21.527  37.470 -14.317 1.00 27.27  ? 1009 PHE   A O   1 
ATOM   2709 C CB  . PHE   A 1 353 ? 19.596  36.631 -11.949 1.00 26.26  ? 1009 PHE   A CB  1 
ATOM   2710 C CG  . PHE   A 1 353 ? 18.581  36.870 -10.858 1.00 27.20  ? 1009 PHE   A CG  1 
ATOM   2711 C CD1 . PHE   A 1 353 ? 18.911  36.663 -9.518  1.00 29.21  ? 1009 PHE   A CD1 1 
ATOM   2712 C CD2 . PHE   A 1 353 ? 17.301  37.343 -11.163 1.00 26.94  ? 1009 PHE   A CD2 1 
ATOM   2713 C CE1 . PHE   A 1 353 ? 17.969  36.897 -8.508  1.00 28.91  ? 1009 PHE   A CE1 1 
ATOM   2714 C CE2 . PHE   A 1 353 ? 16.372  37.596 -10.152 1.00 28.47  ? 1009 PHE   A CE2 1 
ATOM   2715 C CZ  . PHE   A 1 353 ? 16.712  37.369 -8.834  1.00 26.71  ? 1009 PHE   A CZ  1 
ATOM   2716 N N   . LYS   A 1 354 ? 22.867  37.299 -12.507 1.00 29.21  ? 1010 LYS   A N   1 
ATOM   2717 C CA  . LYS   A 1 354 ? 24.114  36.956 -13.211 1.00 30.45  ? 1010 LYS   A CA  1 
ATOM   2718 C C   . LYS   A 1 354 ? 24.292  35.420 -13.329 1.00 37.74  ? 1010 LYS   A C   1 
ATOM   2719 O O   . LYS   A 1 354 ? 25.214  34.950 -14.010 1.00 38.25  ? 1010 LYS   A O   1 
ATOM   2720 C CB  . LYS   A 1 354 ? 25.340  37.569 -12.501 1.00 31.75  ? 1010 LYS   A CB  1 
ATOM   2721 C CG  . LYS   A 1 354 ? 25.154  38.973 -11.926 1.00 42.62  ? 1010 LYS   A CG  1 
ATOM   2722 C CD  . LYS   A 1 354 ? 25.064  40.104 -12.956 1.00 49.13  ? 1010 LYS   A CD  1 
ATOM   2723 C CE  . LYS   A 1 354 ? 25.947  41.288 -12.607 1.00 58.18  ? 1010 LYS   A CE  1 
ATOM   2724 N NZ  . LYS   A 1 354 ? 25.614  41.904 -11.289 1.00 66.13  ? 1010 LYS   A NZ  1 
ATOM   2725 N N   . THR   A 1 355 ? 23.391  34.657 -12.676 1.00 35.27  ? 1011 THR   A N   1 
ATOM   2726 C CA  . THR   A 1 355 ? 23.392  33.192 -12.610 1.00 52.51  ? 1011 THR   A CA  1 
ATOM   2727 C C   . THR   A 1 355 ? 22.338  32.600 -13.534 1.00 84.76  ? 1011 THR   A C   1 
ATOM   2728 O O   . THR   A 1 355 ? 22.293  32.954 -14.710 1.00 55.69  ? 1011 THR   A O   1 
ATOM   2729 C CB  . THR   A 1 355 ? 23.219  32.730 -11.146 1.00 56.21  ? 1011 THR   A CB  1 
ATOM   2730 O OG1 . THR   A 1 355 ? 22.002  33.252 -10.614 1.00 53.10  ? 1011 THR   A OG1 1 
ATOM   2731 C CG2 . THR   A 1 355 ? 24.383  33.147 -10.255 1.00 51.89  ? 1011 THR   A CG2 1 
ATOM   2732 N N   . LYS   B 1 6   ? 51.886  13.599 60.198  1.00 36.03  ? 662  LYS   B N   1 
ATOM   2733 C CA  . LYS   B 1 6   ? 50.491  13.554 59.727  1.00 36.11  ? 662  LYS   B CA  1 
ATOM   2734 C C   . LYS   B 1 6   ? 49.739  14.833 60.094  1.00 37.87  ? 662  LYS   B C   1 
ATOM   2735 O O   . LYS   B 1 6   ? 49.911  15.355 61.198  1.00 39.24  ? 662  LYS   B O   1 
ATOM   2736 C CB  . LYS   B 1 6   ? 49.764  12.323 60.296  1.00 40.21  ? 662  LYS   B CB  1 
ATOM   2737 C CG  . LYS   B 1 6   ? 48.736  11.702 59.350  1.00 60.27  ? 662  LYS   B CG  1 
ATOM   2738 C CD  . LYS   B 1 6   ? 48.059  10.437 59.935  1.00 70.56  ? 662  LYS   B CD  1 
ATOM   2739 C CE  . LYS   B 1 6   ? 48.820  9.145  59.704  1.00 71.07  ? 662  LYS   B CE  1 
ATOM   2740 N NZ  . LYS   B 1 6   ? 47.981  7.953  60.012  1.00 70.06  ? 662  LYS   B NZ  1 
ATOM   2741 N N   . SER   B 1 7   ? 48.883  15.311 59.175  1.00 32.19  ? 663  SER   B N   1 
ATOM   2742 C CA  . SER   B 1 7   ? 48.082  16.530 59.259  1.00 30.37  ? 663  SER   B CA  1 
ATOM   2743 C C   . SER   B 1 7   ? 47.209  16.696 60.522  1.00 35.46  ? 663  SER   B C   1 
ATOM   2744 O O   . SER   B 1 7   ? 46.470  15.787 60.907  1.00 34.41  ? 663  SER   B O   1 
ATOM   2745 C CB  . SER   B 1 7   ? 47.208  16.650 58.009  1.00 30.52  ? 663  SER   B CB  1 
ATOM   2746 O OG  . SER   B 1 7   ? 46.439  17.839 58.006  1.00 26.77  ? 663  SER   B OG  1 
ATOM   2747 N N   . LYS   B 1 8   ? 47.261  17.909 61.112  1.00 33.60  ? 664  LYS   B N   1 
ATOM   2748 C CA  . LYS   B 1 8   ? 46.460  18.354 62.264  1.00 32.11  ? 664  LYS   B CA  1 
ATOM   2749 C C   . LYS   B 1 8   ? 45.112  18.946 61.785  1.00 32.07  ? 664  LYS   B C   1 
ATOM   2750 O O   . LYS   B 1 8   ? 44.265  19.303 62.611  1.00 31.80  ? 664  LYS   B O   1 
ATOM   2751 C CB  . LYS   B 1 8   ? 47.240  19.419 63.070  1.00 35.47  ? 664  LYS   B CB  1 
ATOM   2752 C CG  . LYS   B 1 8   ? 48.399  18.887 63.904  1.00 59.41  ? 664  LYS   B CG  1 
ATOM   2753 C CD  . LYS   B 1 8   ? 49.210  20.030 64.516  1.00 71.77  ? 664  LYS   B CD  1 
ATOM   2754 C CE  . LYS   B 1 8   ? 50.423  19.531 65.269  1.00 84.99  ? 664  LYS   B CE  1 
ATOM   2755 N NZ  . LYS   B 1 8   ? 51.277  20.649 65.756  1.00 92.13  ? 664  LYS   B NZ  1 
ATOM   2756 N N   . LEU   B 1 9   ? 44.915  19.058 60.461  1.00 27.32  ? 665  LEU   B N   1 
ATOM   2757 C CA  . LEU   B 1 9   ? 43.686  19.608 59.872  1.00 26.36  ? 665  LEU   B CA  1 
ATOM   2758 C C   . LEU   B 1 9   ? 42.443  18.804 60.274  1.00 30.31  ? 665  LEU   B C   1 
ATOM   2759 O O   . LEU   B 1 9   ? 42.546  17.575 60.433  1.00 28.10  ? 665  LEU   B O   1 
ATOM   2760 C CB  . LEU   B 1 9   ? 43.775  19.646 58.343  1.00 25.70  ? 665  LEU   B CB  1 
ATOM   2761 C CG  . LEU   B 1 9   ? 44.546  20.803 57.702  1.00 28.26  ? 665  LEU   B CG  1 
ATOM   2762 C CD1 . LEU   B 1 9   ? 44.866  20.474 56.257  1.00 27.34  ? 665  LEU   B CD1 1 
ATOM   2763 C CD2 . LEU   B 1 9   ? 43.714  22.096 57.733  1.00 31.47  ? 665  LEU   B CD2 1 
ATOM   2764 N N   . PRO   B 1 10  ? 41.251  19.460 60.418  1.00 27.34  ? 666  PRO   B N   1 
ATOM   2765 C CA  . PRO   B 1 10  ? 40.033  18.693 60.737  1.00 26.36  ? 666  PRO   B CA  1 
ATOM   2766 C C   . PRO   B 1 10  ? 39.806  17.607 59.693  1.00 28.16  ? 666  PRO   B C   1 
ATOM   2767 O O   . PRO   B 1 10  ? 40.088  17.825 58.527  1.00 26.97  ? 666  PRO   B O   1 
ATOM   2768 C CB  . PRO   B 1 10  ? 38.918  19.753 60.685  1.00 28.38  ? 666  PRO   B CB  1 
ATOM   2769 C CG  . PRO   B 1 10  ? 39.613  21.055 60.910  1.00 32.87  ? 666  PRO   B CG  1 
ATOM   2770 C CD  . PRO   B 1 10  ? 40.948  20.901 60.252  1.00 28.38  ? 666  PRO   B CD  1 
ATOM   2771 N N   . LYS   B 1 11  ? 39.327  16.434 60.114  1.00 26.48  ? 667  LYS   B N   1 
ATOM   2772 C CA  . LYS   B 1 11  ? 39.047  15.318 59.213  1.00 26.19  ? 667  LYS   B CA  1 
ATOM   2773 C C   . LYS   B 1 11  ? 38.126  15.724 58.046  1.00 26.70  ? 667  LYS   B C   1 
ATOM   2774 O O   . LYS   B 1 11  ? 38.498  15.393 56.913  1.00 24.28  ? 667  LYS   B O   1 
ATOM   2775 C CB  . LYS   B 1 11  ? 38.526  14.086 59.968  1.00 29.81  ? 667  LYS   B CB  1 
ATOM   2776 C CG  . LYS   B 1 11  ? 38.956  12.769 59.338  1.00 40.26  ? 667  LYS   B CG  1 
ATOM   2777 C CD  . LYS   B 1 11  ? 37.745  11.897 59.014  1.00 48.45  ? 667  LYS   B CD  1 
ATOM   2778 C CE  . LYS   B 1 11  ? 38.119  10.556 58.430  1.00 54.78  ? 667  LYS   B CE  1 
ATOM   2779 N NZ  . LYS   B 1 11  ? 38.585  10.660 57.024  1.00 56.95  ? 667  LYS   B NZ  1 
ATOM   2780 N N   . PRO   B 1 12  ? 37.014  16.518 58.233  1.00 23.78  ? 668  PRO   B N   1 
ATOM   2781 C CA  . PRO   B 1 12  ? 36.217  16.941 57.063  1.00 23.98  ? 668  PRO   B CA  1 
ATOM   2782 C C   . PRO   B 1 12  ? 36.994  17.773 56.040  1.00 26.34  ? 668  PRO   B C   1 
ATOM   2783 O O   . PRO   B 1 12  ? 36.734  17.635 54.842  1.00 26.31  ? 668  PRO   B O   1 
ATOM   2784 C CB  . PRO   B 1 12  ? 35.051  17.720 57.682  1.00 26.20  ? 668  PRO   B CB  1 
ATOM   2785 C CG  . PRO   B 1 12  ? 34.995  17.282 59.084  1.00 29.54  ? 668  PRO   B CG  1 
ATOM   2786 C CD  . PRO   B 1 12  ? 36.417  17.059 59.471  1.00 24.62  ? 668  PRO   B CD  1 
ATOM   2787 N N   . VAL   B 1 13  ? 37.967  18.593 56.498  1.00 23.23  ? 669  VAL   B N   1 
ATOM   2788 C CA  . VAL   B 1 13  ? 38.820  19.427 55.620  1.00 23.41  ? 669  VAL   B CA  1 
ATOM   2789 C C   . VAL   B 1 13  ? 39.794  18.526 54.826  1.00 26.89  ? 669  VAL   B C   1 
ATOM   2790 O O   . VAL   B 1 13  ? 39.992  18.739 53.634  1.00 24.52  ? 669  VAL   B O   1 
ATOM   2791 C CB  . VAL   B 1 13  ? 39.543  20.553 56.425  1.00 26.15  ? 669  VAL   B CB  1 
ATOM   2792 C CG1 . VAL   B 1 13  ? 40.672  21.203 55.614  1.00 25.54  ? 669  VAL   B CG1 1 
ATOM   2793 C CG2 . VAL   B 1 13  ? 38.525  21.607 56.899  1.00 25.81  ? 669  VAL   B CG2 1 
ATOM   2794 N N   . GLN   B 1 14  ? 40.365  17.500 55.496  1.00 24.13  ? 670  GLN   B N   1 
ATOM   2795 C CA  . GLN   B 1 14  ? 41.284  16.519 54.910  1.00 23.52  ? 670  GLN   B CA  1 
ATOM   2796 C C   . GLN   B 1 14  ? 40.601  15.719 53.801  1.00 27.76  ? 670  GLN   B C   1 
ATOM   2797 O O   . GLN   B 1 14  ? 41.195  15.531 52.735  1.00 26.73  ? 670  GLN   B O   1 
ATOM   2798 C CB  . GLN   B 1 14  ? 41.788  15.553 55.982  1.00 24.53  ? 670  GLN   B CB  1 
ATOM   2799 C CG  . GLN   B 1 14  ? 42.668  16.191 57.054  1.00 32.63  ? 670  GLN   B CG  1 
ATOM   2800 C CD  . GLN   B 1 14  ? 43.495  15.178 57.815  1.00 35.43  ? 670  GLN   B CD  1 
ATOM   2801 O OE1 . GLN   B 1 14  ? 43.835  14.107 57.317  1.00 33.97  ? 670  GLN   B OE1 1 
ATOM   2802 N NE2 . GLN   B 1 14  ? 43.859  15.498 59.033  1.00 21.78  ? 670  GLN   B NE2 1 
ATOM   2803 N N   . ASP   B 1 15  ? 39.337  15.272 54.053  1.00 25.19  ? 671  ASP   B N   1 
ATOM   2804 C CA  . ASP   B 1 15  ? 38.526  14.521 53.100  1.00 24.73  ? 671  ASP   B CA  1 
ATOM   2805 C C   . ASP   B 1 15  ? 38.184  15.373 51.895  1.00 26.28  ? 671  ASP   B C   1 
ATOM   2806 O O   . ASP   B 1 15  ? 38.149  14.850 50.786  1.00 25.44  ? 671  ASP   B O   1 
ATOM   2807 C CB  . ASP   B 1 15  ? 37.251  13.965 53.756  1.00 27.73  ? 671  ASP   B CB  1 
ATOM   2808 C CG  . ASP   B 1 15  ? 37.481  12.892 54.797  1.00 39.92  ? 671  ASP   B CG  1 
ATOM   2809 O OD1 . ASP   B 1 15  ? 38.401  12.042 54.599  1.00 41.53  ? 671  ASP   B OD1 1 
ATOM   2810 O OD2 . ASP   B 1 15  ? 36.728  12.870 55.794  1.00 45.61  ? 671  ASP   B OD2 1 
ATOM   2811 N N   . LEU   B 1 16  ? 37.973  16.684 52.108  1.00 23.32  ? 672  LEU   B N   1 
ATOM   2812 C CA  . LEU   B 1 16  ? 37.669  17.636 51.044  1.00 23.70  ? 672  LEU   B CA  1 
ATOM   2813 C C   . LEU   B 1 16  ? 38.853  17.787 50.092  1.00 29.28  ? 672  LEU   B C   1 
ATOM   2814 O O   . LEU   B 1 16  ? 38.654  17.750 48.881  1.00 29.37  ? 672  LEU   B O   1 
ATOM   2815 C CB  . LEU   B 1 16  ? 37.257  19.012 51.604  1.00 23.77  ? 672  LEU   B CB  1 
ATOM   2816 C CG  . LEU   B 1 16  ? 36.999  20.099 50.541  1.00 28.24  ? 672  LEU   B CG  1 
ATOM   2817 C CD1 . LEU   B 1 16  ? 35.644  19.915 49.852  1.00 28.07  ? 672  LEU   B CD1 1 
ATOM   2818 C CD2 . LEU   B 1 16  ? 37.162  21.493 51.115  1.00 31.25  ? 672  LEU   B CD2 1 
ATOM   2819 N N   . ILE   B 1 17  ? 40.074  17.971 50.643  1.00 27.13  ? 673  ILE   B N   1 
ATOM   2820 C CA  . ILE   B 1 17  ? 41.326  18.122 49.884  1.00 26.22  ? 673  ILE   B CA  1 
ATOM   2821 C C   . ILE   B 1 17  ? 41.579  16.881 49.026  1.00 27.42  ? 673  ILE   B C   1 
ATOM   2822 O O   . ILE   B 1 17  ? 41.975  17.011 47.864  1.00 26.41  ? 673  ILE   B O   1 
ATOM   2823 C CB  . ILE   B 1 17  ? 42.531  18.427 50.847  1.00 29.38  ? 673  ILE   B CB  1 
ATOM   2824 C CG1 . ILE   B 1 17  ? 42.330  19.741 51.657  1.00 30.79  ? 673  ILE   B CG1 1 
ATOM   2825 C CG2 . ILE   B 1 17  ? 43.915  18.410 50.125  1.00 28.99  ? 673  ILE   B CG2 1 
ATOM   2826 C CD1 . ILE   B 1 17  ? 41.900  21.027 50.881  1.00 35.00  ? 673  ILE   B CD1 1 
ATOM   2827 N N   . LYS   B 1 18  ? 41.358  15.687 49.607  1.00 23.27  ? 674  LYS   B N   1 
ATOM   2828 C CA  . LYS   B 1 18  ? 41.587  14.397 48.943  1.00 23.96  ? 674  LYS   B CA  1 
ATOM   2829 C C   . LYS   B 1 18  ? 40.689  14.241 47.753  1.00 28.69  ? 674  LYS   B C   1 
ATOM   2830 O O   . LYS   B 1 18  ? 41.143  13.822 46.696  1.00 27.61  ? 674  LYS   B O   1 
ATOM   2831 C CB  . LYS   B 1 18  ? 41.388  13.220 49.920  1.00 26.29  ? 674  LYS   B CB  1 
ATOM   2832 C CG  . LYS   B 1 18  ? 42.526  13.005 50.907  1.00 41.98  ? 674  LYS   B CG  1 
ATOM   2833 C CD  . LYS   B 1 18  ? 42.427  11.630 51.572  1.00 60.15  ? 674  LYS   B CD  1 
ATOM   2834 C CE  . LYS   B 1 18  ? 41.725  11.654 52.910  1.00 73.83  ? 674  LYS   B CE  1 
ATOM   2835 N NZ  . LYS   B 1 18  ? 41.621  10.299 53.513  1.00 81.97  ? 674  LYS   B NZ  1 
ATOM   2836 N N   . MET   B 1 19  ? 39.408  14.598 47.941  1.00 28.89  ? 675  MET   B N   1 
ATOM   2837 C CA  . MET   B 1 19  ? 38.317  14.556 46.982  1.00 29.77  ? 675  MET   B CA  1 
ATOM   2838 C C   . MET   B 1 19  ? 38.671  15.405 45.774  1.00 32.59  ? 675  MET   B C   1 
ATOM   2839 O O   . MET   B 1 19  ? 38.652  14.918 44.649  1.00 31.97  ? 675  MET   B O   1 
ATOM   2840 C CB  . MET   B 1 19  ? 37.076  15.141 47.675  1.00 33.22  ? 675  MET   B CB  1 
ATOM   2841 C CG  . MET   B 1 19  ? 35.773  14.744 47.079  1.00 38.78  ? 675  MET   B CG  1 
ATOM   2842 S SD  . MET   B 1 19  ? 34.429  15.527 48.018  1.00 44.80  ? 675  MET   B SD  1 
ATOM   2843 C CE  . MET   B 1 19  ? 33.023  15.174 46.972  1.00 41.90  ? 675  MET   B CE  1 
ATOM   2844 N N   . ILE   B 1 20  ? 39.041  16.666 46.043  1.00 27.78  ? 676  ILE   B N   1 
ATOM   2845 C CA  . ILE   B 1 20  ? 39.344  17.749 45.115  1.00 26.35  ? 676  ILE   B CA  1 
ATOM   2846 C C   . ILE   B 1 20  ? 40.634  17.538 44.325  1.00 26.59  ? 676  ILE   B C   1 
ATOM   2847 O O   . ILE   B 1 20  ? 40.694  17.973 43.171  1.00 24.79  ? 676  ILE   B O   1 
ATOM   2848 C CB  . ILE   B 1 20  ? 39.301  19.057 45.950  1.00 29.74  ? 676  ILE   B CB  1 
ATOM   2849 C CG1 . ILE   B 1 20  ? 37.876  19.625 45.920  1.00 30.79  ? 676  ILE   B CG1 1 
ATOM   2850 C CG2 . ILE   B 1 20  ? 40.374  20.100 45.641  1.00 30.13  ? 676  ILE   B CG2 1 
ATOM   2851 C CD1 . ILE   B 1 20  ? 37.588  20.761 46.917  1.00 48.14  ? 676  ILE   B CD1 1 
ATOM   2852 N N   . PHE   B 1 21  ? 41.642  16.863 44.902  1.00 22.97  ? 677  PHE   B N   1 
ATOM   2853 C CA  . PHE   B 1 21  ? 42.920  16.641 44.218  1.00 22.38  ? 677  PHE   B CA  1 
ATOM   2854 C C   . PHE   B 1 21  ? 43.090  15.212 43.643  1.00 29.84  ? 677  PHE   B C   1 
ATOM   2855 O O   . PHE   B 1 21  ? 44.199  14.823 43.246  1.00 29.12  ? 677  PHE   B O   1 
ATOM   2856 C CB  . PHE   B 1 21  ? 44.098  17.037 45.128  1.00 23.81  ? 677  PHE   B CB  1 
ATOM   2857 C CG  . PHE   B 1 21  ? 44.336  18.527 45.144  1.00 23.57  ? 677  PHE   B CG  1 
ATOM   2858 C CD1 . PHE   B 1 21  ? 44.894  19.175 44.039  1.00 26.67  ? 677  PHE   B CD1 1 
ATOM   2859 C CD2 . PHE   B 1 21  ? 43.976  19.287 46.243  1.00 23.46  ? 677  PHE   B CD2 1 
ATOM   2860 C CE1 . PHE   B 1 21  ? 45.118  20.552 44.053  1.00 27.58  ? 677  PHE   B CE1 1 
ATOM   2861 C CE2 . PHE   B 1 21  ? 44.225  20.654 46.269  1.00 26.45  ? 677  PHE   B CE2 1 
ATOM   2862 C CZ  . PHE   B 1 21  ? 44.802  21.279 45.173  1.00 25.37  ? 677  PHE   B CZ  1 
ATOM   2863 N N   . ASP   B 1 22  ? 41.971  14.450 43.562  1.00 30.57  ? 678  ASP   B N   1 
ATOM   2864 C CA  . ASP   B 1 22  ? 41.936  13.078 43.041  1.00 31.00  ? 678  ASP   B CA  1 
ATOM   2865 C C   . ASP   B 1 22  ? 42.213  13.097 41.524  1.00 34.86  ? 678  ASP   B C   1 
ATOM   2866 O O   . ASP   B 1 22  ? 41.415  13.648 40.752  1.00 34.84  ? 678  ASP   B O   1 
ATOM   2867 C CB  . ASP   B 1 22  ? 40.565  12.430 43.351  1.00 32.82  ? 678  ASP   B CB  1 
ATOM   2868 C CG  . ASP   B 1 22  ? 40.572  10.908 43.375  1.00 49.19  ? 678  ASP   B CG  1 
ATOM   2869 O OD1 . ASP   B 1 22  ? 40.600  10.295 42.285  1.00 49.85  ? 678  ASP   B OD1 1 
ATOM   2870 O OD2 . ASP   B 1 22  ? 40.527  10.329 44.485  1.00 57.09  ? 678  ASP   B OD2 1 
ATOM   2871 N N   . VAL   B 1 23  ? 43.367  12.522 41.117  1.00 29.54  ? 679  VAL   B N   1 
ATOM   2872 C CA  . VAL   B 1 23  ? 43.839  12.437 39.721  1.00 27.74  ? 679  VAL   B CA  1 
ATOM   2873 C C   . VAL   B 1 23  ? 42.963  11.495 38.887  1.00 30.74  ? 679  VAL   B C   1 
ATOM   2874 O O   . VAL   B 1 23  ? 42.722  11.765 37.707  1.00 28.51  ? 679  VAL   B O   1 
ATOM   2875 C CB  . VAL   B 1 23  ? 45.347  12.045 39.675  1.00 29.79  ? 679  VAL   B CB  1 
ATOM   2876 C CG1 . VAL   B 1 23  ? 45.790  11.601 38.282  1.00 28.85  ? 679  VAL   B CG1 1 
ATOM   2877 C CG2 . VAL   B 1 23  ? 46.223  13.183 40.176  1.00 29.23  ? 679  VAL   B CG2 1 
ATOM   2878 N N   . GLU   B 1 24  ? 42.528  10.372 39.497  1.00 28.89  ? 680  GLU   B N   1 
ATOM   2879 C CA  . GLU   B 1 24  ? 41.680  9.388  38.841  1.00 28.74  ? 680  GLU   B CA  1 
ATOM   2880 C C   . GLU   B 1 24  ? 40.267  9.936  38.601  1.00 32.73  ? 680  GLU   B C   1 
ATOM   2881 O O   . GLU   B 1 24  ? 39.619  9.501  37.651  1.00 32.33  ? 680  GLU   B O   1 
ATOM   2882 C CB  . GLU   B 1 24  ? 41.671  8.060  39.601  1.00 30.73  ? 680  GLU   B CB  1 
ATOM   2883 C CG  . GLU   B 1 24  ? 43.031  7.363  39.714  1.00 43.92  ? 680  GLU   B CG  1 
ATOM   2884 C CD  . GLU   B 1 24  ? 43.847  7.166  38.444  1.00 65.22  ? 680  GLU   B CD  1 
ATOM   2885 O OE1 . GLU   B 1 24  ? 43.283  6.687  37.432  1.00 62.05  ? 680  GLU   B OE1 1 
ATOM   2886 O OE2 . GLU   B 1 24  ? 45.061  7.479  38.470  1.00 51.08  ? 680  GLU   B OE2 1 
ATOM   2887 N N   . SER   B 1 25  ? 39.802  10.919 39.425  1.00 29.48  ? 681  SER   B N   1 
ATOM   2888 C CA  . SER   B 1 25  ? 38.490  11.562 39.225  1.00 29.93  ? 681  SER   B CA  1 
ATOM   2889 C C   . SER   B 1 25  ? 38.604  12.499 38.020  1.00 35.16  ? 681  SER   B C   1 
ATOM   2890 O O   . SER   B 1 25  ? 37.670  12.580 37.227  1.00 35.26  ? 681  SER   B O   1 
ATOM   2891 C CB  . SER   B 1 25  ? 38.059  12.354 40.456  1.00 33.05  ? 681  SER   B CB  1 
ATOM   2892 O OG  . SER   B 1 25  ? 37.865  11.485 41.558  1.00 42.73  ? 681  SER   B OG  1 
ATOM   2893 N N   . MET   B 1 26  ? 39.765  13.188 37.881  1.00 31.94  ? 682  MET   B N   1 
ATOM   2894 C CA  . MET   B 1 26  ? 40.088  14.090 36.766  1.00 31.86  ? 682  MET   B CA  1 
ATOM   2895 C C   . MET   B 1 26  ? 40.086  13.293 35.469  1.00 37.36  ? 682  MET   B C   1 
ATOM   2896 O O   . MET   B 1 26  ? 39.514  13.746 34.476  1.00 36.46  ? 682  MET   B O   1 
ATOM   2897 C CB  . MET   B 1 26  ? 41.455  14.763 36.959  1.00 33.55  ? 682  MET   B CB  1 
ATOM   2898 C CG  . MET   B 1 26  ? 41.510  15.725 38.114  1.00 35.99  ? 682  MET   B CG  1 
ATOM   2899 S SD  . MET   B 1 26  ? 43.195  16.354 38.274  1.00 38.91  ? 682  MET   B SD  1 
ATOM   2900 C CE  . MET   B 1 26  ? 43.249  16.708 40.025  1.00 35.69  ? 682  MET   B CE  1 
ATOM   2901 N N   . LYS   B 1 27  ? 40.678  12.085 35.507  1.00 34.22  ? 683  LYS   B N   1 
ATOM   2902 C CA  . LYS   B 1 27  ? 40.731  11.153 34.376  1.00 34.87  ? 683  LYS   B CA  1 
ATOM   2903 C C   . LYS   B 1 27  ? 39.326  10.587 34.051  1.00 40.36  ? 683  LYS   B C   1 
ATOM   2904 O O   . LYS   B 1 27  ? 38.935  10.565 32.884  1.00 40.26  ? 683  LYS   B O   1 
ATOM   2905 C CB  . LYS   B 1 27  ? 41.741  10.026 34.644  1.00 35.39  ? 683  LYS   B CB  1 
ATOM   2906 C CG  . LYS   B 1 27  ? 43.188  10.475 34.671  1.00 40.00  ? 683  LYS   B CG  1 
ATOM   2907 C CD  . LYS   B 1 27  ? 44.118  9.326  35.074  1.00 44.77  ? 683  LYS   B CD  1 
ATOM   2908 C CE  . LYS   B 1 27  ? 45.581  9.694  34.958  1.00 58.14  ? 683  LYS   B CE  1 
ATOM   2909 N NZ  . LYS   B 1 27  ? 46.457  8.491  34.991  1.00 72.94  ? 683  LYS   B NZ  1 
ATOM   2910 N N   . LYS   B 1 28  ? 38.566  10.162 35.083  1.00 38.25  ? 684  LYS   B N   1 
ATOM   2911 C CA  . LYS   B 1 28  ? 37.196  9.656  34.939  1.00 38.79  ? 684  LYS   B CA  1 
ATOM   2912 C C   . LYS   B 1 28  ? 36.292  10.740 34.315  1.00 42.24  ? 684  LYS   B C   1 
ATOM   2913 O O   . LYS   B 1 28  ? 35.377  10.405 33.566  1.00 43.93  ? 684  LYS   B O   1 
ATOM   2914 C CB  . LYS   B 1 28  ? 36.625  9.199  36.297  1.00 41.28  ? 684  LYS   B CB  1 
ATOM   2915 C CG  . LYS   B 1 28  ? 35.451  8.234  36.187  1.00 54.63  ? 684  LYS   B CG  1 
ATOM   2916 N N   . ALA   B 1 29  ? 36.556  12.024 34.614  1.00 37.02  ? 685  ALA   B N   1 
ATOM   2917 C CA  . ALA   B 1 29  ? 35.802  13.143 34.054  1.00 36.95  ? 685  ALA   B CA  1 
ATOM   2918 C C   . ALA   B 1 29  ? 36.134  13.326 32.566  1.00 41.82  ? 685  ALA   B C   1 
ATOM   2919 O O   . ALA   B 1 29  ? 35.238  13.613 31.779  1.00 40.67  ? 685  ALA   B O   1 
ATOM   2920 C CB  . ALA   B 1 29  ? 36.086  14.418 34.821  1.00 37.71  ? 685  ALA   B CB  1 
ATOM   2921 N N   . MET   B 1 30  ? 37.397  13.114 32.174  1.00 38.89  ? 686  MET   B N   1 
ATOM   2922 C CA  . MET   B 1 30  ? 37.790  13.224 30.771  1.00 39.78  ? 686  MET   B CA  1 
ATOM   2923 C C   . MET   B 1 30  ? 37.193  12.093 29.929  1.00 48.38  ? 686  MET   B C   1 
ATOM   2924 O O   . MET   B 1 30  ? 36.730  12.346 28.816  1.00 48.72  ? 686  MET   B O   1 
ATOM   2925 C CB  . MET   B 1 30  ? 39.311  13.322 30.622  1.00 41.53  ? 686  MET   B CB  1 
ATOM   2926 C CG  . MET   B 1 30  ? 39.870  14.648 31.133  1.00 44.17  ? 686  MET   B CG  1 
ATOM   2927 S SD  . MET   B 1 30  ? 41.681  14.719 31.207  1.00 46.94  ? 686  MET   B SD  1 
ATOM   2928 C CE  . MET   B 1 30  ? 42.050  14.828 29.439  1.00 43.40  ? 686  MET   B CE  1 
ATOM   2929 N N   . VAL   B 1 31  ? 37.156  10.861 30.494  1.00 46.82  ? 687  VAL   B N   1 
ATOM   2930 C CA  . VAL   B 1 31  ? 36.574  9.648  29.899  1.00 46.31  ? 687  VAL   B CA  1 
ATOM   2931 C C   . VAL   B 1 31  ? 35.053  9.842  29.656  1.00 50.17  ? 687  VAL   B C   1 
ATOM   2932 O O   . VAL   B 1 31  ? 34.540  9.409  28.629  1.00 50.79  ? 687  VAL   B O   1 
ATOM   2933 C CB  . VAL   B 1 31  ? 36.921  8.389  30.753  1.00 49.90  ? 687  VAL   B CB  1 
ATOM   2934 C CG1 . VAL   B 1 31  ? 36.021  7.195  30.423  1.00 49.93  ? 687  VAL   B CG1 1 
ATOM   2935 C CG2 . VAL   B 1 31  ? 38.389  8.005  30.588  1.00 49.51  ? 687  VAL   B CG2 1 
ATOM   2936 N N   . GLU   B 1 32  ? 34.364  10.541 30.574  1.00 46.16  ? 688  GLU   B N   1 
ATOM   2937 C CA  . GLU   B 1 32  ? 32.936  10.868 30.511  1.00 45.81  ? 688  GLU   B CA  1 
ATOM   2938 C C   . GLU   B 1 32  ? 32.618  11.747 29.283  1.00 50.05  ? 688  GLU   B C   1 
ATOM   2939 O O   . GLU   B 1 32  ? 31.507  11.687 28.748  1.00 50.22  ? 688  GLU   B O   1 
ATOM   2940 C CB  . GLU   B 1 32  ? 32.527  11.605 31.788  1.00 47.21  ? 688  GLU   B CB  1 
ATOM   2941 C CG  . GLU   B 1 32  ? 31.086  11.379 32.201  1.00 60.02  ? 688  GLU   B CG  1 
ATOM   2942 C CD  . GLU   B 1 32  ? 30.769  11.775 33.631  1.00 88.67  ? 688  GLU   B CD  1 
ATOM   2943 O OE1 . GLU   B 1 32  ? 29.696  12.381 33.844  1.00 86.55  ? 688  GLU   B OE1 1 
ATOM   2944 O OE2 . GLU   B 1 32  ? 31.589  11.483 34.535  1.00 85.66  ? 688  GLU   B OE2 1 
ATOM   2945 N N   . TYR   B 1 33  ? 33.602  12.554 28.846  1.00 45.19  ? 689  TYR   B N   1 
ATOM   2946 C CA  . TYR   B 1 33  ? 33.507  13.427 27.679  1.00 44.51  ? 689  TYR   B CA  1 
ATOM   2947 C C   . TYR   B 1 33  ? 33.875  12.709 26.376  1.00 47.57  ? 689  TYR   B C   1 
ATOM   2948 O O   . TYR   B 1 33  ? 33.841  13.314 25.303  1.00 46.84  ? 689  TYR   B O   1 
ATOM   2949 C CB  . TYR   B 1 33  ? 34.397  14.653 27.881  1.00 44.98  ? 689  TYR   B CB  1 
ATOM   2950 C CG  . TYR   B 1 33  ? 33.852  15.623 28.901  1.00 45.27  ? 689  TYR   B CG  1 
ATOM   2951 C CD1 . TYR   B 1 33  ? 32.586  16.183 28.753  1.00 46.68  ? 689  TYR   B CD1 1 
ATOM   2952 C CD2 . TYR   B 1 33  ? 34.634  16.050 29.973  1.00 45.83  ? 689  TYR   B CD2 1 
ATOM   2953 C CE1 . TYR   B 1 33  ? 32.102  17.125 29.658  1.00 46.83  ? 689  TYR   B CE1 1 
ATOM   2954 C CE2 . TYR   B 1 33  ? 34.145  16.961 30.909  1.00 46.44  ? 689  TYR   B CE2 1 
ATOM   2955 C CZ  . TYR   B 1 33  ? 32.883  17.505 30.737  1.00 50.97  ? 689  TYR   B CZ  1 
ATOM   2956 O OH  . TYR   B 1 33  ? 32.413  18.414 31.640  1.00 48.35  ? 689  TYR   B OH  1 
ATOM   2957 N N   . GLU   B 1 34  ? 34.230  11.421 26.490  1.00 44.03  ? 690  GLU   B N   1 
ATOM   2958 C CA  . GLU   B 1 34  ? 34.637  10.519 25.417  1.00 44.09  ? 690  GLU   B CA  1 
ATOM   2959 C C   . GLU   B 1 34  ? 35.988  10.940 24.790  1.00 46.77  ? 690  GLU   B C   1 
ATOM   2960 O O   . GLU   B 1 34  ? 36.258  10.590 23.644  1.00 45.01  ? 690  GLU   B O   1 
ATOM   2961 C CB  . GLU   B 1 34  ? 33.517  10.283 24.369  1.00 45.55  ? 690  GLU   B CB  1 
ATOM   2962 C CG  . GLU   B 1 34  ? 32.249  9.732  25.007  1.00 60.21  ? 690  GLU   B CG  1 
ATOM   2963 C CD  . GLU   B 1 34  ? 31.298  8.918  24.151  1.00 85.20  ? 690  GLU   B CD  1 
ATOM   2964 O OE1 . GLU   B 1 34  ? 30.136  9.357  23.987  1.00 77.45  ? 690  GLU   B OE1 1 
ATOM   2965 O OE2 . GLU   B 1 34  ? 31.691  7.825  23.680  1.00 79.20  ? 690  GLU   B OE2 1 
ATOM   2966 N N   . ILE   B 1 35  ? 36.868  11.592 25.580  1.00 43.03  ? 691  ILE   B N   1 
ATOM   2967 C CA  . ILE   B 1 35  ? 38.205  12.001 25.137  1.00 43.03  ? 691  ILE   B CA  1 
ATOM   2968 C C   . ILE   B 1 35  ? 39.110  10.751 25.121  1.00 48.33  ? 691  ILE   B C   1 
ATOM   2969 O O   . ILE   B 1 35  ? 39.065  9.955  26.061  1.00 47.54  ? 691  ILE   B O   1 
ATOM   2970 C CB  . ILE   B 1 35  ? 38.787  13.112 26.065  1.00 45.63  ? 691  ILE   B CB  1 
ATOM   2971 C CG1 . ILE   B 1 35  ? 37.904  14.387 26.082  1.00 45.39  ? 691  ILE   B CG1 1 
ATOM   2972 C CG2 . ILE   B 1 35  ? 40.262  13.433 25.727  1.00 46.07  ? 691  ILE   B CG2 1 
ATOM   2973 C CD1 . ILE   B 1 35  ? 38.007  15.206 27.384  1.00 48.64  ? 691  ILE   B CD1 1 
ATOM   2974 N N   . ASP   B 1 36  ? 39.921  10.576 24.063  1.00 45.99  ? 692  ASP   B N   1 
ATOM   2975 C CA  . ASP   B 1 36  ? 40.848  9.452  23.964  1.00 46.64  ? 692  ASP   B CA  1 
ATOM   2976 C C   . ASP   B 1 36  ? 42.008  9.769  24.898  1.00 51.88  ? 692  ASP   B C   1 
ATOM   2977 O O   . ASP   B 1 36  ? 42.840  10.633 24.600  1.00 51.79  ? 692  ASP   B O   1 
ATOM   2978 C CB  . ASP   B 1 36  ? 41.317  9.222  22.515  1.00 48.73  ? 692  ASP   B CB  1 
ATOM   2979 C CG  . ASP   B 1 36  ? 41.891  7.836  22.263  1.00 61.40  ? 692  ASP   B CG  1 
ATOM   2980 O OD1 . ASP   B 1 36  ? 42.987  7.535  22.793  1.00 61.16  ? 692  ASP   B OD1 1 
ATOM   2981 O OD2 . ASP   B 1 36  ? 41.256  7.060  21.524  1.00 72.99  ? 692  ASP   B OD2 1 
ATOM   2982 N N   . LEU   B 1 37  ? 41.977  9.141  26.082  1.00 49.58  ? 693  LEU   B N   1 
ATOM   2983 C CA  . LEU   B 1 37  ? 42.964  9.364  27.129  1.00 50.24  ? 693  LEU   B CA  1 
ATOM   2984 C C   . LEU   B 1 37  ? 44.344  8.772  26.778  1.00 56.46  ? 693  LEU   B C   1 
ATOM   2985 O O   . LEU   B 1 37  ? 45.352  9.242  27.313  1.00 55.84  ? 693  LEU   B O   1 
ATOM   2986 C CB  . LEU   B 1 37  ? 42.436  8.882  28.494  1.00 50.09  ? 693  LEU   B CB  1 
ATOM   2987 C CG  . LEU   B 1 37  ? 42.858  9.716  29.713  1.00 54.47  ? 693  LEU   B CG  1 
ATOM   2988 C CD1 . LEU   B 1 37  ? 42.150  11.050 29.754  1.00 54.01  ? 693  LEU   B CD1 1 
ATOM   2989 C CD2 . LEU   B 1 37  ? 42.580  8.979  30.999  1.00 57.81  ? 693  LEU   B CD2 1 
ATOM   2990 N N   . GLN   B 1 38  ? 44.391  7.785  25.842  1.00 54.66  ? 694  GLN   B N   1 
ATOM   2991 C CA  . GLN   B 1 38  ? 45.626  7.179  25.337  1.00 54.68  ? 694  GLN   B CA  1 
ATOM   2992 C C   . GLN   B 1 38  ? 46.298  8.176  24.381  1.00 59.18  ? 694  GLN   B C   1 
ATOM   2993 O O   . GLN   B 1 38  ? 47.486  8.474  24.544  1.00 58.95  ? 694  GLN   B O   1 
ATOM   2994 C CB  . GLN   B 1 38  ? 45.332  5.845  24.625  1.00 56.26  ? 694  GLN   B CB  1 
ATOM   2995 C CG  . GLN   B 1 38  ? 45.314  4.641  25.552  1.00 79.89  ? 694  GLN   B CG  1 
ATOM   2996 C CD  . GLN   B 1 38  ? 46.693  4.068  25.740  1.00 102.05 ? 694  GLN   B CD  1 
ATOM   2997 N N   . LYS   B 1 39  ? 45.508  8.737  23.428  1.00 56.40  ? 695  LYS   B N   1 
ATOM   2998 C CA  . LYS   B 1 39  ? 45.939  9.737  22.440  1.00 56.58  ? 695  LYS   B CA  1 
ATOM   2999 C C   . LYS   B 1 39  ? 46.255  11.080 23.098  1.00 60.99  ? 695  LYS   B C   1 
ATOM   3000 O O   . LYS   B 1 39  ? 47.021  11.868 22.537  1.00 60.56  ? 695  LYS   B O   1 
ATOM   3001 C CB  . LYS   B 1 39  ? 44.869  9.936  21.353  1.00 58.76  ? 695  LYS   B CB  1 
ATOM   3002 C CG  . LYS   B 1 39  ? 44.836  8.861  20.271  1.00 70.29  ? 695  LYS   B CG  1 
ATOM   3003 C CD  . LYS   B 1 39  ? 43.718  9.125  19.275  1.00 78.33  ? 695  LYS   B CD  1 
ATOM   3004 C CE  . LYS   B 1 39  ? 43.868  8.334  18.001  1.00 91.17  ? 695  LYS   B CE  1 
ATOM   3005 N NZ  . LYS   B 1 39  ? 43.248  6.990  18.108  1.00 104.06 ? 695  LYS   B NZ  1 
ATOM   3006 N N   . MET   B 1 40  ? 45.633  11.356 24.262  1.00 57.91  ? 696  MET   B N   1 
ATOM   3007 C CA  . MET   B 1 40  ? 45.856  12.589 25.005  1.00 57.90  ? 696  MET   B CA  1 
ATOM   3008 C C   . MET   B 1 40  ? 45.541  12.463 26.510  1.00 58.97  ? 696  MET   B C   1 
ATOM   3009 O O   . MET   B 1 40  ? 44.430  12.785 26.946  1.00 57.88  ? 696  MET   B O   1 
ATOM   3010 C CB  . MET   B 1 40  ? 45.137  13.798 24.375  1.00 60.62  ? 696  MET   B CB  1 
ATOM   3011 C CG  . MET   B 1 40  ? 45.757  15.113 24.809  1.00 64.63  ? 696  MET   B CG  1 
ATOM   3012 S SD  . MET   B 1 40  ? 44.628  16.461 25.202  1.00 69.32  ? 696  MET   B SD  1 
ATOM   3013 C CE  . MET   B 1 40  ? 43.302  15.620 25.960  1.00 66.04  ? 696  MET   B CE  1 
ATOM   3014 N N   . PRO   B 1 41  ? 46.553  12.052 27.312  1.00 54.05  ? 697  PRO   B N   1 
ATOM   3015 C CA  . PRO   B 1 41  ? 46.353  11.959 28.768  1.00 52.80  ? 697  PRO   B CA  1 
ATOM   3016 C C   . PRO   B 1 41  ? 46.239  13.329 29.451  1.00 53.17  ? 697  PRO   B C   1 
ATOM   3017 O O   . PRO   B 1 41  ? 46.367  14.381 28.804  1.00 52.95  ? 697  PRO   B O   1 
ATOM   3018 C CB  . PRO   B 1 41  ? 47.581  11.172 29.243  1.00 54.67  ? 697  PRO   B CB  1 
ATOM   3019 C CG  . PRO   B 1 41  ? 48.633  11.503 28.255  1.00 59.25  ? 697  PRO   B CG  1 
ATOM   3020 C CD  . PRO   B 1 41  ? 47.920  11.637 26.935  1.00 55.01  ? 697  PRO   B CD  1 
ATOM   3021 N N   . LEU   B 1 42  ? 45.985  13.284 30.773  1.00 45.64  ? 698  LEU   B N   1 
ATOM   3022 C CA  . LEU   B 1 42  ? 45.766  14.390 31.694  1.00 43.44  ? 698  LEU   B CA  1 
ATOM   3023 C C   . LEU   B 1 42  ? 46.906  15.427 31.721  1.00 45.92  ? 698  LEU   B C   1 
ATOM   3024 O O   . LEU   B 1 42  ? 46.626  16.622 31.844  1.00 45.31  ? 698  LEU   B O   1 
ATOM   3025 C CB  . LEU   B 1 42  ? 45.492  13.779 33.080  1.00 42.80  ? 698  LEU   B CB  1 
ATOM   3026 C CG  . LEU   B 1 42  ? 45.208  14.674 34.266  1.00 46.83  ? 698  LEU   B CG  1 
ATOM   3027 C CD1 . LEU   B 1 42  ? 44.068  15.670 33.980  1.00 47.48  ? 698  LEU   B CD1 1 
ATOM   3028 C CD2 . LEU   B 1 42  ? 44.869  13.840 35.454  1.00 46.98  ? 698  LEU   B CD2 1 
ATOM   3029 N N   . GLY   B 1 43  ? 48.152  14.958 31.615  1.00 41.08  ? 699  GLY   B N   1 
ATOM   3030 C CA  . GLY   B 1 43  ? 49.360  15.777 31.575  1.00 41.20  ? 699  GLY   B CA  1 
ATOM   3031 C C   . GLY   B 1 43  ? 49.621  16.451 30.239  1.00 46.69  ? 699  GLY   B C   1 
ATOM   3032 O O   . GLY   B 1 43  ? 50.482  17.336 30.152  1.00 46.25  ? 699  GLY   B O   1 
ATOM   3033 N N   . LYS   B 1 44  ? 48.904  16.026 29.175  1.00 43.77  ? 700  LYS   B N   1 
ATOM   3034 C CA  . LYS   B 1 44  ? 49.031  16.636 27.845  1.00 43.80  ? 700  LYS   B CA  1 
ATOM   3035 C C   . LYS   B 1 44  ? 48.031  17.803 27.661  1.00 46.30  ? 700  LYS   B C   1 
ATOM   3036 O O   . LYS   B 1 44  ? 48.162  18.577 26.710  1.00 46.58  ? 700  LYS   B O   1 
ATOM   3037 C CB  . LYS   B 1 44  ? 48.916  15.583 26.724  1.00 46.60  ? 700  LYS   B CB  1 
ATOM   3038 C CG  . LYS   B 1 44  ? 50.213  14.794 26.512  1.00 59.80  ? 700  LYS   B CG  1 
ATOM   3039 C CD  . LYS   B 1 44  ? 50.150  13.889 25.281  1.00 72.56  ? 700  LYS   B CD  1 
ATOM   3040 C CE  . LYS   B 1 44  ? 51.125  12.730 25.387  1.00 90.62  ? 700  LYS   B CE  1 
ATOM   3041 N NZ  . LYS   B 1 44  ? 50.819  11.616 24.445  1.00 101.37 ? 700  LYS   B NZ  1 
ATOM   3042 N N   . LEU   B 1 45  ? 47.069  17.942 28.600  1.00 39.70  ? 701  LEU   B N   1 
ATOM   3043 C CA  . LEU   B 1 45  ? 46.061  19.004 28.616  1.00 38.29  ? 701  LEU   B CA  1 
ATOM   3044 C C   . LEU   B 1 45  ? 46.741  20.359 28.827  1.00 38.41  ? 701  LEU   B C   1 
ATOM   3045 O O   . LEU   B 1 45  ? 47.563  20.501 29.732  1.00 38.65  ? 701  LEU   B O   1 
ATOM   3046 C CB  . LEU   B 1 45  ? 45.077  18.762 29.773  1.00 38.38  ? 701  LEU   B CB  1 
ATOM   3047 C CG  . LEU   B 1 45  ? 43.539  18.896 29.548  1.00 43.16  ? 701  LEU   B CG  1 
ATOM   3048 C CD1 . LEU   B 1 45  ? 42.870  19.544 30.734  1.00 43.27  ? 701  LEU   B CD1 1 
ATOM   3049 C CD2 . LEU   B 1 45  ? 43.172  19.527 28.222  1.00 44.68  ? 701  LEU   B CD2 1 
ATOM   3050 N N   . SER   B 1 46  ? 46.428  21.346 27.983  1.00 31.65  ? 702  SER   B N   1 
ATOM   3051 C CA  . SER   B 1 46  ? 47.044  22.664 28.141  1.00 30.34  ? 702  SER   B CA  1 
ATOM   3052 C C   . SER   B 1 46  ? 46.066  23.775 27.858  1.00 31.57  ? 702  SER   B C   1 
ATOM   3053 O O   . SER   B 1 46  ? 45.116  23.568 27.091  1.00 30.36  ? 702  SER   B O   1 
ATOM   3054 C CB  . SER   B 1 46  ? 48.293  22.806 27.271  1.00 32.45  ? 702  SER   B CB  1 
ATOM   3055 O OG  . SER   B 1 46  ? 47.986  23.201 25.945  1.00 34.96  ? 702  SER   B OG  1 
ATOM   3056 N N   . LYS   B 1 47  ? 46.330  24.974 28.435  1.00 26.49  ? 703  LYS   B N   1 
ATOM   3057 C CA  . LYS   B 1 47  ? 45.457  26.110 28.203  1.00 26.40  ? 703  LYS   B CA  1 
ATOM   3058 C C   . LYS   B 1 47  ? 45.433  26.519 26.725  1.00 28.82  ? 703  LYS   B C   1 
ATOM   3059 O O   . LYS   B 1 47  ? 44.354  26.805 26.220  1.00 27.52  ? 703  LYS   B O   1 
ATOM   3060 C CB  . LYS   B 1 47  ? 45.765  27.294 29.138  1.00 28.85  ? 703  LYS   B CB  1 
ATOM   3061 C CG  . LYS   B 1 47  ? 44.578  28.254 29.227  1.00 45.53  ? 703  LYS   B CG  1 
ATOM   3062 C CD  . LYS   B 1 47  ? 44.838  29.502 30.065  1.00 55.94  ? 703  LYS   B CD  1 
ATOM   3063 C CE  . LYS   B 1 47  ? 43.986  30.688 29.636  1.00 56.47  ? 703  LYS   B CE  1 
ATOM   3064 N NZ  . LYS   B 1 47  ? 42.518  30.407 29.663  1.00 52.70  ? 703  LYS   B NZ  1 
ATOM   3065 N N   . ARG   B 1 48  ? 46.592  26.459 26.021  1.00 24.83  ? 704  ARG   B N   1 
ATOM   3066 C CA  . ARG   B 1 48  ? 46.678  26.866 24.613  1.00 25.17  ? 704  ARG   B CA  1 
ATOM   3067 C C   . ARG   B 1 48  ? 45.972  25.901 23.660  1.00 28.10  ? 704  ARG   B C   1 
ATOM   3068 O O   . ARG   B 1 48  ? 45.457  26.340 22.627  1.00 26.05  ? 704  ARG   B O   1 
ATOM   3069 C CB  . ARG   B 1 48  ? 48.124  27.137 24.166  1.00 27.23  ? 704  ARG   B CB  1 
ATOM   3070 C CG  . ARG   B 1 48  ? 48.896  28.088 25.079  1.00 33.69  ? 704  ARG   B CG  1 
ATOM   3071 C CD  . ARG   B 1 48  ? 50.385  27.779 24.955  1.00 48.92  ? 704  ARG   B CD  1 
ATOM   3072 N NE  . ARG   B 1 48  ? 51.254  28.925 25.240  1.00 56.96  ? 704  ARG   B NE  1 
ATOM   3073 C CZ  . ARG   B 1 48  ? 51.323  30.028 24.499  1.00 67.36  ? 704  ARG   B CZ  1 
ATOM   3074 N NH1 . ARG   B 1 48  ? 52.163  31.000 24.824  1.00 46.58  ? 704  ARG   B NH1 1 
ATOM   3075 N NH2 . ARG   B 1 48  ? 50.546  30.171 23.432  1.00 58.98  ? 704  ARG   B NH2 1 
ATOM   3076 N N   . GLN   B 1 49  ? 45.930  24.601 24.016  1.00 24.51  ? 705  GLN   B N   1 
ATOM   3077 C CA  . GLN   B 1 49  ? 45.190  23.585 23.251  1.00 24.18  ? 705  GLN   B CA  1 
ATOM   3078 C C   . GLN   B 1 49  ? 43.659  23.857 23.428  1.00 26.72  ? 705  GLN   B C   1 
ATOM   3079 O O   . GLN   B 1 49  ? 42.970  24.019 22.429  1.00 25.99  ? 705  GLN   B O   1 
ATOM   3080 C CB  . GLN   B 1 49  ? 45.576  22.178 23.728  1.00 25.46  ? 705  GLN   B CB  1 
ATOM   3081 C CG  . GLN   B 1 49  ? 44.621  21.076 23.276  1.00 37.63  ? 705  GLN   B CG  1 
ATOM   3082 C CD  . GLN   B 1 49  ? 44.925  19.731 23.895  1.00 56.28  ? 705  GLN   B CD  1 
ATOM   3083 O OE1 . GLN   B 1 49  ? 45.329  19.614 25.066  1.00 51.67  ? 705  GLN   B OE1 1 
ATOM   3084 N NE2 . GLN   B 1 49  ? 44.730  18.678 23.110  1.00 44.68  ? 705  GLN   B NE2 1 
ATOM   3085 N N   . ILE   B 1 50  ? 43.165  23.988 24.691  1.00 23.07  ? 706  ILE   B N   1 
ATOM   3086 C CA  . ILE   B 1 50  ? 41.760  24.302 25.037  1.00 22.12  ? 706  ILE   B CA  1 
ATOM   3087 C C   . ILE   B 1 50  ? 41.343  25.644 24.408  1.00 24.39  ? 706  ILE   B C   1 
ATOM   3088 O O   . ILE   B 1 50  ? 40.246  25.747 23.870  1.00 24.09  ? 706  ILE   B O   1 
ATOM   3089 C CB  . ILE   B 1 50  ? 41.489  24.258 26.578  1.00 24.55  ? 706  ILE   B CB  1 
ATOM   3090 C CG1 . ILE   B 1 50  ? 41.834  22.864 27.174  1.00 23.91  ? 706  ILE   B CG1 1 
ATOM   3091 C CG2 . ILE   B 1 50  ? 40.031  24.666 26.926  1.00 24.02  ? 706  ILE   B CG2 1 
ATOM   3092 C CD1 . ILE   B 1 50  ? 42.108  22.889 28.733  1.00 23.14  ? 706  ILE   B CD1 1 
ATOM   3093 N N   . GLN   B 1 51  ? 42.252  26.642 24.419  1.00 20.06  ? 707  GLN   B N   1 
ATOM   3094 C CA  . GLN   B 1 51  ? 42.038  27.944 23.794  1.00 18.83  ? 707  GLN   B CA  1 
ATOM   3095 C C   . GLN   B 1 51  ? 41.930  27.786 22.267  1.00 21.84  ? 707  GLN   B C   1 
ATOM   3096 O O   . GLN   B 1 51  ? 41.115  28.473 21.675  1.00 23.21  ? 707  GLN   B O   1 
ATOM   3097 C CB  . GLN   B 1 51  ? 43.125  28.950 24.200  1.00 19.64  ? 707  GLN   B CB  1 
ATOM   3098 C CG  . GLN   B 1 51  ? 42.800  29.693 25.493  1.00 27.48  ? 707  GLN   B CG  1 
ATOM   3099 C CD  . GLN   B 1 51  ? 43.864  30.721 25.850  1.00 38.67  ? 707  GLN   B CD  1 
ATOM   3100 O OE1 . GLN   B 1 51  ? 45.024  30.415 25.904  1.00 28.19  ? 707  GLN   B OE1 1 
ATOM   3101 N NE2 . GLN   B 1 51  ? 43.499  31.968 26.115  1.00 35.63  ? 707  GLN   B NE2 1 
ATOM   3102 N N   . ALA   B 1 52  ? 42.715  26.875 21.635  1.00 17.46  ? 708  ALA   B N   1 
ATOM   3103 C CA  . ALA   B 1 52  ? 42.623  26.586 20.190  1.00 17.41  ? 708  ALA   B CA  1 
ATOM   3104 C C   . ALA   B 1 52  ? 41.301  25.870 19.852  1.00 19.82  ? 708  ALA   B C   1 
ATOM   3105 O O   . ALA   B 1 52  ? 40.732  26.121 18.793  1.00 20.57  ? 708  ALA   B O   1 
ATOM   3106 C CB  . ALA   B 1 52  ? 43.801  25.749 19.712  1.00 17.85  ? 708  ALA   B CB  1 
ATOM   3107 N N   . ALA   B 1 53  ? 40.820  24.985 20.740  1.00 14.83  ? 709  ALA   B N   1 
ATOM   3108 C CA  . ALA   B 1 53  ? 39.528  24.313 20.571  1.00 15.77  ? 709  ALA   B CA  1 
ATOM   3109 C C   . ALA   B 1 53  ? 38.375  25.347 20.635  1.00 21.10  ? 709  ALA   B C   1 
ATOM   3110 O O   . ALA   B 1 53  ? 37.465  25.259 19.795  1.00 21.11  ? 709  ALA   B O   1 
ATOM   3111 C CB  . ALA   B 1 53  ? 39.338  23.241 21.636  1.00 16.69  ? 709  ALA   B CB  1 
ATOM   3112 N N   . TYR   B 1 54  ? 38.443  26.360 21.584  1.00 19.21  ? 710  TYR   B N   1 
ATOM   3113 C CA  . TYR   B 1 54  ? 37.446  27.465 21.690  1.00 19.70  ? 710  TYR   B CA  1 
ATOM   3114 C C   . TYR   B 1 54  ? 37.402  28.286 20.398  1.00 23.87  ? 710  TYR   B C   1 
ATOM   3115 O O   . TYR   B 1 54  ? 36.313  28.654 19.956  1.00 24.16  ? 710  TYR   B O   1 
ATOM   3116 C CB  . TYR   B 1 54  ? 37.806  28.454 22.798  1.00 21.60  ? 710  TYR   B CB  1 
ATOM   3117 C CG  . TYR   B 1 54  ? 37.389  28.085 24.204  1.00 23.47  ? 710  TYR   B CG  1 
ATOM   3118 C CD1 . TYR   B 1 54  ? 36.058  27.844 24.520  1.00 24.17  ? 710  TYR   B CD1 1 
ATOM   3119 C CD2 . TYR   B 1 54  ? 38.321  28.061 25.243  1.00 24.53  ? 710  TYR   B CD2 1 
ATOM   3120 C CE1 . TYR   B 1 54  ? 35.665  27.568 25.836  1.00 24.95  ? 710  TYR   B CE1 1 
ATOM   3121 C CE2 . TYR   B 1 54  ? 37.944  27.758 26.548  1.00 24.37  ? 710  TYR   B CE2 1 
ATOM   3122 C CZ  . TYR   B 1 54  ? 36.613  27.569 26.852  1.00 24.63  ? 710  TYR   B CZ  1 
ATOM   3123 O OH  . TYR   B 1 54  ? 36.293  27.307 28.160  1.00 20.94  ? 710  TYR   B OH  1 
ATOM   3124 N N   . SER   B 1 55  ? 38.598  28.582 19.801  1.00 20.45  ? 711  SER   B N   1 
ATOM   3125 C CA  . SER   B 1 55  ? 38.771  29.288 18.512  1.00 19.85  ? 711  SER   B CA  1 
ATOM   3126 C C   . SER   B 1 55  ? 38.085  28.505 17.361  1.00 21.96  ? 711  SER   B C   1 
ATOM   3127 O O   . SER   B 1 55  ? 37.530  29.143 16.487  1.00 21.10  ? 711  SER   B O   1 
ATOM   3128 C CB  . SER   B 1 55  ? 40.251  29.517 18.185  1.00 22.38  ? 711  SER   B CB  1 
ATOM   3129 O OG  . SER   B 1 55  ? 40.966  30.137 19.249  1.00 29.13  ? 711  SER   B OG  1 
ATOM   3130 N N   . ILE   B 1 56  ? 38.096  27.144 17.384  1.00 18.37  ? 712  ILE   B N   1 
ATOM   3131 C CA  . ILE   B 1 56  ? 37.394  26.303 16.382  1.00 18.66  ? 712  ILE   B CA  1 
ATOM   3132 C C   . ILE   B 1 56  ? 35.844  26.468 16.545  1.00 22.28  ? 712  ILE   B C   1 
ATOM   3133 O O   . ILE   B 1 56  ? 35.133  26.662 15.549  1.00 22.46  ? 712  ILE   B O   1 
ATOM   3134 C CB  . ILE   B 1 56  ? 37.860  24.809 16.392  1.00 21.49  ? 712  ILE   B CB  1 
ATOM   3135 C CG1 . ILE   B 1 56  ? 39.357  24.690 15.964  1.00 21.81  ? 712  ILE   B CG1 1 
ATOM   3136 C CG2 . ILE   B 1 56  ? 36.955  23.927 15.468  1.00 21.00  ? 712  ILE   B CG2 1 
ATOM   3137 C CD1 . ILE   B 1 56  ? 39.976  23.303 16.109  1.00 24.76  ? 712  ILE   B CD1 1 
ATOM   3138 N N   . LEU   B 1 57  ? 35.350  26.433 17.807  1.00 18.23  ? 713  LEU   B N   1 
ATOM   3139 C CA  . LEU   B 1 57  ? 33.937  26.638 18.149  1.00 19.30  ? 713  LEU   B CA  1 
ATOM   3140 C C   . LEU   B 1 57  ? 33.491  28.041 17.751  1.00 22.27  ? 713  LEU   B C   1 
ATOM   3141 O O   . LEU   B 1 57  ? 32.418  28.198 17.186  1.00 20.95  ? 713  LEU   B O   1 
ATOM   3142 C CB  . LEU   B 1 57  ? 33.682  26.397 19.645  1.00 19.08  ? 713  LEU   B CB  1 
ATOM   3143 C CG  . LEU   B 1 57  ? 33.977  24.973 20.170  1.00 23.20  ? 713  LEU   B CG  1 
ATOM   3144 C CD1 . LEU   B 1 57  ? 33.495  24.832 21.611  1.00 23.24  ? 713  LEU   B CD1 1 
ATOM   3145 C CD2 . LEU   B 1 57  ? 33.311  23.893 19.298  1.00 24.44  ? 713  LEU   B CD2 1 
ATOM   3146 N N   . SER   B 1 58  ? 34.363  29.046 17.973  1.00 19.42  ? 714  SER   B N   1 
ATOM   3147 C CA  . SER   B 1 58  ? 34.062  30.416 17.581  1.00 18.59  ? 714  SER   B CA  1 
ATOM   3148 C C   . SER   B 1 58  ? 33.969  30.529 16.063  1.00 20.79  ? 714  SER   B C   1 
ATOM   3149 O O   . SER   B 1 58  ? 33.048  31.172 15.563  1.00 17.59  ? 714  SER   B O   1 
ATOM   3150 C CB  . SER   B 1 58  ? 35.071  31.384 18.177  1.00 19.11  ? 714  SER   B CB  1 
ATOM   3151 O OG  . SER   B 1 58  ? 34.749  31.540 19.547  1.00 23.59  ? 714  SER   B OG  1 
ATOM   3152 N N   . GLU   B 1 59  ? 34.869  29.839 15.339  1.00 18.77  ? 715  GLU   B N   1 
ATOM   3153 C CA  . GLU   B 1 59  ? 34.797  29.782 13.888  1.00 19.27  ? 715  GLU   B CA  1 
ATOM   3154 C C   . GLU   B 1 59  ? 33.491  29.080 13.410  1.00 23.24  ? 715  GLU   B C   1 
ATOM   3155 O O   . GLU   B 1 59  ? 32.938  29.473 12.376  1.00 21.44  ? 715  GLU   B O   1 
ATOM   3156 C CB  . GLU   B 1 59  ? 36.038  29.129 13.282  1.00 20.58  ? 715  GLU   B CB  1 
ATOM   3157 C CG  . GLU   B 1 59  ? 36.241  29.515 11.817  1.00 29.19  ? 715  GLU   B CG  1 
ATOM   3158 C CD  . GLU   B 1 59  ? 36.632  30.956 11.558  1.00 43.53  ? 715  GLU   B CD  1 
ATOM   3159 O OE1 . GLU   B 1 59  ? 37.496  31.478 12.294  1.00 28.59  ? 715  GLU   B OE1 1 
ATOM   3160 O OE2 . GLU   B 1 59  ? 36.093  31.557 10.602  1.00 45.22  ? 715  GLU   B OE2 1 
ATOM   3161 N N   . VAL   B 1 60  ? 33.017  28.051 14.144  1.00 20.13  ? 716  VAL   B N   1 
ATOM   3162 C CA  . VAL   B 1 60  ? 31.744  27.403 13.822  1.00 20.71  ? 716  VAL   B CA  1 
ATOM   3163 C C   . VAL   B 1 60  ? 30.586  28.424 13.991  1.00 25.24  ? 716  VAL   B C   1 
ATOM   3164 O O   . VAL   B 1 60  ? 29.801  28.554 13.065  1.00 23.59  ? 716  VAL   B O   1 
ATOM   3165 C CB  . VAL   B 1 60  ? 31.469  26.054 14.558  1.00 25.02  ? 716  VAL   B CB  1 
ATOM   3166 C CG1 . VAL   B 1 60  ? 30.017  25.601 14.374  1.00 25.11  ? 716  VAL   B CG1 1 
ATOM   3167 C CG2 . VAL   B 1 60  ? 32.422  24.964 14.090  1.00 24.63  ? 716  VAL   B CG2 1 
ATOM   3168 N N   . GLN   B 1 61  ? 30.528  29.175 15.131  1.00 24.63  ? 717  GLN   B N   1 
ATOM   3169 C CA  . GLN   B 1 61  ? 29.497  30.215 15.445  1.00 24.48  ? 717  GLN   B CA  1 
ATOM   3170 C C   . GLN   B 1 61  ? 29.429  31.233 14.277  1.00 28.13  ? 717  GLN   B C   1 
ATOM   3171 O O   . GLN   B 1 61  ? 28.353  31.501 13.734  1.00 28.04  ? 717  GLN   B O   1 
ATOM   3172 C CB  . GLN   B 1 61  ? 29.833  30.919 16.811  1.00 26.59  ? 717  GLN   B CB  1 
ATOM   3173 C CG  . GLN   B 1 61  ? 29.492  32.450 16.936  1.00 47.40  ? 717  GLN   B CG  1 
ATOM   3174 C CD  . GLN   B 1 61  ? 30.039  33.184 18.173  1.00 52.23  ? 717  GLN   B CD  1 
ATOM   3175 O OE1 . GLN   B 1 61  ? 29.822  32.789 19.310  1.00 47.96  ? 717  GLN   B OE1 1 
ATOM   3176 N NE2 . GLN   B 1 61  ? 30.722  34.307 17.992  1.00 28.88  ? 717  GLN   B NE2 1 
ATOM   3177 N N   . GLN   B 1 62  ? 30.608  31.744 13.881  1.00 24.30  ? 718  GLN   B N   1 
ATOM   3178 C CA  . GLN   B 1 62  ? 30.842  32.691 12.809  1.00 24.68  ? 718  GLN   B CA  1 
ATOM   3179 C C   . GLN   B 1 62  ? 30.339  32.121 11.451  1.00 29.64  ? 718  GLN   B C   1 
ATOM   3180 O O   . GLN   B 1 62  ? 29.620  32.803 10.718  1.00 26.82  ? 718  GLN   B O   1 
ATOM   3181 C CB  . GLN   B 1 62  ? 32.339  33.007 12.784  1.00 25.93  ? 718  GLN   B CB  1 
ATOM   3182 C CG  . GLN   B 1 62  ? 32.690  34.430 12.385  1.00 41.83  ? 718  GLN   B CG  1 
ATOM   3183 C CD  . GLN   B 1 62  ? 32.124  35.556 13.240  1.00 46.38  ? 718  GLN   B CD  1 
ATOM   3184 O OE1 . GLN   B 1 62  ? 31.575  35.388 14.345  1.00 37.32  ? 718  GLN   B OE1 1 
ATOM   3185 N NE2 . GLN   B 1 62  ? 32.267  36.753 12.713  1.00 32.78  ? 718  GLN   B NE2 1 
ATOM   3186 N N   . ALA   B 1 63  ? 30.651  30.843 11.183  1.00 28.31  ? 719  ALA   B N   1 
ATOM   3187 C CA  . ALA   B 1 63  ? 30.235  30.133 9.975   1.00 29.21  ? 719  ALA   B CA  1 
ATOM   3188 C C   . ALA   B 1 63  ? 28.700  29.910 9.924   1.00 33.07  ? 719  ALA   B C   1 
ATOM   3189 O O   . ALA   B 1 63  ? 28.094  30.168 8.891   1.00 32.66  ? 719  ALA   B O   1 
ATOM   3190 C CB  . ALA   B 1 63  ? 30.989  28.809 9.865   1.00 30.03  ? 719  ALA   B CB  1 
ATOM   3191 N N   . VAL   B 1 64  ? 28.081  29.482 11.043  1.00 31.32  ? 720  VAL   B N   1 
ATOM   3192 C CA  . VAL   B 1 64  ? 26.631  29.251 11.183  1.00 31.79  ? 720  VAL   B CA  1 
ATOM   3193 C C   . VAL   B 1 64  ? 25.843  30.560 10.898  1.00 40.28  ? 720  VAL   B C   1 
ATOM   3194 O O   . VAL   B 1 64  ? 24.797  30.506 10.232  1.00 39.47  ? 720  VAL   B O   1 
ATOM   3195 C CB  . VAL   B 1 64  ? 26.285  28.654 12.595  1.00 35.08  ? 720  VAL   B CB  1 
ATOM   3196 C CG1 . VAL   B 1 64  ? 24.794  28.723 12.914  1.00 34.91  ? 720  VAL   B CG1 1 
ATOM   3197 C CG2 . VAL   B 1 64  ? 26.794  27.229 12.753  1.00 34.65  ? 720  VAL   B CG2 1 
ATOM   3198 N N   . SER   B 1 65  ? 26.353  31.725 11.399  1.00 39.70  ? 721  SER   B N   1 
ATOM   3199 C CA  . SER   B 1 65  ? 25.674  33.028 11.286  1.00 41.31  ? 721  SER   B CA  1 
ATOM   3200 C C   . SER   B 1 65  ? 25.742  33.661 9.888   1.00 48.33  ? 721  SER   B C   1 
ATOM   3201 O O   . SER   B 1 65  ? 24.743  34.224 9.444   1.00 48.36  ? 721  SER   B O   1 
ATOM   3202 C CB  . SER   B 1 65  ? 26.156  34.002 12.359  1.00 44.95  ? 721  SER   B CB  1 
ATOM   3203 O OG  . SER   B 1 65  ? 27.355  34.667 11.999  1.00 57.06  ? 721  SER   B OG  1 
ATOM   3204 N N   . GLN   B 1 66  ? 26.888  33.552 9.190   1.00 47.32  ? 722  GLN   B N   1 
ATOM   3205 C CA  . GLN   B 1 66  ? 27.046  34.093 7.837   1.00 48.10  ? 722  GLN   B CA  1 
ATOM   3206 C C   . GLN   B 1 66  ? 26.197  33.306 6.797   1.00 53.33  ? 722  GLN   B C   1 
ATOM   3207 O O   . GLN   B 1 66  ? 25.896  33.847 5.724   1.00 52.75  ? 722  GLN   B O   1 
ATOM   3208 C CB  . GLN   B 1 66  ? 28.547  34.211 7.451   1.00 49.78  ? 722  GLN   B CB  1 
ATOM   3209 C CG  . GLN   B 1 66  ? 29.081  33.300 6.314   1.00 68.26  ? 722  GLN   B CG  1 
ATOM   3210 C CD  . GLN   B 1 66  ? 28.930  33.856 4.896   1.00 85.06  ? 722  GLN   B CD  1 
ATOM   3211 O OE1 . GLN   B 1 66  ? 28.848  35.065 4.659   1.00 81.93  ? 722  GLN   B OE1 1 
ATOM   3212 N NE2 . GLN   B 1 66  ? 28.897  32.978 3.907   1.00 71.53  ? 722  GLN   B NE2 1 
ATOM   3213 N N   . GLY   B 1 67  ? 25.813  32.064 7.138   1.00 50.64  ? 723  GLY   B N   1 
ATOM   3214 C CA  . GLY   B 1 67  ? 25.028  31.179 6.274   1.00 50.59  ? 723  GLY   B CA  1 
ATOM   3215 C C   . GLY   B 1 67  ? 25.835  30.718 5.073   1.00 54.97  ? 723  GLY   B C   1 
ATOM   3216 O O   . GLY   B 1 67  ? 26.910  31.269 4.819   1.00 55.81  ? 723  GLY   B O   1 
ATOM   3217 N N   . SER   B 1 68  ? 25.348  29.703 4.320   1.00 50.19  ? 724  SER   B N   1 
ATOM   3218 C CA  . SER   B 1 68  ? 26.048  29.165 3.131   1.00 49.62  ? 724  SER   B CA  1 
ATOM   3219 C C   . SER   B 1 68  ? 27.536  28.796 3.411   1.00 52.31  ? 724  SER   B C   1 
ATOM   3220 O O   . SER   B 1 68  ? 28.425  29.048 2.587   1.00 51.84  ? 724  SER   B O   1 
ATOM   3221 C CB  . SER   B 1 68  ? 25.921  30.123 1.946   1.00 53.68  ? 724  SER   B CB  1 
ATOM   3222 O OG  . SER   B 1 68  ? 24.564  30.454 1.701   1.00 64.39  ? 724  SER   B OG  1 
ATOM   3223 N N   . SER   B 1 69  ? 27.786  28.221 4.600   1.00 48.46  ? 725  SER   B N   1 
ATOM   3224 C CA  . SER   B 1 69  ? 29.104  27.812 5.085   1.00 48.44  ? 725  SER   B CA  1 
ATOM   3225 C C   . SER   B 1 69  ? 29.071  26.403 5.733   1.00 52.08  ? 725  SER   B C   1 
ATOM   3226 O O   . SER   B 1 69  ? 30.029  26.020 6.406   1.00 52.80  ? 725  SER   B O   1 
ATOM   3227 C CB  . SER   B 1 69  ? 29.640  28.851 6.077   1.00 51.90  ? 725  SER   B CB  1 
ATOM   3228 O OG  . SER   B 1 69  ? 29.989  30.069 5.440   1.00 57.73  ? 725  SER   B OG  1 
ATOM   3229 N N   . ASP   B 1 70  ? 27.976  25.639 5.516   1.00 46.90  ? 726  ASP   B N   1 
ATOM   3230 C CA  . ASP   B 1 70  ? 27.729  24.295 6.059   1.00 45.94  ? 726  ASP   B CA  1 
ATOM   3231 C C   . ASP   B 1 70  ? 28.844  23.266 5.763   1.00 47.11  ? 726  ASP   B C   1 
ATOM   3232 O O   . ASP   B 1 70  ? 29.125  22.417 6.613   1.00 46.37  ? 726  ASP   B O   1 
ATOM   3233 C CB  . ASP   B 1 70  ? 26.358  23.774 5.593   1.00 47.97  ? 726  ASP   B CB  1 
ATOM   3234 C CG  . ASP   B 1 70  ? 25.176  24.582 6.106   1.00 58.84  ? 726  ASP   B CG  1 
ATOM   3235 O OD1 . ASP   B 1 70  ? 25.156  24.908 7.318   1.00 59.29  ? 726  ASP   B OD1 1 
ATOM   3236 O OD2 . ASP   B 1 70  ? 24.263  24.879 5.298   1.00 63.60  ? 726  ASP   B OD2 1 
ATOM   3237 N N   . SER   B 1 71  ? 29.486  23.368 4.578   1.00 41.44  ? 727  SER   B N   1 
ATOM   3238 C CA  . SER   B 1 71  ? 30.598  22.532 4.131   1.00 40.73  ? 727  SER   B CA  1 
ATOM   3239 C C   . SER   B 1 71  ? 31.832  22.833 4.981   1.00 43.83  ? 727  SER   B C   1 
ATOM   3240 O O   . SER   B 1 71  ? 32.617  21.925 5.246   1.00 44.12  ? 727  SER   B O   1 
ATOM   3241 C CB  . SER   B 1 71  ? 30.895  22.807 2.661   1.00 44.38  ? 727  SER   B CB  1 
ATOM   3242 O OG  . SER   B 1 71  ? 31.893  21.953 2.124   1.00 51.04  ? 727  SER   B OG  1 
ATOM   3243 N N   . GLN   B 1 72  ? 31.995  24.097 5.417   1.00 39.01  ? 728  GLN   B N   1 
ATOM   3244 C CA  . GLN   B 1 72  ? 33.102  24.522 6.275   1.00 37.83  ? 728  GLN   B CA  1 
ATOM   3245 C C   . GLN   B 1 72  ? 32.825  24.075 7.708   1.00 39.95  ? 728  GLN   B C   1 
ATOM   3246 O O   . GLN   B 1 72  ? 33.750  23.676 8.403   1.00 39.86  ? 728  GLN   B O   1 
ATOM   3247 C CB  . GLN   B 1 72  ? 33.291  26.051 6.212   1.00 39.25  ? 728  GLN   B CB  1 
ATOM   3248 C CG  . GLN   B 1 72  ? 34.432  26.589 7.104   1.00 53.77  ? 728  GLN   B CG  1 
ATOM   3249 C CD  . GLN   B 1 72  ? 34.523  28.098 7.256   1.00 76.90  ? 728  GLN   B CD  1 
ATOM   3250 O OE1 . GLN   B 1 72  ? 35.462  28.616 7.876   1.00 75.01  ? 728  GLN   B OE1 1 
ATOM   3251 N NE2 . GLN   B 1 72  ? 33.564  28.848 6.718   1.00 70.16  ? 728  GLN   B NE2 1 
ATOM   3252 N N   . ILE   B 1 73  ? 31.560  24.167 8.162   1.00 36.03  ? 729  ILE   B N   1 
ATOM   3253 C CA  . ILE   B 1 73  ? 31.152  23.766 9.519   1.00 35.56  ? 729  ILE   B CA  1 
ATOM   3254 C C   . ILE   B 1 73  ? 31.528  22.281 9.742   1.00 39.04  ? 729  ILE   B C   1 
ATOM   3255 O O   . ILE   B 1 73  ? 32.090  21.931 10.782  1.00 38.58  ? 729  ILE   B O   1 
ATOM   3256 C CB  . ILE   B 1 73  ? 29.648  24.094 9.794   1.00 38.56  ? 729  ILE   B CB  1 
ATOM   3257 C CG1 . ILE   B 1 73  ? 29.376  25.622 9.714   1.00 38.85  ? 729  ILE   B CG1 1 
ATOM   3258 C CG2 . ILE   B 1 73  ? 29.218  23.562 11.151  1.00 37.80  ? 729  ILE   B CG2 1 
ATOM   3259 C CD1 . ILE   B 1 73  ? 27.924  26.046 9.409   1.00 39.51  ? 729  ILE   B CD1 1 
ATOM   3260 N N   . LEU   B 1 74  ? 31.282  21.444 8.720   1.00 34.48  ? 730  LEU   B N   1 
ATOM   3261 C CA  . LEU   B 1 74  ? 31.658  20.029 8.683   1.00 34.36  ? 730  LEU   B CA  1 
ATOM   3262 C C   . LEU   B 1 74  ? 33.195  19.883 8.781   1.00 34.48  ? 730  LEU   B C   1 
ATOM   3263 O O   . LEU   B 1 74  ? 33.662  19.061 9.572   1.00 31.42  ? 730  LEU   B O   1 
ATOM   3264 C CB  . LEU   B 1 74  ? 31.133  19.386 7.383   1.00 34.97  ? 730  LEU   B CB  1 
ATOM   3265 C CG  . LEU   B 1 74  ? 31.608  17.960 7.051   1.00 41.23  ? 730  LEU   B CG  1 
ATOM   3266 C CD1 . LEU   B 1 74  ? 31.260  16.953 8.154   1.00 42.05  ? 730  LEU   B CD1 1 
ATOM   3267 C CD2 . LEU   B 1 74  ? 31.063  17.530 5.707   1.00 44.74  ? 730  LEU   B CD2 1 
ATOM   3268 N N   . ASP   B 1 75  ? 33.970  20.688 8.004   1.00 31.89  ? 731  ASP   B N   1 
ATOM   3269 C CA  . ASP   B 1 75  ? 35.447  20.683 8.077   1.00 32.63  ? 731  ASP   B CA  1 
ATOM   3270 C C   . ASP   B 1 75  ? 35.901  21.053 9.504   1.00 34.37  ? 731  ASP   B C   1 
ATOM   3271 O O   . ASP   B 1 75  ? 36.704  20.333 10.094  1.00 33.27  ? 731  ASP   B O   1 
ATOM   3272 C CB  . ASP   B 1 75  ? 36.072  21.677 7.074   1.00 35.46  ? 731  ASP   B CB  1 
ATOM   3273 C CG  . ASP   B 1 75  ? 36.375  21.140 5.693   1.00 57.16  ? 731  ASP   B CG  1 
ATOM   3274 O OD1 . ASP   B 1 75  ? 36.881  19.993 5.596   1.00 61.19  ? 731  ASP   B OD1 1 
ATOM   3275 O OD2 . ASP   B 1 75  ? 36.144  21.884 4.702   1.00 64.12  ? 731  ASP   B OD2 1 
ATOM   3276 N N   . LEU   B 1 76  ? 35.353  22.160 10.057  1.00 30.15  ? 732  LEU   B N   1 
ATOM   3277 C CA  . LEU   B 1 76  ? 35.661  22.668 11.404  1.00 30.29  ? 732  LEU   B CA  1 
ATOM   3278 C C   . LEU   B 1 76  ? 35.309  21.664 12.507  1.00 32.72  ? 732  LEU   B C   1 
ATOM   3279 O O   . LEU   B 1 76  ? 36.061  21.535 13.472  1.00 31.77  ? 732  LEU   B O   1 
ATOM   3280 C CB  . LEU   B 1 76  ? 34.965  24.015 11.667  1.00 30.23  ? 732  LEU   B CB  1 
ATOM   3281 C CG  . LEU   B 1 76  ? 35.520  25.237 10.933  1.00 34.26  ? 732  LEU   B CG  1 
ATOM   3282 C CD1 . LEU   B 1 76  ? 34.468  26.339 10.863  1.00 34.54  ? 732  LEU   B CD1 1 
ATOM   3283 C CD2 . LEU   B 1 76  ? 36.809  25.743 11.578  1.00 35.43  ? 732  LEU   B CD2 1 
ATOM   3284 N N   . SER   B 1 77  ? 34.196  20.925 12.328  1.00 28.21  ? 733  SER   B N   1 
ATOM   3285 C CA  . SER   B 1 77  ? 33.719  19.891 13.249  1.00 27.94  ? 733  SER   B CA  1 
ATOM   3286 C C   . SER   B 1 77  ? 34.770  18.757 13.382  1.00 30.47  ? 733  SER   B C   1 
ATOM   3287 O O   . SER   B 1 77  ? 35.055  18.325 14.506  1.00 30.23  ? 733  SER   B O   1 
ATOM   3288 C CB  . SER   B 1 77  ? 32.388  19.327 12.760  1.00 31.48  ? 733  SER   B CB  1 
ATOM   3289 O OG  . SER   B 1 77  ? 31.786  18.515 13.752  1.00 42.89  ? 733  SER   B OG  1 
ATOM   3290 N N   . ASN   B 1 78  ? 35.350  18.300 12.240  1.00 26.32  ? 734  ASN   B N   1 
ATOM   3291 C CA  . ASN   B 1 78  ? 36.399  17.263 12.189  1.00 26.03  ? 734  ASN   B CA  1 
ATOM   3292 C C   . ASN   B 1 78  ? 37.707  17.750 12.867  1.00 28.17  ? 734  ASN   B C   1 
ATOM   3293 O O   . ASN   B 1 78  ? 38.394  16.969 13.522  1.00 28.53  ? 734  ASN   B O   1 
ATOM   3294 C CB  . ASN   B 1 78  ? 36.694  16.851 10.736  1.00 28.87  ? 734  ASN   B CB  1 
ATOM   3295 C CG  . ASN   B 1 78  ? 35.692  15.959 10.030  1.00 59.66  ? 734  ASN   B CG  1 
ATOM   3296 O OD1 . ASN   B 1 78  ? 34.776  15.367 10.619  1.00 56.64  ? 734  ASN   B OD1 1 
ATOM   3297 N ND2 . ASN   B 1 78  ? 35.868  15.829 8.724   1.00 54.17  ? 734  ASN   B ND2 1 
ATOM   3298 N N   . ARG   B 1 79  ? 38.039  19.036 12.697  1.00 23.90  ? 735  ARG   B N   1 
ATOM   3299 C CA  . ARG   B 1 79  ? 39.227  19.668 13.292  1.00 23.57  ? 735  ARG   B CA  1 
ATOM   3300 C C   . ARG   B 1 79  ? 39.098  19.703 14.815  1.00 26.36  ? 735  ARG   B C   1 
ATOM   3301 O O   . ARG   B 1 79  ? 40.060  19.385 15.504  1.00 25.00  ? 735  ARG   B O   1 
ATOM   3302 C CB  . ARG   B 1 79  ? 39.457  21.078 12.729  1.00 21.92  ? 735  ARG   B CB  1 
ATOM   3303 C CG  . ARG   B 1 79  ? 39.882  21.066 11.273  1.00 34.53  ? 735  ARG   B CG  1 
ATOM   3304 C CD  . ARG   B 1 79  ? 40.306  22.449 10.885  1.00 46.36  ? 735  ARG   B CD  1 
ATOM   3305 N NE  . ARG   B 1 79  ? 40.149  22.725 9.462   1.00 49.45  ? 735  ARG   B NE  1 
ATOM   3306 C CZ  . ARG   B 1 79  ? 40.263  23.939 8.936   1.00 66.39  ? 735  ARG   B CZ  1 
ATOM   3307 N NH1 . ARG   B 1 79  ? 40.539  24.985 9.711   1.00 53.28  ? 735  ARG   B NH1 1 
ATOM   3308 N NH2 . ARG   B 1 79  ? 40.105  24.120 7.633   1.00 58.46  ? 735  ARG   B NH2 1 
ATOM   3309 N N   . PHE   B 1 80  ? 37.887  20.009 15.340  1.00 22.35  ? 736  PHE   B N   1 
ATOM   3310 C CA  . PHE   B 1 80  ? 37.655  19.967 16.779  1.00 20.73  ? 736  PHE   B CA  1 
ATOM   3311 C C   . PHE   B 1 80  ? 38.061  18.594 17.359  1.00 24.84  ? 736  PHE   B C   1 
ATOM   3312 O O   . PHE   B 1 80  ? 38.863  18.548 18.293  1.00 23.78  ? 736  PHE   B O   1 
ATOM   3313 C CB  . PHE   B 1 80  ? 36.189  20.280 17.117  1.00 21.75  ? 736  PHE   B CB  1 
ATOM   3314 C CG  . PHE   B 1 80  ? 35.950  20.437 18.604  1.00 22.78  ? 736  PHE   B CG  1 
ATOM   3315 C CD1 . PHE   B 1 80  ? 36.171  21.654 19.236  1.00 25.54  ? 736  PHE   B CD1 1 
ATOM   3316 C CD2 . PHE   B 1 80  ? 35.588  19.346 19.388  1.00 23.17  ? 736  PHE   B CD2 1 
ATOM   3317 C CE1 . PHE   B 1 80  ? 35.981  21.790 20.624  1.00 25.31  ? 736  PHE   B CE1 1 
ATOM   3318 C CE2 . PHE   B 1 80  ? 35.444  19.476 20.772  1.00 24.90  ? 736  PHE   B CE2 1 
ATOM   3319 C CZ  . PHE   B 1 80  ? 35.597  20.705 21.373  1.00 22.52  ? 736  PHE   B CZ  1 
ATOM   3320 N N   . TYR   B 1 81  ? 37.540  17.487 16.770  1.00 23.87  ? 737  TYR   B N   1 
ATOM   3321 C CA  . TYR   B 1 81  ? 37.783  16.100 17.184  1.00 24.52  ? 737  TYR   B CA  1 
ATOM   3322 C C   . TYR   B 1 81  ? 39.214  15.593 16.916  1.00 30.82  ? 737  TYR   B C   1 
ATOM   3323 O O   . TYR   B 1 81  ? 39.568  14.518 17.407  1.00 30.73  ? 737  TYR   B O   1 
ATOM   3324 C CB  . TYR   B 1 81  ? 36.731  15.153 16.579  1.00 26.39  ? 737  TYR   B CB  1 
ATOM   3325 C CG  . TYR   B 1 81  ? 35.333  15.412 17.110  1.00 27.96  ? 737  TYR   B CG  1 
ATOM   3326 C CD1 . TYR   B 1 81  ? 35.044  15.276 18.462  1.00 29.51  ? 737  TYR   B CD1 1 
ATOM   3327 C CD2 . TYR   B 1 81  ? 34.298  15.794 16.255  1.00 28.75  ? 737  TYR   B CD2 1 
ATOM   3328 C CE1 . TYR   B 1 81  ? 33.781  15.565 18.966  1.00 30.77  ? 737  TYR   B CE1 1 
ATOM   3329 C CE2 . TYR   B 1 81  ? 33.016  16.053 16.744  1.00 29.48  ? 737  TYR   B CE2 1 
ATOM   3330 C CZ  . TYR   B 1 81  ? 32.761  15.920 18.101  1.00 37.01  ? 737  TYR   B CZ  1 
ATOM   3331 O OH  . TYR   B 1 81  ? 31.521  16.171 18.630  1.00 37.91  ? 737  TYR   B OH  1 
ATOM   3332 N N   . THR   B 1 82  ? 40.025  16.355 16.151  1.00 28.15  ? 738  THR   B N   1 
ATOM   3333 C CA  . THR   B 1 82  ? 41.431  16.062 15.904  1.00 27.77  ? 738  THR   B CA  1 
ATOM   3334 C C   . THR   B 1 82  ? 42.196  16.789 17.007  1.00 36.40  ? 738  THR   B C   1 
ATOM   3335 O O   . THR   B 1 82  ? 43.130  16.224 17.586  1.00 38.18  ? 738  THR   B O   1 
ATOM   3336 C CB  . THR   B 1 82  ? 41.891  16.608 14.546  1.00 30.70  ? 738  THR   B CB  1 
ATOM   3337 O OG1 . THR   B 1 82  ? 41.009  16.178 13.511  1.00 33.97  ? 738  THR   B OG1 1 
ATOM   3338 C CG2 . THR   B 1 82  ? 43.340  16.225 14.218  1.00 22.03  ? 738  THR   B CG2 1 
ATOM   3339 N N   . LEU   B 1 83  ? 41.810  18.062 17.269  1.00 33.82  ? 739  LEU   B N   1 
ATOM   3340 C CA  . LEU   B 1 83  ? 42.374  18.952 18.286  1.00 33.75  ? 739  LEU   B CA  1 
ATOM   3341 C C   . LEU   B 1 83  ? 42.221  18.264 19.646  1.00 36.88  ? 739  LEU   B C   1 
ATOM   3342 O O   . LEU   B 1 83  ? 43.195  18.117 20.378  1.00 37.30  ? 739  LEU   B O   1 
ATOM   3343 C CB  . LEU   B 1 83  ? 41.599  20.302 18.244  1.00 34.19  ? 739  LEU   B CB  1 
ATOM   3344 C CG  . LEU   B 1 83  ? 42.327  21.650 18.445  1.00 38.96  ? 739  LEU   B CG  1 
ATOM   3345 C CD1 . LEU   B 1 83  ? 42.483  21.990 19.909  1.00 38.98  ? 739  LEU   B CD1 1 
ATOM   3346 C CD2 . LEU   B 1 83  ? 43.641  21.757 17.628  1.00 40.03  ? 739  LEU   B CD2 1 
ATOM   3347 N N   . ILE   B 1 84  ? 41.017  17.775 19.939  1.00 33.19  ? 740  ILE   B N   1 
ATOM   3348 C CA  . ILE   B 1 84  ? 40.723  17.039 21.168  1.00 33.31  ? 740  ILE   B CA  1 
ATOM   3349 C C   . ILE   B 1 84  ? 40.394  15.625 20.688  1.00 38.70  ? 740  ILE   B C   1 
ATOM   3350 O O   . ILE   B 1 84  ? 39.297  15.428 20.159  1.00 37.33  ? 740  ILE   B O   1 
ATOM   3351 C CB  . ILE   B 1 84  ? 39.549  17.667 21.982  1.00 35.68  ? 740  ILE   B CB  1 
ATOM   3352 C CG1 . ILE   B 1 84  ? 39.632  19.233 22.064  1.00 34.02  ? 740  ILE   B CG1 1 
ATOM   3353 C CG2 . ILE   B 1 84  ? 39.416  17.005 23.378  1.00 37.04  ? 740  ILE   B CG2 1 
ATOM   3354 C CD1 . ILE   B 1 84  ? 40.864  19.895 22.740  1.00 25.77  ? 740  ILE   B CD1 1 
ATOM   3355 N N   . PRO   B 1 85  ? 41.342  14.655 20.761  1.00 37.69  ? 741  PRO   B N   1 
ATOM   3356 C CA  . PRO   B 1 85  ? 41.041  13.306 20.243  1.00 38.34  ? 741  PRO   B CA  1 
ATOM   3357 C C   . PRO   B 1 85  ? 39.985  12.593 21.060  1.00 44.58  ? 741  PRO   B C   1 
ATOM   3358 O O   . PRO   B 1 85  ? 40.044  12.593 22.282  1.00 43.45  ? 741  PRO   B O   1 
ATOM   3359 C CB  . PRO   B 1 85  ? 42.388  12.578 20.233  1.00 40.08  ? 741  PRO   B CB  1 
ATOM   3360 C CG  . PRO   B 1 85  ? 43.299  13.392 21.054  1.00 44.66  ? 741  PRO   B CG  1 
ATOM   3361 C CD  . PRO   B 1 85  ? 42.698  14.740 21.336  1.00 39.69  ? 741  PRO   B CD  1 
ATOM   3362 N N   . HIS   B 1 86  ? 38.967  12.085 20.377  1.00 43.95  ? 742  HIS   B N   1 
ATOM   3363 C CA  . HIS   B 1 86  ? 37.861  11.398 21.015  1.00 45.28  ? 742  HIS   B CA  1 
ATOM   3364 C C   . HIS   B 1 86  ? 37.853  9.908  20.651  1.00 52.32  ? 742  HIS   B C   1 
ATOM   3365 O O   . HIS   B 1 86  ? 38.542  9.499  19.715  1.00 50.76  ? 742  HIS   B O   1 
ATOM   3366 C CB  . HIS   B 1 86  ? 36.537  12.072 20.636  1.00 46.22  ? 742  HIS   B CB  1 
ATOM   3367 C CG  . HIS   B 1 86  ? 36.201  13.310 21.424  1.00 49.95  ? 742  HIS   B CG  1 
ATOM   3368 N ND1 . HIS   B 1 86  ? 36.932  14.482 21.286  1.00 51.73  ? 742  HIS   B ND1 1 
ATOM   3369 C CD2 . HIS   B 1 86  ? 35.177  13.540 22.282  1.00 51.64  ? 742  HIS   B CD2 1 
ATOM   3370 C CE1 . HIS   B 1 86  ? 36.345  15.371 22.076  1.00 51.04  ? 742  HIS   B CE1 1 
ATOM   3371 N NE2 . HIS   B 1 86  ? 35.280  14.856 22.687  1.00 51.26  ? 742  HIS   B NE2 1 
ATOM   3372 N N   . ASP   B 1 87  ? 37.109  9.100  21.430  1.00 52.78  ? 743  ASP   B N   1 
ATOM   3373 C CA  . ASP   B 1 87  ? 36.923  7.662  21.221  1.00 54.41  ? 743  ASP   B CA  1 
ATOM   3374 C C   . ASP   B 1 87  ? 35.466  7.291  21.524  1.00 61.71  ? 743  ASP   B C   1 
ATOM   3375 O O   . ASP   B 1 87  ? 35.106  6.973  22.667  1.00 61.84  ? 743  ASP   B O   1 
ATOM   3376 C CB  . ASP   B 1 87  ? 37.927  6.797  22.026  1.00 56.31  ? 743  ASP   B CB  1 
ATOM   3377 C CG  . ASP   B 1 87  ? 37.972  5.310  21.644  1.00 63.19  ? 743  ASP   B CG  1 
ATOM   3378 O OD1 . ASP   B 1 87  ? 37.399  4.940  20.586  1.00 62.34  ? 743  ASP   B OD1 1 
ATOM   3379 O OD2 . ASP   B 1 87  ? 38.593  4.521  22.395  1.00 66.49  ? 743  ASP   B OD2 1 
ATOM   3380 N N   . PHE   B 1 88  ? 34.632  7.368  20.471  1.00 59.54  ? 744  PHE   B N   1 
ATOM   3381 C CA  . PHE   B 1 88  ? 33.205  7.068  20.486  1.00 59.83  ? 744  PHE   B CA  1 
ATOM   3382 C C   . PHE   B 1 88  ? 32.928  5.614  20.095  1.00 64.80  ? 744  PHE   B C   1 
ATOM   3383 O O   . PHE   B 1 88  ? 31.763  5.235  19.952  1.00 64.20  ? 744  PHE   B O   1 
ATOM   3384 C CB  . PHE   B 1 88  ? 32.468  8.033  19.535  1.00 61.70  ? 744  PHE   B CB  1 
ATOM   3385 C CG  . PHE   B 1 88  ? 32.365  9.439  20.066  1.00 63.47  ? 744  PHE   B CG  1 
ATOM   3386 C CD1 . PHE   B 1 88  ? 33.363  10.371 19.813  1.00 66.39  ? 744  PHE   B CD1 1 
ATOM   3387 C CD2 . PHE   B 1 88  ? 31.281  9.828  20.843  1.00 66.10  ? 744  PHE   B CD2 1 
ATOM   3388 C CE1 . PHE   B 1 88  ? 33.270  11.670 20.318  1.00 67.33  ? 744  PHE   B CE1 1 
ATOM   3389 C CE2 . PHE   B 1 88  ? 31.200  11.124 21.362  1.00 68.80  ? 744  PHE   B CE2 1 
ATOM   3390 C CZ  . PHE   B 1 88  ? 32.198  12.035 21.098  1.00 66.68  ? 744  PHE   B CZ  1 
ATOM   3391 N N   . GLY   B 1 89  ? 33.990  4.817  19.950  1.00 62.79  ? 745  GLY   B N   1 
ATOM   3392 C CA  . GLY   B 1 89  ? 33.879  3.425  19.537  1.00 63.59  ? 745  GLY   B CA  1 
ATOM   3393 C C   . GLY   B 1 89  ? 33.403  3.330  18.100  1.00 69.68  ? 745  GLY   B C   1 
ATOM   3394 O O   . GLY   B 1 89  ? 34.033  3.900  17.209  1.00 69.41  ? 745  GLY   B O   1 
ATOM   3395 N N   . MET   B 1 90  ? 32.258  2.665  17.874  1.00 67.54  ? 746  MET   B N   1 
ATOM   3396 C CA  . MET   B 1 90  ? 31.661  2.483  16.540  1.00 67.68  ? 746  MET   B CA  1 
ATOM   3397 C C   . MET   B 1 90  ? 30.642  3.568  16.200  1.00 72.41  ? 746  MET   B C   1 
ATOM   3398 O O   . MET   B 1 90  ? 30.036  3.515  15.125  1.00 72.24  ? 746  MET   B O   1 
ATOM   3399 C CB  . MET   B 1 90  ? 30.980  1.102  16.429  1.00 70.07  ? 746  MET   B CB  1 
ATOM   3400 C CG  . MET   B 1 90  ? 31.828  -0.046 16.847  1.00 73.76  ? 746  MET   B CG  1 
ATOM   3401 S SD  . MET   B 1 90  ? 33.268  -0.221 15.804  1.00 77.80  ? 746  MET   B SD  1 
ATOM   3402 C CE  . MET   B 1 90  ? 34.124  -1.420 16.746  1.00 74.47  ? 746  MET   B CE  1 
ATOM   3403 N N   . LYS   B 1 91  ? 30.429  4.524  17.129  1.00 69.53  ? 747  LYS   B N   1 
ATOM   3404 C CA  . LYS   B 1 91  ? 29.471  5.621  16.990  1.00 69.66  ? 747  LYS   B CA  1 
ATOM   3405 C C   . LYS   B 1 91  ? 30.136  6.815  16.314  1.00 72.91  ? 747  LYS   B C   1 
ATOM   3406 O O   . LYS   B 1 91  ? 31.310  7.096  16.575  1.00 73.28  ? 747  LYS   B O   1 
ATOM   3407 C CB  . LYS   B 1 91  ? 28.951  6.079  18.379  1.00 72.55  ? 747  LYS   B CB  1 
ATOM   3408 C CG  . LYS   B 1 91  ? 28.377  4.985  19.280  1.00 90.37  ? 747  LYS   B CG  1 
ATOM   3409 C CD  . LYS   B 1 91  ? 27.896  5.544  20.620  1.00 100.52 ? 747  LYS   B CD  1 
ATOM   3410 C CE  . LYS   B 1 91  ? 28.870  5.381  21.772  1.00 106.67 ? 747  LYS   B CE  1 
ATOM   3411 N NZ  . LYS   B 1 91  ? 29.935  6.417  21.754  1.00 112.05 ? 747  LYS   B NZ  1 
ATOM   3412 N N   . LYS   B 1 92  ? 29.383  7.545  15.474  1.00 67.24  ? 748  LYS   B N   1 
ATOM   3413 C CA  . LYS   B 1 92  ? 29.894  8.776  14.878  1.00 65.92  ? 748  LYS   B CA  1 
ATOM   3414 C C   . LYS   B 1 92  ? 29.851  9.855  15.988  1.00 66.39  ? 748  LYS   B C   1 
ATOM   3415 O O   . LYS   B 1 92  ? 28.866  9.889  16.730  1.00 66.73  ? 748  LYS   B O   1 
ATOM   3416 C CB  . LYS   B 1 92  ? 29.021  9.223  13.689  1.00 68.90  ? 748  LYS   B CB  1 
ATOM   3417 C CG  . LYS   B 1 92  ? 29.232  8.436  12.404  1.00 84.34  ? 748  LYS   B CG  1 
ATOM   3418 C CD  . LYS   B 1 92  ? 28.641  9.182  11.223  1.00 93.24  ? 748  LYS   B CD  1 
ATOM   3419 C CE  . LYS   B 1 92  ? 28.637  8.358  9.968   1.00 105.43 ? 748  LYS   B CE  1 
ATOM   3420 N NZ  . LYS   B 1 92  ? 28.458  9.209  8.760   1.00 114.76 ? 748  LYS   B NZ  1 
ATOM   3421 N N   . PRO   B 1 93  ? 30.885  10.719 16.147  1.00 59.26  ? 749  PRO   B N   1 
ATOM   3422 C CA  . PRO   B 1 93  ? 30.827  11.781 17.174  1.00 57.47  ? 749  PRO   B CA  1 
ATOM   3423 C C   . PRO   B 1 93  ? 29.750  12.826 16.862  1.00 58.66  ? 749  PRO   B C   1 
ATOM   3424 O O   . PRO   B 1 93  ? 29.430  12.996 15.688  1.00 58.15  ? 749  PRO   B O   1 
ATOM   3425 C CB  . PRO   B 1 93  ? 32.201  12.447 17.078  1.00 59.20  ? 749  PRO   B CB  1 
ATOM   3426 C CG  . PRO   B 1 93  ? 33.045  11.535 16.306  1.00 64.45  ? 749  PRO   B CG  1 
ATOM   3427 C CD  . PRO   B 1 93  ? 32.136  10.801 15.382  1.00 60.54  ? 749  PRO   B CD  1 
ATOM   3428 N N   . PRO   B 1 94  ? 29.173  13.545 17.853  1.00 54.16  ? 750  PRO   B N   1 
ATOM   3429 C CA  . PRO   B 1 94  ? 28.131  14.536 17.514  1.00 53.08  ? 750  PRO   B CA  1 
ATOM   3430 C C   . PRO   B 1 94  ? 28.651  15.631 16.588  1.00 54.08  ? 750  PRO   B C   1 
ATOM   3431 O O   . PRO   B 1 94  ? 29.650  16.278 16.894  1.00 53.15  ? 750  PRO   B O   1 
ATOM   3432 C CB  . PRO   B 1 94  ? 27.666  15.068 18.878  1.00 55.16  ? 750  PRO   B CB  1 
ATOM   3433 C CG  . PRO   B 1 94  ? 28.783  14.750 19.822  1.00 60.04  ? 750  PRO   B CG  1 
ATOM   3434 C CD  . PRO   B 1 94  ? 29.418  13.493 19.310  1.00 55.76  ? 750  PRO   B CD  1 
ATOM   3435 N N   . LEU   B 1 95  ? 28.030  15.751 15.403  1.00 48.20  ? 751  LEU   B N   1 
ATOM   3436 C CA  . LEU   B 1 95  ? 28.394  16.743 14.398  1.00 46.43  ? 751  LEU   B CA  1 
ATOM   3437 C C   . LEU   B 1 95  ? 28.092  18.134 14.949  1.00 47.15  ? 751  LEU   B C   1 
ATOM   3438 O O   . LEU   B 1 95  ? 26.969  18.391 15.390  1.00 47.50  ? 751  LEU   B O   1 
ATOM   3439 C CB  . LEU   B 1 95  ? 27.657  16.445 13.074  1.00 46.04  ? 751  LEU   B CB  1 
ATOM   3440 C CG  . LEU   B 1 95  ? 27.924  17.316 11.842  1.00 49.97  ? 751  LEU   B CG  1 
ATOM   3441 C CD1 . LEU   B 1 95  ? 29.400  17.384 11.501  1.00 49.93  ? 751  LEU   B CD1 1 
ATOM   3442 C CD2 . LEU   B 1 95  ? 27.156  16.789 10.642  1.00 50.75  ? 751  LEU   B CD2 1 
ATOM   3443 N N   . LEU   B 1 96  ? 29.123  18.992 14.999  1.00 41.21  ? 752  LEU   B N   1 
ATOM   3444 C CA  . LEU   B 1 96  ? 29.058  20.354 15.548  1.00 40.84  ? 752  LEU   B CA  1 
ATOM   3445 C C   . LEU   B 1 96  ? 28.601  21.386 14.516  1.00 46.47  ? 752  LEU   B C   1 
ATOM   3446 O O   . LEU   B 1 96  ? 29.391  22.216 14.073  1.00 46.66  ? 752  LEU   B O   1 
ATOM   3447 C CB  . LEU   B 1 96  ? 30.406  20.771 16.211  1.00 40.26  ? 752  LEU   B CB  1 
ATOM   3448 C CG  . LEU   B 1 96  ? 31.126  19.742 17.091  1.00 43.69  ? 752  LEU   B CG  1 
ATOM   3449 C CD1 . LEU   B 1 96  ? 32.462  20.268 17.537  1.00 44.10  ? 752  LEU   B CD1 1 
ATOM   3450 C CD2 . LEU   B 1 96  ? 30.292  19.341 18.288  1.00 44.38  ? 752  LEU   B CD2 1 
ATOM   3451 N N   . ASN   B 1 97  ? 27.326  21.307 14.120  1.00 44.64  ? 753  ASN   B N   1 
ATOM   3452 C CA  . ASN   B 1 97  ? 26.676  22.211 13.168  1.00 44.60  ? 753  ASN   B CA  1 
ATOM   3453 C C   . ASN   B 1 97  ? 25.586  23.040 13.871  1.00 49.30  ? 753  ASN   B C   1 
ATOM   3454 O O   . ASN   B 1 97  ? 25.399  24.219 13.555  1.00 49.56  ? 753  ASN   B O   1 
ATOM   3455 C CB  . ASN   B 1 97  ? 26.124  21.440 11.954  1.00 43.69  ? 753  ASN   B CB  1 
ATOM   3456 C CG  . ASN   B 1 97  ? 25.125  20.349 12.265  1.00 58.56  ? 753  ASN   B CG  1 
ATOM   3457 O OD1 . ASN   B 1 97  ? 24.857  20.015 13.422  1.00 61.59  ? 753  ASN   B OD1 1 
ATOM   3458 N ND2 . ASN   B 1 97  ? 24.561  19.750 11.226  1.00 43.47  ? 753  ASN   B ND2 1 
ATOM   3459 N N   . ASN   B 1 98  ? 24.899  22.422 14.849  1.00 45.09  ? 754  ASN   B N   1 
ATOM   3460 C CA  . ASN   B 1 98  ? 23.867  23.066 15.662  1.00 44.42  ? 754  ASN   B CA  1 
ATOM   3461 C C   . ASN   B 1 98  ? 24.452  23.799 16.899  1.00 45.89  ? 754  ASN   B C   1 
ATOM   3462 O O   . ASN   B 1 98  ? 25.600  23.561 17.298  1.00 44.41  ? 754  ASN   B O   1 
ATOM   3463 C CB  . ASN   B 1 98  ? 22.779  22.068 16.056  1.00 45.37  ? 754  ASN   B CB  1 
ATOM   3464 C CG  . ASN   B 1 98  ? 23.248  20.857 16.821  1.00 68.53  ? 754  ASN   B CG  1 
ATOM   3465 O OD1 . ASN   B 1 98  ? 23.104  20.790 18.035  1.00 70.40  ? 754  ASN   B OD1 1 
ATOM   3466 N ND2 . ASN   B 1 98  ? 23.790  19.861 16.135  1.00 60.40  ? 754  ASN   B ND2 1 
ATOM   3467 N N   . ALA   B 1 99  ? 23.657  24.712 17.474  1.00 40.91  ? 755  ALA   B N   1 
ATOM   3468 C CA  . ALA   B 1 99  ? 24.049  25.497 18.638  1.00 39.96  ? 755  ALA   B CA  1 
ATOM   3469 C C   . ALA   B 1 99  ? 24.132  24.647 19.893  1.00 43.80  ? 755  ALA   B C   1 
ATOM   3470 O O   . ALA   B 1 99  ? 24.974  24.940 20.738  1.00 43.65  ? 755  ALA   B O   1 
ATOM   3471 C CB  . ALA   B 1 99  ? 23.090  26.651 18.850  1.00 40.50  ? 755  ALA   B CB  1 
ATOM   3472 N N   . ASP   B 1 100 ? 23.276  23.597 20.016  1.00 39.18  ? 756  ASP   B N   1 
ATOM   3473 C CA  . ASP   B 1 100 ? 23.275  22.691 21.168  1.00 38.01  ? 756  ASP   B CA  1 
ATOM   3474 C C   . ASP   B 1 100 ? 24.606  21.955 21.299  1.00 39.51  ? 756  ASP   B C   1 
ATOM   3475 O O   . ASP   B 1 100 ? 25.124  21.809 22.408  1.00 39.06  ? 756  ASP   B O   1 
ATOM   3476 C CB  . ASP   B 1 100 ? 22.121  21.694 21.098  1.00 39.71  ? 756  ASP   B CB  1 
ATOM   3477 C CG  . ASP   B 1 100 ? 20.758  22.273 21.432  1.00 55.12  ? 756  ASP   B CG  1 
ATOM   3478 O OD1 . ASP   B 1 100 ? 20.655  23.022 22.450  1.00 55.48  ? 756  ASP   B OD1 1 
ATOM   3479 O OD2 . ASP   B 1 100 ? 19.786  21.962 20.699  1.00 60.05  ? 756  ASP   B OD2 1 
ATOM   3480 N N   . SER   B 1 101 ? 25.144  21.486 20.160  1.00 34.47  ? 757  SER   B N   1 
ATOM   3481 C CA  . SER   B 1 101 ? 26.429  20.796 20.070  1.00 33.26  ? 757  SER   B CA  1 
ATOM   3482 C C   . SER   B 1 101 ? 27.586  21.724 20.445  1.00 33.02  ? 757  SER   B C   1 
ATOM   3483 O O   . SER   B 1 101 ? 28.478  21.301 21.179  1.00 31.95  ? 757  SER   B O   1 
ATOM   3484 C CB  . SER   B 1 101 ? 26.630  20.214 18.674  1.00 37.53  ? 757  SER   B CB  1 
ATOM   3485 O OG  . SER   B 1 101 ? 26.126  18.888 18.637  1.00 50.71  ? 757  SER   B OG  1 
ATOM   3486 N N   . VAL   B 1 102 ? 27.559  22.982 19.966  1.00 28.00  ? 758  VAL   B N   1 
ATOM   3487 C CA  . VAL   B 1 102 ? 28.603  23.978 20.243  1.00 27.55  ? 758  VAL   B CA  1 
ATOM   3488 C C   . VAL   B 1 102 ? 28.521  24.389 21.734  1.00 30.96  ? 758  VAL   B C   1 
ATOM   3489 O O   . VAL   B 1 102 ? 29.563  24.535 22.393  1.00 30.36  ? 758  VAL   B O   1 
ATOM   3490 C CB  . VAL   B 1 102 ? 28.541  25.170 19.233  1.00 31.18  ? 758  VAL   B CB  1 
ATOM   3491 C CG1 . VAL   B 1 102 ? 29.325  26.397 19.708  1.00 31.22  ? 758  VAL   B CG1 1 
ATOM   3492 C CG2 . VAL   B 1 102 ? 29.034  24.735 17.866  1.00 30.78  ? 758  VAL   B CG2 1 
ATOM   3493 N N   . GLN   B 1 103 ? 27.275  24.508 22.263  1.00 25.56  ? 759  GLN   B N   1 
ATOM   3494 C CA  . GLN   B 1 103 ? 27.023  24.853 23.659  1.00 24.62  ? 759  GLN   B CA  1 
ATOM   3495 C C   . GLN   B 1 103 ? 27.558  23.772 24.582  1.00 26.20  ? 759  GLN   B C   1 
ATOM   3496 O O   . GLN   B 1 103 ? 28.246  24.106 25.534  1.00 26.28  ? 759  GLN   B O   1 
ATOM   3497 C CB  . GLN   B 1 103 ? 25.540  25.125 23.903  1.00 26.83  ? 759  GLN   B CB  1 
ATOM   3498 C CG  . GLN   B 1 103 ? 25.145  26.535 23.478  1.00 48.68  ? 759  GLN   B CG  1 
ATOM   3499 C CD  . GLN   B 1 103 ? 23.696  26.910 23.650  1.00 70.15  ? 759  GLN   B CD  1 
ATOM   3500 O OE1 . GLN   B 1 103 ? 23.249  27.940 23.127  1.00 64.51  ? 759  GLN   B OE1 1 
ATOM   3501 N NE2 . GLN   B 1 103 ? 22.930  26.111 24.389  1.00 63.82  ? 759  GLN   B NE2 1 
ATOM   3502 N N   . ALA   B 1 104 ? 27.289  22.484 24.274  1.00 22.45  ? 760  ALA   B N   1 
ATOM   3503 C CA  . ALA   B 1 104 ? 27.788  21.321 25.010  1.00 22.60  ? 760  ALA   B CA  1 
ATOM   3504 C C   . ALA   B 1 104 ? 29.334  21.282 24.977  1.00 25.56  ? 760  ALA   B C   1 
ATOM   3505 O O   . ALA   B 1 104 ? 29.939  21.003 26.005  1.00 26.53  ? 760  ALA   B O   1 
ATOM   3506 C CB  . ALA   B 1 104 ? 27.228  20.031 24.417  1.00 23.26  ? 760  ALA   B CB  1 
ATOM   3507 N N   . LYS   B 1 105 ? 29.967  21.548 23.805  1.00 21.27  ? 761  LYS   B N   1 
ATOM   3508 C CA  . LYS   B 1 105 ? 31.440  21.525 23.666  1.00 19.15  ? 761  LYS   B CA  1 
ATOM   3509 C C   . LYS   B 1 105 ? 32.100  22.702 24.365  1.00 22.07  ? 761  LYS   B C   1 
ATOM   3510 O O   . LYS   B 1 105 ? 33.165  22.517 24.938  1.00 22.60  ? 761  LYS   B O   1 
ATOM   3511 C CB  . LYS   B 1 105 ? 31.897  21.387 22.202  1.00 18.38  ? 761  LYS   B CB  1 
ATOM   3512 C CG  . LYS   B 1 105 ? 31.506  20.062 21.553  1.00 29.76  ? 761  LYS   B CG  1 
ATOM   3513 C CD  . LYS   B 1 105 ? 32.217  18.846 22.121  1.00 39.26  ? 761  LYS   B CD  1 
ATOM   3514 C CE  . LYS   B 1 105 ? 31.638  17.545 21.618  1.00 44.74  ? 761  LYS   B CE  1 
ATOM   3515 N NZ  . LYS   B 1 105 ? 31.340  16.631 22.745  1.00 57.97  ? 761  LYS   B NZ  1 
ATOM   3516 N N   . ALA   B 1 106 ? 31.454  23.888 24.373  1.00 18.98  ? 762  ALA   B N   1 
ATOM   3517 C CA  . ALA   B 1 106 ? 31.929  25.053 25.115  1.00 19.60  ? 762  ALA   B CA  1 
ATOM   3518 C C   . ALA   B 1 106 ? 31.941  24.737 26.644  1.00 25.01  ? 762  ALA   B C   1 
ATOM   3519 O O   . ALA   B 1 106 ? 32.945  25.008 27.299  1.00 22.47  ? 762  ALA   B O   1 
ATOM   3520 C CB  . ALA   B 1 106 ? 31.050  26.257 24.826  1.00 20.21  ? 762  ALA   B CB  1 
ATOM   3521 N N   . GLU   B 1 107 ? 30.857  24.111 27.182  1.00 24.68  ? 763  GLU   B N   1 
ATOM   3522 C CA  . GLU   B 1 107 ? 30.743  23.678 28.590  1.00 25.28  ? 763  GLU   B CA  1 
ATOM   3523 C C   . GLU   B 1 107 ? 31.904  22.702 28.913  1.00 27.06  ? 763  GLU   B C   1 
ATOM   3524 O O   . GLU   B 1 107 ? 32.583  22.860 29.941  1.00 25.27  ? 763  GLU   B O   1 
ATOM   3525 C CB  . GLU   B 1 107 ? 29.419  22.921 28.821  1.00 27.43  ? 763  GLU   B CB  1 
ATOM   3526 C CG  . GLU   B 1 107 ? 28.185  23.741 29.163  1.00 43.03  ? 763  GLU   B CG  1 
ATOM   3527 C CD  . GLU   B 1 107 ? 26.899  22.926 29.168  1.00 67.43  ? 763  GLU   B CD  1 
ATOM   3528 O OE1 . GLU   B 1 107 ? 26.858  21.878 29.855  1.00 49.55  ? 763  GLU   B OE1 1 
ATOM   3529 O OE2 . GLU   B 1 107 ? 25.933  23.334 28.480  1.00 67.59  ? 763  GLU   B OE2 1 
ATOM   3530 N N   . MET   B 1 108 ? 32.109  21.688 28.034  1.00 22.29  ? 764  MET   B N   1 
ATOM   3531 C CA  . MET   B 1 108 ? 33.175  20.692 28.179  1.00 22.03  ? 764  MET   B CA  1 
ATOM   3532 C C   . MET   B 1 108 ? 34.542  21.374 28.330  1.00 24.82  ? 764  MET   B C   1 
ATOM   3533 O O   . MET   B 1 108 ? 35.322  20.985 29.208  1.00 24.85  ? 764  MET   B O   1 
ATOM   3534 C CB  . MET   B 1 108 ? 33.199  19.722 26.985  1.00 25.00  ? 764  MET   B CB  1 
ATOM   3535 C CG  . MET   B 1 108 ? 34.370  18.732 27.048  1.00 31.10  ? 764  MET   B CG  1 
ATOM   3536 S SD  . MET   B 1 108 ? 34.854  17.967 25.489  1.00 37.34  ? 764  MET   B SD  1 
ATOM   3537 C CE  . MET   B 1 108 ? 35.774  19.258 24.759  1.00 33.37  ? 764  MET   B CE  1 
ATOM   3538 N N   . LEU   B 1 109 ? 34.820  22.394 27.471  1.00 20.02  ? 765  LEU   B N   1 
ATOM   3539 C CA  . LEU   B 1 109 ? 36.067  23.142 27.470  1.00 18.84  ? 765  LEU   B CA  1 
ATOM   3540 C C   . LEU   B 1 109 ? 36.252  23.938 28.747  1.00 22.21  ? 765  LEU   B C   1 
ATOM   3541 O O   . LEU   B 1 109 ? 37.333  23.899 29.301  1.00 22.44  ? 765  LEU   B O   1 
ATOM   3542 C CB  . LEU   B 1 109 ? 36.227  24.015 26.209  1.00 18.31  ? 765  LEU   B CB  1 
ATOM   3543 C CG  . LEU   B 1 109 ? 36.410  23.279 24.871  1.00 21.30  ? 765  LEU   B CG  1 
ATOM   3544 C CD1 . LEU   B 1 109 ? 36.435  24.258 23.711  1.00 18.78  ? 765  LEU   B CD1 1 
ATOM   3545 C CD2 . LEU   B 1 109 ? 37.662  22.372 24.866  1.00 23.75  ? 765  LEU   B CD2 1 
ATOM   3546 N N   . ASP   B 1 110 ? 35.189  24.616 29.233  1.00 18.02  ? 766  ASP   B N   1 
ATOM   3547 C CA  . ASP   B 1 110 ? 35.146  25.368 30.495  1.00 17.74  ? 766  ASP   B CA  1 
ATOM   3548 C C   . ASP   B 1 110 ? 35.593  24.466 31.649  1.00 19.75  ? 766  ASP   B C   1 
ATOM   3549 O O   . ASP   B 1 110 ? 36.425  24.876 32.449  1.00 16.76  ? 766  ASP   B O   1 
ATOM   3550 C CB  . ASP   B 1 110 ? 33.702  25.825 30.798  1.00 19.02  ? 766  ASP   B CB  1 
ATOM   3551 C CG  . ASP   B 1 110 ? 33.161  27.022 30.021  1.00 22.62  ? 766  ASP   B CG  1 
ATOM   3552 O OD1 . ASP   B 1 110 ? 33.810  27.449 29.042  1.00 20.08  ? 766  ASP   B OD1 1 
ATOM   3553 O OD2 . ASP   B 1 110 ? 32.090  27.526 30.392  1.00 28.26  ? 766  ASP   B OD2 1 
ATOM   3554 N N   . ASN   B 1 111 ? 35.044  23.230 31.710  1.00 16.25  ? 767  ASN   B N   1 
ATOM   3555 C CA  . ASN   B 1 111 ? 35.386  22.212 32.703  1.00 17.19  ? 767  ASN   B CA  1 
ATOM   3556 C C   . ASN   B 1 111 ? 36.857  21.786 32.593  1.00 22.88  ? 767  ASN   B C   1 
ATOM   3557 O O   . ASN   B 1 111 ? 37.534  21.712 33.618  1.00 23.51  ? 767  ASN   B O   1 
ATOM   3558 C CB  . ASN   B 1 111 ? 34.458  20.990 32.569  1.00 18.68  ? 767  ASN   B CB  1 
ATOM   3559 C CG  . ASN   B 1 111 ? 33.093  21.267 33.121  1.00 27.69  ? 767  ASN   B CG  1 
ATOM   3560 O OD1 . ASN   B 1 111 ? 32.952  21.730 34.244  1.00 26.08  ? 767  ASN   B OD1 1 
ATOM   3561 N ND2 . ASN   B 1 111 ? 32.057  21.005 32.340  1.00 19.36  ? 767  ASN   B ND2 1 
ATOM   3562 N N   . LEU   B 1 112 ? 37.347  21.568 31.344  1.00 17.96  ? 768  LEU   B N   1 
ATOM   3563 C CA  . LEU   B 1 112 ? 38.738  21.181 31.066  1.00 17.43  ? 768  LEU   B CA  1 
ATOM   3564 C C   . LEU   B 1 112 ? 39.699  22.272 31.535  1.00 20.57  ? 768  LEU   B C   1 
ATOM   3565 O O   . LEU   B 1 112 ? 40.783  21.947 31.975  1.00 20.95  ? 768  LEU   B O   1 
ATOM   3566 C CB  . LEU   B 1 112 ? 38.973  20.846 29.576  1.00 17.19  ? 768  LEU   B CB  1 
ATOM   3567 C CG  . LEU   B 1 112 ? 38.371  19.558 29.012  1.00 21.70  ? 768  LEU   B CG  1 
ATOM   3568 C CD1 . LEU   B 1 112 ? 38.736  19.377 27.544  1.00 20.10  ? 768  LEU   B CD1 1 
ATOM   3569 C CD2 . LEU   B 1 112 ? 38.835  18.307 29.798  1.00 26.76  ? 768  LEU   B CD2 1 
ATOM   3570 N N   . LEU   B 1 113 ? 39.263  23.532 31.554  1.00 18.43  ? 769  LEU   B N   1 
ATOM   3571 C CA  . LEU   B 1 113 ? 40.081  24.634 32.064  1.00 19.61  ? 769  LEU   B CA  1 
ATOM   3572 C C   . LEU   B 1 113 ? 40.359  24.519 33.590  1.00 24.57  ? 769  LEU   B C   1 
ATOM   3573 O O   . LEU   B 1 113 ? 41.502  24.644 34.001  1.00 23.32  ? 769  LEU   B O   1 
ATOM   3574 C CB  . LEU   B 1 113 ? 39.479  25.994 31.697  1.00 19.46  ? 769  LEU   B CB  1 
ATOM   3575 C CG  . LEU   B 1 113 ? 39.690  26.505 30.269  1.00 22.78  ? 769  LEU   B CG  1 
ATOM   3576 C CD1 . LEU   B 1 113 ? 39.103  27.879 30.128  1.00 22.56  ? 769  LEU   B CD1 1 
ATOM   3577 C CD2 . LEU   B 1 113 ? 41.167  26.598 29.912  1.00 24.15  ? 769  LEU   B CD2 1 
ATOM   3578 N N   . ASP   B 1 114 ? 39.328  24.190 34.393  1.00 22.93  ? 770  ASP   B N   1 
ATOM   3579 C CA  . ASP   B 1 114 ? 39.409  23.967 35.844  1.00 22.02  ? 770  ASP   B CA  1 
ATOM   3580 C C   . ASP   B 1 114 ? 40.247  22.741 36.143  1.00 23.93  ? 770  ASP   B C   1 
ATOM   3581 O O   . ASP   B 1 114 ? 41.046  22.783 37.085  1.00 21.82  ? 770  ASP   B O   1 
ATOM   3582 C CB  . ASP   B 1 114 ? 38.002  23.820 36.458  1.00 23.76  ? 770  ASP   B CB  1 
ATOM   3583 C CG  . ASP   B 1 114 ? 37.349  25.121 36.944  1.00 27.64  ? 770  ASP   B CG  1 
ATOM   3584 O OD1 . ASP   B 1 114 ? 38.100  26.078 37.308  1.00 26.19  ? 770  ASP   B OD1 1 
ATOM   3585 O OD2 . ASP   B 1 114 ? 36.085  25.175 36.989  1.00 18.73  ? 770  ASP   B OD2 1 
ATOM   3586 N N   . ILE   B 1 115 ? 40.112  21.667 35.298  1.00 21.33  ? 771  ILE   B N   1 
ATOM   3587 C CA  . ILE   B 1 115 ? 40.877  20.416 35.441  1.00 22.42  ? 771  ILE   B CA  1 
ATOM   3588 C C   . ILE   B 1 115 ? 42.389  20.652 35.220  1.00 27.45  ? 771  ILE   B C   1 
ATOM   3589 O O   . ILE   B 1 115 ? 43.213  20.142 35.985  1.00 28.19  ? 771  ILE   B O   1 
ATOM   3590 C CB  . ILE   B 1 115 ? 40.287  19.282 34.551  1.00 26.76  ? 771  ILE   B CB  1 
ATOM   3591 C CG1 . ILE   B 1 115 ? 38.946  18.754 35.140  1.00 27.31  ? 771  ILE   B CG1 1 
ATOM   3592 C CG2 . ILE   B 1 115 ? 41.295  18.130 34.365  1.00 28.15  ? 771  ILE   B CG2 1 
ATOM   3593 C CD1 . ILE   B 1 115 ? 38.063  17.865 34.167  1.00 31.89  ? 771  ILE   B CD1 1 
ATOM   3594 N N   . GLU   B 1 116 ? 42.739  21.435 34.181  1.00 22.88  ? 772  GLU   B N   1 
ATOM   3595 C CA  . GLU   B 1 116 ? 44.094  21.812 33.827  1.00 22.26  ? 772  GLU   B CA  1 
ATOM   3596 C C   . GLU   B 1 116 ? 44.740  22.634 34.982  1.00 26.14  ? 772  GLU   B C   1 
ATOM   3597 O O   . GLU   B 1 116 ? 45.910  22.429 35.266  1.00 26.28  ? 772  GLU   B O   1 
ATOM   3598 C CB  . GLU   B 1 116 ? 44.076  22.588 32.487  1.00 24.01  ? 772  GLU   B CB  1 
ATOM   3599 C CG  . GLU   B 1 116 ? 45.421  22.784 31.798  1.00 34.72  ? 772  GLU   B CG  1 
ATOM   3600 C CD  . GLU   B 1 116 ? 46.297  23.880 32.379  1.00 45.66  ? 772  GLU   B CD  1 
ATOM   3601 O OE1 . GLU   B 1 116 ? 45.761  24.950 32.759  1.00 41.09  ? 772  GLU   B OE1 1 
ATOM   3602 O OE2 . GLU   B 1 116 ? 47.526  23.659 32.461  1.00 42.59  ? 772  GLU   B OE2 1 
ATOM   3603 N N   . VAL   B 1 117 ? 43.983  23.524 35.653  1.00 22.58  ? 773  VAL   B N   1 
ATOM   3604 C CA  . VAL   B 1 117 ? 44.501  24.310 36.788  1.00 22.44  ? 773  VAL   B CA  1 
ATOM   3605 C C   . VAL   B 1 117 ? 44.826  23.385 37.971  1.00 26.56  ? 773  VAL   B C   1 
ATOM   3606 O O   . VAL   B 1 117 ? 45.893  23.540 38.582  1.00 28.18  ? 773  VAL   B O   1 
ATOM   3607 C CB  . VAL   B 1 117 ? 43.541  25.459 37.209  1.00 26.37  ? 773  VAL   B CB  1 
ATOM   3608 C CG1 . VAL   B 1 117 ? 43.935  26.059 38.583  1.00 27.22  ? 773  VAL   B CG1 1 
ATOM   3609 C CG2 . VAL   B 1 117 ? 43.481  26.533 36.128  1.00 25.45  ? 773  VAL   B CG2 1 
ATOM   3610 N N   . ALA   B 1 118 ? 43.924  22.420 38.272  1.00 21.89  ? 774  ALA   B N   1 
ATOM   3611 C CA  . ALA   B 1 118 ? 44.060  21.408 39.323  1.00 22.33  ? 774  ALA   B CA  1 
ATOM   3612 C C   . ALA   B 1 118 ? 45.323  20.586 39.132  1.00 28.87  ? 774  ALA   B C   1 
ATOM   3613 O O   . ALA   B 1 118 ? 46.090  20.415 40.085  1.00 28.69  ? 774  ALA   B O   1 
ATOM   3614 C CB  . ALA   B 1 118 ? 42.856  20.483 39.305  1.00 23.27  ? 774  ALA   B CB  1 
ATOM   3615 N N   . TYR   B 1 119 ? 45.534  20.060 37.897  1.00 27.18  ? 775  TYR   B N   1 
ATOM   3616 C CA  . TYR   B 1 119 ? 46.689  19.228 37.573  1.00 27.39  ? 775  TYR   B CA  1 
ATOM   3617 C C   . TYR   B 1 119 ? 48.001  20.024 37.591  1.00 29.66  ? 775  TYR   B C   1 
ATOM   3618 O O   . TYR   B 1 119 ? 49.008  19.517 38.065  1.00 27.39  ? 775  TYR   B O   1 
ATOM   3619 C CB  . TYR   B 1 119 ? 46.474  18.451 36.250  1.00 28.94  ? 775  TYR   B CB  1 
ATOM   3620 C CG  . TYR   B 1 119 ? 47.418  17.264 36.131  1.00 30.80  ? 775  TYR   B CG  1 
ATOM   3621 C CD1 . TYR   B 1 119 ? 47.219  16.113 36.888  1.00 32.60  ? 775  TYR   B CD1 1 
ATOM   3622 C CD2 . TYR   B 1 119 ? 48.536  17.313 35.294  1.00 31.60  ? 775  TYR   B CD2 1 
ATOM   3623 C CE1 . TYR   B 1 119 ? 48.101  15.038 36.817  1.00 32.20  ? 775  TYR   B CE1 1 
ATOM   3624 C CE2 . TYR   B 1 119 ? 49.412  16.232 35.197  1.00 32.65  ? 775  TYR   B CE2 1 
ATOM   3625 C CZ  . TYR   B 1 119 ? 49.193  15.099 35.965  1.00 41.07  ? 775  TYR   B CZ  1 
ATOM   3626 O OH  . TYR   B 1 119 ? 50.035  14.019 35.872  1.00 42.51  ? 775  TYR   B OH  1 
ATOM   3627 N N   . SER   B 1 120 ? 47.955  21.291 37.140  1.00 27.33  ? 776  SER   B N   1 
ATOM   3628 C CA  . SER   B 1 120 ? 49.077  22.244 37.127  1.00 26.37  ? 776  SER   B CA  1 
ATOM   3629 C C   . SER   B 1 120 ? 49.540  22.568 38.565  1.00 29.85  ? 776  SER   B C   1 
ATOM   3630 O O   . SER   B 1 120 ? 50.742  22.604 38.831  1.00 28.85  ? 776  SER   B O   1 
ATOM   3631 C CB  . SER   B 1 120 ? 48.646  23.511 36.381  1.00 32.09  ? 776  SER   B CB  1 
ATOM   3632 O OG  . SER   B 1 120 ? 49.573  24.581 36.448  1.00 47.55  ? 776  SER   B OG  1 
ATOM   3633 N N   . LEU   B 1 121 ? 48.587  22.764 39.482  1.00 27.61  ? 777  LEU   B N   1 
ATOM   3634 C CA  . LEU   B 1 121 ? 48.775  23.046 40.903  1.00 29.25  ? 777  LEU   B CA  1 
ATOM   3635 C C   . LEU   B 1 121 ? 49.487  21.871 41.599  1.00 35.38  ? 777  LEU   B C   1 
ATOM   3636 O O   . LEU   B 1 121 ? 50.556  22.053 42.215  1.00 35.43  ? 777  LEU   B O   1 
ATOM   3637 C CB  . LEU   B 1 121 ? 47.388  23.290 41.531  1.00 30.63  ? 777  LEU   B CB  1 
ATOM   3638 C CG  . LEU   B 1 121 ? 47.226  24.398 42.569  1.00 36.54  ? 777  LEU   B CG  1 
ATOM   3639 C CD1 . LEU   B 1 121 ? 47.955  25.706 42.160  1.00 36.75  ? 777  LEU   B CD1 1 
ATOM   3640 C CD2 . LEU   B 1 121 ? 45.769  24.633 42.846  1.00 38.54  ? 777  LEU   B CD2 1 
ATOM   3641 N N   . LEU   B 1 122 ? 48.951  20.662 41.396  1.00 33.08  ? 778  LEU   B N   1 
ATOM   3642 C CA  . LEU   B 1 122 ? 49.479  19.404 41.909  1.00 34.05  ? 778  LEU   B CA  1 
ATOM   3643 C C   . LEU   B 1 122 ? 50.913  19.097 41.384  1.00 39.40  ? 778  LEU   B C   1 
ATOM   3644 O O   . LEU   B 1 122 ? 51.763  18.673 42.165  1.00 40.62  ? 778  LEU   B O   1 
ATOM   3645 C CB  . LEU   B 1 122 ? 48.474  18.303 41.515  1.00 34.20  ? 778  LEU   B CB  1 
ATOM   3646 C CG  . LEU   B 1 122 ? 48.384  17.047 42.379  1.00 39.54  ? 778  LEU   B CG  1 
ATOM   3647 C CD1 . LEU   B 1 122 ? 47.979  17.354 43.791  1.00 39.71  ? 778  LEU   B CD1 1 
ATOM   3648 C CD2 . LEU   B 1 122 ? 47.360  16.116 41.824  1.00 42.27  ? 778  LEU   B CD2 1 
ATOM   3649 N N   . ARG   B 1 123 ? 51.180  19.335 40.085  1.00 37.24  ? 779  ARG   B N   1 
ATOM   3650 C CA  . ARG   B 1 123 ? 52.483  19.059 39.462  1.00 39.01  ? 779  ARG   B CA  1 
ATOM   3651 C C   . ARG   B 1 123 ? 53.495  20.228 39.595  1.00 42.10  ? 779  ARG   B C   1 
ATOM   3652 O O   . ARG   B 1 123 ? 54.691  20.036 39.397  1.00 42.53  ? 779  ARG   B O   1 
ATOM   3653 C CB  . ARG   B 1 123 ? 52.298  18.594 37.987  1.00 41.79  ? 779  ARG   B CB  1 
ATOM   3654 C CG  . ARG   B 1 123 ? 51.776  17.144 37.840  1.00 53.30  ? 779  ARG   B CG  1 
ATOM   3655 C CD  . ARG   B 1 123 ? 52.614  16.119 38.611  1.00 70.04  ? 779  ARG   B CD  1 
ATOM   3656 N NE  . ARG   B 1 123 ? 52.049  14.760 38.619  1.00 83.19  ? 779  ARG   B NE  1 
ATOM   3657 C CZ  . ARG   B 1 123 ? 51.101  14.338 39.453  1.00 93.87  ? 779  ARG   B CZ  1 
ATOM   3658 N NH1 . ARG   B 1 123 ? 50.677  13.086 39.407  1.00 82.43  ? 779  ARG   B NH1 1 
ATOM   3659 N NH2 . ARG   B 1 123 ? 50.578  15.167 40.350  1.00 76.00  ? 779  ARG   B NH2 1 
ATOM   3660 N N   . GLY   B 1 124 ? 53.010  21.398 39.979  1.00 38.35  ? 780  GLY   B N   1 
ATOM   3661 C CA  . GLY   B 1 124 ? 53.839  22.570 40.186  1.00 37.30  ? 780  GLY   B CA  1 
ATOM   3662 C C   . GLY   B 1 124 ? 54.178  22.720 41.652  1.00 41.93  ? 780  GLY   B C   1 
ATOM   3663 O O   . GLY   B 1 124 ? 53.885  21.833 42.465  1.00 40.23  ? 780  GLY   B O   1 
ATOM   3664 N N   . GLY   B 1 125 ? 54.767  23.870 41.971  1.00 40.26  ? 781  GLY   B N   1 
ATOM   3665 C CA  . GLY   B 1 125 ? 55.162  24.279 43.317  1.00 39.99  ? 781  GLY   B CA  1 
ATOM   3666 C C   . GLY   B 1 125 ? 56.409  23.615 43.862  1.00 42.58  ? 781  GLY   B C   1 
ATOM   3667 O O   . GLY   B 1 125 ? 57.281  23.191 43.103  1.00 39.42  ? 781  GLY   B O   1 
ATOM   3668 N N   . SER   B 1 126 ? 56.486  23.529 45.205  1.00 41.41  ? 782  SER   B N   1 
ATOM   3669 C CA  . SER   B 1 126 ? 57.561  22.888 45.974  1.00 41.59  ? 782  SER   B CA  1 
ATOM   3670 C C   . SER   B 1 126 ? 57.139  21.568 46.599  1.00 45.76  ? 782  SER   B C   1 
ATOM   3671 O O   . SER   B 1 126 ? 56.019  21.437 47.089  1.00 44.60  ? 782  SER   B O   1 
ATOM   3672 C CB  . SER   B 1 126 ? 58.102  23.808 47.060  1.00 45.05  ? 782  SER   B CB  1 
ATOM   3673 O OG  . SER   B 1 126 ? 58.461  25.068 46.524  1.00 53.86  ? 782  SER   B OG  1 
ATOM   3674 N N   . ASP   B 1 127 ? 58.059  20.603 46.579  1.00 45.22  ? 783  ASP   B N   1 
ATOM   3675 C CA  . ASP   B 1 127 ? 57.876  19.252 47.077  1.00 46.54  ? 783  ASP   B CA  1 
ATOM   3676 C C   . ASP   B 1 127 ? 58.677  19.013 48.358  1.00 49.94  ? 783  ASP   B C   1 
ATOM   3677 O O   . ASP   B 1 127 ? 59.887  19.260 48.406  1.00 49.74  ? 783  ASP   B O   1 
ATOM   3678 C CB  . ASP   B 1 127 ? 58.255  18.235 45.982  1.00 49.41  ? 783  ASP   B CB  1 
ATOM   3679 C CG  . ASP   B 1 127 ? 57.618  16.874 46.181  1.00 64.13  ? 783  ASP   B CG  1 
ATOM   3680 O OD1 . ASP   B 1 127 ? 56.349  16.798 46.202  1.00 63.53  ? 783  ASP   B OD1 1 
ATOM   3681 O OD2 . ASP   B 1 127 ? 58.377  15.883 46.335  1.00 69.96  ? 783  ASP   B OD2 1 
ATOM   3682 N N   . ASP   B 1 128 ? 57.988  18.521 49.391  1.00 46.45  ? 784  ASP   B N   1 
ATOM   3683 C CA  . ASP   B 1 128 ? 58.562  18.242 50.697  1.00 46.57  ? 784  ASP   B CA  1 
ATOM   3684 C C   . ASP   B 1 128 ? 58.026  16.900 51.223  1.00 51.29  ? 784  ASP   B C   1 
ATOM   3685 O O   . ASP   B 1 128 ? 56.853  16.800 51.574  1.00 50.59  ? 784  ASP   B O   1 
ATOM   3686 C CB  . ASP   B 1 128 ? 58.226  19.418 51.637  1.00 48.08  ? 784  ASP   B CB  1 
ATOM   3687 C CG  . ASP   B 1 128 ? 58.854  19.433 53.018  1.00 48.12  ? 784  ASP   B CG  1 
ATOM   3688 O OD1 . ASP   B 1 128 ? 59.589  18.477 53.354  1.00 47.07  ? 784  ASP   B OD1 1 
ATOM   3689 O OD2 . ASP   B 1 128 ? 58.606  20.400 53.766  1.00 52.95  ? 784  ASP   B OD2 1 
ATOM   3690 N N   . SER   B 1 129 ? 58.897  15.870 51.252  1.00 48.90  ? 785  SER   B N   1 
ATOM   3691 C CA  . SER   B 1 129 ? 58.572  14.513 51.702  1.00 49.21  ? 785  SER   B CA  1 
ATOM   3692 C C   . SER   B 1 129 ? 58.124  14.477 53.149  1.00 52.25  ? 785  SER   B C   1 
ATOM   3693 O O   . SER   B 1 129 ? 57.173  13.751 53.467  1.00 53.82  ? 785  SER   B O   1 
ATOM   3694 C CB  . SER   B 1 129 ? 59.770  13.587 51.534  1.00 55.85  ? 785  SER   B CB  1 
ATOM   3695 O OG  . SER   B 1 129 ? 60.215  13.539 50.189  1.00 73.89  ? 785  SER   B OG  1 
ATOM   3696 N N   . SER   B 1 130 ? 58.785  15.278 54.020  1.00 45.78  ? 786  SER   B N   1 
ATOM   3697 C CA  . SER   B 1 130 ? 58.519  15.377 55.462  1.00 44.94  ? 786  SER   B CA  1 
ATOM   3698 C C   . SER   B 1 130 ? 57.092  15.820 55.805  1.00 48.24  ? 786  SER   B C   1 
ATOM   3699 O O   . SER   B 1 130 ? 56.636  15.578 56.929  1.00 49.49  ? 786  SER   B O   1 
ATOM   3700 C CB  . SER   B 1 130 ? 59.535  16.300 56.129  1.00 48.50  ? 786  SER   B CB  1 
ATOM   3701 O OG  . SER   B 1 130 ? 59.249  17.671 55.896  1.00 53.16  ? 786  SER   B OG  1 
ATOM   3702 N N   . LYS   B 1 131 ? 56.395  16.465 54.844  1.00 42.63  ? 787  LYS   B N   1 
ATOM   3703 C CA  . LYS   B 1 131 ? 55.037  16.952 55.039  1.00 41.72  ? 787  LYS   B CA  1 
ATOM   3704 C C   . LYS   B 1 131 ? 53.973  16.018 54.444  1.00 42.94  ? 787  LYS   B C   1 
ATOM   3705 O O   . LYS   B 1 131 ? 54.164  15.445 53.365  1.00 42.76  ? 787  LYS   B O   1 
ATOM   3706 C CB  . LYS   B 1 131 ? 54.889  18.385 54.488  1.00 44.87  ? 787  LYS   B CB  1 
ATOM   3707 C CG  . LYS   B 1 131 ? 55.704  19.431 55.235  1.00 60.97  ? 787  LYS   B CG  1 
ATOM   3708 C CD  . LYS   B 1 131 ? 55.319  20.848 54.825  1.00 75.43  ? 787  LYS   B CD  1 
ATOM   3709 C CE  . LYS   B 1 131 ? 55.924  21.877 55.753  1.00 95.07  ? 787  LYS   B CE  1 
ATOM   3710 N NZ  . LYS   B 1 131 ? 55.583  23.269 55.341  1.00 108.35 ? 787  LYS   B NZ  1 
ATOM   3711 N N   . ASP   B 1 132 ? 52.838  15.889 55.170  1.00 37.26  ? 788  ASP   B N   1 
ATOM   3712 C CA  . ASP   B 1 132 ? 51.652  15.149 54.758  1.00 35.15  ? 788  ASP   B CA  1 
ATOM   3713 C C   . ASP   B 1 132 ? 51.139  15.779 53.434  1.00 38.93  ? 788  ASP   B C   1 
ATOM   3714 O O   . ASP   B 1 132 ? 50.936  16.995 53.396  1.00 38.02  ? 788  ASP   B O   1 
ATOM   3715 C CB  . ASP   B 1 132 ? 50.565  15.284 55.847  1.00 35.85  ? 788  ASP   B CB  1 
ATOM   3716 C CG  . ASP   B 1 132 ? 49.303  14.435 55.699  1.00 35.91  ? 788  ASP   B CG  1 
ATOM   3717 O OD1 . ASP   B 1 132 ? 48.799  14.296 54.557  1.00 34.07  ? 788  ASP   B OD1 1 
ATOM   3718 O OD2 . ASP   B 1 132 ? 48.795  13.940 56.732  1.00 37.03  ? 788  ASP   B OD2 1 
ATOM   3719 N N   . PRO   B 1 133 ? 50.924  14.986 52.352  1.00 35.77  ? 789  PRO   B N   1 
ATOM   3720 C CA  . PRO   B 1 133 ? 50.441  15.563 51.080  1.00 35.46  ? 789  PRO   B CA  1 
ATOM   3721 C C   . PRO   B 1 133 ? 49.109  16.323 51.162  1.00 38.31  ? 789  PRO   B C   1 
ATOM   3722 O O   . PRO   B 1 133 ? 48.866  17.178 50.327  1.00 38.36  ? 789  PRO   B O   1 
ATOM   3723 C CB  . PRO   B 1 133 ? 50.363  14.357 50.142  1.00 37.08  ? 789  PRO   B CB  1 
ATOM   3724 C CG  . PRO   B 1 133 ? 51.326  13.370 50.734  1.00 42.48  ? 789  PRO   B CG  1 
ATOM   3725 C CD  . PRO   B 1 133 ? 51.152  13.536 52.215  1.00 38.04  ? 789  PRO   B CD  1 
ATOM   3726 N N   . ILE   B 1 134 ? 48.280  16.047 52.183  1.00 33.70  ? 790  ILE   B N   1 
ATOM   3727 C CA  . ILE   B 1 134 ? 47.018  16.758 52.451  1.00 32.11  ? 790  ILE   B CA  1 
ATOM   3728 C C   . ILE   B 1 134 ? 47.346  18.212 52.875  1.00 34.81  ? 790  ILE   B C   1 
ATOM   3729 O O   . ILE   B 1 134 ? 46.723  19.157 52.373  1.00 33.87  ? 790  ILE   B O   1 
ATOM   3730 C CB  . ILE   B 1 134 ? 46.154  15.998 53.499  1.00 33.91  ? 790  ILE   B CB  1 
ATOM   3731 C CG1 . ILE   B 1 134 ? 45.726  14.622 52.942  1.00 33.80  ? 790  ILE   B CG1 1 
ATOM   3732 C CG2 . ILE   B 1 134 ? 44.923  16.836 53.925  1.00 33.36  ? 790  ILE   B CG2 1 
ATOM   3733 C CD1 . ILE   B 1 134 ? 45.341  13.566 53.977  1.00 41.75  ? 790  ILE   B CD1 1 
ATOM   3734 N N   . ASP   B 1 135 ? 48.357  18.374 53.771  1.00 30.55  ? 791  ASP   B N   1 
ATOM   3735 C CA  . ASP   B 1 135 ? 48.843  19.669 54.231  1.00 29.64  ? 791  ASP   B CA  1 
ATOM   3736 C C   . ASP   B 1 135 ? 49.442  20.459 53.048  1.00 32.24  ? 791  ASP   B C   1 
ATOM   3737 O O   . ASP   B 1 135 ? 49.116  21.634 52.867  1.00 30.93  ? 791  ASP   B O   1 
ATOM   3738 C CB  . ASP   B 1 135 ? 49.867  19.500 55.364  1.00 31.76  ? 791  ASP   B CB  1 
ATOM   3739 C CG  . ASP   B 1 135 ? 49.276  19.304 56.753  1.00 38.30  ? 791  ASP   B CG  1 
ATOM   3740 O OD1 . ASP   B 1 135 ? 48.096  19.635 56.947  1.00 33.41  ? 791  ASP   B OD1 1 
ATOM   3741 O OD2 . ASP   B 1 135 ? 50.017  18.849 57.658  1.00 49.73  ? 791  ASP   B OD2 1 
ATOM   3742 N N   . VAL   B 1 136 ? 50.270  19.784 52.216  1.00 29.90  ? 792  VAL   B N   1 
ATOM   3743 C CA  . VAL   B 1 136 ? 50.919  20.342 51.024  1.00 29.05  ? 792  VAL   B CA  1 
ATOM   3744 C C   . VAL   B 1 136 ? 49.826  20.832 50.072  1.00 30.67  ? 792  VAL   B C   1 
ATOM   3745 O O   . VAL   B 1 136 ? 49.800  22.011 49.744  1.00 30.04  ? 792  VAL   B O   1 
ATOM   3746 C CB  . VAL   B 1 136 ? 51.843  19.296 50.336  1.00 33.44  ? 792  VAL   B CB  1 
ATOM   3747 C CG1 . VAL   B 1 136 ? 52.380  19.794 48.991  1.00 33.15  ? 792  VAL   B CG1 1 
ATOM   3748 C CG2 . VAL   B 1 136 ? 52.984  18.875 51.253  1.00 33.06  ? 792  VAL   B CG2 1 
ATOM   3749 N N   . ASN   B 1 137 ? 48.897  19.950 49.682  1.00 26.90  ? 793  ASN   B N   1 
ATOM   3750 C CA  . ASN   B 1 137 ? 47.829  20.289 48.753  1.00 26.47  ? 793  ASN   B CA  1 
ATOM   3751 C C   . ASN   B 1 137 ? 46.842  21.326 49.309  1.00 31.48  ? 793  ASN   B C   1 
ATOM   3752 O O   . ASN   B 1 137 ? 46.271  22.063 48.521  1.00 30.57  ? 793  ASN   B O   1 
ATOM   3753 C CB  . ASN   B 1 137 ? 47.120  19.035 48.241  1.00 28.74  ? 793  ASN   B CB  1 
ATOM   3754 C CG  . ASN   B 1 137 ? 47.989  18.154 47.371  1.00 43.25  ? 793  ASN   B CG  1 
ATOM   3755 O OD1 . ASN   B 1 137 ? 48.990  18.581 46.784  1.00 24.70  ? 793  ASN   B OD1 1 
ATOM   3756 N ND2 . ASN   B 1 137 ? 47.618  16.892 47.259  1.00 37.60  ? 793  ASN   B ND2 1 
ATOM   3757 N N   . TYR   B 1 138 ? 46.666  21.419 50.643  1.00 29.22  ? 794  TYR   B N   1 
ATOM   3758 C CA  . TYR   B 1 138 ? 45.784  22.431 51.235  1.00 29.69  ? 794  TYR   B CA  1 
ATOM   3759 C C   . TYR   B 1 138 ? 46.368  23.848 51.011  1.00 33.68  ? 794  TYR   B C   1 
ATOM   3760 O O   . TYR   B 1 138 ? 45.629  24.762 50.642  1.00 33.22  ? 794  TYR   B O   1 
ATOM   3761 C CB  . TYR   B 1 138 ? 45.537  22.149 52.742  1.00 31.32  ? 794  TYR   B CB  1 
ATOM   3762 C CG  . TYR   B 1 138 ? 44.792  23.239 53.485  1.00 34.34  ? 794  TYR   B CG  1 
ATOM   3763 C CD1 . TYR   B 1 138 ? 43.404  23.318 53.440  1.00 37.07  ? 794  TYR   B CD1 1 
ATOM   3764 C CD2 . TYR   B 1 138 ? 45.471  24.162 54.274  1.00 36.08  ? 794  TYR   B CD2 1 
ATOM   3765 C CE1 . TYR   B 1 138 ? 42.711  24.315 54.128  1.00 39.05  ? 794  TYR   B CE1 1 
ATOM   3766 C CE2 . TYR   B 1 138 ? 44.790  25.168 54.963  1.00 37.28  ? 794  TYR   B CE2 1 
ATOM   3767 C CZ  . TYR   B 1 138 ? 43.408  25.239 54.888  1.00 44.64  ? 794  TYR   B CZ  1 
ATOM   3768 O OH  . TYR   B 1 138 ? 42.719  26.226 55.558  1.00 47.35  ? 794  TYR   B OH  1 
ATOM   3769 N N   . GLU   B 1 139 ? 47.690  24.013 51.223  1.00 30.87  ? 795  GLU   B N   1 
ATOM   3770 C CA  . GLU   B 1 139 ? 48.381  25.298 51.079  1.00 31.04  ? 795  GLU   B CA  1 
ATOM   3771 C C   . GLU   B 1 139 ? 48.394  25.783 49.641  1.00 34.44  ? 795  GLU   B C   1 
ATOM   3772 O O   . GLU   B 1 139 ? 48.385  26.988 49.409  1.00 34.42  ? 795  GLU   B O   1 
ATOM   3773 C CB  . GLU   B 1 139 ? 49.808  25.262 51.661  1.00 33.06  ? 795  GLU   B CB  1 
ATOM   3774 C CG  . GLU   B 1 139 ? 49.949  24.745 53.093  1.00 45.27  ? 795  GLU   B CG  1 
ATOM   3775 C CD  . GLU   B 1 139 ? 50.123  25.702 54.262  1.00 84.66  ? 795  GLU   B CD  1 
ATOM   3776 O OE1 . GLU   B 1 139 ? 51.242  25.764 54.824  1.00 84.12  ? 795  GLU   B OE1 1 
ATOM   3777 O OE2 . GLU   B 1 139 ? 49.128  26.367 54.633  1.00 91.72  ? 795  GLU   B OE2 1 
ATOM   3778 N N   . LYS   B 1 140 ? 48.378  24.828 48.678  1.00 30.31  ? 796  LYS   B N   1 
ATOM   3779 C CA  . LYS   B 1 140 ? 48.307  25.055 47.230  1.00 29.59  ? 796  LYS   B CA  1 
ATOM   3780 C C   . LYS   B 1 140 ? 47.106  25.942 46.846  1.00 34.14  ? 796  LYS   B C   1 
ATOM   3781 O O   . LYS   B 1 140 ? 47.196  26.720 45.896  1.00 35.19  ? 796  LYS   B O   1 
ATOM   3782 C CB  . LYS   B 1 140 ? 48.167  23.711 46.481  1.00 29.94  ? 796  LYS   B CB  1 
ATOM   3783 C CG  . LYS   B 1 140 ? 49.483  23.091 46.086  1.00 35.55  ? 796  LYS   B CG  1 
ATOM   3784 C CD  . LYS   B 1 140 ? 49.314  21.757 45.370  1.00 37.44  ? 796  LYS   B CD  1 
ATOM   3785 C CE  . LYS   B 1 140 ? 50.576  20.922 45.536  1.00 44.04  ? 796  LYS   B CE  1 
ATOM   3786 N NZ  . LYS   B 1 140 ? 51.747  21.398 44.737  1.00 28.04  ? 796  LYS   B NZ  1 
ATOM   3787 N N   . LEU   B 1 141 ? 45.985  25.795 47.569  1.00 29.54  ? 797  LEU   B N   1 
ATOM   3788 C CA  . LEU   B 1 141 ? 44.704  26.469 47.325  1.00 28.24  ? 797  LEU   B CA  1 
ATOM   3789 C C   . LEU   B 1 141 ? 44.635  27.930 47.707  1.00 34.88  ? 797  LEU   B C   1 
ATOM   3790 O O   . LEU   B 1 141 ? 43.746  28.627 47.199  1.00 35.19  ? 797  LEU   B O   1 
ATOM   3791 C CB  . LEU   B 1 141 ? 43.563  25.710 48.029  1.00 27.26  ? 797  LEU   B CB  1 
ATOM   3792 C CG  . LEU   B 1 141 ? 43.336  24.278 47.572  1.00 29.36  ? 797  LEU   B CG  1 
ATOM   3793 C CD1 . LEU   B 1 141 ? 42.254  23.632 48.384  1.00 30.37  ? 797  LEU   B CD1 1 
ATOM   3794 C CD2 . LEU   B 1 141 ? 43.037  24.212 46.073  1.00 27.55  ? 797  LEU   B CD2 1 
ATOM   3795 N N   . LYS   B 1 142 ? 45.531  28.389 48.618  1.00 32.50  ? 798  LYS   B N   1 
ATOM   3796 C CA  . LYS   B 1 142 ? 45.582  29.764 49.138  1.00 32.11  ? 798  LYS   B CA  1 
ATOM   3797 C C   . LYS   B 1 142 ? 44.169  30.237 49.580  1.00 36.12  ? 798  LYS   B C   1 
ATOM   3798 O O   . LYS   B 1 142 ? 43.735  31.351 49.263  1.00 35.50  ? 798  LYS   B O   1 
ATOM   3799 C CB  . LYS   B 1 142 ? 46.272  30.732 48.133  1.00 34.41  ? 798  LYS   B CB  1 
ATOM   3800 C CG  . LYS   B 1 142 ? 47.648  30.304 47.591  1.00 32.40  ? 798  LYS   B CG  1 
ATOM   3801 C CD  . LYS   B 1 142 ? 48.827  30.402 48.583  1.00 46.46  ? 798  LYS   B CD  1 
ATOM   3802 C CE  . LYS   B 1 142 ? 50.144  29.958 47.979  1.00 56.87  ? 798  LYS   B CE  1 
ATOM   3803 N NZ  . LYS   B 1 142 ? 50.923  29.084 48.909  1.00 59.20  ? 798  LYS   B NZ  1 
ATOM   3804 N N   . THR   B 1 143 ? 43.460  29.330 50.286  1.00 32.67  ? 799  THR   B N   1 
ATOM   3805 C CA  . THR   B 1 143 ? 42.098  29.480 50.817  1.00 33.25  ? 799  THR   B CA  1 
ATOM   3806 C C   . THR   B 1 143 ? 42.083  29.012 52.291  1.00 37.48  ? 799  THR   B C   1 
ATOM   3807 O O   . THR   B 1 143 ? 42.638  27.952 52.615  1.00 37.52  ? 799  THR   B O   1 
ATOM   3808 C CB  . THR   B 1 143 ? 41.070  28.685 49.929  1.00 35.97  ? 799  THR   B CB  1 
ATOM   3809 O OG1 . THR   B 1 143 ? 41.143  29.167 48.595  1.00 41.63  ? 799  THR   B OG1 1 
ATOM   3810 C CG2 . THR   B 1 143 ? 39.607  28.810 50.403  1.00 26.74  ? 799  THR   B CG2 1 
ATOM   3811 N N   . ASP   B 1 144 ? 41.472  29.813 53.176  1.00 32.88  ? 800  ASP   B N   1 
ATOM   3812 C CA  . ASP   B 1 144 ? 41.273  29.423 54.568  1.00 32.80  ? 800  ASP   B CA  1 
ATOM   3813 C C   . ASP   B 1 144 ? 39.960  28.625 54.535  1.00 34.55  ? 800  ASP   B C   1 
ATOM   3814 O O   . ASP   B 1 144 ? 38.947  29.134 54.041  1.00 34.11  ? 800  ASP   B O   1 
ATOM   3815 C CB  . ASP   B 1 144 ? 41.157  30.656 55.494  1.00 35.70  ? 800  ASP   B CB  1 
ATOM   3816 C CG  . ASP   B 1 144 ? 40.817  30.339 56.949  1.00 55.02  ? 800  ASP   B CG  1 
ATOM   3817 O OD1 . ASP   B 1 144 ? 41.569  29.564 57.585  1.00 56.53  ? 800  ASP   B OD1 1 
ATOM   3818 O OD2 . ASP   B 1 144 ? 39.808  30.877 57.454  1.00 67.13  ? 800  ASP   B OD2 1 
ATOM   3819 N N   . ILE   B 1 145 ? 40.012  27.352 54.926  1.00 28.13  ? 801  ILE   B N   1 
ATOM   3820 C CA  . ILE   B 1 145 ? 38.831  26.490 54.931  1.00 25.83  ? 801  ILE   B CA  1 
ATOM   3821 C C   . ILE   B 1 145 ? 38.571  26.086 56.363  1.00 27.97  ? 801  ILE   B C   1 
ATOM   3822 O O   . ILE   B 1 145 ? 39.414  25.443 56.991  1.00 26.73  ? 801  ILE   B O   1 
ATOM   3823 C CB  . ILE   B 1 145 ? 38.967  25.254 53.977  1.00 28.18  ? 801  ILE   B CB  1 
ATOM   3824 C CG1 . ILE   B 1 145 ? 39.331  25.686 52.525  1.00 28.10  ? 801  ILE   B CG1 1 
ATOM   3825 C CG2 . ILE   B 1 145 ? 37.691  24.378 54.001  1.00 26.36  ? 801  ILE   B CG2 1 
ATOM   3826 C CD1 . ILE   B 1 145 ? 39.913  24.573 51.649  1.00 25.05  ? 801  ILE   B CD1 1 
ATOM   3827 N N   . LYS   B 1 146 ? 37.413  26.481 56.890  1.00 26.69  ? 802  LYS   B N   1 
ATOM   3828 C CA  . LYS   B 1 146 ? 37.003  26.138 58.264  1.00 26.82  ? 802  LYS   B CA  1 
ATOM   3829 C C   . LYS   B 1 146 ? 35.677  25.375 58.241  1.00 28.14  ? 802  LYS   B C   1 
ATOM   3830 O O   . LYS   B 1 146 ? 34.899  25.554 57.317  1.00 27.72  ? 802  LYS   B O   1 
ATOM   3831 C CB  . LYS   B 1 146 ? 36.940  27.386 59.163  1.00 30.07  ? 802  LYS   B CB  1 
ATOM   3832 C CG  . LYS   B 1 146 ? 38.331  27.974 59.428  1.00 49.93  ? 802  LYS   B CG  1 
ATOM   3833 C CD  . LYS   B 1 146 ? 38.409  28.867 60.660  1.00 60.52  ? 802  LYS   B CD  1 
ATOM   3834 C CE  . LYS   B 1 146 ? 39.840  29.286 60.924  1.00 67.50  ? 802  LYS   B CE  1 
ATOM   3835 N NZ  . LYS   B 1 146 ? 39.969  30.068 62.181  1.00 76.08  ? 802  LYS   B NZ  1 
ATOM   3836 N N   . VAL   B 1 147 ? 35.458  24.487 59.213  1.00 23.71  ? 803  VAL   B N   1 
ATOM   3837 C CA  . VAL   B 1 147 ? 34.237  23.691 59.326  1.00 22.94  ? 803  VAL   B CA  1 
ATOM   3838 C C   . VAL   B 1 147 ? 33.196  24.511 60.113  1.00 27.86  ? 803  VAL   B C   1 
ATOM   3839 O O   . VAL   B 1 147 ? 33.497  24.999 61.197  1.00 28.28  ? 803  VAL   B O   1 
ATOM   3840 C CB  . VAL   B 1 147 ? 34.487  22.276 59.960  1.00 25.08  ? 803  VAL   B CB  1 
ATOM   3841 C CG1 . VAL   B 1 147 ? 33.244  21.398 59.829  1.00 24.49  ? 803  VAL   B CG1 1 
ATOM   3842 C CG2 . VAL   B 1 147 ? 35.693  21.571 59.337  1.00 24.64  ? 803  VAL   B CG2 1 
ATOM   3843 N N   . VAL   B 1 148 ? 31.994  24.681 59.559  1.00 24.62  ? 804  VAL   B N   1 
ATOM   3844 C CA  . VAL   B 1 148 ? 30.920  25.412 60.243  1.00 25.97  ? 804  VAL   B CA  1 
ATOM   3845 C C   . VAL   B 1 148 ? 30.245  24.479 61.277  1.00 35.51  ? 804  VAL   B C   1 
ATOM   3846 O O   . VAL   B 1 148 ? 29.883  23.345 60.940  1.00 35.81  ? 804  VAL   B O   1 
ATOM   3847 C CB  . VAL   B 1 148 ? 29.914  26.071 59.242  1.00 28.74  ? 804  VAL   B CB  1 
ATOM   3848 C CG1 . VAL   B 1 148 ? 28.652  26.590 59.937  1.00 28.50  ? 804  VAL   B CG1 1 
ATOM   3849 C CG2 . VAL   B 1 148 ? 30.582  27.190 58.450  1.00 27.84  ? 804  VAL   B CG2 1 
ATOM   3850 N N   . ASP   B 1 149 ? 30.108  24.956 62.536  1.00 34.83  ? 805  ASP   B N   1 
ATOM   3851 C CA  . ASP   B 1 149 ? 29.467  24.205 63.617  1.00 36.55  ? 805  ASP   B CA  1 
ATOM   3852 C C   . ASP   B 1 149 ? 28.001  23.950 63.255  1.00 42.54  ? 805  ASP   B C   1 
ATOM   3853 O O   . ASP   B 1 149 ? 27.283  24.896 62.913  1.00 41.67  ? 805  ASP   B O   1 
ATOM   3854 C CB  . ASP   B 1 149 ? 29.598  24.950 64.968  1.00 39.16  ? 805  ASP   B CB  1 
ATOM   3855 C CG  . ASP   B 1 149 ? 29.021  24.218 66.173  1.00 52.23  ? 805  ASP   B CG  1 
ATOM   3856 O OD1 . ASP   B 1 149 ? 29.060  22.965 66.188  1.00 53.95  ? 805  ASP   B OD1 1 
ATOM   3857 O OD2 . ASP   B 1 149 ? 28.540  24.899 67.106  1.00 57.95  ? 805  ASP   B OD2 1 
ATOM   3858 N N   . ARG   B 1 150 ? 27.585  22.674 63.252  1.00 40.77  ? 806  ARG   B N   1 
ATOM   3859 C CA  . ARG   B 1 150 ? 26.219  22.260 62.893  1.00 41.65  ? 806  ARG   B CA  1 
ATOM   3860 C C   . ARG   B 1 150 ? 25.100  23.016 63.629  1.00 47.71  ? 806  ARG   B C   1 
ATOM   3861 O O   . ARG   B 1 150 ? 24.080  23.323 63.018  1.00 47.82  ? 806  ARG   B O   1 
ATOM   3862 C CB  . ARG   B 1 150 ? 26.047  20.745 63.068  1.00 42.87  ? 806  ARG   B CB  1 
ATOM   3863 C CG  . ARG   B 1 150 ? 26.432  19.974 61.818  1.00 60.88  ? 806  ARG   B CG  1 
ATOM   3864 C CD  . ARG   B 1 150 ? 27.282  18.758 62.123  1.00 76.27  ? 806  ARG   B CD  1 
ATOM   3865 N NE  . ARG   B 1 150 ? 27.532  17.943 60.927  1.00 86.61  ? 806  ARG   B NE  1 
ATOM   3866 C CZ  . ARG   B 1 150 ? 26.743  16.954 60.512  1.00 100.49 ? 806  ARG   B CZ  1 
ATOM   3867 N NH1 . ARG   B 1 150 ? 27.050  16.266 59.421  1.00 85.29  ? 806  ARG   B NH1 1 
ATOM   3868 N NH2 . ARG   B 1 150 ? 25.636  16.649 61.183  1.00 85.17  ? 806  ARG   B NH2 1 
ATOM   3869 N N   . ASP   B 1 151 ? 25.298  23.351 64.914  1.00 45.08  ? 807  ASP   B N   1 
ATOM   3870 C CA  . ASP   B 1 151 ? 24.258  24.010 65.701  1.00 45.12  ? 807  ASP   B CA  1 
ATOM   3871 C C   . ASP   B 1 151 ? 24.304  25.550 65.641  1.00 48.66  ? 807  ASP   B C   1 
ATOM   3872 O O   . ASP   B 1 151 ? 23.496  26.201 66.310  1.00 48.51  ? 807  ASP   B O   1 
ATOM   3873 C CB  . ASP   B 1 151 ? 24.281  23.481 67.147  1.00 47.47  ? 807  ASP   B CB  1 
ATOM   3874 C CG  . ASP   B 1 151 ? 23.994  21.984 67.225  1.00 58.58  ? 807  ASP   B CG  1 
ATOM   3875 O OD1 . ASP   B 1 151 ? 22.819  21.589 67.011  1.00 60.04  ? 807  ASP   B OD1 1 
ATOM   3876 O OD2 . ASP   B 1 151 ? 24.944  21.207 67.480  1.00 60.64  ? 807  ASP   B OD2 1 
ATOM   3877 N N   . SER   B 1 152 ? 25.198  26.130 64.807  1.00 44.57  ? 808  SER   B N   1 
ATOM   3878 C CA  . SER   B 1 152 ? 25.320  27.586 64.665  1.00 44.06  ? 808  SER   B CA  1 
ATOM   3879 C C   . SER   B 1 152 ? 24.152  28.204 63.887  1.00 48.18  ? 808  SER   B C   1 
ATOM   3880 O O   . SER   B 1 152 ? 23.391  27.478 63.240  1.00 48.00  ? 808  SER   B O   1 
ATOM   3881 C CB  . SER   B 1 152 ? 26.660  27.969 64.042  1.00 47.94  ? 808  SER   B CB  1 
ATOM   3882 O OG  . SER   B 1 152 ? 26.782  27.536 62.698  1.00 59.07  ? 808  SER   B OG  1 
ATOM   3883 N N   . GLU   B 1 153 ? 23.998  29.541 63.974  1.00 44.15  ? 809  GLU   B N   1 
ATOM   3884 C CA  . GLU   B 1 153 ? 22.947  30.281 63.275  1.00 43.67  ? 809  GLU   B CA  1 
ATOM   3885 C C   . GLU   B 1 153 ? 23.124  30.235 61.742  1.00 44.67  ? 809  GLU   B C   1 
ATOM   3886 O O   . GLU   B 1 153 ? 22.157  29.960 61.025  1.00 44.17  ? 809  GLU   B O   1 
ATOM   3887 C CB  . GLU   B 1 153 ? 22.835  31.728 63.791  1.00 45.14  ? 809  GLU   B CB  1 
ATOM   3888 C CG  . GLU   B 1 153 ? 21.459  32.053 64.361  1.00 59.43  ? 809  GLU   B CG  1 
ATOM   3889 C CD  . GLU   B 1 153 ? 20.326  32.166 63.353  1.00 82.98  ? 809  GLU   B CD  1 
ATOM   3890 O OE1 . GLU   B 1 153 ? 19.960  33.308 62.991  1.00 81.96  ? 809  GLU   B OE1 1 
ATOM   3891 O OE2 . GLU   B 1 153 ? 19.800  31.111 62.930  1.00 73.93  ? 809  GLU   B OE2 1 
ATOM   3892 N N   . GLU   B 1 154 ? 24.364  30.454 61.254  1.00 38.94  ? 810  GLU   B N   1 
ATOM   3893 C CA  . GLU   B 1 154 ? 24.695  30.399 59.822  1.00 37.53  ? 810  GLU   B CA  1 
ATOM   3894 C C   . GLU   B 1 154 ? 24.384  29.022 59.212  1.00 37.24  ? 810  GLU   B C   1 
ATOM   3895 O O   . GLU   B 1 154 ? 23.844  28.973 58.105  1.00 34.82  ? 810  GLU   B O   1 
ATOM   3896 C CB  . GLU   B 1 154 ? 26.143  30.851 59.529  1.00 39.01  ? 810  GLU   B CB  1 
ATOM   3897 C CG  . GLU   B 1 154 ? 27.223  30.112 60.314  1.00 51.37  ? 810  GLU   B CG  1 
ATOM   3898 C CD  . GLU   B 1 154 ? 28.625  30.694 60.293  1.00 65.88  ? 810  GLU   B CD  1 
ATOM   3899 O OE1 . GLU   B 1 154 ? 28.843  31.741 59.638  1.00 47.63  ? 810  GLU   B OE1 1 
ATOM   3900 O OE2 . GLU   B 1 154 ? 29.513  30.094 60.943  1.00 61.59  ? 810  GLU   B OE2 1 
ATOM   3901 N N   . ALA   B 1 155 ? 24.642  27.924 59.977  1.00 31.34  ? 811  ALA   B N   1 
ATOM   3902 C CA  . ALA   B 1 155 ? 24.370  26.536 59.588  1.00 29.96  ? 811  ALA   B CA  1 
ATOM   3903 C C   . ALA   B 1 155 ? 22.865  26.269 59.464  1.00 32.00  ? 811  ALA   B C   1 
ATOM   3904 O O   . ALA   B 1 155 ? 22.446  25.504 58.585  1.00 27.79  ? 811  ALA   B O   1 
ATOM   3905 C CB  . ALA   B 1 155 ? 24.992  25.580 60.595  1.00 30.58  ? 811  ALA   B CB  1 
ATOM   3906 N N   . GLU   B 1 156 ? 22.063  26.882 60.368  1.00 30.44  ? 812  GLU   B N   1 
ATOM   3907 C CA  . GLU   B 1 156 ? 20.601  26.784 60.402  1.00 30.20  ? 812  GLU   B CA  1 
ATOM   3908 C C   . GLU   B 1 156 ? 20.006  27.445 59.161  1.00 33.72  ? 812  GLU   B C   1 
ATOM   3909 O O   . GLU   B 1 156 ? 19.129  26.864 58.525  1.00 34.46  ? 812  GLU   B O   1 
ATOM   3910 C CB  . GLU   B 1 156 ? 20.035  27.429 61.684  1.00 31.89  ? 812  GLU   B CB  1 
ATOM   3911 C CG  . GLU   B 1 156 ? 20.162  26.546 62.922  1.00 47.06  ? 812  GLU   B CG  1 
ATOM   3912 C CD  . GLU   B 1 156 ? 19.881  27.200 64.267  1.00 72.05  ? 812  GLU   B CD  1 
ATOM   3913 O OE1 . GLU   B 1 156 ? 19.066  28.151 64.324  1.00 69.34  ? 812  GLU   B OE1 1 
ATOM   3914 O OE2 . GLU   B 1 156 ? 20.475  26.745 65.273  1.00 63.28  ? 812  GLU   B OE2 1 
ATOM   3915 N N   . ILE   B 1 157 ? 20.507  28.646 58.809  1.00 28.64  ? 813  ILE   B N   1 
ATOM   3916 C CA  . ILE   B 1 157 ? 20.085  29.431 57.639  1.00 28.33  ? 813  ILE   B CA  1 
ATOM   3917 C C   . ILE   B 1 157 ? 20.412  28.687 56.330  1.00 31.81  ? 813  ILE   B C   1 
ATOM   3918 O O   . ILE   B 1 157 ? 19.562  28.636 55.419  1.00 32.13  ? 813  ILE   B O   1 
ATOM   3919 C CB  . ILE   B 1 157 ? 20.713  30.866 57.692  1.00 31.05  ? 813  ILE   B CB  1 
ATOM   3920 C CG1 . ILE   B 1 157 ? 19.940  31.759 58.690  1.00 31.48  ? 813  ILE   B CG1 1 
ATOM   3921 C CG2 . ILE   B 1 157 ? 20.772  31.527 56.304  1.00 30.96  ? 813  ILE   B CG2 1 
ATOM   3922 C CD1 . ILE   B 1 157 ? 20.768  32.849 59.330  1.00 36.39  ? 813  ILE   B CD1 1 
ATOM   3923 N N   . ILE   B 1 158 ? 21.645  28.128 56.250  1.00 25.10  ? 814  ILE   B N   1 
ATOM   3924 C CA  . ILE   B 1 158 ? 22.158  27.366 55.106  1.00 23.74  ? 814  ILE   B CA  1 
ATOM   3925 C C   . ILE   B 1 158 ? 21.303  26.106 54.881  1.00 31.58  ? 814  ILE   B C   1 
ATOM   3926 O O   . ILE   B 1 158 ? 20.953  25.808 53.733  1.00 32.19  ? 814  ILE   B O   1 
ATOM   3927 C CB  . ILE   B 1 158 ? 23.674  27.067 55.279  1.00 24.97  ? 814  ILE   B CB  1 
ATOM   3928 C CG1 . ILE   B 1 158 ? 24.513  28.359 55.169  1.00 23.52  ? 814  ILE   B CG1 1 
ATOM   3929 C CG2 . ILE   B 1 158 ? 24.170  26.012 54.282  1.00 27.43  ? 814  ILE   B CG2 1 
ATOM   3930 C CD1 . ILE   B 1 158 ? 25.933  28.238 55.664  1.00 18.28  ? 814  ILE   B CD1 1 
ATOM   3931 N N   . ARG   B 1 159 ? 20.965  25.378 55.981  1.00 27.61  ? 815  ARG   B N   1 
ATOM   3932 C CA  . ARG   B 1 159 ? 20.155  24.159 55.947  1.00 27.09  ? 815  ARG   B CA  1 
ATOM   3933 C C   . ARG   B 1 159 ? 18.722  24.454 55.530  1.00 32.91  ? 815  ARG   B C   1 
ATOM   3934 O O   . ARG   B 1 159 ? 18.076  23.584 54.959  1.00 33.40  ? 815  ARG   B O   1 
ATOM   3935 C CB  . ARG   B 1 159 ? 20.169  23.444 57.304  1.00 26.25  ? 815  ARG   B CB  1 
ATOM   3936 C CG  . ARG   B 1 159 ? 21.390  22.541 57.534  1.00 42.08  ? 815  ARG   B CG  1 
ATOM   3937 C CD  . ARG   B 1 159 ? 21.186  21.604 58.730  1.00 44.99  ? 815  ARG   B CD  1 
ATOM   3938 N NE  . ARG   B 1 159 ? 20.869  22.359 59.939  1.00 41.51  ? 815  ARG   B NE  1 
ATOM   3939 C CZ  . ARG   B 1 159 ? 21.730  22.616 60.913  1.00 54.60  ? 815  ARG   B CZ  1 
ATOM   3940 N NH1 . ARG   B 1 159 ? 21.364  23.359 61.949  1.00 38.45  ? 815  ARG   B NH1 1 
ATOM   3941 N NH2 . ARG   B 1 159 ? 22.955  22.106 60.876  1.00 48.63  ? 815  ARG   B NH2 1 
ATOM   3942 N N   . LYS   B 1 160 ? 18.211  25.663 55.842  1.00 30.57  ? 816  LYS   B N   1 
ATOM   3943 C CA  . LYS   B 1 160 ? 16.842  26.065 55.476  1.00 30.02  ? 816  LYS   B CA  1 
ATOM   3944 C C   . LYS   B 1 160 ? 16.769  26.395 53.972  1.00 31.92  ? 816  LYS   B C   1 
ATOM   3945 O O   . LYS   B 1 160 ? 15.794  26.037 53.310  1.00 31.42  ? 816  LYS   B O   1 
ATOM   3946 C CB  . LYS   B 1 160 ? 16.359  27.235 56.344  1.00 32.85  ? 816  LYS   B CB  1 
ATOM   3947 C CG  . LYS   B 1 160 ? 14.848  27.360 56.402  1.00 47.35  ? 816  LYS   B CG  1 
ATOM   3948 C CD  . LYS   B 1 160 ? 14.421  28.334 57.481  1.00 61.02  ? 816  LYS   B CD  1 
ATOM   3949 C CE  . LYS   B 1 160 ? 12.917  28.449 57.549  1.00 77.03  ? 816  LYS   B CE  1 
ATOM   3950 N NZ  . LYS   B 1 160 ? 12.488  29.600 58.380  1.00 87.70  ? 816  LYS   B NZ  1 
ATOM   3951 N N   . TYR   B 1 161 ? 17.834  27.020 53.439  1.00 27.17  ? 817  TYR   B N   1 
ATOM   3952 C CA  . TYR   B 1 161 ? 18.007  27.370 52.028  1.00 25.14  ? 817  TYR   B CA  1 
ATOM   3953 C C   . TYR   B 1 161 ? 17.991  26.092 51.177  1.00 27.37  ? 817  TYR   B C   1 
ATOM   3954 O O   . TYR   B 1 161 ? 17.257  26.038 50.203  1.00 28.52  ? 817  TYR   B O   1 
ATOM   3955 C CB  . TYR   B 1 161 ? 19.326  28.142 51.862  1.00 24.86  ? 817  TYR   B CB  1 
ATOM   3956 C CG  . TYR   B 1 161 ? 19.474  29.047 50.654  1.00 23.82  ? 817  TYR   B CG  1 
ATOM   3957 C CD1 . TYR   B 1 161 ? 18.477  29.120 49.677  1.00 26.19  ? 817  TYR   B CD1 1 
ATOM   3958 C CD2 . TYR   B 1 161 ? 20.607  29.835 50.492  1.00 22.97  ? 817  TYR   B CD2 1 
ATOM   3959 C CE1 . TYR   B 1 161 ? 18.622  29.942 48.560  1.00 26.04  ? 817  TYR   B CE1 1 
ATOM   3960 C CE2 . TYR   B 1 161 ? 20.756  30.667 49.389  1.00 23.00  ? 817  TYR   B CE2 1 
ATOM   3961 C CZ  . TYR   B 1 161 ? 19.767  30.715 48.424  1.00 28.01  ? 817  TYR   B CZ  1 
ATOM   3962 O OH  . TYR   B 1 161 ? 19.954  31.536 47.344  1.00 25.89  ? 817  TYR   B OH  1 
ATOM   3963 N N   . VAL   B 1 162 ? 18.731  25.052 51.594  1.00 23.90  ? 818  VAL   B N   1 
ATOM   3964 C CA  . VAL   B 1 162 ? 18.792  23.730 50.950  1.00 23.69  ? 818  VAL   B CA  1 
ATOM   3965 C C   . VAL   B 1 162 ? 17.383  23.090 51.013  1.00 27.63  ? 818  VAL   B C   1 
ATOM   3966 O O   . VAL   B 1 162 ? 16.820  22.727 49.978  1.00 24.72  ? 818  VAL   B O   1 
ATOM   3967 C CB  . VAL   B 1 162 ? 19.875  22.812 51.599  1.00 27.15  ? 818  VAL   B CB  1 
ATOM   3968 C CG1 . VAL   B 1 162 ? 19.855  21.399 51.020  1.00 27.06  ? 818  VAL   B CG1 1 
ATOM   3969 C CG2 . VAL   B 1 162 ? 21.265  23.410 51.490  1.00 26.53  ? 818  VAL   B CG2 1 
ATOM   3970 N N   . LYS   B 1 163 ? 16.816  22.997 52.236  1.00 25.82  ? 819  LYS   B N   1 
ATOM   3971 C CA  . LYS   B 1 163 ? 15.508  22.436 52.524  1.00 26.10  ? 819  LYS   B CA  1 
ATOM   3972 C C   . LYS   B 1 163 ? 14.343  23.066 51.710  1.00 31.68  ? 819  LYS   B C   1 
ATOM   3973 O O   . LYS   B 1 163 ? 13.531  22.322 51.151  1.00 33.18  ? 819  LYS   B O   1 
ATOM   3974 C CB  . LYS   B 1 163 ? 15.241  22.518 54.043  1.00 29.17  ? 819  LYS   B CB  1 
ATOM   3975 C CG  . LYS   B 1 163 ? 13.969  21.827 54.527  1.00 39.97  ? 819  LYS   B CG  1 
ATOM   3976 C CD  . LYS   B 1 163 ? 13.845  21.941 56.027  1.00 51.51  ? 819  LYS   B CD  1 
ATOM   3977 C CE  . LYS   B 1 163 ? 12.781  21.008 56.536  1.00 59.90  ? 819  LYS   B CE  1 
ATOM   3978 N NZ  . LYS   B 1 163 ? 11.408  21.567 56.391  1.00 62.11  ? 819  LYS   B NZ  1 
ATOM   3979 N N   . ASN   B 1 164 ? 14.266  24.407 51.644  1.00 27.10  ? 820  ASN   B N   1 
ATOM   3980 C CA  . ASN   B 1 164 ? 13.157  25.100 51.017  1.00 29.24  ? 820  ASN   B CA  1 
ATOM   3981 C C   . ASN   B 1 164 ? 13.240  25.371 49.513  1.00 34.00  ? 820  ASN   B C   1 
ATOM   3982 O O   . ASN   B 1 164 ? 12.193  25.666 48.929  1.00 31.44  ? 820  ASN   B O   1 
ATOM   3983 C CB  . ASN   B 1 164 ? 12.907  26.429 51.723  1.00 35.99  ? 820  ASN   B CB  1 
ATOM   3984 C CG  . ASN   B 1 164 ? 12.412  26.373 53.151  1.00 59.71  ? 820  ASN   B CG  1 
ATOM   3985 O OD1 . ASN   B 1 164 ? 11.940  25.353 53.659  1.00 56.32  ? 820  ASN   B OD1 1 
ATOM   3986 N ND2 . ASN   B 1 164 ? 12.477  27.509 53.821  1.00 48.81  ? 820  ASN   B ND2 1 
ATOM   3987 N N   . THR   B 1 165 ? 14.454  25.342 48.895  1.00 29.92  ? 821  THR   B N   1 
ATOM   3988 C CA  . THR   B 1 165 ? 14.582  25.713 47.487  1.00 29.74  ? 821  THR   B CA  1 
ATOM   3989 C C   . THR   B 1 165 ? 14.907  24.504 46.565  1.00 32.94  ? 821  THR   B C   1 
ATOM   3990 O O   . THR   B 1 165 ? 15.490  24.673 45.483  1.00 31.23  ? 821  THR   B O   1 
ATOM   3991 C CB  . THR   B 1 165 ? 15.558  26.911 47.312  1.00 34.84  ? 821  THR   B CB  1 
ATOM   3992 O OG1 . THR   B 1 165 ? 16.900  26.510 47.571  1.00 33.34  ? 821  THR   B OG1 1 
ATOM   3993 C CG2 . THR   B 1 165 ? 15.174  28.133 48.158  1.00 32.33  ? 821  THR   B CG2 1 
ATOM   3994 N N   . HIS   B 1 166 ? 14.457  23.303 46.959  1.00 29.70  ? 822  HIS   B N   1 
ATOM   3995 C CA  . HIS   B 1 166 ? 14.627  22.127 46.107  1.00 29.47  ? 822  HIS   B CA  1 
ATOM   3996 C C   . HIS   B 1 166 ? 13.345  22.027 45.281  1.00 33.58  ? 822  HIS   B C   1 
ATOM   3997 O O   . HIS   B 1 166 ? 12.271  21.833 45.845  1.00 31.99  ? 822  HIS   B O   1 
ATOM   3998 C CB  . HIS   B 1 166 ? 14.901  20.851 46.930  1.00 29.43  ? 822  HIS   B CB  1 
ATOM   3999 C CG  . HIS   B 1 166 ? 15.259  19.648 46.108  1.00 32.50  ? 822  HIS   B CG  1 
ATOM   4000 N ND1 . HIS   B 1 166 ? 16.295  18.820 46.477  1.00 34.57  ? 822  HIS   B ND1 1 
ATOM   4001 C CD2 . HIS   B 1 166 ? 14.679  19.147 44.985  1.00 34.31  ? 822  HIS   B CD2 1 
ATOM   4002 C CE1 . HIS   B 1 166 ? 16.350  17.877 45.551  1.00 34.43  ? 822  HIS   B CE1 1 
ATOM   4003 N NE2 . HIS   B 1 166 ? 15.382  18.021 44.644  1.00 34.70  ? 822  HIS   B NE2 1 
ATOM   4004 N N   . ALA   B 1 167 ? 13.463  22.173 43.945  1.00 31.10  ? 823  ALA   B N   1 
ATOM   4005 C CA  . ALA   B 1 167 ? 12.341  22.161 43.016  1.00 29.91  ? 823  ALA   B CA  1 
ATOM   4006 C C   . ALA   B 1 167 ? 11.689  20.795 42.833  1.00 33.54  ? 823  ALA   B C   1 
ATOM   4007 O O   . ALA   B 1 167 ? 12.377  19.786 42.789  1.00 32.38  ? 823  ALA   B O   1 
ATOM   4008 C CB  . ALA   B 1 167 ? 12.760  22.726 41.676  1.00 30.40  ? 823  ALA   B CB  1 
ATOM   4009 N N   . THR   B 1 168 ? 10.347  20.774 42.707  1.00 29.73  ? 824  THR   B N   1 
ATOM   4010 C CA  . THR   B 1 168 ? 9.559   19.555 42.493  1.00 30.67  ? 824  THR   B CA  1 
ATOM   4011 C C   . THR   B 1 168 ? 10.011  18.853 41.214  1.00 35.23  ? 824  THR   B C   1 
ATOM   4012 O O   . THR   B 1 168 ? 10.134  17.632 41.223  1.00 35.61  ? 824  THR   B O   1 
ATOM   4013 C CB  . THR   B 1 168 ? 8.061   19.879 42.486  1.00 43.07  ? 824  THR   B CB  1 
ATOM   4014 O OG1 . THR   B 1 168 ? 7.710   20.463 43.736  1.00 40.44  ? 824  THR   B OG1 1 
ATOM   4015 C CG2 . THR   B 1 168 ? 7.168   18.651 42.258  1.00 48.01  ? 824  THR   B CG2 1 
ATOM   4016 N N   . THR   B 1 169 ? 10.320  19.611 40.143  1.00 31.65  ? 825  THR   B N   1 
ATOM   4017 C CA  . THR   B 1 169 ? 10.748  18.998 38.872  1.00 31.35  ? 825  THR   B CA  1 
ATOM   4018 C C   . THR   B 1 169 ? 12.130  18.296 38.981  1.00 30.70  ? 825  THR   B C   1 
ATOM   4019 O O   . THR   B 1 169 ? 12.484  17.541 38.085  1.00 28.17  ? 825  THR   B O   1 
ATOM   4020 C CB  . THR   B 1 169 ? 10.680  19.986 37.702  1.00 36.74  ? 825  THR   B CB  1 
ATOM   4021 O OG1 . THR   B 1 169 ? 11.786  20.896 37.775  1.00 38.36  ? 825  THR   B OG1 1 
ATOM   4022 C CG2 . THR   B 1 169 ? 9.308   20.701 37.602  1.00 33.16  ? 825  THR   B CG2 1 
ATOM   4023 N N   . HIS   B 1 170 ? 12.860  18.513 40.089  1.00 27.68  ? 826  HIS   B N   1 
ATOM   4024 C CA  . HIS   B 1 170 ? 14.184  17.918 40.381  1.00 26.68  ? 826  HIS   B CA  1 
ATOM   4025 C C   . HIS   B 1 170 ? 14.088  16.856 41.505  1.00 37.61  ? 826  HIS   B C   1 
ATOM   4026 O O   . HIS   B 1 170 ? 15.084  16.587 42.175  1.00 38.88  ? 826  HIS   B O   1 
ATOM   4027 C CB  . HIS   B 1 170 ? 15.199  19.034 40.750  1.00 25.86  ? 826  HIS   B CB  1 
ATOM   4028 C CG  . HIS   B 1 170 ? 15.406  20.068 39.677  1.00 27.69  ? 826  HIS   B CG  1 
ATOM   4029 N ND1 . HIS   B 1 170 ? 15.799  21.355 39.983  1.00 28.80  ? 826  HIS   B ND1 1 
ATOM   4030 C CD2 . HIS   B 1 170 ? 15.221  19.977 38.339  1.00 28.76  ? 826  HIS   B CD2 1 
ATOM   4031 C CE1 . HIS   B 1 170 ? 15.881  21.991 38.828  1.00 28.30  ? 826  HIS   B CE1 1 
ATOM   4032 N NE2 . HIS   B 1 170 ? 15.526  21.205 37.813  1.00 28.73  ? 826  HIS   B NE2 1 
ATOM   4033 N N   . ASN   B 1 171 ? 12.892  16.232 41.671  1.00 38.91  ? 827  ASN   B N   1 
ATOM   4034 C CA  . ASN   B 1 171 ? 12.574  15.240 42.713  1.00 40.76  ? 827  ASN   B CA  1 
ATOM   4035 C C   . ASN   B 1 171 ? 13.148  13.805 42.489  1.00 45.61  ? 827  ASN   B C   1 
ATOM   4036 O O   . ASN   B 1 171 ? 12.973  12.960 43.367  1.00 45.73  ? 827  ASN   B O   1 
ATOM   4037 C CB  . ASN   B 1 171 ? 11.049  15.169 42.979  1.00 46.69  ? 827  ASN   B CB  1 
ATOM   4038 C CG  . ASN   B 1 171 ? 10.222  14.544 41.878  1.00 76.30  ? 827  ASN   B CG  1 
ATOM   4039 O OD1 . ASN   B 1 171 ? 10.621  14.450 40.705  1.00 71.20  ? 827  ASN   B OD1 1 
ATOM   4040 N ND2 . ASN   B 1 171 ? 9.030   14.121 42.239  1.00 73.11  ? 827  ASN   B ND2 1 
ATOM   4041 N N   . ALA   B 1 172 ? 13.866  13.540 41.374  1.00 42.14  ? 828  ALA   B N   1 
ATOM   4042 C CA  . ALA   B 1 172 ? 14.533  12.248 41.128  1.00 41.53  ? 828  ALA   B CA  1 
ATOM   4043 C C   . ALA   B 1 172 ? 15.637  11.976 42.195  1.00 45.12  ? 828  ALA   B C   1 
ATOM   4044 O O   . ALA   B 1 172 ? 16.223  10.888 42.234  1.00 46.44  ? 828  ALA   B O   1 
ATOM   4045 C CB  . ALA   B 1 172 ? 15.141  12.230 39.730  1.00 42.15  ? 828  ALA   B CB  1 
ATOM   4046 N N   . TYR   B 1 173 ? 15.926  12.985 43.041  1.00 38.84  ? 829  TYR   B N   1 
ATOM   4047 C CA  . TYR   B 1 173 ? 16.899  12.924 44.130  1.00 36.95  ? 829  TYR   B CA  1 
ATOM   4048 C C   . TYR   B 1 173 ? 16.509  13.869 45.269  1.00 39.06  ? 829  TYR   B C   1 
ATOM   4049 O O   . TYR   B 1 173 ? 15.804  14.865 45.041  1.00 38.50  ? 829  TYR   B O   1 
ATOM   4050 C CB  . TYR   B 1 173 ? 18.345  13.220 43.639  1.00 37.07  ? 829  TYR   B CB  1 
ATOM   4051 C CG  . TYR   B 1 173 ? 18.607  14.651 43.201  1.00 36.64  ? 829  TYR   B CG  1 
ATOM   4052 C CD1 . TYR   B 1 173 ? 19.029  15.615 44.111  1.00 37.23  ? 829  TYR   B CD1 1 
ATOM   4053 C CD2 . TYR   B 1 173 ? 18.453  15.035 41.872  1.00 37.93  ? 829  TYR   B CD2 1 
ATOM   4054 C CE1 . TYR   B 1 173 ? 19.273  16.934 43.714  1.00 35.34  ? 829  TYR   B CE1 1 
ATOM   4055 C CE2 . TYR   B 1 173 ? 18.703  16.350 41.460  1.00 38.14  ? 829  TYR   B CE2 1 
ATOM   4056 C CZ  . TYR   B 1 173 ? 19.116  17.296 42.385  1.00 39.63  ? 829  TYR   B CZ  1 
ATOM   4057 O OH  . TYR   B 1 173 ? 19.354  18.591 41.990  1.00 36.01  ? 829  TYR   B OH  1 
ATOM   4058 N N   . ASP   B 1 174 ? 16.949  13.514 46.493  1.00 32.81  ? 830  ASP   B N   1 
ATOM   4059 C CA  . ASP   B 1 174 ? 16.869  14.297 47.733  1.00 32.31  ? 830  ASP   B CA  1 
ATOM   4060 C C   . ASP   B 1 174 ? 18.311  14.782 48.013  1.00 33.12  ? 830  ASP   B C   1 
ATOM   4061 O O   . ASP   B 1 174 ? 19.270  14.177 47.510  1.00 30.19  ? 830  ASP   B O   1 
ATOM   4062 C CB  . ASP   B 1 174 ? 16.425  13.433 48.940  1.00 34.77  ? 830  ASP   B CB  1 
ATOM   4063 C CG  . ASP   B 1 174 ? 14.941  13.085 49.069  1.00 46.86  ? 830  ASP   B CG  1 
ATOM   4064 O OD1 . ASP   B 1 174 ? 14.107  13.749 48.408  1.00 48.65  ? 830  ASP   B OD1 1 
ATOM   4065 O OD2 . ASP   B 1 174 ? 14.613  12.161 49.856  1.00 48.91  ? 830  ASP   B OD2 1 
ATOM   4066 N N   . LEU   B 1 175 ? 18.461  15.833 48.847  1.00 29.46  ? 831  LEU   B N   1 
ATOM   4067 C CA  . LEU   B 1 175 ? 19.767  16.364 49.241  1.00 28.73  ? 831  LEU   B CA  1 
ATOM   4068 C C   . LEU   B 1 175 ? 19.974  16.253 50.725  1.00 31.42  ? 831  LEU   B C   1 
ATOM   4069 O O   . LEU   B 1 175 ? 19.078  16.611 51.497  1.00 30.86  ? 831  LEU   B O   1 
ATOM   4070 C CB  . LEU   B 1 175 ? 19.940  17.835 48.815  1.00 28.50  ? 831  LEU   B CB  1 
ATOM   4071 C CG  . LEU   B 1 175 ? 20.095  18.105 47.333  1.00 32.77  ? 831  LEU   B CG  1 
ATOM   4072 C CD1 . LEU   B 1 175 ? 19.977  19.571 47.061  1.00 33.26  ? 831  LEU   B CD1 1 
ATOM   4073 C CD2 . LEU   B 1 175 ? 21.418  17.586 46.818  1.00 34.74  ? 831  LEU   B CD2 1 
ATOM   4074 N N   . GLU   B 1 176 ? 21.167  15.789 51.125  1.00 25.88  ? 832  GLU   B N   1 
ATOM   4075 C CA  . GLU   B 1 176 ? 21.563  15.682 52.525  1.00 26.95  ? 832  GLU   B CA  1 
ATOM   4076 C C   . GLU   B 1 176 ? 22.892  16.431 52.699  1.00 29.09  ? 832  GLU   B C   1 
ATOM   4077 O O   . GLU   B 1 176 ? 23.883  16.094 52.044  1.00 27.98  ? 832  GLU   B O   1 
ATOM   4078 C CB  . GLU   B 1 176 ? 21.716  14.211 52.928  1.00 29.58  ? 832  GLU   B CB  1 
ATOM   4079 C CG  . GLU   B 1 176 ? 21.815  13.971 54.427  1.00 48.29  ? 832  GLU   B CG  1 
ATOM   4080 C CD  . GLU   B 1 176 ? 22.377  12.613 54.805  1.00 81.39  ? 832  GLU   B CD  1 
ATOM   4081 O OE1 . GLU   B 1 176 ? 23.314  12.568 55.636  1.00 76.81  ? 832  GLU   B OE1 1 
ATOM   4082 O OE2 . GLU   B 1 176 ? 21.884  11.593 54.270  1.00 83.03  ? 832  GLU   B OE2 1 
ATOM   4083 N N   . VAL   B 1 177 ? 22.901  17.460 53.556  1.00 24.40  ? 833  VAL   B N   1 
ATOM   4084 C CA  . VAL   B 1 177 ? 24.106  18.252 53.830  1.00 23.77  ? 833  VAL   B CA  1 
ATOM   4085 C C   . VAL   B 1 177 ? 25.045  17.429 54.716  1.00 29.57  ? 833  VAL   B C   1 
ATOM   4086 O O   . VAL   B 1 177 ? 24.672  17.072 55.836  1.00 30.31  ? 833  VAL   B O   1 
ATOM   4087 C CB  . VAL   B 1 177 ? 23.817  19.642 54.462  1.00 26.98  ? 833  VAL   B CB  1 
ATOM   4088 C CG1 . VAL   B 1 177 ? 25.061  20.513 54.432  1.00 26.54  ? 833  VAL   B CG1 1 
ATOM   4089 C CG2 . VAL   B 1 177 ? 22.643  20.359 53.788  1.00 26.84  ? 833  VAL   B CG2 1 
ATOM   4090 N N   . ILE   B 1 178 ? 26.234  17.092 54.205  1.00 26.35  ? 834  ILE   B N   1 
ATOM   4091 C CA  . ILE   B 1 178 ? 27.234  16.337 54.977  1.00 26.78  ? 834  ILE   B CA  1 
ATOM   4092 C C   . ILE   B 1 178 ? 28.104  17.318 55.796  1.00 30.81  ? 834  ILE   B C   1 
ATOM   4093 O O   . ILE   B 1 178 ? 28.211  17.187 57.014  1.00 30.39  ? 834  ILE   B O   1 
ATOM   4094 C CB  . ILE   B 1 178 ? 28.105  15.400 54.088  1.00 30.10  ? 834  ILE   B CB  1 
ATOM   4095 C CG1 . ILE   B 1 178 ? 27.238  14.415 53.271  1.00 30.51  ? 834  ILE   B CG1 1 
ATOM   4096 C CG2 . ILE   B 1 178 ? 29.187  14.669 54.928  1.00 30.89  ? 834  ILE   B CG2 1 
ATOM   4097 C CD1 . ILE   B 1 178 ? 27.914  14.013 52.057  1.00 33.12  ? 834  ILE   B CD1 1 
ATOM   4098 N N   . ASP   B 1 179 ? 28.713  18.289 55.122  1.00 27.81  ? 835  ASP   B N   1 
ATOM   4099 C CA  . ASP   B 1 179 ? 29.588  19.270 55.745  1.00 28.11  ? 835  ASP   B CA  1 
ATOM   4100 C C   . ASP   B 1 179 ? 29.324  20.678 55.197  1.00 32.60  ? 835  ASP   B C   1 
ATOM   4101 O O   . ASP   B 1 179 ? 28.956  20.843 54.027  1.00 31.76  ? 835  ASP   B O   1 
ATOM   4102 C CB  . ASP   B 1 179 ? 31.058  18.913 55.471  1.00 30.10  ? 835  ASP   B CB  1 
ATOM   4103 C CG  . ASP   B 1 179 ? 31.586  17.672 56.161  1.00 43.74  ? 835  ASP   B CG  1 
ATOM   4104 O OD1 . ASP   B 1 179 ? 31.540  17.621 57.411  1.00 44.94  ? 835  ASP   B OD1 1 
ATOM   4105 O OD2 . ASP   B 1 179 ? 32.089  16.769 55.453  1.00 53.12  ? 835  ASP   B OD2 1 
ATOM   4106 N N   . ILE   B 1 180 ? 29.529  21.683 56.052  1.00 27.56  ? 836  ILE   B N   1 
ATOM   4107 C CA  . ILE   B 1 180 ? 29.449  23.090 55.692  1.00 25.88  ? 836  ILE   B CA  1 
ATOM   4108 C C   . ILE   B 1 180 ? 30.829  23.687 55.966  1.00 27.78  ? 836  ILE   B C   1 
ATOM   4109 O O   . ILE   B 1 180 ? 31.339  23.588 57.089  1.00 26.76  ? 836  ILE   B O   1 
ATOM   4110 C CB  . ILE   B 1 180 ? 28.310  23.884 56.405  1.00 28.50  ? 836  ILE   B CB  1 
ATOM   4111 C CG1 . ILE   B 1 180 ? 26.907  23.232 56.185  1.00 28.62  ? 836  ILE   B CG1 1 
ATOM   4112 C CG2 . ILE   B 1 180 ? 28.324  25.357 55.933  1.00 28.53  ? 836  ILE   B CG2 1 
ATOM   4113 C CD1 . ILE   B 1 180 ? 25.705  23.800 57.066  1.00 25.42  ? 836  ILE   B CD1 1 
ATOM   4114 N N   . PHE   B 1 181 ? 31.450  24.282 54.936  1.00 22.25  ? 837  PHE   B N   1 
ATOM   4115 C CA  . PHE   B 1 181 ? 32.746  24.928 55.106  1.00 20.38  ? 837  PHE   B CA  1 
ATOM   4116 C C   . PHE   B 1 181 ? 32.613  26.424 54.926  1.00 26.13  ? 837  PHE   B C   1 
ATOM   4117 O O   . PHE   B 1 181 ? 31.912  26.879 54.009  1.00 25.54  ? 837  PHE   B O   1 
ATOM   4118 C CB  . PHE   B 1 181 ? 33.805  24.374 54.135  1.00 21.02  ? 837  PHE   B CB  1 
ATOM   4119 C CG  . PHE   B 1 181 ? 34.010  22.884 54.219  1.00 21.79  ? 837  PHE   B CG  1 
ATOM   4120 C CD1 . PHE   B 1 181 ? 34.821  22.332 55.205  1.00 23.79  ? 837  PHE   B CD1 1 
ATOM   4121 C CD2 . PHE   B 1 181 ? 33.394  22.027 53.308  1.00 22.53  ? 837  PHE   B CD2 1 
ATOM   4122 C CE1 . PHE   B 1 181 ? 35.002  20.943 55.292  1.00 24.04  ? 837  PHE   B CE1 1 
ATOM   4123 C CE2 . PHE   B 1 181 ? 33.562  20.639 53.404  1.00 24.29  ? 837  PHE   B CE2 1 
ATOM   4124 C CZ  . PHE   B 1 181 ? 34.370  20.106 54.395  1.00 22.41  ? 837  PHE   B CZ  1 
ATOM   4125 N N   . LYS   B 1 182 ? 33.274  27.196 55.801  1.00 23.94  ? 838  LYS   B N   1 
ATOM   4126 C CA  . LYS   B 1 182 ? 33.310  28.641 55.643  1.00 25.20  ? 838  LYS   B CA  1 
ATOM   4127 C C   . LYS   B 1 182 ? 34.612  28.853 54.889  1.00 29.16  ? 838  LYS   B C   1 
ATOM   4128 O O   . LYS   B 1 182 ? 35.665  28.393 55.352  1.00 30.59  ? 838  LYS   B O   1 
ATOM   4129 C CB  . LYS   B 1 182 ? 33.290  29.376 56.997  1.00 28.97  ? 838  LYS   B CB  1 
ATOM   4130 C CG  . LYS   B 1 182 ? 32.883  30.838 56.877  1.00 42.36  ? 838  LYS   B CG  1 
ATOM   4131 C CD  . LYS   B 1 182 ? 33.353  31.646 58.073  1.00 52.58  ? 838  LYS   B CD  1 
ATOM   4132 C CE  . LYS   B 1 182 ? 32.654  32.983 58.191  1.00 62.53  ? 838  LYS   B CE  1 
ATOM   4133 N NZ  . LYS   B 1 182 ? 31.367  32.874 58.932  1.00 69.91  ? 838  LYS   B NZ  1 
ATOM   4134 N N   . ILE   B 1 183 ? 34.541  29.450 53.686  1.00 24.05  ? 839  ILE   B N   1 
ATOM   4135 C CA  . ILE   B 1 183 ? 35.739  29.627 52.862  1.00 23.15  ? 839  ILE   B CA  1 
ATOM   4136 C C   . ILE   B 1 183 ? 36.108  31.105 52.646  1.00 27.27  ? 839  ILE   B C   1 
ATOM   4137 O O   . ILE   B 1 183 ? 35.235  31.980 52.508  1.00 25.67  ? 839  ILE   B O   1 
ATOM   4138 C CB  . ILE   B 1 183 ? 35.668  28.827 51.533  1.00 25.97  ? 839  ILE   B CB  1 
ATOM   4139 C CG1 . ILE   B 1 183 ? 34.492  29.298 50.618  1.00 25.47  ? 839  ILE   B CG1 1 
ATOM   4140 C CG2 . ILE   B 1 183 ? 35.623  27.287 51.816  1.00 24.73  ? 839  ILE   B CG2 1 
ATOM   4141 C CD1 . ILE   B 1 183 ? 34.553  28.812 49.190  1.00 17.23  ? 839  ILE   B CD1 1 
ATOM   4142 N N   . GLU   B 1 184 ? 37.438  31.360 52.674  1.00 25.08  ? 840  GLU   B N   1 
ATOM   4143 C CA  . GLU   B 1 184 ? 38.060  32.660 52.497  1.00 25.68  ? 840  GLU   B CA  1 
ATOM   4144 C C   . GLU   B 1 184 ? 39.248  32.555 51.541  1.00 28.67  ? 840  GLU   B C   1 
ATOM   4145 O O   . GLU   B 1 184 ? 40.348  32.164 51.945  1.00 26.71  ? 840  GLU   B O   1 
ATOM   4146 C CB  . GLU   B 1 184 ? 38.480  33.263 53.853  1.00 27.47  ? 840  GLU   B CB  1 
ATOM   4147 C CG  . GLU   B 1 184 ? 38.853  34.737 53.773  1.00 41.17  ? 840  GLU   B CG  1 
ATOM   4148 C CD  . GLU   B 1 184 ? 39.124  35.432 55.095  1.00 66.83  ? 840  GLU   B CD  1 
ATOM   4149 O OE1 . GLU   B 1 184 ? 38.275  35.331 56.011  1.00 58.15  ? 840  GLU   B OE1 1 
ATOM   4150 O OE2 . GLU   B 1 184 ? 40.179  36.096 55.208  1.00 67.94  ? 840  GLU   B OE2 1 
ATOM   4151 N N   . ARG   B 1 185 ? 39.018  32.903 50.263  1.00 25.47  ? 841  ARG   B N   1 
ATOM   4152 C CA  . ARG   B 1 185 ? 40.068  32.884 49.257  1.00 24.89  ? 841  ARG   B CA  1 
ATOM   4153 C C   . ARG   B 1 185 ? 40.970  34.083 49.480  1.00 29.76  ? 841  ARG   B C   1 
ATOM   4154 O O   . ARG   B 1 185 ? 40.477  35.193 49.729  1.00 29.88  ? 841  ARG   B O   1 
ATOM   4155 C CB  . ARG   B 1 185 ? 39.497  32.949 47.845  1.00 24.81  ? 841  ARG   B CB  1 
ATOM   4156 C CG  . ARG   B 1 185 ? 38.862  31.657 47.316  1.00 29.17  ? 841  ARG   B CG  1 
ATOM   4157 C CD  . ARG   B 1 185 ? 38.537  31.780 45.829  1.00 29.99  ? 841  ARG   B CD  1 
ATOM   4158 N NE  . ARG   B 1 185 ? 39.761  31.905 45.041  1.00 34.49  ? 841  ARG   B NE  1 
ATOM   4159 C CZ  . ARG   B 1 185 ? 40.197  33.028 44.479  1.00 42.88  ? 841  ARG   B CZ  1 
ATOM   4160 N NH1 . ARG   B 1 185 ? 41.346  33.043 43.824  1.00 26.38  ? 841  ARG   B NH1 1 
ATOM   4161 N NH2 . ARG   B 1 185 ? 39.476  34.140 44.551  1.00 36.88  ? 841  ARG   B NH2 1 
ATOM   4162 N N   . GLU   B 1 186 ? 42.290  33.855 49.417  1.00 25.16  ? 842  GLU   B N   1 
ATOM   4163 C CA  . GLU   B 1 186 ? 43.289  34.913 49.557  1.00 25.97  ? 842  GLU   B CA  1 
ATOM   4164 C C   . GLU   B 1 186 ? 43.086  35.961 48.435  1.00 28.99  ? 842  GLU   B C   1 
ATOM   4165 O O   . GLU   B 1 186 ? 42.925  35.602 47.256  1.00 28.47  ? 842  GLU   B O   1 
ATOM   4166 C CB  . GLU   B 1 186 ? 44.690  34.290 49.493  1.00 27.90  ? 842  GLU   B CB  1 
ATOM   4167 C CG  . GLU   B 1 186 ? 45.848  35.207 49.811  1.00 43.72  ? 842  GLU   B CG  1 
ATOM   4168 C CD  . GLU   B 1 186 ? 47.176  34.522 49.561  1.00 70.60  ? 842  GLU   B CD  1 
ATOM   4169 O OE1 . GLU   B 1 186 ? 47.719  33.912 50.512  1.00 80.36  ? 842  GLU   B OE1 1 
ATOM   4170 O OE2 . GLU   B 1 186 ? 47.654  34.558 48.404  1.00 54.21  ? 842  GLU   B OE2 1 
ATOM   4171 N N   . GLY   B 1 187 ? 42.997  37.226 48.848  1.00 26.45  ? 843  GLY   B N   1 
ATOM   4172 C CA  . GLY   B 1 187 ? 42.845  38.389 47.979  1.00 26.37  ? 843  GLY   B CA  1 
ATOM   4173 C C   . GLY   B 1 187 ? 41.431  38.709 47.544  1.00 31.49  ? 843  GLY   B C   1 
ATOM   4174 O O   . GLY   B 1 187 ? 41.166  39.823 47.099  1.00 30.96  ? 843  GLY   B O   1 
ATOM   4175 N N   . GLU   B 1 188 ? 40.519  37.736 47.644  1.00 30.26  ? 844  GLU   B N   1 
ATOM   4176 C CA  . GLU   B 1 188 ? 39.142  37.866 47.189  1.00 30.18  ? 844  GLU   B CA  1 
ATOM   4177 C C   . GLU   B 1 188 ? 38.367  38.981 47.895  1.00 37.12  ? 844  GLU   B C   1 
ATOM   4178 O O   . GLU   B 1 188 ? 37.696  39.761 47.223  1.00 37.21  ? 844  GLU   B O   1 
ATOM   4179 C CB  . GLU   B 1 188 ? 38.422  36.529 47.281  1.00 30.56  ? 844  GLU   B CB  1 
ATOM   4180 C CG  . GLU   B 1 188 ? 37.178  36.486 46.421  1.00 37.73  ? 844  GLU   B CG  1 
ATOM   4181 C CD  . GLU   B 1 188 ? 36.450  35.166 46.474  1.00 47.78  ? 844  GLU   B CD  1 
ATOM   4182 O OE1 . GLU   B 1 188 ? 35.850  34.854 47.526  1.00 58.72  ? 844  GLU   B OE1 1 
ATOM   4183 O OE2 . GLU   B 1 188 ? 36.490  34.436 45.460  1.00 38.18  ? 844  GLU   B OE2 1 
ATOM   4184 N N   . CYS   B 1 189 ? 38.500  39.079 49.220  1.00 36.05  ? 845  CYS   B N   1 
ATOM   4185 C CA  . CYS   B 1 189 ? 37.833  40.081 50.049  1.00 37.69  ? 845  CYS   B CA  1 
ATOM   4186 C C   . CYS   B 1 189 ? 38.206  41.521 49.652  1.00 41.51  ? 845  CYS   B C   1 
ATOM   4187 O O   . CYS   B 1 189 ? 37.338  42.401 49.640  1.00 40.47  ? 845  CYS   B O   1 
ATOM   4188 C CB  . CYS   B 1 189 ? 38.105  39.811 51.526  1.00 39.25  ? 845  CYS   B CB  1 
ATOM   4189 S SG  . CYS   B 1 189 ? 37.137  40.833 52.658  1.00 43.87  ? 845  CYS   B SG  1 
ATOM   4190 N N   . GLN   B 1 190 ? 39.484  41.744 49.304  1.00 37.98  ? 846  GLN   B N   1 
ATOM   4191 C CA  . GLN   B 1 190 ? 39.990  43.040 48.874  1.00 37.55  ? 846  GLN   B CA  1 
ATOM   4192 C C   . GLN   B 1 190 ? 39.509  43.338 47.434  1.00 39.64  ? 846  GLN   B C   1 
ATOM   4193 O O   . GLN   B 1 190 ? 39.203  44.484 47.119  1.00 38.70  ? 846  GLN   B O   1 
ATOM   4194 C CB  . GLN   B 1 190 ? 41.525  43.065 48.964  1.00 39.83  ? 846  GLN   B CB  1 
ATOM   4195 C CG  . GLN   B 1 190 ? 42.058  44.145 49.905  1.00 61.28  ? 846  GLN   B CG  1 
ATOM   4196 C CD  . GLN   B 1 190 ? 43.495  44.527 49.623  1.00 89.61  ? 846  GLN   B CD  1 
ATOM   4197 O OE1 . GLN   B 1 190 ? 44.031  44.315 48.523  1.00 88.00  ? 846  GLN   B OE1 1 
ATOM   4198 N NE2 . GLN   B 1 190 ? 44.152  45.122 50.615  1.00 80.40  ? 846  GLN   B NE2 1 
ATOM   4199 N N   . ARG   B 1 191 ? 39.415  42.296 46.575  1.00 33.64  ? 847  ARG   B N   1 
ATOM   4200 C CA  . ARG   B 1 191 ? 38.941  42.404 45.187  1.00 32.01  ? 847  ARG   B CA  1 
ATOM   4201 C C   . ARG   B 1 191 ? 37.461  42.837 45.167  1.00 36.03  ? 847  ARG   B C   1 
ATOM   4202 O O   . ARG   B 1 191 ? 37.056  43.637 44.318  1.00 33.90  ? 847  ARG   B O   1 
ATOM   4203 C CB  . ARG   B 1 191 ? 39.100  41.045 44.470  1.00 27.32  ? 847  ARG   B CB  1 
ATOM   4204 C CG  . ARG   B 1 191 ? 38.920  41.095 42.955  1.00 28.44  ? 847  ARG   B CG  1 
ATOM   4205 C CD  . ARG   B 1 191 ? 39.073  39.728 42.309  1.00 29.22  ? 847  ARG   B CD  1 
ATOM   4206 N NE  . ARG   B 1 191 ? 37.984  38.823 42.675  1.00 28.40  ? 847  ARG   B NE  1 
ATOM   4207 C CZ  . ARG   B 1 191 ? 37.924  37.534 42.354  1.00 48.10  ? 847  ARG   B CZ  1 
ATOM   4208 N NH1 . ARG   B 1 191 ? 38.894  36.972 41.644  1.00 39.38  ? 847  ARG   B NH1 1 
ATOM   4209 N NH2 . ARG   B 1 191 ? 36.888  36.798 42.735  1.00 32.36  ? 847  ARG   B NH2 1 
ATOM   4210 N N   . TYR   B 1 192 ? 36.673  42.300 46.116  1.00 33.17  ? 848  TYR   B N   1 
ATOM   4211 C CA  . TYR   B 1 192 ? 35.247  42.530 46.256  1.00 33.35  ? 848  TYR   B CA  1 
ATOM   4212 C C   . TYR   B 1 192 ? 34.877  43.912 46.802  1.00 42.17  ? 848  TYR   B C   1 
ATOM   4213 O O   . TYR   B 1 192 ? 33.790  44.387 46.489  1.00 42.75  ? 848  TYR   B O   1 
ATOM   4214 C CB  . TYR   B 1 192 ? 34.624  41.411 47.113  1.00 32.69  ? 848  TYR   B CB  1 
ATOM   4215 C CG  . TYR   B 1 192 ? 33.110  41.443 47.165  1.00 32.21  ? 848  TYR   B CG  1 
ATOM   4216 C CD1 . TYR   B 1 192 ? 32.343  41.047 46.069  1.00 32.84  ? 848  TYR   B CD1 1 
ATOM   4217 C CD2 . TYR   B 1 192 ? 32.441  41.880 48.305  1.00 32.53  ? 848  TYR   B CD2 1 
ATOM   4218 C CE1 . TYR   B 1 192 ? 30.952  41.082 46.110  1.00 30.74  ? 848  TYR   B CE1 1 
ATOM   4219 C CE2 . TYR   B 1 192 ? 31.048  41.898 48.364  1.00 32.78  ? 848  TYR   B CE2 1 
ATOM   4220 C CZ  . TYR   B 1 192 ? 30.309  41.499 47.263  1.00 35.94  ? 848  TYR   B CZ  1 
ATOM   4221 O OH  . TYR   B 1 192 ? 28.939  41.535 47.302  1.00 34.84  ? 848  TYR   B OH  1 
ATOM   4222 N N   . LYS   B 1 193 ? 35.775  44.562 47.588  1.00 40.89  ? 849  LYS   B N   1 
ATOM   4223 C CA  . LYS   B 1 193 ? 35.580  45.869 48.240  1.00 40.96  ? 849  LYS   B CA  1 
ATOM   4224 C C   . LYS   B 1 193 ? 34.803  46.920 47.392  1.00 45.07  ? 849  LYS   B C   1 
ATOM   4225 O O   . LYS   B 1 193 ? 33.846  47.452 47.949  1.00 45.32  ? 849  LYS   B O   1 
ATOM   4226 C CB  . LYS   B 1 193 ? 36.905  46.461 48.760  1.00 43.63  ? 849  LYS   B CB  1 
ATOM   4227 C CG  . LYS   B 1 193 ? 36.709  47.397 49.946  1.00 62.06  ? 849  LYS   B CG  1 
ATOM   4228 C CD  . LYS   B 1 193 ? 38.022  47.936 50.496  1.00 75.67  ? 849  LYS   B CD  1 
ATOM   4229 N N   . PRO   B 1 194 ? 35.101  47.230 46.093  1.00 41.75  ? 850  PRO   B N   1 
ATOM   4230 C CA  . PRO   B 1 194 ? 34.288  48.249 45.382  1.00 41.77  ? 850  PRO   B CA  1 
ATOM   4231 C C   . PRO   B 1 194 ? 32.800  47.911 45.201  1.00 46.85  ? 850  PRO   B C   1 
ATOM   4232 O O   . PRO   B 1 194 ? 32.005  48.793 44.852  1.00 46.59  ? 850  PRO   B O   1 
ATOM   4233 C CB  . PRO   B 1 194 ? 34.989  48.386 44.020  1.00 43.53  ? 850  PRO   B CB  1 
ATOM   4234 C CG  . PRO   B 1 194 ? 36.345  47.813 44.205  1.00 47.52  ? 850  PRO   B CG  1 
ATOM   4235 C CD  . PRO   B 1 194 ? 36.199  46.742 45.231  1.00 43.14  ? 850  PRO   B CD  1 
ATOM   4236 N N   . PHE   B 1 195 ? 32.425  46.641 45.460  1.00 43.11  ? 851  PHE   B N   1 
ATOM   4237 C CA  . PHE   B 1 195 ? 31.075  46.115 45.298  1.00 42.98  ? 851  PHE   B CA  1 
ATOM   4238 C C   . PHE   B 1 195 ? 30.439  45.719 46.632  1.00 51.81  ? 851  PHE   B C   1 
ATOM   4239 O O   . PHE   B 1 195 ? 29.270  45.320 46.644  1.00 51.54  ? 851  PHE   B O   1 
ATOM   4240 C CB  . PHE   B 1 195 ? 31.125  44.892 44.350  1.00 43.94  ? 851  PHE   B CB  1 
ATOM   4241 C CG  . PHE   B 1 195 ? 31.755  45.169 43.004  1.00 44.21  ? 851  PHE   B CG  1 
ATOM   4242 C CD1 . PHE   B 1 195 ? 31.010  45.728 41.970  1.00 46.22  ? 851  PHE   B CD1 1 
ATOM   4243 C CD2 . PHE   B 1 195 ? 33.098  44.891 42.777  1.00 45.37  ? 851  PHE   B CD2 1 
ATOM   4244 C CE1 . PHE   B 1 195 ? 31.603  46.020 40.737  1.00 46.66  ? 851  PHE   B CE1 1 
ATOM   4245 C CE2 . PHE   B 1 195 ? 33.694  45.197 41.549  1.00 47.38  ? 851  PHE   B CE2 1 
ATOM   4246 C CZ  . PHE   B 1 195 ? 32.939  45.740 40.530  1.00 45.39  ? 851  PHE   B CZ  1 
ATOM   4247 N N   . LYS   B 1 196 ? 31.203  45.833 47.752  1.00 51.85  ? 852  LYS   B N   1 
ATOM   4248 C CA  . LYS   B 1 196 ? 30.805  45.423 49.109  1.00 52.90  ? 852  LYS   B CA  1 
ATOM   4249 C C   . LYS   B 1 196 ? 29.552  46.110 49.648  1.00 60.03  ? 852  LYS   B C   1 
ATOM   4250 O O   . LYS   B 1 196 ? 28.821  45.482 50.414  1.00 60.71  ? 852  LYS   B O   1 
ATOM   4251 C CB  . LYS   B 1 196 ? 31.964  45.559 50.111  1.00 55.55  ? 852  LYS   B CB  1 
ATOM   4252 N N   . GLN   B 1 197 ? 29.292  47.366 49.258  1.00 58.30  ? 853  GLN   B N   1 
ATOM   4253 C CA  . GLN   B 1 197 ? 28.110  48.105 49.711  1.00 59.32  ? 853  GLN   B CA  1 
ATOM   4254 C C   . GLN   B 1 197 ? 27.083  48.346 48.586  1.00 64.25  ? 853  GLN   B C   1 
ATOM   4255 O O   . GLN   B 1 197 ? 26.115  49.094 48.795  1.00 64.55  ? 853  GLN   B O   1 
ATOM   4256 C CB  . GLN   B 1 197 ? 28.510  49.426 50.408  1.00 60.99  ? 853  GLN   B CB  1 
ATOM   4257 N N   . LEU   B 1 198 ? 27.274  47.689 47.408  1.00 59.73  ? 854  LEU   B N   1 
ATOM   4258 C CA  . LEU   B 1 198 ? 26.359  47.789 46.263  1.00 58.82  ? 854  LEU   B CA  1 
ATOM   4259 C C   . LEU   B 1 198 ? 24.965  47.281 46.653  1.00 61.48  ? 854  LEU   B C   1 
ATOM   4260 O O   . LEU   B 1 198 ? 24.833  46.478 47.584  1.00 61.37  ? 854  LEU   B O   1 
ATOM   4261 C CB  . LEU   B 1 198 ? 26.890  46.987 45.065  1.00 58.76  ? 854  LEU   B CB  1 
ATOM   4262 C CG  . LEU   B 1 198 ? 26.522  47.483 43.662  1.00 62.86  ? 854  LEU   B CG  1 
ATOM   4263 C CD1 . LEU   B 1 198 ? 27.284  48.748 43.317  1.00 62.91  ? 854  LEU   B CD1 1 
ATOM   4264 C CD2 . LEU   B 1 198 ? 26.834  46.416 42.603  1.00 63.47  ? 854  LEU   B CD2 1 
ATOM   4265 N N   . HIS   B 1 199 ? 23.921  47.795 45.985  1.00 55.02  ? 855  HIS   B N   1 
ATOM   4266 C CA  . HIS   B 1 199 ? 22.571  47.350 46.281  1.00 52.71  ? 855  HIS   B CA  1 
ATOM   4267 C C   . HIS   B 1 199 ? 22.355  45.993 45.621  1.00 52.02  ? 855  HIS   B C   1 
ATOM   4268 O O   . HIS   B 1 199 ? 23.144  45.586 44.760  1.00 51.62  ? 855  HIS   B O   1 
ATOM   4269 C CB  . HIS   B 1 199 ? 21.526  48.401 45.852  1.00 53.34  ? 855  HIS   B CB  1 
ATOM   4270 C CG  . HIS   B 1 199 ? 21.356  48.549 44.373  1.00 56.59  ? 855  HIS   B CG  1 
ATOM   4271 N ND1 . HIS   B 1 199 ? 22.382  49.022 43.575  1.00 58.30  ? 855  HIS   B ND1 1 
ATOM   4272 C CD2 . HIS   B 1 199 ? 20.268  48.312 43.598  1.00 57.81  ? 855  HIS   B CD2 1 
ATOM   4273 C CE1 . HIS   B 1 199 ? 21.896  49.039 42.346  1.00 57.55  ? 855  HIS   B CE1 1 
ATOM   4274 N NE2 . HIS   B 1 199 ? 20.623  48.626 42.313  1.00 57.53  ? 855  HIS   B NE2 1 
ATOM   4275 N N   . ASN   B 1 200 ? 21.343  45.269 46.107  1.00 45.78  ? 856  ASN   B N   1 
ATOM   4276 C CA  . ASN   B 1 200 ? 20.933  43.974 45.619  1.00 43.45  ? 856  ASN   B CA  1 
ATOM   4277 C C   . ASN   B 1 200 ? 22.072  42.924 45.698  1.00 44.24  ? 856  ASN   B C   1 
ATOM   4278 O O   . ASN   B 1 200 ? 22.424  42.300 44.698  1.00 42.82  ? 856  ASN   B O   1 
ATOM   4279 C CB  . ASN   B 1 200 ? 20.345  44.153 44.218  1.00 43.20  ? 856  ASN   B CB  1 
ATOM   4280 C CG  . ASN   B 1 200 ? 19.529  43.028 43.675  1.00 61.64  ? 856  ASN   B CG  1 
ATOM   4281 O OD1 . ASN   B 1 200 ? 18.858  42.284 44.407  1.00 59.47  ? 856  ASN   B OD1 1 
ATOM   4282 N ND2 . ASN   B 1 200 ? 19.556  42.913 42.356  1.00 44.70  ? 856  ASN   B ND2 1 
ATOM   4283 N N   . ARG   B 1 201 ? 22.644  42.739 46.904  1.00 39.33  ? 857  ARG   B N   1 
ATOM   4284 C CA  . ARG   B 1 201 ? 23.667  41.714 47.167  1.00 38.45  ? 857  ARG   B CA  1 
ATOM   4285 C C   . ARG   B 1 201 ? 22.956  40.467 47.691  1.00 40.48  ? 857  ARG   B C   1 
ATOM   4286 O O   . ARG   B 1 201 ? 22.247  40.532 48.703  1.00 39.82  ? 857  ARG   B O   1 
ATOM   4287 C CB  . ARG   B 1 201 ? 24.758  42.196 48.131  1.00 38.06  ? 857  ARG   B CB  1 
ATOM   4288 C CG  . ARG   B 1 201 ? 25.678  43.253 47.524  1.00 45.11  ? 857  ARG   B CG  1 
ATOM   4289 C CD  . ARG   B 1 201 ? 26.581  43.890 48.561  1.00 51.15  ? 857  ARG   B CD  1 
ATOM   4290 N NE  . ARG   B 1 201 ? 25.826  44.644 49.561  1.00 57.84  ? 857  ARG   B NE  1 
ATOM   4291 C CZ  . ARG   B 1 201 ? 25.819  44.374 50.863  1.00 76.00  ? 857  ARG   B CZ  1 
ATOM   4292 N NH1 . ARG   B 1 201 ? 26.551  43.375 51.345  1.00 66.18  ? 857  ARG   B NH1 1 
ATOM   4293 N NH2 . ARG   B 1 201 ? 25.095  45.109 51.694  1.00 62.86  ? 857  ARG   B NH2 1 
ATOM   4294 N N   . ARG   B 1 202 ? 23.075  39.355 46.944  1.00 35.04  ? 858  ARG   B N   1 
ATOM   4295 C CA  . ARG   B 1 202 ? 22.382  38.105 47.259  1.00 33.25  ? 858  ARG   B CA  1 
ATOM   4296 C C   . ARG   B 1 202 ? 23.312  36.933 47.455  1.00 34.36  ? 858  ARG   B C   1 
ATOM   4297 O O   . ARG   B 1 202 ? 24.349  36.847 46.799  1.00 32.61  ? 858  ARG   B O   1 
ATOM   4298 C CB  . ARG   B 1 202 ? 21.347  37.765 46.182  1.00 32.58  ? 858  ARG   B CB  1 
ATOM   4299 C CG  . ARG   B 1 202 ? 20.083  38.577 46.308  1.00 43.15  ? 858  ARG   B CG  1 
ATOM   4300 C CD  . ARG   B 1 202 ? 19.063  38.219 45.255  1.00 49.29  ? 858  ARG   B CD  1 
ATOM   4301 N NE  . ARG   B 1 202 ? 18.317  39.408 44.857  1.00 54.23  ? 858  ARG   B NE  1 
ATOM   4302 C CZ  . ARG   B 1 202 ? 17.315  39.409 43.987  1.00 64.77  ? 858  ARG   B CZ  1 
ATOM   4303 N NH1 . ARG   B 1 202 ? 16.925  38.280 43.410  1.00 53.83  ? 858  ARG   B NH1 1 
ATOM   4304 N NH2 . ARG   B 1 202 ? 16.696  40.541 43.682  1.00 50.26  ? 858  ARG   B NH2 1 
ATOM   4305 N N   . LEU   B 1 203 ? 22.927  36.025 48.362  1.00 30.59  ? 859  LEU   B N   1 
ATOM   4306 C CA  . LEU   B 1 203 ? 23.674  34.813 48.616  1.00 30.24  ? 859  LEU   B CA  1 
ATOM   4307 C C   . LEU   B 1 203 ? 23.056  33.757 47.695  1.00 32.03  ? 859  LEU   B C   1 
ATOM   4308 O O   . LEU   B 1 203 ? 21.885  33.390 47.857  1.00 30.91  ? 859  LEU   B O   1 
ATOM   4309 C CB  . LEU   B 1 203 ? 23.625  34.420 50.101  1.00 30.52  ? 859  LEU   B CB  1 
ATOM   4310 C CG  . LEU   B 1 203 ? 24.610  33.328 50.514  1.00 34.95  ? 859  LEU   B CG  1 
ATOM   4311 C CD1 . LEU   B 1 203 ? 26.040  33.893 50.691  1.00 35.58  ? 859  LEU   B CD1 1 
ATOM   4312 C CD2 . LEU   B 1 203 ? 24.117  32.611 51.759  1.00 34.87  ? 859  LEU   B CD2 1 
ATOM   4313 N N   . LEU   B 1 204 ? 23.825  33.358 46.664  1.00 26.42  ? 860  LEU   B N   1 
ATOM   4314 C CA  . LEU   B 1 204 ? 23.349  32.454 45.627  1.00 25.38  ? 860  LEU   B CA  1 
ATOM   4315 C C   . LEU   B 1 204 ? 24.193  31.217 45.484  1.00 28.91  ? 860  LEU   B C   1 
ATOM   4316 O O   . LEU   B 1 204 ? 25.342  31.194 45.911  1.00 28.84  ? 860  LEU   B O   1 
ATOM   4317 C CB  . LEU   B 1 204 ? 23.249  33.189 44.275  1.00 25.26  ? 860  LEU   B CB  1 
ATOM   4318 C CG  . LEU   B 1 204 ? 22.299  34.413 44.180  1.00 28.58  ? 860  LEU   B CG  1 
ATOM   4319 C CD1 . LEU   B 1 204 ? 22.673  35.283 43.007  1.00 28.44  ? 860  LEU   B CD1 1 
ATOM   4320 C CD2 . LEU   B 1 204 ? 20.825  34.006 44.143  1.00 27.93  ? 860  LEU   B CD2 1 
ATOM   4321 N N   . TRP   B 1 205 ? 23.606  30.185 44.856  1.00 25.16  ? 861  TRP   B N   1 
ATOM   4322 C CA  . TRP   B 1 205 ? 24.213  28.892 44.612  1.00 23.52  ? 861  TRP   B CA  1 
ATOM   4323 C C   . TRP   B 1 205 ? 25.012  28.849 43.323  1.00 24.65  ? 861  TRP   B C   1 
ATOM   4324 O O   . TRP   B 1 205 ? 24.630  29.432 42.311  1.00 22.00  ? 861  TRP   B O   1 
ATOM   4325 C CB  . TRP   B 1 205 ? 23.138  27.802 44.509  1.00 22.44  ? 861  TRP   B CB  1 
ATOM   4326 C CG  . TRP   B 1 205 ? 22.230  27.666 45.684  1.00 24.29  ? 861  TRP   B CG  1 
ATOM   4327 C CD1 . TRP   B 1 205 ? 20.916  28.055 45.767  1.00 27.20  ? 861  TRP   B CD1 1 
ATOM   4328 C CD2 . TRP   B 1 205 ? 22.559  27.075 46.949  1.00 24.23  ? 861  TRP   B CD2 1 
ATOM   4329 N NE1 . TRP   B 1 205 ? 20.402  27.716 46.999  1.00 26.73  ? 861  TRP   B NE1 1 
ATOM   4330 C CE2 . TRP   B 1 205 ? 21.401  27.154 47.761  1.00 28.77  ? 861  TRP   B CE2 1 
ATOM   4331 C CE3 . TRP   B 1 205 ? 23.718  26.469 47.470  1.00 25.30  ? 861  TRP   B CE3 1 
ATOM   4332 C CZ2 . TRP   B 1 205 ? 21.371  26.642 49.064  1.00 28.10  ? 861  TRP   B CZ2 1 
ATOM   4333 C CZ3 . TRP   B 1 205 ? 23.690  25.979 48.762  1.00 27.11  ? 861  TRP   B CZ3 1 
ATOM   4334 C CH2 . TRP   B 1 205 ? 22.533  26.079 49.549  1.00 28.06  ? 861  TRP   B CH2 1 
ATOM   4335 N N   . HIS   B 1 206 ? 26.097  28.065 43.358  1.00 20.05  ? 862  HIS   B N   1 
ATOM   4336 C CA  . HIS   B 1 206 ? 26.921  27.736 42.210  1.00 18.50  ? 862  HIS   B CA  1 
ATOM   4337 C C   . HIS   B 1 206 ? 27.454  26.352 42.438  1.00 22.43  ? 862  HIS   B C   1 
ATOM   4338 O O   . HIS   B 1 206 ? 28.364  26.153 43.250  1.00 21.79  ? 862  HIS   B O   1 
ATOM   4339 C CB  . HIS   B 1 206 ? 28.052  28.731 41.912  1.00 18.10  ? 862  HIS   B CB  1 
ATOM   4340 C CG  . HIS   B 1 206 ? 28.766  28.394 40.631  1.00 20.67  ? 862  HIS   B CG  1 
ATOM   4341 N ND1 . HIS   B 1 206 ? 28.407  28.979 39.432  1.00 21.16  ? 862  HIS   B ND1 1 
ATOM   4342 C CD2 . HIS   B 1 206 ? 29.735  27.470 40.392  1.00 22.03  ? 862  HIS   B CD2 1 
ATOM   4343 C CE1 . HIS   B 1 206 ? 29.198  28.454 38.514  1.00 20.68  ? 862  HIS   B CE1 1 
ATOM   4344 N NE2 . HIS   B 1 206 ? 30.014  27.532 39.039  1.00 21.40  ? 862  HIS   B NE2 1 
ATOM   4345 N N   . GLY   B 1 207 ? 26.827  25.399 41.756  1.00 19.81  ? 863  GLY   B N   1 
ATOM   4346 C CA  . GLY   B 1 207 ? 27.237  24.007 41.771  1.00 19.17  ? 863  GLY   B CA  1 
ATOM   4347 C C   . GLY   B 1 207 ? 28.215  23.780 40.648  1.00 19.93  ? 863  GLY   B C   1 
ATOM   4348 O O   . GLY   B 1 207 ? 28.181  24.477 39.629  1.00 19.88  ? 863  GLY   B O   1 
ATOM   4349 N N   . SER   B 1 208 ? 29.095  22.803 40.833  1.00 16.05  ? 864  SER   B N   1 
ATOM   4350 C CA  . SER   B 1 208 ? 30.105  22.404 39.861  1.00 14.65  ? 864  SER   B CA  1 
ATOM   4351 C C   . SER   B 1 208 ? 30.583  20.995 40.166  1.00 17.57  ? 864  SER   B C   1 
ATOM   4352 O O   . SER   B 1 208 ? 30.292  20.458 41.231  1.00 18.45  ? 864  SER   B O   1 
ATOM   4353 C CB  . SER   B 1 208 ? 31.290  23.375 39.867  1.00 16.70  ? 864  SER   B CB  1 
ATOM   4354 O OG  . SER   B 1 208 ? 31.809  23.472 38.552  1.00 21.43  ? 864  SER   B OG  1 
ATOM   4355 N N   . ARG   B 1 209 ? 31.266  20.369 39.215  1.00 14.00  ? 865  ARG   B N   1 
ATOM   4356 C CA  . ARG   B 1 209 ? 31.788  19.020 39.391  1.00 14.81  ? 865  ARG   B CA  1 
ATOM   4357 C C   . ARG   B 1 209 ? 32.989  19.083 40.366  1.00 22.68  ? 865  ARG   B C   1 
ATOM   4358 O O   . ARG   B 1 209 ? 33.667  20.110 40.441  1.00 22.47  ? 865  ARG   B O   1 
ATOM   4359 C CB  . ARG   B 1 209 ? 32.185  18.398 38.036  1.00 13.83  ? 865  ARG   B CB  1 
ATOM   4360 C CG  . ARG   B 1 209 ? 31.035  18.204 37.035  1.00 18.36  ? 865  ARG   B CG  1 
ATOM   4361 C CD  . ARG   B 1 209 ? 31.607  17.849 35.668  1.00 31.94  ? 865  ARG   B CD  1 
ATOM   4362 N NE  . ARG   B 1 209 ? 30.664  18.086 34.573  1.00 39.01  ? 865  ARG   B NE  1 
ATOM   4363 C CZ  . ARG   B 1 209 ? 30.176  17.141 33.769  1.00 53.59  ? 865  ARG   B CZ  1 
ATOM   4364 N NH1 . ARG   B 1 209 ? 30.536  15.873 33.926  1.00 36.68  ? 865  ARG   B NH1 1 
ATOM   4365 N NH2 . ARG   B 1 209 ? 29.323  17.458 32.806  1.00 46.79  ? 865  ARG   B NH2 1 
ATOM   4366 N N   . THR   B 1 210 ? 33.215  17.997 41.139  1.00 22.35  ? 866  THR   B N   1 
ATOM   4367 C CA  . THR   B 1 210 ? 34.258  17.886 42.164  1.00 22.09  ? 866  THR   B CA  1 
ATOM   4368 C C   . THR   B 1 210 ? 35.634  18.251 41.606  1.00 27.10  ? 866  THR   B C   1 
ATOM   4369 O O   . THR   B 1 210 ? 36.441  18.894 42.289  1.00 26.40  ? 866  THR   B O   1 
ATOM   4370 C CB  . THR   B 1 210 ? 34.214  16.489 42.836  1.00 32.55  ? 866  THR   B CB  1 
ATOM   4371 O OG1 . THR   B 1 210 ? 34.314  15.473 41.843  1.00 38.43  ? 866  THR   B OG1 1 
ATOM   4372 C CG2 . THR   B 1 210 ? 32.958  16.261 43.650  1.00 29.82  ? 866  THR   B CG2 1 
ATOM   4373 N N   . THR   B 1 211 ? 35.848  17.914 40.317  1.00 24.10  ? 867  THR   B N   1 
ATOM   4374 C CA  . THR   B 1 211 ? 37.072  18.151 39.543  1.00 22.47  ? 867  THR   B CA  1 
ATOM   4375 C C   . THR   B 1 211 ? 37.284  19.630 39.172  1.00 24.25  ? 867  THR   B C   1 
ATOM   4376 O O   . THR   B 1 211 ? 38.324  19.956 38.630  1.00 26.75  ? 867  THR   B O   1 
ATOM   4377 C CB  . THR   B 1 211 ? 37.103  17.227 38.315  1.00 19.84  ? 867  THR   B CB  1 
ATOM   4378 O OG1 . THR   B 1 211 ? 35.845  17.298 37.658  1.00 21.84  ? 867  THR   B OG1 1 
ATOM   4379 C CG2 . THR   B 1 211 ? 37.401  15.793 38.675  1.00 15.53  ? 867  THR   B CG2 1 
ATOM   4380 N N   . ASN   B 1 212 ? 36.317  20.509 39.439  1.00 19.63  ? 868  ASN   B N   1 
ATOM   4381 C CA  . ASN   B 1 212 ? 36.420  21.948 39.165  1.00 18.19  ? 868  ASN   B CA  1 
ATOM   4382 C C   . ASN   B 1 212 ? 36.916  22.733 40.389  1.00 21.47  ? 868  ASN   B C   1 
ATOM   4383 O O   . ASN   B 1 212 ? 37.426  23.843 40.250  1.00 19.97  ? 868  ASN   B O   1 
ATOM   4384 C CB  . ASN   B 1 212 ? 35.021  22.510 38.812  1.00 12.42  ? 868  ASN   B CB  1 
ATOM   4385 C CG  . ASN   B 1 212 ? 34.492  22.116 37.461  1.00 28.99  ? 868  ASN   B CG  1 
ATOM   4386 O OD1 . ASN   B 1 212 ? 33.939  21.051 37.272  1.00 30.20  ? 868  ASN   B OD1 1 
ATOM   4387 N ND2 . ASN   B 1 212 ? 34.614  22.981 36.483  1.00 24.04  ? 868  ASN   B ND2 1 
ATOM   4388 N N   . PHE   B 1 213 ? 36.712  22.172 41.584  1.00 18.71  ? 869  PHE   B N   1 
ATOM   4389 C CA  . PHE   B 1 213 ? 36.884  22.818 42.881  1.00 18.34  ? 869  PHE   B CA  1 
ATOM   4390 C C   . PHE   B 1 213 ? 38.312  23.119 43.287  1.00 24.53  ? 869  PHE   B C   1 
ATOM   4391 O O   . PHE   B 1 213 ? 38.496  24.043 44.075  1.00 23.90  ? 869  PHE   B O   1 
ATOM   4392 C CB  . PHE   B 1 213 ? 36.149  22.040 43.956  1.00 19.46  ? 869  PHE   B CB  1 
ATOM   4393 C CG  . PHE   B 1 213 ? 34.705  22.464 43.979  1.00 19.99  ? 869  PHE   B CG  1 
ATOM   4394 C CD1 . PHE   B 1 213 ? 33.759  21.824 43.179  1.00 21.71  ? 869  PHE   B CD1 1 
ATOM   4395 C CD2 . PHE   B 1 213 ? 34.300  23.565 44.726  1.00 21.46  ? 869  PHE   B CD2 1 
ATOM   4396 C CE1 . PHE   B 1 213 ? 32.434  22.251 43.165  1.00 22.79  ? 869  PHE   B CE1 1 
ATOM   4397 C CE2 . PHE   B 1 213 ? 32.979  24.005 44.684  1.00 22.63  ? 869  PHE   B CE2 1 
ATOM   4398 C CZ  . PHE   B 1 213 ? 32.046  23.326 43.933  1.00 20.88  ? 869  PHE   B CZ  1 
ATOM   4399 N N   . ALA   B 1 214 ? 39.320  22.421 42.723  1.00 22.99  ? 870  ALA   B N   1 
ATOM   4400 C CA  . ALA   B 1 214 ? 40.704  22.794 42.987  1.00 24.87  ? 870  ALA   B CA  1 
ATOM   4401 C C   . ALA   B 1 214 ? 40.955  24.095 42.245  1.00 28.45  ? 870  ALA   B C   1 
ATOM   4402 O O   . ALA   B 1 214 ? 41.518  25.031 42.815  1.00 28.16  ? 870  ALA   B O   1 
ATOM   4403 C CB  . ALA   B 1 214 ? 41.662  21.718 42.502  1.00 25.94  ? 870  ALA   B CB  1 
ATOM   4404 N N   . GLY   B 1 215 ? 40.456  24.166 41.016  1.00 25.68  ? 871  GLY   B N   1 
ATOM   4405 C CA  . GLY   B 1 215 ? 40.522  25.377 40.215  1.00 25.83  ? 871  GLY   B CA  1 
ATOM   4406 C C   . GLY   B 1 215 ? 39.788  26.530 40.874  1.00 26.73  ? 871  GLY   B C   1 
ATOM   4407 O O   . GLY   B 1 215 ? 40.382  27.592 41.064  1.00 26.78  ? 871  GLY   B O   1 
ATOM   4408 N N   . ILE   B 1 216 ? 38.505  26.308 41.279  1.00 20.88  ? 872  ILE   B N   1 
ATOM   4409 C CA  . ILE   B 1 216 ? 37.604  27.299 41.901  1.00 19.66  ? 872  ILE   B CA  1 
ATOM   4410 C C   . ILE   B 1 216 ? 38.195  27.864 43.171  1.00 22.06  ? 872  ILE   B C   1 
ATOM   4411 O O   . ILE   B 1 216 ? 38.172  29.066 43.358  1.00 21.16  ? 872  ILE   B O   1 
ATOM   4412 C CB  . ILE   B 1 216 ? 36.146  26.776 42.128  1.00 21.85  ? 872  ILE   B CB  1 
ATOM   4413 C CG1 . ILE   B 1 216 ? 35.431  26.490 40.799  1.00 20.46  ? 872  ILE   B CG1 1 
ATOM   4414 C CG2 . ILE   B 1 216 ? 35.321  27.797 42.953  1.00 23.84  ? 872  ILE   B CG2 1 
ATOM   4415 C CD1 . ILE   B 1 216 ? 34.190  25.543 40.894  1.00 17.90  ? 872  ILE   B CD1 1 
ATOM   4416 N N   . LEU   B 1 217 ? 38.704  27.013 44.054  1.00 20.59  ? 873  LEU   B N   1 
ATOM   4417 C CA  . LEU   B 1 217 ? 39.288  27.526 45.291  1.00 21.57  ? 873  LEU   B CA  1 
ATOM   4418 C C   . LEU   B 1 217 ? 40.577  28.311 45.078  1.00 26.26  ? 873  LEU   B C   1 
ATOM   4419 O O   . LEU   B 1 217 ? 40.797  29.296 45.776  1.00 26.77  ? 873  LEU   B O   1 
ATOM   4420 C CB  . LEU   B 1 217 ? 39.474  26.432 46.340  1.00 21.21  ? 873  LEU   B CB  1 
ATOM   4421 C CG  . LEU   B 1 217 ? 38.176  25.779 46.839  1.00 24.43  ? 873  LEU   B CG  1 
ATOM   4422 C CD1 . LEU   B 1 217 ? 38.465  24.602 47.748  1.00 25.07  ? 873  LEU   B CD1 1 
ATOM   4423 C CD2 . LEU   B 1 217 ? 37.241  26.784 47.498  1.00 23.43  ? 873  LEU   B CD2 1 
ATOM   4424 N N   . SER   B 1 218 ? 41.412  27.918 44.114  1.00 23.73  ? 874  SER   B N   1 
ATOM   4425 C CA  . SER   B 1 218 ? 42.674  28.645 43.909  1.00 23.09  ? 874  SER   B CA  1 
ATOM   4426 C C   . SER   B 1 218 ? 42.553  29.894 43.014  1.00 26.74  ? 874  SER   B C   1 
ATOM   4427 O O   . SER   B 1 218 ? 43.232  30.881 43.277  1.00 26.80  ? 874  SER   B O   1 
ATOM   4428 C CB  . SER   B 1 218 ? 43.755  27.710 43.386  1.00 27.91  ? 874  SER   B CB  1 
ATOM   4429 O OG  . SER   B 1 218 ? 43.641  27.418 42.001  1.00 40.78  ? 874  SER   B OG  1 
ATOM   4430 N N   . GLN   B 1 219 ? 41.701  29.852 41.971  1.00 22.79  ? 875  GLN   B N   1 
ATOM   4431 C CA  . GLN   B 1 219 ? 41.546  30.942 40.990  1.00 21.99  ? 875  GLN   B CA  1 
ATOM   4432 C C   . GLN   B 1 219 ? 40.226  31.676 41.106  1.00 25.22  ? 875  GLN   B C   1 
ATOM   4433 O O   . GLN   B 1 219 ? 40.081  32.751 40.521  1.00 23.80  ? 875  GLN   B O   1 
ATOM   4434 C CB  . GLN   B 1 219 ? 41.673  30.390 39.548  1.00 22.94  ? 875  GLN   B CB  1 
ATOM   4435 C CG  . GLN   B 1 219 ? 42.879  29.477 39.323  1.00 44.78  ? 875  GLN   B CG  1 
ATOM   4436 C CD  . GLN   B 1 219 ? 44.194  30.163 39.003  1.00 62.15  ? 875  GLN   B CD  1 
ATOM   4437 O OE1 . GLN   B 1 219 ? 44.895  29.763 38.067  1.00 51.25  ? 875  GLN   B OE1 1 
ATOM   4438 N NE2 . GLN   B 1 219 ? 44.589  31.186 39.778  1.00 59.67  ? 875  GLN   B NE2 1 
ATOM   4439 N N   . GLY   B 1 220 ? 39.261  31.067 41.812  1.00 20.25  ? 876  GLY   B N   1 
ATOM   4440 C CA  . GLY   B 1 220 ? 37.935  31.621 41.965  1.00 19.60  ? 876  GLY   B CA  1 
ATOM   4441 C C   . GLY   B 1 220 ? 37.080  31.267 40.761  1.00 21.63  ? 876  GLY   B C   1 
ATOM   4442 O O   . GLY   B 1 220 ? 37.558  30.623 39.819  1.00 18.79  ? 876  GLY   B O   1 
ATOM   4443 N N   . LEU   B 1 221 ? 35.789  31.645 40.813  1.00 17.23  ? 877  LEU   B N   1 
ATOM   4444 C CA  . LEU   B 1 221 ? 34.864  31.493 39.696  1.00 16.32  ? 877  LEU   B CA  1 
ATOM   4445 C C   . LEU   B 1 221 ? 35.345  32.534 38.666  1.00 21.03  ? 877  LEU   B C   1 
ATOM   4446 O O   . LEU   B 1 221 ? 35.634  33.679 39.025  1.00 20.11  ? 877  LEU   B O   1 
ATOM   4447 C CB  . LEU   B 1 221 ? 33.415  31.796 40.122  1.00 15.73  ? 877  LEU   B CB  1 
ATOM   4448 C CG  . LEU   B 1 221 ? 32.755  30.859 41.134  1.00 17.98  ? 877  LEU   B CG  1 
ATOM   4449 C CD1 . LEU   B 1 221 ? 31.375  31.382 41.518  1.00 16.43  ? 877  LEU   B CD1 1 
ATOM   4450 C CD2 . LEU   B 1 221 ? 32.680  29.436 40.599  1.00 19.78  ? 877  LEU   B CD2 1 
ATOM   4451 N N   . ARG   B 1 222 ? 35.567  32.082 37.434  1.00 17.72  ? 878  ARG   B N   1 
ATOM   4452 C CA  . ARG   B 1 222 ? 36.081  32.864 36.334  1.00 16.66  ? 878  ARG   B CA  1 
ATOM   4453 C C   . ARG   B 1 222 ? 35.108  32.806 35.176  1.00 21.24  ? 878  ARG   B C   1 
ATOM   4454 O O   . ARG   B 1 222 ? 34.213  31.952 35.143  1.00 20.49  ? 878  ARG   B O   1 
ATOM   4455 C CB  . ARG   B 1 222 ? 37.415  32.278 35.898  1.00 21.28  ? 878  ARG   B CB  1 
ATOM   4456 C CG  . ARG   B 1 222 ? 38.615  32.761 36.725  1.00 29.78  ? 878  ARG   B CG  1 
ATOM   4457 C CD  . ARG   B 1 222 ? 39.857  31.919 36.475  1.00 46.52  ? 878  ARG   B CD  1 
ATOM   4458 N NE  . ARG   B 1 222 ? 39.614  30.487 36.700  1.00 61.58  ? 878  ARG   B NE  1 
ATOM   4459 C CZ  . ARG   B 1 222 ? 40.511  29.520 36.511  1.00 68.89  ? 878  ARG   B CZ  1 
ATOM   4460 N NH1 . ARG   B 1 222 ? 40.183  28.254 36.727  1.00 45.04  ? 878  ARG   B NH1 1 
ATOM   4461 N NH2 . ARG   B 1 222 ? 41.745  29.813 36.113  1.00 52.84  ? 878  ARG   B NH2 1 
ATOM   4462 N N   . ILE   B 1 223 ? 35.252  33.739 34.243  1.00 18.99  ? 879  ILE   B N   1 
ATOM   4463 C CA  . ILE   B 1 223 ? 34.442  33.783 33.023  1.00 18.84  ? 879  ILE   B CA  1 
ATOM   4464 C C   . ILE   B 1 223 ? 35.238  32.982 31.971  1.00 21.74  ? 879  ILE   B C   1 
ATOM   4465 O O   . ILE   B 1 223 ? 36.470  32.857 32.090  1.00 21.04  ? 879  ILE   B O   1 
ATOM   4466 C CB  . ILE   B 1 223 ? 34.175  35.267 32.603  1.00 21.72  ? 879  ILE   B CB  1 
ATOM   4467 C CG1 . ILE   B 1 223 ? 33.197  35.947 33.567  1.00 21.01  ? 879  ILE   B CG1 1 
ATOM   4468 C CG2 . ILE   B 1 223 ? 33.699  35.407 31.158  1.00 22.43  ? 879  ILE   B CG2 1 
ATOM   4469 C CD1 . ILE   B 1 223 ? 33.525  37.314 33.902  1.00 25.14  ? 879  ILE   B CD1 1 
ATOM   4470 N N   . ALA   B 1 224 ? 34.534  32.392 30.986  1.00 17.28  ? 880  ALA   B N   1 
ATOM   4471 C CA  . ALA   B 1 224 ? 35.153  31.666 29.873  1.00 16.44  ? 880  ALA   B CA  1 
ATOM   4472 C C   . ALA   B 1 224 ? 36.150  32.618 29.163  1.00 21.64  ? 880  ALA   B C   1 
ATOM   4473 O O   . ALA   B 1 224 ? 35.908  33.825 29.163  1.00 22.24  ? 880  ALA   B O   1 
ATOM   4474 C CB  . ALA   B 1 224 ? 34.078  31.179 28.910  1.00 16.12  ? 880  ALA   B CB  1 
ATOM   4475 N N   . PRO   B 1 225 ? 37.288  32.130 28.602  1.00 18.83  ? 881  PRO   B N   1 
ATOM   4476 C CA  . PRO   B 1 225 ? 38.303  33.052 28.029  1.00 18.19  ? 881  PRO   B CA  1 
ATOM   4477 C C   . PRO   B 1 225 ? 37.866  33.806 26.771  1.00 22.53  ? 881  PRO   B C   1 
ATOM   4478 O O   . PRO   B 1 225 ? 36.835  33.444 26.206  1.00 20.97  ? 881  PRO   B O   1 
ATOM   4479 C CB  . PRO   B 1 225 ? 39.512  32.134 27.772  1.00 19.37  ? 881  PRO   B CB  1 
ATOM   4480 C CG  . PRO   B 1 225 ? 38.945  30.814 27.622  1.00 24.80  ? 881  PRO   B CG  1 
ATOM   4481 C CD  . PRO   B 1 225 ? 37.767  30.736 28.545  1.00 21.12  ? 881  PRO   B CD  1 
ATOM   4482 N N   . PRO   B 1 226 ? 38.621  34.835 26.294  1.00 20.79  ? 882  PRO   B N   1 
ATOM   4483 C CA  . PRO   B 1 226 ? 38.172  35.581 25.105  1.00 21.97  ? 882  PRO   B CA  1 
ATOM   4484 C C   . PRO   B 1 226 ? 37.952  34.761 23.833  1.00 27.17  ? 882  PRO   B C   1 
ATOM   4485 O O   . PRO   B 1 226 ? 37.120  35.157 23.014  1.00 29.68  ? 882  PRO   B O   1 
ATOM   4486 C CB  . PRO   B 1 226 ? 39.264  36.632 24.913  1.00 23.80  ? 882  PRO   B CB  1 
ATOM   4487 C CG  . PRO   B 1 226 ? 39.861  36.802 26.265  1.00 28.09  ? 882  PRO   B CG  1 
ATOM   4488 C CD  . PRO   B 1 226 ? 39.865  35.423 26.838  1.00 23.55  ? 882  PRO   B CD  1 
ATOM   4489 N N   . GLU   B 1 227 ? 38.668  33.632 23.678  1.00 20.37  ? 883  GLU   B N   1 
ATOM   4490 C CA  . GLU   B 1 227 ? 38.567  32.744 22.516  1.00 20.06  ? 883  GLU   B CA  1 
ATOM   4491 C C   . GLU   B 1 227 ? 37.193  32.073 22.427  1.00 23.47  ? 883  GLU   B C   1 
ATOM   4492 O O   . GLU   B 1 227 ? 36.753  31.768 21.319  1.00 24.40  ? 883  GLU   B O   1 
ATOM   4493 C CB  . GLU   B 1 227 ? 39.680  31.666 22.529  1.00 20.91  ? 883  GLU   B CB  1 
ATOM   4494 C CG  . GLU   B 1 227 ? 41.084  32.173 22.206  1.00 31.65  ? 883  GLU   B CG  1 
ATOM   4495 C CD  . GLU   B 1 227 ? 41.802  32.968 23.286  1.00 44.87  ? 883  GLU   B CD  1 
ATOM   4496 O OE1 . GLU   B 1 227 ? 42.732  33.742 22.950  1.00 39.70  ? 883  GLU   B OE1 1 
ATOM   4497 O OE2 . GLU   B 1 227 ? 41.432  32.821 24.472  1.00 25.64  ? 883  GLU   B OE2 1 
ATOM   4498 N N   . ALA   B 1 228 ? 36.549  31.840 23.589  1.00 18.28  ? 884  ALA   B N   1 
ATOM   4499 C CA  . ALA   B 1 228 ? 35.253  31.195 23.744  1.00 19.26  ? 884  ALA   B CA  1 
ATOM   4500 C C   . ALA   B 1 228 ? 34.098  31.894 22.983  1.00 24.57  ? 884  ALA   B C   1 
ATOM   4501 O O   . ALA   B 1 228 ? 34.010  33.145 23.002  1.00 21.78  ? 884  ALA   B O   1 
ATOM   4502 C CB  . ALA   B 1 228 ? 34.904  31.066 25.213  1.00 20.59  ? 884  ALA   B CB  1 
ATOM   4503 N N   . PRO   B 1 229 ? 33.208  31.105 22.304  1.00 21.16  ? 885  PRO   B N   1 
ATOM   4504 C CA  . PRO   B 1 229 ? 32.109  31.733 21.577  1.00 21.83  ? 885  PRO   B CA  1 
ATOM   4505 C C   . PRO   B 1 229 ? 31.056  32.289 22.547  1.00 27.49  ? 885  PRO   B C   1 
ATOM   4506 O O   . PRO   B 1 229 ? 30.553  31.574 23.421  1.00 25.54  ? 885  PRO   B O   1 
ATOM   4507 C CB  . PRO   B 1 229 ? 31.595  30.604 20.673  1.00 22.85  ? 885  PRO   B CB  1 
ATOM   4508 C CG  . PRO   B 1 229 ? 31.899  29.376 21.408  1.00 25.83  ? 885  PRO   B CG  1 
ATOM   4509 C CD  . PRO   B 1 229 ? 33.171  29.635 22.152  1.00 21.52  ? 885  PRO   B CD  1 
ATOM   4510 N N   . VAL   B 1 230 ? 30.761  33.589 22.417  1.00 25.71  ? 886  VAL   B N   1 
ATOM   4511 C CA  . VAL   B 1 230 ? 29.754  34.241 23.265  1.00 26.80  ? 886  VAL   B CA  1 
ATOM   4512 C C   . VAL   B 1 230 ? 28.345  33.568 23.082  1.00 28.34  ? 886  VAL   B C   1 
ATOM   4513 O O   . VAL   B 1 230 ? 27.585  33.474 24.056  1.00 25.90  ? 886  VAL   B O   1 
ATOM   4514 C CB  . VAL   B 1 230 ? 29.761  35.781 23.100  1.00 32.82  ? 886  VAL   B CB  1 
ATOM   4515 C CG1 . VAL   B 1 230 ? 29.727  36.168 21.640  1.00 33.96  ? 886  VAL   B CG1 1 
ATOM   4516 C CG2 . VAL   B 1 230 ? 28.623  36.470 23.872  1.00 32.63  ? 886  VAL   B CG2 1 
ATOM   4517 N N   . THR   B 1 231 ? 28.082  32.988 21.877  1.00 25.33  ? 887  THR   B N   1 
ATOM   4518 C CA  . THR   B 1 231 ? 26.834  32.283 21.571  1.00 25.61  ? 887  THR   B CA  1 
ATOM   4519 C C   . THR   B 1 231 ? 26.749  30.865 22.166  1.00 29.41  ? 887  THR   B C   1 
ATOM   4520 O O   . THR   B 1 231 ? 25.682  30.276 22.146  1.00 31.64  ? 887  THR   B O   1 
ATOM   4521 C CB  . THR   B 1 231 ? 26.539  32.282 20.074  1.00 35.94  ? 887  THR   B CB  1 
ATOM   4522 O OG1 . THR   B 1 231 ? 27.487  31.459 19.399  1.00 37.76  ? 887  THR   B OG1 1 
ATOM   4523 C CG2 . THR   B 1 231 ? 26.507  33.690 19.480  1.00 32.77  ? 887  THR   B CG2 1 
ATOM   4524 N N   . GLY   B 1 232 ? 27.838  30.356 22.736  1.00 25.60  ? 888  GLY   B N   1 
ATOM   4525 C CA  . GLY   B 1 232 ? 27.861  29.043 23.361  1.00 23.59  ? 888  GLY   B CA  1 
ATOM   4526 C C   . GLY   B 1 232 ? 27.322  29.028 24.776  1.00 25.71  ? 888  GLY   B C   1 
ATOM   4527 O O   . GLY   B 1 232 ? 27.415  28.001 25.443  1.00 27.22  ? 888  GLY   B O   1 
ATOM   4528 N N   . TYR   B 1 233 ? 26.778  30.166 25.256  1.00 20.46  ? 889  TYR   B N   1 
ATOM   4529 C CA  . TYR   B 1 233 ? 26.227  30.371 26.596  1.00 19.50  ? 889  TYR   B CA  1 
ATOM   4530 C C   . TYR   B 1 233 ? 24.981  31.222 26.495  1.00 24.76  ? 889  TYR   B C   1 
ATOM   4531 O O   . TYR   B 1 233 ? 25.008  32.265 25.830  1.00 24.40  ? 889  TYR   B O   1 
ATOM   4532 C CB  . TYR   B 1 233 ? 27.259  31.066 27.512  1.00 20.10  ? 889  TYR   B CB  1 
ATOM   4533 C CG  . TYR   B 1 233 ? 28.669  30.530 27.373  1.00 20.78  ? 889  TYR   B CG  1 
ATOM   4534 C CD1 . TYR   B 1 233 ? 29.090  29.428 28.107  1.00 22.77  ? 889  TYR   B CD1 1 
ATOM   4535 C CD2 . TYR   B 1 233 ? 29.582  31.131 26.511  1.00 21.19  ? 889  TYR   B CD2 1 
ATOM   4536 C CE1 . TYR   B 1 233 ? 30.378  28.915 27.968  1.00 23.74  ? 889  TYR   B CE1 1 
ATOM   4537 C CE2 . TYR   B 1 233 ? 30.871  30.621 26.354  1.00 21.87  ? 889  TYR   B CE2 1 
ATOM   4538 C CZ  . TYR   B 1 233 ? 31.264  29.516 27.088  1.00 26.85  ? 889  TYR   B CZ  1 
ATOM   4539 O OH  . TYR   B 1 233 ? 32.522  29.008 26.929  1.00 26.13  ? 889  TYR   B OH  1 
ATOM   4540 N N   . MET   B 1 234 ? 23.890  30.798 27.169  1.00 21.22  ? 890  MET   B N   1 
ATOM   4541 C CA  . MET   B 1 234 ? 22.571  31.435 27.123  1.00 20.81  ? 890  MET   B CA  1 
ATOM   4542 C C   . MET   B 1 234 ? 22.569  32.957 27.261  1.00 25.41  ? 890  MET   B C   1 
ATOM   4543 O O   . MET   B 1 234 ? 21.899  33.615 26.472  1.00 27.15  ? 890  MET   B O   1 
ATOM   4544 C CB  . MET   B 1 234 ? 21.609  30.808 28.138  1.00 22.80  ? 890  MET   B CB  1 
ATOM   4545 C CG  . MET   B 1 234 ? 20.159  31.074 27.795  1.00 26.41  ? 890  MET   B CG  1 
ATOM   4546 S SD  . MET   B 1 234 ? 19.041  30.330 28.993  1.00 30.11  ? 890  MET   B SD  1 
ATOM   4547 C CE  . MET   B 1 234 ? 17.485  31.295 28.592  1.00 25.85  ? 890  MET   B CE  1 
ATOM   4548 N N   . PHE   B 1 235 ? 23.297  33.505 28.240  1.00 23.04  ? 891  PHE   B N   1 
ATOM   4549 C CA  . PHE   B 1 235 ? 23.376  34.947 28.492  1.00 22.19  ? 891  PHE   B CA  1 
ATOM   4550 C C   . PHE   B 1 235 ? 24.805  35.491 28.294  1.00 24.23  ? 891  PHE   B C   1 
ATOM   4551 O O   . PHE   B 1 235 ? 25.224  36.453 28.937  1.00 23.21  ? 891  PHE   B O   1 
ATOM   4552 C CB  . PHE   B 1 235 ? 22.796  35.278 29.884  1.00 23.66  ? 891  PHE   B CB  1 
ATOM   4553 C CG  . PHE   B 1 235 ? 21.309  35.010 29.991  1.00 24.75  ? 891  PHE   B CG  1 
ATOM   4554 C CD1 . PHE   B 1 235 ? 20.386  35.815 29.326  1.00 27.53  ? 891  PHE   B CD1 1 
ATOM   4555 C CD2 . PHE   B 1 235 ? 20.829  33.942 30.742  1.00 26.24  ? 891  PHE   B CD2 1 
ATOM   4556 C CE1 . PHE   B 1 235 ? 19.008  35.564 29.424  1.00 27.50  ? 891  PHE   B CE1 1 
ATOM   4557 C CE2 . PHE   B 1 235 ? 19.455  33.709 30.856  1.00 28.08  ? 891  PHE   B CE2 1 
ATOM   4558 C CZ  . PHE   B 1 235 ? 18.556  34.518 30.192  1.00 25.87  ? 891  PHE   B CZ  1 
ATOM   4559 N N   . GLY   B 1 236 ? 25.525  34.884 27.368  1.00 19.85  ? 892  GLY   B N   1 
ATOM   4560 C CA  . GLY   B 1 236 ? 26.892  35.284 27.078  1.00 19.03  ? 892  GLY   B CA  1 
ATOM   4561 C C   . GLY   B 1 236 ? 27.890  34.783 28.110  1.00 22.61  ? 892  GLY   B C   1 
ATOM   4562 O O   . GLY   B 1 236 ? 27.608  33.867 28.898  1.00 21.76  ? 892  GLY   B O   1 
ATOM   4563 N N   . LYS   B 1 237 ? 29.062  35.412 28.120  1.00 18.65  ? 893  LYS   B N   1 
ATOM   4564 C CA  . LYS   B 1 237 ? 30.180  35.013 28.964  1.00 17.65  ? 893  LYS   B CA  1 
ATOM   4565 C C   . LYS   B 1 237 ? 30.235  35.758 30.292  1.00 19.32  ? 893  LYS   B C   1 
ATOM   4566 O O   . LYS   B 1 237 ? 30.822  36.824 30.383  1.00 17.95  ? 893  LYS   B O   1 
ATOM   4567 C CB  . LYS   B 1 237 ? 31.515  35.111 28.189  1.00 19.00  ? 893  LYS   B CB  1 
ATOM   4568 C CG  . LYS   B 1 237 ? 31.647  34.080 27.077  1.00 24.80  ? 893  LYS   B CG  1 
ATOM   4569 C CD  . LYS   B 1 237 ? 33.024  34.104 26.408  1.00 25.41  ? 893  LYS   B CD  1 
ATOM   4570 C CE  . LYS   B 1 237 ? 33.184  35.220 25.405  1.00 25.43  ? 893  LYS   B CE  1 
ATOM   4571 N NZ  . LYS   B 1 237 ? 34.543  35.208 24.787  1.00 38.68  ? 893  LYS   B NZ  1 
ATOM   4572 N N   . GLY   B 1 238 ? 29.671  35.129 31.321  1.00 16.42  ? 894  GLY   B N   1 
ATOM   4573 C CA  . GLY   B 1 238 ? 29.653  35.638 32.688  1.00 16.49  ? 894  GLY   B CA  1 
ATOM   4574 C C   . GLY   B 1 238 ? 29.746  34.504 33.694  1.00 20.82  ? 894  GLY   B C   1 
ATOM   4575 O O   . GLY   B 1 238 ? 30.098  33.378 33.316  1.00 20.46  ? 894  GLY   B O   1 
ATOM   4576 N N   . ILE   B 1 239 ? 29.462  34.789 34.988  1.00 16.78  ? 895  ILE   B N   1 
ATOM   4577 C CA  . ILE   B 1 239 ? 29.444  33.770 36.051  1.00 17.48  ? 895  ILE   B CA  1 
ATOM   4578 C C   . ILE   B 1 239 ? 27.973  33.550 36.416  1.00 22.47  ? 895  ILE   B C   1 
ATOM   4579 O O   . ILE   B 1 239 ? 27.284  34.506 36.784  1.00 20.49  ? 895  ILE   B O   1 
ATOM   4580 C CB  . ILE   B 1 239 ? 30.341  34.057 37.294  1.00 20.33  ? 895  ILE   B CB  1 
ATOM   4581 C CG1 . ILE   B 1 239 ? 31.796  34.429 36.895  1.00 21.11  ? 895  ILE   B CG1 1 
ATOM   4582 C CG2 . ILE   B 1 239 ? 30.378  32.827 38.192  1.00 18.38  ? 895  ILE   B CG2 1 
ATOM   4583 C CD1 . ILE   B 1 239 ? 32.594  35.153 37.985  1.00 22.20  ? 895  ILE   B CD1 1 
ATOM   4584 N N   . TYR   B 1 240 ? 27.488  32.309 36.263  1.00 20.23  ? 896  TYR   B N   1 
ATOM   4585 C CA  . TYR   B 1 240 ? 26.083  31.959 36.461  1.00 19.45  ? 896  TYR   B CA  1 
ATOM   4586 C C   . TYR   B 1 240 ? 25.780  31.418 37.861  1.00 22.37  ? 896  TYR   B C   1 
ATOM   4587 O O   . TYR   B 1 240 ? 26.511  30.562 38.365  1.00 21.14  ? 896  TYR   B O   1 
ATOM   4588 C CB  . TYR   B 1 240 ? 25.630  30.948 35.381  1.00 21.39  ? 896  TYR   B CB  1 
ATOM   4589 C CG  . TYR   B 1 240 ? 25.554  31.464 33.954  1.00 22.12  ? 896  TYR   B CG  1 
ATOM   4590 C CD1 . TYR   B 1 240 ? 26.703  31.879 33.278  1.00 23.14  ? 896  TYR   B CD1 1 
ATOM   4591 C CD2 . TYR   B 1 240 ? 24.349  31.442 33.244  1.00 23.61  ? 896  TYR   B CD2 1 
ATOM   4592 C CE1 . TYR   B 1 240 ? 26.647  32.328 31.956  1.00 24.52  ? 896  TYR   B CE1 1 
ATOM   4593 C CE2 . TYR   B 1 240 ? 24.281  31.874 31.915  1.00 24.01  ? 896  TYR   B CE2 1 
ATOM   4594 C CZ  . TYR   B 1 240 ? 25.439  32.313 31.273  1.00 27.46  ? 896  TYR   B CZ  1 
ATOM   4595 O OH  . TYR   B 1 240 ? 25.395  32.737 29.969  1.00 17.54  ? 896  TYR   B OH  1 
ATOM   4596 N N   . PHE   B 1 241 ? 24.693  31.909 38.474  1.00 16.06  ? 897  PHE   B N   1 
ATOM   4597 C CA  . PHE   B 1 241 ? 24.228  31.549 39.824  1.00 16.31  ? 897  PHE   B CA  1 
ATOM   4598 C C   . PHE   B 1 241 ? 22.746  31.239 39.819  1.00 21.87  ? 897  PHE   B C   1 
ATOM   4599 O O   . PHE   B 1 241 ? 22.029  31.727 38.949  1.00 20.96  ? 897  PHE   B O   1 
ATOM   4600 C CB  . PHE   B 1 241 ? 24.474  32.711 40.816  1.00 18.00  ? 897  PHE   B CB  1 
ATOM   4601 C CG  . PHE   B 1 241 ? 25.927  33.042 41.028  1.00 19.02  ? 897  PHE   B CG  1 
ATOM   4602 C CD1 . PHE   B 1 241 ? 26.661  32.412 42.026  1.00 22.26  ? 897  PHE   B CD1 1 
ATOM   4603 C CD2 . PHE   B 1 241 ? 26.578  33.955 40.204  1.00 21.41  ? 897  PHE   B CD2 1 
ATOM   4604 C CE1 . PHE   B 1 241 ? 28.026  32.683 42.192  1.00 22.49  ? 897  PHE   B CE1 1 
ATOM   4605 C CE2 . PHE   B 1 241 ? 27.938  34.232 40.376  1.00 24.36  ? 897  PHE   B CE2 1 
ATOM   4606 C CZ  . PHE   B 1 241 ? 28.655  33.582 41.357  1.00 21.69  ? 897  PHE   B CZ  1 
ATOM   4607 N N   . ALA   B 1 242 ? 22.269  30.471 40.825  1.00 21.83  ? 898  ALA   B N   1 
ATOM   4608 C CA  . ALA   B 1 242 ? 20.853  30.111 40.986  1.00 21.27  ? 898  ALA   B CA  1 
ATOM   4609 C C   . ALA   B 1 242 ? 20.356  30.380 42.408  1.00 23.71  ? 898  ALA   B C   1 
ATOM   4610 O O   . ALA   B 1 242 ? 21.134  30.330 43.349  1.00 20.88  ? 898  ALA   B O   1 
ATOM   4611 C CB  . ALA   B 1 242 ? 20.648  28.633 40.630  1.00 21.90  ? 898  ALA   B CB  1 
ATOM   4612 N N   . ASP   B 1 243 ? 19.038  30.611 42.569  1.00 22.64  ? 899  ASP   B N   1 
ATOM   4613 C CA  . ASP   B 1 243 ? 18.411  30.804 43.885  1.00 22.67  ? 899  ASP   B CA  1 
ATOM   4614 C C   . ASP   B 1 243 ? 17.689  29.531 44.343  1.00 29.11  ? 899  ASP   B C   1 
ATOM   4615 O O   . ASP   B 1 243 ? 17.180  29.491 45.461  1.00 29.97  ? 899  ASP   B O   1 
ATOM   4616 C CB  . ASP   B 1 243 ? 17.509  32.070 43.933  1.00 24.24  ? 899  ASP   B CB  1 
ATOM   4617 C CG  . ASP   B 1 243 ? 16.367  32.170 42.927  1.00 29.86  ? 899  ASP   B CG  1 
ATOM   4618 O OD1 . ASP   B 1 243 ? 15.920  31.124 42.418  1.00 26.27  ? 899  ASP   B OD1 1 
ATOM   4619 O OD2 . ASP   B 1 243 ? 15.880  33.288 42.697  1.00 42.15  ? 899  ASP   B OD2 1 
ATOM   4620 N N   . MET   B 1 244 ? 17.629  28.497 43.458  1.00 26.65  ? 900  MET   B N   1 
ATOM   4621 C CA  . MET   B 1 244 ? 17.043  27.172 43.733  1.00 24.99  ? 900  MET   B CA  1 
ATOM   4622 C C   . MET   B 1 244 ? 18.221  26.206 43.831  1.00 25.59  ? 900  MET   B C   1 
ATOM   4623 O O   . MET   B 1 244 ? 18.871  25.962 42.816  1.00 23.37  ? 900  MET   B O   1 
ATOM   4624 C CB  . MET   B 1 244 ? 16.084  26.696 42.606  1.00 27.61  ? 900  MET   B CB  1 
ATOM   4625 C CG  . MET   B 1 244 ? 14.783  27.515 42.460  1.00 32.76  ? 900  MET   B CG  1 
ATOM   4626 S SD  . MET   B 1 244 ? 13.710  27.512 43.903  1.00 39.18  ? 900  MET   B SD  1 
ATOM   4627 C CE  . MET   B 1 244 ? 12.702  26.101 43.585  1.00 36.72  ? 900  MET   B CE  1 
ATOM   4628 N N   . VAL   B 1 245 ? 18.477  25.651 45.030  1.00 22.35  ? 901  VAL   B N   1 
ATOM   4629 C CA  . VAL   B 1 245 ? 19.583  24.728 45.317  1.00 22.05  ? 901  VAL   B CA  1 
ATOM   4630 C C   . VAL   B 1 245 ? 19.687  23.587 44.287  1.00 25.31  ? 901  VAL   B C   1 
ATOM   4631 O O   . VAL   B 1 245 ? 20.796  23.287 43.847  1.00 24.62  ? 901  VAL   B O   1 
ATOM   4632 C CB  . VAL   B 1 245 ? 19.586  24.190 46.792  1.00 25.82  ? 901  VAL   B CB  1 
ATOM   4633 C CG1 . VAL   B 1 245 ? 18.445  23.203 47.059  1.00 25.51  ? 901  VAL   B CG1 1 
ATOM   4634 C CG2 . VAL   B 1 245 ? 20.948  23.572 47.155  1.00 25.16  ? 901  VAL   B CG2 1 
ATOM   4635 N N   . SER   B 1 246 ? 18.544  22.989 43.894  1.00 21.85  ? 902  SER   B N   1 
ATOM   4636 C CA  . SER   B 1 246 ? 18.449  21.856 42.978  1.00 21.13  ? 902  SER   B CA  1 
ATOM   4637 C C   . SER   B 1 246 ? 18.877  22.223 41.555  1.00 24.32  ? 902  SER   B C   1 
ATOM   4638 O O   . SER   B 1 246 ? 19.464  21.389 40.858  1.00 21.89  ? 902  SER   B O   1 
ATOM   4639 C CB  . SER   B 1 246 ? 17.056  21.225 43.042  1.00 23.57  ? 902  SER   B CB  1 
ATOM   4640 O OG  . SER   B 1 246 ? 15.971  22.069 42.672  1.00 27.43  ? 902  SER   B OG  1 
ATOM   4641 N N   . LYS   B 1 247 ? 18.601  23.480 41.131  1.00 22.05  ? 903  LYS   B N   1 
ATOM   4642 C CA  . LYS   B 1 247 ? 19.039  23.974 39.830  1.00 20.43  ? 903  LYS   B CA  1 
ATOM   4643 C C   . LYS   B 1 247 ? 20.585  23.946 39.767  1.00 23.01  ? 903  LYS   B C   1 
ATOM   4644 O O   . LYS   B 1 247 ? 21.138  23.498 38.763  1.00 23.69  ? 903  LYS   B O   1 
ATOM   4645 C CB  . LYS   B 1 247 ? 18.507  25.380 39.575  1.00 21.00  ? 903  LYS   B CB  1 
ATOM   4646 C CG  . LYS   B 1 247 ? 19.011  25.976 38.255  1.00 16.19  ? 903  LYS   B CG  1 
ATOM   4647 C CD  . LYS   B 1 247 ? 18.113  27.086 37.726  1.00 13.19  ? 903  LYS   B CD  1 
ATOM   4648 C CE  . LYS   B 1 247 ? 18.732  27.643 36.463  1.00 20.05  ? 903  LYS   B CE  1 
ATOM   4649 N NZ  . LYS   B 1 247 ? 17.786  28.523 35.707  1.00 22.80  ? 903  LYS   B NZ  1 
ATOM   4650 N N   . SER   B 1 248 ? 21.279  24.431 40.822  1.00 18.30  ? 904  SER   B N   1 
ATOM   4651 C CA  . SER   B 1 248 ? 22.747  24.424 40.881  1.00 17.63  ? 904  SER   B CA  1 
ATOM   4652 C C   . SER   B 1 248 ? 23.305  23.044 41.145  1.00 21.36  ? 904  SER   B C   1 
ATOM   4653 O O   . SER   B 1 248 ? 24.312  22.693 40.549  1.00 19.42  ? 904  SER   B O   1 
ATOM   4654 C CB  . SER   B 1 248 ? 23.253  25.370 41.958  1.00 20.48  ? 904  SER   B CB  1 
ATOM   4655 O OG  . SER   B 1 248 ? 23.209  26.700 41.476  1.00 24.44  ? 904  SER   B OG  1 
ATOM   4656 N N   . ALA   B 1 249 ? 22.645  22.245 42.012  1.00 20.51  ? 905  ALA   B N   1 
ATOM   4657 C CA  . ALA   B 1 249 ? 23.086  20.885 42.350  1.00 19.98  ? 905  ALA   B CA  1 
ATOM   4658 C C   . ALA   B 1 249 ? 23.058  19.968 41.122  1.00 24.08  ? 905  ALA   B C   1 
ATOM   4659 O O   . ALA   B 1 249 ? 23.801  18.998 41.094  1.00 25.51  ? 905  ALA   B O   1 
ATOM   4660 C CB  . ALA   B 1 249 ? 22.247  20.316 43.482  1.00 20.81  ? 905  ALA   B CB  1 
ATOM   4661 N N   . ASN   B 1 250 ? 22.268  20.323 40.071  1.00 19.61  ? 906  ASN   B N   1 
ATOM   4662 C CA  . ASN   B 1 250 ? 22.225  19.600 38.800  1.00 19.11  ? 906  ASN   B CA  1 
ATOM   4663 C C   . ASN   B 1 250 ? 23.579  19.765 38.072  1.00 24.19  ? 906  ASN   B C   1 
ATOM   4664 O O   . ASN   B 1 250 ? 23.967  18.895 37.305  1.00 23.81  ? 906  ASN   B O   1 
ATOM   4665 C CB  . ASN   B 1 250 ? 21.074  20.091 37.923  1.00 22.47  ? 906  ASN   B CB  1 
ATOM   4666 C CG  . ASN   B 1 250 ? 19.679  19.586 38.270  1.00 37.72  ? 906  ASN   B CG  1 
ATOM   4667 O OD1 . ASN   B 1 250 ? 18.683  20.002 37.670  1.00 36.82  ? 906  ASN   B OD1 1 
ATOM   4668 N ND2 . ASN   B 1 250 ? 19.563  18.675 39.220  1.00 25.42  ? 906  ASN   B ND2 1 
ATOM   4669 N N   . TYR   B 1 251 ? 24.317  20.859 38.360  1.00 22.07  ? 907  TYR   B N   1 
ATOM   4670 C CA  . TYR   B 1 251 ? 25.660  21.115 37.816  1.00 21.04  ? 907  TYR   B CA  1 
ATOM   4671 C C   . TYR   B 1 251 ? 26.775  20.299 38.507  1.00 23.83  ? 907  TYR   B C   1 
ATOM   4672 O O   . TYR   B 1 251 ? 27.907  20.340 38.049  1.00 22.62  ? 907  TYR   B O   1 
ATOM   4673 C CB  . TYR   B 1 251 ? 25.985  22.604 37.800  1.00 21.99  ? 907  TYR   B CB  1 
ATOM   4674 C CG  . TYR   B 1 251 ? 25.305  23.323 36.664  1.00 24.21  ? 907  TYR   B CG  1 
ATOM   4675 C CD1 . TYR   B 1 251 ? 25.818  23.267 35.373  1.00 27.19  ? 907  TYR   B CD1 1 
ATOM   4676 C CD2 . TYR   B 1 251 ? 24.106  24.002 36.861  1.00 25.09  ? 907  TYR   B CD2 1 
ATOM   4677 C CE1 . TYR   B 1 251 ? 25.163  23.879 34.308  1.00 27.65  ? 907  TYR   B CE1 1 
ATOM   4678 C CE2 . TYR   B 1 251 ? 23.440  24.617 35.803  1.00 25.60  ? 907  TYR   B CE2 1 
ATOM   4679 C CZ  . TYR   B 1 251 ? 23.970  24.548 34.529  1.00 33.41  ? 907  TYR   B CZ  1 
ATOM   4680 O OH  . TYR   B 1 251 ? 23.335  25.165 33.485  1.00 37.55  ? 907  TYR   B OH  1 
ATOM   4681 N N   . CYS   B 1 252 ? 26.443  19.532 39.580  1.00 22.51  ? 908  CYS   B N   1 
ATOM   4682 C CA  . CYS   B 1 252 ? 27.391  18.652 40.288  1.00 22.41  ? 908  CYS   B CA  1 
ATOM   4683 C C   . CYS   B 1 252 ? 27.678  17.400 39.471  1.00 30.44  ? 908  CYS   B C   1 
ATOM   4684 O O   . CYS   B 1 252 ? 28.752  16.815 39.619  1.00 29.97  ? 908  CYS   B O   1 
ATOM   4685 C CB  . CYS   B 1 252 ? 26.880  18.291 41.676  1.00 21.93  ? 908  CYS   B CB  1 
ATOM   4686 S SG  . CYS   B 1 252 ? 26.677  19.701 42.782  1.00 25.18  ? 908  CYS   B SG  1 
ATOM   4687 N N   . HIS   B 1 253 ? 26.709  16.987 38.614  1.00 30.57  ? 909  HIS   B N   1 
ATOM   4688 C CA  . HIS   B 1 253 ? 26.773  15.818 37.727  1.00 31.27  ? 909  HIS   B CA  1 
ATOM   4689 C C   . HIS   B 1 253 ? 27.117  14.547 38.511  1.00 37.49  ? 909  HIS   B C   1 
ATOM   4690 O O   . HIS   B 1 253 ? 27.999  13.764 38.135  1.00 37.44  ? 909  HIS   B O   1 
ATOM   4691 C CB  . HIS   B 1 253 ? 27.690  16.070 36.509  1.00 32.13  ? 909  HIS   B CB  1 
ATOM   4692 C CG  . HIS   B 1 253 ? 27.118  17.072 35.548  1.00 35.94  ? 909  HIS   B CG  1 
ATOM   4693 N ND1 . HIS   B 1 253 ? 26.233  16.692 34.540  1.00 37.77  ? 909  HIS   B ND1 1 
ATOM   4694 C CD2 . HIS   B 1 253 ? 27.285  18.417 35.496  1.00 37.53  ? 909  HIS   B CD2 1 
ATOM   4695 C CE1 . HIS   B 1 253 ? 25.901  17.812 33.912  1.00 36.91  ? 909  HIS   B CE1 1 
ATOM   4696 N NE2 . HIS   B 1 253 ? 26.513  18.874 34.448  1.00 37.28  ? 909  HIS   B NE2 1 
ATOM   4697 N N   . THR   B 1 254 ? 26.388  14.368 39.625  1.00 34.91  ? 910  THR   B N   1 
ATOM   4698 C CA  . THR   B 1 254 ? 26.507  13.206 40.492  1.00 34.98  ? 910  THR   B CA  1 
ATOM   4699 C C   . THR   B 1 254 ? 25.646  12.093 39.886  1.00 41.35  ? 910  THR   B C   1 
ATOM   4700 O O   . THR   B 1 254 ? 24.865  12.349 38.968  1.00 40.24  ? 910  THR   B O   1 
ATOM   4701 C CB  . THR   B 1 254 ? 26.071  13.544 41.936  1.00 34.74  ? 910  THR   B CB  1 
ATOM   4702 O OG1 . THR   B 1 254 ? 24.771  14.104 41.911  1.00 32.21  ? 910  THR   B OG1 1 
ATOM   4703 C CG2 . THR   B 1 254 ? 27.053  14.477 42.658  1.00 28.07  ? 910  THR   B CG2 1 
ATOM   4704 N N   . SER   B 1 255 ? 25.811  10.858 40.378  1.00 39.80  ? 911  SER   B N   1 
ATOM   4705 C CA  . SER   B 1 255 ? 25.050  9.698  39.923  1.00 40.24  ? 911  SER   B CA  1 
ATOM   4706 C C   . SER   B 1 255 ? 24.992  8.697  41.049  1.00 43.37  ? 911  SER   B C   1 
ATOM   4707 O O   . SER   B 1 255 ? 25.465  8.981  42.145  1.00 41.89  ? 911  SER   B O   1 
ATOM   4708 C CB  . SER   B 1 255 ? 25.685  9.080  38.674  1.00 45.41  ? 911  SER   B CB  1 
ATOM   4709 O OG  . SER   B 1 255 ? 27.059  8.773  38.876  1.00 60.52  ? 911  SER   B OG  1 
ATOM   4710 N N   . GLN   B 1 256 ? 24.401  7.535  40.787  1.00 42.01  ? 912  GLN   B N   1 
ATOM   4711 C CA  . GLN   B 1 256 ? 24.282  6.431  41.737  1.00 42.83  ? 912  GLN   B CA  1 
ATOM   4712 C C   . GLN   B 1 256 ? 25.683  5.907  42.078  1.00 46.58  ? 912  GLN   B C   1 
ATOM   4713 O O   . GLN   B 1 256 ? 25.909  5.460  43.205  1.00 47.12  ? 912  GLN   B O   1 
ATOM   4714 C CB  . GLN   B 1 256 ? 23.431  5.318  41.112  1.00 44.12  ? 912  GLN   B CB  1 
ATOM   4715 C CG  . GLN   B 1 256 ? 22.254  5.850  40.286  1.00 61.73  ? 912  GLN   B CG  1 
ATOM   4716 C CD  . GLN   B 1 256 ? 20.962  5.857  41.031  1.00 86.77  ? 912  GLN   B CD  1 
ATOM   4717 O OE1 . GLN   B 1 256 ? 20.893  5.576  42.237  1.00 82.38  ? 912  GLN   B OE1 1 
ATOM   4718 N NE2 . GLN   B 1 256 ? 19.869  6.089  40.310  1.00 81.31  ? 912  GLN   B NE2 1 
ATOM   4719 N N   . GLY   B 1 257 ? 26.595  6.005  41.099  1.00 42.43  ? 913  GLY   B N   1 
ATOM   4720 C CA  . GLY   B 1 257 ? 27.992  5.583  41.186  1.00 41.76  ? 913  GLY   B CA  1 
ATOM   4721 C C   . GLY   B 1 257 ? 28.944  6.587  41.801  1.00 44.72  ? 913  GLY   B C   1 
ATOM   4722 O O   . GLY   B 1 257 ? 30.108  6.248  42.040  1.00 45.51  ? 913  GLY   B O   1 
ATOM   4723 N N   . ASP   B 1 258 ? 28.467  7.838  42.044  1.00 38.37  ? 914  ASP   B N   1 
ATOM   4724 C CA  . ASP   B 1 258 ? 29.213  8.940  42.679  1.00 36.86  ? 914  ASP   B CA  1 
ATOM   4725 C C   . ASP   B 1 258 ? 28.177  9.949  43.240  1.00 38.95  ? 914  ASP   B C   1 
ATOM   4726 O O   . ASP   B 1 258 ? 27.899  10.951 42.583  1.00 38.09  ? 914  ASP   B O   1 
ATOM   4727 C CB  . ASP   B 1 258 ? 30.201  9.599  41.686  1.00 38.20  ? 914  ASP   B CB  1 
ATOM   4728 N N   . PRO   B 1 259 ? 27.526  9.669  44.403  1.00 34.48  ? 915  PRO   B N   1 
ATOM   4729 C CA  . PRO   B 1 259 ? 26.449  10.565 44.873  1.00 33.80  ? 915  PRO   B CA  1 
ATOM   4730 C C   . PRO   B 1 259 ? 26.874  11.746 45.753  1.00 35.50  ? 915  PRO   B C   1 
ATOM   4731 O O   . PRO   B 1 259 ? 26.021  12.402 46.339  1.00 34.98  ? 915  PRO   B O   1 
ATOM   4732 C CB  . PRO   B 1 259 ? 25.517  9.607  45.621  1.00 35.03  ? 915  PRO   B CB  1 
ATOM   4733 C CG  . PRO   B 1 259 ? 26.430  8.544  46.155  1.00 39.65  ? 915  PRO   B CG  1 
ATOM   4734 C CD  . PRO   B 1 259 ? 27.676  8.502  45.301  1.00 35.34  ? 915  PRO   B CD  1 
ATOM   4735 N N   . ILE   B 1 260 ? 28.167  12.024 45.842  1.00 30.89  ? 916  ILE   B N   1 
ATOM   4736 C CA  . ILE   B 1 260 ? 28.694  13.113 46.669  1.00 29.18  ? 916  ILE   B CA  1 
ATOM   4737 C C   . ILE   B 1 260 ? 29.056  14.290 45.769  1.00 30.77  ? 916  ILE   B C   1 
ATOM   4738 O O   . ILE   B 1 260 ? 29.889  14.158 44.867  1.00 29.57  ? 916  ILE   B O   1 
ATOM   4739 C CB  . ILE   B 1 260 ? 29.885  12.682 47.603  1.00 31.73  ? 916  ILE   B CB  1 
ATOM   4740 C CG1 . ILE   B 1 260 ? 29.757  11.223 48.135  1.00 31.72  ? 916  ILE   B CG1 1 
ATOM   4741 C CG2 . ILE   B 1 260 ? 30.087  13.683 48.741  1.00 33.07  ? 916  ILE   B CG2 1 
ATOM   4742 C CD1 . ILE   B 1 260 ? 28.520  10.857 49.003  1.00 43.77  ? 916  ILE   B CD1 1 
ATOM   4743 N N   . GLY   B 1 261 ? 28.413  15.427 46.029  1.00 27.27  ? 917  GLY   B N   1 
ATOM   4744 C CA  . GLY   B 1 261 ? 28.630  16.663 45.284  1.00 25.18  ? 917  GLY   B CA  1 
ATOM   4745 C C   . GLY   B 1 261 ? 29.094  17.808 46.150  1.00 25.04  ? 917  GLY   B C   1 
ATOM   4746 O O   . GLY   B 1 261 ? 29.041  17.729 47.379  1.00 23.83  ? 917  GLY   B O   1 
ATOM   4747 N N   . LEU   B 1 262 ? 29.554  18.875 45.496  1.00 20.76  ? 918  LEU   B N   1 
ATOM   4748 C CA  . LEU   B 1 262 ? 30.027  20.112 46.124  1.00 19.36  ? 918  LEU   B CA  1 
ATOM   4749 C C   . LEU   B 1 262 ? 29.289  21.338 45.528  1.00 19.76  ? 918  LEU   B C   1 
ATOM   4750 O O   . LEU   B 1 262 ? 29.110  21.452 44.315  1.00 16.04  ? 918  LEU   B O   1 
ATOM   4751 C CB  . LEU   B 1 262 ? 31.548  20.272 46.014  1.00 19.18  ? 918  LEU   B CB  1 
ATOM   4752 C CG  . LEU   B 1 262 ? 32.445  19.305 46.794  1.00 22.42  ? 918  LEU   B CG  1 
ATOM   4753 C CD1 . LEU   B 1 262 ? 33.928  19.436 46.341  1.00 22.42  ? 918  LEU   B CD1 1 
ATOM   4754 C CD2 . LEU   B 1 262 ? 32.353  19.545 48.288  1.00 22.13  ? 918  LEU   B CD2 1 
ATOM   4755 N N   . ILE   B 1 263 ? 28.844  22.228 46.388  1.00 16.15  ? 919  ILE   B N   1 
ATOM   4756 C CA  . ILE   B 1 263 ? 28.095  23.406 45.939  1.00 18.66  ? 919  ILE   B CA  1 
ATOM   4757 C C   . ILE   B 1 263 ? 28.540  24.636 46.705  1.00 22.44  ? 919  ILE   B C   1 
ATOM   4758 O O   . ILE   B 1 263 ? 28.818  24.551 47.907  1.00 21.08  ? 919  ILE   B O   1 
ATOM   4759 C CB  . ILE   B 1 263 ? 26.559  23.154 46.011  1.00 21.55  ? 919  ILE   B CB  1 
ATOM   4760 C CG1 . ILE   B 1 263 ? 25.745  24.237 45.254  1.00 23.08  ? 919  ILE   B CG1 1 
ATOM   4761 C CG2 . ILE   B 1 263 ? 26.074  22.965 47.444  1.00 22.65  ? 919  ILE   B CG2 1 
ATOM   4762 C CD1 . ILE   B 1 263 ? 24.309  23.855 44.962  1.00 27.76  ? 919  ILE   B CD1 1 
ATOM   4763 N N   . LEU   B 1 264 ? 28.667  25.765 46.001  1.00 17.86  ? 920  LEU   B N   1 
ATOM   4764 C CA  . LEU   B 1 264 ? 29.103  26.989 46.668  1.00 16.87  ? 920  LEU   B CA  1 
ATOM   4765 C C   . LEU   B 1 264 ? 27.921  27.868 46.982  1.00 18.39  ? 920  LEU   B C   1 
ATOM   4766 O O   . LEU   B 1 264 ? 26.882  27.781 46.325  1.00 18.22  ? 920  LEU   B O   1 
ATOM   4767 C CB  . LEU   B 1 264 ? 30.057  27.809 45.773  1.00 16.82  ? 920  LEU   B CB  1 
ATOM   4768 C CG  . LEU   B 1 264 ? 31.355  27.180 45.340  1.00 19.42  ? 920  LEU   B CG  1 
ATOM   4769 C CD1 . LEU   B 1 264 ? 31.824  27.811 44.055  1.00 16.97  ? 920  LEU   B CD1 1 
ATOM   4770 C CD2 . LEU   B 1 264 ? 32.404  27.276 46.465  1.00 21.37  ? 920  LEU   B CD2 1 
ATOM   4771 N N   . LEU   B 1 265 ? 28.121  28.741 47.964  1.00 16.67  ? 921  LEU   B N   1 
ATOM   4772 C CA  . LEU   B 1 265 ? 27.247  29.833 48.369  1.00 19.02  ? 921  LEU   B CA  1 
ATOM   4773 C C   . LEU   B 1 265 ? 28.111  31.079 48.268  1.00 27.72  ? 921  LEU   B C   1 
ATOM   4774 O O   . LEU   B 1 265 ? 29.115  31.208 48.979  1.00 27.71  ? 921  LEU   B O   1 
ATOM   4775 C CB  . LEU   B 1 265 ? 26.674  29.680 49.784  1.00 18.82  ? 921  LEU   B CB  1 
ATOM   4776 C CG  . LEU   B 1 265 ? 25.356  28.936 49.895  1.00 23.57  ? 921  LEU   B CG  1 
ATOM   4777 C CD1 . LEU   B 1 265 ? 24.996  28.716 51.360  1.00 23.70  ? 921  LEU   B CD1 1 
ATOM   4778 C CD2 . LEU   B 1 265 ? 24.209  29.679 49.151  1.00 26.14  ? 921  LEU   B CD2 1 
ATOM   4779 N N   . GLY   B 1 266 ? 27.777  31.936 47.312  1.00 26.51  ? 922  GLY   B N   1 
ATOM   4780 C CA  . GLY   B 1 266 ? 28.559  33.141 47.084  1.00 26.33  ? 922  GLY   B CA  1 
ATOM   4781 C C   . GLY   B 1 266 ? 27.752  34.404 47.261  1.00 30.36  ? 922  GLY   B C   1 
ATOM   4782 O O   . GLY   B 1 266 ? 26.556  34.432 46.949  1.00 30.80  ? 922  GLY   B O   1 
ATOM   4783 N N   . GLU   B 1 267 ? 28.399  35.451 47.774  1.00 25.27  ? 923  GLU   B N   1 
ATOM   4784 C CA  . GLU   B 1 267 ? 27.748  36.738 47.886  1.00 25.45  ? 923  GLU   B CA  1 
ATOM   4785 C C   . GLU   B 1 267 ? 28.023  37.414 46.546  1.00 29.90  ? 923  GLU   B C   1 
ATOM   4786 O O   . GLU   B 1 267 ? 29.183  37.613 46.165  1.00 27.53  ? 923  GLU   B O   1 
ATOM   4787 C CB  . GLU   B 1 267 ? 28.276  37.570 49.058  1.00 26.37  ? 923  GLU   B CB  1 
ATOM   4788 C CG  . GLU   B 1 267 ? 27.674  38.970 49.063  1.00 32.50  ? 923  GLU   B CG  1 
ATOM   4789 C CD  . GLU   B 1 267 ? 28.269  39.958 50.046  1.00 45.43  ? 923  GLU   B CD  1 
ATOM   4790 O OE1 . GLU   B 1 267 ? 28.925  39.514 51.015  1.00 42.20  ? 923  GLU   B OE1 1 
ATOM   4791 O OE2 . GLU   B 1 267 ? 28.060  41.179 49.862  1.00 46.93  ? 923  GLU   B OE2 1 
ATOM   4792 N N   . VAL   B 1 268 ? 26.936  37.713 45.821  1.00 28.10  ? 924  VAL   B N   1 
ATOM   4793 C CA  . VAL   B 1 268 ? 26.983  38.281 44.488  1.00 28.19  ? 924  VAL   B CA  1 
ATOM   4794 C C   . VAL   B 1 268 ? 26.409  39.696 44.502  1.00 33.82  ? 924  VAL   B C   1 
ATOM   4795 O O   . VAL   B 1 268 ? 25.258  39.905 44.901  1.00 32.07  ? 924  VAL   B O   1 
ATOM   4796 C CB  . VAL   B 1 268 ? 26.252  37.346 43.474  1.00 31.99  ? 924  VAL   B CB  1 
ATOM   4797 C CG1 . VAL   B 1 268 ? 26.422  37.835 42.041  1.00 31.71  ? 924  VAL   B CG1 1 
ATOM   4798 C CG2 . VAL   B 1 268 ? 26.718  35.890 43.605  1.00 31.48  ? 924  VAL   B CG2 1 
ATOM   4799 N N   . ALA   B 1 269 ? 27.234  40.670 44.061  1.00 32.27  ? 925  ALA   B N   1 
ATOM   4800 C CA  . ALA   B 1 269 ? 26.843  42.074 43.954  1.00 32.27  ? 925  ALA   B CA  1 
ATOM   4801 C C   . ALA   B 1 269 ? 26.103  42.212 42.622  1.00 35.32  ? 925  ALA   B C   1 
ATOM   4802 O O   . ALA   B 1 269 ? 26.731  42.338 41.569  1.00 34.67  ? 925  ALA   B O   1 
ATOM   4803 C CB  . ALA   B 1 269 ? 28.075  42.963 43.995  1.00 32.98  ? 925  ALA   B CB  1 
ATOM   4804 N N   . LEU   B 1 270 ? 24.760  42.093 42.672  1.00 31.93  ? 926  LEU   B N   1 
ATOM   4805 C CA  . LEU   B 1 270 ? 23.901  42.130 41.492  1.00 31.03  ? 926  LEU   B CA  1 
ATOM   4806 C C   . LEU   B 1 270 ? 23.615  43.527 40.998  1.00 36.16  ? 926  LEU   B C   1 
ATOM   4807 O O   . LEU   B 1 270 ? 23.480  43.726 39.787  1.00 34.70  ? 926  LEU   B O   1 
ATOM   4808 C CB  . LEU   B 1 270 ? 22.583  41.344 41.709  1.00 30.41  ? 926  LEU   B CB  1 
ATOM   4809 C CG  . LEU   B 1 270 ? 22.709  39.844 42.006  1.00 32.86  ? 926  LEU   B CG  1 
ATOM   4810 C CD1 . LEU   B 1 270 ? 21.380  39.277 42.496  1.00 31.99  ? 926  LEU   B CD1 1 
ATOM   4811 C CD2 . LEU   B 1 270 ? 23.205  39.069 40.776  1.00 33.86  ? 926  LEU   B CD2 1 
ATOM   4812 N N   . GLY   B 1 271 ? 23.479  44.470 41.927  1.00 35.02  ? 927  GLY   B N   1 
ATOM   4813 C CA  . GLY   B 1 271 ? 23.163  45.857 41.615  1.00 35.20  ? 927  GLY   B CA  1 
ATOM   4814 C C   . GLY   B 1 271 ? 21.877  45.973 40.832  1.00 40.16  ? 927  GLY   B C   1 
ATOM   4815 O O   . GLY   B 1 271 ? 20.876  45.353 41.201  1.00 40.47  ? 927  GLY   B O   1 
ATOM   4816 N N   . ASN   B 1 272 ? 21.913  46.747 39.725  1.00 37.01  ? 928  ASN   B N   1 
ATOM   4817 C CA  . ASN   B 1 272 ? 20.779  46.938 38.824  1.00 37.05  ? 928  ASN   B CA  1 
ATOM   4818 C C   . ASN   B 1 272 ? 20.742  45.758 37.842  1.00 39.73  ? 928  ASN   B C   1 
ATOM   4819 O O   . ASN   B 1 272 ? 21.649  45.610 37.013  1.00 40.52  ? 928  ASN   B O   1 
ATOM   4820 C CB  . ASN   B 1 272 ? 20.907  48.291 38.098  1.00 43.22  ? 928  ASN   B CB  1 
ATOM   4821 C CG  . ASN   B 1 272 ? 19.633  48.875 37.542  1.00 72.35  ? 928  ASN   B CG  1 
ATOM   4822 O OD1 . ASN   B 1 272 ? 18.748  48.176 37.032  1.00 73.09  ? 928  ASN   B OD1 1 
ATOM   4823 N ND2 . ASN   B 1 272 ? 19.532  50.191 37.599  1.00 66.59  ? 928  ASN   B ND2 1 
ATOM   4824 N N   . MET   B 1 273 ? 19.713  44.888 37.975  1.00 33.47  ? 929  MET   B N   1 
ATOM   4825 C CA  . MET   B 1 273 ? 19.539  43.682 37.156  1.00 31.79  ? 929  MET   B CA  1 
ATOM   4826 C C   . MET   B 1 273 ? 18.858  43.948 35.825  1.00 35.49  ? 929  MET   B C   1 
ATOM   4827 O O   . MET   B 1 273 ? 17.819  44.616 35.772  1.00 36.12  ? 929  MET   B O   1 
ATOM   4828 C CB  . MET   B 1 273 ? 18.741  42.599 37.908  1.00 33.44  ? 929  MET   B CB  1 
ATOM   4829 C CG  . MET   B 1 273 ? 19.354  42.176 39.225  1.00 35.90  ? 929  MET   B CG  1 
ATOM   4830 S SD  . MET   B 1 273 ? 18.385  40.949 40.153  1.00 38.91  ? 929  MET   B SD  1 
ATOM   4831 C CE  . MET   B 1 273 ? 16.805  41.824 40.418  1.00 36.34  ? 929  MET   B CE  1 
ATOM   4832 N N   . TYR   B 1 274 ? 19.425  43.386 34.754  1.00 30.24  ? 930  TYR   B N   1 
ATOM   4833 C CA  . TYR   B 1 274 ? 18.874  43.449 33.409  1.00 29.44  ? 930  TYR   B CA  1 
ATOM   4834 C C   . TYR   B 1 274 ? 18.057  42.153 33.267  1.00 33.20  ? 930  TYR   B C   1 
ATOM   4835 O O   . TYR   B 1 274 ? 18.609  41.054 33.255  1.00 29.96  ? 930  TYR   B O   1 
ATOM   4836 C CB  . TYR   B 1 274 ? 20.015  43.592 32.385  1.00 29.88  ? 930  TYR   B CB  1 
ATOM   4837 C CG  . TYR   B 1 274 ? 19.590  43.645 30.937  1.00 31.09  ? 930  TYR   B CG  1 
ATOM   4838 C CD1 . TYR   B 1 274 ? 18.481  44.387 30.539  1.00 33.05  ? 930  TYR   B CD1 1 
ATOM   4839 C CD2 . TYR   B 1 274 ? 20.346  43.025 29.947  1.00 31.63  ? 930  TYR   B CD2 1 
ATOM   4840 C CE1 . TYR   B 1 274 ? 18.077  44.425 29.207  1.00 33.17  ? 930  TYR   B CE1 1 
ATOM   4841 C CE2 . TYR   B 1 274 ? 19.969  43.079 28.608  1.00 31.69  ? 930  TYR   B CE2 1 
ATOM   4842 C CZ  . TYR   B 1 274 ? 18.835  43.783 28.241  1.00 38.53  ? 930  TYR   B CZ  1 
ATOM   4843 O OH  . TYR   B 1 274 ? 18.449  43.833 26.921  1.00 39.78  ? 930  TYR   B OH  1 
ATOM   4844 N N   . GLU   B 1 275 ? 16.721  42.294 33.321  1.00 32.14  ? 931  GLU   B N   1 
ATOM   4845 C CA  . GLU   B 1 275 ? 15.750  41.186 33.356  1.00 32.11  ? 931  GLU   B CA  1 
ATOM   4846 C C   . GLU   B 1 275 ? 15.397  40.649 31.982  1.00 35.51  ? 931  GLU   B C   1 
ATOM   4847 O O   . GLU   B 1 275 ? 14.876  41.393 31.147  1.00 35.10  ? 931  GLU   B O   1 
ATOM   4848 C CB  . GLU   B 1 275 ? 14.491  41.584 34.152  1.00 33.51  ? 931  GLU   B CB  1 
ATOM   4849 C CG  . GLU   B 1 275 ? 14.795  41.871 35.618  1.00 44.94  ? 931  GLU   B CG  1 
ATOM   4850 C CD  . GLU   B 1 275 ? 13.622  41.998 36.573  1.00 67.36  ? 931  GLU   B CD  1 
ATOM   4851 O OE1 . GLU   B 1 275 ? 12.455  41.991 36.117  1.00 70.55  ? 931  GLU   B OE1 1 
ATOM   4852 O OE2 . GLU   B 1 275 ? 13.881  42.110 37.792  1.00 59.37  ? 931  GLU   B OE2 1 
ATOM   4853 N N   . LEU   B 1 276 ? 15.710  39.357 31.744  1.00 31.32  ? 932  LEU   B N   1 
ATOM   4854 C CA  . LEU   B 1 276 ? 15.474  38.692 30.464  1.00 30.91  ? 932  LEU   B CA  1 
ATOM   4855 C C   . LEU   B 1 276 ? 14.761  37.349 30.637  1.00 33.37  ? 932  LEU   B C   1 
ATOM   4856 O O   . LEU   B 1 276 ? 14.991  36.653 31.617  1.00 32.35  ? 932  LEU   B O   1 
ATOM   4857 C CB  . LEU   B 1 276 ? 16.814  38.490 29.727  1.00 31.17  ? 932  LEU   B CB  1 
ATOM   4858 C CG  . LEU   B 1 276 ? 17.627  39.762 29.387  1.00 35.70  ? 932  LEU   B CG  1 
ATOM   4859 C CD1 . LEU   B 1 276 ? 19.085  39.423 29.131  1.00 35.17  ? 932  LEU   B CD1 1 
ATOM   4860 C CD2 . LEU   B 1 276 ? 16.992  40.537 28.221  1.00 37.63  ? 932  LEU   B CD2 1 
ATOM   4861 N N   . LYS   B 1 277 ? 13.939  36.969 29.660  1.00 29.59  ? 933  LYS   B N   1 
ATOM   4862 C CA  . LYS   B 1 277 ? 13.176  35.715 29.648  1.00 29.66  ? 933  LYS   B CA  1 
ATOM   4863 C C   . LYS   B 1 277 ? 13.755  34.666 28.663  1.00 35.34  ? 933  LYS   B C   1 
ATOM   4864 O O   . LYS   B 1 277 ? 13.367  33.493 28.734  1.00 34.95  ? 933  LYS   B O   1 
ATOM   4865 C CB  . LYS   B 1 277 ? 11.732  35.999 29.219  1.00 31.13  ? 933  LYS   B CB  1 
ATOM   4866 C CG  . LYS   B 1 277 ? 10.915  36.898 30.141  1.00 33.15  ? 933  LYS   B CG  1 
ATOM   4867 C CD  . LYS   B 1 277 ? 9.526   37.110 29.550  1.00 41.10  ? 933  LYS   B CD  1 
ATOM   4868 C CE  . LYS   B 1 277 ? 8.699   38.083 30.349  1.00 48.44  ? 933  LYS   B CE  1 
ATOM   4869 N NZ  . LYS   B 1 277 ? 7.330   38.242 29.793  1.00 54.55  ? 933  LYS   B NZ  1 
ATOM   4870 N N   . HIS   B 1 278 ? 14.603  35.104 27.701  1.00 30.66  ? 934  HIS   B N   1 
ATOM   4871 C CA  . HIS   B 1 278 ? 15.149  34.282 26.613  1.00 30.65  ? 934  HIS   B CA  1 
ATOM   4872 C C   . HIS   B 1 278 ? 16.593  34.612 26.356  1.00 33.15  ? 934  HIS   B C   1 
ATOM   4873 O O   . HIS   B 1 278 ? 17.051  35.682 26.766  1.00 32.50  ? 934  HIS   B O   1 
ATOM   4874 C CB  . HIS   B 1 278 ? 14.344  34.519 25.318  1.00 32.34  ? 934  HIS   B CB  1 
ATOM   4875 C CG  . HIS   B 1 278 ? 12.937  34.044 25.398  1.00 37.01  ? 934  HIS   B CG  1 
ATOM   4876 N ND1 . HIS   B 1 278 ? 11.954  34.774 26.028  1.00 39.57  ? 934  HIS   B ND1 1 
ATOM   4877 C CD2 . HIS   B 1 278 ? 12.400  32.886 24.955  1.00 39.68  ? 934  HIS   B CD2 1 
ATOM   4878 C CE1 . HIS   B 1 278 ? 10.858  34.041 25.947  1.00 39.73  ? 934  HIS   B CE1 1 
ATOM   4879 N NE2 . HIS   B 1 278 ? 11.072  32.910 25.286  1.00 40.17  ? 934  HIS   B NE2 1 
ATOM   4880 N N   . ALA   B 1 279 ? 17.305  33.709 25.644  1.00 28.95  ? 935  ALA   B N   1 
ATOM   4881 C CA  . ALA   B 1 279 ? 18.731  33.850 25.336  1.00 27.69  ? 935  ALA   B CA  1 
ATOM   4882 C C   . ALA   B 1 279 ? 19.092  35.200 24.751  1.00 32.94  ? 935  ALA   B C   1 
ATOM   4883 O O   . ALA   B 1 279 ? 18.393  35.736 23.888  1.00 31.63  ? 935  ALA   B O   1 
ATOM   4884 C CB  . ALA   B 1 279 ? 19.199  32.735 24.417  1.00 28.35  ? 935  ALA   B CB  1 
ATOM   4885 N N   . SER   B 1 280 ? 20.163  35.773 25.285  1.00 31.21  ? 936  SER   B N   1 
ATOM   4886 C CA  . SER   B 1 280 ? 20.711  37.048 24.863  1.00 30.07  ? 936  SER   B CA  1 
ATOM   4887 C C   . SER   B 1 280 ? 22.237  36.919 25.008  1.00 29.13  ? 936  SER   B C   1 
ATOM   4888 O O   . SER   B 1 280 ? 22.768  37.008 26.105  1.00 26.31  ? 936  SER   B O   1 
ATOM   4889 C CB  . SER   B 1 280 ? 20.125  38.179 25.705  1.00 35.77  ? 936  SER   B CB  1 
ATOM   4890 O OG  . SER   B 1 280 ? 20.727  39.431 25.418  1.00 47.50  ? 936  SER   B OG  1 
ATOM   4891 N N   . HIS   B 1 281 ? 22.915  36.610 23.889  1.00 25.86  ? 937  HIS   B N   1 
ATOM   4892 C CA  . HIS   B 1 281 ? 24.365  36.371 23.801  1.00 24.76  ? 937  HIS   B CA  1 
ATOM   4893 C C   . HIS   B 1 281 ? 25.139  37.674 23.795  1.00 32.12  ? 937  HIS   B C   1 
ATOM   4894 O O   . HIS   B 1 281 ? 25.648  38.102 22.753  1.00 31.71  ? 937  HIS   B O   1 
ATOM   4895 C CB  . HIS   B 1 281 ? 24.690  35.488 22.585  1.00 24.11  ? 937  HIS   B CB  1 
ATOM   4896 C CG  . HIS   B 1 281 ? 23.866  34.239 22.549  1.00 25.77  ? 937  HIS   B CG  1 
ATOM   4897 N ND1 . HIS   B 1 281 ? 24.053  33.232 23.465  1.00 26.77  ? 937  HIS   B ND1 1 
ATOM   4898 C CD2 . HIS   B 1 281 ? 22.839  33.900 21.738  1.00 26.05  ? 937  HIS   B CD2 1 
ATOM   4899 C CE1 . HIS   B 1 281 ? 23.153  32.307 23.178  1.00 25.32  ? 937  HIS   B CE1 1 
ATOM   4900 N NE2 . HIS   B 1 281 ? 22.402  32.665 22.147  1.00 25.29  ? 937  HIS   B NE2 1 
ATOM   4901 N N   . ILE   B 1 282 ? 25.215  38.313 24.983  1.00 32.49  ? 938  ILE   B N   1 
ATOM   4902 C CA  . ILE   B 1 282 ? 25.851  39.624 25.199  1.00 33.43  ? 938  ILE   B CA  1 
ATOM   4903 C C   . ILE   B 1 282 ? 27.298  39.559 25.641  1.00 40.18  ? 938  ILE   B C   1 
ATOM   4904 O O   . ILE   B 1 282 ? 27.694  38.658 26.381  1.00 37.40  ? 938  ILE   B O   1 
ATOM   4905 C CB  . ILE   B 1 282 ? 25.034  40.524 26.163  1.00 36.05  ? 938  ILE   B CB  1 
ATOM   4906 C CG1 . ILE   B 1 282 ? 24.827  39.860 27.546  1.00 35.15  ? 938  ILE   B CG1 1 
ATOM   4907 C CG2 . ILE   B 1 282 ? 23.703  40.972 25.514  1.00 36.77  ? 938  ILE   B CG2 1 
ATOM   4908 C CD1 . ILE   B 1 282 ? 24.857  40.811 28.673  1.00 35.87  ? 938  ILE   B CD1 1 
ATOM   4909 N N   . SER   B 1 283 ? 28.072  40.582 25.196  1.00 42.66  ? 939  SER   B N   1 
ATOM   4910 C CA  . SER   B 1 283 ? 29.501  40.782 25.473  1.00 44.30  ? 939  SER   B CA  1 
ATOM   4911 C C   . SER   B 1 283 ? 29.691  41.796 26.622  1.00 48.98  ? 939  SER   B C   1 
ATOM   4912 O O   . SER   B 1 283 ? 30.576  41.639 27.472  1.00 48.18  ? 939  SER   B O   1 
ATOM   4913 C CB  . SER   B 1 283 ? 30.216  41.289 24.218  1.00 49.03  ? 939  SER   B CB  1 
ATOM   4914 O OG  . SER   B 1 283 ? 30.040  40.454 23.086  1.00 55.67  ? 939  SER   B OG  1 
ATOM   4915 N N   . LYS   B 1 284 ? 28.850  42.838 26.623  1.00 45.39  ? 940  LYS   B N   1 
ATOM   4916 C CA  . LYS   B 1 284 ? 28.864  43.914 27.602  1.00 44.78  ? 940  LYS   B CA  1 
ATOM   4917 C C   . LYS   B 1 284 ? 27.406  44.255 27.971  1.00 46.87  ? 940  LYS   B C   1 
ATOM   4918 O O   . LYS   B 1 284 ? 26.523  44.253 27.099  1.00 46.43  ? 940  LYS   B O   1 
ATOM   4919 C CB  . LYS   B 1 284 ? 29.622  45.125 27.009  1.00 47.27  ? 940  LYS   B CB  1 
ATOM   4920 C CG  . LYS   B 1 284 ? 29.594  46.432 27.818  1.00 61.45  ? 940  LYS   B CG  1 
ATOM   4921 C CD  . LYS   B 1 284 ? 30.555  47.497 27.280  1.00 69.24  ? 940  LYS   B CD  1 
ATOM   4922 C CE  . LYS   B 1 284 ? 30.035  48.363 26.145  1.00 81.26  ? 940  LYS   B CE  1 
ATOM   4923 N NZ  . LYS   B 1 284 ? 31.086  49.278 25.616  1.00 90.80  ? 940  LYS   B NZ  1 
ATOM   4924 N N   . LEU   B 1 285 ? 27.168  44.533 29.265  1.00 40.84  ? 941  LEU   B N   1 
ATOM   4925 C CA  . LEU   B 1 285 ? 25.851  44.918 29.772  1.00 39.58  ? 941  LEU   B CA  1 
ATOM   4926 C C   . LEU   B 1 285 ? 25.504  46.329 29.316  1.00 44.39  ? 941  LEU   B C   1 
ATOM   4927 O O   . LEU   B 1 285 ? 26.418  47.153 29.208  1.00 44.59  ? 941  LEU   B O   1 
ATOM   4928 C CB  . LEU   B 1 285 ? 25.854  44.928 31.311  1.00 38.54  ? 941  LEU   B CB  1 
ATOM   4929 C CG  . LEU   B 1 285 ? 25.732  43.625 32.029  1.00 41.05  ? 941  LEU   B CG  1 
ATOM   4930 C CD1 . LEU   B 1 285 ? 26.273  43.762 33.410  1.00 39.96  ? 941  LEU   B CD1 1 
ATOM   4931 C CD2 . LEU   B 1 285 ? 24.296  43.177 32.083  1.00 43.58  ? 941  LEU   B CD2 1 
ATOM   4932 N N   . PRO   B 1 286 ? 24.198  46.681 29.168  1.00 41.59  ? 942  PRO   B N   1 
ATOM   4933 C CA  . PRO   B 1 286 ? 23.859  48.090 28.867  1.00 41.25  ? 942  PRO   B CA  1 
ATOM   4934 C C   . PRO   B 1 286 ? 24.244  48.984 30.048  1.00 44.97  ? 942  PRO   B C   1 
ATOM   4935 O O   . PRO   B 1 286 ? 24.225  48.511 31.187  1.00 43.86  ? 942  PRO   B O   1 
ATOM   4936 C CB  . PRO   B 1 286 ? 22.337  48.076 28.678  1.00 43.13  ? 942  PRO   B CB  1 
ATOM   4937 C CG  . PRO   B 1 286 ? 21.924  46.643 28.653  1.00 47.47  ? 942  PRO   B CG  1 
ATOM   4938 C CD  . PRO   B 1 286 ? 22.983  45.849 29.332  1.00 43.33  ? 942  PRO   B CD  1 
ATOM   4939 N N   . LYS   B 1 287 ? 24.644  50.245 29.778  1.00 42.65  ? 943  LYS   B N   1 
ATOM   4940 C CA  . LYS   B 1 287 ? 25.046  51.251 30.788  1.00 43.65  ? 943  LYS   B CA  1 
ATOM   4941 C C   . LYS   B 1 287 ? 24.029  51.345 31.925  1.00 46.83  ? 943  LYS   B C   1 
ATOM   4942 O O   . LYS   B 1 287 ? 22.820  51.412 31.678  1.00 46.06  ? 943  LYS   B O   1 
ATOM   4943 C CB  . LYS   B 1 287 ? 25.222  52.639 30.128  1.00 48.16  ? 943  LYS   B CB  1 
ATOM   4944 C CG  . LYS   B 1 287 ? 26.674  53.027 29.829  1.00 67.11  ? 943  LYS   B CG  1 
ATOM   4945 C CD  . LYS   B 1 287 ? 26.798  53.944 28.585  1.00 78.34  ? 943  LYS   B CD  1 
ATOM   4946 C CE  . LYS   B 1 287 ? 26.808  53.160 27.275  1.00 87.16  ? 943  LYS   B CE  1 
ATOM   4947 N NZ  . LYS   B 1 287 ? 26.649  54.025 26.072  1.00 92.77  ? 943  LYS   B NZ  1 
ATOM   4948 N N   . GLY   B 1 288 ? 24.516  51.294 33.160  1.00 43.60  ? 944  GLY   B N   1 
ATOM   4949 C CA  . GLY   B 1 288 ? 23.644  51.359 34.331  1.00 43.32  ? 944  GLY   B CA  1 
ATOM   4950 C C   . GLY   B 1 288 ? 23.296  50.015 34.945  1.00 45.65  ? 944  GLY   B C   1 
ATOM   4951 O O   . GLY   B 1 288 ? 22.910  49.967 36.117  1.00 46.69  ? 944  GLY   B O   1 
ATOM   4952 N N   . LYS   B 1 289 ? 23.417  48.918 34.159  1.00 38.89  ? 945  LYS   B N   1 
ATOM   4953 C CA  . LYS   B 1 289 ? 23.183  47.535 34.598  1.00 37.55  ? 945  LYS   B CA  1 
ATOM   4954 C C   . LYS   B 1 289 ? 24.476  46.904 35.134  1.00 40.47  ? 945  LYS   B C   1 
ATOM   4955 O O   . LYS   B 1 289 ? 25.563  47.213 34.633  1.00 39.70  ? 945  LYS   B O   1 
ATOM   4956 C CB  . LYS   B 1 289 ? 22.615  46.677 33.463  1.00 39.68  ? 945  LYS   B CB  1 
ATOM   4957 C CG  . LYS   B 1 289 ? 21.270  47.165 32.915  1.00 46.68  ? 945  LYS   B CG  1 
ATOM   4958 C CD  . LYS   B 1 289 ? 20.145  47.074 33.954  1.00 46.54  ? 945  LYS   B CD  1 
ATOM   4959 C CE  . LYS   B 1 289 ? 18.845  47.580 33.403  1.00 51.13  ? 945  LYS   B CE  1 
ATOM   4960 N NZ  . LYS   B 1 289 ? 17.735  47.345 34.347  1.00 58.54  ? 945  LYS   B NZ  1 
ATOM   4961 N N   . HIS   B 1 290 ? 24.362  46.043 36.166  1.00 36.17  ? 946  HIS   B N   1 
ATOM   4962 C CA  . HIS   B 1 290 ? 25.510  45.376 36.814  1.00 35.47  ? 946  HIS   B CA  1 
ATOM   4963 C C   . HIS   B 1 290 ? 25.429  43.847 36.709  1.00 35.28  ? 946  HIS   B C   1 
ATOM   4964 O O   . HIS   B 1 290 ? 26.396  43.143 37.022  1.00 33.83  ? 946  HIS   B O   1 
ATOM   4965 C CB  . HIS   B 1 290 ? 25.586  45.757 38.305  1.00 36.68  ? 946  HIS   B CB  1 
ATOM   4966 C CG  . HIS   B 1 290 ? 25.550  47.223 38.573  1.00 40.48  ? 946  HIS   B CG  1 
ATOM   4967 N ND1 . HIS   B 1 290 ? 24.350  47.919 38.613  1.00 42.38  ? 946  HIS   B ND1 1 
ATOM   4968 C CD2 . HIS   B 1 290 ? 26.565  48.079 38.829  1.00 42.27  ? 946  HIS   B CD2 1 
ATOM   4969 C CE1 . HIS   B 1 290 ? 24.677  49.169 38.877  1.00 41.98  ? 946  HIS   B CE1 1 
ATOM   4970 N NE2 . HIS   B 1 290 ? 25.998  49.314 39.015  1.00 42.39  ? 946  HIS   B NE2 1 
ATOM   4971 N N   . SER   B 1 291 ? 24.257  43.337 36.316  1.00 30.71  ? 947  SER   B N   1 
ATOM   4972 C CA  . SER   B 1 291 ? 24.006  41.907 36.186  1.00 30.03  ? 947  SER   B CA  1 
ATOM   4973 C C   . SER   B 1 291 ? 22.830  41.654 35.261  1.00 32.93  ? 947  SER   B C   1 
ATOM   4974 O O   . SER   B 1 291 ? 22.116  42.577 34.867  1.00 29.91  ? 947  SER   B O   1 
ATOM   4975 C CB  . SER   B 1 291 ? 23.731  41.270 37.555  1.00 33.40  ? 947  SER   B CB  1 
ATOM   4976 O OG  . SER   B 1 291 ? 22.551  41.792 38.149  1.00 41.68  ? 947  SER   B OG  1 
ATOM   4977 N N   . VAL   B 1 292 ? 22.655  40.388 34.910  1.00 30.32  ? 948  VAL   B N   1 
ATOM   4978 C CA  . VAL   B 1 292 ? 21.536  39.903 34.131  1.00 29.73  ? 948  VAL   B CA  1 
ATOM   4979 C C   . VAL   B 1 292 ? 20.751  38.959 35.041  1.00 31.29  ? 948  VAL   B C   1 
ATOM   4980 O O   . VAL   B 1 292 ? 21.336  38.148 35.768  1.00 31.79  ? 948  VAL   B O   1 
ATOM   4981 C CB  . VAL   B 1 292 ? 21.970  39.226 32.799  1.00 34.51  ? 948  VAL   B CB  1 
ATOM   4982 C CG1 . VAL   B 1 292 ? 20.862  38.334 32.236  1.00 35.12  ? 948  VAL   B CG1 1 
ATOM   4983 C CG2 . VAL   B 1 292 ? 22.362  40.272 31.767  1.00 34.24  ? 948  VAL   B CG2 1 
ATOM   4984 N N   . LYS   B 1 293 ? 19.434  39.091 35.030  1.00 26.66  ? 949  LYS   B N   1 
ATOM   4985 C CA  . LYS   B 1 293 ? 18.594  38.164 35.747  1.00 26.01  ? 949  LYS   B CA  1 
ATOM   4986 C C   . LYS   B 1 293 ? 17.726  37.437 34.717  1.00 30.86  ? 949  LYS   B C   1 
ATOM   4987 O O   . LYS   B 1 293 ? 16.911  38.064 34.052  1.00 29.76  ? 949  LYS   B O   1 
ATOM   4988 C CB  . LYS   B 1 293 ? 17.746  38.827 36.860  1.00 26.59  ? 949  LYS   B CB  1 
ATOM   4989 C CG  . LYS   B 1 293 ? 16.901  37.788 37.617  1.00 30.71  ? 949  LYS   B CG  1 
ATOM   4990 C CD  . LYS   B 1 293 ? 15.974  38.381 38.634  1.00 40.91  ? 949  LYS   B CD  1 
ATOM   4991 C CE  . LYS   B 1 293 ? 15.178  37.294 39.321  1.00 50.87  ? 949  LYS   B CE  1 
ATOM   4992 N NZ  . LYS   B 1 293 ? 14.230  37.855 40.322  1.00 49.98  ? 949  LYS   B NZ  1 
ATOM   4993 N N   . GLY   B 1 294 ? 17.939  36.129 34.587  1.00 29.10  ? 950  GLY   B N   1 
ATOM   4994 C CA  . GLY   B 1 294 ? 17.109  35.250 33.776  1.00 29.27  ? 950  GLY   B CA  1 
ATOM   4995 C C   . GLY   B 1 294 ? 15.824  34.975 34.562  1.00 32.21  ? 950  GLY   B C   1 
ATOM   4996 O O   . GLY   B 1 294 ? 15.876  34.364 35.624  1.00 28.94  ? 950  GLY   B O   1 
ATOM   4997 N N   . LEU   B 1 295 ? 14.676  35.481 34.112  1.00 31.78  ? 951  LEU   B N   1 
ATOM   4998 C CA  . LEU   B 1 295 ? 13.408  35.341 34.853  1.00 32.88  ? 951  LEU   B CA  1 
ATOM   4999 C C   . LEU   B 1 295 ? 12.740  33.974 34.708  1.00 37.68  ? 951  LEU   B C   1 
ATOM   5000 O O   . LEU   B 1 295 ? 12.264  33.634 33.633  1.00 37.24  ? 951  LEU   B O   1 
ATOM   5001 C CB  . LEU   B 1 295 ? 12.406  36.454 34.501  1.00 33.34  ? 951  LEU   B CB  1 
ATOM   5002 C CG  . LEU   B 1 295 ? 12.857  37.924 34.522  1.00 38.43  ? 951  LEU   B CG  1 
ATOM   5003 C CD1 . LEU   B 1 295 ? 11.756  38.817 33.948  1.00 36.47  ? 951  LEU   B CD1 1 
ATOM   5004 C CD2 . LEU   B 1 295 ? 13.227  38.388 35.927  1.00 42.76  ? 951  LEU   B CD2 1 
ATOM   5005 N N   . GLY   B 1 296 ? 12.681  33.218 35.796  1.00 35.85  ? 952  GLY   B N   1 
ATOM   5006 C CA  . GLY   B 1 296 ? 12.050  31.902 35.795  1.00 36.22  ? 952  GLY   B CA  1 
ATOM   5007 C C   . GLY   B 1 296 ? 10.590  31.941 36.165  1.00 42.55  ? 952  GLY   B C   1 
ATOM   5008 O O   . GLY   B 1 296 ? 10.158  32.877 36.841  1.00 44.27  ? 952  GLY   B O   1 
ATOM   5009 N N   . LYS   B 1 297 ? 9.813   30.921 35.722  1.00 38.98  ? 953  LYS   B N   1 
ATOM   5010 C CA  . LYS   B 1 297 ? 8.377   30.759 36.004  1.00 38.19  ? 953  LYS   B CA  1 
ATOM   5011 C C   . LYS   B 1 297 ? 8.140   30.633 37.522  1.00 41.49  ? 953  LYS   B C   1 
ATOM   5012 O O   . LYS   B 1 297 ? 7.110   31.080 38.023  1.00 44.67  ? 953  LYS   B O   1 
ATOM   5013 C CB  . LYS   B 1 297 ? 7.813   29.496 35.307  1.00 40.03  ? 953  LYS   B CB  1 
ATOM   5014 C CG  . LYS   B 1 297 ? 8.017   29.408 33.798  1.00 47.72  ? 953  LYS   B CG  1 
ATOM   5015 C CD  . LYS   B 1 297 ? 6.765   29.724 32.997  1.00 56.66  ? 953  LYS   B CD  1 
ATOM   5016 C CE  . LYS   B 1 297 ? 6.994   29.518 31.519  1.00 65.37  ? 953  LYS   B CE  1 
ATOM   5017 N NZ  . LYS   B 1 297 ? 5.749   29.703 30.729  1.00 79.86  ? 953  LYS   B NZ  1 
ATOM   5018 N N   . THR   B 1 298 ? 9.065   29.996 38.233  1.00 36.33  ? 954  THR   B N   1 
ATOM   5019 C CA  . THR   B 1 298 ? 9.023   29.770 39.678  1.00 35.83  ? 954  THR   B CA  1 
ATOM   5020 C C   . THR   B 1 298 ? 10.143  30.535 40.383  1.00 40.28  ? 954  THR   B C   1 
ATOM   5021 O O   . THR   B 1 298 ? 11.296  30.501 39.944  1.00 39.15  ? 954  THR   B O   1 
ATOM   5022 C CB  . THR   B 1 298 ? 9.098   28.265 39.962  1.00 42.49  ? 954  THR   B CB  1 
ATOM   5023 O OG1 . THR   B 1 298 ? 8.111   27.601 39.172  1.00 41.48  ? 954  THR   B OG1 1 
ATOM   5024 C CG2 . THR   B 1 298 ? 8.934   27.914 41.469  1.00 37.85  ? 954  THR   B CG2 1 
ATOM   5025 N N   . THR   B 1 299 ? 9.798   31.189 41.498  1.00 38.87  ? 955  THR   B N   1 
ATOM   5026 C CA  . THR   B 1 299 ? 10.718  31.956 42.336  1.00 39.66  ? 955  THR   B CA  1 
ATOM   5027 C C   . THR   B 1 299 ? 10.543  31.613 43.824  1.00 45.48  ? 955  THR   B C   1 
ATOM   5028 O O   . THR   B 1 299 ? 9.392   31.432 44.257  1.00 46.12  ? 955  THR   B O   1 
ATOM   5029 C CB  . THR   B 1 299 ? 10.550  33.487 42.093  1.00 47.56  ? 955  THR   B CB  1 
ATOM   5030 O OG1 . THR   B 1 299 ? 11.556  34.183 42.830  1.00 50.83  ? 955  THR   B OG1 1 
ATOM   5031 C CG2 . THR   B 1 299 ? 9.161   34.037 42.517  1.00 41.71  ? 955  THR   B CG2 1 
ATOM   5032 N N   . PRO   B 1 300 ? 11.633  31.596 44.645  1.00 43.04  ? 956  PRO   B N   1 
ATOM   5033 C CA  . PRO   B 1 300 ? 11.438  31.444 46.093  1.00 43.36  ? 956  PRO   B CA  1 
ATOM   5034 C C   . PRO   B 1 300 ? 10.580  32.632 46.567  1.00 49.07  ? 956  PRO   B C   1 
ATOM   5035 O O   . PRO   B 1 300 ? 10.741  33.738 46.042  1.00 48.24  ? 956  PRO   B O   1 
ATOM   5036 C CB  . PRO   B 1 300 ? 12.873  31.542 46.650  1.00 44.93  ? 956  PRO   B CB  1 
ATOM   5037 C CG  . PRO   B 1 300 ? 13.761  31.189 45.511  1.00 48.92  ? 956  PRO   B CG  1 
ATOM   5038 C CD  . PRO   B 1 300 ? 13.072  31.798 44.333  1.00 44.52  ? 956  PRO   B CD  1 
ATOM   5039 N N   . ASP   B 1 301 ? 9.625   32.394 47.481  1.00 47.56  ? 957  ASP   B N   1 
ATOM   5040 C CA  . ASP   B 1 301 ? 8.715   33.427 48.000  1.00 48.04  ? 957  ASP   B CA  1 
ATOM   5041 C C   . ASP   B 1 301 ? 9.486   34.683 48.486  1.00 52.84  ? 957  ASP   B C   1 
ATOM   5042 O O   . ASP   B 1 301 ? 10.219  34.588 49.472  1.00 51.78  ? 957  ASP   B O   1 
ATOM   5043 C CB  . ASP   B 1 301 ? 7.814   32.856 49.109  1.00 49.66  ? 957  ASP   B CB  1 
ATOM   5044 C CG  . ASP   B 1 301 ? 6.657   33.743 49.534  1.00 65.30  ? 957  ASP   B CG  1 
ATOM   5045 O OD1 . ASP   B 1 301 ? 6.387   34.751 48.837  1.00 66.66  ? 957  ASP   B OD1 1 
ATOM   5046 O OD2 . ASP   B 1 301 ? 6.016   33.429 50.557  1.00 73.45  ? 957  ASP   B OD2 1 
ATOM   5047 N N   . PRO   B 1 302 ? 9.336   35.853 47.792  1.00 50.99  ? 958  PRO   B N   1 
ATOM   5048 C CA  . PRO   B 1 302 ? 10.081  37.069 48.192  1.00 50.91  ? 958  PRO   B CA  1 
ATOM   5049 C C   . PRO   B 1 302 ? 9.822   37.601 49.600  1.00 52.78  ? 958  PRO   B C   1 
ATOM   5050 O O   . PRO   B 1 302 ? 10.686  38.279 50.154  1.00 52.81  ? 958  PRO   B O   1 
ATOM   5051 C CB  . PRO   B 1 302 ? 9.671   38.099 47.129  1.00 52.76  ? 958  PRO   B CB  1 
ATOM   5052 C CG  . PRO   B 1 302 ? 9.211   37.291 45.969  1.00 56.78  ? 958  PRO   B CG  1 
ATOM   5053 C CD  . PRO   B 1 302 ? 8.521   36.119 46.587  1.00 52.36  ? 958  PRO   B CD  1 
ATOM   5054 N N   . SER   B 1 303 ? 8.651   37.306 50.180  1.00 47.77  ? 959  SER   B N   1 
ATOM   5055 C CA  . SER   B 1 303 ? 8.334   37.754 51.534  1.00 46.80  ? 959  SER   B CA  1 
ATOM   5056 C C   . SER   B 1 303 ? 9.028   36.902 52.601  1.00 48.99  ? 959  SER   B C   1 
ATOM   5057 O O   . SER   B 1 303 ? 9.053   37.279 53.775  1.00 49.52  ? 959  SER   B O   1 
ATOM   5058 C CB  . SER   B 1 303 ? 6.821   37.852 51.752  1.00 49.58  ? 959  SER   B CB  1 
ATOM   5059 O OG  . SER   B 1 303 ? 6.123   36.704 51.298  1.00 58.07  ? 959  SER   B OG  1 
ATOM   5060 N N   . ALA   B 1 304 ? 9.633   35.777 52.180  1.00 43.11  ? 960  ALA   B N   1 
ATOM   5061 C CA  . ALA   B 1 304 ? 10.351  34.852 53.053  1.00 41.26  ? 960  ALA   B CA  1 
ATOM   5062 C C   . ALA   B 1 304 ? 11.887  35.089 53.088  1.00 45.42  ? 960  ALA   B C   1 
ATOM   5063 O O   . ALA   B 1 304 ? 12.603  34.358 53.782  1.00 43.26  ? 960  ALA   B O   1 
ATOM   5064 C CB  . ALA   B 1 304 ? 10.020  33.422 52.671  1.00 41.28  ? 960  ALA   B CB  1 
ATOM   5065 N N   . ASN   B 1 305 ? 12.378  36.138 52.376  1.00 44.74  ? 961  ASN   B N   1 
ATOM   5066 C CA  . ASN   B 1 305 ? 13.797  36.529 52.340  1.00 45.21  ? 961  ASN   B CA  1 
ATOM   5067 C C   . ASN   B 1 305 ? 14.281  36.924 53.730  1.00 50.47  ? 961  ASN   B C   1 
ATOM   5068 O O   . ASN   B 1 305 ? 13.555  37.592 54.484  1.00 50.97  ? 961  ASN   B O   1 
ATOM   5069 C CB  . ASN   B 1 305 ? 14.020  37.711 51.382  1.00 46.88  ? 961  ASN   B CB  1 
ATOM   5070 C CG  . ASN   B 1 305 ? 14.501  37.323 50.017  1.00 76.98  ? 961  ASN   B CG  1 
ATOM   5071 O OD1 . ASN   B 1 305 ? 15.688  37.479 49.689  1.00 79.86  ? 961  ASN   B OD1 1 
ATOM   5072 N ND2 . ASN   B 1 305 ? 13.588  36.812 49.188  1.00 66.34  ? 961  ASN   B ND2 1 
ATOM   5073 N N   . ILE   B 1 306 ? 15.498  36.516 54.069  1.00 47.29  ? 962  ILE   B N   1 
ATOM   5074 C CA  . ILE   B 1 306 ? 16.096  36.868 55.356  1.00 47.94  ? 962  ILE   B CA  1 
ATOM   5075 C C   . ILE   B 1 306 ? 17.455  37.560 55.127  1.00 54.40  ? 962  ILE   B C   1 
ATOM   5076 O O   . ILE   B 1 306 ? 17.760  37.957 53.996  1.00 53.40  ? 962  ILE   B O   1 
ATOM   5077 C CB  . ILE   B 1 306 ? 16.143  35.667 56.355  1.00 50.88  ? 962  ILE   B CB  1 
ATOM   5078 C CG1 . ILE   B 1 306 ? 17.040  34.521 55.839  1.00 51.39  ? 962  ILE   B CG1 1 
ATOM   5079 C CG2 . ILE   B 1 306 ? 14.736  35.169 56.736  1.00 50.51  ? 962  ILE   B CG2 1 
ATOM   5080 C CD1 . ILE   B 1 306 ? 18.256  34.343 56.606  1.00 56.65  ? 962  ILE   B CD1 1 
ATOM   5081 N N   . SER   B 1 307 ? 18.255  37.720 56.193  1.00 53.48  ? 963  SER   B N   1 
ATOM   5082 C CA  . SER   B 1 307 ? 19.567  38.354 56.097  1.00 53.98  ? 963  SER   B CA  1 
ATOM   5083 C C   . SER   B 1 307 ? 20.662  37.607 56.899  1.00 59.78  ? 963  SER   B C   1 
ATOM   5084 O O   . SER   B 1 307 ? 20.454  37.266 58.067  1.00 60.19  ? 963  SER   B O   1 
ATOM   5085 C CB  . SER   B 1 307 ? 19.476  39.814 56.521  1.00 57.61  ? 963  SER   B CB  1 
ATOM   5086 O OG  . SER   B 1 307 ? 20.665  40.510 56.193  1.00 67.61  ? 963  SER   B OG  1 
ATOM   5087 N N   . LEU   B 1 308 ? 21.805  37.321 56.242  1.00 55.56  ? 964  LEU   B N   1 
ATOM   5088 C CA  . LEU   B 1 308 ? 22.977  36.675 56.841  1.00 54.83  ? 964  LEU   B CA  1 
ATOM   5089 C C   . LEU   B 1 308 ? 24.186  37.543 56.490  1.00 59.49  ? 964  LEU   B C   1 
ATOM   5090 O O   . LEU   B 1 308 ? 24.664  37.514 55.347  1.00 59.26  ? 964  LEU   B O   1 
ATOM   5091 C CB  . LEU   B 1 308 ? 23.138  35.202 56.375  1.00 54.50  ? 964  LEU   B CB  1 
ATOM   5092 C CG  . LEU   B 1 308 ? 24.438  34.404 56.767  1.00 57.75  ? 964  LEU   B CG  1 
ATOM   5093 C CD1 . LEU   B 1 308 ? 24.619  34.294 58.285  1.00 57.92  ? 964  LEU   B CD1 1 
ATOM   5094 C CD2 . LEU   B 1 308 ? 24.426  33.005 56.170  1.00 56.09  ? 964  LEU   B CD2 1 
ATOM   5095 N N   . ASP   B 1 309 ? 24.625  38.367 57.477  1.00 55.99  ? 965  ASP   B N   1 
ATOM   5096 C CA  . ASP   B 1 309 ? 25.729  39.339 57.396  1.00 55.41  ? 965  ASP   B CA  1 
ATOM   5097 C C   . ASP   B 1 309 ? 25.411  40.490 56.417  1.00 56.43  ? 965  ASP   B C   1 
ATOM   5098 O O   . ASP   B 1 309 ? 26.283  40.929 55.661  1.00 56.81  ? 965  ASP   B O   1 
ATOM   5099 C CB  . ASP   B 1 309 ? 27.095  38.664 57.100  1.00 57.72  ? 965  ASP   B CB  1 
ATOM   5100 C CG  . ASP   B 1 309 ? 27.663  37.904 58.281  1.00 74.62  ? 965  ASP   B CG  1 
ATOM   5101 O OD1 . ASP   B 1 309 ? 27.192  36.767 58.541  1.00 76.26  ? 965  ASP   B OD1 1 
ATOM   5102 O OD2 . ASP   B 1 309 ? 28.580  38.443 58.948  1.00 82.70  ? 965  ASP   B OD2 1 
ATOM   5103 N N   . GLY   B 1 310 ? 24.163  40.961 56.453  1.00 49.46  ? 966  GLY   B N   1 
ATOM   5104 C CA  . GLY   B 1 310 ? 23.679  42.057 55.617  1.00 47.89  ? 966  GLY   B CA  1 
ATOM   5105 C C   . GLY   B 1 310 ? 23.407  41.709 54.163  1.00 48.31  ? 966  GLY   B C   1 
ATOM   5106 O O   . GLY   B 1 310 ? 23.084  42.597 53.358  1.00 49.73  ? 966  GLY   B O   1 
ATOM   5107 N N   . VAL   B 1 311 ? 23.518  40.421 53.817  1.00 39.22  ? 967  VAL   B N   1 
ATOM   5108 C CA  . VAL   B 1 311 ? 23.306  39.911 52.459  1.00 36.48  ? 967  VAL   B CA  1 
ATOM   5109 C C   . VAL   B 1 311 ? 21.928  39.248 52.413  1.00 37.78  ? 967  VAL   B C   1 
ATOM   5110 O O   . VAL   B 1 311 ? 21.581  38.519 53.346  1.00 37.06  ? 967  VAL   B O   1 
ATOM   5111 C CB  . VAL   B 1 311 ? 24.432  38.903 52.072  1.00 39.20  ? 967  VAL   B CB  1 
ATOM   5112 C CG1 . VAL   B 1 311 ? 24.372  38.538 50.596  1.00 38.72  ? 967  VAL   B CG1 1 
ATOM   5113 C CG2 . VAL   B 1 311 ? 25.805  39.443 52.436  1.00 38.84  ? 967  VAL   B CG2 1 
ATOM   5114 N N   . ASP   B 1 312 ? 21.149  39.489 51.341  1.00 32.88  ? 968  ASP   B N   1 
ATOM   5115 C CA  . ASP   B 1 312 ? 19.825  38.877 51.191  1.00 31.79  ? 968  ASP   B CA  1 
ATOM   5116 C C   . ASP   B 1 312 ? 19.906  37.386 50.876  1.00 33.52  ? 968  ASP   B C   1 
ATOM   5117 O O   . ASP   B 1 312 ? 20.683  36.965 50.015  1.00 31.29  ? 968  ASP   B O   1 
ATOM   5118 C CB  . ASP   B 1 312 ? 18.949  39.627 50.177  1.00 33.97  ? 968  ASP   B CB  1 
ATOM   5119 C CG  . ASP   B 1 312 ? 18.030  40.643 50.833  1.00 50.08  ? 968  ASP   B CG  1 
ATOM   5120 O OD1 . ASP   B 1 312 ? 17.154  40.228 51.636  1.00 50.24  ? 968  ASP   B OD1 1 
ATOM   5121 O OD2 . ASP   B 1 312 ? 18.190  41.855 50.555  1.00 59.05  ? 968  ASP   B OD2 1 
ATOM   5122 N N   . VAL   B 1 313 ? 19.157  36.575 51.637  1.00 30.49  ? 969  VAL   B N   1 
ATOM   5123 C CA  . VAL   B 1 313 ? 19.172  35.118 51.448  1.00 30.18  ? 969  VAL   B CA  1 
ATOM   5124 C C   . VAL   B 1 313 ? 17.770  34.672 50.970  1.00 34.45  ? 969  VAL   B C   1 
ATOM   5125 O O   . VAL   B 1 313 ? 16.842  34.654 51.780  1.00 31.88  ? 969  VAL   B O   1 
ATOM   5126 C CB  . VAL   B 1 313 ? 19.688  34.350 52.702  1.00 32.61  ? 969  VAL   B CB  1 
ATOM   5127 C CG1 . VAL   B 1 313 ? 19.684  32.838 52.469  1.00 32.21  ? 969  VAL   B CG1 1 
ATOM   5128 C CG2 . VAL   B 1 313 ? 21.078  34.835 53.121  1.00 31.91  ? 969  VAL   B CG2 1 
ATOM   5129 N N   . PRO   B 1 314 ? 17.581  34.357 49.656  1.00 34.39  ? 970  PRO   B N   1 
ATOM   5130 C CA  . PRO   B 1 314 ? 16.224  33.985 49.180  1.00 35.31  ? 970  PRO   B CA  1 
ATOM   5131 C C   . PRO   B 1 314 ? 15.843  32.531 49.503  1.00 41.34  ? 970  PRO   B C   1 
ATOM   5132 O O   . PRO   B 1 314 ? 15.695  31.706 48.592  1.00 41.20  ? 970  PRO   B O   1 
ATOM   5133 C CB  . PRO   B 1 314 ? 16.282  34.276 47.669  1.00 36.62  ? 970  PRO   B CB  1 
ATOM   5134 C CG  . PRO   B 1 314 ? 17.722  34.123 47.308  1.00 40.72  ? 970  PRO   B CG  1 
ATOM   5135 C CD  . PRO   B 1 314 ? 18.568  34.357 48.549  1.00 36.11  ? 970  PRO   B CD  1 
ATOM   5136 N N   . LEU   B 1 315 ? 15.665  32.221 50.804  1.00 38.82  ? 971  LEU   B N   1 
ATOM   5137 C CA  . LEU   B 1 315 ? 15.367  30.856 51.240  1.00 39.17  ? 971  LEU   B CA  1 
ATOM   5138 C C   . LEU   B 1 315 ? 13.864  30.502 51.295  1.00 44.60  ? 971  LEU   B C   1 
ATOM   5139 O O   . LEU   B 1 315 ? 13.516  29.456 51.848  1.00 43.69  ? 971  LEU   B O   1 
ATOM   5140 C CB  . LEU   B 1 315 ? 16.059  30.505 52.573  1.00 39.13  ? 971  LEU   B CB  1 
ATOM   5141 C CG  . LEU   B 1 315 ? 16.027  31.487 53.753  1.00 43.61  ? 971  LEU   B CG  1 
ATOM   5142 C CD1 . LEU   B 1 315 ? 14.594  31.712 54.299  1.00 42.90  ? 971  LEU   B CD1 1 
ATOM   5143 C CD2 . LEU   B 1 315 ? 16.932  30.971 54.871  1.00 46.26  ? 971  LEU   B CD2 1 
ATOM   5144 N N   . GLY   B 1 316 ? 13.002  31.341 50.714  1.00 42.19  ? 972  GLY   B N   1 
ATOM   5145 C CA  . GLY   B 1 316 ? 11.566  31.070 50.666  1.00 42.61  ? 972  GLY   B CA  1 
ATOM   5146 C C   . GLY   B 1 316 ? 11.238  29.863 49.809  1.00 48.60  ? 972  GLY   B C   1 
ATOM   5147 O O   . GLY   B 1 316 ? 12.087  29.435 49.011  1.00 49.27  ? 972  GLY   B O   1 
ATOM   5148 N N   . THR   B 1 317 ? 10.030  29.266 49.995  1.00 44.79  ? 973  THR   B N   1 
ATOM   5149 C CA  . THR   B 1 317 ? 9.633   28.106 49.188  1.00 44.56  ? 973  THR   B CA  1 
ATOM   5150 C C   . THR   B 1 317 ? 9.205   28.588 47.811  1.00 49.38  ? 973  THR   B C   1 
ATOM   5151 O O   . THR   B 1 317 ? 8.776   29.736 47.680  1.00 47.91  ? 973  THR   B O   1 
ATOM   5152 C CB  . THR   B 1 317 ? 8.551   27.236 49.855  1.00 49.80  ? 973  THR   B CB  1 
ATOM   5153 O OG1 . THR   B 1 317 ? 7.367   28.004 50.071  1.00 51.64  ? 973  THR   B OG1 1 
ATOM   5154 C CG2 . THR   B 1 317 ? 9.024   26.577 51.136  1.00 47.40  ? 973  THR   B CG2 1 
ATOM   5155 N N   . GLY   B 1 318 ? 9.364   27.724 46.804  1.00 47.77  ? 974  GLY   B N   1 
ATOM   5156 C CA  . GLY   B 1 318 ? 9.009   28.001 45.418  1.00 48.10  ? 974  GLY   B CA  1 
ATOM   5157 C C   . GLY   B 1 318 ? 7.541   28.335 45.203  1.00 54.42  ? 974  GLY   B C   1 
ATOM   5158 O O   . GLY   B 1 318 ? 6.648   27.547 45.549  1.00 54.25  ? 974  GLY   B O   1 
ATOM   5159 N N   . ILE   B 1 319 ? 7.294   29.542 44.663  1.00 52.28  ? 975  ILE   B N   1 
ATOM   5160 C CA  . ILE   B 1 319 ? 5.971   30.071 44.291  1.00 52.57  ? 975  ILE   B CA  1 
ATOM   5161 C C   . ILE   B 1 319 ? 6.065   30.573 42.827  1.00 54.90  ? 975  ILE   B C   1 
ATOM   5162 O O   . ILE   B 1 319 ? 7.171   30.751 42.312  1.00 54.86  ? 975  ILE   B O   1 
ATOM   5163 C CB  . ILE   B 1 319 ? 5.431   31.173 45.276  1.00 55.87  ? 975  ILE   B CB  1 
ATOM   5164 C CG1 . ILE   B 1 319 ? 6.225   32.502 45.153  1.00 56.27  ? 975  ILE   B CG1 1 
ATOM   5165 C CG2 . ILE   B 1 319 ? 5.381   30.664 46.730  1.00 57.58  ? 975  ILE   B CG2 1 
ATOM   5166 C CD1 . ILE   B 1 319 ? 5.459   33.718 45.446  1.00 59.40  ? 975  ILE   B CD1 1 
ATOM   5167 N N   . SER   B 1 320 ? 4.920   30.796 42.174  1.00 49.72  ? 976  SER   B N   1 
ATOM   5168 C CA  . SER   B 1 320 ? 4.863   31.322 40.813  1.00 49.38  ? 976  SER   B CA  1 
ATOM   5169 C C   . SER   B 1 320 ? 5.365   32.780 40.809  1.00 52.01  ? 976  SER   B C   1 
ATOM   5170 O O   . SER   B 1 320 ? 4.960   33.578 41.669  1.00 50.52  ? 976  SER   B O   1 
ATOM   5171 C CB  . SER   B 1 320 ? 3.429   31.262 40.284  1.00 54.12  ? 976  SER   B CB  1 
ATOM   5172 O OG  . SER   B 1 320 ? 3.268   31.949 39.052  1.00 63.12  ? 976  SER   B OG  1 
ATOM   5173 N N   . SER   B 1 321 ? 6.248   33.118 39.849  1.00 47.91  ? 977  SER   B N   1 
ATOM   5174 C CA  . SER   B 1 321 ? 6.786   34.477 39.718  1.00 47.28  ? 977  SER   B CA  1 
ATOM   5175 C C   . SER   B 1 321 ? 5.756   35.439 39.119  1.00 53.75  ? 977  SER   B C   1 
ATOM   5176 O O   . SER   B 1 321 ? 5.781   36.636 39.419  1.00 54.59  ? 977  SER   B O   1 
ATOM   5177 C CB  . SER   B 1 321 ? 8.053   34.479 38.871  1.00 48.00  ? 977  SER   B CB  1 
ATOM   5178 O OG  . SER   B 1 321 ? 7.782   34.023 37.557  1.00 44.90  ? 977  SER   B OG  1 
ATOM   5179 N N   . GLY   B 1 322 ? 4.872   34.899 38.278  1.00 50.55  ? 978  GLY   B N   1 
ATOM   5180 C CA  . GLY   B 1 322 ? 3.860   35.650 37.545  1.00 49.40  ? 978  GLY   B CA  1 
ATOM   5181 C C   . GLY   B 1 322 ? 4.350   35.930 36.137  1.00 51.27  ? 978  GLY   B C   1 
ATOM   5182 O O   . GLY   B 1 322 ? 3.597   36.425 35.298  1.00 49.62  ? 978  GLY   B O   1 
ATOM   5183 N N   . VAL   B 1 323 ? 5.622   35.566 35.862  1.00 47.75  ? 979  VAL   B N   1 
ATOM   5184 C CA  . VAL   B 1 323 ? 6.281   35.745 34.567  1.00 48.00  ? 979  VAL   B CA  1 
ATOM   5185 C C   . VAL   B 1 323 ? 5.723   34.752 33.526  1.00 55.67  ? 979  VAL   B C   1 
ATOM   5186 O O   . VAL   B 1 323 ? 5.711   33.535 33.736  1.00 53.97  ? 979  VAL   B O   1 
ATOM   5187 C CB  . VAL   B 1 323 ? 7.839   35.728 34.677  1.00 50.76  ? 979  VAL   B CB  1 
ATOM   5188 C CG1 . VAL   B 1 323 ? 8.493   35.770 33.312  1.00 50.71  ? 979  VAL   B CG1 1 
ATOM   5189 C CG2 . VAL   B 1 323 ? 8.348   36.889 35.528  1.00 50.25  ? 979  VAL   B CG2 1 
ATOM   5190 N N   . ASN   B 1 324 ? 5.247   35.313 32.406  1.00 57.10  ? 980  ASN   B N   1 
ATOM   5191 C CA  . ASN   B 1 324 ? 4.676   34.582 31.279  1.00 58.31  ? 980  ASN   B CA  1 
ATOM   5192 C C   . ASN   B 1 324 ? 5.657   34.455 30.103  1.00 63.61  ? 980  ASN   B C   1 
ATOM   5193 O O   . ASN   B 1 324 ? 6.480   35.351 29.877  1.00 63.02  ? 980  ASN   B O   1 
ATOM   5194 C CB  . ASN   B 1 324 ? 3.415   35.280 30.807  1.00 58.60  ? 980  ASN   B CB  1 
ATOM   5195 C CG  . ASN   B 1 324 ? 2.306   35.328 31.835  1.00 94.91  ? 980  ASN   B CG  1 
ATOM   5196 O OD1 . ASN   B 1 324 ? 2.027   34.352 32.549  1.00 91.01  ? 980  ASN   B OD1 1 
ATOM   5197 N ND2 . ASN   B 1 324 ? 1.638   36.470 31.921  1.00 87.39  ? 980  ASN   B ND2 1 
ATOM   5198 N N   . ASP   B 1 325 ? 5.514   33.352 29.328  1.00 60.04  ? 981  ASP   B N   1 
ATOM   5199 C CA  . ASP   B 1 325 ? 6.261   33.037 28.108  1.00 59.31  ? 981  ASP   B CA  1 
ATOM   5200 C C   . ASP   B 1 325 ? 7.771   33.186 28.266  1.00 60.03  ? 981  ASP   B C   1 
ATOM   5201 O O   . ASP   B 1 325 ? 8.426   33.791 27.419  1.00 61.03  ? 981  ASP   B O   1 
ATOM   5202 C CB  . ASP   B 1 325 ? 5.732   33.855 26.902  1.00 62.00  ? 981  ASP   B CB  1 
ATOM   5203 C CG  . ASP   B 1 325 ? 4.238   33.687 26.598  1.00 81.59  ? 981  ASP   B CG  1 
ATOM   5204 O OD1 . ASP   B 1 325 ? 3.569   32.870 27.289  1.00 82.31  ? 981  ASP   B OD1 1 
ATOM   5205 O OD2 . ASP   B 1 325 ? 3.739   34.365 25.663  1.00 91.22  ? 981  ASP   B OD2 1 
ATOM   5206 N N   . THR   B 1 326 ? 8.316   32.648 29.361  1.00 52.57  ? 982  THR   B N   1 
ATOM   5207 C CA  . THR   B 1 326 ? 9.754   32.668 29.624  1.00 49.93  ? 982  THR   B CA  1 
ATOM   5208 C C   . THR   B 1 326 ? 10.358  31.311 29.264  1.00 50.27  ? 982  THR   B C   1 
ATOM   5209 O O   . THR   B 1 326 ? 9.684   30.287 29.388  1.00 51.11  ? 982  THR   B O   1 
ATOM   5210 C CB  . THR   B 1 326 ? 10.090  33.165 31.041  1.00 50.39  ? 982  THR   B CB  1 
ATOM   5211 O OG1 . THR   B 1 326 ? 11.501  33.059 31.217  1.00 51.76  ? 982  THR   B OG1 1 
ATOM   5212 C CG2 . THR   B 1 326 ? 9.376   32.384 32.142  1.00 40.21  ? 982  THR   B CG2 1 
ATOM   5213 N N   . SER   B 1 327 ? 11.617  31.297 28.822  1.00 42.57  ? 983  SER   B N   1 
ATOM   5214 C CA  . SER   B 1 327 ? 12.302  30.065 28.448  1.00 40.53  ? 983  SER   B CA  1 
ATOM   5215 C C   . SER   B 1 327 ? 12.929  29.359 29.675  1.00 41.58  ? 983  SER   B C   1 
ATOM   5216 O O   . SER   B 1 327 ? 13.614  28.335 29.523  1.00 41.58  ? 983  SER   B O   1 
ATOM   5217 C CB  . SER   B 1 327 ? 13.344  30.347 27.369  1.00 44.28  ? 983  SER   B CB  1 
ATOM   5218 O OG  . SER   B 1 327 ? 14.345  31.224 27.837  1.00 59.55  ? 983  SER   B OG  1 
ATOM   5219 N N   . LEU   B 1 328 ? 12.686  29.902 30.887  1.00 34.86  ? 984  LEU   B N   1 
ATOM   5220 C CA  . LEU   B 1 328 ? 13.282  29.375 32.105  1.00 33.88  ? 984  LEU   B CA  1 
ATOM   5221 C C   . LEU   B 1 328 ? 12.291  28.986 33.134  1.00 37.27  ? 984  LEU   B C   1 
ATOM   5222 O O   . LEU   B 1 328 ? 11.400  29.761 33.456  1.00 37.73  ? 984  LEU   B O   1 
ATOM   5223 C CB  . LEU   B 1 328 ? 14.279  30.363 32.734  1.00 33.56  ? 984  LEU   B CB  1 
ATOM   5224 C CG  . LEU   B 1 328 ? 15.460  30.772 31.908  1.00 37.65  ? 984  LEU   B CG  1 
ATOM   5225 C CD1 . LEU   B 1 328 ? 15.900  32.135 32.297  1.00 37.79  ? 984  LEU   B CD1 1 
ATOM   5226 C CD2 . LEU   B 1 328 ? 16.596  29.778 32.030  1.00 40.28  ? 984  LEU   B CD2 1 
ATOM   5227 N N   . LEU   B 1 329 ? 12.509  27.820 33.746  1.00 34.31  ? 985  LEU   B N   1 
ATOM   5228 C CA  . LEU   B 1 329 ? 11.638  27.350 34.822  1.00 33.94  ? 985  LEU   B CA  1 
ATOM   5229 C C   . LEU   B 1 329 ? 12.031  28.114 36.077  1.00 32.28  ? 985  LEU   B C   1 
ATOM   5230 O O   . LEU   B 1 329 ? 11.186  28.561 36.824  1.00 30.05  ? 985  LEU   B O   1 
ATOM   5231 C CB  . LEU   B 1 329 ? 11.813  25.833 35.042  1.00 34.70  ? 985  LEU   B CB  1 
ATOM   5232 C CG  . LEU   B 1 329 ? 11.545  24.904 33.860  1.00 40.31  ? 985  LEU   B CG  1 
ATOM   5233 C CD1 . LEU   B 1 329 ? 11.977  23.492 34.184  1.00 41.19  ? 985  LEU   B CD1 1 
ATOM   5234 C CD2 . LEU   B 1 329 ? 10.080  24.923 33.438  1.00 42.37  ? 985  LEU   B CD2 1 
ATOM   5235 N N   . TYR   B 1 330 ? 13.329  28.255 36.311  1.00 27.57  ? 986  TYR   B N   1 
ATOM   5236 C CA  . TYR   B 1 330 ? 13.823  28.954 37.491  1.00 26.74  ? 986  TYR   B CA  1 
ATOM   5237 C C   . TYR   B 1 330 ? 14.719  30.105 37.094  1.00 27.38  ? 986  TYR   B C   1 
ATOM   5238 O O   . TYR   B 1 330 ? 15.215  30.168 35.962  1.00 25.40  ? 986  TYR   B O   1 
ATOM   5239 C CB  . TYR   B 1 330 ? 14.523  27.962 38.476  1.00 27.78  ? 986  TYR   B CB  1 
ATOM   5240 C CG  . TYR   B 1 330 ? 13.707  26.699 38.629  1.00 29.07  ? 986  TYR   B CG  1 
ATOM   5241 C CD1 . TYR   B 1 330 ? 12.462  26.726 39.259  1.00 31.16  ? 986  TYR   B CD1 1 
ATOM   5242 C CD2 . TYR   B 1 330 ? 14.091  25.519 37.995  1.00 29.82  ? 986  TYR   B CD2 1 
ATOM   5243 C CE1 . TYR   B 1 330 ? 11.643  25.604 39.287  1.00 30.36  ? 986  TYR   B CE1 1 
ATOM   5244 C CE2 . TYR   B 1 330 ? 13.278  24.386 38.021  1.00 30.73  ? 986  TYR   B CE2 1 
ATOM   5245 C CZ  . TYR   B 1 330 ? 12.050  24.440 38.659  1.00 38.90  ? 986  TYR   B CZ  1 
ATOM   5246 O OH  . TYR   B 1 330 ? 11.244  23.337 38.717  1.00 46.72  ? 986  TYR   B OH  1 
ATOM   5247 N N   . ASN   B 1 331 ? 14.881  31.036 38.037  1.00 23.03  ? 987  ASN   B N   1 
ATOM   5248 C CA  . ASN   B 1 331 ? 15.766  32.187 37.916  1.00 22.49  ? 987  ASN   B CA  1 
ATOM   5249 C C   . ASN   B 1 331 ? 17.223  31.797 37.763  1.00 26.79  ? 987  ASN   B C   1 
ATOM   5250 O O   . ASN   B 1 331 ? 17.656  30.730 38.190  1.00 24.24  ? 987  ASN   B O   1 
ATOM   5251 C CB  . ASN   B 1 331 ? 15.656  33.065 39.160  1.00 21.53  ? 987  ASN   B CB  1 
ATOM   5252 C CG  . ASN   B 1 331 ? 14.294  33.658 39.377  1.00 43.48  ? 987  ASN   B CG  1 
ATOM   5253 O OD1 . ASN   B 1 331 ? 13.653  34.117 38.441  1.00 40.94  ? 987  ASN   B OD1 1 
ATOM   5254 N ND2 . ASN   B 1 331 ? 13.831  33.671 40.622  1.00 31.42  ? 987  ASN   B ND2 1 
ATOM   5255 N N   . GLU   B 1 332 ? 17.984  32.700 37.163  1.00 25.51  ? 988  GLU   B N   1 
ATOM   5256 C CA  . GLU   B 1 332 ? 19.429  32.622 37.063  1.00 24.82  ? 988  GLU   B CA  1 
ATOM   5257 C C   . GLU   B 1 332 ? 19.991  34.013 37.057  1.00 25.88  ? 988  GLU   B C   1 
ATOM   5258 O O   . GLU   B 1 332 ? 19.327  34.946 36.622  1.00 25.55  ? 988  GLU   B O   1 
ATOM   5259 C CB  . GLU   B 1 332 ? 19.957  31.715 35.943  1.00 26.50  ? 988  GLU   B CB  1 
ATOM   5260 C CG  . GLU   B 1 332 ? 19.663  32.102 34.505  1.00 32.80  ? 988  GLU   B CG  1 
ATOM   5261 C CD  . GLU   B 1 332 ? 20.101  30.980 33.588  1.00 30.97  ? 988  GLU   B CD  1 
ATOM   5262 O OE1 . GLU   B 1 332 ? 21.080  31.171 32.833  1.00 27.10  ? 988  GLU   B OE1 1 
ATOM   5263 O OE2 . GLU   B 1 332 ? 19.486  29.890 33.652  1.00 26.54  ? 988  GLU   B OE2 1 
ATOM   5264 N N   . TYR   B 1 333 ? 21.165  34.164 37.656  1.00 21.89  ? 989  TYR   B N   1 
ATOM   5265 C CA  . TYR   B 1 333 ? 21.831  35.446 37.835  1.00 20.70  ? 989  TYR   B CA  1 
ATOM   5266 C C   . TYR   B 1 333 ? 23.228  35.372 37.218  1.00 22.77  ? 989  TYR   B C   1 
ATOM   5267 O O   . TYR   B 1 333 ? 23.963  34.429 37.481  1.00 19.85  ? 989  TYR   B O   1 
ATOM   5268 C CB  . TYR   B 1 333 ? 21.897  35.776 39.333  1.00 21.00  ? 989  TYR   B CB  1 
ATOM   5269 C CG  . TYR   B 1 333 ? 20.559  35.735 40.035  1.00 21.01  ? 989  TYR   B CG  1 
ATOM   5270 C CD1 . TYR   B 1 333 ? 20.027  34.533 40.500  1.00 22.43  ? 989  TYR   B CD1 1 
ATOM   5271 C CD2 . TYR   B 1 333 ? 19.829  36.896 40.243  1.00 22.56  ? 989  TYR   B CD2 1 
ATOM   5272 C CE1 . TYR   B 1 333 ? 18.782  34.485 41.123  1.00 22.10  ? 989  TYR   B CE1 1 
ATOM   5273 C CE2 . TYR   B 1 333 ? 18.598  36.867 40.893  1.00 24.85  ? 989  TYR   B CE2 1 
ATOM   5274 C CZ  . TYR   B 1 333 ? 18.082  35.661 41.344  1.00 33.45  ? 989  TYR   B CZ  1 
ATOM   5275 O OH  . TYR   B 1 333 ? 16.876  35.652 42.009  1.00 35.08  ? 989  TYR   B OH  1 
ATOM   5276 N N   . ILE   B 1 334 ? 23.558  36.336 36.344  1.00 19.81  ? 990  ILE   B N   1 
ATOM   5277 C CA  . ILE   B 1 334 ? 24.844  36.366 35.642  1.00 18.39  ? 990  ILE   B CA  1 
ATOM   5278 C C   . ILE   B 1 334 ? 25.540  37.700 35.877  1.00 22.01  ? 990  ILE   B C   1 
ATOM   5279 O O   . ILE   B 1 334 ? 24.928  38.748 35.686  1.00 22.98  ? 990  ILE   B O   1 
ATOM   5280 C CB  . ILE   B 1 334 ? 24.711  36.017 34.111  1.00 20.72  ? 990  ILE   B CB  1 
ATOM   5281 C CG1 . ILE   B 1 334 ? 23.744  34.835 33.830  1.00 19.06  ? 990  ILE   B CG1 1 
ATOM   5282 C CG2 . ILE   B 1 334 ? 26.066  35.771 33.453  1.00 20.02  ? 990  ILE   B CG2 1 
ATOM   5283 C CD1 . ILE   B 1 334 ? 22.275  35.147 33.707  1.00 13.83  ? 990  ILE   B CD1 1 
ATOM   5284 N N   . VAL   B 1 335 ? 26.801  37.645 36.333  1.00 18.01  ? 991  VAL   B N   1 
ATOM   5285 C CA  . VAL   B 1 335 ? 27.712  38.787 36.535  1.00 18.08  ? 991  VAL   B CA  1 
ATOM   5286 C C   . VAL   B 1 335 ? 28.846  38.683 35.491  1.00 24.12  ? 991  VAL   B C   1 
ATOM   5287 O O   . VAL   B 1 335 ? 29.240  37.582 35.120  1.00 24.43  ? 991  VAL   B O   1 
ATOM   5288 C CB  . VAL   B 1 335 ? 28.216  39.001 37.987  1.00 21.19  ? 991  VAL   B CB  1 
ATOM   5289 C CG1 . VAL   B 1 335 ? 27.068  39.418 38.906  1.00 20.14  ? 991  VAL   B CG1 1 
ATOM   5290 C CG2 . VAL   B 1 335 ? 28.975  37.788 38.532  1.00 20.05  ? 991  VAL   B CG2 1 
ATOM   5291 N N   . TYR   B 1 336 ? 29.297  39.811 34.963  1.00 21.96  ? 992  TYR   B N   1 
ATOM   5292 C CA  . TYR   B 1 336 ? 30.267  39.848 33.872  1.00 21.65  ? 992  TYR   B CA  1 
ATOM   5293 C C   . TYR   B 1 336 ? 31.628  40.397 34.322  1.00 29.24  ? 992  TYR   B C   1 
ATOM   5294 O O   . TYR   B 1 336 ? 32.533  40.584 33.500  1.00 30.40  ? 992  TYR   B O   1 
ATOM   5295 C CB  . TYR   B 1 336 ? 29.653  40.603 32.657  1.00 22.65  ? 992  TYR   B CB  1 
ATOM   5296 C CG  . TYR   B 1 336 ? 28.349  39.971 32.182  1.00 23.50  ? 992  TYR   B CG  1 
ATOM   5297 C CD1 . TYR   B 1 336 ? 27.139  40.252 32.818  1.00 24.57  ? 992  TYR   B CD1 1 
ATOM   5298 C CD2 . TYR   B 1 336 ? 28.340  39.038 31.149  1.00 23.67  ? 992  TYR   B CD2 1 
ATOM   5299 C CE1 . TYR   B 1 336 ? 25.951  39.637 32.428  1.00 22.57  ? 992  TYR   B CE1 1 
ATOM   5300 C CE2 . TYR   B 1 336 ? 27.162  38.407 30.757  1.00 23.94  ? 992  TYR   B CE2 1 
ATOM   5301 C CZ  . TYR   B 1 336 ? 25.967  38.714 31.396  1.00 29.96  ? 992  TYR   B CZ  1 
ATOM   5302 O OH  . TYR   B 1 336 ? 24.802  38.114 31.003  1.00 25.86  ? 992  TYR   B OH  1 
ATOM   5303 N N   . ASP   B 1 337 ? 31.801  40.558 35.646  1.00 25.72  ? 993  ASP   B N   1 
ATOM   5304 C CA  . ASP   B 1 337 ? 33.063  40.971 36.270  1.00 24.32  ? 993  ASP   B CA  1 
ATOM   5305 C C   . ASP   B 1 337 ? 33.318  39.992 37.427  1.00 26.20  ? 993  ASP   B C   1 
ATOM   5306 O O   . ASP   B 1 337 ? 32.484  39.868 38.324  1.00 23.93  ? 993  ASP   B O   1 
ATOM   5307 C CB  . ASP   B 1 337 ? 32.979  42.426 36.772  1.00 25.44  ? 993  ASP   B CB  1 
ATOM   5308 C CG  . ASP   B 1 337 ? 34.253  43.047 37.321  1.00 33.85  ? 993  ASP   B CG  1 
ATOM   5309 O OD1 . ASP   B 1 337 ? 35.147  42.294 37.767  1.00 36.56  ? 993  ASP   B OD1 1 
ATOM   5310 O OD2 . ASP   B 1 337 ? 34.341  44.283 37.338  1.00 39.78  ? 993  ASP   B OD2 1 
ATOM   5311 N N   . ILE   B 1 338 ? 34.483  39.314 37.412  1.00 22.69  ? 994  ILE   B N   1 
ATOM   5312 C CA  . ILE   B 1 338 ? 34.872  38.334 38.444  1.00 22.02  ? 994  ILE   B CA  1 
ATOM   5313 C C   . ILE   B 1 338 ? 34.928  38.948 39.859  1.00 25.10  ? 994  ILE   B C   1 
ATOM   5314 O O   . ILE   B 1 338 ? 34.705  38.224 40.824  1.00 24.41  ? 994  ILE   B O   1 
ATOM   5315 C CB  . ILE   B 1 338 ? 36.175  37.556 38.090  1.00 24.50  ? 994  ILE   B CB  1 
ATOM   5316 C CG1 . ILE   B 1 338 ? 37.413  38.504 37.960  1.00 25.12  ? 994  ILE   B CG1 1 
ATOM   5317 C CG2 . ILE   B 1 338 ? 35.954  36.696 36.813  1.00 23.92  ? 994  ILE   B CG2 1 
ATOM   5318 C CD1 . ILE   B 1 338 ? 38.790  37.808 37.948  1.00 22.01  ? 994  ILE   B CD1 1 
ATOM   5319 N N   . ALA   B 1 339 ? 35.180  40.270 39.969  1.00 21.92  ? 995  ALA   B N   1 
ATOM   5320 C CA  . ALA   B 1 339 ? 35.271  40.986 41.245  1.00 22.83  ? 995  ALA   B CA  1 
ATOM   5321 C C   . ALA   B 1 339 ? 33.943  41.087 42.023  1.00 29.99  ? 995  ALA   B C   1 
ATOM   5322 O O   . ALA   B 1 339 ? 33.968  41.246 43.254  1.00 30.53  ? 995  ALA   B O   1 
ATOM   5323 C CB  . ALA   B 1 339 ? 35.877  42.362 41.041  1.00 22.80  ? 995  ALA   B CB  1 
ATOM   5324 N N   . GLN   B 1 340 ? 32.795  40.958 41.307  1.00 25.80  ? 996  GLN   B N   1 
ATOM   5325 C CA  . GLN   B 1 340 ? 31.410  40.996 41.816  1.00 24.63  ? 996  GLN   B CA  1 
ATOM   5326 C C   . GLN   B 1 340 ? 30.990  39.719 42.629  1.00 27.97  ? 996  GLN   B C   1 
ATOM   5327 O O   . GLN   B 1 340 ? 29.857  39.628 43.119  1.00 26.18  ? 996  GLN   B O   1 
ATOM   5328 C CB  . GLN   B 1 340 ? 30.443  41.228 40.640  1.00 25.27  ? 996  GLN   B CB  1 
ATOM   5329 C CG  . GLN   B 1 340 ? 30.460  42.651 40.087  1.00 32.55  ? 996  GLN   B CG  1 
ATOM   5330 C CD  . GLN   B 1 340 ? 29.473  42.873 38.960  1.00 38.69  ? 996  GLN   B CD  1 
ATOM   5331 O OE1 . GLN   B 1 340 ? 29.840  42.930 37.793  1.00 33.94  ? 996  GLN   B OE1 1 
ATOM   5332 N NE2 . GLN   B 1 340 ? 28.195  43.018 39.275  1.00 38.80  ? 996  GLN   B NE2 1 
ATOM   5333 N N   . VAL   B 1 341 ? 31.916  38.747 42.769  1.00 25.48  ? 997  VAL   B N   1 
ATOM   5334 C CA  . VAL   B 1 341 ? 31.705  37.486 43.495  1.00 24.30  ? 997  VAL   B CA  1 
ATOM   5335 C C   . VAL   B 1 341 ? 32.643  37.374 44.711  1.00 29.07  ? 997  VAL   B C   1 
ATOM   5336 O O   . VAL   B 1 341 ? 33.864  37.496 44.578  1.00 28.44  ? 997  VAL   B O   1 
ATOM   5337 C CB  . VAL   B 1 341 ? 31.847  36.235 42.574  1.00 26.07  ? 997  VAL   B CB  1 
ATOM   5338 C CG1 . VAL   B 1 341 ? 31.503  34.950 43.330  1.00 25.20  ? 997  VAL   B CG1 1 
ATOM   5339 C CG2 . VAL   B 1 341 ? 31.010  36.362 41.300  1.00 25.33  ? 997  VAL   B CG2 1 
ATOM   5340 N N   . ASN   B 1 342 ? 32.060  37.116 45.888  1.00 26.40  ? 998  ASN   B N   1 
ATOM   5341 C CA  . ASN   B 1 342 ? 32.819  36.839 47.098  1.00 25.69  ? 998  ASN   B CA  1 
ATOM   5342 C C   . ASN   B 1 342 ? 32.320  35.494 47.636  1.00 26.93  ? 998  ASN   B C   1 
ATOM   5343 O O   . ASN   B 1 342 ? 31.209  35.413 48.172  1.00 26.57  ? 998  ASN   B O   1 
ATOM   5344 C CB  . ASN   B 1 342 ? 32.709  37.963 48.144  1.00 24.78  ? 998  ASN   B CB  1 
ATOM   5345 C CG  . ASN   B 1 342 ? 33.665  37.841 49.335  1.00 38.24  ? 998  ASN   B CG  1 
ATOM   5346 O OD1 . ASN   B 1 342 ? 33.408  38.392 50.404  1.00 36.57  ? 998  ASN   B OD1 1 
ATOM   5347 N ND2 . ASN   B 1 342 ? 34.793  37.133 49.203  1.00 22.16  ? 998  ASN   B ND2 1 
ATOM   5348 N N   . LEU   B 1 343 ? 33.120  34.428 47.423  1.00 21.57  ? 999  LEU   B N   1 
ATOM   5349 C CA  . LEU   B 1 343 ? 32.776  33.073 47.873  1.00 21.97  ? 999  LEU   B CA  1 
ATOM   5350 C C   . LEU   B 1 343 ? 32.676  33.016 49.385  1.00 23.96  ? 999  LEU   B C   1 
ATOM   5351 O O   . LEU   B 1 343 ? 33.575  33.505 50.075  1.00 23.41  ? 999  LEU   B O   1 
ATOM   5352 C CB  . LEU   B 1 343 ? 33.760  32.015 47.343  1.00 21.69  ? 999  LEU   B CB  1 
ATOM   5353 C CG  . LEU   B 1 343 ? 33.840  31.839 45.824  1.00 26.28  ? 999  LEU   B CG  1 
ATOM   5354 C CD1 . LEU   B 1 343 ? 34.786  30.699 45.472  1.00 26.68  ? 999  LEU   B CD1 1 
ATOM   5355 C CD2 . LEU   B 1 343 ? 32.452  31.630 45.191  1.00 27.11  ? 999  LEU   B CD2 1 
ATOM   5356 N N   . LYS   B 1 344 ? 31.557  32.466 49.896  1.00 18.97  ? 1000 LYS   B N   1 
ATOM   5357 C CA  . LYS   B 1 344 ? 31.346  32.463 51.333  1.00 20.08  ? 1000 LYS   B CA  1 
ATOM   5358 C C   . LYS   B 1 344 ? 31.360  31.081 51.939  1.00 24.08  ? 1000 LYS   B C   1 
ATOM   5359 O O   . LYS   B 1 344 ? 32.002  30.876 52.966  1.00 24.84  ? 1000 LYS   B O   1 
ATOM   5360 C CB  . LYS   B 1 344 ? 30.058  33.238 51.699  1.00 22.34  ? 1000 LYS   B CB  1 
ATOM   5361 C CG  . LYS   B 1 344 ? 30.211  34.751 51.558  1.00 34.51  ? 1000 LYS   B CG  1 
ATOM   5362 C CD  . LYS   B 1 344 ? 30.839  35.356 52.824  1.00 43.25  ? 1000 LYS   B CD  1 
ATOM   5363 C CE  . LYS   B 1 344 ? 31.785  36.489 52.526  1.00 45.94  ? 1000 LYS   B CE  1 
ATOM   5364 N NZ  . LYS   B 1 344 ? 32.796  36.652 53.610  1.00 54.50  ? 1000 LYS   B NZ  1 
ATOM   5365 N N   . TYR   B 1 345 ? 30.681  30.130 51.295  1.00 19.89  ? 1001 TYR   B N   1 
ATOM   5366 C CA  . TYR   B 1 345 ? 30.602  28.770 51.796  1.00 19.62  ? 1001 TYR   B CA  1 
ATOM   5367 C C   . TYR   B 1 345 ? 30.783  27.768 50.704  1.00 23.95  ? 1001 TYR   B C   1 
ATOM   5368 O O   . TYR   B 1 345 ? 30.603  28.073 49.523  1.00 22.50  ? 1001 TYR   B O   1 
ATOM   5369 C CB  . TYR   B 1 345 ? 29.251  28.513 52.515  1.00 20.40  ? 1001 TYR   B CB  1 
ATOM   5370 C CG  . TYR   B 1 345 ? 28.987  29.467 53.655  1.00 22.62  ? 1001 TYR   B CG  1 
ATOM   5371 C CD1 . TYR   B 1 345 ? 29.553  29.258 54.914  1.00 25.27  ? 1001 TYR   B CD1 1 
ATOM   5372 C CD2 . TYR   B 1 345 ? 28.174  30.581 53.481  1.00 23.52  ? 1001 TYR   B CD2 1 
ATOM   5373 C CE1 . TYR   B 1 345 ? 29.325  30.147 55.963  1.00 26.00  ? 1001 TYR   B CE1 1 
ATOM   5374 C CE2 . TYR   B 1 345 ? 27.937  31.473 54.524  1.00 24.34  ? 1001 TYR   B CE2 1 
ATOM   5375 C CZ  . TYR   B 1 345 ? 28.527  31.259 55.758  1.00 30.08  ? 1001 TYR   B CZ  1 
ATOM   5376 O OH  . TYR   B 1 345 ? 28.293  32.146 56.775  1.00 33.23  ? 1001 TYR   B OH  1 
ATOM   5377 N N   . LEU   B 1 346 ? 31.137  26.550 51.131  1.00 21.14  ? 1002 LEU   B N   1 
ATOM   5378 C CA  . LEU   B 1 346 ? 31.270  25.364 50.318  1.00 20.73  ? 1002 LEU   B CA  1 
ATOM   5379 C C   . LEU   B 1 346 ? 30.552  24.269 51.081  1.00 25.48  ? 1002 LEU   B C   1 
ATOM   5380 O O   . LEU   B 1 346 ? 30.821  24.068 52.270  1.00 23.88  ? 1002 LEU   B O   1 
ATOM   5381 C CB  . LEU   B 1 346 ? 32.749  25.003 50.103  1.00 20.61  ? 1002 LEU   B CB  1 
ATOM   5382 C CG  . LEU   B 1 346 ? 33.056  23.757 49.244  1.00 25.34  ? 1002 LEU   B CG  1 
ATOM   5383 C CD1 . LEU   B 1 346 ? 32.307  23.797 47.904  1.00 24.73  ? 1002 LEU   B CD1 1 
ATOM   5384 C CD2 . LEU   B 1 346 ? 34.558  23.636 48.992  1.00 26.05  ? 1002 LEU   B CD2 1 
ATOM   5385 N N   . LEU   B 1 347 ? 29.612  23.586 50.412  1.00 23.38  ? 1003 LEU   B N   1 
ATOM   5386 C CA  . LEU   B 1 347 ? 28.854  22.503 51.032  1.00 23.11  ? 1003 LEU   B CA  1 
ATOM   5387 C C   . LEU   B 1 347 ? 29.158  21.187 50.351  1.00 24.03  ? 1003 LEU   B C   1 
ATOM   5388 O O   . LEU   B 1 347 ? 29.239  21.138 49.127  1.00 23.49  ? 1003 LEU   B O   1 
ATOM   5389 C CB  . LEU   B 1 347 ? 27.355  22.768 50.929  1.00 23.37  ? 1003 LEU   B CB  1 
ATOM   5390 C CG  . LEU   B 1 347 ? 26.661  23.608 51.996  1.00 28.56  ? 1003 LEU   B CG  1 
ATOM   5391 C CD1 . LEU   B 1 347 ? 27.001  25.080 51.847  1.00 28.75  ? 1003 LEU   B CD1 1 
ATOM   5392 C CD2 . LEU   B 1 347 ? 25.134  23.431 51.893  1.00 30.55  ? 1003 LEU   B CD2 1 
ATOM   5393 N N   . LYS   B 1 348 ? 29.334  20.127 51.154  1.00 18.52  ? 1004 LYS   B N   1 
ATOM   5394 C CA  . LYS   B 1 348 ? 29.494  18.763 50.686  1.00 18.20  ? 1004 LYS   B CA  1 
ATOM   5395 C C   . LYS   B 1 348 ? 28.121  18.169 50.866  1.00 22.42  ? 1004 LYS   B C   1 
ATOM   5396 O O   . LYS   B 1 348 ? 27.586  18.218 51.975  1.00 19.87  ? 1004 LYS   B O   1 
ATOM   5397 C CB  . LYS   B 1 348 ? 30.548  17.990 51.501  1.00 19.96  ? 1004 LYS   B CB  1 
ATOM   5398 C CG  . LYS   B 1 348 ? 30.781  16.569 51.018  1.00 24.26  ? 1004 LYS   B CG  1 
ATOM   5399 C CD  . LYS   B 1 348 ? 32.138  16.055 51.492  1.00 37.23  ? 1004 LYS   B CD  1 
ATOM   5400 C CE  . LYS   B 1 348 ? 32.028  14.835 52.378  1.00 41.18  ? 1004 LYS   B CE  1 
ATOM   5401 N NZ  . LYS   B 1 348 ? 33.316  14.540 53.063  1.00 47.91  ? 1004 LYS   B NZ  1 
ATOM   5402 N N   . LEU   B 1 349 ? 27.519  17.682 49.769  1.00 21.95  ? 1005 LEU   B N   1 
ATOM   5403 C CA  . LEU   B 1 349 ? 26.169  17.108 49.818  1.00 22.35  ? 1005 LEU   B CA  1 
ATOM   5404 C C   . LEU   B 1 349 ? 26.113  15.673 49.352  1.00 25.98  ? 1005 LEU   B C   1 
ATOM   5405 O O   . LEU   B 1 349 ? 26.782  15.281 48.400  1.00 26.52  ? 1005 LEU   B O   1 
ATOM   5406 C CB  . LEU   B 1 349 ? 25.184  17.922 48.945  1.00 23.22  ? 1005 LEU   B CB  1 
ATOM   5407 C CG  . LEU   B 1 349 ? 25.026  19.429 49.169  1.00 28.69  ? 1005 LEU   B CG  1 
ATOM   5408 C CD1 . LEU   B 1 349 ? 24.225  20.022 48.048  1.00 30.72  ? 1005 LEU   B CD1 1 
ATOM   5409 C CD2 . LEU   B 1 349 ? 24.283  19.724 50.452  1.00 26.39  ? 1005 LEU   B CD2 1 
ATOM   5410 N N   . LYS   B 1 350 ? 25.255  14.915 49.978  1.00 24.57  ? 1006 LYS   B N   1 
ATOM   5411 C CA  . LYS   B 1 350 ? 24.957  13.569 49.555  1.00 25.52  ? 1006 LYS   B CA  1 
ATOM   5412 C C   . LYS   B 1 350 ? 23.618  13.676 48.784  1.00 32.05  ? 1006 LYS   B C   1 
ATOM   5413 O O   . LYS   B 1 350 ? 22.636  14.280 49.271  1.00 30.18  ? 1006 LYS   B O   1 
ATOM   5414 C CB  . LYS   B 1 350 ? 24.830  12.631 50.755  1.00 27.41  ? 1006 LYS   B CB  1 
ATOM   5415 C CG  . LYS   B 1 350 ? 25.041  11.174 50.418  1.00 31.41  ? 1006 LYS   B CG  1 
ATOM   5416 C CD  . LYS   B 1 350 ? 24.729  10.327 51.655  1.00 47.68  ? 1006 LYS   B CD  1 
ATOM   5417 C CE  . LYS   B 1 350 ? 25.640  9.130  51.854  1.00 61.63  ? 1006 LYS   B CE  1 
ATOM   5418 N NZ  . LYS   B 1 350 ? 25.463  8.102  50.793  1.00 72.68  ? 1006 LYS   B NZ  1 
ATOM   5419 N N   . PHE   B 1 351 ? 23.616  13.135 47.554  1.00 30.33  ? 1007 PHE   B N   1 
ATOM   5420 C CA  . PHE   B 1 351 ? 22.459  13.064 46.662  1.00 29.50  ? 1007 PHE   B CA  1 
ATOM   5421 C C   . PHE   B 1 351 ? 21.840  11.700 46.848  1.00 34.82  ? 1007 PHE   B C   1 
ATOM   5422 O O   . PHE   B 1 351 ? 22.501  10.686 46.597  1.00 35.01  ? 1007 PHE   B O   1 
ATOM   5423 C CB  . PHE   B 1 351 ? 22.894  13.248 45.197  1.00 30.38  ? 1007 PHE   B CB  1 
ATOM   5424 C CG  . PHE   B 1 351 ? 23.329  14.646 44.833  1.00 30.67  ? 1007 PHE   B CG  1 
ATOM   5425 C CD1 . PHE   B 1 351 ? 24.521  15.174 45.325  1.00 32.50  ? 1007 PHE   B CD1 1 
ATOM   5426 C CD2 . PHE   B 1 351 ? 22.570  15.423 43.969  1.00 31.07  ? 1007 PHE   B CD2 1 
ATOM   5427 C CE1 . PHE   B 1 351 ? 24.923  16.466 44.991  1.00 32.66  ? 1007 PHE   B CE1 1 
ATOM   5428 C CE2 . PHE   B 1 351 ? 22.971  16.714 43.633  1.00 33.53  ? 1007 PHE   B CE2 1 
ATOM   5429 C CZ  . PHE   B 1 351 ? 24.146  17.227 44.146  1.00 31.94  ? 1007 PHE   B CZ  1 
ATOM   5430 N N   . ASN   B 1 352 ? 20.609  11.653 47.358  1.00 32.93  ? 1008 ASN   B N   1 
ATOM   5431 C CA  . ASN   B 1 352 ? 19.927  10.374 47.571  1.00 32.72  ? 1008 ASN   B CA  1 
ATOM   5432 C C   . ASN   B 1 352 ? 18.896  10.177 46.458  1.00 38.62  ? 1008 ASN   B C   1 
ATOM   5433 O O   . ASN   B 1 352 ? 17.816  10.769 46.491  1.00 36.92  ? 1008 ASN   B O   1 
ATOM   5434 C CB  . ASN   B 1 352 ? 19.372  10.243 49.010  1.00 32.40  ? 1008 ASN   B CB  1 
ATOM   5435 C CG  . ASN   B 1 352 ? 20.460  10.060 50.069  1.00 61.16  ? 1008 ASN   B CG  1 
ATOM   5436 O OD1 . ASN   B 1 352 ? 21.031  8.970  50.233  1.00 56.95  ? 1008 ASN   B OD1 1 
ATOM   5437 N ND2 . ASN   B 1 352 ? 20.784  11.121 50.813  1.00 50.40  ? 1008 ASN   B ND2 1 
ATOM   5438 N N   . PHE   B 1 353 ? 19.307  9.442  45.402  1.00 37.59  ? 1009 PHE   B N   1 
ATOM   5439 C CA  . PHE   B 1 353 ? 18.499  9.178  44.209  1.00 37.92  ? 1009 PHE   B CA  1 
ATOM   5440 C C   . PHE   B 1 353 ? 17.338  8.253  44.501  1.00 45.02  ? 1009 PHE   B C   1 
ATOM   5441 O O   . PHE   B 1 353 ? 17.525  7.187  45.096  1.00 44.04  ? 1009 PHE   B O   1 
ATOM   5442 C CB  . PHE   B 1 353 ? 19.378  8.628  43.056  1.00 39.58  ? 1009 PHE   B CB  1 
ATOM   5443 C CG  . PHE   B 1 353 ? 20.429  9.600  42.579  1.00 40.80  ? 1009 PHE   B CG  1 
ATOM   5444 C CD1 . PHE   B 1 353 ? 20.128  10.558 41.624  1.00 43.93  ? 1009 PHE   B CD1 1 
ATOM   5445 C CD2 . PHE   B 1 353 ? 21.705  9.598  43.130  1.00 42.61  ? 1009 PHE   B CD2 1 
ATOM   5446 C CE1 . PHE   B 1 353 ? 21.099  11.477 41.204  1.00 44.11  ? 1009 PHE   B CE1 1 
ATOM   5447 C CE2 . PHE   B 1 353 ? 22.662  10.529 42.723  1.00 44.90  ? 1009 PHE   B CE2 1 
ATOM   5448 C CZ  . PHE   B 1 353 ? 22.355  11.461 41.765  1.00 42.71  ? 1009 PHE   B CZ  1 
ATOM   5449 N N   . LYS   B 1 354 ? 16.127  8.682  44.140  1.00 44.34  ? 1010 LYS   B N   1 
ATOM   5450 C CA  . LYS   B 1 354 ? 14.946  7.845  44.322  1.00 45.52  ? 1010 LYS   B CA  1 
ATOM   5451 C C   . LYS   B 1 354 ? 14.675  7.188  42.978  1.00 51.98  ? 1010 LYS   B C   1 
ATOM   5452 O O   . LYS   B 1 354 ? 14.566  7.875  41.947  1.00 51.41  ? 1010 LYS   B O   1 
ATOM   5453 C CB  . LYS   B 1 354 ? 13.740  8.631  44.862  1.00 48.02  ? 1010 LYS   B CB  1 
ATOM   5454 C CG  . LYS   B 1 354 ? 13.865  8.958  46.357  1.00 50.41  ? 1010 LYS   B CG  1 
ATOM   5455 C CD  . LYS   B 1 354 ? 13.191  10.267 46.721  1.00 51.43  ? 1010 LYS   B CD  1 
ATOM   5456 C CE  . LYS   B 1 354 ? 13.829  11.459 46.056  1.00 57.81  ? 1010 LYS   B CE  1 
ATOM   5457 N NZ  . LYS   B 1 354 ? 12.933  12.644 46.116  1.00 64.14  ? 1010 LYS   B NZ  1 
ATOM   5458 N N   . THR   B 1 355 ? 14.673  5.843  42.992  1.00 49.61  ? 1011 THR   B N   1 
ATOM   5459 C CA  . THR   B 1 355 ? 14.514  4.983  41.816  1.00 81.02  ? 1011 THR   B CA  1 
ATOM   5460 C C   . THR   B 1 355 ? 13.078  4.998  41.294  1.00 90.02  ? 1011 THR   B C   1 
ATOM   5461 O O   . THR   B 1 355 ? 12.357  4.012  41.416  1.00 51.35  ? 1011 THR   B O   1 
ATOM   5462 C CB  . THR   B 1 355 ? 15.055  3.568  42.108  1.00 87.31  ? 1011 THR   B CB  1 
ATOM   5463 O OG1 . THR   B 1 355 ? 14.462  3.079  43.317  1.00 86.48  ? 1011 THR   B OG1 1 
ATOM   5464 C CG2 . THR   B 1 355 ? 16.586  3.528  42.203  1.00 83.81  ? 1011 THR   B CG2 1 
HETATM 5465 C C1  . A1H64 C 2 .   ? 1.344   41.855 11.900  1.00 25.42  ? 1101 A1H64 A C1  1 
HETATM 5466 C C2  . A1H64 C 2 .   ? 2.564   41.601 11.057  1.00 23.27  ? 1101 A1H64 A C2  1 
HETATM 5467 C C3  . A1H64 C 2 .   ? 2.475   41.680 9.670   1.00 22.21  ? 1101 A1H64 A C3  1 
HETATM 5468 C C7  . A1H64 C 2 .   ? 8.452   41.032 8.764   1.00 20.35  ? 1101 A1H64 A C7  1 
HETATM 5469 C C8  . A1H64 C 2 .   ? 9.698   39.865 7.039   1.00 18.17  ? 1101 A1H64 A C8  1 
HETATM 5470 C C9  . A1H64 C 2 .   ? 10.988  40.635 7.217   1.00 17.24  ? 1101 A1H64 A C9  1 
HETATM 5471 C C10 . A1H64 C 2 .   ? 11.779  40.463 8.363   1.00 17.10  ? 1101 A1H64 A C10 1 
HETATM 5472 C C11 . A1H64 C 2 .   ? 12.976  41.140 8.551   1.00 15.34  ? 1101 A1H64 A C11 1 
HETATM 5473 C C12 . A1H64 C 2 .   ? 13.434  42.027 7.575   1.00 14.20  ? 1101 A1H64 A C12 1 
HETATM 5474 C C13 . A1H64 C 2 .   ? 15.046  43.517 6.865   1.00 11.20  ? 1101 A1H64 A C13 1 
HETATM 5475 C C14 . A1H64 C 2 .   ? 16.336  44.244 7.064   1.00 10.89  ? 1101 A1H64 A C14 1 
HETATM 5476 C C15 . A1H64 C 2 .   ? 14.289  43.800 5.564   1.00 10.32  ? 1101 A1H64 A C15 1 
HETATM 5477 C C16 . A1H64 C 2 .   ? 12.648  42.226 6.378   1.00 14.13  ? 1101 A1H64 A C16 1 
HETATM 5478 C C19 . A1H64 C 2 .   ? 5.984   40.361 7.493   1.00 23.67  ? 1101 A1H64 A C19 1 
HETATM 5479 C C20 . A1H64 C 2 .   ? 4.763   41.074 10.972  1.00 22.48  ? 1101 A1H64 A C20 1 
HETATM 5480 F F1  . A1H64 C 2 .   ? 5.882   40.777 11.643  1.00 24.33  ? 1101 A1H64 A F1  1 
HETATM 5481 N N5  . A1H64 C 2 .   ? 3.701   41.299 11.702  1.00 22.32  ? 1101 A1H64 A N5  1 
HETATM 5482 O O   . A1H64 C 2 .   ? 0.241   42.003 11.386  1.00 26.19  ? 1101 A1H64 A O   1 
HETATM 5483 N N   . A1H64 C 2 .   ? 1.550   41.878 13.218  1.00 22.97  ? 1101 A1H64 A N   1 
HETATM 5484 C C   . A1H64 C 2 .   ? 0.478   42.127 14.163  1.00 20.51  ? 1101 A1H64 A C   1 
HETATM 5485 C C5  . A1H64 C 2 .   ? 4.808   41.125 9.571   1.00 24.16  ? 1101 A1H64 A C5  1 
HETATM 5486 C C4  . A1H64 C 2 .   ? 3.615   41.438 8.917   1.00 23.40  ? 1101 A1H64 A C4  1 
HETATM 5487 N N1  . A1H64 C 2 .   ? 6.026   40.863 8.871   1.00 27.13  ? 1101 A1H64 A N1  1 
HETATM 5488 C C18 . A1H64 C 2 .   ? 7.295   39.674 7.140   1.00 22.39  ? 1101 A1H64 A C18 1 
HETATM 5489 N N2  . A1H64 C 2 .   ? 8.450   40.569 7.366   1.00 19.52  ? 1101 A1H64 A N2  1 
HETATM 5490 C C6  . A1H64 C 2 .   ? 7.165   41.760 9.085   1.00 23.12  ? 1101 A1H64 A C6  1 
HETATM 5491 C C17 . A1H64 C 2 .   ? 11.463  41.519 6.253   1.00 13.99  ? 1101 A1H64 A C17 1 
HETATM 5492 F F   . A1H64 C 2 .   ? 10.739  41.699 5.135   1.00 14.39  ? 1101 A1H64 A F   1 
HETATM 5493 N N4  . A1H64 C 2 .   ? 13.128  43.115 5.422   1.00 12.03  ? 1101 A1H64 A N4  1 
HETATM 5494 O O1  . A1H64 C 2 .   ? 14.683  44.576 4.689   1.00 11.28  ? 1101 A1H64 A O1  1 
HETATM 5495 N N3  . A1H64 C 2 .   ? 14.630  42.698 7.773   1.00 11.73  ? 1101 A1H64 A N3  1 
HETATM 5496 S S   . SO4   D 3 .   ? 24.000  39.796 7.419   1.00 23.60  ? 1102 SO4   A S   1 
HETATM 5497 O O1  . SO4   D 3 .   ? 24.210  39.765 5.978   1.00 26.98  ? 1102 SO4   A O1  1 
HETATM 5498 O O2  . SO4   D 3 .   ? 22.648  39.316 7.688   1.00 28.24  ? 1102 SO4   A O2  1 
HETATM 5499 O O3  . SO4   D 3 .   ? 24.981  38.943 8.096   1.00 23.88  ? 1102 SO4   A O3  1 
HETATM 5500 O O4  . SO4   D 3 .   ? 24.164  41.148 7.889   1.00 24.26  ? 1102 SO4   A O4  1 
HETATM 5501 C C1  . A1H64 E 2 .   ? 38.664  29.868 33.139  1.00 20.89  ? 1101 A1H64 B C1  1 
HETATM 5502 C C2  . A1H64 E 2 .   ? 37.364  29.148 33.398  1.00 20.27  ? 1101 A1H64 B C2  1 
HETATM 5503 C C3  . A1H64 E 2 .   ? 37.356  27.984 34.159  1.00 17.88  ? 1101 A1H64 B C3  1 
HETATM 5504 C C7  . A1H64 E 2 .   ? 31.251  27.332 34.212  1.00 16.42  ? 1101 A1H64 B C7  1 
HETATM 5505 C C8  . A1H64 E 2 .   ? 29.931  25.296 34.335  1.00 20.82  ? 1101 A1H64 B C8  1 
HETATM 5506 C C9  . A1H64 E 2 .   ? 28.676  25.947 34.873  1.00 18.18  ? 1101 A1H64 B C9  1 
HETATM 5507 C C10 . A1H64 E 2 .   ? 27.885  26.765 34.063  1.00 16.93  ? 1101 A1H64 B C10 1 
HETATM 5508 C C11 . A1H64 E 2 .   ? 26.722  27.368 34.522  1.00 17.24  ? 1101 A1H64 B C11 1 
HETATM 5509 C C12 . A1H64 E 2 .   ? 26.305  27.162 35.838  1.00 18.10  ? 1101 A1H64 B C12 1 
HETATM 5510 C C13 . A1H64 E 2 .   ? 24.756  27.577 37.502  1.00 19.61  ? 1101 A1H64 B C13 1 
HETATM 5511 C C14 . A1H64 E 2 .   ? 23.501  28.222 37.992  1.00 17.48  ? 1101 A1H64 B C14 1 
HETATM 5512 C C15 . A1H64 E 2 .   ? 25.526  26.703 38.490  1.00 17.57  ? 1101 A1H64 B C15 1 
HETATM 5513 C C16 . A1H64 E 2 .   ? 27.089  26.326 36.695  1.00 20.08  ? 1101 A1H64 B C16 1 
HETATM 5514 C C19 . A1H64 E 2 .   ? 33.655  25.851 34.553  1.00 18.39  ? 1101 A1H64 B C19 1 
HETATM 5515 C C20 . A1H64 E 2 .   ? 35.117  29.059 33.094  1.00 19.81  ? 1101 A1H64 B C20 1 
HETATM 5516 F F1  . A1H64 E 2 .   ? 34.027  29.619 32.545  1.00 19.05  ? 1101 A1H64 B F1  1 
HETATM 5517 N N5  . A1H64 E 2 .   ? 36.251  29.676 32.871  1.00 18.18  ? 1101 A1H64 B N5  1 
HETATM 5518 O O   . A1H64 E 2 .   ? 39.737  29.384 33.488  1.00 18.49  ? 1101 A1H64 B O   1 
HETATM 5519 N N   . A1H64 E 2 .   ? 38.559  31.036 32.502  1.00 22.04  ? 1101 A1H64 B N   1 
HETATM 5520 C C   . A1H64 E 2 .   ? 39.717  31.851 32.180  1.00 22.10  ? 1101 A1H64 B C   1 
HETATM 5521 C C5  . A1H64 E 2 .   ? 34.967  27.877 33.847  1.00 19.02  ? 1101 A1H64 B C5  1 
HETATM 5522 C C4  . A1H64 E 2 .   ? 36.145  27.351 34.381  1.00 16.73  ? 1101 A1H64 B C4  1 
HETATM 5523 N N1  . A1H64 E 2 .   ? 33.683  27.233 34.055  1.00 20.05  ? 1101 A1H64 B N1  1 
HETATM 5524 C C18 . A1H64 E 2 .   ? 32.343  25.182 34.174  1.00 20.57  ? 1101 A1H64 B C18 1 
HETATM 5525 N N2  . A1H64 E 2 .   ? 31.196  25.947 34.710  1.00 21.27  ? 1101 A1H64 B N2  1 
HETATM 5526 C C6  . A1H64 E 2 .   ? 32.555  27.994 34.597  1.00 18.57  ? 1101 A1H64 B C6  1 
HETATM 5527 C C17 . A1H64 E 2 .   ? 28.243  25.752 36.179  1.00 21.19  ? 1101 A1H64 B C17 1 
HETATM 5528 F F   . A1H64 E 2 .   ? 28.982  24.965 36.988  1.00 19.74  ? 1101 A1H64 B F   1 
HETATM 5529 N N4  . A1H64 E 2 .   ? 26.652  26.138 37.997  1.00 20.33  ? 1101 A1H64 B N4  1 
HETATM 5530 O O1  . A1H64 E 2 .   ? 25.183  26.507 39.645  1.00 17.46  ? 1101 A1H64 B O1  1 
HETATM 5531 N N3  . A1H64 E 2 .   ? 25.142  27.768 36.284  1.00 20.09  ? 1101 A1H64 B N3  1 
HETATM 5532 S S   . SO4   F 3 .   ? 15.907  26.178 33.958  1.00 30.19  ? 1102 SO4   B S   1 
HETATM 5533 O O1  . SO4   F 3 .   ? 17.294  26.390 33.529  1.00 33.11  ? 1102 SO4   B O1  1 
HETATM 5534 O O2  . SO4   F 3 .   ? 15.072  26.208 32.742  1.00 31.39  ? 1102 SO4   B O2  1 
HETATM 5535 O O3  . SO4   F 3 .   ? 15.778  24.893 34.654  1.00 29.15  ? 1102 SO4   B O3  1 
HETATM 5536 O O4  . SO4   F 3 .   ? 15.488  27.192 34.919  1.00 25.94  ? 1102 SO4   B O4  1 
HETATM 5537 O O   . HOH   G 4 .   ? -0.308  42.239 1.951   1.00 25.97  ? 1201 HOH   A O   1 
HETATM 5538 O O   . HOH   G 4 .   ? 8.942   62.252 8.500   1.00 28.11  ? 1202 HOH   A O   1 
HETATM 5539 O O   . HOH   G 4 .   ? 2.354   58.111 18.383  1.00 14.52  ? 1203 HOH   A O   1 
HETATM 5540 O O   . HOH   G 4 .   ? 2.443   44.827 7.901   1.00 18.98  ? 1204 HOH   A O   1 
HETATM 5541 O O   . HOH   G 4 .   ? -12.184 51.612 -2.811  1.00 25.12  ? 1205 HOH   A O   1 
HETATM 5542 O O   . HOH   G 4 .   ? 11.809  50.873 20.082  1.00 14.36  ? 1206 HOH   A O   1 
HETATM 5543 O O   . HOH   G 4 .   ? 28.691  48.946 12.127  1.00 23.01  ? 1207 HOH   A O   1 
HETATM 5544 O O   . HOH   G 4 .   ? 4.336   56.323 12.246  1.00 25.32  ? 1208 HOH   A O   1 
HETATM 5545 O O   . HOH   G 4 .   ? 26.186  55.386 13.632  1.00 18.62  ? 1209 HOH   A O   1 
HETATM 5546 O O   . HOH   G 4 .   ? 25.938  47.575 6.812   1.00 17.23  ? 1210 HOH   A O   1 
HETATM 5547 O O   . HOH   G 4 .   ? 9.182   42.526 -3.655  1.00 11.26  ? 1211 HOH   A O   1 
HETATM 5548 O O   . HOH   G 4 .   ? 17.986  39.658 11.201  1.00 31.29  ? 1212 HOH   A O   1 
HETATM 5549 O O   . HOH   G 4 .   ? 4.188   37.132 1.454   1.00 25.70  ? 1213 HOH   A O   1 
HETATM 5550 O O   . HOH   G 4 .   ? 19.902  39.766 3.180   1.00 18.37  ? 1214 HOH   A O   1 
HETATM 5551 O O   . HOH   G 4 .   ? 7.895   42.818 5.746   1.00 19.16  ? 1215 HOH   A O   1 
HETATM 5552 O O   . HOH   G 4 .   ? 36.366  39.313 13.598  1.00 37.21  ? 1216 HOH   A O   1 
HETATM 5553 O O   . HOH   G 4 .   ? 5.416   51.129 11.665  1.00 28.80  ? 1217 HOH   A O   1 
HETATM 5554 O O   . HOH   G 4 .   ? -2.274  41.297 12.185  1.00 23.36  ? 1218 HOH   A O   1 
HETATM 5555 O O   . HOH   G 4 .   ? 27.607  51.942 15.559  1.00 24.37  ? 1219 HOH   A O   1 
HETATM 5556 O O   . HOH   G 4 .   ? 22.712  47.083 6.272   1.00 15.60  ? 1220 HOH   A O   1 
HETATM 5557 O O   . HOH   G 4 .   ? -5.959  32.702 18.393  1.00 18.16  ? 1221 HOH   A O   1 
HETATM 5558 O O   . HOH   G 4 .   ? 34.726  45.286 10.943  1.00 23.79  ? 1222 HOH   A O   1 
HETATM 5559 O O   . HOH   G 4 .   ? 8.533   39.441 -4.721  1.00 31.20  ? 1223 HOH   A O   1 
HETATM 5560 O O   . HOH   G 4 .   ? 22.828  47.176 -8.627  1.00 20.35  ? 1224 HOH   A O   1 
HETATM 5561 O O   . HOH   G 4 .   ? 2.050   50.322 11.474  1.00 16.89  ? 1225 HOH   A O   1 
HETATM 5562 O O   . HOH   G 4 .   ? 4.232   55.429 21.113  1.00 30.38  ? 1226 HOH   A O   1 
HETATM 5563 O O   . HOH   G 4 .   ? 27.065  56.646 4.596   1.00 22.84  ? 1227 HOH   A O   1 
HETATM 5564 O O   . HOH   G 4 .   ? 8.591   39.464 3.379   1.00 19.05  ? 1228 HOH   A O   1 
HETATM 5565 O O   . HOH   G 4 .   ? -2.004  39.448 14.608  1.00 24.22  ? 1229 HOH   A O   1 
HETATM 5566 O O   . HOH   G 4 .   ? 4.877   51.709 8.869   1.00 17.87  ? 1230 HOH   A O   1 
HETATM 5567 O O   . HOH   G 4 .   ? 0.328   42.538 -1.181  1.00 17.48  ? 1231 HOH   A O   1 
HETATM 5568 O O   . HOH   G 4 .   ? 18.234  62.914 13.058  1.00 26.21  ? 1232 HOH   A O   1 
HETATM 5569 O O   . HOH   G 4 .   ? 8.473   41.277 14.513  1.00 29.31  ? 1233 HOH   A O   1 
HETATM 5570 O O   . HOH   G 4 .   ? -13.062 41.649 4.649   1.00 21.96  ? 1234 HOH   A O   1 
HETATM 5571 O O   . HOH   G 4 .   ? -2.405  53.816 5.243   1.00 24.08  ? 1235 HOH   A O   1 
HETATM 5572 O O   . HOH   G 4 .   ? 2.325   43.307 17.386  1.00 23.23  ? 1236 HOH   A O   1 
HETATM 5573 O O   . HOH   G 4 .   ? -8.761  37.539 10.250  1.00 16.74  ? 1237 HOH   A O   1 
HETATM 5574 O O   . HOH   G 4 .   ? 9.887   57.261 -11.171 1.00 18.06  ? 1238 HOH   A O   1 
HETATM 5575 O O   . HOH   G 4 .   ? 9.436   32.869 4.695   1.00 34.43  ? 1239 HOH   A O   1 
HETATM 5576 O O   . HOH   G 4 .   ? 10.637  43.432 10.389  1.00 16.68  ? 1240 HOH   A O   1 
HETATM 5577 O O   . HOH   G 4 .   ? 4.079   49.397 18.715  1.00 15.91  ? 1241 HOH   A O   1 
HETATM 5578 O O   . HOH   G 4 .   ? -1.209  53.772 11.179  1.00 36.98  ? 1242 HOH   A O   1 
HETATM 5579 O O   . HOH   G 4 .   ? 24.731  50.482 23.235  1.00 24.72  ? 1243 HOH   A O   1 
HETATM 5580 O O   . HOH   G 4 .   ? 2.379   45.548 15.492  1.00 17.77  ? 1244 HOH   A O   1 
HETATM 5581 O O   . HOH   G 4 .   ? 9.518   30.643 1.570   1.00 44.67  ? 1245 HOH   A O   1 
HETATM 5582 O O   . HOH   G 4 .   ? 23.934  67.023 3.668   1.00 24.74  ? 1246 HOH   A O   1 
HETATM 5583 O O   . HOH   G 4 .   ? 10.736  12.623 0.321   1.00 33.10  ? 1247 HOH   A O   1 
HETATM 5584 O O   . HOH   G 4 .   ? 0.214   67.020 14.081  1.00 50.79  ? 1248 HOH   A O   1 
HETATM 5585 O O   . HOH   G 4 .   ? -6.292  39.009 -9.191  1.00 24.82  ? 1249 HOH   A O   1 
HETATM 5586 O O   . HOH   G 4 .   ? 35.330  40.198 8.469   1.00 23.19  ? 1250 HOH   A O   1 
HETATM 5587 O O   . HOH   G 4 .   ? 26.113  54.725 8.652   1.00 28.93  ? 1251 HOH   A O   1 
HETATM 5588 O O   . HOH   G 4 .   ? 2.658   43.326 20.016  1.00 33.17  ? 1252 HOH   A O   1 
HETATM 5589 O O   . HOH   H 4 .   ? 27.010  25.984 27.059  1.00 33.05  ? 1201 HOH   B O   1 
HETATM 5590 O O   . HOH   H 4 .   ? 39.195  19.590 41.757  1.00 25.14  ? 1202 HOH   B O   1 
HETATM 5591 O O   . HOH   H 4 .   ? 29.656  26.616 30.761  1.00 24.86  ? 1203 HOH   B O   1 
HETATM 5592 O O   . HOH   H 4 .   ? 34.438  27.069 37.858  1.00 11.15  ? 1204 HOH   B O   1 
HETATM 5593 O O   . HOH   H 4 .   ? 35.661  39.546 44.415  1.00 32.07  ? 1205 HOH   B O   1 
HETATM 5594 O O   . HOH   H 4 .   ? 37.792  12.219 50.481  1.00 26.25  ? 1206 HOH   B O   1 
HETATM 5595 O O   . HOH   H 4 .   ? 30.350  18.353 42.885  1.00 22.21  ? 1207 HOH   B O   1 
HETATM 5596 O O   . HOH   H 4 .   ? 30.858  13.560 13.493  1.00 27.56  ? 1208 HOH   B O   1 
HETATM 5597 O O   . HOH   H 4 .   ? 42.649  31.292 46.809  1.00 34.77  ? 1209 HOH   B O   1 
HETATM 5598 O O   . HOH   H 4 .   ? 31.047  22.218 36.073  1.00 11.95  ? 1210 HOH   B O   1 
HETATM 5599 O O   . HOH   H 4 .   ? 51.980  23.418 49.010  1.00 23.00  ? 1211 HOH   B O   1 
HETATM 5600 O O   . HOH   H 4 .   ? 22.542  16.770 36.449  1.00 38.34  ? 1212 HOH   B O   1 
HETATM 5601 O O   . HOH   H 4 .   ? 37.677  28.686 37.944  1.00 28.25  ? 1213 HOH   B O   1 
HETATM 5602 O O   . HOH   H 4 .   ? 31.002  15.730 40.641  1.00 21.19  ? 1214 HOH   B O   1 
HETATM 5603 O O   . HOH   H 4 .   ? 35.161  19.150 35.793  1.00 25.43  ? 1215 HOH   B O   1 
HETATM 5604 O O   . HOH   H 4 .   ? 43.437  26.324 32.598  1.00 16.64  ? 1216 HOH   B O   1 
HETATM 5605 O O   . HOH   H 4 .   ? 37.781  32.940 19.108  1.00 21.11  ? 1217 HOH   B O   1 
HETATM 5606 O O   . HOH   H 4 .   ? 35.143  29.459 36.925  1.00 15.95  ? 1218 HOH   B O   1 
HETATM 5607 O O   . HOH   H 4 .   ? 13.063  19.954 35.579  1.00 28.46  ? 1219 HOH   B O   1 
HETATM 5608 O O   . HOH   H 4 .   ? 12.868  34.014 49.377  1.00 26.36  ? 1220 HOH   B O   1 
HETATM 5609 O O   . HOH   H 4 .   ? 37.380  15.336 42.289  1.00 27.26  ? 1221 HOH   B O   1 
HETATM 5610 O O   . HOH   H 4 .   ? 38.277  34.736 40.088  1.00 22.78  ? 1222 HOH   B O   1 
HETATM 5611 O O   . HOH   H 4 .   ? 34.732  35.439 40.897  1.00 15.57  ? 1223 HOH   B O   1 
HETATM 5612 O O   . HOH   H 4 .   ? 31.526  31.299 34.354  1.00 20.90  ? 1224 HOH   B O   1 
HETATM 5613 O O   . HOH   H 4 .   ? 39.819  15.804 41.258  1.00 30.22  ? 1225 HOH   B O   1 
HETATM 5614 O O   . HOH   H 4 .   ? 31.670  25.970 37.460  1.00 19.50  ? 1226 HOH   B O   1 
HETATM 5615 O O   . HOH   H 4 .   ? 13.876  30.216 40.798  1.00 19.64  ? 1227 HOH   B O   1 
HETATM 5616 O O   . HOH   H 4 .   ? 32.372  35.289 19.953  1.00 33.47  ? 1228 HOH   B O   1 
HETATM 5617 O O   . HOH   H 4 .   ? 43.903  33.470 45.831  1.00 22.64  ? 1229 HOH   B O   1 
HETATM 5618 O O   . HOH   H 4 .   ? 17.312  29.486 40.653  1.00 19.76  ? 1230 HOH   B O   1 
HETATM 5619 O O   . HOH   H 4 .   ? 33.141  5.533  24.370  1.00 44.54  ? 1231 HOH   B O   1 
HETATM 5620 O O   . HOH   H 4 .   ? 37.516  23.910 61.055  1.00 26.38  ? 1232 HOH   B O   1 
HETATM 5621 O O   . HOH   H 4 .   ? 34.692  37.911 23.966  1.00 43.06  ? 1233 HOH   B O   1 
HETATM 5622 O O   . HOH   H 4 .   ? 35.724  36.069 27.448  1.00 25.58  ? 1234 HOH   B O   1 
HETATM 5623 O O   . HOH   H 4 .   ? 38.780  45.165 42.658  1.00 25.66  ? 1235 HOH   B O   1 
HETATM 5624 O O   . HOH   H 4 .   ? 19.650  24.911 34.108  1.00 29.77  ? 1236 HOH   B O   1 
HETATM 5625 O O   . HOH   H 4 .   ? 8.832   26.414 36.679  1.00 39.91  ? 1237 HOH   B O   1 
HETATM 5626 O O   . HOH   H 4 .   ? 13.458  32.277 58.184  1.00 36.26  ? 1238 HOH   B O   1 
HETATM 5627 O O   . HOH   H 4 .   ? 46.106  12.872 44.133  1.00 45.90  ? 1239 HOH   B O   1 
HETATM 5628 O O   . HOH   H 4 .   ? 22.351  29.009 31.360  1.00 25.06  ? 1240 HOH   B O   1 
HETATM 5629 O O   . HOH   H 4 .   ? 35.066  33.708 42.980  1.00 15.83  ? 1241 HOH   B O   1 
HETATM 5630 O O   . HOH   H 4 .   ? 36.877  30.755 57.063  1.00 42.26  ? 1242 HOH   B O   1 
HETATM 5631 O O   . HOH   H 4 .   ? 2.083   33.219 23.419  1.00 40.70  ? 1243 HOH   B O   1 
HETATM 5632 O O   . HOH   H 4 .   ? 29.448  30.083 35.628  1.00 15.79  ? 1244 HOH   B O   1 
HETATM 5633 O O   . HOH   H 4 .   ? 22.770  28.066 34.309  1.00 41.04  ? 1245 HOH   B O   1 
HETATM 5634 O O   . HOH   H 4 .   ? 29.401  15.097 30.848  1.00 35.38  ? 1246 HOH   B O   1 
HETATM 5635 O O   . HOH   H 4 .   ? 17.462  18.844 52.910  1.00 51.63  ? 1247 HOH   B O   1 
HETATM 5636 O O   . HOH   H 4 .   ? 13.775  39.924 42.733  1.00 32.10  ? 1248 HOH   B O   1 
HETATM 5637 O O   . HOH   H 4 .   ? 38.316  35.242 31.227  1.00 21.57  ? 1249 HOH   B O   1 
HETATM 5638 O O   . HOH   H 4 .   ? 52.650  15.609 34.833  1.00 32.55  ? 1250 HOH   B O   1 
HETATM 5639 O O   . HOH   H 4 .   ? 28.891  21.072 34.777  1.00 42.31  ? 1251 HOH   B O   1 
HETATM 5640 O O   . HOH   H 4 .   ? 33.092  23.278 63.984  1.00 34.32  ? 1252 HOH   B O   1 
HETATM 5641 O O   . HOH   H 4 .   ? 30.958  31.919 30.455  1.00 26.25  ? 1253 HOH   B O   1 
HETATM 5642 O O   . HOH   H 4 .   ? 29.565  36.629 10.313  1.00 36.50  ? 1254 HOH   B O   1 
HETATM 5643 O O   . HOH   H 4 .   ? 29.042  29.656 32.548  1.00 27.08  ? 1255 HOH   B O   1 
HETATM 5644 O O   . HOH   H 4 .   ? 26.678  28.496 30.999  1.00 32.95  ? 1256 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   . LYS A 6   ? 0.3440 0.7280 0.5155 0.1414  -0.1128 0.1204  662  LYS A N   
2    C CA  . LYS A 6   ? 0.3651 0.7239 0.5254 0.1331  -0.1054 0.1130  662  LYS A CA  
3    C C   . LYS A 6   ? 0.4257 0.7546 0.5943 0.1412  -0.0998 0.1154  662  LYS A C   
4    O O   . LYS A 6   ? 0.4371 0.7602 0.6135 0.1523  -0.1020 0.1278  662  LYS A O   
5    C CB  . LYS A 6   ? 0.3948 0.7554 0.5359 0.1246  -0.1067 0.1183  662  LYS A CB  
6    N N   . SER A 7   ? 0.3649 0.6751 0.5319 0.1354  -0.0926 0.1033  663  SER A N   
7    C CA  . SER A 7   ? 0.3474 0.6293 0.5206 0.1398  -0.0864 0.1015  663  SER A CA  
8    C C   . SER A 7   ? 0.3935 0.6560 0.5626 0.1436  -0.0856 0.1143  663  SER A C   
9    O O   . SER A 7   ? 0.3840 0.6463 0.5390 0.1368  -0.0860 0.1193  663  SER A O   
10   C CB  . SER A 7   ? 0.3548 0.6247 0.5225 0.1298  -0.0799 0.0870  663  SER A CB  
11   O OG  . SER A 7   ? 0.3715 0.6158 0.5444 0.1327  -0.0742 0.0845  663  SER A OG  
12   N N   . LYS A 8   ? 0.3362 0.5814 0.5177 0.1539  -0.0839 0.1185  664  LYS A N   
13   C CA  . LYS A 8   ? 0.3367 0.5593 0.5175 0.1581  -0.0823 0.1296  664  LYS A CA  
14   C C   . LYS A 8   ? 0.3998 0.5974 0.5763 0.1510  -0.0748 0.1211  664  LYS A C   
15   O O   . LYS A 8   ? 0.4174 0.5948 0.5922 0.1519  -0.0726 0.1287  664  LYS A O   
16   C CB  . LYS A 8   ? 0.3567 0.5720 0.5538 0.1728  -0.0840 0.1374  664  LYS A CB  
17   N N   . LEU A 9   ? 0.3305 0.5299 0.5057 0.1438  -0.0711 0.1060  665  LEU A N   
18   C CA  . LEU A 9   ? 0.3237 0.5028 0.4953 0.1369  -0.0645 0.0973  665  LEU A CA  
19   C C   . LEU A 9   ? 0.3686 0.5418 0.5260 0.1283  -0.0628 0.1023  665  LEU A C   
20   O O   . LEU A 9   ? 0.3606 0.5503 0.5077 0.1239  -0.0659 0.1061  665  LEU A O   
21   C CB  . LEU A 9   ? 0.3135 0.4996 0.4850 0.1304  -0.0618 0.0817  665  LEU A CB  
22   C CG  . LEU A 9   ? 0.3473 0.5324 0.5323 0.1365  -0.0603 0.0734  665  LEU A CG  
23   C CD1 . LEU A 9   ? 0.3268 0.5256 0.5102 0.1296  -0.0593 0.0610  665  LEU A CD1 
24   C CD2 . LEU A 9   ? 0.3552 0.5148 0.5453 0.1382  -0.0550 0.0698  665  LEU A CD2 
25   N N   . PRO A 10  ? 0.3239 0.4750 0.4802 0.1252  -0.0577 0.1016  666  PRO A N   
26   C CA  . PRO A 10  ? 0.3302 0.4774 0.4735 0.1167  -0.0554 0.1055  666  PRO A CA  
27   C C   . PRO A 10  ? 0.3818 0.5442 0.5150 0.1075  -0.0545 0.0959  666  PRO A C   
28   O O   . PRO A 10  ? 0.3775 0.5433 0.5144 0.1057  -0.0531 0.0838  666  PRO A O   
29   C CB  . PRO A 10  ? 0.3563 0.4793 0.5033 0.1144  -0.0497 0.1020  666  PRO A CB  
30   C CG  . PRO A 10  ? 0.4110 0.5228 0.5720 0.1238  -0.0502 0.1017  666  PRO A CG  
31   C CD  . PRO A 10  ? 0.3458 0.4759 0.5122 0.1286  -0.0536 0.0961  666  PRO A CD  
32   N N   . LYS A 11  ? 0.3243 0.4957 0.4444 0.1017  -0.0552 0.1013  667  LYS A N   
33   C CA  . LYS A 11  ? 0.3097 0.4941 0.4193 0.0930  -0.0539 0.0920  667  LYS A CA  
34   C C   . LYS A 11  ? 0.3302 0.5031 0.4410 0.0873  -0.0478 0.0790  667  LYS A C   
35   O O   . LYS A 11  ? 0.2955 0.4769 0.4060 0.0840  -0.0476 0.0682  667  LYS A O   
36   C CB  . LYS A 11  ? 0.3501 0.5437 0.4451 0.0878  -0.0545 0.0997  667  LYS A CB  
37   C CG  . LYS A 11  ? 0.5315 0.7461 0.6164 0.0818  -0.0566 0.0929  667  LYS A CG  
38   C CD  . LYS A 11  ? 0.6615 0.8755 0.7334 0.0726  -0.0515 0.0878  667  LYS A CD  
39   C CE  . LYS A 11  ? 0.7870 1.0202 0.8481 0.0662  -0.0531 0.0801  667  LYS A CE  
40   N NZ  . LYS A 11  ? 0.9294 1.1638 0.9961 0.0642  -0.0524 0.0659  667  LYS A NZ  
41   N N   . PRO A 12  ? 0.2863 0.4402 0.3998 0.0862  -0.0431 0.0797  668  PRO A N   
42   C CA  . PRO A 12  ? 0.2796 0.4249 0.3951 0.0813  -0.0380 0.0679  668  PRO A CA  
43   C C   . PRO A 12  ? 0.3015 0.4464 0.4269 0.0844  -0.0386 0.0584  668  PRO A C   
44   O O   . PRO A 12  ? 0.2774 0.4239 0.4018 0.0797  -0.0361 0.0480  668  PRO A O   
45   C CB  . PRO A 12  ? 0.3100 0.4369 0.4279 0.0806  -0.0342 0.0726  668  PRO A CB  
46   C CG  . PRO A 12  ? 0.3693 0.4973 0.4818 0.0820  -0.0361 0.0866  668  PRO A CG  
47   C CD  . PRO A 12  ? 0.3085 0.4485 0.4233 0.0886  -0.0422 0.0915  668  PRO A CD  
48   N N   . VAL A 13  ? 0.2504 0.3938 0.3854 0.0925  -0.0417 0.0623  669  VAL A N   
49   C CA  . VAL A 13  ? 0.2358 0.3807 0.3807 0.0962  -0.0421 0.0540  669  VAL A CA  
50   C C   . VAL A 13  ? 0.2995 0.4646 0.4417 0.0941  -0.0451 0.0486  669  VAL A C   
51   O O   . VAL A 13  ? 0.3110 0.4786 0.4560 0.0914  -0.0435 0.0386  669  VAL A O   
52   C CB  . VAL A 13  ? 0.2782 0.4154 0.4343 0.1060  -0.0439 0.0594  669  VAL A CB  
53   C CG1 . VAL A 13  ? 0.2763 0.4207 0.4421 0.1104  -0.0448 0.0514  669  VAL A CG1 
54   C CG2 . VAL A 13  ? 0.2743 0.3891 0.4338 0.1063  -0.0402 0.0611  669  VAL A CG2 
55   N N   . GLN A 14  ? 0.2569 0.4367 0.3933 0.0946  -0.0494 0.0556  670  GLN A N   
56   C CA  . GLN A 14  ? 0.2518 0.4523 0.3846 0.0916  -0.0529 0.0515  670  GLN A CA  
57   C C   . GLN A 14  ? 0.3115 0.5134 0.4357 0.0818  -0.0495 0.0413  670  GLN A C   
58   O O   . GLN A 14  ? 0.3140 0.5243 0.4399 0.0787  -0.0499 0.0326  670  GLN A O   
59   C CB  . GLN A 14  ? 0.2553 0.4706 0.3818 0.0932  -0.0582 0.0620  670  GLN A CB  
60   C CG  . GLN A 14  ? 0.3466 0.5634 0.4825 0.1038  -0.0624 0.0729  670  GLN A CG  
61   C CD  . GLN A 14  ? 0.4763 0.7136 0.6073 0.1054  -0.0689 0.0820  670  GLN A CD  
62   O OE1 . GLN A 14  ? 0.4014 0.6563 0.5246 0.0989  -0.0711 0.0775  670  GLN A OE1 
63   N NE2 . GLN A 14  ? 0.3316 0.5670 0.4672 0.1139  -0.0721 0.0951  670  GLN A NE2 
64   N N   . ASP A 15  ? 0.2571 0.4501 0.3725 0.0771  -0.0460 0.0426  671  ASP A N   
65   C CA  . ASP A 15  ? 0.2518 0.4440 0.3592 0.0688  -0.0421 0.0336  671  ASP A CA  
66   C C   . ASP A 15  ? 0.2700 0.4515 0.3844 0.0676  -0.0383 0.0244  671  ASP A C   
67   O O   . ASP A 15  ? 0.2655 0.4502 0.3769 0.0621  -0.0367 0.0156  671  ASP A O   
68   C CB  . ASP A 15  ? 0.2891 0.4753 0.3870 0.0653  -0.0388 0.0380  671  ASP A CB  
69   C CG  . ASP A 15  ? 0.4529 0.6518 0.5408 0.0646  -0.0421 0.0463  671  ASP A CG  
70   O OD1 . ASP A 15  ? 0.4291 0.6444 0.5128 0.0630  -0.0461 0.0444  671  ASP A OD1 
71   O OD2 . ASP A 15  ? 0.6091 0.8022 0.6929 0.0651  -0.0406 0.0549  671  ASP A OD2 
72   N N   . LEU A 16  ? 0.1958 0.3643 0.3191 0.0724  -0.0369 0.0265  672  LEU A N   
73   C CA  . LEU A 16  ? 0.1616 0.3206 0.2917 0.0717  -0.0337 0.0186  672  LEU A CA  
74   C C   . LEU A 16  ? 0.1746 0.3438 0.3100 0.0721  -0.0357 0.0121  672  LEU A C   
75   O O   . LEU A 16  ? 0.1383 0.3064 0.2736 0.0675  -0.0334 0.0041  672  LEU A O   
76   C CB  . LEU A 16  ? 0.1540 0.2980 0.2918 0.0765  -0.0322 0.0222  672  LEU A CB  
77   C CG  . LEU A 16  ? 0.2065 0.3423 0.3513 0.0760  -0.0295 0.0141  672  LEU A CG  
78   C CD1 . LEU A 16  ? 0.2049 0.3332 0.3458 0.0699  -0.0253 0.0098  672  LEU A CD1 
79   C CD2 . LEU A 16  ? 0.2374 0.3629 0.3912 0.0822  -0.0295 0.0164  672  LEU A CD2 
80   N N   . ILE A 17  ? 0.1525 0.3318 0.2931 0.0778  -0.0399 0.0162  673  ILE A N   
81   C CA  . ILE A 17  ? 0.1560 0.3479 0.3027 0.0786  -0.0421 0.0111  673  ILE A CA  
82   C C   . ILE A 17  ? 0.1878 0.3917 0.3272 0.0707  -0.0429 0.0054  673  ILE A C   
83   O O   . ILE A 17  ? 0.1842 0.3913 0.3264 0.0671  -0.0418 -0.0021 673  ILE A O   
84   C CB  . ILE A 17  ? 0.2077 0.4099 0.3618 0.0871  -0.0466 0.0181  673  ILE A CB  
85   C CG1 . ILE A 17  ? 0.2160 0.4039 0.3783 0.0953  -0.0454 0.0229  673  ILE A CG1 
86   C CG2 . ILE A 17  ? 0.2100 0.4297 0.3707 0.0876  -0.0492 0.0135  673  ILE A CG2 
87   C CD1 . ILE A 17  ? 0.2811 0.4561 0.4496 0.0958  -0.0412 0.0158  673  ILE A CD1 
88   N N   . LYS A 18  ? 0.1399 0.3500 0.2697 0.0676  -0.0446 0.0088  674  LYS A N   
89   C CA  . LYS A 18  ? 0.1498 0.3709 0.2715 0.0597  -0.0454 0.0030  674  LYS A CA  
90   C C   . LYS A 18  ? 0.2217 0.4315 0.3399 0.0532  -0.0403 -0.0056 674  LYS A C   
91   O O   . LYS A 18  ? 0.2239 0.4385 0.3414 0.0476  -0.0401 -0.0131 674  LYS A O   
92   C CB  . LYS A 18  ? 0.2087 0.4375 0.3196 0.0579  -0.0477 0.0084  674  LYS A CB  
93   C CG  . LYS A 18  ? 0.3381 0.5839 0.4508 0.0625  -0.0540 0.0164  674  LYS A CG  
94   C CD  . LYS A 18  ? 0.3795 0.6365 0.4793 0.0580  -0.0565 0.0194  674  LYS A CD  
95   C CE  . LYS A 18  ? 0.5807 0.8325 0.6760 0.0623  -0.0567 0.0306  674  LYS A CE  
96   N NZ  . LYS A 18  ? 0.6924 0.9567 0.7737 0.0572  -0.0588 0.0332  674  LYS A NZ  
97   N N   . MET A 19  ? 0.2021 0.3967 0.3188 0.0540  -0.0363 -0.0041 675  MET A N   
98   C CA  . MET A 19  ? 0.2090 0.3918 0.3237 0.0497  -0.0314 -0.0103 675  MET A CA  
99   C C   . MET A 19  ? 0.2162 0.3955 0.3387 0.0491  -0.0302 -0.0161 675  MET A C   
100  O O   . MET A 19  ? 0.1995 0.3787 0.3199 0.0436  -0.0286 -0.0228 675  MET A O   
101  C CB  . MET A 19  ? 0.2631 0.4328 0.3780 0.0525  -0.0283 -0.0054 675  MET A CB  
102  C CG  . MET A 19  ? 0.3418 0.5024 0.4522 0.0481  -0.0234 -0.0096 675  MET A CG  
103  S SD  . MET A 19  ? 0.4133 0.5616 0.5255 0.0512  -0.0205 -0.0027 675  MET A SD  
104  C CE  . MET A 19  ? 0.3768 0.5172 0.4873 0.0466  -0.0149 -0.0093 675  MET A CE  
105  N N   . ILE A 20  ? 0.1702 0.3467 0.3016 0.0548  -0.0309 -0.0135 676  ILE A N   
106  C CA  . ILE A 20  ? 0.1631 0.3367 0.3017 0.0547  -0.0295 -0.0183 676  ILE A CA  
107  C C   . ILE A 20  ? 0.2045 0.3921 0.3463 0.0527  -0.0320 -0.0220 676  ILE A C   
108  O O   . ILE A 20  ? 0.2011 0.3871 0.3460 0.0499  -0.0302 -0.0270 676  ILE A O   
109  C CB  . ILE A 20  ? 0.1970 0.3620 0.3432 0.0609  -0.0287 -0.0155 676  ILE A CB  
110  C CG1 . ILE A 20  ? 0.1944 0.3671 0.3466 0.0679  -0.0321 -0.0108 676  ILE A CG1 
111  C CG2 . ILE A 20  ? 0.1883 0.3400 0.3319 0.0613  -0.0261 -0.0123 676  ILE A CG2 
112  C CD1 . ILE A 20  ? 0.2808 0.4482 0.4414 0.0728  -0.0310 -0.0118 676  ILE A CD1 
113  N N   . PHE A 21  ? 0.1747 0.3766 0.3158 0.0538  -0.0361 -0.0193 677  PHE A N   
114  C CA  . PHE A 21  ? 0.1651 0.3823 0.3098 0.0511  -0.0385 -0.0229 677  PHE A CA  
115  C C   . PHE A 21  ? 0.2257 0.4495 0.3623 0.0422  -0.0393 -0.0276 677  PHE A C   
116  O O   . PHE A 21  ? 0.1835 0.4217 0.3222 0.0388  -0.0419 -0.0302 677  PHE A O   
117  C CB  . PHE A 21  ? 0.1729 0.4046 0.3248 0.0581  -0.0429 -0.0176 677  PHE A CB  
118  C CG  . PHE A 21  ? 0.1763 0.4039 0.3385 0.0653  -0.0414 -0.0169 677  PHE A CG  
119  C CD1 . PHE A 21  ? 0.2093 0.4408 0.3775 0.0634  -0.0397 -0.0225 677  PHE A CD1 
120  C CD2 . PHE A 21  ? 0.1880 0.4063 0.3533 0.0732  -0.0412 -0.0111 677  PHE A CD2 
121  C CE1 . PHE A 21  ? 0.2248 0.4530 0.4016 0.0697  -0.0379 -0.0229 677  PHE A CE1 
122  C CE2 . PHE A 21  ? 0.2369 0.4503 0.4113 0.0795  -0.0395 -0.0119 677  PHE A CE2 
123  C CZ  . PHE A 21  ? 0.2107 0.4297 0.3906 0.0779  -0.0378 -0.0181 677  PHE A CZ  
124  N N   . ASP A 22  ? 0.2142 0.4274 0.3419 0.0384  -0.0366 -0.0293 678  ASP A N   
125  C CA  . ASP A 22  ? 0.2180 0.4337 0.3371 0.0302  -0.0363 -0.0349 678  ASP A CA  
126  C C   . ASP A 22  ? 0.2428 0.4562 0.3645 0.0239  -0.0345 -0.0419 678  ASP A C   
127  O O   . ASP A 22  ? 0.2418 0.4417 0.3655 0.0238  -0.0306 -0.0438 678  ASP A O   
128  C CB  . ASP A 22  ? 0.2571 0.4604 0.3676 0.0291  -0.0328 -0.0352 678  ASP A CB  
129  C CG  . ASP A 22  ? 0.4132 0.6220 0.5130 0.0224  -0.0331 -0.0396 678  ASP A CG  
130  O OD1 . ASP A 22  ? 0.4145 0.6197 0.5119 0.0158  -0.0312 -0.0473 678  ASP A OD1 
131  O OD2 . ASP A 22  ? 0.5393 0.7554 0.6328 0.0237  -0.0353 -0.0355 678  ASP A OD2 
132  N N   . VAL A 23  ? 0.1874 0.4147 0.3094 0.0185  -0.0374 -0.0452 679  VAL A N   
133  C CA  . VAL A 23  ? 0.1872 0.4148 0.3118 0.0113  -0.0363 -0.0512 679  VAL A CA  
134  C C   . VAL A 23  ? 0.2661 0.4799 0.3831 0.0044  -0.0326 -0.0574 679  VAL A C   
135  O O   . VAL A 23  ? 0.2744 0.4786 0.3940 0.0010  -0.0297 -0.0605 679  VAL A O   
136  C CB  . VAL A 23  ? 0.2204 0.4689 0.3480 0.0071  -0.0408 -0.0525 679  VAL A CB  
137  C CG1 . VAL A 23  ? 0.2273 0.4755 0.3550 -0.0029 -0.0396 -0.0593 679  VAL A CG1 
138  C CG2 . VAL A 23  ? 0.2038 0.4646 0.3420 0.0146  -0.0433 -0.0472 679  VAL A CG2 
139  N N   . GLU A 24  ? 0.2105 0.4237 0.3181 0.0024  -0.0327 -0.0592 680  GLU A N   
140  C CA  . GLU A 24  ? 0.2088 0.4089 0.3089 -0.0033 -0.0288 -0.0658 680  GLU A CA  
141  C C   . GLU A 24  ? 0.2350 0.4169 0.3364 0.0014  -0.0238 -0.0643 680  GLU A C   
142  O O   . GLU A 24  ? 0.2101 0.3792 0.3097 -0.0022 -0.0200 -0.0693 680  GLU A O   
143  C CB  . GLU A 24  ? 0.2279 0.4345 0.3171 -0.0067 -0.0300 -0.0687 680  GLU A CB  
144  C CG  . GLU A 24  ? 0.3865 0.6117 0.4735 -0.0131 -0.0352 -0.0714 680  GLU A CG  
145  C CD  . GLU A 24  ? 0.5947 0.8217 0.6853 -0.0216 -0.0356 -0.0774 680  GLU A CD  
146  O OE1 . GLU A 24  ? 0.5724 0.7843 0.6604 -0.0269 -0.0315 -0.0839 680  GLU A OE1 
147  O OE2 . GLU A 24  ? 0.3368 0.5807 0.4333 -0.0230 -0.0400 -0.0755 680  GLU A OE2 
148  N N   . SER A 25  ? 0.2238 0.4046 0.3291 0.0094  -0.0239 -0.0574 681  SER A N   
149  C CA  . SER A 25  ? 0.2312 0.3969 0.3389 0.0136  -0.0198 -0.0556 681  SER A CA  
150  C C   . SER A 25  ? 0.2505 0.4106 0.3659 0.0129  -0.0187 -0.0562 681  SER A C   
151  O O   . SER A 25  ? 0.2662 0.4136 0.3824 0.0125  -0.0151 -0.0577 681  SER A O   
152  C CB  . SER A 25  ? 0.2819 0.4485 0.3916 0.0210  -0.0205 -0.0483 681  SER A CB  
153  O OG  . SER A 25  ? 0.3994 0.5713 0.5014 0.0214  -0.0214 -0.0466 681  SER A OG  
154  N N   . MET A 26  ? 0.1953 0.3660 0.3164 0.0129  -0.0217 -0.0548 682  MET A N   
155  C CA  . MET A 26  ? 0.2020 0.3711 0.3298 0.0117  -0.0210 -0.0552 682  MET A CA  
156  C C   . MET A 26  ? 0.2471 0.4101 0.3726 0.0038  -0.0191 -0.0604 682  MET A C   
157  O O   . MET A 26  ? 0.2376 0.3904 0.3657 0.0031  -0.0165 -0.0604 682  MET A O   
158  C CB  . MET A 26  ? 0.2246 0.4094 0.3585 0.0130  -0.0244 -0.0533 682  MET A CB  
159  C CG  . MET A 26  ? 0.2742 0.4629 0.4122 0.0214  -0.0259 -0.0481 682  MET A CG  
160  S SD  . MET A 26  ? 0.3366 0.5452 0.4826 0.0233  -0.0295 -0.0469 682  MET A SD  
161  C CE  . MET A 26  ? 0.2935 0.5059 0.4408 0.0327  -0.0320 -0.0408 682  MET A CE  
162  N N   . LYS A 27  ? 0.2257 0.3942 0.3459 -0.0021 -0.0205 -0.0648 683  LYS A N   
163  C CA  . LYS A 27  ? 0.2328 0.3942 0.3500 -0.0105 -0.0188 -0.0707 683  LYS A CA  
164  C C   . LYS A 27  ? 0.2711 0.4144 0.3842 -0.0096 -0.0143 -0.0731 683  LYS A C   
165  O O   . LYS A 27  ? 0.2698 0.4013 0.3846 -0.0126 -0.0116 -0.0747 683  LYS A O   
166  C CB  . LYS A 27  ? 0.2529 0.4262 0.3650 -0.0173 -0.0217 -0.0755 683  LYS A CB  
167  C CG  . LYS A 27  ? 0.3355 0.5276 0.4531 -0.0195 -0.0259 -0.0738 683  LYS A CG  
168  C CD  . LYS A 27  ? 0.4423 0.6481 0.5547 -0.0262 -0.0295 -0.0782 683  LYS A CD  
169  C CE  . LYS A 27  ? 0.4874 0.7133 0.6065 -0.0294 -0.0335 -0.0770 683  LYS A CE  
170  N NZ  . LYS A 27  ? 0.5384 0.7763 0.6526 -0.0388 -0.0367 -0.0826 683  LYS A NZ  
171  N N   . LYS A 28  ? 0.2404 0.3821 0.3485 -0.0054 -0.0133 -0.0727 684  LYS A N   
172  C CA  . LYS A 28  ? 0.2456 0.3726 0.3505 -0.0034 -0.0087 -0.0748 684  LYS A CA  
173  C C   . LYS A 28  ? 0.2990 0.4156 0.4109 0.0012  -0.0063 -0.0704 684  LYS A C   
174  O O   . LYS A 28  ? 0.3124 0.4160 0.4246 0.0010  -0.0026 -0.0725 684  LYS A O   
175  C CB  . LYS A 28  ? 0.2843 0.4152 0.3834 0.0007  -0.0083 -0.0736 684  LYS A CB  
176  C CG  . LYS A 28  ? 0.4345 0.5538 0.5287 0.0011  -0.0033 -0.0780 684  LYS A CG  
177  C CD  . LYS A 28  ? 0.5547 0.6784 0.6439 0.0055  -0.0023 -0.0754 684  LYS A CD  
178  C CE  . LYS A 28  ? 0.6921 0.8076 0.7863 0.0118  0.0010  -0.0709 684  LYS A CE  
179  N NZ  . LYS A 28  ? 0.7935 0.9086 0.8815 0.0137  0.0046  -0.0722 684  LYS A NZ  
180  N N   . ALA A 29  ? 0.2488 0.3717 0.3664 0.0054  -0.0085 -0.0646 685  ALA A N   
181  C CA  . ALA A 29  ? 0.2450 0.3608 0.3688 0.0091  -0.0071 -0.0606 685  ALA A CA  
182  C C   . ALA A 29  ? 0.3164 0.4274 0.4434 0.0044  -0.0065 -0.0615 685  ALA A C   
183  O O   . ALA A 29  ? 0.3177 0.4183 0.4474 0.0056  -0.0041 -0.0599 685  ALA A O   
184  C CB  . ALA A 29  ? 0.2444 0.3684 0.3725 0.0142  -0.0094 -0.0555 685  ALA A CB  
185  N N   . MET A 30  ? 0.2810 0.4001 0.4079 -0.0013 -0.0087 -0.0636 686  MET A N   
186  C CA  . MET A 30  ? 0.2903 0.4055 0.4200 -0.0069 -0.0081 -0.0639 686  MET A CA  
187  C C   . MET A 30  ? 0.3363 0.4366 0.4628 -0.0111 -0.0051 -0.0680 686  MET A C   
188  O O   . MET A 30  ? 0.3178 0.4077 0.4473 -0.0121 -0.0032 -0.0660 686  MET A O   
189  C CB  . MET A 30  ? 0.3207 0.4503 0.4519 -0.0122 -0.0111 -0.0648 686  MET A CB  
190  C CG  . MET A 30  ? 0.3709 0.5131 0.5072 -0.0072 -0.0132 -0.0605 686  MET A CG  
191  S SD  . MET A 30  ? 0.4366 0.5994 0.5763 -0.0114 -0.0166 -0.0613 686  MET A SD  
192  C CE  . MET A 30  ? 0.3940 0.5534 0.5365 -0.0201 -0.0148 -0.0612 686  MET A CE  
193  N N   . VAL A 31  ? 0.3091 0.4080 0.4295 -0.0131 -0.0044 -0.0737 687  VAL A N   
194  C CA  . VAL A 31  ? 0.3178 0.4022 0.4344 -0.0165 -0.0010 -0.0794 687  VAL A CA  
195  C C   . VAL A 31  ? 0.3964 0.4670 0.5156 -0.0098 0.0028  -0.0770 687  VAL A C   
196  O O   . VAL A 31  ? 0.3845 0.4406 0.5050 -0.0114 0.0057  -0.0784 687  VAL A O   
197  C CB  . VAL A 31  ? 0.3652 0.4546 0.4738 -0.0196 -0.0014 -0.0864 687  VAL A CB  
198  C CG1 . VAL A 31  ? 0.3768 0.4506 0.4808 -0.0204 0.0032  -0.0930 687  VAL A CG1 
199  C CG2 . VAL A 31  ? 0.3536 0.4542 0.4604 -0.0282 -0.0049 -0.0897 687  VAL A CG2 
200  N N   . GLU A 32  ? 0.3915 0.4669 0.5121 -0.0025 0.0027  -0.0728 688  GLU A N   
201  C CA  . GLU A 32  ? 0.4010 0.4675 0.5250 0.0041  0.0057  -0.0697 688  GLU A CA  
202  C C   . GLU A 32  ? 0.4816 0.5412 0.6122 0.0046  0.0059  -0.0646 688  GLU A C   
203  O O   . GLU A 32  ? 0.4650 0.5138 0.5989 0.0081  0.0088  -0.0632 688  GLU A O   
204  C CB  . GLU A 32  ? 0.4074 0.4832 0.5321 0.0101  0.0045  -0.0656 688  GLU A CB  
205  C CG  . GLU A 32  ? 0.4937 0.5635 0.6193 0.0157  0.0081  -0.0650 688  GLU A CG  
206  C CD  . GLU A 32  ? 0.7066 0.7851 0.8309 0.0199  0.0073  -0.0622 688  GLU A CD  
207  O OE1 . GLU A 32  ? 0.4550 0.5317 0.5837 0.0246  0.0088  -0.0584 688  GLU A OE1 
208  O OE2 . GLU A 32  ? 0.5918 0.6793 0.7111 0.0182  0.0051  -0.0633 688  GLU A OE2 
209  N N   . TYR A 33  ? 0.4475 0.5146 0.5803 0.0014  0.0028  -0.0615 689  TYR A N   
210  C CA  . TYR A 33  ? 0.4471 0.5107 0.5850 0.0007  0.0025  -0.0562 689  TYR A CA  
211  C C   . TYR A 33  ? 0.5111 0.5643 0.6487 -0.0058 0.0038  -0.0577 689  TYR A C   
212  O O   . TYR A 33  ? 0.5097 0.5594 0.6509 -0.0072 0.0036  -0.0526 689  TYR A O   
213  C CB  . TYR A 33  ? 0.4526 0.5301 0.5924 0.0003  -0.0008 -0.0527 689  TYR A CB  
214  C CG  . TYR A 33  ? 0.4660 0.5501 0.6075 0.0070  -0.0017 -0.0498 689  TYR A CG  
215  C CD1 . TYR A 33  ? 0.4981 0.5765 0.6428 0.0119  -0.0004 -0.0461 689  TYR A CD1 
216  C CD2 . TYR A 33  ? 0.4617 0.5581 0.6024 0.0082  -0.0041 -0.0504 689  TYR A CD2 
217  C CE1 . TYR A 33  ? 0.5171 0.6012 0.6635 0.0170  -0.0013 -0.0438 689  TYR A CE1 
218  C CE2 . TYR A 33  ? 0.4630 0.5635 0.6054 0.0139  -0.0048 -0.0478 689  TYR A CE2 
219  C CZ  . TYR A 33  ? 0.5282 0.6223 0.6733 0.0178  -0.0034 -0.0448 689  TYR A CZ  
220  O OH  . TYR A 33  ? 0.4772 0.5746 0.6241 0.0224  -0.0041 -0.0425 689  TYR A OH  
221  N N   . GLU A 34  ? 0.4699 0.5182 0.6029 -0.0102 0.0050  -0.0648 690  GLU A N   
222  C CA  . GLU A 34  ? 0.4718 0.5089 0.6037 -0.0177 0.0064  -0.0681 690  GLU A CA  
223  C C   . GLU A 34  ? 0.4856 0.5314 0.6186 -0.0255 0.0037  -0.0662 690  GLU A C   
224  O O   . GLU A 34  ? 0.4920 0.5283 0.6262 -0.0314 0.0047  -0.0654 690  GLU A O   
225  C CB  . GLU A 34  ? 0.5016 0.5200 0.6372 -0.0148 0.0098  -0.0655 690  GLU A CB  
226  C CG  . GLU A 34  ? 0.7039 0.7154 0.8395 -0.0071 0.0131  -0.0680 690  GLU A CG  
227  C CD  . GLU A 34  ? 1.0796 1.0714 1.2180 -0.0048 0.0172  -0.0689 690  GLU A CD  
228  O OE1 . GLU A 34  ? 1.1654 1.1499 1.3009 -0.0033 0.0206  -0.0763 690  GLU A OE1 
229  O OE2 . GLU A 34  ? 1.0217 1.0057 1.1654 -0.0043 0.0172  -0.0621 690  GLU A OE2 
230  N N   . ILE A 35  ? 0.4092 0.4732 0.5419 -0.0257 0.0005  -0.0656 691  ILE A N   
231  C CA  . ILE A 35  ? 0.4021 0.4780 0.5364 -0.0325 -0.0019 -0.0643 691  ILE A CA  
232  C C   . ILE A 35  ? 0.4752 0.5524 0.6057 -0.0415 -0.0024 -0.0715 691  ILE A C   
233  O O   . ILE A 35  ? 0.4790 0.5585 0.6049 -0.0408 -0.0028 -0.0773 691  ILE A O   
234  C CB  . ILE A 35  ? 0.4274 0.5227 0.5639 -0.0281 -0.0048 -0.0614 691  ILE A CB  
235  C CG1 . ILE A 35  ? 0.4224 0.5165 0.5621 -0.0204 -0.0043 -0.0553 691  ILE A CG1 
236  C CG2 . ILE A 35  ? 0.4357 0.5462 0.5744 -0.0347 -0.0069 -0.0610 691  ILE A CG2 
237  C CD1 . ILE A 35  ? 0.4292 0.5359 0.5697 -0.0136 -0.0063 -0.0546 691  ILE A CD1 
238  N N   . ASP A 36  ? 0.4353 0.5119 0.5673 -0.0506 -0.0026 -0.0710 692  ASP A N   
239  C CA  . ASP A 36  ? 0.4430 0.5223 0.5722 -0.0608 -0.0035 -0.0777 692  ASP A CA  
240  C C   . ASP A 36  ? 0.4906 0.5950 0.6208 -0.0619 -0.0074 -0.0782 692  ASP A C   
241  O O   . ASP A 36  ? 0.4727 0.5896 0.6078 -0.0634 -0.0087 -0.0735 692  ASP A O   
242  C CB  . ASP A 36  ? 0.4745 0.5436 0.6058 -0.0704 -0.0020 -0.0760 692  ASP A CB  
243  C CG  . ASP A 36  ? 0.6472 0.7110 0.7750 -0.0817 -0.0018 -0.0840 692  ASP A CG  
244  O OD1 . ASP A 36  ? 0.6400 0.7218 0.7674 -0.0880 -0.0048 -0.0875 692  ASP A OD1 
245  O OD2 . ASP A 36  ? 0.7544 0.7962 0.8804 -0.0844 0.0013  -0.0869 692  ASP A OD2 
246  N N   . LEU A 37  ? 0.4569 0.5695 0.5828 -0.0606 -0.0093 -0.0836 693  LEU A N   
247  C CA  . LEU A 37  ? 0.4374 0.5740 0.5646 -0.0602 -0.0133 -0.0836 693  LEU A CA  
248  C C   . LEU A 37  ? 0.5082 0.6569 0.6366 -0.0717 -0.0155 -0.0869 693  LEU A C   
249  O O   . LEU A 37  ? 0.5012 0.6717 0.6334 -0.0717 -0.0188 -0.0854 693  LEU A O   
250  C CB  . LEU A 37  ? 0.4335 0.5754 0.5555 -0.0545 -0.0149 -0.0866 693  LEU A CB  
251  C CG  . LEU A 37  ? 0.4955 0.6365 0.6186 -0.0424 -0.0144 -0.0815 693  LEU A CG  
252  C CD1 . LEU A 37  ? 0.5096 0.6510 0.6260 -0.0386 -0.0148 -0.0847 693  LEU A CD1 
253  C CD2 . LEU A 37  ? 0.4950 0.6535 0.6241 -0.0374 -0.0170 -0.0760 693  LEU A CD2 
254  N N   . GLN A 38  ? 0.4789 0.6137 0.6048 -0.0814 -0.0136 -0.0914 694  GLN A N   
255  C CA  . GLN A 38  ? 0.4770 0.6215 0.6044 -0.0941 -0.0153 -0.0946 694  GLN A CA  
256  C C   . GLN A 38  ? 0.5269 0.6767 0.6616 -0.0967 -0.0146 -0.0875 694  GLN A C   
257  O O   . GLN A 38  ? 0.5051 0.6767 0.6446 -0.1007 -0.0172 -0.0864 694  GLN A O   
258  C CB  . GLN A 38  ? 0.5002 0.6253 0.6222 -0.1039 -0.0131 -0.1022 694  GLN A CB  
259  C CG  . GLN A 38  ? 0.5434 0.6739 0.6580 -0.1070 -0.0152 -0.1113 694  GLN A CG  
260  C CD  . GLN A 38  ? 0.8296 0.9799 0.9452 -0.1190 -0.0191 -0.1154 694  GLN A CD  
261  O OE1 . GLN A 38  ? 0.7450 0.9208 0.8649 -0.1173 -0.0231 -0.1121 694  GLN A OE1 
262  N NE2 . GLN A 38  ? 0.7684 0.9074 0.8806 -0.1316 -0.0180 -0.1228 694  GLN A NE2 
263  N N   . LYS A 39  ? 0.4994 0.6308 0.6352 -0.0936 -0.0112 -0.0825 695  LYS A N   
264  C CA  . LYS A 39  ? 0.4886 0.6228 0.6299 -0.0954 -0.0099 -0.0749 695  LYS A CA  
265  C C   . LYS A 39  ? 0.5124 0.6664 0.6581 -0.0864 -0.0115 -0.0700 695  LYS A C   
266  O O   . LYS A 39  ? 0.5150 0.6810 0.6655 -0.0892 -0.0113 -0.0655 695  LYS A O   
267  C CB  . LYS A 39  ? 0.5284 0.6377 0.6689 -0.0932 -0.0063 -0.0704 695  LYS A CB  
268  C CG  . LYS A 39  ? 0.7235 0.8128 0.8621 -0.1039 -0.0041 -0.0730 695  LYS A CG  
269  C CD  . LYS A 39  ? 0.8581 0.9234 0.9970 -0.0992 -0.0008 -0.0672 695  LYS A CD  
270  C CE  . LYS A 39  ? 1.0005 1.0459 1.1393 -0.1098 0.0016  -0.0670 695  LYS A CE  
271  N NZ  . LYS A 39  ? 1.1044 1.1306 1.2389 -0.1121 0.0032  -0.0761 695  LYS A NZ  
272  N N   . MET A 40  ? 0.4496 0.6060 0.5936 -0.0757 -0.0126 -0.0708 696  MET A N   
273  C CA  . MET A 40  ? 0.4277 0.6003 0.5756 -0.0665 -0.0140 -0.0670 696  MET A CA  
274  C C   . MET A 40  ? 0.3900 0.5679 0.5356 -0.0577 -0.0162 -0.0694 696  MET A C   
275  O O   . MET A 40  ? 0.3864 0.5532 0.5299 -0.0492 -0.0150 -0.0677 696  MET A O   
276  C CB  . MET A 40  ? 0.4707 0.6356 0.6204 -0.0607 -0.0116 -0.0606 696  MET A CB  
277  C CG  . MET A 40  ? 0.5192 0.7037 0.6741 -0.0556 -0.0125 -0.0575 696  MET A CG  
278  S SD  . MET A 40  ? 0.5908 0.7696 0.7459 -0.0432 -0.0114 -0.0533 696  MET A SD  
279  C CE  . MET A 40  ? 0.5594 0.7192 0.7090 -0.0376 -0.0114 -0.0558 696  MET A CE  
280  N N   . PRO A 41  ? 0.2762 0.4732 0.4231 -0.0592 -0.0195 -0.0721 697  PRO A N   
281  C CA  . PRO A 41  ? 0.2588 0.4616 0.4035 -0.0508 -0.0218 -0.0729 697  PRO A CA  
282  C C   . PRO A 41  ? 0.2916 0.5013 0.4407 -0.0394 -0.0221 -0.0679 697  PRO A C   
283  O O   . PRO A 41  ? 0.2874 0.4992 0.4412 -0.0378 -0.0205 -0.0645 697  PRO A O   
284  C CB  . PRO A 41  ? 0.2719 0.4941 0.4171 -0.0570 -0.0257 -0.0766 697  PRO A CB  
285  C CG  . PRO A 41  ? 0.3247 0.5585 0.4761 -0.0652 -0.0256 -0.0759 697  PRO A CG  
286  C CD  . PRO A 41  ? 0.2844 0.4985 0.4347 -0.0691 -0.0215 -0.0743 697  PRO A CD  
287  N N   . LEU A 42  ? 0.2248 0.4377 0.3719 -0.0318 -0.0241 -0.0677 698  LEU A N   
288  C CA  . LEU A 42  ? 0.2136 0.4318 0.3643 -0.0209 -0.0247 -0.0637 698  LEU A CA  
289  C C   . LEU A 42  ? 0.2143 0.4513 0.3733 -0.0193 -0.0258 -0.0617 698  LEU A C   
290  O O   . LEU A 42  ? 0.1835 0.4203 0.3464 -0.0123 -0.0244 -0.0589 698  LEU A O   
291  C CB  . LEU A 42  ? 0.2225 0.4456 0.3698 -0.0158 -0.0276 -0.0637 698  LEU A CB  
292  C CG  . LEU A 42  ? 0.3037 0.5119 0.4461 -0.0090 -0.0261 -0.0621 698  LEU A CG  
293  C CD1 . LEU A 42  ? 0.3126 0.5292 0.4518 -0.0052 -0.0293 -0.0612 698  LEU A CD1 
294  C CD2 . LEU A 42  ? 0.3436 0.5465 0.4905 -0.0010 -0.0244 -0.0580 698  LEU A CD2 
295  N N   . GLY A 43  ? 0.1680 0.4220 0.3299 -0.0259 -0.0281 -0.0637 699  GLY A N   
296  C CA  . GLY A 43  ? 0.1556 0.4311 0.3265 -0.0247 -0.0291 -0.0624 699  GLY A CA  
297  C C   . GLY A 43  ? 0.2264 0.5024 0.4009 -0.0295 -0.0258 -0.0617 699  GLY A C   
298  O O   . GLY A 43  ? 0.2066 0.4991 0.3886 -0.0268 -0.0254 -0.0605 699  GLY A O   
299  N N   . LYS A 44  ? 0.2091 0.4677 0.3785 -0.0366 -0.0233 -0.0622 700  LYS A N   
300  C CA  . LYS A 44  ? 0.2012 0.4582 0.3727 -0.0419 -0.0201 -0.0604 700  LYS A CA  
301  C C   . LYS A 44  ? 0.2329 0.4780 0.4034 -0.0344 -0.0174 -0.0572 700  LYS A C   
302  O O   . LYS A 44  ? 0.2141 0.4612 0.3865 -0.0368 -0.0150 -0.0550 700  LYS A O   
303  C CB  . LYS A 44  ? 0.2413 0.4870 0.4088 -0.0541 -0.0190 -0.0619 700  LYS A CB  
304  C CG  . LYS A 44  ? 0.5134 0.7766 0.6842 -0.0643 -0.0210 -0.0647 700  LYS A CG  
305  C CD  . LYS A 44  ? 0.7237 0.9739 0.8910 -0.0772 -0.0195 -0.0660 700  LYS A CD  
306  C CE  . LYS A 44  ? 0.8617 1.1236 1.0296 -0.0877 -0.0222 -0.0707 700  LYS A CE  
307  N NZ  . LYS A 44  ? 0.9122 1.1562 1.0756 -0.1000 -0.0204 -0.0729 700  LYS A NZ  
308  N N   . LEU A 45  ? 0.1898 0.4242 0.3573 -0.0257 -0.0180 -0.0569 701  LEU A N   
309  C CA  . LEU A 45  ? 0.1968 0.4203 0.3634 -0.0186 -0.0160 -0.0544 701  LEU A CA  
310  C C   . LEU A 45  ? 0.2162 0.4549 0.3889 -0.0133 -0.0153 -0.0537 701  LEU A C   
311  O O   . LEU A 45  ? 0.1863 0.4395 0.3637 -0.0088 -0.0171 -0.0549 701  LEU A O   
312  C CB  . LEU A 45  ? 0.2089 0.4212 0.3719 -0.0112 -0.0172 -0.0546 701  LEU A CB  
313  C CG  . LEU A 45  ? 0.2663 0.4585 0.4248 -0.0086 -0.0153 -0.0530 701  LEU A CG  
314  C CD1 . LEU A 45  ? 0.2705 0.4501 0.4259 -0.0161 -0.0135 -0.0525 701  LEU A CD1 
315  C CD2 . LEU A 45  ? 0.2589 0.4439 0.4141 -0.0033 -0.0165 -0.0537 701  LEU A CD2 
316  N N   . SER A 46  ? 0.1663 0.4025 0.3389 -0.0141 -0.0126 -0.0519 702  SER A N   
317  C CA  . SER A 46  ? 0.1473 0.3967 0.3245 -0.0096 -0.0111 -0.0521 702  SER A CA  
318  C C   . SER A 46  ? 0.2051 0.4438 0.3791 -0.0067 -0.0090 -0.0504 702  SER A C   
319  O O   . SER A 46  ? 0.2394 0.4641 0.4087 -0.0108 -0.0085 -0.0478 702  SER A O   
320  C CB  . SER A 46  ? 0.1661 0.4332 0.3474 -0.0168 -0.0098 -0.0523 702  SER A CB  
321  O OG  . SER A 46  ? 0.1623 0.4235 0.3401 -0.0244 -0.0075 -0.0495 702  SER A OG  
322  N N   . LYS A 47  ? 0.1559 0.4013 0.3328 0.0003  -0.0080 -0.0520 703  LYS A N   
323  C CA  . LYS A 47  ? 0.1563 0.3941 0.3301 0.0033  -0.0063 -0.0514 703  LYS A CA  
324  C C   . LYS A 47  ? 0.2138 0.4530 0.3844 -0.0046 -0.0043 -0.0486 703  LYS A C   
325  O O   . LYS A 47  ? 0.2030 0.4295 0.3690 -0.0062 -0.0042 -0.0455 703  LYS A O   
326  C CB  . LYS A 47  ? 0.1710 0.4181 0.3490 0.0113  -0.0051 -0.0551 703  LYS A CB  
327  C CG  . LYS A 47  ? 0.2231 0.4655 0.4038 0.0199  -0.0071 -0.0567 703  LYS A CG  
328  C CD  . LYS A 47  ? 0.4171 0.6739 0.6050 0.0269  -0.0062 -0.0603 703  LYS A CD  
329  C CE  . LYS A 47  ? 0.5465 0.7992 0.7345 0.0332  -0.0042 -0.0635 703  LYS A CE  
330  N NZ  . LYS A 47  ? 0.6500 0.9176 0.8456 0.0397  -0.0025 -0.0676 703  LYS A NZ  
331  N N   . ARG A 48  ? 0.1660 0.4217 0.3397 -0.0096 -0.0027 -0.0490 704  ARG A N   
332  C CA  . ARG A 48  ? 0.1535 0.4149 0.3251 -0.0184 -0.0007 -0.0458 704  ARG A CA  
333  C C   . ARG A 48  ? 0.1758 0.4196 0.3423 -0.0250 -0.0016 -0.0407 704  ARG A C   
334  O O   . ARG A 48  ? 0.1715 0.4105 0.3339 -0.0286 -0.0005 -0.0364 704  ARG A O   
335  C CB  . ARG A 48  ? 0.1617 0.4423 0.3391 -0.0229 0.0000  -0.0474 704  ARG A CB  
336  C CG  . ARG A 48  ? 0.2485 0.5409 0.4255 -0.0323 0.0027  -0.0446 704  ARG A CG  
337  C CD  . ARG A 48  ? 0.1472 0.4601 0.3312 -0.0361 0.0032  -0.0467 704  ARG A CD  
338  N NE  . ARG A 48  ? 0.1979 0.5276 0.3885 -0.0271 0.0041  -0.0518 704  ARG A NE  
339  C CZ  . ARG A 48  ? 0.2847 0.6200 0.4812 -0.0211 0.0017  -0.0549 704  ARG A CZ  
340  N NH1 . ARG A 48  ? 0.1404 0.4892 0.3433 -0.0119 0.0028  -0.0589 704  ARG A NH1 
341  N NH2 . ARG A 48  ? 0.0790 0.4062 0.2750 -0.0239 -0.0017 -0.0540 704  ARG A NH2 
342  N N   . GLN A 49  ? 0.1359 0.3715 0.3028 -0.0268 -0.0035 -0.0412 705  GLN A N   
343  C CA  . GLN A 49  ? 0.1428 0.3609 0.3058 -0.0325 -0.0040 -0.0376 705  GLN A CA  
344  C C   . GLN A 49  ? 0.1874 0.3884 0.3469 -0.0267 -0.0046 -0.0358 705  GLN A C   
345  O O   . GLN A 49  ? 0.1930 0.3831 0.3495 -0.0300 -0.0040 -0.0310 705  GLN A O   
346  C CB  . GLN A 49  ? 0.1509 0.3663 0.3151 -0.0360 -0.0057 -0.0404 705  GLN A CB  
347  C CG  . GLN A 49  ? 0.2213 0.4518 0.3888 -0.0449 -0.0052 -0.0410 705  GLN A CG  
348  C CD  . GLN A 49  ? 0.4317 0.6613 0.5999 -0.0493 -0.0072 -0.0444 705  GLN A CD  
349  O OE1 . GLN A 49  ? 0.4233 0.6458 0.5899 -0.0587 -0.0069 -0.0435 705  GLN A OE1 
350  N NE2 . GLN A 49  ? 0.3191 0.5562 0.4896 -0.0431 -0.0093 -0.0482 705  GLN A NE2 
351  N N   . ILE A 50  ? 0.1547 0.3541 0.3151 -0.0181 -0.0058 -0.0391 706  ILE A N   
352  C CA  . ILE A 50  ? 0.1612 0.3467 0.3193 -0.0122 -0.0064 -0.0379 706  ILE A CA  
353  C C   . ILE A 50  ? 0.2033 0.3902 0.3595 -0.0119 -0.0054 -0.0349 706  ILE A C   
354  O O   . ILE A 50  ? 0.2156 0.3909 0.3692 -0.0127 -0.0056 -0.0306 706  ILE A O   
355  C CB  . ILE A 50  ? 0.1923 0.3768 0.3519 -0.0040 -0.0078 -0.0417 706  ILE A CB  
356  C CG1 . ILE A 50  ? 0.1937 0.3769 0.3538 -0.0049 -0.0091 -0.0440 706  ILE A CG1 
357  C CG2 . ILE A 50  ? 0.1571 0.3279 0.3145 0.0009  -0.0081 -0.0400 706  ILE A CG2 
358  C CD1 . ILE A 50  ? 0.2006 0.3900 0.3632 0.0019  -0.0107 -0.0471 706  ILE A CD1 
359  N N   . GLN A 51  ? 0.1347 0.3366 0.2920 -0.0111 -0.0043 -0.0369 707  GLN A N   
360  C CA  . GLN A 51  ? 0.1257 0.3320 0.2803 -0.0115 -0.0033 -0.0349 707  GLN A CA  
361  C C   . GLN A 51  ? 0.1483 0.3525 0.2996 -0.0194 -0.0026 -0.0282 707  GLN A C   
362  O O   . GLN A 51  ? 0.1173 0.3170 0.2652 -0.0195 -0.0030 -0.0241 707  GLN A O   
363  C CB  . GLN A 51  ? 0.1370 0.3608 0.2936 -0.0094 -0.0015 -0.0397 707  GLN A CB  
364  C CG  . GLN A 51  ? 0.3257 0.5491 0.4850 -0.0006 -0.0020 -0.0453 707  GLN A CG  
365  C CD  . GLN A 51  ? 0.4396 0.6791 0.6036 0.0027  -0.0003 -0.0508 707  GLN A CD  
366  O OE1 . GLN A 51  ? 0.2538 0.5079 0.4192 -0.0016 0.0017  -0.0511 707  GLN A OE1 
367  N NE2 . GLN A 51  ? 0.3426 0.5800 0.5098 0.0107  -0.0009 -0.0551 707  GLN A NE2 
368  N N   . ALA A 52  ? 0.1165 0.3239 0.2689 -0.0264 -0.0018 -0.0267 708  ALA A N   
369  C CA  . ALA A 52  ? 0.1074 0.3110 0.2572 -0.0346 -0.0010 -0.0197 708  ALA A CA  
370  C C   . ALA A 52  ? 0.1616 0.3444 0.3099 -0.0336 -0.0025 -0.0154 708  ALA A C   
371  O O   . ALA A 52  ? 0.1584 0.3357 0.3040 -0.0364 -0.0025 -0.0084 708  ALA A O   
372  C CB  . ALA A 52  ? 0.0999 0.3103 0.2523 -0.0424 0.0000  -0.0202 708  ALA A CB  
373  N N   . ALA A 53  ? 0.1120 0.2844 0.2622 -0.0296 -0.0036 -0.0192 709  ALA A N   
374  C CA  . ALA A 53  ? 0.1123 0.2658 0.2619 -0.0272 -0.0044 -0.0166 709  ALA A CA  
375  C C   . ALA A 53  ? 0.1589 0.3089 0.3073 -0.0212 -0.0054 -0.0138 709  ALA A C   
376  O O   . ALA A 53  ? 0.1640 0.3026 0.3119 -0.0210 -0.0058 -0.0082 709  ALA A O   
377  C CB  . ALA A 53  ? 0.1162 0.2632 0.2673 -0.0240 -0.0050 -0.0224 709  ALA A CB  
378  N N   . TYR A 54  ? 0.1204 0.2802 0.2690 -0.0162 -0.0058 -0.0177 710  TYR A N   
379  C CA  . TYR A 54  ? 0.1199 0.2788 0.2673 -0.0116 -0.0069 -0.0160 710  TYR A CA  
380  C C   . TYR A 54  ? 0.1853 0.3489 0.3296 -0.0158 -0.0070 -0.0094 710  TYR A C   
381  O O   . TYR A 54  ? 0.1848 0.3427 0.3284 -0.0141 -0.0084 -0.0044 710  TYR A O   
382  C CB  . TYR A 54  ? 0.1080 0.2774 0.2559 -0.0072 -0.0070 -0.0222 710  TYR A CB  
383  C CG  . TYR A 54  ? 0.1188 0.2825 0.2692 -0.0009 -0.0077 -0.0271 710  TYR A CG  
384  C CD1 . TYR A 54  ? 0.1541 0.3065 0.3052 0.0028  -0.0087 -0.0253 710  TYR A CD1 
385  C CD2 . TYR A 54  ? 0.1285 0.2993 0.2810 0.0016  -0.0072 -0.0329 710  TYR A CD2 
386  C CE1 . TYR A 54  ? 0.1782 0.3264 0.3312 0.0080  -0.0091 -0.0292 710  TYR A CE1 
387  C CE2 . TYR A 54  ? 0.1390 0.3046 0.2935 0.0073  -0.0080 -0.0362 710  TYR A CE2 
388  C CZ  . TYR A 54  ? 0.2320 0.3864 0.3863 0.0102  -0.0088 -0.0344 710  TYR A CZ  
389  O OH  . TYR A 54  ? 0.2550 0.4052 0.4109 0.0152  -0.0093 -0.0372 710  TYR A OH  
390  N N   . SER A 55  ? 0.1362 0.3124 0.2788 -0.0211 -0.0056 -0.0094 711  SER A N   
391  C CA  . SER A 55  ? 0.1318 0.3159 0.2704 -0.0260 -0.0053 -0.0032 711  SER A CA  
392  C C   . SER A 55  ? 0.2012 0.3727 0.3392 -0.0299 -0.0059 0.0063  711  SER A C   
393  O O   . SER A 55  ? 0.1859 0.3575 0.3212 -0.0303 -0.0072 0.0133  711  SER A O   
394  C CB  . SER A 55  ? 0.1581 0.3587 0.2958 -0.0310 -0.0029 -0.0059 711  SER A CB  
395  O OG  . SER A 55  ? 0.3337 0.5446 0.4665 -0.0356 -0.0023 -0.0005 711  SER A OG  
396  N N   . ILE A 56  ? 0.1689 0.3290 0.3096 -0.0324 -0.0052 0.0065  712  ILE A N   
397  C CA  . ILE A 56  ? 0.1697 0.3146 0.3107 -0.0354 -0.0054 0.0147  712  ILE A CA  
398  C C   . ILE A 56  ? 0.2238 0.3559 0.3667 -0.0282 -0.0072 0.0173  712  ILE A C   
399  O O   . ILE A 56  ? 0.2122 0.3378 0.3548 -0.0285 -0.0082 0.0261  712  ILE A O   
400  C CB  . ILE A 56  ? 0.2084 0.3445 0.3515 -0.0411 -0.0038 0.0132  712  ILE A CB  
401  C CG1 . ILE A 56  ? 0.2147 0.3652 0.3564 -0.0497 -0.0021 0.0131  712  ILE A CG1 
402  C CG2 . ILE A 56  ? 0.2219 0.3376 0.3661 -0.0426 -0.0038 0.0202  712  ILE A CG2 
403  C CD1 . ILE A 56  ? 0.3305 0.4842 0.4690 -0.0582 -0.0012 0.0236  712  ILE A CD1 
404  N N   . LEU A 57  ? 0.1977 0.3280 0.3429 -0.0215 -0.0077 0.0101  713  LEU A N   
405  C CA  . LEU A 57  ? 0.2104 0.3316 0.3580 -0.0146 -0.0091 0.0114  713  LEU A CA  
406  C C   . LEU A 57  ? 0.2712 0.4010 0.4170 -0.0130 -0.0112 0.0167  713  LEU A C   
407  O O   . LEU A 57  ? 0.2818 0.4050 0.4299 -0.0094 -0.0127 0.0223  713  LEU A O   
408  C CB  . LEU A 57  ? 0.2194 0.3411 0.3689 -0.0092 -0.0090 0.0027  713  LEU A CB  
409  C CG  . LEU A 57  ? 0.2877 0.3953 0.4404 -0.0047 -0.0084 0.0006  713  LEU A CG  
410  C CD1 . LEU A 57  ? 0.2887 0.3824 0.4423 -0.0081 -0.0069 0.0035  713  LEU A CD1 
411  C CD2 . LEU A 57  ? 0.2929 0.4035 0.4459 -0.0024 -0.0078 -0.0081 713  LEU A CD2 
412  N N   . SER A 58  ? 0.2140 0.3596 0.3560 -0.0156 -0.0113 0.0145  714  SER A N   
413  C CA  . SER A 58  ? 0.2146 0.3711 0.3533 -0.0157 -0.0132 0.0184  714  SER A CA  
414  C C   . SER A 58  ? 0.2972 0.4529 0.4335 -0.0203 -0.0139 0.0296  714  SER A C   
415  O O   . SER A 58  ? 0.2979 0.4554 0.4336 -0.0187 -0.0165 0.0364  714  SER A O   
416  C CB  . SER A 58  ? 0.1970 0.3700 0.3319 -0.0175 -0.0123 0.0116  714  SER A CB  
417  O OG  . SER A 58  ? 0.2217 0.3942 0.3591 -0.0122 -0.0122 0.0026  714  SER A OG  
418  N N   . GLU A 59  ? 0.2737 0.4268 0.4092 -0.0263 -0.0119 0.0323  715  GLU A N   
419  C CA  . GLU A 59  ? 0.2880 0.4379 0.4214 -0.0312 -0.0124 0.0440  715  GLU A CA  
420  C C   . GLU A 59  ? 0.3366 0.4678 0.4751 -0.0268 -0.0137 0.0506  715  GLU A C   
421  O O   . GLU A 59  ? 0.3541 0.4843 0.4920 -0.0266 -0.0157 0.0611  715  GLU A O   
422  C CB  . GLU A 59  ? 0.3116 0.4627 0.4434 -0.0394 -0.0097 0.0450  715  GLU A CB  
423  C CG  . GLU A 59  ? 0.5138 0.6726 0.6404 -0.0460 -0.0100 0.0560  715  GLU A CG  
424  C CD  . GLU A 59  ? 0.8464 1.0015 0.9725 -0.0548 -0.0076 0.0606  715  GLU A CD  
425  O OE1 . GLU A 59  ? 0.8322 0.9830 0.9614 -0.0570 -0.0055 0.0533  715  GLU A OE1 
426  O OE2 . GLU A 59  ? 0.7515 0.9084 0.8740 -0.0601 -0.0080 0.0719  715  GLU A OE2 
427  N N   . VAL A 60  ? 0.2656 0.3834 0.4091 -0.0228 -0.0124 0.0444  716  VAL A N   
428  C CA  . VAL A 60  ? 0.2701 0.3701 0.4191 -0.0176 -0.0127 0.0483  716  VAL A CA  
429  C C   . VAL A 60  ? 0.3090 0.4145 0.4599 -0.0109 -0.0157 0.0518  716  VAL A C   
430  O O   . VAL A 60  ? 0.2823 0.3821 0.4357 -0.0086 -0.0173 0.0617  716  VAL A O   
431  C CB  . VAL A 60  ? 0.3177 0.4053 0.4703 -0.0149 -0.0104 0.0390  716  VAL A CB  
432  C CG1 . VAL A 60  ? 0.3089 0.3800 0.4674 -0.0083 -0.0102 0.0418  716  VAL A CG1 
433  C CG2 . VAL A 60  ? 0.3166 0.3993 0.4675 -0.0223 -0.0079 0.0359  716  VAL A CG2 
434  N N   . GLN A 61  ? 0.2775 0.3946 0.4274 -0.0082 -0.0165 0.0440  717  GLN A N   
435  C CA  . GLN A 61  ? 0.2877 0.4128 0.4391 -0.0032 -0.0193 0.0451  717  GLN A CA  
436  C C   . GLN A 61  ? 0.3574 0.4926 0.5055 -0.0056 -0.0224 0.0557  717  GLN A C   
437  O O   . GLN A 61  ? 0.3729 0.5086 0.5247 -0.0013 -0.0251 0.0619  717  GLN A O   
438  C CB  . GLN A 61  ? 0.3048 0.4408 0.4539 -0.0026 -0.0191 0.0342  717  GLN A CB  
439  C CG  . GLN A 61  ? 0.5814 0.7314 0.7287 -0.0015 -0.0221 0.0343  717  GLN A CG  
440  C CD  . GLN A 61  ? 0.6906 0.8527 0.8330 -0.0039 -0.0214 0.0250  717  GLN A CD  
441  O OE1 . GLN A 61  ? 0.5225 0.6864 0.6664 -0.0008 -0.0216 0.0177  717  GLN A OE1 
442  N NE2 . GLN A 61  ? 0.5383 0.7092 0.6750 -0.0095 -0.0203 0.0253  717  GLN A NE2 
443  N N   . GLN A 62  ? 0.3199 0.4643 0.4614 -0.0125 -0.0220 0.0580  718  GLN A N   
444  C CA  . GLN A 62  ? 0.3260 0.4817 0.4626 -0.0160 -0.0247 0.0682  718  GLN A CA  
445  C C   . GLN A 62  ? 0.4100 0.5536 0.5501 -0.0151 -0.0257 0.0815  718  GLN A C   
446  O O   . GLN A 62  ? 0.3923 0.5413 0.5328 -0.0131 -0.0293 0.0909  718  GLN A O   
447  C CB  . GLN A 62  ? 0.3394 0.5081 0.4680 -0.0239 -0.0230 0.0667  718  GLN A CB  
448  C CG  . GLN A 62  ? 0.6355 0.8237 0.7582 -0.0250 -0.0243 0.0611  718  GLN A CG  
449  C CD  . GLN A 62  ? 0.9244 1.1275 1.0386 -0.0319 -0.0249 0.0683  718  GLN A CD  
450  O OE1 . GLN A 62  ? 0.7943 0.9997 0.9050 -0.0379 -0.0220 0.0694  718  GLN A OE1 
451  N NE2 . GLN A 62  ? 0.8999 1.1148 1.0103 -0.0317 -0.0287 0.0734  718  GLN A NE2 
452  N N   . ALA A 63  ? 0.4025 0.5294 0.5456 -0.0164 -0.0228 0.0819  719  ALA A N   
453  C CA  . ALA A 63  ? 0.4273 0.5381 0.5746 -0.0153 -0.0230 0.0933  719  ALA A CA  
454  C C   . ALA A 63  ? 0.5364 0.6375 0.6923 -0.0056 -0.0244 0.0954  719  ALA A C   
455  O O   . ALA A 63  ? 0.5452 0.6417 0.7045 -0.0028 -0.0266 0.1075  719  ALA A O   
456  C CB  . ALA A 63  ? 0.4410 0.5362 0.5892 -0.0197 -0.0191 0.0904  719  ALA A CB  
457  N N   . VAL A 64  ? 0.5296 0.6288 0.6895 -0.0004 -0.0233 0.0843  720  VAL A N   
458  C CA  . VAL A 64  ? 0.5437 0.6353 0.7123 0.0086  -0.0240 0.0856  720  VAL A CA  
459  C C   . VAL A 64  ? 0.5991 0.7071 0.7689 0.0119  -0.0287 0.0918  720  VAL A C   
460  O O   . VAL A 64  ? 0.5939 0.6982 0.7700 0.0174  -0.0307 0.1015  720  VAL A O   
461  C CB  . VAL A 64  ? 0.6026 0.6861 0.7753 0.0129  -0.0209 0.0730  720  VAL A CB  
462  C CG1 . VAL A 64  ? 0.6021 0.6714 0.7730 0.0088  -0.0169 0.0670  720  VAL A CG1 
463  C CG2 . VAL A 64  ? 0.6016 0.7001 0.7716 0.0130  -0.0218 0.0635  720  VAL A CG2 
464  N N   . SER A 65  ? 0.5631 0.6891 0.7267 0.0084  -0.0304 0.0862  721  SER A N   
465  C CA  . SER A 65  ? 0.5530 0.6965 0.7162 0.0098  -0.0349 0.0899  721  SER A CA  
466  C C   . SER A 65  ? 0.6169 0.7678 0.7772 0.0075  -0.0387 0.1045  721  SER A C   
467  O O   . SER A 65  ? 0.6197 0.7797 0.7837 0.0113  -0.0429 0.1118  721  SER A O   
468  C CB  . SER A 65  ? 0.5844 0.7427 0.7409 0.0058  -0.0352 0.0790  721  SER A CB  
469  O OG  . SER A 65  ? 0.6694 0.8381 0.8163 -0.0018 -0.0352 0.0800  721  SER A OG  
470  N N   . GLN A 66  ? 0.5741 0.7216 0.7283 0.0013  -0.0372 0.1094  722  GLN A N   
471  C CA  . GLN A 66  ? 0.5727 0.7265 0.7230 -0.0019 -0.0403 0.1243  722  GLN A CA  
472  C C   . GLN A 66  ? 0.6378 0.7729 0.7960 0.0027  -0.0402 0.1366  722  GLN A C   
473  O O   . GLN A 66  ? 0.6252 0.7612 0.7809 0.0003  -0.0423 0.1507  722  GLN A O   
474  C CB  . GLN A 66  ? 0.5885 0.7511 0.7278 -0.0117 -0.0387 0.1237  722  GLN A CB  
475  C CG  . GLN A 66  ? 0.7971 0.9794 0.9290 -0.0153 -0.0391 0.1125  722  GLN A CG  
476  C CD  . GLN A 66  ? 1.0657 1.2684 1.1881 -0.0211 -0.0424 0.1197  722  GLN A CD  
477  O OE1 . GLN A 66  ? 1.0507 1.2561 1.1664 -0.0276 -0.0412 0.1265  722  GLN A OE1 
478  N NE2 . GLN A 66  ? 0.9206 1.1388 1.0415 -0.0194 -0.0463 0.1178  722  GLN A NE2 
479  N N   . GLY A 67  ? 0.6043 0.7228 0.7717 0.0096  -0.0376 0.1311  723  GLY A N   
480  C CA  . GLY A 67  ? 0.6106 0.7091 0.7871 0.0158  -0.0366 0.1397  723  GLY A CA  
481  C C   . GLY A 67  ? 0.6722 0.7548 0.8462 0.0105  -0.0342 0.1472  723  GLY A C   
482  O O   . GLY A 67  ? 0.6838 0.7614 0.8603 0.0121  -0.0364 0.1622  723  GLY A O   
483  N N   . SER A 68  ? 0.6189 0.6934 0.7884 0.0042  -0.0299 0.1374  724  SER A N   
484  C CA  . SER A 68  ? 0.6223 0.6804 0.7900 -0.0019 -0.0272 0.1430  724  SER A CA  
485  C C   . SER A 68  ? 0.6810 0.7128 0.8583 0.0045  -0.0241 0.1418  724  SER A C   
486  O O   . SER A 68  ? 0.6712 0.7000 0.8548 0.0121  -0.0230 0.1331  724  SER A O   
487  C CB  . SER A 68  ? 0.6659 0.7286 0.8256 -0.0117 -0.0241 0.1328  724  SER A CB  
488  O OG  . SER A 68  ? 0.7471 0.8328 0.8978 -0.0180 -0.0262 0.1346  724  SER A OG  
489  N N   . SER A 69  ? 0.6545 0.6674 0.8332 0.0015  -0.0224 0.1506  725  SER A N   
490  C CA  . SER A 69  ? 0.6629 0.6486 0.8502 0.0069  -0.0189 0.1490  725  SER A CA  
491  C C   . SER A 69  ? 0.7255 0.7017 0.9108 0.0024  -0.0141 0.1323  725  SER A C   
492  O O   . SER A 69  ? 0.7159 0.7034 0.8933 -0.0066 -0.0136 0.1260  725  SER A O   
493  C CB  . SER A 69  ? 0.7122 0.6798 0.9009 0.0039  -0.0187 0.1639  725  SER A CB  
494  O OG  . SER A 69  ? 0.8114 0.7775 0.9919 -0.0089 -0.0168 0.1637  725  SER A OG  
495  N N   . ASP A 70  ? 0.6863 0.6425 0.8788 0.0086  -0.0107 0.1253  726  ASP A N   
496  C CA  . ASP A 70  ? 0.6815 0.6271 0.8723 0.0048  -0.0063 0.1098  726  ASP A CA  
497  C C   . ASP A 70  ? 0.7096 0.6449 0.8949 -0.0074 -0.0042 0.1102  726  ASP A C   
498  O O   . ASP A 70  ? 0.6910 0.6277 0.8720 -0.0139 -0.0020 0.0981  726  ASP A O   
499  C CB  . ASP A 70  ? 0.7153 0.6409 0.9147 0.0142  -0.0029 0.1039  726  ASP A CB  
500  C CG  . ASP A 70  ? 0.8833 0.8203 1.0884 0.0254  -0.0039 0.1003  726  ASP A CG  
501  O OD1 . ASP A 70  ? 0.8873 0.8463 1.0908 0.0267  -0.0081 0.1051  726  ASP A OD1 
502  O OD2 . ASP A 70  ? 0.9494 0.8739 1.1605 0.0324  -0.0004 0.0925  726  ASP A OD2 
503  N N   . SER A 71  ? 0.6712 0.5974 0.8569 -0.0108 -0.0052 0.1249  727  SER A N   
504  C CA  . SER A 71  ? 0.6690 0.5866 0.8498 -0.0235 -0.0035 0.1280  727  SER A CA  
505  C C   . SER A 71  ? 0.6758 0.6200 0.8475 -0.0327 -0.0053 0.1277  727  SER A C   
506  O O   . SER A 71  ? 0.6700 0.6156 0.8371 -0.0430 -0.0032 0.1209  727  SER A O   
507  C CB  . SER A 71  ? 0.7312 0.6311 0.9154 -0.0236 -0.0040 0.1452  727  SER A CB  
508  O OG  . SER A 71  ? 0.8571 0.7692 1.0434 -0.0160 -0.0084 0.1586  727  SER A OG  
509  N N   . GLN A 72  ? 0.5923 0.5583 0.7617 -0.0288 -0.0093 0.1342  728  GLN A N   
510  C CA  . GLN A 72  ? 0.5646 0.5574 0.7256 -0.0357 -0.0110 0.1336  728  GLN A CA  
511  C C   . GLN A 72  ? 0.5567 0.5630 0.7152 -0.0361 -0.0097 0.1163  728  GLN A C   
512  O O   . GLN A 72  ? 0.5462 0.5641 0.6990 -0.0450 -0.0085 0.1116  728  GLN A O   
513  C CB  . GLN A 72  ? 0.5761 0.5864 0.7354 -0.0309 -0.0156 0.1451  728  GLN A CB  
514  N N   . ILE A 73  ? 0.4865 0.4914 0.6496 -0.0265 -0.0099 0.1076  729  ILE A N   
515  C CA  . ILE A 73  ? 0.4852 0.5014 0.6466 -0.0256 -0.0090 0.0923  729  ILE A CA  
516  C C   . ILE A 73  ? 0.5194 0.5238 0.6806 -0.0312 -0.0053 0.0817  729  ILE A C   
517  O O   . ILE A 73  ? 0.5129 0.5299 0.6708 -0.0342 -0.0047 0.0713  729  ILE A O   
518  C CB  . ILE A 73  ? 0.5321 0.5523 0.6980 -0.0145 -0.0102 0.0866  729  ILE A CB  
519  C CG1 . ILE A 73  ? 0.5482 0.5727 0.7175 -0.0074 -0.0137 0.0986  729  ILE A CG1 
520  C CG2 . ILE A 73  ? 0.5249 0.5647 0.6866 -0.0151 -0.0107 0.0754  729  ILE A CG2 
521  C CD1 . ILE A 73  ? 0.6759 0.6957 0.8533 0.0041  -0.0140 0.0953  729  ILE A CD1 
522  N N   . LEU A 74  ? 0.4758 0.4564 0.6407 -0.0326 -0.0030 0.0841  730  LEU A N   
523  C CA  . LEU A 74  ? 0.4744 0.4418 0.6391 -0.0385 0.0003  0.0738  730  LEU A CA  
524  C C   . LEU A 74  ? 0.5170 0.5006 0.6759 -0.0489 0.0007  0.0679  730  LEU A C   
525  O O   . LEU A 74  ? 0.5154 0.5031 0.6735 -0.0498 0.0018  0.0554  730  LEU A O   
526  C CB  . LEU A 74  ? 0.4794 0.4196 0.6475 -0.0415 0.0025  0.0799  730  LEU A CB  
527  C CG  . LEU A 74  ? 0.5248 0.4501 0.6921 -0.0500 0.0059  0.0703  730  LEU A CG  
528  C CD1 . LEU A 74  ? 0.5236 0.4452 0.6923 -0.0445 0.0076  0.0551  730  LEU A CD1 
529  C CD2 . LEU A 74  ? 0.5131 0.4116 0.6836 -0.0536 0.0079  0.0782  730  LEU A CD2 
530  N N   . ASP A 75  ? 0.4766 0.4715 0.6319 -0.0560 -0.0003 0.0772  731  ASP A N   
531  C CA  . ASP A 75  ? 0.4719 0.4850 0.6224 -0.0658 0.0002  0.0739  731  ASP A CA  
532  C C   . ASP A 75  ? 0.4657 0.5005 0.6142 -0.0620 -0.0007 0.0634  731  ASP A C   
533  O O   . ASP A 75  ? 0.4774 0.5198 0.6250 -0.0671 0.0005  0.0541  731  ASP A O   
534  C CB  . ASP A 75  ? 0.5087 0.5307 0.6555 -0.0725 -0.0006 0.0875  731  ASP A CB  
535  C CG  . ASP A 75  ? 0.7165 0.7157 0.8652 -0.0773 0.0004  0.0987  731  ASP A CG  
536  O OD1 . ASP A 75  ? 0.7232 0.7155 0.8714 -0.0880 0.0027  0.0976  731  ASP A OD1 
537  O OD2 . ASP A 75  ? 0.8066 0.7943 0.9581 -0.0702 -0.0011 0.1086  731  ASP A OD2 
538  N N   . LEU A 76  ? 0.3662 0.4103 0.5148 -0.0530 -0.0030 0.0647  732  LEU A N   
539  C CA  . LEU A 76  ? 0.3390 0.4016 0.4861 -0.0485 -0.0040 0.0555  732  LEU A CA  
540  C C   . LEU A 76  ? 0.3848 0.4401 0.5349 -0.0430 -0.0031 0.0437  732  LEU A C   
541  O O   . LEU A 76  ? 0.3709 0.4393 0.5198 -0.0424 -0.0031 0.0346  732  LEU A O   
542  C CB  . LEU A 76  ? 0.3275 0.4006 0.4736 -0.0416 -0.0067 0.0608  732  LEU A CB  
543  C CG  . LEU A 76  ? 0.3736 0.4563 0.5158 -0.0453 -0.0083 0.0732  732  LEU A CG  
544  C CD1 . LEU A 76  ? 0.3599 0.4565 0.5006 -0.0389 -0.0112 0.0742  732  LEU A CD1 
545  C CD2 . LEU A 76  ? 0.3989 0.4964 0.5360 -0.0552 -0.0068 0.0731  732  LEU A CD2 
546  N N   . SER A 77  ? 0.3401 0.3750 0.4942 -0.0383 -0.0023 0.0442  733  SER A N   
547  C CA  . SER A 77  ? 0.3336 0.3606 0.4900 -0.0334 -0.0011 0.0335  733  SER A CA  
548  C C   . SER A 77  ? 0.3685 0.3940 0.5232 -0.0415 0.0007  0.0251  733  SER A C   
549  O O   . SER A 77  ? 0.3530 0.3854 0.5069 -0.0397 0.0008  0.0153  733  SER A O   
550  C CB  . SER A 77  ? 0.3597 0.3654 0.5208 -0.0271 0.0000  0.0361  733  SER A CB  
551  O OG  . SER A 77  ? 0.3748 0.3747 0.5374 -0.0222 0.0016  0.0256  733  SER A OG  
552  N N   . ASN A 78  ? 0.3264 0.3433 0.4804 -0.0506 0.0019  0.0296  734  ASN A N   
553  C CA  . ASN A 78  ? 0.3267 0.3423 0.4796 -0.0600 0.0035  0.0224  734  ASN A CA  
554  C C   . ASN A 78  ? 0.3610 0.4013 0.5115 -0.0643 0.0026  0.0179  734  ASN A C   
555  O O   . ASN A 78  ? 0.3382 0.3830 0.4884 -0.0678 0.0029  0.0088  734  ASN A O   
556  C CB  . ASN A 78  ? 0.3636 0.3645 0.5167 -0.0695 0.0050  0.0293  734  ASN A CB  
557  C CG  . ASN A 78  ? 0.6920 0.6651 0.8483 -0.0668 0.0066  0.0319  734  ASN A CG  
558  O OD1 . ASN A 78  ? 0.6172 0.5799 0.7753 -0.0590 0.0074  0.0255  734  ASN A OD1 
559  N ND2 . ASN A 78  ? 0.6021 0.5621 0.7590 -0.0733 0.0075  0.0415  734  ASN A ND2 
560  N N   . ARG A 79  ? 0.3167 0.3735 0.4655 -0.0637 0.0014  0.0243  735  ARG A N   
561  C CA  . ARG A 79  ? 0.3012 0.3824 0.4484 -0.0666 0.0010  0.0208  735  ARG A CA  
562  C C   . ARG A 79  ? 0.3254 0.4162 0.4733 -0.0595 0.0001  0.0106  735  ARG A C   
563  O O   . ARG A 79  ? 0.3260 0.4327 0.4739 -0.0625 0.0001  0.0050  735  ARG A O   
564  C CB  . ARG A 79  ? 0.3223 0.4168 0.4670 -0.0661 0.0002  0.0294  735  ARG A CB  
565  C CG  . ARG A 79  ? 0.4498 0.5531 0.5925 -0.0770 0.0015  0.0356  735  ARG A CG  
566  C CD  . ARG A 79  ? 0.5596 0.6547 0.7003 -0.0792 0.0012  0.0491  735  ARG A CD  
567  N NE  . ARG A 79  ? 0.5358 0.6484 0.6729 -0.0763 0.0000  0.0540  735  ARG A NE  
568  C CZ  . ARG A 79  ? 0.6200 0.7348 0.7537 -0.0799 -0.0004 0.0659  735  ARG A CZ  
569  N NH1 . ARG A 79  ? 0.4761 0.6085 0.6055 -0.0776 -0.0015 0.0686  735  ARG A NH1 
570  N NH2 . ARG A 79  ? 0.4070 0.5062 0.5412 -0.0863 0.0004  0.0753  735  ARG A NH2 
571  N N   . PHE A 80  ? 0.2713 0.3529 0.4202 -0.0502 -0.0007 0.0089  736  PHE A N   
572  C CA  . PHE A 80  ? 0.2569 0.3446 0.4063 -0.0431 -0.0015 0.0004  736  PHE A CA  
573  C C   . PHE A 80  ? 0.2906 0.3725 0.4404 -0.0459 -0.0008 -0.0077 736  PHE A C   
574  O O   . PHE A 80  ? 0.2684 0.3632 0.4181 -0.0457 -0.0015 -0.0143 736  PHE A O   
575  C CB  . PHE A 80  ? 0.2783 0.3576 0.4290 -0.0333 -0.0023 0.0020  736  PHE A CB  
576  C CG  . PHE A 80  ? 0.2959 0.3793 0.4471 -0.0266 -0.0028 -0.0059 736  PHE A CG  
577  C CD1 . PHE A 80  ? 0.3207 0.4190 0.4714 -0.0225 -0.0041 -0.0078 736  PHE A CD1 
578  C CD2 . PHE A 80  ? 0.3176 0.3898 0.4693 -0.0249 -0.0019 -0.0118 736  PHE A CD2 
579  C CE1 . PHE A 80  ? 0.3130 0.4141 0.4643 -0.0167 -0.0046 -0.0143 736  PHE A CE1 
580  C CE2 . PHE A 80  ? 0.3318 0.4088 0.4833 -0.0194 -0.0023 -0.0183 736  PHE A CE2 
581  C CZ  . PHE A 80  ? 0.2933 0.3841 0.4448 -0.0152 -0.0038 -0.0189 736  PHE A CZ  
582  N N   . TYR A 81  ? 0.2544 0.3167 0.4046 -0.0484 0.0006  -0.0072 737  TYR A N   
583  C CA  . TYR A 81  ? 0.2598 0.3137 0.4095 -0.0521 0.0015  -0.0152 737  TYR A CA  
584  C C   . TYR A 81  ? 0.3607 0.4257 0.5099 -0.0625 0.0013  -0.0182 737  TYR A C   
585  O O   . TYR A 81  ? 0.3821 0.4474 0.5304 -0.0659 0.0012  -0.0262 737  TYR A O   
586  C CB  . TYR A 81  ? 0.2778 0.3069 0.4283 -0.0525 0.0035  -0.0137 737  TYR A CB  
587  C CG  . TYR A 81  ? 0.2906 0.3094 0.4427 -0.0417 0.0040  -0.0132 737  TYR A CG  
588  C CD1 . TYR A 81  ? 0.3098 0.3316 0.4610 -0.0355 0.0040  -0.0209 737  TYR A CD1 
589  C CD2 . TYR A 81  ? 0.2970 0.3036 0.4517 -0.0379 0.0046  -0.0046 737  TYR A CD2 
590  C CE1 . TYR A 81  ? 0.3118 0.3258 0.4650 -0.0260 0.0048  -0.0204 737  TYR A CE1 
591  C CE2 . TYR A 81  ? 0.2978 0.2968 0.4551 -0.0279 0.0051  -0.0040 737  TYR A CE2 
592  C CZ  . TYR A 81  ? 0.3611 0.3640 0.5177 -0.0222 0.0054  -0.0122 737  TYR A CZ  
593  O OH  . TYR A 81  ? 0.3687 0.3656 0.5285 -0.0129 0.0063  -0.0115 737  TYR A OH  
594  N N   . THR A 82  ? 0.3151 0.3911 0.4646 -0.0677 0.0013  -0.0119 738  THR A N   
595  C CA  . THR A 82  ? 0.3139 0.4046 0.4639 -0.0777 0.0014  -0.0132 738  THR A CA  
596  C C   . THR A 82  ? 0.3543 0.4685 0.5053 -0.0737 -0.0001 -0.0186 738  THR A C   
597  O O   . THR A 82  ? 0.3501 0.4766 0.5025 -0.0793 -0.0006 -0.0236 738  THR A O   
598  C CB  . THR A 82  ? 0.4069 0.4997 0.5568 -0.0841 0.0024  -0.0032 738  THR A CB  
599  O OG1 . THR A 82  ? 0.4145 0.4834 0.5641 -0.0870 0.0036  0.0021  738  THR A OG1 
600  C CG2 . THR A 82  ? 0.3741 0.4843 0.5251 -0.0950 0.0030  -0.0037 738  THR A CG2 
601  N N   . LEU A 83  ? 0.2926 0.4129 0.4434 -0.0640 -0.0009 -0.0174 739  LEU A N   
602  C CA  . LEU A 83  ? 0.2599 0.4000 0.4120 -0.0588 -0.0020 -0.0219 739  LEU A CA  
603  C C   . LEU A 83  ? 0.2395 0.3765 0.3916 -0.0523 -0.0033 -0.0289 739  LEU A C   
604  O O   . LEU A 83  ? 0.1889 0.3404 0.3426 -0.0511 -0.0045 -0.0338 739  LEU A O   
605  C CB  . LEU A 83  ? 0.2524 0.3999 0.4039 -0.0527 -0.0020 -0.0176 739  LEU A CB  
606  C CG  . LEU A 83  ? 0.3026 0.4569 0.4531 -0.0589 -0.0007 -0.0105 739  LEU A CG  
607  C CD1 . LEU A 83  ? 0.3064 0.4610 0.4548 -0.0530 -0.0011 -0.0058 739  LEU A CD1 
608  C CD2 . LEU A 83  ? 0.3064 0.4829 0.4589 -0.0638 0.0002  -0.0130 739  LEU A CD2 
609  N N   . ILE A 84  ? 0.2089 0.3277 0.3594 -0.0481 -0.0031 -0.0288 740  ILE A N   
610  C CA  . ILE A 84  ? 0.2244 0.3389 0.3739 -0.0427 -0.0039 -0.0349 740  ILE A CA  
611  C C   . ILE A 84  ? 0.2920 0.3888 0.4398 -0.0473 -0.0027 -0.0375 740  ILE A C   
612  O O   . ILE A 84  ? 0.2845 0.3648 0.4318 -0.0440 -0.0013 -0.0352 740  ILE A O   
613  C CB  . ILE A 84  ? 0.2645 0.3771 0.4140 -0.0319 -0.0043 -0.0342 740  ILE A CB  
614  C CG1 . ILE A 84  ? 0.2597 0.3881 0.4108 -0.0280 -0.0052 -0.0322 740  ILE A CG1 
615  C CG2 . ILE A 84  ? 0.2874 0.3979 0.4356 -0.0273 -0.0050 -0.0401 740  ILE A CG2 
616  C CD1 . ILE A 84  ? 0.3275 0.4751 0.4805 -0.0273 -0.0064 -0.0368 740  ILE A CD1 
617  N N   . PRO A 85  ? 0.2722 0.3725 0.4193 -0.0553 -0.0030 -0.0426 741  PRO A N   
618  C CA  . PRO A 85  ? 0.2823 0.3646 0.4271 -0.0605 -0.0016 -0.0465 741  PRO A CA  
619  C C   . PRO A 85  ? 0.3385 0.4091 0.4806 -0.0536 -0.0009 -0.0514 741  PRO A C   
620  O O   . PRO A 85  ? 0.3276 0.4081 0.4684 -0.0487 -0.0023 -0.0553 741  PRO A O   
621  C CB  . PRO A 85  ? 0.2967 0.3899 0.4412 -0.0707 -0.0028 -0.0517 741  PRO A CB  
622  C CG  . PRO A 85  ? 0.3405 0.4578 0.4881 -0.0701 -0.0047 -0.0498 741  PRO A CG  
623  C CD  . PRO A 85  ? 0.2765 0.3982 0.4253 -0.0598 -0.0047 -0.0453 741  PRO A CD  
624  N N   . HIS A 86  ? 0.3104 0.3598 0.4520 -0.0532 0.0016  -0.0508 742  HIS A N   
625  C CA  . HIS A 86  ? 0.3084 0.3455 0.4479 -0.0468 0.0033  -0.0555 742  HIS A CA  
626  C C   . HIS A 86  ? 0.3644 0.3878 0.5005 -0.0539 0.0051  -0.0635 742  HIS A C   
627  O O   . HIS A 86  ? 0.3155 0.3348 0.4517 -0.0637 0.0053  -0.0640 742  HIS A O   
628  C CB  . HIS A 86  ? 0.3164 0.3415 0.4589 -0.0384 0.0050  -0.0491 742  HIS A CB  
629  C CG  . HIS A 86  ? 0.3488 0.3871 0.4932 -0.0305 0.0032  -0.0441 742  HIS A CG  
630  N ND1 . HIS A 86  ? 0.3623 0.4146 0.5083 -0.0323 0.0012  -0.0389 742  HIS A ND1 
631  C CD2 . HIS A 86  ? 0.3615 0.4001 0.5067 -0.0214 0.0035  -0.0439 742  HIS A CD2 
632  C CE1 . HIS A 86  ? 0.3424 0.4023 0.4896 -0.0244 0.0002  -0.0365 742  HIS A CE1 
633  N NE2 . HIS A 86  ? 0.3508 0.4031 0.4978 -0.0180 0.0014  -0.0391 742  HIS A NE2 
634  N N   . ASP A 87  ? 0.3846 0.4022 0.5174 -0.0495 0.0065  -0.0703 743  ASP A N   
635  C CA  . ASP A 87  ? 0.4063 0.4122 0.5347 -0.0555 0.0085  -0.0798 743  ASP A CA  
636  C C   . ASP A 87  ? 0.4944 0.4758 0.6239 -0.0522 0.0127  -0.0805 743  ASP A C   
637  O O   . ASP A 87  ? 0.5098 0.4859 0.6386 -0.0437 0.0150  -0.0829 743  ASP A O   
638  C CB  . ASP A 87  ? 0.4363 0.4536 0.5590 -0.0538 0.0074  -0.0876 743  ASP A CB  
639  C CG  . ASP A 87  ? 0.6273 0.6409 0.7441 -0.0631 0.0078  -0.0982 743  ASP A CG  
640  O OD1 . ASP A 87  ? 0.6233 0.6299 0.7408 -0.0731 0.0080  -0.0997 743  ASP A OD1 
641  O OD2 . ASP A 87  ? 0.7488 0.7671 0.8599 -0.0610 0.0079  -0.1051 743  ASP A OD2 
642  N N   . PHE A 88  ? 0.4565 0.4231 0.5885 -0.0586 0.0141  -0.0778 744  PHE A N   
643  C CA  . PHE A 88  ? 0.4554 0.3965 0.5897 -0.0560 0.0182  -0.0778 744  PHE A CA  
644  C C   . PHE A 88  ? 0.4930 0.4178 0.6249 -0.0673 0.0200  -0.0846 744  PHE A C   
645  O O   . PHE A 88  ? 0.5215 0.4228 0.6550 -0.0659 0.0239  -0.0865 744  PHE A O   
646  C CB  . PHE A 88  ? 0.4756 0.4112 0.6164 -0.0503 0.0182  -0.0652 744  PHE A CB  
647  C CG  . PHE A 88  ? 0.4876 0.4352 0.6308 -0.0386 0.0171  -0.0601 744  PHE A CG  
648  C CD1 . PHE A 88  ? 0.5311 0.4714 0.6751 -0.0291 0.0199  -0.0634 744  PHE A CD1 
649  C CD2 . PHE A 88  ? 0.5080 0.4742 0.6527 -0.0375 0.0136  -0.0526 744  PHE A CD2 
650  C CE1 . PHE A 88  ? 0.5284 0.4802 0.6750 -0.0193 0.0189  -0.0587 744  PHE A CE1 
651  C CE2 . PHE A 88  ? 0.5407 0.5168 0.6875 -0.0276 0.0127  -0.0485 744  PHE A CE2 
652  C CZ  . PHE A 88  ? 0.5141 0.4830 0.6618 -0.0189 0.0152  -0.0514 744  PHE A CZ  
653  N N   . GLY A 89  ? 0.4194 0.3572 0.5480 -0.0782 0.0173  -0.0887 745  GLY A N   
654  C CA  . GLY A 89  ? 0.4033 0.3298 0.5295 -0.0913 0.0183  -0.0956 745  GLY A CA  
655  C C   . GLY A 89  ? 0.4645 0.3772 0.5958 -0.0968 0.0191  -0.0865 745  GLY A C   
656  O O   . GLY A 89  ? 0.4456 0.3714 0.5805 -0.0969 0.0167  -0.0762 745  GLY A O   
657  N N   . MET A 90  ? 0.4608 0.3460 0.5925 -0.1007 0.0228  -0.0901 746  MET A N   
658  C CA  . MET A 90  ? 0.4743 0.3412 0.6107 -0.1063 0.0242  -0.0814 746  MET A CA  
659  C C   . MET A 90  ? 0.5141 0.3645 0.6562 -0.0940 0.0265  -0.0715 746  MET A C   
660  O O   . MET A 90  ? 0.5008 0.3326 0.6468 -0.0971 0.0280  -0.0637 746  MET A O   
661  C CB  . MET A 90  ? 0.5185 0.3639 0.6525 -0.1188 0.0268  -0.0907 746  MET A CB  
662  C CG  . MET A 90  ? 0.5773 0.4406 0.7066 -0.1326 0.0239  -0.0991 746  MET A CG  
663  S SD  . MET A 90  ? 0.6321 0.5237 0.7646 -0.1410 0.0192  -0.0879 746  MET A SD  
664  C CE  . MET A 90  ? 0.5803 0.5081 0.7090 -0.1358 0.0149  -0.0939 746  MET A CE  
665  N N   . LYS A 91  ? 0.4679 0.3259 0.6106 -0.0804 0.0267  -0.0712 747  LYS A N   
666  C CA  . LYS A 91  ? 0.4740 0.3214 0.6227 -0.0676 0.0283  -0.0621 747  LYS A CA  
667  C C   . LYS A 91  ? 0.5076 0.3730 0.6593 -0.0646 0.0246  -0.0483 747  LYS A C   
668  O O   . LYS A 91  ? 0.4939 0.3837 0.6429 -0.0673 0.0213  -0.0486 747  LYS A O   
669  C CB  . LYS A 91  ? 0.5107 0.3605 0.6588 -0.0551 0.0303  -0.0688 747  LYS A CB  
670  C CG  . LYS A 91  ? 0.7175 0.5531 0.8611 -0.0569 0.0343  -0.0841 747  LYS A CG  
671  C CD  . LYS A 91  ? 0.8464 0.6921 0.9878 -0.0466 0.0357  -0.0908 747  LYS A CD  
672  C CE  . LYS A 91  ? 0.9733 0.8001 1.1203 -0.0347 0.0406  -0.0907 747  LYS A CE  
673  N NZ  . LYS A 91  ? 1.0318 0.8704 1.1771 -0.0249 0.0421  -0.0962 747  LYS A NZ  
674  N N   . LYS A 92  ? 0.4572 0.3112 0.6147 -0.0583 0.0252  -0.0365 748  LYS A N   
675  C CA  . LYS A 92  ? 0.4428 0.3128 0.6029 -0.0545 0.0219  -0.0233 748  LYS A CA  
676  C C   . LYS A 92  ? 0.5057 0.3953 0.6655 -0.0438 0.0203  -0.0251 748  LYS A C   
677  O O   . LYS A 92  ? 0.4964 0.3791 0.6576 -0.0350 0.0226  -0.0307 748  LYS A O   
678  C CB  . LYS A 92  ? 0.4591 0.3115 0.6254 -0.0493 0.0229  -0.0106 748  LYS A CB  
679  C CG  . LYS A 92  ? 0.4651 0.3006 0.6319 -0.0602 0.0238  -0.0047 748  LYS A CG  
680  C CD  . LYS A 92  ? 0.5280 0.3480 0.7010 -0.0542 0.0241  0.0098  748  LYS A CD  
681  C CE  . LYS A 92  ? 0.6063 0.4052 0.7801 -0.0649 0.0256  0.0153  748  LYS A CE  
682  N NZ  . LYS A 92  ? 0.7256 0.5022 0.9061 -0.0575 0.0269  0.0274  748  LYS A NZ  
683  N N   . PRO A 93  ? 0.4877 0.4018 0.6458 -0.0446 0.0167  -0.0211 749  PRO A N   
684  C CA  . PRO A 93  ? 0.4849 0.4157 0.6429 -0.0351 0.0153  -0.0227 749  PRO A CA  
685  C C   . PRO A 93  ? 0.5229 0.4496 0.6866 -0.0240 0.0154  -0.0139 749  PRO A C   
686  O O   . PRO A 93  ? 0.5091 0.4260 0.6761 -0.0242 0.0152  -0.0039 749  PRO A O   
687  C CB  . PRO A 93  ? 0.4992 0.4544 0.6546 -0.0397 0.0117  -0.0202 749  PRO A CB  
688  C CG  . PRO A 93  ? 0.5623 0.5156 0.7165 -0.0518 0.0115  -0.0178 749  PRO A CG  
689  C CD  . PRO A 93  ? 0.5124 0.4396 0.6691 -0.0540 0.0142  -0.0148 749  PRO A CD  
690  N N   . PRO A 94  ? 0.4860 0.4205 0.6509 -0.0144 0.0154  -0.0166 750  PRO A N   
691  C CA  . PRO A 94  ? 0.4824 0.4156 0.6535 -0.0044 0.0150  -0.0077 750  PRO A CA  
692  C C   . PRO A 94  ? 0.5045 0.4522 0.6760 -0.0056 0.0111  0.0036  750  PRO A C   
693  O O   . PRO A 94  ? 0.4912 0.4573 0.6589 -0.0090 0.0087  0.0021  750  PRO A O   
694  C CB  . PRO A 94  ? 0.5018 0.4437 0.6733 0.0038  0.0158  -0.0141 750  PRO A CB  
695  C CG  . PRO A 94  ? 0.5521 0.5058 0.7171 -0.0018 0.0150  -0.0233 750  PRO A CG  
696  C CD  . PRO A 94  ? 0.4960 0.4416 0.6571 -0.0124 0.0156  -0.0268 750  PRO A CD  
697  N N   . LEU A 95  ? 0.4494 0.3892 0.6256 -0.0026 0.0105  0.0147  751  LEU A N   
698  C CA  . LEU A 95  ? 0.4342 0.3872 0.6103 -0.0035 0.0069  0.0262  751  LEU A CA  
699  C C   . LEU A 95  ? 0.4481 0.4210 0.6246 0.0027  0.0043  0.0264  751  LEU A C   
700  O O   . LEU A 95  ? 0.4438 0.4154 0.6248 0.0115  0.0050  0.0250  751  LEU A O   
701  C CB  . LEU A 95  ? 0.4356 0.3747 0.6173 0.0001  0.0068  0.0385  751  LEU A CB  
702  C CG  . LEU A 95  ? 0.4908 0.4314 0.6706 -0.0070 0.0046  0.0507  751  LEU A CG  
703  C CD1 . LEU A 95  ? 0.4932 0.4228 0.6794 -0.0005 0.0038  0.0637  751  LEU A CD1 
704  C CD2 . LEU A 95  ? 0.5114 0.4770 0.6864 -0.0102 0.0011  0.0539  751  LEU A CD2 
705  N N   . LEU A 96  ? 0.3874 0.3787 0.5594 -0.0019 0.0015  0.0281  752  LEU A N   
706  C CA  . LEU A 96  ? 0.3772 0.3868 0.5491 0.0028  -0.0011 0.0285  752  LEU A CA  
707  C C   . LEU A 96  ? 0.4432 0.4576 0.6170 0.0045  -0.0039 0.0412  752  LEU A C   
708  O O   . LEU A 96  ? 0.4415 0.4652 0.6112 -0.0016 -0.0057 0.0466  752  LEU A O   
709  C CB  . LEU A 96  ? 0.3713 0.3980 0.5376 -0.0023 -0.0022 0.0221  752  LEU A CB  
710  C CG  . LEU A 96  ? 0.4306 0.4553 0.5939 -0.0062 -0.0002 0.0111  752  LEU A CG  
711  C CD1 . LEU A 96  ? 0.4112 0.4528 0.5701 -0.0119 -0.0016 0.0081  752  LEU A CD1 
712  C CD2 . LEU A 96  ? 0.4804 0.5036 0.6452 0.0006  0.0010  0.0034  752  LEU A CD2 
713  N N   . ASN A 97  ? 0.4149 0.4234 0.5953 0.0127  -0.0042 0.0464  753  ASN A N   
714  C CA  . ASN A 97  ? 0.4133 0.4263 0.5965 0.0156  -0.0072 0.0592  753  ASN A CA  
715  C C   . ASN A 97  ? 0.4544 0.4815 0.6414 0.0229  -0.0097 0.0601  753  ASN A C   
716  O O   . ASN A 97  ? 0.4756 0.5080 0.6658 0.0261  -0.0127 0.0705  753  ASN A O   
717  C CB  . ASN A 97  ? 0.4376 0.4300 0.6268 0.0187  -0.0056 0.0669  753  ASN A CB  
718  C CG  . ASN A 97  ? 0.6516 0.6314 0.8482 0.0277  -0.0026 0.0617  753  ASN A CG  
719  O OD1 . ASN A 97  ? 0.5920 0.5712 0.7875 0.0285  0.0000  0.0499  753  ASN A OD1 
720  N ND2 . ASN A 97  ? 0.4923 0.4629 0.6968 0.0348  -0.0027 0.0707  753  ASN A ND2 
721  N N   . ASN A 98  ? 0.3804 0.4141 0.5669 0.0249  -0.0088 0.0499  754  ASN A N   
722  C CA  . ASN A 98  ? 0.3620 0.4083 0.5523 0.0310  -0.0108 0.0497  754  ASN A CA  
723  C C   . ASN A 98  ? 0.4029 0.4637 0.5880 0.0280  -0.0117 0.0413  754  ASN A C   
724  O O   . ASN A 98  ? 0.3908 0.4513 0.5702 0.0227  -0.0103 0.0346  754  ASN A O   
725  C CB  . ASN A 98  ? 0.3416 0.3781 0.5401 0.0394  -0.0080 0.0472  754  ASN A CB  
726  C CG  . ASN A 98  ? 0.7246 0.7501 0.9214 0.0390  -0.0036 0.0361  754  ASN A CG  
727  O OD1 . ASN A 98  ? 0.6139 0.6454 0.8099 0.0405  -0.0025 0.0282  754  ASN A OD1 
728  N ND2 . ASN A 98  ? 0.7173 0.7262 0.9131 0.0365  -0.0009 0.0352  754  ASN A ND2 
729  N N   . ALA A 99  ? 0.3410 0.4148 0.5285 0.0313  -0.0142 0.0421  755  ALA A N   
730  C CA  . ALA A 99  ? 0.3302 0.4166 0.5137 0.0292  -0.0152 0.0349  755  ALA A CA  
731  C C   . ALA A 99  ? 0.3574 0.4384 0.5413 0.0312  -0.0120 0.0250  755  ALA A C   
732  O O   . ALA A 99  ? 0.3412 0.4276 0.5203 0.0280  -0.0119 0.0183  755  ALA A O   
733  C CB  . ALA A 99  ? 0.3375 0.4377 0.5241 0.0317  -0.0186 0.0386  755  ALA A CB  
734  N N   . ASP A 100 ? 0.3251 0.3959 0.5147 0.0366  -0.0093 0.0243  756  ASP A N   
735  C CA  . ASP A 100 ? 0.3152 0.3811 0.5046 0.0384  -0.0060 0.0154  756  ASP A CA  
736  C C   . ASP A 100 ? 0.3431 0.4024 0.5261 0.0333  -0.0042 0.0093  756  ASP A C   
737  O O   . ASP A 100 ? 0.3146 0.3770 0.4940 0.0320  -0.0034 0.0021  756  ASP A O   
738  C CB  . ASP A 100 ? 0.3377 0.3944 0.5344 0.0452  -0.0029 0.0158  756  ASP A CB  
739  C CG  . ASP A 100 ? 0.4931 0.5594 0.6972 0.0507  -0.0041 0.0195  756  ASP A CG  
740  O OD1 . ASP A 100 ? 0.5441 0.6216 0.7470 0.0496  -0.0056 0.0167  756  ASP A OD1 
741  O OD2 . ASP A 100 ? 0.5269 0.5894 0.7386 0.0562  -0.0036 0.0253  756  ASP A OD2 
742  N N   . SER A 101 ? 0.3387 0.3897 0.5202 0.0299  -0.0039 0.0129  757  SER A N   
743  C CA  . SER A 101 ? 0.3499 0.3949 0.5261 0.0238  -0.0025 0.0084  757  SER A CA  
744  C C   . SER A 101 ? 0.4143 0.4723 0.5849 0.0184  -0.0046 0.0062  757  SER A C   
745  O O   . SER A 101 ? 0.4182 0.4773 0.5851 0.0153  -0.0036 -0.0006 757  SER A O   
746  C CB  . SER A 101 ? 0.3897 0.4227 0.5670 0.0213  -0.0019 0.0146  757  SER A CB  
747  O OG  . SER A 101 ? 0.4580 0.4775 0.6411 0.0272  0.0006  0.0158  757  SER A OG  
748  N N   . VAL A 102 ? 0.3636 0.4324 0.5338 0.0176  -0.0074 0.0118  758  VAL A N   
749  C CA  . VAL A 102 ? 0.3478 0.4298 0.5132 0.0131  -0.0090 0.0096  758  VAL A CA  
750  C C   . VAL A 102 ? 0.3445 0.4335 0.5096 0.0160  -0.0092 0.0025  758  VAL A C   
751  O O   . VAL A 102 ? 0.3131 0.4076 0.4749 0.0134  -0.0090 -0.0030 758  VAL A O   
752  C CB  . VAL A 102 ? 0.3904 0.4815 0.5545 0.0110  -0.0117 0.0176  758  VAL A CB  
753  C CG1 . VAL A 102 ? 0.3786 0.4851 0.5384 0.0082  -0.0131 0.0140  758  VAL A CG1 
754  C CG2 . VAL A 102 ? 0.3896 0.4744 0.5525 0.0063  -0.0113 0.0243  758  VAL A CG2 
755  N N   . GLN A 103 ? 0.2887 0.3772 0.4578 0.0213  -0.0094 0.0030  759  GLN A N   
756  C CA  . GLN A 103 ? 0.2806 0.3740 0.4502 0.0240  -0.0094 -0.0025 759  GLN A CA  
757  C C   . GLN A 103 ? 0.3225 0.4101 0.4901 0.0239  -0.0070 -0.0092 759  GLN A C   
758  O O   . GLN A 103 ? 0.3255 0.4187 0.4902 0.0227  -0.0074 -0.0139 759  GLN A O   
759  C CB  . GLN A 103 ? 0.2949 0.3879 0.4702 0.0292  -0.0095 0.0001  759  GLN A CB  
760  C CG  . GLN A 103 ? 0.4393 0.5385 0.6154 0.0309  -0.0100 -0.0039 759  GLN A CG  
761  C CD  . GLN A 103 ? 0.6132 0.7112 0.7954 0.0356  -0.0089 -0.0025 759  GLN A CD  
762  O OE1 . GLN A 103 ? 0.5551 0.6505 0.7422 0.0385  -0.0087 0.0026  759  GLN A OE1 
763  N NE2 . GLN A 103 ? 0.4406 0.5408 0.6230 0.0367  -0.0082 -0.0066 759  GLN A NE2 
764  N N   . ALA A 104 ? 0.2680 0.3445 0.4370 0.0251  -0.0046 -0.0095 760  ALA A N   
765  C CA  . ALA A 104 ? 0.2577 0.3287 0.4241 0.0244  -0.0024 -0.0159 760  ALA A CA  
766  C C   . ALA A 104 ? 0.2884 0.3637 0.4501 0.0188  -0.0032 -0.0190 760  ALA A C   
767  O O   . ALA A 104 ? 0.2877 0.3672 0.4470 0.0186  -0.0032 -0.0240 760  ALA A O   
768  C CB  . ALA A 104 ? 0.2661 0.3239 0.4343 0.0257  0.0004  -0.0158 760  ALA A CB  
769  N N   . LYS A 105 ? 0.2434 0.3190 0.4043 0.0144  -0.0040 -0.0153 761  LYS A N   
770  C CA  . LYS A 105 ? 0.2387 0.3203 0.3961 0.0087  -0.0045 -0.0178 761  LYS A CA  
771  C C   . LYS A 105 ? 0.2769 0.3726 0.4333 0.0090  -0.0062 -0.0195 761  LYS A C   
772  O O   . LYS A 105 ? 0.3017 0.4035 0.4563 0.0071  -0.0063 -0.0239 761  LYS A O   
773  C CB  . LYS A 105 ? 0.2641 0.3422 0.4211 0.0032  -0.0043 -0.0131 761  LYS A CB  
774  C CG  . LYS A 105 ? 0.3312 0.3934 0.4891 0.0021  -0.0022 -0.0127 761  LYS A CG  
775  C CD  . LYS A 105 ? 0.3491 0.4079 0.5046 -0.0009 -0.0008 -0.0203 761  LYS A CD  
776  C CE  . LYS A 105 ? 0.2429 0.2852 0.3988 -0.0029 0.0015  -0.0212 761  LYS A CE  
777  N NZ  . LYS A 105 ? 0.4722 0.5079 0.6279 0.0017  0.0035  -0.0271 761  LYS A NZ  
778  N N   . ALA A 106 ? 0.1978 0.2987 0.3553 0.0115  -0.0076 -0.0164 762  ALA A N   
779  C CA  . ALA A 106 ? 0.1828 0.2953 0.3394 0.0123  -0.0089 -0.0188 762  ALA A CA  
780  C C   . ALA A 106 ? 0.2313 0.3438 0.3883 0.0159  -0.0086 -0.0241 762  ALA A C   
781  O O   . ALA A 106 ? 0.1814 0.3012 0.3375 0.0157  -0.0089 -0.0278 762  ALA A O   
782  C CB  . ALA A 106 ? 0.1842 0.3007 0.3418 0.0138  -0.0104 -0.0150 762  ALA A CB  
783  N N   . GLU A 107 ? 0.2133 0.3178 0.3720 0.0194  -0.0078 -0.0241 763  GLU A N   
784  C CA  . GLU A 107 ? 0.2058 0.3093 0.3645 0.0227  -0.0072 -0.0278 763  GLU A CA  
785  C C   . GLU A 107 ? 0.2070 0.3111 0.3631 0.0209  -0.0067 -0.0317 763  GLU A C   
786  O O   . GLU A 107 ? 0.2153 0.3241 0.3707 0.0226  -0.0074 -0.0344 763  GLU A O   
787  C CB  . GLU A 107 ? 0.2303 0.3262 0.3912 0.0260  -0.0058 -0.0265 763  GLU A CB  
788  C CG  . GLU A 107 ? 0.3798 0.4777 0.5443 0.0283  -0.0067 -0.0231 763  GLU A CG  
789  C CD  . GLU A 107 ? 0.7126 0.8047 0.8808 0.0314  -0.0051 -0.0206 763  GLU A CD  
790  O OE1 . GLU A 107 ? 0.6409 0.7261 0.8086 0.0323  -0.0027 -0.0224 763  GLU A OE1 
791  O OE2 . GLU A 107 ? 0.6222 0.7175 0.7941 0.0329  -0.0062 -0.0172 763  GLU A OE2 
792  N N   . MET A 108 ? 0.1283 0.2274 0.2831 0.0174  -0.0058 -0.0319 764  MET A N   
793  C CA  . MET A 108 ? 0.1249 0.2256 0.2771 0.0144  -0.0056 -0.0358 764  MET A CA  
794  C C   . MET A 108 ? 0.1677 0.2804 0.3199 0.0125  -0.0072 -0.0370 764  MET A C   
795  O O   . MET A 108 ? 0.1447 0.2635 0.2963 0.0134  -0.0081 -0.0400 764  MET A O   
796  C CB  . MET A 108 ? 0.1654 0.2581 0.3167 0.0098  -0.0043 -0.0358 764  MET A CB  
797  C CG  . MET A 108 ? 0.2289 0.3256 0.3776 0.0047  -0.0047 -0.0399 764  MET A CG  
798  S SD  . MET A 108 ? 0.3063 0.3957 0.4544 -0.0031 -0.0036 -0.0393 764  MET A SD  
799  C CE  . MET A 108 ? 0.2528 0.3506 0.4030 -0.0052 -0.0046 -0.0339 764  MET A CE  
800  N N   . LEU A 109 ? 0.1311 0.2482 0.2844 0.0102  -0.0075 -0.0343 765  LEU A N   
801  C CA  . LEU A 109 ? 0.1333 0.2629 0.2871 0.0085  -0.0083 -0.0356 765  LEU A CA  
802  C C   . LEU A 109 ? 0.1549 0.2909 0.3099 0.0137  -0.0092 -0.0380 765  LEU A C   
803  O O   . LEU A 109 ? 0.1347 0.2794 0.2907 0.0140  -0.0097 -0.0407 765  LEU A O   
804  C CB  . LEU A 109 ? 0.1399 0.2731 0.2935 0.0048  -0.0080 -0.0320 765  LEU A CB  
805  C CG  . LEU A 109 ? 0.2101 0.3380 0.3628 -0.0014 -0.0072 -0.0290 765  LEU A CG  
806  C CD1 . LEU A 109 ? 0.2025 0.3340 0.3546 -0.0045 -0.0071 -0.0240 765  LEU A CD1 
807  C CD2 . LEU A 109 ? 0.2554 0.3890 0.4079 -0.0064 -0.0070 -0.0323 765  LEU A CD2 
808  N N   . ASP A 110 ? 0.1375 0.2691 0.2932 0.0177  -0.0093 -0.0369 766  ASP A N   
809  C CA  . ASP A 110 ? 0.1182 0.2526 0.2753 0.0225  -0.0099 -0.0389 766  ASP A CA  
810  C C   . ASP A 110 ? 0.1264 0.2609 0.2834 0.0249  -0.0104 -0.0409 766  ASP A C   
811  O O   . ASP A 110 ? 0.1344 0.2756 0.2930 0.0275  -0.0111 -0.0428 766  ASP A O   
812  C CB  . ASP A 110 ? 0.1253 0.2526 0.2831 0.0252  -0.0100 -0.0371 766  ASP A CB  
813  C CG  . ASP A 110 ? 0.2009 0.3299 0.3589 0.0240  -0.0103 -0.0352 766  ASP A CG  
814  O OD1 . ASP A 110 ? 0.2333 0.3681 0.3903 0.0207  -0.0103 -0.0346 766  ASP A OD1 
815  O OD2 . ASP A 110 ? 0.2202 0.3456 0.3795 0.0258  -0.0107 -0.0341 766  ASP A OD2 
816  N N   . ASN A 111 ? 0.0800 0.2076 0.2351 0.0241  -0.0099 -0.0403 767  ASN A N   
817  C CA  . ASN A 111 ? 0.0939 0.2221 0.2475 0.0255  -0.0104 -0.0418 767  ASN A CA  
818  C C   . ASN A 111 ? 0.1655 0.3032 0.3191 0.0229  -0.0115 -0.0438 767  ASN A C   
819  O O   . ASN A 111 ? 0.1596 0.3034 0.3137 0.0257  -0.0129 -0.0446 767  ASN A O   
820  C CB  . ASN A 111 ? 0.1498 0.2691 0.3007 0.0245  -0.0091 -0.0416 767  ASN A CB  
821  C CG  . ASN A 111 ? 0.1157 0.2285 0.2674 0.0282  -0.0081 -0.0396 767  ASN A CG  
822  O OD1 . ASN A 111 ? 0.1084 0.2226 0.2609 0.0316  -0.0087 -0.0390 767  ASN A OD1 
823  N ND2 . ASN A 111 ? 0.1139 0.2197 0.2662 0.0276  -0.0065 -0.0382 767  ASN A ND2 
824  N N   . LEU A 112 ? 0.1250 0.2647 0.2784 0.0174  -0.0110 -0.0442 768  LEU A N   
825  C CA  . LEU A 112 ? 0.1059 0.2563 0.2600 0.0136  -0.0119 -0.0461 768  LEU A CA  
826  C C   . LEU A 112 ? 0.1789 0.3415 0.3370 0.0169  -0.0127 -0.0467 768  LEU A C   
827  O O   . LEU A 112 ? 0.1772 0.3503 0.3371 0.0170  -0.0141 -0.0482 768  LEU A O   
828  C CB  . LEU A 112 ? 0.0970 0.2462 0.2505 0.0064  -0.0109 -0.0456 768  LEU A CB  
829  C CG  . LEU A 112 ? 0.1495 0.2869 0.2997 0.0023  -0.0099 -0.0461 768  LEU A CG  
830  C CD1 . LEU A 112 ? 0.1503 0.2868 0.3007 -0.0051 -0.0090 -0.0450 768  LEU A CD1 
831  C CD2 . LEU A 112 ? 0.1473 0.2863 0.2950 0.0013  -0.0109 -0.0496 768  LEU A CD2 
832  N N   . LEU A 113 ? 0.1481 0.3095 0.3077 0.0199  -0.0119 -0.0459 769  LEU A N   
833  C CA  . LEU A 113 ? 0.1342 0.3055 0.2975 0.0239  -0.0120 -0.0475 769  LEU A CA  
834  C C   . LEU A 113 ? 0.1817 0.3541 0.3470 0.0302  -0.0134 -0.0480 769  LEU A C   
835  O O   . LEU A 113 ? 0.1719 0.3547 0.3412 0.0333  -0.0139 -0.0495 769  LEU A O   
836  C CB  . LEU A 113 ? 0.1283 0.2970 0.2916 0.0251  -0.0108 -0.0474 769  LEU A CB  
837  C CG  . LEU A 113 ? 0.1698 0.3434 0.3320 0.0196  -0.0096 -0.0467 769  LEU A CG  
838  C CD1 . LEU A 113 ? 0.1756 0.3476 0.3370 0.0211  -0.0089 -0.0468 769  LEU A CD1 
839  C CD2 . LEU A 113 ? 0.1740 0.3629 0.3390 0.0176  -0.0090 -0.0487 769  LEU A CD2 
840  N N   . ASP A 114 ? 0.1296 0.2917 0.2924 0.0324  -0.0139 -0.0464 770  ASP A N   
841  C CA  . ASP A 114 ? 0.1199 0.2825 0.2839 0.0379  -0.0154 -0.0455 770  ASP A CA  
842  C C   . ASP A 114 ? 0.1513 0.3216 0.3143 0.0364  -0.0172 -0.0454 770  ASP A C   
843  O O   . ASP A 114 ? 0.1360 0.3139 0.3019 0.0408  -0.0189 -0.0448 770  ASP A O   
844  C CB  . ASP A 114 ? 0.1404 0.2906 0.3020 0.0402  -0.0150 -0.0433 770  ASP A CB  
845  C CG  . ASP A 114 ? 0.2208 0.3653 0.3847 0.0438  -0.0142 -0.0434 770  ASP A CG  
846  O OD1 . ASP A 114 ? 0.2499 0.3999 0.4175 0.0467  -0.0142 -0.0454 770  ASP A OD1 
847  O OD2 . ASP A 114 ? 0.2445 0.3798 0.4069 0.0436  -0.0134 -0.0418 770  ASP A OD2 
848  N N   . ILE A 115 ? 0.1116 0.2798 0.2706 0.0304  -0.0170 -0.0461 771  ILE A N   
849  C CA  . ILE A 115 ? 0.1000 0.2755 0.2569 0.0271  -0.0188 -0.0470 771  ILE A CA  
850  C C   . ILE A 115 ? 0.1520 0.3438 0.3137 0.0259  -0.0202 -0.0483 771  ILE A C   
851  O O   . ILE A 115 ? 0.1410 0.3430 0.3037 0.0272  -0.0228 -0.0480 771  ILE A O   
852  C CB  . ILE A 115 ? 0.1396 0.3070 0.2913 0.0204  -0.0176 -0.0486 771  ILE A CB  
853  C CG1 . ILE A 115 ? 0.1528 0.3079 0.3000 0.0226  -0.0164 -0.0476 771  ILE A CG1 
854  C CG2 . ILE A 115 ? 0.1429 0.3198 0.2929 0.0148  -0.0194 -0.0511 771  ILE A CG2 
855  C CD1 . ILE A 115 ? 0.1540 0.2979 0.2974 0.0177  -0.0141 -0.0493 771  ILE A CD1 
856  N N   . GLU A 116 ? 0.1263 0.3217 0.2911 0.0236  -0.0186 -0.0494 772  GLU A N   
857  C CA  . GLU A 116 ? 0.1349 0.3468 0.3051 0.0223  -0.0190 -0.0507 772  GLU A CA  
858  C C   . GLU A 116 ? 0.2003 0.4211 0.3762 0.0309  -0.0202 -0.0502 772  GLU A C   
859  O O   . GLU A 116 ? 0.1807 0.4169 0.3611 0.0314  -0.0220 -0.0506 772  GLU A O   
860  C CB  . GLU A 116 ? 0.1564 0.3684 0.3275 0.0185  -0.0164 -0.0514 772  GLU A CB  
861  C CG  . GLU A 116 ? 0.2981 0.5275 0.4739 0.0148  -0.0160 -0.0528 772  GLU A CG  
862  C CD  . GLU A 116 ? 0.5779 0.8209 0.7607 0.0217  -0.0156 -0.0540 772  GLU A CD  
863  O OE1 . GLU A 116 ? 0.4111 0.6478 0.5944 0.0279  -0.0143 -0.0544 772  GLU A OE1 
864  O OE2 . GLU A 116 ? 0.4593 0.7195 0.6474 0.0208  -0.0165 -0.0550 772  GLU A OE2 
865  N N   . VAL A 117 ? 0.1600 0.3712 0.3364 0.0376  -0.0194 -0.0492 773  VAL A N   
866  C CA  . VAL A 117 ? 0.1506 0.3669 0.3326 0.0463  -0.0202 -0.0486 773  VAL A CA  
867  C C   . VAL A 117 ? 0.1795 0.3999 0.3614 0.0493  -0.0235 -0.0456 773  VAL A C   
868  O O   . VAL A 117 ? 0.1503 0.3843 0.3383 0.0538  -0.0253 -0.0449 773  VAL A O   
869  C CB  . VAL A 117 ? 0.2063 0.4096 0.3885 0.0515  -0.0184 -0.0488 773  VAL A CB  
870  C CG1 . VAL A 117 ? 0.1975 0.4032 0.3855 0.0606  -0.0192 -0.0479 773  VAL A CG1 
871  C CG2 . VAL A 117 ? 0.2062 0.4097 0.3887 0.0489  -0.0155 -0.0520 773  VAL A CG2 
872  N N   . ALA A 118 ? 0.1221 0.3322 0.2972 0.0468  -0.0243 -0.0437 774  ALA A N   
873  C CA  . ALA A 118 ? 0.1172 0.3304 0.2897 0.0483  -0.0274 -0.0407 774  ALA A CA  
874  C C   . ALA A 118 ? 0.1915 0.4227 0.3657 0.0445  -0.0301 -0.0416 774  ALA A C   
875  O O   . ALA A 118 ? 0.1778 0.4205 0.3554 0.0491  -0.0333 -0.0388 774  ALA A O   
876  C CB  . ALA A 118 ? 0.1308 0.3309 0.2948 0.0442  -0.0266 -0.0401 774  ALA A CB  
877  N N   . TYR A 119 ? 0.1606 0.3943 0.3327 0.0359  -0.0291 -0.0451 775  TYR A N   
878  C CA  . TYR A 119 ? 0.1877 0.4379 0.3610 0.0302  -0.0315 -0.0467 775  TYR A CA  
879  C C   . TYR A 119 ? 0.2004 0.4691 0.3836 0.0336  -0.0322 -0.0468 775  TYR A C   
880  O O   . TYR A 119 ? 0.1832 0.4686 0.3697 0.0337  -0.0356 -0.0459 775  TYR A O   
881  C CB  . TYR A 119 ? 0.2317 0.4767 0.3999 0.0195  -0.0299 -0.0503 775  TYR A CB  
882  C CG  . TYR A 119 ? 0.2795 0.5376 0.4463 0.0122  -0.0328 -0.0524 775  TYR A CG  
883  C CD1 . TYR A 119 ? 0.3207 0.5783 0.4809 0.0109  -0.0353 -0.0523 775  TYR A CD1 
884  C CD2 . TYR A 119 ? 0.2874 0.5598 0.4592 0.0061  -0.0330 -0.0545 775  TYR A CD2 
885  C CE1 . TYR A 119 ? 0.3335 0.6044 0.4920 0.0035  -0.0383 -0.0548 775  TYR A CE1 
886  C CE2 . TYR A 119 ? 0.2989 0.5841 0.4697 -0.0016 -0.0359 -0.0567 775  TYR A CE2 
887  C CZ  . TYR A 119 ? 0.4059 0.6903 0.5698 -0.0029 -0.0387 -0.0572 775  TYR A CZ  
888  O OH  . TYR A 119 ? 0.4187 0.7161 0.5809 -0.0115 -0.0418 -0.0602 775  TYR A OH  
889  N N   . SER A 120 ? 0.1353 0.4017 0.3232 0.0369  -0.0291 -0.0479 776  SER A N   
890  C CA  . SER A 120 ? 0.1272 0.4101 0.3249 0.0413  -0.0285 -0.0488 776  SER A CA  
891  C C   . SER A 120 ? 0.1544 0.4445 0.3582 0.0521  -0.0312 -0.0455 776  SER A C   
892  O O   . SER A 120 ? 0.1174 0.4271 0.3292 0.0548  -0.0331 -0.0450 776  SER A O   
893  C CB  . SER A 120 ? 0.1884 0.4638 0.3874 0.0429  -0.0242 -0.0511 776  SER A CB  
894  O OG  . SER A 120 ? 0.3402 0.6297 0.5482 0.0484  -0.0228 -0.0527 776  SER A OG  
895  N N   . LEU A 121 ? 0.1381 0.4125 0.3386 0.0580  -0.0314 -0.0427 777  LEU A N   
896  C CA  . LEU A 121 ? 0.1437 0.4195 0.3489 0.0684  -0.0337 -0.0383 777  LEU A CA  
897  C C   . LEU A 121 ? 0.1830 0.4732 0.3879 0.0677  -0.0387 -0.0345 777  LEU A C   
898  O O   . LEU A 121 ? 0.1607 0.4679 0.3742 0.0737  -0.0412 -0.0322 777  LEU A O   
899  C CB  . LEU A 121 ? 0.1542 0.4073 0.3535 0.0713  -0.0324 -0.0362 777  LEU A CB  
900  C CG  . LEU A 121 ? 0.2262 0.4707 0.4309 0.0818  -0.0314 -0.0341 777  LEU A CG  
901  C CD1 . LEU A 121 ? 0.2314 0.4830 0.4451 0.0866  -0.0287 -0.0385 777  LEU A CD1 
902  C CD2 . LEU A 121 ? 0.2325 0.4547 0.4307 0.0811  -0.0294 -0.0335 777  LEU A CD2 
903  N N   . LEU A 122 ? 0.1409 0.4263 0.3362 0.0597  -0.0400 -0.0346 778  LEU A N   
904  C CA  . LEU A 122 ? 0.1591 0.4573 0.3512 0.0564  -0.0447 -0.0322 778  LEU A CA  
905  C C   . LEU A 122 ? 0.2266 0.5493 0.4252 0.0519  -0.0470 -0.0345 778  LEU A C   
906  O O   . LEU A 122 ? 0.2236 0.5638 0.4261 0.0549  -0.0515 -0.0310 778  LEU A O   
907  C CB  . LEU A 122 ? 0.1806 0.4654 0.3604 0.0478  -0.0440 -0.0341 778  LEU A CB  
908  C CG  . LEU A 122 ? 0.2465 0.5354 0.4189 0.0465  -0.0479 -0.0308 778  LEU A CG  
909  C CD1 . LEU A 122 ? 0.2400 0.5234 0.4129 0.0564  -0.0494 -0.0236 778  LEU A CD1 
910  C CD2 . LEU A 122 ? 0.2765 0.5518 0.4378 0.0382  -0.0459 -0.0344 778  LEU A CD2 
911  N N   . ARG A 123 ? 0.1911 0.5159 0.3913 0.0448  -0.0439 -0.0397 779  ARG A N   
912  C CA  . ARG A 123 ? 0.1765 0.5239 0.3829 0.0389  -0.0453 -0.0421 779  ARG A CA  
913  C C   . ARG A 123 ? 0.2309 0.5947 0.4507 0.0467  -0.0443 -0.0417 779  ARG A C   
914  O O   . ARG A 123 ? 0.1930 0.5801 0.4203 0.0439  -0.0461 -0.0426 779  ARG A O   
915  C CB  . ARG A 123 ? 0.2035 0.5453 0.4045 0.0262  -0.0427 -0.0472 779  ARG A CB  
916  C CG  . ARG A 123 ? 0.3546 0.6892 0.5446 0.0169  -0.0447 -0.0489 779  ARG A CG  
917  C CD  . ARG A 123 ? 0.5689 0.9225 0.7590 0.0153  -0.0504 -0.0474 779  ARG A CD  
918  N NE  . ARG A 123 ? 0.7396 1.0851 0.9179 0.0074  -0.0520 -0.0496 779  ARG A NE  
919  C CZ  . ARG A 123 ? 0.9812 1.3139 1.1512 0.0112  -0.0526 -0.0474 779  ARG A CZ  
920  N NH1 . ARG A 123 ? 0.8844 1.2085 1.0565 0.0221  -0.0517 -0.0424 779  ARG A NH1 
921  N NH2 . ARG A 123 ? 0.8144 1.1421 0.9739 0.0035  -0.0536 -0.0505 779  ARG A NH2 
922  N N   . GLY A 124 ? 0.1802 0.5325 0.4032 0.0566  -0.0415 -0.0407 780  GLY A N   
923  C CA  . GLY A 124 ? 0.1747 0.5397 0.4101 0.0661  -0.0400 -0.0408 780  GLY A CA  
924  C C   . GLY A 124 ? 0.2311 0.6039 0.4728 0.0774  -0.0442 -0.0349 780  GLY A C   
925  O O   . GLY A 124 ? 0.2639 0.6333 0.4994 0.0768  -0.0483 -0.0305 780  GLY A O   
926  N N   . GLY A 125 ? 0.1309 0.5144 0.3847 0.0878  -0.0431 -0.0345 781  GLY A N   
927  C CA  . GLY A 125 ? 0.1323 0.5223 0.3927 0.0992  -0.0473 -0.0278 781  GLY A CA  
928  C C   . GLY A 125 ? 0.1798 0.5973 0.4460 0.0985  -0.0532 -0.0238 781  GLY A C   
929  O O   . GLY A 125 ? 0.1685 0.6053 0.4371 0.0898  -0.0538 -0.0272 781  GLY A O   
930  N N   . SER A 126 ? 0.1437 0.5629 0.4123 0.1076  -0.0578 -0.0161 782  SER A N   
931  C CA  . SER A 126 ? 0.1315 0.5771 0.4069 0.1103  -0.0642 -0.0105 782  SER A CA  
932  C C   . SER A 126 ? 0.2210 0.6655 0.4845 0.1043  -0.0700 -0.0053 782  SER A C   
933  O O   . SER A 126 ? 0.2185 0.6396 0.4708 0.1037  -0.0693 -0.0033 782  SER A O   
934  C CB  . SER A 126 ? 0.1626 0.6138 0.4519 0.1273  -0.0652 -0.0045 782  SER A CB  
935  O OG  . SER A 126 ? 0.2642 0.7192 0.5651 0.1335  -0.0596 -0.0101 782  SER A OG  
936  N N   . ASP A 127 ? 0.1851 0.6568 0.4515 0.1000  -0.0758 -0.0032 783  ASP A N   
937  C CA  . ASP A 127 ? 0.2126 0.6896 0.4687 0.0946  -0.0820 0.0015  783  ASP A CA  
938  C C   . ASP A 127 ? 0.2431 0.7395 0.5081 0.1062  -0.0887 0.0120  783  ASP A C   
939  O O   . ASP A 127 ? 0.2200 0.7431 0.4992 0.1108  -0.0912 0.0134  783  ASP A O   
940  C CB  . ASP A 127 ? 0.2537 0.7457 0.5037 0.0784  -0.0840 -0.0047 783  ASP A CB  
941  C CG  . ASP A 127 ? 0.4878 0.9758 0.7221 0.0698  -0.0882 -0.0032 783  ASP A CG  
942  O OD1 . ASP A 127 ? 0.5458 1.0074 0.7679 0.0677  -0.0850 -0.0043 783  ASP A OD1 
943  O OD2 . ASP A 127 ? 0.5609 1.0736 0.7953 0.0651  -0.0945 -0.0013 783  ASP A OD2 
944  N N   . ASP A 128 ? 0.2243 0.7073 0.4812 0.1109  -0.0913 0.0197  784  ASP A N   
945  C CA  . ASP A 128 ? 0.2242 0.7207 0.4871 0.1222  -0.0977 0.0315  784  ASP A CA  
946  C C   . ASP A 128 ? 0.3002 0.7910 0.5467 0.1163  -0.1020 0.0369  784  ASP A C   
947  O O   . ASP A 128 ? 0.3038 0.7677 0.5402 0.1168  -0.0988 0.0383  784  ASP A O   
948  C CB  . ASP A 128 ? 0.2513 0.7311 0.5246 0.1385  -0.0944 0.0366  784  ASP A CB  
949  C CG  . ASP A 128 ? 0.3401 0.8313 0.6231 0.1530  -0.1001 0.0495  784  ASP A CG  
950  O OD1 . ASP A 128 ? 0.3161 0.8304 0.5973 0.1510  -0.1076 0.0561  784  ASP A OD1 
951  O OD2 . ASP A 128 ? 0.4480 0.9247 0.7402 0.1663  -0.0972 0.0530  784  ASP A OD2 
952  N N   . SER A 129 ? 0.2899 0.8072 0.5333 0.1102  -0.1091 0.0395  785  SER A N   
953  C CA  . SER A 129 ? 0.3122 0.8297 0.5393 0.1036  -0.1138 0.0440  785  SER A CA  
954  C C   . SER A 129 ? 0.3625 0.8687 0.5878 0.1155  -0.1160 0.0571  785  SER A C   
955  O O   . SER A 129 ? 0.3864 0.8757 0.5964 0.1111  -0.1152 0.0590  785  SER A O   
956  C CB  . SER A 129 ? 0.3808 0.9333 0.6078 0.0966  -0.1218 0.0451  785  SER A CB  
957  O OG  . SER A 129 ? 0.5563 1.1215 0.7860 0.0849  -0.1204 0.0338  785  SER A OG  
958  N N   . SER A 130 ? 0.2985 0.8136 0.5399 0.1307  -0.1184 0.0661  786  SER A N   
959  C CA  . SER A 130 ? 0.2880 0.7936 0.5310 0.1437  -0.1209 0.0801  786  SER A CA  
960  C C   . SER A 130 ? 0.3254 0.7933 0.5619 0.1466  -0.1141 0.0801  786  SER A C   
961  O O   . SER A 130 ? 0.3251 0.7817 0.5573 0.1531  -0.1160 0.0914  786  SER A O   
962  C CB  . SER A 130 ? 0.3054 0.8275 0.5693 0.1596  -0.1239 0.0877  786  SER A CB  
963  O OG  . SER A 130 ? 0.4078 0.9128 0.6836 0.1674  -0.1166 0.0818  786  SER A OG  
964  N N   . LYS A 131 ? 0.2676 0.7167 0.5033 0.1414  -0.1064 0.0680  787  LYS A N   
965  C CA  . LYS A 131 ? 0.2576 0.6722 0.4877 0.1426  -0.0997 0.0663  787  LYS A CA  
966  C C   . LYS A 131 ? 0.2827 0.6835 0.4942 0.1287  -0.0970 0.0603  787  LYS A C   
967  O O   . LYS A 131 ? 0.2648 0.6752 0.4711 0.1172  -0.0964 0.0507  787  LYS A O   
968  C CB  . LYS A 131 ? 0.2795 0.6818 0.5214 0.1474  -0.0929 0.0578  787  LYS A CB  
969  C CG  . LYS A 131 ? 0.5011 0.9119 0.7618 0.1634  -0.0942 0.0636  787  LYS A CG  
970  C CD  . LYS A 131 ? 0.6048 0.9990 0.8753 0.1689  -0.0867 0.0553  787  LYS A CD  
971  C CE  . LYS A 131 ? 0.7065 1.1026 0.9942 0.1861  -0.0872 0.0618  787  LYS A CE  
972  N NZ  . LYS A 131 ? 0.7694 1.1506 1.0662 0.1915  -0.0798 0.0527  787  LYS A NZ  
973  N N   . ASP A 132 ? 0.2305 0.6091 0.4326 0.1297  -0.0951 0.0659  788  ASP A N   
974  C CA  . ASP A 132 ? 0.2328 0.5970 0.4182 0.1180  -0.0918 0.0608  788  ASP A CA  
975  C C   . ASP A 132 ? 0.2668 0.6165 0.4535 0.1122  -0.0848 0.0476  788  ASP A C   
976  O O   . ASP A 132 ? 0.2607 0.5953 0.4564 0.1192  -0.0807 0.0463  788  ASP A O   
977  C CB  . ASP A 132 ? 0.2683 0.6110 0.4471 0.1222  -0.0904 0.0702  788  ASP A CB  
978  C CG  . ASP A 132 ? 0.2960 0.6269 0.4575 0.1116  -0.0875 0.0674  788  ASP A CG  
979  O OD1 . ASP A 132 ? 0.2865 0.6109 0.4432 0.1026  -0.0831 0.0558  788  ASP A OD1 
980  O OD2 . ASP A 132 ? 0.3798 0.7079 0.5328 0.1125  -0.0895 0.0773  788  ASP A OD2 
981  N N   . PRO A 133 ? 0.2401 0.5939 0.4180 0.0996  -0.0834 0.0377  789  PRO A N   
982  C CA  . PRO A 133 ? 0.2321 0.5720 0.4110 0.0942  -0.0770 0.0264  789  PRO A CA  
983  C C   . PRO A 133 ? 0.2562 0.5673 0.4323 0.0962  -0.0711 0.0258  789  PRO A C   
984  O O   . PRO A 133 ? 0.2372 0.5377 0.4182 0.0957  -0.0664 0.0188  789  PRO A O   
985  C CB  . PRO A 133 ? 0.2558 0.6028 0.4235 0.0805  -0.0772 0.0183  789  PRO A CB  
986  C CG  . PRO A 133 ? 0.3142 0.6858 0.4789 0.0790  -0.0844 0.0235  789  PRO A CG  
987  C CD  . PRO A 133 ? 0.2622 0.6328 0.4285 0.0897  -0.0876 0.0364  789  PRO A CD  
988  N N   . ILE A 134 ? 0.2329 0.5329 0.4014 0.0981  -0.0715 0.0335  790  ILE A N   
989  C CA  . ILE A 134 ? 0.2335 0.5076 0.3997 0.0999  -0.0664 0.0345  790  ILE A CA  
990  C C   . ILE A 134 ? 0.2863 0.5516 0.4661 0.1112  -0.0651 0.0373  790  ILE A C   
991  O O   . ILE A 134 ? 0.2931 0.5418 0.4759 0.1112  -0.0601 0.0316  790  ILE A O   
992  C CB  . ILE A 134 ? 0.2724 0.5405 0.4271 0.0987  -0.0675 0.0430  790  ILE A CB  
993  C CG1 . ILE A 134 ? 0.2822 0.5573 0.4229 0.0872  -0.0675 0.0377  790  ILE A CG1 
994  C CG2 . ILE A 134 ? 0.2804 0.5231 0.4348 0.1012  -0.0627 0.0454  790  ILE A CG2 
995  C CD1 . ILE A 134 ? 0.3564 0.6373 0.4851 0.0852  -0.0704 0.0460  790  ILE A CD1 
996  N N   . ASP A 135 ? 0.2308 0.5081 0.4192 0.1207  -0.0697 0.0456  791  ASP A N   
997  C CA  . ASP A 135 ? 0.2376 0.5087 0.4400 0.1324  -0.0687 0.0480  791  ASP A CA  
998  C C   . ASP A 135 ? 0.2739 0.5504 0.4856 0.1321  -0.0656 0.0370  791  ASP A C   
999  O O   . ASP A 135 ? 0.2752 0.5357 0.4926 0.1360  -0.0609 0.0327  791  ASP A O   
1000 C CB  . ASP A 135 ? 0.2574 0.5441 0.4674 0.1426  -0.0749 0.0596  791  ASP A CB  
1001 C CG  . ASP A 135 ? 0.4084 0.6830 0.6137 0.1472  -0.0768 0.0724  791  ASP A CG  
1002 O OD1 . ASP A 135 ? 0.4290 0.6801 0.6284 0.1446  -0.0725 0.0722  791  ASP A OD1 
1003 O OD2 . ASP A 135 ? 0.4557 0.7448 0.6637 0.1535  -0.0827 0.0833  791  ASP A OD2 
1004 N N   . VAL A 136 ? 0.1899 0.4890 0.4019 0.1265  -0.0679 0.0322  792  VAL A N   
1005 C CA  . VAL A 136 ? 0.1740 0.4821 0.3935 0.1242  -0.0653 0.0224  792  VAL A CA  
1006 C C   . VAL A 136 ? 0.2599 0.5476 0.4735 0.1172  -0.0590 0.0136  792  VAL A C   
1007 O O   . VAL A 136 ? 0.2705 0.5492 0.4911 0.1213  -0.0549 0.0090  792  VAL A O   
1008 C CB  . VAL A 136 ? 0.2035 0.5378 0.4216 0.1164  -0.0692 0.0196  792  VAL A CB  
1009 C CG1 . VAL A 136 ? 0.1939 0.5362 0.4183 0.1120  -0.0658 0.0095  792  VAL A CG1 
1010 C CG2 . VAL A 136 ? 0.1906 0.5481 0.4158 0.1236  -0.0759 0.0284  792  VAL A CG2 
1011 N N   . ASN A 137 ? 0.2201 0.5003 0.4206 0.1071  -0.0582 0.0117  793  ASN A N   
1012 C CA  . ASN A 137 ? 0.2206 0.4834 0.4155 0.1003  -0.0529 0.0043  793  ASN A CA  
1013 C C   . ASN A 137 ? 0.2916 0.5310 0.4874 0.1055  -0.0493 0.0060  793  ASN A C   
1014 O O   . ASN A 137 ? 0.3120 0.5402 0.5082 0.1028  -0.0449 -0.0006 793  ASN A O   
1015 C CB  . ASN A 137 ? 0.2113 0.4730 0.3933 0.0893  -0.0530 0.0018  793  ASN A CB  
1016 C CG  . ASN A 137 ? 0.4548 0.7362 0.6359 0.0819  -0.0553 -0.0030 793  ASN A CG  
1017 O OD1 . ASN A 137 ? 0.4140 0.7084 0.6040 0.0827  -0.0554 -0.0064 793  ASN A OD1 
1018 N ND2 . ASN A 137 ? 0.3738 0.6579 0.5440 0.0738  -0.0568 -0.0037 793  ASN A ND2 
1019 N N   . TYR A 138 ? 0.2424 0.4752 0.4391 0.1126  -0.0512 0.0149  794  TYR A N   
1020 C CA  . TYR A 138 ? 0.2490 0.4593 0.4473 0.1171  -0.0479 0.0166  794  TYR A CA  
1021 C C   . TYR A 138 ? 0.2791 0.4865 0.4893 0.1243  -0.0453 0.0117  794  TYR A C   
1022 O O   . TYR A 138 ? 0.2665 0.4580 0.4767 0.1230  -0.0410 0.0064  794  TYR A O   
1023 C CB  . TYR A 138 ? 0.2551 0.4590 0.4517 0.1228  -0.0507 0.0283  794  TYR A CB  
1024 C CG  . TYR A 138 ? 0.2678 0.4488 0.4680 0.1280  -0.0477 0.0309  794  TYR A CG  
1025 C CD1 . TYR A 138 ? 0.3049 0.4681 0.4976 0.1219  -0.0444 0.0300  794  TYR A CD1 
1026 C CD2 . TYR A 138 ? 0.2715 0.4489 0.4830 0.1392  -0.0483 0.0345  794  TYR A CD2 
1027 C CE1 . TYR A 138 ? 0.3074 0.4499 0.5034 0.1255  -0.0418 0.0322  794  TYR A CE1 
1028 C CE2 . TYR A 138 ? 0.2915 0.4463 0.5062 0.1433  -0.0454 0.0363  794  TYR A CE2 
1029 C CZ  . TYR A 138 ? 0.3773 0.5148 0.5840 0.1359  -0.0423 0.0352  794  TYR A CZ  
1030 O OH  . TYR A 138 ? 0.4468 0.5622 0.6565 0.1389  -0.0397 0.0368  794  TYR A OH  
1031 N N   . GLU A 139 ? 0.2275 0.4517 0.4477 0.1318  -0.0478 0.0131  795  GLU A N   
1032 C CA  . GLU A 139 ? 0.2156 0.4399 0.4480 0.1398  -0.0451 0.0083  795  GLU A CA  
1033 C C   . GLU A 139 ? 0.2486 0.4754 0.4808 0.1334  -0.0410 -0.0029 795  GLU A C   
1034 O O   . GLU A 139 ? 0.2149 0.4338 0.4531 0.1375  -0.0370 -0.0086 795  GLU A O   
1035 C CB  . GLU A 139 ? 0.2233 0.4680 0.4670 0.1491  -0.0488 0.0127  795  GLU A CB  
1036 C CG  . GLU A 139 ? 0.4078 0.6515 0.6529 0.1569  -0.0534 0.0252  795  GLU A CG  
1037 C CD  . GLU A 139 ? 0.6830 0.9483 0.9412 0.1672  -0.0570 0.0292  795  GLU A CD  
1038 O OE1 . GLU A 139 ? 0.6783 0.9548 0.9360 0.1702  -0.0627 0.0394  795  GLU A OE1 
1039 O OE2 . GLU A 139 ? 0.5663 0.8389 0.8353 0.1722  -0.0542 0.0224  795  GLU A OE2 
1040 N N   . LYS A 140 ? 0.2108 0.4477 0.4356 0.1229  -0.0416 -0.0061 796  LYS A N   
1041 C CA  . LYS A 140 ? 0.1953 0.4354 0.4188 0.1156  -0.0381 -0.0154 796  LYS A CA  
1042 C C   . LYS A 140 ? 0.2596 0.4784 0.4785 0.1126  -0.0337 -0.0198 796  LYS A C   
1043 O O   . LYS A 140 ? 0.2848 0.5040 0.5057 0.1105  -0.0302 -0.0269 796  LYS A O   
1044 C CB  . LYS A 140 ? 0.2056 0.4571 0.4213 0.1048  -0.0400 -0.0167 796  LYS A CB  
1045 C CG  . LYS A 140 ? 0.2778 0.5522 0.4972 0.1058  -0.0448 -0.0130 796  LYS A CG  
1046 C CD  . LYS A 140 ? 0.3071 0.5962 0.5235 0.0953  -0.0452 -0.0181 796  LYS A CD  
1047 C CE  . LYS A 140 ? 0.2417 0.5555 0.4623 0.0954  -0.0503 -0.0150 796  LYS A CE  
1048 N NZ  . LYS A 140 ? 0.3292 0.6560 0.5633 0.1073  -0.0518 -0.0116 796  LYS A NZ  
1049 N N   . LEU A 141 ? 0.2131 0.4147 0.4257 0.1119  -0.0339 -0.0153 797  LEU A N   
1050 C CA  . LEU A 141 ? 0.2240 0.4059 0.4319 0.1084  -0.0304 -0.0184 797  LEU A CA  
1051 C C   . LEU A 141 ? 0.3009 0.4709 0.5155 0.1150  -0.0274 -0.0215 797  LEU A C   
1052 O O   . LEU A 141 ? 0.3058 0.4636 0.5173 0.1110  -0.0243 -0.0265 797  LEU A O   
1053 C CB  . LEU A 141 ? 0.2319 0.4017 0.4315 0.1052  -0.0315 -0.0121 797  LEU A CB  
1054 C CG  . LEU A 141 ? 0.2991 0.4773 0.4900 0.0973  -0.0333 -0.0108 797  LEU A CG  
1055 C CD1 . LEU A 141 ? 0.3045 0.4715 0.4878 0.0952  -0.0338 -0.0048 797  LEU A CD1 
1056 C CD2 . LEU A 141 ? 0.3429 0.5229 0.5301 0.0889  -0.0309 -0.0184 797  LEU A CD2 
1057 N N   . LYS A 142 ? 0.2432 0.4164 0.4671 0.1254  -0.0285 -0.0186 798  LYS A N   
1058 C CA  . LYS A 142 ? 0.2414 0.4022 0.4726 0.1330  -0.0256 -0.0219 798  LYS A CA  
1059 C C   . LYS A 142 ? 0.3052 0.4419 0.5309 0.1299  -0.0237 -0.0213 798  LYS A C   
1060 O O   . LYS A 142 ? 0.3055 0.4314 0.5321 0.1291  -0.0202 -0.0284 798  LYS A O   
1061 C CB  . LYS A 142 ? 0.2623 0.4320 0.4985 0.1335  -0.0220 -0.0321 798  LYS A CB  
1062 C CG  . LYS A 142 ? 0.3877 0.5825 0.6303 0.1362  -0.0236 -0.0323 798  LYS A CG  
1063 C CD  . LYS A 142 ? 0.4394 0.6455 0.6834 0.1324  -0.0201 -0.0415 798  LYS A CD  
1064 C CE  . LYS A 142 ? 0.2826 0.5146 0.5331 0.1338  -0.0219 -0.0410 798  LYS A CE  
1065 N NZ  . LYS A 142 ? 0.3392 0.5833 0.5941 0.1330  -0.0176 -0.0498 798  LYS A NZ  
1066 N N   . THR A 143 ? 0.2622 0.3924 0.4818 0.1272  -0.0262 -0.0129 799  THR A N   
1067 C CA  . THR A 143 ? 0.2608 0.3712 0.4750 0.1233  -0.0250 -0.0102 799  THR A CA  
1068 C C   . THR A 143 ? 0.3155 0.4192 0.5305 0.1287  -0.0278 0.0011  799  THR A C   
1069 O O   . THR A 143 ? 0.3134 0.4301 0.5267 0.1298  -0.0314 0.0078  799  THR A O   
1070 C CB  . THR A 143 ? 0.2778 0.3897 0.4818 0.1121  -0.0246 -0.0116 799  THR A CB  
1071 O OG1 . THR A 143 ? 0.2690 0.3867 0.4726 0.1077  -0.0223 -0.0207 799  THR A OG1 
1072 C CG2 . THR A 143 ? 0.2397 0.3340 0.4386 0.1074  -0.0232 -0.0088 799  THR A CG2 
1073 N N   . ASP A 144 ? 0.2802 0.3640 0.4977 0.1315  -0.0262 0.0033  800  ASP A N   
1074 C CA  . ASP A 144 ? 0.2824 0.3569 0.4998 0.1355  -0.0285 0.0150  800  ASP A CA  
1075 C C   . ASP A 144 ? 0.3332 0.4030 0.5401 0.1255  -0.0283 0.0187  800  ASP A C   
1076 O O   . ASP A 144 ? 0.3335 0.3932 0.5375 0.1189  -0.0253 0.0131  800  ASP A O   
1077 C CB  . ASP A 144 ? 0.3145 0.3678 0.5394 0.1420  -0.0265 0.0154  800  ASP A CB  
1078 C CG  . ASP A 144 ? 0.5104 0.5509 0.7351 0.1452  -0.0284 0.0284  800  ASP A CG  
1079 O OD1 . ASP A 144 ? 0.5443 0.5954 0.7703 0.1511  -0.0322 0.0379  800  ASP A OD1 
1080 O OD2 . ASP A 144 ? 0.5922 0.6126 0.8157 0.1418  -0.0262 0.0294  800  ASP A OD2 
1081 N N   . ILE A 145 ? 0.2818 0.3616 0.4827 0.1241  -0.0314 0.0272  801  ILE A N   
1082 C CA  . ILE A 145 ? 0.2846 0.3624 0.4755 0.1153  -0.0308 0.0307  801  ILE A CA  
1083 C C   . ILE A 145 ? 0.3552 0.4257 0.5442 0.1180  -0.0327 0.0436  801  ILE A C   
1084 O O   . ILE A 145 ? 0.3568 0.4377 0.5464 0.1235  -0.0364 0.0512  801  ILE A O   
1085 C CB  . ILE A 145 ? 0.3232 0.4196 0.5067 0.1094  -0.0320 0.0278  801  ILE A CB  
1086 C CG1 . ILE A 145 ? 0.3310 0.4348 0.5169 0.1069  -0.0303 0.0161  801  ILE A CG1 
1087 C CG2 . ILE A 145 ? 0.3335 0.4271 0.5069 0.1009  -0.0306 0.0305  801  ILE A CG2 
1088 C CD1 . ILE A 145 ? 0.4122 0.5350 0.5936 0.1031  -0.0321 0.0133  801  ILE A CD1 
1089 N N   . LYS A 146 ? 0.3035 0.3567 0.4906 0.1141  -0.0302 0.0464  802  LYS A N   
1090 C CA  . LYS A 146 ? 0.3050 0.3495 0.4897 0.1153  -0.0314 0.0595  802  LYS A CA  
1091 C C   . LYS A 146 ? 0.3661 0.4099 0.5410 0.1054  -0.0294 0.0620  802  LYS A C   
1092 O O   . LYS A 146 ? 0.3461 0.3883 0.5192 0.0987  -0.0264 0.0535  802  LYS A O   
1093 C CB  . LYS A 146 ? 0.3329 0.3554 0.5260 0.1204  -0.0301 0.0621  802  LYS A CB  
1094 C CG  . LYS A 146 ? 0.5243 0.5483 0.7275 0.1321  -0.0321 0.0618  802  LYS A CG  
1095 C CD  . LYS A 146 ? 0.6451 0.6477 0.8559 0.1389  -0.0317 0.0685  802  LYS A CD  
1096 C CE  . LYS A 146 ? 0.6148 0.6220 0.8361 0.1517  -0.0340 0.0692  802  LYS A CE  
1097 N NZ  . LYS A 146 ? 0.7536 0.7387 0.9829 0.1595  -0.0336 0.0764  802  LYS A NZ  
1098 N N   . VAL A 147 ? 0.3423 0.3888 0.5109 0.1046  -0.0311 0.0738  803  VAL A N   
1099 C CA  . VAL A 147 ? 0.3508 0.3982 0.5100 0.0958  -0.0288 0.0772  803  VAL A CA  
1100 C C   . VAL A 147 ? 0.4192 0.4460 0.5812 0.0929  -0.0259 0.0818  803  VAL A C   
1101 O O   . VAL A 147 ? 0.4381 0.4529 0.6046 0.0981  -0.0272 0.0905  803  VAL A O   
1102 C CB  . VAL A 147 ? 0.3965 0.4586 0.5464 0.0955  -0.0316 0.0873  803  VAL A CB  
1103 C CG1 . VAL A 147 ? 0.3964 0.4626 0.5361 0.0861  -0.0284 0.0878  803  VAL A CG1 
1104 C CG2 . VAL A 147 ? 0.3856 0.4672 0.5342 0.0989  -0.0352 0.0832  803  VAL A CG2 
1105 N N   . VAL A 148 ? 0.3661 0.3888 0.5262 0.0847  -0.0220 0.0761  804  VAL A N   
1106 C CA  . VAL A 148 ? 0.3727 0.3775 0.5353 0.0801  -0.0191 0.0798  804  VAL A CA  
1107 C C   . VAL A 148 ? 0.4939 0.5006 0.6487 0.0760  -0.0186 0.0928  804  VAL A C   
1108 O O   . VAL A 148 ? 0.4852 0.5071 0.6316 0.0717  -0.0178 0.0930  804  VAL A O   
1109 C CB  . VAL A 148 ? 0.4015 0.4026 0.5663 0.0730  -0.0156 0.0685  804  VAL A CB  
1110 C CG1 . VAL A 148 ? 0.4005 0.3871 0.5668 0.0662  -0.0126 0.0730  804  VAL A CG1 
1111 C CG2 . VAL A 148 ? 0.3900 0.3868 0.5625 0.0771  -0.0160 0.0573  804  VAL A CG2 
1112 N N   . ASP A 149 ? 0.5076 0.4988 0.6652 0.0774  -0.0189 0.1036  805  ASP A N   
1113 C CA  . ASP A 149 ? 0.5366 0.5277 0.6874 0.0734  -0.0182 0.1174  805  ASP A CA  
1114 C C   . ASP A 149 ? 0.6111 0.6046 0.7578 0.0626  -0.0135 0.1147  805  ASP A C   
1115 O O   . ASP A 149 ? 0.6043 0.5870 0.7569 0.0581  -0.0108 0.1077  805  ASP A O   
1116 C CB  . ASP A 149 ? 0.5778 0.5481 0.7343 0.0769  -0.0191 0.1288  805  ASP A CB  
1117 C CG  . ASP A 149 ? 0.8096 0.7786 0.9592 0.0730  -0.0188 0.1452  805  ASP A CG  
1118 O OD1 . ASP A 149 ? 0.8255 0.8132 0.9650 0.0717  -0.0197 0.1503  805  ASP A OD1 
1119 O OD2 . ASP A 149 ? 0.9205 0.8698 1.0743 0.0711  -0.0175 0.1530  805  ASP A OD2 
1120 N N   . ARG A 150 ? 0.5848 0.5938 0.7213 0.0586  -0.0126 0.1198  806  ARG A N   
1121 C CA  . ARG A 150 ? 0.5895 0.6054 0.7214 0.0493  -0.0078 0.1178  806  ARG A CA  
1122 C C   . ARG A 150 ? 0.6658 0.6664 0.8023 0.0423  -0.0044 0.1226  806  ARG A C   
1123 O O   . ARG A 150 ? 0.6575 0.6602 0.7959 0.0355  -0.0007 0.1159  806  ARG A O   
1124 C CB  . ARG A 150 ? 0.5864 0.6198 0.7060 0.0472  -0.0074 0.1251  806  ARG A CB  
1125 C CG  . ARG A 150 ? 0.7038 0.7543 0.8181 0.0437  -0.0047 0.1145  806  ARG A CG  
1126 C CD  . ARG A 150 ? 0.7990 0.8631 0.9020 0.0383  -0.0017 0.1210  806  ARG A CD  
1127 N NE  . ARG A 150 ? 0.8752 0.9370 0.9799 0.0303  0.0040  0.1213  806  ARG A NE  
1128 C CZ  . ARG A 150 ? 0.9580 1.0276 1.0638 0.0264  0.0081  0.1110  806  ARG A CZ  
1129 N NH1 . ARG A 150 ? 0.7381 0.8161 0.8432 0.0296  0.0072  0.0994  806  ARG A NH1 
1130 N NH2 . ARG A 150 ? 0.6840 0.7528 0.7924 0.0194  0.0130  0.1125  806  ARG A NH2 
1131 N N   . ASP A 151 ? 0.6413 0.6270 0.7799 0.0439  -0.0057 0.1345  807  ASP A N   
1132 C CA  . ASP A 151 ? 0.6596 0.6294 0.8022 0.0367  -0.0027 0.1409  807  ASP A CA  
1133 C C   . ASP A 151 ? 0.7181 0.6664 0.8722 0.0373  -0.0029 0.1341  807  ASP A C   
1134 O O   . ASP A 151 ? 0.7320 0.6652 0.8902 0.0307  -0.0006 0.1387  807  ASP A O   
1135 C CB  . ASP A 151 ? 0.6983 0.6634 0.8356 0.0365  -0.0034 0.1592  807  ASP A CB  
1136 C CG  . ASP A 151 ? 0.9165 0.9029 1.0414 0.0334  -0.0022 0.1659  807  ASP A CG  
1137 O OD1 . ASP A 151 ? 0.9452 0.9399 1.0669 0.0246  0.0025  0.1649  807  ASP A OD1 
1138 O OD2 . ASP A 151 ? 0.9938 0.9899 1.1122 0.0398  -0.0059 0.1718  807  ASP A OD2 
1139 N N   . SER A 152 ? 0.6481 0.5956 0.8072 0.0443  -0.0054 0.1228  808  SER A N   
1140 C CA  . SER A 152 ? 0.6358 0.5645 0.8048 0.0453  -0.0054 0.1147  808  SER A CA  
1141 C C   . SER A 152 ? 0.6855 0.6143 0.8579 0.0358  -0.0021 0.1042  808  SER A C   
1142 O O   . SER A 152 ? 0.6856 0.6312 0.8535 0.0306  0.0000  0.1016  808  SER A O   
1143 C CB  . SER A 152 ? 0.6636 0.5938 0.8364 0.0557  -0.0086 0.1062  808  SER A CB  
1144 O OG  . SER A 152 ? 0.7355 0.6843 0.9055 0.0557  -0.0087 0.0952  808  SER A OG  
1145 N N   . GLU A 153 ? 0.6313 0.5417 0.8118 0.0338  -0.0015 0.0982  809  GLU A N   
1146 C CA  . GLU A 153 ? 0.6200 0.5300 0.8044 0.0247  0.0009  0.0882  809  GLU A CA  
1147 C C   . GLU A 153 ? 0.6084 0.5346 0.7923 0.0268  0.0002  0.0748  809  GLU A C   
1148 O O   . GLU A 153 ? 0.6068 0.5457 0.7898 0.0201  0.0022  0.0706  809  GLU A O   
1149 C CB  . GLU A 153 ? 0.6488 0.5347 0.8411 0.0219  0.0013  0.0847  809  GLU A CB  
1150 N N   . GLU A 154 ? 0.5151 0.4419 0.7000 0.0361  -0.0024 0.0687  810  GLU A N   
1151 C CA  . GLU A 154 ? 0.4902 0.4317 0.6745 0.0386  -0.0032 0.0569  810  GLU A CA  
1152 C C   . GLU A 154 ? 0.4770 0.4398 0.6544 0.0374  -0.0026 0.0586  810  GLU A C   
1153 O O   . GLU A 154 ? 0.4649 0.4384 0.6422 0.0340  -0.0016 0.0505  810  GLU A O   
1154 C CB  . GLU A 154 ? 0.5062 0.4450 0.6931 0.0487  -0.0058 0.0513  810  GLU A CB  
1155 C CG  . GLU A 154 ? 0.6407 0.5808 0.8251 0.0574  -0.0081 0.0610  810  GLU A CG  
1156 C CD  . GLU A 154 ? 0.8073 0.7422 0.9966 0.0678  -0.0104 0.0573  810  GLU A CD  
1157 O OE1 . GLU A 154 ? 0.5271 0.4571 0.7213 0.0686  -0.0098 0.0459  810  GLU A OE1 
1158 O OE2 . GLU A 154 ? 0.7818 0.7190 0.9701 0.0752  -0.0127 0.0659  810  GLU A OE2 
1159 N N   . ALA A 155 ? 0.3994 0.3675 0.5709 0.0397  -0.0030 0.0694  811  ALA A N   
1160 C CA  . ALA A 155 ? 0.3822 0.3692 0.5460 0.0385  -0.0021 0.0717  811  ALA A CA  
1161 C C   . ALA A 155 ? 0.4071 0.3998 0.5702 0.0292  0.0018  0.0723  811  ALA A C   
1162 O O   . ALA A 155 ? 0.3648 0.3726 0.5248 0.0276  0.0033  0.0676  811  ALA A O   
1163 C CB  . ALA A 155 ? 0.3899 0.3798 0.5473 0.0426  -0.0036 0.0837  811  ALA A CB  
1164 N N   . GLU A 156 ? 0.3999 0.3805 0.5665 0.0230  0.0036  0.0783  812  GLU A N   
1165 C CA  . GLU A 156 ? 0.4017 0.3871 0.5695 0.0134  0.0074  0.0796  812  GLU A CA  
1166 C C   . GLU A 156 ? 0.4012 0.3914 0.5747 0.0102  0.0080  0.0674  812  GLU A C   
1167 O O   . GLU A 156 ? 0.3833 0.3882 0.5561 0.0065  0.0105  0.0651  812  GLU A O   
1168 C CB  . GLU A 156 ? 0.4327 0.4018 0.6039 0.0073  0.0087  0.0887  812  GLU A CB  
1169 C CG  . GLU A 156 ? 0.6180 0.5865 0.7826 0.0077  0.0093  0.1033  812  GLU A CG  
1170 C CD  . GLU A 156 ? 0.9898 0.9390 1.1576 0.0031  0.0099  0.1138  812  GLU A CD  
1171 O OE1 . GLU A 156 ? 0.9247 0.8641 1.0995 -0.0045 0.0115  0.1104  812  GLU A OE1 
1172 O OE2 . GLU A 156 ? 0.9723 0.9165 1.1355 0.0067  0.0087  0.1257  812  GLU A OE2 
1173 N N   . ILE A 157 ? 0.3371 0.3158 0.5161 0.0120  0.0057  0.0597  813  ILE A N   
1174 C CA  . ILE A 157 ? 0.3092 0.2918 0.4933 0.0093  0.0054  0.0482  813  ILE A CA  
1175 C C   . ILE A 157 ? 0.3158 0.3151 0.4965 0.0140  0.0048  0.0418  813  ILE A C   
1176 O O   . ILE A 157 ? 0.2950 0.3054 0.4779 0.0103  0.0061  0.0367  813  ILE A O   
1177 C CB  . ILE A 157 ? 0.3370 0.3028 0.5262 0.0109  0.0032  0.0416  813  ILE A CB  
1178 C CG1 . ILE A 157 ? 0.3347 0.2847 0.5288 0.0030  0.0045  0.0449  813  ILE A CG1 
1179 C CG2 . ILE A 157 ? 0.3260 0.2987 0.5176 0.0116  0.0019  0.0290  813  ILE A CG2 
1180 C CD1 . ILE A 157 ? 0.4577 0.3864 0.6552 0.0063  0.0029  0.0427  813  ILE A CD1 
1181 N N   . ILE A 158 ? 0.2475 0.2487 0.4236 0.0220  0.0029  0.0424  814  ILE A N   
1182 C CA  . ILE A 158 ? 0.2388 0.2539 0.4113 0.0265  0.0021  0.0367  814  ILE A CA  
1183 C C   . ILE A 158 ? 0.2737 0.3032 0.4420 0.0236  0.0050  0.0394  814  ILE A C   
1184 O O   . ILE A 158 ? 0.2538 0.2937 0.4227 0.0232  0.0058  0.0331  814  ILE A O   
1185 C CB  . ILE A 158 ? 0.2824 0.2964 0.4516 0.0349  -0.0008 0.0375  814  ILE A CB  
1186 C CG1 . ILE A 158 ? 0.2854 0.2879 0.4600 0.0386  -0.0030 0.0316  814  ILE A CG1 
1187 C CG2 . ILE A 158 ? 0.2930 0.3220 0.4573 0.0382  -0.0012 0.0334  814  ILE A CG2 
1188 C CD1 . ILE A 158 ? 0.3856 0.3853 0.5590 0.0468  -0.0056 0.0342  814  ILE A CD1 
1189 N N   . ARG A 159 ? 0.2453 0.2752 0.4095 0.0217  0.0068  0.0491  815  ARG A N   
1190 C CA  . ARG A 159 ? 0.2409 0.2844 0.4004 0.0189  0.0103  0.0521  815  ARG A CA  
1191 C C   . ARG A 159 ? 0.2405 0.2892 0.4059 0.0123  0.0135  0.0496  815  ARG A C   
1192 O O   . ARG A 159 ? 0.2365 0.2984 0.4003 0.0115  0.0164  0.0477  815  ARG A O   
1193 C CB  . ARG A 159 ? 0.2620 0.3046 0.4152 0.0181  0.0115  0.0636  815  ARG A CB  
1194 C CG  . ARG A 159 ? 0.4133 0.4600 0.5584 0.0246  0.0089  0.0663  815  ARG A CG  
1195 C CD  . ARG A 159 ? 0.5514 0.6022 0.6888 0.0227  0.0106  0.0777  815  ARG A CD  
1196 N NE  . ARG A 159 ? 0.6413 0.6784 0.7818 0.0195  0.0106  0.0873  815  ARG A NE  
1197 C CZ  . ARG A 159 ? 0.8353 0.8619 0.9747 0.0235  0.0074  0.0951  815  ARG A CZ  
1198 N NH1 . ARG A 159 ? 0.7088 0.7394 0.8440 0.0308  0.0037  0.0948  815  ARG A NH1 
1199 N NH2 . ARG A 159 ? 0.6535 0.6657 0.7966 0.0202  0.0077  0.1035  815  ARG A NH2 
1200 N N   . LYS A 160 ? 0.1922 0.2310 0.3648 0.0074  0.0131  0.0495  816  LYS A N   
1201 C CA  . LYS A 160 ? 0.1902 0.2350 0.3696 0.0004  0.0155  0.0473  816  LYS A CA  
1202 C C   . LYS A 160 ? 0.2092 0.2614 0.3925 0.0023  0.0141  0.0370  816  LYS A C   
1203 O O   . LYS A 160 ? 0.1845 0.2493 0.3710 0.0001  0.0164  0.0351  816  LYS A O   
1204 C CB  . LYS A 160 ? 0.2116 0.2433 0.3969 -0.0065 0.0152  0.0503  816  LYS A CB  
1205 C CG  . LYS A 160 ? 0.1998 0.2399 0.3911 -0.0152 0.0184  0.0519  816  LYS A CG  
1206 C CD  . LYS A 160 ? 0.2976 0.3239 0.4934 -0.0230 0.0184  0.0565  816  LYS A CD  
1207 C CE  . LYS A 160 ? 0.3643 0.4011 0.5669 -0.0326 0.0216  0.0583  816  LYS A CE  
1208 N NZ  . LYS A 160 ? 0.3960 0.4187 0.6042 -0.0414 0.0211  0.0604  816  LYS A NZ  
1209 N N   . TYR A 161 ? 0.1726 0.2177 0.3555 0.0071  0.0104  0.0312  817  TYR A N   
1210 C CA  . TYR A 161 ? 0.1579 0.2087 0.3432 0.0094  0.0086  0.0224  817  TYR A CA  
1211 C C   . TYR A 161 ? 0.1940 0.2581 0.3756 0.0132  0.0102  0.0209  817  TYR A C   
1212 O O   . TYR A 161 ? 0.1672 0.2407 0.3527 0.0121  0.0111  0.0172  817  TYR A O   
1213 C CB  . TYR A 161 ? 0.1695 0.2102 0.3537 0.0141  0.0051  0.0178  817  TYR A CB  
1214 C CG  . TYR A 161 ? 0.1904 0.2330 0.3781 0.0143  0.0028  0.0090  817  TYR A CG  
1215 C CD1 . TYR A 161 ? 0.2054 0.2588 0.3970 0.0110  0.0034  0.0058  817  TYR A CD1 
1216 C CD2 . TYR A 161 ? 0.2018 0.2364 0.3889 0.0181  0.0002  0.0042  817  TYR A CD2 
1217 C CE1 . TYR A 161 ? 0.2091 0.2652 0.4030 0.0110  0.0011  -0.0013 817  TYR A CE1 
1218 C CE2 . TYR A 161 ? 0.2134 0.2510 0.4026 0.0179  -0.0016 -0.0037 817  TYR A CE2 
1219 C CZ  . TYR A 161 ? 0.2407 0.2889 0.4328 0.0142  -0.0014 -0.0061 817  TYR A CZ  
1220 O OH  . TYR A 161 ? 0.1773 0.2290 0.3708 0.0139  -0.0034 -0.0130 817  TYR A OH  
1221 N N   . VAL A 162 ? 0.1702 0.2352 0.3444 0.0175  0.0107  0.0242  818  VAL A N   
1222 C CA  . VAL A 162 ? 0.1671 0.2430 0.3364 0.0207  0.0126  0.0227  818  VAL A CA  
1223 C C   . VAL A 162 ? 0.2462 0.3323 0.4177 0.0168  0.0172  0.0251  818  VAL A C   
1224 O O   . VAL A 162 ? 0.2628 0.3576 0.4371 0.0177  0.0188  0.0206  818  VAL A O   
1225 C CB  . VAL A 162 ? 0.2041 0.2791 0.3646 0.0247  0.0119  0.0262  818  VAL A CB  
1226 C CG1 . VAL A 162 ? 0.1882 0.2743 0.3430 0.0269  0.0142  0.0236  818  VAL A CG1 
1227 C CG2 . VAL A 162 ? 0.2089 0.2763 0.3688 0.0291  0.0075  0.0236  818  VAL A CG2 
1228 N N   . LYS A 163 ? 0.2120 0.2968 0.3828 0.0126  0.0195  0.0325  819  LYS A N   
1229 C CA  . LYS A 163 ? 0.2090 0.3041 0.3820 0.0083  0.0243  0.0359  819  LYS A CA  
1230 C C   . LYS A 163 ? 0.2653 0.3674 0.4486 0.0050  0.0253  0.0321  819  LYS A C   
1231 O O   . LYS A 163 ? 0.2721 0.3866 0.4576 0.0056  0.0290  0.0306  819  LYS A O   
1232 C CB  . LYS A 163 ? 0.2381 0.3283 0.4090 0.0035  0.0258  0.0453  819  LYS A CB  
1233 C CG  . LYS A 163 ? 0.4132 0.5151 0.5851 -0.0014 0.0314  0.0502  819  LYS A CG  
1234 C CD  . LYS A 163 ? 0.4632 0.5584 0.6317 -0.0063 0.0324  0.0606  819  LYS A CD  
1235 C CE  . LYS A 163 ? 0.5444 0.6418 0.7206 -0.0150 0.0353  0.0654  819  LYS A CE  
1236 N NZ  . LYS A 163 ? 0.4696 0.5854 0.6472 -0.0173 0.0413  0.0660  819  LYS A NZ  
1237 N N   . ASN A 164 ? 0.2078 0.3027 0.3975 0.0017  0.0222  0.0305  820  ASN A N   
1238 C CA  . ASN A 164 ? 0.1914 0.2936 0.3909 -0.0026 0.0223  0.0278  820  ASN A CA  
1239 C C   . ASN A 164 ? 0.2089 0.3162 0.4121 0.0011  0.0199  0.0206  820  ASN A C   
1240 O O   . ASN A 164 ? 0.1923 0.3095 0.4036 -0.0016 0.0204  0.0194  820  ASN A O   
1241 C CB  . ASN A 164 ? 0.2190 0.3116 0.4233 -0.0094 0.0201  0.0294  820  ASN A CB  
1242 C CG  . ASN A 164 ? 0.3887 0.4774 0.5927 -0.0156 0.0228  0.0375  820  ASN A CG  
1243 O OD1 . ASN A 164 ? 0.3239 0.4208 0.5252 -0.0161 0.0271  0.0429  820  ASN A OD1 
1244 N ND2 . ASN A 164 ? 0.2383 0.3143 0.4450 -0.0208 0.0206  0.0384  820  ASN A ND2 
1245 N N   . THR A 165 ? 0.1457 0.2471 0.3436 0.0068  0.0171  0.0164  821  THR A N   
1246 C CA  . THR A 165 ? 0.1297 0.2349 0.3307 0.0096  0.0145  0.0104  821  THR A CA  
1247 C C   . THR A 165 ? 0.1664 0.2773 0.3637 0.0159  0.0161  0.0079  821  THR A C   
1248 O O   . THR A 165 ? 0.1551 0.2654 0.3520 0.0192  0.0137  0.0036  821  THR A O   
1249 C CB  . THR A 165 ? 0.2395 0.3340 0.4394 0.0096  0.0098  0.0065  821  THR A CB  
1250 O OG1 . THR A 165 ? 0.1909 0.2774 0.3831 0.0144  0.0088  0.0060  821  THR A OG1 
1251 C CG2 . THR A 165 ? 0.1528 0.2400 0.3566 0.0030  0.0085  0.0076  821  THR A CG2 
1252 N N   . HIS A 166 ? 0.1510 0.2678 0.3458 0.0170  0.0205  0.0105  822  HIS A N   
1253 C CA  . HIS A 166 ? 0.1420 0.2638 0.3338 0.0224  0.0227  0.0074  822  HIS A CA  
1254 C C   . HIS A 166 ? 0.1441 0.2774 0.3452 0.0226  0.0251  0.0066  822  HIS A C   
1255 O O   . HIS A 166 ? 0.1015 0.2427 0.3071 0.0197  0.0286  0.0099  822  HIS A O   
1256 C CB  . HIS A 166 ? 0.1555 0.2783 0.3388 0.0236  0.0264  0.0096  822  HIS A CB  
1257 C CG  . HIS A 166 ? 0.2047 0.3303 0.3833 0.0286  0.0284  0.0050  822  HIS A CG  
1258 N ND1 . HIS A 166 ? 0.2367 0.3585 0.4052 0.0305  0.0281  0.0041  822  HIS A ND1 
1259 C CD2 . HIS A 166 ? 0.2206 0.3522 0.4037 0.0317  0.0308  0.0012  822  HIS A CD2 
1260 C CE1 . HIS A 166 ? 0.2285 0.3533 0.3951 0.0339  0.0303  -0.0009 822  HIS A CE1 
1261 N NE2 . HIS A 166 ? 0.2223 0.3521 0.3977 0.0352  0.0322  -0.0027 822  HIS A NE2 
1262 N N   . ALA A 167 ? 0.0867 0.2214 0.2912 0.0260  0.0232  0.0029  823  ALA A N   
1263 C CA  . ALA A 167 ? 0.0600 0.2054 0.2742 0.0275  0.0246  0.0026  823  ALA A CA  
1264 C C   . ALA A 167 ? 0.1278 0.2807 0.3429 0.0316  0.0305  0.0020  823  ALA A C   
1265 O O   . ALA A 167 ? 0.1104 0.2587 0.3176 0.0350  0.0326  -0.0006 823  ALA A O   
1266 C CB  . ALA A 167 ? 0.0663 0.2098 0.2828 0.0301  0.0204  -0.0002 823  ALA A CB  
1267 N N   . THR A 168 ? 0.1215 0.2867 0.3467 0.0313  0.0333  0.0040  824  THR A N   
1268 C CA  . THR A 168 ? 0.1221 0.2963 0.3505 0.0357  0.0396  0.0030  824  THR A CA  
1269 C C   . THR A 168 ? 0.1877 0.3573 0.4148 0.0428  0.0399  -0.0016 824  THR A C   
1270 O O   . THR A 168 ? 0.2007 0.3693 0.4228 0.0464  0.0447  -0.0047 824  THR A O   
1271 C CB  . THR A 168 ? 0.1896 0.3795 0.4317 0.0344  0.0417  0.0062  824  THR A CB  
1272 O OG1 . THR A 168 ? 0.2054 0.3985 0.4480 0.0268  0.0418  0.0104  824  THR A OG1 
1273 C CG2 . THR A 168 ? 0.0572 0.2578 0.3047 0.0402  0.0487  0.0047  824  THR A CG2 
1274 N N   . THR A 169 ? 0.1296 0.2956 0.3602 0.0442  0.0348  -0.0021 825  THR A N   
1275 C CA  . THR A 169 ? 0.1284 0.2888 0.3582 0.0504  0.0348  -0.0055 825  THR A CA  
1276 C C   . THR A 169 ? 0.1945 0.3424 0.4114 0.0509  0.0348  -0.0096 825  THR A C   
1277 O O   . THR A 169 ? 0.2182 0.3605 0.4331 0.0552  0.0360  -0.0131 825  THR A O   
1278 C CB  . THR A 169 ? 0.1975 0.3584 0.4338 0.0513  0.0295  -0.0039 825  THR A CB  
1279 O OG1 . THR A 169 ? 0.2792 0.4319 0.5087 0.0472  0.0240  -0.0042 825  THR A OG1 
1280 C CG2 . THR A 169 ? 0.1471 0.3224 0.3964 0.0502  0.0287  0.0003  825  THR A CG2 
1281 N N   . HIS A 170 ? 0.1458 0.2895 0.3543 0.0464  0.0335  -0.0090 826  HIS A N   
1282 C CA  . HIS A 170 ? 0.1358 0.2701 0.3323 0.0463  0.0328  -0.0120 826  HIS A CA  
1283 C C   . HIS A 170 ? 0.2371 0.3742 0.4265 0.0455  0.0377  -0.0124 826  HIS A C   
1284 O O   . HIS A 170 ? 0.2477 0.3796 0.4272 0.0437  0.0364  -0.0128 826  HIS A O   
1285 C CB  . HIS A 170 ? 0.1219 0.2497 0.3144 0.0426  0.0269  -0.0105 826  HIS A CB  
1286 C CG  . HIS A 170 ? 0.1444 0.2704 0.3420 0.0428  0.0223  -0.0106 826  HIS A CG  
1287 N ND1 . HIS A 170 ? 0.1602 0.2837 0.3579 0.0392  0.0177  -0.0091 826  HIS A ND1 
1288 C CD2 . HIS A 170 ? 0.1412 0.2676 0.3434 0.0461  0.0217  -0.0119 826  HIS A CD2 
1289 C CE1 . HIS A 170 ? 0.1397 0.2636 0.3414 0.0401  0.0146  -0.0098 826  HIS A CE1 
1290 N NE2 . HIS A 170 ? 0.1353 0.2608 0.3399 0.0442  0.0167  -0.0107 826  HIS A NE2 
1291 N N   . ASN A 171 ? 0.2133 0.3597 0.4079 0.0469  0.0434  -0.0120 827  ASN A N   
1292 C CA  . ASN A 171 ? 0.2229 0.3748 0.4114 0.0458  0.0489  -0.0119 827  ASN A CA  
1293 C C   . ASN A 171 ? 0.2615 0.4103 0.4403 0.0486  0.0525  -0.0182 827  ASN A C   
1294 O O   . ASN A 171 ? 0.2447 0.3985 0.4165 0.0471  0.0567  -0.0182 827  ASN A O   
1295 C CB  . ASN A 171 ? 0.2723 0.4374 0.4707 0.0459  0.0540  -0.0094 827  ASN A CB  
1296 C CG  . ASN A 171 ? 0.3541 0.5243 0.5610 0.0521  0.0582  -0.0132 827  ASN A CG  
1297 O OD1 . ASN A 171 ? 0.3357 0.4986 0.5438 0.0563  0.0564  -0.0168 827  ASN A OD1 
1298 N ND2 . ASN A 171 ? 0.3055 0.4883 0.5188 0.0529  0.0642  -0.0122 827  ASN A ND2 
1299 N N   . ALA A 172 ? 0.2210 0.3614 0.3981 0.0518  0.0508  -0.0233 828  ALA A N   
1300 C CA  . ALA A 172 ? 0.2205 0.3564 0.3879 0.0534  0.0536  -0.0301 828  ALA A CA  
1301 C C   . ALA A 172 ? 0.2756 0.4096 0.4298 0.0491  0.0510  -0.0294 828  ALA A C   
1302 O O   . ALA A 172 ? 0.2874 0.4193 0.4319 0.0491  0.0527  -0.0348 828  ALA A O   
1303 C CB  . ALA A 172 ? 0.2332 0.3594 0.4027 0.0564  0.0512  -0.0345 828  ALA A CB  
1304 N N   . TYR A 173 ? 0.2097 0.3439 0.3639 0.0457  0.0467  -0.0228 829  TYR A N   
1305 C CA  . TYR A 173 ? 0.1946 0.3275 0.3384 0.0424  0.0437  -0.0201 829  TYR A CA  
1306 C C   . TYR A 173 ? 0.2438 0.3791 0.3905 0.0392  0.0421  -0.0119 829  TYR A C   
1307 O O   . TYR A 173 ? 0.2352 0.3709 0.3919 0.0388  0.0410  -0.0092 829  TYR A O   
1308 C CB  . TYR A 173 ? 0.1790 0.3037 0.3187 0.0424  0.0378  -0.0224 829  TYR A CB  
1309 C CG  . TYR A 173 ? 0.1542 0.2737 0.3016 0.0424  0.0326  -0.0195 829  TYR A CG  
1310 C CD1 . TYR A 173 ? 0.1708 0.2887 0.3179 0.0401  0.0287  -0.0140 829  TYR A CD1 
1311 C CD2 . TYR A 173 ? 0.1548 0.2709 0.3095 0.0446  0.0317  -0.0224 829  TYR A CD2 
1312 C CE1 . TYR A 173 ? 0.1383 0.2516 0.2918 0.0399  0.0243  -0.0126 829  TYR A CE1 
1313 C CE2 . TYR A 173 ? 0.1732 0.2860 0.3339 0.0441  0.0271  -0.0201 829  TYR A CE2 
1314 C CZ  . TYR A 173 ? 0.2162 0.3279 0.3760 0.0416  0.0236  -0.0158 829  TYR A CZ  
1315 O OH  . TYR A 173 ? 0.1068 0.2154 0.2718 0.0409  0.0194  -0.0146 829  TYR A OH  
1316 N N   . ASP A 174 ? 0.2292 0.3658 0.3671 0.0366  0.0413  -0.0079 830  ASP A N   
1317 C CA  . ASP A 174 ? 0.2239 0.3599 0.3631 0.0332  0.0393  0.0003  830  ASP A CA  
1318 C C   . ASP A 174 ? 0.2335 0.3624 0.3668 0.0332  0.0334  0.0021  830  ASP A C   
1319 O O   . ASP A 174 ? 0.2270 0.3543 0.3548 0.0351  0.0316  -0.0028 830  ASP A O   
1320 C CB  . ASP A 174 ? 0.2612 0.4057 0.3963 0.0303  0.0443  0.0053  830  ASP A CB  
1321 C CG  . ASP A 174 ? 0.5460 0.6948 0.6677 0.0301  0.0460  0.0043  830  ASP A CG  
1322 O OD1 . ASP A 174 ? 0.6010 0.7472 0.7156 0.0287  0.0422  0.0095  830  ASP A OD1 
1323 O OD2 . ASP A 174 ? 0.6946 0.8498 0.8131 0.0315  0.0511  -0.0016 830  ASP A OD2 
1324 N N   . LEU A 175 ? 0.1771 0.3017 0.3128 0.0313  0.0304  0.0086  831  LEU A N   
1325 C CA  . LEU A 175 ? 0.1927 0.3105 0.3248 0.0322  0.0248  0.0107  831  LEU A CA  
1326 C C   . LEU A 175 ? 0.2797 0.3976 0.4061 0.0303  0.0244  0.0191  831  LEU A C   
1327 O O   . LEU A 175 ? 0.2807 0.3988 0.4101 0.0271  0.0266  0.0249  831  LEU A O   
1328 C CB  . LEU A 175 ? 0.1914 0.3013 0.3325 0.0325  0.0210  0.0103  831  LEU A CB  
1329 C CG  . LEU A 175 ? 0.2147 0.3233 0.3606 0.0346  0.0197  0.0032  831  LEU A CG  
1330 C CD1 . LEU A 175 ? 0.2000 0.3030 0.3542 0.0338  0.0168  0.0035  831  LEU A CD1 
1331 C CD2 . LEU A 175 ? 0.2026 0.3102 0.3424 0.0371  0.0170  -0.0010 831  LEU A CD2 
1332 N N   . GLU A 176 ? 0.2695 0.3876 0.3878 0.0319  0.0213  0.0202  832  GLU A N   
1333 C CA  . GLU A 176 ? 0.2875 0.4054 0.3998 0.0311  0.0197  0.0291  832  GLU A CA  
1334 C C   . GLU A 176 ? 0.3355 0.4461 0.4491 0.0343  0.0136  0.0308  832  GLU A C   
1335 O O   . GLU A 176 ? 0.3212 0.4341 0.4322 0.0368  0.0109  0.0256  832  GLU A O   
1336 C CB  . GLU A 176 ? 0.3108 0.4392 0.4110 0.0303  0.0218  0.0295  832  GLU A CB  
1337 C CG  . GLU A 176 ? 0.3948 0.5254 0.4882 0.0285  0.0214  0.0405  832  GLU A CG  
1338 C CD  . GLU A 176 ? 0.6227 0.7640 0.7029 0.0283  0.0213  0.0410  832  GLU A CD  
1339 O OE1 . GLU A 176 ? 0.5832 0.7248 0.6584 0.0294  0.0170  0.0484  832  GLU A OE1 
1340 O OE2 . GLU A 176 ? 0.6084 0.7579 0.6833 0.0271  0.0255  0.0338  832  GLU A OE2 
1341 N N   . VAL A 177 ? 0.3093 0.4113 0.4277 0.0341  0.0116  0.0377  833  VAL A N   
1342 C CA  . VAL A 177 ? 0.3074 0.4019 0.4282 0.0379  0.0064  0.0396  833  VAL A CA  
1343 C C   . VAL A 177 ? 0.3600 0.4598 0.4721 0.0399  0.0038  0.0459  833  VAL A C   
1344 O O   . VAL A 177 ? 0.3623 0.4631 0.4698 0.0379  0.0051  0.0547  833  VAL A O   
1345 C CB  . VAL A 177 ? 0.3467 0.4285 0.4757 0.0372  0.0054  0.0442  833  VAL A CB  
1346 C CG1 . VAL A 177 ? 0.3409 0.4151 0.4739 0.0421  0.0007  0.0430  833  VAL A CG1 
1347 C CG2 . VAL A 177 ? 0.3384 0.4176 0.4751 0.0334  0.0084  0.0396  833  VAL A CG2 
1348 N N   . ILE A 178 ? 0.3259 0.4302 0.4355 0.0434  0.0002  0.0418  834  ILE A N   
1349 C CA  . ILE A 178 ? 0.3202 0.4317 0.4220 0.0455  -0.0032 0.0476  834  ILE A CA  
1350 C C   . ILE A 178 ? 0.3517 0.4549 0.4590 0.0502  -0.0076 0.0547  834  ILE A C   
1351 O O   . ILE A 178 ? 0.3359 0.4383 0.4398 0.0510  -0.0089 0.0653  834  ILE A O   
1352 C CB  . ILE A 178 ? 0.3607 0.4831 0.4572 0.0462  -0.0049 0.0398  834  ILE A CB  
1353 C CG1 . ILE A 178 ? 0.3648 0.4934 0.4562 0.0421  0.0000  0.0320  834  ILE A CG1 
1354 C CG2 . ILE A 178 ? 0.3721 0.5039 0.4610 0.0482  -0.0093 0.0461  834  ILE A CG2 
1355 C CD1 . ILE A 178 ? 0.4290 0.5675 0.5086 0.0383  0.0037  0.0357  834  ILE A CD1 
1356 N N   . ASP A 179 ? 0.2892 0.3864 0.4049 0.0535  -0.0097 0.0490  835  ASP A N   
1357 C CA  . ASP A 179 ? 0.2813 0.3703 0.4035 0.0588  -0.0134 0.0536  835  ASP A CA  
1358 C C   . ASP A 179 ? 0.3040 0.3807 0.4362 0.0593  -0.0124 0.0480  835  ASP A C   
1359 O O   . ASP A 179 ? 0.3063 0.3845 0.4407 0.0570  -0.0107 0.0390  835  ASP A O   
1360 C CB  . ASP A 179 ? 0.3074 0.4059 0.4287 0.0636  -0.0179 0.0517  835  ASP A CB  
1361 C CG  . ASP A 179 ? 0.5081 0.6195 0.6200 0.0639  -0.0203 0.0583  835  ASP A CG  
1362 O OD1 . ASP A 179 ? 0.5285 0.6374 0.6380 0.0652  -0.0214 0.0694  835  ASP A OD1 
1363 O OD2 . ASP A 179 ? 0.6111 0.7350 0.7179 0.0627  -0.0214 0.0525  835  ASP A OD2 
1364 N N   . ILE A 180 ? 0.2439 0.3085 0.3820 0.0624  -0.0137 0.0534  836  ILE A N   
1365 C CA  . ILE A 180 ? 0.2459 0.2984 0.3931 0.0633  -0.0133 0.0479  836  ILE A CA  
1366 C C   . ILE A 180 ? 0.2927 0.3426 0.4450 0.0710  -0.0169 0.0484  836  ILE A C   
1367 O O   . ILE A 180 ? 0.3056 0.3524 0.4577 0.0752  -0.0190 0.0577  836  ILE A O   
1368 C CB  . ILE A 180 ? 0.3008 0.3392 0.4515 0.0591  -0.0107 0.0520  836  ILE A CB  
1369 C CG1 . ILE A 180 ? 0.3061 0.3497 0.4527 0.0516  -0.0067 0.0521  836  ILE A CG1 
1370 C CG2 . ILE A 180 ? 0.3330 0.3602 0.4924 0.0598  -0.0105 0.0444  836  ILE A CG2 
1371 C CD1 . ILE A 180 ? 0.3684 0.4009 0.5177 0.0462  -0.0041 0.0583  836  ILE A CD1 
1372 N N   . PHE A 181 ? 0.2310 0.2830 0.3879 0.0733  -0.0175 0.0390  837  PHE A N   
1373 C CA  . PHE A 181 ? 0.2179 0.2687 0.3810 0.0809  -0.0203 0.0381  837  PHE A CA  
1374 C C   . PHE A 181 ? 0.3065 0.3438 0.4775 0.0819  -0.0188 0.0322  837  PHE A C   
1375 O O   . PHE A 181 ? 0.3019 0.3378 0.4734 0.0769  -0.0166 0.0245  837  PHE A O   
1376 C CB  . PHE A 181 ? 0.2229 0.2895 0.3850 0.0830  -0.0223 0.0321  837  PHE A CB  
1377 C CG  . PHE A 181 ? 0.2336 0.3143 0.3873 0.0814  -0.0239 0.0362  837  PHE A CG  
1378 C CD1 . PHE A 181 ? 0.2779 0.3644 0.4300 0.0861  -0.0273 0.0451  837  PHE A CD1 
1379 C CD2 . PHE A 181 ? 0.2536 0.3420 0.4011 0.0752  -0.0220 0.0312  837  PHE A CD2 
1380 C CE1 . PHE A 181 ? 0.2984 0.3989 0.4416 0.0838  -0.0289 0.0483  837  PHE A CE1 
1381 C CE2 . PHE A 181 ? 0.3006 0.4014 0.4397 0.0732  -0.0231 0.0338  837  PHE A CE2 
1382 C CZ  . PHE A 181 ? 0.2857 0.3931 0.4223 0.0771  -0.0266 0.0420  837  PHE A CZ  
1383 N N   . LYS A 182 ? 0.2950 0.3221 0.4720 0.0883  -0.0200 0.0356  838  LYS A N   
1384 C CA  . LYS A 182 ? 0.3038 0.3180 0.4882 0.0900  -0.0185 0.0286  838  LYS A CA  
1385 C C   . LYS A 182 ? 0.3427 0.3675 0.5309 0.0961  -0.0199 0.0217  838  LYS A C   
1386 O O   . LYS A 182 ? 0.3453 0.3774 0.5350 0.1028  -0.0226 0.0267  838  LYS A O   
1387 C CB  . LYS A 182 ? 0.3443 0.3401 0.5338 0.0939  -0.0185 0.0353  838  LYS A CB  
1388 C CG  . LYS A 182 ? 0.4804 0.4602 0.6757 0.0924  -0.0160 0.0271  838  LYS A CG  
1389 C CD  . LYS A 182 ? 0.6162 0.5781 0.8185 0.0992  -0.0162 0.0316  838  LYS A CD  
1390 C CE  . LYS A 182 ? 0.7724 0.7154 0.9788 0.0952  -0.0134 0.0245  838  LYS A CE  
1391 N NZ  . LYS A 182 ? 0.8965 0.8279 1.1002 0.0868  -0.0121 0.0311  838  LYS A NZ  
1392 N N   . ILE A 183 ? 0.3062 0.3345 0.4955 0.0932  -0.0183 0.0109  839  ILE A N   
1393 C CA  . ILE A 183 ? 0.3034 0.3437 0.4959 0.0977  -0.0192 0.0042  839  ILE A CA  
1394 C C   . ILE A 183 ? 0.3722 0.4042 0.5716 0.1011  -0.0173 -0.0044 839  ILE A C   
1395 O O   . ILE A 183 ? 0.3815 0.4022 0.5812 0.0964  -0.0151 -0.0092 839  ILE A O   
1396 C CB  . ILE A 183 ? 0.3328 0.3888 0.5199 0.0922  -0.0192 -0.0006 839  ILE A CB  
1397 C CG1 . ILE A 183 ? 0.3322 0.3840 0.5170 0.0844  -0.0167 -0.0069 839  ILE A CG1 
1398 C CG2 . ILE A 183 ? 0.3358 0.4016 0.5163 0.0905  -0.0211 0.0069  839  ILE A CG2 
1399 C CD1 . ILE A 183 ? 0.3677 0.4327 0.5490 0.0801  -0.0165 -0.0124 839  ILE A CD1 
1400 N N   . GLU A 184 ? 0.3180 0.3570 0.5231 0.1092  -0.0182 -0.0064 840  GLU A N   
1401 C CA  . GLU A 184 ? 0.3177 0.3519 0.5298 0.1141  -0.0162 -0.0149 840  GLU A CA  
1402 C C   . GLU A 184 ? 0.3565 0.4099 0.5710 0.1174  -0.0166 -0.0205 840  GLU A C   
1403 O O   . GLU A 184 ? 0.3611 0.4238 0.5800 0.1249  -0.0186 -0.0164 840  GLU A O   
1404 C CB  . GLU A 184 ? 0.3411 0.3605 0.5604 0.1229  -0.0163 -0.0103 840  GLU A CB  
1405 C CG  . GLU A 184 ? 0.5299 0.5398 0.7560 0.1273  -0.0133 -0.0204 840  GLU A CG  
1406 C CD  . GLU A 184 ? 0.9069 0.8985 1.1408 0.1359  -0.0127 -0.0170 840  GLU A CD  
1407 O OE1 . GLU A 184 ? 0.8887 0.8645 1.1211 0.1337  -0.0132 -0.0091 840  GLU A OE1 
1408 O OE2 . GLU A 184 ? 0.8111 0.8039 1.0529 0.1449  -0.0113 -0.0223 840  GLU A OE2 
1409 N N   . ARG A 185 ? 0.2880 0.3481 0.4995 0.1115  -0.0148 -0.0292 841  ARG A N   
1410 C CA  . ARG A 185 ? 0.2643 0.3424 0.4776 0.1131  -0.0146 -0.0348 841  ARG A CA  
1411 C C   . ARG A 185 ? 0.3066 0.3827 0.5282 0.1210  -0.0125 -0.0413 841  ARG A C   
1412 O O   . ARG A 185 ? 0.3108 0.3722 0.5338 0.1210  -0.0099 -0.0467 841  ARG A O   
1413 C CB  . ARG A 185 ? 0.2648 0.3492 0.4722 0.1041  -0.0133 -0.0412 841  ARG A CB  
1414 C CG  . ARG A 185 ? 0.2853 0.3762 0.4855 0.0969  -0.0150 -0.0364 841  ARG A CG  
1415 C CD  . ARG A 185 ? 0.2166 0.3150 0.4126 0.0898  -0.0137 -0.0426 841  ARG A CD  
1416 N NE  . ARG A 185 ? 0.2903 0.4039 0.4892 0.0919  -0.0133 -0.0470 841  ARG A NE  
1417 C CZ  . ARG A 185 ? 0.3431 0.4597 0.5448 0.0929  -0.0109 -0.0547 841  ARG A CZ  
1418 N NH1 . ARG A 185 ? 0.1774 0.3094 0.3821 0.0948  -0.0104 -0.0578 841  ARG A NH1 
1419 N NH2 . ARG A 185 ? 0.2128 0.3179 0.4140 0.0914  -0.0090 -0.0595 841  ARG A NH2 
1420 N N   . GLU A 186 ? 0.2550 0.3465 0.4824 0.1278  -0.0133 -0.0411 842  GLU A N   
1421 C CA  . GLU A 186 ? 0.2540 0.3471 0.4903 0.1365  -0.0108 -0.0475 842  GLU A CA  
1422 C C   . GLU A 186 ? 0.3060 0.4005 0.5400 0.1316  -0.0069 -0.0595 842  GLU A C   
1423 O O   . GLU A 186 ? 0.2968 0.4033 0.5250 0.1239  -0.0069 -0.0620 842  GLU A O   
1424 C CB  . GLU A 186 ? 0.2660 0.3801 0.5086 0.1431  -0.0127 -0.0446 842  GLU A CB  
1425 C CG  . GLU A 186 ? 0.4313 0.5492 0.6854 0.1545  -0.0104 -0.0491 842  GLU A CG  
1426 C CD  . GLU A 186 ? 0.6551 0.7977 0.9154 0.1592  -0.0126 -0.0463 842  GLU A CD  
1427 O OE1 . GLU A 186 ? 0.6104 0.7561 0.8756 0.1662  -0.0161 -0.0371 842  GLU A OE1 
1428 O OE2 . GLU A 186 ? 0.4891 0.6488 0.7489 0.1554  -0.0109 -0.0527 842  GLU A OE2 
1429 N N   . GLY A 187 ? 0.2504 0.3312 0.4882 0.1355  -0.0037 -0.0665 843  GLY A N   
1430 C CA  . GLY A 187 ? 0.2418 0.3233 0.4774 0.1316  0.0002  -0.0784 843  GLY A CA  
1431 C C   . GLY A 187 ? 0.2676 0.3384 0.4944 0.1209  0.0005  -0.0813 843  GLY A C   
1432 O O   . GLY A 187 ? 0.2171 0.2841 0.4420 0.1180  0.0035  -0.0911 843  GLY A O   
1433 N N   . GLU A 188 ? 0.2639 0.3308 0.4854 0.1149  -0.0025 -0.0729 844  GLU A N   
1434 C CA  . GLU A 188 ? 0.2706 0.3301 0.4846 0.1048  -0.0027 -0.0740 844  GLU A CA  
1435 C C   . GLU A 188 ? 0.3770 0.4164 0.5919 0.1038  -0.0009 -0.0789 844  GLU A C   
1436 O O   . GLU A 188 ? 0.3686 0.4065 0.5791 0.0970  0.0004  -0.0862 844  GLU A O   
1437 C CB  . GLU A 188 ? 0.2804 0.3408 0.4899 0.1000  -0.0059 -0.0638 844  GLU A CB  
1438 C CG  . GLU A 188 ? 0.4096 0.4695 0.6119 0.0898  -0.0061 -0.0650 844  GLU A CG  
1439 C CD  . GLU A 188 ? 0.5369 0.5980 0.7351 0.0855  -0.0084 -0.0559 844  GLU A CD  
1440 O OE1 . GLU A 188 ? 0.3674 0.4169 0.5661 0.0859  -0.0092 -0.0498 844  GLU A OE1 
1441 O OE2 . GLU A 188 ? 0.3793 0.4530 0.5736 0.0816  -0.0092 -0.0551 844  GLU A OE2 
1442 N N   . CYS A 189 ? 0.3817 0.4060 0.6021 0.1104  -0.0010 -0.0749 845  CYS A N   
1443 C CA  . CYS A 189 ? 0.4189 0.4217 0.6410 0.1095  0.0008  -0.0789 845  CYS A CA  
1444 C C   . CYS A 189 ? 0.4569 0.4577 0.6806 0.1110  0.0046  -0.0929 845  CYS A C   
1445 O O   . CYS A 189 ? 0.4788 0.4681 0.6995 0.1045  0.0059  -0.0997 845  CYS A O   
1446 C CB  . CYS A 189 ? 0.4544 0.4420 0.6827 0.1173  -0.0001 -0.0706 845  CYS A CB  
1447 S SG  . CYS A 189 ? 0.5293 0.4872 0.7594 0.1145  0.0017  -0.0733 845  CYS A SG  
1448 N N   . GLN A 190 ? 0.3655 0.3791 0.5937 0.1188  0.0064  -0.0976 846  GLN A N   
1449 C CA  . GLN A 190 ? 0.3373 0.3525 0.5668 0.1208  0.0106  -0.1114 846  GLN A CA  
1450 C C   . GLN A 190 ? 0.3084 0.3373 0.5290 0.1104  0.0110  -0.1181 846  GLN A C   
1451 O O   . GLN A 190 ? 0.2975 0.3215 0.5150 0.1066  0.0137  -0.1291 846  GLN A O   
1452 C CB  . GLN A 190 ? 0.3413 0.3688 0.5790 0.1326  0.0126  -0.1133 846  GLN A CB  
1453 N N   . ARG A 191 ? 0.1974 0.2429 0.4136 0.1057  0.0083  -0.1111 847  ARG A N   
1454 C CA  . ARG A 191 ? 0.1861 0.2446 0.3940 0.0961  0.0080  -0.1145 847  ARG A CA  
1455 C C   . ARG A 191 ? 0.2153 0.2616 0.4174 0.0865  0.0070  -0.1161 847  ARG A C   
1456 O O   . ARG A 191 ? 0.2014 0.2528 0.3980 0.0800  0.0080  -0.1238 847  ARG A O   
1457 C CB  . ARG A 191 ? 0.1409 0.2147 0.3463 0.0935  0.0051  -0.1050 847  ARG A CB  
1458 C CG  . ARG A 191 ? 0.1170 0.2069 0.3156 0.0857  0.0052  -0.1078 847  ARG A CG  
1459 C CD  . ARG A 191 ? 0.1831 0.2856 0.3799 0.0835  0.0025  -0.0988 847  ARG A CD  
1460 N NE  . ARG A 191 ? 0.3200 0.4135 0.5144 0.0795  -0.0005 -0.0903 847  ARG A NE  
1461 C CZ  . ARG A 191 ? 0.5724 0.6724 0.7651 0.0776  -0.0029 -0.0823 847  ARG A CZ  
1462 N NH1 . ARG A 191 ? 0.4848 0.6000 0.6780 0.0786  -0.0029 -0.0812 847  ARG A NH1 
1463 N NH2 . ARG A 191 ? 0.4746 0.5662 0.6652 0.0743  -0.0049 -0.0757 847  ARG A NH2 
1464 N N   . TYR A 192 ? 0.1598 0.1912 0.3633 0.0856  0.0048  -0.1084 848  TYR A N   
1465 C CA  . TYR A 192 ? 0.1647 0.1853 0.3644 0.0767  0.0035  -0.1077 848  TYR A CA  
1466 C C   . TYR A 192 ? 0.2530 0.2577 0.4535 0.0749  0.0057  -0.1178 848  TYR A C   
1467 O O   . TYR A 192 ? 0.2542 0.2557 0.4503 0.0657  0.0049  -0.1208 848  TYR A O   
1468 C CB  . TYR A 192 ? 0.1837 0.1960 0.3849 0.0765  0.0008  -0.0952 848  TYR A CB  
1469 C CG  . TYR A 192 ? 0.2150 0.2199 0.4127 0.0668  -0.0007 -0.0929 848  TYR A CG  
1470 C CD1 . TYR A 192 ? 0.2293 0.2469 0.4218 0.0592  -0.0024 -0.0912 848  TYR A CD1 
1471 C CD2 . TYR A 192 ? 0.2330 0.2185 0.4336 0.0653  -0.0003 -0.0922 848  TYR A CD2 
1472 C CE1 . TYR A 192 ? 0.2572 0.2701 0.4478 0.0507  -0.0037 -0.0889 848  TYR A CE1 
1473 C CE2 . TYR A 192 ? 0.2411 0.2215 0.4393 0.0559  -0.0016 -0.0898 848  TYR A CE2 
1474 C CZ  . TYR A 192 ? 0.2743 0.2694 0.4678 0.0488  -0.0033 -0.0883 848  TYR A CZ  
1475 O OH  . TYR A 192 ? 0.2795 0.2721 0.4718 0.0400  -0.0046 -0.0861 848  TYR A OH  
1476 N N   . LYS A 193 ? 0.2835 0.2784 0.4899 0.0836  0.0086  -0.1234 849  LYS A N   
1477 C CA  . LYS A 193 ? 0.2941 0.2708 0.5022 0.0834  0.0115  -0.1340 849  LYS A CA  
1478 C C   . LYS A 193 ? 0.3457 0.3257 0.5463 0.0727  0.0120  -0.1451 849  LYS A C   
1479 O O   . LYS A 193 ? 0.3597 0.3239 0.5597 0.0663  0.0117  -0.1476 849  LYS A O   
1480 C CB  . LYS A 193 ? 0.3278 0.3007 0.5429 0.0953  0.0153  -0.1409 849  LYS A CB  
1481 C CG  . LYS A 193 ? 0.6783 0.6248 0.8980 0.0977  0.0178  -0.1471 849  LYS A CG  
1482 C CD  . LYS A 193 ? 0.8897 0.8313 1.1175 0.1108  0.0220  -0.1539 849  LYS A CD  
1483 C CE  . LYS A 193 ? 1.0036 0.9176 1.2354 0.1123  0.0250  -0.1623 849  LYS A CE  
1484 N NZ  . LYS A 193 ? 1.1322 1.0388 1.3740 0.1270  0.0289  -0.1666 849  LYS A NZ  
1485 N N   . PRO A 194 ? 0.2732 0.2733 0.4680 0.0695  0.0126  -0.1510 850  PRO A N   
1486 C CA  . PRO A 194 ? 0.2648 0.2678 0.4521 0.0590  0.0126  -0.1608 850  PRO A CA  
1487 C C   . PRO A 194 ? 0.2930 0.2945 0.4766 0.0481  0.0086  -0.1544 850  PRO A C   
1488 O O   . PRO A 194 ? 0.2841 0.2849 0.4628 0.0391  0.0080  -0.1619 850  PRO A O   
1489 C CB  . PRO A 194 ? 0.2743 0.3012 0.4562 0.0586  0.0136  -0.1649 850  PRO A CB  
1490 C CG  . PRO A 194 ? 0.3214 0.3544 0.5095 0.0700  0.0157  -0.1616 850  PRO A CG  
1491 C CD  . PRO A 194 ? 0.2673 0.2882 0.4619 0.0748  0.0134  -0.1495 850  PRO A CD  
1492 N N   . PHE A 195 ? 0.2421 0.2437 0.4282 0.0488  0.0058  -0.1410 851  PHE A N   
1493 C CA  . PHE A 195 ? 0.2348 0.2374 0.4188 0.0401  0.0023  -0.1332 851  PHE A CA  
1494 C C   . PHE A 195 ? 0.2943 0.2778 0.4835 0.0401  0.0016  -0.1261 851  PHE A C   
1495 O O   . PHE A 195 ? 0.2787 0.2621 0.4670 0.0327  -0.0008 -0.1201 851  PHE A O   
1496 C CB  . PHE A 195 ? 0.2398 0.2608 0.4216 0.0404  0.0000  -0.1232 851  PHE A CB  
1497 C CG  . PHE A 195 ? 0.2395 0.2795 0.4162 0.0400  0.0005  -0.1281 851  PHE A CG  
1498 C CD1 . PHE A 195 ? 0.2820 0.3329 0.4525 0.0313  -0.0011 -0.1318 851  PHE A CD1 
1499 C CD2 . PHE A 195 ? 0.2619 0.3099 0.4402 0.0480  0.0025  -0.1285 851  PHE A CD2 
1500 C CE1 . PHE A 195 ? 0.2897 0.3581 0.4550 0.0305  -0.0005 -0.1356 851  PHE A CE1 
1501 C CE2 . PHE A 195 ? 0.3014 0.3671 0.4750 0.0470  0.0034  -0.1329 851  PHE A CE2 
1502 C CZ  . PHE A 195 ? 0.2801 0.3555 0.4468 0.0382  0.0020  -0.1360 851  PHE A CZ  
1503 N N   . LYS A 196 ? 0.2820 0.2498 0.4769 0.0484  0.0039  -0.1265 852  LYS A N   
1504 C CA  . LYS A 196 ? 0.3014 0.2502 0.5014 0.0499  0.0035  -0.1186 852  LYS A CA  
1505 C C   . LYS A 196 ? 0.3837 0.3180 0.5835 0.0397  0.0031  -0.1213 852  LYS A C   
1506 O O   . LYS A 196 ? 0.3889 0.3148 0.5909 0.0370  0.0018  -0.1115 852  LYS A O   
1507 C CB  . LYS A 196 ? 0.3346 0.2699 0.5411 0.0618  0.0061  -0.1191 852  LYS A CB  
1508 C CG  . LYS A 196 ? 0.4733 0.3909 0.6825 0.0634  0.0094  -0.1317 852  LYS A CG  
1509 C CD  . LYS A 196 ? 0.5779 0.4831 0.7949 0.0766  0.0116  -0.1296 852  LYS A CD  
1510 C CE  . LYS A 196 ? 0.6206 0.5077 0.8408 0.0796  0.0156  -0.1430 852  LYS A CE  
1511 N NZ  . LYS A 196 ? 0.6662 0.5432 0.8953 0.0940  0.0178  -0.1406 852  LYS A NZ  
1512 N N   . GLN A 197 ? 0.3549 0.2873 0.5517 0.0335  0.0041  -0.1344 853  GLN A N   
1513 C CA  . GLN A 197 ? 0.3589 0.2788 0.5554 0.0225  0.0035  -0.1383 853  GLN A CA  
1514 C C   . GLN A 197 ? 0.3865 0.3243 0.5771 0.0110  0.0006  -0.1410 853  GLN A C   
1515 O O   . GLN A 197 ? 0.3798 0.3112 0.5698 0.0007  -0.0002 -0.1459 853  GLN A O   
1516 C CB  . GLN A 197 ? 0.3879 0.2872 0.5862 0.0234  0.0068  -0.1514 853  GLN A CB  
1517 C CG  . GLN A 197 ? 0.6122 0.4888 0.8180 0.0329  0.0091  -0.1466 853  GLN A CG  
1518 C CD  . GLN A 197 ? 0.9562 0.8150 1.1642 0.0370  0.0131  -0.1608 853  GLN A CD  
1519 O OE1 . GLN A 197 ? 0.9535 0.8128 1.1643 0.0487  0.0158  -0.1643 853  GLN A OE1 
1520 N NE2 . GLN A 197 ? 0.8529 0.6958 1.0601 0.0274  0.0138  -0.1697 853  GLN A NE2 
1521 N N   . LEU A 198 ? 0.3137 0.2740 0.5005 0.0125  -0.0010 -0.1370 854  LEU A N   
1522 C CA  . LEU A 198 ? 0.3025 0.2814 0.4844 0.0033  -0.0040 -0.1375 854  LEU A CA  
1523 C C   . LEU A 198 ? 0.3542 0.3315 0.5389 -0.0048 -0.0066 -0.1288 854  LEU A C   
1524 O O   . LEU A 198 ? 0.3488 0.3154 0.5382 -0.0019 -0.0061 -0.1195 854  LEU A O   
1525 C CB  . LEU A 198 ? 0.2864 0.2865 0.4650 0.0078  -0.0051 -0.1322 854  LEU A CB  
1526 C CG  . LEU A 198 ? 0.3228 0.3427 0.4949 0.0014  -0.0070 -0.1371 854  LEU A CG  
1527 C CD1 . LEU A 198 ? 0.3301 0.3505 0.4976 0.0016  -0.0046 -0.1516 854  LEU A CD1 
1528 C CD2 . LEU A 198 ? 0.3049 0.3428 0.4752 0.0053  -0.0083 -0.1284 854  LEU A CD2 
1529 N N   . HIS A 199 ? 0.3156 0.3040 0.4976 -0.0152 -0.0092 -0.1319 855  HIS A N   
1530 C CA  . HIS A 199 ? 0.3199 0.3103 0.5054 -0.0231 -0.0115 -0.1239 855  HIS A CA  
1531 C C   . HIS A 199 ? 0.3552 0.3617 0.5412 -0.0193 -0.0131 -0.1118 855  HIS A C   
1532 O O   . HIS A 199 ? 0.3558 0.3727 0.5386 -0.0127 -0.0129 -0.1113 855  HIS A O   
1533 C CB  . HIS A 199 ? 0.3336 0.3314 0.5169 -0.0355 -0.0141 -0.1315 855  HIS A CB  
1534 C CG  . HIS A 199 ? 0.3774 0.3988 0.5552 -0.0378 -0.0169 -0.1336 855  HIS A CG  
1535 N ND1 . HIS A 199 ? 0.4091 0.4368 0.5807 -0.0333 -0.0157 -0.1415 855  HIS A ND1 
1536 C CD2 . HIS A 199 ? 0.4000 0.4400 0.5781 -0.0443 -0.0206 -0.1284 855  HIS A CD2 
1537 C CE1 . HIS A 199 ? 0.3987 0.4480 0.5664 -0.0374 -0.0189 -0.1400 855  HIS A CE1 
1538 N NE2 . HIS A 199 ? 0.3987 0.4557 0.5703 -0.0436 -0.0221 -0.1322 855  HIS A NE2 
1539 N N   . ASN A 200 ? 0.2856 0.2939 0.4758 -0.0232 -0.0142 -0.1022 856  ASN A N   
1540 C CA  . ASN A 200 ? 0.2672 0.2892 0.4584 -0.0195 -0.0151 -0.0912 856  ASN A CA  
1541 C C   . ASN A 200 ? 0.3142 0.3314 0.5049 -0.0084 -0.0130 -0.0859 856  ASN A C   
1542 O O   . ASN A 200 ? 0.2901 0.3198 0.4781 -0.0036 -0.0135 -0.0835 856  ASN A O   
1543 C CB  . ASN A 200 ? 0.3008 0.3443 0.4886 -0.0217 -0.0178 -0.0921 856  ASN A CB  
1544 C CG  . ASN A 200 ? 0.6369 0.6930 0.8272 -0.0309 -0.0207 -0.0900 856  ASN A CG  
1545 O OD1 . ASN A 200 ? 0.4575 0.5182 0.6461 -0.0386 -0.0228 -0.0976 856  ASN A OD1 
1546 N ND2 . ASN A 200 ? 0.6423 0.7060 0.8367 -0.0299 -0.0211 -0.0798 856  ASN A ND2 
1547 N N   . ARG A 201 ? 0.2752 0.2749 0.4685 -0.0046 -0.0109 -0.0837 857  ARG A N   
1548 C CA  . ARG A 201 ? 0.2603 0.2575 0.4535 0.0054  -0.0095 -0.0775 857  ARG A CA  
1549 C C   . ARG A 201 ? 0.3133 0.3114 0.5088 0.0050  -0.0095 -0.0658 857  ARG A C   
1550 O O   . ARG A 201 ? 0.3081 0.2952 0.5069 0.0006  -0.0088 -0.0624 857  ARG A O   
1551 C CB  . ARG A 201 ? 0.2127 0.1925 0.4072 0.0119  -0.0074 -0.0813 857  ARG A CB  
1552 C CG  . ARG A 201 ? 0.2063 0.1878 0.3982 0.0144  -0.0067 -0.0931 857  ARG A CG  
1553 C CD  . ARG A 201 ? 0.1494 0.1123 0.3442 0.0204  -0.0042 -0.0978 857  ARG A CD  
1554 N NE  . ARG A 201 ? 0.3151 0.2596 0.5127 0.0140  -0.0036 -0.1004 857  ARG A NE  
1555 C CZ  . ARG A 201 ? 0.5158 0.4423 0.7177 0.0165  -0.0025 -0.0941 857  ARG A CZ  
1556 N NH1 . ARG A 201 ? 0.3571 0.2826 0.5608 0.0256  -0.0022 -0.0849 857  ARG A NH1 
1557 N NH2 . ARG A 201 ? 0.4240 0.3337 0.6285 0.0095  -0.0019 -0.0967 857  ARG A NH2 
1558 N N   . ARG A 202 ? 0.2562 0.2680 0.4501 0.0086  -0.0100 -0.0601 858  ARG A N   
1559 C CA  . ARG A 202 ? 0.2446 0.2602 0.4398 0.0084  -0.0096 -0.0500 858  ARG A CA  
1560 C C   . ARG A 202 ? 0.2458 0.2620 0.4391 0.0167  -0.0087 -0.0441 858  ARG A C   
1561 O O   . ARG A 202 ? 0.2243 0.2456 0.4151 0.0221  -0.0091 -0.0472 858  ARG A O   
1562 C CB  . ARG A 202 ? 0.2336 0.2657 0.4292 0.0037  -0.0108 -0.0484 858  ARG A CB  
1563 C CG  . ARG A 202 ? 0.3431 0.3759 0.5422 -0.0058 -0.0117 -0.0504 858  ARG A CG  
1564 C CD  . ARG A 202 ? 0.4227 0.4731 0.6235 -0.0094 -0.0132 -0.0480 858  ARG A CD  
1565 N NE  . ARG A 202 ? 0.5330 0.5883 0.7351 -0.0175 -0.0155 -0.0542 858  ARG A NE  
1566 C CZ  . ARG A 202 ? 0.7209 0.7921 0.9255 -0.0218 -0.0176 -0.0530 858  ARG A CZ  
1567 N NH1 . ARG A 202 ? 0.5729 0.6553 0.7793 -0.0185 -0.0172 -0.0459 858  ARG A NH1 
1568 N NH2 . ARG A 202 ? 0.6218 0.6979 0.8270 -0.0295 -0.0200 -0.0590 858  ARG A NH2 
1569 N N   . LEU A 203 ? 0.1823 0.1945 0.3764 0.0170  -0.0077 -0.0356 859  LEU A N   
1570 C CA  . LEU A 203 ? 0.1878 0.2021 0.3795 0.0239  -0.0071 -0.0294 859  LEU A CA  
1571 C C   . LEU A 203 ? 0.2159 0.2452 0.4061 0.0227  -0.0070 -0.0262 859  LEU A C   
1572 O O   . LEU A 203 ? 0.1914 0.2239 0.3833 0.0180  -0.0061 -0.0221 859  LEU A O   
1573 C CB  . LEU A 203 ? 0.1952 0.1977 0.3878 0.0248  -0.0060 -0.0218 859  LEU A CB  
1574 C CG  . LEU A 203 ? 0.2524 0.2564 0.4420 0.0322  -0.0060 -0.0158 859  LEU A CG  
1575 C CD1 . LEU A 203 ? 0.2517 0.2497 0.4419 0.0396  -0.0069 -0.0197 859  LEU A CD1 
1576 C CD2 . LEU A 203 ? 0.3042 0.3024 0.4935 0.0310  -0.0049 -0.0059 859  LEU A CD2 
1577 N N   . LEU A 204 ? 0.1641 0.2024 0.3516 0.0268  -0.0078 -0.0288 860  LEU A N   
1578 C CA  . LEU A 204 ? 0.1533 0.2042 0.3395 0.0263  -0.0077 -0.0270 860  LEU A CA  
1579 C C   . LEU A 204 ? 0.1897 0.2448 0.3722 0.0318  -0.0073 -0.0240 860  LEU A C   
1580 O O   . LEU A 204 ? 0.1901 0.2411 0.3710 0.0365  -0.0078 -0.0245 860  LEU A O   
1581 C CB  . LEU A 204 ? 0.1549 0.2138 0.3412 0.0242  -0.0091 -0.0329 860  LEU A CB  
1582 C CG  . LEU A 204 ? 0.2172 0.2758 0.4067 0.0176  -0.0101 -0.0366 860  LEU A CG  
1583 C CD1 . LEU A 204 ? 0.2118 0.2770 0.3998 0.0167  -0.0118 -0.0430 860  LEU A CD1 
1584 C CD2 . LEU A 204 ? 0.2410 0.3056 0.4341 0.0127  -0.0096 -0.0320 860  LEU A CD2 
1585 N N   . TRP A 205 ? 0.1209 0.1844 0.3024 0.0312  -0.0064 -0.0213 861  TRP A N   
1586 C CA  . TRP A 205 ? 0.1162 0.1844 0.2937 0.0350  -0.0058 -0.0191 861  TRP A CA  
1587 C C   . TRP A 205 ? 0.1621 0.2365 0.3379 0.0369  -0.0069 -0.0233 861  TRP A C   
1588 O O   . TRP A 205 ? 0.1375 0.2161 0.3150 0.0346  -0.0076 -0.0262 861  TRP A O   
1589 C CB  . TRP A 205 ? 0.0980 0.1716 0.2754 0.0333  -0.0036 -0.0152 861  TRP A CB  
1590 C CG  . TRP A 205 ? 0.1173 0.1874 0.2962 0.0306  -0.0019 -0.0102 861  TRP A CG  
1591 C CD1 . TRP A 205 ? 0.1510 0.2229 0.3345 0.0259  -0.0008 -0.0089 861  TRP A CD1 
1592 C CD2 . TRP A 205 ? 0.1171 0.1824 0.2927 0.0321  -0.0010 -0.0051 861  TRP A CD2 
1593 N NE1 . TRP A 205 ? 0.1486 0.2169 0.3319 0.0240  0.0011  -0.0034 861  TRP A NE1 
1594 C CE2 . TRP A 205 ? 0.1657 0.2294 0.3440 0.0278  0.0009  -0.0008 861  TRP A CE2 
1595 C CE3 . TRP A 205 ? 0.1275 0.1911 0.2985 0.0365  -0.0018 -0.0033 861  TRP A CE3 
1596 C CZ2 . TRP A 205 ? 0.1627 0.2221 0.3384 0.0276  0.0022  0.0058  861  TRP A CZ2 
1597 C CZ3 . TRP A 205 ? 0.1418 0.2017 0.3103 0.0367  -0.0010 0.0032  861  TRP A CZ3 
1598 C CH2 . TRP A 205 ? 0.1495 0.2067 0.3201 0.0323  0.0011  0.0078  861  TRP A CH2 
1599 N N   . HIS A 206 ? 0.1222 0.1983 0.2946 0.0406  -0.0071 -0.0229 862  HIS A N   
1600 C CA  . HIS A 206 ? 0.1075 0.1897 0.2779 0.0418  -0.0078 -0.0258 862  HIS A CA  
1601 C C   . HIS A 206 ? 0.1495 0.2343 0.3159 0.0440  -0.0073 -0.0234 862  HIS A C   
1602 O O   . HIS A 206 ? 0.1315 0.2154 0.2964 0.0468  -0.0082 -0.0222 862  HIS A O   
1603 C CB  . HIS A 206 ? 0.1078 0.1905 0.2788 0.0435  -0.0093 -0.0303 862  HIS A CB  
1604 C CG  . HIS A 206 ? 0.1320 0.2220 0.3012 0.0435  -0.0098 -0.0327 862  HIS A CG  
1605 N ND1 . HIS A 206 ? 0.1454 0.2391 0.3153 0.0408  -0.0101 -0.0350 862  HIS A ND1 
1606 C CD2 . HIS A 206 ? 0.1279 0.2222 0.2946 0.0452  -0.0100 -0.0325 862  HIS A CD2 
1607 C CE1 . HIS A 206 ? 0.1180 0.2171 0.2859 0.0410  -0.0103 -0.0358 862  HIS A CE1 
1608 N NE2 . HIS A 206 ? 0.1162 0.2157 0.2822 0.0433  -0.0102 -0.0348 862  HIS A NE2 
1609 N N   . GLY A 207 ? 0.1092 0.1974 0.2742 0.0426  -0.0059 -0.0228 863  GLY A N   
1610 C CA  . GLY A 207 ? 0.1075 0.1987 0.2680 0.0436  -0.0050 -0.0220 863  GLY A CA  
1611 C C   . GLY A 207 ? 0.1533 0.2484 0.3124 0.0437  -0.0061 -0.0255 863  GLY A C   
1612 O O   . GLY A 207 ? 0.1440 0.2400 0.3054 0.0425  -0.0066 -0.0277 863  GLY A O   
1613 N N   . SER A 208 ? 0.1376 0.2357 0.2926 0.0446  -0.0066 -0.0258 864  SER A N   
1614 C CA  . SER A 208 ? 0.1292 0.2315 0.2826 0.0437  -0.0074 -0.0290 864  SER A CA  
1615 C C   . SER A 208 ? 0.1562 0.2616 0.3044 0.0433  -0.0072 -0.0291 864  SER A C   
1616 O O   . SER A 208 ? 0.1501 0.2552 0.2955 0.0443  -0.0068 -0.0263 864  SER A O   
1617 C CB  . SER A 208 ? 0.1717 0.2772 0.3275 0.0451  -0.0096 -0.0306 864  SER A CB  
1618 O OG  . SER A 208 ? 0.2402 0.3493 0.3963 0.0429  -0.0099 -0.0335 864  SER A OG  
1619 N N   . ARG A 209 ? 0.1093 0.2178 0.2556 0.0412  -0.0075 -0.0322 865  ARG A N   
1620 C CA  . ARG A 209 ? 0.1295 0.2417 0.2703 0.0399  -0.0077 -0.0336 865  ARG A CA  
1621 C C   . ARG A 209 ? 0.1815 0.3005 0.3214 0.0419  -0.0106 -0.0319 865  ARG A C   
1622 O O   . ARG A 209 ? 0.1945 0.3156 0.3387 0.0442  -0.0124 -0.0311 865  ARG A O   
1623 C CB  . ARG A 209 ? 0.1857 0.2984 0.3254 0.0363  -0.0072 -0.0376 865  ARG A CB  
1624 C CG  . ARG A 209 ? 0.3098 0.4153 0.4501 0.0351  -0.0041 -0.0388 865  ARG A CG  
1625 C CD  . ARG A 209 ? 0.3642 0.4681 0.5070 0.0326  -0.0043 -0.0404 865  ARG A CD  
1626 N NE  . ARG A 209 ? 0.3871 0.4838 0.5308 0.0318  -0.0016 -0.0412 865  ARG A NE  
1627 C CZ  . ARG A 209 ? 0.6052 0.6982 0.7457 0.0293  0.0001  -0.0446 865  ARG A CZ  
1628 N NH1 . ARG A 209 ? 0.5706 0.6673 0.7061 0.0268  -0.0008 -0.0477 865  ARG A NH1 
1629 N NH2 . ARG A 209 ? 0.4637 0.5492 0.6063 0.0296  0.0027  -0.0449 865  ARG A NH2 
1630 N N   . THR A 210 ? 0.1340 0.2570 0.2683 0.0414  -0.0111 -0.0313 866  THR A N   
1631 C CA  . THR A 210 ? 0.1519 0.2826 0.2851 0.0436  -0.0143 -0.0285 866  THR A CA  
1632 C C   . THR A 210 ? 0.1992 0.3375 0.3359 0.0434  -0.0168 -0.0309 866  THR A C   
1633 O O   . THR A 210 ? 0.1993 0.3422 0.3398 0.0473  -0.0192 -0.0283 866  THR A O   
1634 C CB  . THR A 210 ? 0.2285 0.3635 0.3538 0.0420  -0.0143 -0.0278 866  THR A CB  
1635 O OG1 . THR A 210 ? 0.2741 0.4035 0.3980 0.0436  -0.0121 -0.0237 866  THR A OG1 
1636 C CG2 . THR A 210 ? 0.2864 0.4317 0.4100 0.0436  -0.0182 -0.0250 866  THR A CG2 
1637 N N   . THR A 211 ? 0.1739 0.3126 0.3104 0.0391  -0.0160 -0.0356 867  THR A N   
1638 C CA  . THR A 211 ? 0.1729 0.3196 0.3127 0.0372  -0.0177 -0.0382 867  THR A CA  
1639 C C   . THR A 211 ? 0.2141 0.3602 0.3607 0.0399  -0.0177 -0.0379 867  THR A C   
1640 O O   . THR A 211 ? 0.1876 0.3416 0.3373 0.0389  -0.0188 -0.0397 867  THR A O   
1641 C CB  . THR A 211 ? 0.3106 0.4557 0.4472 0.0309  -0.0164 -0.0428 867  THR A CB  
1642 O OG1 . THR A 211 ? 0.2973 0.4310 0.4338 0.0302  -0.0132 -0.0433 867  THR A OG1 
1643 C CG2 . THR A 211 ? 0.3130 0.4626 0.4429 0.0276  -0.0172 -0.0448 867  THR A CG2 
1644 N N   . ASN A 212 ? 0.1744 0.3119 0.3230 0.0427  -0.0162 -0.0361 868  ASN A N   
1645 C CA  . ASN A 212 ? 0.1530 0.2896 0.3070 0.0449  -0.0159 -0.0366 868  ASN A CA  
1646 C C   . ASN A 212 ? 0.1645 0.3029 0.3222 0.0506  -0.0174 -0.0344 868  ASN A C   
1647 O O   . ASN A 212 ? 0.1358 0.2767 0.2982 0.0529  -0.0174 -0.0361 868  ASN A O   
1648 C CB  . ASN A 212 ? 0.1181 0.2447 0.2724 0.0441  -0.0138 -0.0362 868  ASN A CB  
1649 C CG  . ASN A 212 ? 0.2917 0.4157 0.4446 0.0397  -0.0122 -0.0380 868  ASN A CG  
1650 O OD1 . ASN A 212 ? 0.2215 0.3420 0.3711 0.0376  -0.0110 -0.0380 868  ASN A OD1 
1651 N ND2 . ASN A 212 ? 0.0714 0.1967 0.2269 0.0383  -0.0120 -0.0393 868  ASN A ND2 
1652 N N   . PHE A 213 ? 0.1429 0.2792 0.2983 0.0531  -0.0182 -0.0305 869  PHE A N   
1653 C CA  . PHE A 213 ? 0.1433 0.2775 0.3019 0.0588  -0.0194 -0.0269 869  PHE A CA  
1654 C C   . PHE A 213 ? 0.1868 0.3309 0.3501 0.0632  -0.0217 -0.0267 869  PHE A C   
1655 O O   . PHE A 213 ? 0.1964 0.3370 0.3646 0.0685  -0.0219 -0.0255 869  PHE A O   
1656 C CB  . PHE A 213 ? 0.1655 0.2949 0.3198 0.0595  -0.0195 -0.0217 869  PHE A CB  
1657 C CG  . PHE A 213 ? 0.1814 0.2998 0.3350 0.0574  -0.0167 -0.0215 869  PHE A CG  
1658 C CD1 . PHE A 213 ? 0.2051 0.3219 0.3545 0.0529  -0.0147 -0.0230 869  PHE A CD1 
1659 C CD2 . PHE A 213 ? 0.2127 0.3229 0.3707 0.0597  -0.0160 -0.0206 869  PHE A CD2 
1660 C CE1 . PHE A 213 ? 0.2150 0.3239 0.3651 0.0513  -0.0123 -0.0226 869  PHE A CE1 
1661 C CE2 . PHE A 213 ? 0.2341 0.3361 0.3921 0.0570  -0.0138 -0.0205 869  PHE A CE2 
1662 C CZ  . PHE A 213 ? 0.2003 0.3026 0.3548 0.0530  -0.0121 -0.0212 869  PHE A CZ  
1663 N N   . ALA A 214 ? 0.1438 0.3001 0.3064 0.0611  -0.0233 -0.0284 870  ALA A N   
1664 C CA  . ALA A 214 ? 0.1212 0.2892 0.2899 0.0655  -0.0254 -0.0285 870  ALA A CA  
1665 C C   . ALA A 214 ? 0.1602 0.3279 0.3345 0.0666  -0.0233 -0.0330 870  ALA A C   
1666 O O   . ALA A 214 ? 0.1705 0.3397 0.3510 0.0728  -0.0234 -0.0330 870  ALA A O   
1667 C CB  . ALA A 214 ? 0.1261 0.3086 0.2930 0.0618  -0.0276 -0.0295 870  ALA A CB  
1668 N N   . GLY A 215 ? 0.1144 0.2789 0.2863 0.0609  -0.0212 -0.0367 871  GLY A N   
1669 C CA  . GLY A 215 ? 0.1030 0.2676 0.2783 0.0606  -0.0191 -0.0409 871  GLY A CA  
1670 C C   . GLY A 215 ? 0.1500 0.3029 0.3270 0.0643  -0.0177 -0.0411 871  GLY A C   
1671 O O   . GLY A 215 ? 0.1397 0.2943 0.3214 0.0679  -0.0166 -0.0442 871  GLY A O   
1672 N N   . ILE A 216 ? 0.1200 0.2615 0.2934 0.0631  -0.0174 -0.0383 872  ILE A N   
1673 C CA  . ILE A 216 ? 0.1134 0.2429 0.2881 0.0652  -0.0162 -0.0381 872  ILE A CA  
1674 C C   . ILE A 216 ? 0.1521 0.2792 0.3316 0.0724  -0.0170 -0.0365 872  ILE A C   
1675 O O   . ILE A 216 ? 0.1393 0.2612 0.3225 0.0750  -0.0157 -0.0396 872  ILE A O   
1676 C CB  . ILE A 216 ? 0.1437 0.2632 0.3140 0.0619  -0.0156 -0.0349 872  ILE A CB  
1677 C CG1 . ILE A 216 ? 0.1382 0.2583 0.3054 0.0558  -0.0144 -0.0369 872  ILE A CG1 
1678 C CG2 . ILE A 216 ? 0.1078 0.2155 0.2804 0.0637  -0.0147 -0.0343 872  ILE A CG2 
1679 C CD1 . ILE A 216 ? 0.0599 0.1570 0.2030 0.0450  -0.0136 -0.0339 872  ILE A CD1 
1680 N N   . LEU A 217 ? 0.1348 0.2656 0.3144 0.0756  -0.0191 -0.0316 873  LEU A N   
1681 C CA  . LEU A 217 ? 0.1473 0.2753 0.3322 0.0832  -0.0201 -0.0289 873  LEU A CA  
1682 C C   . LEU A 217 ? 0.2061 0.3435 0.3981 0.0884  -0.0199 -0.0330 873  LEU A C   
1683 O O   . LEU A 217 ? 0.2122 0.3432 0.4096 0.0944  -0.0190 -0.0339 873  LEU A O   
1684 C CB  . LEU A 217 ? 0.1469 0.2772 0.3298 0.0856  -0.0228 -0.0213 873  LEU A CB  
1685 C CG  . LEU A 217 ? 0.2055 0.3261 0.3819 0.0817  -0.0224 -0.0167 873  LEU A CG  
1686 C CD1 . LEU A 217 ? 0.1988 0.3251 0.3718 0.0832  -0.0252 -0.0095 873  LEU A CD1 
1687 C CD2 . LEU A 217 ? 0.2438 0.3484 0.4222 0.0827  -0.0206 -0.0158 873  LEU A CD2 
1688 N N   . SER A 218 ? 0.1608 0.3128 0.3530 0.0859  -0.0202 -0.0359 874  SER A N   
1689 C CA  . SER A 218 ? 0.1616 0.3248 0.3611 0.0907  -0.0196 -0.0398 874  SER A CA  
1690 C C   . SER A 218 ? 0.1990 0.3606 0.3996 0.0889  -0.0162 -0.0472 874  SER A C   
1691 O O   . SER A 218 ? 0.2067 0.3704 0.4136 0.0949  -0.0146 -0.0509 874  SER A O   
1692 C CB  . SER A 218 ? 0.2236 0.4057 0.4242 0.0891  -0.0216 -0.0391 874  SER A CB  
1693 O OG  . SER A 218 ? 0.3694 0.5573 0.5660 0.0809  -0.0205 -0.0427 874  SER A OG  
1694 N N   . GLN A 219 ? 0.1154 0.2737 0.3099 0.0811  -0.0150 -0.0493 875  GLN A N   
1695 C CA  . GLN A 219 ? 0.1021 0.2610 0.2961 0.0782  -0.0122 -0.0556 875  GLN A CA  
1696 C C   . GLN A 219 ? 0.1696 0.3136 0.3602 0.0758  -0.0111 -0.0569 875  GLN A C   
1697 O O   . GLN A 219 ? 0.1680 0.3119 0.3580 0.0740  -0.0090 -0.0623 875  GLN A O   
1698 C CB  . GLN A 219 ? 0.1082 0.2772 0.2983 0.0707  -0.0120 -0.0565 875  GLN A CB  
1699 C CG  . GLN A 219 ? 0.2791 0.4639 0.4719 0.0707  -0.0134 -0.0551 875  GLN A CG  
1700 C CD  . GLN A 219 ? 0.6319 0.8315 0.8309 0.0737  -0.0117 -0.0594 875  GLN A CD  
1701 O OE1 . GLN A 219 ? 0.7081 0.9208 0.9071 0.0689  -0.0113 -0.0603 875  GLN A OE1 
1702 N NE2 . GLN A 219 ? 0.4099 0.6079 0.6147 0.0815  -0.0104 -0.0621 875  GLN A NE2 
1703 N N   . GLY A 220 ? 0.1371 0.2701 0.3251 0.0751  -0.0124 -0.0520 876  GLY A N   
1704 C CA  . GLY A 220 ? 0.1361 0.2558 0.3215 0.0722  -0.0116 -0.0525 876  GLY A CA  
1705 C C   . GLY A 220 ? 0.1988 0.3201 0.3790 0.0647  -0.0115 -0.0523 876  GLY A C   
1706 O O   . GLY A 220 ? 0.2083 0.3393 0.3867 0.0619  -0.0118 -0.0521 876  GLY A O   
1707 N N   . LEU A 221 ? 0.1589 0.2704 0.3371 0.0615  -0.0112 -0.0519 877  LEU A N   
1708 C CA  . LEU A 221 ? 0.1349 0.2475 0.3093 0.0553  -0.0110 -0.0516 877  LEU A CA  
1709 C C   . LEU A 221 ? 0.1750 0.2953 0.3490 0.0533  -0.0101 -0.0568 877  LEU A C   
1710 O O   . LEU A 221 ? 0.1823 0.3022 0.3582 0.0556  -0.0090 -0.0618 877  LEU A O   
1711 C CB  . LEU A 221 ? 0.1293 0.2316 0.3031 0.0528  -0.0110 -0.0500 877  LEU A CB  
1712 C CG  . LEU A 221 ? 0.1679 0.2644 0.3409 0.0530  -0.0115 -0.0440 877  LEU A CG  
1713 C CD1 . LEU A 221 ? 0.1673 0.2555 0.3408 0.0500  -0.0111 -0.0428 877  LEU A CD1 
1714 C CD2 . LEU A 221 ? 0.1338 0.2361 0.3038 0.0509  -0.0117 -0.0411 877  LEU A CD2 
1715 N N   . ARG A 222 ? 0.1298 0.2575 0.3011 0.0493  -0.0102 -0.0557 878  ARG A N   
1716 C CA  . ARG A 222 ? 0.1070 0.2440 0.2772 0.0469  -0.0093 -0.0593 878  ARG A CA  
1717 C C   . ARG A 222 ? 0.1472 0.2847 0.3137 0.0412  -0.0097 -0.0570 878  ARG A C   
1718 O O   . ARG A 222 ? 0.1293 0.2618 0.2950 0.0397  -0.0106 -0.0526 878  ARG A O   
1719 C CB  . ARG A 222 ? 0.0586 0.1693 0.1891 0.0349  -0.0111 -0.0586 878  ARG A CB  
1720 C CG  . ARG A 222 ? 0.0931 0.2438 0.2692 0.0542  -0.0085 -0.0619 878  ARG A CG  
1721 C CD  . ARG A 222 ? 0.1901 0.3539 0.3682 0.0544  -0.0085 -0.0615 878  ARG A CD  
1722 N NE  . ARG A 222 ? 0.3782 0.5412 0.5548 0.0525  -0.0104 -0.0566 878  ARG A NE  
1723 C CZ  . ARG A 222 ? 0.4237 0.5970 0.6012 0.0509  -0.0110 -0.0556 878  ARG A CZ  
1724 N NH1 . ARG A 222 ? 0.2772 0.4636 0.4578 0.0511  -0.0098 -0.0586 878  ARG A NH1 
1725 N NH2 . ARG A 222 ? 0.2113 0.3826 0.3865 0.0487  -0.0126 -0.0521 878  ARG A NH2 
1726 N N   . ILE A 223 ? 0.1387 0.2829 0.3032 0.0383  -0.0091 -0.0600 879  ILE A N   
1727 C CA  . ILE A 223 ? 0.1452 0.2917 0.3063 0.0330  -0.0098 -0.0573 879  ILE A CA  
1728 C C   . ILE A 223 ? 0.1995 0.3537 0.3592 0.0304  -0.0094 -0.0546 879  ILE A C   
1729 O O   . ILE A 223 ? 0.2204 0.3820 0.3812 0.0317  -0.0082 -0.0572 879  ILE A O   
1730 C CB  . ILE A 223 ? 0.1851 0.3361 0.3439 0.0309  -0.0094 -0.0621 879  ILE A CB  
1731 C CG1 . ILE A 223 ? 0.1927 0.3351 0.3532 0.0326  -0.0098 -0.0655 879  ILE A CG1 
1732 C CG2 . ILE A 223 ? 0.1793 0.3360 0.3342 0.0255  -0.0106 -0.0585 879  ILE A CG2 
1733 C CD1 . ILE A 223 ? 0.2718 0.4175 0.4306 0.0321  -0.0086 -0.0733 879  ILE A CD1 
1734 N N   . ALA A 224 ? 0.1595 0.3120 0.3173 0.0268  -0.0103 -0.0493 880  ALA A N   
1735 C CA  . ALA A 224 ? 0.1594 0.3168 0.3157 0.0233  -0.0100 -0.0460 880  ALA A CA  
1736 C C   . ALA A 224 ? 0.2062 0.3758 0.3605 0.0208  -0.0087 -0.0487 880  ALA A C   
1737 O O   . ALA A 224 ? 0.1915 0.3643 0.3439 0.0204  -0.0087 -0.0516 880  ALA A O   
1738 C CB  . ALA A 224 ? 0.1704 0.3228 0.3255 0.0204  -0.0110 -0.0401 880  ALA A CB  
1739 N N   . PRO A 225 ? 0.1718 0.3490 0.3262 0.0186  -0.0076 -0.0484 881  PRO A N   
1740 C CA  . PRO A 225 ? 0.1628 0.3534 0.3156 0.0164  -0.0058 -0.0513 881  PRO A CA  
1741 C C   . PRO A 225 ? 0.2121 0.4074 0.3599 0.0112  -0.0060 -0.0481 881  PRO A C   
1742 O O   . PRO A 225 ? 0.1936 0.3816 0.3400 0.0093  -0.0078 -0.0424 881  PRO A O   
1743 C CB  . PRO A 225 ? 0.1789 0.3763 0.3339 0.0146  -0.0048 -0.0505 881  PRO A CB  
1744 C CG  . PRO A 225 ? 0.2317 0.4186 0.3871 0.0133  -0.0063 -0.0458 881  PRO A CG  
1745 C CD  . PRO A 225 ? 0.1822 0.3573 0.3383 0.0177  -0.0077 -0.0460 881  PRO A CD  
1746 N N   . PRO A 226 ? 0.1782 0.3862 0.3231 0.0090  -0.0041 -0.0512 882  PRO A N   
1747 C CA  . PRO A 226 ? 0.1708 0.3845 0.3099 0.0037  -0.0047 -0.0473 882  PRO A CA  
1748 C C   . PRO A 226 ? 0.2074 0.4192 0.3449 -0.0015 -0.0056 -0.0381 882  PRO A C   
1749 O O   . PRO A 226 ? 0.2030 0.4147 0.3367 -0.0044 -0.0073 -0.0328 882  PRO A O   
1750 C CB  . PRO A 226 ? 0.1916 0.4208 0.3281 0.0024  -0.0017 -0.0530 882  PRO A CB  
1751 C CG  . PRO A 226 ? 0.2574 0.4859 0.3990 0.0088  -0.0001 -0.0613 882  PRO A CG  
1752 C CD  . PRO A 226 ? 0.1979 0.4167 0.3450 0.0116  -0.0014 -0.0584 882  PRO A CD  
1753 N N   . GLU A 227 ? 0.1692 0.3794 0.3096 -0.0027 -0.0048 -0.0361 883  GLU A N   
1754 C CA  . GLU A 227 ? 0.1661 0.3722 0.3056 -0.0079 -0.0053 -0.0280 883  GLU A CA  
1755 C C   . GLU A 227 ? 0.2222 0.4131 0.3627 -0.0062 -0.0077 -0.0228 883  GLU A C   
1756 O O   . GLU A 227 ? 0.2290 0.4158 0.3679 -0.0097 -0.0085 -0.0153 883  GLU A O   
1757 C CB  . GLU A 227 ? 0.1751 0.3829 0.3178 -0.0099 -0.0038 -0.0288 883  GLU A CB  
1758 C CG  . GLU A 227 ? 0.2338 0.4588 0.3760 -0.0135 -0.0011 -0.0313 883  GLU A CG  
1759 C CD  . GLU A 227 ? 0.4627 0.6977 0.6075 -0.0082 0.0005  -0.0402 883  GLU A CD  
1760 O OE1 . GLU A 227 ? 0.3120 0.5625 0.4559 -0.0103 0.0032  -0.0428 883  GLU A OE1 
1761 O OE2 . GLU A 227 ? 0.4128 0.6403 0.5609 -0.0018 -0.0006 -0.0443 883  GLU A OE2 
1762 N N   . ALA A 228 ? 0.1548 0.3376 0.2983 -0.0005 -0.0086 -0.0267 884  ALA A N   
1763 C CA  . ALA A 228 ? 0.1525 0.3223 0.2980 0.0022  -0.0104 -0.0233 884  ALA A CA  
1764 C C   . ALA A 228 ? 0.1837 0.3533 0.3272 0.0012  -0.0123 -0.0177 884  ALA A C   
1765 O O   . ALA A 228 ? 0.1580 0.3365 0.2986 0.0005  -0.0129 -0.0197 884  ALA A O   
1766 C CB  . ALA A 228 ? 0.1566 0.3212 0.3051 0.0077  -0.0106 -0.0287 884  ALA A CB  
1767 N N   . PRO A 229 ? 0.1657 0.3257 0.3109 0.0012  -0.0133 -0.0109 885  PRO A N   
1768 C CA  . PRO A 229 ? 0.1819 0.3426 0.3265 0.0011  -0.0156 -0.0045 885  PRO A CA  
1769 C C   . PRO A 229 ? 0.2631 0.4234 0.4098 0.0051  -0.0171 -0.0076 885  PRO A C   
1770 O O   . PRO A 229 ? 0.2741 0.4255 0.4250 0.0090  -0.0167 -0.0094 885  PRO A O   
1771 C CB  . PRO A 229 ? 0.2089 0.3577 0.3565 0.0015  -0.0156 0.0026  885  PRO A CB  
1772 C CG  . PRO A 229 ? 0.2594 0.3992 0.4095 0.0033  -0.0136 -0.0024 885  PRO A CG  
1773 C CD  . PRO A 229 ? 0.1937 0.3421 0.3417 0.0017  -0.0123 -0.0094 885  PRO A CD  
1774 N N   . VAL A 230 ? 0.2283 0.3989 0.3720 0.0036  -0.0187 -0.0087 886  VAL A N   
1775 C CA  . VAL A 230 ? 0.2359 0.4076 0.3812 0.0058  -0.0204 -0.0122 886  VAL A CA  
1776 C C   . VAL A 230 ? 0.2639 0.4290 0.4145 0.0086  -0.0222 -0.0061 886  VAL A C   
1777 O O   . VAL A 230 ? 0.2402 0.4016 0.3945 0.0114  -0.0225 -0.0092 886  VAL A O   
1778 C CB  . VAL A 230 ? 0.3033 0.4880 0.4432 0.0024  -0.0218 -0.0151 886  VAL A CB  
1779 C CG1 . VAL A 230 ? 0.3115 0.5048 0.4470 -0.0018 -0.0233 -0.0072 886  VAL A CG1 
1780 C CG2 . VAL A 230 ? 0.3062 0.4922 0.4479 0.0033  -0.0239 -0.0185 886  VAL A CG2 
1781 N N   . THR A 231 ? 0.2081 0.3702 0.3597 0.0083  -0.0228 0.0024  887  THR A N   
1782 C CA  . THR A 231 ? 0.2093 0.3656 0.3669 0.0118  -0.0240 0.0087  887  THR A CA  
1783 C C   . THR A 231 ? 0.2615 0.4046 0.4238 0.0158  -0.0214 0.0066  887  THR A C   
1784 O O   . THR A 231 ? 0.2240 0.3625 0.3920 0.0196  -0.0217 0.0098  887  THR A O   
1785 C CB  . THR A 231 ? 0.2700 0.4279 0.4274 0.0105  -0.0258 0.0192  887  THR A CB  
1786 O OG1 . THR A 231 ? 0.2406 0.3904 0.3967 0.0091  -0.0236 0.0216  887  THR A OG1 
1787 C CG2 . THR A 231 ? 0.2401 0.4127 0.3920 0.0063  -0.0288 0.0221  887  THR A CG2 
1788 N N   . GLY A 232 ? 0.2295 0.3683 0.3896 0.0151  -0.0189 0.0008  888  GLY A N   
1789 C CA  . GLY A 232 ? 0.2288 0.3567 0.3919 0.0182  -0.0165 -0.0020 888  GLY A CA  
1790 C C   . GLY A 232 ? 0.2714 0.3984 0.4372 0.0214  -0.0161 -0.0069 888  GLY A C   
1791 O O   . GLY A 232 ? 0.2761 0.3954 0.4436 0.0239  -0.0142 -0.0092 888  GLY A O   
1792 N N   . TYR A 233 ? 0.2096 0.3444 0.3750 0.0208  -0.0180 -0.0088 889  TYR A N   
1793 C CA  . TYR A 233 ? 0.1810 0.3154 0.3486 0.0226  -0.0178 -0.0133 889  TYR A CA  
1794 C C   . TYR A 233 ? 0.1907 0.3316 0.3611 0.0221  -0.0204 -0.0107 889  TYR A C   
1795 O O   . TYR A 233 ? 0.1771 0.3266 0.3447 0.0190  -0.0226 -0.0093 889  TYR A O   
1796 C CB  . TYR A 233 ? 0.1889 0.3256 0.3527 0.0214  -0.0173 -0.0203 889  TYR A CB  
1797 C CG  . TYR A 233 ? 0.2171 0.3524 0.3780 0.0207  -0.0156 -0.0222 889  TYR A CG  
1798 C CD1 . TYR A 233 ? 0.2350 0.3767 0.3923 0.0174  -0.0159 -0.0210 889  TYR A CD1 
1799 C CD2 . TYR A 233 ? 0.2250 0.3538 0.3866 0.0230  -0.0138 -0.0247 889  TYR A CD2 
1800 C CE1 . TYR A 233 ? 0.2355 0.3773 0.3909 0.0161  -0.0143 -0.0225 889  TYR A CE1 
1801 C CE2 . TYR A 233 ? 0.2334 0.3629 0.3928 0.0218  -0.0127 -0.0265 889  TYR A CE2 
1802 C CZ  . TYR A 233 ? 0.2641 0.4001 0.4208 0.0183  -0.0129 -0.0255 889  TYR A CZ  
1803 O OH  . TYR A 233 ? 0.2617 0.3997 0.4170 0.0165  -0.0117 -0.0271 889  TYR A OH  
1804 N N   . MET A 234 ? 0.1303 0.2687 0.3059 0.0245  -0.0200 -0.0102 890  MET A N   
1805 C CA  . MET A 234 ? 0.1235 0.2691 0.3035 0.0241  -0.0224 -0.0072 890  MET A CA  
1806 C C   . MET A 234 ? 0.1719 0.3268 0.3486 0.0197  -0.0252 -0.0102 890  MET A C   
1807 O O   . MET A 234 ? 0.1408 0.3049 0.3183 0.0178  -0.0282 -0.0061 890  MET A O   
1808 C CB  . MET A 234 ? 0.1452 0.2874 0.3311 0.0267  -0.0208 -0.0077 890  MET A CB  
1809 C CG  . MET A 234 ? 0.1844 0.3349 0.3769 0.0270  -0.0230 -0.0028 890  MET A CG  
1810 S SD  . MET A 234 ? 0.2358 0.3844 0.4356 0.0294  -0.0206 -0.0033 890  MET A SD  
1811 C CE  . MET A 234 ? 0.1814 0.3452 0.3885 0.0272  -0.0246 0.0012  890  MET A CE  
1812 N N   . PHE A 235 ? 0.1417 0.2944 0.3148 0.0181  -0.0242 -0.0175 891  PHE A N   
1813 C CA  . PHE A 235 ? 0.1256 0.2852 0.2953 0.0140  -0.0261 -0.0224 891  PHE A CA  
1814 C C   . PHE A 235 ? 0.1892 0.3500 0.3522 0.0127  -0.0250 -0.0271 891  PHE A C   
1815 O O   . PHE A 235 ? 0.1805 0.3425 0.3404 0.0108  -0.0248 -0.0341 891  PHE A O   
1816 C CB  . PHE A 235 ? 0.1447 0.3005 0.3173 0.0134  -0.0257 -0.0273 891  PHE A CB  
1817 C CG  . PHE A 235 ? 0.1783 0.3372 0.3578 0.0133  -0.0270 -0.0228 891  PHE A CG  
1818 C CD1 . PHE A 235 ? 0.2146 0.3851 0.3956 0.0100  -0.0306 -0.0201 891  PHE A CD1 
1819 C CD2 . PHE A 235 ? 0.2085 0.3604 0.3930 0.0165  -0.0247 -0.0211 891  PHE A CD2 
1820 C CE1 . PHE A 235 ? 0.2175 0.3928 0.4060 0.0101  -0.0319 -0.0158 891  PHE A CE1 
1821 C CE2 . PHE A 235 ? 0.2362 0.3926 0.4277 0.0166  -0.0254 -0.0172 891  PHE A CE2 
1822 C CZ  . PHE A 235 ? 0.2079 0.3761 0.4019 0.0135  -0.0290 -0.0145 891  PHE A CZ  
1823 N N   . GLY A 236 ? 0.1430 0.3036 0.3040 0.0136  -0.0242 -0.0232 892  GLY A N   
1824 C CA  . GLY A 236 ? 0.1246 0.2881 0.2800 0.0121  -0.0229 -0.0267 892  GLY A CA  
1825 C C   . GLY A 236 ? 0.1894 0.3456 0.3451 0.0149  -0.0200 -0.0323 892  GLY A C   
1826 O O   . GLY A 236 ? 0.1878 0.3357 0.3474 0.0179  -0.0190 -0.0321 892  GLY A O   
1827 N N   . LYS A 237 ? 0.1588 0.3195 0.3107 0.0139  -0.0188 -0.0372 893  LYS A N   
1828 C CA  . LYS A 237 ? 0.1440 0.3004 0.2966 0.0168  -0.0163 -0.0419 893  LYS A CA  
1829 C C   . LYS A 237 ? 0.1773 0.3304 0.3310 0.0187  -0.0156 -0.0492 893  LYS A C   
1830 O O   . LYS A 237 ? 0.1721 0.3304 0.3231 0.0177  -0.0149 -0.0551 893  LYS A O   
1831 C CB  . LYS A 237 ? 0.1746 0.3384 0.3238 0.0152  -0.0149 -0.0425 893  LYS A CB  
1832 C CG  . LYS A 237 ? 0.1988 0.3618 0.3480 0.0137  -0.0150 -0.0353 893  LYS A CG  
1833 C CD  . LYS A 237 ? 0.3331 0.5037 0.4794 0.0113  -0.0134 -0.0357 893  LYS A CD  
1834 C CE  . LYS A 237 ? 0.3339 0.5158 0.4752 0.0069  -0.0138 -0.0348 893  LYS A CE  
1835 N NZ  . LYS A 237 ? 0.2141 0.4046 0.3528 0.0041  -0.0117 -0.0351 893  LYS A NZ  
1836 N N   . GLY A 238 ? 0.1328 0.2767 0.2904 0.0214  -0.0156 -0.0486 894  GLY A N   
1837 C CA  . GLY A 238 ? 0.1386 0.2763 0.2981 0.0234  -0.0149 -0.0539 894  GLY A CA  
1838 C C   . GLY A 238 ? 0.1986 0.3275 0.3613 0.0274  -0.0139 -0.0518 894  GLY A C   
1839 O O   . GLY A 238 ? 0.2055 0.3346 0.3683 0.0285  -0.0135 -0.0480 894  GLY A O   
1840 N N   . ILE A 239 ? 0.1380 0.2593 0.3031 0.0291  -0.0136 -0.0542 895  ILE A N   
1841 C CA  . ILE A 239 ? 0.1171 0.2305 0.2847 0.0326  -0.0129 -0.0515 895  ILE A CA  
1842 C C   . ILE A 239 ? 0.1496 0.2586 0.3195 0.0306  -0.0135 -0.0481 895  ILE A C   
1843 O O   . ILE A 239 ? 0.1059 0.2131 0.2769 0.0281  -0.0141 -0.0506 895  ILE A O   
1844 C CB  . ILE A 239 ? 0.1377 0.2456 0.3068 0.0368  -0.0118 -0.0551 895  ILE A CB  
1845 C CG1 . ILE A 239 ? 0.1080 0.2227 0.2760 0.0389  -0.0110 -0.0593 895  ILE A CG1 
1846 C CG2 . ILE A 239 ? 0.1449 0.2472 0.3154 0.0399  -0.0115 -0.0505 895  ILE A CG2 
1847 C CD1 . ILE A 239 ? 0.1440 0.2542 0.3145 0.0433  -0.0098 -0.0642 895  ILE A CD1 
1848 N N   . TYR A 240 ? 0.1358 0.2440 0.3065 0.0313  -0.0132 -0.0428 896  TYR A N   
1849 C CA  . TYR A 240 ? 0.1152 0.2217 0.2887 0.0297  -0.0132 -0.0391 896  TYR A CA  
1850 C C   . TYR A 240 ? 0.1715 0.2705 0.3467 0.0313  -0.0120 -0.0374 896  TYR A C   
1851 O O   . TYR A 240 ? 0.1726 0.2688 0.3463 0.0344  -0.0110 -0.0364 896  TYR A O   
1852 C CB  . TYR A 240 ? 0.1218 0.2321 0.2956 0.0298  -0.0130 -0.0346 896  TYR A CB  
1853 C CG  . TYR A 240 ? 0.1337 0.2512 0.3066 0.0276  -0.0146 -0.0340 896  TYR A CG  
1854 C CD1 . TYR A 240 ? 0.1501 0.2712 0.3194 0.0272  -0.0149 -0.0364 896  TYR A CD1 
1855 C CD2 . TYR A 240 ? 0.1327 0.2543 0.3086 0.0261  -0.0156 -0.0301 896  TYR A CD2 
1856 C CE1 . TYR A 240 ? 0.1441 0.2723 0.3119 0.0248  -0.0162 -0.0347 896  TYR A CE1 
1857 C CE2 . TYR A 240 ? 0.1331 0.2617 0.3081 0.0243  -0.0173 -0.0282 896  TYR A CE2 
1858 C CZ  . TYR A 240 ? 0.1508 0.2822 0.3212 0.0234  -0.0176 -0.0303 896  TYR A CZ  
1859 O OH  . TYR A 240 ? 0.1422 0.2807 0.3110 0.0213  -0.0193 -0.0274 896  TYR A OH  
1860 N N   . PHE A 241 ? 0.1191 0.2158 0.2972 0.0287  -0.0122 -0.0368 897  PHE A N   
1861 C CA  . PHE A 241 ? 0.1101 0.1998 0.2900 0.0291  -0.0109 -0.0344 897  PHE A CA  
1862 C C   . PHE A 241 ? 0.1566 0.2494 0.3403 0.0261  -0.0104 -0.0306 897  PHE A C   
1863 O O   . PHE A 241 ? 0.1519 0.2514 0.3378 0.0234  -0.0117 -0.0309 897  PHE A O   
1864 C CB  . PHE A 241 ? 0.1250 0.2074 0.3057 0.0280  -0.0113 -0.0380 897  PHE A CB  
1865 C CG  . PHE A 241 ? 0.1268 0.2062 0.3053 0.0319  -0.0113 -0.0417 897  PHE A CG  
1866 C CD1 . PHE A 241 ? 0.1548 0.2284 0.3328 0.0362  -0.0105 -0.0394 897  PHE A CD1 
1867 C CD2 . PHE A 241 ? 0.1387 0.2225 0.3156 0.0315  -0.0121 -0.0471 897  PHE A CD2 
1868 C CE1 . PHE A 241 ? 0.1444 0.2170 0.3215 0.0405  -0.0106 -0.0424 897  PHE A CE1 
1869 C CE2 . PHE A 241 ? 0.1622 0.2449 0.3379 0.0356  -0.0117 -0.0507 897  PHE A CE2 
1870 C CZ  . PHE A 241 ? 0.1277 0.2051 0.3041 0.0403  -0.0110 -0.0482 897  PHE A CZ  
1871 N N   . ALA A 242 ? 0.0981 0.1871 0.2828 0.0266  -0.0086 -0.0269 898  ALA A N   
1872 C CA  . ALA A 242 ? 0.0649 0.1576 0.2538 0.0241  -0.0073 -0.0231 898  ALA A CA  
1873 C C   . ALA A 242 ? 0.1226 0.2090 0.3133 0.0214  -0.0063 -0.0212 898  ALA A C   
1874 O O   . ALA A 242 ? 0.1379 0.2161 0.3259 0.0233  -0.0059 -0.0210 898  ALA A O   
1875 C CB  . ALA A 242 ? 0.0618 0.1581 0.2498 0.0272  -0.0050 -0.0199 898  ALA A CB  
1876 N N   . ASP A 243 ? 0.0997 0.1902 0.2955 0.0170  -0.0058 -0.0192 899  ASP A N   
1877 C CA  . ASP A 243 ? 0.0968 0.1819 0.2950 0.0132  -0.0045 -0.0165 899  ASP A CA  
1878 C C   . ASP A 243 ? 0.1620 0.2512 0.3610 0.0140  -0.0012 -0.0108 899  ASP A C   
1879 O O   . ASP A 243 ? 0.1881 0.2736 0.3884 0.0110  0.0004  -0.0073 899  ASP A O   
1880 C CB  . ASP A 243 ? 0.1045 0.1913 0.3078 0.0064  -0.0063 -0.0187 899  ASP A CB  
1881 C CG  . ASP A 243 ? 0.2057 0.3063 0.4144 0.0037  -0.0072 -0.0181 899  ASP A CG  
1882 O OD1 . ASP A 243 ? 0.2190 0.3276 0.4294 0.0068  -0.0055 -0.0146 899  ASP A OD1 
1883 O OD2 . ASP A 243 ? 0.2189 0.3226 0.4305 -0.0016 -0.0096 -0.0212 899  ASP A OD2 
1884 N N   . MET A 244 ? 0.1168 0.2136 0.3152 0.0179  0.0001  -0.0101 900  MET A N   
1885 C CA  . MET A 244 ? 0.1172 0.2185 0.3154 0.0196  0.0038  -0.0062 900  MET A CA  
1886 C C   . MET A 244 ? 0.1578 0.2547 0.3485 0.0245  0.0045  -0.0066 900  MET A C   
1887 O O   . MET A 244 ? 0.1517 0.2497 0.3402 0.0276  0.0034  -0.0096 900  MET A O   
1888 C CB  . MET A 244 ? 0.1346 0.2473 0.3381 0.0207  0.0050  -0.0059 900  MET A CB  
1889 C CG  . MET A 244 ? 0.1778 0.2988 0.3899 0.0159  0.0042  -0.0047 900  MET A CG  
1890 S SD  . MET A 244 ? 0.2247 0.3478 0.4412 0.0101  0.0072  -0.0002 900  MET A SD  
1891 C CE  . MET A 244 ? 0.1633 0.2982 0.3834 0.0137  0.0121  0.0027  900  MET A CE  
1892 N N   . VAL A 245 ? 0.0941 0.1865 0.2807 0.0246  0.0062  -0.0032 901  VAL A N   
1893 C CA  . VAL A 245 ? 0.0919 0.1815 0.2711 0.0286  0.0065  -0.0030 901  VAL A CA  
1894 C C   . VAL A 245 ? 0.1420 0.2376 0.3188 0.0318  0.0080  -0.0054 901  VAL A C   
1895 O O   . VAL A 245 ? 0.1567 0.2504 0.3290 0.0345  0.0065  -0.0080 901  VAL A O   
1896 C CB  . VAL A 245 ? 0.1525 0.2390 0.3277 0.0278  0.0082  0.0025  901  VAL A CB  
1897 C CG1 . VAL A 245 ? 0.1416 0.2357 0.3170 0.0262  0.0126  0.0057  901  VAL A CG1 
1898 C CG2 . VAL A 245 ? 0.1466 0.2299 0.3145 0.0317  0.0068  0.0027  901  VAL A CG2 
1899 N N   . SER A 246 ? 0.0916 0.1942 0.2718 0.0314  0.0113  -0.0046 902  SER A N   
1900 C CA  . SER A 246 ? 0.0770 0.1839 0.2558 0.0345  0.0136  -0.0071 902  SER A CA  
1901 C C   . SER A 246 ? 0.1487 0.2550 0.3297 0.0362  0.0110  -0.0108 902  SER A C   
1902 O O   . SER A 246 ? 0.1557 0.2609 0.3329 0.0387  0.0114  -0.0135 902  SER A O   
1903 C CB  . SER A 246 ? 0.1116 0.2262 0.2951 0.0341  0.0180  -0.0054 902  SER A CB  
1904 O OG  . SER A 246 ? 0.1085 0.2278 0.3011 0.0318  0.0171  -0.0041 902  SER A OG  
1905 N N   . LYS A 247 ? 0.1187 0.2256 0.3052 0.0343  0.0081  -0.0108 903  LYS A N   
1906 C CA  . LYS A 247 ? 0.1121 0.2192 0.2998 0.0354  0.0054  -0.0134 903  LYS A CA  
1907 C C   . LYS A 247 ? 0.1777 0.2793 0.3588 0.0367  0.0034  -0.0161 903  LYS A C   
1908 O O   . LYS A 247 ? 0.1658 0.2673 0.3454 0.0383  0.0029  -0.0181 903  LYS A O   
1909 C CB  . LYS A 247 ? 0.1246 0.2348 0.3180 0.0324  0.0026  -0.0131 903  LYS A CB  
1910 C CG  . LYS A 247 ? 0.0901 0.2025 0.2846 0.0334  0.0000  -0.0146 903  LYS A CG  
1911 C CD  . LYS A 247 ? 0.1108 0.2286 0.3104 0.0300  -0.0029 -0.0143 903  LYS A CD  
1912 C CE  . LYS A 247 ? 0.2759 0.3947 0.4736 0.0305  -0.0059 -0.0159 903  LYS A CE  
1913 N NZ  . LYS A 247 ? 0.2002 0.3276 0.4032 0.0281  -0.0086 -0.0144 903  LYS A NZ  
1914 N N   . SER A 248 ? 0.1390 0.2362 0.3168 0.0359  0.0023  -0.0158 904  SER A N   
1915 C CA  . SER A 248 ? 0.1248 0.2185 0.2976 0.0375  0.0003  -0.0179 904  SER A CA  
1916 C C   . SER A 248 ? 0.1733 0.2672 0.3403 0.0394  0.0020  -0.0179 904  SER A C   
1917 O O   . SER A 248 ? 0.1682 0.2623 0.3321 0.0405  0.0009  -0.0205 904  SER A O   
1918 C CB  . SER A 248 ? 0.1287 0.2176 0.3013 0.0368  -0.0014 -0.0174 904  SER A CB  
1919 O OG  . SER A 248 ? 0.1851 0.2737 0.3613 0.0351  -0.0035 -0.0198 904  SER A OG  
1920 N N   . ALA A 249 ? 0.1307 0.2255 0.2961 0.0392  0.0047  -0.0152 905  ALA A N   
1921 C CA  . ALA A 249 ? 0.1362 0.2324 0.2951 0.0404  0.0064  -0.0154 905  ALA A CA  
1922 C C   . ALA A 249 ? 0.1833 0.2812 0.3411 0.0413  0.0080  -0.0193 905  ALA A C   
1923 O O   . ALA A 249 ? 0.1604 0.2587 0.3123 0.0418  0.0083  -0.0215 905  ALA A O   
1924 C CB  . ALA A 249 ? 0.1485 0.2465 0.3058 0.0395  0.0093  -0.0116 905  ALA A CB  
1925 N N   . ASN A 250 ? 0.1371 0.2356 0.3009 0.0415  0.0087  -0.0201 906  ASN A N   
1926 C CA  . ASN A 250 ? 0.1336 0.2316 0.2978 0.0427  0.0100  -0.0231 906  ASN A CA  
1927 C C   . ASN A 250 ? 0.1597 0.2552 0.3209 0.0422  0.0070  -0.0257 906  ASN A C   
1928 O O   . ASN A 250 ? 0.1635 0.2570 0.3221 0.0424  0.0081  -0.0286 906  ASN A O   
1929 C CB  . ASN A 250 ? 0.1048 0.2047 0.2770 0.0435  0.0108  -0.0218 906  ASN A CB  
1930 C CG  . ASN A 250 ? 0.2904 0.3945 0.4668 0.0444  0.0146  -0.0200 906  ASN A CG  
1931 O OD1 . ASN A 250 ? 0.2986 0.4064 0.4827 0.0451  0.0148  -0.0181 906  ASN A OD1 
1932 N ND2 . ASN A 250 ? 0.0996 0.2049 0.2715 0.0445  0.0178  -0.0203 906  ASN A ND2 
1933 N N   . TYR A 251 ? 0.1222 0.2177 0.2837 0.0414  0.0037  -0.0250 907  TYR A N   
1934 C CA  . TYR A 251 ? 0.1155 0.2107 0.2745 0.0409  0.0011  -0.0273 907  TYR A CA  
1935 C C   . TYR A 251 ? 0.1777 0.2740 0.3306 0.0409  0.0005  -0.0286 907  TYR A C   
1936 O O   . TYR A 251 ? 0.1703 0.2681 0.3215 0.0402  -0.0014 -0.0307 907  TYR A O   
1937 C CB  . TYR A 251 ? 0.1091 0.2050 0.2711 0.0404  -0.0018 -0.0268 907  TYR A CB  
1938 C CG  . TYR A 251 ? 0.1120 0.2089 0.2785 0.0395  -0.0023 -0.0264 907  TYR A CG  
1939 C CD1 . TYR A 251 ? 0.1397 0.2370 0.3058 0.0387  -0.0030 -0.0275 907  TYR A CD1 
1940 C CD2 . TYR A 251 ? 0.1091 0.2071 0.2803 0.0390  -0.0021 -0.0243 907  TYR A CD2 
1941 C CE1 . TYR A 251 ? 0.1715 0.2703 0.3413 0.0380  -0.0038 -0.0260 907  TYR A CE1 
1942 C CE2 . TYR A 251 ? 0.1090 0.2096 0.2843 0.0382  -0.0031 -0.0233 907  TYR A CE2 
1943 C CZ  . TYR A 251 ? 0.1509 0.2519 0.3253 0.0379  -0.0040 -0.0239 907  TYR A CZ  
1944 O OH  . TYR A 251 ? 0.1868 0.2910 0.3649 0.0372  -0.0053 -0.0218 907  TYR A OH  
1945 N N   . CYS A 252 ? 0.1440 0.2410 0.2935 0.0414  0.0021  -0.0272 908  CYS A N   
1946 C CA  . CYS A 252 ? 0.1560 0.2558 0.2991 0.0413  0.0014  -0.0279 908  CYS A CA  
1947 C C   . CYS A 252 ? 0.2382 0.3382 0.3770 0.0398  0.0029  -0.0323 908  CYS A C   
1948 O O   . CYS A 252 ? 0.2616 0.3649 0.3958 0.0387  0.0012  -0.0342 908  CYS A O   
1949 C CB  . CYS A 252 ? 0.1531 0.2541 0.2933 0.0420  0.0026  -0.0242 908  CYS A CB  
1950 S SG  . CYS A 252 ? 0.2126 0.3111 0.3574 0.0431  0.0008  -0.0190 908  CYS A SG  
1951 N N   . HIS A 253 ? 0.2158 0.3125 0.3568 0.0398  0.0060  -0.0340 909  HIS A N   
1952 C CA  . HIS A 253 ? 0.2345 0.3285 0.3726 0.0386  0.0083  -0.0387 909  HIS A CA  
1953 C C   . HIS A 253 ? 0.2816 0.3788 0.4113 0.0373  0.0095  -0.0414 909  HIS A C   
1954 O O   . HIS A 253 ? 0.3027 0.4002 0.4276 0.0348  0.0088  -0.0456 909  HIS A O   
1955 C CB  . HIS A 253 ? 0.2642 0.3558 0.4037 0.0367  0.0062  -0.0409 909  HIS A CB  
1956 C CG  . HIS A 253 ? 0.3206 0.4093 0.4671 0.0377  0.0059  -0.0386 909  HIS A CG  
1957 N ND1 . HIS A 253 ? 0.3483 0.4317 0.4981 0.0386  0.0085  -0.0392 909  HIS A ND1 
1958 C CD2 . HIS A 253 ? 0.3481 0.4390 0.4986 0.0380  0.0032  -0.0356 909  HIS A CD2 
1959 C CE1 . HIS A 253 ? 0.3413 0.4250 0.4968 0.0393  0.0068  -0.0358 909  HIS A CE1 
1960 N NE2 . HIS A 253 ? 0.3445 0.4328 0.5002 0.0386  0.0037  -0.0341 909  HIS A NE2 
1961 N N   . THR A 254 ? 0.1934 0.2938 0.3210 0.0385  0.0112  -0.0386 910  THR A N   
1962 C CA  . THR A 254 ? 0.1866 0.2915 0.3056 0.0373  0.0126  -0.0401 910  THR A CA  
1963 C C   . THR A 254 ? 0.2363 0.3384 0.3533 0.0372  0.0179  -0.0455 910  THR A C   
1964 O O   . THR A 254 ? 0.2432 0.3401 0.3668 0.0390  0.0202  -0.0464 910  THR A O   
1965 C CB  . THR A 254 ? 0.2277 0.3369 0.3454 0.0384  0.0125  -0.0338 910  THR A CB  
1966 O OG1 . THR A 254 ? 0.2368 0.3439 0.3612 0.0399  0.0154  -0.0310 910  THR A OG1 
1967 C CG2 . THR A 254 ? 0.1637 0.2750 0.2824 0.0389  0.0075  -0.0290 910  THR A CG2 
1968 N N   . SER A 255 ? 0.1947 0.3006 0.3027 0.0354  0.0198  -0.0491 911  SER A N   
1969 C CA  . SER A 255 ? 0.1903 0.2939 0.2954 0.0355  0.0255  -0.0556 911  SER A CA  
1970 C C   . SER A 255 ? 0.2611 0.3726 0.3558 0.0338  0.0274  -0.0566 911  SER A C   
1971 O O   . SER A 255 ? 0.2732 0.3914 0.3641 0.0329  0.0241  -0.0511 911  SER A O   
1972 C CB  . SER A 255 ? 0.2553 0.3519 0.3593 0.0334  0.0256  -0.0630 911  SER A CB  
1973 O OG  . SER A 255 ? 0.3773 0.4777 0.4745 0.0293  0.0213  -0.0649 911  SER A OG  
1974 N N   . GLN A 256 ? 0.2479 0.3588 0.3381 0.0336  0.0329  -0.0634 912  GLN A N   
1975 C CA  . GLN A 256 ? 0.2643 0.3834 0.3430 0.0315  0.0356  -0.0659 912  GLN A CA  
1976 C C   . GLN A 256 ? 0.3464 0.4704 0.4154 0.0269  0.0307  -0.0682 912  GLN A C   
1977 O O   . GLN A 256 ? 0.3309 0.4648 0.3908 0.0250  0.0297  -0.0658 912  GLN A O   
1978 C CB  . GLN A 256 ? 0.2866 0.4024 0.3633 0.0324  0.0430  -0.0749 912  GLN A CB  
1979 C CG  . GLN A 256 ? 0.4637 0.5817 0.5467 0.0365  0.0489  -0.0721 912  GLN A CG  
1980 C CD  . GLN A 256 ? 0.5480 0.6578 0.6449 0.0410  0.0502  -0.0708 912  GLN A CD  
1981 O OE1 . GLN A 256 ? 0.4465 0.5497 0.5496 0.0411  0.0455  -0.0686 912  GLN A OE1 
1982 N NE2 . GLN A 256 ? 0.3596 0.4712 0.4622 0.0448  0.0563  -0.0715 912  GLN A NE2 
1983 N N   . GLY A 257 ? 0.3525 0.4706 0.4241 0.0251  0.0275  -0.0721 913  GLY A N   
1984 C CA  . GLY A 257 ? 0.3665 0.4894 0.4312 0.0205  0.0226  -0.0747 913  GLY A CA  
1985 C C   . GLY A 257 ? 0.4260 0.5550 0.4938 0.0209  0.0157  -0.0664 913  GLY A C   
1986 O O   . GLY A 257 ? 0.4236 0.5592 0.4867 0.0175  0.0112  -0.0676 913  GLY A O   
1987 N N   . ASP A 258 ? 0.3733 0.5000 0.4497 0.0252  0.0150  -0.0583 914  ASP A N   
1988 C CA  . ASP A 258 ? 0.3525 0.4832 0.4332 0.0268  0.0094  -0.0503 914  ASP A CA  
1989 C C   . ASP A 258 ? 0.3322 0.4600 0.4195 0.0309  0.0110  -0.0429 914  ASP A C   
1990 O O   . ASP A 258 ? 0.3122 0.4334 0.4087 0.0329  0.0108  -0.0416 914  ASP A O   
1991 C CB  . ASP A 258 ? 0.3853 0.5126 0.4726 0.0261  0.0058  -0.0520 914  ASP A CB  
1992 C CG  . ASP A 258 ? 0.6204 0.7521 0.7124 0.0282  0.0004  -0.0451 914  ASP A CG  
1993 O OD1 . ASP A 258 ? 0.6382 0.7768 0.7270 0.0297  -0.0017 -0.0393 914  ASP A OD1 
1994 O OD2 . ASP A 258 ? 0.7351 0.8635 0.8341 0.0286  -0.0014 -0.0455 914  ASP A OD2 
1995 N N   . PRO A 259 ? 0.2594 0.3921 0.3420 0.0314  0.0129  -0.0383 915  PRO A N   
1996 C CA  . PRO A 259 ? 0.2423 0.3718 0.3315 0.0341  0.0150  -0.0319 915  PRO A CA  
1997 C C   . PRO A 259 ? 0.2820 0.4113 0.3757 0.0359  0.0106  -0.0233 915  PRO A C   
1998 O O   . PRO A 259 ? 0.2848 0.4119 0.3829 0.0371  0.0122  -0.0178 915  PRO A O   
1999 C CB  . PRO A 259 ? 0.2621 0.3972 0.3440 0.0330  0.0199  -0.0315 915  PRO A CB  
2000 C CG  . PRO A 259 ? 0.3090 0.4525 0.3791 0.0302  0.0178  -0.0334 915  PRO A CG  
2001 C CD  . PRO A 259 ? 0.2574 0.3994 0.3281 0.0290  0.0136  -0.0387 915  PRO A CD  
2002 N N   . ILE A 260 ? 0.2405 0.3723 0.3338 0.0362  0.0053  -0.0223 916  ILE A N   
2003 C CA  . ILE A 260 ? 0.2253 0.3564 0.3231 0.0388  0.0013  -0.0148 916  ILE A CA  
2004 C C   . ILE A 260 ? 0.2514 0.3762 0.3587 0.0405  -0.0006 -0.0166 916  ILE A C   
2005 O O   . ILE A 260 ? 0.1985 0.3245 0.3065 0.0396  -0.0024 -0.0217 916  ILE A O   
2006 C CB  . ILE A 260 ? 0.2616 0.4014 0.3532 0.0393  -0.0033 -0.0106 916  ILE A CB  
2007 C CG1 . ILE A 260 ? 0.2691 0.4179 0.3487 0.0363  -0.0019 -0.0113 916  ILE A CG1 
2008 C CG2 . ILE A 260 ? 0.2441 0.3816 0.3400 0.0427  -0.0061 -0.0011 916  ILE A CG2 
2009 C CD1 . ILE A 260 ? 0.3507 0.5000 0.4258 0.0354  0.0027  -0.0070 916  ILE A CD1 
2010 N N   . GLY A 261 ? 0.2431 0.3617 0.3574 0.0422  -0.0001 -0.0127 917  GLY A N   
2011 C CA  . GLY A 261 ? 0.2349 0.3482 0.3577 0.0435  -0.0017 -0.0143 917  GLY A CA  
2012 C C   . GLY A 261 ? 0.2406 0.3511 0.3678 0.0463  -0.0046 -0.0090 917  GLY A C   
2013 O O   . GLY A 261 ? 0.2299 0.3409 0.3546 0.0474  -0.0053 -0.0028 917  GLY A O   
2014 N N   . LEU A 262 ? 0.1648 0.2720 0.2985 0.0475  -0.0062 -0.0114 918  LEU A N   
2015 C CA  . LEU A 262 ? 0.1409 0.2440 0.2798 0.0504  -0.0085 -0.0084 918  LEU A CA  
2016 C C   . LEU A 262 ? 0.1796 0.2760 0.3251 0.0497  -0.0073 -0.0106 918  LEU A C   
2017 O O   . LEU A 262 ? 0.1850 0.2822 0.3322 0.0481  -0.0066 -0.0153 918  LEU A O   
2018 C CB  . LEU A 262 ? 0.1219 0.2303 0.2619 0.0531  -0.0121 -0.0099 918  LEU A CB  
2019 C CG  . LEU A 262 ? 0.1514 0.2680 0.2862 0.0545  -0.0145 -0.0066 918  LEU A CG  
2020 C CD1 . LEU A 262 ? 0.1138 0.2383 0.2511 0.0563  -0.0177 -0.0095 918  LEU A CD1 
2021 C CD2 . LEU A 262 ? 0.1744 0.2878 0.3090 0.0575  -0.0156 0.0014  918  LEU A CD2 
2022 N N   . ILE A 263 ? 0.1397 0.2296 0.2886 0.0504  -0.0073 -0.0069 919  ILE A N   
2023 C CA  . ILE A 263 ? 0.1445 0.2289 0.2992 0.0488  -0.0065 -0.0092 919  ILE A CA  
2024 C C   . ILE A 263 ? 0.2056 0.2831 0.3645 0.0511  -0.0081 -0.0080 919  ILE A C   
2025 O O   . ILE A 263 ? 0.2225 0.2964 0.3806 0.0532  -0.0088 -0.0027 919  ILE A O   
2026 C CB  . ILE A 263 ? 0.1814 0.2646 0.3367 0.0453  -0.0034 -0.0073 919  ILE A CB  
2027 C CG1 . ILE A 263 ? 0.1654 0.2461 0.3266 0.0430  -0.0030 -0.0103 919  ILE A CG1 
2028 C CG2 . ILE A 263 ? 0.2235 0.3032 0.3772 0.0448  -0.0024 -0.0006 919  ILE A CG2 
2029 C CD1 . ILE A 263 ? 0.2829 0.3658 0.4457 0.0400  -0.0002 -0.0093 919  ILE A CD1 
2030 N N   . LEU A 264 ? 0.1510 0.2264 0.3142 0.0509  -0.0086 -0.0129 920  LEU A N   
2031 C CA  . LEU A 264 ? 0.1460 0.2139 0.3133 0.0532  -0.0097 -0.0134 920  LEU A CA  
2032 C C   . LEU A 264 ? 0.1960 0.2560 0.3665 0.0495  -0.0085 -0.0131 920  LEU A C   
2033 O O   . LEU A 264 ? 0.1744 0.2372 0.3453 0.0453  -0.0072 -0.0142 920  LEU A O   
2034 C CB  . LEU A 264 ? 0.1373 0.2083 0.3070 0.0550  -0.0108 -0.0198 920  LEU A CB  
2035 C CG  . LEU A 264 ? 0.1982 0.2779 0.3663 0.0581  -0.0122 -0.0210 920  LEU A CG  
2036 C CD1 . LEU A 264 ? 0.1861 0.2712 0.3556 0.0571  -0.0122 -0.0274 920  LEU A CD1 
2037 C CD2 . LEU A 264 ? 0.2131 0.2912 0.3830 0.0638  -0.0137 -0.0180 920  LEU A CD2 
2038 N N   . LEU A 265 ? 0.1679 0.2183 0.3414 0.0511  -0.0089 -0.0120 921  LEU A N   
2039 C CA  . LEU A 265 ? 0.1759 0.2169 0.3532 0.0474  -0.0081 -0.0132 921  LEU A CA  
2040 C C   . LEU A 265 ? 0.2281 0.2640 0.4086 0.0503  -0.0090 -0.0194 921  LEU A C   
2041 O O   . LEU A 265 ? 0.2118 0.2433 0.3935 0.0559  -0.0098 -0.0180 921  LEU A O   
2042 C CB  . LEU A 265 ? 0.1816 0.2133 0.3593 0.0463  -0.0073 -0.0058 921  LEU A CB  
2043 C CG  . LEU A 265 ? 0.2322 0.2675 0.4085 0.0410  -0.0054 -0.0013 921  LEU A CG  
2044 C CD1 . LEU A 265 ? 0.2390 0.2658 0.4149 0.0400  -0.0045 0.0071  921  LEU A CD1 
2045 C CD2 . LEU A 265 ? 0.2386 0.2755 0.4184 0.0350  -0.0046 -0.0058 921  LEU A CD2 
2046 N N   . GLY A 266 ? 0.1819 0.2202 0.3636 0.0470  -0.0090 -0.0261 922  GLY A N   
2047 C CA  . GLY A 266 ? 0.1727 0.2078 0.3566 0.0492  -0.0093 -0.0334 922  GLY A CA  
2048 C C   . GLY A 266 ? 0.2474 0.2741 0.4338 0.0443  -0.0088 -0.0380 922  GLY A C   
2049 O O   . GLY A 266 ? 0.2400 0.2689 0.4264 0.0380  -0.0087 -0.0374 922  GLY A O   
2050 N N   . GLU A 267 ? 0.2138 0.2312 0.4027 0.0470  -0.0084 -0.0429 923  GLU A N   
2051 C CA  . GLU A 267 ? 0.2054 0.2145 0.3960 0.0419  -0.0079 -0.0491 923  GLU A CA  
2052 C C   . GLU A 267 ? 0.2502 0.2700 0.4388 0.0404  -0.0082 -0.0575 923  GLU A C   
2053 O O   . GLU A 267 ? 0.2372 0.2613 0.4254 0.0457  -0.0079 -0.0617 923  GLU A O   
2054 C CB  . GLU A 267 ? 0.2347 0.2272 0.4289 0.0456  -0.0069 -0.0513 923  GLU A CB  
2055 C CG  . GLU A 267 ? 0.3445 0.3284 0.5400 0.0396  -0.0062 -0.0599 923  GLU A CG  
2056 C CD  . GLU A 267 ? 0.4815 0.4477 0.6805 0.0434  -0.0048 -0.0646 923  GLU A CD  
2057 O OE1 . GLU A 267 ? 0.3105 0.2682 0.5122 0.0503  -0.0044 -0.0584 923  GLU A OE1 
2058 O OE2 . GLU A 267 ? 0.4236 0.3844 0.6229 0.0395  -0.0040 -0.0743 923  GLU A OE2 
2059 N N   . VAL A 268 ? 0.1947 0.2204 0.3821 0.0330  -0.0090 -0.0593 924  VAL A N   
2060 C CA  . VAL A 268 ? 0.1782 0.2157 0.3629 0.0304  -0.0097 -0.0655 924  VAL A CA  
2061 C C   . VAL A 268 ? 0.2478 0.2807 0.4327 0.0243  -0.0099 -0.0735 924  VAL A C   
2062 O O   . VAL A 268 ? 0.2123 0.2411 0.3990 0.0180  -0.0105 -0.0720 924  VAL A O   
2063 C CB  . VAL A 268 ? 0.2036 0.2542 0.3866 0.0276  -0.0109 -0.0601 924  VAL A CB  
2064 C CG1 . VAL A 268 ? 0.1851 0.2482 0.3651 0.0255  -0.0119 -0.0646 924  VAL A CG1 
2065 C CG2 . VAL A 268 ? 0.1945 0.2476 0.3770 0.0327  -0.0105 -0.0528 924  VAL A CG2 
2066 N N   . ALA A 269 ? 0.2229 0.2574 0.4059 0.0259  -0.0092 -0.0824 925  ALA A N   
2067 C CA  . ALA A 269 ? 0.2106 0.2423 0.3924 0.0201  -0.0092 -0.0919 925  ALA A CA  
2068 C C   . ALA A 269 ? 0.2447 0.2928 0.4228 0.0137  -0.0115 -0.0923 925  ALA A C   
2069 O O   . ALA A 269 ? 0.2355 0.2956 0.4098 0.0152  -0.0116 -0.0948 925  ALA A O   
2070 C CB  . ALA A 269 ? 0.2182 0.2465 0.3990 0.0251  -0.0070 -0.1013 925  ALA A CB  
2071 N N   . LEU A 270 ? 0.1781 0.2276 0.3579 0.0068  -0.0133 -0.0886 926  LEU A N   
2072 C CA  . LEU A 270 ? 0.1663 0.2317 0.3442 0.0012  -0.0158 -0.0872 926  LEU A CA  
2073 C C   . LEU A 270 ? 0.2296 0.3000 0.4040 -0.0055 -0.0172 -0.0966 926  LEU A C   
2074 O O   . LEU A 270 ? 0.2082 0.2937 0.3789 -0.0079 -0.0191 -0.0969 926  LEU A O   
2075 C CB  . LEU A 270 ? 0.1611 0.2289 0.3433 -0.0025 -0.0171 -0.0786 926  LEU A CB  
2076 C CG  . LEU A 270 ? 0.2103 0.2766 0.3948 0.0032  -0.0159 -0.0691 926  LEU A CG  
2077 C CD1 . LEU A 270 ? 0.2000 0.2664 0.3892 -0.0010 -0.0162 -0.0624 926  LEU A CD1 
2078 C CD2 . LEU A 270 ? 0.2144 0.2930 0.3961 0.0074  -0.0164 -0.0657 926  LEU A CD2 
2079 N N   . GLY A 271 ? 0.2257 0.2833 0.4009 -0.0086 -0.0162 -0.1043 927  GLY A N   
2080 C CA  . GLY A 271 ? 0.2390 0.3003 0.4104 -0.0159 -0.0173 -0.1147 927  GLY A CA  
2081 C C   . GLY A 271 ? 0.3143 0.3912 0.4854 -0.0241 -0.0212 -0.1113 927  GLY A C   
2082 O O   . GLY A 271 ? 0.2980 0.3763 0.4742 -0.0259 -0.0224 -0.1027 927  GLY A O   
2083 N N   . ASN A 272 ? 0.2930 0.3838 0.4582 -0.0283 -0.0231 -0.1172 928  ASN A N   
2084 C CA  . ASN A 272 ? 0.2877 0.3963 0.4522 -0.0357 -0.0274 -0.1140 928  ASN A CA  
2085 C C   . ASN A 272 ? 0.2849 0.4060 0.4505 -0.0306 -0.0286 -0.1024 928  ASN A C   
2086 O O   . ASN A 272 ? 0.2746 0.4018 0.4355 -0.0258 -0.0278 -0.1021 928  ASN A O   
2087 C CB  . ASN A 272 ? 0.3570 0.4758 0.5136 -0.0416 -0.0289 -0.1246 928  ASN A CB  
2088 C CG  . ASN A 272 ? 0.7452 0.8796 0.9011 -0.0516 -0.0338 -0.1245 928  ASN A CG  
2089 O OD1 . ASN A 272 ? 0.6456 0.7918 0.8059 -0.0526 -0.0368 -0.1143 928  ASN A OD1 
2090 N ND2 . ASN A 272 ? 0.7174 0.8533 0.8678 -0.0591 -0.0347 -0.1364 928  ASN A ND2 
2091 N N   . MET A 273 ? 0.2052 0.3293 0.3774 -0.0314 -0.0300 -0.0931 929  MET A N   
2092 C CA  . MET A 273 ? 0.1776 0.3111 0.3522 -0.0264 -0.0307 -0.0821 929  MET A CA  
2093 C C   . MET A 273 ? 0.2059 0.3593 0.3789 -0.0301 -0.0349 -0.0787 929  MET A C   
2094 O O   . MET A 273 ? 0.1995 0.3616 0.3743 -0.0374 -0.0380 -0.0800 929  MET A O   
2095 C CB  . MET A 273 ? 0.1988 0.3270 0.3813 -0.0251 -0.0298 -0.0741 929  MET A CB  
2096 C CG  . MET A 273 ? 0.2512 0.3608 0.4354 -0.0210 -0.0260 -0.0749 929  MET A CG  
2097 S SD  . MET A 273 ? 0.3027 0.4072 0.4949 -0.0202 -0.0245 -0.0653 929  MET A SD  
2098 C CE  . MET A 273 ? 0.2627 0.3745 0.4601 -0.0317 -0.0274 -0.0671 929  MET A CE  
2099 N N   . TYR A 274 ? 0.1640 0.3248 0.3341 -0.0251 -0.0349 -0.0736 930  TYR A N   
2100 C CA  . TYR A 274 ? 0.1653 0.3441 0.3343 -0.0269 -0.0387 -0.0679 930  TYR A CA  
2101 C C   . TYR A 274 ? 0.1869 0.3677 0.3641 -0.0228 -0.0389 -0.0568 930  TYR A C   
2102 O O   . TYR A 274 ? 0.1600 0.3338 0.3384 -0.0160 -0.0361 -0.0522 930  TYR A O   
2103 C CB  . TYR A 274 ? 0.1966 0.3802 0.3578 -0.0238 -0.0381 -0.0685 930  TYR A CB  
2104 C CG  . TYR A 274 ? 0.2124 0.4133 0.3715 -0.0251 -0.0419 -0.0613 930  TYR A CG  
2105 C CD1 . TYR A 274 ? 0.2312 0.4464 0.3911 -0.0317 -0.0465 -0.0603 930  TYR A CD1 
2106 C CD2 . TYR A 274 ? 0.2267 0.4302 0.3828 -0.0203 -0.0409 -0.0556 930  TYR A CD2 
2107 C CE1 . TYR A 274 ? 0.2389 0.4706 0.3973 -0.0323 -0.0504 -0.0524 930  TYR A CE1 
2108 C CE2 . TYR A 274 ? 0.2374 0.4556 0.3917 -0.0214 -0.0444 -0.0479 930  TYR A CE2 
2109 C CZ  . TYR A 274 ? 0.2988 0.5313 0.4541 -0.0271 -0.0492 -0.0461 930  TYR A CZ  
2110 O OH  . TYR A 274 ? 0.2960 0.5433 0.4496 -0.0276 -0.0529 -0.0375 930  TYR A OH  
2111 N N   . GLU A 275 ? 0.1492 0.3389 0.3325 -0.0274 -0.0417 -0.0537 931  GLU A N   
2112 C CA  . GLU A 275 ? 0.1609 0.3536 0.3535 -0.0244 -0.0415 -0.0446 931  GLU A CA  
2113 C C   . GLU A 275 ? 0.2377 0.4439 0.4322 -0.0208 -0.0440 -0.0355 931  GLU A C   
2114 O O   . GLU A 275 ? 0.2574 0.4789 0.4509 -0.0248 -0.0484 -0.0341 931  GLU A O   
2115 C CB  . GLU A 275 ? 0.1736 0.3702 0.3732 -0.0312 -0.0430 -0.0456 931  GLU A CB  
2116 C CG  . GLU A 275 ? 0.2795 0.4595 0.4785 -0.0340 -0.0400 -0.0527 931  GLU A CG  
2117 C CD  . GLU A 275 ? 0.6004 0.7808 0.8071 -0.0403 -0.0403 -0.0525 931  GLU A CD  
2118 O OE1 . GLU A 275 ? 0.5201 0.7166 0.7334 -0.0437 -0.0433 -0.0477 931  GLU A OE1 
2119 O OE2 . GLU A 275 ? 0.6435 0.8084 0.8503 -0.0420 -0.0374 -0.0567 931  GLU A OE2 
2120 N N   . LEU A 276 ? 0.1565 0.3565 0.3536 -0.0132 -0.0411 -0.0294 932  LEU A N   
2121 C CA  . LEU A 276 ? 0.1263 0.3351 0.3257 -0.0085 -0.0425 -0.0205 932  LEU A CA  
2122 C C   . LEU A 276 ? 0.1810 0.3874 0.3895 -0.0030 -0.0400 -0.0139 932  LEU A C   
2123 O O   . LEU A 276 ? 0.1738 0.3685 0.3837 -0.0008 -0.0361 -0.0159 932  LEU A O   
2124 C CB  . LEU A 276 ? 0.1259 0.3290 0.3172 -0.0049 -0.0411 -0.0207 932  LEU A CB  
2125 C CG  . LEU A 276 ? 0.1575 0.3645 0.3391 -0.0097 -0.0429 -0.0271 932  LEU A CG  
2126 C CD1 . LEU A 276 ? 0.1600 0.3584 0.3350 -0.0060 -0.0398 -0.0289 932  LEU A CD1 
2127 C CD2 . LEU A 276 ? 0.1413 0.3660 0.3215 -0.0133 -0.0479 -0.0226 932  LEU A CD2 
2128 N N   . LYS A 277 ? 0.1532 0.3712 0.3679 -0.0003 -0.0423 -0.0057 933  LYS A N   
2129 C CA  . LYS A 277 ? 0.1541 0.3721 0.3784 0.0057  -0.0398 0.0007  933  LYS A CA  
2130 C C   . LYS A 277 ? 0.2429 0.4546 0.4661 0.0132  -0.0379 0.0059  933  LYS A C   
2131 O O   . LYS A 277 ? 0.2611 0.4687 0.4906 0.0189  -0.0345 0.0093  933  LYS A O   
2132 C CB  . LYS A 277 ? 0.1406 0.3768 0.3747 0.0043  -0.0435 0.0064  933  LYS A CB  
2133 C CG  . LYS A 277 ? 0.2626 0.5067 0.5002 -0.0035 -0.0454 0.0022  933  LYS A CG  
2134 C CD  . LYS A 277 ? 0.4042 0.6690 0.6526 -0.0044 -0.0494 0.0090  933  LYS A CD  
2135 C CE  . LYS A 277 ? 0.6208 0.8955 0.8724 -0.0138 -0.0521 0.0046  933  LYS A CE  
2136 N NZ  . LYS A 277 ? 0.7557 1.0527 1.0191 -0.0146 -0.0561 0.0115  933  LYS A NZ  
2137 N N   . HIS A 278 ? 0.1908 0.4032 0.4066 0.0127  -0.0400 0.0068  934  HIS A N   
2138 C CA  . HIS A 278 ? 0.1818 0.3888 0.3964 0.0184  -0.0388 0.0124  934  HIS A CA  
2139 C C   . HIS A 278 ? 0.2132 0.4125 0.4169 0.0167  -0.0381 0.0085  934  HIS A C   
2140 O O   . HIS A 278 ? 0.1951 0.3967 0.3923 0.0113  -0.0394 0.0022  934  HIS A O   
2141 C CB  . HIS A 278 ? 0.1827 0.4031 0.4024 0.0202  -0.0430 0.0219  934  HIS A CB  
2142 C CG  . HIS A 278 ? 0.2101 0.4437 0.4406 0.0203  -0.0451 0.0254  934  HIS A CG  
2143 N ND1 . HIS A 278 ? 0.2285 0.4601 0.4692 0.0264  -0.0419 0.0286  934  HIS A ND1 
2144 C CD2 . HIS A 278 ? 0.2186 0.4676 0.4507 0.0143  -0.0497 0.0247  934  HIS A CD2 
2145 C CE1 . HIS A 278 ? 0.2081 0.4553 0.4573 0.0243  -0.0447 0.0308  934  HIS A CE1 
2146 N NE2 . HIS A 278 ? 0.2074 0.4653 0.4518 0.0167  -0.0497 0.0285  934  HIS A NE2 
2147 N N   . ALA A 279 ? 0.1608 0.3513 0.3628 0.0211  -0.0358 0.0118  935  ALA A N   
2148 C CA  . ALA A 279 ? 0.1625 0.3464 0.3554 0.0197  -0.0346 0.0088  935  ALA A CA  
2149 C C   . ALA A 279 ? 0.2232 0.4178 0.4090 0.0143  -0.0383 0.0082  935  ALA A C   
2150 O O   . ALA A 279 ? 0.2111 0.4176 0.3985 0.0131  -0.0422 0.0145  935  ALA A O   
2151 C CB  . ALA A 279 ? 0.1661 0.3418 0.3596 0.0241  -0.0326 0.0143  935  ALA A CB  
2152 N N   . SER A 280 ? 0.1858 0.3772 0.3642 0.0111  -0.0369 0.0004  936  SER A N   
2153 C CA  . SER A 280 ? 0.1927 0.3933 0.3631 0.0059  -0.0391 -0.0025 936  SER A CA  
2154 C C   . SER A 280 ? 0.2185 0.4112 0.3822 0.0060  -0.0357 -0.0077 936  SER A C   
2155 O O   . SER A 280 ? 0.2047 0.3908 0.3674 0.0061  -0.0333 -0.0156 936  SER A O   
2156 C CB  . SER A 280 ? 0.2666 0.4738 0.4364 0.0012  -0.0411 -0.0093 936  SER A CB  
2157 O OG  . SER A 280 ? 0.4223 0.6378 0.5834 -0.0040 -0.0426 -0.0141 936  SER A OG  
2158 N N   . HIS A 281 ? 0.1780 0.3712 0.3385 0.0064  -0.0354 -0.0023 937  HIS A N   
2159 C CA  . HIS A 281 ? 0.1844 0.3724 0.3396 0.0062  -0.0322 -0.0056 937  HIS A CA  
2160 C C   . HIS A 281 ? 0.2850 0.4822 0.4322 0.0016  -0.0324 -0.0119 937  HIS A C   
2161 O O   . HIS A 281 ? 0.2800 0.4850 0.4217 -0.0013 -0.0331 -0.0084 937  HIS A O   
2162 C CB  . HIS A 281 ? 0.1728 0.3574 0.3284 0.0076  -0.0317 0.0032  937  HIS A CB  
2163 C CG  . HIS A 281 ? 0.1999 0.3754 0.3635 0.0125  -0.0311 0.0085  937  HIS A CG  
2164 N ND1 . HIS A 281 ? 0.2162 0.3803 0.3832 0.0159  -0.0279 0.0042  937  HIS A ND1 
2165 C CD2 . HIS A 281 ? 0.2134 0.3906 0.3822 0.0148  -0.0333 0.0173  937  HIS A CD2 
2166 C CE1 . HIS A 281 ? 0.2099 0.3690 0.3835 0.0199  -0.0278 0.0097  937  HIS A CE1 
2167 N NE2 . HIS A 281 ? 0.2127 0.3790 0.3882 0.0198  -0.0308 0.0177  937  HIS A NE2 
2168 N N   . ILE A 282 ? 0.2872 0.4830 0.4339 0.0009  -0.0315 -0.0215 938  ILE A N   
2169 C CA  . ILE A 282 ? 0.3037 0.5070 0.4435 -0.0030 -0.0312 -0.0298 938  ILE A CA  
2170 C C   . ILE A 282 ? 0.3884 0.5874 0.5254 -0.0015 -0.0272 -0.0365 938  ILE A C   
2171 O O   . ILE A 282 ? 0.3551 0.5435 0.4965 0.0026  -0.0249 -0.0378 938  ILE A O   
2172 C CB  . ILE A 282 ? 0.3427 0.5471 0.4836 -0.0053 -0.0328 -0.0368 938  ILE A CB  
2173 C CG1 . ILE A 282 ? 0.3442 0.5349 0.4917 -0.0016 -0.0308 -0.0404 938  ILE A CG1 
2174 C CG2 . ILE A 282 ? 0.3691 0.5841 0.5111 -0.0086 -0.0375 -0.0310 938  ILE A CG2 
2175 C CD1 . ILE A 282 ? 0.3627 0.5502 0.5091 -0.0036 -0.0300 -0.0508 938  ILE A CD1 
2176 N N   . SER A 283 ? 0.4111 0.6200 0.5410 -0.0049 -0.0264 -0.0412 939  SER A N   
2177 C CA  . SER A 283 ? 0.4328 0.6418 0.5601 -0.0038 -0.0225 -0.0480 939  SER A CA  
2178 C C   . SER A 283 ? 0.4892 0.6968 0.6154 -0.0036 -0.0210 -0.0601 939  SER A C   
2179 O O   . SER A 283 ? 0.4958 0.6973 0.6242 0.0001  -0.0177 -0.0662 939  SER A O   
2180 C CB  . SER A 283 ? 0.5020 0.7239 0.6221 -0.0076 -0.0219 -0.0453 939  SER A CB  
2181 O OG  . SER A 283 ? 0.6413 0.8637 0.7622 -0.0084 -0.0233 -0.0338 939  SER A OG  
2182 N N   . LYS A 284 ? 0.4231 0.6364 0.5460 -0.0077 -0.0234 -0.0634 940  LYS A N   
2183 C CA  . LYS A 284 ? 0.4068 0.6182 0.5281 -0.0088 -0.0223 -0.0752 940  LYS A CA  
2184 C C   . LYS A 284 ? 0.4081 0.6174 0.5317 -0.0119 -0.0260 -0.0751 940  LYS A C   
2185 O O   . LYS A 284 ? 0.4034 0.6212 0.5263 -0.0151 -0.0298 -0.0675 940  LYS A O   
2186 C CB  . LYS A 284 ? 0.4477 0.6729 0.5598 -0.0128 -0.0208 -0.0819 940  LYS A CB  
2187 C CG  . LYS A 284 ? 0.7188 0.9428 0.8278 -0.0146 -0.0193 -0.0956 940  LYS A CG  
2188 C CD  . LYS A 284 ? 0.8520 1.0908 0.9514 -0.0181 -0.0170 -0.1026 940  LYS A CD  
2189 C CE  . LYS A 284 ? 0.9044 1.1402 1.0048 -0.0131 -0.0113 -0.1112 940  LYS A CE  
2190 N NZ  . LYS A 284 ? 0.9771 1.2284 1.0682 -0.0168 -0.0086 -0.1189 940  LYS A NZ  
2191 N N   . LEU A 285 ? 0.3211 0.5195 0.4482 -0.0109 -0.0248 -0.0829 941  LEU A N   
2192 C CA  . LEU A 285 ? 0.3075 0.5039 0.4372 -0.0148 -0.0280 -0.0841 941  LEU A CA  
2193 C C   . LEU A 285 ? 0.3921 0.6009 0.5142 -0.0221 -0.0301 -0.0908 941  LEU A C   
2194 O O   . LEU A 285 ? 0.4205 0.6334 0.5360 -0.0229 -0.0274 -0.0992 941  LEU A O   
2195 C CB  . LEU A 285 ? 0.2935 0.4736 0.4284 -0.0124 -0.0257 -0.0909 941  LEU A CB  
2196 C CG  . LEU A 285 ? 0.3380 0.5059 0.4809 -0.0070 -0.0248 -0.0843 941  LEU A CG  
2197 C CD1 . LEU A 285 ? 0.3411 0.4942 0.4870 -0.0037 -0.0217 -0.0914 941  LEU A CD1 
2198 C CD2 . LEU A 285 ? 0.3550 0.5237 0.5030 -0.0097 -0.0280 -0.0775 941  LEU A CD2 
2199 N N   . PRO A 286 ? 0.3386 0.5541 0.4616 -0.0275 -0.0345 -0.0884 942  PRO A N   
2200 C CA  . PRO A 286 ? 0.3352 0.5625 0.4505 -0.0353 -0.0368 -0.0963 942  PRO A CA  
2201 C C   . PRO A 286 ? 0.3775 0.5936 0.4914 -0.0366 -0.0336 -0.1112 942  PRO A C   
2202 O O   . PRO A 286 ? 0.3660 0.5655 0.4869 -0.0328 -0.0313 -0.1130 942  PRO A O   
2203 C CB  . PRO A 286 ? 0.3435 0.5784 0.4629 -0.0401 -0.0424 -0.0898 942  PRO A CB  
2204 C CG  . PRO A 286 ? 0.3960 0.6252 0.5244 -0.0343 -0.0427 -0.0778 942  PRO A CG  
2205 C CD  . PRO A 286 ? 0.3476 0.5608 0.4790 -0.0271 -0.0376 -0.0793 942  PRO A CD  
2206 N N   . LYS A 287 ? 0.3400 0.5651 0.4447 -0.0419 -0.0332 -0.1216 943  LYS A N   
2207 C CA  . LYS A 287 ? 0.3375 0.5528 0.4397 -0.0438 -0.0300 -0.1373 943  LYS A CA  
2208 C C   . LYS A 287 ? 0.3862 0.5880 0.4955 -0.0467 -0.0315 -0.1401 943  LYS A C   
2209 O O   . LYS A 287 ? 0.3704 0.5800 0.4816 -0.0526 -0.0365 -0.1351 943  LYS A O   
2210 C CB  . LYS A 287 ? 0.3546 0.5857 0.4448 -0.0512 -0.0307 -0.1469 943  LYS A CB  
2211 C CG  . LYS A 287 ? 0.4642 0.6986 0.5473 -0.0479 -0.0253 -0.1550 943  LYS A CG  
2212 C CD  . LYS A 287 ? 0.6395 0.8914 0.7098 -0.0561 -0.0261 -0.1647 943  LYS A CD  
2213 C CE  . LYS A 287 ? 0.7244 0.9681 0.7921 -0.0618 -0.0253 -0.1810 943  LYS A CE  
2214 N NZ  . LYS A 287 ? 0.7258 0.9865 0.7798 -0.0693 -0.0251 -0.1922 943  LYS A NZ  
2215 N N   . GLY A 288 ? 0.3583 0.5407 0.4722 -0.0425 -0.0273 -0.1473 944  GLY A N   
2216 C CA  . GLY A 288 ? 0.3546 0.5216 0.4753 -0.0451 -0.0279 -0.1499 944  GLY A CA  
2217 C C   . GLY A 288 ? 0.3979 0.5539 0.5288 -0.0395 -0.0279 -0.1384 944  GLY A C   
2218 O O   . GLY A 288 ? 0.4090 0.5492 0.5459 -0.0400 -0.0270 -0.1406 944  GLY A O   
2219 N N   . LYS A 289 ? 0.3288 0.4930 0.4614 -0.0347 -0.0289 -0.1262 945  LYS A N   
2220 C CA  . LYS A 289 ? 0.3149 0.4706 0.4561 -0.0290 -0.0286 -0.1152 945  LYS A CA  
2221 C C   . LYS A 289 ? 0.3569 0.5004 0.5000 -0.0200 -0.0240 -0.1156 945  LYS A C   
2222 O O   . LYS A 289 ? 0.3562 0.5042 0.4943 -0.0171 -0.0217 -0.1199 945  LYS A O   
2223 C CB  . LYS A 289 ? 0.3172 0.4873 0.4596 -0.0285 -0.0319 -0.1026 945  LYS A CB  
2224 C CG  . LYS A 289 ? 0.2580 0.4421 0.4004 -0.0364 -0.0370 -0.0999 945  LYS A CG  
2225 C CD  . LYS A 289 ? 0.2534 0.4301 0.4034 -0.0403 -0.0383 -0.0997 945  LYS A CD  
2226 C CE  . LYS A 289 ? 0.2090 0.4021 0.3599 -0.0482 -0.0436 -0.0971 945  LYS A CE  
2227 N NZ  . LYS A 289 ? 0.2183 0.4059 0.3780 -0.0517 -0.0445 -0.0952 945  LYS A NZ  
2228 N N   . HIS A 290 ? 0.2948 0.4240 0.4452 -0.0159 -0.0227 -0.1111 946  HIS A N   
2229 C CA  . HIS A 290 ? 0.2877 0.4054 0.4407 -0.0073 -0.0189 -0.1105 946  HIS A CA  
2230 C C   . HIS A 290 ? 0.2629 0.3807 0.4204 -0.0025 -0.0193 -0.0986 946  HIS A C   
2231 O O   . HIS A 290 ? 0.2330 0.3455 0.3919 0.0043  -0.0169 -0.0966 946  HIS A O   
2232 C CB  . HIS A 290 ? 0.3109 0.4098 0.4680 -0.0062 -0.0167 -0.1163 946  HIS A CB  
2233 C CG  . HIS A 290 ? 0.3660 0.4614 0.5195 -0.0113 -0.0161 -0.1290 946  HIS A CG  
2234 N ND1 . HIS A 290 ? 0.3892 0.4871 0.5419 -0.0206 -0.0190 -0.1320 946  HIS A ND1 
2235 C CD2 . HIS A 290 ? 0.3978 0.4876 0.5486 -0.0083 -0.0127 -0.1398 946  HIS A CD2 
2236 C CE1 . HIS A 290 ? 0.3893 0.4824 0.5380 -0.0236 -0.0173 -0.1449 946  HIS A CE1 
2237 N NE2 . HIS A 290 ? 0.3986 0.4864 0.5461 -0.0161 -0.0133 -0.1501 946  HIS A NE2 
2238 N N   . SER A 291 ? 0.2027 0.3266 0.3626 -0.0060 -0.0222 -0.0910 947  SER A N   
2239 C CA  . SER A 291 ? 0.1868 0.3108 0.3509 -0.0019 -0.0223 -0.0804 947  SER A CA  
2240 C C   . SER A 291 ? 0.2173 0.3536 0.3828 -0.0058 -0.0256 -0.0737 947  SER A C   
2241 O O   . SER A 291 ? 0.2183 0.3631 0.3821 -0.0120 -0.0283 -0.0765 947  SER A O   
2242 C CB  . SER A 291 ? 0.2150 0.3248 0.3848 0.0004  -0.0207 -0.0780 947  SER A CB  
2243 O OG  . SER A 291 ? 0.3108 0.4180 0.4837 -0.0058 -0.0221 -0.0793 947  SER A OG  
2244 N N   . VAL A 292 ? 0.1646 0.3022 0.3332 -0.0019 -0.0254 -0.0649 948  VAL A N   
2245 C CA  . VAL A 292 ? 0.1595 0.3070 0.3313 -0.0035 -0.0279 -0.0572 948  VAL A CA  
2246 C C   . VAL A 292 ? 0.2055 0.3459 0.3843 -0.0020 -0.0267 -0.0525 948  VAL A C   
2247 O O   . VAL A 292 ? 0.1897 0.3198 0.3693 0.0026  -0.0239 -0.0515 948  VAL A O   
2248 C CB  . VAL A 292 ? 0.1954 0.3506 0.3651 -0.0003 -0.0284 -0.0510 948  VAL A CB  
2249 C CG1 . VAL A 292 ? 0.1929 0.3539 0.3684 0.0006  -0.0299 -0.0419 948  VAL A CG1 
2250 C CG2 . VAL A 292 ? 0.1843 0.3506 0.3475 -0.0038 -0.0303 -0.0539 948  VAL A CG2 
2251 N N   . LYS A 293 ? 0.1543 0.3014 0.3379 -0.0061 -0.0288 -0.0495 949  LYS A N   
2252 C CA  . LYS A 293 ? 0.1466 0.2900 0.3369 -0.0049 -0.0274 -0.0443 949  LYS A CA  
2253 C C   . LYS A 293 ? 0.2009 0.3562 0.3957 -0.0032 -0.0289 -0.0363 949  LYS A C   
2254 O O   . LYS A 293 ? 0.1804 0.3483 0.3771 -0.0071 -0.0323 -0.0350 949  LYS A O   
2255 C CB  . LYS A 293 ? 0.1559 0.2957 0.3501 -0.0109 -0.0277 -0.0474 949  LYS A CB  
2256 C CG  . LYS A 293 ? 0.0529 0.1903 0.2539 -0.0097 -0.0256 -0.0412 949  LYS A CG  
2257 C CD  . LYS A 293 ? 0.1175 0.2528 0.3231 -0.0165 -0.0259 -0.0429 949  LYS A CD  
2258 C CE  . LYS A 293 ? 0.1233 0.2580 0.3353 -0.0153 -0.0233 -0.0363 949  LYS A CE  
2259 N NZ  . LYS A 293 ? 0.1761 0.3096 0.3931 -0.0231 -0.0235 -0.0373 949  LYS A NZ  
2260 N N   . GLY A 294 ? 0.1727 0.3241 0.3691 0.0028  -0.0264 -0.0313 950  GLY A N   
2261 C CA  . GLY A 294 ? 0.1617 0.3212 0.3635 0.0057  -0.0267 -0.0239 950  GLY A CA  
2262 C C   . GLY A 294 ? 0.1845 0.3470 0.3943 0.0037  -0.0259 -0.0215 950  GLY A C   
2263 O O   . GLY A 294 ? 0.1748 0.3284 0.3855 0.0049  -0.0227 -0.0218 950  GLY A O   
2264 N N   . LEU A 295 ? 0.1535 0.3293 0.3691 0.0003  -0.0289 -0.0188 951  LEU A N   
2265 C CA  . LEU A 295 ? 0.1294 0.3106 0.3534 -0.0027 -0.0283 -0.0167 951  LEU A CA  
2266 C C   . LEU A 295 ? 0.1710 0.3550 0.4020 0.0031  -0.0252 -0.0103 951  LEU A C   
2267 O O   . LEU A 295 ? 0.1901 0.3837 0.4254 0.0066  -0.0265 -0.0054 951  LEU A O   
2268 C CB  . LEU A 295 ? 0.1177 0.3138 0.3459 -0.0094 -0.0329 -0.0168 951  LEU A CB  
2269 C CG  . LEU A 295 ? 0.1662 0.3626 0.3876 -0.0163 -0.0363 -0.0240 951  LEU A CG  
2270 C CD1 . LEU A 295 ? 0.1478 0.3629 0.3737 -0.0225 -0.0414 -0.0227 951  LEU A CD1 
2271 C CD2 . LEU A 295 ? 0.1968 0.3794 0.4155 -0.0207 -0.0342 -0.0307 951  LEU A CD2 
2272 N N   . GLY A 296 ? 0.0944 0.2701 0.3264 0.0041  -0.0210 -0.0104 952  GLY A N   
2273 C CA  . GLY A 296 ? 0.0928 0.2711 0.3307 0.0091  -0.0172 -0.0057 952  GLY A CA  
2274 C C   . GLY A 296 ? 0.1665 0.3581 0.4148 0.0058  -0.0172 -0.0024 952  GLY A C   
2275 O O   . GLY A 296 ? 0.1724 0.3682 0.4226 -0.0017 -0.0197 -0.0045 952  GLY A O   
2276 N N   . LYS A 297 ? 0.1218 0.3210 0.3777 0.0113  -0.0144 0.0024  953  LYS A N   
2277 C CA  . LYS A 297 ? 0.1231 0.3373 0.3907 0.0095  -0.0134 0.0061  953  LYS A CA  
2278 C C   . LYS A 297 ? 0.1714 0.3802 0.4385 0.0045  -0.0099 0.0047  953  LYS A C   
2279 O O   . LYS A 297 ? 0.1440 0.3629 0.4184 -0.0016 -0.0104 0.0059  953  LYS A O   
2280 C CB  . LYS A 297 ? 0.1716 0.3926 0.4466 0.0181  -0.0098 0.0107  953  LYS A CB  
2281 C CG  . LYS A 297 ? 0.4641 0.6874 0.7396 0.0244  -0.0124 0.0133  953  LYS A CG  
2282 C CD  . LYS A 297 ? 0.7272 0.9703 1.0154 0.0256  -0.0153 0.0187  953  LYS A CD  
2283 C CE  . LYS A 297 ? 0.9039 1.1479 1.1929 0.0327  -0.0175 0.0227  953  LYS A CE  
2284 N NZ  . LYS A 297 ? 0.9804 1.2439 1.2832 0.0359  -0.0197 0.0293  953  LYS A NZ  
2285 N N   . THR A 298 ? 0.1447 0.3380 0.4033 0.0069  -0.0065 0.0026  954  THR A N   
2286 C CA  . THR A 298 ? 0.1172 0.3037 0.3741 0.0029  -0.0031 0.0024  954  THR A CA  
2287 C C   . THR A 298 ? 0.1180 0.2893 0.3656 -0.0010 -0.0051 -0.0019 954  THR A C   
2288 O O   . THR A 298 ? 0.0900 0.2530 0.3304 0.0024  -0.0068 -0.0048 954  THR A O   
2289 C CB  . THR A 298 ? 0.1322 0.3162 0.3880 0.0091  0.0028  0.0045  954  THR A CB  
2290 O OG1 . THR A 298 ? 0.1618 0.3615 0.4282 0.0116  0.0051  0.0080  954  THR A OG1 
2291 C CG2 . THR A 298 ? 0.0937 0.2688 0.3447 0.0058  0.0063  0.0049  954  THR A CG2 
2292 N N   . THR A 299 ? 0.0783 0.2456 0.3268 -0.0080 -0.0045 -0.0021 955  THR A N   
2293 C CA  . THR A 299 ? 0.0772 0.2289 0.3185 -0.0116 -0.0057 -0.0059 955  THR A CA  
2294 C C   . THR A 299 ? 0.1608 0.3046 0.4016 -0.0149 -0.0020 -0.0030 955  THR A C   
2295 O O   . THR A 299 ? 0.1500 0.3033 0.3981 -0.0193 -0.0001 0.0006  955  THR A O   
2296 C CB  . THR A 299 ? 0.1571 0.3105 0.3995 -0.0188 -0.0105 -0.0104 955  THR A CB  
2297 O OG1 . THR A 299 ? 0.1974 0.3338 0.4327 -0.0207 -0.0110 -0.0148 955  THR A OG1 
2298 C CG2 . THR A 299 ? 0.1015 0.2659 0.3531 -0.0277 -0.0112 -0.0088 955  THR A CG2 
2299 N N   . PRO A 300 ? 0.1485 0.2758 0.3814 -0.0135 -0.0012 -0.0041 956  PRO A N   
2300 C CA  . PRO A 300 ? 0.1500 0.2691 0.3825 -0.0176 0.0016  -0.0006 956  PRO A CA  
2301 C C   . PRO A 300 ? 0.2437 0.3638 0.4823 -0.0277 -0.0002 -0.0017 956  PRO A C   
2302 O O   . PRO A 300 ? 0.2625 0.3817 0.5012 -0.0306 -0.0041 -0.0073 956  PRO A O   
2303 C CB  . PRO A 300 ? 0.1662 0.2678 0.3901 -0.0140 0.0011  -0.0025 956  PRO A CB  
2304 C CG  . PRO A 300 ? 0.2299 0.3335 0.4493 -0.0065 -0.0003 -0.0057 956  PRO A CG  
2305 C CD  . PRO A 300 ? 0.1788 0.2950 0.4036 -0.0085 -0.0030 -0.0083 956  PRO A CD  
2306 N N   . ASP A 301 ? 0.2072 0.3311 0.4509 -0.0335 0.0027  0.0033  957  ASP A N   
2307 C CA  . ASP A 301 ? 0.2134 0.3391 0.4637 -0.0444 0.0014  0.0027  957  ASP A CA  
2308 C C   . ASP A 301 ? 0.3546 0.4618 0.6005 -0.0485 -0.0016 -0.0030 957  ASP A C   
2309 O O   . ASP A 301 ? 0.3515 0.4416 0.5922 -0.0474 0.0001  -0.0013 957  ASP A O   
2310 C CB  . ASP A 301 ? 0.2309 0.3597 0.4856 -0.0497 0.0058  0.0098  957  ASP A CB  
2311 C CG  . ASP A 301 ? 0.3011 0.4364 0.5645 -0.0619 0.0049  0.0101  957  ASP A CG  
2312 O OD1 . ASP A 301 ? 0.3032 0.4440 0.5702 -0.0661 0.0005  0.0045  957  ASP A OD1 
2313 O OD2 . ASP A 301 ? 0.3086 0.4441 0.5752 -0.0676 0.0084  0.0159  957  ASP A OD2 
2314 N N   . PRO A 302 ? 0.3549 0.4658 0.6026 -0.0529 -0.0059 -0.0098 958  PRO A N   
2315 C CA  . PRO A 302 ? 0.3647 0.4582 0.6079 -0.0566 -0.0082 -0.0167 958  PRO A CA  
2316 C C   . PRO A 302 ? 0.4537 0.5321 0.6987 -0.0651 -0.0066 -0.0155 958  PRO A C   
2317 O O   . PRO A 302 ? 0.4739 0.5329 0.7142 -0.0649 -0.0070 -0.0196 958  PRO A O   
2318 C CB  . PRO A 302 ? 0.3792 0.4848 0.6248 -0.0612 -0.0127 -0.0235 958  PRO A CB  
2319 C CG  . PRO A 302 ? 0.4261 0.5524 0.6752 -0.0559 -0.0132 -0.0198 958  PRO A CG  
2320 C CD  . PRO A 302 ? 0.3660 0.4975 0.6196 -0.0546 -0.0088 -0.0114 958  PRO A CD  
2321 N N   . SER A 303 ? 0.4036 0.4906 0.6558 -0.0727 -0.0047 -0.0098 959  SER A N   
2322 C CA  . SER A 303 ? 0.4071 0.4796 0.6613 -0.0817 -0.0030 -0.0075 959  SER A CA  
2323 C C   . SER A 303 ? 0.4438 0.5008 0.6929 -0.0762 0.0010  0.0000  959  SER A C   
2324 O O   . SER A 303 ? 0.4466 0.4867 0.6958 -0.0820 0.0024  0.0026  959  SER A O   
2325 C CB  . SER A 303 ? 0.4638 0.5521 0.7278 -0.0928 -0.0024 -0.0040 959  SER A CB  
2326 O OG  . SER A 303 ? 0.6178 0.7273 0.8861 -0.0887 0.0000  0.0024  959  SER A OG  
2327 N N   . ALA A 304 ? 0.3726 0.4346 0.6169 -0.0652 0.0024  0.0033  960  ALA A N   
2328 C CA  . ALA A 304 ? 0.3616 0.4124 0.6002 -0.0590 0.0055  0.0102  960  ALA A CA  
2329 C C   . ALA A 304 ? 0.3941 0.4277 0.6250 -0.0505 0.0039  0.0064  960  ALA A C   
2330 O O   . ALA A 304 ? 0.3632 0.3882 0.5891 -0.0447 0.0057  0.0121  960  ALA A O   
2331 C CB  . ALA A 304 ? 0.3631 0.4307 0.6011 -0.0532 0.0084  0.0159  960  ALA A CB  
2332 N N   . ASN A 305 ? 0.3672 0.3967 0.5975 -0.0503 0.0004  -0.0031 961  ASN A N   
2333 C CA  . ASN A 305 ? 0.3813 0.3961 0.6057 -0.0428 -0.0010 -0.0081 961  ASN A CA  
2334 C C   . ASN A 305 ? 0.4494 0.4412 0.6727 -0.0438 0.0003  -0.0050 961  ASN A C   
2335 O O   . ASN A 305 ? 0.4432 0.4266 0.6707 -0.0532 0.0008  -0.0045 961  ASN A O   
2336 C CB  . ASN A 305 ? 0.3707 0.3872 0.5951 -0.0443 -0.0043 -0.0192 961  ASN A CB  
2337 C CG  . ASN A 305 ? 0.5660 0.5969 0.7874 -0.0369 -0.0059 -0.0223 961  ASN A CG  
2338 O OD1 . ASN A 305 ? 0.6278 0.6528 0.8443 -0.0297 -0.0067 -0.0264 961  ASN A OD1 
2339 N ND2 . ASN A 305 ? 0.3036 0.3537 0.5283 -0.0384 -0.0063 -0.0202 961  ASN A ND2 
2340 N N   . ILE A 306 ? 0.4214 0.4039 0.6395 -0.0343 0.0008  -0.0021 962  ILE A N   
2341 C CA  . ILE A 306 ? 0.4332 0.3944 0.6498 -0.0320 0.0018  0.0025  962  ILE A CA  
2342 C C   . ILE A 306 ? 0.4949 0.4450 0.7089 -0.0239 0.0000  -0.0052 962  ILE A C   
2343 O O   . ILE A 306 ? 0.4797 0.4411 0.6916 -0.0193 -0.0015 -0.0117 962  ILE A O   
2344 C CB  . ILE A 306 ? 0.4770 0.4420 0.6903 -0.0276 0.0040  0.0146  962  ILE A CB  
2345 C CG1 . ILE A 306 ? 0.4857 0.4391 0.7011 -0.0348 0.0063  0.0240  962  ILE A CG1 
2346 C CG2 . ILE A 306 ? 0.5005 0.4619 0.7082 -0.0157 0.0033  0.0163  962  ILE A CG2 
2347 C CD1 . ILE A 306 ? 0.4165 0.3855 0.6352 -0.0434 0.0087  0.0296  962  ILE A CD1 
2348 N N   . SER A 307 ? 0.4829 0.4113 0.6974 -0.0220 0.0004  -0.0045 963  SER A N   
2349 C CA  . SER A 307 ? 0.4865 0.4039 0.6996 -0.0138 -0.0006 -0.0117 963  SER A CA  
2350 C C   . SER A 307 ? 0.5584 0.4670 0.7693 -0.0035 -0.0002 -0.0034 963  SER A C   
2351 O O   . SER A 307 ? 0.5686 0.4656 0.7804 -0.0049 0.0010  0.0064  963  SER A O   
2352 C CB  . SER A 307 ? 0.5330 0.4320 0.7496 -0.0195 -0.0006 -0.0203 963  SER A CB  
2353 O OG  . SER A 307 ? 0.6874 0.5791 0.9029 -0.0117 -0.0012 -0.0295 963  SER A OG  
2354 N N   . LEU A 308 ? 0.5125 0.4282 0.7206 0.0064  -0.0013 -0.0066 964  LEU A N   
2355 C CA  . LEU A 308 ? 0.5188 0.4300 0.7252 0.0170  -0.0016 0.0000  964  LEU A CA  
2356 C C   . LEU A 308 ? 0.5764 0.4815 0.7841 0.0248  -0.0024 -0.0097 964  LEU A C   
2357 O O   . LEU A 308 ? 0.5691 0.4882 0.7747 0.0280  -0.0033 -0.0167 964  LEU A O   
2358 C CB  . LEU A 308 ? 0.5146 0.4451 0.7161 0.0210  -0.0021 0.0067  964  LEU A CB  
2359 C CG  . LEU A 308 ? 0.5699 0.5011 0.7688 0.0317  -0.0032 0.0128  964  LEU A CG  
2360 C CD1 . LEU A 308 ? 0.5787 0.4936 0.7788 0.0336  -0.0028 0.0236  964  LEU A CD1 
2361 C CD2 . LEU A 308 ? 0.5881 0.5391 0.7817 0.0334  -0.0035 0.0171  964  LEU A CD2 
2362 N N   . ASP A 309 ? 0.5473 0.4308 0.7587 0.0273  -0.0017 -0.0103 965  ASP A N   
2363 C CA  . ASP A 309 ? 0.5524 0.4262 0.7665 0.0348  -0.0015 -0.0196 965  ASP A CA  
2364 C C   . ASP A 309 ? 0.5862 0.4626 0.8003 0.0290  -0.0012 -0.0345 965  ASP A C   
2365 O O   . ASP A 309 ? 0.5795 0.4615 0.7931 0.0348  -0.0013 -0.0436 965  ASP A O   
2366 C CB  . ASP A 309 ? 0.5808 0.4652 0.7938 0.0471  -0.0027 -0.0176 965  ASP A CB  
2367 C CG  . ASP A 309 ? 0.7980 0.6748 1.0120 0.0542  -0.0032 -0.0043 965  ASP A CG  
2368 O OD1 . ASP A 309 ? 0.8164 0.7018 1.0268 0.0517  -0.0039 0.0063  965  ASP A OD1 
2369 O OD2 . ASP A 309 ? 0.9054 0.7683 1.1240 0.0626  -0.0030 -0.0045 965  ASP A OD2 
2370 N N   . GLY A 310 ? 0.5309 0.4043 0.7456 0.0172  -0.0009 -0.0366 966  GLY A N   
2371 C CA  . GLY A 310 ? 0.5237 0.4004 0.7380 0.0098  -0.0010 -0.0497 966  GLY A CA  
2372 C C   . GLY A 310 ? 0.5543 0.4561 0.7647 0.0078  -0.0026 -0.0535 966  GLY A C   
2373 O O   . GLY A 310 ? 0.5720 0.4794 0.7813 0.0022  -0.0032 -0.0640 966  GLY A O   
2374 N N   . VAL A 311 ? 0.4645 0.3813 0.6726 0.0121  -0.0033 -0.0448 967  VAL A N   
2375 C CA  . VAL A 311 ? 0.4318 0.3713 0.6366 0.0112  -0.0047 -0.0465 967  VAL A CA  
2376 C C   . VAL A 311 ? 0.4379 0.3868 0.6433 0.0031  -0.0049 -0.0395 967  VAL A C   
2377 O O   . VAL A 311 ? 0.4145 0.3581 0.6209 0.0025  -0.0039 -0.0297 967  VAL A O   
2378 C CB  . VAL A 311 ? 0.4627 0.4123 0.6648 0.0215  -0.0050 -0.0427 967  VAL A CB  
2379 C CG1 . VAL A 311 ? 0.4490 0.4193 0.6479 0.0209  -0.0062 -0.0460 967  VAL A CG1 
2380 C CG2 . VAL A 311 ? 0.4590 0.3983 0.6623 0.0305  -0.0044 -0.0473 967  VAL A CG2 
2381 N N   . ASP A 312 ? 0.3817 0.3454 0.5866 -0.0031 -0.0061 -0.0442 968  ASP A N   
2382 C CA  . ASP A 312 ? 0.3659 0.3409 0.5726 -0.0102 -0.0062 -0.0382 968  ASP A CA  
2383 C C   . ASP A 312 ? 0.3421 0.3299 0.5466 -0.0048 -0.0057 -0.0298 968  ASP A C   
2384 O O   . ASP A 312 ? 0.3269 0.3237 0.5283 0.0016  -0.0064 -0.0317 968  ASP A O   
2385 C CB  . ASP A 312 ? 0.4052 0.3924 0.6130 -0.0181 -0.0080 -0.0453 968  ASP A CB  
2386 C CG  . ASP A 312 ? 0.6567 0.6340 0.8683 -0.0286 -0.0081 -0.0488 968  ASP A CG  
2387 O OD1 . ASP A 312 ? 0.6876 0.6618 0.9027 -0.0339 -0.0069 -0.0415 968  ASP A OD1 
2388 O OD2 . ASP A 312 ? 0.7763 0.7493 0.9870 -0.0319 -0.0092 -0.0592 968  ASP A OD2 
2389 N N   . VAL A 313 ? 0.2538 0.2415 0.4598 -0.0074 -0.0041 -0.0206 969  VAL A N   
2390 C CA  . VAL A 313 ? 0.2515 0.2505 0.4549 -0.0030 -0.0030 -0.0130 969  VAL A CA  
2391 C C   . VAL A 313 ? 0.2630 0.2771 0.4693 -0.0093 -0.0023 -0.0103 969  VAL A C   
2392 O O   . VAL A 313 ? 0.2474 0.2590 0.4570 -0.0157 -0.0008 -0.0054 969  VAL A O   
2393 C CB  . VAL A 313 ? 0.3053 0.2942 0.5066 0.0012  -0.0015 -0.0040 969  VAL A CB  
2394 C CG1 . VAL A 313 ? 0.3033 0.3053 0.5009 0.0052  -0.0004 0.0025  969  VAL A CG1 
2395 C CG2 . VAL A 313 ? 0.2971 0.2728 0.4970 0.0086  -0.0026 -0.0067 969  VAL A CG2 
2396 N N   . PRO A 314 ? 0.2237 0.2536 0.4298 -0.0078 -0.0032 -0.0134 970  PRO A N   
2397 C CA  . PRO A 314 ? 0.2239 0.2686 0.4344 -0.0130 -0.0025 -0.0108 970  PRO A CA  
2398 C C   . PRO A 314 ? 0.2840 0.3358 0.4935 -0.0105 0.0005  -0.0028 970  PRO A C   
2399 O O   . PRO A 314 ? 0.2699 0.3343 0.4788 -0.0068 0.0010  -0.0025 970  PRO A O   
2400 C CB  . PRO A 314 ? 0.2309 0.2879 0.4415 -0.0114 -0.0049 -0.0168 970  PRO A CB  
2401 C CG  . PRO A 314 ? 0.2791 0.3311 0.4839 -0.0035 -0.0057 -0.0198 970  PRO A CG  
2402 C CD  . PRO A 314 ? 0.2226 0.2576 0.4251 -0.0014 -0.0050 -0.0188 970  PRO A CD  
2403 N N   . LEU A 315 ? 0.2540 0.2976 0.4632 -0.0128 0.0027  0.0037  971  LEU A N   
2404 C CA  . LEU A 315 ? 0.2432 0.2933 0.4501 -0.0107 0.0059  0.0113  971  LEU A CA  
2405 C C   . LEU A 315 ? 0.2934 0.3565 0.5060 -0.0170 0.0086  0.0151  971  LEU A C   
2406 O O   . LEU A 315 ? 0.2857 0.3540 0.4965 -0.0164 0.0120  0.0214  971  LEU A O   
2407 C CB  . LEU A 315 ? 0.2414 0.2783 0.4436 -0.0088 0.0070  0.0178  971  LEU A CB  
2408 C CG  . LEU A 315 ? 0.3108 0.3309 0.5153 -0.0139 0.0066  0.0200  971  LEU A CG  
2409 C CD1 . LEU A 315 ? 0.3140 0.3374 0.5245 -0.0242 0.0088  0.0239  971  LEU A CD1 
2410 C CD2 . LEU A 315 ? 0.3442 0.3528 0.5434 -0.0092 0.0072  0.0271  971  LEU A CD2 
2411 N N   . GLY A 316 ? 0.2548 0.3246 0.4742 -0.0229 0.0072  0.0112  972  GLY A N   
2412 C CA  . GLY A 316 ? 0.2418 0.3266 0.4684 -0.0287 0.0094  0.0144  972  GLY A CA  
2413 C C   . GLY A 316 ? 0.2679 0.3686 0.4946 -0.0229 0.0117  0.0155  972  GLY A C   
2414 O O   . GLY A 316 ? 0.2601 0.3605 0.4820 -0.0153 0.0106  0.0124  972  GLY A O   
2415 N N   . THR A 317 ? 0.2157 0.3301 0.4481 -0.0263 0.0152  0.0200  973  THR A N   
2416 C CA  . THR A 317 ? 0.2060 0.3354 0.4396 -0.0203 0.0180  0.0204  973  THR A CA  
2417 C C   . THR A 317 ? 0.2268 0.3671 0.4669 -0.0190 0.0150  0.0157  973  THR A C   
2418 O O   . THR A 317 ? 0.2105 0.3520 0.4559 -0.0252 0.0118  0.0135  973  THR A O   
2419 C CB  . THR A 317 ? 0.3488 0.4900 0.5860 -0.0232 0.0236  0.0264  973  THR A CB  
2420 O OG1 . THR A 317 ? 0.2753 0.4256 0.5227 -0.0318 0.0235  0.0279  973  THR A OG1 
2421 C CG2 . THR A 317 ? 0.4069 0.5386 0.6360 -0.0236 0.0266  0.0321  973  THR A CG2 
2422 N N   . GLY A 318 ? 0.1770 0.3246 0.4162 -0.0112 0.0160  0.0141  974  GLY A N   
2423 C CA  . GLY A 318 ? 0.1754 0.3337 0.4206 -0.0086 0.0133  0.0110  974  GLY A CA  
2424 C C   . GLY A 318 ? 0.2084 0.3841 0.4657 -0.0135 0.0136  0.0131  974  GLY A C   
2425 O O   . GLY A 318 ? 0.1796 0.3665 0.4421 -0.0135 0.0183  0.0168  974  GLY A O   
2426 N N   . ILE A 319 ? 0.1623 0.3414 0.4240 -0.0180 0.0086  0.0105  975  ILE A N   
2427 C CA  . ILE A 319 ? 0.1456 0.3429 0.4193 -0.0232 0.0073  0.0119  975  ILE A CA  
2428 C C   . ILE A 319 ? 0.1880 0.3924 0.4638 -0.0197 0.0022  0.0090  975  ILE A C   
2429 O O   . ILE A 319 ? 0.1739 0.3671 0.4414 -0.0155 -0.0002 0.0056  975  ILE A O   
2430 C CB  . ILE A 319 ? 0.1716 0.3670 0.4486 -0.0352 0.0057  0.0120  975  ILE A CB  
2431 C CG1 . ILE A 319 ? 0.1598 0.3428 0.4314 -0.0393 0.0002  0.0061  975  ILE A CG1 
2432 C CG2 . ILE A 319 ? 0.1834 0.3702 0.4575 -0.0389 0.0106  0.0160  975  ILE A CG2 
2433 C CD1 . ILE A 319 ? 0.0623 0.2502 0.3399 -0.0505 -0.0029 0.0044  975  ILE A CD1 
2434 N N   . SER A 320 ? 0.1100 0.3338 0.3970 -0.0214 0.0006  0.0110  976  SER A N   
2435 C CA  . SER A 320 ? 0.1097 0.3428 0.3996 -0.0189 -0.0046 0.0098  976  SER A CA  
2436 C C   . SER A 320 ? 0.1766 0.4022 0.4609 -0.0262 -0.0103 0.0048  976  SER A C   
2437 O O   . SER A 320 ? 0.1708 0.3949 0.4566 -0.0358 -0.0112 0.0033  976  SER A O   
2438 C CB  . SER A 320 ? 0.1272 0.3845 0.4316 -0.0200 -0.0052 0.0139  976  SER A CB  
2439 O OG  . SER A 320 ? 0.2440 0.5118 0.5515 -0.0191 -0.0112 0.0137  976  SER A OG  
2440 N N   . SER A 321 ? 0.1466 0.3672 0.4242 -0.0220 -0.0138 0.0019  977  SER A N   
2441 C CA  . SER A 321 ? 0.1448 0.3598 0.4165 -0.0281 -0.0189 -0.0037 977  SER A CA  
2442 C C   . SER A 321 ? 0.1835 0.4180 0.4632 -0.0348 -0.0241 -0.0035 977  SER A C   
2443 O O   . SER A 321 ? 0.1831 0.4159 0.4603 -0.0434 -0.0276 -0.0085 977  SER A O   
2444 C CB  . SER A 321 ? 0.1727 0.3784 0.4349 -0.0215 -0.0205 -0.0064 977  SER A CB  
2445 O OG  . SER A 321 ? 0.1329 0.3509 0.3990 -0.0150 -0.0219 -0.0025 977  SER A OG  
2446 N N   . GLY A 322 ? 0.1334 0.3863 0.4226 -0.0304 -0.0245 0.0020  978  GLY A N   
2447 C CA  . GLY A 322 ? 0.1242 0.3988 0.4219 -0.0351 -0.0298 0.0037  978  GLY A CA  
2448 C C   . GLY A 322 ? 0.1860 0.4654 0.4800 -0.0294 -0.0342 0.0046  978  GLY A C   
2449 O O   . GLY A 322 ? 0.1848 0.4839 0.4859 -0.0307 -0.0390 0.0078  978  GLY A O   
2450 N N   . VAL A 323 ? 0.1369 0.3991 0.4202 -0.0231 -0.0327 0.0025  979  VAL A N   
2451 C CA  . VAL A 323 ? 0.1426 0.4063 0.4207 -0.0177 -0.0361 0.0035  979  VAL A CA  
2452 C C   . VAL A 323 ? 0.2233 0.4982 0.5102 -0.0081 -0.0352 0.0115  979  VAL A C   
2453 O O   . VAL A 323 ? 0.2300 0.4989 0.5197 -0.0012 -0.0298 0.0138  979  VAL A O   
2454 C CB  . VAL A 323 ? 0.1929 0.4355 0.4575 -0.0150 -0.0344 -0.0015 979  VAL A CB  
2455 C CG1 . VAL A 323 ? 0.1975 0.4419 0.4572 -0.0094 -0.0372 0.0007  979  VAL A CG1 
2456 C CG2 . VAL A 323 ? 0.1898 0.4232 0.4467 -0.0239 -0.0360 -0.0095 979  VAL A CG2 
2457 N N   . ASN A 324 ? 0.1904 0.4817 0.4815 -0.0077 -0.0406 0.0156  980  ASN A N   
2458 C CA  . ASN A 324 ? 0.1871 0.4899 0.4873 0.0015  -0.0408 0.0238  980  ASN A CA  
2459 C C   . ASN A 324 ? 0.2339 0.5287 0.5262 0.0080  -0.0424 0.0259  980  ASN A C   
2460 O O   . ASN A 324 ? 0.2037 0.4934 0.4852 0.0034  -0.0457 0.0221  980  ASN A O   
2461 C CB  . ASN A 324 ? 0.1705 0.4992 0.4821 -0.0021 -0.0463 0.0286  980  ASN A CB  
2462 C CG  . ASN A 324 ? 0.4979 0.8379 0.8197 -0.0086 -0.0449 0.0277  980  ASN A CG  
2463 O OD1 . ASN A 324 ? 0.4259 0.7614 0.7528 -0.0054 -0.0386 0.0281  980  ASN A OD1 
2464 N ND2 . ASN A 324 ? 0.4345 0.7904 0.7591 -0.0185 -0.0506 0.0264  980  ASN A ND2 
2465 N N   . ASP A 325 ? 0.2022 0.4966 0.5004 0.0183  -0.0398 0.0320  981  ASP A N   
2466 C CA  . ASP A 325 ? 0.1978 0.4852 0.4912 0.0252  -0.0408 0.0359  981  ASP A CA  
2467 C C   . ASP A 325 ? 0.2238 0.4917 0.5019 0.0233  -0.0397 0.0300  981  ASP A C   
2468 O O   . ASP A 325 ? 0.2167 0.4847 0.4877 0.0223  -0.0435 0.0313  981  ASP A O   
2469 C CB  . ASP A 325 ? 0.2085 0.5145 0.5061 0.0250  -0.0480 0.0431  981  ASP A CB  
2470 C CG  . ASP A 325 ? 0.3085 0.6359 0.6228 0.0284  -0.0496 0.0503  981  ASP A CG  
2471 O OD1 . ASP A 325 ? 0.2877 0.6160 0.6110 0.0313  -0.0445 0.0497  981  ASP A OD1 
2472 O OD2 . ASP A 325 ? 0.4104 0.7547 0.7289 0.0284  -0.0559 0.0570  981  ASP A OD2 
2473 N N   . THR A 326 ? 0.1686 0.4214 0.4418 0.0225  -0.0345 0.0238  982  THR A N   
2474 C CA  . THR A 326 ? 0.1782 0.4135 0.4383 0.0213  -0.0331 0.0181  982  THR A CA  
2475 C C   . THR A 326 ? 0.2152 0.4369 0.4737 0.0295  -0.0283 0.0195  982  THR A C   
2476 O O   . THR A 326 ? 0.1999 0.4223 0.4663 0.0347  -0.0243 0.0218  982  THR A O   
2477 C CB  . THR A 326 ? 0.2654 0.4930 0.5200 0.0143  -0.0317 0.0105  982  THR A CB  
2478 O OG1 . THR A 326 ? 0.2172 0.4286 0.4607 0.0150  -0.0299 0.0058  982  THR A OG1 
2479 C CG2 . THR A 326 ? 0.2316 0.4581 0.4929 0.0147  -0.0270 0.0101  982  THR A CG2 
2480 N N   . SER A 327 ? 0.1632 0.3735 0.4118 0.0302  -0.0284 0.0176  983  SER A N   
2481 C CA  . SER A 327 ? 0.1683 0.3650 0.4142 0.0366  -0.0242 0.0180  983  SER A CA  
2482 C C   . SER A 327 ? 0.1894 0.3731 0.4303 0.0362  -0.0193 0.0118  983  SER A C   
2483 O O   . SER A 327 ? 0.1936 0.3660 0.4309 0.0403  -0.0159 0.0106  983  SER A O   
2484 C CB  . SER A 327 ? 0.2158 0.4072 0.4536 0.0365  -0.0266 0.0190  983  SER A CB  
2485 O OG  . SER A 327 ? 0.3732 0.5744 0.6153 0.0385  -0.0304 0.0266  983  SER A OG  
2486 N N   . LEU A 328 ? 0.0958 0.2815 0.3364 0.0310  -0.0192 0.0079  984  LEU A N   
2487 C CA  . LEU A 328 ? 0.0901 0.2644 0.3258 0.0304  -0.0152 0.0032  984  LEU A CA  
2488 C C   . LEU A 328 ? 0.1070 0.2857 0.3493 0.0296  -0.0123 0.0037  984  LEU A C   
2489 O O   . LEU A 328 ? 0.0684 0.2573 0.3162 0.0250  -0.0144 0.0045  984  LEU A O   
2490 C CB  . LEU A 328 ? 0.0939 0.2617 0.3208 0.0249  -0.0171 -0.0022 984  LEU A CB  
2491 C CG  . LEU A 328 ? 0.1668 0.3302 0.3860 0.0251  -0.0193 -0.0037 984  LEU A CG  
2492 C CD1 . LEU A 328 ? 0.1870 0.3513 0.4011 0.0191  -0.0223 -0.0084 984  LEU A CD1 
2493 C CD2 . LEU A 328 ? 0.2434 0.3942 0.4564 0.0287  -0.0159 -0.0059 984  LEU A CD2 
2494 N N   . LEU A 329 ? 0.1045 0.2755 0.3453 0.0331  -0.0073 0.0026  985  LEU A N   
2495 C CA  . LEU A 329 ? 0.1092 0.2831 0.3544 0.0323  -0.0035 0.0029  985  LEU A CA  
2496 C C   . LEU A 329 ? 0.1172 0.2858 0.3574 0.0258  -0.0042 -0.0001 985  LEU A C   
2497 O O   . LEU A 329 ? 0.1001 0.2745 0.3453 0.0219  -0.0032 0.0009  985  LEU A O   
2498 C CB  . LEU A 329 ? 0.1180 0.2843 0.3605 0.0379  0.0020  0.0020  985  LEU A CB  
2499 C CG  . LEU A 329 ? 0.1704 0.3406 0.4194 0.0450  0.0043  0.0046  985  LEU A CG  
2500 C CD1 . LEU A 329 ? 0.1689 0.3301 0.4133 0.0493  0.0099  0.0018  985  LEU A CD1 
2501 C CD2 . LEU A 329 ? 0.2170 0.4028 0.4786 0.0455  0.0048  0.0085  985  LEU A CD2 
2502 N N   . TYR A 330 ? 0.0980 0.2553 0.3287 0.0249  -0.0055 -0.0037 986  TYR A N   
2503 C CA  . TYR A 330 ? 0.1077 0.2574 0.3335 0.0201  -0.0059 -0.0067 986  TYR A CA  
2504 C C   . TYR A 330 ? 0.1470 0.2928 0.3674 0.0176  -0.0099 -0.0104 986  TYR A C   
2505 O O   . TYR A 330 ? 0.1523 0.2990 0.3703 0.0201  -0.0117 -0.0106 986  TYR A O   
2506 C CB  . TYR A 330 ? 0.1241 0.2632 0.3437 0.0227  -0.0020 -0.0075 986  TYR A CB  
2507 C CG  . TYR A 330 ? 0.1372 0.2807 0.3606 0.0258  0.0026  -0.0047 986  TYR A CG  
2508 C CD1 . TYR A 330 ? 0.1401 0.2913 0.3703 0.0227  0.0046  -0.0020 986  TYR A CD1 
2509 C CD2 . TYR A 330 ? 0.1521 0.2935 0.3734 0.0316  0.0051  -0.0050 986  TYR A CD2 
2510 C CE1 . TYR A 330 ? 0.1184 0.2760 0.3529 0.0258  0.0092  0.0003  986  TYR A CE1 
2511 C CE2 . TYR A 330 ? 0.1649 0.3108 0.3898 0.0348  0.0098  -0.0034 986  TYR A CE2 
2512 C CZ  . TYR A 330 ? 0.2272 0.3820 0.4589 0.0322  0.0120  -0.0008 986  TYR A CZ  
2513 O OH  . TYR A 330 ? 0.2229 0.3837 0.4585 0.0356  0.0172  0.0004  986  TYR A OH  
2514 N N   . ASN A 331 ? 0.1042 0.2457 0.3230 0.0124  -0.0110 -0.0132 987  ASN A N   
2515 C CA  . ASN A 331 ? 0.1333 0.2701 0.3467 0.0098  -0.0141 -0.0180 987  ASN A CA  
2516 C C   . ASN A 331 ? 0.1681 0.2958 0.3739 0.0143  -0.0133 -0.0203 987  ASN A C   
2517 O O   . ASN A 331 ? 0.1495 0.2714 0.3531 0.0181  -0.0104 -0.0189 987  ASN A O   
2518 C CB  . ASN A 331 ? 0.1872 0.3177 0.4005 0.0042  -0.0143 -0.0210 987  ASN A CB  
2519 C CG  . ASN A 331 ? 0.2141 0.3537 0.4346 -0.0020 -0.0156 -0.0197 987  ASN A CG  
2520 O OD1 . ASN A 331 ? 0.0830 0.2347 0.3071 -0.0037 -0.0184 -0.0190 987  ASN A OD1 
2521 N ND2 . ASN A 331 ? 0.1327 0.2672 0.3556 -0.0059 -0.0136 -0.0190 987  ASN A ND2 
2522 N N   . GLU A 332 ? 0.1499 0.2775 0.3515 0.0133  -0.0159 -0.0241 988  GLU A N   
2523 C CA  . GLU A 332 ? 0.1410 0.2617 0.3361 0.0163  -0.0155 -0.0271 988  GLU A CA  
2524 C C   . GLU A 332 ? 0.1823 0.3021 0.3741 0.0130  -0.0176 -0.0328 988  GLU A C   
2525 O O   . GLU A 332 ? 0.1797 0.3067 0.3731 0.0086  -0.0201 -0.0341 988  GLU A O   
2526 C CB  . GLU A 332 ? 0.1590 0.2819 0.3520 0.0207  -0.0150 -0.0248 988  GLU A CB  
2527 C CG  . GLU A 332 ? 0.1284 0.2606 0.3223 0.0200  -0.0174 -0.0229 988  GLU A CG  
2528 C CD  . GLU A 332 ? 0.3357 0.4667 0.5284 0.0243  -0.0161 -0.0199 988  GLU A CD  
2529 O OE1 . GLU A 332 ? 0.1365 0.2671 0.3244 0.0246  -0.0169 -0.0212 988  GLU A OE1 
2530 O OE2 . GLU A 332 ? 0.2224 0.3525 0.4186 0.0272  -0.0138 -0.0167 988  GLU A OE2 
2531 N N   . TYR A 333 ? 0.1402 0.2514 0.3278 0.0151  -0.0166 -0.0366 989  TYR A N   
2532 C CA  . TYR A 333 ? 0.1381 0.2467 0.3226 0.0129  -0.0177 -0.0432 989  TYR A CA  
2533 C C   . TYR A 333 ? 0.1965 0.3056 0.3762 0.0167  -0.0173 -0.0456 989  TYR A C   
2534 O O   . TYR A 333 ? 0.1922 0.2970 0.3709 0.0210  -0.0156 -0.0438 989  TYR A O   
2535 C CB  . TYR A 333 ? 0.1403 0.2374 0.3260 0.0123  -0.0163 -0.0456 989  TYR A CB  
2536 C CG  . TYR A 333 ? 0.1381 0.2346 0.3289 0.0080  -0.0162 -0.0425 989  TYR A CG  
2537 C CD1 . TYR A 333 ? 0.1580 0.2536 0.3514 0.0099  -0.0143 -0.0362 989  TYR A CD1 
2538 C CD2 . TYR A 333 ? 0.1342 0.2318 0.3270 0.0015  -0.0179 -0.0462 989  TYR A CD2 
2539 C CE1 . TYR A 333 ? 0.1712 0.2680 0.3697 0.0057  -0.0138 -0.0331 989  TYR A CE1 
2540 C CE2 . TYR A 333 ? 0.1456 0.2438 0.3437 -0.0033 -0.0178 -0.0432 989  TYR A CE2 
2541 C CZ  . TYR A 333 ? 0.2763 0.3743 0.4776 -0.0011 -0.0156 -0.0364 989  TYR A CZ  
2542 O OH  . TYR A 333 ? 0.2859 0.3858 0.4927 -0.0062 -0.0151 -0.0334 989  TYR A OH  
2543 N N   . ILE A 334 ? 0.1461 0.2620 0.3226 0.0144  -0.0188 -0.0494 990  ILE A N   
2544 C CA  . ILE A 334 ? 0.1454 0.2641 0.3175 0.0170  -0.0183 -0.0516 990  ILE A CA  
2545 C C   . ILE A 334 ? 0.2016 0.3197 0.3707 0.0155  -0.0182 -0.0598 990  ILE A C   
2546 O O   . ILE A 334 ? 0.1887 0.3106 0.3568 0.0107  -0.0197 -0.0634 990  ILE A O   
2547 C CB  . ILE A 334 ? 0.1735 0.3025 0.3441 0.0162  -0.0197 -0.0471 990  ILE A CB  
2548 C CG1 . ILE A 334 ? 0.1814 0.3109 0.3561 0.0175  -0.0197 -0.0397 990  ILE A CG1 
2549 C CG2 . ILE A 334 ? 0.1568 0.2879 0.3234 0.0187  -0.0186 -0.0480 990  ILE A CG2 
2550 C CD1 . ILE A 334 ? 0.1876 0.3225 0.3665 0.0142  -0.0217 -0.0369 990  ILE A CD1 
2551 N N   . VAL A 335 ? 0.1622 0.2758 0.3300 0.0198  -0.0162 -0.0631 991  VAL A N   
2552 C CA  . VAL A 335 ? 0.1445 0.2576 0.3098 0.0202  -0.0151 -0.0714 991  VAL A CA  
2553 C C   . VAL A 335 ? 0.1900 0.3127 0.3517 0.0219  -0.0143 -0.0719 991  VAL A C   
2554 O O   . VAL A 335 ? 0.1634 0.2879 0.3257 0.0244  -0.0140 -0.0665 991  VAL A O   
2555 C CB  . VAL A 335 ? 0.1781 0.2785 0.3462 0.0239  -0.0132 -0.0753 991  VAL A CB  
2556 C CG1 . VAL A 335 ? 0.1711 0.2626 0.3419 0.0202  -0.0139 -0.0759 991  VAL A CG1 
2557 C CG2 . VAL A 335 ? 0.1758 0.2719 0.3461 0.0299  -0.0121 -0.0703 991  VAL A CG2 
2558 N N   . TYR A 336 ? 0.1630 0.2927 0.3209 0.0197  -0.0140 -0.0782 992  TYR A N   
2559 C CA  . TYR A 336 ? 0.1534 0.2941 0.3074 0.0199  -0.0131 -0.0785 992  TYR A CA  
2560 C C   . TYR A 336 ? 0.2193 0.3603 0.3731 0.0238  -0.0101 -0.0861 992  TYR A C   
2561 O O   . TYR A 336 ? 0.2330 0.3845 0.3838 0.0236  -0.0088 -0.0877 992  TYR A O   
2562 C CB  . TYR A 336 ? 0.1552 0.3075 0.3041 0.0138  -0.0151 -0.0780 992  TYR A CB  
2563 C CG  . TYR A 336 ? 0.1719 0.3250 0.3226 0.0111  -0.0181 -0.0698 992  TYR A CG  
2564 C CD1 . TYR A 336 ? 0.1933 0.3418 0.3468 0.0086  -0.0198 -0.0702 992  TYR A CD1 
2565 C CD2 . TYR A 336 ? 0.1652 0.3232 0.3158 0.0113  -0.0189 -0.0616 992  TYR A CD2 
2566 C CE1 . TYR A 336 ? 0.2115 0.3621 0.3680 0.0069  -0.0222 -0.0626 992  TYR A CE1 
2567 C CE2 . TYR A 336 ? 0.1696 0.3278 0.3230 0.0101  -0.0212 -0.0542 992  TYR A CE2 
2568 C CZ  . TYR A 336 ? 0.2342 0.3896 0.3908 0.0082  -0.0228 -0.0547 992  TYR A CZ  
2569 O OH  . TYR A 336 ? 0.1242 0.2816 0.2846 0.0076  -0.0248 -0.0475 992  TYR A OH  
2570 N N   . ASP A 337 ? 0.1669 0.2962 0.3247 0.0278  -0.0088 -0.0900 993  ASP A N   
2571 C CA  . ASP A 337 ? 0.1613 0.2889 0.3211 0.0334  -0.0059 -0.0964 993  ASP A CA  
2572 C C   . ASP A 337 ? 0.2215 0.3386 0.3871 0.0394  -0.0057 -0.0919 993  ASP A C   
2573 O O   . ASP A 337 ? 0.2115 0.3169 0.3795 0.0391  -0.0067 -0.0900 993  ASP A O   
2574 C CB  . ASP A 337 ? 0.1691 0.2920 0.3277 0.0324  -0.0044 -0.1069 993  ASP A CB  
2575 C CG  . ASP A 337 ? 0.2241 0.3461 0.3851 0.0386  -0.0008 -0.1149 993  ASP A CG  
2576 O OD1 . ASP A 337 ? 0.2257 0.3468 0.3915 0.0452  0.0003  -0.1117 993  ASP A OD1 
2577 O OD2 . ASP A 337 ? 0.3417 0.4641 0.5000 0.0371  0.0011  -0.1247 993  ASP A OD2 
2578 N N   . ILE A 338 ? 0.1916 0.3139 0.3595 0.0443  -0.0047 -0.0900 994  ILE A N   
2579 C CA  . ILE A 338 ? 0.1877 0.3030 0.3604 0.0500  -0.0049 -0.0852 994  ILE A CA  
2580 C C   . ILE A 338 ? 0.2334 0.3354 0.4105 0.0548  -0.0038 -0.0889 994  ILE A C   
2581 O O   . ILE A 338 ? 0.2354 0.3282 0.4154 0.0577  -0.0048 -0.0834 994  ILE A O   
2582 C CB  . ILE A 338 ? 0.2217 0.3477 0.3961 0.0537  -0.0043 -0.0830 994  ILE A CB  
2583 C CG1 . ILE A 338 ? 0.2142 0.3486 0.3904 0.0574  -0.0014 -0.0907 994  ILE A CG1 
2584 C CG2 . ILE A 338 ? 0.2400 0.3749 0.4105 0.0485  -0.0056 -0.0775 994  ILE A CG2 
2585 C CD1 . ILE A 338 ? 0.2840 0.4286 0.4643 0.0624  -0.0008 -0.0888 994  ILE A CD1 
2586 N N   . ALA A 339 ? 0.1899 0.2903 0.3668 0.0554  -0.0017 -0.0981 995  ALA A N   
2587 C CA  . ALA A 339 ? 0.2105 0.2964 0.3917 0.0600  -0.0003 -0.1027 995  ALA A CA  
2588 C C   . ALA A 339 ? 0.2387 0.3094 0.4200 0.0559  -0.0018 -0.1003 995  ALA A C   
2589 O O   . ALA A 339 ? 0.2265 0.2829 0.4122 0.0600  -0.0012 -0.1001 995  ALA A O   
2590 C CB  . ALA A 339 ? 0.2245 0.3127 0.4050 0.0611  0.0028  -0.1143 995  ALA A CB  
2591 N N   . GLN A 340 ? 0.1939 0.2683 0.3711 0.0480  -0.0038 -0.0977 996  GLN A N   
2592 C CA  . GLN A 340 ? 0.1902 0.2546 0.3675 0.0426  -0.0055 -0.0950 996  GLN A CA  
2593 C C   . GLN A 340 ? 0.2503 0.3078 0.4305 0.0444  -0.0067 -0.0847 996  GLN A C   
2594 O O   . GLN A 340 ? 0.2573 0.3075 0.4382 0.0400  -0.0077 -0.0815 996  GLN A O   
2595 C CB  . GLN A 340 ? 0.1976 0.2724 0.3702 0.0344  -0.0073 -0.0951 996  GLN A CB  
2596 C CG  . GLN A 340 ? 0.3210 0.4003 0.4897 0.0304  -0.0066 -0.1055 996  GLN A CG  
2597 C CD  . GLN A 340 ? 0.4656 0.5563 0.6297 0.0224  -0.0091 -0.1043 996  GLN A CD  
2598 O OE1 . GLN A 340 ? 0.2766 0.3811 0.4365 0.0212  -0.0094 -0.1045 996  GLN A OE1 
2599 N NE2 . GLN A 340 ? 0.2081 0.2938 0.3733 0.0168  -0.0111 -0.1026 996  GLN A NE2 
2600 N N   . VAL A 341 ? 0.2082 0.2693 0.3900 0.0506  -0.0065 -0.0798 997  VAL A N   
2601 C CA  . VAL A 341 ? 0.1940 0.2510 0.3775 0.0527  -0.0075 -0.0705 997  VAL A CA  
2602 C C   . VAL A 341 ? 0.2367 0.2855 0.4245 0.0606  -0.0068 -0.0689 997  VAL A C   
2603 O O   . VAL A 341 ? 0.2109 0.2656 0.4004 0.0662  -0.0060 -0.0718 997  VAL A O   
2604 C CB  . VAL A 341 ? 0.2258 0.2954 0.4066 0.0522  -0.0086 -0.0650 997  VAL A CB  
2605 C CG1 . VAL A 341 ? 0.2195 0.2852 0.4008 0.0536  -0.0094 -0.0563 997  VAL A CG1 
2606 C CG2 . VAL A 341 ? 0.2119 0.2898 0.3892 0.0455  -0.0094 -0.0658 997  VAL A CG2 
2607 N N   . ASN A 342 ? 0.1807 0.2167 0.3705 0.0609  -0.0071 -0.0636 998  ASN A N   
2608 C CA  . ASN A 342 ? 0.1806 0.2085 0.3744 0.0684  -0.0070 -0.0594 998  ASN A CA  
2609 C C   . ASN A 342 ? 0.2379 0.2657 0.4302 0.0677  -0.0085 -0.0488 998  ASN A C   
2610 O O   . ASN A 342 ? 0.2420 0.2613 0.4338 0.0630  -0.0085 -0.0450 998  ASN A O   
2611 C CB  . ASN A 342 ? 0.1997 0.2101 0.3975 0.0700  -0.0056 -0.0633 998  ASN A CB  
2612 C CG  . ASN A 342 ? 0.3841 0.3862 0.5872 0.0794  -0.0053 -0.0595 998  ASN A CG  
2613 O OD1 . ASN A 342 ? 0.3205 0.3057 0.5269 0.0807  -0.0046 -0.0587 998  ASN A OD1 
2614 N ND2 . ASN A 342 ? 0.2559 0.2694 0.4603 0.0860  -0.0061 -0.0566 998  ASN A ND2 
2615 N N   . LEU A 343 ? 0.2157 0.2543 0.4071 0.0715  -0.0096 -0.0445 999  LEU A N   
2616 C CA  . LEU A 343 ? 0.2212 0.2618 0.4099 0.0709  -0.0108 -0.0353 999  LEU A CA  
2617 C C   . LEU A 343 ? 0.2497 0.2775 0.4408 0.0742  -0.0111 -0.0286 999  LEU A C   
2618 O O   . LEU A 343 ? 0.2314 0.2539 0.4269 0.0810  -0.0111 -0.0290 999  LEU A O   
2619 C CB  . LEU A 343 ? 0.2191 0.2742 0.4061 0.0739  -0.0121 -0.0333 999  LEU A CB  
2620 C CG  . LEU A 343 ? 0.2752 0.3427 0.4593 0.0701  -0.0119 -0.0381 999  LEU A CG  
2621 C CD1 . LEU A 343 ? 0.2694 0.3495 0.4520 0.0723  -0.0133 -0.0356 999  LEU A CD1 
2622 C CD2 . LEU A 343 ? 0.2759 0.3427 0.4565 0.0627  -0.0114 -0.0376 999  LEU A CD2 
2623 N N   . LYS A 344 ? 0.2028 0.2255 0.3914 0.0694  -0.0110 -0.0224 1000 LYS A N   
2624 C CA  . LYS A 344 ? 0.2039 0.2135 0.3944 0.0712  -0.0110 -0.0152 1000 LYS A CA  
2625 C C   . LYS A 344 ? 0.2546 0.2692 0.4414 0.0724  -0.0121 -0.0051 1000 LYS A C   
2626 O O   . LYS A 344 ? 0.2516 0.2617 0.4400 0.0781  -0.0133 0.0012  1000 LYS A O   
2627 C CB  . LYS A 344 ? 0.2227 0.2196 0.4143 0.0645  -0.0095 -0.0162 1000 LYS A CB  
2628 C CG  . LYS A 344 ? 0.3472 0.3349 0.5430 0.0647  -0.0085 -0.0256 1000 LYS A CG  
2629 C CD  . LYS A 344 ? 0.5283 0.4999 0.7290 0.0709  -0.0081 -0.0235 1000 LYS A CD  
2630 C CE  . LYS A 344 ? 0.7457 0.7141 0.9503 0.0759  -0.0072 -0.0336 1000 LYS A CE  
2631 N NZ  . LYS A 344 ? 0.9380 0.8957 1.1481 0.0854  -0.0071 -0.0303 1000 LYS A NZ  
2632 N N   . TYR A 345 ? 0.2197 0.2442 0.4016 0.0674  -0.0119 -0.0038 1001 TYR A N   
2633 C CA  . TYR A 345 ? 0.2197 0.2504 0.3966 0.0675  -0.0125 0.0044  1001 TYR A CA  
2634 C C   . TYR A 345 ? 0.2611 0.3069 0.4336 0.0661  -0.0129 0.0018  1001 TYR A C   
2635 O O   . TYR A 345 ? 0.2599 0.3103 0.4327 0.0634  -0.0122 -0.0052 1001 TYR A O   
2636 C CB  . TYR A 345 ? 0.2380 0.2621 0.4130 0.0618  -0.0108 0.0106  1001 TYR A CB  
2637 C CG  . TYR A 345 ? 0.2706 0.2780 0.4500 0.0619  -0.0104 0.0140  1001 TYR A CG  
2638 C CD1 . TYR A 345 ? 0.2860 0.2865 0.4657 0.0667  -0.0115 0.0227  1001 TYR A CD1 
2639 C CD2 . TYR A 345 ? 0.2798 0.2780 0.4629 0.0570  -0.0089 0.0086  1001 TYR A CD2 
2640 C CE1 . TYR A 345 ? 0.2868 0.2698 0.4709 0.0669  -0.0110 0.0261  1001 TYR A CE1 
2641 C CE2 . TYR A 345 ? 0.3004 0.2817 0.4877 0.0564  -0.0083 0.0109  1001 TYR A CE2 
2642 C CZ  . TYR A 345 ? 0.3907 0.3635 0.5786 0.0615  -0.0092 0.0197  1001 TYR A CZ  
2643 O OH  . TYR A 345 ? 0.4282 0.3823 0.6204 0.0609  -0.0084 0.0223  1001 TYR A OH  
2644 N N   . LEU A 346 ? 0.1987 0.2517 0.3665 0.0676  -0.0140 0.0077  1002 LEU A N   
2645 C CA  . LEU A 346 ? 0.1863 0.2523 0.3487 0.0658  -0.0142 0.0062  1002 LEU A CA  
2646 C C   . LEU A 346 ? 0.2536 0.3212 0.4101 0.0632  -0.0133 0.0134  1002 LEU A C   
2647 O O   . LEU A 346 ? 0.2795 0.3442 0.4350 0.0659  -0.0145 0.0211  1002 LEU A O   
2648 C CB  . LEU A 346 ? 0.1817 0.2575 0.3444 0.0706  -0.0169 0.0049  1002 LEU A CB  
2649 C CG  . LEU A 346 ? 0.2372 0.3261 0.3942 0.0682  -0.0174 0.0026  1002 LEU A CG  
2650 C CD1 . LEU A 346 ? 0.2568 0.3467 0.4131 0.0631  -0.0151 -0.0040 1002 LEU A CD1 
2651 C CD2 . LEU A 346 ? 0.2173 0.3162 0.3762 0.0723  -0.0201 0.0007  1002 LEU A CD2 
2652 N N   . LEU A 347 ? 0.1971 0.2692 0.3499 0.0583  -0.0110 0.0113  1003 LEU A N   
2653 C CA  . LEU A 347 ? 0.1858 0.2611 0.3325 0.0555  -0.0094 0.0170  1003 LEU A CA  
2654 C C   . LEU A 347 ? 0.2268 0.3139 0.3671 0.0546  -0.0093 0.0141  1003 LEU A C   
2655 O O   . LEU A 347 ? 0.2050 0.2955 0.3462 0.0534  -0.0088 0.0070  1003 LEU A O   
2656 C CB  . LEU A 347 ? 0.1860 0.2570 0.3344 0.0505  -0.0059 0.0168  1003 LEU A CB  
2657 C CG  . LEU A 347 ? 0.2391 0.2990 0.3913 0.0488  -0.0051 0.0224  1003 LEU A CG  
2658 C CD1 . LEU A 347 ? 0.2473 0.2976 0.4067 0.0503  -0.0065 0.0182  1003 LEU A CD1 
2659 C CD2 . LEU A 347 ? 0.2230 0.2838 0.3758 0.0430  -0.0014 0.0229  1003 LEU A CD2 
2660 N N   . LYS A 348 ? 0.2047 0.2976 0.3381 0.0548  -0.0098 0.0196  1004 LYS A N   
2661 C CA  . LYS A 348 ? 0.2149 0.3187 0.3407 0.0529  -0.0093 0.0168  1004 LYS A CA  
2662 C C   . LYS A 348 ? 0.2931 0.3970 0.4150 0.0487  -0.0049 0.0182  1004 LYS A C   
2663 O O   . LYS A 348 ? 0.3097 0.4109 0.4300 0.0480  -0.0040 0.0258  1004 LYS A O   
2664 C CB  . LYS A 348 ? 0.2512 0.3632 0.3711 0.0552  -0.0127 0.0218  1004 LYS A CB  
2665 C CG  . LYS A 348 ? 0.2575 0.3810 0.3687 0.0524  -0.0124 0.0179  1004 LYS A CG  
2666 C CD  . LYS A 348 ? 0.3125 0.4462 0.4201 0.0549  -0.0172 0.0208  1004 LYS A CD  
2667 C CE  . LYS A 348 ? 0.4054 0.5477 0.5025 0.0530  -0.0173 0.0264  1004 LYS A CE  
2668 N NZ  . LYS A 348 ? 0.4079 0.5603 0.5026 0.0561  -0.0228 0.0317  1004 LYS A NZ  
2669 N N   . LEU A 349 ? 0.2471 0.3537 0.3683 0.0462  -0.0020 0.0113  1005 LEU A N   
2670 C CA  . LEU A 349 ? 0.2377 0.3457 0.3566 0.0429  0.0027  0.0116  1005 LEU A CA  
2671 C C   . LEU A 349 ? 0.2414 0.3579 0.3523 0.0413  0.0050  0.0070  1005 LEU A C   
2672 O O   . LEU A 349 ? 0.1947 0.3136 0.3045 0.0416  0.0037  0.0005  1005 LEU A O   
2673 C CB  . LEU A 349 ? 0.2406 0.3435 0.3678 0.0417  0.0051  0.0077  1005 LEU A CB  
2674 C CG  . LEU A 349 ? 0.3048 0.3989 0.4402 0.0421  0.0035  0.0099  1005 LEU A CG  
2675 C CD1 . LEU A 349 ? 0.3168 0.4094 0.4589 0.0406  0.0051  0.0047  1005 LEU A CD1 
2676 C CD2 . LEU A 349 ? 0.3316 0.4221 0.4677 0.0401  0.0050  0.0175  1005 LEU A CD2 
2677 N N   . LYS A 350 ? 0.2070 0.3279 0.3124 0.0391  0.0088  0.0098  1006 LYS A N   
2678 C CA  . LYS A 350 ? 0.1915 0.3198 0.2892 0.0373  0.0121  0.0044  1006 LYS A CA  
2679 C C   . LYS A 350 ? 0.2199 0.3462 0.3232 0.0364  0.0175  0.0003  1006 LYS A C   
2680 O O   . LYS A 350 ? 0.2150 0.3405 0.3220 0.0353  0.0201  0.0052  1006 LYS A O   
2681 C CB  . LYS A 350 ? 0.2071 0.3434 0.2943 0.0356  0.0131  0.0101  1006 LYS A CB  
2682 C CG  . LYS A 350 ? 0.4098 0.5538 0.4891 0.0332  0.0186  0.0047  1006 LYS A CG  
2683 C CD  . LYS A 350 ? 0.4798 0.6313 0.5485 0.0321  0.0168  -0.0005 1006 LYS A CD  
2684 C CE  . LYS A 350 ? 0.4975 0.6550 0.5587 0.0298  0.0228  -0.0076 1006 LYS A CE  
2685 N NZ  . LYS A 350 ? 0.5127 0.6782 0.5623 0.0276  0.0211  -0.0129 1006 LYS A NZ  
2686 N N   . PHE A 351 ? 0.1677 0.2933 0.2724 0.0369  0.0188  -0.0080 1007 PHE A N   
2687 C CA  . PHE A 351 ? 0.1675 0.2919 0.2782 0.0372  0.0236  -0.0124 1007 PHE A CA  
2688 C C   . PHE A 351 ? 0.2400 0.3713 0.3431 0.0361  0.0291  -0.0156 1007 PHE A C   
2689 O O   . PHE A 351 ? 0.2619 0.3958 0.3569 0.0354  0.0291  -0.0211 1007 PHE A O   
2690 C CB  . PHE A 351 ? 0.1751 0.2944 0.2905 0.0386  0.0221  -0.0192 1007 PHE A CB  
2691 C CG  . PHE A 351 ? 0.1655 0.2791 0.2886 0.0395  0.0177  -0.0172 1007 PHE A CG  
2692 C CD1 . PHE A 351 ? 0.1620 0.2746 0.2834 0.0399  0.0128  -0.0146 1007 PHE A CD1 
2693 C CD2 . PHE A 351 ? 0.1643 0.2745 0.2967 0.0404  0.0186  -0.0182 1007 PHE A CD2 
2694 C CE1 . PHE A 351 ? 0.1651 0.2729 0.2936 0.0409  0.0094  -0.0136 1007 PHE A CE1 
2695 C CE2 . PHE A 351 ? 0.1801 0.2860 0.3186 0.0408  0.0147  -0.0170 1007 PHE A CE2 
2696 C CZ  . PHE A 351 ? 0.1536 0.2579 0.2899 0.0410  0.0104  -0.0150 1007 PHE A CZ  
2697 N N   . ASN A 352 ? 0.1899 0.3251 0.2951 0.0354  0.0338  -0.0125 1008 ASN A N   
2698 C CA  . ASN A 352 ? 0.1958 0.3387 0.2946 0.0346  0.0400  -0.0160 1008 ASN A CA  
2699 C C   . ASN A 352 ? 0.2545 0.3962 0.3616 0.0371  0.0449  -0.0222 1008 ASN A C   
2700 O O   . ASN A 352 ? 0.2366 0.3803 0.3526 0.0375  0.0476  -0.0190 1008 ASN A O   
2701 C CB  . ASN A 352 ? 0.2610 0.4113 0.3555 0.0321  0.0427  -0.0080 1008 ASN A CB  
2702 C CG  . ASN A 352 ? 0.5582 0.7182 0.6476 0.0312  0.0503  -0.0112 1008 ASN A CG  
2703 O OD1 . ASN A 352 ? 0.3263 0.4888 0.4098 0.0320  0.0535  -0.0200 1008 ASN A OD1 
2704 N ND2 . ASN A 352 ? 0.5456 0.7116 0.6368 0.0291  0.0537  -0.0041 1008 ASN A ND2 
2705 N N   . PHE A 353 ? 0.2266 0.3650 0.3313 0.0385  0.0458  -0.0310 1009 PHE A N   
2706 C CA  . PHE A 353 ? 0.2336 0.3693 0.3459 0.0417  0.0501  -0.0373 1009 PHE A CA  
2707 C C   . PHE A 353 ? 0.2835 0.4274 0.3950 0.0427  0.0582  -0.0398 1009 PHE A C   
2708 O O   . PHE A 353 ? 0.2619 0.4120 0.3623 0.0407  0.0611  -0.0420 1009 PHE A O   
2709 C CB  . PHE A 353 ? 0.2535 0.3816 0.3628 0.0424  0.0486  -0.0456 1009 PHE A CB  
2710 C CG  . PHE A 353 ? 0.2666 0.3878 0.3791 0.0418  0.0415  -0.0432 1009 PHE A CG  
2711 C CD1 . PHE A 353 ? 0.2903 0.4057 0.4140 0.0441  0.0398  -0.0419 1009 PHE A CD1 
2712 C CD2 . PHE A 353 ? 0.2657 0.3878 0.3702 0.0391  0.0365  -0.0419 1009 PHE A CD2 
2713 C CE1 . PHE A 353 ? 0.2874 0.3977 0.4134 0.0433  0.0338  -0.0400 1009 PHE A CE1 
2714 C CE2 . PHE A 353 ? 0.2854 0.4027 0.3935 0.0389  0.0305  -0.0399 1009 PHE A CE2 
2715 C CZ  . PHE A 353 ? 0.2618 0.3731 0.3802 0.0408  0.0294  -0.0393 1009 PHE A CZ  
2716 N N   . LYS A 354 ? 0.2803 0.4257 0.4038 0.0457  0.0617  -0.0391 1010 LYS A N   
2717 C CA  . LYS A 354 ? 0.2921 0.4465 0.4182 0.0476  0.0698  -0.0414 1010 LYS A CA  
2718 C C   . LYS A 354 ? 0.3856 0.5357 0.5126 0.0521  0.0748  -0.0519 1010 LYS A C   
2719 O O   . LYS A 354 ? 0.3894 0.5465 0.5176 0.0545  0.0824  -0.0560 1010 LYS A O   
2720 C CB  . LYS A 354 ? 0.3021 0.4619 0.4422 0.0487  0.0709  -0.0348 1010 LYS A CB  
2721 C CG  . LYS A 354 ? 0.4390 0.5985 0.5817 0.0447  0.0651  -0.0252 1010 LYS A CG  
2722 C CD  . LYS A 354 ? 0.5225 0.6883 0.6559 0.0399  0.0657  -0.0191 1010 LYS A CD  
2723 C CE  . LYS A 354 ? 0.6328 0.8033 0.7745 0.0367  0.0652  -0.0101 1010 LYS A CE  
2724 N NZ  . LYS A 354 ? 0.7339 0.8957 0.8832 0.0361  0.0583  -0.0065 1010 LYS A NZ  
2725 N N   . THR A 355 ? 0.3583 0.4968 0.4851 0.0530  0.0707  -0.0562 1011 THR A N   
2726 C CA  . THR A 355 ? 0.5788 0.7091 0.7072 0.0568  0.0741  -0.0656 1011 THR A CA  
2727 C C   . THR A 355 ? 0.9933 1.1200 1.1072 0.0537  0.0746  -0.0739 1011 THR A C   
2728 O O   . THR A 355 ? 0.6258 0.7611 0.7290 0.0508  0.0774  -0.0754 1011 THR A O   
2729 C CB  . THR A 355 ? 0.6255 0.7455 0.7647 0.0594  0.0694  -0.0637 1011 THR A CB  
2730 O OG1 . THR A 355 ? 0.5893 0.7044 0.7238 0.0553  0.0617  -0.0604 1011 THR A OG1 
2731 C CG2 . THR A 355 ? 0.5642 0.6893 0.7181 0.0627  0.0695  -0.0567 1011 THR A CG2 
2732 N N   . LYS B 6   ? 0.1691 0.7163 0.4835 0.0781  -0.1031 0.2557  662  LYS B N   
2733 C CA  . LYS B 6   ? 0.1935 0.6819 0.4967 0.0751  -0.0959 0.2389  662  LYS B CA  
2734 C C   . LYS B 6   ? 0.2252 0.7011 0.5127 0.0457  -0.0984 0.2244  662  LYS B C   
2735 O O   . LYS B 6   ? 0.2395 0.7346 0.5169 0.0296  -0.1056 0.2291  662  LYS B O   
2736 C CB  . LYS B 6   ? 0.2595 0.7126 0.5556 0.0895  -0.0933 0.2461  662  LYS B CB  
2737 C CG  . LYS B 6   ? 0.5329 0.9316 0.8253 0.0988  -0.0846 0.2344  662  LYS B CG  
2738 C CD  . LYS B 6   ? 0.6777 1.0413 0.9619 0.1114  -0.0828 0.2435  662  LYS B CD  
2739 C CE  . LYS B 6   ? 0.6821 1.0453 0.9730 0.1412  -0.0804 0.2577  662  LYS B CE  
2740 N NZ  . LYS B 6   ? 0.6893 1.0043 0.9684 0.1511  -0.0775 0.2628  662  LYS B NZ  
2741 N N   . SER B 7   ? 0.1658 0.6078 0.4494 0.0400  -0.0922 0.2071  663  SER B N   
2742 C CA  . SER B 7   ? 0.1539 0.5776 0.4223 0.0165  -0.0922 0.1917  663  SER B CA  
2743 C C   . SER B 7   ? 0.2305 0.6366 0.4803 0.0041  -0.0940 0.1911  663  SER B C   
2744 O O   . SER B 7   ? 0.2258 0.6081 0.4734 0.0138  -0.0910 0.1952  663  SER B O   
2745 C CB  . SER B 7   ? 0.1674 0.5548 0.4372 0.0197  -0.0841 0.1764  663  SER B CB  
2746 O OG  . SER B 7   ? 0.1308 0.5003 0.3863 0.0001  -0.0831 0.1622  663  SER B OG  
2747 N N   . LYS B 8   ? 0.2092 0.6243 0.4433 -0.0182 -0.0985 0.1850  664  LYS B N   
2748 C CA  . LYS B 8   ? 0.2030 0.6020 0.4149 -0.0321 -0.0995 0.1816  664  LYS B CA  
2749 C C   . LYS B 8   ? 0.2201 0.5774 0.4212 -0.0373 -0.0914 0.1647  664  LYS B C   
2750 O O   . LYS B 8   ? 0.2287 0.5684 0.4114 -0.0458 -0.0896 0.1606  664  LYS B O   
2751 C CB  . LYS B 8   ? 0.2417 0.6679 0.4380 -0.0537 -0.1084 0.1822  664  LYS B CB  
2752 C CG  . LYS B 8   ? 0.5284 0.9982 0.7306 -0.0519 -0.1177 0.2006  664  LYS B CG  
2753 C CD  . LYS B 8   ? 0.6809 1.1788 0.8674 -0.0768 -0.1275 0.2002  664  LYS B CD  
2754 C CE  . LYS B 8   ? 0.8284 1.3770 1.0237 -0.0755 -0.1377 0.2199  664  LYS B CE  
2755 N NZ  . LYS B 8   ? 0.9136 1.4926 1.0944 -0.1025 -0.1486 0.2199  664  LYS B NZ  
2756 N N   . LEU B 9   ? 0.1606 0.5045 0.3728 -0.0316 -0.0863 0.1558  665  LEU B N   
2757 C CA  . LEU B 9   ? 0.1626 0.4715 0.3674 -0.0349 -0.0789 0.1412  665  LEU B CA  
2758 C C   . LEU B 9   ? 0.2219 0.5051 0.4246 -0.0273 -0.0736 0.1428  665  LEU B C   
2759 O O   . LEU B 9   ? 0.1898 0.4747 0.4030 -0.0146 -0.0741 0.1539  665  LEU B O   
2760 C CB  . LEU B 9   ? 0.1516 0.4540 0.3708 -0.0276 -0.0751 0.1340  665  LEU B CB  
2761 C CG  . LEU B 9   ? 0.1799 0.4967 0.3972 -0.0392 -0.0776 0.1273  665  LEU B CG  
2762 C CD1 . LEU B 9   ? 0.1616 0.4801 0.3969 -0.0276 -0.0742 0.1250  665  LEU B CD1 
2763 C CD2 . LEU B 9   ? 0.2358 0.5273 0.4325 -0.0540 -0.0746 0.1135  665  LEU B CD2 
2764 N N   . PRO B 10  ? 0.1969 0.4560 0.3859 -0.0344 -0.0681 0.1328  666  PRO B N   
2765 C CA  . PRO B 10  ? 0.1910 0.4303 0.3803 -0.0284 -0.0628 0.1356  666  PRO B CA  
2766 C C   . PRO B 10  ? 0.2116 0.4388 0.4196 -0.0152 -0.0604 0.1378  666  PRO B C   
2767 O O   . PRO B 10  ? 0.1942 0.4193 0.4112 -0.0121 -0.0595 0.1309  666  PRO B O   
2768 C CB  . PRO B 10  ? 0.2277 0.4478 0.4028 -0.0361 -0.0565 0.1231  666  PRO B CB  
2769 C CG  . PRO B 10  ? 0.2875 0.5152 0.4463 -0.0483 -0.0597 0.1160  666  PRO B CG  
2770 C CD  . PRO B 10  ? 0.2190 0.4677 0.3916 -0.0470 -0.0660 0.1195  666  PRO B CD  
2771 N N   . LYS B 11  ? 0.1921 0.4102 0.4039 -0.0083 -0.0596 0.1475  667  LYS B N   
2772 C CA  . LYS B 11  ? 0.1902 0.3904 0.4146 0.0028  -0.0577 0.1496  667  LYS B CA  
2773 C C   . LYS B 11  ? 0.2019 0.3829 0.4297 0.0006  -0.0527 0.1370  667  LYS B C   
2774 O O   . LYS B 11  ? 0.1701 0.3451 0.4072 0.0082  -0.0526 0.1333  667  LYS B O   
2775 C CB  . LYS B 11  ? 0.2403 0.4288 0.4634 0.0070  -0.0578 0.1623  667  LYS B CB  
2776 C CG  . LYS B 11  ? 0.3743 0.5491 0.6063 0.0212  -0.0589 0.1691  667  LYS B CG  
2777 C CD  . LYS B 11  ? 0.4887 0.6324 0.7198 0.0203  -0.0558 0.1704  667  LYS B CD  
2778 C CE  . LYS B 11  ? 0.5753 0.6969 0.8093 0.0338  -0.0567 0.1765  667  LYS B CE  
2779 N NZ  . LYS B 11  ? 0.6028 0.7178 0.8433 0.0414  -0.0554 0.1659  667  LYS B NZ  
2780 N N   . PRO B 12  ? 0.1698 0.3438 0.3898 -0.0084 -0.0484 0.1299  668  PRO B N   
2781 C CA  . PRO B 12  ? 0.1755 0.3356 0.4000 -0.0094 -0.0442 0.1191  668  PRO B CA  
2782 C C   . PRO B 12  ? 0.2025 0.3681 0.4300 -0.0088 -0.0451 0.1095  668  PRO B C   
2783 O O   . PRO B 12  ? 0.2032 0.3580 0.4384 -0.0052 -0.0435 0.1036  668  PRO B O   
2784 C CB  . PRO B 12  ? 0.2078 0.3656 0.4220 -0.0170 -0.0392 0.1157  668  PRO B CB  
2785 C CG  . PRO B 12  ? 0.2504 0.4152 0.4566 -0.0191 -0.0401 0.1261  668  PRO B CG  
2786 C CD  . PRO B 12  ? 0.1835 0.3624 0.3896 -0.0164 -0.0464 0.1318  668  PRO B CD  
2787 N N   . VAL B 13  ? 0.1597 0.3426 0.3803 -0.0134 -0.0481 0.1087  669  VAL B N   
2788 C CA  . VAL B 13  ? 0.1585 0.3500 0.3810 -0.0154 -0.0495 0.1014  669  VAL B CA  
2789 C C   . VAL B 13  ? 0.1949 0.3949 0.4322 -0.0044 -0.0520 0.1059  669  VAL B C   
2790 O O   . VAL B 13  ? 0.1635 0.3610 0.4071 -0.0014 -0.0505 0.0993  669  VAL B O   
2791 C CB  . VAL B 13  ? 0.1930 0.3996 0.4010 -0.0268 -0.0528 0.1001  669  VAL B CB  
2792 C CG1 . VAL B 13  ? 0.1792 0.4003 0.3909 -0.0302 -0.0559 0.0963  669  VAL B CG1 
2793 C CG2 . VAL B 13  ? 0.1999 0.3909 0.3898 -0.0352 -0.0483 0.0922  669  VAL B CG2 
2794 N N   . GLN B 14  ? 0.1554 0.3645 0.3970 0.0032  -0.0551 0.1177  670  GLN B N   
2795 C CA  . GLN B 14  ? 0.1415 0.3574 0.3948 0.0174  -0.0564 0.1240  670  GLN B CA  
2796 C C   . GLN B 14  ? 0.2026 0.3911 0.4609 0.0263  -0.0525 0.1192  670  GLN B C   
2797 O O   . GLN B 14  ? 0.1869 0.3768 0.4520 0.0350  -0.0513 0.1160  670  GLN B O   
2798 C CB  . GLN B 14  ? 0.1507 0.3766 0.4046 0.0247  -0.0599 0.1386  670  GLN B CB  
2799 C CG  . GLN B 14  ? 0.2444 0.5018 0.4937 0.0166  -0.0653 0.1451  670  GLN B CG  
2800 C CD  . GLN B 14  ? 0.2728 0.5471 0.5265 0.0278  -0.0693 0.1612  670  GLN B CD  
2801 O OE1 . GLN B 14  ? 0.2535 0.5217 0.5157 0.0447  -0.0680 0.1673  670  GLN B OE1 
2802 N NE2 . GLN B 14  ? 0.0955 0.3905 0.3417 0.0194  -0.0743 0.1686  670  GLN B NE2 
2803 N N   . ASP B 15  ? 0.1796 0.3443 0.4334 0.0228  -0.0505 0.1189  671  ASP B N   
2804 C CA  . ASP B 15  ? 0.1823 0.3194 0.4380 0.0268  -0.0479 0.1147  671  ASP B CA  
2805 C C   . ASP B 15  ? 0.2025 0.3360 0.4600 0.0227  -0.0454 0.1018  671  ASP B C   
2806 O O   . ASP B 15  ? 0.1960 0.3147 0.4560 0.0292  -0.0443 0.0973  671  ASP B O   
2807 C CB  . ASP B 15  ? 0.2279 0.3469 0.4787 0.0203  -0.0471 0.1190  671  ASP B CB  
2808 C CG  . ASP B 15  ? 0.3845 0.5001 0.6323 0.0251  -0.0494 0.1326  671  ASP B CG  
2809 O OD1 . ASP B 15  ? 0.4052 0.5179 0.6548 0.0382  -0.0510 0.1385  671  ASP B OD1 
2810 O OD2 . ASP B 15  ? 0.4583 0.5736 0.7012 0.0170  -0.0492 0.1382  671  ASP B OD2 
2811 N N   . LEU B 16  ? 0.1622 0.3076 0.4162 0.0125  -0.0446 0.0961  672  LEU B N   
2812 C CA  . LEU B 16  ? 0.1677 0.3106 0.4220 0.0084  -0.0422 0.0849  672  LEU B CA  
2813 C C   . LEU B 16  ? 0.2328 0.3870 0.4925 0.0147  -0.0428 0.0820  672  LEU B C   
2814 O O   . LEU B 16  ? 0.2364 0.3806 0.4988 0.0178  -0.0410 0.0751  672  LEU B O   
2815 C CB  . LEU B 16  ? 0.1695 0.3189 0.4149 -0.0025 -0.0408 0.0805  672  LEU B CB  
2816 C CG  . LEU B 16  ? 0.2280 0.3734 0.4715 -0.0062 -0.0383 0.0700  672  LEU B CG  
2817 C CD1 . LEU B 16  ? 0.2306 0.3595 0.4764 -0.0060 -0.0352 0.0660  672  LEU B CD1 
2818 C CD2 . LEU B 16  ? 0.2682 0.4198 0.4992 -0.0153 -0.0378 0.0665  672  LEU B CD2 
2819 N N   . ILE B 17  ? 0.1973 0.3751 0.4585 0.0160  -0.0456 0.0878  673  ILE B N   
2820 C CA  . ILE B 17  ? 0.1771 0.3742 0.4450 0.0218  -0.0461 0.0878  673  ILE B CA  
2821 C C   . ILE B 17  ? 0.1939 0.3802 0.4680 0.0382  -0.0441 0.0893  673  ILE B C   
2822 O O   . ILE B 17  ? 0.1791 0.3675 0.4566 0.0434  -0.0418 0.0839  673  ILE B O   
2823 C CB  . ILE B 17  ? 0.2061 0.4351 0.4752 0.0189  -0.0505 0.0969  673  ILE B CB  
2824 C CG1 . ILE B 17  ? 0.2259 0.4608 0.4833 0.0010  -0.0527 0.0938  673  ILE B CG1 
2825 C CG2 . ILE B 17  ? 0.1886 0.4453 0.4676 0.0264  -0.0510 0.1002  673  ILE B CG2 
2826 C CD1 . ILE B 17  ? 0.2846 0.5102 0.5348 -0.0097 -0.0505 0.0823  673  ILE B CD1 
2827 N N   . LYS B 18  ? 0.1460 0.3188 0.4192 0.0464  -0.0448 0.0968  674  LYS B N   
2828 C CA  . LYS B 18  ? 0.1605 0.3155 0.4343 0.0630  -0.0428 0.0988  674  LYS B CA  
2829 C C   . LYS B 18  ? 0.2313 0.3580 0.5008 0.0617  -0.0402 0.0880  674  LYS B C   
2830 O O   . LYS B 18  ? 0.2199 0.3400 0.4891 0.0729  -0.0376 0.0841  674  LYS B O   
2831 C CB  . LYS B 18  ? 0.1962 0.3366 0.4661 0.0692  -0.0444 0.1095  674  LYS B CB  
2832 C CG  . LYS B 18  ? 0.3841 0.5526 0.6585 0.0771  -0.0470 0.1225  674  LYS B CG  
2833 C CD  . LYS B 18  ? 0.6227 0.7706 0.8920 0.0884  -0.0477 0.1334  674  LYS B CD  
2834 C CE  . LYS B 18  ? 0.7980 0.9446 1.0628 0.0764  -0.0508 0.1402  674  LYS B CE  
2835 N NZ  . LYS B 18  ? 0.9107 1.0346 1.1692 0.0865  -0.0515 0.1516  674  LYS B NZ  
2836 N N   . MET B 19  ? 0.2399 0.3522 0.5056 0.0483  -0.0407 0.0836  675  MET B N   
2837 C CA  . MET B 19  ? 0.2600 0.3491 0.5220 0.0430  -0.0395 0.0747  675  MET B CA  
2838 C C   . MET B 19  ? 0.2919 0.3902 0.5561 0.0432  -0.0375 0.0654  675  MET B C   
2839 O O   . MET B 19  ? 0.2903 0.3732 0.5513 0.0496  -0.0360 0.0597  675  MET B O   
2840 C CB  . MET B 19  ? 0.3045 0.3922 0.5653 0.0284  -0.0402 0.0745  675  MET B CB  
2841 C CG  . MET B 19  ? 0.3835 0.4486 0.6413 0.0221  -0.0403 0.0704  675  MET B CG  
2842 S SD  . MET B 19  ? 0.4570 0.5299 0.7154 0.0080  -0.0396 0.0728  675  MET B SD  
2843 C CE  . MET B 19  ? 0.4263 0.4812 0.6844 0.0006  -0.0402 0.0678  675  MET B CE  
2844 N N   . ILE B 20  ? 0.2219 0.3442 0.4893 0.0360  -0.0375 0.0643  676  ILE B N   
2845 C CA  . ILE B 20  ? 0.1996 0.3335 0.4681 0.0323  -0.0359 0.0570  676  ILE B CA  
2846 C C   . ILE B 20  ? 0.1963 0.3449 0.4689 0.0436  -0.0343 0.0573  676  ILE B C   
2847 O O   . ILE B 20  ? 0.1737 0.3224 0.4458 0.0437  -0.0322 0.0504  676  ILE B O   
2848 C CB  . ILE B 20  ? 0.2382 0.3874 0.5044 0.0197  -0.0370 0.0575  676  ILE B CB  
2849 C CG1 . ILE B 20  ? 0.2584 0.3919 0.5195 0.0109  -0.0358 0.0522  676  ILE B CG1 
2850 C CG2 . ILE B 20  ? 0.2351 0.4074 0.5022 0.0158  -0.0372 0.0565  676  ILE B CG2 
2851 C CD1 . ILE B 20  ? 0.4784 0.6181 0.7325 0.0007  -0.0358 0.0528  676  ILE B CD1 
2852 N N   . PHE B 21  ? 0.1445 0.3069 0.4213 0.0539  -0.0349 0.0661  677  PHE B N   
2853 C CA  . PHE B 21  ? 0.1286 0.3109 0.4107 0.0669  -0.0325 0.0684  677  PHE B CA  
2854 C C   . PHE B 21  ? 0.2313 0.3927 0.5097 0.0863  -0.0293 0.0690  677  PHE B C   
2855 O O   . PHE B 21  ? 0.2153 0.3935 0.4976 0.1017  -0.0263 0.0730  677  PHE B O   
2856 C CB  . PHE B 21  ? 0.1316 0.3517 0.4215 0.0660  -0.0350 0.0787  677  PHE B CB  
2857 C CG  . PHE B 21  ? 0.1211 0.3627 0.4115 0.0487  -0.0369 0.0761  677  PHE B CG  
2858 C CD1 . PHE B 21  ? 0.1546 0.4108 0.4477 0.0477  -0.0345 0.0720  677  PHE B CD1 
2859 C CD2 . PHE B 21  ? 0.1206 0.3645 0.4061 0.0332  -0.0409 0.0775  677  PHE B CD2 
2860 C CE1 . PHE B 21  ? 0.1617 0.4335 0.4526 0.0303  -0.0365 0.0701  677  PHE B CE1 
2861 C CE2 . PHE B 21  ? 0.1553 0.4129 0.4368 0.0170  -0.0427 0.0747  677  PHE B CE2 
2862 C CZ  . PHE B 21  ? 0.1363 0.4071 0.4205 0.0151  -0.0408 0.0713  677  PHE B CZ  
2863 N N   . ASP B 22  ? 0.2561 0.3801 0.5254 0.0852  -0.0299 0.0650  678  ASP B N   
2864 C CA  . ASP B 22  ? 0.2751 0.3681 0.5347 0.1006  -0.0276 0.0642  678  ASP B CA  
2865 C C   . ASP B 22  ? 0.3275 0.4149 0.5822 0.1086  -0.0232 0.0547  678  ASP B C   
2866 O O   . ASP B 22  ? 0.3317 0.4093 0.5829 0.0972  -0.0238 0.0453  678  ASP B O   
2867 C CB  . ASP B 22  ? 0.3137 0.3696 0.5639 0.0910  -0.0306 0.0623  678  ASP B CB  
2868 C CG  . ASP B 22  ? 0.5369 0.5576 0.7745 0.1043  -0.0299 0.0656  678  ASP B CG  
2869 O OD1 . ASP B 22  ? 0.5577 0.5530 0.7834 0.1131  -0.0273 0.0582  678  ASP B OD1 
2870 O OD2 . ASP B 22  ? 0.6386 0.6546 0.8759 0.1055  -0.0320 0.0755  678  ASP B OD2 
2871 N N   . VAL B 23  ? 0.2571 0.3537 0.5114 0.1290  -0.0186 0.0581  679  VAL B N   
2872 C CA  . VAL B 23  ? 0.2370 0.3317 0.4854 0.1407  -0.0130 0.0504  679  VAL B CA  
2873 C C   . VAL B 23  ? 0.2985 0.3428 0.5268 0.1436  -0.0122 0.0405  679  VAL B C   
2874 O O   . VAL B 23  ? 0.2753 0.3116 0.4964 0.1415  -0.0102 0.0304  679  VAL B O   
2875 C CB  . VAL B 23  ? 0.2515 0.3744 0.5058 0.1640  -0.0074 0.0589  679  VAL B CB  
2876 C CG1 . VAL B 23  ? 0.2472 0.3589 0.4902 0.1816  0.0000  0.0514  679  VAL B CG1 
2877 C CG2 . VAL B 23  ? 0.2199 0.3975 0.4934 0.1563  -0.0088 0.0669  679  VAL B CG2 
2878 N N   . GLU B 24  ? 0.2901 0.3000 0.5076 0.1478  -0.0141 0.0440  680  GLU B N   
2879 C CA  . GLU B 24  ? 0.3129 0.2708 0.5082 0.1477  -0.0147 0.0357  680  GLU B CA  
2880 C C   . GLU B 24  ? 0.3676 0.3140 0.5619 0.1224  -0.0205 0.0282  680  GLU B C   
2881 O O   . GLU B 24  ? 0.3789 0.2929 0.5564 0.1187  -0.0212 0.0186  680  GLU B O   
2882 C CB  . GLU B 24  ? 0.3537 0.2774 0.5366 0.1581  -0.0153 0.0430  680  GLU B CB  
2883 C CG  . GLU B 24  ? 0.5195 0.4494 0.6999 0.1875  -0.0088 0.0506  680  GLU B CG  
2884 C CD  . GLU B 24  ? 0.7932 0.7213 0.9635 0.2081  -0.0007 0.0434  680  GLU B CD  
2885 O OE1 . GLU B 24  ? 0.7741 0.6612 0.9222 0.2072  0.0003  0.0314  680  GLU B OE1 
2886 O OE2 . GLU B 24  ? 0.5959 0.5653 0.7796 0.2250  0.0046  0.0503  680  GLU B OE2 
2887 N N   . SER B 25  ? 0.3118 0.2855 0.5228 0.1056  -0.0244 0.0326  681  SER B N   
2888 C CA  . SER B 25  ? 0.3184 0.2880 0.5307 0.0842  -0.0288 0.0272  681  SER B CA  
2889 C C   . SER B 25  ? 0.3790 0.3641 0.5930 0.0820  -0.0267 0.0183  681  SER B C   
2890 O O   . SER B 25  ? 0.3878 0.3574 0.5944 0.0716  -0.0291 0.0107  681  SER B O   
2891 C CB  . SER B 25  ? 0.3452 0.3384 0.5720 0.0709  -0.0319 0.0345  681  SER B CB  
2892 O OG  . SER B 25  ? 0.4732 0.4525 0.6978 0.0718  -0.0340 0.0433  681  SER B OG  
2893 N N   . MET B 26  ? 0.3242 0.3417 0.5477 0.0913  -0.0225 0.0202  682  MET B N   
2894 C CA  . MET B 26  ? 0.3166 0.3521 0.5419 0.0906  -0.0197 0.0136  682  MET B CA  
2895 C C   . MET B 26  ? 0.4013 0.4093 0.6088 0.1005  -0.0169 0.0045  682  MET B C   
2896 O O   . MET B 26  ? 0.3934 0.3966 0.5953 0.0924  -0.0177 -0.0035 682  MET B O   
2897 C CB  . MET B 26  ? 0.3204 0.3961 0.5584 0.0988  -0.0159 0.0197  682  MET B CB  
2898 C CG  . MET B 26  ? 0.3376 0.4402 0.5895 0.0865  -0.0191 0.0271  682  MET B CG  
2899 S SD  . MET B 26  ? 0.3547 0.5045 0.6193 0.0942  -0.0159 0.0352  682  MET B SD  
2900 C CE  . MET B 26  ? 0.3053 0.4716 0.5791 0.0840  -0.0210 0.0454  682  MET B CE  
2901 N N   . LYS B 27  ? 0.3722 0.3595 0.5686 0.1182  -0.0137 0.0059  683  LYS B N   
2902 C CA  . LYS B 27  ? 0.3993 0.3526 0.5730 0.1301  -0.0103 -0.0031 683  LYS B CA  
2903 C C   . LYS B 27  ? 0.4886 0.3995 0.6453 0.1145  -0.0166 -0.0105 683  LYS B C   
2904 O O   . LYS B 27  ? 0.4975 0.3924 0.6398 0.1111  -0.0167 -0.0206 683  LYS B O   
2905 C CB  . LYS B 27  ? 0.4133 0.3534 0.5780 0.1551  -0.0046 0.0016  683  LYS B CB  
2906 C CG  . LYS B 27  ? 0.4518 0.4365 0.6315 0.1725  0.0022  0.0088  683  LYS B CG  
2907 C CD  . LYS B 27  ? 0.5181 0.4924 0.6907 0.1989  0.0077  0.0161  683  LYS B CD  
2908 C CE  . LYS B 27  ? 0.6666 0.6888 0.8535 0.2182  0.0152  0.0237  683  LYS B CE  
2909 N NZ  . LYS B 27  ? 0.8632 0.8703 1.0378 0.2493  0.0227  0.0285  683  LYS B NZ  
2910 N N   . LYS B 28  ? 0.4662 0.3622 0.6249 0.1036  -0.0221 -0.0047 684  LYS B N   
2911 C CA  . LYS B 28  ? 0.4886 0.3509 0.6344 0.0855  -0.0291 -0.0088 684  LYS B CA  
2912 C C   . LYS B 28  ? 0.5231 0.4047 0.6771 0.0670  -0.0329 -0.0138 684  LYS B C   
2913 O O   . LYS B 28  ? 0.5573 0.4150 0.6970 0.0552  -0.0375 -0.0205 684  LYS B O   
2914 C CB  . LYS B 28  ? 0.5208 0.3752 0.6724 0.0766  -0.0335 0.0012  684  LYS B CB  
2915 C CG  . LYS B 28  ? 0.7100 0.5223 0.8434 0.0612  -0.0400 -0.0011 684  LYS B CG  
2916 N N   . ALA B 29  ? 0.4361 0.3593 0.6113 0.0645  -0.0314 -0.0099 685  ALA B N   
2917 C CA  . ALA B 29  ? 0.4264 0.3686 0.6091 0.0503  -0.0339 -0.0133 685  ALA B CA  
2918 C C   . ALA B 29  ? 0.4927 0.4323 0.6638 0.0557  -0.0313 -0.0229 685  ALA B C   
2919 O O   . ALA B 29  ? 0.4815 0.4165 0.6472 0.0439  -0.0352 -0.0281 685  ALA B O   
2920 C CB  . ALA B 29  ? 0.4164 0.3966 0.6200 0.0474  -0.0324 -0.0067 685  ALA B CB  
2921 N N   . MET B 30  ? 0.4558 0.3996 0.6225 0.0739  -0.0245 -0.0245 686  MET B N   
2922 C CA  . MET B 30  ? 0.4719 0.4138 0.6259 0.0809  -0.0208 -0.0333 686  MET B CA  
2923 C C   . MET B 30  ? 0.6048 0.5020 0.7314 0.0800  -0.0234 -0.0428 686  MET B C   
2924 O O   . MET B 30  ? 0.6144 0.5066 0.7300 0.0732  -0.0251 -0.0506 686  MET B O   
2925 C CB  . MET B 30  ? 0.4854 0.4492 0.6435 0.1011  -0.0122 -0.0309 686  MET B CB  
2926 C CG  . MET B 30  ? 0.4956 0.5051 0.6775 0.0970  -0.0107 -0.0232 686  MET B CG  
2927 S SD  . MET B 30  ? 0.5164 0.5598 0.7073 0.1180  -0.0018 -0.0166 686  MET B SD  
2928 C CE  . MET B 30  ? 0.4770 0.5199 0.6522 0.1264  0.0042  -0.0262 686  MET B CE  
2929 N N   . VAL B 31  ? 0.6008 0.4638 0.7145 0.0852  -0.0243 -0.0417 687  VAL B N   
2930 C CA  . VAL B 31  ? 0.6213 0.4333 0.7048 0.0823  -0.0276 -0.0500 687  VAL B CA  
2931 C C   . VAL B 31  ? 0.6733 0.4779 0.7549 0.0556  -0.0377 -0.0523 687  VAL B C   
2932 O O   . VAL B 31  ? 0.6980 0.4756 0.7563 0.0484  -0.0412 -0.0617 687  VAL B O   
2933 C CB  . VAL B 31  ? 0.6820 0.4602 0.7538 0.0936  -0.0262 -0.0456 687  VAL B CB  
2934 C CG1 . VAL B 31  ? 0.7115 0.4331 0.7524 0.0825  -0.0324 -0.0522 687  VAL B CG1 
2935 C CG2 . VAL B 31  ? 0.6785 0.4582 0.7445 0.1232  -0.0157 -0.0454 687  VAL B CG2 
2936 N N   . GLU B 32  ? 0.6056 0.4372 0.7113 0.0415  -0.0421 -0.0433 688  GLU B N   
2937 C CA  . GLU B 32  ? 0.5980 0.4343 0.7084 0.0179  -0.0508 -0.0422 688  GLU B CA  
2938 C C   . GLU B 32  ? 0.6462 0.4999 0.7554 0.0122  -0.0520 -0.0486 688  GLU B C   
2939 O O   . GLU B 32  ? 0.6533 0.4997 0.7550 -0.0049 -0.0596 -0.0511 688  GLU B O   
2940 C CB  . GLU B 32  ? 0.5959 0.4641 0.7338 0.0106  -0.0519 -0.0307 688  GLU B CB  
2941 C CG  . GLU B 32  ? 0.7585 0.6227 0.8991 -0.0108 -0.0602 -0.0258 688  GLU B CG  
2942 C CD  . GLU B 32  ? 1.1071 0.9930 1.2690 -0.0148 -0.0601 -0.0142 688  GLU B CD  
2943 O OE1 . GLU B 32  ? 1.0691 0.9757 1.2435 -0.0291 -0.0641 -0.0092 688  GLU B OE1 
2944 O OE2 . GLU B 32  ? 1.0685 0.9521 1.2341 -0.0031 -0.0558 -0.0097 688  GLU B OE2 
2945 N N   . TYR B 33  ? 0.5742 0.4522 0.6908 0.0260  -0.0449 -0.0502 689  TYR B N   
2946 C CA  . TYR B 33  ? 0.5602 0.4556 0.6752 0.0235  -0.0446 -0.0554 689  TYR B CA  
2947 C C   . TYR B 33  ? 0.6180 0.4854 0.7040 0.0306  -0.0429 -0.0671 689  TYR B C   
2948 O O   . TYR B 33  ? 0.6065 0.4856 0.6875 0.0292  -0.0425 -0.0719 689  TYR B O   
2949 C CB  . TYR B 33  ? 0.5467 0.4805 0.6819 0.0329  -0.0379 -0.0505 689  TYR B CB  
2950 C CG  . TYR B 33  ? 0.5335 0.4941 0.6925 0.0234  -0.0402 -0.0410 689  TYR B CG  
2951 C CD1 . TYR B 33  ? 0.5467 0.5159 0.7111 0.0080  -0.0464 -0.0390 689  TYR B CD1 
2952 C CD2 . TYR B 33  ? 0.5289 0.5084 0.7040 0.0306  -0.0357 -0.0338 689  TYR B CD2 
2953 C CE1 . TYR B 33  ? 0.5342 0.5270 0.7180 0.0022  -0.0469 -0.0306 689  TYR B CE1 
2954 C CE2 . TYR B 33  ? 0.5237 0.5242 0.7165 0.0224  -0.0372 -0.0262 689  TYR B CE2 
2955 C CZ  . TYR B 33  ? 0.5781 0.5841 0.7746 0.0093  -0.0422 -0.0249 689  TYR B CZ  
2956 O OH  . TYR B 33  ? 0.5337 0.5584 0.7449 0.0040  -0.0423 -0.0177 689  TYR B OH  
2957 N N   . GLU B 34  ? 0.5931 0.4217 0.6581 0.0388  -0.0415 -0.0714 690  GLU B N   
2958 C CA  . GLU B 34  ? 0.6172 0.4091 0.6488 0.0484  -0.0388 -0.0831 690  GLU B CA  
2959 C C   . GLU B 34  ? 0.6450 0.4559 0.6762 0.0712  -0.0275 -0.0860 690  GLU B C   
2960 O O   . GLU B 34  ? 0.6376 0.4294 0.6431 0.0783  -0.0244 -0.0962 690  GLU B O   
2961 C CB  . GLU B 34  ? 0.6500 0.4210 0.6596 0.0290  -0.0478 -0.0916 690  GLU B CB  
2962 C CG  . GLU B 34  ? 0.8409 0.5958 0.8509 0.0059  -0.0589 -0.0873 690  GLU B CG  
2963 C CD  . GLU B 34  ? 1.1812 0.8971 1.1590 -0.0123 -0.0684 -0.0962 690  GLU B CD  
2964 O OE1 . GLU B 34  ? 1.0746 0.8080 1.0601 -0.0344 -0.0779 -0.0932 690  GLU B OE1 
2965 O OE2 . GLU B 34  ? 1.1327 0.8001 1.0763 -0.0047 -0.0665 -0.1056 690  GLU B OE2 
2966 N N   . ILE B 35  ? 0.5769 0.4237 0.6344 0.0825  -0.0212 -0.0767 691  ILE B N   
2967 C CA  . ILE B 35  ? 0.5673 0.4392 0.6285 0.1028  -0.0106 -0.0765 691  ILE B CA  
2968 C C   . ILE B 35  ? 0.6515 0.4929 0.6917 0.1265  -0.0030 -0.0800 691  ILE B C   
2969 O O   . ILE B 35  ? 0.6493 0.4688 0.6882 0.1297  -0.0044 -0.0760 691  ILE B O   
2970 C CB  . ILE B 35  ? 0.5726 0.4931 0.6681 0.1034  -0.0081 -0.0643 691  ILE B CB  
2971 C CG1 . ILE B 35  ? 0.5552 0.5013 0.6682 0.0826  -0.0146 -0.0609 691  ILE B CG1 
2972 C CG2 . ILE B 35  ? 0.5665 0.5164 0.6675 0.1237  0.0026  -0.0618 691  ILE B CG2 
2973 C CD1 . ILE B 35  ? 0.5772 0.5528 0.7181 0.0771  -0.0157 -0.0496 691  ILE B CD1 
2974 N N   . ASP B 36  ? 0.6285 0.4679 0.6510 0.1440  0.0057  -0.0870 692  ASP B N   
2975 C CA  . ASP B 36  ? 0.6530 0.4652 0.6539 0.1707  0.0149  -0.0901 692  ASP B CA  
2976 C C   . ASP B 36  ? 0.6962 0.5496 0.7254 0.1876  0.0221  -0.0770 692  ASP B C   
2977 O O   . ASP B 36  ? 0.6739 0.5736 0.7203 0.1945  0.0283  -0.0722 692  ASP B O   
2978 C CB  . ASP B 36  ? 0.6931 0.4930 0.6654 0.1849  0.0227  -0.1016 692  ASP B CB  
2979 C CG  . ASP B 36  ? 0.8812 0.6330 0.8186 0.2102  0.0308  -0.1087 692  ASP B CG  
2980 O OD1 . ASP B 36  ? 0.8705 0.6367 0.8167 0.2353  0.0403  -0.1010 692  ASP B OD1 
2981 O OD2 . ASP B 36  ? 1.0579 0.7574 0.9579 0.2053  0.0276  -0.1216 692  ASP B OD2 
2982 N N   . LEU B 37  ? 0.6700 0.5088 0.7049 0.1904  0.0197  -0.0699 693  LEU B N   
2983 C CA  . LEU B 37  ? 0.6571 0.5333 0.7185 0.2037  0.0243  -0.0562 693  LEU B CA  
2984 C C   . LEU B 37  ? 0.7366 0.6195 0.7890 0.2373  0.0373  -0.0545 693  LEU B C   
2985 O O   . LEU B 37  ? 0.7045 0.6351 0.7820 0.2484  0.0422  -0.0428 693  LEU B O   
2986 C CB  . LEU B 37  ? 0.6583 0.5173 0.7276 0.1953  0.0172  -0.0487 693  LEU B CB  
2987 C CG  . LEU B 37  ? 0.6855 0.5936 0.7904 0.1907  0.0155  -0.0345 693  LEU B CG  
2988 C CD1 . LEU B 37  ? 0.6630 0.6014 0.7879 0.1649  0.0088  -0.0337 693  LEU B CD1 
2989 C CD2 . LEU B 37  ? 0.7340 0.6216 0.8411 0.1899  0.0112  -0.0267 693  LEU B CD2 
2990 N N   . GLN B 38  ? 0.7414 0.5784 0.7572 0.2532  0.0429  -0.0661 694  GLN B N   
2991 C CA  . GLN B 38  ? 0.7456 0.5845 0.7474 0.2880  0.0569  -0.0661 694  GLN B CA  
2992 C C   . GLN B 38  ? 0.7821 0.6714 0.7952 0.2914  0.0639  -0.0665 694  GLN B C   
2993 O O   . GLN B 38  ? 0.7567 0.6942 0.7891 0.3103  0.0728  -0.0560 694  GLN B O   
2994 C CB  . GLN B 38  ? 0.8060 0.5720 0.7596 0.3018  0.0603  -0.0799 694  GLN B CB  
2995 C CG  . GLN B 38  ? 1.1256 0.8452 1.0648 0.3135  0.0595  -0.0760 694  GLN B CG  
2996 C CD  . GLN B 38  ? 1.4039 1.1334 1.3402 0.3537  0.0736  -0.0683 694  GLN B CD  
2997 N N   . LYS B 39  ? 0.7528 0.6345 0.7557 0.2711  0.0589  -0.0770 695  LYS B N   
2998 C CA  . LYS B 39  ? 0.7384 0.6624 0.7489 0.2692  0.0638  -0.0781 695  LYS B CA  
2999 C C   . LYS B 39  ? 0.7589 0.7468 0.8116 0.2546  0.0606  -0.0643 695  LYS B C   
3000 O O   . LYS B 39  ? 0.7342 0.7677 0.7989 0.2591  0.0672  -0.0599 695  LYS B O   
3001 C CB  . LYS B 39  ? 0.7833 0.6785 0.7709 0.2491  0.0573  -0.0920 695  LYS B CB  
3002 C CG  . LYS B 39  ? 0.9622 0.8047 0.9036 0.2649  0.0632  -0.1072 695  LYS B CG  
3003 C CD  . LYS B 39  ? 1.0790 0.8972 0.9998 0.2409  0.0545  -0.1196 695  LYS B CD  
3004 C CE  . LYS B 39  ? 1.2707 1.0478 1.1456 0.2559  0.0616  -0.1349 695  LYS B CE  
3005 N NZ  . LYS B 39  ? 1.4710 1.1748 1.3081 0.2570  0.0574  -0.1454 695  LYS B NZ  
3006 N N   . MET B 40  ? 0.7128 0.7021 0.7855 0.2357  0.0504  -0.0578 696  MET B N   
3007 C CA  . MET B 40  ? 0.6835 0.7249 0.7915 0.2205  0.0466  -0.0456 696  MET B CA  
3008 C C   . MET B 40  ? 0.6918 0.7314 0.8174 0.2119  0.0392  -0.0369 696  MET B C   
3009 O O   . MET B 40  ? 0.6820 0.7059 0.8113 0.1894  0.0293  -0.0387 696  MET B O   
3010 C CB  . MET B 40  ? 0.7113 0.7670 0.8249 0.1956  0.0407  -0.0490 696  MET B CB  
3011 C CG  . MET B 40  ? 0.7334 0.8452 0.8770 0.1858  0.0407  -0.0371 696  MET B CG  
3012 S SD  . MET B 40  ? 0.7854 0.9042 0.9442 0.1526  0.0290  -0.0353 696  MET B SD  
3013 C CE  . MET B 40  ? 0.7627 0.8334 0.9130 0.1440  0.0198  -0.0403 696  MET B CE  
3014 N N   . PRO B 41  ? 0.6183 0.6793 0.7562 0.2304  0.0443  -0.0261 697  PRO B N   
3015 C CA  . PRO B 41  ? 0.5960 0.6595 0.7506 0.2231  0.0376  -0.0166 697  PRO B CA  
3016 C C   . PRO B 41  ? 0.5777 0.6828 0.7599 0.1994  0.0310  -0.0087 697  PRO B C   
3017 O O   . PRO B 41  ? 0.5633 0.6960 0.7525 0.1888  0.0316  -0.0096 697  PRO B O   
3018 C CB  . PRO B 41  ? 0.6132 0.6925 0.7715 0.2520  0.0459  -0.0068 697  PRO B CB  
3019 C CG  . PRO B 41  ? 0.6589 0.7742 0.8184 0.2677  0.0562  -0.0060 697  PRO B CG  
3020 C CD  . PRO B 41  ? 0.6225 0.7085 0.7593 0.2599  0.0566  -0.0211 697  PRO B CD  
3021 N N   . LEU B 42  ? 0.4778 0.5837 0.6727 0.1914  0.0247  -0.0011 698  LEU B N   
3022 C CA  . LEU B 42  ? 0.4334 0.5677 0.6496 0.1698  0.0178  0.0061  698  LEU B CA  
3023 C C   . LEU B 42  ? 0.4393 0.6304 0.6750 0.1685  0.0208  0.0155  698  LEU B C   
3024 O O   . LEU B 42  ? 0.4224 0.6316 0.6677 0.1476  0.0163  0.0166  698  LEU B O   
3025 C CB  . LEU B 42  ? 0.4282 0.5488 0.6491 0.1692  0.0128  0.0128  698  LEU B CB  
3026 C CG  . LEU B 42  ? 0.4665 0.6079 0.7049 0.1492  0.0056  0.0201  698  LEU B CG  
3027 C CD1 . LEU B 42  ? 0.4782 0.6104 0.7156 0.1255  0.0002  0.0129  698  LEU B CD1 
3028 C CD2 . LEU B 42  ? 0.4754 0.5965 0.7132 0.1516  0.0019  0.0254  698  LEU B CD2 
3029 N N   . GLY B 43  ? 0.3677 0.5854 0.6078 0.1904  0.0284  0.0227  699  GLY B N   
3030 C CA  . GLY B 43  ? 0.3438 0.6196 0.6021 0.1908  0.0319  0.0332  699  GLY B CA  
3031 C C   . GLY B 43  ? 0.4093 0.7012 0.6635 0.1884  0.0371  0.0283  699  GLY B C   
3032 O O   . GLY B 43  ? 0.3828 0.7227 0.6518 0.1816  0.0386  0.0369  699  GLY B O   
3033 N N   . LYS B 44  ? 0.3926 0.6451 0.6253 0.1929  0.0397  0.0151  700  LYS B N   
3034 C CA  . LYS B 44  ? 0.3917 0.6552 0.6174 0.1903  0.0444  0.0096  700  LYS B CA  
3035 C C   . LYS B 44  ? 0.4261 0.6808 0.6523 0.1615  0.0363  0.0047  700  LYS B C   
3036 O O   . LYS B 44  ? 0.4253 0.6954 0.6492 0.1547  0.0388  0.0030  700  LYS B O   
3037 C CB  . LYS B 44  ? 0.4472 0.6764 0.6471 0.2116  0.0520  -0.0017 700  LYS B CB  
3038 C CG  . LYS B 44  ? 0.6067 0.8591 0.8062 0.2429  0.0638  0.0046  700  LYS B CG  
3039 C CD  . LYS B 44  ? 0.7898 1.0077 0.9594 0.2641  0.0726  -0.0077 700  LYS B CD  
3040 C CE  . LYS B 44  ? 1.0201 1.2400 1.1832 0.2993  0.0835  -0.0030 700  LYS B CE  
3041 N NZ  . LYS B 44  ? 1.1866 1.3519 1.3130 0.3199  0.0903  -0.0172 700  LYS B NZ  
3042 N N   . LEU B 45  ? 0.3491 0.5809 0.5783 0.1460  0.0273  0.0037  701  LEU B N   
3043 C CA  . LEU B 45  ? 0.3343 0.5565 0.5642 0.1215  0.0200  0.0004  701  LEU B CA  
3044 C C   . LEU B 45  ? 0.3169 0.5806 0.5617 0.1069  0.0191  0.0095  701  LEU B C   
3045 O O   . LEU B 45  ? 0.3055 0.5984 0.5645 0.1067  0.0187  0.0196  701  LEU B O   
3046 C CB  . LEU B 45  ? 0.3435 0.5394 0.5755 0.1120  0.0121  0.0000  701  LEU B CB  
3047 C CG  . LEU B 45  ? 0.4193 0.5793 0.6411 0.0980  0.0059  -0.0087 701  LEU B CG  
3048 C CD1 . LEU B 45  ? 0.4175 0.5772 0.6494 0.0817  -0.0009 -0.0042 701  LEU B CD1 
3049 C CD2 . LEU B 45  ? 0.4425 0.6005 0.6548 0.0920  0.0069  -0.0151 701  LEU B CD2 
3050 N N   . SER B 46  ? 0.2322 0.4982 0.4722 0.0941  0.0187  0.0065  702  SER B N   
3051 C CA  . SER B 46  ? 0.2010 0.5004 0.4512 0.0779  0.0175  0.0151  702  SER B CA  
3052 C C   . SER B 46  ? 0.2249 0.5064 0.4682 0.0586  0.0125  0.0113  702  SER B C   
3053 O O   . SER B 46  ? 0.2229 0.4766 0.4540 0.0601  0.0120  0.0025  702  SER B O   
3054 C CB  . SER B 46  ? 0.2137 0.5520 0.4673 0.0860  0.0254  0.0207  702  SER B CB  
3055 O OG  . SER B 46  ? 0.2518 0.5832 0.4932 0.0841  0.0284  0.0149  702  SER B OG  
3056 N N   . LYS B 47  ? 0.1533 0.4506 0.4027 0.0404  0.0089  0.0184  703  LYS B N   
3057 C CA  . LYS B 47  ? 0.1610 0.4400 0.4022 0.0236  0.0049  0.0160  703  LYS B CA  
3058 C C   . LYS B 47  ? 0.1942 0.4751 0.4259 0.0237  0.0087  0.0134  703  LYS B C   
3059 O O   . LYS B 47  ? 0.1896 0.4447 0.4114 0.0199  0.0063  0.0075  703  LYS B O   
3060 C CB  . LYS B 47  ? 0.1874 0.4770 0.4320 0.0046  0.0006  0.0236  703  LYS B CB  
3061 C CG  . LYS B 47  ? 0.4125 0.6713 0.6462 -0.0083 -0.0037 0.0199  703  LYS B CG  
3062 C CD  . LYS B 47  ? 0.5447 0.8059 0.7751 -0.0276 -0.0074 0.0260  703  LYS B CD  
3063 C CE  . LYS B 47  ? 0.5649 0.8000 0.7807 -0.0383 -0.0089 0.0240  703  LYS B CE  
3064 N NZ  . LYS B 47  ? 0.5291 0.7329 0.7404 -0.0310 -0.0103 0.0169  703  LYS B NZ  
3065 N N   . ARG B 48  ? 0.1317 0.4450 0.3666 0.0295  0.0148  0.0181  704  ARG B N   
3066 C CA  . ARG B 48  ? 0.1373 0.4564 0.3626 0.0295  0.0192  0.0167  704  ARG B CA  
3067 C C   . ARG B 48  ? 0.1866 0.4814 0.3995 0.0448  0.0217  0.0058  704  ARG B C   
3068 O O   . ARG B 48  ? 0.1681 0.4526 0.3692 0.0409  0.0219  0.0021  704  ARG B O   
3069 C CB  . ARG B 48  ? 0.1459 0.5104 0.3784 0.0302  0.0255  0.0263  704  ARG B CB  
3070 C CG  . ARG B 48  ? 0.2154 0.6060 0.4587 0.0117  0.0219  0.0378  704  ARG B CG  
3071 C CD  . ARG B 48  ? 0.3870 0.8288 0.6429 0.0187  0.0282  0.0480  704  ARG B CD  
3072 N NE  . ARG B 48  ? 0.4761 0.9501 0.7381 -0.0036 0.0256  0.0604  704  ARG B NE  
3073 C CZ  . ARG B 48  ? 0.6097 1.0864 0.8631 -0.0207 0.0255  0.0642  704  ARG B CZ  
3074 N NH1 . ARG B 48  ? 0.3358 0.8405 0.5934 -0.0426 0.0226  0.0760  704  ARG B NH1 
3075 N NH2 . ARG B 48  ? 0.5171 0.9677 0.7563 -0.0173 0.0277  0.0567  704  ARG B NH2 
3076 N N   . GLN B 49  ? 0.1448 0.4283 0.3583 0.0610  0.0231  0.0008  705  GLN B N   
3077 C CA  . GLN B 49  ? 0.1558 0.4090 0.3540 0.0735  0.0241  -0.0106 705  GLN B CA  
3078 C C   . GLN B 49  ? 0.2013 0.4204 0.3935 0.0611  0.0156  -0.0162 705  GLN B C   
3079 O O   . GLN B 49  ? 0.2008 0.4064 0.3803 0.0583  0.0145  -0.0216 705  GLN B O   
3080 C CB  . GLN B 49  ? 0.1742 0.4204 0.3728 0.0926  0.0273  -0.0131 705  GLN B CB  
3081 C CG  . GLN B 49  ? 0.3482 0.5529 0.5287 0.1013  0.0259  -0.0252 705  GLN B CG  
3082 C CD  . GLN B 49  ? 0.5895 0.7805 0.7683 0.1190  0.0284  -0.0268 705  GLN B CD  
3083 O OE1 . GLN B 49  ? 0.5223 0.7248 0.7161 0.1201  0.0271  -0.0194 705  GLN B OE1 
3084 N NE2 . GLN B 49  ? 0.4586 0.6224 0.6166 0.1331  0.0320  -0.0365 705  GLN B NE2 
3085 N N   . ILE B 50  ? 0.1551 0.3647 0.3568 0.0534  0.0098  -0.0136 706  ILE B N   
3086 C CA  . ILE B 50  ? 0.1525 0.3362 0.3517 0.0426  0.0026  -0.0165 706  ILE B CA  
3087 C C   . ILE B 50  ? 0.1819 0.3683 0.3765 0.0299  0.0010  -0.0141 706  ILE B C   
3088 O O   . ILE B 50  ? 0.1868 0.3552 0.3734 0.0265  -0.0027 -0.0182 706  ILE B O   
3089 C CB  . ILE B 50  ? 0.1813 0.3600 0.3916 0.0379  -0.0016 -0.0126 706  ILE B CB  
3090 C CG1 . ILE B 50  ? 0.1742 0.3471 0.3873 0.0512  -0.0002 -0.0142 706  ILE B CG1 
3091 C CG2 . ILE B 50  ? 0.1826 0.3391 0.3910 0.0279  -0.0078 -0.0144 706  ILE B CG2 
3092 C CD1 . ILE B 50  ? 0.1575 0.3381 0.3836 0.0481  -0.0026 -0.0073 706  ILE B CD1 
3093 N N   . GLN B 51  ? 0.1178 0.3275 0.3167 0.0229  0.0036  -0.0066 707  GLN B N   
3094 C CA  . GLN B 51  ? 0.1040 0.3151 0.2964 0.0112  0.0029  -0.0029 707  GLN B CA  
3095 C C   . GLN B 51  ? 0.1460 0.3576 0.3263 0.0165  0.0058  -0.0071 707  GLN B C   
3096 O O   . GLN B 51  ? 0.1700 0.3699 0.3420 0.0101  0.0030  -0.0072 707  GLN B O   
3097 C CB  . GLN B 51  ? 0.1048 0.3391 0.3025 0.0004  0.0046  0.0065  707  GLN B CB  
3098 C CG  . GLN B 51  ? 0.2065 0.4299 0.4077 -0.0111 -0.0001 0.0102  707  GLN B CG  
3099 C CD  . GLN B 51  ? 0.3413 0.5841 0.5436 -0.0253 0.0004  0.0192  707  GLN B CD  
3100 O OE1 . GLN B 51  ? 0.1961 0.4681 0.4070 -0.0241 0.0031  0.0238  707  GLN B OE1 
3101 N NE2 . GLN B 51  ? 0.3114 0.5384 0.5041 -0.0395 -0.0024 0.0225  707  GLN B NE2 
3102 N N   . ALA B 52  ? 0.0872 0.3112 0.2650 0.0292  0.0115  -0.0104 708  ALA B N   
3103 C CA  . ALA B 52  ? 0.0921 0.3143 0.2551 0.0357  0.0146  -0.0159 708  ALA B CA  
3104 C C   . ALA B 52  ? 0.1367 0.3278 0.2887 0.0382  0.0092  -0.0255 708  ALA B C   
3105 O O   . ALA B 52  ? 0.1527 0.3370 0.2920 0.0355  0.0076  -0.0284 708  ALA B O   
3106 C CB  . ALA B 52  ? 0.0917 0.3335 0.2530 0.0509  0.0232  -0.0172 708  ALA B CB  
3107 N N   . ALA B 53  ? 0.0776 0.2515 0.2342 0.0420  0.0058  -0.0294 709  ALA B N   
3108 C CA  . ALA B 53  ? 0.1018 0.2478 0.2496 0.0408  -0.0005 -0.0369 709  ALA B CA  
3109 C C   . ALA B 53  ? 0.1700 0.3111 0.3204 0.0276  -0.0071 -0.0328 709  ALA B C   
3110 O O   . ALA B 53  ? 0.1774 0.3080 0.3168 0.0248  -0.0112 -0.0367 709  ALA B O   
3111 C CB  . ALA B 53  ? 0.1167 0.2474 0.2702 0.0457  -0.0026 -0.0395 709  ALA B CB  
3112 N N   . TYR B 54  ? 0.1392 0.2883 0.3023 0.0201  -0.0078 -0.0246 710  TYR B N   
3113 C CA  . TYR B 54  ? 0.1471 0.2906 0.3108 0.0106  -0.0123 -0.0197 710  TYR B CA  
3114 C C   . TYR B 54  ? 0.2018 0.3510 0.3542 0.0077  -0.0115 -0.0177 710  TYR B C   
3115 O O   . TYR B 54  ? 0.2098 0.3510 0.3573 0.0044  -0.0160 -0.0168 710  TYR B O   
3116 C CB  . TYR B 54  ? 0.1665 0.3150 0.3393 0.0042  -0.0114 -0.0122 710  TYR B CB  
3117 C CG  . TYR B 54  ? 0.1897 0.3294 0.3725 0.0039  -0.0140 -0.0119 710  TYR B CG  
3118 C CD1 . TYR B 54  ? 0.2028 0.3287 0.3868 0.0033  -0.0188 -0.0133 710  TYR B CD1 
3119 C CD2 . TYR B 54  ? 0.1975 0.3460 0.3887 0.0033  -0.0118 -0.0090 710  TYR B CD2 
3120 C CE1 . TYR B 54  ? 0.2118 0.3315 0.4046 0.0026  -0.0206 -0.0121 710  TYR B CE1 
3121 C CE2 . TYR B 54  ? 0.1954 0.3363 0.3944 0.0027  -0.0141 -0.0083 710  TYR B CE2 
3122 C CZ  . TYR B 54  ? 0.2035 0.3294 0.4029 0.0023  -0.0181 -0.0098 710  TYR B CZ  
3123 O OH  . TYR B 54  ? 0.1561 0.2767 0.3628 0.0016  -0.0197 -0.0082 710  TYR B OH  
3124 N N   . SER B 55  ? 0.1540 0.3200 0.3030 0.0090  -0.0055 -0.0156 711  SER B N   
3125 C CA  . SER B 55  ? 0.1476 0.3220 0.2848 0.0065  -0.0034 -0.0130 711  SER B CA  
3126 C C   . SER B 55  ? 0.1816 0.3477 0.3052 0.0115  -0.0058 -0.0209 711  SER B C   
3127 O O   . SER B 55  ? 0.1739 0.3394 0.2883 0.0075  -0.0081 -0.0183 711  SER B O   
3128 C CB  . SER B 55  ? 0.1716 0.3694 0.3094 0.0075  0.0041  -0.0091 711  SER B CB  
3129 O OG  . SER B 55  ? 0.2500 0.4574 0.3992 0.0006  0.0053  -0.0018 711  SER B OG  
3130 N N   . ILE B 56  ? 0.1399 0.2977 0.2602 0.0197  -0.0056 -0.0301 712  ILE B N   
3131 C CA  . ILE B 56  ? 0.1536 0.2982 0.2571 0.0223  -0.0090 -0.0388 712  ILE B CA  
3132 C C   . ILE B 56  ? 0.2032 0.3349 0.3082 0.0140  -0.0187 -0.0379 712  ILE B C   
3133 O O   . ILE B 56  ? 0.2099 0.3405 0.3031 0.0103  -0.0230 -0.0386 712  ILE B O   
3134 C CB  . ILE B 56  ? 0.1961 0.3293 0.2911 0.0332  -0.0058 -0.0491 712  ILE B CB  
3135 C CG1 . ILE B 56  ? 0.1954 0.3469 0.2862 0.0438  0.0046  -0.0490 712  ILE B CG1 
3136 C CG2 . ILE B 56  ? 0.2038 0.3157 0.2784 0.0321  -0.0117 -0.0590 712  ILE B CG2 
3137 C CD1 . ILE B 56  ? 0.2360 0.3802 0.3246 0.0569  0.0095  -0.0551 712  ILE B CD1 
3138 N N   . LEU B 57  ? 0.1491 0.2746 0.2689 0.0114  -0.0219 -0.0351 713  LEU B N   
3139 C CA  . LEU B 57  ? 0.1631 0.2822 0.2879 0.0047  -0.0298 -0.0321 713  LEU B CA  
3140 C C   . LEU B 57  ? 0.1975 0.3258 0.3227 0.0007  -0.0308 -0.0230 713  LEU B C   
3141 O O   . LEU B 57  ? 0.1822 0.3108 0.3030 -0.0027 -0.0368 -0.0211 713  LEU B O   
3142 C CB  . LEU B 57  ? 0.1570 0.2705 0.2975 0.0041  -0.0310 -0.0301 713  LEU B CB  
3143 C CG  . LEU B 57  ? 0.2135 0.3143 0.3536 0.0079  -0.0309 -0.0376 713  LEU B CG  
3144 C CD1 . LEU B 57  ? 0.2103 0.3070 0.3655 0.0056  -0.0332 -0.0339 713  LEU B CD1 
3145 C CD2 . LEU B 57  ? 0.2392 0.3259 0.3636 0.0057  -0.0365 -0.0459 713  LEU B CD2 
3146 N N   . SER B 58  ? 0.1579 0.2936 0.2864 0.0008  -0.0250 -0.0168 714  SER B N   
3147 C CA  . SER B 58  ? 0.1474 0.2865 0.2724 -0.0026 -0.0252 -0.0077 714  SER B CA  
3148 C C   . SER B 58  ? 0.1783 0.3234 0.2881 -0.0028 -0.0262 -0.0081 714  SER B C   
3149 O O   . SER B 58  ? 0.1391 0.2845 0.2448 -0.0045 -0.0304 -0.0023 714  SER B O   
3150 C CB  . SER B 58  ? 0.1520 0.2937 0.2805 -0.0052 -0.0194 -0.0016 714  SER B CB  
3151 O OG  . SER B 58  ? 0.2078 0.3413 0.3473 -0.0059 -0.0203 0.0003  714  SER B OG  
3152 N N   . GLU B 59  ? 0.1539 0.3045 0.2549 0.0000  -0.0222 -0.0148 715  GLU B N   
3153 C CA  . GLU B 59  ? 0.1642 0.3199 0.2482 0.0002  -0.0229 -0.0168 715  GLU B CA  
3154 C C   . GLU B 59  ? 0.2191 0.3676 0.2962 -0.0018 -0.0319 -0.0216 715  GLU B C   
3155 O O   . GLU B 59  ? 0.1984 0.3519 0.2641 -0.0044 -0.0357 -0.0186 715  GLU B O   
3156 C CB  . GLU B 59  ? 0.1816 0.3443 0.2563 0.0058  -0.0156 -0.0235 715  GLU B CB  
3157 C CG  . GLU B 59  ? 0.2933 0.4655 0.3501 0.0054  -0.0137 -0.0222 715  GLU B CG  
3158 C CD  . GLU B 59  ? 0.4709 0.6544 0.5285 0.0003  -0.0106 -0.0098 715  GLU B CD  
3159 O OE1 . GLU B 59  ? 0.2760 0.4659 0.3443 -0.0015 -0.0054 -0.0044 715  GLU B OE1 
3160 O OE2 . GLU B 59  ? 0.4954 0.6810 0.5416 -0.0028 -0.0137 -0.0050 715  GLU B OE2 
3161 N N   . VAL B 60  ? 0.1814 0.3191 0.2644 -0.0019 -0.0358 -0.0280 716  VAL B N   
3162 C CA  . VAL B 60  ? 0.1923 0.3245 0.2701 -0.0072 -0.0454 -0.0312 716  VAL B CA  
3163 C C   . VAL B 60  ? 0.2431 0.3849 0.3308 -0.0109 -0.0510 -0.0196 716  VAL B C   
3164 O O   . VAL B 60  ? 0.2231 0.3717 0.3017 -0.0147 -0.0574 -0.0173 716  VAL B O   
3165 C CB  . VAL B 60  ? 0.2512 0.3682 0.3314 -0.0084 -0.0486 -0.0399 716  VAL B CB  
3166 C CG1 . VAL B 60  ? 0.2536 0.3688 0.3317 -0.0177 -0.0598 -0.0398 716  VAL B CG1 
3167 C CG2 . VAL B 60  ? 0.2560 0.3602 0.3196 -0.0028 -0.0438 -0.0519 716  VAL B CG2 
3168 N N   . GLN B 61  ? 0.2296 0.3721 0.3339 -0.0088 -0.0482 -0.0119 717  GLN B N   
3169 C CA  . GLN B 61  ? 0.2227 0.3718 0.3357 -0.0084 -0.0513 -0.0001 717  GLN B CA  
3170 C C   . GLN B 61  ? 0.2702 0.4271 0.3714 -0.0076 -0.0513 0.0073  717  GLN B C   
3171 O O   . GLN B 61  ? 0.2665 0.4330 0.3660 -0.0083 -0.0578 0.0135  717  GLN B O   
3172 C CB  . GLN B 61  ? 0.2471 0.3899 0.3733 -0.0049 -0.0456 0.0048  717  GLN B CB  
3173 C CG  . GLN B 61  ? 0.5108 0.6531 0.6370 -0.0012 -0.0432 0.0170  717  GLN B CG  
3174 C CD  . GLN B 61  ? 0.5739 0.7045 0.7059 0.0007  -0.0370 0.0200  717  GLN B CD  
3175 O OE1 . GLN B 61  ? 0.5175 0.6445 0.6604 0.0015  -0.0368 0.0181  717  GLN B OE1 
3176 N NE2 . GLN B 61  ? 0.2836 0.4070 0.4067 0.0003  -0.0322 0.0254  717  GLN B NE2 
3177 N N   . GLN B 62  ? 0.2252 0.3801 0.3182 -0.0065 -0.0443 0.0072  718  GLN B N   
3178 C CA  . GLN B 62  ? 0.2325 0.3927 0.3126 -0.0064 -0.0427 0.0141  718  GLN B CA  
3179 C C   . GLN B 62  ? 0.2971 0.4663 0.3628 -0.0089 -0.0489 0.0106  718  GLN B C   
3180 O O   . GLN B 62  ? 0.2608 0.4378 0.3206 -0.0088 -0.0532 0.0193  718  GLN B O   
3181 C CB  . GLN B 62  ? 0.2501 0.4090 0.3260 -0.0070 -0.0339 0.0129  718  GLN B CB  
3182 C CG  . GLN B 62  ? 0.4544 0.6127 0.5224 -0.0083 -0.0302 0.0244  718  GLN B CG  
3183 C CD  . GLN B 62  ? 0.5142 0.6604 0.5877 -0.0068 -0.0303 0.0346  718  GLN B CD  
3184 O OE1 . GLN B 62  ? 0.3976 0.5371 0.4832 -0.0043 -0.0317 0.0337  718  GLN B OE1 
3185 N NE2 . GLN B 62  ? 0.3473 0.4887 0.4095 -0.0080 -0.0281 0.0449  718  GLN B NE2 
3186 N N   . ALA B 63  ? 0.2834 0.4499 0.3425 -0.0107 -0.0498 -0.0020 719  ALA B N   
3187 C CA  . ALA B 63  ? 0.2995 0.4695 0.3409 -0.0144 -0.0559 -0.0082 719  ALA B CA  
3188 C C   . ALA B 63  ? 0.3450 0.5216 0.3901 -0.0198 -0.0675 -0.0045 719  ALA B C   
3189 O O   . ALA B 63  ? 0.3400 0.5274 0.3737 -0.0228 -0.0735 -0.0002 719  ALA B O   
3190 C CB  . ALA B 63  ? 0.3171 0.4758 0.3482 -0.0137 -0.0530 -0.0233 719  ALA B CB  
3191 N N   . VAL B 64  ? 0.3183 0.4916 0.3800 -0.0212 -0.0706 -0.0046 720  VAL B N   
3192 C CA  . VAL B 64  ? 0.3180 0.5023 0.3875 -0.0268 -0.0811 0.0006  720  VAL B CA  
3193 C C   . VAL B 64  ? 0.4177 0.6196 0.4930 -0.0224 -0.0831 0.0167  720  VAL B C   
3194 O O   . VAL B 64  ? 0.4029 0.6215 0.4753 -0.0271 -0.0925 0.0223  720  VAL B O   
3195 C CB  . VAL B 64  ? 0.3556 0.5339 0.4435 -0.0280 -0.0816 -0.0011 720  VAL B CB  
3196 C CG1 . VAL B 64  ? 0.3431 0.5394 0.4441 -0.0322 -0.0905 0.0085  720  VAL B CG1 
3197 C CG2 . VAL B 64  ? 0.3591 0.5190 0.4386 -0.0329 -0.0819 -0.0159 720  VAL B CG2 
3198 N N   . SER B 65  ? 0.4098 0.6070 0.4917 -0.0136 -0.0747 0.0247  721  SER B N   
3199 C CA  . SER B 65  ? 0.4257 0.6325 0.5112 -0.0066 -0.0749 0.0403  721  SER B CA  
3200 C C   . SER B 65  ? 0.5179 0.7324 0.5861 -0.0063 -0.0764 0.0463  721  SER B C   
3201 O O   . SER B 65  ? 0.5129 0.7428 0.5818 -0.0030 -0.0819 0.0584  721  SER B O   
3202 C CB  . SER B 65  ? 0.4737 0.6663 0.5678 0.0014  -0.0658 0.0458  721  SER B CB  
3203 O OG  . SER B 65  ? 0.6351 0.8156 0.7174 0.0020  -0.0583 0.0455  721  SER B OG  
3204 N N   . GLN B 66  ? 0.5128 0.7195 0.5657 -0.0090 -0.0716 0.0390  722  GLN B N   
3205 C CA  . GLN B 66  ? 0.5263 0.7405 0.5609 -0.0095 -0.0725 0.0443  722  GLN B CA  
3206 C C   . GLN B 66  ? 0.5908 0.8209 0.6145 -0.0164 -0.0837 0.0413  722  GLN B C   
3207 O O   . GLN B 66  ? 0.5838 0.8256 0.5948 -0.0164 -0.0872 0.0494  722  GLN B O   
3208 C CB  . GLN B 66  ? 0.5549 0.7594 0.5772 -0.0103 -0.0630 0.0384  722  GLN B CB  
3209 C CG  . GLN B 66  ? 0.7942 1.0026 0.7969 -0.0152 -0.0639 0.0269  722  GLN B CG  
3210 C CD  . GLN B 66  ? 1.0094 1.2296 0.9928 -0.0165 -0.0668 0.0341  722  GLN B CD  
3211 O OE1 . GLN B 66  ? 0.9690 1.1924 0.9514 -0.0132 -0.0655 0.0484  722  GLN B OE1 
3212 N NE2 . GLN B 66  ? 0.8426 1.0674 0.8077 -0.0213 -0.0709 0.0244  722  GLN B NE2 
3213 N N   . GLY B 67  ? 0.5557 0.7851 0.5832 -0.0234 -0.0895 0.0306  723  GLY B N   
3214 C CA  . GLY B 67  ? 0.5555 0.7960 0.5706 -0.0335 -0.1011 0.0259  723  GLY B CA  
3215 C C   . GLY B 67  ? 0.6223 0.8559 0.6103 -0.0374 -0.0996 0.0151  723  GLY B C   
3216 O O   . GLY B 67  ? 0.6376 0.8643 0.6187 -0.0313 -0.0896 0.0150  723  GLY B O   
3217 N N   . SER B 68  ? 0.5672 0.8020 0.5377 -0.0483 -0.1092 0.0060  724  SER B N   
3218 C CA  . SER B 68  ? 0.5731 0.7992 0.5130 -0.0515 -0.1078 -0.0058 724  SER B CA  
3219 C C   . SER B 68  ? 0.6162 0.8211 0.5503 -0.0438 -0.0940 -0.0179 724  SER B C   
3220 O O   . SER B 68  ? 0.6162 0.8207 0.5329 -0.0395 -0.0868 -0.0203 724  SER B O   
3221 C CB  . SER B 68  ? 0.6230 0.8671 0.5495 -0.0502 -0.1096 0.0053  724  SER B CB  
3222 O OG  . SER B 68  ? 0.7492 1.0161 0.6813 -0.0560 -0.1225 0.0174  724  SER B OG  
3223 N N   . SER B 69  ? 0.5670 0.7575 0.5167 -0.0418 -0.0903 -0.0241 725  SER B N   
3224 C CA  . SER B 69  ? 0.5724 0.7463 0.5217 -0.0337 -0.0780 -0.0339 725  SER B CA  
3225 C C   . SER B 69  ? 0.6269 0.7787 0.5733 -0.0367 -0.0801 -0.0481 725  SER B C   
3226 O O   . SER B 69  ? 0.6386 0.7776 0.5898 -0.0289 -0.0707 -0.0546 725  SER B O   
3227 C CB  . SER B 69  ? 0.6060 0.7852 0.5806 -0.0258 -0.0695 -0.0232 725  SER B CB  
3228 O OG  . SER B 69  ? 0.6765 0.8688 0.6484 -0.0226 -0.0652 -0.0117 725  SER B OG  
3229 N N   . ASP B 70  ? 0.5656 0.7132 0.5031 -0.0488 -0.0927 -0.0521 726  ASP B N   
3230 C CA  . ASP B 70  ? 0.5634 0.6874 0.4949 -0.0553 -0.0971 -0.0643 726  ASP B CA  
3231 C C   . ASP B 70  ? 0.5961 0.6912 0.5024 -0.0484 -0.0887 -0.0813 726  ASP B C   
3232 O O   . ASP B 70  ? 0.5927 0.6666 0.5026 -0.0460 -0.0859 -0.0887 726  ASP B O   
3233 C CB  . ASP B 70  ? 0.5914 0.7190 0.5122 -0.0728 -0.1133 -0.0643 726  ASP B CB  
3234 C CG  . ASP B 70  ? 0.7099 0.8668 0.6590 -0.0780 -0.1214 -0.0471 726  ASP B CG  
3235 O OD1 . ASP B 70  ? 0.7053 0.8654 0.6819 -0.0725 -0.1172 -0.0407 726  ASP B OD1 
3236 O OD2 . ASP B 70  ? 0.7652 0.9429 0.7083 -0.0869 -0.1319 -0.0398 726  ASP B OD2 
3237 N N   . SER B 71  ? 0.5329 0.6280 0.4138 -0.0437 -0.0839 -0.0865 727  SER B N   
3238 C CA  . SER B 71  ? 0.5404 0.6123 0.3949 -0.0335 -0.0738 -0.1015 727  SER B CA  
3239 C C   . SER B 71  ? 0.5714 0.6472 0.4467 -0.0175 -0.0592 -0.0988 727  SER B C   
3240 O O   . SER B 71  ? 0.5857 0.6400 0.4507 -0.0078 -0.0516 -0.1097 727  SER B O   
3241 C CB  . SER B 71  ? 0.5937 0.6731 0.4196 -0.0322 -0.0719 -0.1042 727  SER B CB  
3242 O OG  . SER B 71  ? 0.6952 0.7526 0.4916 -0.0210 -0.0617 -0.1190 727  SER B OG  
3243 N N   . GLN B 72  ? 0.4922 0.5946 0.3953 -0.0148 -0.0556 -0.0838 728  GLN B N   
3244 C CA  . GLN B 72  ? 0.4677 0.5777 0.3920 -0.0032 -0.0435 -0.0792 728  GLN B CA  
3245 C C   . GLN B 72  ? 0.4909 0.5897 0.4374 -0.0042 -0.0458 -0.0791 728  GLN B C   
3246 O O   . GLN B 72  ? 0.4895 0.5819 0.4430 0.0057  -0.0372 -0.0825 728  GLN B O   
3247 C CB  . GLN B 72  ? 0.4708 0.6080 0.4124 -0.0032 -0.0403 -0.0633 728  GLN B CB  
3248 C CG  . GLN B 72  ? 0.6446 0.7914 0.6072 0.0051  -0.0291 -0.0573 728  GLN B CG  
3249 C CD  . GLN B 72  ? 0.9256 1.0917 0.9047 0.0022  -0.0275 -0.0414 728  GLN B CD  
3250 O OE1 . GLN B 72  ? 0.8941 1.0685 0.8875 0.0058  -0.0195 -0.0358 728  GLN B OE1 
3251 N NE2 . GLN B 72  ? 0.8390 1.0116 0.8153 -0.0047 -0.0353 -0.0332 728  GLN B NE2 
3252 N N   . ILE B 73  ? 0.4370 0.5367 0.3952 -0.0155 -0.0573 -0.0739 729  ILE B N   
3253 C CA  . ILE B 73  ? 0.4270 0.5181 0.4060 -0.0178 -0.0602 -0.0726 729  ILE B CA  
3254 C C   . ILE B 73  ? 0.4866 0.5474 0.4492 -0.0149 -0.0587 -0.0871 729  ILE B C   
3255 O O   . ILE B 73  ? 0.4790 0.5319 0.4550 -0.0078 -0.0530 -0.0879 729  ILE B O   
3256 C CB  . ILE B 73  ? 0.4572 0.5587 0.4491 -0.0305 -0.0727 -0.0638 729  ILE B CB  
3257 C CG1 . ILE B 73  ? 0.4466 0.5744 0.4550 -0.0290 -0.0720 -0.0484 729  ILE B CG1 
3258 C CG2 . ILE B 73  ? 0.4445 0.5368 0.4548 -0.0335 -0.0755 -0.0632 729  ILE B CG2 
3259 C CD1 . ILE B 73  ? 0.4480 0.5923 0.4609 -0.0387 -0.0839 -0.0388 729  ILE B CD1 
3260 N N   . LEU B 74  ? 0.4456 0.4881 0.3765 -0.0195 -0.0632 -0.0984 730  LEU B N   
3261 C CA  . LEU B 74  ? 0.4643 0.4712 0.3702 -0.0157 -0.0613 -0.1135 730  LEU B CA  
3262 C C   . LEU B 74  ? 0.4672 0.4715 0.3712 0.0047  -0.0455 -0.1176 730  LEU B C   
3263 O O   . LEU B 74  ? 0.4345 0.4190 0.3402 0.0126  -0.0411 -0.1224 730  LEU B O   
3264 C CB  . LEU B 74  ? 0.4907 0.4796 0.3582 -0.0249 -0.0687 -0.1244 730  LEU B CB  
3265 C CG  . LEU B 74  ? 0.5968 0.5423 0.4275 -0.0194 -0.0655 -0.1421 730  LEU B CG  
3266 C CD1 . LEU B 74  ? 0.6154 0.5318 0.4503 -0.0241 -0.0698 -0.1457 730  LEU B CD1 
3267 C CD2 . LEU B 74  ? 0.6597 0.5896 0.4507 -0.0306 -0.0736 -0.1520 730  LEU B CD2 
3268 N N   . ASP B 75  ? 0.4279 0.4545 0.3291 0.0131  -0.0371 -0.1141 731  ASP B N   
3269 C CA  . ASP B 75  ? 0.4343 0.4684 0.3371 0.0318  -0.0218 -0.1151 731  ASP B CA  
3270 C C   . ASP B 75  ? 0.4404 0.4875 0.3781 0.0363  -0.0177 -0.1056 731  ASP B C   
3271 O O   . ASP B 75  ? 0.4295 0.4663 0.3683 0.0490  -0.0101 -0.1098 731  ASP B O   
3272 C CB  . ASP B 75  ? 0.4619 0.5246 0.3608 0.0358  -0.0149 -0.1092 731  ASP B CB  
3273 C CG  . ASP B 75  ? 0.7529 0.8049 0.6140 0.0415  -0.0110 -0.1204 731  ASP B CG  
3274 O OD1 . ASP B 75  ? 0.8203 0.8458 0.6589 0.0533  -0.0050 -0.1332 731  ASP B OD1 
3275 O OD2 . ASP B 75  ? 0.8384 0.9076 0.6905 0.0355  -0.0130 -0.1161 731  ASP B OD2 
3276 N N   . LEU B 76  ? 0.3710 0.4395 0.3352 0.0263  -0.0228 -0.0928 732  LEU B N   
3277 C CA  . LEU B 76  ? 0.3582 0.4390 0.3535 0.0279  -0.0202 -0.0834 732  LEU B CA  
3278 C C   . LEU B 76  ? 0.3945 0.4527 0.3961 0.0277  -0.0239 -0.0878 732  LEU B C   
3279 O O   . LEU B 76  ? 0.3764 0.4375 0.3931 0.0360  -0.0177 -0.0854 732  LEU B O   
3280 C CB  . LEU B 76  ? 0.3443 0.4451 0.3594 0.0173  -0.0256 -0.0702 732  LEU B CB  
3281 C CG  . LEU B 76  ? 0.3873 0.5119 0.4026 0.0179  -0.0203 -0.0618 732  LEU B CG  
3282 C CD1 . LEU B 76  ? 0.3849 0.5189 0.4086 0.0074  -0.0282 -0.0513 732  LEU B CD1 
3283 C CD2 . LEU B 76  ? 0.3913 0.5323 0.4225 0.0248  -0.0102 -0.0555 732  LEU B CD2 
3284 N N   . SER B 77  ? 0.3490 0.3854 0.3376 0.0174  -0.0342 -0.0940 733  SER B N   
3285 C CA  . SER B 77  ? 0.3533 0.3649 0.3434 0.0141  -0.0391 -0.0982 733  SER B CA  
3286 C C   . SER B 77  ? 0.3984 0.3863 0.3731 0.0297  -0.0303 -0.1079 733  SER B C   
3287 O O   . SER B 77  ? 0.3930 0.3740 0.3814 0.0348  -0.0281 -0.1059 733  SER B O   
3288 C CB  . SER B 77  ? 0.4095 0.4038 0.3829 -0.0020 -0.0520 -0.1030 733  SER B CB  
3289 O OG  . SER B 77  ? 0.5588 0.5333 0.5375 -0.0087 -0.0578 -0.1041 733  SER B OG  
3290 N N   . ASN B 78  ? 0.3594 0.3359 0.3048 0.0387  -0.0248 -0.1177 734  ASN B N   
3291 C CA  . ASN B 78  ? 0.3693 0.3237 0.2960 0.0575  -0.0145 -0.1270 734  ASN B CA  
3292 C C   . ASN B 78  ? 0.3787 0.3619 0.3299 0.0738  -0.0023 -0.1183 734  ASN B C   
3293 O O   . ASN B 78  ? 0.3873 0.3580 0.3389 0.0878  0.0040  -0.1203 734  ASN B O   
3294 C CB  . ASN B 78  ? 0.4226 0.3626 0.3117 0.0640  -0.0104 -0.1386 734  ASN B CB  
3295 C CG  . ASN B 78  ? 0.8373 0.7381 0.6913 0.0515  -0.0207 -0.1510 734  ASN B CG  
3296 O OD1 . ASN B 78  ? 0.8071 0.6846 0.6606 0.0379  -0.0311 -0.1525 734  ASN B OD1 
3297 N ND2 . ASN B 78  ? 0.7811 0.6742 0.6029 0.0548  -0.0180 -0.1600 734  ASN B ND2 
3298 N N   . ARG B 79  ? 0.3055 0.3269 0.2758 0.0711  0.0005  -0.1081 735  ARG B N   
3299 C CA  . ARG B 79  ? 0.2826 0.3362 0.2767 0.0814  0.0103  -0.0982 735  ARG B CA  
3300 C C   . ARG B 79  ? 0.3083 0.3637 0.3294 0.0779  0.0070  -0.0910 735  ARG B C   
3301 O O   . ARG B 79  ? 0.2850 0.3484 0.3163 0.0908  0.0144  -0.0882 735  ARG B O   
3302 C CB  . ARG B 79  ? 0.2465 0.3353 0.2512 0.0747  0.0121  -0.0887 735  ARG B CB  
3303 C CG  . ARG B 79  ? 0.4128 0.5065 0.3925 0.0815  0.0184  -0.0941 735  ARG B CG  
3304 C CD  . ARG B 79  ? 0.5462 0.6763 0.5390 0.0758  0.0216  -0.0824 735  ARG B CD  
3305 N NE  . ARG B 79  ? 0.5918 0.7253 0.5619 0.0735  0.0221  -0.0854 735  ARG B NE  
3306 C CZ  . ARG B 79  ? 0.7957 0.9551 0.7718 0.0657  0.0228  -0.0753 735  ARG B CZ  
3307 N NH1 . ARG B 79  ? 0.6136 0.7948 0.6160 0.0590  0.0231  -0.0624 735  ARG B NH1 
3308 N NH2 . ARG B 79  ? 0.7019 0.8636 0.6556 0.0641  0.0231  -0.0780 735  ARG B NH2 
3309 N N   . PHE B 80  ? 0.2566 0.3046 0.2878 0.0616  -0.0040 -0.0881 736  PHE B N   
3310 C CA  . PHE B 80  ? 0.2291 0.2760 0.2826 0.0581  -0.0073 -0.0821 736  PHE B CA  
3311 C C   . PHE B 80  ? 0.2925 0.3136 0.3376 0.0701  -0.0043 -0.0884 736  PHE B C   
3312 O O   . PHE B 80  ? 0.2699 0.3025 0.3313 0.0789  0.0009  -0.0827 736  PHE B O   
3313 C CB  . PHE B 80  ? 0.2419 0.2820 0.3026 0.0406  -0.0190 -0.0793 736  PHE B CB  
3314 C CG  . PHE B 80  ? 0.2457 0.2895 0.3302 0.0368  -0.0214 -0.0718 736  PHE B CG  
3315 C CD1 . PHE B 80  ? 0.2651 0.3341 0.3711 0.0335  -0.0198 -0.0614 736  PHE B CD1 
3316 C CD2 . PHE B 80  ? 0.2592 0.2792 0.3421 0.0368  -0.0248 -0.0751 736  PHE B CD2 
3317 C CE1 . PHE B 80  ? 0.2552 0.3263 0.3802 0.0305  -0.0216 -0.0552 736  PHE B CE1 
3318 C CE2 . PHE B 80  ? 0.2725 0.2974 0.3763 0.0341  -0.0262 -0.0678 736  PHE B CE2 
3319 C CZ  . PHE B 80  ? 0.2267 0.2776 0.3513 0.0309  -0.0248 -0.0583 736  PHE B CZ  
3320 N N   . TYR B 81  ? 0.3014 0.2868 0.3188 0.0703  -0.0077 -0.0998 737  TYR B N   
3321 C CA  . TYR B 81  ? 0.3262 0.2770 0.3284 0.0810  -0.0056 -0.1068 737  TYR B CA  
3322 C C   . TYR B 81  ? 0.4087 0.3614 0.4010 0.1058  0.0078  -0.1096 737  TYR B C   
3323 O O   . TYR B 81  ? 0.4197 0.3460 0.4019 0.1184  0.0111  -0.1132 737  TYR B O   
3324 C CB  . TYR B 81  ? 0.3739 0.2829 0.3458 0.0704  -0.0144 -0.1180 737  TYR B CB  
3325 C CG  . TYR B 81  ? 0.3897 0.2979 0.3746 0.0476  -0.0275 -0.1132 737  TYR B CG  
3326 C CD1 . TYR B 81  ? 0.4025 0.3103 0.4086 0.0435  -0.0306 -0.1060 737  TYR B CD1 
3327 C CD2 . TYR B 81  ? 0.4017 0.3127 0.3779 0.0308  -0.0366 -0.1150 737  TYR B CD2 
3328 C CE1 . TYR B 81  ? 0.4122 0.3249 0.4319 0.0241  -0.0413 -0.1002 737  TYR B CE1 
3329 C CE2 . TYR B 81  ? 0.4045 0.3210 0.3947 0.0114  -0.0479 -0.1089 737  TYR B CE2 
3330 C CZ  . TYR B 81  ? 0.4925 0.4096 0.5042 0.0085  -0.0498 -0.1016 737  TYR B CZ  
3331 O OH  . TYR B 81  ? 0.4960 0.4219 0.5226 -0.0088 -0.0597 -0.0946 737  TYR B OH  
3332 N N   . THR B 82  ? 0.3633 0.3480 0.3583 0.1132  0.0158  -0.1069 738  THR B N   
3333 C CA  . THR B 82  ? 0.3551 0.3541 0.3461 0.1368  0.0295  -0.1065 738  THR B CA  
3334 C C   . THR B 82  ? 0.4392 0.4780 0.4659 0.1387  0.0328  -0.0923 738  THR B C   
3335 O O   . THR B 82  ? 0.4579 0.5026 0.4903 0.1565  0.0404  -0.0890 738  THR B O   
3336 C CB  . THR B 82  ? 0.3902 0.4087 0.3674 0.1409  0.0361  -0.1090 738  THR B CB  
3337 O OG1 . THR B 82  ? 0.4534 0.4387 0.3986 0.1332  0.0303  -0.1213 738  THR B OG1 
3338 C CG2 . THR B 82  ? 0.2765 0.3124 0.2480 0.1673  0.0515  -0.1084 738  THR B CG2 
3339 N N   . LEU B 83  ? 0.3900 0.4559 0.4390 0.1206  0.0270  -0.0835 739  LEU B N   
3340 C CA  . LEU B 83  ? 0.3670 0.4683 0.4472 0.1166  0.0279  -0.0704 739  LEU B CA  
3341 C C   . LEU B 83  ? 0.4080 0.4941 0.4992 0.1187  0.0245  -0.0682 739  LEU B C   
3342 O O   . LEU B 83  ? 0.4024 0.5076 0.5073 0.1301  0.0301  -0.0614 739  LEU B O   
3343 C CB  . LEU B 83  ? 0.3638 0.4792 0.4562 0.0951  0.0203  -0.0645 739  LEU B CB  
3344 C CG  . LEU B 83  ? 0.4042 0.5596 0.5166 0.0885  0.0233  -0.0525 739  LEU B CG  
3345 C CD1 . LEU B 83  ? 0.3930 0.5592 0.5288 0.0831  0.0205  -0.0439 739  LEU B CD1 
3346 C CD2 . LEU B 83  ? 0.4094 0.5939 0.5177 0.1010  0.0344  -0.0500 739  LEU B CD2 
3347 N N   . ILE B 84  ? 0.3748 0.4276 0.4587 0.1082  0.0154  -0.0735 740  ILE B N   
3348 C CA  . ILE B 84  ? 0.3803 0.4140 0.4713 0.1085  0.0114  -0.0718 740  ILE B CA  
3349 C C   . ILE B 84  ? 0.4735 0.4621 0.5348 0.1169  0.0112  -0.0834 740  ILE B C   
3350 O O   . ILE B 84  ? 0.4696 0.4333 0.5153 0.1038  0.0036  -0.0905 740  ILE B O   
3351 C CB  . ILE B 84  ? 0.4054 0.4382 0.5118 0.0876  0.0009  -0.0672 740  ILE B CB  
3352 C CG1 . ILE B 84  ? 0.3662 0.4345 0.4921 0.0766  0.0003  -0.0585 740  ILE B CG1 
3353 C CG2 . ILE B 84  ? 0.4235 0.4437 0.5402 0.0882  -0.0020 -0.0631 740  ILE B CG2 
3354 C CD1 . ILE B 84  ? 0.2436 0.3465 0.3889 0.0819  0.0064  -0.0487 740  ILE B CD1 
3355 N N   . PRO B 85  ? 0.4681 0.4453 0.5187 0.1389  0.0197  -0.0856 741  PRO B N   
3356 C CA  . PRO B 85  ? 0.5046 0.4312 0.5208 0.1473  0.0200  -0.0977 741  PRO B CA  
3357 C C   . PRO B 85  ? 0.5970 0.4873 0.6095 0.1343  0.0100  -0.0990 741  PRO B C   
3358 O O   . PRO B 85  ? 0.5728 0.4719 0.6063 0.1332  0.0082  -0.0901 741  PRO B O   
3359 C CB  . PRO B 85  ? 0.5288 0.4567 0.5373 0.1768  0.0329  -0.0972 741  PRO B CB  
3360 C CG  . PRO B 85  ? 0.5588 0.5361 0.6022 0.1810  0.0367  -0.0829 741  PRO B CG  
3361 C CD  . PRO B 85  ? 0.4770 0.4860 0.5448 0.1569  0.0291  -0.0764 741  PRO B CD  
3362 N N   . HIS B 86  ? 0.6100 0.4633 0.5966 0.1217  0.0027  -0.1091 742  HIS B N   
3363 C CA  . HIS B 86  ? 0.6403 0.4593 0.6208 0.1056  -0.0078 -0.1102 742  HIS B CA  
3364 C C   . HIS B 86  ? 0.7624 0.5226 0.7031 0.1145  -0.0067 -0.1214 742  HIS B C   
3365 O O   . HIS B 86  ? 0.7561 0.5014 0.6711 0.1321  0.0017  -0.1301 742  HIS B O   
3366 C CB  . HIS B 86  ? 0.6483 0.4749 0.6330 0.0790  -0.0194 -0.1107 742  HIS B CB  
3367 C CG  . HIS B 86  ? 0.6686 0.5386 0.6906 0.0674  -0.0229 -0.0984 742  HIS B CG  
3368 N ND1 . HIS B 86  ? 0.6703 0.5827 0.7124 0.0736  -0.0166 -0.0924 742  HIS B ND1 
3369 C CD2 . HIS B 86  ? 0.6828 0.5573 0.7218 0.0498  -0.0317 -0.0917 742  HIS B CD2 
3370 C CE1 . HIS B 86  ? 0.6449 0.5814 0.7129 0.0604  -0.0218 -0.0831 742  HIS B CE1 
3371 N NE2 . HIS B 86  ? 0.6543 0.5710 0.7222 0.0469  -0.0304 -0.0823 742  HIS B NE2 
3372 N N   . ASP B 87  ? 0.7816 0.5076 0.7160 0.1031  -0.0146 -0.1207 743  ASP B N   
3373 C CA  . ASP B 87  ? 0.8370 0.4993 0.7312 0.1066  -0.0158 -0.1306 743  ASP B CA  
3374 C C   . ASP B 87  ? 0.9400 0.5770 0.8279 0.0762  -0.0306 -0.1308 743  ASP B C   
3375 O O   . ASP B 87  ? 0.9385 0.5704 0.8407 0.0687  -0.0350 -0.1223 743  ASP B O   
3376 C CB  . ASP B 87  ? 0.8690 0.5113 0.7592 0.1323  -0.0066 -0.1268 743  ASP B CB  
3377 C CG  . ASP B 87  ? 0.9963 0.5666 0.8380 0.1419  -0.0050 -0.1381 743  ASP B CG  
3378 O OD1 . ASP B 87  ? 1.0088 0.5441 0.8156 0.1310  -0.0095 -0.1511 743  ASP B OD1 
3379 O OD2 . ASP B 87  ? 1.0474 0.5948 0.8841 0.1605  0.0007  -0.1338 743  ASP B OD2 
3380 N N   . PHE B 88  ? 0.9233 0.5485 0.7905 0.0582  -0.0383 -0.1397 744  PHE B N   
3381 C CA  . PHE B 88  ? 0.9358 0.5424 0.7949 0.0270  -0.0532 -0.1403 744  PHE B CA  
3382 C C   . PHE B 88  ? 1.0390 0.5740 0.8490 0.0220  -0.0572 -0.1520 744  PHE B C   
3383 O O   . PHE B 88  ? 1.0428 0.5574 0.8390 -0.0061 -0.0704 -0.1538 744  PHE B O   
3384 C CB  . PHE B 88  ? 0.9463 0.5860 0.8121 0.0093  -0.0602 -0.1416 744  PHE B CB  
3385 C CG  . PHE B 88  ? 0.9321 0.6350 0.8446 0.0068  -0.0596 -0.1285 744  PHE B CG  
3386 C CD1 . PHE B 88  ? 0.9511 0.6909 0.8806 0.0256  -0.0491 -0.1262 744  PHE B CD1 
3387 C CD2 . PHE B 88  ? 0.9497 0.6743 0.8875 -0.0144 -0.0693 -0.1181 744  PHE B CD2 
3388 C CE1 . PHE B 88  ? 0.9329 0.7244 0.9009 0.0222  -0.0489 -0.1146 744  PHE B CE1 
3389 C CE2 . PHE B 88  ? 0.9533 0.7308 0.9301 -0.0147 -0.0679 -0.1066 744  PHE B CE2 
3390 C CZ  . PHE B 88  ? 0.9118 0.7196 0.9020 0.0032  -0.0579 -0.1054 744  PHE B CZ  
3391 N N   . GLY B 89  ? 1.0349 0.5326 0.8184 0.0489  -0.0461 -0.1590 745  GLY B N   
3392 C CA  . GLY B 89  ? 1.0879 0.5098 0.8185 0.0485  -0.0479 -0.1714 745  GLY B CA  
3393 C C   . GLY B 89  ? 1.1848 0.5846 0.8781 0.0353  -0.0533 -0.1861 745  GLY B C   
3394 O O   . GLY B 89  ? 1.1743 0.5974 0.8655 0.0506  -0.0452 -0.1916 745  GLY B O   
3395 N N   . MET B 90  ? 1.1806 0.5397 0.8458 0.0048  -0.0677 -0.1913 746  MET B N   
3396 C CA  . MET B 90  ? 1.2035 0.5383 0.8295 -0.0129 -0.0756 -0.2052 746  MET B CA  
3397 C C   . MET B 90  ? 1.2342 0.6265 0.8904 -0.0407 -0.0877 -0.1983 746  MET B C   
3398 O O   . MET B 90  ? 1.2455 0.6256 0.8735 -0.0592 -0.0965 -0.2076 746  MET B O   
3399 C CB  . MET B 90  ? 1.2787 0.5327 0.8508 -0.0326 -0.0855 -0.2155 746  MET B CB  
3400 C CG  . MET B 90  ? 1.3574 0.5478 0.8975 -0.0075 -0.0751 -0.2207 746  MET B CG  
3401 S SD  . MET B 90  ? 1.4274 0.5958 0.9330 0.0361  -0.0555 -0.2356 746  MET B SD  
3402 C CE  . MET B 90  ? 1.4122 0.5203 0.8971 0.0647  -0.0446 -0.2341 746  MET B CE  
3403 N N   . LYS B 91  ? 1.1591 0.6122 0.8703 -0.0435 -0.0883 -0.1819 747  LYS B N   
3404 C CA  . LYS B 91  ? 1.1305 0.6414 0.8750 -0.0658 -0.0983 -0.1726 747  LYS B CA  
3405 C C   . LYS B 91  ? 1.1490 0.7087 0.9124 -0.0483 -0.0894 -0.1723 747  LYS B C   
3406 O O   . LYS B 91  ? 1.1453 0.7177 0.9213 -0.0198 -0.0752 -0.1710 747  LYS B O   
3407 C CB  . LYS B 91  ? 1.1384 0.6878 0.9304 -0.0744 -0.1016 -0.1550 747  LYS B CB  
3408 C CG  . LYS B 91  ? 1.3810 0.8904 1.1623 -0.0908 -0.1092 -0.1515 747  LYS B CG  
3409 C CD  . LYS B 91  ? 1.4787 1.0326 1.3080 -0.0974 -0.1111 -0.1338 747  LYS B CD  
3410 C CE  . LYS B 91  ? 1.5531 1.1019 1.3980 -0.0732 -0.0997 -0.1280 747  LYS B CE  
3411 N NZ  . LYS B 91  ? 1.5988 1.1891 1.4696 -0.0455 -0.0867 -0.1260 747  LYS B NZ  
3412 N N   . LYS B 92  ? 1.0660 0.6560 0.8329 -0.0658 -0.0979 -0.1718 748  LYS B N   
3413 C CA  . LYS B 92  ? 1.0262 0.6650 0.8134 -0.0522 -0.0906 -0.1691 748  LYS B CA  
3414 C C   . LYS B 92  ? 0.9955 0.6896 0.8373 -0.0493 -0.0882 -0.1519 748  LYS B C   
3415 O O   . LYS B 92  ? 0.9895 0.6953 0.8506 -0.0685 -0.0979 -0.1426 748  LYS B O   
3416 C CB  . LYS B 92  ? 1.0634 0.7173 0.8372 -0.0724 -0.1014 -0.1723 748  LYS B CB  
3417 C CG  . LYS B 92  ? 1.2930 0.8999 1.0118 -0.0723 -0.1018 -0.1901 748  LYS B CG  
3418 C CD  . LYS B 92  ? 1.3976 1.0342 1.1109 -0.0855 -0.1092 -0.1910 748  LYS B CD  
3419 C CE  . LYS B 92  ? 1.5869 1.1763 1.2427 -0.0914 -0.1126 -0.2087 748  LYS B CE  
3420 N NZ  . LYS B 92  ? 1.6952 1.3184 1.3468 -0.0951 -0.1150 -0.2094 748  LYS B NZ  
3421 N N   . PRO B 93  ? 0.8862 0.6135 0.7517 -0.0265 -0.0756 -0.1472 749  PRO B N   
3422 C CA  . PRO B 93  ? 0.8320 0.6072 0.7446 -0.0253 -0.0739 -0.1319 749  PRO B CA  
3423 C C   . PRO B 93  ? 0.8272 0.6423 0.7594 -0.0437 -0.0832 -0.1236 749  PRO B C   
3424 O O   . PRO B 93  ? 0.8267 0.6429 0.7400 -0.0508 -0.0876 -0.1292 749  PRO B O   
3425 C CB  . PRO B 93  ? 0.8425 0.6404 0.7666 0.0002  -0.0594 -0.1309 749  PRO B CB  
3426 C CG  . PRO B 93  ? 0.9337 0.6941 0.8208 0.0161  -0.0520 -0.1443 749  PRO B CG  
3427 C CD  . PRO B 93  ? 0.9086 0.6331 0.7584 -0.0020 -0.0625 -0.1551 749  PRO B CD  
3428 N N   . PRO B 94  ? 0.7471 0.5953 0.7154 -0.0504 -0.0861 -0.1101 750  PRO B N   
3429 C CA  . PRO B 94  ? 0.7153 0.6011 0.7006 -0.0648 -0.0941 -0.1015 750  PRO B CA  
3430 C C   . PRO B 94  ? 0.7182 0.6306 0.7060 -0.0544 -0.0883 -0.1013 750  PRO B C   
3431 O O   . PRO B 94  ? 0.6967 0.6239 0.6989 -0.0373 -0.0775 -0.0985 750  PRO B O   
3432 C CB  . PRO B 94  ? 0.7208 0.6328 0.7422 -0.0674 -0.0944 -0.0877 750  PRO B CB  
3433 C CG  . PRO B 94  ? 0.7848 0.6836 0.8128 -0.0500 -0.0840 -0.0885 750  PRO B CG  
3434 C CD  . PRO B 94  ? 0.7575 0.6104 0.7507 -0.0443 -0.0819 -0.1018 750  PRO B CD  
3435 N N   . LEU B 95  ? 0.6485 0.5643 0.6184 -0.0654 -0.0957 -0.1048 751  LEU B N   
3436 C CA  . LEU B 95  ? 0.6187 0.5582 0.5871 -0.0581 -0.0917 -0.1042 751  LEU B CA  
3437 C C   . LEU B 95  ? 0.6018 0.5839 0.6059 -0.0565 -0.0905 -0.0891 751  LEU B C   
3438 O O   . LEU B 95  ? 0.5951 0.5944 0.6154 -0.0692 -0.0990 -0.0799 751  LEU B O   
3439 C CB  . LEU B 95  ? 0.6261 0.5578 0.5653 -0.0728 -0.1018 -0.1108 751  LEU B CB  
3440 C CG  . LEU B 95  ? 0.6715 0.6245 0.6025 -0.0681 -0.0997 -0.1108 751  LEU B CG  
3441 C CD1 . LEU B 95  ? 0.6771 0.6223 0.5978 -0.0467 -0.0851 -0.1177 751  LEU B CD1 
3442 C CD2 . LEU B 95  ? 0.6966 0.6367 0.5951 -0.0849 -0.1112 -0.1184 751  LEU B CD2 
3443 N N   . LEU B 96  ? 0.5176 0.5152 0.5331 -0.0405 -0.0795 -0.0861 752  LEU B N   
3444 C CA  . LEU B 96  ? 0.4922 0.5227 0.5369 -0.0367 -0.0763 -0.0730 752  LEU B CA  
3445 C C   . LEU B 96  ? 0.5563 0.6104 0.5991 -0.0400 -0.0795 -0.0674 752  LEU B C   
3446 O O   . LEU B 96  ? 0.5546 0.6204 0.5979 -0.0306 -0.0720 -0.0653 752  LEU B O   
3447 C CB  . LEU B 96  ? 0.4795 0.5138 0.5364 -0.0206 -0.0638 -0.0716 752  LEU B CB  
3448 C CG  . LEU B 96  ? 0.5308 0.5426 0.5865 -0.0131 -0.0589 -0.0774 752  LEU B CG  
3449 C CD1 . LEU B 96  ? 0.5286 0.5517 0.5953 0.0017  -0.0474 -0.0749 752  LEU B CD1 
3450 C CD2 . LEU B 96  ? 0.5361 0.5431 0.6070 -0.0215 -0.0646 -0.0724 752  LEU B CD2 
3451 N N   . ASN B 97  ? 0.5313 0.5935 0.5715 -0.0541 -0.0910 -0.0639 753  ASN B N   
3452 C CA  . ASN B 97  ? 0.5230 0.6095 0.5620 -0.0583 -0.0960 -0.0567 753  ASN B CA  
3453 C C   . ASN B 97  ? 0.5645 0.6784 0.6303 -0.0620 -0.1006 -0.0416 753  ASN B C   
3454 O O   . ASN B 97  ? 0.5576 0.6936 0.6319 -0.0569 -0.0992 -0.0317 753  ASN B O   
3455 C CB  . ASN B 97  ? 0.5244 0.6011 0.5347 -0.0711 -0.1060 -0.0648 753  ASN B CB  
3456 C CG  . ASN B 97  ? 0.7185 0.7829 0.7235 -0.0883 -0.1174 -0.0676 753  ASN B CG  
3457 O OD1 . ASN B 97  ? 0.7522 0.8135 0.7745 -0.0905 -0.1177 -0.0640 753  ASN B OD1 
3458 N ND2 . ASN B 97  ? 0.5389 0.5951 0.5177 -0.1023 -0.1275 -0.0739 753  ASN B ND2 
3459 N N   . ASN B 98  ? 0.5079 0.6194 0.5860 -0.0695 -0.1053 -0.0393 754  ASN B N   
3460 C CA  . ASN B 98  ? 0.4822 0.6197 0.5860 -0.0714 -0.1083 -0.0251 754  ASN B CA  
3461 C C   . ASN B 98  ? 0.4933 0.6324 0.6178 -0.0579 -0.0976 -0.0198 754  ASN B C   
3462 O O   . ASN B 98  ? 0.4820 0.6021 0.6031 -0.0501 -0.0894 -0.0272 754  ASN B O   
3463 C CB  . ASN B 98  ? 0.4931 0.6315 0.5994 -0.0879 -0.1189 -0.0239 754  ASN B CB  
3464 C CG  . ASN B 98  ? 0.7985 0.9061 0.8990 -0.0915 -0.1174 -0.0332 754  ASN B CG  
3465 O OD1 . ASN B 98  ? 0.8152 0.9256 0.9342 -0.0902 -0.1149 -0.0278 754  ASN B OD1 
3466 N ND2 . ASN B 98  ? 0.7151 0.7917 0.7882 -0.0955 -0.1188 -0.0470 754  ASN B ND2 
3467 N N   . ALA B 99  ? 0.4157 0.5785 0.5601 -0.0546 -0.0976 -0.0066 755  ALA B N   
3468 C CA  . ALA B 99  ? 0.3978 0.5616 0.5588 -0.0431 -0.0884 -0.0011 755  ALA B CA  
3469 C C   . ALA B 99  ? 0.4474 0.5994 0.6175 -0.0458 -0.0871 -0.0040 755  ALA B C   
3470 O O   . ALA B 99  ? 0.4469 0.5891 0.6226 -0.0372 -0.0788 -0.0053 755  ALA B O   
3471 C CB  . ALA B 99  ? 0.3915 0.5805 0.5669 -0.0374 -0.0884 0.0134  755  ALA B CB  
3472 N N   . ASP B 100 ? 0.3885 0.5413 0.5587 -0.0590 -0.0957 -0.0044 756  ASP B N   
3473 C CA  . ASP B 100 ? 0.3756 0.5160 0.5527 -0.0633 -0.0954 -0.0063 756  ASP B CA  
3474 C C   . ASP B 100 ? 0.4093 0.5185 0.5735 -0.0587 -0.0899 -0.0186 756  ASP B C   
3475 O O   . ASP B 100 ? 0.4036 0.5042 0.5764 -0.0532 -0.0842 -0.0185 756  ASP B O   
3476 C CB  . ASP B 100 ? 0.3956 0.5415 0.5717 -0.0811 -0.1067 -0.0041 756  ASP B CB  
3477 C CG  . ASP B 100 ? 0.5720 0.7545 0.7679 -0.0847 -0.1110 0.0110  756  ASP B CG  
3478 O OD1 . ASP B 100 ? 0.5664 0.7615 0.7802 -0.0740 -0.1038 0.0192  756  ASP B OD1 
3479 O OD2 . ASP B 100 ? 0.6298 0.8293 0.8225 -0.0982 -0.1215 0.0150  756  ASP B OD2 
3480 N N   . SER B 101 ? 0.3579 0.4513 0.5004 -0.0603 -0.0916 -0.0286 757  SER B N   
3481 C CA  . SER B 101 ? 0.3567 0.4226 0.4843 -0.0532 -0.0856 -0.0401 757  SER B CA  
3482 C C   . SER B 101 ? 0.3489 0.4205 0.4852 -0.0380 -0.0745 -0.0386 757  SER B C   
3483 O O   . SER B 101 ? 0.3391 0.3976 0.4772 -0.0310 -0.0686 -0.0421 757  SER B O   
3484 C CB  . SER B 101 ? 0.4250 0.4756 0.5256 -0.0572 -0.0893 -0.0505 757  SER B CB  
3485 O OG  . SER B 101 ? 0.6045 0.6320 0.6901 -0.0699 -0.0971 -0.0567 757  SER B OG  
3486 N N   . VAL B 102 ? 0.2773 0.3682 0.4184 -0.0338 -0.0722 -0.0325 758  VAL B N   
3487 C CA  . VAL B 102 ? 0.2678 0.3641 0.4150 -0.0228 -0.0628 -0.0301 758  VAL B CA  
3488 C C   . VAL B 102 ? 0.3032 0.4038 0.4693 -0.0199 -0.0594 -0.0231 758  VAL B C   
3489 O O   . VAL B 102 ? 0.2959 0.3920 0.4657 -0.0134 -0.0526 -0.0243 758  VAL B O   
3490 C CB  . VAL B 102 ? 0.3103 0.4213 0.4531 -0.0207 -0.0621 -0.0252 758  VAL B CB  
3491 C CG1 . VAL B 102 ? 0.3062 0.4232 0.4569 -0.0130 -0.0538 -0.0194 758  VAL B CG1 
3492 C CG2 . VAL B 102 ? 0.3142 0.4190 0.4362 -0.0212 -0.0627 -0.0335 758  VAL B CG2 
3493 N N   . GLN B 103 ? 0.2275 0.3387 0.4048 -0.0251 -0.0643 -0.0157 759  GLN B N   
3494 C CA  . GLN B 103 ? 0.2089 0.3246 0.4020 -0.0225 -0.0612 -0.0091 759  GLN B CA  
3495 C C   . GLN B 103 ? 0.2333 0.3339 0.4283 -0.0233 -0.0600 -0.0140 759  GLN B C   
3496 O O   . GLN B 103 ? 0.2328 0.3314 0.4344 -0.0176 -0.0541 -0.0125 759  GLN B O   
3497 C CB  . GLN B 103 ? 0.2273 0.3610 0.4311 -0.0268 -0.0663 0.0004  759  GLN B CB  
3498 C CG  . GLN B 103 ? 0.4983 0.6471 0.7042 -0.0200 -0.0640 0.0086  759  GLN B CG  
3499 C CD  . GLN B 103 ? 0.7591 0.9303 0.9760 -0.0206 -0.0679 0.0197  759  GLN B CD  
3500 O OE1 . GLN B 103 ? 0.6837 0.8672 0.9001 -0.0145 -0.0672 0.0269  759  GLN B OE1 
3501 N NE2 . GLN B 103 ? 0.6731 0.8517 0.9001 -0.0273 -0.0717 0.0225  759  GLN B NE2 
3502 N N   . ALA B 104 ? 0.1929 0.2807 0.3794 -0.0307 -0.0657 -0.0198 760  ALA B N   
3503 C CA  . ALA B 104 ? 0.2021 0.2705 0.3862 -0.0310 -0.0650 -0.0245 760  ALA B CA  
3504 C C   . ALA B 104 ? 0.2450 0.3031 0.4230 -0.0198 -0.0573 -0.0306 760  ALA B C   
3505 O O   . ALA B 104 ? 0.2567 0.3099 0.4413 -0.0151 -0.0534 -0.0296 760  ALA B O   
3506 C CB  . ALA B 104 ? 0.2209 0.2722 0.3907 -0.0418 -0.0729 -0.0303 760  ALA B CB  
3507 N N   . LYS B 105 ? 0.1950 0.2526 0.3606 -0.0156 -0.0552 -0.0360 761  LYS B N   
3508 C CA  . LYS B 105 ? 0.1710 0.2249 0.3316 -0.0047 -0.0474 -0.0405 761  LYS B CA  
3509 C C   . LYS B 105 ? 0.1979 0.2686 0.3720 0.0001  -0.0414 -0.0337 761  LYS B C   
3510 O O   . LYS B 105 ? 0.2036 0.2741 0.3810 0.0068  -0.0363 -0.0341 761  LYS B O   
3511 C CB  . LYS B 105 ? 0.1688 0.2186 0.3109 -0.0018 -0.0464 -0.0478 761  LYS B CB  
3512 C CG  . LYS B 105 ? 0.3276 0.3532 0.4501 -0.0058 -0.0516 -0.0567 761  LYS B CG  
3513 C CD  . LYS B 105 ? 0.4580 0.4603 0.5734 0.0015  -0.0484 -0.0621 761  LYS B CD  
3514 C CE  . LYS B 105 ? 0.5452 0.5167 0.6380 -0.0051 -0.0546 -0.0707 761  LYS B CE  
3515 N NZ  . LYS B 105 ? 0.7174 0.6711 0.8141 -0.0094 -0.0578 -0.0687 761  LYS B NZ  
3516 N N   . ALA B 106 ? 0.1520 0.2361 0.3330 -0.0035 -0.0424 -0.0270 762  ALA B N   
3517 C CA  . ALA B 106 ? 0.1536 0.2476 0.3436 -0.0011 -0.0375 -0.0208 762  ALA B CA  
3518 C C   . ALA B 106 ? 0.2194 0.3104 0.4204 -0.0009 -0.0367 -0.0179 762  ALA B C   
3519 O O   . ALA B 106 ? 0.1851 0.2791 0.3896 0.0022  -0.0322 -0.0167 762  ALA B O   
3520 C CB  . ALA B 106 ? 0.1581 0.2605 0.3493 -0.0036 -0.0389 -0.0143 762  ALA B CB  
3521 N N   . GLU B 107 ? 0.2149 0.3019 0.4208 -0.0051 -0.0413 -0.0163 763  GLU B N   
3522 C CA  . GLU B 107 ? 0.2204 0.3045 0.4356 -0.0056 -0.0410 -0.0132 763  GLU B CA  
3523 C C   . GLU B 107 ? 0.2469 0.3215 0.4596 -0.0007 -0.0386 -0.0176 763  GLU B C   
3524 O O   . GLU B 107 ? 0.2211 0.2990 0.4401 0.0023  -0.0353 -0.0147 763  GLU B O   
3525 C CB  . GLU B 107 ? 0.2472 0.3290 0.4659 -0.0125 -0.0469 -0.0110 763  GLU B CB  
3526 C CG  . GLU B 107 ? 0.4372 0.5334 0.6643 -0.0152 -0.0482 -0.0031 763  GLU B CG  
3527 C CD  . GLU B 107 ? 0.7437 0.8435 0.9747 -0.0240 -0.0549 -0.0001 763  GLU B CD  
3528 O OE1 . GLU B 107 ? 0.5199 0.6104 0.7524 -0.0282 -0.0568 -0.0005 763  GLU B OE1 
3529 O OE2 . GLU B 107 ? 0.7410 0.8540 0.9732 -0.0273 -0.0585 0.0037  763  GLU B OE2 
3530 N N   . MET B 108 ? 0.1943 0.2566 0.3962 0.0007  -0.0404 -0.0243 764  MET B N   
3531 C CA  . MET B 108 ? 0.1964 0.2475 0.3930 0.0085  -0.0374 -0.0284 764  MET B CA  
3532 C C   . MET B 108 ? 0.2253 0.2915 0.4263 0.0163  -0.0309 -0.0266 764  MET B C   
3533 O O   . MET B 108 ? 0.2234 0.2910 0.4296 0.0218  -0.0282 -0.0243 764  MET B O   
3534 C CB  . MET B 108 ? 0.2457 0.2792 0.4248 0.0104  -0.0391 -0.0370 764  MET B CB  
3535 C CG  . MET B 108 ? 0.3299 0.3505 0.5011 0.0225  -0.0344 -0.0411 764  MET B CG  
3536 S SD  . MET B 108 ? 0.4230 0.4258 0.5698 0.0302  -0.0322 -0.0520 764  MET B SD  
3537 C CE  . MET B 108 ? 0.3612 0.3936 0.5129 0.0357  -0.0258 -0.0502 764  MET B CE  
3538 N N   . LEU B 109 ? 0.1612 0.2399 0.3597 0.0157  -0.0287 -0.0266 765  LEU B N   
3539 C CA  . LEU B 109 ? 0.1396 0.2351 0.3412 0.0196  -0.0232 -0.0240 765  LEU B CA  
3540 C C   . LEU B 109 ? 0.1756 0.2804 0.3880 0.0155  -0.0225 -0.0171 765  LEU B C   
3541 O O   . LEU B 109 ? 0.1734 0.2888 0.3905 0.0190  -0.0194 -0.0145 765  LEU B O   
3542 C CB  . LEU B 109 ? 0.1323 0.2366 0.3266 0.0180  -0.0215 -0.0249 765  LEU B CB  
3543 C CG  . LEU B 109 ? 0.1769 0.2750 0.3575 0.0236  -0.0205 -0.0322 765  LEU B CG  
3544 C CD1 . LEU B 109 ? 0.1438 0.2521 0.3176 0.0206  -0.0193 -0.0315 765  LEU B CD1 
3545 C CD2 . LEU B 109 ? 0.2080 0.3081 0.3861 0.0356  -0.0148 -0.0349 765  LEU B CD2 
3546 N N   . ASP B 110 ? 0.1226 0.2241 0.3379 0.0088  -0.0253 -0.0139 766  ASP B N   
3547 C CA  . ASP B 110 ? 0.1160 0.2208 0.3373 0.0049  -0.0247 -0.0085 766  ASP B CA  
3548 C C   . ASP B 110 ? 0.1395 0.2437 0.3672 0.0077  -0.0248 -0.0072 766  ASP B C   
3549 O O   . ASP B 110 ? 0.0976 0.2108 0.3285 0.0067  -0.0230 -0.0036 766  ASP B O   
3550 C CB  . ASP B 110 ? 0.1339 0.2326 0.3562 0.0010  -0.0272 -0.0060 766  ASP B CB  
3551 C CG  . ASP B 110 ? 0.1811 0.2808 0.3976 -0.0010 -0.0268 -0.0043 766  ASP B CG  
3552 O OD1 . ASP B 110 ? 0.1497 0.2533 0.3601 -0.0009 -0.0252 -0.0057 766  ASP B OD1 
3553 O OD2 . ASP B 110 ? 0.2529 0.3504 0.4706 -0.0017 -0.0276 -0.0008 766  ASP B OD2 
3554 N N   . ASN B 111 ? 0.0987 0.1916 0.3269 0.0103  -0.0273 -0.0095 767  ASN B N   
3555 C CA  . ASN B 111 ? 0.1108 0.1992 0.3431 0.0141  -0.0276 -0.0078 767  ASN B CA  
3556 C C   . ASN B 111 ? 0.1800 0.2770 0.4124 0.0228  -0.0241 -0.0080 767  ASN B C   
3557 O O   . ASN B 111 ? 0.1830 0.2887 0.4216 0.0246  -0.0232 -0.0032 767  ASN B O   
3558 C CB  . ASN B 111 ? 0.1369 0.2071 0.3657 0.0134  -0.0314 -0.0104 767  ASN B CB  
3559 C CG  . ASN B 111 ? 0.2500 0.3189 0.4832 0.0051  -0.0347 -0.0068 767  ASN B CG  
3560 O OD1 . ASN B 111 ? 0.2253 0.3006 0.4650 0.0032  -0.0338 -0.0016 767  ASN B OD1 
3561 N ND2 . ASN B 111 ? 0.1479 0.2105 0.3773 0.0001  -0.0385 -0.0090 767  ASN B ND2 
3562 N N   . LEU B 112 ? 0.1198 0.2173 0.3454 0.0284  -0.0219 -0.0128 768  LEU B N   
3563 C CA  . LEU B 112 ? 0.1090 0.2186 0.3345 0.0390  -0.0172 -0.0124 768  LEU B CA  
3564 C C   . LEU B 112 ? 0.1373 0.2732 0.3710 0.0351  -0.0151 -0.0060 768  LEU B C   
3565 O O   . LEU B 112 ? 0.1350 0.2865 0.3743 0.0418  -0.0127 -0.0018 768  LEU B O   
3566 C CB  . LEU B 112 ? 0.1111 0.2165 0.3254 0.0458  -0.0144 -0.0190 768  LEU B CB  
3567 C CG  . LEU B 112 ? 0.1821 0.2593 0.3833 0.0512  -0.0160 -0.0262 768  LEU B CG  
3568 C CD1 . LEU B 112 ? 0.1673 0.2417 0.3546 0.0580  -0.0125 -0.0331 768  LEU B CD1 
3569 C CD2 . LEU B 112 ? 0.2504 0.3156 0.4510 0.0621  -0.0148 -0.0248 768  LEU B CD2 
3570 N N   . LEU B 113 ? 0.1091 0.2485 0.3426 0.0238  -0.0165 -0.0046 769  LEU B N   
3571 C CA  . LEU B 113 ? 0.1165 0.2751 0.3537 0.0163  -0.0156 0.0012  769  LEU B CA  
3572 C C   . LEU B 113 ? 0.1753 0.3390 0.4192 0.0140  -0.0175 0.0065  769  LEU B C   
3573 O O   . LEU B 113 ? 0.1506 0.3356 0.3997 0.0139  -0.0165 0.0117  769  LEU B O   
3574 C CB  . LEU B 113 ? 0.1184 0.2718 0.3491 0.0056  -0.0164 0.0012  769  LEU B CB  
3575 C CG  . LEU B 113 ? 0.1610 0.3193 0.3853 0.0053  -0.0141 -0.0008 769  LEU B CG  
3576 C CD1 . LEU B 113 ? 0.1633 0.3137 0.3803 -0.0047 -0.0151 0.0009  769  LEU B CD1 
3577 C CD2 . LEU B 113 ? 0.1689 0.3525 0.3961 0.0067  -0.0105 0.0028  769  LEU B CD2 
3578 N N   . ASP B 114 ? 0.1602 0.3069 0.4043 0.0125  -0.0202 0.0059  770  ASP B N   
3579 C CA  . ASP B 114 ? 0.1464 0.2951 0.3950 0.0108  -0.0221 0.0106  770  ASP B CA  
3580 C C   . ASP B 114 ? 0.1660 0.3226 0.4206 0.0217  -0.0213 0.0134  770  ASP B C   
3581 O O   . ASP B 114 ? 0.1323 0.3050 0.3919 0.0208  -0.0221 0.0195  770  ASP B O   
3582 C CB  . ASP B 114 ? 0.1754 0.3050 0.4224 0.0079  -0.0242 0.0095  770  ASP B CB  
3583 C CG  . ASP B 114 ? 0.2279 0.3529 0.4693 -0.0015 -0.0244 0.0103  770  ASP B CG  
3584 O OD1 . ASP B 114 ? 0.2079 0.3417 0.4454 -0.0081 -0.0240 0.0125  770  ASP B OD1 
3585 O OD2 . ASP B 114 ? 0.1198 0.2323 0.3597 -0.0023 -0.0249 0.0091  770  ASP B OD2 
3586 N N   . ILE B 115 ? 0.1378 0.2827 0.3900 0.0324  -0.0199 0.0091  771  ILE B N   
3587 C CA  . ILE B 115 ? 0.1503 0.2968 0.4046 0.0464  -0.0181 0.0113  771  ILE B CA  
3588 C C   . ILE B 115 ? 0.2017 0.3793 0.4619 0.0527  -0.0145 0.0162  771  ILE B C   
3589 O O   . ILE B 115 ? 0.2040 0.3964 0.4708 0.0600  -0.0141 0.0231  771  ILE B O   
3590 C CB  . ILE B 115 ? 0.2174 0.3371 0.4621 0.0551  -0.0174 0.0044  771  ILE B CB  
3591 C CG1 . ILE B 115 ? 0.2340 0.3281 0.4758 0.0486  -0.0219 0.0033  771  ILE B CG1 
3592 C CG2 . ILE B 115 ? 0.2356 0.3559 0.4782 0.0732  -0.0133 0.0057  771  ILE B CG2 
3593 C CD1 . ILE B 115 ? 0.3059 0.3707 0.5352 0.0499  -0.0233 -0.0044 771  ILE B CD1 
3594 N N   . GLU B 116 ? 0.1405 0.3303 0.3987 0.0496  -0.0120 0.0139  772  GLU B N   
3595 C CA  . GLU B 116 ? 0.1194 0.3427 0.3835 0.0527  -0.0084 0.0192  772  GLU B CA  
3596 C C   . GLU B 116 ? 0.1576 0.4056 0.4298 0.0407  -0.0117 0.0279  772  GLU B C   
3597 O O   . GLU B 116 ? 0.1465 0.4247 0.4273 0.0462  -0.0103 0.0357  772  GLU B O   
3598 C CB  . GLU B 116 ? 0.1426 0.3693 0.4006 0.0482  -0.0058 0.0148  772  GLU B CB  
3599 C CG  . GLU B 116 ? 0.2650 0.5265 0.5278 0.0537  -0.0006 0.0198  772  GLU B CG  
3600 C CD  . GLU B 116 ? 0.3902 0.6838 0.6610 0.0392  -0.0026 0.0290  772  GLU B CD  
3601 O OE1 . GLU B 116 ? 0.3370 0.6206 0.6035 0.0216  -0.0069 0.0285  772  GLU B OE1 
3602 O OE2 . GLU B 116 ? 0.3363 0.6651 0.6166 0.0455  0.0003  0.0370  772  GLU B OE2 
3603 N N   . VAL B 117 ? 0.1181 0.3536 0.3864 0.0250  -0.0160 0.0270  773  VAL B N   
3604 C CA  . VAL B 117 ? 0.1098 0.3622 0.3806 0.0119  -0.0198 0.0337  773  VAL B CA  
3605 C C   . VAL B 117 ? 0.1572 0.4169 0.4351 0.0193  -0.0217 0.0397  773  VAL B C   
3606 O O   . VAL B 117 ? 0.1655 0.4552 0.4501 0.0163  -0.0234 0.0481  773  VAL B O   
3607 C CB  . VAL B 117 ? 0.1703 0.4012 0.4305 -0.0040 -0.0227 0.0302  773  VAL B CB  
3608 C CG1 . VAL B 117 ? 0.1787 0.4186 0.4370 -0.0165 -0.0270 0.0357  773  VAL B CG1 
3609 C CG2 . VAL B 117 ? 0.1618 0.3905 0.4145 -0.0124 -0.0211 0.0272  773  VAL B CG2 
3610 N N   . ALA B 118 ? 0.1073 0.3411 0.3834 0.0280  -0.0220 0.0364  774  ALA B N   
3611 C CA  . ALA B 118 ? 0.1113 0.3452 0.3921 0.0364  -0.0236 0.0419  774  ALA B CA  
3612 C C   . ALA B 118 ? 0.1829 0.4421 0.4721 0.0524  -0.0207 0.0487  774  ALA B C   
3613 O O   . ALA B 118 ? 0.1705 0.4526 0.4668 0.0537  -0.0229 0.0580  774  ALA B O   
3614 C CB  . ALA B 118 ? 0.1365 0.3356 0.4119 0.0426  -0.0236 0.0366  774  ALA B CB  
3615 N N   . TYR B 119 ? 0.1631 0.4189 0.4506 0.0657  -0.0155 0.0445  775  TYR B N   
3616 C CA  . TYR B 119 ? 0.1563 0.4343 0.4500 0.0851  -0.0108 0.0505  775  TYR B CA  
3617 C C   . TYR B 119 ? 0.1651 0.4920 0.4699 0.0800  -0.0103 0.0596  775  TYR B C   
3618 O O   . TYR B 119 ? 0.1233 0.4796 0.4378 0.0911  -0.0094 0.0698  775  TYR B O   
3619 C CB  . TYR B 119 ? 0.1864 0.4425 0.4708 0.1009  -0.0047 0.0422  775  TYR B CB  
3620 C CG  . TYR B 119 ? 0.2063 0.4718 0.4924 0.1262  0.0009  0.0475  775  TYR B CG  
3621 C CD1 . TYR B 119 ? 0.2377 0.4810 0.5202 0.1385  0.0001  0.0504  775  TYR B CD1 
3622 C CD2 . TYR B 119 ? 0.2042 0.5017 0.4948 0.1387  0.0076  0.0510  775  TYR B CD2 
3623 C CE1 . TYR B 119 ? 0.2306 0.4801 0.5127 0.1641  0.0059  0.0562  775  TYR B CE1 
3624 C CE2 . TYR B 119 ? 0.2141 0.5210 0.5054 0.1651  0.0140  0.0566  775  TYR B CE2 
3625 C CZ  . TYR B 119 ? 0.3309 0.6122 0.6174 0.1785  0.0131  0.0592  775  TYR B CZ  
3626 O OH  . TYR B 119 ? 0.3481 0.6343 0.6327 0.2070  0.0200  0.0651  775  TYR B OH  
3627 N N   . SER B 120 ? 0.1333 0.4687 0.4362 0.0620  -0.0116 0.0569  776  SER B N   
3628 C CA  . SER B 120 ? 0.1041 0.4830 0.4149 0.0504  -0.0125 0.0653  776  SER B CA  
3629 C C   . SER B 120 ? 0.1391 0.5392 0.4557 0.0384  -0.0193 0.0748  776  SER B C   
3630 O O   . SER B 120 ? 0.1080 0.5522 0.4360 0.0392  -0.0199 0.0861  776  SER B O   
3631 C CB  . SER B 120 ? 0.1826 0.5519 0.4848 0.0318  -0.0132 0.0591  776  SER B CB  
3632 O OG  . SER B 120 ? 0.3653 0.7700 0.6715 0.0153  -0.0152 0.0669  776  SER B OG  
3633 N N   . LEU B 121 ? 0.1232 0.4941 0.4318 0.0280  -0.0242 0.0707  777  LEU B N   
3634 C CA  . LEU B 121 ? 0.1404 0.5216 0.4494 0.0161  -0.0308 0.0773  777  LEU B CA  
3635 C C   . LEU B 121 ? 0.2069 0.6100 0.5273 0.0335  -0.0309 0.0876  777  LEU B C   
3636 O O   . LEU B 121 ? 0.1911 0.6348 0.5202 0.0289  -0.0345 0.0990  777  LEU B O   
3637 C CB  . LEU B 121 ? 0.1762 0.5150 0.4725 0.0073  -0.0334 0.0689  777  LEU B CB  
3638 C CG  . LEU B 121 ? 0.2551 0.5919 0.5414 -0.0146 -0.0395 0.0698  777  LEU B CG  
3639 C CD1 . LEU B 121 ? 0.2526 0.6093 0.5345 -0.0339 -0.0416 0.0716  777  LEU B CD1 
3640 C CD2 . LEU B 121 ? 0.2987 0.5933 0.5723 -0.0187 -0.0392 0.0605  777  LEU B CD2 
3641 N N   . LEU B 122 ? 0.1867 0.5639 0.5062 0.0539  -0.0269 0.0842  778  LEU B N   
3642 C CA  . LEU B 122 ? 0.1933 0.5805 0.5201 0.0746  -0.0256 0.0930  778  LEU B CA  
3643 C C   . LEU B 122 ? 0.2410 0.6748 0.5811 0.0901  -0.0213 0.1033  778  LEU B C   
3644 O O   . LEU B 122 ? 0.2425 0.7084 0.5925 0.0976  -0.0233 0.1161  778  LEU B O   
3645 C CB  . LEU B 122 ? 0.2138 0.5540 0.5316 0.0902  -0.0218 0.0847  778  LEU B CB  
3646 C CG  . LEU B 122 ? 0.2860 0.6128 0.6035 0.1058  -0.0224 0.0911  778  LEU B CG  
3647 C CD1 . LEU B 122 ? 0.2887 0.6148 0.6054 0.0909  -0.0294 0.0957  778  LEU B CD1 
3648 C CD2 . LEU B 122 ? 0.3410 0.6188 0.6465 0.1160  -0.0192 0.0818  778  LEU B CD2 
3649 N N   . ARG B 123 ? 0.2115 0.6519 0.5517 0.0948  -0.0153 0.0987  779  ARG B N   
3650 C CA  . ARG B 123 ? 0.2147 0.7006 0.5670 0.1110  -0.0095 0.1082  779  ARG B CA  
3651 C C   . ARG B 123 ? 0.2319 0.7722 0.5956 0.0909  -0.0135 0.1182  779  ARG B C   
3652 O O   . ARG B 123 ? 0.2162 0.8061 0.5937 0.1019  -0.0103 0.1303  779  ARG B O   
3653 C CB  . ARG B 123 ? 0.2588 0.7253 0.6038 0.1285  -0.0001 0.0989  779  ARG B CB  
3654 C CG  . ARG B 123 ? 0.4220 0.8464 0.7567 0.1545  0.0048  0.0936  779  ARG B CG  
3655 C CD  . ARG B 123 ? 0.6244 1.0695 0.9674 0.1770  0.0064  0.1070  779  ARG B CD  
3656 N NE  . ARG B 123 ? 0.8114 1.2085 1.1408 0.1990  0.0100  0.1023  779  ARG B NE  
3657 C CZ  . ARG B 123 ? 0.9625 1.3205 1.2837 0.1928  0.0044  0.0994  779  ARG B CZ  
3658 N NH1 . ARG B 123 ? 0.8366 1.1515 1.1440 0.2119  0.0077  0.0963  779  ARG B NH1 
3659 N NH2 . ARG B 123 ? 0.7340 1.0946 1.0590 0.1671  -0.0041 0.0998  779  ARG B NH2 
3660 N N   . GLY B 124 ? 0.1902 0.7203 0.5467 0.0620  -0.0204 0.1138  780  GLY B N   
3661 C CA  . GLY B 124 ? 0.1611 0.7331 0.5229 0.0380  -0.0258 0.1220  780  GLY B CA  
3662 C C   . GLY B 124 ? 0.2123 0.8037 0.5771 0.0251  -0.0349 0.1315  780  GLY B C   
3663 O O   . GLY B 124 ? 0.1948 0.7734 0.5603 0.0383  -0.0361 0.1335  780  GLY B O   
3664 N N   . GLY B 125 ? 0.1819 0.8019 0.5461 -0.0022 -0.0416 0.1371  781  GLY B N   
3665 C CA  . GLY B 125 ? 0.1719 0.8125 0.5350 -0.0212 -0.0518 0.1456  781  GLY B CA  
3666 C C   . GLY B 125 ? 0.1780 0.8790 0.5608 -0.0102 -0.0539 0.1640  781  GLY B C   
3667 O O   . GLY B 125 ? 0.1190 0.8607 0.5182 0.0063  -0.0479 0.1728  781  GLY B O   
3668 N N   . SER B 126 ? 0.1615 0.8696 0.5422 -0.0186 -0.0624 0.1703  782  SER B N   
3669 C CA  . SER B 126 ? 0.1395 0.9032 0.5374 -0.0091 -0.0664 0.1888  782  SER B CA  
3670 C C   . SER B 126 ? 0.1985 0.9415 0.5986 0.0186  -0.0638 0.1905  782  SER B C   
3671 O O   . SER B 126 ? 0.2067 0.8967 0.5914 0.0167  -0.0647 0.1793  782  SER B O   
3672 C CB  . SER B 126 ? 0.1753 0.9685 0.5680 -0.0418 -0.0793 0.1970  782  SER B CB  
3673 O OG  . SER B 126 ? 0.2844 1.0909 0.6711 -0.0708 -0.0826 0.1955  782  SER B OG  
3674 N N   . ASP B 127 ? 0.1710 0.9573 0.5898 0.0446  -0.0603 0.2056  783  ASP B N   
3675 C CA  . ASP B 127 ? 0.1915 0.9634 0.6134 0.0746  -0.0570 0.2105  783  ASP B CA  
3676 C C   . ASP B 127 ? 0.2155 1.0348 0.6471 0.0727  -0.0659 0.2292  783  ASP B C   
3677 O O   . ASP B 127 ? 0.1851 1.0714 0.6333 0.0690  -0.0692 0.2452  783  ASP B O   
3678 C CB  . ASP B 127 ? 0.2231 0.9994 0.6550 0.1114  -0.0444 0.2126  783  ASP B CB  
3679 C CG  . ASP B 127 ? 0.4273 1.1573 0.8520 0.1411  -0.0389 0.2097  783  ASP B CG  
3680 O OD1 . ASP B 127 ? 0.4465 1.1137 0.8538 0.1344  -0.0390 0.1943  783  ASP B OD1 
3681 O OD2 . ASP B 127 ? 0.4888 1.2451 0.9244 0.1707  -0.0345 0.2235  783  ASP B OD2 
3682 N N   . ASP B 128 ? 0.1857 0.9722 0.6070 0.0747  -0.0699 0.2279  784  ASP B N   
3683 C CA  . ASP B 128 ? 0.1734 0.9961 0.6001 0.0729  -0.0788 0.2444  784  ASP B CA  
3684 C C   . ASP B 128 ? 0.2459 1.0341 0.6690 0.1014  -0.0751 0.2470  784  ASP B C   
3685 O O   . ASP B 128 ? 0.2618 0.9927 0.6677 0.0957  -0.0753 0.2346  784  ASP B O   
3686 C CB  . ASP B 128 ? 0.1998 1.0164 0.6106 0.0332  -0.0907 0.2392  784  ASP B CB  
3687 C CG  . ASP B 128 ? 0.1860 1.0435 0.5987 0.0219  -0.1024 0.2550  784  ASP B CG  
3688 O OD1 . ASP B 128 ? 0.1547 1.0501 0.5835 0.0462  -0.1020 0.2727  784  ASP B OD1 
3689 O OD2 . ASP B 128 ? 0.2551 1.1055 0.6513 -0.0107 -0.1119 0.2500  784  ASP B OD2 
3690 N N   . SER B 129 ? 0.1984 1.0222 0.6372 0.1326  -0.0712 0.2641  785  SER B N   
3691 C CA  . SER B 129 ? 0.2135 1.0076 0.6488 0.1628  -0.0672 0.2697  785  SER B CA  
3692 C C   . SER B 129 ? 0.2593 1.0417 0.6844 0.1485  -0.0770 0.2740  785  SER B C   
3693 O O   . SER B 129 ? 0.3019 1.0294 0.7136 0.1585  -0.0744 0.2680  785  SER B O   
3694 C CB  . SER B 129 ? 0.2745 1.1189 0.7286 0.1976  -0.0621 0.2901  785  SER B CB  
3695 O OG  . SER B 129 ? 0.4966 1.3522 0.9589 0.2145  -0.0514 0.2866  785  SER B OG  
3696 N N   . SER B 130 ? 0.1589 0.9919 0.5886 0.1235  -0.0886 0.2842  786  SER B N   
3697 C CA  . SER B 130 ? 0.1523 0.9839 0.5715 0.1069  -0.0992 0.2897  786  SER B CA  
3698 C C   . SER B 130 ? 0.2241 0.9893 0.6193 0.0861  -0.1002 0.2700  786  SER B C   
3699 O O   . SER B 130 ? 0.2488 0.9989 0.6327 0.0805  -0.1056 0.2732  786  SER B O   
3700 C CB  . SER B 130 ? 0.1724 1.0717 0.5989 0.0805  -0.1116 0.3024  786  SER B CB  
3701 O OG  . SER B 130 ? 0.2383 1.1285 0.6529 0.0443  -0.1161 0.2878  786  SER B OG  
3702 N N   . LYS B 131 ? 0.1679 0.8964 0.5554 0.0755  -0.0947 0.2508  787  LYS B N   
3703 C CA  . LYS B 131 ? 0.1833 0.8524 0.5495 0.0575  -0.0944 0.2323  787  LYS B CA  
3704 C C   . LYS B 131 ? 0.2205 0.8301 0.5811 0.0789  -0.0845 0.2220  787  LYS B C   
3705 O O   . LYS B 131 ? 0.2171 0.8213 0.5864 0.1004  -0.0763 0.2205  787  LYS B O   
3706 C CB  . LYS B 131 ? 0.2266 0.8932 0.5852 0.0287  -0.0962 0.2186  787  LYS B CB  
3707 C CG  . LYS B 131 ? 0.4164 1.1281 0.7719 -0.0004 -0.1077 0.2259  787  LYS B CG  
3708 C CD  . LYS B 131 ? 0.6115 1.3032 0.9513 -0.0305 -0.1094 0.2102  787  LYS B CD  
3709 C CE  . LYS B 131 ? 0.8540 1.5761 1.1822 -0.0629 -0.1218 0.2152  787  LYS B CE  
3710 N NZ  . LYS B 131 ? 1.0366 1.7343 1.3460 -0.0917 -0.1232 0.2003  787  LYS B NZ  
3711 N N   . ASP B 132 ? 0.1686 0.7339 0.5131 0.0715  -0.0856 0.2151  788  ASP B N   
3712 C CA  . ASP B 132 ? 0.1641 0.6712 0.5003 0.0840  -0.0781 0.2048  788  ASP B CA  
3713 C C   . ASP B 132 ? 0.2205 0.7039 0.5549 0.0782  -0.0721 0.1875  788  ASP B C   
3714 O O   . ASP B 132 ? 0.2103 0.6960 0.5382 0.0544  -0.0750 0.1785  788  ASP B O   
3715 C CB  . ASP B 132 ? 0.1893 0.6643 0.5088 0.0689  -0.0815 0.2006  788  ASP B CB  
3716 C CG  . ASP B 132 ? 0.2114 0.6310 0.5222 0.0789  -0.0756 0.1937  788  ASP B CG  
3717 O OD1 . ASP B 132 ? 0.1973 0.5887 0.5085 0.0855  -0.0690 0.1825  788  ASP B OD1 
3718 O OD2 . ASP B 132 ? 0.2331 0.6384 0.5357 0.0782  -0.0779 0.1997  788  ASP B OD2 
3719 N N   . PRO B 133 ? 0.1877 0.6461 0.5253 0.0994  -0.0638 0.1828  789  PRO B N   
3720 C CA  . PRO B 133 ? 0.1916 0.6289 0.5267 0.0940  -0.0585 0.1671  789  PRO B CA  
3721 C C   . PRO B 133 ? 0.2453 0.6442 0.5663 0.0727  -0.0593 0.1522  789  PRO B C   
3722 O O   . PRO B 133 ? 0.2484 0.6418 0.5673 0.0617  -0.0574 0.1412  789  PRO B O   
3723 C CB  . PRO B 133 ? 0.2204 0.6318 0.5568 0.1215  -0.0504 0.1657  789  PRO B CB  
3724 C CG  . PRO B 133 ? 0.2775 0.7147 0.6219 0.1436  -0.0509 0.1835  789  PRO B CG  
3725 C CD  . PRO B 133 ? 0.2193 0.6659 0.5602 0.1294  -0.0590 0.1917  789  PRO B CD  
3726 N N   . ILE B 134 ? 0.1980 0.5733 0.5094 0.0675  -0.0618 0.1531  790  ILE B N   
3727 C CA  . ILE B 134 ? 0.1927 0.5365 0.4907 0.0489  -0.0622 0.1414  790  ILE B CA  
3728 C C   . ILE B 134 ? 0.2213 0.5879 0.5134 0.0253  -0.0672 0.1385  790  ILE B C   
3729 O O   . ILE B 134 ? 0.2179 0.5670 0.5021 0.0123  -0.0654 0.1263  790  ILE B O   
3730 C CB  . ILE B 134 ? 0.2265 0.5453 0.5164 0.0507  -0.0631 0.1457  790  ILE B CB  
3731 C CG1 . ILE B 134 ? 0.2351 0.5226 0.5266 0.0707  -0.0581 0.1467  790  ILE B CG1 
3732 C CG2 . ILE B 134 ? 0.2320 0.5270 0.5085 0.0318  -0.0630 0.1355  790  ILE B CG2 
3733 C CD1 . ILE B 134 ? 0.3430 0.6140 0.6293 0.0774  -0.0596 0.1569  790  ILE B CD1 
3734 N N   . ASP B 135 ? 0.1536 0.5588 0.4483 0.0200  -0.0738 0.1503  791  ASP B N   
3735 C CA  . ASP B 135 ? 0.1372 0.5652 0.4239 -0.0037 -0.0800 0.1491  791  ASP B CA  
3736 C C   . ASP B 135 ? 0.1629 0.6064 0.4557 -0.0097 -0.0785 0.1438  791  ASP B C   
3737 O O   . ASP B 135 ? 0.1548 0.5856 0.4349 -0.0289 -0.0793 0.1338  791  ASP B O   
3738 C CB  . ASP B 135 ? 0.1492 0.6188 0.4387 -0.0073 -0.0882 0.1646  791  ASP B CB  
3739 C CG  . ASP B 135 ? 0.2411 0.6972 0.5167 -0.0130 -0.0918 0.1678  791  ASP B CG  
3740 O OD1 . ASP B 135 ? 0.1970 0.6147 0.4578 -0.0203 -0.0887 0.1567  791  ASP B OD1 
3741 O OD2 . ASP B 135 ? 0.3743 0.8614 0.6538 -0.0101 -0.0978 0.1822  791  ASP B OD2 
3742 N N   . VAL B 136 ? 0.1192 0.5870 0.4298 0.0084  -0.0753 0.1507  792  VAL B N   
3743 C CA  . VAL B 136 ? 0.0991 0.5866 0.4180 0.0065  -0.0728 0.1480  792  VAL B CA  
3744 C C   . VAL B 136 ? 0.1373 0.5812 0.4468 0.0026  -0.0669 0.1314  792  VAL B C   
3745 O O   . VAL B 136 ? 0.1326 0.5750 0.4339 -0.0164 -0.0683 0.1244  792  VAL B O   
3746 C CB  . VAL B 136 ? 0.1387 0.6547 0.4770 0.0330  -0.0682 0.1584  792  VAL B CB  
3747 C CG1 . VAL B 136 ? 0.1269 0.6597 0.4730 0.0335  -0.0636 0.1547  792  VAL B CG1 
3748 C CG2 . VAL B 136 ? 0.1139 0.6793 0.4631 0.0379  -0.0741 0.1769  792  VAL B CG2 
3749 N N   . ASN B 137 ? 0.1020 0.5094 0.4108 0.0190  -0.0611 0.1256  793  ASN B N   
3750 C CA  . ASN B 137 ? 0.1117 0.4810 0.4131 0.0168  -0.0559 0.1113  793  ASN B CA  
3751 C C   . ASN B 137 ? 0.1893 0.5329 0.4739 -0.0034 -0.0581 0.1023  793  ASN B C   
3752 O O   . ASN B 137 ? 0.1862 0.5107 0.4645 -0.0103 -0.0552 0.0921  793  ASN B O   
3753 C CB  . ASN B 137 ? 0.1498 0.4887 0.4535 0.0375  -0.0504 0.1085  793  ASN B CB  
3754 C CG  . ASN B 137 ? 0.3242 0.6795 0.6395 0.0590  -0.0460 0.1136  793  ASN B CG  
3755 O OD1 . ASN B 137 ? 0.0755 0.4641 0.3989 0.0591  -0.0453 0.1168  793  ASN B OD1 
3756 N ND2 . ASN B 137 ? 0.2610 0.5921 0.5756 0.0780  -0.0426 0.1148  793  ASN B ND2 
3757 N N   . TYR B 138 ? 0.1635 0.5072 0.4396 -0.0119 -0.0627 0.1065  794  TYR B N   
3758 C CA  . TYR B 138 ? 0.1838 0.5034 0.4411 -0.0292 -0.0637 0.0981  794  TYR B CA  
3759 C C   . TYR B 138 ? 0.2337 0.5646 0.4813 -0.0492 -0.0668 0.0944  794  TYR B C   
3760 O O   . TYR B 138 ? 0.2411 0.5454 0.4755 -0.0581 -0.0642 0.0840  794  TYR B O   
3761 C CB  . TYR B 138 ? 0.2075 0.5262 0.4561 -0.0329 -0.0674 0.1040  794  TYR B CB  
3762 C CG  . TYR B 138 ? 0.2604 0.5579 0.4865 -0.0500 -0.0682 0.0962  794  TYR B CG  
3763 C CD1 . TYR B 138 ? 0.3093 0.5720 0.5271 -0.0474 -0.0626 0.0879  794  TYR B CD1 
3764 C CD2 . TYR B 138 ? 0.2821 0.5948 0.4940 -0.0684 -0.0745 0.0979  794  TYR B CD2 
3765 C CE1 . TYR B 138 ? 0.3484 0.5914 0.5441 -0.0598 -0.0618 0.0811  794  TYR B CE1 
3766 C CE2 . TYR B 138 ? 0.3140 0.6020 0.5005 -0.0827 -0.0744 0.0899  794  TYR B CE2 
3767 C CZ  . TYR B 138 ? 0.4216 0.6745 0.6001 -0.0768 -0.0674 0.0814  794  TYR B CZ  
3768 O OH  . TYR B 138 ? 0.4729 0.7010 0.6252 -0.0876 -0.0658 0.0737  794  TYR B OH  
3769 N N   . GLU B 139 ? 0.1828 0.5536 0.4367 -0.0560 -0.0724 0.1038  795  GLU B N   
3770 C CA  . GLU B 139 ? 0.1834 0.5683 0.4275 -0.0780 -0.0768 0.1024  795  GLU B CA  
3771 C C   . GLU B 139 ? 0.2270 0.6062 0.4753 -0.0777 -0.0721 0.0960  795  GLU B C   
3772 O O   . GLU B 139 ? 0.2354 0.6040 0.4684 -0.0962 -0.0736 0.0903  795  GLU B O   
3773 C CB  . GLU B 139 ? 0.1896 0.6247 0.4416 -0.0864 -0.0849 0.1162  795  GLU B CB  
3774 C CG  . GLU B 139 ? 0.3415 0.7884 0.5899 -0.0868 -0.0906 0.1246  795  GLU B CG  
3775 C CD  . GLU B 139 ? 0.8491 1.2943 1.0734 -0.1123 -0.0987 0.1238  795  GLU B CD  
3776 O OE1 . GLU B 139 ? 0.8276 1.3141 1.0546 -0.1239 -0.1072 0.1350  795  GLU B OE1 
3777 O OE2 . GLU B 139 ? 0.9602 1.3631 1.1618 -0.1199 -0.0963 0.1123  795  GLU B OE2 
3778 N N   . LYS B 140 ? 0.1676 0.5503 0.4338 -0.0564 -0.0662 0.0968  796  LYS B N   
3779 C CA  . LYS B 140 ? 0.1589 0.5355 0.4300 -0.0519 -0.0607 0.0908  796  LYS B CA  
3780 C C   . LYS B 140 ? 0.2367 0.5698 0.4905 -0.0602 -0.0576 0.0777  796  LYS B C   
3781 O O   . LYS B 140 ? 0.2526 0.5819 0.5027 -0.0673 -0.0558 0.0733  796  LYS B O   
3782 C CB  . LYS B 140 ? 0.1581 0.5342 0.4453 -0.0257 -0.0546 0.0919  796  LYS B CB  
3783 C CG  . LYS B 140 ? 0.2082 0.6292 0.5134 -0.0137 -0.0544 0.1037  796  LYS B CG  
3784 C CD  . LYS B 140 ? 0.2318 0.6436 0.5471 0.0136  -0.0477 0.1035  796  LYS B CD  
3785 C CE  . LYS B 140 ? 0.2954 0.7511 0.6269 0.0296  -0.0474 0.1177  796  LYS B CE  
3786 N NZ  . LYS B 140 ? 0.0756 0.5726 0.4173 0.0278  -0.0457 0.1228  796  LYS B NZ  
3787 N N   . LEU B 141 ? 0.1921 0.4943 0.4359 -0.0582 -0.0567 0.0727  797  LEU B N   
3788 C CA  . LEU B 141 ? 0.1938 0.4565 0.4228 -0.0615 -0.0530 0.0619  797  LEU B CA  
3789 C C   . LEU B 141 ? 0.2904 0.5383 0.4965 -0.0817 -0.0553 0.0572  797  LEU B C   
3790 O O   . LEU B 141 ? 0.3081 0.5263 0.5025 -0.0830 -0.0513 0.0490  797  LEU B O   
3791 C CB  . LEU B 141 ? 0.1889 0.4298 0.4169 -0.0513 -0.0507 0.0603  797  LEU B CB  
3792 C CG  . LEU B 141 ? 0.2094 0.4515 0.4546 -0.0321 -0.0479 0.0630  797  LEU B CG  
3793 C CD1 . LEU B 141 ? 0.2298 0.4519 0.4720 -0.0267 -0.0468 0.0630  797  LEU B CD1 
3794 C CD2 . LEU B 141 ? 0.1877 0.4203 0.4389 -0.0246 -0.0435 0.0569  797  LEU B CD2 
3795 N N   . LYS B 142 ? 0.2570 0.5234 0.4545 -0.0972 -0.0618 0.0627  798  LYS B N   
3796 C CA  . LYS B 142 ? 0.2669 0.5160 0.4371 -0.1191 -0.0652 0.0584  798  LYS B CA  
3797 C C   . LYS B 142 ? 0.3395 0.5440 0.4889 -0.1164 -0.0604 0.0487  798  LYS B C   
3798 O O   . LYS B 142 ? 0.3482 0.5235 0.4772 -0.1247 -0.0581 0.0414  798  LYS B O   
3799 C CB  . LYS B 142 ? 0.2956 0.5502 0.4616 -0.1329 -0.0663 0.0577  798  LYS B CB  
3800 C CG  . LYS B 142 ? 0.2465 0.5498 0.4349 -0.1338 -0.0696 0.0681  798  LYS B CG  
3801 C CD  . LYS B 142 ? 0.4129 0.7523 0.6001 -0.1502 -0.0787 0.0781  798  LYS B CD  
3802 C CE  . LYS B 142 ? 0.5187 0.9115 0.7307 -0.1482 -0.0808 0.0899  798  LYS B CE  
3803 N NZ  . LYS B 142 ? 0.5300 0.9632 0.7561 -0.1439 -0.0862 0.1019  798  LYS B NZ  
3804 N N   . THR B 143 ? 0.2949 0.4959 0.4507 -0.1033 -0.0582 0.0499  799  THR B N   
3805 C CA  . THR B 143 ? 0.3177 0.4861 0.4597 -0.0970 -0.0529 0.0436  799  THR B CA  
3806 C C   . THR B 143 ? 0.3714 0.5460 0.5068 -0.0984 -0.0558 0.0481  799  THR B C   
3807 O O   . THR B 143 ? 0.3569 0.5585 0.5103 -0.0925 -0.0591 0.0567  799  THR B O   
3808 C CB  . THR B 143 ? 0.3488 0.5088 0.5092 -0.0782 -0.0464 0.0416  799  THR B CB  
3809 O OG1 . THR B 143 ? 0.4209 0.5760 0.5848 -0.0781 -0.0443 0.0377  799  THR B OG1 
3810 C CG2 . THR B 143 ? 0.2445 0.3774 0.3942 -0.0710 -0.0405 0.0370  799  THR B CG2 
3811 N N   . ASP B 144 ? 0.3309 0.4796 0.4388 -0.1052 -0.0540 0.0426  800  ASP B N   
3812 C CA  . ASP B 144 ? 0.3323 0.4831 0.4308 -0.1056 -0.0554 0.0459  800  ASP B CA  
3813 C C   . ASP B 144 ? 0.3540 0.4943 0.4644 -0.0874 -0.0479 0.0457  800  ASP B C   
3814 O O   . ASP B 144 ? 0.3587 0.4750 0.4625 -0.0814 -0.0411 0.0390  800  ASP B O   
3815 C CB  . ASP B 144 ? 0.3904 0.5152 0.4506 -0.1203 -0.0560 0.0391  800  ASP B CB  
3816 C CG  . ASP B 144 ? 0.6402 0.7640 0.6864 -0.1201 -0.0562 0.0414  800  ASP B CG  
3817 O OD1 . ASP B 144 ? 0.6457 0.7992 0.7032 -0.1229 -0.0628 0.0505  800  ASP B OD1 
3818 O OD2 . ASP B 144 ? 0.8110 0.9053 0.8343 -0.1165 -0.0495 0.0346  800  ASP B OD2 
3819 N N   . ILE B 145 ? 0.2597 0.4197 0.3893 -0.0786 -0.0494 0.0542  801  ILE B N   
3820 C CA  . ILE B 145 ? 0.2292 0.3817 0.3706 -0.0644 -0.0436 0.0558  801  ILE B CA  
3821 C C   . ILE B 145 ? 0.2584 0.4142 0.3903 -0.0650 -0.0441 0.0611  801  ILE B C   
3822 O O   . ILE B 145 ? 0.2337 0.4106 0.3713 -0.0673 -0.0502 0.0694  801  ILE B O   
3823 C CB  . ILE B 145 ? 0.2447 0.4108 0.4153 -0.0527 -0.0442 0.0609  801  ILE B CB  
3824 C CG1 . ILE B 145 ? 0.2413 0.4065 0.4198 -0.0526 -0.0438 0.0557  801  ILE B CG1 
3825 C CG2 . ILE B 145 ? 0.2218 0.3778 0.4019 -0.0417 -0.0391 0.0629  801  ILE B CG2 
3826 C CD1 . ILE B 145 ? 0.1894 0.3710 0.3915 -0.0428 -0.0455 0.0606  801  ILE B CD1 
3827 N N   . LYS B 146 ? 0.2535 0.3902 0.3703 -0.0622 -0.0375 0.0572  802  LYS B N   
3828 C CA  . LYS B 146 ? 0.2582 0.3968 0.3639 -0.0621 -0.0364 0.0620  802  LYS B CA  
3829 C C   . LYS B 146 ? 0.2721 0.4070 0.3902 -0.0501 -0.0294 0.0655  802  LYS B C   
3830 O O   . LYS B 146 ? 0.2677 0.3924 0.3933 -0.0439 -0.0243 0.0611  802  LYS B O   
3831 C CB  . LYS B 146 ? 0.3170 0.4381 0.3873 -0.0714 -0.0346 0.0549  802  LYS B CB  
3832 C CG  . LYS B 146 ? 0.5707 0.6993 0.6272 -0.0875 -0.0437 0.0539  802  LYS B CG  
3833 C CD  . LYS B 146 ? 0.7220 0.8364 0.7412 -0.0989 -0.0445 0.0495  802  LYS B CD  
3834 C CE  . LYS B 146 ? 0.8093 0.9372 0.8180 -0.1176 -0.0555 0.0508  802  LYS B CE  
3835 N NZ  . LYS B 146 ? 0.9361 1.0491 0.9053 -0.1310 -0.0576 0.0464  802  LYS B NZ  
3836 N N   . VAL B 147 ? 0.2115 0.3567 0.3328 -0.0479 -0.0299 0.0745  803  VAL B N   
3837 C CA  . VAL B 147 ? 0.1981 0.3427 0.3306 -0.0395 -0.0242 0.0798  803  VAL B CA  
3838 C C   . VAL B 147 ? 0.2714 0.4052 0.3820 -0.0382 -0.0157 0.0760  803  VAL B C   
3839 O O   . VAL B 147 ? 0.2849 0.4171 0.3726 -0.0435 -0.0160 0.0753  803  VAL B O   
3840 C CB  . VAL B 147 ? 0.2161 0.3752 0.3617 -0.0378 -0.0285 0.0928  803  VAL B CB  
3841 C CG1 . VAL B 147 ? 0.2046 0.3617 0.3642 -0.0318 -0.0236 0.0986  803  VAL B CG1 
3842 C CG2 . VAL B 147 ? 0.2015 0.3712 0.3634 -0.0370 -0.0363 0.0968  803  VAL B CG2 
3843 N N   . VAL B 148 ? 0.2307 0.3579 0.3470 -0.0308 -0.0081 0.0737  804  VAL B N   
3844 C CA  . VAL B 148 ? 0.2566 0.3764 0.3539 -0.0258 0.0017  0.0713  804  VAL B CA  
3845 C C   . VAL B 148 ? 0.3711 0.5053 0.4726 -0.0240 0.0045  0.0825  804  VAL B C   
3846 O O   . VAL B 148 ? 0.3633 0.5090 0.4885 -0.0229 0.0026  0.0912  804  VAL B O   
3847 C CB  . VAL B 148 ? 0.2932 0.4042 0.3947 -0.0173 0.0090  0.0658  804  VAL B CB  
3848 C CG1 . VAL B 148 ? 0.2956 0.4050 0.3825 -0.0082 0.0205  0.0665  804  VAL B CG1 
3849 C CG2 . VAL B 148 ? 0.2918 0.3846 0.3813 -0.0198 0.0072  0.0549  804  VAL B CG2 
3850 N N   . ASP B 149 ? 0.3719 0.5037 0.4479 -0.0245 0.0089  0.0822  805  ASP B N   
3851 C CA  . ASP B 149 ? 0.3891 0.5350 0.4648 -0.0231 0.0125  0.0929  805  ASP B CA  
3852 C C   . ASP B 149 ? 0.4568 0.6116 0.5477 -0.0145 0.0215  0.0979  805  ASP B C   
3853 O O   . ASP B 149 ? 0.4513 0.5984 0.5334 -0.0066 0.0297  0.0911  805  ASP B O   
3854 C CB  . ASP B 149 ? 0.4360 0.5752 0.4767 -0.0247 0.0164  0.0896  805  ASP B CB  
3855 C CG  . ASP B 149 ? 0.5974 0.7524 0.6348 -0.0238 0.0203  0.1010  805  ASP B CG  
3856 O OD1 . ASP B 149 ? 0.6063 0.7768 0.6666 -0.0266 0.0154  0.1131  805  ASP B OD1 
3857 O OD2 . ASP B 149 ? 0.6806 0.8305 0.6906 -0.0200 0.0287  0.0980  805  ASP B OD2 
3858 N N   . ARG B 150 ? 0.4215 0.5922 0.5354 -0.0166 0.0193  0.1102  806  ARG B N   
3859 C CA  . ARG B 150 ? 0.4224 0.6066 0.5537 -0.0122 0.0258  0.1173  806  ARG B CA  
3860 C C   . ARG B 150 ? 0.5018 0.6938 0.6173 -0.0034 0.0388  0.1180  806  ARG B C   
3861 O O   . ARG B 150 ? 0.4973 0.6973 0.6226 0.0037  0.0455  0.1185  806  ARG B O   
3862 C CB  . ARG B 150 ? 0.4269 0.6236 0.5782 -0.0191 0.0207  0.1315  806  ARG B CB  
3863 C CG  . ARG B 150 ? 0.6499 0.8398 0.8233 -0.0231 0.0120  0.1313  806  ARG B CG  
3864 C CD  . ARG B 150 ? 0.8439 1.0307 1.0232 -0.0292 0.0031  0.1396  806  ARG B CD  
3865 N NE  . ARG B 150 ? 0.9716 1.1493 1.1697 -0.0315 -0.0038 0.1396  806  ARG B NE  
3866 C CZ  . ARG B 150 ? 1.1421 1.3210 1.3550 -0.0362 -0.0050 0.1479  806  ARG B CZ  
3867 N NH1 . ARG B 150 ? 0.9500 1.1158 1.1748 -0.0380 -0.0113 0.1461  806  ARG B NH1 
3868 N NH2 . ARG B 150 ? 0.9430 1.1360 1.1572 -0.0398 0.0002  0.1582  806  ARG B NH2 
3869 N N   . ASP B 151 ? 0.4774 0.6679 0.5676 -0.0028 0.0426  0.1181  807  ASP B N   
3870 C CA  . ASP B 151 ? 0.4814 0.6792 0.5538 0.0074  0.0562  0.1192  807  ASP B CA  
3871 C C   . ASP B 151 ? 0.5438 0.7185 0.5865 0.0172  0.0634  0.1043  807  ASP B C   
3872 O O   . ASP B 151 ? 0.5480 0.7243 0.5707 0.0285  0.0759  0.1037  807  ASP B O   
3873 C CB  . ASP B 151 ? 0.5118 0.7209 0.5708 0.0035  0.0578  0.1284  807  ASP B CB  
3874 C CG  . ASP B 151 ? 0.6364 0.8667 0.7227 -0.0050 0.0527  0.1449  807  ASP B CG  
3875 O OD1 . ASP B 151 ? 0.6422 0.8927 0.7463 -0.0024 0.0589  0.1543  807  ASP B OD1 
3876 O OD2 . ASP B 151 ? 0.6628 0.8891 0.7520 -0.0144 0.0423  0.1490  807  ASP B OD2 
3877 N N   . SER B 152 ? 0.5007 0.6532 0.5396 0.0138  0.0564  0.0928  808  SER B N   
3878 C CA  . SER B 152 ? 0.5135 0.6382 0.5223 0.0210  0.0621  0.0788  808  SER B CA  
3879 C C   . SER B 152 ? 0.5630 0.6893 0.5784 0.0365  0.0727  0.0778  808  SER B C   
3880 O O   . SER B 152 ? 0.5418 0.6927 0.5892 0.0386  0.0730  0.0873  808  SER B O   
3881 C CB  . SER B 152 ? 0.5716 0.6748 0.5752 0.0101  0.0507  0.0689  808  SER B CB  
3882 O OG  . SER B 152 ? 0.6999 0.8095 0.7349 0.0081  0.0445  0.0702  808  SER B OG  
3883 N N   . GLU B 153 ? 0.5314 0.6312 0.5149 0.0473  0.0812  0.0669  809  GLU B N   
3884 C CA  . GLU B 153 ? 0.5251 0.6238 0.5105 0.0650  0.0920  0.0659  809  GLU B CA  
3885 C C   . GLU B 153 ? 0.5289 0.6273 0.5409 0.0620  0.0846  0.0643  809  GLU B C   
3886 O O   . GLU B 153 ? 0.5065 0.6277 0.5443 0.0702  0.0883  0.0720  809  GLU B O   
3887 C CB  . GLU B 153 ? 0.5708 0.6343 0.5101 0.0783  0.1032  0.0543  809  GLU B CB  
3888 C CG  . GLU B 153 ? 0.7498 0.8277 0.6806 0.1003  0.1206  0.0602  809  GLU B CG  
3889 C CD  . GLU B 153 ? 1.0323 1.1314 0.9893 0.1162  0.1276  0.0672  809  GLU B CD  
3890 O OE1 . GLU B 153 ? 1.0345 1.1097 0.9700 0.1332  0.1367  0.0604  809  GLU B OE1 
3891 O OE2 . GLU B 153 ? 0.8909 1.0298 0.8885 0.1113  0.1237  0.0801  809  GLU B OE2 
3892 N N   . GLU B 154 ? 0.4658 0.5416 0.4720 0.0493  0.0737  0.0555  810  GLU B N   
3893 C CA  . GLU B 154 ? 0.4411 0.5152 0.4697 0.0452  0.0660  0.0533  810  GLU B CA  
3894 C C   . GLU B 154 ? 0.4125 0.5194 0.4831 0.0394  0.0596  0.0645  810  GLU B C   
3895 O O   . GLU B 154 ? 0.3722 0.4876 0.4632 0.0438  0.0594  0.0665  810  GLU B O   
3896 C CB  . GLU B 154 ? 0.4734 0.5215 0.4875 0.0315  0.0559  0.0432  810  GLU B CB  
3897 C CG  . GLU B 154 ? 0.6280 0.6825 0.6414 0.0159  0.0461  0.0451  810  GLU B CG  
3898 C CD  . GLU B 154 ? 0.8259 0.8582 0.8190 0.0021  0.0374  0.0361  810  GLU B CD  
3899 O OE1 . GLU B 154 ? 0.6086 0.6157 0.5856 0.0028  0.0383  0.0273  810  GLU B OE1 
3900 O OE2 . GLU B 154 ? 0.7684 0.8099 0.7617 -0.0099 0.0292  0.0389  810  GLU B OE2 
3901 N N   . ALA B 155 ? 0.3289 0.4525 0.4096 0.0301  0.0547  0.0722  811  ALA B N   
3902 C CA  . ALA B 155 ? 0.2916 0.4406 0.4063 0.0231  0.0486  0.0832  811  ALA B CA  
3903 C C   . ALA B 155 ? 0.3032 0.4781 0.4346 0.0318  0.0569  0.0932  811  ALA B C   
3904 O O   . ALA B 155 ? 0.2355 0.4260 0.3943 0.0276  0.0522  0.0994  811  ALA B O   
3905 C CB  . ALA B 155 ? 0.2971 0.4529 0.4117 0.0128  0.0428  0.0894  811  ALA B CB  
3906 N N   . GLU B 156 ? 0.2875 0.4680 0.4012 0.0436  0.0691  0.0953  812  GLU B N   
3907 C CA  . GLU B 156 ? 0.2701 0.4801 0.3971 0.0541  0.0791  0.1061  812  GLU B CA  
3908 C C   . GLU B 156 ? 0.3110 0.5222 0.4480 0.0641  0.0817  0.1036  812  GLU B C   
3909 O O   . GLU B 156 ? 0.3019 0.5412 0.4664 0.0632  0.0808  0.1134  812  GLU B O   
3910 C CB  . GLU B 156 ? 0.2996 0.5120 0.4001 0.0672  0.0929  0.1072  812  GLU B CB  
3911 C CG  . GLU B 156 ? 0.4879 0.7139 0.5861 0.0583  0.0921  0.1156  812  GLU B CG  
3912 C CD  . GLU B 156 ? 0.8165 1.0389 0.8821 0.0694  0.1046  0.1144  812  GLU B CD  
3913 O OE1 . GLU B 156 ? 0.7874 1.0090 0.8381 0.0881  0.1178  0.1120  812  GLU B OE1 
3914 O OE2 . GLU B 156 ? 0.7102 0.9303 0.7639 0.0602  0.1014  0.1162  812  GLU B OE2 
3915 N N   . ILE B 157 ? 0.2649 0.4448 0.3786 0.0721  0.0839  0.0909  813  ILE B N   
3916 C CA  . ILE B 157 ? 0.2613 0.4360 0.3792 0.0827  0.0863  0.0876  813  ILE B CA  
3917 C C   . ILE B 157 ? 0.2932 0.4750 0.4404 0.0698  0.0737  0.0886  813  ILE B C   
3918 O O   . ILE B 157 ? 0.2839 0.4856 0.4512 0.0748  0.0744  0.0945  813  ILE B O   
3919 C CB  . ILE B 157 ? 0.3224 0.4545 0.4030 0.0915  0.0908  0.0734  813  ILE B CB  
3920 C CG1 . ILE B 157 ? 0.3394 0.4657 0.3909 0.1112  0.1068  0.0734  813  ILE B CG1 
3921 C CG2 . ILE B 157 ? 0.3241 0.4428 0.4094 0.0957  0.0882  0.0684  813  ILE B CG2 
3922 C CD1 . ILE B 157 ? 0.4323 0.5121 0.4384 0.1130  0.1098  0.0594  813  ILE B CD1 
3923 N N   . ILE B 158 ? 0.2131 0.3795 0.3612 0.0541  0.0624  0.0832  814  ILE B N   
3924 C CA  . ILE B 158 ? 0.1876 0.3559 0.3586 0.0422  0.0506  0.0827  814  ILE B CA  
3925 C C   . ILE B 158 ? 0.2667 0.4663 0.4670 0.0356  0.0474  0.0952  814  ILE B C   
3926 O O   . ILE B 158 ? 0.2652 0.4737 0.4842 0.0329  0.0427  0.0970  814  ILE B O   
3927 C CB  . ILE B 158 ? 0.2126 0.3604 0.3757 0.0297  0.0411  0.0755  814  ILE B CB  
3928 C CG1 . ILE B 158 ? 0.2133 0.3308 0.3495 0.0326  0.0423  0.0632  814  ILE B CG1 
3929 C CG2 . ILE B 158 ? 0.2344 0.3868 0.4213 0.0187  0.0300  0.0769  814  ILE B CG2 
3930 C CD1 . ILE B 158 ? 0.1559 0.2585 0.2801 0.0209  0.0346  0.0578  814  ILE B CD1 
3931 N N   . ARG B 159 ? 0.2105 0.4258 0.4128 0.0318  0.0497  0.1042  815  ARG B N   
3932 C CA  . ARG B 159 ? 0.1864 0.4297 0.4131 0.0227  0.0466  0.1174  815  ARG B CA  
3933 C C   . ARG B 159 ? 0.2458 0.5188 0.4859 0.0312  0.0536  0.1260  815  ARG B C   
3934 O O   . ARG B 159 ? 0.2374 0.5317 0.5001 0.0214  0.0483  0.1350  815  ARG B O   
3935 C CB  . ARG B 159 ? 0.1746 0.4262 0.3968 0.0170  0.0482  0.1256  815  ARG B CB  
3936 C CG  . ARG B 159 ? 0.3816 0.6148 0.6026 0.0042  0.0377  0.1234  815  ARG B CG  
3937 C CD  . ARG B 159 ? 0.4141 0.6599 0.6356 -0.0029 0.0382  0.1351  815  ARG B CD  
3938 N NE  . ARG B 159 ? 0.3745 0.6267 0.5762 0.0069  0.0492  0.1360  815  ARG B NE  
3939 C CZ  . ARG B 159 ? 0.5526 0.7897 0.7324 0.0074  0.0495  0.1314  815  ARG B CZ  
3940 N NH1 . ARG B 159 ? 0.3539 0.5946 0.5125 0.0169  0.0601  0.1311  815  ARG B NH1 
3941 N NH2 . ARG B 159 ? 0.4834 0.7029 0.6616 -0.0014 0.0393  0.1277  815  ARG B NH2 
3942 N N   . LYS B 160 ? 0.2206 0.4952 0.4455 0.0493  0.0655  0.1239  816  LYS B N   
3943 C CA  . LYS B 160 ? 0.1990 0.5053 0.4362 0.0614  0.0737  0.1331  816  LYS B CA  
3944 C C   . LYS B 160 ? 0.2202 0.5237 0.4689 0.0625  0.0680  0.1292  816  LYS B C   
3945 O O   . LYS B 160 ? 0.1957 0.5310 0.4670 0.0605  0.0665  0.1394  816  LYS B O   
3946 C CB  . LYS B 160 ? 0.2429 0.5485 0.4568 0.0834  0.0894  0.1322  816  LYS B CB  
3947 C CG  . LYS B 160 ? 0.4067 0.7568 0.6357 0.0961  0.0997  0.1468  816  LYS B CG  
3948 C CD  . LYS B 160 ? 0.5889 0.9377 0.7920 0.1185  0.1165  0.1466  816  LYS B CD  
3949 C CE  . LYS B 160 ? 0.7695 1.1680 0.9893 0.1332  0.1277  0.1628  816  LYS B CE  
3950 N NZ  . LYS B 160 ? 0.9161 1.3089 1.1074 0.1606  0.1458  0.1611  816  LYS B NZ  
3951 N N   . TYR B 161 ? 0.1773 0.4443 0.4107 0.0635  0.0640  0.1152  817  TYR B N   
3952 C CA  . TYR B 161 ? 0.1522 0.4106 0.3924 0.0636  0.0582  0.1098  817  TYR B CA  
3953 C C   . TYR B 161 ? 0.1676 0.4395 0.4330 0.0451  0.0456  0.1143  817  TYR B C   
3954 O O   . TYR B 161 ? 0.1703 0.4617 0.4517 0.0450  0.0431  0.1193  817  TYR B O   
3955 C CB  . TYR B 161 ? 0.1705 0.3868 0.3874 0.0644  0.0560  0.0948  817  TYR B CB  
3956 C CG  . TYR B 161 ? 0.1637 0.3649 0.3762 0.0714  0.0550  0.0883  817  TYR B CG  
3957 C CD1 . TYR B 161 ? 0.1798 0.4051 0.4100 0.0772  0.0553  0.0955  817  TYR B CD1 
3958 C CD2 . TYR B 161 ? 0.1726 0.3372 0.3631 0.0712  0.0535  0.0760  817  TYR B CD2 
3959 C CE1 . TYR B 161 ? 0.1842 0.3956 0.4095 0.0838  0.0543  0.0904  817  TYR B CE1 
3960 C CE2 . TYR B 161 ? 0.1796 0.3294 0.3650 0.0767  0.0527  0.0709  817  TYR B CE2 
3961 C CZ  . TYR B 161 ? 0.2298 0.4022 0.4324 0.0836  0.0533  0.0780  817  TYR B CZ  
3962 O OH  . TYR B 161 ? 0.2103 0.3672 0.4064 0.0890  0.0523  0.0736  817  TYR B OH  
3963 N N   . VAL B 162 ? 0.1262 0.3883 0.3937 0.0300  0.0382  0.1134  818  VAL B N   
3964 C CA  . VAL B 162 ? 0.1157 0.3829 0.4016 0.0122  0.0267  0.1170  818  VAL B CA  
3965 C C   . VAL B 162 ? 0.1461 0.4521 0.4516 0.0067  0.0276  0.1324  818  VAL B C   
3966 O O   . VAL B 162 ? 0.0995 0.4196 0.4202 -0.0006 0.0214  0.1361  818  VAL B O   
3967 C CB  . VAL B 162 ? 0.1683 0.4149 0.4484 0.0009  0.0206  0.1142  818  VAL B CB  
3968 C CG1 . VAL B 162 ? 0.1619 0.4093 0.4570 -0.0160 0.0099  0.1188  818  VAL B CG1 
3969 C CG2 . VAL B 162 ? 0.1765 0.3916 0.4400 0.0045  0.0187  0.1008  818  VAL B CG2 
3970 N N   . LYS B 163 ? 0.1174 0.4421 0.4214 0.0097  0.0354  0.1417  819  LYS B N   
3971 C CA  . LYS B 163 ? 0.1014 0.4671 0.4231 0.0044  0.0377  0.1580  819  LYS B CA  
3972 C C   . LYS B 163 ? 0.1564 0.5554 0.4919 0.0134  0.0414  0.1650  819  LYS B C   
3973 O O   . LYS B 163 ? 0.1593 0.5865 0.5149 -0.0002 0.0350  0.1757  819  LYS B O   
3974 C CB  . LYS B 163 ? 0.1394 0.5170 0.4520 0.0109  0.0481  0.1650  819  LYS B CB  
3975 C CG  . LYS B 163 ? 0.2554 0.6776 0.5859 0.0031  0.0509  0.1837  819  LYS B CG  
3976 C CD  . LYS B 163 ? 0.4028 0.8330 0.7214 0.0099  0.0613  0.1892  819  LYS B CD  
3977 C CE  . LYS B 163 ? 0.4892 0.9609 0.8259 -0.0032 0.0619  0.2085  819  LYS B CE  
3978 N NZ  . LYS B 163 ? 0.4960 1.0167 0.8472 0.0085  0.0714  0.2210  819  LYS B NZ  
3979 N N   . ASN B 164 ? 0.1036 0.4988 0.4274 0.0355  0.0512  0.1597  820  ASN B N   
3980 C CA  . ASN B 164 ? 0.1160 0.5441 0.4510 0.0487  0.0567  0.1678  820  ASN B CA  
3981 C C   . ASN B 164 ? 0.1760 0.5982 0.5177 0.0475  0.0487  0.1627  820  ASN B C   
3982 O O   . ASN B 164 ? 0.1268 0.5846 0.4832 0.0542  0.0507  0.1729  820  ASN B O   
3983 C CB  . ASN B 164 ? 0.2083 0.6344 0.5246 0.0761  0.0727  0.1662  820  ASN B CB  
3984 C CG  . ASN B 164 ? 0.5041 0.9495 0.8150 0.0832  0.0841  0.1748  820  ASN B CG  
3985 O OD1 . ASN B 164 ? 0.4466 0.9202 0.7730 0.0686  0.0816  0.1866  820  ASN B OD1 
3986 N ND2 . ASN B 164 ? 0.3796 0.8090 0.6660 0.1061  0.0975  0.1692  820  ASN B ND2 
3987 N N   . THR B 165 ? 0.1417 0.5224 0.4726 0.0407  0.0405  0.1479  821  THR B N   
3988 C CA  . THR B 165 ? 0.1409 0.5142 0.4749 0.0413  0.0342  0.1424  821  THR B CA  
3989 C C   . THR B 165 ? 0.1794 0.5472 0.5250 0.0177  0.0191  0.1403  821  THR B C   
3990 O O   . THR B 165 ? 0.1656 0.5135 0.5076 0.0155  0.0127  0.1312  821  THR B O   
3991 C CB  . THR B 165 ? 0.2266 0.5601 0.5369 0.0562  0.0389  0.1281  821  THR B CB  
3992 O OG1 . THR B 165 ? 0.2239 0.5211 0.5219 0.0456  0.0333  0.1164  821  THR B OG1 
3993 C CG2 . THR B 165 ? 0.2005 0.5336 0.4942 0.0799  0.0539  0.1295  821  THR B CG2 
3994 N N   . HIS B 166 ? 0.1281 0.5138 0.4864 0.0001  0.0139  0.1496  822  HIS B N   
3995 C CA  . HIS B 166 ? 0.1251 0.5035 0.4912 -0.0223 0.0000  0.1484  822  HIS B CA  
3996 C C   . HIS B 166 ? 0.1571 0.5770 0.5417 -0.0284 -0.0041 0.1605  822  HIS B C   
3997 O O   . HIS B 166 ? 0.1193 0.5788 0.5173 -0.0307 -0.0005 0.1754  822  HIS B O   
3998 C CB  . HIS B 166 ? 0.1279 0.4964 0.4938 -0.0396 -0.0045 0.1517  822  HIS B CB  
3999 C CG  . HIS B 166 ? 0.1732 0.5216 0.5400 -0.0608 -0.0180 0.1481  822  HIS B CG  
4000 N ND1 . HIS B 166 ? 0.2151 0.5276 0.5709 -0.0683 -0.0222 0.1412  822  HIS B ND1 
4001 C CD2 . HIS B 166 ? 0.1898 0.5488 0.5651 -0.0751 -0.0277 0.1508  822  HIS B CD2 
4002 C CE1 . HIS B 166 ? 0.2180 0.5163 0.5740 -0.0850 -0.0333 0.1389  822  HIS B CE1 
4003 N NE2 . HIS B 166 ? 0.2089 0.5338 0.5757 -0.0911 -0.0374 0.1442  822  HIS B NE2 
4004 N N   . ALA B 167 ? 0.1276 0.5411 0.5129 -0.0312 -0.0116 0.1546  823  ALA B N   
4005 C CA  . ALA B 167 ? 0.0943 0.5464 0.4956 -0.0372 -0.0170 0.1651  823  ALA B CA  
4006 C C   . ALA B 167 ? 0.1304 0.6006 0.5435 -0.0654 -0.0285 0.1746  823  ALA B C   
4007 O O   . ALA B 167 ? 0.1295 0.5667 0.5340 -0.0823 -0.0366 0.1673  823  ALA B O   
4008 C CB  . ALA B 167 ? 0.1080 0.5439 0.5032 -0.0325 -0.0219 0.1552  823  ALA B CB  
4009 N N   . THR B 168 ? 0.0581 0.5812 0.4902 -0.0704 -0.0294 0.1915  824  THR B N   
4010 C CA  . THR B 168 ? 0.0584 0.6049 0.5021 -0.0999 -0.0411 0.2029  824  THR B CA  
4011 C C   . THR B 168 ? 0.1292 0.6456 0.5637 -0.1194 -0.0560 0.1924  824  THR B C   
4012 O O   . THR B 168 ? 0.1424 0.6391 0.5713 -0.1439 -0.0656 0.1917  824  THR B O   
4013 C CB  . THR B 168 ? 0.1849 0.7999 0.6518 -0.0990 -0.0388 0.2237  824  THR B CB  
4014 O OG1 . THR B 168 ? 0.1419 0.7806 0.6141 -0.0795 -0.0237 0.2325  824  THR B OG1 
4015 C CG2 . THR B 168 ? 0.2334 0.8777 0.7129 -0.1329 -0.0519 0.2374  824  THR B CG2 
4016 N N   . THR B 169 ? 0.0884 0.5963 0.5180 -0.1078 -0.0573 0.1835  825  THR B N   
4017 C CA  . THR B 169 ? 0.0976 0.5776 0.5162 -0.1248 -0.0707 0.1729  825  THR B CA  
4018 C C   . THR B 169 ? 0.1170 0.5350 0.5145 -0.1296 -0.0731 0.1558  825  THR B C   
4019 O O   . THR B 169 ? 0.0979 0.4888 0.4837 -0.1456 -0.0839 0.1474  825  THR B O   
4020 C CB  . THR B 169 ? 0.1624 0.6524 0.5812 -0.1113 -0.0713 0.1693  825  THR B CB  
4021 O OG1 . THR B 169 ? 0.1988 0.6541 0.6045 -0.0877 -0.0621 0.1556  825  THR B OG1 
4022 C CG2 . THR B 169 ? 0.0885 0.6426 0.5288 -0.1037 -0.0685 0.1879  825  THR B CG2 
4023 N N   . HIS B 170 ? 0.0873 0.4851 0.4794 -0.1158 -0.0632 0.1518  826  HIS B N   
4024 C CA  . HIS B 170 ? 0.0979 0.4433 0.4724 -0.1167 -0.0638 0.1381  826  HIS B CA  
4025 C C   . HIS B 170 ? 0.2383 0.5777 0.6128 -0.1305 -0.0645 0.1455  826  HIS B C   
4026 O O   . HIS B 170 ? 0.2691 0.5755 0.6326 -0.1249 -0.0610 0.1383  826  HIS B O   
4027 C CB  . HIS B 170 ? 0.0965 0.4230 0.4630 -0.0911 -0.0528 0.1278  826  HIS B CB  
4028 C CG  . HIS B 170 ? 0.1205 0.4472 0.4843 -0.0780 -0.0519 0.1207  826  HIS B CG  
4029 N ND1 . HIS B 170 ? 0.1361 0.4616 0.4964 -0.0554 -0.0413 0.1172  826  HIS B ND1 
4030 C CD2 . HIS B 170 ? 0.1342 0.4619 0.4966 -0.0856 -0.0604 0.1174  826  HIS B CD2 
4031 C CE1 . HIS B 170 ? 0.1311 0.4556 0.4886 -0.0498 -0.0436 0.1122  826  HIS B CE1 
4032 N NE2 . HIS B 170 ? 0.1348 0.4626 0.4941 -0.0671 -0.0549 0.1124  826  HIS B NE2 
4033 N N   . ASN B 171 ? 0.2397 0.6123 0.6264 -0.1496 -0.0697 0.1606  827  ASN B N   
4034 C CA  . ASN B 171 ? 0.2621 0.6360 0.6505 -0.1655 -0.0708 0.1711  827  ASN B CA  
4035 C C   . ASN B 171 ? 0.3456 0.6711 0.7162 -0.1871 -0.0815 0.1650  827  ASN B C   
4036 O O   . ASN B 171 ? 0.3492 0.6697 0.7185 -0.2000 -0.0825 0.1735  827  ASN B O   
4037 C CB  . ASN B 171 ? 0.3109 0.7433 0.7198 -0.1785 -0.0718 0.1916  827  ASN B CB  
4038 C CG  . ASN B 171 ? 0.6796 1.1274 1.0921 -0.2042 -0.0858 0.1969  827  ASN B CG  
4039 O OD1 . ASN B 171 ? 0.6274 1.0495 1.0284 -0.2086 -0.0940 0.1850  827  ASN B OD1 
4040 N ND2 . ASN B 171 ? 0.6189 1.1118 1.0470 -0.2225 -0.0890 0.2156  827  ASN B ND2 
4041 N N   . ALA B 172 ? 0.3195 0.6073 0.6745 -0.1893 -0.0886 0.1503  828  ALA B N   
4042 C CA  . ALA B 172 ? 0.3365 0.5715 0.6701 -0.2046 -0.0971 0.1425  828  ALA B CA  
4043 C C   . ALA B 172 ? 0.3963 0.5976 0.7204 -0.1917 -0.0901 0.1381  828  ALA B C   
4044 O O   . ALA B 172 ? 0.4337 0.5909 0.7401 -0.2008 -0.0952 0.1338  828  ALA B O   
4045 C CB  . ALA B 172 ? 0.3594 0.5644 0.6778 -0.2034 -0.1033 0.1269  828  ALA B CB  
4046 N N   . TYR B 173 ? 0.3069 0.5279 0.6409 -0.1701 -0.0785 0.1393  829  TYR B N   
4047 C CA  . TYR B 173 ? 0.2924 0.4917 0.6199 -0.1570 -0.0714 0.1368  829  TYR B CA  
4048 C C   . TYR B 173 ? 0.3022 0.5388 0.6432 -0.1433 -0.0603 0.1456  829  TYR B C   
4049 O O   . TYR B 173 ? 0.2788 0.5519 0.6322 -0.1353 -0.0558 0.1490  829  TYR B O   
4050 C CB  . TYR B 173 ? 0.3105 0.4734 0.6246 -0.1400 -0.0696 0.1200  829  TYR B CB  
4051 C CG  . TYR B 173 ? 0.2974 0.4776 0.6173 -0.1207 -0.0631 0.1126  829  TYR B CG  
4052 C CD1 . TYR B 173 ? 0.3001 0.4913 0.6232 -0.1029 -0.0530 0.1124  829  TYR B CD1 
4053 C CD2 . TYR B 173 ? 0.3130 0.4958 0.6324 -0.1212 -0.0673 0.1057  829  TYR B CD2 
4054 C CE1 . TYR B 173 ? 0.2721 0.4738 0.5970 -0.0865 -0.0472 0.1058  829  TYR B CE1 
4055 C CE2 . TYR B 173 ? 0.3102 0.5060 0.6331 -0.1039 -0.0613 0.0998  829  TYR B CE2 
4056 C CZ  . TYR B 173 ? 0.3256 0.5293 0.6508 -0.0868 -0.0513 0.0999  829  TYR B CZ  
4057 O OH  . TYR B 173 ? 0.2770 0.4886 0.6024 -0.0710 -0.0456 0.0944  829  TYR B OH  
4058 N N   . ASP B 174 ? 0.2279 0.4541 0.5646 -0.1404 -0.0558 0.1498  830  ASP B N   
4059 C CA  . ASP B 174 ? 0.2116 0.4620 0.5541 -0.1262 -0.0447 0.1557  830  ASP B CA  
4060 C C   . ASP B 174 ? 0.2357 0.4567 0.5660 -0.1079 -0.0402 0.1428  830  ASP B C   
4061 O O   . ASP B 174 ? 0.2143 0.3993 0.5336 -0.1092 -0.0459 0.1337  830  ASP B O   
4062 C CB  . ASP B 174 ? 0.2401 0.4974 0.5838 -0.1384 -0.0440 0.1701  830  ASP B CB  
4063 C CG  . ASP B 174 ? 0.3747 0.6725 0.7330 -0.1557 -0.0457 0.1870  830  ASP B CG  
4064 O OD1 . ASP B 174 ? 0.3820 0.7135 0.7528 -0.1542 -0.0450 0.1895  830  ASP B OD1 
4065 O OD2 . ASP B 174 ? 0.4010 0.6991 0.7584 -0.1706 -0.0475 0.1990  830  ASP B OD2 
4066 N N   . LEU B 175 ? 0.1841 0.4205 0.5147 -0.0914 -0.0302 0.1425  831  LEU B N   
4067 C CA  . LEU B 175 ? 0.1864 0.4000 0.5052 -0.0766 -0.0263 0.1320  831  LEU B CA  
4068 C C   . LEU B 175 ? 0.2211 0.4376 0.5350 -0.0735 -0.0208 0.1386  831  LEU B C   
4069 O O   . LEU B 175 ? 0.2027 0.4479 0.5221 -0.0721 -0.0142 0.1482  831  LEU B O   
4070 C CB  . LEU B 175 ? 0.1813 0.4028 0.4988 -0.0602 -0.0201 0.1231  831  LEU B CB  
4071 C CG  . LEU B 175 ? 0.2379 0.4508 0.5565 -0.0598 -0.0251 0.1139  831  LEU B CG  
4072 C CD1 . LEU B 175 ? 0.2404 0.4653 0.5580 -0.0446 -0.0180 0.1091  831  LEU B CD1 
4073 C CD2 . LEU B 175 ? 0.2777 0.4559 0.5863 -0.0601 -0.0306 0.1033  831  LEU B CD2 
4074 N N   . GLU B 176 ? 0.1636 0.3527 0.4671 -0.0712 -0.0232 0.1340  832  GLU B N   
4075 C CA  . GLU B 176 ? 0.1795 0.3687 0.4759 -0.0678 -0.0190 0.1395  832  GLU B CA  
4076 C C   . GLU B 176 ? 0.2153 0.3893 0.5008 -0.0545 -0.0170 0.1283  832  GLU B C   
4077 O O   . GLU B 176 ? 0.2099 0.3613 0.4918 -0.0532 -0.0224 0.1209  832  GLU B O   
4078 C CB  . GLU B 176 ? 0.2193 0.3914 0.5133 -0.0801 -0.0252 0.1482  832  GLU B CB  
4079 C CG  . GLU B 176 ? 0.4561 0.6343 0.7445 -0.0794 -0.0212 0.1578  832  GLU B CG  
4080 C CD  . GLU B 176 ? 0.8861 1.0384 1.1678 -0.0870 -0.0275 0.1642  832  GLU B CD  
4081 O OE1 . GLU B 176 ? 0.8339 0.9776 1.1068 -0.0795 -0.0264 0.1645  832  GLU B OE1 
4082 O OE2 . GLU B 176 ? 0.9106 1.0500 1.1941 -0.1007 -0.0339 0.1693  832  GLU B OE2 
4083 N N   . VAL B 177 ? 0.1539 0.3405 0.4328 -0.0451 -0.0092 0.1274  833  VAL B N   
4084 C CA  . VAL B 177 ? 0.1541 0.3284 0.4206 -0.0355 -0.0076 0.1177  833  VAL B CA  
4085 C C   . VAL B 177 ? 0.2336 0.3963 0.4935 -0.0379 -0.0113 0.1220  833  VAL B C   
4086 O O   . VAL B 177 ? 0.2408 0.4128 0.4980 -0.0408 -0.0087 0.1317  833  VAL B O   
4087 C CB  . VAL B 177 ? 0.1943 0.3802 0.4506 -0.0256 0.0016  0.1145  833  VAL B CB  
4088 C CG1 . VAL B 177 ? 0.1986 0.3686 0.4412 -0.0193 0.0013  0.1032  833  VAL B CG1 
4089 C CG2 . VAL B 177 ? 0.1847 0.3869 0.4482 -0.0212 0.0068  0.1147  833  VAL B CG2 
4090 N N   . ILE B 178 ? 0.1995 0.3440 0.4574 -0.0362 -0.0171 0.1160  834  ILE B N   
4091 C CA  . ILE B 178 ? 0.2102 0.3451 0.4624 -0.0359 -0.0209 0.1206  834  ILE B CA  
4092 C C   . ILE B 178 ? 0.2632 0.4037 0.5035 -0.0298 -0.0182 0.1163  834  ILE B C   
4093 O O   . ILE B 178 ? 0.2584 0.4050 0.4911 -0.0306 -0.0168 0.1232  834  ILE B O   
4094 C CB  . ILE B 178 ? 0.2580 0.3724 0.5131 -0.0351 -0.0278 0.1180  834  ILE B CB  
4095 C CG1 . ILE B 178 ? 0.2646 0.3682 0.5266 -0.0433 -0.0313 0.1211  834  ILE B CG1 
4096 C CG2 . ILE B 178 ? 0.2724 0.3795 0.5217 -0.0317 -0.0311 0.1241  834  ILE B CG2 
4097 C CD1 . ILE B 178 ? 0.3039 0.3882 0.5661 -0.0402 -0.0358 0.1133  834  ILE B CD1 
4098 N N   . ASP B 179 ? 0.2273 0.3651 0.4644 -0.0253 -0.0179 0.1053  835  ASP B N   
4099 C CA  . ASP B 179 ? 0.2347 0.3749 0.4584 -0.0225 -0.0167 0.1002  835  ASP B CA  
4100 C C   . ASP B 179 ? 0.2941 0.4333 0.5112 -0.0196 -0.0120 0.0900  835  ASP B C   
4101 O O   . ASP B 179 ? 0.2818 0.4177 0.5072 -0.0182 -0.0120 0.0853  835  ASP B O   
4102 C CB  . ASP B 179 ? 0.2613 0.3964 0.4859 -0.0210 -0.0232 0.0984  835  ASP B CB  
4103 C CG  . ASP B 179 ? 0.4335 0.5683 0.6603 -0.0210 -0.0276 0.1088  835  ASP B CG  
4104 O OD1 . ASP B 179 ? 0.4489 0.5911 0.6676 -0.0230 -0.0265 0.1156  835  ASP B OD1 
4105 O OD2 . ASP B 179 ? 0.5524 0.6784 0.7874 -0.0180 -0.0319 0.1101  835  ASP B OD2 
4106 N N   . ILE B 180 ? 0.2359 0.3757 0.4355 -0.0187 -0.0082 0.0867  836  ILE B N   
4107 C CA  . ILE B 180 ? 0.2212 0.3539 0.4083 -0.0157 -0.0038 0.0770  836  ILE B CA  
4108 C C   . ILE B 180 ? 0.2520 0.3786 0.4251 -0.0197 -0.0081 0.0714  836  ILE B C   
4109 O O   . ILE B 180 ? 0.2415 0.3718 0.4036 -0.0232 -0.0097 0.0748  836  ILE B O   
4110 C CB  . ILE B 180 ? 0.2581 0.3928 0.4321 -0.0106 0.0057  0.0773  836  ILE B CB  
4111 C CG1 . ILE B 180 ? 0.2494 0.3981 0.4400 -0.0079 0.0097  0.0855  836  ILE B CG1 
4112 C CG2 . ILE B 180 ? 0.2686 0.3891 0.4264 -0.0061 0.0101  0.0668  836  ILE B CG2 
4113 C CD1 . ILE B 180 ? 0.2090 0.3676 0.3893 -0.0010 0.0204  0.0895  836  ILE B CD1 
4114 N N   . PHE B 181 ? 0.1840 0.3036 0.3577 -0.0205 -0.0106 0.0638  837  PHE B N   
4115 C CA  . PHE B 181 ? 0.1656 0.2822 0.3266 -0.0266 -0.0150 0.0592  837  PHE B CA  
4116 C C   . PHE B 181 ? 0.2507 0.3512 0.3908 -0.0275 -0.0107 0.0501  837  PHE B C   
4117 O O   . PHE B 181 ? 0.2446 0.3376 0.3882 -0.0222 -0.0067 0.0462  837  PHE B O   
4118 C CB  . PHE B 181 ? 0.1664 0.2894 0.3431 -0.0279 -0.0217 0.0593  837  PHE B CB  
4119 C CG  . PHE B 181 ? 0.1670 0.3000 0.3612 -0.0250 -0.0256 0.0680  837  PHE B CG  
4120 C CD1 . PHE B 181 ? 0.1895 0.3329 0.3816 -0.0272 -0.0300 0.0750  837  PHE B CD1 
4121 C CD2 . PHE B 181 ? 0.1717 0.3018 0.3824 -0.0202 -0.0253 0.0694  837  PHE B CD2 
4122 C CE1 . PHE B 181 ? 0.1863 0.3349 0.3922 -0.0228 -0.0331 0.0838  837  PHE B CE1 
4123 C CE2 . PHE B 181 ? 0.1894 0.3219 0.4117 -0.0176 -0.0287 0.0772  837  PHE B CE2 
4124 C CZ  . PHE B 181 ? 0.1637 0.3044 0.3834 -0.0180 -0.0322 0.0845  837  PHE B CZ  
4125 N N   . LYS B 182 ? 0.2331 0.3269 0.3497 -0.0346 -0.0119 0.0469  838  LYS B N   
4126 C CA  . LYS B 182 ? 0.2646 0.3366 0.3563 -0.0373 -0.0087 0.0377  838  LYS B CA  
4127 C C   . LYS B 182 ? 0.3123 0.3875 0.4080 -0.0468 -0.0164 0.0353  838  LYS B C   
4128 O O   . LYS B 182 ? 0.3242 0.4148 0.4233 -0.0547 -0.0236 0.0395  838  LYS B O   
4129 C CB  . LYS B 182 ? 0.3275 0.3863 0.3869 -0.0414 -0.0060 0.0349  838  LYS B CB  
4130 C CG  . LYS B 182 ? 0.5172 0.5455 0.5468 -0.0400 0.0003  0.0253  838  LYS B CG  
4131 C CD  . LYS B 182 ? 0.6652 0.6755 0.6573 -0.0493 -0.0002 0.0204  838  LYS B CD  
4132 C CE  . LYS B 182 ? 0.8147 0.7889 0.7721 -0.0433 0.0090  0.0113  838  LYS B CE  
4133 N NZ  . LYS B 182 ? 0.9107 0.8838 0.8616 -0.0275 0.0201  0.0133  838  LYS B NZ  
4134 N N   . ILE B 183 ? 0.2501 0.3153 0.3482 -0.0453 -0.0150 0.0303  839  ILE B N   
4135 C CA  . ILE B 183 ? 0.2348 0.3062 0.3386 -0.0540 -0.0215 0.0290  839  ILE B CA  
4136 C C   . ILE B 183 ? 0.3037 0.3518 0.3804 -0.0633 -0.0212 0.0214  839  ILE B C   
4137 O O   . ILE B 183 ? 0.2976 0.3208 0.3569 -0.0578 -0.0143 0.0162  839  ILE B O   
4138 C CB  . ILE B 183 ? 0.2568 0.3408 0.3892 -0.0468 -0.0224 0.0311  839  ILE B CB  
4139 C CG1 . ILE B 183 ? 0.2552 0.3243 0.3884 -0.0377 -0.0158 0.0270  839  ILE B CG1 
4140 C CG2 . ILE B 183 ? 0.2268 0.3307 0.3822 -0.0408 -0.0247 0.0389  839  ILE B CG2 
4141 C CD1 . ILE B 183 ? 0.1408 0.2183 0.2955 -0.0336 -0.0174 0.0272  839  ILE B CD1 
4142 N N   . GLU B 184 ? 0.2746 0.3317 0.3468 -0.0779 -0.0287 0.0221  840  GLU B N   
4143 C CA  . GLU B 184 ? 0.2972 0.3348 0.3436 -0.0920 -0.0309 0.0165  840  GLU B CA  
4144 C C   . GLU B 184 ? 0.3225 0.3816 0.3852 -0.1012 -0.0375 0.0197  840  GLU B C   
4145 O O   . GLU B 184 ? 0.2870 0.3715 0.3562 -0.1113 -0.0448 0.0251  840  GLU B O   
4146 C CB  . GLU B 184 ? 0.3343 0.3603 0.3492 -0.1055 -0.0340 0.0145  840  GLU B CB  
4147 C CG  . GLU B 184 ? 0.5305 0.5241 0.5098 -0.1205 -0.0350 0.0072  840  GLU B CG  
4148 C CD  . GLU B 184 ? 0.8751 0.8483 0.8160 -0.1343 -0.0376 0.0031  840  GLU B CD  
4149 O OE1 . GLU B 184 ? 0.7729 0.7352 0.7015 -0.1246 -0.0319 0.0013  840  GLU B OE1 
4150 O OE2 . GLU B 184 ? 0.8973 0.8654 0.8188 -0.1557 -0.0452 0.0018  840  GLU B OE2 
4151 N N   . ARG B 185 ? 0.2823 0.3337 0.3518 -0.0969 -0.0345 0.0171  841  ARG B N   
4152 C CA  . ARG B 185 ? 0.2637 0.3347 0.3472 -0.1044 -0.0392 0.0200  841  ARG B CA  
4153 C C   . ARG B 185 ? 0.3382 0.3977 0.3949 -0.1259 -0.0441 0.0181  841  ARG B C   
4154 O O   . ARG B 185 ? 0.3625 0.3848 0.3881 -0.1308 -0.0411 0.0117  841  ARG B O   
4155 C CB  . ARG B 185 ? 0.2609 0.3253 0.3564 -0.0941 -0.0345 0.0178  841  ARG B CB  
4156 C CG  . ARG B 185 ? 0.3010 0.3817 0.4257 -0.0766 -0.0318 0.0204  841  ARG B CG  
4157 C CD  . ARG B 185 ? 0.3092 0.3864 0.4436 -0.0700 -0.0289 0.0183  841  ARG B CD  
4158 N NE  . ARG B 185 ? 0.3581 0.4533 0.4991 -0.0789 -0.0328 0.0206  841  ARG B NE  
4159 C CZ  . ARG B 185 ? 0.4732 0.5572 0.5990 -0.0901 -0.0334 0.0189  841  ARG B CZ  
4160 N NH1 . ARG B 185 ? 0.2539 0.3603 0.3879 -0.0986 -0.0369 0.0226  841  ARG B NH1 
4161 N NH2 . ARG B 185 ? 0.4167 0.4667 0.5180 -0.0922 -0.0299 0.0141  841  ARG B NH2 
4162 N N   . GLU B 186 ? 0.2658 0.3569 0.3331 -0.1388 -0.0516 0.0243  842  GLU B N   
4163 C CA  . GLU B 186 ? 0.2851 0.3720 0.3296 -0.1631 -0.0579 0.0244  842  GLU B CA  
4164 C C   . GLU B 186 ? 0.3368 0.3965 0.3680 -0.1673 -0.0546 0.0198  842  GLU B C   
4165 O O   . GLU B 186 ? 0.3195 0.3897 0.3725 -0.1559 -0.0510 0.0211  842  GLU B O   
4166 C CB  . GLU B 186 ? 0.2855 0.4221 0.3527 -0.1725 -0.0658 0.0345  842  GLU B CB  
4167 C CG  . GLU B 186 ? 0.4899 0.6339 0.5373 -0.2009 -0.0745 0.0374  842  GLU B CG  
4168 C CD  . GLU B 186 ? 0.8018 1.0029 0.8777 -0.2060 -0.0810 0.0493  842  GLU B CD  
4169 O OE1 . GLU B 186 ? 0.9134 1.1430 0.9971 -0.2075 -0.0864 0.0559  842  GLU B OE1 
4170 O OE2 . GLU B 186 ? 0.5830 0.8022 0.6744 -0.2064 -0.0800 0.0528  842  GLU B OE2 
4171 N N   . GLY B 187 ? 0.3305 0.3511 0.3233 -0.1823 -0.0552 0.0141  843  GLY B N   
4172 C CA  . GLY B 187 ? 0.3478 0.3346 0.3195 -0.1890 -0.0526 0.0102  843  GLY B CA  
4173 C C   . GLY B 187 ? 0.4277 0.3776 0.3910 -0.1684 -0.0426 0.0039  843  GLY B C   
4174 O O   . GLY B 187 ? 0.4429 0.3543 0.3792 -0.1730 -0.0398 -0.0001 843  GLY B O   
4175 N N   . GLU B 188 ? 0.4005 0.3628 0.3866 -0.1459 -0.0373 0.0040  844  GLU B N   
4176 C CA  . GLU B 188 ? 0.4077 0.3462 0.3929 -0.1250 -0.0282 0.0002  844  GLU B CA  
4177 C C   . GLU B 188 ? 0.5257 0.4147 0.4699 -0.1233 -0.0227 -0.0066 844  GLU B C   
4178 O O   . GLU B 188 ? 0.5415 0.4006 0.4716 -0.1154 -0.0169 -0.0092 844  GLU B O   
4179 C CB  . GLU B 188 ? 0.3927 0.3583 0.4101 -0.1055 -0.0252 0.0029  844  GLU B CB  
4180 C CG  . GLU B 188 ? 0.4838 0.4394 0.5106 -0.0861 -0.0177 0.0018  844  GLU B CG  
4181 C CD  . GLU B 188 ? 0.5926 0.5735 0.6493 -0.0701 -0.0156 0.0049  844  GLU B CD  
4182 O OE1 . GLU B 188 ? 0.7334 0.7118 0.7859 -0.0640 -0.0130 0.0047  844  GLU B OE1 
4183 O OE2 . GLU B 188 ? 0.4553 0.4574 0.5381 -0.0644 -0.0167 0.0075  844  GLU B OE2 
4184 N N   . CYS B 189 ? 0.5223 0.4018 0.4457 -0.1304 -0.0243 -0.0092 845  CYS B N   
4185 C CA  . CYS B 189 ? 0.5736 0.4046 0.4539 -0.1283 -0.0186 -0.0164 845  CYS B CA  
4186 C C   . CYS B 189 ? 0.6501 0.4359 0.4913 -0.1432 -0.0194 -0.0208 845  CYS B C   
4187 O O   . CYS B 189 ? 0.6617 0.4027 0.4735 -0.1317 -0.0112 -0.0259 845  CYS B O   
4188 C CB  . CYS B 189 ? 0.5970 0.4315 0.4629 -0.1362 -0.0218 -0.0180 845  CYS B CB  
4189 S SG  . CYS B 189 ? 0.6918 0.4694 0.5056 -0.1277 -0.0125 -0.0274 845  CYS B SG  
4190 N N   . GLN B 190 ? 0.6010 0.3995 0.4424 -0.1679 -0.0290 -0.0178 846  GLN B N   
4191 C CA  . GLN B 190 ? 0.6206 0.3797 0.4265 -0.1868 -0.0315 -0.0202 846  GLN B CA  
4192 C C   . GLN B 190 ? 0.6457 0.3969 0.4633 -0.1741 -0.0260 -0.0180 846  GLN B C   
4193 O O   . GLN B 190 ? 0.6619 0.3638 0.4446 -0.1753 -0.0222 -0.0215 846  GLN B O   
4194 C CB  . GLN B 190 ? 0.6402 0.4254 0.4476 -0.2186 -0.0440 -0.0154 846  GLN B CB  
4195 C CG  . GLN B 190 ? 0.9437 0.6861 0.6987 -0.2449 -0.0496 -0.0210 846  GLN B CG  
4196 C CD  . GLN B 190 ? 1.2976 1.0582 1.0489 -0.2793 -0.0616 -0.0151 846  GLN B CD  
4197 O OE1 . GLN B 190 ? 1.2568 1.0498 1.0369 -0.2834 -0.0640 -0.0076 846  GLN B OE1 
4198 N NE2 . GLN B 190 ? 1.1999 0.9408 0.9141 -0.3058 -0.0696 -0.0182 846  GLN B NE2 
4199 N N   . ARG B 191 ? 0.5387 0.3363 0.4030 -0.1611 -0.0255 -0.0121 847  ARG B N   
4200 C CA  . ARG B 191 ? 0.5131 0.3107 0.3926 -0.1483 -0.0210 -0.0094 847  ARG B CA  
4201 C C   . ARG B 191 ? 0.5808 0.3427 0.4454 -0.1232 -0.0103 -0.0132 847  ARG B C   
4202 O O   . ARG B 191 ? 0.5678 0.3018 0.4184 -0.1175 -0.0062 -0.0128 847  ARG B O   
4203 C CB  . ARG B 191 ? 0.4179 0.2721 0.3480 -0.1389 -0.0228 -0.0036 847  ARG B CB  
4204 C CG  . ARG B 191 ? 0.4241 0.2857 0.3706 -0.1316 -0.0206 -0.0002 847  ARG B CG  
4205 C CD  . ARG B 191 ? 0.4022 0.3145 0.3934 -0.1220 -0.0221 0.0041  847  ARG B CD  
4206 N NE  . ARG B 191 ? 0.3827 0.3045 0.3918 -0.1008 -0.0176 0.0028  847  ARG B NE  
4207 C CZ  . ARG B 191 ? 0.6084 0.5671 0.6521 -0.0910 -0.0185 0.0055  847  ARG B CZ  
4208 N NH1 . ARG B 191 ? 0.4807 0.4707 0.5449 -0.0977 -0.0228 0.0092  847  ARG B NH1 
4209 N NH2 . ARG B 191 ? 0.4033 0.3668 0.4596 -0.0745 -0.0148 0.0048  847  ARG B NH2 
4210 N N   . TYR B 192 ? 0.5422 0.3079 0.4102 -0.1080 -0.0058 -0.0156 848  TYR B N   
4211 C CA  . TYR B 192 ? 0.5549 0.2982 0.4141 -0.0823 0.0048  -0.0176 848  TYR B CA  
4212 C C   . TYR B 192 ? 0.7049 0.3862 0.5111 -0.0811 0.0108  -0.0238 848  TYR B C   
4213 O O   . TYR B 192 ? 0.7232 0.3815 0.5196 -0.0591 0.0201  -0.0238 848  TYR B O   
4214 C CB  . TYR B 192 ? 0.5284 0.3025 0.4113 -0.0687 0.0073  -0.0167 848  TYR B CB  
4215 C CG  . TYR B 192 ? 0.5249 0.2903 0.4084 -0.0413 0.0182  -0.0162 848  TYR B CG  
4216 C CD1 . TYR B 192 ? 0.5165 0.3025 0.4287 -0.0253 0.0212  -0.0111 848  TYR B CD1 
4217 C CD2 . TYR B 192 ? 0.5477 0.2862 0.4022 -0.0313 0.0256  -0.0204 848  TYR B CD2 
4218 C CE1 . TYR B 192 ? 0.4897 0.2737 0.4044 -0.0009 0.0307  -0.0089 848  TYR B CE1 
4219 C CE2 . TYR B 192 ? 0.5506 0.2871 0.4077 -0.0049 0.0364  -0.0184 848  TYR B CE2 
4220 C CZ  . TYR B 192 ? 0.5720 0.3331 0.4604 0.0099  0.0386  -0.0120 848  TYR B CZ  
4221 O OH  . TYR B 192 ? 0.5557 0.3199 0.4480 0.0350  0.0486  -0.0084 848  TYR B OH  
4222 N N   . LYS B 193 ? 0.7098 0.3633 0.4804 -0.1043 0.0054  -0.0286 849  LYS B N   
4223 C CA  . LYS B 193 ? 0.7519 0.3398 0.4646 -0.1069 0.0100  -0.0360 849  LYS B CA  
4224 C C   . LYS B 193 ? 0.8270 0.3693 0.5161 -0.0907 0.0186  -0.0360 849  LYS B C   
4225 O O   . LYS B 193 ? 0.8520 0.3574 0.5125 -0.0703 0.0290  -0.0402 849  LYS B O   
4226 C CB  . LYS B 193 ? 0.8032 0.3707 0.4838 -0.1419 -0.0004 -0.0395 849  LYS B CB  
4227 C CG  . LYS B 193 ? 1.0763 0.5837 0.6981 -0.1455 0.0033  -0.0490 849  LYS B CG  
4228 C CD  . LYS B 193 ? 1.2654 0.7548 0.8548 -0.1834 -0.0087 -0.0522 849  LYS B CD  
4229 N N   . PRO B 194 ? 0.7810 0.3250 0.4803 -0.0959 0.0159  -0.0308 850  PRO B N   
4230 C CA  . PRO B 194 ? 0.8050 0.3033 0.4790 -0.0781 0.0246  -0.0299 850  PRO B CA  
4231 C C   . PRO B 194 ? 0.8589 0.3694 0.5518 -0.0411 0.0361  -0.0269 850  PRO B C   
4232 O O   . PRO B 194 ? 0.8779 0.3477 0.5447 -0.0220 0.0449  -0.0262 850  PRO B O   
4233 C CB  . PRO B 194 ? 0.8167 0.3294 0.5077 -0.0924 0.0181  -0.0233 850  PRO B CB  
4234 C CG  . PRO B 194 ? 0.8497 0.3982 0.5577 -0.1229 0.0061  -0.0226 850  PRO B CG  
4235 C CD  . PRO B 194 ? 0.7745 0.3595 0.5051 -0.1174 0.0055  -0.0250 850  PRO B CD  
4236 N N   . PHE B 195 ? 0.7782 0.3446 0.5151 -0.0313 0.0358  -0.0243 851  PHE B N   
4237 C CA  . PHE B 195 ? 0.7599 0.3509 0.5224 -0.0005 0.0446  -0.0198 851  PHE B CA  
4238 C C   . PHE B 195 ? 0.8720 0.4673 0.6293 0.0119  0.0509  -0.0232 851  PHE B C   
4239 O O   . PHE B 195 ? 0.8555 0.4714 0.6313 0.0372  0.0590  -0.0189 851  PHE B O   
4240 C CB  . PHE B 195 ? 0.7324 0.3859 0.5512 -0.0009 0.0387  -0.0129 851  PHE B CB  
4241 C CG  . PHE B 195 ? 0.7326 0.3880 0.5592 -0.0124 0.0329  -0.0091 851  PHE B CG  
4242 C CD1 . PHE B 195 ? 0.7632 0.4057 0.5874 0.0043  0.0381  -0.0041 851  PHE B CD1 
4243 C CD2 . PHE B 195 ? 0.7391 0.4106 0.5743 -0.0394 0.0226  -0.0097 851  PHE B CD2 
4244 C CE1 . PHE B 195 ? 0.7670 0.4101 0.5958 -0.0068 0.0330  -0.0003 851  PHE B CE1 
4245 C CE2 . PHE B 195 ? 0.7622 0.4356 0.6023 -0.0501 0.0182  -0.0057 851  PHE B CE2 
4246 C CZ  . PHE B 195 ? 0.7430 0.4019 0.5799 -0.0341 0.0234  -0.0012 851  PHE B CZ  
4247 N N   . LYS B 196 ? 0.8867 0.4647 0.6186 -0.0065 0.0469  -0.0302 852  LYS B N   
4248 C CA  . LYS B 196 ? 0.9008 0.4838 0.6254 0.0006  0.0514  -0.0338 852  LYS B CA  
4249 C C   . LYS B 196 ? 1.0125 0.5614 0.7070 0.0298  0.0663  -0.0357 852  LYS B C   
4250 O O   . LYS B 196 ? 1.0086 0.5821 0.7161 0.0448  0.0723  -0.0343 852  LYS B O   
4251 C CB  . LYS B 196 ? 0.9489 0.5153 0.6463 -0.0273 0.0432  -0.0409 852  LYS B CB  
4252 N N   . GLN B 197 ? 1.0223 0.5159 0.6768 0.0388  0.0727  -0.0381 853  GLN B N   
4253 C CA  . GLN B 197 ? 1.0578 0.5157 0.6804 0.0700  0.0882  -0.0393 853  GLN B CA  
4254 C C   . GLN B 197 ? 1.1112 0.5779 0.7521 0.0975  0.0959  -0.0301 853  GLN B C   
4255 O O   . GLN B 197 ? 1.1347 0.5700 0.7479 0.1260  0.1094  -0.0295 853  GLN B O   
4256 C CB  . GLN B 197 ? 1.1291 0.5071 0.6810 0.0631  0.0918  -0.0500 853  GLN B CB  
4257 N N   . LEU B 198 ? 1.0236 0.5350 0.7107 0.0903  0.0877  -0.0224 854  LEU B N   
4258 C CA  . LEU B 198 ? 0.9992 0.5273 0.7083 0.1131  0.0926  -0.0126 854  LEU B CA  
4259 C C   . LEU B 198 ? 1.0139 0.5773 0.7447 0.1437  0.1035  -0.0060 854  LEU B C   
4260 O O   . LEU B 198 ? 0.9978 0.5904 0.7435 0.1421  0.1039  -0.0074 854  LEU B O   
4261 C CB  . LEU B 198 ? 0.9674 0.5422 0.7230 0.0969  0.0808  -0.0068 854  LEU B CB  
4262 C CG  . LEU B 198 ? 1.0185 0.5896 0.7804 0.1074  0.0816  0.0008  854  LEU B CG  
4263 C CD1 . LEU B 198 ? 1.0554 0.5636 0.7713 0.0950  0.0802  -0.0033 854  LEU B CD1 
4264 C CD2 . LEU B 198 ? 0.9903 0.6180 0.8032 0.0950  0.0711  0.0064  854  LEU B CD2 
4265 N N   . HIS B 199 ? 0.9331 0.4935 0.6638 0.1718  0.1126  0.0020  855  HIS B N   
4266 C CA  . HIS B 199 ? 0.8830 0.4829 0.6367 0.2008  0.1228  0.0104  855  HIS B CA  
4267 C C   . HIS B 199 ? 0.8292 0.5026 0.6446 0.1930  0.1139  0.0188  855  HIS B C   
4268 O O   . HIS B 199 ? 0.8129 0.4997 0.6487 0.1710  0.1018  0.0183  855  HIS B O   
4269 C CB  . HIS B 199 ? 0.9074 0.4807 0.6384 0.2351  0.1360  0.0174  855  HIS B CB  
4270 C CG  . HIS B 199 ? 0.9369 0.5243 0.6890 0.2384  0.1313  0.0266  855  HIS B CG  
4271 N ND1 . HIS B 199 ? 0.9742 0.5289 0.7119 0.2167  0.1221  0.0227  855  HIS B ND1 
4272 C CD2 . HIS B 199 ? 0.9269 0.5581 0.7113 0.2607  0.1348  0.0400  855  HIS B CD2 
4273 C CE1 . HIS B 199 ? 0.9490 0.5273 0.7101 0.2269  0.1205  0.0333  855  HIS B CE1 
4274 N NE2 . HIS B 199 ? 0.9240 0.5484 0.7134 0.2532  0.1276  0.0439  855  HIS B NE2 
4275 N N   . ASN B 200 ? 0.7261 0.4451 0.5682 0.2092  0.1198  0.0259  856  ASN B N   
4276 C CA  . ASN B 200 ? 0.6560 0.4423 0.5526 0.2040  0.1128  0.0344  856  ASN B CA  
4277 C C   . ASN B 200 ? 0.6525 0.4576 0.5709 0.1714  0.0988  0.0284  856  ASN B C   
4278 O O   . ASN B 200 ? 0.6157 0.4472 0.5640 0.1579  0.0886  0.0310  856  ASN B O   
4279 C CB  . ASN B 200 ? 0.6399 0.4449 0.5564 0.2150  0.1113  0.0444  856  ASN B CB  
4280 C CG  . ASN B 200 ? 0.8345 0.7067 0.8009 0.2180  0.1074  0.0557  856  ASN B CG  
4281 O OD1 . ASN B 200 ? 0.7884 0.6972 0.7741 0.2233  0.1109  0.0602  856  ASN B OD1 
4282 N ND2 . ASN B 200 ? 0.6079 0.4964 0.5941 0.2139  0.1000  0.0609  856  ASN B ND2 
4283 N N   . ARG B 201 ? 0.6004 0.3918 0.5022 0.1603  0.0988  0.0205  857  ARG B N   
4284 C CA  . ARG B 201 ? 0.5760 0.3876 0.4974 0.1330  0.0869  0.0162  857  ARG B CA  
4285 C C   . ARG B 201 ? 0.5726 0.4361 0.5294 0.1365  0.0874  0.0230  857  ARG B C   
4286 O O   . ARG B 201 ? 0.5670 0.4326 0.5132 0.1506  0.0970  0.0246  857  ARG B O   
4287 C CB  . ARG B 201 ? 0.5974 0.3674 0.4813 0.1165  0.0849  0.0050  857  ARG B CB  
4288 C CG  . ARG B 201 ? 0.7130 0.4353 0.5655 0.1048  0.0811  -0.0012 857  ARG B CG  
4289 C CD  . ARG B 201 ? 0.8190 0.4966 0.6280 0.0895  0.0800  -0.0116 857  ARG B CD  
4290 N NE  . ARG B 201 ? 0.9280 0.5713 0.6984 0.1095  0.0931  -0.0150 857  ARG B NE  
4291 C CZ  . ARG B 201 ? 1.1625 0.8054 0.9195 0.1082  0.0962  -0.0192 857  ARG B CZ  
4292 N NH1 . ARG B 201 ? 1.0203 0.6948 0.7995 0.0872  0.0864  -0.0201 857  ARG B NH1 
4293 N NH2 . ARG B 201 ? 1.0197 0.6297 0.7391 0.1288  0.1094  -0.0224 857  ARG B NH2 
4294 N N   . ARG B 202 ? 0.4764 0.3809 0.4740 0.1248  0.0777  0.0278  858  ARG B N   
4295 C CA  . ARG B 202 ? 0.4259 0.3789 0.4583 0.1255  0.0766  0.0354  858  ARG B CA  
4296 C C   . ARG B 202 ? 0.4277 0.3980 0.4799 0.1024  0.0654  0.0327  858  ARG B C   
4297 O O   . ARG B 202 ? 0.4080 0.3688 0.4622 0.0868  0.0565  0.0277  858  ARG B O   
4298 C CB  . ARG B 202 ? 0.3953 0.3845 0.4583 0.1361  0.0763  0.0459  858  ARG B CB  
4299 C CG  . ARG B 202 ? 0.5323 0.5225 0.5846 0.1635  0.0893  0.0532  858  ARG B CG  
4300 C CD  . ARG B 202 ? 0.5859 0.6172 0.6698 0.1724  0.0878  0.0650  858  ARG B CD  
4301 N NE  . ARG B 202 ? 0.6592 0.6759 0.7254 0.1975  0.0977  0.0699  858  ARG B NE  
4302 C CZ  . ARG B 202 ? 0.7746 0.8243 0.8620 0.2106  0.0986  0.0816  858  ARG B CZ  
4303 N NH1 . ARG B 202 ? 0.6071 0.7052 0.7331 0.1989  0.0896  0.0888  858  ARG B NH1 
4304 N NH2 . ARG B 202 ? 0.6024 0.6361 0.6711 0.2355  0.1082  0.0865  858  ARG B NH2 
4305 N N   . LEU B 203 ? 0.3663 0.3629 0.4329 0.1013  0.0665  0.0368  859  LEU B N   
4306 C CA  . LEU B 203 ? 0.3494 0.3640 0.4356 0.0825  0.0567  0.0362  859  LEU B CA  
4307 C C   . LEU B 203 ? 0.3470 0.3993 0.4707 0.0804  0.0512  0.0442  859  LEU B C   
4308 O O   . LEU B 203 ? 0.3185 0.3985 0.4575 0.0901  0.0559  0.0531  859  LEU B O   
4309 C CB  . LEU B 203 ? 0.3540 0.3731 0.4323 0.0815  0.0605  0.0368  859  LEU B CB  
4310 C CG  . LEU B 203 ? 0.4022 0.4321 0.4935 0.0626  0.0506  0.0357  859  LEU B CG  
4311 C CD1 . LEU B 203 ? 0.4281 0.4278 0.4962 0.0492  0.0451  0.0261  859  LEU B CD1 
4312 C CD2 . LEU B 203 ? 0.3936 0.4424 0.4890 0.0640  0.0543  0.0413  859  LEU B CD2 
4313 N N   . LEU B 204 ? 0.2716 0.3242 0.4079 0.0680  0.0416  0.0412  860  LEU B N   
4314 C CA  . LEU B 204 ? 0.2391 0.3201 0.4052 0.0646  0.0355  0.0468  860  LEU B CA  
4315 C C   . LEU B 204 ? 0.2753 0.3652 0.4579 0.0481  0.0255  0.0449  860  LEU B C   
4316 O O   . LEU B 204 ? 0.2831 0.3573 0.4554 0.0391  0.0223  0.0389  860  LEU B O   
4317 C CB  . LEU B 204 ? 0.2404 0.3142 0.4050 0.0698  0.0346  0.0461  860  LEU B CB  
4318 C CG  . LEU B 204 ? 0.2901 0.3560 0.4398 0.0897  0.0446  0.0499  860  LEU B CG  
4319 C CD1 . LEU B 204 ? 0.2983 0.3446 0.4378 0.0916  0.0429  0.0470  860  LEU B CD1 
4320 C CD2 . LEU B 204 ? 0.2625 0.3655 0.4330 0.1009  0.0484  0.0615  860  LEU B CD2 
4321 N N   . TRP B 205 ? 0.2112 0.3262 0.4185 0.0441  0.0206  0.0505  861  TRP B N   
4322 C CA  . TRP B 205 ? 0.1829 0.3052 0.4056 0.0307  0.0117  0.0497  861  TRP B CA  
4323 C C   . TRP B 205 ? 0.1992 0.3131 0.4244 0.0249  0.0052  0.0439  861  TRP B C   
4324 O O   . TRP B 205 ? 0.1654 0.2798 0.3906 0.0297  0.0055  0.0439  861  TRP B O   
4325 C CB  . TRP B 205 ? 0.1530 0.3024 0.3973 0.0276  0.0091  0.0584  861  TRP B CB  
4326 C CG  . TRP B 205 ? 0.1705 0.3357 0.4167 0.0322  0.0153  0.0664  861  TRP B CG  
4327 C CD1 . TRP B 205 ? 0.1984 0.3850 0.4501 0.0423  0.0216  0.0748  861  TRP B CD1 
4328 C CD2 . TRP B 205 ? 0.1710 0.3352 0.4143 0.0274  0.0161  0.0679  861  TRP B CD2 
4329 N NE1 . TRP B 205 ? 0.1878 0.3876 0.4404 0.0436  0.0267  0.0814  861  TRP B NE1 
4330 C CE2 . TRP B 205 ? 0.2208 0.4053 0.4670 0.0345  0.0235  0.0769  861  TRP B CE2 
4331 C CE3 . TRP B 205 ? 0.1906 0.3410 0.4296 0.0184  0.0114  0.0636  861  TRP B CE3 
4332 C CZ2 . TRP B 205 ? 0.2114 0.4011 0.4552 0.0318  0.0261  0.0811  861  TRP B CZ2 
4333 C CZ3 . TRP B 205 ? 0.2127 0.3678 0.4493 0.0162  0.0135  0.0680  861  TRP B CZ3 
4334 C CH2 . TRP B 205 ? 0.2182 0.3916 0.4564 0.0224  0.0208  0.0764  861  TRP B CH2 
4335 N N   . HIS B 206 ? 0.1417 0.2504 0.3698 0.0154  -0.0006 0.0400  862  HIS B N   
4336 C CA  . HIS B 206 ? 0.1221 0.2264 0.3543 0.0099  -0.0066 0.0351  862  HIS B CA  
4337 C C   . HIS B 206 ? 0.1673 0.2753 0.4095 0.0026  -0.0120 0.0354  862  HIS B C   
4338 O O   . HIS B 206 ? 0.1626 0.2652 0.4000 -0.0001 -0.0125 0.0341  862  HIS B O   
4339 C CB  . HIS B 206 ? 0.1277 0.2153 0.3448 0.0092  -0.0059 0.0288  862  HIS B CB  
4340 C CG  . HIS B 206 ? 0.1583 0.2461 0.3808 0.0050  -0.0109 0.0249  862  HIS B CG  
4341 N ND1 . HIS B 206 ? 0.1652 0.2522 0.3866 0.0080  -0.0109 0.0242  862  HIS B ND1 
4342 C CD2 . HIS B 206 ? 0.1727 0.2626 0.4016 -0.0003 -0.0155 0.0225  862  HIS B CD2 
4343 C CE1 . HIS B 206 ? 0.1573 0.2453 0.3829 0.0035  -0.0152 0.0205  862  HIS B CE1 
4344 N NE2 . HIS B 206 ? 0.1644 0.2541 0.3946 -0.0007 -0.0178 0.0193  862  HIS B NE2 
4345 N N   . GLY B 207 ? 0.1271 0.2437 0.3818 -0.0006 -0.0163 0.0378  863  GLY B N   
4346 C CA  . GLY B 207 ? 0.1174 0.2319 0.3790 -0.0069 -0.0216 0.0380  863  GLY B CA  
4347 C C   . GLY B 207 ? 0.1305 0.2363 0.3903 -0.0078 -0.0253 0.0312  863  GLY B C   
4348 O O   . GLY B 207 ? 0.1310 0.2365 0.3879 -0.0059 -0.0250 0.0279  863  GLY B O   
4349 N N   . SER B 208 ? 0.0835 0.1825 0.3440 -0.0096 -0.0282 0.0299  864  SER B N   
4350 C CA  . SER B 208 ? 0.0689 0.1606 0.3273 -0.0084 -0.0306 0.0241  864  SER B CA  
4351 C C   . SER B 208 ? 0.1080 0.1914 0.3681 -0.0088 -0.0337 0.0253  864  SER B C   
4352 O O   . SER B 208 ? 0.1183 0.2018 0.3808 -0.0107 -0.0339 0.0308  864  SER B O   
4353 C CB  . SER B 208 ? 0.0963 0.1894 0.3487 -0.0055 -0.0280 0.0209  864  SER B CB  
4354 O OG  . SER B 208 ? 0.1574 0.2488 0.4079 -0.0041 -0.0290 0.0157  864  SER B OG  
4355 N N   . ARG B 209 ? 0.0841 0.1325 0.3155 -0.0050 -0.0321 0.0205  865  ARG B N   
4356 C CA  . ARG B 209 ? 0.0818 0.1438 0.3373 -0.0037 -0.0377 0.0210  865  ARG B CA  
4357 C C   . ARG B 209 ? 0.1788 0.2473 0.4355 0.0020  -0.0355 0.0242  865  ARG B C   
4358 O O   . ARG B 209 ? 0.1720 0.2529 0.4288 0.0034  -0.0331 0.0232  865  ARG B O   
4359 C CB  . ARG B 209 ? 0.0786 0.1235 0.3233 -0.0004 -0.0385 0.0141  865  ARG B CB  
4360 C CG  . ARG B 209 ? 0.1365 0.1790 0.3822 -0.0077 -0.0428 0.0111  865  ARG B CG  
4361 C CD  . ARG B 209 ? 0.3155 0.3465 0.5515 -0.0033 -0.0433 0.0030  865  ARG B CD  
4362 N NE  . ARG B 209 ? 0.4062 0.4373 0.6387 -0.0104 -0.0466 -0.0005 865  ARG B NE  
4363 C CZ  . ARG B 209 ? 0.6004 0.6134 0.8225 -0.0158 -0.0513 -0.0046 865  ARG B CZ  
4364 N NH1 . ARG B 209 ? 0.3976 0.3862 0.6099 -0.0139 -0.0526 -0.0063 865  ARG B NH1 
4365 N NH2 . ARG B 209 ? 0.5135 0.5312 0.7331 -0.0232 -0.0549 -0.0068 865  ARG B NH2 
4366 N N   . THR B 210 ? 0.1776 0.2377 0.4340 0.0042  -0.0369 0.0290  866  THR B N   
4367 C CA  . THR B 210 ? 0.1710 0.2392 0.4291 0.0095  -0.0358 0.0340  866  THR B CA  
4368 C C   . THR B 210 ? 0.2309 0.3097 0.4890 0.0171  -0.0340 0.0311  866  THR B C   
4369 O O   . THR B 210 ? 0.2157 0.3115 0.4761 0.0174  -0.0332 0.0343  866  THR B O   
4370 C CB  . THR B 210 ? 0.3091 0.3624 0.5653 0.0119  -0.0379 0.0400  866  THR B CB  
4371 O OG1 . THR B 210 ? 0.3927 0.4249 0.6424 0.0167  -0.0391 0.0360  866  THR B OG1 
4372 C CG2 . THR B 210 ? 0.2753 0.3250 0.5328 0.0024  -0.0393 0.0455  866  THR B CG2 
4373 N N   . THR B 211 ? 0.1968 0.2673 0.4515 0.0220  -0.0335 0.0250  867  THR B N   
4374 C CA  . THR B 211 ? 0.1725 0.2541 0.4271 0.0302  -0.0310 0.0221  867  THR B CA  
4375 C C   . THR B 211 ? 0.1886 0.2878 0.4449 0.0241  -0.0295 0.0196  867  THR B C   
4376 O O   . THR B 211 ? 0.2154 0.3285 0.4726 0.0285  -0.0275 0.0188  867  THR B O   
4377 C CB  . THR B 211 ? 0.1480 0.2110 0.3948 0.0378  -0.0304 0.0161  867  THR B CB  
4378 O OG1 . THR B 211 ? 0.1795 0.2286 0.4219 0.0290  -0.0327 0.0112  867  THR B OG1 
4379 C CG2 . THR B 211 ? 0.1013 0.1457 0.3431 0.0473  -0.0307 0.0192  867  THR B CG2 
4380 N N   . ASN B 212 ? 0.1305 0.2290 0.3862 0.0147  -0.0302 0.0191  868  ASN B N   
4381 C CA  . ASN B 212 ? 0.1096 0.2183 0.3632 0.0089  -0.0287 0.0172  868  ASN B CA  
4382 C C   . ASN B 212 ? 0.1476 0.2675 0.4004 0.0037  -0.0286 0.0217  868  ASN B C   
4383 O O   . ASN B 212 ? 0.1274 0.2553 0.3761 -0.0014 -0.0277 0.0209  868  ASN B O   
4384 C CB  . ASN B 212 ? 0.0703 0.1249 0.2768 0.0013  -0.0236 0.0145  868  ASN B CB  
4385 C CG  . ASN B 212 ? 0.2536 0.3449 0.5030 0.0052  -0.0298 0.0098  868  ASN B CG  
4386 O OD1 . ASN B 212 ? 0.2726 0.3528 0.5221 0.0061  -0.0320 0.0092  868  ASN B OD1 
4387 N ND2 . ASN B 212 ? 0.1908 0.2858 0.4367 0.0043  -0.0285 0.0065  868  ASN B ND2 
4388 N N   . PHE B 213 ? 0.1126 0.2311 0.3672 0.0037  -0.0298 0.0265  869  PHE B N   
4389 C CA  . PHE B 213 ? 0.1070 0.2322 0.3577 -0.0022 -0.0302 0.0304  869  PHE B CA  
4390 C C   . PHE B 213 ? 0.1792 0.3226 0.4301 -0.0038 -0.0315 0.0338  869  PHE B C   
4391 O O   . PHE B 213 ? 0.1725 0.3199 0.4158 -0.0121 -0.0321 0.0348  869  PHE B O   
4392 C CB  . PHE B 213 ? 0.1228 0.2418 0.3749 -0.0016 -0.0309 0.0351  869  PHE B CB  
4393 C CG  . PHE B 213 ? 0.1337 0.2427 0.3830 -0.0050 -0.0291 0.0334  869  PHE B CG  
4394 C CD1 . PHE B 213 ? 0.1569 0.2571 0.4107 -0.0034 -0.0296 0.0319  869  PHE B CD1 
4395 C CD2 . PHE B 213 ? 0.1552 0.2642 0.3960 -0.0095 -0.0268 0.0334  869  PHE B CD2 
4396 C CE1 . PHE B 213 ? 0.1718 0.2692 0.4250 -0.0062 -0.0280 0.0320  869  PHE B CE1 
4397 C CE2 . PHE B 213 ? 0.1727 0.2757 0.4114 -0.0097 -0.0240 0.0327  869  PHE B CE2 
4398 C CZ  . PHE B 213 ? 0.1487 0.2490 0.3955 -0.0080 -0.0248 0.0329  869  PHE B CZ  
4399 N N   . ALA B 214 ? 0.1535 0.3085 0.4115 0.0037  -0.0318 0.0355  870  ALA B N   
4400 C CA  . ALA B 214 ? 0.1685 0.3478 0.4287 0.0015  -0.0331 0.0401  870  ALA B CA  
4401 C C   . ALA B 214 ? 0.2143 0.3978 0.4687 -0.0076 -0.0322 0.0360  870  ALA B C   
4402 O O   . ALA B 214 ? 0.2093 0.4030 0.4576 -0.0188 -0.0341 0.0382  870  ALA B O   
4403 C CB  . ALA B 214 ? 0.1746 0.3671 0.4440 0.0147  -0.0323 0.0437  870  ALA B CB  
4404 N N   . GLY B 215 ? 0.1831 0.3558 0.4370 -0.0044 -0.0297 0.0302  871  GLY B N   
4405 C CA  . GLY B 215 ? 0.1875 0.3597 0.4344 -0.0124 -0.0285 0.0267  871  GLY B CA  
4406 C C   . GLY B 215 ? 0.2081 0.3652 0.4424 -0.0230 -0.0289 0.0249  871  GLY B C   
4407 O O   . GLY B 215 ? 0.2102 0.3718 0.4356 -0.0339 -0.0300 0.0259  871  GLY B O   
4408 N N   . ILE B 216 ? 0.1407 0.2798 0.3729 -0.0199 -0.0280 0.0230  872  ILE B N   
4409 C CA  . ILE B 216 ? 0.1350 0.2577 0.3542 -0.0254 -0.0266 0.0212  872  ILE B CA  
4410 C C   . ILE B 216 ? 0.1679 0.2934 0.3770 -0.0343 -0.0284 0.0238  872  ILE B C   
4411 O O   . ILE B 216 ? 0.1657 0.2796 0.3586 -0.0425 -0.0276 0.0217  872  ILE B O   
4412 C CB  . ILE B 216 ? 0.1658 0.2763 0.3880 -0.0190 -0.0249 0.0207  872  ILE B CB  
4413 C CG1 . ILE B 216 ? 0.1478 0.2538 0.3759 -0.0136 -0.0240 0.0176  872  ILE B CG1 
4414 C CG2 . ILE B 216 ? 0.2003 0.2972 0.4085 -0.0220 -0.0222 0.0201  872  ILE B CG2 
4415 C CD1 . ILE B 216 ? 0.1145 0.2156 0.3501 -0.0088 -0.0242 0.0188  872  ILE B CD1 
4416 N N   . LEU B 217 ? 0.1427 0.2811 0.3586 -0.0329 -0.0309 0.0285  873  LEU B N   
4417 C CA  . LEU B 217 ? 0.1571 0.3001 0.3621 -0.0426 -0.0335 0.0313  873  LEU B CA  
4418 C C   . LEU B 217 ? 0.2138 0.3706 0.4133 -0.0543 -0.0366 0.0327  873  LEU B C   
4419 O O   . LEU B 217 ? 0.2287 0.3780 0.4104 -0.0667 -0.0383 0.0318  873  LEU B O   
4420 C CB  . LEU B 217 ? 0.1460 0.3007 0.3590 -0.0383 -0.0358 0.0373  873  LEU B CB  
4421 C CG  . LEU B 217 ? 0.1908 0.3317 0.4058 -0.0309 -0.0332 0.0374  873  LEU B CG  
4422 C CD1 . LEU B 217 ? 0.1925 0.3444 0.4158 -0.0264 -0.0357 0.0446  873  LEU B CD1 
4423 C CD2 . LEU B 217 ? 0.1899 0.3128 0.3875 -0.0354 -0.0301 0.0340  873  LEU B CD2 
4424 N N   . SER B 218 ? 0.1709 0.3472 0.3837 -0.0511 -0.0372 0.0348  874  SER B N   
4425 C CA  . SER B 218 ? 0.1576 0.3529 0.3670 -0.0637 -0.0402 0.0380  874  SER B CA  
4426 C C   . SER B 218 ? 0.2132 0.3932 0.4094 -0.0729 -0.0385 0.0334  874  SER B C   
4427 O O   . SER B 218 ? 0.2180 0.3997 0.4006 -0.0892 -0.0416 0.0347  874  SER B O   
4428 C CB  . SER B 218 ? 0.2011 0.4295 0.4301 -0.0558 -0.0410 0.0442  874  SER B CB  
4429 O OG  . SER B 218 ? 0.3614 0.5895 0.5987 -0.0461 -0.0370 0.0412  874  SER B OG  
4430 N N   . GLN B 219 ? 0.1675 0.3321 0.3663 -0.0636 -0.0342 0.0286  875  GLN B N   
4431 C CA  . GLN B 219 ? 0.1659 0.3163 0.3533 -0.0697 -0.0323 0.0253  875  GLN B CA  
4432 C C   . GLN B 219 ? 0.2235 0.3398 0.3950 -0.0678 -0.0292 0.0200  875  GLN B C   
4433 O O   . GLN B 219 ? 0.2159 0.3154 0.3730 -0.0737 -0.0278 0.0180  875  GLN B O   
4434 C CB  . GLN B 219 ? 0.1691 0.3316 0.3707 -0.0600 -0.0298 0.0249  875  GLN B CB  
4435 C CG  . GLN B 219 ? 0.4286 0.6257 0.6472 -0.0560 -0.0309 0.0303  875  GLN B CG  
4436 C CD  . GLN B 219 ? 0.6410 0.8622 0.8583 -0.0692 -0.0327 0.0356  875  GLN B CD  
4437 O OE1 . GLN B 219 ? 0.4917 0.7355 0.7199 -0.0640 -0.0306 0.0382  875  GLN B OE1 
4438 N NE2 . GLN B 219 ? 0.6155 0.8334 0.8184 -0.0873 -0.0366 0.0378  875  GLN B NE2 
4439 N N   . GLY B 220 ? 0.1624 0.2700 0.3370 -0.0586 -0.0277 0.0188  876  GLY B N   
4440 C CA  . GLY B 220 ? 0.1670 0.2481 0.3295 -0.0535 -0.0238 0.0152  876  GLY B CA  
4441 C C   . GLY B 220 ? 0.1896 0.2691 0.3630 -0.0425 -0.0212 0.0136  876  GLY B C   
4442 O O   . GLY B 220 ? 0.1439 0.2390 0.3310 -0.0397 -0.0224 0.0141  876  GLY B O   
4443 N N   . LEU B 221 ? 0.1420 0.2039 0.3089 -0.0355 -0.0176 0.0121  877  LEU B N   
4444 C CA  . LEU B 221 ? 0.1283 0.1889 0.3029 -0.0267 -0.0157 0.0114  877  LEU B CA  
4445 C C   . LEU B 221 ? 0.1941 0.2469 0.3578 -0.0318 -0.0153 0.0104  877  LEU B C   
4446 O O   . LEU B 221 ? 0.1949 0.2304 0.3388 -0.0391 -0.0143 0.0100  877  LEU B O   
4447 C CB  . LEU B 221 ? 0.1266 0.1747 0.2962 -0.0182 -0.0117 0.0119  877  LEU B CB  
4448 C CG  . LEU B 221 ? 0.1493 0.2052 0.3287 -0.0136 -0.0114 0.0141  877  LEU B CG  
4449 C CD1 . LEU B 221 ? 0.1350 0.1815 0.3077 -0.0051 -0.0063 0.0157  877  LEU B CD1 
4450 C CD2 . LEU B 221 ? 0.1595 0.2322 0.3599 -0.0110 -0.0149 0.0152  877  LEU B CD2 
4451 N N   . ARG B 222 ? 0.1446 0.2094 0.3194 -0.0296 -0.0164 0.0102  878  ARG B N   
4452 C CA  . ARG B 222 ? 0.1343 0.1968 0.3018 -0.0343 -0.0162 0.0103  878  ARG B CA  
4453 C C   . ARG B 222 ? 0.1917 0.2520 0.3631 -0.0257 -0.0150 0.0099  878  ARG B C   
4454 O O   . ARG B 222 ? 0.1767 0.2423 0.3596 -0.0176 -0.0154 0.0094  878  ARG B O   
4455 C CB  . ARG B 222 ? 0.1820 0.2670 0.3595 -0.0395 -0.0185 0.0112  878  ARG B CB  
4456 C CG  . ARG B 222 ? 0.2904 0.3808 0.4604 -0.0524 -0.0204 0.0135  878  ARG B CG  
4457 C CD  . ARG B 222 ? 0.4872 0.6079 0.6724 -0.0536 -0.0223 0.0161  878  ARG B CD  
4458 N NE  . ARG B 222 ? 0.6687 0.8004 0.8706 -0.0416 -0.0225 0.0153  878  ARG B NE  
4459 C CZ  . ARG B 222 ? 0.7490 0.9041 0.9643 -0.0370 -0.0230 0.0173  878  ARG B CZ  
4460 N NH1 . ARG B 222 ? 0.4426 0.5999 0.6689 -0.0258 -0.0231 0.0164  878  ARG B NH1 
4461 N NH2 . ARG B 222 ? 0.5381 0.7144 0.7551 -0.0432 -0.0232 0.0211  878  ARG B NH2 
4462 N N   . ILE B 223 ? 0.1697 0.2218 0.3302 -0.0285 -0.0139 0.0108  879  ILE B N   
4463 C CA  . ILE B 223 ? 0.1670 0.2191 0.3297 -0.0213 -0.0134 0.0113  879  ILE B CA  
4464 C C   . ILE B 223 ? 0.1935 0.2655 0.3671 -0.0227 -0.0153 0.0098  879  ILE B C   
4465 O O   . ILE B 223 ? 0.1804 0.2633 0.3556 -0.0295 -0.0158 0.0099  879  ILE B O   
4466 C CB  . ILE B 223 ? 0.2174 0.2478 0.3601 -0.0226 -0.0109 0.0141  879  ILE B CB  
4467 C CG1 . ILE B 223 ? 0.2195 0.2287 0.3502 -0.0164 -0.0077 0.0152  879  ILE B CG1 
4468 C CG2 . ILE B 223 ? 0.2248 0.2590 0.3685 -0.0176 -0.0111 0.0158  879  ILE B CG2 
4469 C CD1 . ILE B 223 ? 0.2896 0.2707 0.3949 -0.0223 -0.0053 0.0162  879  ILE B CD1 
4470 N N   . ALA B 224 ? 0.1327 0.2108 0.3131 -0.0159 -0.0164 0.0086  880  ALA B N   
4471 C CA  . ALA B 224 ? 0.1152 0.2080 0.3014 -0.0153 -0.0173 0.0063  880  ALA B CA  
4472 C C   . ALA B 224 ? 0.1837 0.2786 0.3600 -0.0224 -0.0155 0.0087  880  ALA B C   
4473 O O   . ALA B 224 ? 0.2005 0.2805 0.3638 -0.0261 -0.0144 0.0121  880  ALA B O   
4474 C CB  . ALA B 224 ? 0.1098 0.2037 0.2989 -0.0091 -0.0193 0.0048  880  ALA B CB  
4475 N N   . PRO B 225 ? 0.1408 0.2533 0.3215 -0.0243 -0.0148 0.0079  881  PRO B N   
4476 C CA  . PRO B 225 ? 0.1335 0.2521 0.3056 -0.0332 -0.0130 0.0119  881  PRO B CA  
4477 C C   . PRO B 225 ? 0.1943 0.3059 0.3557 -0.0333 -0.0122 0.0139  881  PRO B C   
4478 O O   . PRO B 225 ? 0.1758 0.2826 0.3383 -0.0254 -0.0134 0.0116  881  PRO B O   
4479 C CB  . PRO B 225 ? 0.1364 0.2809 0.3189 -0.0316 -0.0116 0.0111  881  PRO B CB  
4480 C CG  . PRO B 225 ? 0.2020 0.3473 0.3932 -0.0199 -0.0123 0.0055  881  PRO B CG  
4481 C CD  . PRO B 225 ? 0.1607 0.2884 0.3533 -0.0181 -0.0149 0.0043  881  PRO B CD  
4482 N N   . PRO B 226 ? 0.1758 0.2878 0.3263 -0.0432 -0.0107 0.0189  882  PRO B N   
4483 C CA  . PRO B 226 ? 0.1974 0.3012 0.3363 -0.0429 -0.0100 0.0219  882  PRO B CA  
4484 C C   . PRO B 226 ? 0.2566 0.3751 0.4004 -0.0346 -0.0098 0.0188  882  PRO B C   
4485 O O   . PRO B 226 ? 0.2939 0.4038 0.4301 -0.0310 -0.0107 0.0203  882  PRO B O   
4486 C CB  . PRO B 226 ? 0.2241 0.3289 0.3515 -0.0572 -0.0085 0.0282  882  PRO B CB  
4487 C CG  . PRO B 226 ? 0.2789 0.3813 0.4072 -0.0660 -0.0095 0.0287  882  PRO B CG  
4488 C CD  . PRO B 226 ? 0.2094 0.3290 0.3564 -0.0566 -0.0101 0.0232  882  PRO B CD  
4489 N N   . GLU B 227 ? 0.1601 0.2992 0.3145 -0.0306 -0.0087 0.0146  883  GLU B N   
4490 C CA  . GLU B 227 ? 0.1523 0.3023 0.3077 -0.0225 -0.0080 0.0100  883  GLU B CA  
4491 C C   . GLU B 227 ? 0.1989 0.3369 0.3560 -0.0147 -0.0120 0.0050  883  GLU B C   
4492 O O   . GLU B 227 ? 0.2118 0.3518 0.3633 -0.0109 -0.0130 0.0025  883  GLU B O   
4493 C CB  . GLU B 227 ? 0.1530 0.3241 0.3173 -0.0177 -0.0049 0.0066  883  GLU B CB  
4494 C CG  . GLU B 227 ? 0.2818 0.4753 0.4455 -0.0243 -0.0005 0.0126  883  GLU B CG  
4495 C CD  . GLU B 227 ? 0.4472 0.6441 0.6136 -0.0365 -0.0011 0.0192  883  GLU B CD  
4496 O OE1 . GLU B 227 ? 0.3782 0.5896 0.5405 -0.0470 0.0010  0.0261  883  GLU B OE1 
4497 O OE2 . GLU B 227 ? 0.2060 0.3909 0.3771 -0.0370 -0.0040 0.0177  883  GLU B OE2 
4498 N N   . ALA B 228 ? 0.1341 0.2619 0.2984 -0.0134 -0.0143 0.0040  884  ALA B N   
4499 C CA  . ALA B 228 ? 0.1479 0.2676 0.3162 -0.0082 -0.0183 0.0009  884  ALA B CA  
4500 C C   . ALA B 228 ? 0.2196 0.3332 0.3807 -0.0072 -0.0208 0.0046  884  ALA B C   
4501 O O   . ALA B 228 ? 0.1894 0.2952 0.3429 -0.0096 -0.0193 0.0109  884  ALA B O   
4502 C CB  . ALA B 228 ? 0.1645 0.2769 0.3411 -0.0082 -0.0191 0.0015  884  ALA B CB  
4503 N N   . PRO B 229 ? 0.1753 0.2916 0.3372 -0.0040 -0.0250 0.0012  885  PRO B N   
4504 C CA  . PRO B 229 ? 0.1858 0.3015 0.3423 -0.0027 -0.0281 0.0061  885  PRO B CA  
4505 C C   . PRO B 229 ? 0.2577 0.3670 0.4197 0.0000  -0.0289 0.0118  885  PRO B C   
4506 O O   . PRO B 229 ? 0.2295 0.3393 0.4016 0.0009  -0.0306 0.0099  885  PRO B O   
4507 C CB  . PRO B 229 ? 0.1970 0.3192 0.3522 -0.0024 -0.0330 0.0004  885  PRO B CB  
4508 C CG  . PRO B 229 ? 0.2331 0.3525 0.3956 -0.0023 -0.0334 -0.0065 885  PRO B CG  
4509 C CD  . PRO B 229 ? 0.1778 0.2965 0.3433 -0.0020 -0.0275 -0.0065 885  PRO B CD  
4510 N N   . VAL B 230 ? 0.2402 0.3424 0.3942 0.0021  -0.0269 0.0194  886  VAL B N   
4511 C CA  . VAL B 230 ? 0.2558 0.3507 0.4118 0.0079  -0.0261 0.0255  886  VAL B CA  
4512 C C   . VAL B 230 ? 0.2671 0.3765 0.4333 0.0121  -0.0314 0.0274  886  VAL B C   
4513 O O   . VAL B 230 ? 0.2329 0.3435 0.4076 0.0159  -0.0311 0.0299  886  VAL B O   
4514 C CB  . VAL B 230 ? 0.3422 0.4213 0.4835 0.0109  -0.0223 0.0332  886  VAL B CB  
4515 C CG1 . VAL B 230 ? 0.3581 0.4423 0.4901 0.0107  -0.0239 0.0370  886  VAL B CG1 
4516 C CG2 . VAL B 230 ? 0.3428 0.4136 0.4835 0.0209  -0.0204 0.0399  886  VAL B CG2 
4517 N N   . THR B 231 ? 0.2251 0.3470 0.3902 0.0095  -0.0365 0.0258  887  THR B N   
4518 C CA  . THR B 231 ? 0.2206 0.3586 0.3938 0.0094  -0.0432 0.0278  887  THR B CA  
4519 C C   . THR B 231 ? 0.2644 0.4054 0.4476 0.0036  -0.0466 0.0206  887  THR B C   
4520 O O   . THR B 231 ? 0.2859 0.4396 0.4767 0.0013  -0.0523 0.0231  887  THR B O   
4521 C CB  . THR B 231 ? 0.3506 0.4992 0.5156 0.0075  -0.0482 0.0292  887  THR B CB  
4522 O OG1 . THR B 231 ? 0.3772 0.5226 0.5350 0.0010  -0.0491 0.0192  887  THR B OG1 
4523 C CG2 . THR B 231 ? 0.3151 0.4602 0.4696 0.0137  -0.0451 0.0381  887  THR B CG2 
4524 N N   . GLY B 232 ? 0.2198 0.3499 0.4029 0.0012  -0.0433 0.0132  888  GLY B N   
4525 C CA  . GLY B 232 ? 0.1925 0.3209 0.3829 -0.0031 -0.0458 0.0071  888  GLY B CA  
4526 C C   . GLY B 232 ? 0.2155 0.3441 0.4175 -0.0013 -0.0443 0.0111  888  GLY B C   
4527 O O   . GLY B 232 ? 0.2337 0.3591 0.4414 -0.0048 -0.0457 0.0071  888  GLY B O   
4528 N N   . TYR B 233 ? 0.1477 0.2782 0.3513 0.0050  -0.0408 0.0191  889  TYR B N   
4529 C CA  . TYR B 233 ? 0.1328 0.2636 0.3446 0.0089  -0.0378 0.0237  889  TYR B CA  
4530 C C   . TYR B 233 ? 0.1949 0.3371 0.4089 0.0167  -0.0373 0.0338  889  TYR B C   
4531 O O   . TYR B 233 ? 0.1947 0.3330 0.3993 0.0223  -0.0352 0.0377  889  TYR B O   
4532 C CB  . TYR B 233 ? 0.1480 0.2620 0.3537 0.0112  -0.0311 0.0217  889  TYR B CB  
4533 C CG  . TYR B 233 ? 0.1602 0.2670 0.3624 0.0055  -0.0307 0.0139  889  TYR B CG  
4534 C CD1 . TYR B 233 ? 0.1832 0.2894 0.3925 0.0022  -0.0316 0.0093  889  TYR B CD1 
4535 C CD2 . TYR B 233 ? 0.1702 0.2728 0.3622 0.0042  -0.0290 0.0123  889  TYR B CD2 
4536 C CE1 . TYR B 233 ? 0.1975 0.3001 0.4044 -0.0003 -0.0306 0.0033  889  TYR B CE1 
4537 C CE2 . TYR B 233 ? 0.1797 0.2814 0.3701 0.0004  -0.0279 0.0064  889  TYR B CE2 
4538 C CZ  . TYR B 233 ? 0.2400 0.3422 0.4381 -0.0008 -0.0286 0.0021  889  TYR B CZ  
4539 O OH  . TYR B 233 ? 0.2307 0.3346 0.4276 -0.0019 -0.0269 -0.0025 889  TYR B OH  
4540 N N   . MET B 234 ? 0.1409 0.2982 0.3672 0.0178  -0.0389 0.0391  890  MET B N   
4541 C CA  . MET B 234 ? 0.1276 0.3034 0.3595 0.0265  -0.0385 0.0504  890  MET B CA  
4542 C C   . MET B 234 ? 0.1936 0.3573 0.4145 0.0404  -0.0309 0.0561  890  MET B C   
4543 O O   . MET B 234 ? 0.2130 0.3869 0.4317 0.0476  -0.0317 0.0638  890  MET B O   
4544 C CB  . MET B 234 ? 0.1421 0.3354 0.3889 0.0261  -0.0389 0.0556  890  MET B CB  
4545 C CG  . MET B 234 ? 0.1743 0.3980 0.4311 0.0320  -0.0412 0.0681  890  MET B CG  
4546 S SD  . MET B 234 ? 0.2064 0.4559 0.4818 0.0303  -0.0412 0.0759  890  MET B SD  
4547 C CE  . MET B 234 ? 0.1372 0.4235 0.4216 0.0459  -0.0397 0.0937  890  MET B CE  
4548 N N   . PHE B 235 ? 0.1741 0.3149 0.3863 0.0438  -0.0239 0.0526  891  PHE B N   
4549 C CA  . PHE B 235 ? 0.1754 0.2959 0.3718 0.0556  -0.0163 0.0566  891  PHE B CA  
4550 C C   . PHE B 235 ? 0.2160 0.3089 0.3957 0.0492  -0.0144 0.0495  891  PHE B C   
4551 O O   . PHE B 235 ? 0.2166 0.2847 0.3807 0.0533  -0.0083 0.0494  891  PHE B O   
4552 C CB  . PHE B 235 ? 0.1950 0.3121 0.3918 0.0656  -0.0095 0.0601  891  PHE B CB  
4553 C CG  . PHE B 235 ? 0.1932 0.3415 0.4057 0.0743  -0.0100 0.0703  891  PHE B CG  
4554 C CD1 . PHE B 235 ? 0.2252 0.3849 0.4361 0.0879  -0.0085 0.0809  891  PHE B CD1 
4555 C CD2 . PHE B 235 ? 0.1997 0.3682 0.4290 0.0686  -0.0122 0.0706  891  PHE B CD2 
4556 C CE1 . PHE B 235 ? 0.2074 0.4026 0.4350 0.0960  -0.0092 0.0921  891  PHE B CE1 
4557 C CE2 . PHE B 235 ? 0.2068 0.4084 0.4516 0.0750  -0.0127 0.0815  891  PHE B CE2 
4558 C CZ  . PHE B 235 ? 0.1738 0.3907 0.4186 0.0887  -0.0113 0.0923  891  PHE B CZ  
4559 N N   . GLY B 236 ? 0.1583 0.2561 0.3397 0.0388  -0.0195 0.0442  892  GLY B N   
4560 C CA  . GLY B 236 ? 0.1584 0.2378 0.3269 0.0315  -0.0181 0.0388  892  GLY B CA  
4561 C C   . GLY B 236 ? 0.2058 0.2772 0.3761 0.0239  -0.0166 0.0316  892  GLY B C   
4562 O O   . GLY B 236 ? 0.1878 0.2684 0.3704 0.0229  -0.0179 0.0295  892  GLY B O   
4563 N N   . LYS B 237 ? 0.1653 0.2206 0.3228 0.0179  -0.0142 0.0291  893  LYS B N   
4564 C CA  . LYS B 237 ? 0.1535 0.2049 0.3121 0.0095  -0.0136 0.0234  893  LYS B CA  
4565 C C   . LYS B 237 ? 0.1847 0.2167 0.3327 0.0104  -0.0093 0.0241  893  LYS B C   
4566 O O   . LYS B 237 ? 0.1801 0.1918 0.3102 0.0066  -0.0067 0.0251  893  LYS B O   
4567 C CB  . LYS B 237 ? 0.1722 0.2244 0.3252 0.0002  -0.0143 0.0209  893  LYS B CB  
4568 C CG  . LYS B 237 ? 0.2361 0.3073 0.3991 -0.0008 -0.0180 0.0177  893  LYS B CG  
4569 C CD  . LYS B 237 ? 0.2436 0.3196 0.4021 -0.0082 -0.0172 0.0155  893  LYS B CD  
4570 C CE  . LYS B 237 ? 0.2509 0.3201 0.3952 -0.0101 -0.0158 0.0203  893  LYS B CE  
4571 N NZ  . LYS B 237 ? 0.4166 0.4951 0.5578 -0.0181 -0.0146 0.0194  893  LYS B NZ  
4572 N N   . GLY B 238 ? 0.1428 0.1807 0.3005 0.0140  -0.0090 0.0234  894  GLY B N   
4573 C CA  . GLY B 238 ? 0.1523 0.1740 0.3001 0.0154  -0.0049 0.0232  894  GLY B CA  
4574 C C   . GLY B 238 ? 0.1981 0.2327 0.3601 0.0126  -0.0065 0.0203  894  GLY B C   
4575 O O   . GLY B 238 ? 0.1831 0.2346 0.3599 0.0081  -0.0107 0.0178  894  GLY B O   
4576 N N   . ILE B 239 ? 0.1527 0.1770 0.3078 0.0156  -0.0028 0.0207  895  ILE B N   
4577 C CA  . ILE B 239 ? 0.1538 0.1894 0.3208 0.0137  -0.0038 0.0194  895  ILE B CA  
4578 C C   . ILE B 239 ? 0.2110 0.2567 0.3861 0.0245  -0.0013 0.0243  895  ILE B C   
4579 O O   . ILE B 239 ? 0.1942 0.2278 0.3566 0.0341  0.0044  0.0274  895  ILE B O   
4580 C CB  . ILE B 239 ? 0.1986 0.2208 0.3531 0.0069  -0.0025 0.0164  895  ILE B CB  
4581 C CG1 . ILE B 239 ? 0.2133 0.2294 0.3593 -0.0051 -0.0051 0.0135  895  ILE B CG1 
4582 C CG2 . ILE B 239 ? 0.1638 0.2015 0.3332 0.0048  -0.0046 0.0161  895  ILE B CG2 
4583 C CD1 . ILE B 239 ? 0.2395 0.2378 0.3662 -0.0137 -0.0041 0.0115  895  ILE B CD1 
4584 N N   . TYR B 240 ? 0.1688 0.2362 0.3638 0.0232  -0.0053 0.0257  896  TYR B N   
4585 C CA  . TYR B 240 ? 0.1495 0.2337 0.3559 0.0305  -0.0042 0.0319  896  TYR B CA  
4586 C C   . TYR B 240 ? 0.1833 0.2726 0.3942 0.0308  -0.0019 0.0336  896  TYR B C   
4587 O O   . TYR B 240 ? 0.1659 0.2557 0.3817 0.0226  -0.0050 0.0304  896  TYR B O   
4588 C CB  . TYR B 240 ? 0.1620 0.2660 0.3849 0.0261  -0.0109 0.0332  896  TYR B CB  
4589 C CG  . TYR B 240 ? 0.1721 0.2768 0.3916 0.0278  -0.0131 0.0336  896  TYR B CG  
4590 C CD1 . TYR B 240 ? 0.1931 0.2838 0.4023 0.0234  -0.0138 0.0283  896  TYR B CD1 
4591 C CD2 . TYR B 240 ? 0.1820 0.3051 0.4098 0.0324  -0.0150 0.0402  896  TYR B CD2 
4592 C CE1 . TYR B 240 ? 0.2115 0.3034 0.4167 0.0245  -0.0157 0.0292  896  TYR B CE1 
4593 C CE2 . TYR B 240 ? 0.1876 0.3128 0.4118 0.0336  -0.0176 0.0412  896  TYR B CE2 
4594 C CZ  . TYR B 240 ? 0.2409 0.3491 0.4531 0.0298  -0.0178 0.0354  896  TYR B CZ  
4595 O OH  . TYR B 240 ? 0.1163 0.2265 0.3238 0.0306  -0.0201 0.0368  896  TYR B OH  
4596 N N   . PHE B 241 ? 0.1023 0.1966 0.3112 0.0414  0.0040  0.0396  897  PHE B N   
4597 C CA  . PHE B 241 ? 0.1024 0.2035 0.3139 0.0438  0.0078  0.0426  897  PHE B CA  
4598 C C   . PHE B 241 ? 0.1588 0.2871 0.3852 0.0510  0.0095  0.0521  897  PHE B C   
4599 O O   . PHE B 241 ? 0.1433 0.2808 0.3724 0.0584  0.0100  0.0567  897  PHE B O   
4600 C CB  . PHE B 241 ? 0.1397 0.2168 0.3274 0.0513  0.0159  0.0404  897  PHE B CB  
4601 C CG  . PHE B 241 ? 0.1659 0.2189 0.3379 0.0415  0.0138  0.0323  897  PHE B CG  
4602 C CD1 . PHE B 241 ? 0.2070 0.2595 0.3793 0.0329  0.0118  0.0295  897  PHE B CD1 
4603 C CD2 . PHE B 241 ? 0.2072 0.2411 0.3653 0.0398  0.0131  0.0286  897  PHE B CD2 
4604 C CE1 . PHE B 241 ? 0.2194 0.2558 0.3794 0.0228  0.0089  0.0235  897  PHE B CE1 
4605 C CE2 . PHE B 241 ? 0.2544 0.2713 0.3999 0.0284  0.0105  0.0225  897  PHE B CE2 
4606 C CZ  . PHE B 241 ? 0.2188 0.2389 0.3662 0.0200  0.0081  0.0202  897  PHE B CZ  
4607 N N   . ALA B 242 ? 0.1502 0.2934 0.3860 0.0489  0.0106  0.0564  898  ALA B N   
4608 C CA  . ALA B 242 ? 0.1275 0.3019 0.3789 0.0539  0.0124  0.0671  898  ALA B CA  
4609 C C   . ALA B 242 ? 0.1591 0.3371 0.4045 0.0628  0.0215  0.0714  898  ALA B C   
4610 O O   . ALA B 242 ? 0.1331 0.2933 0.3671 0.0593  0.0232  0.0660  898  ALA B O   
4611 C CB  . ALA B 242 ? 0.1224 0.3159 0.3937 0.0385  0.0032  0.0696  898  ALA B CB  
4612 N N   . ASP B 243 ? 0.1338 0.3387 0.3876 0.0742  0.0272  0.0821  899  ASP B N   
4613 C CA  . ASP B 243 ? 0.1325 0.3468 0.3820 0.0844  0.0368  0.0877  899  ASP B CA  
4614 C C   . ASP B 243 ? 0.1952 0.4437 0.4672 0.0737  0.0334  0.0970  899  ASP B C   
4615 O O   . ASP B 243 ? 0.2024 0.4631 0.4733 0.0795  0.0407  0.1027  899  ASP B O   
4616 C CB  . ASP B 243 ? 0.1545 0.3730 0.3936 0.1080  0.0483  0.0937  899  ASP B CB  
4617 C CG  . ASP B 243 ? 0.2081 0.4611 0.4655 0.1157  0.0472  0.1050  899  ASP B CG  
4618 O OD1 . ASP B 243 ? 0.1444 0.4279 0.4258 0.1016  0.0384  0.1110  899  ASP B OD1 
4619 O OD2 . ASP B 243 ? 0.3684 0.6181 0.6149 0.1359  0.0554  0.1086  899  ASP B OD2 
4620 N N   . MET B 244 ? 0.1531 0.4159 0.4435 0.0576  0.0222  0.0988  900  MET B N   
4621 C CA  . MET B 244 ? 0.1168 0.4063 0.4265 0.0427  0.0165  0.1071  900  MET B CA  
4622 C C   . MET B 244 ? 0.1341 0.3978 0.4403 0.0264  0.0085  0.0980  900  MET B C   
4623 O O   . MET B 244 ? 0.1113 0.3598 0.4166 0.0190  0.0008  0.0908  900  MET B O   
4624 C CB  . MET B 244 ? 0.1330 0.4539 0.4621 0.0351  0.0090  0.1156  900  MET B CB  
4625 C CG  . MET B 244 ? 0.1836 0.5400 0.5211 0.0513  0.0161  0.1280  900  MET B CG  
4626 S SD  . MET B 244 ? 0.2510 0.6419 0.5960 0.0608  0.0273  0.1419  900  MET B SD  
4627 C CE  . MET B 244 ? 0.1957 0.6312 0.5684 0.0375  0.0165  0.1557  900  MET B CE  
4628 N N   . VAL B 245 ? 0.0951 0.3553 0.3989 0.0219  0.0105  0.0993  901  VAL B N   
4629 C CA  . VAL B 245 ? 0.1002 0.3375 0.4000 0.0093  0.0041  0.0927  901  VAL B CA  
4630 C C   . VAL B 245 ? 0.1386 0.3743 0.4488 -0.0063 -0.0073 0.0918  901  VAL B C   
4631 O O   . VAL B 245 ? 0.1404 0.3513 0.4438 -0.0106 -0.0123 0.0824  901  VAL B O   
4632 C CB  . VAL B 245 ? 0.1476 0.3880 0.4454 0.0066  0.0077  0.0978  901  VAL B CB  
4633 C CG1 . VAL B 245 ? 0.1281 0.3984 0.4429 -0.0034 0.0056  0.1111  901  VAL B CG1 
4634 C CG2 . VAL B 245 ? 0.1513 0.3642 0.4405 -0.0009 0.0028  0.0901  901  VAL B CG2 
4635 N N   . SER B 246 ? 0.0809 0.3433 0.4061 -0.0147 -0.0113 0.1015  902  SER B N   
4636 C CA  . SER B 246 ? 0.0702 0.3304 0.4021 -0.0317 -0.0224 0.1013  902  SER B CA  
4637 C C   . SER B 246 ? 0.1162 0.3640 0.4438 -0.0304 -0.0272 0.0924  902  SER B C   
4638 O O   . SER B 246 ? 0.0934 0.3215 0.4170 -0.0408 -0.0351 0.0858  902  SER B O   
4639 C CB  . SER B 246 ? 0.0843 0.3792 0.4319 -0.0429 -0.0254 0.1154  902  SER B CB  
4640 O OG  . SER B 246 ? 0.1186 0.4477 0.4760 -0.0341 -0.0215 0.1236  902  SER B OG  
4641 N N   . LYS B 247 ? 0.0847 0.3422 0.4109 -0.0164 -0.0218 0.0922  903  LYS B N   
4642 C CA  . LYS B 247 ? 0.0699 0.3159 0.3906 -0.0138 -0.0253 0.0844  903  LYS B CA  
4643 C C   . LYS B 247 ? 0.1189 0.3297 0.4258 -0.0132 -0.0259 0.0717  903  LYS B C   
4644 O O   . LYS B 247 ? 0.1330 0.3304 0.4367 -0.0197 -0.0323 0.0648  903  LYS B O   
4645 C CB  . LYS B 247 ? 0.0730 0.3324 0.3925 0.0027  -0.0183 0.0878  903  LYS B CB  
4646 C CG  . LYS B 247 ? 0.0477 0.2508 0.3168 0.0037  -0.0179 0.0804  903  LYS B CG  
4647 C CD  . LYS B 247 ? 0.0413 0.2062 0.2538 0.0092  -0.0089 0.0871  903  LYS B CD  
4648 C CE  . LYS B 247 ? 0.0689 0.3192 0.3739 0.0217  -0.0201 0.0806  903  LYS B CE  
4649 N NZ  . LYS B 247 ? 0.0952 0.3674 0.4038 0.0331  -0.0183 0.0892  903  LYS B NZ  
4650 N N   . SER B 248 ? 0.0665 0.2642 0.3648 -0.0054 -0.0191 0.0689  904  SER B N   
4651 C CA  . SER B 248 ? 0.0707 0.2414 0.3577 -0.0054 -0.0197 0.0588  904  SER B CA  
4652 C C   . SER B 248 ? 0.1209 0.2810 0.4099 -0.0160 -0.0254 0.0574  904  SER B C   
4653 O O   . SER B 248 ? 0.1036 0.2467 0.3874 -0.0180 -0.0290 0.0498  904  SER B O   
4654 C CB  . SER B 248 ? 0.1137 0.2754 0.3893 0.0039  -0.0118 0.0572  904  SER B CB  
4655 O OG  . SER B 248 ? 0.1681 0.3257 0.4349 0.0139  -0.0072 0.0548  904  SER B OG  
4656 N N   . ALA B 249 ? 0.1044 0.2747 0.4004 -0.0222 -0.0260 0.0653  905  ALA B N   
4657 C CA  . ALA B 249 ? 0.1019 0.2592 0.3980 -0.0320 -0.0312 0.0656  905  ALA B CA  
4658 C C   . ALA B 249 ? 0.1570 0.3044 0.4533 -0.0416 -0.0396 0.0620  905  ALA B C   
4659 O O   . ALA B 249 ? 0.1841 0.3106 0.4747 -0.0458 -0.0435 0.0583  905  ALA B O   
4660 C CB  . ALA B 249 ? 0.1054 0.2770 0.4082 -0.0375 -0.0299 0.0764  905  ALA B CB  
4661 N N   . ASN B 250 ? 0.0946 0.2554 0.3951 -0.0439 -0.0422 0.0626  906  ASN B N   
4662 C CA  . ASN B 250 ? 0.0927 0.2436 0.3898 -0.0532 -0.0503 0.0580  906  ASN B CA  
4663 C C   . ASN B 250 ? 0.1685 0.2960 0.4545 -0.0461 -0.0501 0.0462  906  ASN B C   
4664 O O   . ASN B 250 ? 0.1724 0.2815 0.4508 -0.0519 -0.0555 0.0404  906  ASN B O   
4665 C CB  . ASN B 250 ? 0.1246 0.3001 0.4290 -0.0562 -0.0529 0.0626  906  ASN B CB  
4666 C CG  . ASN B 250 ? 0.3051 0.5068 0.6212 -0.0680 -0.0562 0.0750  906  ASN B CG  
4667 O OD1 . ASN B 250 ? 0.2821 0.5104 0.6064 -0.0698 -0.0582 0.0811  906  ASN B OD1 
4668 N ND2 . ASN B 250 ? 0.1503 0.3475 0.4679 -0.0766 -0.0572 0.0802  906  ASN B ND2 
4669 N N   . TYR B 251 ? 0.1425 0.2702 0.4260 -0.0341 -0.0435 0.0429  907  TYR B N   
4670 C CA  . TYR B 251 ? 0.1379 0.2491 0.4125 -0.0278 -0.0424 0.0337  907  TYR B CA  
4671 C C   . TYR B 251 ? 0.1803 0.2746 0.4506 -0.0266 -0.0423 0.0313  907  TYR B C   
4672 O O   . TYR B 251 ? 0.1704 0.2544 0.4347 -0.0215 -0.0416 0.0248  907  TYR B O   
4673 C CB  . TYR B 251 ? 0.1488 0.2660 0.4208 -0.0184 -0.0365 0.0321  907  TYR B CB  
4674 C CG  . TYR B 251 ? 0.1735 0.3005 0.4459 -0.0172 -0.0375 0.0321  907  TYR B CG  
4675 C CD1 . TYR B 251 ? 0.2157 0.3350 0.4822 -0.0180 -0.0406 0.0255  907  TYR B CD1 
4676 C CD2 . TYR B 251 ? 0.1764 0.3221 0.4549 -0.0146 -0.0352 0.0397  907  TYR B CD2 
4677 C CE1 . TYR B 251 ? 0.2183 0.3475 0.4847 -0.0175 -0.0422 0.0264  907  TYR B CE1 
4678 C CE2 . TYR B 251 ? 0.1788 0.3357 0.4583 -0.0127 -0.0366 0.0413  907  TYR B CE2 
4679 C CZ  . TYR B 251 ? 0.2827 0.4310 0.5560 -0.0149 -0.0406 0.0347  907  TYR B CZ  
4680 O OH  . TYR B 251 ? 0.3311 0.4911 0.6046 -0.0130 -0.0423 0.0369  907  TYR B OH  
4681 N N   . CYS B 252 ? 0.1627 0.2563 0.4363 -0.0309 -0.0428 0.0376  908  CYS B N   
4682 C CA  . CYS B 252 ? 0.1679 0.2462 0.4375 -0.0293 -0.0432 0.0374  908  CYS B CA  
4683 C C   . CYS B 252 ? 0.2793 0.3357 0.5415 -0.0329 -0.0484 0.0331  908  CYS B C   
4684 O O   . CYS B 252 ? 0.2803 0.3217 0.5367 -0.0268 -0.0479 0.0304  908  CYS B O   
4685 C CB  . CYS B 252 ? 0.1583 0.2426 0.4323 -0.0328 -0.0419 0.0464  908  CYS B CB  
4686 S SG  . CYS B 252 ? 0.1918 0.2960 0.4688 -0.0266 -0.0346 0.0503  908  CYS B SG  
4687 N N   . HIS B 253 ? 0.2819 0.3365 0.5430 -0.0426 -0.0535 0.0328  909  HIS B N   
4688 C CA  . HIS B 253 ? 0.3030 0.3327 0.5524 -0.0485 -0.0592 0.0278  909  HIS B CA  
4689 C C   . HIS B 253 ? 0.3917 0.3982 0.6344 -0.0502 -0.0607 0.0311  909  HIS B C   
4690 O O   . HIS B 253 ? 0.4039 0.3845 0.6341 -0.0442 -0.0611 0.0254  909  HIS B O   
4691 C CB  . HIS B 253 ? 0.3202 0.3402 0.5605 -0.0402 -0.0583 0.0173  909  HIS B CB  
4692 C CG  . HIS B 253 ? 0.3613 0.3993 0.6050 -0.0421 -0.0589 0.0151  909  HIS B CG  
4693 N ND1 . HIS B 253 ? 0.3871 0.4225 0.6255 -0.0529 -0.0653 0.0133  909  HIS B ND1 
4694 C CD2 . HIS B 253 ? 0.3726 0.4303 0.6232 -0.0350 -0.0542 0.0153  909  HIS B CD2 
4695 C CE1 . HIS B 253 ? 0.3676 0.4234 0.6114 -0.0506 -0.0641 0.0132  909  HIS B CE1 
4696 N NE2 . HIS B 253 ? 0.3660 0.4338 0.6165 -0.0395 -0.0572 0.0142  909  HIS B NE2 
4697 N N   . THR B 254 ? 0.3530 0.3697 0.6035 -0.0573 -0.0609 0.0410  910  THR B N   
4698 C CA  . THR B 254 ? 0.3625 0.3593 0.6073 -0.0609 -0.0626 0.0468  910  THR B CA  
4699 C C   . THR B 254 ? 0.4537 0.4294 0.6881 -0.0774 -0.0703 0.0475  910  THR B C   
4700 O O   . THR B 254 ? 0.4365 0.4210 0.6715 -0.0867 -0.0743 0.0450  910  THR B O   
4701 C CB  . THR B 254 ? 0.3484 0.3668 0.6048 -0.0623 -0.0592 0.0577  910  THR B CB  
4702 O OG1 . THR B 254 ? 0.3040 0.3489 0.5710 -0.0719 -0.0598 0.0631  910  THR B OG1 
4703 C CG2 . THR B 254 ? 0.2579 0.2895 0.5191 -0.0478 -0.0526 0.0566  910  THR B CG2 
4704 N N   . SER B 255 ? 0.4477 0.3939 0.6706 -0.0816 -0.0730 0.0510  911  SER B N   
4705 C CA  . SER B 255 ? 0.4671 0.3861 0.6756 -0.0996 -0.0809 0.0521  911  SER B CA  
4706 C C   . SER B 255 ? 0.5146 0.4152 0.7180 -0.1052 -0.0819 0.0621  911  SER B C   
4707 O O   . SER B 255 ? 0.4885 0.4021 0.7012 -0.0948 -0.0765 0.0681  911  SER B O   
4708 C CB  . SER B 255 ? 0.5526 0.4340 0.7389 -0.0954 -0.0834 0.0396  911  SER B CB  
4709 O OG  . SER B 255 ? 0.7539 0.6139 0.9317 -0.0754 -0.0780 0.0354  911  SER B OG  
4710 N N   . GLN B 256 ? 0.5132 0.3828 0.7003 -0.1227 -0.0892 0.0643  912  GLN B N   
4711 C CA  . GLN B 256 ? 0.5351 0.3795 0.7128 -0.1308 -0.0914 0.0744  912  GLN B CA  
4712 C C   . GLN B 256 ? 0.5977 0.4097 0.7624 -0.1094 -0.0866 0.0710  912  GLN B C   
4713 O O   . GLN B 256 ? 0.6063 0.4125 0.7714 -0.1066 -0.0848 0.0809  912  GLN B O   
4714 C CB  . GLN B 256 ? 0.5694 0.3802 0.7267 -0.1554 -0.1012 0.0749  912  GLN B CB  
4715 C CG  . GLN B 256 ? 0.7796 0.6200 0.9459 -0.1739 -0.1070 0.0740  912  GLN B CG  
4716 C CD  . GLN B 256 ? 1.0802 0.9541 1.2624 -0.1954 -0.1105 0.0895  912  GLN B CD  
4717 O OE1 . GLN B 256 ? 1.0207 0.9002 1.2093 -0.1965 -0.1077 0.1011  912  GLN B OE1 
4718 N NE2 . GLN B 256 ? 1.0015 0.8987 1.1891 -0.2146 -0.1173 0.0910  912  GLN B NE2 
4719 N N   . GLY B 257 ? 0.5543 0.3494 0.7085 -0.0939 -0.0844 0.0581  913  GLY B N   
4720 C CA  . GLY B 257 ? 0.5582 0.3275 0.7008 -0.0706 -0.0792 0.0541  913  GLY B CA  
4721 C C   . GLY B 257 ? 0.5770 0.3826 0.7394 -0.0506 -0.0716 0.0555  913  GLY B C   
4722 O O   . GLY B 257 ? 0.5936 0.3857 0.7499 -0.0313 -0.0673 0.0552  913  GLY B O   
4723 N N   . ASP B 258 ? 0.4738 0.3255 0.6586 -0.0548 -0.0698 0.0572  914  ASP B N   
4724 C CA  . ASP B 258 ? 0.4369 0.3242 0.6392 -0.0405 -0.0635 0.0586  914  ASP B CA  
4725 C C   . ASP B 258 ? 0.4443 0.3705 0.6649 -0.0520 -0.0631 0.0644  914  ASP B C   
4726 O O   . ASP B 258 ? 0.4233 0.3716 0.6522 -0.0526 -0.0620 0.0587  914  ASP B O   
4727 C CB  . ASP B 258 ? 0.4521 0.3454 0.6540 -0.0253 -0.0598 0.0473  914  ASP B CB  
4728 N N   . PRO B 259 ? 0.3835 0.3175 0.6092 -0.0611 -0.0636 0.0762  915  PRO B N   
4729 C CA  . PRO B 259 ? 0.3574 0.3280 0.5987 -0.0707 -0.0623 0.0819  915  PRO B CA  
4730 C C   . PRO B 259 ? 0.3647 0.3663 0.6177 -0.0597 -0.0557 0.0836  915  PRO B C   
4731 O O   . PRO B 259 ? 0.3460 0.3744 0.6089 -0.0651 -0.0532 0.0894  915  PRO B O   
4732 C CB  . PRO B 259 ? 0.3764 0.3394 0.6153 -0.0869 -0.0659 0.0941  915  PRO B CB  
4733 C CG  . PRO B 259 ? 0.4504 0.3802 0.6758 -0.0798 -0.0665 0.0972  915  PRO B CG  
4734 C CD  . PRO B 259 ? 0.4057 0.3151 0.6218 -0.0630 -0.0653 0.0856  915  PRO B CD  
4735 N N   . ILE B 260 ? 0.3082 0.3068 0.5588 -0.0447 -0.0527 0.0788  916  ILE B N   
4736 C CA  . ILE B 260 ? 0.2758 0.2996 0.5334 -0.0362 -0.0476 0.0797  916  ILE B CA  
4737 C C   . ILE B 260 ? 0.2907 0.3269 0.5516 -0.0300 -0.0452 0.0695  916  ILE B C   
4738 O O   . ILE B 260 ? 0.2809 0.3053 0.5372 -0.0229 -0.0460 0.0621  916  ILE B O   
4739 C CB  . ILE B 260 ? 0.3112 0.3296 0.5649 -0.0261 -0.0466 0.0843  916  ILE B CB  
4740 C CG1 . ILE B 260 ? 0.3218 0.3157 0.5678 -0.0298 -0.0499 0.0933  916  ILE B CG1 
4741 C CG2 . ILE B 260 ? 0.3178 0.3623 0.5763 -0.0236 -0.0426 0.0879  916  ILE B CG2 
4742 C CD1 . ILE B 260 ? 0.4720 0.4709 0.7201 -0.0442 -0.0509 0.1042  916  ILE B CD1 
4743 N N   . GLY B 261 ? 0.2366 0.2957 0.5038 -0.0320 -0.0418 0.0699  917  GLY B N   
4744 C CA  . GLY B 261 ? 0.2059 0.2761 0.4747 -0.0270 -0.0392 0.0617  917  GLY B CA  
4745 C C   . GLY B 261 ? 0.1995 0.2846 0.4675 -0.0216 -0.0344 0.0618  917  GLY B C   
4746 O O   . GLY B 261 ? 0.1825 0.2733 0.4496 -0.0222 -0.0328 0.0684  917  GLY B O   
4747 N N   . LEU B 262 ? 0.1443 0.2340 0.4107 -0.0171 -0.0325 0.0545  918  LEU B N   
4748 C CA  . LEU B 262 ? 0.1250 0.2241 0.3865 -0.0138 -0.0284 0.0528  918  LEU B CA  
4749 C C   . LEU B 262 ? 0.1286 0.2335 0.3887 -0.0130 -0.0250 0.0489  918  LEU B C   
4750 O O   . LEU B 262 ? 0.0814 0.1840 0.3440 -0.0129 -0.0265 0.0445  918  LEU B O   
4751 C CB  . LEU B 262 ? 0.1244 0.2219 0.3823 -0.0096 -0.0296 0.0490  918  LEU B CB  
4752 C CG  . LEU B 262 ? 0.1659 0.2619 0.4240 -0.0073 -0.0320 0.0542  918  LEU B CG  
4753 C CD1 . LEU B 262 ? 0.1648 0.2646 0.4223 -0.0020 -0.0332 0.0510  918  LEU B CD1 
4754 C CD2 . LEU B 262 ? 0.1611 0.2649 0.4150 -0.0096 -0.0305 0.0603  918  LEU B CD2 
4755 N N   . ILE B 263 ? 0.0825 0.1939 0.3372 -0.0117 -0.0202 0.0509  919  ILE B N   
4756 C CA  . ILE B 263 ? 0.1142 0.2291 0.3656 -0.0083 -0.0159 0.0485  919  ILE B CA  
4757 C C   . ILE B 263 ? 0.1685 0.2792 0.4050 -0.0051 -0.0112 0.0457  919  ILE B C   
4758 O O   . ILE B 263 ? 0.1532 0.2644 0.3835 -0.0062 -0.0100 0.0484  919  ILE B O   
4759 C CB  . ILE B 263 ? 0.1438 0.2714 0.4036 -0.0087 -0.0140 0.0553  919  ILE B CB  
4760 C CG1 . ILE B 263 ? 0.1617 0.2949 0.4205 -0.0030 -0.0102 0.0538  919  ILE B CG1 
4761 C CG2 . ILE B 263 ? 0.1557 0.2912 0.4136 -0.0088 -0.0101 0.0625  919  ILE B CG2 
4762 C CD1 . ILE B 263 ? 0.2108 0.3623 0.4817 -0.0044 -0.0101 0.0614  919  ILE B CD1 
4763 N N   . LEU B 264 ? 0.1153 0.2193 0.3438 -0.0021 -0.0090 0.0403  920  LEU B N   
4764 C CA  . LEU B 264 ? 0.1126 0.2063 0.3222 -0.0008 -0.0049 0.0368  920  LEU B CA  
4765 C C   . LEU B 264 ? 0.1351 0.2274 0.3363 0.0071  0.0025  0.0385  920  LEU B C   
4766 O O   . LEU B 264 ? 0.1264 0.2280 0.3378 0.0118  0.0039  0.0418  920  LEU B O   
4767 C CB  . LEU B 264 ? 0.1181 0.2012 0.3196 -0.0030 -0.0067 0.0303  920  LEU B CB  
4768 C CG  . LEU B 264 ? 0.1477 0.2344 0.3558 -0.0088 -0.0127 0.0286  920  LEU B CG  
4769 C CD1 . LEU B 264 ? 0.1189 0.2010 0.3250 -0.0095 -0.0136 0.0240  920  LEU B CD1 
4770 C CD2 . LEU B 264 ? 0.1756 0.2623 0.3741 -0.0144 -0.0143 0.0290  920  LEU B CD2 
4771 N N   . LEU B 265 ? 0.1241 0.2045 0.3049 0.0088  0.0070  0.0364  921  LEU B N   
4772 C CA  . LEU B 265 ? 0.1622 0.2338 0.3266 0.0186  0.0157  0.0362  921  LEU B CA  
4773 C C   . LEU B 265 ? 0.2893 0.3349 0.4290 0.0163  0.0163  0.0285  921  LEU B C   
4774 O O   . LEU B 265 ? 0.2966 0.3331 0.4232 0.0076  0.0135  0.0252  921  LEU B O   
4775 C CB  . LEU B 265 ? 0.1604 0.2372 0.3176 0.0223  0.0212  0.0404  921  LEU B CB  
4776 C CG  . LEU B 265 ? 0.2061 0.3073 0.3820 0.0279  0.0243  0.0495  921  LEU B CG  
4777 C CD1 . LEU B 265 ? 0.2084 0.3157 0.3763 0.0297  0.0294  0.0540  921  LEU B CD1 
4778 C CD2 . LEU B 265 ? 0.2364 0.3427 0.4142 0.0404  0.0305  0.0520  921  LEU B CD2 
4779 N N   . GLY B 266 ? 0.2793 0.3144 0.4135 0.0223  0.0189  0.0265  922  GLY B N   
4780 C CA  . GLY B 266 ? 0.2945 0.3020 0.4041 0.0186  0.0192  0.0199  922  GLY B CA  
4781 C C   . GLY B 266 ? 0.3613 0.3458 0.4464 0.0313  0.0284  0.0187  922  GLY B C   
4782 O O   . GLY B 266 ? 0.3605 0.3555 0.4544 0.0451  0.0339  0.0237  922  GLY B O   
4783 N N   . GLU B 267 ? 0.3181 0.2710 0.3711 0.0268  0.0301  0.0125  923  GLU B N   
4784 C CA  . GLU B 267 ? 0.3403 0.2627 0.3640 0.0396  0.0392  0.0104  923  GLU B CA  
4785 C C   . GLU B 267 ? 0.4018 0.3108 0.4233 0.0383  0.0369  0.0093  923  GLU B C   
4786 O O   . GLU B 267 ? 0.3771 0.2763 0.3928 0.0225  0.0301  0.0054  923  GLU B O   
4787 C CB  . GLU B 267 ? 0.3763 0.2647 0.3611 0.0343  0.0420  0.0036  923  GLU B CB  
4788 C CG  . GLU B 267 ? 0.4792 0.3275 0.4283 0.0483  0.0517  0.0004  923  GLU B CG  
4789 C CD  . GLU B 267 ? 0.6730 0.4773 0.5759 0.0410  0.0538  -0.0080 923  GLU B CD  
4790 O OE1 . GLU B 267 ? 0.6316 0.4416 0.5301 0.0278  0.0493  -0.0105 923  GLU B OE1 
4791 O OE2 . GLU B 267 ? 0.7173 0.4797 0.5862 0.0485  0.0598  -0.0118 923  GLU B OE2 
4792 N N   . VAL B 268 ? 0.3755 0.2888 0.4036 0.0550  0.0425  0.0140  924  VAL B N   
4793 C CA  . VAL B 268 ? 0.3792 0.2842 0.4078 0.0565  0.0409  0.0149  924  VAL B CA  
4794 C C   . VAL B 268 ? 0.4741 0.3416 0.4694 0.0719  0.0502  0.0144  924  VAL B C   
4795 O O   . VAL B 268 ? 0.4519 0.3225 0.4443 0.0916  0.0592  0.0186  924  VAL B O   
4796 C CB  . VAL B 268 ? 0.4018 0.3460 0.4676 0.0619  0.0378  0.0220  924  VAL B CB  
4797 C CG1 . VAL B 268 ? 0.3997 0.3381 0.4669 0.0615  0.0349  0.0230  924  VAL B CG1 
4798 C CG2 . VAL B 268 ? 0.3754 0.3509 0.4698 0.0489  0.0298  0.0224  924  VAL B CG2 
4799 N N   . ALA B 269 ? 0.4751 0.3066 0.4442 0.0628  0.0482  0.0097  925  ALA B N   
4800 C CA  . ALA B 269 ? 0.5021 0.2894 0.4348 0.0757  0.0563  0.0089  925  ALA B CA  
4801 C C   . ALA B 269 ? 0.5304 0.3316 0.4800 0.0892  0.0574  0.0165  925  ALA B C   
4802 O O   . ALA B 269 ? 0.5208 0.3210 0.4755 0.0783  0.0511  0.0169  925  ALA B O   
4803 C CB  . ALA B 269 ? 0.5366 0.2811 0.4353 0.0565  0.0521  0.0018  925  ALA B CB  
4804 N N   . LEU B 270 ? 0.4772 0.2977 0.4383 0.1124  0.0651  0.0237  926  LEU B N   
4805 C CA  . LEU B 270 ? 0.4525 0.2941 0.4325 0.1265  0.0659  0.0326  926  LEU B CA  
4806 C C   . LEU B 270 ? 0.5420 0.3423 0.4898 0.1415  0.0727  0.0347  926  LEU B C   
4807 O O   . LEU B 270 ? 0.5181 0.3253 0.4751 0.1441  0.0698  0.0402  926  LEU B O   
4808 C CB  . LEU B 270 ? 0.4194 0.3069 0.4290 0.1429  0.0700  0.0415  926  LEU B CB  
4809 C CG  . LEU B 270 ? 0.4244 0.3551 0.4690 0.1283  0.0625  0.0416  926  LEU B CG  
4810 C CD1 . LEU B 270 ? 0.3939 0.3624 0.4590 0.1439  0.0684  0.0506  926  LEU B CD1 
4811 C CD2 . LEU B 270 ? 0.4201 0.3748 0.4918 0.1128  0.0512  0.0423  926  LEU B CD2 
4812 N N   . GLY B 271 ? 0.5552 0.3117 0.4638 0.1522  0.0821  0.0306  927  GLY B N   
4813 C CA  . GLY B 271 ? 0.5862 0.2942 0.4571 0.1692  0.0902  0.0323  927  GLY B CA  
4814 C C   . GLY B 271 ? 0.6344 0.3686 0.5228 0.1961  0.0960  0.0449  927  GLY B C   
4815 O O   . GLY B 271 ? 0.6169 0.3918 0.5292 0.2115  0.1007  0.0513  927  GLY B O   
4816 N N   . ASN B 272 ? 0.6048 0.3189 0.4825 0.2006  0.0951  0.0495  928  ASN B N   
4817 C CA  . ASN B 272 ? 0.5917 0.3308 0.4852 0.2251  0.0991  0.0627  928  ASN B CA  
4818 C C   . ASN B 272 ? 0.5892 0.3891 0.5315 0.2114  0.0875  0.0679  928  ASN B C   
4819 O O   . ASN B 272 ? 0.5984 0.3954 0.5457 0.1902  0.0778  0.0645  928  ASN B O   
4820 C CB  . ASN B 272 ? 0.6997 0.3861 0.5565 0.2348  0.1028  0.0655  928  ASN B CB  
4821 C CG  . ASN B 272 ? 1.0658 0.7608 0.9226 0.2688  0.1116  0.0794  928  ASN B CG  
4822 O OD1 . ASN B 272 ? 1.0424 0.7966 0.9382 0.2793  0.1100  0.0900  928  ASN B OD1 
4823 N ND2 . ASN B 272 ? 1.0281 0.6627 0.8394 0.2862  0.1207  0.0803  928  ASN B ND2 
4824 N N   . MET B 273 ? 0.4798 0.3348 0.4569 0.2223  0.0886  0.0759  929  MET B N   
4825 C CA  . MET B 273 ? 0.4248 0.3370 0.4461 0.2096  0.0778  0.0806  929  MET B CA  
4826 C C   . MET B 273 ? 0.4605 0.3937 0.4941 0.2211  0.0756  0.0923  929  MET B C   
4827 O O   . MET B 273 ? 0.4693 0.4062 0.4968 0.2482  0.0843  0.1030  929  MET B O   
4828 C CB  . MET B 273 ? 0.4194 0.3805 0.4707 0.2125  0.0788  0.0846  929  MET B CB  
4829 C CG  . MET B 273 ? 0.4573 0.4057 0.5011 0.2002  0.0799  0.0743  929  MET B CG  
4830 S SD  . MET B 273 ? 0.4661 0.4698 0.5424 0.2040  0.0821  0.0807  929  MET B SD  
4831 C CE  . MET B 273 ? 0.4326 0.4473 0.5007 0.2427  0.0976  0.0946  929  MET B CE  
4832 N N   . TYR B 274 ? 0.3827 0.3323 0.4338 0.2016  0.0640  0.0909  930  TYR B N   
4833 C CA  . TYR B 274 ? 0.3593 0.3343 0.4249 0.2076  0.0594  0.1013  930  TYR B CA  
4834 C C   . TYR B 274 ? 0.3723 0.4103 0.4787 0.2035  0.0532  0.1073  930  TYR B C   
4835 O O   . TYR B 274 ? 0.3191 0.3751 0.4443 0.1812  0.0445  0.1002  930  TYR B O   
4836 C CB  . TYR B 274 ? 0.3747 0.3288 0.4320 0.1878  0.0511  0.0955  930  TYR B CB  
4837 C CG  . TYR B 274 ? 0.3781 0.3558 0.4473 0.1913  0.0454  0.1052  930  TYR B CG  
4838 C CD1 . TYR B 274 ? 0.4018 0.3869 0.4672 0.2172  0.0511  0.1190  930  TYR B CD1 
4839 C CD2 . TYR B 274 ? 0.3768 0.3670 0.4580 0.1698  0.0348  0.1009  930  TYR B CD2 
4840 C CE1 . TYR B 274 ? 0.3916 0.4010 0.4679 0.2200  0.0451  0.1288  930  TYR B CE1 
4841 C CE2 . TYR B 274 ? 0.3677 0.3788 0.4574 0.1723  0.0294  0.1094  930  TYR B CE2 
4842 C CZ  . TYR B 274 ? 0.4519 0.4729 0.5392 0.1967  0.0340  0.1235  930  TYR B CZ  
4843 O OH  . TYR B 274 ? 0.4574 0.5012 0.5527 0.1988  0.0280  0.1328  930  TYR B OH  
4844 N N   . GLU B 275 ? 0.3443 0.4145 0.4625 0.2259  0.0587  0.1207  931  GLU B N   
4845 C CA  . GLU B 275 ? 0.3113 0.4428 0.4660 0.2238  0.0542  0.1290  931  GLU B CA  
4846 C C   . GLU B 275 ? 0.3339 0.5038 0.5116 0.2147  0.0428  0.1362  931  GLU B C   
4847 O O   . GLU B 275 ? 0.3289 0.5030 0.5018 0.2302  0.0440  0.1465  931  GLU B O   
4848 C CB  . GLU B 275 ? 0.3211 0.4739 0.4781 0.2516  0.0661  0.1411  931  GLU B CB  
4849 C CG  . GLU B 275 ? 0.4841 0.6038 0.6198 0.2579  0.0769  0.1328  931  GLU B CG  
4850 C CD  . GLU B 275 ? 0.7575 0.9037 0.8984 0.2822  0.0888  0.1431  931  GLU B CD  
4851 O OE1 . GLU B 275 ? 0.7755 0.9683 0.9367 0.2986  0.0903  0.1592  931  GLU B OE1 
4852 O OE2 . GLU B 275 ? 0.6699 0.7919 0.7940 0.2849  0.0968  0.1356  931  GLU B OE2 
4853 N N   . LEU B 276 ? 0.2650 0.4600 0.4651 0.1896  0.0316  0.1306  932  LEU B N   
4854 C CA  . LEU B 276 ? 0.2424 0.4706 0.4614 0.1768  0.0194  0.1348  932  LEU B CA  
4855 C C   . LEU B 276 ? 0.2469 0.5246 0.4964 0.1634  0.0120  0.1389  932  LEU B C   
4856 O O   . LEU B 276 ? 0.2326 0.5091 0.4876 0.1541  0.0131  0.1327  932  LEU B O   
4857 C CB  . LEU B 276 ? 0.2594 0.4576 0.4675 0.1563  0.0120  0.1216  932  LEU B CB  
4858 C CG  . LEU B 276 ? 0.3428 0.4930 0.5207 0.1640  0.0172  0.1182  932  LEU B CG  
4859 C CD1 . LEU B 276 ? 0.3484 0.4706 0.5171 0.1419  0.0119  0.1039  932  LEU B CD1 
4860 C CD2 . LEU B 276 ? 0.3650 0.5255 0.5394 0.1779  0.0162  0.1306  932  LEU B CD2 
4861 N N   . LYS B 277 ? 0.1790 0.4987 0.4464 0.1603  0.0036  0.1493  933  LYS B N   
4862 C CA  . LYS B 277 ? 0.1548 0.5227 0.4495 0.1447  -0.0054 0.1548  933  LYS B CA  
4863 C C   . LYS B 277 ? 0.2248 0.5938 0.5242 0.1172  -0.0197 0.1458  933  LYS B C   
4864 O O   . LYS B 277 ? 0.2049 0.6015 0.5215 0.0992  -0.0279 0.1465  933  LYS B O   
4865 C CB  . LYS B 277 ? 0.1503 0.5706 0.4620 0.1594  -0.0058 0.1748  933  LYS B CB  
4866 C CG  . LYS B 277 ? 0.1727 0.6034 0.4834 0.1890  0.0086  0.1868  933  LYS B CG  
4867 C CD  . LYS B 277 ? 0.2473 0.7367 0.5776 0.2028  0.0068  0.2081  933  LYS B CD  
4868 C CE  . LYS B 277 ? 0.3378 0.8376 0.6651 0.2371  0.0225  0.2212  933  LYS B CE  
4869 N NZ  . LYS B 277 ? 0.3862 0.9507 0.7357 0.2513  0.0208  0.2439  933  LYS B NZ  
4870 N N   . HIS B 278 ? 0.1806 0.5210 0.4635 0.1145  -0.0225 0.1384  934  HIS B N   
4871 C CA  . HIS B 278 ? 0.1808 0.5203 0.4636 0.0927  -0.0346 0.1302  934  HIS B CA  
4872 C C   . HIS B 278 ? 0.2350 0.5277 0.4968 0.0883  -0.0325 0.1160  934  HIS B C   
4873 O O   . HIS B 278 ? 0.2420 0.5048 0.4879 0.1025  -0.0230 0.1151  934  HIS B O   
4874 C CB  . HIS B 278 ? 0.1900 0.5611 0.4775 0.0952  -0.0420 0.1419  934  HIS B CB  
4875 C CG  . HIS B 278 ? 0.2235 0.6487 0.5340 0.0948  -0.0468 0.1568  934  HIS B CG  
4876 N ND1 . HIS B 278 ? 0.2448 0.6947 0.5641 0.1173  -0.0381 0.1719  934  HIS B ND1 
4877 C CD2 . HIS B 278 ? 0.2414 0.6995 0.5665 0.0734  -0.0593 0.1587  934  HIS B CD2 
4878 C CE1 . HIS B 278 ? 0.2220 0.7239 0.5638 0.1086  -0.0456 0.1836  934  HIS B CE1 
4879 N NE2 . HIS B 278 ? 0.2245 0.7322 0.5697 0.0810  -0.0591 0.1762  934  HIS B NE2 
4880 N N   . ALA B 279 ? 0.1845 0.4706 0.4447 0.0685  -0.0413 0.1055  935  ALA B N   
4881 C CA  . ALA B 279 ? 0.1870 0.4354 0.4298 0.0623  -0.0400 0.0924  935  ALA B CA  
4882 C C   . ALA B 279 ? 0.2660 0.4943 0.4914 0.0752  -0.0348 0.0957  935  ALA B C   
4883 O O   . ALA B 279 ? 0.2439 0.4891 0.4688 0.0833  -0.0370 0.1060  935  ALA B O   
4884 C CB  . ALA B 279 ? 0.1943 0.4457 0.4374 0.0432  -0.0501 0.0835  935  ALA B CB  
4885 N N   . SER B 280 ? 0.2611 0.4533 0.4714 0.0768  -0.0278 0.0880  936  SER B N   
4886 C CA  . SER B 280 ? 0.2627 0.4273 0.4524 0.0856  -0.0225 0.0898  936  SER B CA  
4887 C C   . SER B 280 ? 0.2645 0.3994 0.4427 0.0728  -0.0213 0.0769  936  SER B C   
4888 O O   . SER B 280 ? 0.2367 0.3524 0.4106 0.0722  -0.0161 0.0716  936  SER B O   
4889 C CB  . SER B 280 ? 0.3420 0.4939 0.5233 0.1057  -0.0127 0.0982  936  SER B CB  
4890 O OG  . SER B 280 ? 0.5104 0.6270 0.6675 0.1128  -0.0072 0.0991  936  SER B OG  
4891 N N   . HIS B 281 ? 0.2242 0.3598 0.3984 0.0621  -0.0267 0.0723  937  HIS B N   
4892 C CA  . HIS B 281 ? 0.2194 0.3361 0.3853 0.0498  -0.0263 0.0615  937  HIS B CA  
4893 C C   . HIS B 281 ? 0.3295 0.4160 0.4747 0.0529  -0.0201 0.0630  937  HIS B C   
4894 O O   . HIS B 281 ? 0.3297 0.4111 0.4641 0.0495  -0.0212 0.0642  937  HIS B O   
4895 C CB  . HIS B 281 ? 0.2052 0.3369 0.3740 0.0389  -0.0336 0.0565  937  HIS B CB  
4896 C CG  . HIS B 281 ? 0.2125 0.3693 0.3975 0.0338  -0.0406 0.0552  937  HIS B CG  
4897 N ND1 . HIS B 281 ? 0.2217 0.3787 0.4166 0.0274  -0.0412 0.0483  937  HIS B ND1 
4898 C CD2 . HIS B 281 ? 0.2057 0.3872 0.3968 0.0333  -0.0476 0.0610  937  HIS B CD2 
4899 C CE1 . HIS B 281 ? 0.1925 0.3713 0.3982 0.0223  -0.0484 0.0498  937  HIS B CE1 
4900 N NE2 . HIS B 281 ? 0.1872 0.3826 0.3913 0.0249  -0.0527 0.0573  937  HIS B NE2 
4901 N N   . ILE B 282 ? 0.3439 0.4090 0.4816 0.0585  -0.0135 0.0632  938  ILE B N   
4902 C CA  . ILE B 282 ? 0.3755 0.4054 0.4895 0.0607  -0.0075 0.0649  938  ILE B CA  
4903 C C   . ILE B 282 ? 0.4692 0.4819 0.5756 0.0459  -0.0066 0.0562  938  ILE B C   
4904 O O   . ILE B 282 ? 0.4271 0.4485 0.5454 0.0389  -0.0078 0.0490  938  ILE B O   
4905 C CB  . ILE B 282 ? 0.4182 0.4298 0.5220 0.0769  -0.0004 0.0708  938  ILE B CB  
4906 C CG1 . ILE B 282 ? 0.4012 0.4184 0.5162 0.0771  0.0017  0.0658  938  ILE B CG1 
4907 C CG2 . ILE B 282 ? 0.4214 0.4479 0.5277 0.0945  0.0000  0.0830  938  ILE B CG2 
4908 C CD1 . ILE B 282 ? 0.4280 0.4120 0.5228 0.0853  0.0097  0.0658  938  ILE B CD1 
4909 N N   . SER B 283 ? 0.5157 0.5040 0.6013 0.0411  -0.0044 0.0582  939  SER B N   
4910 C CA  . SER B 283 ? 0.5452 0.5178 0.6203 0.0254  -0.0037 0.0527  939  SER B CA  
4911 C C   . SER B 283 ? 0.6239 0.5598 0.6775 0.0258  0.0016  0.0527  939  SER B C   
4912 O O   . SER B 283 ? 0.6168 0.5457 0.6681 0.0142  0.0017  0.0467  939  SER B O   
4913 C CB  . SER B 283 ? 0.6095 0.5795 0.6737 0.0175  -0.0050 0.0561  939  SER B CB  
4914 O OG  . SER B 283 ? 0.6787 0.6789 0.7576 0.0175  -0.0094 0.0557  939  SER B OG  
4915 N N   . LYS B 284 ? 0.5923 0.5041 0.6283 0.0396  0.0059  0.0597  940  LYS B N   
4916 C CA  . LYS B 284 ? 0.6075 0.4774 0.6167 0.0430  0.0117  0.0600  940  LYS B CA  
4917 C C   . LYS B 284 ? 0.6360 0.5015 0.6433 0.0670  0.0169  0.0659  940  LYS B C   
4918 O O   . LYS B 284 ? 0.6215 0.5049 0.6376 0.0798  0.0161  0.0738  940  LYS B O   
4919 C CB  . LYS B 284 ? 0.6605 0.4952 0.6403 0.0338  0.0128  0.0639  940  LYS B CB  
4920 C CG  . LYS B 284 ? 0.8703 0.6510 0.8135 0.0372  0.0188  0.0650  940  LYS B CG  
4921 C CD  . LYS B 284 ? 0.9907 0.7359 0.9041 0.0221  0.0184  0.0685  940  LYS B CD  
4922 C CE  . LYS B 284 ? 1.1527 0.8830 1.0519 0.0339  0.0201  0.0794  940  LYS B CE  
4923 N NZ  . LYS B 284 ? 1.2928 0.9922 1.1650 0.0152  0.0189  0.0831  940  LYS B NZ  
4924 N N   . LEU B 285 ? 0.5705 0.4149 0.5664 0.0731  0.0222  0.0626  941  LEU B N   
4925 C CA  . LEU B 285 ? 0.5576 0.3970 0.5494 0.0975  0.0290  0.0684  941  LEU B CA  
4926 C C   . LEU B 285 ? 0.6422 0.4417 0.6026 0.1112  0.0346  0.0764  941  LEU B C   
4927 O O   . LEU B 285 ? 0.6671 0.4273 0.5998 0.0989  0.0348  0.0744  941  LEU B O   
4928 C CB  . LEU B 285 ? 0.5533 0.3754 0.5356 0.0994  0.0341  0.0618  941  LEU B CB  
4929 C CG  . LEU B 285 ? 0.5629 0.4224 0.5744 0.0950  0.0312  0.0569  941  LEU B CG  
4930 C CD1 . LEU B 285 ? 0.5626 0.3976 0.5580 0.0884  0.0344  0.0489  941  LEU B CD1 
4931 C CD2 . LEU B 285 ? 0.5773 0.4691 0.6094 0.1152  0.0339  0.0643  941  LEU B CD2 
4932 N N   . PRO B 286 ? 0.6042 0.4104 0.5657 0.1371  0.0397  0.0862  942  PRO B N   
4933 C CA  . PRO B 286 ? 0.6263 0.3877 0.5533 0.1536  0.0465  0.0943  942  PRO B CA  
4934 C C   . PRO B 286 ? 0.7054 0.4090 0.5943 0.1545  0.0540  0.0878  942  PRO B C   
4935 O O   . PRO B 286 ? 0.6881 0.3964 0.5819 0.1530  0.0562  0.0802  942  PRO B O   
4936 C CB  . PRO B 286 ? 0.6357 0.4256 0.5773 0.1830  0.0509  0.1060  942  PRO B CB  
4937 C CG  . PRO B 286 ? 0.6556 0.5078 0.6403 0.1773  0.0444  0.1047  942  PRO B CG  
4938 C CD  . PRO B 286 ? 0.6002 0.4537 0.5925 0.1527  0.0400  0.0911  942  PRO B CD  
4939 N N   . LYS B 287 ? 0.7079 0.3557 0.5568 0.1547  0.0574  0.0904  943  LYS B N   
4940 C CA  . LYS B 287 ? 0.7575 0.3399 0.5613 0.1538  0.0641  0.0843  943  LYS B CA  
4941 C C   . LYS B 287 ? 0.8023 0.3777 0.5992 0.1798  0.0742  0.0834  943  LYS B C   
4942 O O   . LYS B 287 ? 0.7823 0.3778 0.5899 0.2085  0.0798  0.0935  943  LYS B O   
4943 C CB  . LYS B 287 ? 0.8479 0.3723 0.6097 0.1579  0.0673  0.0913  943  LYS B CB  
4944 C CG  . LYS B 287 ? 1.1060 0.5980 0.8459 0.1243  0.0608  0.0862  943  LYS B CG  
4945 C CD  . LYS B 287 ? 1.2645 0.7289 0.9831 0.1253  0.0602  0.0972  943  LYS B CD  
4946 C CE  . LYS B 287 ? 1.3434 0.8670 1.1013 0.1182  0.0522  0.1035  943  LYS B CE  
4947 N NZ  . LYS B 287 ? 1.4273 0.9303 1.1673 0.1247  0.0525  0.1162  943  LYS B NZ  
4948 N N   . GLY B 288 ? 0.7745 0.3266 0.5554 0.1696  0.0762  0.0722  944  GLY B N   
4949 C CA  . GLY B 288 ? 0.7764 0.3212 0.5484 0.1927  0.0863  0.0703  944  GLY B CA  
4950 C C   . GLY B 288 ? 0.7714 0.3770 0.5861 0.1911  0.0838  0.0672  944  GLY B C   
4951 O O   . GLY B 288 ? 0.7900 0.3884 0.5958 0.2015  0.0909  0.0627  944  GLY B O   
4952 N N   . LYS B 289 ? 0.6518 0.3153 0.5106 0.1782  0.0741  0.0696  945  LYS B N   
4953 C CA  . LYS B 289 ? 0.6019 0.3227 0.5021 0.1727  0.0699  0.0671  945  LYS B CA  
4954 C C   . LYS B 289 ? 0.6377 0.3583 0.5416 0.1423  0.0624  0.0553  945  LYS B C   
4955 O O   . LYS B 289 ? 0.6390 0.3389 0.5305 0.1216  0.0566  0.0517  945  LYS B O   
4956 C CB  . LYS B 289 ? 0.5958 0.3746 0.5373 0.1748  0.0633  0.0757  945  LYS B CB  
4957 C CG  . LYS B 289 ? 0.6794 0.4708 0.6234 0.2049  0.0695  0.0895  945  LYS B CG  
4958 C CD  . LYS B 289 ? 0.6713 0.4773 0.6195 0.2290  0.0793  0.0933  945  LYS B CD  
4959 C CE  . LYS B 289 ? 0.7221 0.5461 0.6746 0.2598  0.0856  0.1087  945  LYS B CE  
4960 N NZ  . LYS B 289 ? 0.8033 0.6541 0.7667 0.2820  0.0947  0.1138  945  LYS B NZ  
4961 N N   . HIS B 290 ? 0.5696 0.3144 0.4903 0.1399  0.0627  0.0504  946  HIS B N   
4962 C CA  . HIS B 290 ? 0.5579 0.3064 0.4835 0.1140  0.0560  0.0404  946  HIS B CA  
4963 C C   . HIS B 290 ? 0.5210 0.3278 0.4917 0.1061  0.0490  0.0406  946  HIS B C   
4964 O O   . HIS B 290 ? 0.4958 0.3132 0.4764 0.0856  0.0425  0.0341  946  HIS B O   
4965 C CB  . HIS B 290 ? 0.5931 0.3097 0.4909 0.1163  0.0625  0.0334  946  HIS B CB  
4966 C CG  . HIS B 290 ? 0.6789 0.3321 0.5271 0.1258  0.0704  0.0320  946  HIS B CG  
4967 N ND1 . HIS B 290 ? 0.7131 0.3508 0.5464 0.1564  0.0813  0.0387  946  HIS B ND1 
4968 C CD2 . HIS B 290 ? 0.7315 0.3332 0.5412 0.1082  0.0687  0.0252  946  HIS B CD2 
4969 C CE1 . HIS B 290 ? 0.7459 0.3188 0.5302 0.1577  0.0864  0.0350  946  HIS B CE1 
4970 N NE2 . HIS B 290 ? 0.7648 0.3132 0.5326 0.1276  0.0786  0.0267  946  HIS B NE2 
4971 N N   . SER B 291 ? 0.4421 0.2861 0.4386 0.1226  0.0505  0.0486  947  SER B N   
4972 C CA  . SER B 291 ? 0.4031 0.2987 0.4393 0.1160  0.0441  0.0497  947  SER B CA  
4973 C C   . SER B 291 ? 0.4207 0.3512 0.4792 0.1306  0.0437  0.0602  947  SER B C   
4974 O O   . SER B 291 ? 0.3911 0.3092 0.4361 0.1493  0.0496  0.0677  947  SER B O   
4975 C CB  . SER B 291 ? 0.4396 0.3468 0.4824 0.1173  0.0473  0.0467  947  SER B CB  
4976 O OG  . SER B 291 ? 0.5483 0.4531 0.5823 0.1411  0.0575  0.0527  947  SER B OG  
4977 N N   . VAL B 292 ? 0.3624 0.3358 0.4538 0.1216  0.0363  0.0612  948  VAL B N   
4978 C CA  . VAL B 292 ? 0.3333 0.3470 0.4493 0.1308  0.0338  0.0710  948  VAL B CA  
4979 C C   . VAL B 292 ? 0.3349 0.3815 0.4723 0.1335  0.0350  0.0737  948  VAL B C   
4980 O O   . VAL B 292 ? 0.3384 0.3872 0.4825 0.1198  0.0323  0.0667  948  VAL B O   
4981 C CB  . VAL B 292 ? 0.3818 0.4153 0.5143 0.1159  0.0234  0.0701  948  VAL B CB  
4982 C CG1 . VAL B 292 ? 0.3641 0.4449 0.5254 0.1186  0.0183  0.0783  948  VAL B CG1 
4983 C CG2 . VAL B 292 ? 0.3929 0.4018 0.5060 0.1184  0.0235  0.0721  948  VAL B CG2 
4984 N N   . LYS B 293 ? 0.2641 0.3372 0.4119 0.1514  0.0394  0.0850  949  LYS B N   
4985 C CA  . LYS B 293 ? 0.2355 0.3463 0.4063 0.1524  0.0398  0.0900  949  LYS B CA  
4986 C C   . LYS B 293 ? 0.2720 0.4295 0.4710 0.1497  0.0319  0.0996  949  LYS B C   
4987 O O   . LYS B 293 ? 0.2533 0.4242 0.4531 0.1653  0.0342  0.1099  949  LYS B O   
4988 C CB  . LYS B 293 ? 0.2474 0.3556 0.4073 0.1749  0.0526  0.0958  949  LYS B CB  
4989 C CG  . LYS B 293 ? 0.2764 0.4285 0.4622 0.1734  0.0527  0.1020  949  LYS B CG  
4990 C CD  . LYS B 293 ? 0.4067 0.5637 0.5841 0.1971  0.0660  0.1093  949  LYS B CD  
4991 C CE  . LYS B 293 ? 0.5080 0.7123 0.7127 0.1930  0.0655  0.1168  949  LYS B CE  
4992 N NZ  . LYS B 293 ? 0.4960 0.7098 0.6931 0.2179  0.0798  0.1249  949  LYS B NZ  
4993 N N   . GLY B 294 ? 0.2354 0.4153 0.4551 0.1297  0.0225  0.0961  950  GLY B N   
4994 C CA  . GLY B 294 ? 0.2145 0.4381 0.4596 0.1225  0.0138  0.1042  950  GLY B CA  
4995 C C   . GLY B 294 ? 0.2335 0.4949 0.4952 0.1324  0.0185  0.1162  950  GLY B C   
4996 O O   . GLY B 294 ? 0.1899 0.4537 0.4561 0.1269  0.0208  0.1138  950  GLY B O   
4997 N N   . LEU B 295 ? 0.2152 0.5072 0.4852 0.1485  0.0210  0.1302  951  LEU B N   
4998 C CA  . LEU B 295 ? 0.2100 0.5431 0.4962 0.1606  0.0270  0.1438  951  LEU B CA  
4999 C C   . LEU B 295 ? 0.2453 0.6259 0.5605 0.1409  0.0167  0.1503  951  LEU B C   
5000 O O   . LEU B 295 ? 0.2258 0.6348 0.5545 0.1329  0.0071  0.1568  951  LEU B O   
5001 C CB  . LEU B 295 ? 0.2107 0.5614 0.4945 0.1887  0.0350  0.1582  951  LEU B CB  
5002 C CG  . LEU B 295 ? 0.3019 0.6044 0.5539 0.2110  0.0455  0.1544  951  LEU B CG  
5003 C CD1 . LEU B 295 ? 0.2682 0.5954 0.5221 0.2378  0.0512  0.1712  951  LEU B CD1 
5004 C CD2 . LEU B 295 ? 0.3756 0.6429 0.6061 0.2213  0.0579  0.1471  951  LEU B CD2 
5005 N N   . GLY B 296 ? 0.2172 0.6052 0.5399 0.1326  0.0185  0.1492  952  GLY B N   
5006 C CA  . GLY B 296 ? 0.2000 0.6287 0.5475 0.1122  0.0091  0.1559  952  GLY B CA  
5007 C C   . GLY B 296 ? 0.2551 0.7392 0.6225 0.1234  0.0137  0.1749  952  GLY B C   
5008 O O   . GLY B 296 ? 0.2782 0.7649 0.6388 0.1490  0.0273  0.1812  952  GLY B O   
5009 N N   . LYS B 297 ? 0.1870 0.7162 0.5780 0.1041  0.0026  0.1847  953  LYS B N   
5010 C CA  . LYS B 297 ? 0.1480 0.7405 0.5628 0.1091  0.0046  0.2051  953  LYS B CA  
5011 C C   . LYS B 297 ? 0.1867 0.7861 0.6036 0.1164  0.0161  0.2086  953  LYS B C   
5012 O O   . LYS B 297 ? 0.2097 0.8501 0.6374 0.1355  0.0258  0.2243  953  LYS B O   
5013 C CB  . LYS B 297 ? 0.1515 0.7822 0.5873 0.0785  -0.0120 0.2119  953  LYS B CB  
5014 C CG  . LYS B 297 ? 0.2512 0.8777 0.6844 0.0668  -0.0251 0.2081  953  LYS B CG  
5015 C CD  . LYS B 297 ? 0.3381 1.0247 0.7900 0.0723  -0.0295 0.2276  953  LYS B CD  
5016 C CE  . LYS B 297 ? 0.4516 1.1333 0.8990 0.0573  -0.0438 0.2231  953  LYS B CE  
5017 N NZ  . LYS B 297 ? 0.6071 1.3529 1.0744 0.0575  -0.0508 0.2432  953  LYS B NZ  
5018 N N   . THR B 298 ? 0.1370 0.6995 0.5439 0.1016  0.0150  0.1952  954  THR B N   
5019 C CA  . THR B 298 ? 0.1310 0.6936 0.5366 0.1050  0.0245  0.1964  954  THR B CA  
5020 C C   . THR B 298 ? 0.2164 0.7208 0.5933 0.1191  0.0344  0.1806  954  THR B C   
5021 O O   . THR B 298 ? 0.2219 0.6815 0.5839 0.1095  0.0286  0.1652  954  THR B O   
5022 C CB  . THR B 298 ? 0.2082 0.7797 0.6264 0.0735  0.0136  0.1962  954  THR B CB  
5023 O OG1 . THR B 298 ? 0.1710 0.7927 0.6124 0.0574  0.0028  0.2101  954  THR B OG1 
5024 C CG2 . THR B 298 ? 0.1471 0.7249 0.5662 0.0748  0.0227  0.2000  954  THR B CG2 
5025 N N   . THR B 299 ? 0.2004 0.7074 0.5689 0.1410  0.0494  0.1849  955  THR B N   
5026 C CA  . THR B 299 ? 0.2377 0.6924 0.5766 0.1543  0.0596  0.1714  955  THR B CA  
5027 C C   . THR B 299 ? 0.3098 0.7715 0.6467 0.1560  0.0684  0.1738  955  THR B C   
5028 O O   . THR B 299 ? 0.2956 0.8068 0.6500 0.1633  0.0742  0.1897  955  THR B O   
5029 C CB  . THR B 299 ? 0.3506 0.7870 0.6694 0.1855  0.0713  0.1719  955  THR B CB  
5030 O OG1 . THR B 299 ? 0.4216 0.8016 0.7082 0.1931  0.0790  0.1571  955  THR B OG1 
5031 C CG2 . THR B 299 ? 0.2582 0.7405 0.5861 0.2125  0.0843  0.1899  955  THR B CG2 
5032 N N   . PRO B 300 ? 0.3013 0.7173 0.6166 0.1510  0.0705  0.1595  956  PRO B N   
5033 C CA  . PRO B 300 ? 0.3056 0.7269 0.6149 0.1562  0.0805  0.1620  956  PRO B CA  
5034 C C   . PRO B 300 ? 0.3780 0.8108 0.6756 0.1895  0.0976  0.1700  956  PRO B C   
5035 O O   . PRO B 300 ? 0.3824 0.7889 0.6618 0.2078  0.1024  0.1655  956  PRO B O   
5036 C CB  . PRO B 300 ? 0.3533 0.7175 0.6361 0.1484  0.0792  0.1440  956  PRO B CB  
5037 C CG  . PRO B 300 ? 0.4103 0.7524 0.6962 0.1304  0.0653  0.1345  956  PRO B CG  
5038 C CD  . PRO B 300 ? 0.3456 0.7060 0.6399 0.1418  0.0647  0.1414  956  PRO B CD  
5039 N N   . ASP B 301 ? 0.3417 0.8155 0.6499 0.1980  0.1069  0.1832  957  ASP B N   
5040 C CA  . ASP B 301 ? 0.3456 0.8359 0.6437 0.2320  0.1248  0.1924  957  ASP B CA  
5041 C C   . ASP B 301 ? 0.4423 0.8685 0.6968 0.2528  0.1359  0.1771  957  ASP B C   
5042 O O   . ASP B 301 ? 0.4468 0.8400 0.6805 0.2464  0.1385  0.1662  957  ASP B O   
5043 C CB  . ASP B 301 ? 0.3451 0.8840 0.6579 0.2343  0.1332  0.2066  957  ASP B CB  
5044 C CG  . ASP B 301 ? 0.5331 1.1050 0.8428 0.2701  0.1518  0.2204  957  ASP B CG  
5045 O OD1 . ASP B 301 ? 0.5560 1.1200 0.8568 0.2939  0.1573  0.2219  957  ASP B OD1 
5046 O OD2 . ASP B 301 ? 0.6230 1.2291 0.9388 0.2753  0.1614  0.2305  957  ASP B OD2 
5047 N N   . PRO B 302 ? 0.4307 0.8373 0.6694 0.2763  0.1419  0.1764  958  PRO B N   
5048 C CA  . PRO B 302 ? 0.4670 0.8068 0.6605 0.2937  0.1515  0.1616  958  PRO B CA  
5049 C C   . PRO B 302 ? 0.5043 0.8307 0.6702 0.3148  0.1689  0.1602  958  PRO B C   
5050 O O   . PRO B 302 ? 0.5376 0.8041 0.6647 0.3171  0.1730  0.1447  958  PRO B O   
5051 C CB  . PRO B 302 ? 0.4944 0.8282 0.6819 0.3166  0.1551  0.1666  958  PRO B CB  
5052 C CG  . PRO B 302 ? 0.5151 0.8992 0.7433 0.3003  0.1412  0.1778  958  PRO B CG  
5053 C CD  . PRO B 302 ? 0.4293 0.8713 0.6888 0.2867  0.1391  0.1893  958  PRO B CD  
5054 N N   . SER B 303 ? 0.4163 0.7983 0.6006 0.3294  0.1790  0.1765  959  SER B N   
5055 C CA  . SER B 303 ? 0.4151 0.7893 0.5737 0.3508  0.1966  0.1762  959  SER B CA  
5056 C C   . SER B 303 ? 0.4475 0.8120 0.6019 0.3262  0.1922  0.1680  959  SER B C   
5057 O O   . SER B 303 ? 0.4700 0.8155 0.5959 0.3394  0.2050  0.1635  959  SER B O   
5058 C CB  . SER B 303 ? 0.4219 0.8613 0.6005 0.3784  0.2108  0.1977  959  SER B CB  
5059 O OG  . SER B 303 ? 0.4891 1.0004 0.7171 0.3594  0.2003  0.2145  959  SER B OG  
5060 N N   . ALA B 304 ? 0.3614 0.7352 0.5413 0.2913  0.1740  0.1655  960  ALA B N   
5061 C CA  . ALA B 304 ? 0.3408 0.7066 0.5202 0.2661  0.1674  0.1590  960  ALA B CA  
5062 C C   . ALA B 304 ? 0.4255 0.7244 0.5757 0.2499  0.1588  0.1382  960  ALA B C   
5063 O O   . ALA B 304 ? 0.4020 0.6912 0.5503 0.2292  0.1523  0.1323  960  ALA B O   
5064 C CB  . ALA B 304 ? 0.3093 0.7266 0.5325 0.2392  0.1539  0.1707  960  ALA B CB  
5065 N N   . ASN B 305 ? 0.4395 0.6939 0.5664 0.2598  0.1590  0.1282  961  ASN B N   
5066 C CA  . ASN B 305 ? 0.4757 0.6685 0.5734 0.2457  0.1516  0.1098  961  ASN B CA  
5067 C C   . ASN B 305 ? 0.5671 0.7240 0.6266 0.2494  0.1602  0.0998  961  ASN B C   
5068 O O   . ASN B 305 ? 0.5810 0.7364 0.6191 0.2748  0.1764  0.1029  961  ASN B O   
5069 C CB  . ASN B 305 ? 0.5165 0.6710 0.5938 0.2590  0.1530  0.1038  961  ASN B CB  
5070 C CG  . ASN B 305 ? 0.8884 1.0471 0.9893 0.2404  0.1375  0.1029  961  ASN B CG  
5071 O OD1 . ASN B 305 ? 0.9429 1.0618 1.0296 0.2236  0.1284  0.0902  961  ASN B OD1 
5072 N ND2 . ASN B 305 ? 0.7250 0.9339 0.8617 0.2426  0.1342  0.1167  961  ASN B ND2 
5073 N N   . ILE B 306 ? 0.5393 0.6682 0.5893 0.2249  0.1497  0.0883  962  ILE B N   
5074 C CA  . ILE B 306 ? 0.5721 0.6653 0.5841 0.2243  0.1553  0.0779  962  ILE B CA  
5075 C C   . ILE B 306 ? 0.6847 0.7179 0.6645 0.2113  0.1476  0.0613  962  ILE B C   
5076 O O   . ILE B 306 ? 0.6756 0.6939 0.6593 0.2091  0.1416  0.0587  962  ILE B O   
5077 C CB  . ILE B 306 ? 0.5936 0.7179 0.6218 0.2085  0.1520  0.0829  962  ILE B CB  
5078 C CG1 . ILE B 306 ? 0.5870 0.7216 0.6440 0.1778  0.1335  0.0818  962  ILE B CG1 
5079 C CG2 . ILE B 306 ? 0.5621 0.7426 0.6145 0.2231  0.1623  0.0998  962  ILE B CG2 
5080 C CD1 . ILE B 306 ? 0.6710 0.7745 0.7070 0.1599  0.1265  0.0708  962  ILE B CD1 
5081 N N   . SER B 307 ? 0.6943 0.6955 0.6423 0.2021  0.1477  0.0510  963  SER B N   
5082 C CA  . SER B 307 ? 0.7288 0.6769 0.6454 0.1867  0.1399  0.0363  963  SER B CA  
5083 C C   . SER B 307 ? 0.8035 0.7496 0.7181 0.1605  0.1292  0.0307  963  SER B C   
5084 O O   . SER B 307 ? 0.8084 0.7645 0.7140 0.1621  0.1344  0.0323  963  SER B O   
5085 C CB  . SER B 307 ? 0.8109 0.7044 0.6737 0.2057  0.1525  0.0270  963  SER B CB  
5086 O OG  . SER B 307 ? 0.9642 0.8067 0.7981 0.1896  0.1441  0.0143  963  SER B OG  
5087 N N   . LEU B 308 ? 0.7497 0.6869 0.6745 0.1375  0.1143  0.0256  964  LEU B N   
5088 C CA  . LEU B 308 ? 0.7413 0.6766 0.6652 0.1131  0.1029  0.0210  964  LEU B CA  
5089 C C   . LEU B 308 ? 0.8251 0.7151 0.7201 0.0992  0.0956  0.0091  964  LEU B C   
5090 O O   . LEU B 308 ? 0.8163 0.7068 0.7286 0.0907  0.0873  0.0088  964  LEU B O   
5091 C CB  . LEU B 308 ? 0.7059 0.6865 0.6784 0.0985  0.0916  0.0300  964  LEU B CB  
5092 C CG  . LEU B 308 ? 0.7444 0.7275 0.7225 0.0741  0.0783  0.0272  964  LEU B CG  
5093 C CD1 . LEU B 308 ? 0.7557 0.7345 0.7104 0.0711  0.0814  0.0259  964  LEU B CD1 
5094 C CD2 . LEU B 308 ? 0.6952 0.7175 0.7185 0.0648  0.0693  0.0363  964  LEU B CD2 
5095 N N   . ASP B 309 ? 0.8099 0.6597 0.6579 0.0971  0.0994  -0.0005 965  ASP B N   
5096 C CA  . ASP B 309 ? 0.8313 0.6323 0.6417 0.0823  0.0936  -0.0122 965  ASP B CA  
5097 C C   . ASP B 309 ? 0.8620 0.6278 0.6542 0.0952  0.0992  -0.0156 965  ASP B C   
5098 O O   . ASP B 309 ? 0.8765 0.6201 0.6619 0.0803  0.0907  -0.0203 965  ASP B O   
5099 C CB  . ASP B 309 ? 0.8493 0.6642 0.6794 0.0538  0.0766  -0.0130 965  ASP B CB  
5100 C CG  . ASP B 309 ? 1.0575 0.8901 0.8877 0.0398  0.0709  -0.0122 965  ASP B CG  
5101 O OD1 . ASP B 309 ? 1.0526 0.9275 0.9173 0.0431  0.0705  -0.0029 965  ASP B OD1 
5102 O OD2 . ASP B 309 ? 1.1814 0.9850 0.9760 0.0246  0.0663  -0.0203 965  ASP B OD2 
5103 N N   . GLY B 310 ? 0.7773 0.5402 0.5619 0.1233  0.1139  -0.0120 966  GLY B N   
5104 C CA  . GLY B 310 ? 0.7743 0.5048 0.5404 0.1409  0.1214  -0.0133 966  GLY B CA  
5105 C C   . GLY B 310 ? 0.7559 0.5159 0.5639 0.1430  0.1163  -0.0049 966  GLY B C   
5106 O O   . GLY B 310 ? 0.7868 0.5211 0.5815 0.1558  0.1209  -0.0051 966  GLY B O   
5107 N N   . VAL B 311 ? 0.6071 0.4191 0.4639 0.1310  0.1069  0.0024  967  VAL B N   
5108 C CA  . VAL B 311 ? 0.5483 0.3917 0.4460 0.1301  0.1007  0.0100  967  VAL B CA  
5109 C C   . VAL B 311 ? 0.5380 0.4289 0.4684 0.1490  0.1080  0.0223  967  VAL B C   
5110 O O   . VAL B 311 ? 0.5171 0.4339 0.4572 0.1493  0.1106  0.0262  967  VAL B O   
5111 C CB  . VAL B 311 ? 0.5660 0.4311 0.4922 0.1026  0.0848  0.0092  967  VAL B CB  
5112 C CG1 . VAL B 311 ? 0.5412 0.4287 0.5011 0.1005  0.0781  0.0145  967  VAL B CG1 
5113 C CG2 . VAL B 311 ? 0.5847 0.4116 0.4793 0.0821  0.0777  -0.0014 967  VAL B CG2 
5114 N N   . ASP B 312 ? 0.4660 0.3704 0.4131 0.1637  0.1109  0.0295  968  ASP B N   
5115 C CA  . ASP B 312 ? 0.4245 0.3788 0.4044 0.1798  0.1166  0.0428  968  ASP B CA  
5116 C C   . ASP B 312 ? 0.4152 0.4177 0.4407 0.1614  0.1051  0.0493  968  ASP B C   
5117 O O   . ASP B 312 ? 0.3814 0.3848 0.4227 0.1438  0.0931  0.0465  968  ASP B O   
5118 C CB  . ASP B 312 ? 0.4509 0.4067 0.4332 0.2016  0.1230  0.0495  968  ASP B CB  
5119 C CG  . ASP B 312 ? 0.6718 0.6084 0.6225 0.2320  0.1404  0.0513  968  ASP B CG  
5120 O OD1 . ASP B 312 ? 0.6606 0.6286 0.6198 0.2444  0.1493  0.0586  968  ASP B OD1 
5121 O OD2 . ASP B 312 ? 0.8129 0.7019 0.7287 0.2438  0.1458  0.0458  968  ASP B OD2 
5122 N N   . VAL B 313 ? 0.3583 0.3983 0.4019 0.1648  0.1091  0.0577  969  VAL B N   
5123 C CA  . VAL B 313 ? 0.3274 0.4090 0.4104 0.1471  0.0987  0.0644  969  VAL B CA  
5124 C C   . VAL B 313 ? 0.3547 0.4849 0.4691 0.1588  0.1024  0.0792  969  VAL B C   
5125 O O   . VAL B 313 ? 0.3147 0.4673 0.4293 0.1725  0.1129  0.0871  969  VAL B O   
5126 C CB  . VAL B 313 ? 0.3584 0.4429 0.4378 0.1338  0.0966  0.0625  969  VAL B CB  
5127 C CG1 . VAL B 313 ? 0.3280 0.4503 0.4455 0.1164  0.0861  0.0701  969  VAL B CG1 
5128 C CG2 . VAL B 313 ? 0.3743 0.4149 0.4232 0.1212  0.0918  0.0491  969  VAL B CG2 
5129 N N   . PRO B 314 ? 0.3394 0.4880 0.4793 0.1536  0.0943  0.0835  970  PRO B N   
5130 C CA  . PRO B 314 ? 0.3251 0.5225 0.4940 0.1632  0.0969  0.0984  970  PRO B CA  
5131 C C   . PRO B 314 ? 0.3772 0.6166 0.5772 0.1466  0.0904  0.1074  970  PRO B C   
5132 O O   . PRO B 314 ? 0.3586 0.6213 0.5854 0.1328  0.0799  0.1121  970  PRO B O   
5133 C CB  . PRO B 314 ? 0.3392 0.5344 0.5178 0.1624  0.0898  0.0981  970  PRO B CB  
5134 C CG  . PRO B 314 ? 0.4058 0.5660 0.5753 0.1428  0.0791  0.0850  970  PRO B CG  
5135 C CD  . PRO B 314 ? 0.3674 0.4951 0.5095 0.1392  0.0827  0.0755  970  PRO B CD  
5136 N N   . LEU B 315 ? 0.3447 0.5918 0.5386 0.1476  0.0969  0.1101  971  LEU B N   
5137 C CA  . LEU B 315 ? 0.3291 0.6108 0.5484 0.1307  0.0911  0.1189  971  LEU B CA  
5138 C C   . LEU B 315 ? 0.3713 0.7079 0.6153 0.1386  0.0968  0.1368  971  LEU B C   
5139 O O   . LEU B 315 ? 0.3444 0.7096 0.6058 0.1254  0.0940  0.1456  971  LEU B O   
5140 C CB  . LEU B 315 ? 0.3398 0.6043 0.5426 0.1231  0.0926  0.1139  971  LEU B CB  
5141 C CG  . LEU B 315 ? 0.4147 0.6582 0.5840 0.1412  0.1067  0.1094  971  LEU B CG  
5142 C CD1 . LEU B 315 ? 0.3912 0.6729 0.5658 0.1617  0.1211  0.1230  971  LEU B CD1 
5143 C CD2 . LEU B 315 ? 0.4589 0.6848 0.6142 0.1274  0.1036  0.1036  971  LEU B CD2 
5144 N N   . GLY B 316 ? 0.3348 0.6873 0.5808 0.1590  0.1043  0.1430  972  GLY B N   
5145 C CA  . GLY B 316 ? 0.3122 0.7230 0.5838 0.1672  0.1094  0.1615  972  GLY B CA  
5146 C C   . GLY B 316 ? 0.3649 0.8108 0.6708 0.1429  0.0948  0.1703  972  GLY B C   
5147 O O   . GLY B 316 ? 0.3808 0.8022 0.6889 0.1249  0.0817  0.1609  972  GLY B O   
5148 N N   . THR B 317 ? 0.2890 0.7921 0.6206 0.1410  0.0968  0.1884  973  THR B N   
5149 C CA  . THR B 317 ? 0.2650 0.8012 0.6267 0.1155  0.0823  0.1975  973  THR B CA  
5150 C C   . THR B 317 ? 0.3176 0.8683 0.6902 0.1217  0.0776  0.2007  973  THR B C   
5151 O O   . THR B 317 ? 0.3006 0.8550 0.6646 0.1488  0.0885  0.2031  973  THR B O   
5152 C CB  . THR B 317 ? 0.3052 0.8970 0.6899 0.1061  0.0841  0.2163  973  THR B CB  
5153 O OG1 . THR B 317 ? 0.3111 0.9479 0.7030 0.1312  0.0979  0.2309  973  THR B OG1 
5154 C CG2 . THR B 317 ? 0.2831 0.8599 0.6579 0.0958  0.0864  0.2139  973  THR B CG2 
5155 N N   . GLY B 318 ? 0.2908 0.8452 0.6790 0.0972  0.0616  0.2000  974  GLY B N   
5156 C CA  . GLY B 318 ? 0.2866 0.8555 0.6857 0.0978  0.0544  0.2029  974  GLY B CA  
5157 C C   . GLY B 318 ? 0.3385 0.9705 0.7587 0.1112  0.0599  0.2232  974  GLY B C   
5158 O O   . GLY B 318 ? 0.3127 0.9937 0.7548 0.0988  0.0581  0.2388  974  GLY B O   
5159 N N   . ILE B 319 ? 0.3140 0.9454 0.7269 0.1376  0.0673  0.2242  975  ILE B N   
5160 C CA  . ILE B 319 ? 0.2923 0.9817 0.7234 0.1564  0.0732  0.2435  975  ILE B CA  
5161 C C   . ILE B 319 ? 0.3242 1.0063 0.7556 0.1592  0.0649  0.2409  975  ILE B C   
5162 O O   . ILE B 319 ? 0.3479 0.9758 0.7607 0.1530  0.0590  0.2235  975  ILE B O   
5163 C CB  . ILE B 319 ? 0.3356 1.0335 0.7538 0.1938  0.0946  0.2499  975  ILE B CB  
5164 C CG1 . ILE B 319 ? 0.3726 1.0091 0.7564 0.2194  0.1034  0.2345  975  ILE B CG1 
5165 C CG2 . ILE B 319 ? 0.3562 1.0599 0.7717 0.1903  0.1029  0.2517  975  ILE B CG2 
5166 C CD1 . ILE B 319 ? 0.4113 1.0609 0.7847 0.2587  0.1213  0.2437  975  ILE B CD1 
5167 N N   . SER B 320 ? 0.2327 0.9713 0.6852 0.1683  0.0644  0.2591  976  SER B N   
5168 C CA  . SER B 320 ? 0.2281 0.9667 0.6815 0.1733  0.0573  0.2596  976  SER B CA  
5169 C C   . SER B 320 ? 0.2870 0.9781 0.7111 0.2068  0.0703  0.2503  976  SER B C   
5170 O O   . SER B 320 ? 0.2706 0.9644 0.6844 0.2362  0.0873  0.2555  976  SER B O   
5171 C CB  . SER B 320 ? 0.2519 1.0690 0.7353 0.1779  0.0551  0.2840  976  SER B CB  
5172 O OG  . SER B 320 ? 0.3648 1.1857 0.8478 0.1892  0.0507  0.2870  976  SER B OG  
5173 N N   . SER B 321 ? 0.2552 0.9013 0.6639 0.2020  0.0626  0.2369  977  SER B N   
5174 C CA  . SER B 321 ? 0.2737 0.8703 0.6525 0.2294  0.0728  0.2281  977  SER B CA  
5175 C C   . SER B 321 ? 0.3419 0.9737 0.7267 0.2591  0.0797  0.2452  977  SER B C   
5176 O O   . SER B 321 ? 0.3704 0.9728 0.7311 0.2906  0.0939  0.2440  977  SER B O   
5177 C CB  . SER B 321 ? 0.3066 0.8485 0.6687 0.2124  0.0620  0.2099  977  SER B CB  
5178 O OG  . SER B 321 ? 0.2519 0.8217 0.6322 0.1966  0.0475  0.2155  977  SER B OG  
5179 N N   . GLY B 322 ? 0.2710 0.9637 0.6859 0.2484  0.0692  0.2610  978  GLY B N   
5180 C CA  . GLY B 322 ? 0.2382 0.9745 0.6642 0.2728  0.0725  0.2796  978  GLY B CA  
5181 C C   . GLY B 322 ? 0.2720 0.9854 0.6908 0.2659  0.0608  0.2740  978  GLY B C   
5182 O O   . GLY B 322 ? 0.2354 0.9852 0.6646 0.2806  0.0594  0.2892  978  GLY B O   
5183 N N   . VAL B 323 ? 0.2522 0.9082 0.6540 0.2427  0.0520  0.2528  979  VAL B N   
5184 C CA  . VAL B 323 ? 0.2678 0.8959 0.6600 0.2328  0.0409  0.2446  979  VAL B CA  
5185 C C   . VAL B 323 ? 0.3388 1.0183 0.7581 0.2061  0.0229  0.2537  979  VAL B C   
5186 O O   . VAL B 323 ? 0.3064 1.0034 0.7407 0.1770  0.0131  0.2514  979  VAL B O   
5187 C CB  . VAL B 323 ? 0.3368 0.8902 0.7018 0.2186  0.0389  0.2202  979  VAL B CB  
5188 C CG1 . VAL B 323 ? 0.3456 0.8776 0.7037 0.2054  0.0268  0.2128  979  VAL B CG1 
5189 C CG2 . VAL B 323 ? 0.3580 0.8593 0.6921 0.2452  0.0554  0.2125  979  VAL B CG2 
5190 N N   . ASN B 324 ? 0.3484 1.0499 0.7714 0.2167  0.0187  0.2644  980  ASN B N   
5191 C CA  . ASN B 324 ? 0.3405 1.0901 0.7849 0.1944  0.0016  0.2739  980  ASN B CA  
5192 C C   . ASN B 324 ? 0.4267 1.1348 0.8553 0.1756  -0.0108 0.2586  980  ASN B C   
5193 O O   . ASN B 324 ? 0.4453 1.1005 0.8488 0.1901  -0.0046 0.2480  980  ASN B O   
5194 C CB  . ASN B 324 ? 0.3189 1.1283 0.7793 0.2193  0.0047  0.2983  980  ASN B CB  
5195 C CG  . ASN B 324 ? 0.7539 1.6179 1.2343 0.2372  0.0161  0.3167  980  ASN B CG  
5196 O OD1 . ASN B 324 ? 0.6896 1.5813 1.1871 0.2167  0.0130  0.3187  980  ASN B OD1 
5197 N ND2 . ASN B 324 ? 0.6537 1.5349 1.1318 0.2767  0.0300  0.3314  980  ASN B ND2 
5198 N N   . ASP B 325 ? 0.3683 1.1024 0.8105 0.1432  -0.0283 0.2586  981  ASP B N   
5199 C CA  . ASP B 325 ? 0.3723 1.0789 0.8022 0.1227  -0.0417 0.2462  981  ASP B CA  
5200 C C   . ASP B 325 ? 0.4152 1.0473 0.8183 0.1197  -0.0378 0.2229  981  ASP B C   
5201 O O   . ASP B 325 ? 0.4443 1.0449 0.8298 0.1246  -0.0390 0.2160  981  ASP B O   
5202 C CB  . ASP B 325 ? 0.3981 1.1295 0.8282 0.1373  -0.0454 0.2591  981  ASP B CB  
5203 C CG  . ASP B 325 ? 0.6099 1.4222 1.0680 0.1383  -0.0516 0.2839  981  ASP B CG  
5204 O OD1 . ASP B 325 ? 0.5986 1.4513 1.0775 0.1258  -0.0534 0.2920  981  ASP B OD1 
5205 O OD2 . ASP B 325 ? 0.7230 1.5604 1.1827 0.1508  -0.0551 0.2963  981  ASP B OD2 
5206 N N   . THR B 326 ? 0.3303 0.9368 0.7304 0.1116  -0.0331 0.2120  982  THR B N   
5207 C CA  . THR B 326 ? 0.3259 0.8677 0.7033 0.1066  -0.0300 0.1910  982  THR B CA  
5208 C C   . THR B 326 ? 0.3342 0.8635 0.7122 0.0734  -0.0434 0.1783  982  THR B C   
5209 O O   . THR B 326 ? 0.3279 0.8913 0.7229 0.0547  -0.0515 0.1844  982  THR B O   
5210 C CB  . THR B 326 ? 0.3439 0.8586 0.7121 0.1236  -0.0148 0.1867  982  THR B CB  
5211 O OG1 . THR B 326 ? 0.3868 0.8446 0.7350 0.1142  -0.0144 0.1671  982  THR B OG1 
5212 C CG2 . THR B 326 ? 0.1976 0.7459 0.5844 0.1175  -0.0127 0.1943  982  THR B CG2 
5213 N N   . SER B 327 ? 0.2593 0.7400 0.6180 0.0664  -0.0453 0.1613  983  SER B N   
5214 C CA  . SER B 327 ? 0.2408 0.7034 0.5958 0.0389  -0.0564 0.1481  983  SER B CA  
5215 C C   . SER B 327 ? 0.2628 0.7007 0.6165 0.0310  -0.0522 0.1386  983  SER B C   
5216 O O   . SER B 327 ? 0.2718 0.6880 0.6201 0.0112  -0.0595 0.1270  983  SER B O   
5217 C CB  . SER B 327 ? 0.3066 0.7337 0.6423 0.0364  -0.0597 0.1357  983  SER B CB  
5218 O OG  . SER B 327 ? 0.5191 0.9049 0.8386 0.0514  -0.0488 0.1271  983  SER B OG  
5219 N N   . LEU B 328 ? 0.1756 0.6163 0.5326 0.0477  -0.0403 0.1439  984  LEU B N   
5220 C CA  . LEU B 328 ? 0.1717 0.5896 0.5259 0.0427  -0.0355 0.1360  984  LEU B CA  
5221 C C   . LEU B 328 ? 0.1972 0.6503 0.5684 0.0430  -0.0321 0.1482  984  LEU B C   
5222 O O   . LEU B 328 ? 0.1908 0.6730 0.5697 0.0620  -0.0241 0.1613  984  LEU B O   
5223 C CB  . LEU B 328 ? 0.1882 0.5635 0.5232 0.0597  -0.0239 0.1265  984  LEU B CB  
5224 C CG  . LEU B 328 ? 0.2590 0.5957 0.5757 0.0585  -0.0258 0.1139  984  LEU B CG  
5225 C CD1 . LEU B 328 ? 0.2756 0.5852 0.5751 0.0794  -0.0143 0.1121  984  LEU B CD1 
5226 C CD2 . LEU B 328 ? 0.3038 0.6120 0.6147 0.0403  -0.0309 0.0997  984  LEU B CD2 
5227 N N   . LEU B 329 ? 0.1601 0.6079 0.5356 0.0239  -0.0365 0.1440  985  LEU B N   
5228 C CA  . LEU B 329 ? 0.1395 0.6194 0.5305 0.0215  -0.0332 0.1556  985  LEU B CA  
5229 C C   . LEU B 329 ? 0.1285 0.5881 0.5099 0.0418  -0.0184 0.1528  985  LEU B C   
5230 O O   . LEU B 329 ? 0.0879 0.5762 0.4775 0.0566  -0.0093 0.1647  985  LEU B O   
5231 C CB  . LEU B 329 ? 0.1497 0.6241 0.5447 -0.0067 -0.0433 0.1517  985  LEU B CB  
5232 C CG  . LEU B 329 ? 0.2162 0.7009 0.6147 -0.0309 -0.0589 0.1517  985  LEU B CG  
5233 C CD1 . LEU B 329 ? 0.2365 0.6981 0.6305 -0.0557 -0.0669 0.1445  985  LEU B CD1 
5234 C CD2 . LEU B 329 ? 0.2157 0.7601 0.6342 -0.0347 -0.0638 0.1706  985  LEU B CD2 
5235 N N   . TYR B 330 ? 0.0913 0.5021 0.4541 0.0422  -0.0161 0.1371  986  TYR B N   
5236 C CA  . TYR B 330 ? 0.0931 0.4799 0.4429 0.0582  -0.0036 0.1328  986  TYR B CA  
5237 C C   . TYR B 330 ? 0.1211 0.4697 0.4496 0.0724  0.0014  0.1228  986  TYR B C   
5238 O O   . TYR B 330 ? 0.1020 0.4374 0.4256 0.0667  -0.0054 0.1169  986  TYR B O   
5239 C CB  . TYR B 330 ? 0.1135 0.4810 0.4611 0.0435  -0.0050 0.1256  986  TYR B CB  
5240 C CG  . TYR B 330 ? 0.1124 0.5130 0.4791 0.0246  -0.0126 0.1352  986  TYR B CG  
5241 C CD1 . TYR B 330 ? 0.1191 0.5636 0.5013 0.0301  -0.0074 0.1510  986  TYR B CD1 
5242 C CD2 . TYR B 330 ? 0.1247 0.5148 0.4933 0.0012  -0.0252 0.1295  986  TYR B CD2 
5243 C CE1 . TYR B 330 ? 0.0917 0.5700 0.4918 0.0101  -0.0154 0.1616  986  TYR B CE1 
5244 C CE2 . TYR B 330 ? 0.1221 0.5400 0.5055 -0.0185 -0.0333 0.1389  986  TYR B CE2 
5245 C CZ  . TYR B 330 ? 0.2050 0.6682 0.6048 -0.0153 -0.0289 0.1553  986  TYR B CZ  
5246 O OH  . TYR B 330 ? 0.2897 0.7817 0.7038 -0.0371 -0.0372 0.1658  986  TYR B OH  
5247 N N   . ASN B 331 ? 0.0766 0.4076 0.3908 0.0905  0.0137  0.1216  987  ASN B N   
5248 C CA  . ASN B 331 ? 0.0918 0.3811 0.3815 0.1027  0.0195  0.1122  987  ASN B CA  
5249 C C   . ASN B 331 ? 0.1623 0.4147 0.4408 0.0870  0.0135  0.0973  987  ASN B C   
5250 O O   . ASN B 331 ? 0.1282 0.3796 0.4134 0.0712  0.0084  0.0930  987  ASN B O   
5251 C CB  . ASN B 331 ? 0.0900 0.3647 0.3635 0.1217  0.0332  0.1129  987  ASN B CB  
5252 C CG  . ASN B 331 ? 0.3546 0.6625 0.6351 0.1432  0.0422  0.1277  987  ASN B CG  
5253 O OD1 . ASN B 331 ? 0.3143 0.6406 0.6008 0.1527  0.0412  0.1358  987  ASN B OD1 
5254 N ND2 . ASN B 331 ? 0.1988 0.5168 0.4783 0.1525  0.0517  0.1321  987  ASN B ND2 
5255 N N   . GLU B 332 ? 0.1621 0.3843 0.4228 0.0921  0.0147  0.0904  988  GLU B N   
5256 C CA  . GLU B 332 ? 0.1694 0.3569 0.4167 0.0808  0.0113  0.0774  988  GLU B CA  
5257 C C   . GLU B 332 ? 0.2026 0.3560 0.4248 0.0926  0.0183  0.0732  988  GLU B C   
5258 O O   . GLU B 332 ? 0.2000 0.3549 0.4159 0.1080  0.0231  0.0798  988  GLU B O   
5259 C CB  . GLU B 332 ? 0.1864 0.3776 0.4430 0.0639  0.0000  0.0725  988  GLU B CB  
5260 C CG  . GLU B 332 ? 0.2630 0.4623 0.5208 0.0660  -0.0044 0.0755  988  GLU B CG  
5261 C CD  . GLU B 332 ? 0.2356 0.4395 0.5016 0.0484  -0.0152 0.0700  988  GLU B CD  
5262 O OE1 . GLU B 332 ? 0.1968 0.3807 0.4523 0.0442  -0.0176 0.0622  988  GLU B OE1 
5263 O OE2 . GLU B 332 ? 0.1671 0.3933 0.4482 0.0383  -0.0209 0.0735  988  GLU B OE2 
5264 N N   . TYR B 333 ? 0.1675 0.2902 0.3740 0.0857  0.0193  0.0634  989  TYR B N   
5265 C CA  . TYR B 333 ? 0.1743 0.2593 0.3530 0.0924  0.0253  0.0584  989  TYR B CA  
5266 C C   . TYR B 333 ? 0.2093 0.2746 0.3812 0.0770  0.0188  0.0494  989  TYR B C   
5267 O O   . TYR B 333 ? 0.1678 0.2378 0.3487 0.0633  0.0135  0.0442  989  TYR B O   
5268 C CB  . TYR B 333 ? 0.1887 0.2573 0.3520 0.0978  0.0332  0.0560  989  TYR B CB  
5269 C CG  . TYR B 333 ? 0.1782 0.2705 0.3494 0.1131  0.0404  0.0653  989  TYR B CG  
5270 C CD1 . TYR B 333 ? 0.1771 0.3031 0.3722 0.1065  0.0374  0.0699  989  TYR B CD1 
5271 C CD2 . TYR B 333 ? 0.2073 0.2884 0.3613 0.1347  0.0508  0.0703  989  TYR B CD2 
5272 C CE1 . TYR B 333 ? 0.1607 0.3140 0.3649 0.1197  0.0443  0.0800  989  TYR B CE1 
5273 C CE2 . TYR B 333 ? 0.2249 0.3323 0.3871 0.1508  0.0587  0.0799  989  TYR B CE2 
5274 C CZ  . TYR B 333 ? 0.3123 0.4580 0.5005 0.1425  0.0554  0.0851  989  TYR B CZ  
5275 O OH  . TYR B 333 ? 0.3203 0.4956 0.5170 0.1578  0.0636  0.0958  989  TYR B OH  
5276 N N   . ILE B 334 ? 0.1832 0.2292 0.3402 0.0799  0.0193  0.0487  990  ILE B N   
5277 C CA  . ILE B 334 ? 0.1722 0.2035 0.3230 0.0659  0.0139  0.0419  990  ILE B CA  
5278 C C   . ILE B 334 ? 0.2413 0.2335 0.3617 0.0670  0.0188  0.0388  990  ILE B C   
5279 O O   . ILE B 334 ? 0.2641 0.2401 0.3687 0.0807  0.0245  0.0433  990  ILE B O   
5280 C CB  . ILE B 334 ? 0.1915 0.2406 0.3550 0.0629  0.0075  0.0444  990  ILE B CB  
5281 C CG1 . ILE B 334 ? 0.1498 0.2352 0.3391 0.0624  0.0027  0.0490  990  ILE B CG1 
5282 C CG2 . ILE B 334 ? 0.1862 0.2273 0.3471 0.0481  0.0023  0.0374  990  ILE B CG2 
5283 C CD1 . ILE B 334 ? 0.0857 0.1775 0.2623 0.0656  0.0080  0.0581  990  ILE B CD1 
5284 N N   . VAL B 335 ? 0.1986 0.1757 0.3101 0.0525  0.0164  0.0316  991  VAL B N   
5285 C CA  . VAL B 335 ? 0.2216 0.1617 0.3036 0.0464  0.0186  0.0278  991  VAL B CA  
5286 C C   . VAL B 335 ? 0.2961 0.2391 0.3812 0.0315  0.0123  0.0255  991  VAL B C   
5287 O O   . VAL B 335 ? 0.2838 0.2533 0.3910 0.0240  0.0068  0.0239  991  VAL B O   
5288 C CB  . VAL B 335 ? 0.2733 0.1936 0.3381 0.0411  0.0213  0.0227  991  VAL B CB  
5289 C CG1 . VAL B 335 ? 0.2668 0.1776 0.3208 0.0587  0.0297  0.0253  991  VAL B CG1 
5290 C CG2 . VAL B 335 ? 0.2449 0.1883 0.3287 0.0279  0.0155  0.0190  991  VAL B CG2 
5291 N N   . TYR B 336 ? 0.2854 0.2013 0.3478 0.0284  0.0135  0.0261  992  TYR B N   
5292 C CA  . TYR B 336 ? 0.2795 0.1996 0.3435 0.0157  0.0087  0.0258  992  TYR B CA  
5293 C C   . TYR B 336 ? 0.3887 0.2885 0.4337 -0.0022 0.0071  0.0220  992  TYR B C   
5294 O O   . TYR B 336 ? 0.4032 0.3055 0.4464 -0.0142 0.0039  0.0227  992  TYR B O   
5295 C CB  . TYR B 336 ? 0.2972 0.2095 0.3538 0.0251  0.0103  0.0319  992  TYR B CB  
5296 C CG  . TYR B 336 ? 0.2918 0.2313 0.3696 0.0404  0.0103  0.0367  992  TYR B CG  
5297 C CD1 . TYR B 336 ? 0.3074 0.2434 0.3826 0.0576  0.0159  0.0407  992  TYR B CD1 
5298 C CD2 . TYR B 336 ? 0.2762 0.2468 0.3763 0.0370  0.0046  0.0372  992  TYR B CD2 
5299 C CE1 . TYR B 336 ? 0.2647 0.2315 0.3613 0.0694  0.0151  0.0465  992  TYR B CE1 
5300 C CE2 . TYR B 336 ? 0.2648 0.2615 0.3835 0.0475  0.0032  0.0416  992  TYR B CE2 
5301 C CZ  . TYR B 336 ? 0.3411 0.3380 0.4592 0.0629  0.0081  0.0469  992  TYR B CZ  
5302 O OH  . TYR B 336 ? 0.2726 0.2998 0.4101 0.0714  0.0060  0.0529  992  TYR B OH  
5303 N N   . ASP B 337 ? 0.3535 0.2380 0.3859 -0.0055 0.0089  0.0184  993  ASP B N   
5304 C CA  . ASP B 337 ? 0.3466 0.2159 0.3617 -0.0246 0.0061  0.0149  993  ASP B CA  
5305 C C   . ASP B 337 ? 0.3591 0.2481 0.3883 -0.0281 0.0041  0.0114  993  ASP B C   
5306 O O   . ASP B 337 ? 0.3332 0.2164 0.3597 -0.0171 0.0080  0.0103  993  ASP B O   
5307 C CB  . ASP B 337 ? 0.3909 0.2102 0.3655 -0.0257 0.0105  0.0141  993  ASP B CB  
5308 C CG  . ASP B 337 ? 0.5124 0.3107 0.4631 -0.0489 0.0067  0.0112  993  ASP B CG  
5309 O OD1 . ASP B 337 ? 0.5330 0.3575 0.4987 -0.0624 0.0014  0.0094  993  ASP B OD1 
5310 O OD2 . ASP B 337 ? 0.6136 0.3686 0.5293 -0.0537 0.0089  0.0113  993  ASP B OD2 
5311 N N   . ILE B 338 ? 0.3019 0.2150 0.3453 -0.0426 -0.0017 0.0106  994  ILE B N   
5312 C CA  . ILE B 338 ? 0.2818 0.2157 0.3392 -0.0465 -0.0044 0.0086  994  ILE B CA  
5313 C C   . ILE B 338 ? 0.3378 0.2460 0.3699 -0.0517 -0.0030 0.0056  994  ILE B C   
5314 O O   . ILE B 338 ? 0.3222 0.2421 0.3631 -0.0480 -0.0029 0.0045  994  ILE B O   
5315 C CB  . ILE B 338 ? 0.2964 0.2619 0.3726 -0.0591 -0.0103 0.0096  994  ILE B CB  
5316 C CG1 . ILE B 338 ? 0.3140 0.2693 0.3711 -0.0790 -0.0134 0.0108  994  ILE B CG1 
5317 C CG2 . ILE B 338 ? 0.2721 0.2631 0.3734 -0.0505 -0.0109 0.0112  994  ILE B CG2 
5318 C CD1 . ILE B 338 ? 0.2575 0.2476 0.3313 -0.0919 -0.0188 0.0131  994  ILE B CD1 
5319 N N   . ALA B 339 ? 0.3212 0.1920 0.3196 -0.0600 -0.0016 0.0043  995  ALA B N   
5320 C CA  . ALA B 339 ? 0.3538 0.1929 0.3207 -0.0665 -0.0003 0.0003  995  ALA B CA  
5321 C C   . ALA B 339 ? 0.4534 0.2751 0.4107 -0.0465 0.0074  -0.0016 995  ALA B C   
5322 O O   . ALA B 339 ? 0.4715 0.2782 0.4102 -0.0495 0.0086  -0.0053 995  ALA B O   
5323 C CB  . ALA B 339 ? 0.3789 0.1782 0.3093 -0.0817 -0.0012 -0.0007 995  ALA B CB  
5324 N N   . GLN B 340 ? 0.3941 0.2216 0.3646 -0.0265 0.0126  0.0015  996  GLN B N   
5325 C CA  . GLN B 340 ? 0.3825 0.2031 0.3502 -0.0046 0.0208  0.0023  996  GLN B CA  
5326 C C   . GLN B 340 ? 0.4046 0.2596 0.3987 0.0010  0.0205  0.0031  996  GLN B C   
5327 O O   . GLN B 340 ? 0.3808 0.2376 0.3762 0.0180  0.0272  0.0049  996  GLN B O   
5328 C CB  . GLN B 340 ? 0.3865 0.2101 0.3634 0.0123  0.0247  0.0076  996  GLN B CB  
5329 C CG  . GLN B 340 ? 0.5041 0.2847 0.4478 0.0135  0.0279  0.0080  996  GLN B CG  
5330 C CD  . GLN B 340 ? 0.5769 0.3630 0.5299 0.0317  0.0317  0.0146  996  GLN B CD  
5331 O OE1 . GLN B 340 ? 0.5112 0.3053 0.4729 0.0260  0.0276  0.0175  996  GLN B OE1 
5332 N NE2 . GLN B 340 ? 0.5795 0.3639 0.5308 0.0544  0.0395  0.0178  996  GLN B NE2 
5333 N N   . VAL B 341 ? 0.3569 0.2398 0.3716 -0.0130 0.0131  0.0027  997  VAL B N   
5334 C CA  . VAL B 341 ? 0.3238 0.2371 0.3625 -0.0104 0.0116  0.0041  997  VAL B CA  
5335 C C   . VAL B 341 ? 0.3892 0.2996 0.4159 -0.0245 0.0080  0.0011  997  VAL B C   
5336 O O   . VAL B 341 ? 0.3820 0.2939 0.4048 -0.0412 0.0017  -0.0001 997  VAL B O   
5337 C CB  . VAL B 341 ? 0.3217 0.2720 0.3968 -0.0111 0.0063  0.0073  997  VAL B CB  
5338 C CG1 . VAL B 341 ? 0.2950 0.2709 0.3917 -0.0077 0.0052  0.0095  997  VAL B CG1 
5339 C CG2 . VAL B 341 ? 0.3075 0.2619 0.3929 0.0000  0.0084  0.0102  997  VAL B CG2 
5340 N N   . ASN B 342 ? 0.3570 0.2672 0.3788 -0.0179 0.0117  0.0008  998  ASN B N   
5341 C CA  . ASN B 342 ? 0.3501 0.2628 0.3633 -0.0298 0.0080  -0.0010 998  ASN B CA  
5342 C C   . ASN B 342 ? 0.3460 0.2906 0.3867 -0.0225 0.0079  0.0035  998  ASN B C   
5343 O O   . ASN B 342 ? 0.3423 0.2858 0.3816 -0.0091 0.0146  0.0050  998  ASN B O   
5344 C CB  . ASN B 342 ? 0.3653 0.2395 0.3367 -0.0314 0.0127  -0.0062 998  ASN B CB  
5345 C CG  . ASN B 342 ? 0.5404 0.4149 0.4977 -0.0479 0.0071  -0.0085 998  ASN B CG  
5346 O OD1 . ASN B 342 ? 0.5374 0.3874 0.4647 -0.0470 0.0111  -0.0125 998  ASN B OD1 
5347 N ND2 . ASN B 342 ? 0.3209 0.2233 0.2977 -0.0627 -0.0022 -0.0057 998  ASN B ND2 
5348 N N   . LEU B 343 ? 0.2602 0.2333 0.3260 -0.0305 0.0006  0.0064  999  LEU B N   
5349 C CA  . LEU B 343 ? 0.2480 0.2482 0.3387 -0.0254 -0.0006 0.0112  999  LEU B CA  
5350 C C   . LEU B 343 ? 0.2792 0.2758 0.3555 -0.0267 0.0012  0.0114  999  LEU B C   
5351 O O   . LEU B 343 ? 0.2821 0.2689 0.3386 -0.0387 -0.0022 0.0087  999  LEU B O   
5352 C CB  . LEU B 343 ? 0.2276 0.2535 0.3431 -0.0323 -0.0081 0.0140  999  LEU B CB  
5353 C CG  . LEU B 343 ? 0.2779 0.3110 0.4096 -0.0300 -0.0096 0.0139  999  LEU B CG  
5354 C CD1 . LEU B 343 ? 0.2677 0.3250 0.4210 -0.0338 -0.0156 0.0167  999  LEU B CD1 
5355 C CD2 . LEU B 343 ? 0.2846 0.3183 0.4270 -0.0170 -0.0051 0.0153  999  LEU B CD2 
5356 N N   . LYS B 344 ? 0.2103 0.2155 0.2950 -0.0153 0.0063  0.0151  1000 LYS B N   
5357 C CA  . LYS B 344 ? 0.2309 0.2323 0.2997 -0.0150 0.0093  0.0156  1000 LYS B CA  
5358 C C   . LYS B 344 ? 0.2653 0.2934 0.3561 -0.0160 0.0059  0.0223  1000 LYS B C   
5359 O O   . LYS B 344 ? 0.2771 0.3079 0.3587 -0.0237 0.0027  0.0231  1000 LYS B O   
5360 C CB  . LYS B 344 ? 0.2710 0.2558 0.3221 -0.0006 0.0201  0.0145  1000 LYS B CB  
5361 C CG  . LYS B 344 ? 0.4489 0.3967 0.4654 -0.0006 0.0240  0.0071  1000 LYS B CG  
5362 C CD  . LYS B 344 ? 0.5786 0.5044 0.5605 -0.0102 0.0236  0.0019  1000 LYS B CD  
5363 C CE  . LYS B 344 ? 0.6332 0.5266 0.5856 -0.0229 0.0202  -0.0053 1000 LYS B CE  
5364 N NZ  . LYS B 344 ? 0.7526 0.6371 0.6810 -0.0402 0.0144  -0.0087 1000 LYS B NZ  
5365 N N   . TYR B 345 ? 0.1970 0.2436 0.3150 -0.0094 0.0060  0.0275  1001 TYR B N   
5366 C CA  . TYR B 345 ? 0.1801 0.2478 0.3177 -0.0104 0.0029  0.0346  1001 TYR B CA  
5367 C C   . TYR B 345 ? 0.2218 0.3027 0.3855 -0.0110 -0.0025 0.0372  1001 TYR B C   
5368 O O   . TYR B 345 ? 0.2025 0.2802 0.3722 -0.0086 -0.0024 0.0343  1001 TYR B O   
5369 C CB  . TYR B 345 ? 0.1870 0.2619 0.3261 -0.0016 0.0101  0.0400  1001 TYR B CB  
5370 C CG  . TYR B 345 ? 0.2296 0.2900 0.3399 0.0016  0.0170  0.0372  1001 TYR B CG  
5371 C CD1 . TYR B 345 ? 0.2672 0.3282 0.3646 -0.0047 0.0152  0.0383  1001 TYR B CD1 
5372 C CD2 . TYR B 345 ? 0.2516 0.2966 0.3454 0.0120  0.0256  0.0336  1001 TYR B CD2 
5373 C CE1 . TYR B 345 ? 0.2922 0.3369 0.3589 -0.0020 0.0217  0.0346  1001 TYR B CE1 
5374 C CE2 . TYR B 345 ? 0.2784 0.3052 0.3412 0.0167  0.0329  0.0300  1001 TYR B CE2 
5375 C CZ  . TYR B 345 ? 0.3563 0.3821 0.4046 0.0089  0.0308  0.0299  1001 TYR B CZ  
5376 O OH  . TYR B 345 ? 0.4144 0.4196 0.4285 0.0133  0.0381  0.0254  1001 TYR B OH  
5377 N N   . LEU B 346 ? 0.1773 0.2714 0.3545 -0.0139 -0.0069 0.0429  1002 LEU B N   
5378 C CA  . LEU B 346 ? 0.1618 0.2652 0.3607 -0.0138 -0.0117 0.0460  1002 LEU B CA  
5379 C C   . LEU B 346 ? 0.2160 0.3281 0.4239 -0.0128 -0.0113 0.0542  1002 LEU B C   
5380 O O   . LEU B 346 ? 0.1971 0.3124 0.3978 -0.0150 -0.0114 0.0581  1002 LEU B O   
5381 C CB  . LEU B 346 ? 0.1580 0.2652 0.3601 -0.0182 -0.0180 0.0452  1002 LEU B CB  
5382 C CG  . LEU B 346 ? 0.2099 0.3225 0.4304 -0.0158 -0.0223 0.0477  1002 LEU B CG  
5383 C CD1 . LEU B 346 ? 0.2012 0.3091 0.4295 -0.0128 -0.0211 0.0440  1002 LEU B CD1 
5384 C CD2 . LEU B 346 ? 0.2160 0.3354 0.4383 -0.0175 -0.0268 0.0470  1002 LEU B CD2 
5385 N N   . LEU B 347 ? 0.1833 0.2996 0.4056 -0.0110 -0.0111 0.0573  1003 LEU B N   
5386 C CA  . LEU B 347 ? 0.1743 0.2984 0.4054 -0.0125 -0.0112 0.0661  1003 LEU B CA  
5387 C C   . LEU B 347 ? 0.1825 0.3037 0.4267 -0.0153 -0.0175 0.0685  1003 LEU B C   
5388 O O   . LEU B 347 ? 0.1755 0.2919 0.4253 -0.0148 -0.0198 0.0636  1003 LEU B O   
5389 C CB  . LEU B 347 ? 0.1734 0.3061 0.4086 -0.0100 -0.0059 0.0694  1003 LEU B CB  
5390 C CG  . LEU B 347 ? 0.2414 0.3795 0.4642 -0.0052 0.0022  0.0715  1003 LEU B CG  
5391 C CD1 . LEU B 347 ? 0.2536 0.3796 0.4590 0.0002  0.0064  0.0627  1003 LEU B CD1 
5392 C CD2 . LEU B 347 ? 0.2575 0.4123 0.4910 -0.0028 0.0067  0.0789  1003 LEU B CD2 
5393 N N   . LYS B 348 ? 0.1119 0.2335 0.3583 -0.0178 -0.0200 0.0759  1004 LYS B N   
5394 C CA  . LYS B 348 ? 0.1078 0.2212 0.3626 -0.0198 -0.0253 0.0795  1004 LYS B CA  
5395 C C   . LYS B 348 ? 0.1578 0.2754 0.4185 -0.0255 -0.0243 0.0869  1004 LYS B C   
5396 O O   . LYS B 348 ? 0.1232 0.2504 0.3813 -0.0271 -0.0210 0.0939  1004 LYS B O   
5397 C CB  . LYS B 348 ? 0.1321 0.2422 0.3840 -0.0182 -0.0285 0.0847  1004 LYS B CB  
5398 C CG  . LYS B 348 ? 0.1898 0.2854 0.4465 -0.0180 -0.0332 0.0884  1004 LYS B CG  
5399 C CD  . LYS B 348 ? 0.3558 0.4491 0.6096 -0.0117 -0.0360 0.0916  1004 LYS B CD  
5400 C CE  . LYS B 348 ? 0.4088 0.4948 0.6610 -0.0127 -0.0380 0.1030  1004 LYS B CE  
5401 N NZ  . LYS B 348 ? 0.4935 0.5841 0.7429 -0.0054 -0.0402 0.1080  1004 LYS B NZ  
5402 N N   . LEU B 349 ? 0.1512 0.2638 0.4191 -0.0293 -0.0271 0.0856  1005 LEU B N   
5403 C CA  . LEU B 349 ? 0.1516 0.2714 0.4262 -0.0376 -0.0274 0.0934  1005 LEU B CA  
5404 C C   . LEU B 349 ? 0.2029 0.3051 0.4789 -0.0455 -0.0339 0.0968  1005 LEU B C   
5405 O O   . LEU B 349 ? 0.2166 0.3011 0.4899 -0.0434 -0.0379 0.0900  1005 LEU B O   
5406 C CB  . LEU B 349 ? 0.1562 0.2892 0.4367 -0.0378 -0.0252 0.0904  1005 LEU B CB  
5407 C CG  . LEU B 349 ? 0.2225 0.3684 0.4991 -0.0290 -0.0180 0.0865  1005 LEU B CG  
5408 C CD1 . LEU B 349 ? 0.2434 0.3981 0.5259 -0.0279 -0.0175 0.0837  1005 LEU B CD1 
5409 C CD2 . LEU B 349 ? 0.1884 0.3509 0.4634 -0.0277 -0.0116 0.0948  1005 LEU B CD2 
5410 N N   . LYS B 350 ? 0.1830 0.2891 0.4616 -0.0548 -0.0348 0.1073  1006 LYS B N   
5411 C CA  . LYS B 350 ? 0.2019 0.2887 0.4791 -0.0655 -0.0413 0.1115  1006 LYS B CA  
5412 C C   . LYS B 350 ? 0.2770 0.3784 0.5623 -0.0764 -0.0429 0.1132  1006 LYS B C   
5413 O O   . LYS B 350 ? 0.2411 0.3712 0.5346 -0.0784 -0.0385 0.1197  1006 LYS B O   
5414 C CB  . LYS B 350 ? 0.2284 0.3106 0.5024 -0.0716 -0.0419 0.1238  1006 LYS B CB  
5415 C CG  . LYS B 350 ? 0.2930 0.3420 0.5585 -0.0788 -0.0487 0.1267  1006 LYS B CG  
5416 C CD  . LYS B 350 ? 0.5009 0.5475 0.7632 -0.0863 -0.0490 0.1410  1006 LYS B CD  
5417 C CE  . LYS B 350 ? 0.6939 0.7044 0.9433 -0.0832 -0.0530 0.1438  1006 LYS B CE  
5418 N NZ  . LYS B 350 ? 0.8484 0.8247 1.0884 -0.0921 -0.0595 0.1407  1006 LYS B NZ  
5419 N N   . PHE B 351 ? 0.2625 0.3453 0.5446 -0.0822 -0.0491 0.1073  1007 PHE B N   
5420 C CA  . PHE B 351 ? 0.2465 0.3400 0.5344 -0.0947 -0.0531 0.1087  1007 PHE B CA  
5421 C C   . PHE B 351 ? 0.3203 0.3990 0.6037 -0.1129 -0.0596 0.1179  1007 PHE B C   
5422 O O   . PHE B 351 ? 0.3394 0.3814 0.6094 -0.1151 -0.0643 0.1148  1007 PHE B O   
5423 C CB  . PHE B 351 ? 0.2642 0.3430 0.5472 -0.0915 -0.0567 0.0960  1007 PHE B CB  
5424 C CG  . PHE B 351 ? 0.2613 0.3556 0.5485 -0.0768 -0.0511 0.0879  1007 PHE B CG  
5425 C CD1 . PHE B 351 ? 0.2877 0.3762 0.5708 -0.0627 -0.0464 0.0828  1007 PHE B CD1 
5426 C CD2 . PHE B 351 ? 0.2575 0.3715 0.5515 -0.0779 -0.0512 0.0859  1007 PHE B CD2 
5427 C CE1 . PHE B 351 ? 0.2856 0.3852 0.5701 -0.0518 -0.0418 0.0757  1007 PHE B CE1 
5428 C CE2 . PHE B 351 ? 0.2849 0.4090 0.5802 -0.0646 -0.0460 0.0790  1007 PHE B CE2 
5429 C CZ  . PHE B 351 ? 0.2695 0.3847 0.5593 -0.0525 -0.0414 0.0738  1007 PHE B CZ  
5430 N N   . ASN B 352 ? 0.2839 0.3902 0.5772 -0.1254 -0.0593 0.1302  1008 ASN B N   
5431 C CA  . ASN B 352 ? 0.2866 0.3811 0.5755 -0.1464 -0.0659 0.1409  1008 ASN B CA  
5432 C C   . ASN B 352 ? 0.3570 0.4610 0.6495 -0.1639 -0.0732 0.1416  1008 ASN B C   
5433 O O   . ASN B 352 ? 0.3163 0.4622 0.6243 -0.1693 -0.0715 0.1496  1008 ASN B O   
5434 C CB  . ASN B 352 ? 0.2728 0.3897 0.5684 -0.1509 -0.0613 0.1562  1008 ASN B CB  
5435 C CG  . ASN B 352 ? 0.6463 0.7443 0.9332 -0.1379 -0.0572 0.1562  1008 ASN B CG  
5436 O OD1 . ASN B 352 ? 0.6095 0.6713 0.8830 -0.1419 -0.0617 0.1577  1008 ASN B OD1 
5437 N ND2 . ASN B 352 ? 0.5006 0.6214 0.7930 -0.1219 -0.0487 0.1548  1008 ASN B ND2 
5438 N N   . PHE B 353 ? 0.3618 0.4277 0.6389 -0.1702 -0.0809 0.1323  1009 PHE B N   
5439 C CA  . PHE B 353 ? 0.3661 0.4334 0.6413 -0.1878 -0.0895 0.1305  1009 PHE B CA  
5440 C C   . PHE B 353 ? 0.4536 0.5276 0.7292 -0.2155 -0.0966 0.1449  1009 PHE B C   
5441 O O   . PHE B 353 ? 0.4557 0.4991 0.7184 -0.2250 -0.0993 0.1505  1009 PHE B O   
5442 C CB  . PHE B 353 ? 0.4102 0.4296 0.6640 -0.1852 -0.0949 0.1152  1009 PHE B CB  
5443 C CG  . PHE B 353 ? 0.4254 0.4445 0.6805 -0.1606 -0.0885 0.1018  1009 PHE B CG  
5444 C CD1 . PHE B 353 ? 0.4541 0.4974 0.7175 -0.1567 -0.0884 0.0957  1009 PHE B CD1 
5445 C CD2 . PHE B 353 ? 0.4573 0.4554 0.7061 -0.1417 -0.0828 0.0968  1009 PHE B CD2 
5446 C CE1 . PHE B 353 ? 0.4565 0.4993 0.7203 -0.1356 -0.0826 0.0844  1009 PHE B CE1 
5447 C CE2 . PHE B 353 ? 0.4844 0.4863 0.7353 -0.1214 -0.0772 0.0859  1009 PHE B CE2 
5448 C CZ  . PHE B 353 ? 0.4474 0.4703 0.7052 -0.1190 -0.0771 0.0797  1009 PHE B CZ  
5449 N N   . LYS B 354 ? 0.4256 0.5425 0.7165 -0.2283 -0.0994 0.1526  1010 LYS B N   
5450 C CA  . LYS B 354 ? 0.4353 0.5658 0.7285 -0.2579 -0.1071 0.1677  1010 LYS B CA  
5451 C C   . LYS B 354 ? 0.5306 0.6363 0.8082 -0.2781 -0.1196 0.1608  1010 LYS B C   
5452 O O   . LYS B 354 ? 0.5166 0.6379 0.7989 -0.2728 -0.1212 0.1528  1010 LYS B O   
5453 C CB  . LYS B 354 ? 0.4351 0.6339 0.7556 -0.2601 -0.1021 0.1834  1010 LYS B CB  
5454 C CG  . LYS B 354 ? 0.4560 0.6735 0.7860 -0.2461 -0.0908 0.1924  1010 LYS B CG  
5455 C CD  . LYS B 354 ? 0.4408 0.7188 0.7944 -0.2308 -0.0807 0.1993  1010 LYS B CD  
5456 C CE  . LYS B 354 ? 0.5211 0.7994 0.8761 -0.2053 -0.0752 0.1844  1010 LYS B CE  
5457 N NZ  . LYS B 354 ? 0.5755 0.9107 0.9510 -0.1940 -0.0677 0.1921  1010 LYS B NZ  
5458 N N   . THR B 355 ? 0.5229 0.5837 0.7784 -0.3000 -0.1284 0.1629  1011 THR B N   
5459 C CA  . THR B 355 ? 0.9413 0.9639 1.1731 -0.3220 -0.1411 0.1554  1011 THR B CA  
5460 C C   . THR B 355 ? 1.0366 1.1034 1.2805 -0.3509 -0.1506 0.1669  1011 THR B C   
5461 O O   . THR B 355 ? 0.5528 0.6107 0.7874 -0.3818 -0.1598 0.1778  1011 THR B O   
5462 C CB  . THR B 355 ? 1.0544 1.0082 1.2547 -0.3333 -0.1460 0.1538  1011 THR B CB  
5463 O OG1 . THR B 355 ? 1.0369 1.0045 1.2444 -0.3484 -0.1456 0.1722  1011 THR B OG1 
5464 C CG2 . THR B 355 ? 1.0308 0.9379 1.2157 -0.3030 -0.1383 0.1395  1011 THR B CG2 
# 
