data_8TRW
# 
_entry.id   8TRW 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   8TRW         pdb_00008trw 10.2210/pdb8trw/pdb 
WWPDB D_1000276530 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-11 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8TRW 
_pdbx_database_status.recvd_initial_deposition_date   2023-08-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              sjb14@psu.edu 
_pdbx_contact_author.name_first         Squire 
_pdbx_contact_author.name_last          Booker 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7211-5937 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Esakova, O.A.' 1 0000-0001-8377-8368 
'Warui, D.M.'   2 ?                   
'Neti, S.S.'    3 ?                   
'Alumasa, J.N.' 4 ?                   
'Booker, S.J.'  5 0000-0002-7211-5937 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Structural basis for the mechanism of the human lipoyl synthase (LIAS) and its complex with the H-protein' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Esakova, O.A.' 1 0000-0001-8377-8368 
primary 'Warui, D.M.'   2 ?                   
primary 'Neti, S.S.'    3 0000-0003-3343-8642 
primary 'Alumasa, J.N.' 4 0000-0002-9373-9618 
primary 'Booker, S.J.'  5 0000-0002-7211-5937 
# 
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 'Lipoyl synthase, mitochondrial'                    41543.613 1   ? ? ? ? 
2 branched    syn 'alpha-D-glucopyranose-(1-1)-alpha-D-glucopyranose' 342.297   1   ? ? ? ? 
3 non-polymer syn 2,3-DIHYDROXY-1,4-DITHIOBUTANE                      154.251   1   ? ? ? ? 
4 non-polymer syn 'SULFATE ION'                                       96.063    1   ? ? ? ? 
5 non-polymer syn 'IRON/SULFUR CLUSTER'                               351.640   2   ? ? ? ? 
6 water       nat water                                               18.015    371 ? ? ? ? 
# 
_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       
;MSLRCGDAARTLGPRVFGRYFCSPVRPLSSLPDKKKELLQNGPDLQDFVSGDLADRSTWDEYKGNLKRQKGERLRLPPWL
KTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGGGEYATATATIMLMGDTCTRGCRFCSVKTARNPPPLDASEP
YNTAKAIAEWGLDYVVLTSVDRDDMPDGGAEHIAKTVSYLKERNPKILVECLTPDFRGDLKAIEKVALSGLDVYAHNVET
VPELQSKVRDPRVNFDQSLRVLKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREADVDCLTLGQYMQPTRRHLKVE
EYITPEKFKYWEKVGNELGFHYTASGPLVRSSYKAGEFFLKNLVAKRK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSLRCGDAARTLGPRVFGRYFCSPVRPLSSLPDKKKELLQNGPDLQDFVSGDLADRSTWDEYKGNLKRQKGERLRLPPWL
KTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGGGEYATATATIMLMGDTCTRGCRFCSVKTARNPPPLDASEP
YNTAKAIAEWGLDYVVLTSVDRDDMPDGGAEHIAKTVSYLKERNPKILVECLTPDFRGDLKAIEKVALSGLDVYAHNVET
VPELQSKVRDPRVNFDQSLRVLKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREADVDCLTLGQYMQPTRRHLKVE
EYITPEKFKYWEKVGNELGFHYTASGPLVRSSYKAGEFFLKNLVAKRK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 2,3-DIHYDROXY-1,4-DITHIOBUTANE DTT 
4 'SULFATE ION'                  SO4 
5 'IRON/SULFUR CLUSTER'          SF4 
6 water                          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   LEU n 
1 4   ARG n 
1 5   CYS n 
1 6   GLY n 
1 7   ASP n 
1 8   ALA n 
1 9   ALA n 
1 10  ARG n 
1 11  THR n 
1 12  LEU n 
1 13  GLY n 
1 14  PRO n 
1 15  ARG n 
1 16  VAL n 
1 17  PHE n 
1 18  GLY n 
1 19  ARG n 
1 20  TYR n 
1 21  PHE n 
1 22  CYS n 
1 23  SER n 
1 24  PRO n 
1 25  VAL n 
1 26  ARG n 
1 27  PRO n 
1 28  LEU n 
1 29  SER n 
1 30  SER n 
1 31  LEU n 
1 32  PRO n 
1 33  ASP n 
1 34  LYS n 
1 35  LYS n 
1 36  LYS n 
1 37  GLU n 
1 38  LEU n 
1 39  LEU n 
1 40  GLN n 
1 41  ASN n 
1 42  GLY n 
1 43  PRO n 
1 44  ASP n 
1 45  LEU n 
1 46  GLN n 
1 47  ASP n 
1 48  PHE n 
1 49  VAL n 
1 50  SER n 
1 51  GLY n 
1 52  ASP n 
1 53  LEU n 
1 54  ALA n 
1 55  ASP n 
1 56  ARG n 
1 57  SER n 
1 58  THR n 
1 59  TRP n 
1 60  ASP n 
1 61  GLU n 
1 62  TYR n 
1 63  LYS n 
1 64  GLY n 
1 65  ASN n 
1 66  LEU n 
1 67  LYS n 
1 68  ARG n 
1 69  GLN n 
1 70  LYS n 
1 71  GLY n 
1 72  GLU n 
1 73  ARG n 
1 74  LEU n 
1 75  ARG n 
1 76  LEU n 
1 77  PRO n 
1 78  PRO n 
1 79  TRP n 
1 80  LEU n 
1 81  LYS n 
1 82  THR n 
1 83  GLU n 
1 84  ILE n 
1 85  PRO n 
1 86  MET n 
1 87  GLY n 
1 88  LYS n 
1 89  ASN n 
1 90  TYR n 
1 91  ASN n 
1 92  LYS n 
1 93  LEU n 
1 94  LYS n 
1 95  ASN n 
1 96  THR n 
1 97  LEU n 
1 98  ARG n 
1 99  ASN n 
1 100 LEU n 
1 101 ASN n 
1 102 LEU n 
1 103 HIS n 
1 104 THR n 
1 105 VAL n 
1 106 CYS n 
1 107 GLU n 
1 108 GLU n 
1 109 ALA n 
1 110 ARG n 
1 111 CYS n 
1 112 PRO n 
1 113 ASN n 
1 114 ILE n 
1 115 GLY n 
1 116 GLU n 
1 117 CYS n 
1 118 TRP n 
1 119 GLY n 
1 120 GLY n 
1 121 GLY n 
1 122 GLU n 
1 123 TYR n 
1 124 ALA n 
1 125 THR n 
1 126 ALA n 
1 127 THR n 
1 128 ALA n 
1 129 THR n 
1 130 ILE n 
1 131 MET n 
1 132 LEU n 
1 133 MET n 
1 134 GLY n 
1 135 ASP n 
1 136 THR n 
1 137 CYS n 
1 138 THR n 
1 139 ARG n 
1 140 GLY n 
1 141 CYS n 
1 142 ARG n 
1 143 PHE n 
1 144 CYS n 
1 145 SER n 
1 146 VAL n 
1 147 LYS n 
1 148 THR n 
1 149 ALA n 
1 150 ARG n 
1 151 ASN n 
1 152 PRO n 
1 153 PRO n 
1 154 PRO n 
1 155 LEU n 
1 156 ASP n 
1 157 ALA n 
1 158 SER n 
1 159 GLU n 
1 160 PRO n 
1 161 TYR n 
1 162 ASN n 
1 163 THR n 
1 164 ALA n 
1 165 LYS n 
1 166 ALA n 
1 167 ILE n 
1 168 ALA n 
1 169 GLU n 
1 170 TRP n 
1 171 GLY n 
1 172 LEU n 
1 173 ASP n 
1 174 TYR n 
1 175 VAL n 
1 176 VAL n 
1 177 LEU n 
1 178 THR n 
1 179 SER n 
1 180 VAL n 
1 181 ASP n 
1 182 ARG n 
1 183 ASP n 
1 184 ASP n 
1 185 MET n 
1 186 PRO n 
1 187 ASP n 
1 188 GLY n 
1 189 GLY n 
1 190 ALA n 
1 191 GLU n 
1 192 HIS n 
1 193 ILE n 
1 194 ALA n 
1 195 LYS n 
1 196 THR n 
1 197 VAL n 
1 198 SER n 
1 199 TYR n 
1 200 LEU n 
1 201 LYS n 
1 202 GLU n 
1 203 ARG n 
1 204 ASN n 
1 205 PRO n 
1 206 LYS n 
1 207 ILE n 
1 208 LEU n 
1 209 VAL n 
1 210 GLU n 
1 211 CYS n 
1 212 LEU n 
1 213 THR n 
1 214 PRO n 
1 215 ASP n 
1 216 PHE n 
1 217 ARG n 
1 218 GLY n 
1 219 ASP n 
1 220 LEU n 
1 221 LYS n 
1 222 ALA n 
1 223 ILE n 
1 224 GLU n 
1 225 LYS n 
1 226 VAL n 
1 227 ALA n 
1 228 LEU n 
1 229 SER n 
1 230 GLY n 
1 231 LEU n 
1 232 ASP n 
1 233 VAL n 
1 234 TYR n 
1 235 ALA n 
1 236 HIS n 
1 237 ASN n 
1 238 VAL n 
1 239 GLU n 
1 240 THR n 
1 241 VAL n 
1 242 PRO n 
1 243 GLU n 
1 244 LEU n 
1 245 GLN n 
1 246 SER n 
1 247 LYS n 
1 248 VAL n 
1 249 ARG n 
1 250 ASP n 
1 251 PRO n 
1 252 ARG n 
1 253 VAL n 
1 254 ASN n 
1 255 PHE n 
1 256 ASP n 
1 257 GLN n 
1 258 SER n 
1 259 LEU n 
1 260 ARG n 
1 261 VAL n 
1 262 LEU n 
1 263 LYS n 
1 264 HIS n 
1 265 ALA n 
1 266 LYS n 
1 267 LYS n 
1 268 VAL n 
1 269 GLN n 
1 270 PRO n 
1 271 ASP n 
1 272 VAL n 
1 273 ILE n 
1 274 SER n 
1 275 LYS n 
1 276 THR n 
1 277 SER n 
1 278 ILE n 
1 279 MET n 
1 280 LEU n 
1 281 GLY n 
1 282 LEU n 
1 283 GLY n 
1 284 GLU n 
1 285 ASN n 
1 286 ASP n 
1 287 GLU n 
1 288 GLN n 
1 289 VAL n 
1 290 TYR n 
1 291 ALA n 
1 292 THR n 
1 293 MET n 
1 294 LYS n 
1 295 ALA n 
1 296 LEU n 
1 297 ARG n 
1 298 GLU n 
1 299 ALA n 
1 300 ASP n 
1 301 VAL n 
1 302 ASP n 
1 303 CYS n 
1 304 LEU n 
1 305 THR n 
1 306 LEU n 
1 307 GLY n 
1 308 GLN n 
1 309 TYR n 
1 310 MET n 
1 311 GLN n 
1 312 PRO n 
1 313 THR n 
1 314 ARG n 
1 315 ARG n 
1 316 HIS n 
1 317 LEU n 
1 318 LYS n 
1 319 VAL n 
1 320 GLU n 
1 321 GLU n 
1 322 TYR n 
1 323 ILE n 
1 324 THR n 
1 325 PRO n 
1 326 GLU n 
1 327 LYS n 
1 328 PHE n 
1 329 LYS n 
1 330 TYR n 
1 331 TRP n 
1 332 GLU n 
1 333 LYS n 
1 334 VAL n 
1 335 GLY n 
1 336 ASN n 
1 337 GLU n 
1 338 LEU n 
1 339 GLY n 
1 340 PHE n 
1 341 HIS n 
1 342 TYR n 
1 343 THR n 
1 344 ALA n 
1 345 SER n 
1 346 GLY n 
1 347 PRO n 
1 348 LEU n 
1 349 VAL n 
1 350 ARG n 
1 351 SER n 
1 352 SER n 
1 353 TYR n 
1 354 LYS n 
1 355 ALA n 
1 356 GLY n 
1 357 GLU n 
1 358 PHE n 
1 359 PHE n 
1 360 LEU n 
1 361 LYS n 
1 362 ASN n 
1 363 LEU n 
1 364 VAL n 
1 365 ALA n 
1 366 LYS n 
1 367 ARG n 
1 368 LYS 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                   368 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 LIAS 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     561 
_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                   ? 
# 
_pdbx_entity_branch.entity_id   2 
_pdbx_entity_branch.type        oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 2 DGlcpa1-1DGlcpa                             'Glycam Condensed Sequence' GMML       1.0   
2 2 'WURCS=2.0/1,2,1/[a2122h-1a_1-5]/1-1/a1-b1' WURCS                       PDB2Glycan 1.1.0 
3 2 '[][a-D-Glcp]{[(1+1)][a-D-Glcp]{}}'         LINUCS                      PDB-CARE   ?     
# 
_pdbx_entity_branch_link.link_id                    1 
_pdbx_entity_branch_link.entity_id                  2 
_pdbx_entity_branch_link.entity_branch_list_num_1   2 
_pdbx_entity_branch_link.comp_id_1                  GLC 
_pdbx_entity_branch_link.atom_id_1                  C1 
_pdbx_entity_branch_link.leaving_atom_id_1          O1 
_pdbx_entity_branch_link.entity_branch_list_num_2   1 
_pdbx_entity_branch_link.comp_id_2                  GLC 
_pdbx_entity_branch_link.atom_id_2                  O1 
_pdbx_entity_branch_link.leaving_atom_id_2          HO1 
_pdbx_entity_branch_link.value_order                sing 
_pdbx_entity_branch_link.details                    ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking'           y ALANINE                        ?                                     'C3 H7 N O2'     89.093  
ARG 'L-peptide linking'           y ARGININE                       ?                                     'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking'           y ASPARAGINE                     ?                                     'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking'           y 'ASPARTIC ACID'                ?                                     'C4 H7 N O4'     133.103 
CYS 'L-peptide linking'           y CYSTEINE                       ?                                     'C3 H7 N O2 S'   121.158 
DTT non-polymer                   . 2,3-DIHYDROXY-1,4-DITHIOBUTANE 1,4-DITHIOTHREITOL                    'C4 H10 O2 S2'   154.251 
GLC 'D-saccharide, alpha linking' . alpha-D-glucopyranose          'alpha-D-glucose; D-glucose; glucose' 'C6 H12 O6'      180.156 
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 
SF4 non-polymer                   . 'IRON/SULFUR CLUSTER'          ?                                     'Fe4 S4'         351.640 
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_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
GLC 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpa            
GLC 'COMMON NAME'                         GMML     1.0 a-D-glucopyranose 
GLC 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Glcp          
GLC 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Glc               
# 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   LEU 3   3   ?   ?   ?   A . n 
A 1 4   ARG 4   4   ?   ?   ?   A . n 
A 1 5   CYS 5   5   ?   ?   ?   A . n 
A 1 6   GLY 6   6   ?   ?   ?   A . n 
A 1 7   ASP 7   7   ?   ?   ?   A . n 
A 1 8   ALA 8   8   ?   ?   ?   A . n 
A 1 9   ALA 9   9   ?   ?   ?   A . n 
A 1 10  ARG 10  10  ?   ?   ?   A . n 
A 1 11  THR 11  11  ?   ?   ?   A . n 
A 1 12  LEU 12  12  ?   ?   ?   A . n 
A 1 13  GLY 13  13  ?   ?   ?   A . n 
A 1 14  PRO 14  14  ?   ?   ?   A . n 
A 1 15  ARG 15  15  ?   ?   ?   A . n 
A 1 16  VAL 16  16  ?   ?   ?   A . n 
A 1 17  PHE 17  17  ?   ?   ?   A . n 
A 1 18  GLY 18  18  ?   ?   ?   A . n 
A 1 19  ARG 19  19  ?   ?   ?   A . n 
A 1 20  TYR 20  20  ?   ?   ?   A . n 
A 1 21  PHE 21  21  ?   ?   ?   A . n 
A 1 22  CYS 22  22  ?   ?   ?   A . n 
A 1 23  SER 23  23  ?   ?   ?   A . n 
A 1 24  PRO 24  24  ?   ?   ?   A . n 
A 1 25  VAL 25  25  ?   ?   ?   A . n 
A 1 26  ARG 26  26  ?   ?   ?   A . n 
A 1 27  PRO 27  27  ?   ?   ?   A . n 
A 1 28  LEU 28  28  ?   ?   ?   A . n 
A 1 29  SER 29  29  ?   ?   ?   A . n 
A 1 30  SER 30  30  ?   ?   ?   A . n 
A 1 31  LEU 31  31  ?   ?   ?   A . n 
A 1 32  PRO 32  32  ?   ?   ?   A . n 
A 1 33  ASP 33  33  ?   ?   ?   A . n 
A 1 34  LYS 34  34  ?   ?   ?   A . n 
A 1 35  LYS 35  35  ?   ?   ?   A . n 
A 1 36  LYS 36  36  ?   ?   ?   A . n 
A 1 37  GLU 37  37  ?   ?   ?   A . n 
A 1 38  LEU 38  38  ?   ?   ?   A . n 
A 1 39  LEU 39  39  ?   ?   ?   A . n 
A 1 40  GLN 40  40  ?   ?   ?   A . n 
A 1 41  ASN 41  41  ?   ?   ?   A . n 
A 1 42  GLY 42  42  ?   ?   ?   A . n 
A 1 43  PRO 43  43  ?   ?   ?   A . n 
A 1 44  ASP 44  44  ?   ?   ?   A . n 
A 1 45  LEU 45  45  ?   ?   ?   A . n 
A 1 46  GLN 46  46  ?   ?   ?   A . n 
A 1 47  ASP 47  47  ?   ?   ?   A . n 
A 1 48  PHE 48  48  ?   ?   ?   A . n 
A 1 49  VAL 49  49  ?   ?   ?   A . n 
A 1 50  SER 50  50  ?   ?   ?   A . n 
A 1 51  GLY 51  51  ?   ?   ?   A . n 
A 1 52  ASP 52  52  ?   ?   ?   A . n 
A 1 53  LEU 53  53  ?   ?   ?   A . n 
A 1 54  ALA 54  54  ?   ?   ?   A . n 
A 1 55  ASP 55  55  ?   ?   ?   A . n 
A 1 56  ARG 56  56  ?   ?   ?   A . n 
A 1 57  SER 57  57  ?   ?   ?   A . n 
A 1 58  THR 58  58  ?   ?   ?   A . n 
A 1 59  TRP 59  59  ?   ?   ?   A . n 
A 1 60  ASP 60  60  ?   ?   ?   A . n 
A 1 61  GLU 61  61  ?   ?   ?   A . n 
A 1 62  TYR 62  62  ?   ?   ?   A . n 
A 1 63  LYS 63  63  ?   ?   ?   A . n 
A 1 64  GLY 64  64  ?   ?   ?   A . n 
A 1 65  ASN 65  65  ?   ?   ?   A . n 
A 1 66  LEU 66  66  ?   ?   ?   A . n 
A 1 67  LYS 67  67  ?   ?   ?   A . n 
A 1 68  ARG 68  68  ?   ?   ?   A . n 
A 1 69  GLN 69  69  ?   ?   ?   A . n 
A 1 70  LYS 70  70  ?   ?   ?   A . n 
A 1 71  GLY 71  71  ?   ?   ?   A . n 
A 1 72  GLU 72  72  ?   ?   ?   A . n 
A 1 73  ARG 73  73  ?   ?   ?   A . n 
A 1 74  LEU 74  74  ?   ?   ?   A . n 
A 1 75  ARG 75  75  75  ARG ARG A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  PRO 77  77  77  PRO PRO A . n 
A 1 78  PRO 78  78  78  PRO PRO A . n 
A 1 79  TRP 79  79  79  TRP TRP A . n 
A 1 80  LEU 80  80  80  LEU LEU A . n 
A 1 81  LYS 81  81  81  LYS LYS A . n 
A 1 82  THR 82  82  82  THR THR A . n 
A 1 83  GLU 83  83  83  GLU GLU A . n 
A 1 84  ILE 84  84  84  ILE ILE A . n 
A 1 85  PRO 85  85  85  PRO PRO A . n 
A 1 86  MET 86  86  86  MET MET A . n 
A 1 87  GLY 87  87  87  GLY GLY A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  ASN 89  89  89  ASN ASN A . n 
A 1 90  TYR 90  90  90  TYR TYR A . n 
A 1 91  ASN 91  91  91  ASN ASN A . n 
A 1 92  LYS 92  92  92  LYS LYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  LYS 94  94  94  LYS LYS A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  THR 96  96  96  THR THR A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  ARG 98  98  98  ARG ARG A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 HIS 103 103 103 HIS HIS A . n 
A 1 104 THR 104 104 104 THR THR A . n 
A 1 105 VAL 105 105 105 VAL VAL A . n 
A 1 106 CYS 106 106 106 CYS CYS A . n 
A 1 107 GLU 107 107 107 GLU GLU A . n 
A 1 108 GLU 108 108 108 GLU GLU A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 ARG 110 110 110 ARG ARG A . n 
A 1 111 CYS 111 111 111 CYS CYS A . n 
A 1 112 PRO 112 112 112 PRO PRO A . n 
A 1 113 ASN 113 113 113 ASN ASN A . n 
A 1 114 ILE 114 114 114 ILE ILE A . n 
A 1 115 GLY 115 115 115 GLY GLY A . n 
A 1 116 GLU 116 116 116 GLU GLU A . n 
A 1 117 CYS 117 117 117 CYS CYS A . n 
A 1 118 TRP 118 118 118 TRP TRP A . n 
A 1 119 GLY 119 119 119 GLY GLY A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 GLY 121 121 121 GLY GLY A . n 
A 1 122 GLU 122 122 122 GLU GLU A . n 
A 1 123 TYR 123 123 123 TYR TYR A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 ALA 126 126 126 ALA ALA A . n 
A 1 127 THR 127 127 127 THR THR A . n 
A 1 128 ALA 128 128 128 ALA ALA A . n 
A 1 129 THR 129 129 129 THR THR A . n 
A 1 130 ILE 130 130 130 ILE ILE A . n 
A 1 131 MET 131 131 131 MET MET A . n 
A 1 132 LEU 132 132 132 LEU LEU A . n 
A 1 133 MET 133 133 133 MET MET A . n 
A 1 134 GLY 134 134 134 GLY GLY A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 THR 136 136 136 THR THR A . n 
A 1 137 CYS 137 137 137 CYS CYS A . n 
A 1 138 THR 138 138 138 THR THR A . n 
A 1 139 ARG 139 139 139 ARG ARG A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 CYS 141 141 141 CYS CYS A . n 
A 1 142 ARG 142 142 142 ARG ARG A . n 
A 1 143 PHE 143 143 143 PHE PHE A . n 
A 1 144 CYS 144 144 144 CYS CYS A . n 
A 1 145 SER 145 145 145 SER SER A . n 
A 1 146 VAL 146 146 146 VAL VAL A . n 
A 1 147 LYS 147 147 147 LYS LYS A . n 
A 1 148 THR 148 148 148 THR THR A . n 
A 1 149 ALA 149 149 149 ALA ALA A . n 
A 1 150 ARG 150 150 150 ARG ARG A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 PRO 152 152 152 PRO PRO A . n 
A 1 153 PRO 153 153 153 PRO PRO A . n 
A 1 154 PRO 154 154 154 PRO PRO A . n 
A 1 155 LEU 155 155 155 LEU LEU A . n 
A 1 156 ASP 156 156 156 ASP ASP A . n 
A 1 157 ALA 157 157 157 ALA ALA A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 GLU 159 159 159 GLU GLU A . n 
A 1 160 PRO 160 160 160 PRO PRO A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASN 162 162 162 ASN ASN A . n 
A 1 163 THR 163 163 163 THR THR A . n 
A 1 164 ALA 164 164 164 ALA ALA A . n 
A 1 165 LYS 165 165 165 LYS LYS A . n 
A 1 166 ALA 166 166 166 ALA ALA A . n 
A 1 167 ILE 167 167 167 ILE ILE A . n 
A 1 168 ALA 168 168 168 ALA ALA A . n 
A 1 169 GLU 169 169 169 GLU GLU A . n 
A 1 170 TRP 170 170 170 TRP TRP A . n 
A 1 171 GLY 171 171 171 GLY GLY A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 ASP 173 173 173 ASP ASP A . n 
A 1 174 TYR 174 174 174 TYR TYR A . n 
A 1 175 VAL 175 175 175 VAL VAL A . n 
A 1 176 VAL 176 176 176 VAL VAL A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 THR 178 178 178 THR THR A . n 
A 1 179 SER 179 179 179 SER SER A . n 
A 1 180 VAL 180 180 180 VAL VAL A . n 
A 1 181 ASP 181 181 181 ASP ASP A . n 
A 1 182 ARG 182 182 182 ARG ARG A . n 
A 1 183 ASP 183 183 183 ASP ASP A . n 
A 1 184 ASP 184 184 184 ASP ASP A . n 
A 1 185 MET 185 185 185 MET MET A . n 
A 1 186 PRO 186 186 186 PRO PRO A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 GLY 188 188 188 GLY GLY A . n 
A 1 189 GLY 189 189 189 GLY GLY A . n 
A 1 190 ALA 190 190 190 ALA ALA A . n 
A 1 191 GLU 191 191 191 GLU GLU A . n 
A 1 192 HIS 192 192 192 HIS HIS A . n 
A 1 193 ILE 193 193 193 ILE ILE A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 LYS 195 195 195 LYS LYS A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 VAL 197 197 197 VAL VAL A . n 
A 1 198 SER 198 198 198 SER SER A . n 
A 1 199 TYR 199 199 199 TYR TYR A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 LYS 201 201 201 LYS LYS A . n 
A 1 202 GLU 202 202 202 GLU GLU A . n 
A 1 203 ARG 203 203 203 ARG ARG A . n 
A 1 204 ASN 204 204 204 ASN ASN A . n 
A 1 205 PRO 205 205 205 PRO PRO A . n 
A 1 206 LYS 206 206 206 LYS LYS A . n 
A 1 207 ILE 207 207 207 ILE ILE A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 VAL 209 209 209 VAL VAL A . n 
A 1 210 GLU 210 210 210 GLU GLU A . n 
A 1 211 CYS 211 211 211 CYS CYS A . n 
A 1 212 LEU 212 212 212 LEU LEU A . n 
A 1 213 THR 213 213 213 THR THR A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 ASP 215 215 215 ASP ASP A . n 
A 1 216 PHE 216 216 216 PHE PHE A . n 
A 1 217 ARG 217 217 217 ARG ARG A . n 
A 1 218 GLY 218 218 218 GLY GLY A . n 
A 1 219 ASP 219 219 219 ASP ASP A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 LYS 221 221 221 LYS LYS A . n 
A 1 222 ALA 222 222 222 ALA ALA A . n 
A 1 223 ILE 223 223 223 ILE ILE A . n 
A 1 224 GLU 224 224 224 GLU GLU A . n 
A 1 225 LYS 225 225 225 LYS LYS A . n 
A 1 226 VAL 226 226 226 VAL VAL A . n 
A 1 227 ALA 227 227 227 ALA ALA A . n 
A 1 228 LEU 228 228 228 LEU LEU A . n 
A 1 229 SER 229 229 229 SER SER A . n 
A 1 230 GLY 230 230 230 GLY GLY A . n 
A 1 231 LEU 231 231 231 LEU LEU A . n 
A 1 232 ASP 232 232 232 ASP ASP A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 TYR 234 234 234 TYR TYR A . n 
A 1 235 ALA 235 235 235 ALA ALA A . n 
A 1 236 HIS 236 236 236 HIS HIS A . n 
A 1 237 ASN 237 237 237 ASN ASN A . n 
A 1 238 VAL 238 238 238 VAL VAL A . n 
A 1 239 GLU 239 239 239 GLU GLU A . n 
A 1 240 THR 240 240 240 THR THR A . n 
A 1 241 VAL 241 241 241 VAL VAL A . n 
A 1 242 PRO 242 242 242 PRO PRO A . n 
A 1 243 GLU 243 243 243 GLU GLU A . n 
A 1 244 LEU 244 244 244 LEU LEU A . n 
A 1 245 GLN 245 245 245 GLN GLN A . n 
A 1 246 SER 246 246 246 SER SER A . n 
A 1 247 LYS 247 247 247 LYS LYS A . n 
A 1 248 VAL 248 248 248 VAL VAL A . n 
A 1 249 ARG 249 249 249 ARG ARG A . n 
A 1 250 ASP 250 250 250 ASP ASP A . n 
A 1 251 PRO 251 251 251 PRO PRO A . n 
A 1 252 ARG 252 252 252 ARG ARG A . n 
A 1 253 VAL 253 253 253 VAL VAL A . n 
A 1 254 ASN 254 254 254 ASN ASN A . n 
A 1 255 PHE 255 255 255 PHE PHE A . n 
A 1 256 ASP 256 256 256 ASP ASP A . n 
A 1 257 GLN 257 257 257 GLN GLN A . n 
A 1 258 SER 258 258 258 SER SER A . n 
A 1 259 LEU 259 259 259 LEU LEU A . n 
A 1 260 ARG 260 260 260 ARG ARG A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 LYS 263 263 263 LYS LYS A . n 
A 1 264 HIS 264 264 264 HIS HIS A . n 
A 1 265 ALA 265 265 265 ALA ALA A . n 
A 1 266 LYS 266 266 266 LYS LYS A . n 
A 1 267 LYS 267 267 267 LYS LYS A . n 
A 1 268 VAL 268 268 268 VAL VAL A . n 
A 1 269 GLN 269 269 269 GLN GLN A . n 
A 1 270 PRO 270 270 270 PRO PRO A . n 
A 1 271 ASP 271 271 271 ASP ASP A . n 
A 1 272 VAL 272 272 272 VAL VAL A . n 
A 1 273 ILE 273 273 273 ILE ILE A . n 
A 1 274 SER 274 274 274 SER SER A . n 
A 1 275 LYS 275 275 275 LYS LYS A . n 
A 1 276 THR 276 276 276 THR THR A . n 
A 1 277 SER 277 277 277 SER SER A . n 
A 1 278 ILE 278 278 278 ILE ILE A . n 
A 1 279 MET 279 279 279 MET MET A . n 
A 1 280 LEU 280 280 280 LEU LEU A . n 
A 1 281 GLY 281 281 281 GLY GLY A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 GLU 284 284 284 GLU GLU A . n 
A 1 285 ASN 285 285 285 ASN ASN A . n 
A 1 286 ASP 286 286 286 ASP ASP A . n 
A 1 287 GLU 287 287 287 GLU GLU A . n 
A 1 288 GLN 288 288 288 GLN GLN A . n 
A 1 289 VAL 289 289 289 VAL VAL A . n 
A 1 290 TYR 290 290 290 TYR TYR A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 THR 292 292 292 THR THR A . n 
A 1 293 MET 293 293 293 MET MET A . n 
A 1 294 LYS 294 294 294 LYS LYS A . n 
A 1 295 ALA 295 295 295 ALA ALA A . n 
A 1 296 LEU 296 296 296 LEU LEU A . n 
A 1 297 ARG 297 297 297 ARG ARG A . n 
A 1 298 GLU 298 298 298 GLU GLU A . n 
A 1 299 ALA 299 299 299 ALA ALA A . n 
A 1 300 ASP 300 300 300 ASP ASP A . n 
A 1 301 VAL 301 301 301 VAL VAL A . n 
A 1 302 ASP 302 302 302 ASP ASP A . n 
A 1 303 CYS 303 303 303 CYS CYS A . n 
A 1 304 LEU 304 304 304 LEU LEU A . n 
A 1 305 THR 305 305 305 THR THR A . n 
A 1 306 LEU 306 306 306 LEU LEU A . n 
A 1 307 GLY 307 307 307 GLY GLY A . n 
A 1 308 GLN 308 308 308 GLN GLN A . n 
A 1 309 TYR 309 309 309 TYR TYR A . n 
A 1 310 MET 310 310 310 MET MET A . n 
A 1 311 GLN 311 311 311 GLN GLN A . n 
A 1 312 PRO 312 312 312 PRO PRO A . n 
A 1 313 THR 313 313 313 THR THR A . n 
A 1 314 ARG 314 314 314 ARG ARG A . n 
A 1 315 ARG 315 315 315 ARG ARG A . n 
A 1 316 HIS 316 316 316 HIS HIS A . n 
A 1 317 LEU 317 317 317 LEU LEU A . n 
A 1 318 LYS 318 318 318 LYS LYS A . n 
A 1 319 VAL 319 319 319 VAL VAL A . n 
A 1 320 GLU 320 320 320 GLU GLU A . n 
A 1 321 GLU 321 321 321 GLU GLU A . n 
A 1 322 TYR 322 322 322 TYR TYR A . n 
A 1 323 ILE 323 323 323 ILE ILE A . n 
A 1 324 THR 324 324 324 THR THR A . n 
A 1 325 PRO 325 325 325 PRO PRO A . n 
A 1 326 GLU 326 326 326 GLU GLU A . n 
A 1 327 LYS 327 327 327 LYS LYS A . n 
A 1 328 PHE 328 328 328 PHE PHE A . n 
A 1 329 LYS 329 329 329 LYS LYS A . n 
A 1 330 TYR 330 330 330 TYR TYR A . n 
A 1 331 TRP 331 331 331 TRP TRP A . n 
A 1 332 GLU 332 332 332 GLU GLU A . n 
A 1 333 LYS 333 333 333 LYS LYS A . n 
A 1 334 VAL 334 334 334 VAL VAL A . n 
A 1 335 GLY 335 335 335 GLY GLY A . n 
A 1 336 ASN 336 336 336 ASN ASN A . n 
A 1 337 GLU 337 337 337 GLU GLU A . n 
A 1 338 LEU 338 338 338 LEU LEU A . n 
A 1 339 GLY 339 339 339 GLY GLY A . n 
A 1 340 PHE 340 340 340 PHE PHE A . n 
A 1 341 HIS 341 341 341 HIS HIS A . n 
A 1 342 TYR 342 342 342 TYR TYR A . n 
A 1 343 THR 343 343 343 THR THR A . n 
A 1 344 ALA 344 344 344 ALA ALA A . n 
A 1 345 SER 345 345 345 SER SER A . n 
A 1 346 GLY 346 346 346 GLY GLY A . n 
A 1 347 PRO 347 347 347 PRO PRO A . n 
A 1 348 LEU 348 348 348 LEU LEU A . n 
A 1 349 VAL 349 349 349 VAL VAL A . n 
A 1 350 ARG 350 350 350 ARG ARG A . n 
A 1 351 SER 351 351 351 SER SER A . n 
A 1 352 SER 352 352 352 SER SER A . n 
A 1 353 TYR 353 353 353 TYR TYR A . n 
A 1 354 LYS 354 354 354 LYS LYS A . n 
A 1 355 ALA 355 355 355 ALA ALA A . n 
A 1 356 GLY 356 356 356 GLY GLY A . n 
A 1 357 GLU 357 357 357 GLU GLU A . n 
A 1 358 PHE 358 358 358 PHE PHE A . n 
A 1 359 PHE 359 359 359 PHE PHE A . n 
A 1 360 LEU 360 360 360 LEU LEU A . n 
A 1 361 LYS 361 361 361 LYS LYS A . n 
A 1 362 ASN 362 362 362 ASN ASN A . n 
A 1 363 LEU 363 363 363 LEU LEU A . n 
A 1 364 VAL 364 364 364 VAL VAL A . n 
A 1 365 ALA 365 365 365 ALA ALA A . n 
A 1 366 LYS 366 366 366 LYS LYS A . n 
A 1 367 ARG 367 367 367 ARG ARG A . n 
A 1 368 LYS 368 368 368 LYS LYS A . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
B 2 GLC 1 E GLC 1 A T6P 845 n 
B 2 GLC 2 E GLC 2 A T6P 845 n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        SF4 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   SF4 
_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 3 DTT 1   401 745 DTT DTT A . 
D 4 SO4 1   402 1   SO4 SO4 A . 
E 5 SF4 1   403 401 SF4 SF4 A . 
F 5 SF4 1   404 645 SF4 SF4 A . 
G 6 HOH 1   501 173 HOH HOH A . 
G 6 HOH 2   502 307 HOH HOH A . 
G 6 HOH 3   503 136 HOH HOH A . 
G 6 HOH 4   504 209 HOH HOH A . 
G 6 HOH 5   505 65  HOH HOH A . 
G 6 HOH 6   506 106 HOH HOH A . 
G 6 HOH 7   507 314 HOH HOH A . 
G 6 HOH 8   508 75  HOH HOH A . 
G 6 HOH 9   509 303 HOH HOH A . 
G 6 HOH 10  510 312 HOH HOH A . 
G 6 HOH 11  511 305 HOH HOH A . 
G 6 HOH 12  512 214 HOH HOH A . 
G 6 HOH 13  513 330 HOH HOH A . 
G 6 HOH 14  514 113 HOH HOH A . 
G 6 HOH 15  515 238 HOH HOH A . 
G 6 HOH 16  516 320 HOH HOH A . 
G 6 HOH 17  517 90  HOH HOH A . 
G 6 HOH 18  518 326 HOH HOH A . 
G 6 HOH 19  519 245 HOH HOH A . 
G 6 HOH 20  520 203 HOH HOH A . 
G 6 HOH 21  521 81  HOH HOH A . 
G 6 HOH 22  522 52  HOH HOH A . 
G 6 HOH 23  523 183 HOH HOH A . 
G 6 HOH 24  524 12  HOH HOH A . 
G 6 HOH 25  525 310 HOH HOH A . 
G 6 HOH 26  526 151 HOH HOH A . 
G 6 HOH 27  527 324 HOH HOH A . 
G 6 HOH 28  528 191 HOH HOH A . 
G 6 HOH 29  529 244 HOH HOH A . 
G 6 HOH 30  530 99  HOH HOH A . 
G 6 HOH 31  531 194 HOH HOH A . 
G 6 HOH 32  532 32  HOH HOH A . 
G 6 HOH 33  533 284 HOH HOH A . 
G 6 HOH 34  534 206 HOH HOH A . 
G 6 HOH 35  535 27  HOH HOH A . 
G 6 HOH 36  536 157 HOH HOH A . 
G 6 HOH 37  537 179 HOH HOH A . 
G 6 HOH 38  538 121 HOH HOH A . 
G 6 HOH 39  539 105 HOH HOH A . 
G 6 HOH 40  540 21  HOH HOH A . 
G 6 HOH 41  541 287 HOH HOH A . 
G 6 HOH 42  542 45  HOH HOH A . 
G 6 HOH 43  543 141 HOH HOH A . 
G 6 HOH 44  544 333 HOH HOH A . 
G 6 HOH 45  545 334 HOH HOH A . 
G 6 HOH 46  546 111 HOH HOH A . 
G 6 HOH 47  547 282 HOH HOH A . 
G 6 HOH 48  548 351 HOH HOH A . 
G 6 HOH 49  549 29  HOH HOH A . 
G 6 HOH 50  550 20  HOH HOH A . 
G 6 HOH 51  551 338 HOH HOH A . 
G 6 HOH 52  552 302 HOH HOH A . 
G 6 HOH 53  553 68  HOH HOH A . 
G 6 HOH 54  554 60  HOH HOH A . 
G 6 HOH 55  555 169 HOH HOH A . 
G 6 HOH 56  556 174 HOH HOH A . 
G 6 HOH 57  557 230 HOH HOH A . 
G 6 HOH 58  558 108 HOH HOH A . 
G 6 HOH 59  559 30  HOH HOH A . 
G 6 HOH 60  560 145 HOH HOH A . 
G 6 HOH 61  561 36  HOH HOH A . 
G 6 HOH 62  562 212 HOH HOH A . 
G 6 HOH 63  563 291 HOH HOH A . 
G 6 HOH 64  564 293 HOH HOH A . 
G 6 HOH 65  565 64  HOH HOH A . 
G 6 HOH 66  566 135 HOH HOH A . 
G 6 HOH 67  567 1   HOH HOH A . 
G 6 HOH 68  568 110 HOH HOH A . 
G 6 HOH 69  569 166 HOH HOH A . 
G 6 HOH 70  570 378 HOH HOH A . 
G 6 HOH 71  571 85  HOH HOH A . 
G 6 HOH 72  572 226 HOH HOH A . 
G 6 HOH 73  573 202 HOH HOH A . 
G 6 HOH 74  574 69  HOH HOH A . 
G 6 HOH 75  575 286 HOH HOH A . 
G 6 HOH 76  576 77  HOH HOH A . 
G 6 HOH 77  577 11  HOH HOH A . 
G 6 HOH 78  578 109 HOH HOH A . 
G 6 HOH 79  579 122 HOH HOH A . 
G 6 HOH 80  580 14  HOH HOH A . 
G 6 HOH 81  581 186 HOH HOH A . 
G 6 HOH 82  582 79  HOH HOH A . 
G 6 HOH 83  583 53  HOH HOH A . 
G 6 HOH 84  584 72  HOH HOH A . 
G 6 HOH 85  585 54  HOH HOH A . 
G 6 HOH 86  586 195 HOH HOH A . 
G 6 HOH 87  587 348 HOH HOH A . 
G 6 HOH 88  588 274 HOH HOH A . 
G 6 HOH 89  589 38  HOH HOH A . 
G 6 HOH 90  590 276 HOH HOH A . 
G 6 HOH 91  591 49  HOH HOH A . 
G 6 HOH 92  592 94  HOH HOH A . 
G 6 HOH 93  593 361 HOH HOH A . 
G 6 HOH 94  594 356 HOH HOH A . 
G 6 HOH 95  595 98  HOH HOH A . 
G 6 HOH 96  596 216 HOH HOH A . 
G 6 HOH 97  597 323 HOH HOH A . 
G 6 HOH 98  598 156 HOH HOH A . 
G 6 HOH 99  599 231 HOH HOH A . 
G 6 HOH 100 600 42  HOH HOH A . 
G 6 HOH 101 601 182 HOH HOH A . 
G 6 HOH 102 602 23  HOH HOH A . 
G 6 HOH 103 603 93  HOH HOH A . 
G 6 HOH 104 604 16  HOH HOH A . 
G 6 HOH 105 605 198 HOH HOH A . 
G 6 HOH 106 606 22  HOH HOH A . 
G 6 HOH 107 607 95  HOH HOH A . 
G 6 HOH 108 608 164 HOH HOH A . 
G 6 HOH 109 609 124 HOH HOH A . 
G 6 HOH 110 610 112 HOH HOH A . 
G 6 HOH 111 611 3   HOH HOH A . 
G 6 HOH 112 612 131 HOH HOH A . 
G 6 HOH 113 613 237 HOH HOH A . 
G 6 HOH 114 614 114 HOH HOH A . 
G 6 HOH 115 615 101 HOH HOH A . 
G 6 HOH 116 616 196 HOH HOH A . 
G 6 HOH 117 617 59  HOH HOH A . 
G 6 HOH 118 618 321 HOH HOH A . 
G 6 HOH 119 619 152 HOH HOH A . 
G 6 HOH 120 620 47  HOH HOH A . 
G 6 HOH 121 621 153 HOH HOH A . 
G 6 HOH 122 622 97  HOH HOH A . 
G 6 HOH 123 623 28  HOH HOH A . 
G 6 HOH 124 624 40  HOH HOH A . 
G 6 HOH 125 625 115 HOH HOH A . 
G 6 HOH 126 626 5   HOH HOH A . 
G 6 HOH 127 627 35  HOH HOH A . 
G 6 HOH 128 628 134 HOH HOH A . 
G 6 HOH 129 629 51  HOH HOH A . 
G 6 HOH 130 630 187 HOH HOH A . 
G 6 HOH 131 631 57  HOH HOH A . 
G 6 HOH 132 632 41  HOH HOH A . 
G 6 HOH 133 633 364 HOH HOH A . 
G 6 HOH 134 634 9   HOH HOH A . 
G 6 HOH 135 635 262 HOH HOH A . 
G 6 HOH 136 636 140 HOH HOH A . 
G 6 HOH 137 637 355 HOH HOH A . 
G 6 HOH 138 638 7   HOH HOH A . 
G 6 HOH 139 639 78  HOH HOH A . 
G 6 HOH 140 640 376 HOH HOH A . 
G 6 HOH 141 641 84  HOH HOH A . 
G 6 HOH 142 642 177 HOH HOH A . 
G 6 HOH 143 643 13  HOH HOH A . 
G 6 HOH 144 644 62  HOH HOH A . 
G 6 HOH 145 645 6   HOH HOH A . 
G 6 HOH 146 646 100 HOH HOH A . 
G 6 HOH 147 647 70  HOH HOH A . 
G 6 HOH 148 648 2   HOH HOH A . 
G 6 HOH 149 649 290 HOH HOH A . 
G 6 HOH 150 650 247 HOH HOH A . 
G 6 HOH 151 651 18  HOH HOH A . 
G 6 HOH 152 652 46  HOH HOH A . 
G 6 HOH 153 653 263 HOH HOH A . 
G 6 HOH 154 654 148 HOH HOH A . 
G 6 HOH 155 655 116 HOH HOH A . 
G 6 HOH 156 656 26  HOH HOH A . 
G 6 HOH 157 657 15  HOH HOH A . 
G 6 HOH 158 658 8   HOH HOH A . 
G 6 HOH 159 659 256 HOH HOH A . 
G 6 HOH 160 660 103 HOH HOH A . 
G 6 HOH 161 661 171 HOH HOH A . 
G 6 HOH 162 662 371 HOH HOH A . 
G 6 HOH 163 663 340 HOH HOH A . 
G 6 HOH 164 664 55  HOH HOH A . 
G 6 HOH 165 665 31  HOH HOH A . 
G 6 HOH 166 666 241 HOH HOH A . 
G 6 HOH 167 667 91  HOH HOH A . 
G 6 HOH 168 668 37  HOH HOH A . 
G 6 HOH 169 669 120 HOH HOH A . 
G 6 HOH 170 670 102 HOH HOH A . 
G 6 HOH 171 671 34  HOH HOH A . 
G 6 HOH 172 672 239 HOH HOH A . 
G 6 HOH 173 673 242 HOH HOH A . 
G 6 HOH 174 674 167 HOH HOH A . 
G 6 HOH 175 675 89  HOH HOH A . 
G 6 HOH 176 676 199 HOH HOH A . 
G 6 HOH 177 677 264 HOH HOH A . 
G 6 HOH 178 678 261 HOH HOH A . 
G 6 HOH 179 679 347 HOH HOH A . 
G 6 HOH 180 680 322 HOH HOH A . 
G 6 HOH 181 681 87  HOH HOH A . 
G 6 HOH 182 682 357 HOH HOH A . 
G 6 HOH 183 683 225 HOH HOH A . 
G 6 HOH 184 684 67  HOH HOH A . 
G 6 HOH 185 685 175 HOH HOH A . 
G 6 HOH 186 686 150 HOH HOH A . 
G 6 HOH 187 687 267 HOH HOH A . 
G 6 HOH 188 688 83  HOH HOH A . 
G 6 HOH 189 689 58  HOH HOH A . 
G 6 HOH 190 690 219 HOH HOH A . 
G 6 HOH 191 691 279 HOH HOH A . 
G 6 HOH 192 692 71  HOH HOH A . 
G 6 HOH 193 693 24  HOH HOH A . 
G 6 HOH 194 694 373 HOH HOH A . 
G 6 HOH 195 695 107 HOH HOH A . 
G 6 HOH 196 696 218 HOH HOH A . 
G 6 HOH 197 697 352 HOH HOH A . 
G 6 HOH 198 698 213 HOH HOH A . 
G 6 HOH 199 699 127 HOH HOH A . 
G 6 HOH 200 700 271 HOH HOH A . 
G 6 HOH 201 701 222 HOH HOH A . 
G 6 HOH 202 702 25  HOH HOH A . 
G 6 HOH 203 703 154 HOH HOH A . 
G 6 HOH 204 704 236 HOH HOH A . 
G 6 HOH 205 705 73  HOH HOH A . 
G 6 HOH 206 706 200 HOH HOH A . 
G 6 HOH 207 707 266 HOH HOH A . 
G 6 HOH 208 708 184 HOH HOH A . 
G 6 HOH 209 709 331 HOH HOH A . 
G 6 HOH 210 710 159 HOH HOH A . 
G 6 HOH 211 711 155 HOH HOH A . 
G 6 HOH 212 712 161 HOH HOH A . 
G 6 HOH 213 713 283 HOH HOH A . 
G 6 HOH 214 714 33  HOH HOH A . 
G 6 HOH 215 715 170 HOH HOH A . 
G 6 HOH 216 716 375 HOH HOH A . 
G 6 HOH 217 717 96  HOH HOH A . 
G 6 HOH 218 718 88  HOH HOH A . 
G 6 HOH 219 719 129 HOH HOH A . 
G 6 HOH 220 720 318 HOH HOH A . 
G 6 HOH 221 721 43  HOH HOH A . 
G 6 HOH 222 722 185 HOH HOH A . 
G 6 HOH 223 723 146 HOH HOH A . 
G 6 HOH 224 724 138 HOH HOH A . 
G 6 HOH 225 725 220 HOH HOH A . 
G 6 HOH 226 726 265 HOH HOH A . 
G 6 HOH 227 727 56  HOH HOH A . 
G 6 HOH 228 728 332 HOH HOH A . 
G 6 HOH 229 729 165 HOH HOH A . 
G 6 HOH 230 730 128 HOH HOH A . 
G 6 HOH 231 731 66  HOH HOH A . 
G 6 HOH 232 732 360 HOH HOH A . 
G 6 HOH 233 733 295 HOH HOH A . 
G 6 HOH 234 734 144 HOH HOH A . 
G 6 HOH 235 735 163 HOH HOH A . 
G 6 HOH 236 736 4   HOH HOH A . 
G 6 HOH 237 737 268 HOH HOH A . 
G 6 HOH 238 738 50  HOH HOH A . 
G 6 HOH 239 739 285 HOH HOH A . 
G 6 HOH 240 740 63  HOH HOH A . 
G 6 HOH 241 741 61  HOH HOH A . 
G 6 HOH 242 742 253 HOH HOH A . 
G 6 HOH 243 743 325 HOH HOH A . 
G 6 HOH 244 744 217 HOH HOH A . 
G 6 HOH 245 745 345 HOH HOH A . 
G 6 HOH 246 746 297 HOH HOH A . 
G 6 HOH 247 747 372 HOH HOH A . 
G 6 HOH 248 748 82  HOH HOH A . 
G 6 HOH 249 749 251 HOH HOH A . 
G 6 HOH 250 750 207 HOH HOH A . 
G 6 HOH 251 751 349 HOH HOH A . 
G 6 HOH 252 752 354 HOH HOH A . 
G 6 HOH 253 753 139 HOH HOH A . 
G 6 HOH 254 754 260 HOH HOH A . 
G 6 HOH 255 755 76  HOH HOH A . 
G 6 HOH 256 756 228 HOH HOH A . 
G 6 HOH 257 757 344 HOH HOH A . 
G 6 HOH 258 758 254 HOH HOH A . 
G 6 HOH 259 759 309 HOH HOH A . 
G 6 HOH 260 760 137 HOH HOH A . 
G 6 HOH 261 761 193 HOH HOH A . 
G 6 HOH 262 762 315 HOH HOH A . 
G 6 HOH 263 763 92  HOH HOH A . 
G 6 HOH 264 764 48  HOH HOH A . 
G 6 HOH 265 765 308 HOH HOH A . 
G 6 HOH 266 766 229 HOH HOH A . 
G 6 HOH 267 767 123 HOH HOH A . 
G 6 HOH 268 768 250 HOH HOH A . 
G 6 HOH 269 769 221 HOH HOH A . 
G 6 HOH 270 770 319 HOH HOH A . 
G 6 HOH 271 771 208 HOH HOH A . 
G 6 HOH 272 772 301 HOH HOH A . 
G 6 HOH 273 773 197 HOH HOH A . 
G 6 HOH 274 774 234 HOH HOH A . 
G 6 HOH 275 775 142 HOH HOH A . 
G 6 HOH 276 776 288 HOH HOH A . 
G 6 HOH 277 777 39  HOH HOH A . 
G 6 HOH 278 778 270 HOH HOH A . 
G 6 HOH 279 779 17  HOH HOH A . 
G 6 HOH 280 780 118 HOH HOH A . 
G 6 HOH 281 781 249 HOH HOH A . 
G 6 HOH 282 782 243 HOH HOH A . 
G 6 HOH 283 783 86  HOH HOH A . 
G 6 HOH 284 784 292 HOH HOH A . 
G 6 HOH 285 785 257 HOH HOH A . 
G 6 HOH 286 786 168 HOH HOH A . 
G 6 HOH 287 787 172 HOH HOH A . 
G 6 HOH 288 788 300 HOH HOH A . 
G 6 HOH 289 789 335 HOH HOH A . 
G 6 HOH 290 790 336 HOH HOH A . 
G 6 HOH 291 791 210 HOH HOH A . 
G 6 HOH 292 792 367 HOH HOH A . 
G 6 HOH 293 793 311 HOH HOH A . 
G 6 HOH 294 794 227 HOH HOH A . 
G 6 HOH 295 795 126 HOH HOH A . 
G 6 HOH 296 796 158 HOH HOH A . 
G 6 HOH 297 797 192 HOH HOH A . 
G 6 HOH 298 798 80  HOH HOH A . 
G 6 HOH 299 799 374 HOH HOH A . 
G 6 HOH 300 800 269 HOH HOH A . 
G 6 HOH 301 801 329 HOH HOH A . 
G 6 HOH 302 802 339 HOH HOH A . 
G 6 HOH 303 803 377 HOH HOH A . 
G 6 HOH 304 804 359 HOH HOH A . 
G 6 HOH 305 805 280 HOH HOH A . 
G 6 HOH 306 806 224 HOH HOH A . 
G 6 HOH 307 807 117 HOH HOH A . 
G 6 HOH 308 808 278 HOH HOH A . 
G 6 HOH 309 809 341 HOH HOH A . 
G 6 HOH 310 810 132 HOH HOH A . 
G 6 HOH 311 811 178 HOH HOH A . 
G 6 HOH 312 812 313 HOH HOH A . 
G 6 HOH 313 813 215 HOH HOH A . 
G 6 HOH 314 814 133 HOH HOH A . 
G 6 HOH 315 815 327 HOH HOH A . 
G 6 HOH 316 816 365 HOH HOH A . 
G 6 HOH 317 817 317 HOH HOH A . 
G 6 HOH 318 818 235 HOH HOH A . 
G 6 HOH 319 819 104 HOH HOH A . 
G 6 HOH 320 820 294 HOH HOH A . 
G 6 HOH 321 821 353 HOH HOH A . 
G 6 HOH 322 822 369 HOH HOH A . 
G 6 HOH 323 823 281 HOH HOH A . 
G 6 HOH 324 824 160 HOH HOH A . 
G 6 HOH 325 825 180 HOH HOH A . 
G 6 HOH 326 826 273 HOH HOH A . 
G 6 HOH 327 827 259 HOH HOH A . 
G 6 HOH 328 828 248 HOH HOH A . 
G 6 HOH 329 829 366 HOH HOH A . 
G 6 HOH 330 830 149 HOH HOH A . 
G 6 HOH 331 831 304 HOH HOH A . 
G 6 HOH 332 832 233 HOH HOH A . 
G 6 HOH 333 833 346 HOH HOH A . 
G 6 HOH 334 834 289 HOH HOH A . 
G 6 HOH 335 835 232 HOH HOH A . 
G 6 HOH 336 836 162 HOH HOH A . 
G 6 HOH 337 837 181 HOH HOH A . 
G 6 HOH 338 838 205 HOH HOH A . 
G 6 HOH 339 839 328 HOH HOH A . 
G 6 HOH 340 840 277 HOH HOH A . 
G 6 HOH 341 841 10  HOH HOH A . 
G 6 HOH 342 842 342 HOH HOH A . 
G 6 HOH 343 843 189 HOH HOH A . 
G 6 HOH 344 844 190 HOH HOH A . 
G 6 HOH 345 845 188 HOH HOH A . 
G 6 HOH 346 846 74  HOH HOH A . 
G 6 HOH 347 847 252 HOH HOH A . 
G 6 HOH 348 848 211 HOH HOH A . 
G 6 HOH 349 849 337 HOH HOH A . 
G 6 HOH 350 850 363 HOH HOH A . 
G 6 HOH 351 851 255 HOH HOH A . 
G 6 HOH 352 852 240 HOH HOH A . 
G 6 HOH 353 853 223 HOH HOH A . 
G 6 HOH 354 854 204 HOH HOH A . 
G 6 HOH 355 855 343 HOH HOH A . 
G 6 HOH 356 856 143 HOH HOH A . 
G 6 HOH 357 857 298 HOH HOH A . 
G 6 HOH 358 858 362 HOH HOH A . 
G 6 HOH 359 859 358 HOH HOH A . 
G 6 HOH 360 860 246 HOH HOH A . 
G 6 HOH 361 861 201 HOH HOH A . 
G 6 HOH 362 862 19  HOH HOH A . 
G 6 HOH 363 863 176 HOH HOH A . 
G 6 HOH 364 864 272 HOH HOH A . 
G 6 HOH 365 865 368 HOH HOH A . 
G 6 HOH 366 866 275 HOH HOH A . 
G 6 HOH 367 867 119 HOH HOH A . 
G 6 HOH 368 868 130 HOH HOH A . 
G 6 HOH 369 869 125 HOH HOH A . 
G 6 HOH 370 870 258 HOH HOH A . 
G 6 HOH 371 871 299 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8TRW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     68.353 
_cell.length_a_esd                 ? 
_cell.length_b                     88.789 
_cell.length_b_esd                 ? 
_cell.length_c                     108.166 
_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                         8TRW 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_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                   8TRW 
_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             1.95 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          37.04 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M HEPES pH 7.5, 0.2 M Sodium sulfate, 30% (w/v) PEG 3350, 3% (w/v) D-(+)-trehalose' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MARMOSAIC 225 mm CCD' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-10-30 
_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   0.97872 
_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                        'APS BEAMLINE 21-ID-F' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97872 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   21-ID-F 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8TRW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.54 
_reflns.d_resolution_low                               50.00 
_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                                     199757 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          21 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.54 
_reflns_shell.d_res_low                                     1.57 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2402 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.709 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8TRW 
_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                            1.54 
_refine.ls_d_res_low                             27.08 
_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                     75051 
_refine.ls_number_reflns_R_free                  3168 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    78.96 
_refine.ls_percent_reflns_R_free                 4.22 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1532 
_refine.ls_R_factor_R_free                       0.1804 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1521 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 16.16 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.14 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.54 
_refine_hist.d_res_low                        27.08 
_refine_hist.number_atoms_solvent             371 
_refine_hist.number_atoms_total               2746 
_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        2339 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         36 
_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  ? 2548 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.182  ? 3482 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 24.084 ? 990  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.079  ? 393  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.013  ? 440  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.54 1.56  . . 59  1322 33.00 . . . . 0.2502 . . . . . . . . . . . 0.2332 
'X-RAY DIFFRACTION' 1.56 1.58  . . 70  1632 42.00 . . . . 0.2346 . . . . . . . . . . . 0.2933 
'X-RAY DIFFRACTION' 1.58 1.61  . . 80  1794 45.00 . . . . 0.2132 . . . . . . . . . . . 0.1904 
'X-RAY DIFFRACTION' 1.61 1.64  . . 89  2024 51.00 . . . . 0.1959 . . . . . . . . . . . 0.1952 
'X-RAY DIFFRACTION' 1.64 1.67  . . 95  2200 55.00 . . . . 0.1806 . . . . . . . . . . . 0.1897 
'X-RAY DIFFRACTION' 1.67 1.70  . . 102 2344 59.00 . . . . 0.1758 . . . . . . . . . . . 0.2084 
'X-RAY DIFFRACTION' 1.70 1.73  . . 106 2547 64.00 . . . . 0.1699 . . . . . . . . . . . 0.1843 
'X-RAY DIFFRACTION' 1.73 1.77  . . 124 2848 72.00 . . . . 0.1540 . . . . . . . . . . . 0.1733 
'X-RAY DIFFRACTION' 1.77 1.81  . . 142 3139 79.00 . . . . 0.1548 . . . . . . . . . . . 0.1792 
'X-RAY DIFFRACTION' 1.81 1.86  . . 153 3347 85.00 . . . . 0.1513 . . . . . . . . . . . 0.1573 
'X-RAY DIFFRACTION' 1.86 1.91  . . 149 3517 89.00 . . . . 0.1516 . . . . . . . . . . . 0.1678 
'X-RAY DIFFRACTION' 1.91 1.96  . . 157 3654 93.00 . . . . 0.1418 . . . . . . . . . . . 0.1493 
'X-RAY DIFFRACTION' 1.96 2.03  . . 164 3754 95.00 . . . . 0.1451 . . . . . . . . . . . 0.1782 
'X-RAY DIFFRACTION' 2.03 2.10  . . 170 3865 97.00 . . . . 0.1525 . . . . . . . . . . . 0.1960 
'X-RAY DIFFRACTION' 2.10 2.18  . . 176 3838 98.00 . . . . 0.1447 . . . . . . . . . . . 0.1713 
'X-RAY DIFFRACTION' 2.18 2.28  . . 166 3874 97.00 . . . . 0.1495 . . . . . . . . . . . 0.1872 
'X-RAY DIFFRACTION' 2.28 2.40  . . 170 3774 97.00 . . . . 0.1400 . . . . . . . . . . . 0.1833 
'X-RAY DIFFRACTION' 2.40 2.55  . . 172 3838 97.00 . . . . 0.1532 . . . . . . . . . . . 0.1632 
'X-RAY DIFFRACTION' 2.55 2.75  . . 170 3786 96.00 . . . . 0.1596 . . . . . . . . . . . 0.1998 
'X-RAY DIFFRACTION' 2.75 3.03  . . 172 3813 96.00 . . . . 0.1551 . . . . . . . . . . . 0.1943 
'X-RAY DIFFRACTION' 3.03 3.46  . . 163 3743 95.00 . . . . 0.1514 . . . . . . . . . . . 0.1774 
'X-RAY DIFFRACTION' 3.46 4.36  . . 167 3724 94.00 . . . . 0.1351 . . . . . . . . . . . 0.1848 
'X-RAY DIFFRACTION' 4.36 27.08 . . 152 3506 88.00 . . . . 0.1524 . . . . . . . . . . . 0.1675 
# 
_struct.entry_id                     8TRW 
_struct.title                        'Structure of human LIAS' 
_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        8TRW 
_struct_keywords.text            'Lipoyl synthase, LIAS, BIOSYNTHETIC PROTEIN' 
_struct_keywords.pdbx_keywords   'BIOSYNTHETIC PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 5 ? 
G N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    LIAS_HUMAN 
_struct_ref.pdbx_db_accession          O43766 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSLRCGDAARTLGPRVFGRYFCSPVRPLSSLPDKKKELLQNGPDLQDFVSGDLADRSTWDEYKGNLKRQKGERLRLPPWL
KTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGGGEYATATATIMLMGDTCTRGCRFCSVKTARNPPPLDASEP
YNTAKAIAEWGLDYVVLTSVDRDDMPDGGAEHIAKTVSYLKERNPKILVECLTPDFRGDLKAIEKVALSGLDVYAHNVET
VPELQSKVRDPRANFDQSLRVLKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREADVDCLTLGQYMQPTRRHLKVE
EYITPEKFKYWEKVGNELGFHYTASGPLVRSSYKAGEFFLKNLVAKRK
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8TRW 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 368 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             O43766 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  368 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       368 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             8TRW 
_struct_ref_seq_dif.mon_id                       VAL 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      253 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   O43766 
_struct_ref_seq_dif.db_mon_id                    ALA 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          253 
_struct_ref_seq_dif.details                      conflict 
_struct_ref_seq_dif.pdbx_auth_seq_num            253 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_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 77  ? LYS A 81  ? PRO A 77  LYS A 81  5 ? 5  
HELX_P HELX_P2  AA2 GLY A 87  ? ASN A 99  ? GLY A 87  ASN A 99  1 ? 13 
HELX_P HELX_P3  AA3 THR A 104 ? ALA A 109 ? THR A 104 ALA A 109 1 ? 6  
HELX_P HELX_P4  AA4 ASN A 113 ? TRP A 118 ? ASN A 113 TRP A 118 1 ? 6  
HELX_P HELX_P5  AA5 SER A 158 ? GLY A 171 ? SER A 158 GLY A 171 1 ? 14 
HELX_P HELX_P6  AA6 GLY A 189 ? ASN A 204 ? GLY A 189 ASN A 204 1 ? 16 
HELX_P HELX_P7  AA7 ASP A 215 ? GLY A 218 ? ASP A 215 GLY A 218 5 ? 4  
HELX_P HELX_P8  AA8 ASP A 219 ? LEU A 228 ? ASP A 219 LEU A 228 1 ? 10 
HELX_P HELX_P9  AA9 VAL A 241 ? GLU A 243 ? VAL A 241 GLU A 243 5 ? 3  
HELX_P HELX_P10 AB1 LEU A 244 ? ARG A 249 ? LEU A 244 ARG A 249 1 ? 6  
HELX_P HELX_P11 AB2 ASN A 254 ? GLN A 269 ? ASN A 254 GLN A 269 1 ? 16 
HELX_P HELX_P12 AB3 ASN A 285 ? ALA A 299 ? ASN A 285 ALA A 299 1 ? 15 
HELX_P HELX_P13 AB4 THR A 324 ? GLY A 339 ? THR A 324 GLY A 339 1 ? 16 
HELX_P HELX_P14 AB5 LYS A 354 ? LEU A 363 ? LYS A 354 LEU A 363 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1  covale both ? B GLC .   O1 ? ? ? 1_555 B GLC . C1  ? ? E GLC 1   E GLC 2   1_555 ? ? ? ? ? ? ? 1.394 ? ? 
metalc1  metalc ?    ? A CYS 106 SG ? ? ? 1_555 F SF4 . FE2 ? ? A CYS 106 A SF4 404 1_555 ? ? ? ? ? ? ? 2.342 ? ? 
metalc2  metalc ?    ? A CYS 111 SG ? ? ? 1_555 F SF4 . FE4 ? ? A CYS 111 A SF4 404 1_555 ? ? ? ? ? ? ? 2.317 ? ? 
metalc3  metalc ?    ? A CYS 117 SG ? ? ? 1_555 F SF4 . FE3 ? ? A CYS 117 A SF4 404 1_555 ? ? ? ? ? ? ? 2.329 ? ? 
metalc4  metalc ?    ? A CYS 137 SG ? ? ? 1_555 E SF4 . FE2 ? ? A CYS 137 A SF4 403 1_555 ? ? ? ? ? ? ? 2.309 ? ? 
metalc5  metalc ?    ? A CYS 141 SG ? ? ? 1_555 E SF4 . FE1 ? ? A CYS 141 A SF4 403 1_555 ? ? ? ? ? ? ? 2.351 ? ? 
metalc6  metalc ?    ? A CYS 144 SG ? ? ? 1_555 E SF4 . FE4 ? ? A CYS 144 A SF4 403 1_555 ? ? ? ? ? ? ? 2.357 ? ? 
metalc7  metalc ?    ? A SER 352 OG ? ? ? 1_555 F SF4 . FE1 ? ? A SER 352 A SF4 404 1_555 ? ? ? ? ? ? ? 2.080 ? ? 
metalc8  metalc ?    ? C DTT .   S1 A ? ? 1_555 E SF4 . FE3 ? ? A DTT 401 A SF4 403 1_555 ? ? ? ? ? ? ? 2.416 ? ? 
metalc9  metalc ?    ? C DTT .   S1 B ? ? 1_555 E SF4 . FE3 ? ? A DTT 401 A SF4 403 1_555 ? ? ? ? ? ? ? 2.333 ? ? 
metalc10 metalc ?    ? C DTT .   O2 B ? ? 1_555 E SF4 . FE3 ? ? A DTT 401 A SF4 403 1_555 ? ? ? ? ? ? ? 2.599 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 106 ? A CYS 106 ? 1_555 FE2 ? F SF4 . ? A SF4 404 ? 1_555 S1 ? F SF4 . ? A SF4 404 ? 1_555 108.2 ? 
2  SG ? A CYS 106 ? A CYS 106 ? 1_555 FE2 ? F SF4 . ? A SF4 404 ? 1_555 S3 ? F SF4 . ? A SF4 404 ? 1_555 118.0 ? 
3  S1 ? F SF4 .   ? A SF4 404 ? 1_555 FE2 ? F SF4 . ? A SF4 404 ? 1_555 S3 ? F SF4 . ? A SF4 404 ? 1_555 106.2 ? 
4  SG ? A CYS 106 ? A CYS 106 ? 1_555 FE2 ? F SF4 . ? A SF4 404 ? 1_555 S4 ? F SF4 . ? A SF4 404 ? 1_555 113.6 ? 
5  S1 ? F SF4 .   ? A SF4 404 ? 1_555 FE2 ? F SF4 . ? A SF4 404 ? 1_555 S4 ? F SF4 . ? A SF4 404 ? 1_555 104.7 ? 
6  S3 ? F SF4 .   ? A SF4 404 ? 1_555 FE2 ? F SF4 . ? A SF4 404 ? 1_555 S4 ? F SF4 . ? A SF4 404 ? 1_555 105.2 ? 
7  SG ? A CYS 111 ? A CYS 111 ? 1_555 FE4 ? F SF4 . ? A SF4 404 ? 1_555 S1 ? F SF4 . ? A SF4 404 ? 1_555 108.2 ? 
8  SG ? A CYS 111 ? A CYS 111 ? 1_555 FE4 ? F SF4 . ? A SF4 404 ? 1_555 S2 ? F SF4 . ? A SF4 404 ? 1_555 110.8 ? 
9  S1 ? F SF4 .   ? A SF4 404 ? 1_555 FE4 ? F SF4 . ? A SF4 404 ? 1_555 S2 ? F SF4 . ? A SF4 404 ? 1_555 105.9 ? 
10 SG ? A CYS 111 ? A CYS 111 ? 1_555 FE4 ? F SF4 . ? A SF4 404 ? 1_555 S3 ? F SF4 . ? A SF4 404 ? 1_555 120.8 ? 
11 S1 ? F SF4 .   ? A SF4 404 ? 1_555 FE4 ? F SF4 . ? A SF4 404 ? 1_555 S3 ? F SF4 . ? A SF4 404 ? 1_555 105.6 ? 
12 S2 ? F SF4 .   ? A SF4 404 ? 1_555 FE4 ? F SF4 . ? A SF4 404 ? 1_555 S3 ? F SF4 . ? A SF4 404 ? 1_555 104.6 ? 
13 SG ? A CYS 117 ? A CYS 117 ? 1_555 FE3 ? F SF4 . ? A SF4 404 ? 1_555 S1 ? F SF4 . ? A SF4 404 ? 1_555 112.5 ? 
14 SG ? A CYS 117 ? A CYS 117 ? 1_555 FE3 ? F SF4 . ? A SF4 404 ? 1_555 S2 ? F SF4 . ? A SF4 404 ? 1_555 109.4 ? 
15 S1 ? F SF4 .   ? A SF4 404 ? 1_555 FE3 ? F SF4 . ? A SF4 404 ? 1_555 S2 ? F SF4 . ? A SF4 404 ? 1_555 105.8 ? 
16 SG ? A CYS 117 ? A CYS 117 ? 1_555 FE3 ? F SF4 . ? A SF4 404 ? 1_555 S4 ? F SF4 . ? A SF4 404 ? 1_555 117.0 ? 
17 S1 ? F SF4 .   ? A SF4 404 ? 1_555 FE3 ? F SF4 . ? A SF4 404 ? 1_555 S4 ? F SF4 . ? A SF4 404 ? 1_555 104.6 ? 
18 S2 ? F SF4 .   ? A SF4 404 ? 1_555 FE3 ? F SF4 . ? A SF4 404 ? 1_555 S4 ? F SF4 . ? A SF4 404 ? 1_555 106.8 ? 
19 SG ? A CYS 137 ? A CYS 137 ? 1_555 FE2 ? E SF4 . ? A SF4 403 ? 1_555 S1 ? E SF4 . ? A SF4 403 ? 1_555 114.0 ? 
20 SG ? A CYS 137 ? A CYS 137 ? 1_555 FE2 ? E SF4 . ? A SF4 403 ? 1_555 S3 ? E SF4 . ? A SF4 403 ? 1_555 114.7 ? 
21 S1 ? E SF4 .   ? A SF4 403 ? 1_555 FE2 ? E SF4 . ? A SF4 403 ? 1_555 S3 ? E SF4 . ? A SF4 403 ? 1_555 105.4 ? 
22 SG ? A CYS 137 ? A CYS 137 ? 1_555 FE2 ? E SF4 . ? A SF4 403 ? 1_555 S4 ? E SF4 . ? A SF4 403 ? 1_555 111.2 ? 
23 S1 ? E SF4 .   ? A SF4 403 ? 1_555 FE2 ? E SF4 . ? A SF4 403 ? 1_555 S4 ? E SF4 . ? A SF4 403 ? 1_555 106.5 ? 
24 S3 ? E SF4 .   ? A SF4 403 ? 1_555 FE2 ? E SF4 . ? A SF4 403 ? 1_555 S4 ? E SF4 . ? A SF4 403 ? 1_555 104.2 ? 
25 SG ? A CYS 141 ? A CYS 141 ? 1_555 FE1 ? E SF4 . ? A SF4 403 ? 1_555 S2 ? E SF4 . ? A SF4 403 ? 1_555 113.2 ? 
26 SG ? A CYS 141 ? A CYS 141 ? 1_555 FE1 ? E SF4 . ? A SF4 403 ? 1_555 S3 ? E SF4 . ? A SF4 403 ? 1_555 106.1 ? 
27 S2 ? E SF4 .   ? A SF4 403 ? 1_555 FE1 ? E SF4 . ? A SF4 403 ? 1_555 S3 ? E SF4 . ? A SF4 403 ? 1_555 108.1 ? 
28 SG ? A CYS 141 ? A CYS 141 ? 1_555 FE1 ? E SF4 . ? A SF4 403 ? 1_555 S4 ? E SF4 . ? A SF4 403 ? 1_555 120.4 ? 
29 S2 ? E SF4 .   ? A SF4 403 ? 1_555 FE1 ? E SF4 . ? A SF4 403 ? 1_555 S4 ? E SF4 . ? A SF4 403 ? 1_555 103.9 ? 
30 S3 ? E SF4 .   ? A SF4 403 ? 1_555 FE1 ? E SF4 . ? A SF4 403 ? 1_555 S4 ? E SF4 . ? A SF4 403 ? 1_555 104.3 ? 
31 SG ? A CYS 144 ? A CYS 144 ? 1_555 FE4 ? E SF4 . ? A SF4 403 ? 1_555 S1 ? E SF4 . ? A SF4 403 ? 1_555 119.8 ? 
32 SG ? A CYS 144 ? A CYS 144 ? 1_555 FE4 ? E SF4 . ? A SF4 403 ? 1_555 S2 ? E SF4 . ? A SF4 403 ? 1_555 110.3 ? 
33 S1 ? E SF4 .   ? A SF4 403 ? 1_555 FE4 ? E SF4 . ? A SF4 403 ? 1_555 S2 ? E SF4 . ? A SF4 403 ? 1_555 105.0 ? 
34 SG ? A CYS 144 ? A CYS 144 ? 1_555 FE4 ? E SF4 . ? A SF4 403 ? 1_555 S3 ? E SF4 . ? A SF4 403 ? 1_555 108.2 ? 
35 S1 ? E SF4 .   ? A SF4 403 ? 1_555 FE4 ? E SF4 . ? A SF4 403 ? 1_555 S3 ? E SF4 . ? A SF4 403 ? 1_555 105.0 ? 
36 S2 ? E SF4 .   ? A SF4 403 ? 1_555 FE4 ? E SF4 . ? A SF4 403 ? 1_555 S3 ? E SF4 . ? A SF4 403 ? 1_555 107.9 ? 
37 OG ? A SER 352 ? A SER 352 ? 1_555 FE1 ? F SF4 . ? A SF4 404 ? 1_555 S2 ? F SF4 . ? A SF4 404 ? 1_555 115.7 ? 
38 OG ? A SER 352 ? A SER 352 ? 1_555 FE1 ? F SF4 . ? A SF4 404 ? 1_555 S3 ? F SF4 . ? A SF4 404 ? 1_555 118.3 ? 
39 S2 ? F SF4 .   ? A SF4 404 ? 1_555 FE1 ? F SF4 . ? A SF4 404 ? 1_555 S3 ? F SF4 . ? A SF4 404 ? 1_555 103.6 ? 
40 OG ? A SER 352 ? A SER 352 ? 1_555 FE1 ? F SF4 . ? A SF4 404 ? 1_555 S4 ? F SF4 . ? A SF4 404 ? 1_555 106.6 ? 
41 S2 ? F SF4 .   ? A SF4 404 ? 1_555 FE1 ? F SF4 . ? A SF4 404 ? 1_555 S4 ? F SF4 . ? A SF4 404 ? 1_555 108.4 ? 
42 S3 ? F SF4 .   ? A SF4 404 ? 1_555 FE1 ? F SF4 . ? A SF4 404 ? 1_555 S4 ? F SF4 . ? A SF4 404 ? 1_555 103.4 ? 
43 S1 A C DTT .   ? A DTT 401 ? 1_555 FE3 ? E SF4 . ? A SF4 403 ? 1_555 S1 ? E SF4 . ? A SF4 403 ? 1_555 118.7 ? 
44 S1 A C DTT .   ? A DTT 401 ? 1_555 FE3 ? E SF4 . ? A SF4 403 ? 1_555 S2 ? E SF4 . ? A SF4 403 ? 1_555 123.0 ? 
45 S1 ? E SF4 .   ? A SF4 403 ? 1_555 FE3 ? E SF4 . ? A SF4 403 ? 1_555 S2 ? E SF4 . ? A SF4 403 ? 1_555 105.2 ? 
46 S1 A C DTT .   ? A DTT 401 ? 1_555 FE3 ? E SF4 . ? A SF4 403 ? 1_555 S4 ? E SF4 . ? A SF4 403 ? 1_555 100.4 ? 
47 S1 ? E SF4 .   ? A SF4 403 ? 1_555 FE3 ? E SF4 . ? A SF4 403 ? 1_555 S4 ? E SF4 . ? A SF4 403 ? 1_555 104.3 ? 
48 S2 ? E SF4 .   ? A SF4 403 ? 1_555 FE3 ? E SF4 . ? A SF4 403 ? 1_555 S4 ? E SF4 . ? A SF4 403 ? 1_555 102.0 ? 
49 S1 A C DTT .   ? A DTT 401 ? 1_555 FE3 ? E SF4 . ? A SF4 403 ? 1_555 S1 B C DTT . ? A DTT 401 ? 1_555 6.3   ? 
50 S1 ? E SF4 .   ? A SF4 403 ? 1_555 FE3 ? E SF4 . ? A SF4 403 ? 1_555 S1 B C DTT . ? A DTT 401 ? 1_555 113.9 ? 
51 S2 ? E SF4 .   ? A SF4 403 ? 1_555 FE3 ? E SF4 . ? A SF4 403 ? 1_555 S1 B C DTT . ? A DTT 401 ? 1_555 129.3 ? 
52 S4 ? E SF4 .   ? A SF4 403 ? 1_555 FE3 ? E SF4 . ? A SF4 403 ? 1_555 S1 B C DTT . ? A DTT 401 ? 1_555 98.3  ? 
53 S1 A C DTT .   ? A DTT 401 ? 1_555 FE3 ? E SF4 . ? A SF4 403 ? 1_555 O2 B C DTT . ? A DTT 401 ? 1_555 73.8  ? 
54 S1 ? E SF4 .   ? A SF4 403 ? 1_555 FE3 ? E SF4 . ? A SF4 403 ? 1_555 O2 B C DTT . ? A DTT 401 ? 1_555 87.4  ? 
55 S2 ? E SF4 .   ? A SF4 403 ? 1_555 FE3 ? E SF4 . ? A SF4 403 ? 1_555 O2 B C DTT . ? A DTT 401 ? 1_555 73.8  ? 
56 S4 ? E SF4 .   ? A SF4 403 ? 1_555 FE3 ? E SF4 . ? A SF4 403 ? 1_555 O2 B C DTT . ? A DTT 401 ? 1_555 168.3 ? 
57 S1 B C DTT .   ? A DTT 401 ? 1_555 FE3 ? E SF4 . ? A SF4 403 ? 1_555 O2 B C DTT . ? A DTT 401 ? 1_555 77.0  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel 
AA1 2 3 ? parallel 
AA1 3 4 ? parallel 
AA1 4 5 ? parallel 
AA1 5 6 ? parallel 
AA1 6 7 ? parallel 
AA2 1 2 ? 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 127 ? MET A 131 ? THR A 127 MET A 131 
AA1 2 TYR A 174 ? THR A 178 ? TYR A 174 THR A 178 
AA1 3 LEU A 208 ? LEU A 212 ? LEU A 208 LEU A 212 
AA1 4 VAL A 233 ? ALA A 235 ? VAL A 233 ALA A 235 
AA1 5 ILE A 273 ? LEU A 280 ? ILE A 273 LEU A 280 
AA1 6 CYS A 303 ? GLN A 308 ? CYS A 303 GLN A 308 
AA1 7 TYR A 342 ? SER A 345 ? TYR A 342 SER A 345 
AA2 1 THR A 136 ? CYS A 137 ? THR A 136 CYS A 137 
AA2 2 LYS A 147 ? THR A 148 ? LYS A 147 THR A 148 
# 
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 ILE A 130 ? N ILE A 130 O VAL A 176 ? O VAL A 176 
AA1 2 3 N LEU A 177 ? N LEU A 177 O GLU A 210 ? O GLU A 210 
AA1 3 4 N CYS A 211 ? N CYS A 211 O ALA A 235 ? O ALA A 235 
AA1 4 5 N TYR A 234 ? N TYR A 234 O ILE A 273 ? O ILE A 273 
AA1 5 6 N LEU A 280 ? N LEU A 280 O GLY A 307 ? O GLY A 307 
AA1 6 7 N LEU A 306 ? N LEU A 306 O ALA A 344 ? O ALA A 344 
AA2 1 2 N CYS A 137 ? N CYS A 137 O LYS A 147 ? O LYS A 147 
# 
_pdbx_entry_details.entry_id                   8TRW 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A HOH 599 ? ? O A HOH 773 ? ? 2.13 
2 1 O   A HOH 552 ? ? O A HOH 589 ? ? 2.14 
3 1 O   A HOH 621 ? ? O A HOH 770 ? ? 2.17 
4 1 O   A HOH 789 ? ? O A HOH 799 ? ? 2.18 
5 1 O   A HOH 749 ? ? O A HOH 756 ? ? 2.18 
6 1 OD2 A ASP 183 ? ? O A HOH 501 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OE1 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    GLU 
_pdbx_validate_symm_contact.auth_seq_id_1     298 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    B 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     825 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   7_655 
_pdbx_validate_symm_contact.dist              2.17 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    GLU 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     239 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             70.74 
_pdbx_validate_torsion.psi             -43.80 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 579 ? G HOH . 
2 1 A HOH 725 ? G HOH . 
3 1 A HOH 729 ? G HOH . 
4 1 A HOH 802 ? G HOH . 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         46.0838 
_pdbx_refine_tls.origin_y         15.7920 
_pdbx_refine_tls.origin_z         36.7668 
_pdbx_refine_tls.T[1][1]          0.0954 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0143 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0025 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.0771 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0177 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0871 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.4306 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.2132 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.1237 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.5425 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.1326 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.7364 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0245 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0473 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0699 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0094 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0106 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0287 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0448 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0141 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0073 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_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   all 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 865 ? 6.35 . 
2 1 O ? A HOH 866 ? 6.42 . 
# 
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 MET 1  ? A MET 1  
2  1 Y 1 A SER 2  ? A SER 2  
3  1 Y 1 A LEU 3  ? A LEU 3  
4  1 Y 1 A ARG 4  ? A ARG 4  
5  1 Y 1 A CYS 5  ? A CYS 5  
6  1 Y 1 A GLY 6  ? A GLY 6  
7  1 Y 1 A ASP 7  ? A ASP 7  
8  1 Y 1 A ALA 8  ? A ALA 8  
9  1 Y 1 A ALA 9  ? A ALA 9  
10 1 Y 1 A ARG 10 ? A ARG 10 
11 1 Y 1 A THR 11 ? A THR 11 
12 1 Y 1 A LEU 12 ? A LEU 12 
13 1 Y 1 A GLY 13 ? A GLY 13 
14 1 Y 1 A PRO 14 ? A PRO 14 
15 1 Y 1 A ARG 15 ? A ARG 15 
16 1 Y 1 A VAL 16 ? A VAL 16 
17 1 Y 1 A PHE 17 ? A PHE 17 
18 1 Y 1 A GLY 18 ? A GLY 18 
19 1 Y 1 A ARG 19 ? A ARG 19 
20 1 Y 1 A TYR 20 ? A TYR 20 
21 1 Y 1 A PHE 21 ? A PHE 21 
22 1 Y 1 A CYS 22 ? A CYS 22 
23 1 Y 1 A SER 23 ? A SER 23 
24 1 Y 1 A PRO 24 ? A PRO 24 
25 1 Y 1 A VAL 25 ? A VAL 25 
26 1 Y 1 A ARG 26 ? A ARG 26 
27 1 Y 1 A PRO 27 ? A PRO 27 
28 1 Y 1 A LEU 28 ? A LEU 28 
29 1 Y 1 A SER 29 ? A SER 29 
30 1 Y 1 A SER 30 ? A SER 30 
31 1 Y 1 A LEU 31 ? A LEU 31 
32 1 Y 1 A PRO 32 ? A PRO 32 
33 1 Y 1 A ASP 33 ? A ASP 33 
34 1 Y 1 A LYS 34 ? A LYS 34 
35 1 Y 1 A LYS 35 ? A LYS 35 
36 1 Y 1 A LYS 36 ? A LYS 36 
37 1 Y 1 A GLU 37 ? A GLU 37 
38 1 Y 1 A LEU 38 ? A LEU 38 
39 1 Y 1 A LEU 39 ? A LEU 39 
40 1 Y 1 A GLN 40 ? A GLN 40 
41 1 Y 1 A ASN 41 ? A ASN 41 
42 1 Y 1 A GLY 42 ? A GLY 42 
43 1 Y 1 A PRO 43 ? A PRO 43 
44 1 Y 1 A ASP 44 ? A ASP 44 
45 1 Y 1 A LEU 45 ? A LEU 45 
46 1 Y 1 A GLN 46 ? A GLN 46 
47 1 Y 1 A ASP 47 ? A ASP 47 
48 1 Y 1 A PHE 48 ? A PHE 48 
49 1 Y 1 A VAL 49 ? A VAL 49 
50 1 Y 1 A SER 50 ? A SER 50 
51 1 Y 1 A GLY 51 ? A GLY 51 
52 1 Y 1 A ASP 52 ? A ASP 52 
53 1 Y 1 A LEU 53 ? A LEU 53 
54 1 Y 1 A ALA 54 ? A ALA 54 
55 1 Y 1 A ASP 55 ? A ASP 55 
56 1 Y 1 A ARG 56 ? A ARG 56 
57 1 Y 1 A SER 57 ? A SER 57 
58 1 Y 1 A THR 58 ? A THR 58 
59 1 Y 1 A TRP 59 ? A TRP 59 
60 1 Y 1 A ASP 60 ? A ASP 60 
61 1 Y 1 A GLU 61 ? A GLU 61 
62 1 Y 1 A TYR 62 ? A TYR 62 
63 1 Y 1 A LYS 63 ? A LYS 63 
64 1 Y 1 A GLY 64 ? A GLY 64 
65 1 Y 1 A ASN 65 ? A ASN 65 
66 1 Y 1 A LEU 66 ? A LEU 66 
67 1 Y 1 A LYS 67 ? A LYS 67 
68 1 Y 1 A ARG 68 ? A ARG 68 
69 1 Y 1 A GLN 69 ? A GLN 69 
70 1 Y 1 A LYS 70 ? A LYS 70 
71 1 Y 1 A GLY 71 ? A GLY 71 
72 1 Y 1 A GLU 72 ? A GLU 72 
73 1 Y 1 A ARG 73 ? A ARG 73 
74 1 Y 1 A LEU 74 ? A LEU 74 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
DTT S1   S  N N 88  
DTT C1   C  N N 89  
DTT C2   C  N R 90  
DTT O2   O  N N 91  
DTT C3   C  N R 92  
DTT O3   O  N N 93  
DTT C4   C  N N 94  
DTT S4   S  N N 95  
DTT HS1  H  N N 96  
DTT H11  H  N N 97  
DTT H12  H  N N 98  
DTT H2   H  N N 99  
DTT HO2  H  N N 100 
DTT H3   H  N N 101 
DTT HO3  H  N N 102 
DTT H41  H  N N 103 
DTT H42  H  N N 104 
DTT HS2  H  N N 105 
GLC C1   C  N S 106 
GLC C2   C  N R 107 
GLC C3   C  N S 108 
GLC C4   C  N S 109 
GLC C5   C  N R 110 
GLC C6   C  N N 111 
GLC O1   O  N N 112 
GLC O2   O  N N 113 
GLC O3   O  N N 114 
GLC O4   O  N N 115 
GLC O5   O  N N 116 
GLC O6   O  N N 117 
GLC H1   H  N N 118 
GLC H2   H  N N 119 
GLC H3   H  N N 120 
GLC H4   H  N N 121 
GLC H5   H  N N 122 
GLC H61  H  N N 123 
GLC H62  H  N N 124 
GLC HO1  H  N N 125 
GLC HO2  H  N N 126 
GLC HO3  H  N N 127 
GLC HO4  H  N N 128 
GLC HO6  H  N N 129 
GLN N    N  N N 130 
GLN CA   C  N S 131 
GLN C    C  N N 132 
GLN O    O  N N 133 
GLN CB   C  N N 134 
GLN CG   C  N N 135 
GLN CD   C  N N 136 
GLN OE1  O  N N 137 
GLN NE2  N  N N 138 
GLN OXT  O  N N 139 
GLN H    H  N N 140 
GLN H2   H  N N 141 
GLN HA   H  N N 142 
GLN HB2  H  N N 143 
GLN HB3  H  N N 144 
GLN HG2  H  N N 145 
GLN HG3  H  N N 146 
GLN HE21 H  N N 147 
GLN HE22 H  N N 148 
GLN HXT  H  N N 149 
GLU N    N  N N 150 
GLU CA   C  N S 151 
GLU C    C  N N 152 
GLU O    O  N N 153 
GLU CB   C  N N 154 
GLU CG   C  N N 155 
GLU CD   C  N N 156 
GLU OE1  O  N N 157 
GLU OE2  O  N N 158 
GLU OXT  O  N N 159 
GLU H    H  N N 160 
GLU H2   H  N N 161 
GLU HA   H  N N 162 
GLU HB2  H  N N 163 
GLU HB3  H  N N 164 
GLU HG2  H  N N 165 
GLU HG3  H  N N 166 
GLU HE2  H  N N 167 
GLU HXT  H  N N 168 
GLY N    N  N N 169 
GLY CA   C  N N 170 
GLY C    C  N N 171 
GLY O    O  N N 172 
GLY OXT  O  N N 173 
GLY H    H  N N 174 
GLY H2   H  N N 175 
GLY HA2  H  N N 176 
GLY HA3  H  N N 177 
GLY HXT  H  N N 178 
HIS N    N  N N 179 
HIS CA   C  N S 180 
HIS C    C  N N 181 
HIS O    O  N N 182 
HIS CB   C  N N 183 
HIS CG   C  Y N 184 
HIS ND1  N  Y N 185 
HIS CD2  C  Y N 186 
HIS CE1  C  Y N 187 
HIS NE2  N  Y N 188 
HIS OXT  O  N N 189 
HIS H    H  N N 190 
HIS H2   H  N N 191 
HIS HA   H  N N 192 
HIS HB2  H  N N 193 
HIS HB3  H  N N 194 
HIS HD1  H  N N 195 
HIS HD2  H  N N 196 
HIS HE1  H  N N 197 
HIS HE2  H  N N 198 
HIS HXT  H  N N 199 
HOH O    O  N N 200 
HOH H1   H  N N 201 
HOH H2   H  N N 202 
ILE N    N  N N 203 
ILE CA   C  N S 204 
ILE C    C  N N 205 
ILE O    O  N N 206 
ILE CB   C  N S 207 
ILE CG1  C  N N 208 
ILE CG2  C  N N 209 
ILE CD1  C  N N 210 
ILE OXT  O  N N 211 
ILE H    H  N N 212 
ILE H2   H  N N 213 
ILE HA   H  N N 214 
ILE HB   H  N N 215 
ILE HG12 H  N N 216 
ILE HG13 H  N N 217 
ILE HG21 H  N N 218 
ILE HG22 H  N N 219 
ILE HG23 H  N N 220 
ILE HD11 H  N N 221 
ILE HD12 H  N N 222 
ILE HD13 H  N N 223 
ILE HXT  H  N N 224 
LEU N    N  N N 225 
LEU CA   C  N S 226 
LEU C    C  N N 227 
LEU O    O  N N 228 
LEU CB   C  N N 229 
LEU CG   C  N N 230 
LEU CD1  C  N N 231 
LEU CD2  C  N N 232 
LEU OXT  O  N N 233 
LEU H    H  N N 234 
LEU H2   H  N N 235 
LEU HA   H  N N 236 
LEU HB2  H  N N 237 
LEU HB3  H  N N 238 
LEU HG   H  N N 239 
LEU HD11 H  N N 240 
LEU HD12 H  N N 241 
LEU HD13 H  N N 242 
LEU HD21 H  N N 243 
LEU HD22 H  N N 244 
LEU HD23 H  N N 245 
LEU HXT  H  N N 246 
LYS N    N  N N 247 
LYS CA   C  N S 248 
LYS C    C  N N 249 
LYS O    O  N N 250 
LYS CB   C  N N 251 
LYS CG   C  N N 252 
LYS CD   C  N N 253 
LYS CE   C  N N 254 
LYS NZ   N  N N 255 
LYS OXT  O  N N 256 
LYS H    H  N N 257 
LYS H2   H  N N 258 
LYS HA   H  N N 259 
LYS HB2  H  N N 260 
LYS HB3  H  N N 261 
LYS HG2  H  N N 262 
LYS HG3  H  N N 263 
LYS HD2  H  N N 264 
LYS HD3  H  N N 265 
LYS HE2  H  N N 266 
LYS HE3  H  N N 267 
LYS HZ1  H  N N 268 
LYS HZ2  H  N N 269 
LYS HZ3  H  N N 270 
LYS HXT  H  N N 271 
MET N    N  N N 272 
MET CA   C  N S 273 
MET C    C  N N 274 
MET O    O  N N 275 
MET CB   C  N N 276 
MET CG   C  N N 277 
MET SD   S  N N 278 
MET CE   C  N N 279 
MET OXT  O  N N 280 
MET H    H  N N 281 
MET H2   H  N N 282 
MET HA   H  N N 283 
MET HB2  H  N N 284 
MET HB3  H  N N 285 
MET HG2  H  N N 286 
MET HG3  H  N N 287 
MET HE1  H  N N 288 
MET HE2  H  N N 289 
MET HE3  H  N N 290 
MET HXT  H  N N 291 
PHE N    N  N N 292 
PHE CA   C  N S 293 
PHE C    C  N N 294 
PHE O    O  N N 295 
PHE CB   C  N N 296 
PHE CG   C  Y N 297 
PHE CD1  C  Y N 298 
PHE CD2  C  Y N 299 
PHE CE1  C  Y N 300 
PHE CE2  C  Y N 301 
PHE CZ   C  Y N 302 
PHE OXT  O  N N 303 
PHE H    H  N N 304 
PHE H2   H  N N 305 
PHE HA   H  N N 306 
PHE HB2  H  N N 307 
PHE HB3  H  N N 308 
PHE HD1  H  N N 309 
PHE HD2  H  N N 310 
PHE HE1  H  N N 311 
PHE HE2  H  N N 312 
PHE HZ   H  N N 313 
PHE HXT  H  N N 314 
PRO N    N  N N 315 
PRO CA   C  N S 316 
PRO C    C  N N 317 
PRO O    O  N N 318 
PRO CB   C  N N 319 
PRO CG   C  N N 320 
PRO CD   C  N N 321 
PRO OXT  O  N N 322 
PRO H    H  N N 323 
PRO HA   H  N N 324 
PRO HB2  H  N N 325 
PRO HB3  H  N N 326 
PRO HG2  H  N N 327 
PRO HG3  H  N N 328 
PRO HD2  H  N N 329 
PRO HD3  H  N N 330 
PRO HXT  H  N N 331 
SER N    N  N N 332 
SER CA   C  N S 333 
SER C    C  N N 334 
SER O    O  N N 335 
SER CB   C  N N 336 
SER OG   O  N N 337 
SER OXT  O  N N 338 
SER H    H  N N 339 
SER H2   H  N N 340 
SER HA   H  N N 341 
SER HB2  H  N N 342 
SER HB3  H  N N 343 
SER HG   H  N N 344 
SER HXT  H  N N 345 
SF4 FE1  FE N N 346 
SF4 FE2  FE N N 347 
SF4 FE3  FE N N 348 
SF4 FE4  FE N N 349 
SF4 S1   S  N N 350 
SF4 S2   S  N N 351 
SF4 S3   S  N N 352 
SF4 S4   S  N N 353 
SO4 S    S  N N 354 
SO4 O1   O  N N 355 
SO4 O2   O  N N 356 
SO4 O3   O  N N 357 
SO4 O4   O  N N 358 
THR N    N  N N 359 
THR CA   C  N S 360 
THR C    C  N N 361 
THR O    O  N N 362 
THR CB   C  N R 363 
THR OG1  O  N N 364 
THR CG2  C  N N 365 
THR OXT  O  N N 366 
THR H    H  N N 367 
THR H2   H  N N 368 
THR HA   H  N N 369 
THR HB   H  N N 370 
THR HG1  H  N N 371 
THR HG21 H  N N 372 
THR HG22 H  N N 373 
THR HG23 H  N N 374 
THR HXT  H  N N 375 
TRP N    N  N N 376 
TRP CA   C  N S 377 
TRP C    C  N N 378 
TRP O    O  N N 379 
TRP CB   C  N N 380 
TRP CG   C  Y N 381 
TRP CD1  C  Y N 382 
TRP CD2  C  Y N 383 
TRP NE1  N  Y N 384 
TRP CE2  C  Y N 385 
TRP CE3  C  Y N 386 
TRP CZ2  C  Y N 387 
TRP CZ3  C  Y N 388 
TRP CH2  C  Y N 389 
TRP OXT  O  N N 390 
TRP H    H  N N 391 
TRP H2   H  N N 392 
TRP HA   H  N N 393 
TRP HB2  H  N N 394 
TRP HB3  H  N N 395 
TRP HD1  H  N N 396 
TRP HE1  H  N N 397 
TRP HE3  H  N N 398 
TRP HZ2  H  N N 399 
TRP HZ3  H  N N 400 
TRP HH2  H  N N 401 
TRP HXT  H  N N 402 
TYR N    N  N N 403 
TYR CA   C  N S 404 
TYR C    C  N N 405 
TYR O    O  N N 406 
TYR CB   C  N N 407 
TYR CG   C  Y N 408 
TYR CD1  C  Y N 409 
TYR CD2  C  Y N 410 
TYR CE1  C  Y N 411 
TYR CE2  C  Y N 412 
TYR CZ   C  Y N 413 
TYR OH   O  N N 414 
TYR OXT  O  N N 415 
TYR H    H  N N 416 
TYR H2   H  N N 417 
TYR HA   H  N N 418 
TYR HB2  H  N N 419 
TYR HB3  H  N N 420 
TYR HD1  H  N N 421 
TYR HD2  H  N N 422 
TYR HE1  H  N N 423 
TYR HE2  H  N N 424 
TYR HH   H  N N 425 
TYR HXT  H  N N 426 
VAL N    N  N N 427 
VAL CA   C  N S 428 
VAL C    C  N N 429 
VAL O    O  N N 430 
VAL CB   C  N N 431 
VAL CG1  C  N N 432 
VAL CG2  C  N N 433 
VAL OXT  O  N N 434 
VAL H    H  N N 435 
VAL H2   H  N N 436 
VAL HA   H  N N 437 
VAL HB   H  N N 438 
VAL HG11 H  N N 439 
VAL HG12 H  N N 440 
VAL HG13 H  N N 441 
VAL HG21 H  N N 442 
VAL HG22 H  N N 443 
VAL HG23 H  N N 444 
VAL HXT  H  N N 445 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
DTT S1  C1   sing N N 83  
DTT S1  HS1  sing N N 84  
DTT C1  C2   sing N N 85  
DTT C1  H11  sing N N 86  
DTT C1  H12  sing N N 87  
DTT C2  O2   sing N N 88  
DTT C2  C3   sing N N 89  
DTT C2  H2   sing N N 90  
DTT O2  HO2  sing N N 91  
DTT C3  O3   sing N N 92  
DTT C3  C4   sing N N 93  
DTT C3  H3   sing N N 94  
DTT O3  HO3  sing N N 95  
DTT C4  S4   sing N N 96  
DTT C4  H41  sing N N 97  
DTT C4  H42  sing N N 98  
DTT S4  HS2  sing N N 99  
GLC C1  C2   sing N N 100 
GLC C1  O1   sing N N 101 
GLC C1  O5   sing N N 102 
GLC C1  H1   sing N N 103 
GLC C2  C3   sing N N 104 
GLC C2  O2   sing N N 105 
GLC C2  H2   sing N N 106 
GLC C3  C4   sing N N 107 
GLC C3  O3   sing N N 108 
GLC C3  H3   sing N N 109 
GLC C4  C5   sing N N 110 
GLC C4  O4   sing N N 111 
GLC C4  H4   sing N N 112 
GLC C5  C6   sing N N 113 
GLC C5  O5   sing N N 114 
GLC C5  H5   sing N N 115 
GLC C6  O6   sing N N 116 
GLC C6  H61  sing N N 117 
GLC C6  H62  sing N N 118 
GLC O1  HO1  sing N N 119 
GLC O2  HO2  sing N N 120 
GLC O3  HO3  sing N N 121 
GLC O4  HO4  sing N N 122 
GLC O6  HO6  sing N N 123 
GLN N   CA   sing N N 124 
GLN N   H    sing N N 125 
GLN N   H2   sing N N 126 
GLN CA  C    sing N N 127 
GLN CA  CB   sing N N 128 
GLN CA  HA   sing N N 129 
GLN C   O    doub N N 130 
GLN C   OXT  sing N N 131 
GLN CB  CG   sing N N 132 
GLN CB  HB2  sing N N 133 
GLN CB  HB3  sing N N 134 
GLN CG  CD   sing N N 135 
GLN CG  HG2  sing N N 136 
GLN CG  HG3  sing N N 137 
GLN CD  OE1  doub N N 138 
GLN CD  NE2  sing N N 139 
GLN NE2 HE21 sing N N 140 
GLN NE2 HE22 sing N N 141 
GLN OXT HXT  sing N N 142 
GLU N   CA   sing N N 143 
GLU N   H    sing N N 144 
GLU N   H2   sing N N 145 
GLU CA  C    sing N N 146 
GLU CA  CB   sing N N 147 
GLU CA  HA   sing N N 148 
GLU C   O    doub N N 149 
GLU C   OXT  sing N N 150 
GLU CB  CG   sing N N 151 
GLU CB  HB2  sing N N 152 
GLU CB  HB3  sing N N 153 
GLU CG  CD   sing N N 154 
GLU CG  HG2  sing N N 155 
GLU CG  HG3  sing N N 156 
GLU CD  OE1  doub N N 157 
GLU CD  OE2  sing N N 158 
GLU OE2 HE2  sing N N 159 
GLU OXT HXT  sing N N 160 
GLY N   CA   sing N N 161 
GLY N   H    sing N N 162 
GLY N   H2   sing N N 163 
GLY CA  C    sing N N 164 
GLY CA  HA2  sing N N 165 
GLY CA  HA3  sing N N 166 
GLY C   O    doub N N 167 
GLY C   OXT  sing N N 168 
GLY OXT HXT  sing N N 169 
HIS N   CA   sing N N 170 
HIS N   H    sing N N 171 
HIS N   H2   sing N N 172 
HIS CA  C    sing N N 173 
HIS CA  CB   sing N N 174 
HIS CA  HA   sing N N 175 
HIS C   O    doub N N 176 
HIS C   OXT  sing N N 177 
HIS CB  CG   sing N N 178 
HIS CB  HB2  sing N N 179 
HIS CB  HB3  sing N N 180 
HIS CG  ND1  sing Y N 181 
HIS CG  CD2  doub Y N 182 
HIS ND1 CE1  doub Y N 183 
HIS ND1 HD1  sing N N 184 
HIS CD2 NE2  sing Y N 185 
HIS CD2 HD2  sing N N 186 
HIS CE1 NE2  sing Y N 187 
HIS CE1 HE1  sing N N 188 
HIS NE2 HE2  sing N N 189 
HIS OXT HXT  sing N N 190 
HOH O   H1   sing N N 191 
HOH O   H2   sing N N 192 
ILE N   CA   sing N N 193 
ILE N   H    sing N N 194 
ILE N   H2   sing N N 195 
ILE CA  C    sing N N 196 
ILE CA  CB   sing N N 197 
ILE CA  HA   sing N N 198 
ILE C   O    doub N N 199 
ILE C   OXT  sing N N 200 
ILE CB  CG1  sing N N 201 
ILE CB  CG2  sing N N 202 
ILE CB  HB   sing N N 203 
ILE CG1 CD1  sing N N 204 
ILE CG1 HG12 sing N N 205 
ILE CG1 HG13 sing N N 206 
ILE CG2 HG21 sing N N 207 
ILE CG2 HG22 sing N N 208 
ILE CG2 HG23 sing N N 209 
ILE CD1 HD11 sing N N 210 
ILE CD1 HD12 sing N N 211 
ILE CD1 HD13 sing N N 212 
ILE OXT HXT  sing N N 213 
LEU N   CA   sing N N 214 
LEU N   H    sing N N 215 
LEU N   H2   sing N N 216 
LEU CA  C    sing N N 217 
LEU CA  CB   sing N N 218 
LEU CA  HA   sing N N 219 
LEU C   O    doub N N 220 
LEU C   OXT  sing N N 221 
LEU CB  CG   sing N N 222 
LEU CB  HB2  sing N N 223 
LEU CB  HB3  sing N N 224 
LEU CG  CD1  sing N N 225 
LEU CG  CD2  sing N N 226 
LEU CG  HG   sing N N 227 
LEU CD1 HD11 sing N N 228 
LEU CD1 HD12 sing N N 229 
LEU CD1 HD13 sing N N 230 
LEU CD2 HD21 sing N N 231 
LEU CD2 HD22 sing N N 232 
LEU CD2 HD23 sing N N 233 
LEU OXT HXT  sing N N 234 
LYS N   CA   sing N N 235 
LYS N   H    sing N N 236 
LYS N   H2   sing N N 237 
LYS CA  C    sing N N 238 
LYS CA  CB   sing N N 239 
LYS CA  HA   sing N N 240 
LYS C   O    doub N N 241 
LYS C   OXT  sing N N 242 
LYS CB  CG   sing N N 243 
LYS CB  HB2  sing N N 244 
LYS CB  HB3  sing N N 245 
LYS CG  CD   sing N N 246 
LYS CG  HG2  sing N N 247 
LYS CG  HG3  sing N N 248 
LYS CD  CE   sing N N 249 
LYS CD  HD2  sing N N 250 
LYS CD  HD3  sing N N 251 
LYS CE  NZ   sing N N 252 
LYS CE  HE2  sing N N 253 
LYS CE  HE3  sing N N 254 
LYS NZ  HZ1  sing N N 255 
LYS NZ  HZ2  sing N N 256 
LYS NZ  HZ3  sing N N 257 
LYS OXT HXT  sing N N 258 
MET N   CA   sing N N 259 
MET N   H    sing N N 260 
MET N   H2   sing N N 261 
MET CA  C    sing N N 262 
MET CA  CB   sing N N 263 
MET CA  HA   sing N N 264 
MET C   O    doub N N 265 
MET C   OXT  sing N N 266 
MET CB  CG   sing N N 267 
MET CB  HB2  sing N N 268 
MET CB  HB3  sing N N 269 
MET CG  SD   sing N N 270 
MET CG  HG2  sing N N 271 
MET CG  HG3  sing N N 272 
MET SD  CE   sing N N 273 
MET CE  HE1  sing N N 274 
MET CE  HE2  sing N N 275 
MET CE  HE3  sing N N 276 
MET OXT HXT  sing N N 277 
PHE N   CA   sing N N 278 
PHE N   H    sing N N 279 
PHE N   H2   sing N N 280 
PHE CA  C    sing N N 281 
PHE CA  CB   sing N N 282 
PHE CA  HA   sing N N 283 
PHE C   O    doub N N 284 
PHE C   OXT  sing N N 285 
PHE CB  CG   sing N N 286 
PHE CB  HB2  sing N N 287 
PHE CB  HB3  sing N N 288 
PHE CG  CD1  doub Y N 289 
PHE CG  CD2  sing Y N 290 
PHE CD1 CE1  sing Y N 291 
PHE CD1 HD1  sing N N 292 
PHE CD2 CE2  doub Y N 293 
PHE CD2 HD2  sing N N 294 
PHE CE1 CZ   doub Y N 295 
PHE CE1 HE1  sing N N 296 
PHE CE2 CZ   sing Y N 297 
PHE CE2 HE2  sing N N 298 
PHE CZ  HZ   sing N N 299 
PHE OXT HXT  sing N N 300 
PRO N   CA   sing N N 301 
PRO N   CD   sing N N 302 
PRO N   H    sing N N 303 
PRO CA  C    sing N N 304 
PRO CA  CB   sing N N 305 
PRO CA  HA   sing N N 306 
PRO C   O    doub N N 307 
PRO C   OXT  sing N N 308 
PRO CB  CG   sing N N 309 
PRO CB  HB2  sing N N 310 
PRO CB  HB3  sing N N 311 
PRO CG  CD   sing N N 312 
PRO CG  HG2  sing N N 313 
PRO CG  HG3  sing N N 314 
PRO CD  HD2  sing N N 315 
PRO CD  HD3  sing N N 316 
PRO OXT HXT  sing N N 317 
SER N   CA   sing N N 318 
SER N   H    sing N N 319 
SER N   H2   sing N N 320 
SER CA  C    sing N N 321 
SER CA  CB   sing N N 322 
SER CA  HA   sing N N 323 
SER C   O    doub N N 324 
SER C   OXT  sing N N 325 
SER CB  OG   sing N N 326 
SER CB  HB2  sing N N 327 
SER CB  HB3  sing N N 328 
SER OG  HG   sing N N 329 
SER OXT HXT  sing N N 330 
SF4 FE1 S2   sing N N 331 
SF4 FE1 S3   sing N N 332 
SF4 FE1 S4   sing N N 333 
SF4 FE2 S1   sing N N 334 
SF4 FE2 S3   sing N N 335 
SF4 FE2 S4   sing N N 336 
SF4 FE3 S1   sing N N 337 
SF4 FE3 S2   sing N N 338 
SF4 FE3 S4   sing N N 339 
SF4 FE4 S1   sing N N 340 
SF4 FE4 S2   sing N N 341 
SF4 FE4 S3   sing N N 342 
SO4 S   O1   doub N N 343 
SO4 S   O2   doub N N 344 
SO4 S   O3   sing N N 345 
SO4 S   O4   sing N N 346 
THR N   CA   sing N N 347 
THR N   H    sing N N 348 
THR N   H2   sing N N 349 
THR CA  C    sing N N 350 
THR CA  CB   sing N N 351 
THR CA  HA   sing N N 352 
THR C   O    doub N N 353 
THR C   OXT  sing N N 354 
THR CB  OG1  sing N N 355 
THR CB  CG2  sing N N 356 
THR CB  HB   sing N N 357 
THR OG1 HG1  sing N N 358 
THR CG2 HG21 sing N N 359 
THR CG2 HG22 sing N N 360 
THR CG2 HG23 sing N N 361 
THR OXT HXT  sing N N 362 
TRP N   CA   sing N N 363 
TRP N   H    sing N N 364 
TRP N   H2   sing N N 365 
TRP CA  C    sing N N 366 
TRP CA  CB   sing N N 367 
TRP CA  HA   sing N N 368 
TRP C   O    doub N N 369 
TRP C   OXT  sing N N 370 
TRP CB  CG   sing N N 371 
TRP CB  HB2  sing N N 372 
TRP CB  HB3  sing N N 373 
TRP CG  CD1  doub Y N 374 
TRP CG  CD2  sing Y N 375 
TRP CD1 NE1  sing Y N 376 
TRP CD1 HD1  sing N N 377 
TRP CD2 CE2  doub Y N 378 
TRP CD2 CE3  sing Y N 379 
TRP NE1 CE2  sing Y N 380 
TRP NE1 HE1  sing N N 381 
TRP CE2 CZ2  sing Y N 382 
TRP CE3 CZ3  doub Y N 383 
TRP CE3 HE3  sing N N 384 
TRP CZ2 CH2  doub Y N 385 
TRP CZ2 HZ2  sing N N 386 
TRP CZ3 CH2  sing Y N 387 
TRP CZ3 HZ3  sing N N 388 
TRP CH2 HH2  sing N N 389 
TRP OXT HXT  sing N N 390 
TYR N   CA   sing N N 391 
TYR N   H    sing N N 392 
TYR N   H2   sing N N 393 
TYR CA  C    sing N N 394 
TYR CA  CB   sing N N 395 
TYR CA  HA   sing N N 396 
TYR C   O    doub N N 397 
TYR C   OXT  sing N N 398 
TYR CB  CG   sing N N 399 
TYR CB  HB2  sing N N 400 
TYR CB  HB3  sing N N 401 
TYR CG  CD1  doub Y N 402 
TYR CG  CD2  sing Y N 403 
TYR CD1 CE1  sing Y N 404 
TYR CD1 HD1  sing N N 405 
TYR CD2 CE2  doub Y N 406 
TYR CD2 HD2  sing N N 407 
TYR CE1 CZ   doub Y N 408 
TYR CE1 HE1  sing N N 409 
TYR CE2 CZ   sing Y N 410 
TYR CE2 HE2  sing N N 411 
TYR CZ  OH   sing N N 412 
TYR OH  HH   sing N N 413 
TYR OXT HXT  sing N N 414 
VAL N   CA   sing N N 415 
VAL N   H    sing N N 416 
VAL N   H2   sing N N 417 
VAL CA  C    sing N N 418 
VAL CA  CB   sing N N 419 
VAL CA  HA   sing N N 420 
VAL C   O    doub N N 421 
VAL C   OXT  sing N N 422 
VAL CB  CG1  sing N N 423 
VAL CB  CG2  sing N N 424 
VAL CB  HB   sing N N 425 
VAL CG1 HG11 sing N N 426 
VAL CG1 HG12 sing N N 427 
VAL CG1 HG13 sing N N 428 
VAL CG2 HG21 sing N N 429 
VAL CG2 HG22 sing N N 430 
VAL CG2 HG23 sing N N 431 
VAL OXT HXT  sing N N 432 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' GM-122595  1 
'National Science Foundation (NSF, United States)'                                         'United States' MCB1716686 2 
'Howard Hughes Medical Institute (HHMI)'                                                   'United States' SJB        3 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 GLC 1 n 
2 GLC 2 n 
# 
_atom_sites.entry_id                    8TRW 
_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]   0.014630 
_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]   0.011263 
_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]   0.009245 
_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  
FE 
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   . ARG A 1 75  ? 18.843 13.640  34.289 1.00 33.22 ? 75  ARG A N   1 
ATOM   2    C  CA  . ARG A 1 75  ? 19.354 13.334  32.951 1.00 32.70 ? 75  ARG A CA  1 
ATOM   3    C  C   . ARG A 1 75  ? 20.499 14.289  32.589 1.00 23.21 ? 75  ARG A C   1 
ATOM   4    O  O   . ARG A 1 75  ? 20.261 15.480  32.410 1.00 26.58 ? 75  ARG A O   1 
ATOM   5    C  CB  . ARG A 1 75  ? 18.214 13.426  31.924 1.00 26.59 ? 75  ARG A CB  1 
ATOM   6    C  CG  . ARG A 1 75  ? 18.581 13.175  30.456 1.00 25.19 ? 75  ARG A CG  1 
ATOM   7    C  CD  . ARG A 1 75  ? 17.292 12.984  29.616 1.00 27.36 ? 75  ARG A CD  1 
ATOM   8    N  NE  . ARG A 1 75  ? 16.557 11.817  30.099 1.00 32.63 ? 75  ARG A NE  1 
ATOM   9    C  CZ  . ARG A 1 75  ? 15.318 11.480  29.749 1.00 35.62 ? 75  ARG A CZ  1 
ATOM   10   N  NH1 . ARG A 1 75  ? 14.742 10.381  30.217 1.00 40.81 ? 75  ARG A NH1 1 
ATOM   11   N  NH2 . ARG A 1 75  ? 14.631 12.268  28.920 1.00 30.03 ? 75  ARG A NH2 1 
ATOM   12   N  N   . LEU A 1 76  ? 21.719 13.756  32.479 1.00 23.15 ? 76  LEU A N   1 
ATOM   13   C  CA  . LEU A 1 76  ? 22.878 14.577  32.160 1.00 19.70 ? 76  LEU A CA  1 
ATOM   14   C  C   . LEU A 1 76  ? 22.724 15.207  30.775 1.00 16.56 ? 76  LEU A C   1 
ATOM   15   O  O   . LEU A 1 76  ? 22.117 14.625  29.875 1.00 16.97 ? 76  LEU A O   1 
ATOM   16   C  CB  . LEU A 1 76  ? 24.155 13.741  32.197 1.00 25.94 ? 76  LEU A CB  1 
ATOM   17   C  CG  . LEU A 1 76  ? 24.583 13.139  33.539 1.00 27.15 ? 76  LEU A CG  1 
ATOM   18   C  CD1 . LEU A 1 76  ? 25.886 12.391  33.341 1.00 28.79 ? 76  LEU A CD1 1 
ATOM   19   C  CD2 . LEU A 1 76  ? 24.735 14.227  34.606 1.00 32.54 ? 76  LEU A CD2 1 
ATOM   20   N  N   . PRO A 1 77  ? 23.285 16.390  30.570 1.00 17.15 ? 77  PRO A N   1 
ATOM   21   C  CA  . PRO A 1 77  ? 23.278 16.990  29.238 1.00 16.87 ? 77  PRO A CA  1 
ATOM   22   C  C   . PRO A 1 77  ? 24.143 16.193  28.277 1.00 12.07 ? 77  PRO A C   1 
ATOM   23   O  O   . PRO A 1 77  ? 25.077 15.490  28.687 1.00 15.15 ? 77  PRO A O   1 
ATOM   24   C  CB  . PRO A 1 77  ? 23.843 18.393  29.483 1.00 13.01 ? 77  PRO A CB  1 
ATOM   25   C  CG  . PRO A 1 77  ? 24.660 18.278  30.723 1.00 12.41 ? 77  PRO A CG  1 
ATOM   26   C  CD  . PRO A 1 77  ? 23.896 17.266  31.580 1.00 15.68 ? 77  PRO A CD  1 
ATOM   27   N  N   . PRO A 1 78  ? 23.890 16.311  26.977 1.00 13.93 ? 78  PRO A N   1 
ATOM   28   C  CA  . PRO A 1 78  ? 24.531 15.409  26.010 1.00 16.81 ? 78  PRO A CA  1 
ATOM   29   C  C   . PRO A 1 78  ? 26.021 15.678  25.839 1.00 15.17 ? 78  PRO A C   1 
ATOM   30   O  O   . PRO A 1 78  ? 26.769 14.778  25.422 1.00 19.94 ? 78  PRO A O   1 
ATOM   31   C  CB  . PRO A 1 78  ? 23.748 15.670  24.716 1.00 24.96 ? 78  PRO A CB  1 
ATOM   32   C  CG  . PRO A 1 78  ? 23.181 17.000  24.888 1.00 17.09 ? 78  PRO A CG  1 
ATOM   33   C  CD  . PRO A 1 78  ? 22.870 17.170  26.370 1.00 15.53 ? 78  PRO A CD  1 
ATOM   34   N  N   . TRP A 1 79  ? 26.492 16.858  26.240 1.00 13.90 ? 79  TRP A N   1 
ATOM   35   C  CA  . TRP A 1 79  ? 27.908 17.140  26.128 1.00 15.09 ? 79  TRP A CA  1 
ATOM   36   C  C   . TRP A 1 79  ? 28.745 16.472  27.224 1.00 16.42 ? 79  TRP A C   1 
ATOM   37   O  O   . TRP A 1 79  ? 29.969 16.645  27.246 1.00 15.95 ? 79  TRP A O   1 
ATOM   38   C  CB  . TRP A 1 79  ? 28.090 18.667  26.136 1.00 14.90 ? 79  TRP A CB  1 
ATOM   39   C  CG  . TRP A 1 79  ? 27.624 19.348  27.392 1.00 12.07 ? 79  TRP A CG  1 
ATOM   40   C  CD1 . TRP A 1 79  ? 28.229 19.284  28.611 1.00 11.33 ? 79  TRP A CD1 1 
ATOM   41   C  CD2 . TRP A 1 79  ? 26.492 20.234  27.555 1.00 10.76 ? 79  TRP A CD2 1 
ATOM   42   N  NE1 . TRP A 1 79  ? 27.570 20.069  29.516 1.00 10.31 ? 79  TRP A NE1 1 
ATOM   43   C  CE2 . TRP A 1 79  ? 26.504 20.672  28.895 1.00 10.41 ? 79  TRP A CE2 1 
ATOM   44   C  CE3 . TRP A 1 79  ? 25.500 20.735  26.684 1.00 11.36 ? 79  TRP A CE3 1 
ATOM   45   C  CZ2 . TRP A 1 79  ? 25.568 21.569  29.410 1.00 11.06 ? 79  TRP A CZ2 1 
ATOM   46   C  CZ3 . TRP A 1 79  ? 24.565 21.606  27.191 1.00 11.57 ? 79  TRP A CZ3 1 
ATOM   47   C  CH2 . TRP A 1 79  ? 24.586 22.021  28.538 1.00 11.22 ? 79  TRP A CH2 1 
ATOM   48   N  N   . LEU A 1 80  ? 28.130 15.701  28.127 1.00 12.77 ? 80  LEU A N   1 
ATOM   49   C  CA  . LEU A 1 80  ? 28.870 14.932  29.124 1.00 13.16 ? 80  LEU A CA  1 
ATOM   50   C  C   . LEU A 1 80  ? 28.947 13.456  28.764 1.00 17.07 ? 80  LEU A C   1 
ATOM   51   O  O   . LEU A 1 80  ? 29.406 12.649  29.580 1.00 22.36 ? 80  LEU A O   1 
ATOM   52   C  CB  . LEU A 1 80  ? 28.243 15.098  30.510 1.00 14.85 ? 80  LEU A CB  1 
ATOM   53   C  CG  . LEU A 1 80  ? 28.409 16.503  31.087 1.00 22.53 ? 80  LEU A CG  1 
ATOM   54   C  CD1 . LEU A 1 80  ? 27.626 16.620  32.400 1.00 24.82 ? 80  LEU A CD1 1 
ATOM   55   C  CD2 . LEU A 1 80  ? 29.864 16.872  31.310 1.00 19.04 ? 80  LEU A CD2 1 
ATOM   56   N  N   . LYS A 1 81  ? 28.535 13.111  27.552 1.00 17.14 ? 81  LYS A N   1 
ATOM   57   C  CA  A LYS A 1 81  ? 28.553 11.749  27.053 0.42 25.39 ? 81  LYS A CA  1 
ATOM   58   C  CA  B LYS A 1 81  ? 28.525 11.756  27.027 0.58 25.39 ? 81  LYS A CA  1 
ATOM   59   C  C   . LYS A 1 81  ? 29.570 11.634  25.926 1.00 30.17 ? 81  LYS A C   1 
ATOM   60   O  O   . LYS A 1 81  ? 29.869 12.611  25.233 1.00 33.01 ? 81  LYS A O   1 
ATOM   61   C  CB  A LYS A 1 81  ? 27.168 11.344  26.539 0.42 29.66 ? 81  LYS A CB  1 
ATOM   62   C  CB  B LYS A 1 81  ? 27.146 11.409  26.444 0.58 29.68 ? 81  LYS A CB  1 
ATOM   63   C  CG  A LYS A 1 81  ? 26.926 11.719  25.090 0.42 30.02 ? 81  LYS A CG  1 
ATOM   64   C  CG  B LYS A 1 81  ? 27.102 11.453  24.910 0.58 32.10 ? 81  LYS A CG  1 
ATOM   65   C  CD  A LYS A 1 81  ? 25.451 11.825  24.733 0.42 33.08 ? 81  LYS A CD  1 
ATOM   66   C  CD  B LYS A 1 81  ? 25.844 12.105  24.354 0.58 35.31 ? 81  LYS A CD  1 
ATOM   67   C  CE  A LYS A 1 81  ? 25.310 12.234  23.273 0.42 31.77 ? 81  LYS A CE  1 
ATOM   68   C  CE  B LYS A 1 81  ? 26.170 12.879  23.070 0.58 32.91 ? 81  LYS A CE  1 
ATOM   69   N  NZ  A LYS A 1 81  ? 23.940 12.671  22.922 0.42 30.44 ? 81  LYS A NZ  1 
ATOM   70   N  NZ  B LYS A 1 81  ? 27.238 13.908  23.289 0.58 29.22 ? 81  LYS A NZ  1 
ATOM   71   N  N   . THR A 1 82  ? 30.112 10.430  25.754 1.00 30.19 ? 82  THR A N   1 
ATOM   72   C  CA  . THR A 1 82  ? 30.920 10.146  24.573 1.00 31.18 ? 82  THR A CA  1 
ATOM   73   C  C   . THR A 1 82  ? 30.438 8.859   23.927 1.00 31.58 ? 82  THR A C   1 
ATOM   74   O  O   . THR A 1 82  ? 29.772 8.028   24.558 1.00 31.46 ? 82  THR A O   1 
ATOM   75   C  CB  . THR A 1 82  ? 32.433 10.000  24.850 1.00 31.74 ? 82  THR A CB  1 
ATOM   76   O  OG1 . THR A 1 82  ? 32.666 8.945   25.801 1.00 37.36 ? 82  THR A OG1 1 
ATOM   77   C  CG2 . THR A 1 82  ? 33.030 11.312  25.332 1.00 22.40 ? 82  THR A CG2 1 
ATOM   78   N  N   . GLU A 1 83  ? 30.805 8.714   22.656 1.00 38.78 ? 83  GLU A N   1 
ATOM   79   C  CA  . GLU A 1 83  ? 30.615 7.460   21.947 1.00 40.05 ? 83  GLU A CA  1 
ATOM   80   C  C   . GLU A 1 83  ? 31.572 6.411   22.482 1.00 34.84 ? 83  GLU A C   1 
ATOM   81   O  O   . GLU A 1 83  ? 32.638 6.730   23.023 1.00 35.55 ? 83  GLU A O   1 
ATOM   82   C  CB  . GLU A 1 83  ? 30.839 7.652   20.450 1.00 41.26 ? 83  GLU A CB  1 
ATOM   83   C  CG  . GLU A 1 83  ? 29.596 8.136   19.749 1.00 45.03 ? 83  GLU A CG  1 
ATOM   84   C  CD  . GLU A 1 83  ? 28.410 7.272   20.105 1.00 49.50 ? 83  GLU A CD  1 
ATOM   85   O  OE1 . GLU A 1 83  ? 28.458 6.062   19.796 1.00 48.27 ? 83  GLU A OE1 1 
ATOM   86   O  OE2 . GLU A 1 83  ? 27.455 7.789   20.724 1.00 50.40 ? 83  GLU A OE2 1 
ATOM   87   N  N   . ILE A 1 84  ? 31.170 5.150   22.342 1.00 34.39 ? 84  ILE A N   1 
ATOM   88   C  CA  . ILE A 1 84  ? 32.019 4.030   22.718 1.00 34.48 ? 84  ILE A CA  1 
ATOM   89   C  C   . ILE A 1 84  ? 33.354 4.209   22.007 1.00 30.61 ? 84  ILE A C   1 
ATOM   90   O  O   . ILE A 1 84  ? 33.393 4.686   20.860 1.00 34.46 ? 84  ILE A O   1 
ATOM   91   C  CB  . ILE A 1 84  ? 31.371 2.680   22.372 1.00 34.66 ? 84  ILE A CB  1 
ATOM   92   C  CG1 . ILE A 1 84  ? 31.114 2.571   20.868 1.00 32.61 ? 84  ILE A CG1 1 
ATOM   93   C  CG2 . ILE A 1 84  ? 30.077 2.504   23.144 1.00 38.12 ? 84  ILE A CG2 1 
ATOM   94   C  CD1 . ILE A 1 84  ? 30.857 1.157   20.409 1.00 38.08 ? 84  ILE A CD1 1 
ATOM   95   N  N   . PRO A 1 85  ? 34.464 3.881   22.656 1.00 32.03 ? 85  PRO A N   1 
ATOM   96   C  CA  . PRO A 1 85  ? 35.758 3.939   21.971 1.00 28.52 ? 85  PRO A CA  1 
ATOM   97   C  C   . PRO A 1 85  ? 35.846 2.811   20.960 1.00 30.73 ? 85  PRO A C   1 
ATOM   98   O  O   . PRO A 1 85  ? 35.523 1.663   21.274 1.00 29.70 ? 85  PRO A O   1 
ATOM   99   C  CB  . PRO A 1 85  ? 36.768 3.764   23.107 1.00 25.82 ? 85  PRO A CB  1 
ATOM   100  C  CG  . PRO A 1 85  ? 36.033 2.978   24.143 1.00 30.54 ? 85  PRO A CG  1 
ATOM   101  C  CD  . PRO A 1 85  ? 34.576 3.361   24.029 1.00 30.39 ? 85  PRO A CD  1 
ATOM   102  N  N   . MET A 1 86  ? 36.270 3.148   19.736 1.00 29.69 ? 86  MET A N   1 
ATOM   103  C  CA  . MET A 1 86  ? 36.336 2.169   18.659 1.00 37.46 ? 86  MET A CA  1 
ATOM   104  C  C   . MET A 1 86  ? 37.574 2.303   17.788 1.00 32.63 ? 86  MET A C   1 
ATOM   105  O  O   . MET A 1 86  ? 37.717 1.537   16.829 1.00 37.04 ? 86  MET A O   1 
ATOM   106  C  CB  . MET A 1 86  ? 35.096 2.268   17.765 1.00 36.47 ? 86  MET A CB  1 
ATOM   107  C  CG  . MET A 1 86  ? 33.820 1.872   18.452 1.00 39.36 ? 86  MET A CG  1 
ATOM   108  S  SD  . MET A 1 86  ? 32.473 1.628   17.285 1.00 61.53 ? 86  MET A SD  1 
ATOM   109  C  CE  . MET A 1 86  ? 32.227 3.303   16.711 1.00 43.89 ? 86  MET A CE  1 
ATOM   110  N  N   . GLY A 1 87  ? 38.466 3.239   18.084 1.00 27.31 ? 87  GLY A N   1 
ATOM   111  C  CA  . GLY A 1 87  ? 39.580 3.486   17.192 1.00 33.71 ? 87  GLY A CA  1 
ATOM   112  C  C   . GLY A 1 87  ? 40.546 2.318   17.123 1.00 35.41 ? 87  GLY A C   1 
ATOM   113  O  O   . GLY A 1 87  ? 40.705 1.544   18.069 1.00 31.31 ? 87  GLY A O   1 
ATOM   114  N  N   . LYS A 1 88  ? 41.174 2.198   15.953 1.00 33.88 ? 88  LYS A N   1 
ATOM   115  C  CA  . LYS A 1 88  ? 42.272 1.266   15.720 1.00 33.30 ? 88  LYS A CA  1 
ATOM   116  C  C   . LYS A 1 88  ? 43.378 1.423   16.765 1.00 33.97 ? 88  LYS A C   1 
ATOM   117  O  O   . LYS A 1 88  ? 43.903 0.434   17.295 1.00 28.35 ? 88  LYS A O   1 
ATOM   118  C  CB  . LYS A 1 88  ? 42.793 1.532   14.305 1.00 36.56 ? 88  LYS A CB  1 
ATOM   119  C  CG  . LYS A 1 88  ? 43.938 0.726   13.771 1.00 44.03 ? 88  LYS A CG  1 
ATOM   120  C  CD  . LYS A 1 88  ? 44.357 1.378   12.434 1.00 46.90 ? 88  LYS A CD  1 
ATOM   121  C  CE  . LYS A 1 88  ? 45.250 0.505   11.572 1.00 48.94 ? 88  LYS A CE  1 
ATOM   122  N  NZ  . LYS A 1 88  ? 44.450 -0.412  10.700 1.00 50.29 ? 88  LYS A NZ  1 
ATOM   123  N  N   . ASN A 1 89  ? 43.760 2.667   17.057 1.00 26.73 ? 89  ASN A N   1 
ATOM   124  C  CA  . ASN A 1 89  ? 44.835 2.911   18.019 1.00 19.36 ? 89  ASN A CA  1 
ATOM   125  C  C   . ASN A 1 89  ? 44.413 2.536   19.430 1.00 25.71 ? 89  ASN A C   1 
ATOM   126  O  O   . ASN A 1 89  ? 45.199 1.953   20.190 1.00 21.41 ? 89  ASN A O   1 
ATOM   127  C  CB  . ASN A 1 89  ? 45.242 4.383   17.975 1.00 24.18 ? 89  ASN A CB  1 
ATOM   128  C  CG  . ASN A 1 89  ? 45.970 4.750   16.690 1.00 31.96 ? 89  ASN A CG  1 
ATOM   129  O  OD1 . ASN A 1 89  ? 46.586 3.895   16.039 1.00 36.29 ? 89  ASN A OD1 1 
ATOM   130  N  ND2 . ASN A 1 89  ? 45.910 6.022   16.322 1.00 28.29 ? 89  ASN A ND2 1 
ATOM   131  N  N   . TYR A 1 90  ? 43.194 2.922   19.819 1.00 25.14 ? 90  TYR A N   1 
ATOM   132  C  CA  . TYR A 1 90  ? 42.659 2.510   21.111 1.00 22.84 ? 90  TYR A CA  1 
ATOM   133  C  C   . TYR A 1 90  ? 42.682 0.996   21.243 1.00 25.85 ? 90  TYR A C   1 
ATOM   134  O  O   . TYR A 1 90  ? 43.110 0.447   22.264 1.00 22.58 ? 90  TYR A O   1 
ATOM   135  C  CB  . TYR A 1 90  ? 41.230 3.047   21.282 1.00 25.09 ? 90  TYR A CB  1 
ATOM   136  C  CG  . TYR A 1 90  ? 40.470 2.378   22.402 1.00 19.60 ? 90  TYR A CG  1 
ATOM   137  C  CD1 . TYR A 1 90  ? 40.848 2.549   23.722 1.00 22.25 ? 90  TYR A CD1 1 
ATOM   138  C  CD2 . TYR A 1 90  ? 39.389 1.548   22.130 1.00 27.74 ? 90  TYR A CD2 1 
ATOM   139  C  CE1 . TYR A 1 90  ? 40.157 1.930   24.763 1.00 22.27 ? 90  TYR A CE1 1 
ATOM   140  C  CE2 . TYR A 1 90  ? 38.693 0.922   23.152 1.00 31.50 ? 90  TYR A CE2 1 
ATOM   141  C  CZ  . TYR A 1 90  ? 39.077 1.117   24.462 1.00 34.79 ? 90  TYR A CZ  1 
ATOM   142  O  OH  . TYR A 1 90  ? 38.382 0.496   25.473 1.00 31.62 ? 90  TYR A OH  1 
ATOM   143  N  N   . ASN A 1 91  ? 42.241 0.293   20.202 1.00 21.50 ? 91  ASN A N   1 
ATOM   144  C  CA  . ASN A 1 91  ? 42.163 -1.156  20.318 1.00 26.61 ? 91  ASN A CA  1 
ATOM   145  C  C   . ASN A 1 91  ? 43.544 -1.773  20.506 1.00 27.51 ? 91  ASN A C   1 
ATOM   146  O  O   . ASN A 1 91  ? 43.718 -2.677  21.332 1.00 22.78 ? 91  ASN A O   1 
ATOM   147  C  CB  . ASN A 1 91  ? 41.472 -1.733  19.089 1.00 27.73 ? 91  ASN A CB  1 
ATOM   148  C  CG  . ASN A 1 91  ? 41.095 -3.173  19.288 1.00 41.39 ? 91  ASN A CG  1 
ATOM   149  O  OD1 . ASN A 1 91  ? 40.268 -3.488  20.148 1.00 46.58 ? 91  ASN A OD1 1 
ATOM   150  N  ND2 . ASN A 1 91  ? 41.717 -4.064  18.520 1.00 46.61 ? 91  ASN A ND2 1 
ATOM   151  N  N   . LYS A 1 92  ? 44.543 -1.268  19.777 1.00 25.52 ? 92  LYS A N   1 
ATOM   152  C  CA  . LYS A 1 92  ? 45.897 -1.797  19.893 1.00 22.61 ? 92  LYS A CA  1 
ATOM   153  C  C   . LYS A 1 92  ? 46.480 -1.539  21.279 1.00 24.91 ? 92  LYS A C   1 
ATOM   154  O  O   . LYS A 1 92  ? 47.075 -2.445  21.879 1.00 23.11 ? 92  LYS A O   1 
ATOM   155  C  CB  . LYS A 1 92  ? 46.788 -1.199  18.806 1.00 25.43 ? 92  LYS A CB  1 
ATOM   156  C  CG  . LYS A 1 92  ? 48.102 -1.953  18.636 1.00 38.92 ? 92  LYS A CG  1 
ATOM   157  C  CD  . LYS A 1 92  ? 48.830 -1.609  17.333 1.00 38.47 ? 92  LYS A CD  1 
ATOM   158  C  CE  . LYS A 1 92  ? 50.139 -2.398  17.246 1.00 48.19 ? 92  LYS A CE  1 
ATOM   159  N  NZ  . LYS A 1 92  ? 51.003 -2.040  16.076 1.00 48.43 ? 92  LYS A NZ  1 
ATOM   160  N  N   . LEU A 1 93  ? 46.304 -0.320  21.820 1.00 20.49 ? 93  LEU A N   1 
ATOM   161  C  CA  . LEU A 1 93  ? 46.755 -0.046  23.189 1.00 17.58 ? 93  LEU A CA  1 
ATOM   162  C  C   . LEU A 1 93  ? 46.043 -0.930  24.204 1.00 18.70 ? 93  LEU A C   1 
ATOM   163  O  O   . LEU A 1 93  ? 46.665 -1.460  25.137 1.00 19.15 ? 93  LEU A O   1 
ATOM   164  C  CB  . LEU A 1 93  ? 46.519 1.422   23.529 1.00 17.22 ? 93  LEU A CB  1 
ATOM   165  C  CG  . LEU A 1 93  ? 47.493 2.383   22.847 1.00 24.65 ? 93  LEU A CG  1 
ATOM   166  C  CD1 . LEU A 1 93  ? 46.839 3.752   22.719 1.00 22.85 ? 93  LEU A CD1 1 
ATOM   167  C  CD2 . LEU A 1 93  ? 48.763 2.447   23.675 1.00 21.75 ? 93  LEU A CD2 1 
ATOM   168  N  N   . LYS A 1 94  ? 44.731 -1.096  24.038 1.00 20.47 ? 94  LYS A N   1 
ATOM   169  C  CA  . LYS A 1 94  ? 43.948 -1.905  24.961 1.00 21.57 ? 94  LYS A CA  1 
ATOM   170  C  C   . LYS A 1 94  ? 44.411 -3.362  24.953 1.00 25.78 ? 94  LYS A C   1 
ATOM   171  O  O   . LYS A 1 94  ? 44.581 -3.971  26.013 1.00 23.96 ? 94  LYS A O   1 
ATOM   172  C  CB  . LYS A 1 94  ? 42.469 -1.805  24.588 1.00 23.39 ? 94  LYS A CB  1 
ATOM   173  C  CG  . LYS A 1 94  ? 41.544 -2.549  25.531 1.00 32.68 ? 94  LYS A CG  1 
ATOM   174  C  CD  . LYS A 1 94  ? 41.285 -1.762  26.787 1.00 33.46 ? 94  LYS A CD  1 
ATOM   175  C  CE  . LYS A 1 94  ? 39.942 -2.130  27.395 1.00 36.43 ? 94  LYS A CE  1 
ATOM   176  N  NZ  . LYS A 1 94  ? 39.842 -1.649  28.806 1.00 43.42 ? 94  LYS A NZ  1 
ATOM   177  N  N   . ASN A 1 95  ? 44.657 -3.929  23.767 1.00 23.82 ? 95  ASN A N   1 
ATOM   178  C  CA  . ASN A 1 95  ? 45.091 -5.321  23.721 1.00 28.52 ? 95  ASN A CA  1 
ATOM   179  C  C   . ASN A 1 95  ? 46.450 -5.490  24.392 1.00 30.11 ? 95  ASN A C   1 
ATOM   180  O  O   . ASN A 1 95  ? 46.626 -6.370  25.240 1.00 30.68 ? 95  ASN A O   1 
ATOM   181  C  CB  . ASN A 1 95  ? 45.120 -5.816  22.278 1.00 30.78 ? 95  ASN A CB  1 
ATOM   182  C  CG  . ASN A 1 95  ? 43.724 -6.108  21.737 1.00 43.74 ? 95  ASN A CG  1 
ATOM   183  O  OD1 . ASN A 1 95  ? 42.824 -6.513  22.485 1.00 44.49 ? 95  ASN A OD1 1 
ATOM   184  N  ND2 . ASN A 1 95  ? 43.536 -5.901  20.435 1.00 49.79 ? 95  ASN A ND2 1 
ATOM   185  N  N   . THR A 1 96  ? 47.403 -4.612  24.066 1.00 26.02 ? 96  THR A N   1 
ATOM   186  C  CA  . THR A 1 96  ? 48.741 -4.699  24.659 1.00 24.49 ? 96  THR A CA  1 
ATOM   187  C  C   . THR A 1 96  ? 48.698 -4.584  26.182 1.00 26.93 ? 96  THR A C   1 
ATOM   188  O  O   . THR A 1 96  ? 49.412 -5.310  26.892 1.00 25.86 ? 96  THR A O   1 
ATOM   189  C  CB  . THR A 1 96  ? 49.636 -3.613  24.078 1.00 27.54 ? 96  THR A CB  1 
ATOM   190  O  OG1 . THR A 1 96  ? 49.705 -3.765  22.659 1.00 28.10 ? 96  THR A OG1 1 
ATOM   191  C  CG2 . THR A 1 96  ? 51.045 -3.709  24.641 1.00 24.35 ? 96  THR A CG2 1 
ATOM   192  N  N   . LEU A 1 97  ? 47.869 -3.676  26.705 1.00 26.63 ? 97  LEU A N   1 
ATOM   193  C  CA  . LEU A 1 97  ? 47.798 -3.477  28.149 1.00 18.18 ? 97  LEU A CA  1 
ATOM   194  C  C   . LEU A 1 97  ? 47.348 -4.737  28.871 1.00 25.89 ? 97  LEU A C   1 
ATOM   195  O  O   . LEU A 1 97  ? 47.725 -4.961  30.020 1.00 22.60 ? 97  LEU A O   1 
ATOM   196  C  CB  . LEU A 1 97  ? 46.834 -2.329  28.469 1.00 17.97 ? 97  LEU A CB  1 
ATOM   197  C  CG  . LEU A 1 97  ? 46.591 -1.990  29.941 1.00 26.01 ? 97  LEU A CG  1 
ATOM   198  C  CD1 . LEU A 1 97  ? 47.859 -1.520  30.653 1.00 21.54 ? 97  LEU A CD1 1 
ATOM   199  C  CD2 . LEU A 1 97  ? 45.487 -0.935  30.060 1.00 20.48 ? 97  LEU A CD2 1 
ATOM   200  N  N   . ARG A 1 98  ? 46.542 -5.575  28.226 1.00 26.72 ? 98  ARG A N   1 
ATOM   201  C  CA  . ARG A 1 98  ? 45.926 -6.648  28.999 1.00 36.24 ? 98  ARG A CA  1 
ATOM   202  C  C   . ARG A 1 98  ? 46.944 -7.693  29.437 1.00 32.03 ? 98  ARG A C   1 
ATOM   203  O  O   . ARG A 1 98  ? 46.755 -8.348  30.472 1.00 35.51 ? 98  ARG A O   1 
ATOM   204  C  CB  . ARG A 1 98  ? 44.808 -7.296  28.205 1.00 37.07 ? 98  ARG A CB  1 
ATOM   205  C  CG  . ARG A 1 98  ? 44.100 -8.372  28.989 1.00 43.42 ? 98  ARG A CG  1 
ATOM   206  C  CD  . ARG A 1 98  ? 43.094 -9.052  28.115 1.00 51.53 ? 98  ARG A CD  1 
ATOM   207  N  NE  . ARG A 1 98  ? 43.420 -8.896  26.700 1.00 52.41 ? 98  ARG A NE  1 
ATOM   208  C  CZ  . ARG A 1 98  ? 42.711 -8.169  25.845 1.00 49.59 ? 98  ARG A CZ  1 
ATOM   209  N  NH1 . ARG A 1 98  ? 43.090 -8.021  24.584 1.00 49.91 ? 98  ARG A NH1 1 
ATOM   210  N  NH2 . ARG A 1 98  ? 41.592 -7.580  26.264 1.00 41.61 ? 98  ARG A NH2 1 
ATOM   211  N  N   . ASN A 1 99  ? 48.038 -7.849  28.696 1.00 28.51 ? 99  ASN A N   1 
ATOM   212  C  CA  . ASN A 1 99  ? 49.074 -8.786  29.104 1.00 35.53 ? 99  ASN A CA  1 
ATOM   213  C  C   . ASN A 1 99  ? 50.166 -8.134  29.939 1.00 31.47 ? 99  ASN A C   1 
ATOM   214  O  O   . ASN A 1 99  ? 51.136 -8.810  30.290 1.00 35.73 ? 99  ASN A O   1 
ATOM   215  C  CB  . ASN A 1 99  ? 49.675 -9.484  27.875 1.00 33.91 ? 99  ASN A CB  1 
ATOM   216  C  CG  . ASN A 1 99  ? 48.819 -10.662 27.413 1.00 41.48 ? 99  ASN A CG  1 
ATOM   217  O  OD1 . ASN A 1 99  ? 47.713 -10.871 27.928 1.00 34.28 ? 99  ASN A OD1 1 
ATOM   218  N  ND2 . ASN A 1 99  ? 49.321 -11.433 26.455 1.00 27.45 ? 99  ASN A ND2 1 
ATOM   219  N  N   . LEU A 1 100 ? 50.024 -6.854  30.289 1.00 29.98 ? 100 LEU A N   1 
ATOM   220  C  CA  . LEU A 1 100 ? 50.949 -6.183  31.196 1.00 27.82 ? 100 LEU A CA  1 
ATOM   221  C  C   . LEU A 1 100 ? 50.387 -6.181  32.609 1.00 32.36 ? 100 LEU A C   1 
ATOM   222  O  O   . LEU A 1 100 ? 49.190 -6.375  32.824 1.00 40.06 ? 100 LEU A O   1 
ATOM   223  C  CB  . LEU A 1 100 ? 51.202 -4.739  30.764 1.00 27.21 ? 100 LEU A CB  1 
ATOM   224  C  CG  . LEU A 1 100 ? 51.741 -4.485  29.365 1.00 32.72 ? 100 LEU A CG  1 
ATOM   225  C  CD1 . LEU A 1 100 ? 51.696 -2.993  29.108 1.00 32.44 ? 100 LEU A CD1 1 
ATOM   226  C  CD2 . LEU A 1 100 ? 53.156 -5.009  29.219 1.00 37.11 ? 100 LEU A CD2 1 
ATOM   227  N  N   . ASN A 1 101 ? 51.264 -5.930  33.576 1.00 36.18 ? 101 ASN A N   1 
ATOM   228  C  CA  . ASN A 1 101 ? 50.855 -5.796  34.975 1.00 37.92 ? 101 ASN A CA  1 
ATOM   229  C  C   . ASN A 1 101 ? 50.817 -4.305  35.301 1.00 39.16 ? 101 ASN A C   1 
ATOM   230  O  O   . ASN A 1 101 ? 51.797 -3.725  35.780 1.00 40.77 ? 101 ASN A O   1 
ATOM   231  C  CB  . ASN A 1 101 ? 51.797 -6.562  35.891 1.00 44.17 ? 101 ASN A CB  1 
ATOM   232  C  CG  . ASN A 1 101 ? 51.435 -6.413  37.347 1.00 43.78 ? 101 ASN A CG  1 
ATOM   233  O  OD1 . ASN A 1 101 ? 50.283 -6.134  37.691 1.00 51.07 ? 101 ASN A OD1 1 
ATOM   234  N  ND2 . ASN A 1 101 ? 52.422 -6.594  38.221 1.00 50.25 ? 101 ASN A ND2 1 
ATOM   235  N  N   . LEU A 1 102 ? 49.663 -3.685  35.042 1.00 31.23 ? 102 LEU A N   1 
ATOM   236  C  CA  . LEU A 1 102 ? 49.532 -2.233  35.089 1.00 29.96 ? 102 LEU A CA  1 
ATOM   237  C  C   . LEU A 1 102 ? 48.053 -1.874  35.107 1.00 24.99 ? 102 LEU A C   1 
ATOM   238  O  O   . LEU A 1 102 ? 47.303 -2.328  34.241 1.00 32.71 ? 102 LEU A O   1 
ATOM   239  C  CB  . LEU A 1 102 ? 50.225 -1.605  33.872 1.00 25.38 ? 102 LEU A CB  1 
ATOM   240  C  CG  . LEU A 1 102 ? 50.387 -0.090  33.817 1.00 25.30 ? 102 LEU A CG  1 
ATOM   241  C  CD1 . LEU A 1 102 ? 51.298 0.329   34.949 1.00 27.86 ? 102 LEU A CD1 1 
ATOM   242  C  CD2 . LEU A 1 102 ? 50.948 0.341   32.461 1.00 22.85 ? 102 LEU A CD2 1 
ATOM   243  N  N   . HIS A 1 103 ? 47.635 -1.085  36.098 1.00 22.27 ? 103 HIS A N   1 
ATOM   244  C  CA  . HIS A 1 103 ? 46.287 -0.536  36.149 1.00 27.71 ? 103 HIS A CA  1 
ATOM   245  C  C   . HIS A 1 103 ? 46.291 0.938   35.764 1.00 21.27 ? 103 HIS A C   1 
ATOM   246  O  O   . HIS A 1 103 ? 47.217 1.679   36.100 1.00 22.53 ? 103 HIS A O   1 
ATOM   247  C  CB  . HIS A 1 103 ? 45.689 -0.670  37.550 1.00 26.95 ? 103 HIS A CB  1 
ATOM   248  C  CG  . HIS A 1 103 ? 45.472 -2.083  37.983 1.00 32.23 ? 103 HIS A CG  1 
ATOM   249  N  ND1 . HIS A 1 103 ? 46.249 -2.695  38.942 1.00 43.71 ? 103 HIS A ND1 1 
ATOM   250  C  CD2 . HIS A 1 103 ? 44.555 -3.003  37.596 1.00 43.73 ? 103 HIS A CD2 1 
ATOM   251  C  CE1 . HIS A 1 103 ? 45.824 -3.933  39.124 1.00 40.50 ? 103 HIS A CE1 1 
ATOM   252  N  NE2 . HIS A 1 103 ? 44.798 -4.146  38.319 1.00 48.22 ? 103 HIS A NE2 1 
ATOM   253  N  N   . THR A 1 104 ? 45.224 1.378   35.104 1.00 18.63 ? 104 THR A N   1 
ATOM   254  C  CA  . THR A 1 104 ? 45.107 2.783   34.734 1.00 16.84 ? 104 THR A CA  1 
ATOM   255  C  C   . THR A 1 104 ? 43.892 3.408   35.391 1.00 16.62 ? 104 THR A C   1 
ATOM   256  O  O   . THR A 1 104 ? 42.868 2.747   35.612 1.00 16.86 ? 104 THR A O   1 
ATOM   257  C  CB  . THR A 1 104 ? 44.997 2.981   33.230 1.00 14.37 ? 104 THR A CB  1 
ATOM   258  O  OG1 . THR A 1 104 ? 43.761 2.404   32.773 1.00 17.35 ? 104 THR A OG1 1 
ATOM   259  C  CG2 . THR A 1 104 ? 46.178 2.348   32.506 1.00 19.88 ? 104 THR A CG2 1 
ATOM   260  N  N   . VAL A 1 105 ? 44.028 4.693   35.721 1.00 13.27 ? 105 VAL A N   1 
ATOM   261  C  CA  . VAL A 1 105 ? 42.879 5.475   36.164 1.00 13.11 ? 105 VAL A CA  1 
ATOM   262  C  C   . VAL A 1 105 ? 41.847 5.528   35.049 1.00 13.75 ? 105 VAL A C   1 
ATOM   263  O  O   . VAL A 1 105 ? 40.637 5.508   35.312 1.00 16.72 ? 105 VAL A O   1 
ATOM   264  C  CB  . VAL A 1 105 ? 43.319 6.900   36.585 1.00 14.35 ? 105 VAL A CB  1 
ATOM   265  C  CG1 . VAL A 1 105 ? 42.128 7.801   36.860 1.00 18.12 ? 105 VAL A CG1 1 
ATOM   266  C  CG2 . VAL A 1 105 ? 44.213 6.858   37.796 1.00 12.05 ? 105 VAL A CG2 1 
ATOM   267  N  N   . CYS A 1 106 ? 42.314 5.573   33.784 1.00 13.91 ? 106 CYS A N   1 
ATOM   268  C  CA  . CYS A 1 106 ? 41.427 5.634   32.626 1.00 12.67 ? 106 CYS A CA  1 
ATOM   269  C  C   . CYS A 1 106 ? 40.377 4.549   32.708 1.00 15.91 ? 106 CYS A C   1 
ATOM   270  O  O   . CYS A 1 106 ? 39.188 4.794   32.479 1.00 18.49 ? 106 CYS A O   1 
ATOM   271  C  CB  . CYS A 1 106 ? 42.236 5.463   31.339 1.00 10.57 ? 106 CYS A CB  1 
ATOM   272  S  SG  . CYS A 1 106 ? 43.758 6.484   31.318 1.00 11.67 ? 106 CYS A SG  1 
ATOM   273  N  N   . GLU A 1 107 ? 40.815 3.338   33.019 1.00 14.17 ? 107 GLU A N   1 
ATOM   274  C  CA  . GLU A 1 107 ? 39.885 2.215   33.109 1.00 18.37 ? 107 GLU A CA  1 
ATOM   275  C  C   . GLU A 1 107 ? 39.190 2.157   34.457 1.00 22.79 ? 107 GLU A C   1 
ATOM   276  O  O   . GLU A 1 107 ? 37.979 1.913   34.527 1.00 21.45 ? 107 GLU A O   1 
ATOM   277  C  CB  . GLU A 1 107 ? 40.628 0.913   32.861 1.00 19.03 ? 107 GLU A CB  1 
ATOM   278  C  CG  . GLU A 1 107 ? 41.273 0.831   31.512 1.00 25.02 ? 107 GLU A CG  1 
ATOM   279  C  CD  . GLU A 1 107 ? 42.237 -0.326  31.429 1.00 37.29 ? 107 GLU A CD  1 
ATOM   280  O  OE1 . GLU A 1 107 ? 43.180 -0.386  32.269 1.00 37.76 ? 107 GLU A OE1 1 
ATOM   281  O  OE2 . GLU A 1 107 ? 42.032 -1.174  30.533 1.00 33.88 ? 107 GLU A OE2 1 
ATOM   282  N  N   . GLU A 1 108 ? 39.937 2.351   35.537 1.00 22.10 ? 108 GLU A N   1 
ATOM   283  C  CA  . GLU A 1 108 ? 39.360 2.175   36.863 1.00 27.33 ? 108 GLU A CA  1 
ATOM   284  C  C   . GLU A 1 108 ? 38.257 3.187   37.127 1.00 28.89 ? 108 GLU A C   1 
ATOM   285  O  O   . GLU A 1 108 ? 37.215 2.846   37.708 1.00 25.60 ? 108 GLU A O   1 
ATOM   286  C  CB  . GLU A 1 108 ? 40.468 2.262   37.912 1.00 27.52 ? 108 GLU A CB  1 
ATOM   287  C  CG  . GLU A 1 108 ? 41.367 1.036   37.872 1.00 31.71 ? 108 GLU A CG  1 
ATOM   288  C  CD  . GLU A 1 108 ? 40.571 -0.261  37.929 1.00 44.08 ? 108 GLU A CD  1 
ATOM   289  O  OE1 . GLU A 1 108 ? 39.685 -0.381  38.812 1.00 44.27 ? 108 GLU A OE1 1 
ATOM   290  O  OE2 . GLU A 1 108 ? 40.818 -1.148  37.079 1.00 46.57 ? 108 GLU A OE2 1 
ATOM   291  N  N   . ALA A 1 109 ? 38.450 4.428   36.679 1.00 19.20 ? 109 ALA A N   1 
ATOM   292  C  CA  . ALA A 1 109 ? 37.464 5.488   36.821 1.00 19.48 ? 109 ALA A CA  1 
ATOM   293  C  C   . ALA A 1 109 ? 36.402 5.463   35.725 1.00 20.70 ? 109 ALA A C   1 
ATOM   294  O  O   . ALA A 1 109 ? 35.543 6.360   35.703 1.00 28.24 ? 109 ALA A O   1 
ATOM   295  C  CB  . ALA A 1 109 ? 38.162 6.857   36.833 1.00 28.00 ? 109 ALA A CB  1 
ATOM   296  N  N   . ARG A 1 110 ? 36.450 4.487   34.820 1.00 19.43 ? 110 ARG A N   1 
ATOM   297  C  CA  . ARG A 1 110 ? 35.508 4.405   33.712 1.00 19.33 ? 110 ARG A CA  1 
ATOM   298  C  C   . ARG A 1 110 ? 35.459 5.741   32.977 1.00 24.40 ? 110 ARG A C   1 
ATOM   299  O  O   . ARG A 1 110 ? 34.400 6.344   32.793 1.00 20.76 ? 110 ARG A O   1 
ATOM   300  C  CB  . ARG A 1 110 ? 34.105 4.007   34.206 1.00 21.63 ? 110 ARG A CB  1 
ATOM   301  C  CG  . ARG A 1 110 ? 34.071 2.865   35.214 1.00 27.27 ? 110 ARG A CG  1 
ATOM   302  C  CD  . ARG A 1 110 ? 32.723 2.861   35.979 1.00 29.50 ? 110 ARG A CD  1 
ATOM   303  N  NE  . ARG A 1 110 ? 32.652 1.781   36.959 1.00 34.14 ? 110 ARG A NE  1 
ATOM   304  C  CZ  . ARG A 1 110 ? 32.352 0.525   36.657 1.00 33.56 ? 110 ARG A CZ  1 
ATOM   305  N  NH1 . ARG A 1 110 ? 32.302 -0.418  37.585 1.00 33.14 ? 110 ARG A NH1 1 
ATOM   306  N  NH2 . ARG A 1 110 ? 32.096 0.209   35.391 1.00 36.41 ? 110 ARG A NH2 1 
ATOM   307  N  N   . CYS A 1 111 ? 36.637 6.244   32.596 1.00 17.51 ? 111 CYS A N   1 
ATOM   308  C  CA  . CYS A 1 111 ? 36.672 7.605   32.093 1.00 15.04 ? 111 CYS A CA  1 
ATOM   309  C  C   . CYS A 1 111 ? 36.049 7.666   30.703 1.00 14.55 ? 111 CYS A C   1 
ATOM   310  O  O   . CYS A 1 111 ? 36.355 6.840   29.840 1.00 17.32 ? 111 CYS A O   1 
ATOM   311  C  CB  . CYS A 1 111 ? 38.108 8.128   32.036 1.00 14.70 ? 111 CYS A CB  1 
ATOM   312  S  SG  . CYS A 1 111 ? 38.220 9.870   31.514 1.00 13.09 ? 111 CYS A SG  1 
ATOM   313  N  N   . PRO A 1 112 ? 35.208 8.664   30.437 1.00 15.27 ? 112 PRO A N   1 
ATOM   314  C  CA  . PRO A 1 112 ? 34.591 8.754   29.110 1.00 16.78 ? 112 PRO A CA  1 
ATOM   315  C  C   . PRO A 1 112 ? 35.555 9.174   28.032 1.00 15.65 ? 112 PRO A C   1 
ATOM   316  O  O   . PRO A 1 112 ? 35.185 9.118   26.857 1.00 16.54 ? 112 PRO A O   1 
ATOM   317  C  CB  . PRO A 1 112 ? 33.484 9.802   29.293 1.00 18.37 ? 112 PRO A CB  1 
ATOM   318  C  CG  . PRO A 1 112 ? 33.844 10.545  30.535 1.00 25.18 ? 112 PRO A CG  1 
ATOM   319  C  CD  . PRO A 1 112 ? 34.714 9.674   31.379 1.00 14.34 ? 112 PRO A CD  1 
ATOM   320  N  N   . ASN A 1 113 ? 36.784 9.589   28.381 1.00 12.70 ? 113 ASN A N   1 
ATOM   321  C  CA  . ASN A 1 113 ? 37.682 10.133  27.373 1.00 13.59 ? 113 ASN A CA  1 
ATOM   322  C  C   . ASN A 1 113 ? 38.640 9.108   26.779 1.00 12.83 ? 113 ASN A C   1 
ATOM   323  O  O   . ASN A 1 113 ? 39.451 9.478   25.933 1.00 11.23 ? 113 ASN A O   1 
ATOM   324  C  CB  . ASN A 1 113 ? 38.489 11.293  27.967 1.00 12.22 ? 113 ASN A CB  1 
ATOM   325  C  CG  . ASN A 1 113 ? 37.593 12.415  28.469 1.00 13.02 ? 113 ASN A CG  1 
ATOM   326  O  OD1 . ASN A 1 113 ? 36.637 12.756  27.801 1.00 14.27 ? 113 ASN A OD1 1 
ATOM   327  N  ND2 . ASN A 1 113 ? 37.916 12.996  29.632 1.00 11.63 ? 113 ASN A ND2 1 
ATOM   328  N  N   . ILE A 1 114 ? 38.528 7.830   27.146 1.00 12.59 ? 114 ILE A N   1 
ATOM   329  C  CA  . ILE A 1 114 ? 39.610 6.891   26.837 1.00 13.64 ? 114 ILE A CA  1 
ATOM   330  C  C   . ILE A 1 114 ? 39.834 6.752   25.334 1.00 15.13 ? 114 ILE A C   1 
ATOM   331  O  O   . ILE A 1 114 ? 40.979 6.661   24.875 1.00 15.55 ? 114 ILE A O   1 
ATOM   332  C  CB  . ILE A 1 114 ? 39.342 5.551   27.534 1.00 13.40 ? 114 ILE A CB  1 
ATOM   333  C  CG1 . ILE A 1 114 ? 40.562 4.642   27.466 1.00 17.26 ? 114 ILE A CG1 1 
ATOM   334  C  CG2 . ILE A 1 114 ? 38.135 4.860   26.920 1.00 16.14 ? 114 ILE A CG2 1 
ATOM   335  C  CD1 . ILE A 1 114 ? 40.514 3.529   28.481 1.00 21.64 ? 114 ILE A CD1 1 
ATOM   336  N  N   . GLY A 1 115 ? 38.763 6.773   24.537 1.00 14.20 ? 115 GLY A N   1 
ATOM   337  C  CA  . GLY A 1 115 ? 38.929 6.640   23.101 1.00 19.00 ? 115 GLY A CA  1 
ATOM   338  C  C   . GLY A 1 115 ? 39.682 7.796   22.484 1.00 19.98 ? 115 GLY A C   1 
ATOM   339  O  O   . GLY A 1 115 ? 40.339 7.640   21.445 1.00 24.04 ? 115 GLY A O   1 
ATOM   340  N  N   . GLU A 1 116 ? 39.601 8.963   23.107 1.00 14.31 ? 116 GLU A N   1 
ATOM   341  C  CA  . GLU A 1 116 ? 40.318 10.131  22.623 1.00 16.39 ? 116 GLU A CA  1 
ATOM   342  C  C   . GLU A 1 116 ? 41.756 10.139  23.145 1.00 14.17 ? 116 GLU A C   1 
ATOM   343  O  O   . GLU A 1 116 ? 42.706 10.359  22.381 1.00 15.06 ? 116 GLU A O   1 
ATOM   344  C  CB  . GLU A 1 116 ? 39.569 11.393  23.059 1.00 19.49 ? 116 GLU A CB  1 
ATOM   345  C  CG  . GLU A 1 116 ? 40.017 12.653  22.391 1.00 30.77 ? 116 GLU A CG  1 
ATOM   346  C  CD  . GLU A 1 116 ? 39.510 12.780  20.958 1.00 29.45 ? 116 GLU A CD  1 
ATOM   347  O  OE1 . GLU A 1 116 ? 38.440 12.208  20.651 1.00 42.35 ? 116 GLU A OE1 1 
ATOM   348  O  OE2 . GLU A 1 116 ? 40.191 13.447  20.147 1.00 39.03 ? 116 GLU A OE2 1 
ATOM   349  N  N   . CYS A 1 117 ? 41.938 9.888   24.436 1.00 11.51 ? 117 CYS A N   1 
ATOM   350  C  CA  . CYS A 1 117 ? 43.303 9.935   24.989 1.00 11.76 ? 117 CYS A CA  1 
ATOM   351  C  C   . CYS A 1 117 ? 44.193 8.818   24.454 1.00 12.76 ? 117 CYS A C   1 
ATOM   352  O  O   . CYS A 1 117 ? 45.391 9.020   24.256 1.00 11.84 ? 117 CYS A O   1 
ATOM   353  C  CB  . CYS A 1 117 ? 43.268 9.868   26.507 1.00 11.04 ? 117 CYS A CB  1 
ATOM   354  S  SG  . CYS A 1 117 ? 42.430 11.339  27.207 1.00 11.28 ? 117 CYS A SG  1 
ATOM   355  N  N   . TRP A 1 118 ? 43.656 7.612   24.297 1.00 12.24 ? 118 TRP A N   1 
ATOM   356  C  CA  . TRP A 1 118 ? 44.452 6.477   23.823 1.00 12.44 ? 118 TRP A CA  1 
ATOM   357  C  C   . TRP A 1 118 ? 44.488 6.446   22.287 1.00 13.30 ? 118 TRP A C   1 
ATOM   358  O  O   . TRP A 1 118 ? 43.902 5.582   21.628 1.00 19.10 ? 118 TRP A O   1 
ATOM   359  C  CB  . TRP A 1 118 ? 43.888 5.182   24.401 1.00 13.26 ? 118 TRP A CB  1 
ATOM   360  C  CG  . TRP A 1 118 ? 43.992 5.043   25.870 1.00 11.67 ? 118 TRP A CG  1 
ATOM   361  C  CD1 . TRP A 1 118 ? 44.193 6.040   26.812 1.00 11.48 ? 118 TRP A CD1 1 
ATOM   362  C  CD2 . TRP A 1 118 ? 43.869 3.835   26.603 1.00 13.69 ? 118 TRP A CD2 1 
ATOM   363  N  NE1 . TRP A 1 118 ? 44.220 5.498   28.073 1.00 13.84 ? 118 TRP A NE1 1 
ATOM   364  C  CE2 . TRP A 1 118 ? 44.023 4.142   27.971 1.00 14.01 ? 118 TRP A CE2 1 
ATOM   365  C  CE3 . TRP A 1 118 ? 43.654 2.506   26.234 1.00 17.40 ? 118 TRP A CE3 1 
ATOM   366  C  CZ2 . TRP A 1 118 ? 43.961 3.163   28.968 1.00 14.86 ? 118 TRP A CZ2 1 
ATOM   367  C  CZ3 . TRP A 1 118 ? 43.589 1.551   27.208 1.00 17.17 ? 118 TRP A CZ3 1 
ATOM   368  C  CH2 . TRP A 1 118 ? 43.737 1.873   28.564 1.00 15.72 ? 118 TRP A CH2 1 
ATOM   369  N  N   . GLY A 1 119 ? 45.186 7.432   21.710 1.00 13.06 ? 119 GLY A N   1 
ATOM   370  C  CA  . GLY A 1 119 ? 45.471 7.422   20.292 1.00 14.96 ? 119 GLY A CA  1 
ATOM   371  C  C   . GLY A 1 119 ? 44.419 8.030   19.406 1.00 16.93 ? 119 GLY A C   1 
ATOM   372  O  O   . GLY A 1 119 ? 44.550 7.945   18.180 1.00 19.40 ? 119 GLY A O   1 
ATOM   373  N  N   . GLY A 1 120 ? 43.415 8.696   19.971 1.00 17.22 ? 120 GLY A N   1 
ATOM   374  C  CA  . GLY A 1 120 ? 42.345 9.193   19.141 1.00 19.16 ? 120 GLY A CA  1 
ATOM   375  C  C   . GLY A 1 120 ? 42.507 10.597  18.605 1.00 19.21 ? 120 GLY A C   1 
ATOM   376  O  O   . GLY A 1 120 ? 41.663 11.045  17.814 1.00 26.04 ? 120 GLY A O   1 
ATOM   377  N  N   . GLY A 1 121 ? 43.558 11.316  18.991 1.00 18.64 ? 121 GLY A N   1 
ATOM   378  C  CA  . GLY A 1 121 ? 43.699 12.718  18.640 1.00 25.66 ? 121 GLY A CA  1 
ATOM   379  C  C   . GLY A 1 121 ? 44.487 12.945  17.353 1.00 23.97 ? 121 GLY A C   1 
ATOM   380  O  O   . GLY A 1 121 ? 44.894 12.014  16.657 1.00 21.17 ? 121 GLY A O   1 
ATOM   381  N  N   . GLU A 1 122 ? 44.734 14.234  17.076 1.00 20.39 ? 122 GLU A N   1 
ATOM   382  C  CA  . GLU A 1 122 ? 45.344 14.678  15.823 1.00 24.23 ? 122 GLU A CA  1 
ATOM   383  C  C   . GLU A 1 122 ? 46.752 14.122  15.628 1.00 26.30 ? 122 GLU A C   1 
ATOM   384  O  O   . GLU A 1 122 ? 47.151 13.808  14.502 1.00 26.12 ? 122 GLU A O   1 
ATOM   385  C  CB  . GLU A 1 122 ? 45.352 16.207  15.804 1.00 33.54 ? 122 GLU A CB  1 
ATOM   386  C  CG  . GLU A 1 122 ? 46.316 16.875  14.843 1.00 37.77 ? 122 GLU A CG  1 
ATOM   387  C  CD  . GLU A 1 122 ? 46.290 18.395  14.994 1.00 44.82 ? 122 GLU A CD  1 
ATOM   388  O  OE1 . GLU A 1 122 ? 46.009 18.875  16.121 1.00 42.85 ? 122 GLU A OE1 1 
ATOM   389  O  OE2 . GLU A 1 122 ? 46.529 19.107  13.988 1.00 48.56 ? 122 GLU A OE2 1 
ATOM   390  N  N   . TYR A 1 123 ? 47.530 14.013  16.698 1.00 23.61 ? 123 TYR A N   1 
ATOM   391  C  CA  . TYR A 1 123 ? 48.861 13.429  16.619 1.00 22.38 ? 123 TYR A CA  1 
ATOM   392  C  C   . TYR A 1 123 ? 48.882 11.944  16.923 1.00 24.28 ? 123 TYR A C   1 
ATOM   393  O  O   . TYR A 1 123 ? 49.969 11.346  16.965 1.00 24.19 ? 123 TYR A O   1 
ATOM   394  C  CB  . TYR A 1 123 ? 49.808 14.121  17.587 1.00 23.18 ? 123 TYR A CB  1 
ATOM   395  C  CG  . TYR A 1 123 ? 50.118 15.543  17.262 1.00 23.92 ? 123 TYR A CG  1 
ATOM   396  C  CD1 . TYR A 1 123 ? 51.121 15.867  16.359 1.00 25.23 ? 123 TYR A CD1 1 
ATOM   397  C  CD2 . TYR A 1 123 ? 49.423 16.573  17.873 1.00 23.79 ? 123 TYR A CD2 1 
ATOM   398  C  CE1 . TYR A 1 123 ? 51.408 17.184  16.080 1.00 24.18 ? 123 TYR A CE1 1 
ATOM   399  C  CE2 . TYR A 1 123 ? 49.705 17.882  17.593 1.00 28.17 ? 123 TYR A CE2 1 
ATOM   400  C  CZ  . TYR A 1 123 ? 50.691 18.179  16.689 1.00 20.09 ? 123 TYR A CZ  1 
ATOM   401  O  OH  . TYR A 1 123 ? 50.975 19.504  16.435 1.00 30.11 ? 123 TYR A OH  1 
ATOM   402  N  N   . ALA A 1 124 ? 47.718 11.350  17.197 1.00 20.71 ? 124 ALA A N   1 
ATOM   403  C  CA  . ALA A 1 124 ? 47.616 9.938   17.530 1.00 22.70 ? 124 ALA A CA  1 
ATOM   404  C  C   . ALA A 1 124 ? 48.456 9.571   18.753 1.00 19.66 ? 124 ALA A C   1 
ATOM   405  O  O   . ALA A 1 124 ? 48.905 8.432   18.872 1.00 21.49 ? 124 ALA A O   1 
ATOM   406  C  CB  . ALA A 1 124 ? 48.004 9.067   16.331 1.00 22.02 ? 124 ALA A CB  1 
ATOM   407  N  N   . THR A 1 125 ? 48.664 10.517  19.677 1.00 17.36 ? 125 THR A N   1 
ATOM   408  C  CA  . THR A 1 125 ? 49.424 10.198  20.877 1.00 16.53 ? 125 THR A CA  1 
ATOM   409  C  C   . THR A 1 125 ? 48.595 9.357   21.820 1.00 15.89 ? 125 THR A C   1 
ATOM   410  O  O   . THR A 1 125 ? 47.357 9.411   21.816 1.00 16.35 ? 125 THR A O   1 
ATOM   411  C  CB  . THR A 1 125 ? 49.900 11.448  21.623 1.00 21.78 ? 125 THR A CB  1 
ATOM   412  O  OG1 . THR A 1 125 ? 48.787 12.145  22.184 1.00 23.41 ? 125 THR A OG1 1 
ATOM   413  C  CG2 . THR A 1 125 ? 50.650 12.361  20.709 1.00 26.85 ? 125 THR A CG2 1 
ATOM   414  N  N   . ALA A 1 126 ? 49.296 8.559   22.622 1.00 15.36 ? 126 ALA A N   1 
ATOM   415  C  CA  . ALA A 1 126 ? 48.683 7.791   23.696 1.00 14.01 ? 126 ALA A CA  1 
ATOM   416  C  C   . ALA A 1 126 ? 49.047 8.450   25.024 1.00 14.28 ? 126 ALA A C   1 
ATOM   417  O  O   . ALA A 1 126 ? 50.229 8.504   25.388 1.00 12.42 ? 126 ALA A O   1 
ATOM   418  C  CB  . ALA A 1 126 ? 49.147 6.337   23.663 1.00 14.56 ? 126 ALA A CB  1 
ATOM   419  N  N   . THR A 1 127 ? 48.026 8.962   25.718 1.00 13.11 ? 127 THR A N   1 
ATOM   420  C  CA  . THR A 1 127 ? 48.119 9.497   27.073 1.00 11.03 ? 127 THR A CA  1 
ATOM   421  C  C   . THR A 1 127 ? 47.342 8.589   28.015 1.00 9.45  ? 127 THR A C   1 
ATOM   422  O  O   . THR A 1 127 ? 46.218 8.187   27.713 1.00 10.88 ? 127 THR A O   1 
ATOM   423  C  CB  . THR A 1 127 ? 47.524 10.911  27.154 1.00 10.77 ? 127 THR A CB  1 
ATOM   424  O  OG1 . THR A 1 127 ? 48.211 11.770  26.237 1.00 11.25 ? 127 THR A OG1 1 
ATOM   425  C  CG2 . THR A 1 127 ? 47.661 11.491  28.573 1.00 10.52 ? 127 THR A CG2 1 
ATOM   426  N  N   . ALA A 1 128 ? 47.901 8.309   29.187 1.00 10.58 ? 128 ALA A N   1 
ATOM   427  C  CA  . ALA A 1 128 ? 47.152 7.581   30.205 1.00 11.12 ? 128 ALA A CA  1 
ATOM   428  C  C   . ALA A 1 128 ? 47.607 8.069   31.575 1.00 11.65 ? 128 ALA A C   1 
ATOM   429  O  O   . ALA A 1 128 ? 48.681 8.670   31.720 1.00 10.60 ? 128 ALA A O   1 
ATOM   430  C  CB  . ALA A 1 128 ? 47.350 6.055   30.061 1.00 13.90 ? 128 ALA A CB  1 
ATOM   431  N  N   . THR A 1 129 ? 46.777 7.810   32.585 1.00 9.73  ? 129 THR A N   1 
ATOM   432  C  CA  . THR A 1 129 ? 47.020 8.213   33.949 1.00 8.94  ? 129 THR A CA  1 
ATOM   433  C  C   . THR A 1 129 ? 47.156 6.974   34.811 1.00 11.30 ? 129 THR A C   1 
ATOM   434  O  O   . THR A 1 129 ? 46.302 6.082   34.748 1.00 12.92 ? 129 THR A O   1 
ATOM   435  C  CB  . THR A 1 129 ? 45.884 9.095   34.458 1.00 11.17 ? 129 THR A CB  1 
ATOM   436  O  OG1 . THR A 1 129 ? 45.857 10.284  33.652 1.00 11.71 ? 129 THR A OG1 1 
ATOM   437  C  CG2 . THR A 1 129 ? 46.104 9.464   35.896 1.00 12.88 ? 129 THR A CG2 1 
ATOM   438  N  N   . ILE A 1 130 ? 48.235 6.921   35.593 1.00 10.55 ? 130 ILE A N   1 
ATOM   439  C  CA  . ILE A 1 130 ? 48.558 5.779   36.445 1.00 11.08 ? 130 ILE A CA  1 
ATOM   440  C  C   . ILE A 1 130 ? 48.764 6.280   37.869 1.00 12.08 ? 130 ILE A C   1 
ATOM   441  O  O   . ILE A 1 130 ? 49.535 7.214   38.092 1.00 11.81 ? 130 ILE A O   1 
ATOM   442  C  CB  . ILE A 1 130 ? 49.808 5.038   35.936 1.00 11.76 ? 130 ILE A CB  1 
ATOM   443  C  CG1 . ILE A 1 130 ? 49.477 4.384   34.579 1.00 23.77 ? 130 ILE A CG1 1 
ATOM   444  C  CG2 . ILE A 1 130 ? 50.259 3.980   36.963 1.00 13.77 ? 130 ILE A CG2 1 
ATOM   445  C  CD1 . ILE A 1 130 ? 50.666 3.950   33.827 1.00 27.27 ? 130 ILE A CD1 1 
ATOM   446  N  N   . MET A 1 131 ? 48.068 5.675   38.836 1.00 13.09 ? 131 MET A N   1 
ATOM   447  C  CA  A MET A 1 131 ? 48.184 6.096   40.224 0.52 11.01 ? 131 MET A CA  1 
ATOM   448  C  CA  B MET A 1 131 ? 48.178 6.091   40.232 0.48 11.04 ? 131 MET A CA  1 
ATOM   449  C  C   . MET A 1 131 ? 49.295 5.312   40.911 1.00 15.91 ? 131 MET A C   1 
ATOM   450  O  O   . MET A 1 131 ? 49.326 4.083   40.843 1.00 19.78 ? 131 MET A O   1 
ATOM   451  C  CB  A MET A 1 131 ? 46.860 5.893   40.965 0.52 14.85 ? 131 MET A CB  1 
ATOM   452  C  CB  B MET A 1 131 ? 46.866 5.861   40.993 0.48 14.84 ? 131 MET A CB  1 
ATOM   453  C  CG  A MET A 1 131 ? 46.817 6.604   42.294 0.52 11.90 ? 131 MET A CG  1 
ATOM   454  C  CG  B MET A 1 131 ? 45.808 6.955   40.826 0.48 9.71  ? 131 MET A CG  1 
ATOM   455  S  SD  A MET A 1 131 ? 45.188 6.634   43.045 0.52 26.95 ? 131 MET A SD  1 
ATOM   456  S  SD  B MET A 1 131 ? 44.320 6.509   41.730 0.48 31.90 ? 131 MET A SD  1 
ATOM   457  C  CE  A MET A 1 131 ? 44.558 8.176   42.384 0.52 17.77 ? 131 MET A CE  1 
ATOM   458  C  CE  B MET A 1 131 ? 44.849 6.915   43.382 0.48 24.66 ? 131 MET A CE  1 
ATOM   459  N  N   . LEU A 1 132 ? 50.196 6.023   41.565 1.00 12.39 ? 132 LEU A N   1 
ATOM   460  C  CA  . LEU A 1 132 ? 51.271 5.399   42.333 1.00 14.50 ? 132 LEU A CA  1 
ATOM   461  C  C   . LEU A 1 132 ? 50.854 5.341   43.798 1.00 16.24 ? 132 LEU A C   1 
ATOM   462  O  O   . LEU A 1 132 ? 50.103 6.197   44.273 1.00 17.66 ? 132 LEU A O   1 
ATOM   463  C  CB  . LEU A 1 132 ? 52.575 6.189   42.189 1.00 15.57 ? 132 LEU A CB  1 
ATOM   464  C  CG  . LEU A 1 132 ? 53.103 6.323   40.772 1.00 12.49 ? 132 LEU A CG  1 
ATOM   465  C  CD1 . LEU A 1 132 ? 54.338 7.254   40.789 1.00 15.34 ? 132 LEU A CD1 1 
ATOM   466  C  CD2 . LEU A 1 132 ? 53.425 4.966   40.133 1.00 19.23 ? 132 LEU A CD2 1 
ATOM   467  N  N   . MET A 1 133 ? 51.345 4.322   44.518 1.00 14.48 ? 133 MET A N   1 
ATOM   468  C  CA  . MET A 1 133 ? 51.139 4.201   45.967 1.00 17.43 ? 133 MET A CA  1 
ATOM   469  C  C   . MET A 1 133 ? 49.671 3.998   46.327 1.00 28.54 ? 133 MET A C   1 
ATOM   470  O  O   . MET A 1 133 ? 49.199 4.523   47.346 1.00 20.36 ? 133 MET A O   1 
ATOM   471  C  CB  . MET A 1 133 ? 51.701 5.411   46.721 1.00 21.00 ? 133 MET A CB  1 
ATOM   472  C  CG  . MET A 1 133 ? 53.140 5.682   46.394 1.00 20.99 ? 133 MET A CG  1 
ATOM   473  S  SD  . MET A 1 133 ? 53.917 7.050   47.261 1.00 22.02 ? 133 MET A SD  1 
ATOM   474  C  CE  . MET A 1 133 ? 53.009 8.446   46.540 1.00 22.82 ? 133 MET A CE  1 
ATOM   475  N  N   . GLY A 1 134 ? 48.939 3.271   45.496 1.00 18.87 ? 134 GLY A N   1 
ATOM   476  C  CA  . GLY A 1 134 ? 47.605 2.828   45.856 1.00 21.55 ? 134 GLY A CA  1 
ATOM   477  C  C   . GLY A 1 134 ? 46.529 3.597   45.117 1.00 26.98 ? 134 GLY A C   1 
ATOM   478  O  O   . GLY A 1 134 ? 46.687 4.780   44.788 1.00 30.14 ? 134 GLY A O   1 
ATOM   479  N  N   . ASP A 1 135 ? 45.401 2.924   44.870 1.00 21.54 ? 135 ASP A N   1 
ATOM   480  C  CA  . ASP A 1 135 ? 44.299 3.522   44.129 1.00 19.18 ? 135 ASP A CA  1 
ATOM   481  C  C   . ASP A 1 135 ? 43.157 3.980   45.044 1.00 15.90 ? 135 ASP A C   1 
ATOM   482  O  O   . ASP A 1 135 ? 42.034 4.199   44.575 1.00 23.03 ? 135 ASP A O   1 
ATOM   483  C  CB  . ASP A 1 135 ? 43.789 2.562   43.048 1.00 29.30 ? 135 ASP A CB  1 
ATOM   484  C  CG  . ASP A 1 135 ? 43.056 1.352   43.604 1.00 32.93 ? 135 ASP A CG  1 
ATOM   485  O  OD1 . ASP A 1 135 ? 43.204 1.018   44.804 1.00 39.82 ? 135 ASP A OD1 1 
ATOM   486  O  OD2 . ASP A 1 135 ? 42.319 0.709   42.819 1.00 39.74 ? 135 ASP A OD2 1 
ATOM   487  N  N   . THR A 1 136 ? 43.415 4.110   46.333 1.00 13.43 ? 136 THR A N   1 
ATOM   488  C  CA  . THR A 1 136 ? 42.430 4.658   47.257 1.00 14.19 ? 136 THR A CA  1 
ATOM   489  C  C   . THR A 1 136 ? 43.048 5.815   48.027 1.00 14.64 ? 136 THR A C   1 
ATOM   490  O  O   . THR A 1 136 ? 44.275 5.991   48.052 1.00 16.35 ? 136 THR A O   1 
ATOM   491  C  CB  . THR A 1 136 ? 41.921 3.604   48.253 1.00 16.08 ? 136 THR A CB  1 
ATOM   492  O  OG1 . THR A 1 136 ? 43.029 3.086   48.993 1.00 18.24 ? 136 THR A OG1 1 
ATOM   493  C  CG2 . THR A 1 136 ? 41.203 2.475   47.537 1.00 20.21 ? 136 THR A CG2 1 
ATOM   494  N  N   . CYS A 1 137 ? 42.191 6.601   48.682 1.00 12.58 ? 137 CYS A N   1 
ATOM   495  C  CA  . CYS A 1 137 ? 42.649 7.679   49.556 1.00 11.91 ? 137 CYS A CA  1 
ATOM   496  C  C   . CYS A 1 137 ? 41.839 7.649   50.840 1.00 13.64 ? 137 CYS A C   1 
ATOM   497  O  O   . CYS A 1 137 ? 40.653 7.340   50.813 1.00 13.34 ? 137 CYS A O   1 
ATOM   498  C  CB  . CYS A 1 137 ? 42.490 9.071   48.915 1.00 12.61 ? 137 CYS A CB  1 
ATOM   499  S  SG  . CYS A 1 137 ? 43.250 10.375  49.899 1.00 11.89 ? 137 CYS A SG  1 
ATOM   500  N  N   . THR A 1 138 ? 42.467 8.034   51.952 1.00 12.91 ? 138 THR A N   1 
ATOM   501  C  CA  . THR A 1 138 ? 41.730 8.063   53.204 1.00 13.59 ? 138 THR A CA  1 
ATOM   502  C  C   . THR A 1 138 ? 41.000 9.367   53.489 1.00 13.35 ? 138 THR A C   1 
ATOM   503  O  O   . THR A 1 138 ? 40.215 9.397   54.443 1.00 13.99 ? 138 THR A O   1 
ATOM   504  C  CB  . THR A 1 138 ? 42.680 7.803   54.388 1.00 15.89 ? 138 THR A CB  1 
ATOM   505  O  OG1 . THR A 1 138 ? 43.593 8.903   54.510 1.00 16.80 ? 138 THR A OG1 1 
ATOM   506  C  CG2 . THR A 1 138 ? 43.409 6.504   54.196 1.00 19.24 ? 138 THR A CG2 1 
ATOM   507  N  N   . ARG A 1 139 ? 41.204 10.454  52.709 1.00 12.60 ? 139 ARG A N   1 
ATOM   508  C  CA  A ARG A 1 139 ? 40.739 11.769  53.150 0.37 13.13 ? 139 ARG A CA  1 
ATOM   509  C  CA  B ARG A 1 139 ? 40.733 11.751  53.191 0.63 13.18 ? 139 ARG A CA  1 
ATOM   510  C  C   . ARG A 1 139 ? 39.253 12.001  52.922 1.00 16.53 ? 139 ARG A C   1 
ATOM   511  O  O   . ARG A 1 139 ? 38.653 12.822  53.625 1.00 14.33 ? 139 ARG A O   1 
ATOM   512  C  CB  A ARG A 1 139 ? 41.531 12.873  52.450 0.37 13.22 ? 139 ARG A CB  1 
ATOM   513  C  CB  B ARG A 1 139 ? 41.557 12.896  52.586 0.63 12.79 ? 139 ARG A CB  1 
ATOM   514  C  CG  A ARG A 1 139 ? 42.962 12.880  52.827 0.37 18.30 ? 139 ARG A CG  1 
ATOM   515  C  CG  B ARG A 1 139 ? 43.045 12.766  52.749 0.63 18.45 ? 139 ARG A CG  1 
ATOM   516  C  CD  A ARG A 1 139 ? 43.059 12.513  54.283 0.37 23.10 ? 139 ARG A CD  1 
ATOM   517  C  CD  B ARG A 1 139 ? 43.450 12.546  54.199 0.63 25.74 ? 139 ARG A CD  1 
ATOM   518  N  NE  A ARG A 1 139 ? 44.109 13.252  54.954 0.37 33.00 ? 139 ARG A NE  1 
ATOM   519  N  NE  B ARG A 1 139 ? 44.803 13.035  54.446 0.63 24.19 ? 139 ARG A NE  1 
ATOM   520  C  CZ  A ARG A 1 139 ? 45.375 12.872  55.000 0.37 26.74 ? 139 ARG A CZ  1 
ATOM   521  C  CZ  B ARG A 1 139 ? 45.293 13.329  55.644 0.63 29.19 ? 139 ARG A CZ  1 
ATOM   522  N  NH1 A ARG A 1 139 ? 46.267 13.555  55.691 0.37 35.59 ? 139 ARG A NH1 1 
ATOM   523  N  NH1 B ARG A 1 139 ? 46.406 14.037  55.780 0.63 34.82 ? 139 ARG A NH1 1 
ATOM   524  N  NH2 A ARG A 1 139 ? 45.751 11.778  54.339 0.37 28.56 ? 139 ARG A NH2 1 
ATOM   525  N  NH2 B ARG A 1 139 ? 44.647 12.913  56.731 0.63 27.95 ? 139 ARG A NH2 1 
ATOM   526  N  N   . GLY A 1 140 ? 38.658 11.353  51.918 1.00 13.49 ? 140 GLY A N   1 
ATOM   527  C  CA  . GLY A 1 140 ? 37.214 11.534  51.708 1.00 14.53 ? 140 GLY A CA  1 
ATOM   528  C  C   . GLY A 1 140 ? 36.756 12.940  51.355 1.00 12.50 ? 140 GLY A C   1 
ATOM   529  O  O   . GLY A 1 140 ? 35.673 13.370  51.784 1.00 13.18 ? 140 GLY A O   1 
ATOM   530  N  N   . CYS A 1 141 ? 37.550 13.667  50.571 1.00 11.10 ? 141 CYS A N   1 
ATOM   531  C  CA  . CYS A 1 141 ? 37.199 15.048  50.226 1.00 10.76 ? 141 CYS A CA  1 
ATOM   532  C  C   . CYS A 1 141 ? 35.854 15.113  49.514 1.00 12.53 ? 141 CYS A C   1 
ATOM   533  O  O   . CYS A 1 141 ? 35.458 14.193  48.793 1.00 12.21 ? 141 CYS A O   1 
ATOM   534  C  CB  . CYS A 1 141 ? 38.259 15.681  49.324 1.00 10.17 ? 141 CYS A CB  1 
ATOM   535  S  SG  . CYS A 1 141 ? 39.844 15.902  50.185 1.00 13.26 ? 141 CYS A SG  1 
ATOM   536  N  N   . ARG A 1 142 ? 35.176 16.247  49.703 1.00 10.88 ? 142 ARG A N   1 
ATOM   537  C  CA  . ARG A 1 142 ? 33.773 16.425  49.321 1.00 11.59 ? 142 ARG A CA  1 
ATOM   538  C  C   . ARG A 1 142 ? 33.526 16.378  47.816 1.00 11.53 ? 142 ARG A C   1 
ATOM   539  O  O   . ARG A 1 142 ? 32.379 16.206  47.410 1.00 12.34 ? 142 ARG A O   1 
ATOM   540  C  CB  . ARG A 1 142 ? 33.264 17.773  49.836 1.00 12.96 ? 142 ARG A CB  1 
ATOM   541  C  CG  . ARG A 1 142 ? 33.245 17.880  51.383 1.00 11.67 ? 142 ARG A CG  1 
ATOM   542  C  CD  . ARG A 1 142 ? 32.841 19.270  51.794 1.00 14.53 ? 142 ARG A CD  1 
ATOM   543  N  NE  . ARG A 1 142 ? 32.634 19.407  53.240 1.00 13.54 ? 142 ARG A NE  1 
ATOM   544  C  CZ  . ARG A 1 142 ? 32.553 20.565  53.876 1.00 14.57 ? 142 ARG A CZ  1 
ATOM   545  N  NH1 . ARG A 1 142 ? 32.694 21.723  53.245 1.00 16.19 ? 142 ARG A NH1 1 
ATOM   546  N  NH2 . ARG A 1 142 ? 32.363 20.571  55.194 1.00 13.96 ? 142 ARG A NH2 1 
ATOM   547  N  N   . PHE A 1 143 ? 34.557 16.547  46.995 1.00 10.50 ? 143 PHE A N   1 
ATOM   548  C  CA  . PHE A 1 143 ? 34.404 16.629  45.539 1.00 10.69 ? 143 PHE A CA  1 
ATOM   549  C  C   . PHE A 1 143 ? 35.055 15.456  44.835 1.00 13.45 ? 143 PHE A C   1 
ATOM   550  O  O   . PHE A 1 143 ? 34.917 15.318  43.616 1.00 12.83 ? 143 PHE A O   1 
ATOM   551  C  CB  . PHE A 1 143 ? 35.042 17.923  45.013 1.00 10.87 ? 143 PHE A CB  1 
ATOM   552  C  CG  . PHE A 1 143 ? 36.524 17.935  45.160 1.00 9.38  ? 143 PHE A CG  1 
ATOM   553  C  CD1 . PHE A 1 143 ? 37.345 17.437  44.149 1.00 12.49 ? 143 PHE A CD1 1 
ATOM   554  C  CD2 . PHE A 1 143 ? 37.122 18.380  46.333 1.00 10.49 ? 143 PHE A CD2 1 
ATOM   555  C  CE1 . PHE A 1 143 ? 38.747 17.380  44.347 1.00 13.91 ? 143 PHE A CE1 1 
ATOM   556  C  CE2 . PHE A 1 143 ? 38.484 18.330  46.498 1.00 13.80 ? 143 PHE A CE2 1 
ATOM   557  C  CZ  . PHE A 1 143 ? 39.288 17.827  45.507 1.00 15.53 ? 143 PHE A CZ  1 
ATOM   558  N  N   . CYS A 1 144 ? 35.807 14.634  45.544 1.00 11.04 ? 144 CYS A N   1 
ATOM   559  C  CA  . CYS A 1 144 ? 36.805 13.783  44.911 1.00 9.74  ? 144 CYS A CA  1 
ATOM   560  C  C   . CYS A 1 144 ? 36.254 12.418  44.525 1.00 11.43 ? 144 CYS A C   1 
ATOM   561  O  O   . CYS A 1 144 ? 35.510 11.798  45.286 1.00 13.04 ? 144 CYS A O   1 
ATOM   562  C  CB  . CYS A 1 144 ? 37.996 13.619  45.855 1.00 10.43 ? 144 CYS A CB  1 
ATOM   563  S  SG  . CYS A 1 144 ? 39.305 12.609  45.116 1.00 12.01 ? 144 CYS A SG  1 
ATOM   564  N  N   A SER A 1 145 ? 36.629 11.959  43.321 0.41 12.74 ? 145 SER A N   1 
ATOM   565  N  N   B SER A 1 145 ? 36.624 11.950  43.330 0.59 12.73 ? 145 SER A N   1 
ATOM   566  C  CA  A SER A 1 145 ? 36.159 10.690  42.783 0.41 14.02 ? 145 SER A CA  1 
ATOM   567  C  CA  B SER A 1 145 ? 36.121 10.678  42.839 0.59 13.86 ? 145 SER A CA  1 
ATOM   568  C  C   A SER A 1 145 ? 37.054 9.514   43.138 0.41 14.28 ? 145 SER A C   1 
ATOM   569  C  C   B SER A 1 145 ? 37.056 9.513   43.131 0.59 14.23 ? 145 SER A C   1 
ATOM   570  O  O   A SER A 1 145 ? 36.689 8.372   42.835 0.41 16.79 ? 145 SER A O   1 
ATOM   571  O  O   B SER A 1 145 ? 36.726 8.377   42.771 0.59 16.83 ? 145 SER A O   1 
ATOM   572  C  CB  A SER A 1 145 ? 36.037 10.761  41.248 0.41 16.02 ? 145 SER A CB  1 
ATOM   573  C  CB  B SER A 1 145 ? 35.879 10.753  41.323 0.59 16.36 ? 145 SER A CB  1 
ATOM   574  O  OG  A SER A 1 145 ? 35.090 11.732  40.864 0.41 16.28 ? 145 SER A OG  1 
ATOM   575  O  OG  B SER A 1 145 ? 37.107 11.045  40.706 0.59 15.84 ? 145 SER A OG  1 
ATOM   576  N  N   . VAL A 1 146 ? 38.220 9.756   43.745 1.00 12.93 ? 146 VAL A N   1 
ATOM   577  C  CA  . VAL A 1 146 ? 39.098 8.645   44.102 1.00 12.95 ? 146 VAL A CA  1 
ATOM   578  C  C   . VAL A 1 146 ? 38.370 7.759   45.104 1.00 13.61 ? 146 VAL A C   1 
ATOM   579  O  O   . VAL A 1 146 ? 37.682 8.255   46.006 1.00 13.64 ? 146 VAL A O   1 
ATOM   580  C  CB  . VAL A 1 146 ? 40.428 9.156   44.681 1.00 11.74 ? 146 VAL A CB  1 
ATOM   581  C  CG1 . VAL A 1 146 ? 41.324 7.976   45.136 1.00 12.40 ? 146 VAL A CG1 1 
ATOM   582  C  CG2 . VAL A 1 146 ? 41.205 9.970   43.632 1.00 13.27 ? 146 VAL A CG2 1 
ATOM   583  N  N   . LYS A 1 147 ? 38.529 6.438   44.963 1.00 15.03 ? 147 LYS A N   1 
ATOM   584  C  CA  . LYS A 1 147 ? 37.899 5.510   45.906 1.00 13.59 ? 147 LYS A CA  1 
ATOM   585  C  C   . LYS A 1 147 ? 38.395 5.751   47.327 1.00 12.20 ? 147 LYS A C   1 
ATOM   586  O  O   . LYS A 1 147 ? 39.582 5.970   47.540 1.00 15.48 ? 147 LYS A O   1 
ATOM   587  C  CB  . LYS A 1 147 ? 38.203 4.065   45.532 1.00 16.95 ? 147 LYS A CB  1 
ATOM   588  C  CG  . LYS A 1 147 ? 37.740 3.656   44.171 1.00 33.77 ? 147 LYS A CG  1 
ATOM   589  C  CD  . LYS A 1 147 ? 38.141 2.205   43.888 1.00 33.34 ? 147 LYS A CD  1 
ATOM   590  C  CE  . LYS A 1 147 ? 36.927 1.313   43.972 1.00 41.92 ? 147 LYS A CE  1 
ATOM   591  N  NZ  . LYS A 1 147 ? 35.788 1.960   43.257 1.00 48.00 ? 147 LYS A NZ  1 
ATOM   592  N  N   . THR A 1 148 ? 37.483 5.675   48.306 1.00 15.30 ? 148 THR A N   1 
ATOM   593  C  CA  . THR A 1 148 ? 37.827 5.921   49.706 1.00 13.11 ? 148 THR A CA  1 
ATOM   594  C  C   . THR A 1 148 ? 38.167 4.604   50.398 1.00 15.71 ? 148 THR A C   1 
ATOM   595  O  O   . THR A 1 148 ? 37.605 3.552   50.077 1.00 20.74 ? 148 THR A O   1 
ATOM   596  C  CB  . THR A 1 148 ? 36.679 6.609   50.451 1.00 17.46 ? 148 THR A CB  1 
ATOM   597  O  OG1 . THR A 1 148 ? 36.364 7.835   49.791 1.00 20.68 ? 148 THR A OG1 1 
ATOM   598  C  CG2 . THR A 1 148 ? 37.059 6.934   51.894 1.00 25.12 ? 148 THR A CG2 1 
ATOM   599  N  N   . ALA A 1 149 ? 39.099 4.677   51.344 1.00 14.27 ? 149 ALA A N   1 
ATOM   600  C  CA  . ALA A 1 149 ? 39.430 3.528   52.185 1.00 17.30 ? 149 ALA A CA  1 
ATOM   601  C  C   . ALA A 1 149 ? 39.816 4.040   53.560 1.00 18.61 ? 149 ALA A C   1 
ATOM   602  O  O   . ALA A 1 149 ? 40.262 5.179   53.718 1.00 23.36 ? 149 ALA A O   1 
ATOM   603  C  CB  . ALA A 1 149 ? 40.554 2.685   51.584 1.00 18.98 ? 149 ALA A CB  1 
ATOM   604  N  N   . ARG A 1 150 ? 39.663 3.185   54.583 1.00 18.78 ? 150 ARG A N   1 
ATOM   605  C  CA  . ARG A 1 150 ? 40.004 3.703   55.905 1.00 22.07 ? 150 ARG A CA  1 
ATOM   606  C  C   . ARG A 1 150 ? 41.504 3.743   56.176 1.00 24.65 ? 150 ARG A C   1 
ATOM   607  O  O   . ARG A 1 150 ? 41.950 4.538   57.009 1.00 29.81 ? 150 ARG A O   1 
ATOM   608  C  CB  . ARG A 1 150 ? 39.297 2.914   57.006 1.00 29.92 ? 150 ARG A CB  1 
ATOM   609  C  CG  . ARG A 1 150 ? 37.916 3.478   57.270 1.00 33.21 ? 150 ARG A CG  1 
ATOM   610  C  CD  . ARG A 1 150 ? 37.209 2.762   58.397 1.00 33.33 ? 150 ARG A CD  1 
ATOM   611  N  NE  . ARG A 1 150 ? 35.822 3.194   58.507 1.00 40.32 ? 150 ARG A NE  1 
ATOM   612  C  CZ  . ARG A 1 150 ? 34.848 2.795   57.698 1.00 39.76 ? 150 ARG A CZ  1 
ATOM   613  N  NH1 . ARG A 1 150 ? 35.079 1.970   56.691 1.00 40.59 ? 150 ARG A NH1 1 
ATOM   614  N  NH2 . ARG A 1 150 ? 33.609 3.232   57.910 1.00 41.98 ? 150 ARG A NH2 1 
ATOM   615  N  N   . ASN A 1 151 ? 42.309 2.949   55.502 1.00 19.91 ? 151 ASN A N   1 
ATOM   616  C  CA  . ASN A 1 151 ? 43.724 3.170   55.738 1.00 23.53 ? 151 ASN A CA  1 
ATOM   617  C  C   . ASN A 1 151 ? 44.509 3.139   54.440 1.00 24.98 ? 151 ASN A C   1 
ATOM   618  O  O   . ASN A 1 151 ? 44.043 2.610   53.420 1.00 18.35 ? 151 ASN A O   1 
ATOM   619  C  CB  . ASN A 1 151 ? 44.297 2.186   56.773 1.00 29.55 ? 151 ASN A CB  1 
ATOM   620  C  CG  . ASN A 1 151 ? 43.999 0.755   56.467 1.00 37.07 ? 151 ASN A CG  1 
ATOM   621  O  OD1 . ASN A 1 151 ? 44.478 0.203   55.477 1.00 35.89 ? 151 ASN A OD1 1 
ATOM   622  N  ND2 . ASN A 1 151 ? 43.270 0.111   57.362 1.00 30.78 ? 151 ASN A ND2 1 
ATOM   623  N  N   . PRO A 1 152 ? 45.696 3.744   54.432 1.00 21.12 ? 152 PRO A N   1 
ATOM   624  C  CA  . PRO A 1 152 ? 46.532 3.675   53.250 1.00 20.34 ? 152 PRO A CA  1 
ATOM   625  C  C   . PRO A 1 152 ? 47.049 2.268   53.053 1.00 22.32 ? 152 PRO A C   1 
ATOM   626  O  O   . PRO A 1 152 ? 47.249 1.515   54.027 1.00 22.81 ? 152 PRO A O   1 
ATOM   627  C  CB  . PRO A 1 152 ? 47.680 4.654   53.561 1.00 22.73 ? 152 PRO A CB  1 
ATOM   628  C  CG  . PRO A 1 152 ? 47.452 5.192   54.928 1.00 26.16 ? 152 PRO A CG  1 
ATOM   629  C  CD  . PRO A 1 152 ? 46.364 4.405   55.571 1.00 27.20 ? 152 PRO A CD  1 
ATOM   630  N  N   . PRO A 1 153 ? 47.302 1.865   51.818 1.00 24.55 ? 153 PRO A N   1 
ATOM   631  C  CA  . PRO A 1 153 ? 47.922 0.569   51.554 1.00 26.21 ? 153 PRO A CA  1 
ATOM   632  C  C   . PRO A 1 153 ? 49.415 0.646   51.794 1.00 21.61 ? 153 PRO A C   1 
ATOM   633  O  O   . PRO A 1 153 ? 49.981 1.746   51.868 1.00 26.81 ? 153 PRO A O   1 
ATOM   634  C  CB  . PRO A 1 153 ? 47.613 0.333   50.071 1.00 23.18 ? 153 PRO A CB  1 
ATOM   635  C  CG  . PRO A 1 153 ? 47.645 1.739   49.508 1.00 23.53 ? 153 PRO A CG  1 
ATOM   636  C  CD  . PRO A 1 153 ? 47.074 2.642   50.585 1.00 21.93 ? 153 PRO A CD  1 
ATOM   637  N  N   . PRO A 1 154 ? 50.096 -0.491  51.899 1.00 20.64 ? 154 PRO A N   1 
ATOM   638  C  CA  . PRO A 1 154 ? 51.546 -0.448  52.104 1.00 22.99 ? 154 PRO A CA  1 
ATOM   639  C  C   . PRO A 1 154 ? 52.287 0.003   50.844 1.00 22.81 ? 154 PRO A C   1 
ATOM   640  O  O   . PRO A 1 154 ? 51.856 -0.230  49.712 1.00 23.91 ? 154 PRO A O   1 
ATOM   641  C  CB  . PRO A 1 154 ? 51.901 -1.897  52.462 1.00 29.01 ? 154 PRO A CB  1 
ATOM   642  C  CG  . PRO A 1 154 ? 50.604 -2.627  52.613 1.00 34.71 ? 154 PRO A CG  1 
ATOM   643  C  CD  . PRO A 1 154 ? 49.587 -1.869  51.825 1.00 26.79 ? 154 PRO A CD  1 
ATOM   644  N  N   . LEU A 1 155 ? 53.430 0.631   51.064 1.00 30.94 ? 155 LEU A N   1 
ATOM   645  C  CA  . LEU A 1 155 ? 54.298 1.018   49.963 1.00 31.33 ? 155 LEU A CA  1 
ATOM   646  C  C   . LEU A 1 155 ? 54.964 -0.223  49.376 1.00 29.38 ? 155 LEU A C   1 
ATOM   647  O  O   . LEU A 1 155 ? 55.599 -0.991  50.105 1.00 27.07 ? 155 LEU A O   1 
ATOM   648  C  CB  . LEU A 1 155 ? 55.338 2.013   50.466 1.00 35.39 ? 155 LEU A CB  1 
ATOM   649  C  CG  . LEU A 1 155 ? 55.792 3.063   49.462 1.00 34.03 ? 155 LEU A CG  1 
ATOM   650  C  CD1 . LEU A 1 155 ? 54.594 3.845   48.986 1.00 34.05 ? 155 LEU A CD1 1 
ATOM   651  C  CD2 . LEU A 1 155 ? 56.822 3.990   50.089 1.00 39.27 ? 155 LEU A CD2 1 
ATOM   652  N  N   . ASP A 1 156 ? 54.799 -0.441  48.073 1.00 25.41 ? 156 ASP A N   1 
ATOM   653  C  CA  . ASP A 1 156 ? 55.460 -1.540  47.377 1.00 23.79 ? 156 ASP A CA  1 
ATOM   654  C  C   . ASP A 1 156 ? 56.791 -1.029  46.829 1.00 26.08 ? 156 ASP A C   1 
ATOM   655  O  O   . ASP A 1 156 ? 56.818 -0.209  45.901 1.00 21.10 ? 156 ASP A O   1 
ATOM   656  C  CB  . ASP A 1 156 ? 54.571 -2.090  46.259 1.00 25.27 ? 156 ASP A CB  1 
ATOM   657  C  CG  . ASP A 1 156 ? 55.272 -3.138  45.398 1.00 30.84 ? 156 ASP A CG  1 
ATOM   658  O  OD1 . ASP A 1 156 ? 56.434 -3.514  45.685 1.00 30.32 ? 156 ASP A OD1 1 
ATOM   659  O  OD2 . ASP A 1 156 ? 54.654 -3.587  44.406 1.00 36.14 ? 156 ASP A OD2 1 
ATOM   660  N  N   . ALA A 1 157 ? 57.901 -1.533  47.378 1.00 23.06 ? 157 ALA A N   1 
ATOM   661  C  CA  . ALA A 1 157 ? 59.204 -1.025  46.957 1.00 21.98 ? 157 ALA A CA  1 
ATOM   662  C  C   . ALA A 1 157 ? 59.563 -1.411  45.528 1.00 19.90 ? 157 ALA A C   1 
ATOM   663  O  O   . ALA A 1 157 ? 60.448 -0.775  44.945 1.00 22.30 ? 157 ALA A O   1 
ATOM   664  C  CB  . ALA A 1 157 ? 60.301 -1.494  47.916 1.00 25.02 ? 157 ALA A CB  1 
ATOM   665  N  N   . SER A 1 158 ? 58.893 -2.402  44.947 1.00 20.24 ? 158 SER A N   1 
ATOM   666  C  CA  . SER A 1 158 ? 59.158 -2.784  43.569 1.00 25.43 ? 158 SER A CA  1 
ATOM   667  C  C   . SER A 1 158 ? 58.314 -2.007  42.571 1.00 23.56 ? 158 SER A C   1 
ATOM   668  O  O   . SER A 1 158 ? 58.506 -2.189  41.359 1.00 21.17 ? 158 SER A O   1 
ATOM   669  C  CB  . SER A 1 158 ? 58.913 -4.284  43.381 1.00 34.00 ? 158 SER A CB  1 
ATOM   670  O  OG  . SER A 1 158 ? 57.565 -4.613  43.669 1.00 40.89 ? 158 SER A OG  1 
ATOM   671  N  N   . GLU A 1 159 ? 57.374 -1.177  43.052 1.00 18.92 ? 159 GLU A N   1 
ATOM   672  C  CA  . GLU A 1 159 ? 56.479 -0.469  42.138 1.00 14.79 ? 159 GLU A CA  1 
ATOM   673  C  C   . GLU A 1 159 ? 57.210 0.516   41.224 1.00 17.68 ? 159 GLU A C   1 
ATOM   674  O  O   . GLU A 1 159 ? 56.892 0.543   40.024 1.00 17.93 ? 159 GLU A O   1 
ATOM   675  C  CB  . GLU A 1 159 ? 55.374 0.261   42.923 1.00 18.64 ? 159 GLU A CB  1 
ATOM   676  C  CG  . GLU A 1 159 ? 54.461 1.104   41.998 1.00 22.41 ? 159 GLU A CG  1 
ATOM   677  C  CD  . GLU A 1 159 ? 53.300 1.777   42.725 1.00 22.61 ? 159 GLU A CD  1 
ATOM   678  O  OE1 . GLU A 1 159 ? 53.515 2.469   43.751 1.00 19.71 ? 159 GLU A OE1 1 
ATOM   679  O  OE2 . GLU A 1 159 ? 52.166 1.572   42.257 1.00 22.18 ? 159 GLU A OE2 1 
ATOM   680  N  N   . PRO A 1 160 ? 58.159 1.333   41.695 1.00 16.80 ? 160 PRO A N   1 
ATOM   681  C  CA  . PRO A 1 160 ? 58.849 2.241   40.753 1.00 16.25 ? 160 PRO A CA  1 
ATOM   682  C  C   . PRO A 1 160 ? 59.484 1.517   39.576 1.00 15.90 ? 160 PRO A C   1 
ATOM   683  O  O   . PRO A 1 160 ? 59.254 1.902   38.426 1.00 17.00 ? 160 PRO A O   1 
ATOM   684  C  CB  . PRO A 1 160 ? 59.886 2.934   41.643 1.00 15.86 ? 160 PRO A CB  1 
ATOM   685  C  CG  . PRO A 1 160 ? 59.271 2.926   42.998 1.00 20.55 ? 160 PRO A CG  1 
ATOM   686  C  CD  . PRO A 1 160 ? 58.563 1.592   43.082 1.00 16.31 ? 160 PRO A CD  1 
ATOM   687  N  N   . TYR A 1 161 ? 60.245 0.442   39.837 1.00 16.72 ? 161 TYR A N   1 
ATOM   688  C  CA  . TYR A 1 161 ? 60.854 -0.332  38.756 1.00 19.30 ? 161 TYR A CA  1 
ATOM   689  C  C   . TYR A 1 161 ? 59.793 -0.995  37.883 1.00 19.91 ? 161 TYR A C   1 
ATOM   690  O  O   . TYR A 1 161 ? 59.869 -0.948  36.649 1.00 20.68 ? 161 TYR A O   1 
ATOM   691  C  CB  . TYR A 1 161 ? 61.798 -1.390  39.348 1.00 17.31 ? 161 TYR A CB  1 
ATOM   692  C  CG  . TYR A 1 161 ? 62.379 -2.325  38.306 1.00 26.41 ? 161 TYR A CG  1 
ATOM   693  C  CD1 . TYR A 1 161 ? 63.585 -2.036  37.671 1.00 28.82 ? 161 TYR A CD1 1 
ATOM   694  C  CD2 . TYR A 1 161 ? 61.718 -3.494  37.959 1.00 25.39 ? 161 TYR A CD2 1 
ATOM   695  C  CE1 . TYR A 1 161 ? 64.113 -2.906  36.683 1.00 26.29 ? 161 TYR A CE1 1 
ATOM   696  C  CE2 . TYR A 1 161 ? 62.226 -4.349  36.985 1.00 31.48 ? 161 TYR A CE2 1 
ATOM   697  C  CZ  . TYR A 1 161 ? 63.426 -4.063  36.363 1.00 29.48 ? 161 TYR A CZ  1 
ATOM   698  O  OH  . TYR A 1 161 ? 63.921 -4.943  35.407 1.00 34.20 ? 161 TYR A OH  1 
ATOM   699  N  N   . ASN A 1 162 ? 58.815 -1.663  38.506 1.00 17.96 ? 162 ASN A N   1 
ATOM   700  C  CA  . ASN A 1 162 ? 57.859 -2.434  37.713 1.00 21.26 ? 162 ASN A CA  1 
ATOM   701  C  C   . ASN A 1 162 ? 56.961 -1.526  36.885 1.00 16.49 ? 162 ASN A C   1 
ATOM   702  O  O   . ASN A 1 162 ? 56.629 -1.847  35.741 1.00 19.13 ? 162 ASN A O   1 
ATOM   703  C  CB  . ASN A 1 162 ? 57.021 -3.323  38.637 1.00 19.35 ? 162 ASN A CB  1 
ATOM   704  C  CG  . ASN A 1 162 ? 57.801 -4.535  39.132 1.00 26.48 ? 162 ASN A CG  1 
ATOM   705  O  OD1 . ASN A 1 162 ? 58.696 -5.034  38.442 1.00 26.08 ? 162 ASN A OD1 1 
ATOM   706  N  ND2 . ASN A 1 162 ? 57.458 -5.016  40.320 1.00 28.75 ? 162 ASN A ND2 1 
ATOM   707  N  N   . THR A 1 163 ? 56.525 -0.409  37.469 1.00 15.90 ? 163 THR A N   1 
ATOM   708  C  CA  . THR A 1 163 ? 55.606 0.480   36.770 1.00 14.73 ? 163 THR A CA  1 
ATOM   709  C  C   . THR A 1 163 ? 56.304 1.222   35.643 1.00 15.56 ? 163 THR A C   1 
ATOM   710  O  O   . THR A 1 163 ? 55.750 1.351   34.544 1.00 16.09 ? 163 THR A O   1 
ATOM   711  C  CB  . THR A 1 163 ? 54.974 1.455   37.764 1.00 17.34 ? 163 THR A CB  1 
ATOM   712  O  OG1 . THR A 1 163 ? 54.069 0.738   38.620 1.00 23.78 ? 163 THR A OG1 1 
ATOM   713  C  CG2 . THR A 1 163 ? 54.208 2.552   37.028 1.00 16.43 ? 163 THR A CG2 1 
ATOM   714  N  N   . ALA A 1 164 ? 57.546 1.650   35.868 1.00 16.85 ? 164 ALA A N   1 
ATOM   715  C  CA  . ALA A 1 164 ? 58.316 2.241   34.775 1.00 15.27 ? 164 ALA A CA  1 
ATOM   716  C  C   . ALA A 1 164 ? 58.512 1.239   33.647 1.00 15.75 ? 164 ALA A C   1 
ATOM   717  O  O   . ALA A 1 164 ? 58.376 1.583   32.473 1.00 15.91 ? 164 ALA A O   1 
ATOM   718  C  CB  . ALA A 1 164 ? 59.661 2.749   35.295 1.00 15.68 ? 164 ALA A CB  1 
ATOM   719  N  N   . LYS A 1 165 ? 58.812 -0.020  33.994 1.00 16.44 ? 165 LYS A N   1 
ATOM   720  C  CA  . LYS A 1 165 ? 59.021 -1.034  32.963 1.00 17.95 ? 165 LYS A CA  1 
ATOM   721  C  C   . LYS A 1 165 ? 57.751 -1.249  32.153 1.00 19.21 ? 165 LYS A C   1 
ATOM   722  O  O   . LYS A 1 165 ? 57.793 -1.294  30.913 1.00 20.43 ? 165 LYS A O   1 
ATOM   723  C  CB  . LYS A 1 165 ? 59.499 -2.325  33.639 1.00 23.44 ? 165 LYS A CB  1 
ATOM   724  C  CG  . LYS A 1 165 ? 59.911 -3.477  32.736 1.00 25.20 ? 165 LYS A CG  1 
ATOM   725  C  CD  . LYS A 1 165 ? 60.306 -4.682  33.621 1.00 25.82 ? 165 LYS A CD  1 
ATOM   726  C  CE  . LYS A 1 165 ? 61.601 -5.335  33.172 1.00 39.54 ? 165 LYS A CE  1 
ATOM   727  N  NZ  . LYS A 1 165 ? 61.622 -5.582  31.705 1.00 46.03 ? 165 LYS A NZ  1 
ATOM   728  N  N   . ALA A 1 166 ? 56.599 -1.339  32.832 1.00 17.16 ? 166 ALA A N   1 
ATOM   729  C  CA  . ALA A 1 166 ? 55.343 -1.609  32.145 1.00 21.46 ? 166 ALA A CA  1 
ATOM   730  C  C   . ALA A 1 166 ? 54.935 -0.449  31.244 1.00 19.33 ? 166 ALA A C   1 
ATOM   731  O  O   . ALA A 1 166 ? 54.461 -0.663  30.121 1.00 20.55 ? 166 ALA A O   1 
ATOM   732  C  CB  . ALA A 1 166 ? 54.242 -1.900  33.166 1.00 21.65 ? 166 ALA A CB  1 
ATOM   733  N  N   . ILE A 1 167 ? 55.108 0.789   31.725 1.00 15.33 ? 167 ILE A N   1 
ATOM   734  C  CA  . ILE A 1 167 ? 54.765 1.951   30.906 1.00 13.94 ? 167 ILE A CA  1 
ATOM   735  C  C   . ILE A 1 167 ? 55.587 1.965   29.628 1.00 14.67 ? 167 ILE A C   1 
ATOM   736  O  O   . ILE A 1 167 ? 55.063 2.219   28.531 1.00 19.41 ? 167 ILE A O   1 
ATOM   737  C  CB  . ILE A 1 167 ? 54.982 3.250   31.703 1.00 14.35 ? 167 ILE A CB  1 
ATOM   738  C  CG1 . ILE A 1 167 ? 53.974 3.308   32.834 1.00 15.28 ? 167 ILE A CG1 1 
ATOM   739  C  CG2 . ILE A 1 167 ? 54.828 4.480   30.764 1.00 13.55 ? 167 ILE A CG2 1 
ATOM   740  C  CD1 . ILE A 1 167 ? 54.286 4.380   33.892 1.00 14.42 ? 167 ILE A CD1 1 
ATOM   741  N  N   . ALA A 1 168 ? 56.899 1.735   29.764 1.00 16.84 ? 168 ALA A N   1 
ATOM   742  C  CA  . ALA A 1 168 ? 57.790 1.736   28.603 1.00 17.74 ? 168 ALA A CA  1 
ATOM   743  C  C   . ALA A 1 168 ? 57.428 0.625   27.623 1.00 22.12 ? 168 ALA A C   1 
ATOM   744  O  O   . ALA A 1 168 ? 57.419 0.850   26.410 1.00 25.02 ? 168 ALA A O   1 
ATOM   745  C  CB  . ALA A 1 168 ? 59.237 1.603   29.066 1.00 22.48 ? 168 ALA A CB  1 
ATOM   746  N  N   . GLU A 1 169 ? 57.093 -0.570  28.130 1.00 19.52 ? 169 GLU A N   1 
ATOM   747  C  CA  A GLU A 1 169 ? 56.702 -1.631  27.215 0.50 28.36 ? 169 GLU A CA  1 
ATOM   748  C  CA  B GLU A 1 169 ? 56.651 -1.679  27.278 0.50 28.37 ? 169 GLU A CA  1 
ATOM   749  C  C   . GLU A 1 169 ? 55.383 -1.302  26.523 1.00 26.50 ? 169 GLU A C   1 
ATOM   750  O  O   . GLU A 1 169 ? 55.275 -1.483  25.304 1.00 30.56 ? 169 GLU A O   1 
ATOM   751  C  CB  A GLU A 1 169 ? 56.633 -2.968  27.948 0.50 28.66 ? 169 GLU A CB  1 
ATOM   752  C  CB  B GLU A 1 169 ? 56.394 -2.943  28.127 0.50 29.00 ? 169 GLU A CB  1 
ATOM   753  C  CG  A GLU A 1 169 ? 56.380 -4.147  27.020 0.50 29.23 ? 169 GLU A CG  1 
ATOM   754  C  CG  B GLU A 1 169 ? 57.592 -3.483  28.919 0.50 25.49 ? 169 GLU A CG  1 
ATOM   755  C  CD  A GLU A 1 169 ? 57.398 -4.263  25.887 0.50 28.12 ? 169 GLU A CD  1 
ATOM   756  C  CD  B GLU A 1 169 ? 57.334 -4.758  29.773 0.50 26.42 ? 169 GLU A CD  1 
ATOM   757  O  OE1 A GLU A 1 169 ? 58.614 -4.119  26.147 0.50 23.40 ? 169 GLU A OE1 1 
ATOM   758  O  OE1 B GLU A 1 169 ? 56.178 -5.204  29.912 0.50 36.40 ? 169 GLU A OE1 1 
ATOM   759  O  OE2 A GLU A 1 169 ? 56.972 -4.490  24.729 0.50 23.57 ? 169 GLU A OE2 1 
ATOM   760  O  OE2 B GLU A 1 169 ? 58.313 -5.316  30.333 0.50 25.13 ? 169 GLU A OE2 1 
ATOM   761  N  N   . TRP A 1 170 ? 54.398 -0.768  27.261 1.00 22.80 ? 170 TRP A N   1 
ATOM   762  C  CA  . TRP A 1 170 ? 53.101 -0.414  26.687 1.00 22.70 ? 170 TRP A CA  1 
ATOM   763  C  C   . TRP A 1 170 ? 53.248 0.560   25.530 1.00 25.22 ? 170 TRP A C   1 
ATOM   764  O  O   . TRP A 1 170 ? 52.556 0.440   24.512 1.00 32.22 ? 170 TRP A O   1 
ATOM   765  C  CB  . TRP A 1 170 ? 52.220 0.197   27.776 1.00 22.00 ? 170 TRP A CB  1 
ATOM   766  C  CG  . TRP A 1 170 ? 50.787 0.353   27.426 1.00 21.10 ? 170 TRP A CG  1 
ATOM   767  C  CD1 . TRP A 1 170 ? 50.118 -0.214  26.370 1.00 23.61 ? 170 TRP A CD1 1 
ATOM   768  C  CD2 . TRP A 1 170 ? 49.821 1.117   28.152 1.00 16.13 ? 170 TRP A CD2 1 
ATOM   769  N  NE1 . TRP A 1 170 ? 48.796 0.160   26.400 1.00 21.23 ? 170 TRP A NE1 1 
ATOM   770  C  CE2 . TRP A 1 170 ? 48.583 0.966   27.493 1.00 21.72 ? 170 TRP A CE2 1 
ATOM   771  C  CE3 . TRP A 1 170 ? 49.878 1.897   29.322 1.00 15.67 ? 170 TRP A CE3 1 
ATOM   772  C  CZ2 . TRP A 1 170 ? 47.420 1.587   27.941 1.00 18.28 ? 170 TRP A CZ2 1 
ATOM   773  C  CZ3 . TRP A 1 170 ? 48.720 2.510   29.770 1.00 17.03 ? 170 TRP A CZ3 1 
ATOM   774  C  CH2 . TRP A 1 170 ? 47.505 2.356   29.078 1.00 18.45 ? 170 TRP A CH2 1 
ATOM   775  N  N   . GLY A 1 171 ? 54.155 1.513   25.654 1.00 23.18 ? 171 GLY A N   1 
ATOM   776  C  CA  . GLY A 1 171 ? 54.393 2.439   24.573 1.00 29.97 ? 171 GLY A CA  1 
ATOM   777  C  C   . GLY A 1 171 ? 53.560 3.695   24.630 1.00 23.70 ? 171 GLY A C   1 
ATOM   778  O  O   . GLY A 1 171 ? 53.226 4.247   23.580 1.00 28.68 ? 171 GLY A O   1 
ATOM   779  N  N   . LEU A 1 172 ? 53.235 4.180   25.824 1.00 22.04 ? 172 LEU A N   1 
ATOM   780  C  CA  . LEU A 1 172 ? 52.610 5.491   25.934 1.00 16.36 ? 172 LEU A CA  1 
ATOM   781  C  C   . LEU A 1 172 ? 53.531 6.570   25.393 1.00 19.56 ? 172 LEU A C   1 
ATOM   782  O  O   . LEU A 1 172 ? 54.762 6.450   25.423 1.00 19.42 ? 172 LEU A O   1 
ATOM   783  C  CB  . LEU A 1 172 ? 52.289 5.813   27.393 1.00 15.36 ? 172 LEU A CB  1 
ATOM   784  C  CG  . LEU A 1 172 ? 51.271 4.948   28.109 1.00 18.46 ? 172 LEU A CG  1 
ATOM   785  C  CD1 . LEU A 1 172 ? 51.086 5.472   29.526 1.00 15.10 ? 172 LEU A CD1 1 
ATOM   786  C  CD2 . LEU A 1 172 ? 49.945 4.973   27.347 1.00 16.58 ? 172 LEU A CD2 1 
ATOM   787  N  N   . ASP A 1 173 ? 52.933 7.657   24.934 1.00 13.58 ? 173 ASP A N   1 
ATOM   788  C  CA  . ASP A 1 173 ? 53.714 8.825   24.569 1.00 14.42 ? 173 ASP A CA  1 
ATOM   789  C  C   . ASP A 1 173 ? 53.803 9.832   25.695 1.00 12.55 ? 173 ASP A C   1 
ATOM   790  O  O   . ASP A 1 173 ? 54.763 10.616  25.745 1.00 12.71 ? 173 ASP A O   1 
ATOM   791  C  CB  . ASP A 1 173 ? 53.087 9.474   23.352 1.00 14.59 ? 173 ASP A CB  1 
ATOM   792  C  CG  . ASP A 1 173 ? 53.052 8.518   22.181 1.00 24.40 ? 173 ASP A CG  1 
ATOM   793  O  OD1 . ASP A 1 173 ? 54.154 8.116   21.736 1.00 23.72 ? 173 ASP A OD1 1 
ATOM   794  O  OD2 . ASP A 1 173 ? 51.943 8.129   21.760 1.00 19.75 ? 173 ASP A OD2 1 
ATOM   795  N  N   . TYR A 1 174 ? 52.801 9.835   26.569 1.00 10.14 ? 174 TYR A N   1 
ATOM   796  C  CA  . TYR A 1 174 ? 52.716 10.786  27.673 1.00 9.26  ? 174 TYR A CA  1 
ATOM   797  C  C   . TYR A 1 174 ? 52.032 10.077  28.823 1.00 10.85 ? 174 TYR A C   1 
ATOM   798  O  O   . TYR A 1 174 ? 50.953 9.505   28.630 1.00 10.62 ? 174 TYR A O   1 
ATOM   799  C  CB  . TYR A 1 174 ? 51.887 11.999  27.262 1.00 9.65  ? 174 TYR A CB  1 
ATOM   800  C  CG  . TYR A 1 174 ? 51.871 13.177  28.196 1.00 8.98  ? 174 TYR A CG  1 
ATOM   801  C  CD1 . TYR A 1 174 ? 52.477 14.390  27.803 1.00 9.00  ? 174 TYR A CD1 1 
ATOM   802  C  CD2 . TYR A 1 174 ? 51.146 13.155  29.391 1.00 9.63  ? 174 TYR A CD2 1 
ATOM   803  C  CE1 . TYR A 1 174 ? 52.423 15.507  28.615 1.00 9.44  ? 174 TYR A CE1 1 
ATOM   804  C  CE2 . TYR A 1 174 ? 51.105 14.275  30.210 1.00 8.89  ? 174 TYR A CE2 1 
ATOM   805  C  CZ  . TYR A 1 174 ? 51.742 15.449  29.817 1.00 9.08  ? 174 TYR A CZ  1 
ATOM   806  O  OH  . TYR A 1 174 ? 51.645 16.562  30.623 1.00 11.11 ? 174 TYR A OH  1 
ATOM   807  N  N   . VAL A 1 175 ? 52.655 10.088  30.001 1.00 8.99  ? 175 VAL A N   1 
ATOM   808  C  CA  . VAL A 1 175 ? 52.056 9.440   31.165 1.00 10.58 ? 175 VAL A CA  1 
ATOM   809  C  C   . VAL A 1 175 ? 51.885 10.471  32.272 1.00 10.44 ? 175 VAL A C   1 
ATOM   810  O  O   . VAL A 1 175 ? 52.778 11.294  32.526 1.00 9.90  ? 175 VAL A O   1 
ATOM   811  C  CB  . VAL A 1 175 ? 52.877 8.220   31.630 1.00 11.30 ? 175 VAL A CB  1 
ATOM   812  C  CG1 . VAL A 1 175 ? 54.284 8.631   32.125 1.00 10.20 ? 175 VAL A CG1 1 
ATOM   813  C  CG2 . VAL A 1 175 ? 52.080 7.426   32.695 1.00 12.57 ? 175 VAL A CG2 1 
ATOM   814  N  N   . VAL A 1 176 ? 50.716 10.441  32.907 1.00 11.00 ? 176 VAL A N   1 
ATOM   815  C  CA  . VAL A 1 176 ? 50.470 11.222  34.116 1.00 9.09  ? 176 VAL A CA  1 
ATOM   816  C  C   . VAL A 1 176 ? 50.601 10.262  35.284 1.00 11.13 ? 176 VAL A C   1 
ATOM   817  O  O   . VAL A 1 176 ? 49.760 9.374   35.438 1.00 12.40 ? 176 VAL A O   1 
ATOM   818  C  CB  . VAL A 1 176 ? 49.088 11.880  34.107 1.00 9.92  ? 176 VAL A CB  1 
ATOM   819  C  CG1 . VAL A 1 176 ? 48.893 12.643  35.402 1.00 13.48 ? 176 VAL A CG1 1 
ATOM   820  C  CG2 . VAL A 1 176 ? 48.923 12.804  32.901 1.00 9.52  ? 176 VAL A CG2 1 
ATOM   821  N  N   . LEU A 1 177 ? 51.651 10.434  36.086 1.00 8.76  ? 177 LEU A N   1 
ATOM   822  C  CA  . LEU A 1 177 ? 51.834 9.695   37.333 1.00 9.38  ? 177 LEU A CA  1 
ATOM   823  C  C   . LEU A 1 177 ? 51.162 10.490  38.437 1.00 11.65 ? 177 LEU A C   1 
ATOM   824  O  O   . LEU A 1 177 ? 51.508 11.652  38.658 1.00 13.42 ? 177 LEU A O   1 
ATOM   825  C  CB  . LEU A 1 177 ? 53.316 9.524   37.649 1.00 11.48 ? 177 LEU A CB  1 
ATOM   826  C  CG  . LEU A 1 177 ? 54.092 8.715   36.591 1.00 11.90 ? 177 LEU A CG  1 
ATOM   827  C  CD1 . LEU A 1 177 ? 55.599 8.729   36.871 1.00 13.90 ? 177 LEU A CD1 1 
ATOM   828  C  CD2 . LEU A 1 177 ? 53.593 7.276   36.549 1.00 15.02 ? 177 LEU A CD2 1 
ATOM   829  N  N   . THR A 1 178 ? 50.206 9.890   39.129 1.00 11.05 ? 178 THR A N   1 
ATOM   830  C  CA  . THR A 1 178 ? 49.499 10.669  40.128 1.00 11.75 ? 178 THR A CA  1 
ATOM   831  C  C   . THR A 1 178 ? 49.478 9.929   41.456 1.00 14.32 ? 178 THR A C   1 
ATOM   832  O  O   . THR A 1 178 ? 49.714 8.725   41.526 1.00 14.63 ? 178 THR A O   1 
ATOM   833  C  CB  . THR A 1 178 ? 48.109 11.002  39.646 1.00 19.80 ? 178 THR A CB  1 
ATOM   834  O  OG1 . THR A 1 178 ? 47.540 11.964  40.539 1.00 26.23 ? 178 THR A OG1 1 
ATOM   835  C  CG2 . THR A 1 178 ? 47.272 9.756   39.599 1.00 14.18 ? 178 THR A CG2 1 
ATOM   836  N  N   . SER A 1 179 ? 49.320 10.694  42.524 1.00 13.24 ? 179 SER A N   1 
ATOM   837  C  CA  . SER A 1 179 ? 49.248 10.059  43.830 1.00 14.07 ? 179 SER A CA  1 
ATOM   838  C  C   . SER A 1 179 ? 48.359 10.883  44.730 1.00 14.32 ? 179 SER A C   1 
ATOM   839  O  O   . SER A 1 179 ? 48.143 12.077  44.505 1.00 13.66 ? 179 SER A O   1 
ATOM   840  C  CB  . SER A 1 179 ? 50.624 9.891   44.458 1.00 23.54 ? 179 SER A CB  1 
ATOM   841  O  OG  . SER A 1 179 ? 51.228 11.153  44.609 1.00 21.57 ? 179 SER A OG  1 
ATOM   842  N  N   . VAL A 1 180 ? 47.832 10.212  45.747 1.00 13.02 ? 180 VAL A N   1 
ATOM   843  C  CA  . VAL A 1 180 ? 46.898 10.854  46.677 1.00 13.55 ? 180 VAL A CA  1 
ATOM   844  C  C   . VAL A 1 180 ? 47.690 11.416  47.846 1.00 18.23 ? 180 VAL A C   1 
ATOM   845  O  O   . VAL A 1 180 ? 48.910 11.226  47.942 1.00 19.86 ? 180 VAL A O   1 
ATOM   846  C  CB  . VAL A 1 180 ? 45.824 9.866   47.169 1.00 12.14 ? 180 VAL A CB  1 
ATOM   847  C  CG1 . VAL A 1 180 ? 45.147 9.168   45.988 1.00 17.09 ? 180 VAL A CG1 1 
ATOM   848  C  CG2 . VAL A 1 180 ? 46.466 8.845   48.120 1.00 14.16 ? 180 VAL A CG2 1 
ATOM   849  N  N   . ASP A 1 181 ? 47.004 12.095  48.762 1.00 14.44 ? 181 ASP A N   1 
ATOM   850  C  CA  . ASP A 1 181 ? 47.661 12.610  49.953 1.00 14.99 ? 181 ASP A CA  1 
ATOM   851  C  C   . ASP A 1 181 ? 48.044 11.434  50.848 1.00 21.05 ? 181 ASP A C   1 
ATOM   852  O  O   . ASP A 1 181 ? 47.179 10.736  51.383 1.00 19.93 ? 181 ASP A O   1 
ATOM   853  C  CB  . ASP A 1 181 ? 46.750 13.583  50.683 1.00 16.18 ? 181 ASP A CB  1 
ATOM   854  C  CG  . ASP A 1 181 ? 47.449 14.253  51.832 1.00 32.49 ? 181 ASP A CG  1 
ATOM   855  O  OD1 . ASP A 1 181 ? 48.062 15.304  51.617 1.00 38.61 ? 181 ASP A OD1 1 
ATOM   856  O  OD2 . ASP A 1 181 ? 47.435 13.691  52.939 1.00 35.91 ? 181 ASP A OD2 1 
ATOM   857  N  N   . ARG A 1 182 ? 49.344 11.179  50.965 1.00 19.59 ? 182 ARG A N   1 
ATOM   858  C  CA  . ARG A 1 182 ? 49.855 10.097  51.803 1.00 22.88 ? 182 ARG A CA  1 
ATOM   859  C  C   . ARG A 1 182 ? 50.424 10.738  53.067 1.00 23.76 ? 182 ARG A C   1 
ATOM   860  O  O   . ARG A 1 182 ? 51.620 10.989  53.190 1.00 31.52 ? 182 ARG A O   1 
ATOM   861  C  CB  . ARG A 1 182 ? 50.892 9.268   51.045 1.00 21.31 ? 182 ARG A CB  1 
ATOM   862  C  CG  . ARG A 1 182 ? 50.338 8.459   49.851 1.00 21.95 ? 182 ARG A CG  1 
ATOM   863  C  CD  . ARG A 1 182 ? 49.418 7.339   50.347 1.00 21.94 ? 182 ARG A CD  1 
ATOM   864  N  NE  . ARG A 1 182 ? 50.084 6.509   51.351 1.00 22.93 ? 182 ARG A NE  1 
ATOM   865  C  CZ  . ARG A 1 182 ? 50.366 5.220   51.216 1.00 21.47 ? 182 ARG A CZ  1 
ATOM   866  N  NH1 . ARG A 1 182 ? 50.070 4.557   50.114 1.00 25.40 ? 182 ARG A NH1 1 
ATOM   867  N  NH2 . ARG A 1 182 ? 50.927 4.568   52.237 1.00 21.93 ? 182 ARG A NH2 1 
ATOM   868  N  N   . ASP A 1 183 ? 49.528 10.987  54.029 1.00 32.06 ? 183 ASP A N   1 
ATOM   869  C  CA  . ASP A 1 183 ? 49.932 11.592  55.295 1.00 40.37 ? 183 ASP A CA  1 
ATOM   870  C  C   . ASP A 1 183 ? 50.816 10.669  56.106 1.00 35.34 ? 183 ASP A C   1 
ATOM   871  O  O   . ASP A 1 183 ? 51.600 11.136  56.936 1.00 42.75 ? 183 ASP A O   1 
ATOM   872  C  CB  . ASP A 1 183 ? 48.712 11.982  56.124 1.00 38.60 ? 183 ASP A CB  1 
ATOM   873  C  CG  . ASP A 1 183 ? 47.921 10.773  56.656 1.00 42.95 ? 183 ASP A CG  1 
ATOM   874  O  OD1 . ASP A 1 183 ? 47.276 10.908  57.724 1.00 44.53 ? 183 ASP A OD1 1 
ATOM   875  O  OD2 . ASP A 1 183 ? 47.934 9.695   56.015 1.00 47.62 ? 183 ASP A OD2 1 
ATOM   876  N  N   . ASP A 1 184 ? 50.710 9.362   55.876 1.00 34.06 ? 184 ASP A N   1 
ATOM   877  C  CA  . ASP A 1 184 ? 51.487 8.409   56.643 1.00 35.78 ? 184 ASP A CA  1 
ATOM   878  C  C   . ASP A 1 184 ? 52.979 8.522   56.367 1.00 31.08 ? 184 ASP A C   1 
ATOM   879  O  O   . ASP A 1 184 ? 53.780 8.016   57.160 1.00 37.61 ? 184 ASP A O   1 
ATOM   880  C  CB  . ASP A 1 184 ? 51.000 6.989   56.352 1.00 35.04 ? 184 ASP A CB  1 
ATOM   881  C  CG  . ASP A 1 184 ? 50.931 6.683   54.869 1.00 24.58 ? 184 ASP A CG  1 
ATOM   882  O  OD1 . ASP A 1 184 ? 50.263 7.444   54.115 1.00 31.65 ? 184 ASP A OD1 1 
ATOM   883  O  OD2 . ASP A 1 184 ? 51.548 5.679   54.457 1.00 38.24 ? 184 ASP A OD2 1 
ATOM   884  N  N   . MET A 1 185 ? 53.381 9.182   55.255 1.00 24.05 ? 185 MET A N   1 
ATOM   885  C  CA  . MET A 1 185 ? 54.811 9.193   55.016 1.00 28.66 ? 185 MET A CA  1 
ATOM   886  C  C   . MET A 1 185 ? 55.405 10.579  55.211 1.00 22.26 ? 185 MET A C   1 
ATOM   887  O  O   . MET A 1 185 ? 54.788 11.578  54.816 1.00 26.61 ? 185 MET A O   1 
ATOM   888  C  CB  . MET A 1 185 ? 55.100 8.705   53.599 1.00 27.25 ? 185 MET A CB  1 
ATOM   889  C  CG  . MET A 1 185 ? 54.826 7.230   53.472 1.00 38.49 ? 185 MET A CG  1 
ATOM   890  S  SD  . MET A 1 185 ? 55.191 6.681   51.814 1.00 54.23 ? 185 MET A SD  1 
ATOM   891  C  CE  . MET A 1 185 ? 53.850 7.474   50.987 1.00 19.79 ? 185 MET A CE  1 
ATOM   892  N  N   . PRO A 1 186 ? 56.598 10.667  55.817 1.00 30.79 ? 186 PRO A N   1 
ATOM   893  C  CA  . PRO A 1 186 ? 57.174 11.992  56.107 1.00 31.67 ? 186 PRO A CA  1 
ATOM   894  C  C   . PRO A 1 186 ? 57.331 12.860  54.876 1.00 27.82 ? 186 PRO A C   1 
ATOM   895  O  O   . PRO A 1 186 ? 57.086 14.070  54.939 1.00 39.89 ? 186 PRO A O   1 
ATOM   896  C  CB  . PRO A 1 186 ? 58.535 11.665  56.744 1.00 26.67 ? 186 PRO A CB  1 
ATOM   897  C  CG  . PRO A 1 186 ? 58.785 10.199  56.458 1.00 39.41 ? 186 PRO A CG  1 
ATOM   898  C  CD  . PRO A 1 186 ? 57.431 9.561   56.322 1.00 32.17 ? 186 PRO A CD  1 
ATOM   899  N  N   . ASP A 1 187 ? 57.748 12.279  53.754 1.00 26.68 ? 187 ASP A N   1 
ATOM   900  C  CA  . ASP A 1 187 ? 57.903 13.046  52.528 1.00 25.32 ? 187 ASP A CA  1 
ATOM   901  C  C   . ASP A 1 187 ? 56.709 12.909  51.601 1.00 19.29 ? 187 ASP A C   1 
ATOM   902  O  O   . ASP A 1 187 ? 56.808 13.287  50.427 1.00 21.57 ? 187 ASP A O   1 
ATOM   903  C  CB  . ASP A 1 187 ? 59.185 12.639  51.797 1.00 25.16 ? 187 ASP A CB  1 
ATOM   904  C  CG  . ASP A 1 187 ? 59.100 11.266  51.173 1.00 28.33 ? 187 ASP A CG  1 
ATOM   905  O  OD1 . ASP A 1 187 ? 58.139 10.509  51.460 1.00 26.84 ? 187 ASP A OD1 1 
ATOM   906  O  OD2 . ASP A 1 187 ? 60.004 10.941  50.371 1.00 24.06 ? 187 ASP A OD2 1 
ATOM   907  N  N   . GLY A 1 188 ? 55.592 12.370  52.090 1.00 20.28 ? 188 GLY A N   1 
ATOM   908  C  CA  . GLY A 1 188 ? 54.404 12.244  51.267 1.00 21.43 ? 188 GLY A CA  1 
ATOM   909  C  C   . GLY A 1 188 ? 54.549 11.334  50.069 1.00 20.82 ? 188 GLY A C   1 
ATOM   910  O  O   . GLY A 1 188 ? 53.695 11.370  49.170 1.00 19.23 ? 188 GLY A O   1 
ATOM   911  N  N   . GLY A 1 189 ? 55.594 10.515  50.020 1.00 17.15 ? 189 GLY A N   1 
ATOM   912  C  CA  . GLY A 1 189 ? 55.825 9.678   48.866 1.00 19.72 ? 189 GLY A CA  1 
ATOM   913  C  C   . GLY A 1 189 ? 56.726 10.282  47.808 1.00 17.74 ? 189 GLY A C   1 
ATOM   914  O  O   . GLY A 1 189 ? 56.906 9.665   46.752 1.00 17.09 ? 189 GLY A O   1 
ATOM   915  N  N   . ALA A 1 190 ? 57.345 11.436  48.079 1.00 15.84 ? 190 ALA A N   1 
ATOM   916  C  CA  . ALA A 1 190 ? 58.106 12.124  47.041 1.00 16.77 ? 190 ALA A CA  1 
ATOM   917  C  C   . ALA A 1 190 ? 59.261 11.284  46.510 1.00 19.03 ? 190 ALA A C   1 
ATOM   918  O  O   . ALA A 1 190 ? 59.532 11.300  45.305 1.00 16.93 ? 190 ALA A O   1 
ATOM   919  C  CB  . ALA A 1 190 ? 58.623 13.461  47.569 1.00 16.38 ? 190 ALA A CB  1 
ATOM   920  N  N   . GLU A 1 191 ? 59.974 10.561  47.378 1.00 17.06 ? 191 GLU A N   1 
ATOM   921  C  CA  . GLU A 1 191 ? 61.103 9.783   46.871 1.00 16.19 ? 191 GLU A CA  1 
ATOM   922  C  C   . GLU A 1 191 ? 60.623 8.641   45.994 1.00 15.58 ? 191 GLU A C   1 
ATOM   923  O  O   . GLU A 1 191 ? 61.237 8.340   44.965 1.00 17.52 ? 191 GLU A O   1 
ATOM   924  C  CB  . GLU A 1 191 ? 61.966 9.249   48.017 1.00 22.62 ? 191 GLU A CB  1 
ATOM   925  C  CG  . GLU A 1 191 ? 63.177 8.444   47.480 1.00 26.91 ? 191 GLU A CG  1 
ATOM   926  C  CD  . GLU A 1 191 ? 64.004 9.230   46.430 1.00 41.31 ? 191 GLU A CD  1 
ATOM   927  O  OE1 . GLU A 1 191 ? 64.701 10.186  46.839 1.00 47.66 ? 191 GLU A OE1 1 
ATOM   928  O  OE2 . GLU A 1 191 ? 63.945 8.913   45.202 1.00 40.33 ? 191 GLU A OE2 1 
ATOM   929  N  N   . HIS A 1 192 ? 59.500 8.019   46.371 1.00 14.15 ? 192 HIS A N   1 
ATOM   930  C  CA  . HIS A 1 192 ? 58.918 6.926   45.601 1.00 15.77 ? 192 HIS A CA  1 
ATOM   931  C  C   . HIS A 1 192 ? 58.491 7.415   44.226 1.00 16.90 ? 192 HIS A C   1 
ATOM   932  O  O   . HIS A 1 192 ? 58.758 6.761   43.208 1.00 17.00 ? 192 HIS A O   1 
ATOM   933  C  CB  . HIS A 1 192 ? 57.745 6.352   46.404 1.00 15.69 ? 192 HIS A CB  1 
ATOM   934  C  CG  . HIS A 1 192 ? 57.070 5.165   45.795 1.00 16.62 ? 192 HIS A CG  1 
ATOM   935  N  ND1 . HIS A 1 192 ? 57.357 3.868   46.181 1.00 22.99 ? 192 HIS A ND1 1 
ATOM   936  C  CD2 . HIS A 1 192 ? 56.080 5.075   44.885 1.00 18.71 ? 192 HIS A CD2 1 
ATOM   937  C  CE1 . HIS A 1 192 ? 56.569 3.036   45.522 1.00 23.75 ? 192 HIS A CE1 1 
ATOM   938  N  NE2 . HIS A 1 192 ? 55.784 3.743   44.727 1.00 20.18 ? 192 HIS A NE2 1 
ATOM   939  N  N   . ILE A 1 193 ? 57.860 8.589   44.176 1.00 13.30 ? 193 ILE A N   1 
ATOM   940  C  CA  . ILE A 1 193 ? 57.492 9.178   42.887 1.00 13.38 ? 193 ILE A CA  1 
ATOM   941  C  C   . ILE A 1 193 ? 58.738 9.459   42.059 1.00 13.46 ? 193 ILE A C   1 
ATOM   942  O  O   . ILE A 1 193 ? 58.827 9.074   40.888 1.00 13.81 ? 193 ILE A O   1 
ATOM   943  C  CB  . ILE A 1 193 ? 56.676 10.463  43.106 1.00 12.83 ? 193 ILE A CB  1 
ATOM   944  C  CG1 . ILE A 1 193 ? 55.358 10.123  43.797 1.00 15.64 ? 193 ILE A CG1 1 
ATOM   945  C  CG2 . ILE A 1 193 ? 56.464 11.173  41.763 1.00 12.94 ? 193 ILE A CG2 1 
ATOM   946  C  CD1 . ILE A 1 193 ? 54.680 11.311  44.455 1.00 18.23 ? 193 ILE A CD1 1 
ATOM   947  N  N   . ALA A 1 194 ? 59.719 10.134  42.659 1.00 14.12 ? 194 ALA A N   1 
ATOM   948  C  CA  . ALA A 1 194 ? 60.929 10.495  41.919 1.00 13.50 ? 194 ALA A CA  1 
ATOM   949  C  C   . ALA A 1 194 ? 61.665 9.265   41.392 1.00 13.56 ? 194 ALA A C   1 
ATOM   950  O  O   . ALA A 1 194 ? 62.221 9.291   40.289 1.00 14.44 ? 194 ALA A O   1 
ATOM   951  C  CB  . ALA A 1 194 ? 61.854 11.328  42.806 1.00 16.50 ? 194 ALA A CB  1 
ATOM   952  N  N   . LYS A 1 195 ? 61.705 8.188   42.173 1.00 14.97 ? 195 LYS A N   1 
ATOM   953  C  CA  . LYS A 1 195 ? 62.332 6.961   41.703 1.00 15.75 ? 195 LYS A CA  1 
ATOM   954  C  C   . LYS A 1 195 ? 61.637 6.418   40.457 1.00 13.54 ? 195 LYS A C   1 
ATOM   955  O  O   . LYS A 1 195 ? 62.295 5.865   39.552 1.00 14.78 ? 195 LYS A O   1 
ATOM   956  C  CB  . LYS A 1 195 ? 62.294 5.936   42.841 1.00 17.85 ? 195 LYS A CB  1 
ATOM   957  C  CG  . LYS A 1 195 ? 63.195 4.723   42.675 1.00 27.77 ? 195 LYS A CG  1 
ATOM   958  C  CD  . LYS A 1 195 ? 63.263 3.960   44.028 1.00 26.61 ? 195 LYS A CD  1 
ATOM   959  C  CE  . LYS A 1 195 ? 64.367 2.923   44.038 1.00 38.80 ? 195 LYS A CE  1 
ATOM   960  N  NZ  . LYS A 1 195 ? 64.263 2.018   45.213 1.00 37.89 ? 195 LYS A NZ  1 
ATOM   961  N  N   . THR A 1 196 ? 60.295 6.495   40.427 1.00 12.52 ? 196 THR A N   1 
ATOM   962  C  CA  . THR A 1 196 ? 59.548 5.989   39.279 1.00 12.07 ? 196 THR A CA  1 
ATOM   963  C  C   . THR A 1 196 ? 59.868 6.810   38.041 1.00 13.57 ? 196 THR A C   1 
ATOM   964  O  O   . THR A 1 196 ? 60.101 6.259   36.960 1.00 13.18 ? 196 THR A O   1 
ATOM   965  C  CB  . THR A 1 196 ? 58.042 6.025   39.560 1.00 14.90 ? 196 THR A CB  1 
ATOM   966  O  OG1 . THR A 1 196 ? 57.774 5.349   40.785 1.00 13.13 ? 196 THR A OG1 1 
ATOM   967  C  CG2 . THR A 1 196 ? 57.276 5.366   38.435 1.00 15.12 ? 196 THR A CG2 1 
ATOM   968  N  N   . VAL A 1 197 ? 59.853 8.140   38.184 1.00 12.37 ? 197 VAL A N   1 
ATOM   969  C  CA  . VAL A 1 197 ? 60.215 9.007   37.060 1.00 12.67 ? 197 VAL A CA  1 
ATOM   970  C  C   . VAL A 1 197 ? 61.608 8.654   36.546 1.00 12.09 ? 197 VAL A C   1 
ATOM   971  O  O   . VAL A 1 197 ? 61.845 8.540   35.336 1.00 13.65 ? 197 VAL A O   1 
ATOM   972  C  CB  . VAL A 1 197 ? 60.144 10.482  37.497 1.00 12.24 ? 197 VAL A CB  1 
ATOM   973  C  CG1 . VAL A 1 197 ? 60.615 11.387  36.344 1.00 13.57 ? 197 VAL A CG1 1 
ATOM   974  C  CG2 . VAL A 1 197 ? 58.742 10.848  37.927 1.00 11.58 ? 197 VAL A CG2 1 
ATOM   975  N  N   . SER A 1 198 ? 62.548 8.465   37.471 1.00 12.08 ? 198 SER A N   1 
ATOM   976  C  CA  . SER A 1 198 ? 63.940 8.238   37.099 1.00 15.56 ? 198 SER A CA  1 
ATOM   977  C  C   . SER A 1 198 ? 64.107 6.937   36.328 1.00 16.74 ? 198 SER A C   1 
ATOM   978  O  O   . SER A 1 198 ? 64.794 6.900   35.302 1.00 14.95 ? 198 SER A O   1 
ATOM   979  C  CB  . SER A 1 198 ? 64.809 8.227   38.353 1.00 19.05 ? 198 SER A CB  1 
ATOM   980  O  OG  . SER A 1 198 ? 64.785 9.506   38.981 1.00 23.64 ? 198 SER A OG  1 
ATOM   981  N  N   . TYR A 1 199 ? 63.478 5.851   36.805 1.00 15.02 ? 199 TYR A N   1 
ATOM   982  C  CA  . TYR A 1 199 ? 63.519 4.603   36.044 1.00 17.18 ? 199 TYR A CA  1 
ATOM   983  C  C   . TYR A 1 199 ? 62.922 4.778   34.657 1.00 15.34 ? 199 TYR A C   1 
ATOM   984  O  O   . TYR A 1 199 ? 63.440 4.223   33.684 1.00 17.37 ? 199 TYR A O   1 
ATOM   985  C  CB  . TYR A 1 199 ? 62.755 3.490   36.763 1.00 15.01 ? 199 TYR A CB  1 
ATOM   986  C  CG  . TYR A 1 199 ? 63.490 2.769   37.878 1.00 17.84 ? 199 TYR A CG  1 
ATOM   987  C  CD1 . TYR A 1 199 ? 64.766 2.240   37.675 1.00 18.36 ? 199 TYR A CD1 1 
ATOM   988  C  CD2 . TYR A 1 199 ? 62.878 2.568   39.111 1.00 18.86 ? 199 TYR A CD2 1 
ATOM   989  C  CE1 . TYR A 1 199 ? 65.419 1.556   38.706 1.00 20.91 ? 199 TYR A CE1 1 
ATOM   990  C  CE2 . TYR A 1 199 ? 63.512 1.887   40.127 1.00 17.83 ? 199 TYR A CE2 1 
ATOM   991  C  CZ  . TYR A 1 199 ? 64.778 1.384   39.917 1.00 21.89 ? 199 TYR A CZ  1 
ATOM   992  O  OH  . TYR A 1 199 ? 65.419 0.719   40.942 1.00 28.88 ? 199 TYR A OH  1 
ATOM   993  N  N   . LEU A 1 200 ? 61.784 5.482   34.559 1.00 13.24 ? 200 LEU A N   1 
ATOM   994  C  CA  . LEU A 1 200 ? 61.116 5.619   33.273 1.00 13.49 ? 200 LEU A CA  1 
ATOM   995  C  C   . LEU A 1 200 ? 61.975 6.414   32.295 1.00 15.66 ? 200 LEU A C   1 
ATOM   996  O  O   . LEU A 1 200 ? 62.118 6.027   31.132 1.00 16.86 ? 200 LEU A O   1 
ATOM   997  C  CB  . LEU A 1 200 ? 59.735 6.269   33.476 1.00 14.26 ? 200 LEU A CB  1 
ATOM   998  C  CG  . LEU A 1 200 ? 58.862 6.388   32.233 1.00 17.93 ? 200 LEU A CG  1 
ATOM   999  C  CD1 . LEU A 1 200 ? 58.797 5.093   31.424 1.00 22.34 ? 200 LEU A CD1 1 
ATOM   1000 C  CD2 . LEU A 1 200 ? 57.428 6.832   32.649 1.00 20.42 ? 200 LEU A CD2 1 
ATOM   1001 N  N   . LYS A 1 201 ? 62.562 7.531   32.757 1.00 13.61 ? 201 LYS A N   1 
ATOM   1002 C  CA  . LYS A 1 201 ? 63.360 8.375   31.863 1.00 16.04 ? 201 LYS A CA  1 
ATOM   1003 C  C   . LYS A 1 201 ? 64.649 7.683   31.454 1.00 14.63 ? 201 LYS A C   1 
ATOM   1004 O  O   . LYS A 1 201 ? 65.186 7.957   30.371 1.00 18.17 ? 201 LYS A O   1 
ATOM   1005 C  CB  . LYS A 1 201 ? 63.674 9.715   32.535 1.00 14.26 ? 201 LYS A CB  1 
ATOM   1006 C  CG  . LYS A 1 201 ? 62.492 10.677  32.561 1.00 15.08 ? 201 LYS A CG  1 
ATOM   1007 C  CD  . LYS A 1 201 ? 62.222 11.204  31.159 1.00 13.04 ? 201 LYS A CD  1 
ATOM   1008 C  CE  . LYS A 1 201 ? 61.095 12.224  31.188 1.00 11.55 ? 201 LYS A CE  1 
ATOM   1009 N  NZ  . LYS A 1 201 ? 60.696 12.568  29.810 1.00 10.37 ? 201 LYS A NZ  1 
ATOM   1010 N  N   . GLU A 1 202 ? 65.173 6.805   32.315 1.00 14.41 ? 202 GLU A N   1 
ATOM   1011 C  CA  . GLU A 1 202 ? 66.348 6.020   31.936 1.00 15.22 ? 202 GLU A CA  1 
ATOM   1012 C  C   . GLU A 1 202 ? 65.978 4.964   30.900 1.00 17.94 ? 202 GLU A C   1 
ATOM   1013 O  O   . GLU A 1 202 ? 66.734 4.705   29.960 1.00 21.61 ? 202 GLU A O   1 
ATOM   1014 C  CB  . GLU A 1 202 ? 66.949 5.390   33.199 1.00 19.29 ? 202 GLU A CB  1 
ATOM   1015 C  CG  . GLU A 1 202 ? 67.972 4.280   32.980 1.00 28.98 ? 202 GLU A CG  1 
ATOM   1016 C  CD  . GLU A 1 202 ? 68.594 3.797   34.291 1.00 39.80 ? 202 GLU A CD  1 
ATOM   1017 O  OE1 . GLU A 1 202 ? 69.839 3.921   34.416 1.00 40.17 ? 202 GLU A OE1 1 
ATOM   1018 O  OE2 . GLU A 1 202 ? 67.840 3.324   35.198 1.00 35.18 ? 202 GLU A OE2 1 
ATOM   1019 N  N   . ARG A 1 203 ? 64.791 4.393   31.025 1.00 18.45 ? 203 ARG A N   1 
ATOM   1020 C  CA  . ARG A 1 203 ? 64.348 3.328   30.138 1.00 16.65 ? 203 ARG A CA  1 
ATOM   1021 C  C   . ARG A 1 203 ? 63.936 3.856   28.767 1.00 15.12 ? 203 ARG A C   1 
ATOM   1022 O  O   . ARG A 1 203 ? 64.260 3.258   27.736 1.00 21.78 ? 203 ARG A O   1 
ATOM   1023 C  CB  . ARG A 1 203 ? 63.189 2.600   30.814 1.00 24.14 ? 203 ARG A CB  1 
ATOM   1024 C  CG  . ARG A 1 203 ? 63.046 1.154   30.478 1.00 36.15 ? 203 ARG A CG  1 
ATOM   1025 C  CD  . ARG A 1 203 ? 61.982 0.529   31.362 1.00 25.01 ? 203 ARG A CD  1 
ATOM   1026 N  NE  . ARG A 1 203 ? 62.566 -0.302  32.409 1.00 26.12 ? 203 ARG A NE  1 
ATOM   1027 C  CZ  . ARG A 1 203 ? 63.099 -1.500  32.200 1.00 29.70 ? 203 ARG A CZ  1 
ATOM   1028 N  NH1 . ARG A 1 203 ? 63.156 -2.029  30.989 1.00 29.87 ? 203 ARG A NH1 1 
ATOM   1029 N  NH2 . ARG A 1 203 ? 63.590 -2.180  33.228 1.00 30.37 ? 203 ARG A NH2 1 
ATOM   1030 N  N   . ASN A 1 204 ? 63.163 4.942   28.724 1.00 15.53 ? 204 ASN A N   1 
ATOM   1031 C  CA  . ASN A 1 204 ? 62.754 5.533   27.450 1.00 19.45 ? 204 ASN A CA  1 
ATOM   1032 C  C   . ASN A 1 204 ? 62.616 7.028   27.628 1.00 15.21 ? 204 ASN A C   1 
ATOM   1033 O  O   . ASN A 1 204 ? 61.560 7.531   28.040 1.00 14.36 ? 204 ASN A O   1 
ATOM   1034 C  CB  . ASN A 1 204 ? 61.457 4.946   26.898 1.00 26.95 ? 204 ASN A CB  1 
ATOM   1035 C  CG  . ASN A 1 204 ? 61.194 5.399   25.459 1.00 25.22 ? 204 ASN A CG  1 
ATOM   1036 O  OD1 . ASN A 1 204 ? 61.896 6.272   24.931 1.00 25.96 ? 204 ASN A OD1 1 
ATOM   1037 N  ND2 . ASN A 1 204 ? 60.204 4.787   24.806 1.00 26.39 ? 204 ASN A ND2 1 
ATOM   1038 N  N   . PRO A 1 205 ? 63.673 7.782   27.304 1.00 17.49 ? 205 PRO A N   1 
ATOM   1039 C  CA  . PRO A 1 205 ? 63.612 9.248   27.386 1.00 14.65 ? 205 PRO A CA  1 
ATOM   1040 C  C   . PRO A 1 205 ? 62.651 9.877   26.425 1.00 13.45 ? 205 PRO A C   1 
ATOM   1041 O  O   . PRO A 1 205 ? 62.402 11.085  26.546 1.00 17.10 ? 205 PRO A O   1 
ATOM   1042 C  CB  . PRO A 1 205 ? 65.051 9.680   27.051 1.00 17.01 ? 205 PRO A CB  1 
ATOM   1043 C  CG  . PRO A 1 205 ? 65.519 8.557   26.132 1.00 17.78 ? 205 PRO A CG  1 
ATOM   1044 C  CD  . PRO A 1 205 ? 64.971 7.321   26.787 1.00 21.44 ? 205 PRO A CD  1 
ATOM   1045 N  N   . LYS A 1 206 ? 62.092 9.121   25.479 1.00 15.11 ? 206 LYS A N   1 
ATOM   1046 C  CA  . LYS A 1 206 ? 61.105 9.708   24.591 1.00 14.87 ? 206 LYS A CA  1 
ATOM   1047 C  C   . LYS A 1 206 ? 59.759 9.891   25.275 1.00 12.95 ? 206 LYS A C   1 
ATOM   1048 O  O   . LYS A 1 206 ? 58.938 10.655  24.770 1.00 15.60 ? 206 LYS A O   1 
ATOM   1049 C  CB  . LYS A 1 206 ? 60.883 8.838   23.356 1.00 15.99 ? 206 LYS A CB  1 
ATOM   1050 C  CG  . LYS A 1 206 ? 62.158 8.562   22.553 1.00 18.75 ? 206 LYS A CG  1 
ATOM   1051 C  CD  . LYS A 1 206 ? 61.811 7.715   21.333 1.00 22.90 ? 206 LYS A CD  1 
ATOM   1052 C  CE  . LYS A 1 206 ? 63.071 7.257   20.602 1.00 31.12 ? 206 LYS A CE  1 
ATOM   1053 N  NZ  . LYS A 1 206 ? 62.768 6.876   19.181 1.00 43.43 ? 206 LYS A NZ  1 
ATOM   1054 N  N   . ILE A 1 207 ? 59.498 9.187   26.378 1.00 11.44 ? 207 ILE A N   1 
ATOM   1055 C  CA  . ILE A 1 207 ? 58.158 9.263   26.970 1.00 13.32 ? 207 ILE A CA  1 
ATOM   1056 C  C   . ILE A 1 207 ? 58.063 10.522  27.806 1.00 11.21 ? 207 ILE A C   1 
ATOM   1057 O  O   . ILE A 1 207 ? 58.919 10.779  28.664 1.00 13.24 ? 207 ILE A O   1 
ATOM   1058 C  CB  . ILE A 1 207 ? 57.850 8.018   27.812 1.00 11.86 ? 207 ILE A CB  1 
ATOM   1059 C  CG1 . ILE A 1 207 ? 57.856 6.775   26.906 1.00 20.25 ? 207 ILE A CG1 1 
ATOM   1060 C  CG2 . ILE A 1 207 ? 56.465 8.152   28.440 1.00 15.37 ? 207 ILE A CG2 1 
ATOM   1061 C  CD1 . ILE A 1 207 ? 57.551 5.477   27.641 1.00 20.90 ? 207 ILE A CD1 1 
ATOM   1062 N  N   . LEU A 1 208 ? 57.019 11.315  27.565 1.00 10.58 ? 208 LEU A N   1 
ATOM   1063 C  CA  . LEU A 1 208 ? 56.811 12.520  28.360 1.00 9.45  ? 208 LEU A CA  1 
ATOM   1064 C  C   . LEU A 1 208 ? 56.160 12.143  29.683 1.00 10.31 ? 208 LEU A C   1 
ATOM   1065 O  O   . LEU A 1 208 ? 55.296 11.263  29.722 1.00 9.16  ? 208 LEU A O   1 
ATOM   1066 C  CB  . LEU A 1 208 ? 55.913 13.502  27.617 1.00 9.23  ? 208 LEU A CB  1 
ATOM   1067 C  CG  . LEU A 1 208 ? 56.521 14.096  26.335 1.00 10.16 ? 208 LEU A CG  1 
ATOM   1068 C  CD1 . LEU A 1 208 ? 55.483 14.730  25.432 1.00 12.39 ? 208 LEU A CD1 1 
ATOM   1069 C  CD2 . LEU A 1 208 ? 57.598 15.125  26.751 1.00 11.14 ? 208 LEU A CD2 1 
ATOM   1070 N  N   . VAL A 1 209 ? 56.579 12.806  30.759 1.00 8.96  ? 209 VAL A N   1 
ATOM   1071 C  CA  . VAL A 1 209 ? 56.139 12.446  32.113 1.00 8.79  ? 209 VAL A CA  1 
ATOM   1072 C  C   . VAL A 1 209 ? 55.598 13.667  32.835 1.00 8.96  ? 209 VAL A C   1 
ATOM   1073 O  O   . VAL A 1 209 ? 56.305 14.662  33.010 1.00 10.10 ? 209 VAL A O   1 
ATOM   1074 C  CB  . VAL A 1 209 ? 57.273 11.830  32.937 1.00 9.12  ? 209 VAL A CB  1 
ATOM   1075 C  CG1 . VAL A 1 209 ? 56.760 11.463  34.329 1.00 13.59 ? 209 VAL A CG1 1 
ATOM   1076 C  CG2 . VAL A 1 209 ? 57.793 10.576  32.244 1.00 11.72 ? 209 VAL A CG2 1 
ATOM   1077 N  N   . GLU A 1 210 ? 54.362 13.565  33.300 1.00 8.99  ? 210 GLU A N   1 
ATOM   1078 C  CA  . GLU A 1 210 ? 53.751 14.550  34.163 1.00 9.50  ? 210 GLU A CA  1 
ATOM   1079 C  C   . GLU A 1 210 ? 53.555 13.893  35.521 1.00 11.45 ? 210 GLU A C   1 
ATOM   1080 O  O   . GLU A 1 210 ? 53.144 12.734  35.580 1.00 10.80 ? 210 GLU A O   1 
ATOM   1081 C  CB  . GLU A 1 210 ? 52.396 14.989  33.583 1.00 10.50 ? 210 GLU A CB  1 
ATOM   1082 C  CG  . GLU A 1 210 ? 51.571 15.865  34.538 1.00 11.00 ? 210 GLU A CG  1 
ATOM   1083 C  CD  . GLU A 1 210 ? 50.234 16.324  33.923 1.00 16.73 ? 210 GLU A CD  1 
ATOM   1084 O  OE1 . GLU A 1 210 ? 50.147 16.529  32.676 1.00 14.78 ? 210 GLU A OE1 1 
ATOM   1085 O  OE2 . GLU A 1 210 ? 49.252 16.462  34.703 1.00 18.14 ? 210 GLU A OE2 1 
ATOM   1086 N  N   . CYS A 1 211 ? 53.863 14.613  36.597 1.00 9.74  ? 211 CYS A N   1 
ATOM   1087 C  CA  . CYS A 1 211 ? 53.495 14.184  37.943 1.00 8.21  ? 211 CYS A CA  1 
ATOM   1088 C  C   . CYS A 1 211 ? 52.404 15.103  38.445 1.00 10.43 ? 211 CYS A C   1 
ATOM   1089 O  O   . CYS A 1 211 ? 52.590 16.324  38.469 1.00 12.43 ? 211 CYS A O   1 
ATOM   1090 C  CB  . CYS A 1 211 ? 54.681 14.237  38.907 1.00 10.75 ? 211 CYS A CB  1 
ATOM   1091 S  SG  . CYS A 1 211 ? 55.957 13.034  38.484 1.00 15.14 ? 211 CYS A SG  1 
ATOM   1092 N  N   . LEU A 1 212 ? 51.289 14.514  38.850 1.00 10.31 ? 212 LEU A N   1 
ATOM   1093 C  CA  . LEU A 1 212 ? 50.184 15.249  39.443 1.00 8.32  ? 212 LEU A CA  1 
ATOM   1094 C  C   . LEU A 1 212 ? 50.156 14.868  40.917 1.00 10.31 ? 212 LEU A C   1 
ATOM   1095 O  O   . LEU A 1 212 ? 49.852 13.716  41.263 1.00 12.00 ? 212 LEU A O   1 
ATOM   1096 C  CB  . LEU A 1 212 ? 48.880 14.890  38.737 1.00 10.36 ? 212 LEU A CB  1 
ATOM   1097 C  CG  . LEU A 1 212 ? 47.594 15.424  39.381 1.00 11.60 ? 212 LEU A CG  1 
ATOM   1098 C  CD1 . LEU A 1 212 ? 47.601 16.960  39.368 1.00 14.42 ? 212 LEU A CD1 1 
ATOM   1099 C  CD2 . LEU A 1 212 ? 46.372 14.908  38.652 1.00 13.27 ? 212 LEU A CD2 1 
ATOM   1100 N  N   . THR A 1 213 ? 50.507 15.807  41.780 1.00 11.60 ? 213 THR A N   1 
ATOM   1101 C  CA  . THR A 1 213 ? 50.788 15.472  43.169 1.00 12.00 ? 213 THR A CA  1 
ATOM   1102 C  C   . THR A 1 213 ? 49.953 16.293  44.128 1.00 11.47 ? 213 THR A C   1 
ATOM   1103 O  O   . THR A 1 213 ? 49.427 17.359  43.784 1.00 10.21 ? 213 THR A O   1 
ATOM   1104 C  CB  . THR A 1 213 ? 52.271 15.681  43.500 1.00 19.87 ? 213 THR A CB  1 
ATOM   1105 O  OG1 . THR A 1 213 ? 52.608 17.050  43.275 1.00 19.16 ? 213 THR A OG1 1 
ATOM   1106 C  CG2 . THR A 1 213 ? 53.159 14.739  42.687 1.00 25.34 ? 213 THR A CG2 1 
ATOM   1107 N  N   . PRO A 1 214 ? 49.820 15.818  45.341 1.00 13.44 ? 214 PRO A N   1 
ATOM   1108 C  CA  . PRO A 1 214 ? 49.255 16.641  46.402 1.00 11.21 ? 214 PRO A CA  1 
ATOM   1109 C  C   . PRO A 1 214 ? 50.207 17.747  46.819 1.00 13.21 ? 214 PRO A C   1 
ATOM   1110 O  O   . PRO A 1 214 ? 51.288 17.896  46.226 1.00 12.01 ? 214 PRO A O   1 
ATOM   1111 C  CB  . PRO A 1 214 ? 49.042 15.630  47.538 1.00 14.61 ? 214 PRO A CB  1 
ATOM   1112 C  CG  . PRO A 1 214 ? 50.155 14.634  47.328 1.00 19.74 ? 214 PRO A CG  1 
ATOM   1113 C  CD  . PRO A 1 214 ? 50.285 14.498  45.808 1.00 13.13 ? 214 PRO A CD  1 
ATOM   1114 N  N   . ASP A 1 215 ? 49.849 18.507  47.854 1.00 13.24 ? 215 ASP A N   1 
ATOM   1115 C  CA  . ASP A 1 215 ? 50.684 19.658  48.190 1.00 13.56 ? 215 ASP A CA  1 
ATOM   1116 C  C   . ASP A 1 215 ? 51.818 19.321  49.138 1.00 14.33 ? 215 ASP A C   1 
ATOM   1117 O  O   . ASP A 1 215 ? 52.605 20.222  49.464 1.00 17.04 ? 215 ASP A O   1 
ATOM   1118 C  CB  . ASP A 1 215 ? 49.848 20.834  48.760 1.00 15.38 ? 215 ASP A CB  1 
ATOM   1119 C  CG  . ASP A 1 215 ? 49.323 20.606  50.185 1.00 20.82 ? 215 ASP A CG  1 
ATOM   1120 O  OD1 . ASP A 1 215 ? 49.468 19.529  50.769 1.00 19.08 ? 215 ASP A OD1 1 
ATOM   1121 O  OD2 . ASP A 1 215 ? 48.706 21.540  50.716 1.00 21.53 ? 215 ASP A OD2 1 
ATOM   1122 N  N   . PHE A 1 216 ? 51.933 18.058  49.568 1.00 14.02 ? 216 PHE A N   1 
ATOM   1123 C  CA  . PHE A 1 216 ? 53.015 17.620  50.445 1.00 14.36 ? 216 PHE A CA  1 
ATOM   1124 C  C   . PHE A 1 216 ? 53.085 18.454  51.717 1.00 19.01 ? 216 PHE A C   1 
ATOM   1125 O  O   . PHE A 1 216 ? 54.161 18.599  52.309 1.00 18.94 ? 216 PHE A O   1 
ATOM   1126 C  CB  . PHE A 1 216 ? 54.366 17.642  49.715 1.00 12.98 ? 216 PHE A CB  1 
ATOM   1127 C  CG  . PHE A 1 216 ? 54.436 16.701  48.522 1.00 16.88 ? 216 PHE A CG  1 
ATOM   1128 C  CD1 . PHE A 1 216 ? 54.382 15.325  48.697 1.00 15.84 ? 216 PHE A CD1 1 
ATOM   1129 C  CD2 . PHE A 1 216 ? 54.587 17.197  47.231 1.00 18.96 ? 216 PHE A CD2 1 
ATOM   1130 C  CE1 . PHE A 1 216 ? 54.469 14.453  47.598 1.00 17.27 ? 216 PHE A CE1 1 
ATOM   1131 C  CE2 . PHE A 1 216 ? 54.672 16.341  46.127 1.00 20.17 ? 216 PHE A CE2 1 
ATOM   1132 C  CZ  . PHE A 1 216 ? 54.599 14.963  46.311 1.00 15.09 ? 216 PHE A CZ  1 
ATOM   1133 N  N   . ARG A 1 217 ? 51.934 18.993  52.123 1.00 16.64 ? 217 ARG A N   1 
ATOM   1134 C  CA  A ARG A 1 217 ? 51.856 19.874  53.288 0.57 19.06 ? 217 ARG A CA  1 
ATOM   1135 C  CA  B ARG A 1 217 ? 51.803 19.912  53.259 0.43 19.09 ? 217 ARG A CA  1 
ATOM   1136 C  C   . ARG A 1 217 ? 52.779 21.081  53.165 1.00 21.30 ? 217 ARG A C   1 
ATOM   1137 O  O   . ARG A 1 217 ? 53.200 21.651  54.174 1.00 27.26 ? 217 ARG A O   1 
ATOM   1138 C  CB  A ARG A 1 217 ? 52.172 19.107  54.569 0.57 24.42 ? 217 ARG A CB  1 
ATOM   1139 C  CB  B ARG A 1 217 ? 51.956 19.172  54.587 0.43 24.32 ? 217 ARG A CB  1 
ATOM   1140 C  CG  A ARG A 1 217 ? 51.229 17.993  54.808 0.57 27.02 ? 217 ARG A CG  1 
ATOM   1141 C  CG  B ARG A 1 217 ? 50.716 18.399  54.983 0.43 27.47 ? 217 ARG A CG  1 
ATOM   1142 C  CD  A ARG A 1 217 ? 49.830 18.539  54.923 0.57 30.03 ? 217 ARG A CD  1 
ATOM   1143 C  CD  B ARG A 1 217 ? 51.090 17.001  55.413 0.43 31.01 ? 217 ARG A CD  1 
ATOM   1144 N  NE  A ARG A 1 217 ? 48.911 17.472  55.266 0.57 36.46 ? 217 ARG A NE  1 
ATOM   1145 N  NE  B ARG A 1 217 ? 52.416 16.996  56.011 0.43 29.69 ? 217 ARG A NE  1 
ATOM   1146 C  CZ  A ARG A 1 217 ? 48.068 16.913  54.413 0.57 22.46 ? 217 ARG A CZ  1 
ATOM   1147 C  CZ  B ARG A 1 217 ? 53.094 15.903  56.328 0.43 32.53 ? 217 ARG A CZ  1 
ATOM   1148 N  NH1 A ARG A 1 217 ? 47.448 15.786  54.706 0.57 39.71 ? 217 ARG A NH1 1 
ATOM   1149 N  NH1 B ARG A 1 217 ? 54.343 15.967  56.758 0.43 32.92 ? 217 ARG A NH1 1 
ATOM   1150 N  NH2 A ARG A 1 217 ? 47.828 17.511  53.247 0.57 31.00 ? 217 ARG A NH2 1 
ATOM   1151 N  NH2 B ARG A 1 217 ? 52.508 14.716  56.198 0.43 35.70 ? 217 ARG A NH2 1 
ATOM   1152 N  N   . GLY A 1 218 ? 53.112 21.475  51.943 1.00 17.45 ? 218 GLY A N   1 
ATOM   1153 C  CA  . GLY A 1 218 ? 54.012 22.583  51.741 1.00 21.50 ? 218 GLY A CA  1 
ATOM   1154 C  C   . GLY A 1 218 ? 55.462 22.295  52.062 1.00 25.43 ? 218 GLY A C   1 
ATOM   1155 O  O   . GLY A 1 218 ? 56.258 23.237  52.115 1.00 29.95 ? 218 GLY A O   1 
ATOM   1156 N  N   . ASP A 1 219 ? 55.817 21.024  52.282 1.00 19.51 ? 219 ASP A N   1 
ATOM   1157 C  CA  . ASP A 1 219 ? 57.185 20.577  52.572 1.00 21.84 ? 219 ASP A CA  1 
ATOM   1158 C  C   . ASP A 1 219 ? 58.032 20.860  51.343 1.00 18.28 ? 219 ASP A C   1 
ATOM   1159 O  O   . ASP A 1 219 ? 57.959 20.138  50.344 1.00 18.40 ? 219 ASP A O   1 
ATOM   1160 C  CB  . ASP A 1 219 ? 57.172 19.092  52.923 1.00 18.92 ? 219 ASP A CB  1 
ATOM   1161 C  CG  . ASP A 1 219 ? 58.559 18.495  53.200 1.00 26.80 ? 219 ASP A CG  1 
ATOM   1162 O  OD1 . ASP A 1 219 ? 59.598 19.128  52.929 1.00 30.64 ? 219 ASP A OD1 1 
ATOM   1163 O  OD2 . ASP A 1 219 ? 58.589 17.343  53.689 1.00 37.64 ? 219 ASP A OD2 1 
ATOM   1164 N  N   . LEU A 1 220 ? 58.850 21.911  51.418 1.00 20.57 ? 220 LEU A N   1 
ATOM   1165 C  CA  . LEU A 1 220 ? 59.600 22.352  50.248 1.00 20.93 ? 220 LEU A CA  1 
ATOM   1166 C  C   . LEU A 1 220 ? 60.576 21.290  49.767 1.00 19.46 ? 220 LEU A C   1 
ATOM   1167 O  O   . LEU A 1 220 ? 60.864 21.231  48.569 1.00 19.77 ? 220 LEU A O   1 
ATOM   1168 C  CB  . LEU A 1 220 ? 60.350 23.659  50.551 1.00 25.41 ? 220 LEU A CB  1 
ATOM   1169 C  CG  . LEU A 1 220 ? 59.524 24.891  50.943 1.00 28.34 ? 220 LEU A CG  1 
ATOM   1170 C  CD1 . LEU A 1 220 ? 60.445 26.095  51.076 1.00 33.91 ? 220 LEU A CD1 1 
ATOM   1171 C  CD2 . LEU A 1 220 ? 58.385 25.190  49.979 1.00 28.07 ? 220 LEU A CD2 1 
ATOM   1172 N  N   . LYS A 1 221 ? 61.096 20.449  50.670 1.00 19.50 ? 221 LYS A N   1 
ATOM   1173 C  CA  A LYS A 1 221 ? 62.061 19.430  50.264 0.50 21.02 ? 221 LYS A CA  1 
ATOM   1174 C  CA  B LYS A 1 221 ? 62.064 19.437  50.255 0.50 21.02 ? 221 LYS A CA  1 
ATOM   1175 C  C   . LYS A 1 221 ? 61.387 18.307  49.491 1.00 21.92 ? 221 LYS A C   1 
ATOM   1176 O  O   . LYS A 1 221 ? 61.976 17.747  48.558 1.00 21.17 ? 221 LYS A O   1 
ATOM   1177 C  CB  A LYS A 1 221 ? 62.782 18.868  51.487 0.50 24.44 ? 221 LYS A CB  1 
ATOM   1178 C  CB  B LYS A 1 221 ? 62.817 18.880  51.464 0.50 24.45 ? 221 LYS A CB  1 
ATOM   1179 C  CG  A LYS A 1 221 ? 63.617 19.892  52.232 0.50 28.84 ? 221 LYS A CG  1 
ATOM   1180 C  CG  B LYS A 1 221 ? 63.681 19.897  52.215 0.50 28.80 ? 221 LYS A CG  1 
ATOM   1181 C  CD  A LYS A 1 221 ? 64.525 20.642  51.280 0.50 29.99 ? 221 LYS A CD  1 
ATOM   1182 C  CD  B LYS A 1 221 ? 64.661 20.627  51.306 0.50 30.07 ? 221 LYS A CD  1 
ATOM   1183 C  CE  A LYS A 1 221 ? 65.978 20.277  51.508 0.50 36.02 ? 221 LYS A CE  1 
ATOM   1184 C  CE  B LYS A 1 221 ? 65.891 19.785  50.971 0.50 33.83 ? 221 LYS A CE  1 
ATOM   1185 N  NZ  A LYS A 1 221 ? 66.401 20.662  52.876 0.50 32.40 ? 221 LYS A NZ  1 
ATOM   1186 N  NZ  B LYS A 1 221 ? 66.911 20.579  50.208 0.50 32.70 ? 221 LYS A NZ  1 
ATOM   1187 N  N   . ALA A 1 222 ? 60.155 17.962  49.871 1.00 17.45 ? 222 ALA A N   1 
ATOM   1188 C  CA  . ALA A 1 222 ? 59.389 16.955  49.130 1.00 16.37 ? 222 ALA A CA  1 
ATOM   1189 C  C   . ALA A 1 222 ? 59.051 17.462  47.737 1.00 16.92 ? 222 ALA A C   1 
ATOM   1190 O  O   . ALA A 1 222 ? 59.236 16.753  46.739 1.00 15.35 ? 222 ALA A O   1 
ATOM   1191 C  CB  . ALA A 1 222 ? 58.112 16.602  49.894 1.00 19.88 ? 222 ALA A CB  1 
ATOM   1192 N  N   . ILE A 1 223 ? 58.577 18.704  47.656 1.00 15.06 ? 223 ILE A N   1 
ATOM   1193 C  CA  . ILE A 1 223 ? 58.289 19.319  46.359 1.00 15.04 ? 223 ILE A CA  1 
ATOM   1194 C  C   . ILE A 1 223 ? 59.539 19.322  45.491 1.00 14.26 ? 223 ILE A C   1 
ATOM   1195 O  O   . ILE A 1 223 ? 59.498 18.966  44.308 1.00 14.89 ? 223 ILE A O   1 
ATOM   1196 C  CB  . ILE A 1 223 ? 57.747 20.740  46.565 1.00 13.25 ? 223 ILE A CB  1 
ATOM   1197 C  CG1 . ILE A 1 223 ? 56.395 20.678  47.297 1.00 16.77 ? 223 ILE A CG1 1 
ATOM   1198 C  CG2 . ILE A 1 223 ? 57.654 21.525  45.224 1.00 17.77 ? 223 ILE A CG2 1 
ATOM   1199 C  CD1 . ILE A 1 223 ? 55.980 21.980  47.995 1.00 16.74 ? 223 ILE A CD1 1 
ATOM   1200 N  N   . GLU A 1 224 ? 60.678 19.714  46.084 1.00 14.11 ? 224 GLU A N   1 
ATOM   1201 C  CA  . GLU A 1 224 ? 61.947 19.740  45.356 1.00 14.51 ? 224 GLU A CA  1 
ATOM   1202 C  C   . GLU A 1 224 ? 62.326 18.356  44.843 1.00 15.28 ? 224 GLU A C   1 
ATOM   1203 O  O   . GLU A 1 224 ? 62.798 18.221  43.712 1.00 17.65 ? 224 GLU A O   1 
ATOM   1204 C  CB  . GLU A 1 224 ? 63.049 20.305  46.266 1.00 18.67 ? 224 GLU A CB  1 
ATOM   1205 C  CG  . GLU A 1 224 ? 64.442 20.270  45.668 1.00 23.90 ? 224 GLU A CG  1 
ATOM   1206 C  CD  . GLU A 1 224 ? 65.517 20.717  46.669 1.00 33.44 ? 224 GLU A CD  1 
ATOM   1207 O  OE1 . GLU A 1 224 ? 65.201 20.848  47.869 1.00 32.81 ? 224 GLU A OE1 1 
ATOM   1208 O  OE2 . GLU A 1 224 ? 66.679 20.922  46.256 1.00 37.26 ? 224 GLU A OE2 1 
ATOM   1209 N  N   . LYS A 1 225 ? 62.100 17.310  45.642 1.00 15.61 ? 225 LYS A N   1 
ATOM   1210 C  CA  . LYS A 1 225 ? 62.434 15.959  45.205 1.00 13.49 ? 225 LYS A CA  1 
ATOM   1211 C  C   . LYS A 1 225 ? 61.683 15.584  43.925 1.00 15.20 ? 225 LYS A C   1 
ATOM   1212 O  O   . LYS A 1 225 ? 62.258 15.004  42.993 1.00 16.62 ? 225 LYS A O   1 
ATOM   1213 C  CB  . LYS A 1 225 ? 62.133 14.963  46.329 1.00 18.34 ? 225 LYS A CB  1 
ATOM   1214 C  CG  . LYS A 1 225 ? 62.480 13.524  46.026 1.00 26.89 ? 225 LYS A CG  1 
ATOM   1215 C  CD  . LYS A 1 225 ? 63.983 13.271  45.985 1.00 35.51 ? 225 LYS A CD  1 
ATOM   1216 C  CE  . LYS A 1 225 ? 64.609 13.331  47.383 1.00 37.18 ? 225 LYS A CE  1 
ATOM   1217 N  NZ  . LYS A 1 225 ? 64.227 12.180  48.264 1.00 43.03 ? 225 LYS A NZ  1 
ATOM   1218 N  N   . VAL A 1 226 ? 60.391 15.888  43.877 1.00 13.37 ? 226 VAL A N   1 
ATOM   1219 C  CA  . VAL A 1 226 ? 59.615 15.604  42.672 1.00 12.41 ? 226 VAL A CA  1 
ATOM   1220 C  C   . VAL A 1 226 ? 60.049 16.509  41.526 1.00 11.74 ? 226 VAL A C   1 
ATOM   1221 O  O   . VAL A 1 226 ? 60.209 16.060  40.383 1.00 13.62 ? 226 VAL A O   1 
ATOM   1222 C  CB  . VAL A 1 226 ? 58.120 15.752  42.969 1.00 11.73 ? 226 VAL A CB  1 
ATOM   1223 C  CG1 . VAL A 1 226 ? 57.304 15.448  41.699 1.00 13.31 ? 226 VAL A CG1 1 
ATOM   1224 C  CG2 . VAL A 1 226 ? 57.749 14.776  44.069 1.00 14.84 ? 226 VAL A CG2 1 
ATOM   1225 N  N   . ALA A 1 227 ? 60.218 17.801  41.800 1.00 11.28 ? 227 ALA A N   1 
ATOM   1226 C  CA  . ALA A 1 227 ? 60.541 18.727  40.716 1.00 13.82 ? 227 ALA A CA  1 
ATOM   1227 C  C   . ALA A 1 227 ? 61.919 18.487  40.117 1.00 14.30 ? 227 ALA A C   1 
ATOM   1228 O  O   . ALA A 1 227 ? 62.134 18.870  38.957 1.00 16.03 ? 227 ALA A O   1 
ATOM   1229 C  CB  . ALA A 1 227 ? 60.428 20.193  41.175 1.00 13.32 ? 227 ALA A CB  1 
ATOM   1230 N  N   . LEU A 1 228 ? 62.842 17.872  40.858 1.00 13.45 ? 228 LEU A N   1 
ATOM   1231 C  CA  . LEU A 1 228 ? 64.177 17.573  40.340 1.00 13.53 ? 228 LEU A CA  1 
ATOM   1232 C  C   . LEU A 1 228 ? 64.285 16.170  39.753 1.00 13.53 ? 228 LEU A C   1 
ATOM   1233 O  O   . LEU A 1 228 ? 65.388 15.737  39.377 1.00 16.74 ? 228 LEU A O   1 
ATOM   1234 C  CB  . LEU A 1 228 ? 65.222 17.747  41.450 1.00 19.78 ? 228 LEU A CB  1 
ATOM   1235 C  CG  . LEU A 1 228 ? 65.512 19.204  41.831 1.00 24.55 ? 228 LEU A CG  1 
ATOM   1236 C  CD1 . LEU A 1 228 ? 66.566 19.256  42.946 1.00 22.61 ? 228 LEU A CD1 1 
ATOM   1237 C  CD2 . LEU A 1 228 ? 65.970 20.000  40.631 1.00 24.63 ? 228 LEU A CD2 1 
ATOM   1238 N  N   . SER A 1 229 ? 63.164 15.454  39.648 1.00 13.12 ? 229 SER A N   1 
ATOM   1239 C  CA  . SER A 1 229 ? 63.192 14.039  39.305 1.00 13.03 ? 229 SER A CA  1 
ATOM   1240 C  C   . SER A 1 229 ? 63.456 13.769  37.832 1.00 14.10 ? 229 SER A C   1 
ATOM   1241 O  O   . SER A 1 229 ? 63.692 12.609  37.485 1.00 15.85 ? 229 SER A O   1 
ATOM   1242 C  CB  . SER A 1 229 ? 61.865 13.387  39.687 1.00 13.16 ? 229 SER A CB  1 
ATOM   1243 O  OG  . SER A 1 229 ? 60.823 13.942  38.879 1.00 13.83 ? 229 SER A OG  1 
ATOM   1244 N  N   . GLY A 1 230 ? 63.387 14.786  36.955 1.00 10.71 ? 230 GLY A N   1 
ATOM   1245 C  CA  . GLY A 1 230 ? 63.496 14.579  35.528 1.00 10.94 ? 230 GLY A CA  1 
ATOM   1246 C  C   . GLY A 1 230 ? 62.175 14.616  34.789 1.00 12.03 ? 230 GLY A C   1 
ATOM   1247 O  O   . GLY A 1 230 ? 62.135 14.303  33.583 1.00 11.54 ? 230 GLY A O   1 
ATOM   1248 N  N   . LEU A 1 231 ? 61.089 14.926  35.487 1.00 10.30 ? 231 LEU A N   1 
ATOM   1249 C  CA  . LEU A 1 231 ? 59.786 15.018  34.846 1.00 9.31  ? 231 LEU A CA  1 
ATOM   1250 C  C   . LEU A 1 231 ? 59.747 16.187  33.865 1.00 10.30 ? 231 LEU A C   1 
ATOM   1251 O  O   . LEU A 1 231 ? 60.554 17.126  33.930 1.00 11.83 ? 231 LEU A O   1 
ATOM   1252 C  CB  . LEU A 1 231 ? 58.677 15.156  35.908 1.00 10.29 ? 231 LEU A CB  1 
ATOM   1253 C  CG  . LEU A 1 231 ? 58.547 16.515  36.614 1.00 9.88  ? 231 LEU A CG  1 
ATOM   1254 C  CD1 . LEU A 1 231 ? 57.478 16.433  37.703 1.00 11.54 ? 231 LEU A CD1 1 
ATOM   1255 C  CD2 . LEU A 1 231 ? 59.871 17.135  37.166 1.00 11.33 ? 231 LEU A CD2 1 
ATOM   1256 N  N   . ASP A 1 232 ? 58.782 16.118  32.947 1.00 9.41  ? 232 ASP A N   1 
ATOM   1257 C  CA  . ASP A 1 232 ? 58.554 17.231  32.028 1.00 8.90  ? 232 ASP A CA  1 
ATOM   1258 C  C   . ASP A 1 232 ? 57.574 18.260  32.572 1.00 9.55  ? 232 ASP A C   1 
ATOM   1259 O  O   . ASP A 1 232 ? 57.737 19.471  32.335 1.00 10.07 ? 232 ASP A O   1 
ATOM   1260 C  CB  . ASP A 1 232 ? 58.038 16.693  30.700 1.00 9.52  ? 232 ASP A CB  1 
ATOM   1261 C  CG  . ASP A 1 232 ? 59.004 15.725  30.083 1.00 11.30 ? 232 ASP A CG  1 
ATOM   1262 O  OD1 . ASP A 1 232 ? 60.021 16.198  29.492 1.00 11.33 ? 232 ASP A OD1 1 
ATOM   1263 O  OD2 . ASP A 1 232 ? 58.791 14.502  30.212 1.00 9.91  ? 232 ASP A OD2 1 
ATOM   1264 N  N   . VAL A 1 233 ? 56.537 17.796  33.277 1.00 8.27  ? 233 VAL A N   1 
ATOM   1265 C  CA  . VAL A 1 233 ? 55.423 18.627  33.701 1.00 7.99  ? 233 VAL A CA  1 
ATOM   1266 C  C   . VAL A 1 233 ? 55.168 18.369  35.168 1.00 7.93  ? 233 VAL A C   1 
ATOM   1267 O  O   . VAL A 1 233 ? 54.998 17.210  35.570 1.00 8.30  ? 233 VAL A O   1 
ATOM   1268 C  CB  . VAL A 1 233 ? 54.158 18.309  32.878 1.00 7.74  ? 233 VAL A CB  1 
ATOM   1269 C  CG1 . VAL A 1 233 ? 52.973 19.194  33.356 1.00 8.01  ? 233 VAL A CG1 1 
ATOM   1270 C  CG2 . VAL A 1 233 ? 54.446 18.566  31.399 1.00 8.84  ? 233 VAL A CG2 1 
ATOM   1271 N  N   . TYR A 1 234 ? 55.126 19.454  35.964 1.00 8.00  ? 234 TYR A N   1 
ATOM   1272 C  CA  . TYR A 1 234 ? 54.789 19.395  37.381 1.00 8.01  ? 234 TYR A CA  1 
ATOM   1273 C  C   . TYR A 1 234 ? 53.370 19.935  37.510 1.00 8.87  ? 234 TYR A C   1 
ATOM   1274 O  O   . TYR A 1 234 ? 53.135 21.143  37.353 1.00 7.87  ? 234 TYR A O   1 
ATOM   1275 C  CB  . TYR A 1 234 ? 55.783 20.221  38.223 1.00 8.49  ? 234 TYR A CB  1 
ATOM   1276 C  CG  . TYR A 1 234 ? 55.641 19.977  39.707 1.00 9.05  ? 234 TYR A CG  1 
ATOM   1277 C  CD1 . TYR A 1 234 ? 56.672 19.367  40.425 1.00 11.14 ? 234 TYR A CD1 1 
ATOM   1278 C  CD2 . TYR A 1 234 ? 54.502 20.377  40.392 1.00 11.75 ? 234 TYR A CD2 1 
ATOM   1279 C  CE1 . TYR A 1 234 ? 56.550 19.127  41.778 1.00 11.71 ? 234 TYR A CE1 1 
ATOM   1280 C  CE2 . TYR A 1 234 ? 54.351 20.112  41.748 1.00 14.01 ? 234 TYR A CE2 1 
ATOM   1281 C  CZ  . TYR A 1 234 ? 55.375 19.502  42.427 1.00 14.81 ? 234 TYR A CZ  1 
ATOM   1282 O  OH  . TYR A 1 234 ? 55.214 19.263  43.784 1.00 16.50 ? 234 TYR A OH  1 
ATOM   1283 N  N   . ALA A 1 235 ? 52.427 19.058  37.814 1.00 7.97  ? 235 ALA A N   1 
ATOM   1284 C  CA  . ALA A 1 235 ? 51.035 19.461  37.975 1.00 8.52  ? 235 ALA A CA  1 
ATOM   1285 C  C   . ALA A 1 235 ? 50.600 19.374  39.432 1.00 8.66  ? 235 ALA A C   1 
ATOM   1286 O  O   . ALA A 1 235 ? 50.920 18.414  40.134 1.00 9.32  ? 235 ALA A O   1 
ATOM   1287 C  CB  . ALA A 1 235 ? 50.120 18.588  37.099 1.00 9.85  ? 235 ALA A CB  1 
ATOM   1288 N  N   . HIS A 1 236 ? 49.832 20.375  39.865 1.00 7.60  ? 236 HIS A N   1 
ATOM   1289 C  CA  . HIS A 1 236 ? 49.287 20.369  41.210 1.00 7.66  ? 236 HIS A CA  1 
ATOM   1290 C  C   . HIS A 1 236 ? 48.017 21.195  41.139 1.00 8.95  ? 236 HIS A C   1 
ATOM   1291 O  O   . HIS A 1 236 ? 48.075 22.356  40.725 1.00 9.56  ? 236 HIS A O   1 
ATOM   1292 C  CB  . HIS A 1 236 ? 50.272 20.956  42.239 1.00 8.65  ? 236 HIS A CB  1 
ATOM   1293 C  CG  . HIS A 1 236 ? 49.633 21.165  43.565 1.00 10.75 ? 236 HIS A CG  1 
ATOM   1294 N  ND1 . HIS A 1 236 ? 49.211 20.116  44.355 1.00 13.39 ? 236 HIS A ND1 1 
ATOM   1295 C  CD2 . HIS A 1 236 ? 49.195 22.295  44.170 1.00 12.85 ? 236 HIS A CD2 1 
ATOM   1296 C  CE1 . HIS A 1 236 ? 48.587 20.598  45.417 1.00 15.79 ? 236 HIS A CE1 1 
ATOM   1297 N  NE2 . HIS A 1 236 ? 48.556 21.914  45.323 1.00 13.69 ? 236 HIS A NE2 1 
ATOM   1298 N  N   . ASN A 1 237 ? 46.881 20.607  41.540 1.00 9.09  ? 237 ASN A N   1 
ATOM   1299 C  CA  . ASN A 1 237 ? 45.573 21.201  41.252 1.00 9.27  ? 237 ASN A CA  1 
ATOM   1300 C  C   . ASN A 1 237 ? 45.087 22.131  42.359 1.00 11.36 ? 237 ASN A C   1 
ATOM   1301 O  O   . ASN A 1 237 ? 45.031 21.734  43.521 1.00 13.41 ? 237 ASN A O   1 
ATOM   1302 C  CB  . ASN A 1 237 ? 44.552 20.082  41.041 1.00 9.77  ? 237 ASN A CB  1 
ATOM   1303 C  CG  . ASN A 1 237 ? 44.750 19.401  39.722 1.00 12.04 ? 237 ASN A CG  1 
ATOM   1304 O  OD1 . ASN A 1 237 ? 45.515 19.872  38.904 1.00 13.32 ? 237 ASN A OD1 1 
ATOM   1305 N  ND2 . ASN A 1 237 ? 44.023 18.306  39.496 1.00 16.58 ? 237 ASN A ND2 1 
ATOM   1306 N  N   . VAL A 1 238 ? 44.664 23.341  41.983 1.00 10.03 ? 238 VAL A N   1 
ATOM   1307 C  CA  . VAL A 1 238 ? 43.996 24.246  42.934 1.00 9.21  ? 238 VAL A CA  1 
ATOM   1308 C  C   . VAL A 1 238 ? 42.515 23.918  43.082 1.00 9.79  ? 238 VAL A C   1 
ATOM   1309 O  O   . VAL A 1 238 ? 41.902 24.292  44.085 1.00 10.97 ? 238 VAL A O   1 
ATOM   1310 C  CB  . VAL A 1 238 ? 44.165 25.714  42.503 1.00 11.87 ? 238 VAL A CB  1 
ATOM   1311 C  CG1 . VAL A 1 238 ? 45.632 26.105  42.519 1.00 14.80 ? 238 VAL A CG1 1 
ATOM   1312 C  CG2 . VAL A 1 238 ? 43.576 25.945  41.121 1.00 14.30 ? 238 VAL A CG2 1 
ATOM   1313 N  N   . GLU A 1 239 ? 41.921 23.242  42.088 1.00 9.51  ? 239 GLU A N   1 
ATOM   1314 C  CA  . GLU A 1 239 ? 40.571 22.685  42.100 1.00 10.52 ? 239 GLU A CA  1 
ATOM   1315 C  C   . GLU A 1 239 ? 39.449 23.723  42.046 1.00 10.90 ? 239 GLU A C   1 
ATOM   1316 O  O   . GLU A 1 239 ? 38.459 23.486  41.341 1.00 11.16 ? 239 GLU A O   1 
ATOM   1317 C  CB  . GLU A 1 239 ? 40.312 21.798  43.330 1.00 14.07 ? 239 GLU A CB  1 
ATOM   1318 C  CG  . GLU A 1 239 ? 41.282 20.605  43.461 1.00 15.05 ? 239 GLU A CG  1 
ATOM   1319 C  CD  . GLU A 1 239 ? 41.128 19.526  42.377 1.00 23.35 ? 239 GLU A CD  1 
ATOM   1320 O  OE1 . GLU A 1 239 ? 40.375 19.699  41.394 1.00 26.89 ? 239 GLU A OE1 1 
ATOM   1321 O  OE2 . GLU A 1 239 ? 41.826 18.490  42.492 1.00 24.63 ? 239 GLU A OE2 1 
ATOM   1322 N  N   . THR A 1 240 ? 39.534 24.820  42.809 1.00 9.12  ? 240 THR A N   1 
ATOM   1323 C  CA  . THR A 1 240 ? 38.458 25.812  42.757 1.00 10.32 ? 240 THR A CA  1 
ATOM   1324 C  C   . THR A 1 240 ? 39.021 27.194  43.090 1.00 8.96  ? 240 THR A C   1 
ATOM   1325 O  O   . THR A 1 240 ? 40.203 27.362  43.406 1.00 12.38 ? 240 THR A O   1 
ATOM   1326 C  CB  . THR A 1 240 ? 37.277 25.445  43.685 1.00 12.02 ? 240 THR A CB  1 
ATOM   1327 O  OG1 . THR A 1 240 ? 36.169 26.319  43.423 1.00 12.48 ? 240 THR A OG1 1 
ATOM   1328 C  CG2 . THR A 1 240 ? 37.666 25.575  45.161 1.00 12.83 ? 240 THR A CG2 1 
ATOM   1329 N  N   . VAL A 1 241 ? 38.151 28.189  43.021 1.00 12.58 ? 241 VAL A N   1 
ATOM   1330 C  CA  . VAL A 1 241 ? 38.558 29.573  43.253 1.00 12.07 ? 241 VAL A CA  1 
ATOM   1331 C  C   . VAL A 1 241 ? 38.801 29.799  44.742 1.00 13.37 ? 241 VAL A C   1 
ATOM   1332 O  O   . VAL A 1 241 ? 38.304 29.034  45.586 1.00 13.46 ? 241 VAL A O   1 
ATOM   1333 C  CB  . VAL A 1 241 ? 37.510 30.552  42.684 1.00 12.17 ? 241 VAL A CB  1 
ATOM   1334 C  CG1 . VAL A 1 241 ? 37.277 30.264  41.183 1.00 13.09 ? 241 VAL A CG1 1 
ATOM   1335 C  CG2 . VAL A 1 241 ? 36.188 30.483  43.481 1.00 13.75 ? 241 VAL A CG2 1 
ATOM   1336 N  N   . PRO A 1 242 ? 39.547 30.839  45.119 1.00 15.44 ? 242 PRO A N   1 
ATOM   1337 C  CA  . PRO A 1 242 ? 39.870 30.999  46.552 1.00 18.50 ? 242 PRO A CA  1 
ATOM   1338 C  C   . PRO A 1 242 ? 38.649 31.071  47.458 1.00 15.43 ? 242 PRO A C   1 
ATOM   1339 O  O   . PRO A 1 242 ? 38.640 30.463  48.529 1.00 18.47 ? 242 PRO A O   1 
ATOM   1340 C  CB  . PRO A 1 242 ? 40.683 32.299  46.571 1.00 17.27 ? 242 PRO A CB  1 
ATOM   1341 C  CG  . PRO A 1 242 ? 41.340 32.334  45.233 1.00 16.87 ? 242 PRO A CG  1 
ATOM   1342 C  CD  . PRO A 1 242 ? 40.347 31.739  44.264 1.00 15.36 ? 242 PRO A CD  1 
ATOM   1343 N  N   . GLU A 1 243 ? 37.581 31.735  47.015 1.00 15.69 ? 243 GLU A N   1 
ATOM   1344 C  CA  . GLU A 1 243 ? 36.404 31.926  47.849 1.00 18.23 ? 243 GLU A CA  1 
ATOM   1345 C  C   . GLU A 1 243 ? 35.674 30.620  48.152 1.00 18.49 ? 243 GLU A C   1 
ATOM   1346 O  O   . GLU A 1 243 ? 34.878 30.579  49.104 1.00 20.54 ? 243 GLU A O   1 
ATOM   1347 C  CB  . GLU A 1 243 ? 35.462 32.921  47.159 1.00 21.28 ? 243 GLU A CB  1 
ATOM   1348 C  CG  . GLU A 1 243 ? 36.040 34.344  47.030 1.00 32.42 ? 243 GLU A CG  1 
ATOM   1349 C  CD  . GLU A 1 243 ? 36.932 34.577  45.783 1.00 32.44 ? 243 GLU A CD  1 
ATOM   1350 O  OE1 . GLU A 1 243 ? 37.333 33.620  45.059 1.00 23.22 ? 243 GLU A OE1 1 
ATOM   1351 O  OE2 . GLU A 1 243 ? 37.224 35.758  45.517 1.00 38.11 ? 243 GLU A OE2 1 
ATOM   1352 N  N   . LEU A 1 244 ? 35.937 29.541  47.394 1.00 13.94 ? 244 LEU A N   1 
ATOM   1353 C  CA  . LEU A 1 244 ? 35.261 28.262  47.604 1.00 14.03 ? 244 LEU A CA  1 
ATOM   1354 C  C   . LEU A 1 244 ? 36.168 27.183  48.184 1.00 14.01 ? 244 LEU A C   1 
ATOM   1355 O  O   . LEU A 1 244 ? 35.719 26.045  48.344 1.00 13.80 ? 244 LEU A O   1 
ATOM   1356 C  CB  . LEU A 1 244 ? 34.651 27.755  46.289 1.00 15.91 ? 244 LEU A CB  1 
ATOM   1357 C  CG  . LEU A 1 244 ? 33.467 28.563  45.768 1.00 17.21 ? 244 LEU A CG  1 
ATOM   1358 C  CD1 . LEU A 1 244 ? 32.937 27.959  44.495 1.00 19.79 ? 244 LEU A CD1 1 
ATOM   1359 C  CD2 . LEU A 1 244 ? 32.384 28.652  46.822 1.00 25.51 ? 244 LEU A CD2 1 
ATOM   1360 N  N   . GLN A 1 245 ? 37.416 27.515  48.520 1.00 13.97 ? 245 GLN A N   1 
ATOM   1361 C  CA  . GLN A 1 245 ? 38.361 26.505  48.996 1.00 13.29 ? 245 GLN A CA  1 
ATOM   1362 C  C   . GLN A 1 245 ? 37.830 25.799  50.248 1.00 11.94 ? 245 GLN A C   1 
ATOM   1363 O  O   . GLN A 1 245 ? 37.871 24.566  50.335 1.00 17.00 ? 245 GLN A O   1 
ATOM   1364 C  CB  . GLN A 1 245 ? 39.723 27.151  49.254 1.00 15.82 ? 245 GLN A CB  1 
ATOM   1365 C  CG  . GLN A 1 245 ? 40.469 27.654  48.000 1.00 16.18 ? 245 GLN A CG  1 
ATOM   1366 C  CD  . GLN A 1 245 ? 41.268 26.547  47.348 1.00 14.51 ? 245 GLN A CD  1 
ATOM   1367 O  OE1 . GLN A 1 245 ? 41.939 25.785  48.039 1.00 16.66 ? 245 GLN A OE1 1 
ATOM   1368 N  NE2 . GLN A 1 245 ? 41.211 26.449  46.017 1.00 13.50 ? 245 GLN A NE2 1 
ATOM   1369 N  N   . SER A 1 246 ? 37.271 26.548  51.202 1.00 14.71 ? 246 SER A N   1 
ATOM   1370 C  CA  . SER A 1 246 ? 36.845 25.889  52.443 1.00 15.20 ? 246 SER A CA  1 
ATOM   1371 C  C   . SER A 1 246 ? 35.610 25.010  52.233 1.00 20.74 ? 246 SER A C   1 
ATOM   1372 O  O   . SER A 1 246 ? 35.477 23.951  52.868 1.00 20.85 ? 246 SER A O   1 
ATOM   1373 C  CB  . SER A 1 246 ? 36.600 26.940  53.533 1.00 24.27 ? 246 SER A CB  1 
ATOM   1374 O  OG  . SER A 1 246 ? 35.411 27.674  53.276 1.00 32.38 ? 246 SER A OG  1 
ATOM   1375 N  N   . LYS A 1 247 ? 34.708 25.411  51.332 1.00 15.06 ? 247 LYS A N   1 
ATOM   1376 C  CA  . LYS A 1 247 ? 33.559 24.581  51.010 1.00 18.17 ? 247 LYS A CA  1 
ATOM   1377 C  C   . LYS A 1 247 ? 33.986 23.314  50.282 1.00 17.19 ? 247 LYS A C   1 
ATOM   1378 O  O   . LYS A 1 247 ? 33.442 22.238  50.527 1.00 16.91 ? 247 LYS A O   1 
ATOM   1379 C  CB  . LYS A 1 247 ? 32.557 25.382  50.168 1.00 23.47 ? 247 LYS A CB  1 
ATOM   1380 C  CG  . LYS A 1 247 ? 31.381 24.568  49.591 1.00 25.76 ? 247 LYS A CG  1 
ATOM   1381 C  CD  . LYS A 1 247 ? 30.496 25.381  48.638 1.00 33.42 ? 247 LYS A CD  1 
ATOM   1382 C  CE  . LYS A 1 247 ? 29.822 24.477  47.591 1.00 38.33 ? 247 LYS A CE  1 
ATOM   1383 N  NZ  . LYS A 1 247 ? 28.925 25.181  46.595 1.00 37.33 ? 247 LYS A NZ  1 
ATOM   1384 N  N   . VAL A 1 248 ? 34.966 23.410  49.388 1.00 11.07 ? 248 VAL A N   1 
ATOM   1385 C  CA  . VAL A 1 248 ? 35.249 22.319  48.456 1.00 12.27 ? 248 VAL A CA  1 
ATOM   1386 C  C   . VAL A 1 248 ? 36.397 21.431  48.937 1.00 11.42 ? 248 VAL A C   1 
ATOM   1387 O  O   . VAL A 1 248 ? 36.297 20.207  48.904 1.00 12.60 ? 248 VAL A O   1 
ATOM   1388 C  CB  . VAL A 1 248 ? 35.531 22.902  47.051 1.00 14.41 ? 248 VAL A CB  1 
ATOM   1389 C  CG1 . VAL A 1 248 ? 35.970 21.805  46.072 1.00 14.97 ? 248 VAL A CG1 1 
ATOM   1390 C  CG2 . VAL A 1 248 ? 34.268 23.602  46.524 1.00 12.34 ? 248 VAL A CG2 1 
ATOM   1391 N  N   . ARG A 1 249 ? 37.521 22.037  49.313 1.00 12.38 ? 249 ARG A N   1 
ATOM   1392 C  CA  . ARG A 1 249 ? 38.754 21.314  49.589 1.00 14.10 ? 249 ARG A CA  1 
ATOM   1393 C  C   . ARG A 1 249 ? 38.898 21.100  51.084 1.00 14.06 ? 249 ARG A C   1 
ATOM   1394 O  O   . ARG A 1 249 ? 38.317 21.820  51.898 1.00 16.03 ? 249 ARG A O   1 
ATOM   1395 C  CB  . ARG A 1 249 ? 39.985 22.074  49.067 1.00 12.94 ? 249 ARG A CB  1 
ATOM   1396 C  CG  . ARG A 1 249 ? 39.938 22.285  47.569 1.00 13.41 ? 249 ARG A CG  1 
ATOM   1397 C  CD  . ARG A 1 249 ? 41.219 23.045  47.156 1.00 15.44 ? 249 ARG A CD  1 
ATOM   1398 N  NE  . ARG A 1 249 ? 42.395 22.202  47.083 1.00 14.78 ? 249 ARG A NE  1 
ATOM   1399 C  CZ  . ARG A 1 249 ? 43.642 22.651  47.008 1.00 12.86 ? 249 ARG A CZ  1 
ATOM   1400 N  NH1 . ARG A 1 249 ? 43.918 23.943  47.093 1.00 14.58 ? 249 ARG A NH1 1 
ATOM   1401 N  NH2 . ARG A 1 249 ? 44.638 21.778  46.902 1.00 20.26 ? 249 ARG A NH2 1 
ATOM   1402 N  N   . ASP A 1 250 ? 39.682 20.094  51.431 1.00 13.57 ? 250 ASP A N   1 
ATOM   1403 C  CA  . ASP A 1 250 ? 39.880 19.855  52.852 1.00 15.62 ? 250 ASP A CA  1 
ATOM   1404 C  C   . ASP A 1 250 ? 40.618 21.030  53.479 1.00 14.94 ? 250 ASP A C   1 
ATOM   1405 O  O   . ASP A 1 250 ? 41.489 21.614  52.846 1.00 14.73 ? 250 ASP A O   1 
ATOM   1406 C  CB  . ASP A 1 250 ? 40.667 18.592  53.109 1.00 21.86 ? 250 ASP A CB  1 
ATOM   1407 C  CG  . ASP A 1 250 ? 40.651 18.251  54.578 1.00 24.80 ? 250 ASP A CG  1 
ATOM   1408 O  OD1 . ASP A 1 250 ? 39.626 17.693  55.040 1.00 26.33 ? 250 ASP A OD1 1 
ATOM   1409 O  OD2 . ASP A 1 250 ? 41.622 18.623  55.265 1.00 21.37 ? 250 ASP A OD2 1 
ATOM   1410 N  N   . PRO A 1 251 ? 40.293 21.410  54.726 1.00 15.26 ? 251 PRO A N   1 
ATOM   1411 C  CA  . PRO A 1 251 ? 40.968 22.570  55.331 1.00 16.47 ? 251 PRO A CA  1 
ATOM   1412 C  C   . PRO A 1 251 ? 42.478 22.400  55.502 1.00 16.09 ? 251 PRO A C   1 
ATOM   1413 O  O   . PRO A 1 251 ? 43.152 23.400  55.778 1.00 20.23 ? 251 PRO A O   1 
ATOM   1414 C  CB  . PRO A 1 251 ? 40.248 22.732  56.685 1.00 25.17 ? 251 PRO A CB  1 
ATOM   1415 C  CG  . PRO A 1 251 ? 38.888 22.113  56.438 1.00 29.18 ? 251 PRO A CG  1 
ATOM   1416 C  CD  . PRO A 1 251 ? 39.162 20.939  55.543 1.00 21.35 ? 251 PRO A CD  1 
ATOM   1417 N  N   . ARG A 1 252 ? 43.038 21.196  55.326 1.00 16.39 ? 252 ARG A N   1 
ATOM   1418 C  CA  A ARG A 1 252 ? 44.493 21.052  55.375 0.65 13.98 ? 252 ARG A CA  1 
ATOM   1419 C  CA  B ARG A 1 252 ? 44.492 20.988  55.329 0.35 14.02 ? 252 ARG A CA  1 
ATOM   1420 C  C   . ARG A 1 252 ? 45.193 21.668  54.162 1.00 15.05 ? 252 ARG A C   1 
ATOM   1421 O  O   . ARG A 1 252 ? 46.418 21.833  54.196 1.00 17.84 ? 252 ARG A O   1 
ATOM   1422 C  CB  A ARG A 1 252 ? 44.875 19.573  55.493 0.65 16.86 ? 252 ARG A CB  1 
ATOM   1423 C  CB  B ARG A 1 252 ? 44.842 19.506  55.226 0.35 17.51 ? 252 ARG A CB  1 
ATOM   1424 C  CG  A ARG A 1 252 ? 44.513 18.740  54.260 0.65 25.10 ? 252 ARG A CG  1 
ATOM   1425 C  CG  B ARG A 1 252 ? 44.629 18.643  56.435 0.35 21.13 ? 252 ARG A CG  1 
ATOM   1426 C  CD  A ARG A 1 252 ? 44.819 17.260  54.430 0.65 27.67 ? 252 ARG A CD  1 
ATOM   1427 C  CD  B ARG A 1 252 ? 44.826 17.193  55.997 0.35 29.65 ? 252 ARG A CD  1 
ATOM   1428 N  NE  A ARG A 1 252 ? 44.030 16.622  55.474 0.65 25.03 ? 252 ARG A NE  1 
ATOM   1429 N  NE  B ARG A 1 252 ? 43.703 16.349  56.387 0.35 30.12 ? 252 ARG A NE  1 
ATOM   1430 C  CZ  A ARG A 1 252 ? 42.879 16.000  55.263 0.65 28.30 ? 252 ARG A CZ  1 
ATOM   1431 C  CZ  B ARG A 1 252 ? 42.766 15.893  55.563 0.35 27.38 ? 252 ARG A CZ  1 
ATOM   1432 N  NH1 A ARG A 1 252 ? 42.204 15.441  56.259 0.65 20.48 ? 252 ARG A NH1 1 
ATOM   1433 N  NH1 B ARG A 1 252 ? 42.799 16.145  54.262 0.35 30.52 ? 252 ARG A NH1 1 
ATOM   1434 N  NH2 A ARG A 1 252 ? 42.395 15.940  54.022 0.65 32.00 ? 252 ARG A NH2 1 
ATOM   1435 N  NH2 B ARG A 1 252 ? 41.764 15.168  56.060 0.35 23.33 ? 252 ARG A NH2 1 
ATOM   1436 N  N   . VAL A 1 253 ? 44.458 22.028  53.117 1.00 13.24 ? 253 VAL A N   1 
ATOM   1437 C  CA  . VAL A 1 253 ? 45.031 22.620  51.918 1.00 13.89 ? 253 VAL A CA  1 
ATOM   1438 C  C   . VAL A 1 253 ? 44.333 23.954  51.684 1.00 17.24 ? 253 VAL A C   1 
ATOM   1439 O  O   . VAL A 1 253 ? 43.265 24.228  52.239 1.00 17.41 ? 253 VAL A O   1 
ATOM   1440 C  CB  . VAL A 1 253 ? 44.891 21.697  50.679 1.00 15.38 ? 253 VAL A CB  1 
ATOM   1441 C  CG1 . VAL A 1 253 ? 45.633 20.388  50.902 1.00 19.46 ? 253 VAL A CG1 1 
ATOM   1442 C  CG2 . VAL A 1 253 ? 43.433 21.493  50.318 1.00 15.18 ? 253 VAL A CG2 1 
ATOM   1443 N  N   . ASN A 1 254 ? 44.946 24.802  50.861 1.00 13.53 ? 254 ASN A N   1 
ATOM   1444 C  CA  . ASN A 1 254 ? 44.318 26.081  50.543 1.00 12.41 ? 254 ASN A CA  1 
ATOM   1445 C  C   . ASN A 1 254 ? 44.948 26.647  49.272 1.00 14.41 ? 254 ASN A C   1 
ATOM   1446 O  O   . ASN A 1 254 ? 45.911 26.097  48.736 1.00 15.98 ? 254 ASN A O   1 
ATOM   1447 C  CB  . ASN A 1 254 ? 44.451 27.056  51.720 1.00 15.34 ? 254 ASN A CB  1 
ATOM   1448 C  CG  . ASN A 1 254 ? 45.905 27.264  52.143 1.00 21.72 ? 254 ASN A CG  1 
ATOM   1449 O  OD1 . ASN A 1 254 ? 46.644 27.951  51.472 1.00 19.55 ? 254 ASN A OD1 1 
ATOM   1450 N  ND2 . ASN A 1 254 ? 46.298 26.693  53.287 1.00 26.81 ? 254 ASN A ND2 1 
ATOM   1451 N  N   . PHE A 1 255 ? 44.372 27.753  48.781 1.00 15.68 ? 255 PHE A N   1 
ATOM   1452 C  CA  . PHE A 1 255 ? 44.806 28.297  47.495 1.00 13.14 ? 255 PHE A CA  1 
ATOM   1453 C  C   . PHE A 1 255 ? 46.233 28.822  47.571 1.00 13.84 ? 255 PHE A C   1 
ATOM   1454 O  O   . PHE A 1 255 ? 47.064 28.518  46.699 1.00 14.63 ? 255 PHE A O   1 
ATOM   1455 C  CB  . PHE A 1 255 ? 43.839 29.394  47.045 1.00 17.73 ? 255 PHE A CB  1 
ATOM   1456 C  CG  . PHE A 1 255 ? 44.104 29.903  45.663 1.00 15.13 ? 255 PHE A CG  1 
ATOM   1457 C  CD1 . PHE A 1 255 ? 43.646 29.199  44.556 1.00 16.77 ? 255 PHE A CD1 1 
ATOM   1458 C  CD2 . PHE A 1 255 ? 44.795 31.096  45.463 1.00 19.09 ? 255 PHE A CD2 1 
ATOM   1459 C  CE1 . PHE A 1 255 ? 43.874 29.662  43.277 1.00 18.55 ? 255 PHE A CE1 1 
ATOM   1460 C  CE2 . PHE A 1 255 ? 45.017 31.569  44.179 1.00 24.27 ? 255 PHE A CE2 1 
ATOM   1461 C  CZ  . PHE A 1 255 ? 44.552 30.848  43.076 1.00 18.83 ? 255 PHE A CZ  1 
ATOM   1462 N  N   . ASP A 1 256 ? 46.556 29.567  48.638 1.00 15.63 ? 256 ASP A N   1 
ATOM   1463 C  CA  . ASP A 1 256 ? 47.899 30.136  48.745 1.00 19.13 ? 256 ASP A CA  1 
ATOM   1464 C  C   . ASP A 1 256 ? 48.963 29.059  48.838 1.00 17.53 ? 256 ASP A C   1 
ATOM   1465 O  O   . ASP A 1 256 ? 50.030 29.189  48.236 1.00 16.77 ? 256 ASP A O   1 
ATOM   1466 C  CB  . ASP A 1 256 ? 47.984 31.061  49.957 1.00 19.79 ? 256 ASP A CB  1 
ATOM   1467 C  CG  . ASP A 1 256 ? 47.240 32.359  49.732 1.00 32.20 ? 256 ASP A CG  1 
ATOM   1468 O  OD1 . ASP A 1 256 ? 46.823 32.617  48.575 1.00 34.91 ? 256 ASP A OD1 1 
ATOM   1469 O  OD2 . ASP A 1 256 ? 47.045 33.105  50.716 1.00 44.20 ? 256 ASP A OD2 1 
ATOM   1470 N  N   . GLN A 1 257 ? 48.705 28.008  49.619 1.00 14.94 ? 257 GLN A N   1 
ATOM   1471 C  CA  A GLN A 1 257 ? 49.688 26.945  49.731 0.63 14.52 ? 257 GLN A CA  1 
ATOM   1472 C  CA  B GLN A 1 257 ? 49.658 26.914  49.744 0.37 14.58 ? 257 GLN A CA  1 
ATOM   1473 C  C   . GLN A 1 257 ? 49.859 26.211  48.406 1.00 14.10 ? 257 GLN A C   1 
ATOM   1474 O  O   . GLN A 1 257 ? 50.988 25.894  48.020 1.00 15.73 ? 257 GLN A O   1 
ATOM   1475 C  CB  A GLN A 1 257 ? 49.312 25.970  50.834 0.63 19.79 ? 257 GLN A CB  1 
ATOM   1476 C  CB  B GLN A 1 257 ? 49.169 25.930  50.808 0.37 19.63 ? 257 GLN A CB  1 
ATOM   1477 C  CG  A GLN A 1 257 ? 50.390 24.945  51.041 0.63 18.60 ? 257 GLN A CG  1 
ATOM   1478 C  CG  B GLN A 1 257 ? 50.001 24.676  50.942 0.37 21.34 ? 257 GLN A CG  1 
ATOM   1479 C  CD  A GLN A 1 257 ? 50.312 24.312  52.408 0.63 26.56 ? 257 GLN A CD  1 
ATOM   1480 C  CD  B GLN A 1 257 ? 51.275 24.908  51.712 0.37 25.89 ? 257 GLN A CD  1 
ATOM   1481 O  OE1 A GLN A 1 257 ? 50.869 24.836  53.374 0.63 33.10 ? 257 GLN A OE1 1 
ATOM   1482 O  OE1 B GLN A 1 257 ? 52.284 25.323  51.149 0.37 25.14 ? 257 GLN A OE1 1 
ATOM   1483 N  NE2 A GLN A 1 257 ? 49.603 23.195  52.506 0.63 24.15 ? 257 GLN A NE2 1 
ATOM   1484 N  NE2 B GLN A 1 257 ? 51.237 24.649  53.014 0.37 28.12 ? 257 GLN A NE2 1 
ATOM   1485 N  N   . SER A 1 258 ? 48.759 25.968  47.683 1.00 13.12 ? 258 SER A N   1 
ATOM   1486 C  CA  . SER A 1 258 ? 48.875 25.300  46.390 1.00 12.87 ? 258 SER A CA  1 
ATOM   1487 C  C   . SER A 1 258 ? 49.651 26.161  45.391 1.00 14.43 ? 258 SER A C   1 
ATOM   1488 O  O   . SER A 1 258 ? 50.444 25.642  44.589 1.00 14.32 ? 258 SER A O   1 
ATOM   1489 C  CB  . SER A 1 258 ? 47.475 24.934  45.867 1.00 14.01 ? 258 SER A CB  1 
ATOM   1490 O  OG  . SER A 1 258 ? 47.001 23.793  46.584 1.00 13.32 ? 258 SER A OG  1 
ATOM   1491 N  N   . LEU A 1 259 ? 49.448 27.482  45.425 1.00 12.76 ? 259 LEU A N   1 
ATOM   1492 C  CA  . LEU A 1 259 ? 50.249 28.337  44.558 1.00 13.99 ? 259 LEU A CA  1 
ATOM   1493 C  C   . LEU A 1 259 ? 51.716 28.309  44.962 1.00 16.82 ? 259 LEU A C   1 
ATOM   1494 O  O   . LEU A 1 259 ? 52.581 28.391  44.094 1.00 18.42 ? 259 LEU A O   1 
ATOM   1495 C  CB  . LEU A 1 259 ? 49.736 29.771  44.554 1.00 19.12 ? 259 LEU A CB  1 
ATOM   1496 C  CG  . LEU A 1 259 ? 48.958 30.091  43.278 1.00 24.46 ? 259 LEU A CG  1 
ATOM   1497 C  CD1 . LEU A 1 259 ? 47.764 29.141  43.166 1.00 28.40 ? 259 LEU A CD1 1 
ATOM   1498 C  CD2 . LEU A 1 259 ? 48.482 31.531  43.289 1.00 32.06 ? 259 LEU A CD2 1 
ATOM   1499 N  N   . ARG A 1 260 ? 52.012 28.161  46.262 1.00 15.82 ? 260 ARG A N   1 
ATOM   1500 C  CA  . ARG A 1 260 ? 53.400 28.091  46.699 1.00 15.43 ? 260 ARG A CA  1 
ATOM   1501 C  C   . ARG A 1 260 ? 54.069 26.809  46.229 1.00 16.20 ? 260 ARG A C   1 
ATOM   1502 O  O   . ARG A 1 260 ? 55.279 26.813  45.952 1.00 19.20 ? 260 ARG A O   1 
ATOM   1503 C  CB  . ARG A 1 260 ? 53.475 28.241  48.230 1.00 20.57 ? 260 ARG A CB  1 
ATOM   1504 C  CG  . ARG A 1 260 ? 53.178 29.688  48.699 1.00 26.64 ? 260 ARG A CG  1 
ATOM   1505 C  CD  . ARG A 1 260 ? 53.677 30.013  50.130 1.00 29.78 ? 260 ARG A CD  1 
ATOM   1506 N  NE  . ARG A 1 260 ? 53.031 29.186  51.140 1.00 32.36 ? 260 ARG A NE  1 
ATOM   1507 C  CZ  . ARG A 1 260 ? 51.903 29.512  51.764 1.00 37.33 ? 260 ARG A CZ  1 
ATOM   1508 N  NH1 . ARG A 1 260 ? 51.276 30.655  51.518 1.00 35.45 ? 260 ARG A NH1 1 
ATOM   1509 N  NH2 . ARG A 1 260 ? 51.391 28.673  52.657 1.00 36.35 ? 260 ARG A NH2 1 
ATOM   1510 N  N   . VAL A 1 261 ? 53.308 25.708  46.124 1.00 14.79 ? 261 VAL A N   1 
ATOM   1511 C  CA  . VAL A 1 261 ? 53.828 24.471  45.534 1.00 13.34 ? 261 VAL A CA  1 
ATOM   1512 C  C   . VAL A 1 261 ? 54.281 24.730  44.108 1.00 12.74 ? 261 VAL A C   1 
ATOM   1513 O  O   . VAL A 1 261 ? 55.411 24.398  43.720 1.00 14.33 ? 261 VAL A O   1 
ATOM   1514 C  CB  . VAL A 1 261 ? 52.757 23.359  45.552 1.00 14.07 ? 261 VAL A CB  1 
ATOM   1515 C  CG1 . VAL A 1 261 ? 53.239 22.136  44.730 1.00 17.11 ? 261 VAL A CG1 1 
ATOM   1516 C  CG2 . VAL A 1 261 ? 52.428 22.937  46.994 1.00 21.01 ? 261 VAL A CG2 1 
ATOM   1517 N  N   . LEU A 1 262 ? 53.379 25.286  43.295 1.00 14.59 ? 262 LEU A N   1 
ATOM   1518 C  CA  . LEU A 1 262 ? 53.692 25.523  41.887 1.00 16.05 ? 262 LEU A CA  1 
ATOM   1519 C  C   . LEU A 1 262 ? 54.865 26.480  41.731 1.00 16.86 ? 262 LEU A C   1 
ATOM   1520 O  O   . LEU A 1 262 ? 55.729 26.284  40.872 1.00 16.19 ? 262 LEU A O   1 
ATOM   1521 C  CB  . LEU A 1 262 ? 52.452 26.076  41.181 1.00 13.60 ? 262 LEU A CB  1 
ATOM   1522 C  CG  . LEU A 1 262 ? 51.316 25.042  41.069 1.00 16.46 ? 262 LEU A CG  1 
ATOM   1523 C  CD1 . LEU A 1 262 ? 49.946 25.704  40.909 1.00 17.99 ? 262 LEU A CD1 1 
ATOM   1524 C  CD2 . LEU A 1 262 ? 51.569 24.083  39.912 1.00 20.38 ? 262 LEU A CD2 1 
ATOM   1525 N  N   . LYS A 1 263 ? 54.892 27.542  42.533 1.00 14.00 ? 263 LYS A N   1 
ATOM   1526 C  CA  . LYS A 1 263 ? 56.024 28.474  42.464 1.00 15.20 ? 263 LYS A CA  1 
ATOM   1527 C  C   . LYS A 1 263 ? 57.331 27.810  42.870 1.00 16.32 ? 263 LYS A C   1 
ATOM   1528 O  O   . LYS A 1 263 ? 58.379 28.068  42.260 1.00 16.74 ? 263 LYS A O   1 
ATOM   1529 C  CB  . LYS A 1 263 ? 55.748 29.689  43.347 1.00 14.43 ? 263 LYS A CB  1 
ATOM   1530 C  CG  . LYS A 1 263 ? 54.703 30.587  42.709 1.00 23.30 ? 263 LYS A CG  1 
ATOM   1531 C  CD  . LYS A 1 263 ? 54.272 31.756  43.576 1.00 30.81 ? 263 LYS A CD  1 
ATOM   1532 C  CE  . LYS A 1 263 ? 55.371 32.802  43.721 1.00 36.11 ? 263 LYS A CE  1 
ATOM   1533 N  NZ  . LYS A 1 263 ? 56.060 33.107  42.421 1.00 45.12 ? 263 LYS A NZ  1 
ATOM   1534 N  N   . HIS A 1 264 ? 57.302 26.972  43.904 1.00 13.73 ? 264 HIS A N   1 
ATOM   1535 C  CA  . HIS A 1 264 ? 58.549 26.364  44.358 1.00 13.77 ? 264 HIS A CA  1 
ATOM   1536 C  C   . HIS A 1 264 ? 59.074 25.360  43.346 1.00 13.58 ? 264 HIS A C   1 
ATOM   1537 O  O   . HIS A 1 264 ? 60.283 25.256  43.137 1.00 16.26 ? 264 HIS A O   1 
ATOM   1538 C  CB  . HIS A 1 264 ? 58.372 25.692  45.704 1.00 15.96 ? 264 HIS A CB  1 
ATOM   1539 C  CG  . HIS A 1 264 ? 59.668 25.280  46.321 1.00 19.08 ? 264 HIS A CG  1 
ATOM   1540 N  ND1 . HIS A 1 264 ? 60.667 26.191  46.603 1.00 22.11 ? 264 HIS A ND1 1 
ATOM   1541 C  CD2 . HIS A 1 264 ? 60.139 24.069  46.700 1.00 19.33 ? 264 HIS A CD2 1 
ATOM   1542 C  CE1 . HIS A 1 264 ? 61.695 25.555  47.134 1.00 17.81 ? 264 HIS A CE1 1 
ATOM   1543 N  NE2 . HIS A 1 264 ? 61.395 24.272  47.226 1.00 22.98 ? 264 HIS A NE2 1 
ATOM   1544 N  N   . ALA A 1 265 ? 58.179 24.617  42.693 1.00 16.44 ? 265 ALA A N   1 
ATOM   1545 C  CA  . ALA A 1 265 ? 58.632 23.688  41.662 1.00 16.04 ? 265 ALA A CA  1 
ATOM   1546 C  C   . ALA A 1 265 ? 59.380 24.428  40.559 1.00 12.92 ? 265 ALA A C   1 
ATOM   1547 O  O   . ALA A 1 265 ? 60.418 23.949  40.076 1.00 15.90 ? 265 ALA A O   1 
ATOM   1548 C  CB  . ALA A 1 265 ? 57.434 22.919  41.087 1.00 15.12 ? 265 ALA A CB  1 
ATOM   1549 N  N   . LYS A 1 266 ? 58.864 25.594  40.140 1.00 14.84 ? 266 LYS A N   1 
ATOM   1550 C  CA  . LYS A 1 266 ? 59.536 26.372  39.099 1.00 16.65 ? 266 LYS A CA  1 
ATOM   1551 C  C   . LYS A 1 266 ? 60.801 27.040  39.623 1.00 17.99 ? 266 LYS A C   1 
ATOM   1552 O  O   . LYS A 1 266 ? 61.750 27.246  38.863 1.00 20.56 ? 266 LYS A O   1 
ATOM   1553 C  CB  . LYS A 1 266 ? 58.604 27.444  38.516 1.00 20.65 ? 266 LYS A CB  1 
ATOM   1554 C  CG  . LYS A 1 266 ? 57.405 26.950  37.687 1.00 29.78 ? 266 LYS A CG  1 
ATOM   1555 C  CD  . LYS A 1 266 ? 57.779 26.531  36.270 1.00 24.96 ? 266 LYS A CD  1 
ATOM   1556 C  CE  . LYS A 1 266 ? 57.536 27.610  35.237 1.00 27.62 ? 266 LYS A CE  1 
ATOM   1557 N  NZ  . LYS A 1 266 ? 58.021 27.118  33.885 1.00 33.66 ? 266 LYS A NZ  1 
ATOM   1558 N  N   . LYS A 1 267 ? 60.838 27.414  40.900 1.00 15.09 ? 267 LYS A N   1 
ATOM   1559 C  CA  . LYS A 1 267 ? 62.083 27.983  41.441 1.00 16.60 ? 267 LYS A CA  1 
ATOM   1560 C  C   . LYS A 1 267 ? 63.220 26.970  41.421 1.00 20.32 ? 267 LYS A C   1 
ATOM   1561 O  O   . LYS A 1 267 ? 64.354 27.300  41.026 1.00 21.52 ? 267 LYS A O   1 
ATOM   1562 C  CB  . LYS A 1 267 ? 61.853 28.482  42.868 1.00 24.17 ? 267 LYS A CB  1 
ATOM   1563 C  CG  . LYS A 1 267 ? 63.135 28.955  43.553 1.00 27.13 ? 267 LYS A CG  1 
ATOM   1564 C  CD  . LYS A 1 267 ? 62.868 29.421  44.975 1.00 31.40 ? 267 LYS A CD  1 
ATOM   1565 C  CE  . LYS A 1 267 ? 64.126 30.040  45.597 1.00 35.97 ? 267 LYS A CE  1 
ATOM   1566 N  NZ  . LYS A 1 267 ? 63.910 30.378  47.029 1.00 47.88 ? 267 LYS A NZ  1 
ATOM   1567 N  N   . VAL A 1 268 ? 62.953 25.727  41.838 1.00 18.54 ? 268 VAL A N   1 
ATOM   1568 C  CA  . VAL A 1 268 ? 64.047 24.767  41.932 1.00 22.17 ? 268 VAL A CA  1 
ATOM   1569 C  C   . VAL A 1 268 ? 64.352 24.101  40.595 1.00 19.16 ? 268 VAL A C   1 
ATOM   1570 O  O   . VAL A 1 268 ? 65.484 23.638  40.399 1.00 21.49 ? 268 VAL A O   1 
ATOM   1571 C  CB  . VAL A 1 268 ? 63.818 23.695  43.012 1.00 27.37 ? 268 VAL A CB  1 
ATOM   1572 C  CG1 . VAL A 1 268 ? 63.268 24.328  44.285 1.00 32.34 ? 268 VAL A CG1 1 
ATOM   1573 C  CG2 . VAL A 1 268 ? 62.935 22.602  42.526 1.00 24.37 ? 268 VAL A CG2 1 
ATOM   1574 N  N   . GLN A 1 269 ? 63.389 24.043  39.673 1.00 16.52 ? 269 GLN A N   1 
ATOM   1575 C  CA  . GLN A 1 269 ? 63.609 23.476  38.340 1.00 16.58 ? 269 GLN A CA  1 
ATOM   1576 C  C   . GLN A 1 269 ? 62.975 24.399  37.313 1.00 16.02 ? 269 GLN A C   1 
ATOM   1577 O  O   . GLN A 1 269 ? 61.846 24.188  36.854 1.00 14.58 ? 269 GLN A O   1 
ATOM   1578 C  CB  . GLN A 1 269 ? 63.072 22.046  38.240 1.00 16.45 ? 269 GLN A CB  1 
ATOM   1579 C  CG  . GLN A 1 269 ? 63.309 21.410  36.885 1.00 18.88 ? 269 GLN A CG  1 
ATOM   1580 C  CD  . GLN A 1 269 ? 64.755 21.454  36.499 1.00 24.18 ? 269 GLN A CD  1 
ATOM   1581 O  OE1 . GLN A 1 269 ? 65.240 22.472  36.000 1.00 23.43 ? 269 GLN A OE1 1 
ATOM   1582 N  NE2 . GLN A 1 269 ? 65.468 20.362  36.748 1.00 28.66 ? 269 GLN A NE2 1 
ATOM   1583 N  N   . PRO A 1 270 ? 63.691 25.440  36.899 1.00 15.11 ? 270 PRO A N   1 
ATOM   1584 C  CA  . PRO A 1 270 ? 63.065 26.444  36.037 1.00 14.58 ? 270 PRO A CA  1 
ATOM   1585 C  C   . PRO A 1 270 ? 62.635 25.925  34.667 1.00 16.73 ? 270 PRO A C   1 
ATOM   1586 O  O   . PRO A 1 270 ? 61.802 26.564  34.020 1.00 20.44 ? 270 PRO A O   1 
ATOM   1587 C  CB  . PRO A 1 270 ? 64.149 27.527  35.924 1.00 22.45 ? 270 PRO A CB  1 
ATOM   1588 C  CG  . PRO A 1 270 ? 64.903 27.400  37.215 1.00 22.21 ? 270 PRO A CG  1 
ATOM   1589 C  CD  . PRO A 1 270 ? 64.964 25.915  37.494 1.00 20.70 ? 270 PRO A CD  1 
ATOM   1590 N  N   . ASP A 1 271 ? 63.152 24.785  34.208 1.00 18.57 ? 271 ASP A N   1 
ATOM   1591 C  CA  A ASP A 1 271 ? 62.596 24.473  32.898 0.48 18.27 ? 271 ASP A CA  1 
ATOM   1592 C  CA  B ASP A 1 271 ? 62.873 24.084  32.954 0.52 19.32 ? 271 ASP A CA  1 
ATOM   1593 C  C   . ASP A 1 271 ? 61.511 23.399  32.959 1.00 17.22 ? 271 ASP A C   1 
ATOM   1594 O  O   . ASP A 1 271 ? 60.998 23.011  31.898 1.00 14.81 ? 271 ASP A O   1 
ATOM   1595 C  CB  A ASP A 1 271 ? 63.684 24.150  31.868 0.48 18.80 ? 271 ASP A CB  1 
ATOM   1596 C  CB  B ASP A 1 271 ? 63.947 22.991  32.734 0.52 11.28 ? 271 ASP A CB  1 
ATOM   1597 C  CG  A ASP A 1 271 ? 64.187 25.416  31.103 0.48 20.50 ? 271 ASP A CG  1 
ATOM   1598 C  CG  B ASP A 1 271 ? 65.343 23.544  32.482 0.52 19.08 ? 271 ASP A CG  1 
ATOM   1599 O  OD1 A ASP A 1 271 ? 63.549 26.504  31.151 0.48 21.46 ? 271 ASP A OD1 1 
ATOM   1600 O  OD1 B ASP A 1 271 ? 65.449 24.583  31.806 0.52 17.04 ? 271 ASP A OD1 1 
ATOM   1601 O  OD2 A ASP A 1 271 ? 65.237 25.319  30.442 0.48 19.40 ? 271 ASP A OD2 1 
ATOM   1602 O  OD2 B ASP A 1 271 ? 66.339 22.920  32.949 0.52 17.00 ? 271 ASP A OD2 1 
ATOM   1603 N  N   . VAL A 1 272 ? 61.009 23.084  34.155 1.00 14.07 ? 272 VAL A N   1 
ATOM   1604 C  CA  . VAL A 1 272 ? 59.805 22.255  34.233 1.00 11.35 ? 272 VAL A CA  1 
ATOM   1605 C  C   . VAL A 1 272 ? 58.605 23.081  33.796 1.00 12.29 ? 272 VAL A C   1 
ATOM   1606 O  O   . VAL A 1 272 ? 58.576 24.308  33.958 1.00 12.78 ? 272 VAL A O   1 
ATOM   1607 C  CB  . VAL A 1 272 ? 59.615 21.683  35.650 1.00 14.15 ? 272 VAL A CB  1 
ATOM   1608 C  CG1 . VAL A 1 272 ? 59.027 22.713  36.604 1.00 16.80 ? 272 VAL A CG1 1 
ATOM   1609 C  CG2 . VAL A 1 272 ? 58.732 20.401  35.609 1.00 14.74 ? 272 VAL A CG2 1 
ATOM   1610 N  N   . ILE A 1 273 ? 57.632 22.413  33.162 1.00 9.99  ? 273 ILE A N   1 
ATOM   1611 C  CA  . ILE A 1 273 ? 56.360 23.039  32.798 1.00 9.24  ? 273 ILE A CA  1 
ATOM   1612 C  C   . ILE A 1 273 ? 55.436 22.890  34.000 1.00 11.68 ? 273 ILE A C   1 
ATOM   1613 O  O   . ILE A 1 273 ? 55.270 21.782  34.503 1.00 11.15 ? 273 ILE A O   1 
ATOM   1614 C  CB  . ILE A 1 273 ? 55.751 22.362  31.563 1.00 9.47  ? 273 ILE A CB  1 
ATOM   1615 C  CG1 . ILE A 1 273 ? 56.639 22.566  30.319 1.00 12.80 ? 273 ILE A CG1 1 
ATOM   1616 C  CG2 . ILE A 1 273 ? 54.331 22.868  31.323 1.00 11.66 ? 273 ILE A CG2 1 
ATOM   1617 C  CD1 . ILE A 1 273 ? 56.676 24.017  29.847 1.00 17.32 ? 273 ILE A CD1 1 
ATOM   1618 N  N   . SER A 1 274 ? 54.864 23.991  34.483 1.00 8.65  ? 274 SER A N   1 
ATOM   1619 C  CA  . SER A 1 274 ? 53.936 23.911  35.609 1.00 8.31  ? 274 SER A CA  1 
ATOM   1620 C  C   . SER A 1 274 ? 52.501 23.935  35.103 1.00 8.83  ? 274 SER A C   1 
ATOM   1621 O  O   . SER A 1 274 ? 52.183 24.574  34.095 1.00 8.73  ? 274 SER A O   1 
ATOM   1622 C  CB  . SER A 1 274 ? 54.144 25.061  36.609 1.00 11.23 ? 274 SER A CB  1 
ATOM   1623 O  OG  . SER A 1 274 ? 54.103 26.314  35.946 1.00 12.99 ? 274 SER A OG  1 
ATOM   1624 N  N   . LYS A 1 275 ? 51.634 23.212  35.812 1.00 8.12  ? 275 LYS A N   1 
ATOM   1625 C  CA  . LYS A 1 275 ? 50.277 22.988  35.335 1.00 7.40  ? 275 LYS A CA  1 
ATOM   1626 C  C   . LYS A 1 275 ? 49.335 22.907  36.523 1.00 7.98  ? 275 LYS A C   1 
ATOM   1627 O  O   . LYS A 1 275 ? 49.683 22.326  37.560 1.00 8.23  ? 275 LYS A O   1 
ATOM   1628 C  CB  . LYS A 1 275 ? 50.250 21.694  34.522 1.00 7.59  ? 275 LYS A CB  1 
ATOM   1629 C  CG  . LYS A 1 275 ? 48.882 21.219  34.044 1.00 11.83 ? 275 LYS A CG  1 
ATOM   1630 C  CD  . LYS A 1 275 ? 49.134 20.012  33.140 1.00 12.53 ? 275 LYS A CD  1 
ATOM   1631 C  CE  . LYS A 1 275 ? 47.827 19.455  32.607 1.00 28.10 ? 275 LYS A CE  1 
ATOM   1632 N  NZ  . LYS A 1 275 ? 48.094 18.252  31.722 1.00 26.38 ? 275 LYS A NZ  1 
ATOM   1633 N  N   . THR A 1 276 ? 48.121 23.445  36.346 1.00 7.94  ? 276 THR A N   1 
ATOM   1634 C  CA  . THR A 1 276 ? 47.095 23.254  37.359 1.00 7.66  ? 276 THR A CA  1 
ATOM   1635 C  C   . THR A 1 276 ? 45.743 23.078  36.684 1.00 8.06  ? 276 THR A C   1 
ATOM   1636 O  O   . THR A 1 276 ? 45.550 23.410  35.509 1.00 8.63  ? 276 THR A O   1 
ATOM   1637 C  CB  . THR A 1 276 ? 47.068 24.409  38.387 1.00 9.58  ? 276 THR A CB  1 
ATOM   1638 O  OG1 . THR A 1 276 ? 46.338 24.012  39.552 1.00 9.99  ? 276 THR A OG1 1 
ATOM   1639 C  CG2 . THR A 1 276 ? 46.431 25.684  37.803 1.00 13.40 ? 276 THR A CG2 1 
ATOM   1640 N  N   . SER A 1 277 ? 44.795 22.545  37.456 1.00 7.03  ? 277 SER A N   1 
ATOM   1641 C  CA  . SER A 1 277 ? 43.438 22.302  36.986 1.00 9.36  ? 277 SER A CA  1 
ATOM   1642 C  C   . SER A 1 277 ? 42.429 22.872  37.969 1.00 10.58 ? 277 SER A C   1 
ATOM   1643 O  O   . SER A 1 277 ? 42.651 22.852  39.189 1.00 10.70 ? 277 SER A O   1 
ATOM   1644 C  CB  . SER A 1 277 ? 43.180 20.824  36.833 1.00 11.05 ? 277 SER A CB  1 
ATOM   1645 O  OG  . SER A 1 277 ? 44.038 20.282  35.828 1.00 15.51 ? 277 SER A OG  1 
ATOM   1646 N  N   . ILE A 1 278 ? 41.331 23.382  37.421 1.00 9.99  ? 278 ILE A N   1 
ATOM   1647 C  CA  . ILE A 1 278 ? 40.205 23.859  38.207 1.00 8.35  ? 278 ILE A CA  1 
ATOM   1648 C  C   . ILE A 1 278 ? 38.933 23.204  37.682 1.00 9.12  ? 278 ILE A C   1 
ATOM   1649 O  O   . ILE A 1 278 ? 38.815 22.879  36.489 1.00 9.27  ? 278 ILE A O   1 
ATOM   1650 C  CB  . ILE A 1 278 ? 40.139 25.391  38.128 1.00 17.08 ? 278 ILE A CB  1 
ATOM   1651 C  CG1 . ILE A 1 278 ? 39.090 25.949  39.081 1.00 24.58 ? 278 ILE A CG1 1 
ATOM   1652 C  CG2 . ILE A 1 278 ? 39.872 25.839  36.732 1.00 24.58 ? 278 ILE A CG2 1 
ATOM   1653 C  CD1 . ILE A 1 278 ? 39.411 27.381  39.502 1.00 26.19 ? 278 ILE A CD1 1 
ATOM   1654 N  N   . MET A 1 279 ? 37.998 22.944  38.588 1.00 7.99  ? 279 MET A N   1 
ATOM   1655 C  CA  . MET A 1 279 ? 36.676 22.455  38.225 1.00 10.12 ? 279 MET A CA  1 
ATOM   1656 C  C   . MET A 1 279 ? 35.689 23.611  38.263 1.00 12.32 ? 279 MET A C   1 
ATOM   1657 O  O   . MET A 1 279 ? 35.718 24.438  39.179 1.00 13.21 ? 279 MET A O   1 
ATOM   1658 C  CB  . MET A 1 279 ? 36.170 21.377  39.194 1.00 13.20 ? 279 MET A CB  1 
ATOM   1659 C  CG  . MET A 1 279 ? 36.974 20.107  39.238 1.00 19.50 ? 279 MET A CG  1 
ATOM   1660 S  SD  . MET A 1 279 ? 36.469 19.149  40.707 1.00 22.65 ? 279 MET A SD  1 
ATOM   1661 C  CE  . MET A 1 279 ? 37.003 20.166  42.081 1.00 27.62 ? 279 MET A CE  1 
ATOM   1662 N  N   . LEU A 1 280 ? 34.827 23.662  37.271 1.00 8.53  ? 280 LEU A N   1 
ATOM   1663 C  CA  . LEU A 1 280 ? 33.700 24.574  37.269 1.00 8.76  ? 280 LEU A CA  1 
ATOM   1664 C  C   . LEU A 1 280 ? 32.425 23.823  37.592 1.00 9.04  ? 280 LEU A C   1 
ATOM   1665 O  O   . LEU A 1 280 ? 32.364 22.597  37.505 1.00 11.23 ? 280 LEU A O   1 
ATOM   1666 C  CB  . LEU A 1 280 ? 33.555 25.283  35.920 1.00 9.09  ? 280 LEU A CB  1 
ATOM   1667 C  CG  . LEU A 1 280 ? 34.826 26.043  35.517 1.00 11.18 ? 280 LEU A CG  1 
ATOM   1668 C  CD1 . LEU A 1 280 ? 34.549 26.794  34.204 1.00 13.74 ? 280 LEU A CD1 1 
ATOM   1669 C  CD2 . LEU A 1 280 ? 35.299 26.996  36.617 1.00 11.41 ? 280 LEU A CD2 1 
ATOM   1670 N  N   . GLY A 1 281 ? 31.401 24.586  37.971 1.00 8.99  ? 281 GLY A N   1 
ATOM   1671 C  CA  . GLY A 1 281 ? 30.122 24.024  38.350 1.00 12.47 ? 281 GLY A CA  1 
ATOM   1672 C  C   . GLY A 1 281 ? 29.902 23.856  39.836 1.00 13.09 ? 281 GLY A C   1 
ATOM   1673 O  O   . GLY A 1 281 ? 28.951 23.162  40.233 1.00 15.85 ? 281 GLY A O   1 
ATOM   1674 N  N   . LEU A 1 282 ? 30.753 24.451  40.672 1.00 11.30 ? 282 LEU A N   1 
ATOM   1675 C  CA  . LEU A 1 282 ? 30.647 24.358  42.122 1.00 13.44 ? 282 LEU A CA  1 
ATOM   1676 C  C   . LEU A 1 282 ? 30.119 25.643  42.749 1.00 14.77 ? 282 LEU A C   1 
ATOM   1677 O  O   . LEU A 1 282 ? 30.168 25.789  43.976 1.00 18.88 ? 282 LEU A O   1 
ATOM   1678 C  CB  . LEU A 1 282 ? 32.007 24.012  42.726 1.00 14.95 ? 282 LEU A CB  1 
ATOM   1679 C  CG  . LEU A 1 282 ? 32.609 22.626  42.432 1.00 20.71 ? 282 LEU A CG  1 
ATOM   1680 C  CD1 . LEU A 1 282 ? 34.131 22.642  42.459 1.00 25.06 ? 282 LEU A CD1 1 
ATOM   1681 C  CD2 . LEU A 1 282 ? 32.067 21.601  43.399 1.00 25.75 ? 282 LEU A CD2 1 
ATOM   1682 N  N   . GLY A 1 283 ? 29.620 26.573  41.951 1.00 16.73 ? 283 GLY A N   1 
ATOM   1683 C  CA  . GLY A 1 283 ? 29.076 27.813  42.470 1.00 22.87 ? 283 GLY A CA  1 
ATOM   1684 C  C   . GLY A 1 283 ? 29.948 29.033  42.244 1.00 18.78 ? 283 GLY A C   1 
ATOM   1685 O  O   . GLY A 1 283 ? 29.532 30.142  42.613 1.00 21.02 ? 283 GLY A O   1 
ATOM   1686 N  N   . GLU A 1 284 ? 31.127 28.870  41.643 1.00 14.93 ? 284 GLU A N   1 
ATOM   1687 C  CA  . GLU A 1 284 ? 31.991 30.003  41.353 1.00 13.32 ? 284 GLU A CA  1 
ATOM   1688 C  C   . GLU A 1 284 ? 31.298 30.930  40.354 1.00 15.98 ? 284 GLU A C   1 
ATOM   1689 O  O   . GLU A 1 284 ? 30.451 30.496  39.573 1.00 18.70 ? 284 GLU A O   1 
ATOM   1690 C  CB  . GLU A 1 284 ? 33.341 29.512  40.800 1.00 12.99 ? 284 GLU A CB  1 
ATOM   1691 C  CG  . GLU A 1 284 ? 33.277 28.911  39.390 1.00 14.03 ? 284 GLU A CG  1 
ATOM   1692 C  CD  . GLU A 1 284 ? 32.454 27.616  39.284 1.00 14.90 ? 284 GLU A CD  1 
ATOM   1693 O  OE1 . GLU A 1 284 ? 32.493 26.798  40.241 1.00 14.25 ? 284 GLU A OE1 1 
ATOM   1694 O  OE2 . GLU A 1 284 ? 31.800 27.424  38.225 1.00 14.42 ? 284 GLU A OE2 1 
ATOM   1695 N  N   . ASN A 1 285 ? 31.647 32.219  40.393 1.00 13.42 ? 285 ASN A N   1 
ATOM   1696 C  CA  . ASN A 1 285 ? 31.164 33.150  39.377 1.00 14.79 ? 285 ASN A CA  1 
ATOM   1697 C  C   . ASN A 1 285 ? 32.318 33.563  38.464 1.00 13.95 ? 285 ASN A C   1 
ATOM   1698 O  O   . ASN A 1 285 ? 33.491 33.264  38.726 1.00 14.32 ? 285 ASN A O   1 
ATOM   1699 C  CB  . ASN A 1 285 ? 30.463 34.362  40.018 1.00 22.28 ? 285 ASN A CB  1 
ATOM   1700 C  CG  . ASN A 1 285 ? 31.392 35.260  40.792 1.00 19.33 ? 285 ASN A CG  1 
ATOM   1701 O  OD1 . ASN A 1 285 ? 32.510 35.527  40.377 1.00 18.72 ? 285 ASN A OD1 1 
ATOM   1702 N  ND2 . ASN A 1 285 ? 30.918 35.754  41.945 1.00 22.12 ? 285 ASN A ND2 1 
ATOM   1703 N  N   . ASP A 1 286 ? 31.969 34.244  37.368 1.00 15.90 ? 286 ASP A N   1 
ATOM   1704 C  CA  . ASP A 1 286 ? 32.959 34.547  36.329 1.00 13.46 ? 286 ASP A CA  1 
ATOM   1705 C  C   . ASP A 1 286 ? 34.066 35.457  36.836 1.00 16.88 ? 286 ASP A C   1 
ATOM   1706 O  O   . ASP A 1 286 ? 35.236 35.331  36.436 1.00 18.66 ? 286 ASP A O   1 
ATOM   1707 C  CB  . ASP A 1 286 ? 32.266 35.197  35.134 1.00 16.55 ? 286 ASP A CB  1 
ATOM   1708 C  CG  . ASP A 1 286 ? 31.407 34.225  34.356 1.00 21.85 ? 286 ASP A CG  1 
ATOM   1709 O  OD1 . ASP A 1 286 ? 31.248 33.067  34.807 1.00 22.20 ? 286 ASP A OD1 1 
ATOM   1710 O  OD2 . ASP A 1 286 ? 30.916 34.614  33.270 1.00 25.89 ? 286 ASP A OD2 1 
ATOM   1711 N  N   . GLU A 1 287 ? 33.701 36.424  37.672 1.00 16.62 ? 287 GLU A N   1 
ATOM   1712 C  CA  A GLU A 1 287 ? 34.684 37.333  38.235 0.56 17.08 ? 287 GLU A CA  1 
ATOM   1713 C  CA  B GLU A 1 287 ? 34.694 37.331  38.240 0.44 17.11 ? 287 GLU A CA  1 
ATOM   1714 C  C   . GLU A 1 287 ? 35.727 36.566  39.056 1.00 14.55 ? 287 GLU A C   1 
ATOM   1715 O  O   . GLU A 1 287 ? 36.935 36.859  38.991 1.00 16.77 ? 287 GLU A O   1 
ATOM   1716 C  CB  A GLU A 1 287 ? 33.931 38.384  39.061 0.56 20.42 ? 287 GLU A CB  1 
ATOM   1717 C  CB  B GLU A 1 287 ? 33.990 38.378  39.104 0.44 20.41 ? 287 GLU A CB  1 
ATOM   1718 C  CG  A GLU A 1 287 ? 32.876 39.244  38.248 0.56 26.03 ? 287 GLU A CG  1 
ATOM   1719 C  CG  B GLU A 1 287 ? 34.864 39.494  39.625 0.44 27.29 ? 287 GLU A CG  1 
ATOM   1720 C  CD  A GLU A 1 287 ? 31.662 38.474  37.628 0.56 28.94 ? 287 GLU A CD  1 
ATOM   1721 C  CD  B GLU A 1 287 ? 34.166 40.278  40.728 0.44 27.24 ? 287 GLU A CD  1 
ATOM   1722 O  OE1 A GLU A 1 287 ? 30.989 37.650  38.304 0.56 22.11 ? 287 GLU A OE1 1 
ATOM   1723 O  OE1 B GLU A 1 287 ? 32.920 40.323  40.710 0.44 28.50 ? 287 GLU A OE1 1 
ATOM   1724 O  OE2 A GLU A 1 287 ? 31.366 38.716  36.431 0.56 38.45 ? 287 GLU A OE2 1 
ATOM   1725 O  OE2 B GLU A 1 287 ? 34.855 40.824  41.620 0.44 31.20 ? 287 GLU A OE2 1 
ATOM   1726 N  N   . GLN A 1 288 ? 35.280 35.563  39.812 1.00 16.27 ? 288 GLN A N   1 
ATOM   1727 C  CA  . GLN A 1 288 ? 36.184 34.751  40.613 1.00 14.56 ? 288 GLN A CA  1 
ATOM   1728 C  C   . GLN A 1 288 ? 37.084 33.886  39.739 1.00 12.87 ? 288 GLN A C   1 
ATOM   1729 O  O   . GLN A 1 288 ? 38.271 33.701  40.053 1.00 13.98 ? 288 GLN A O   1 
ATOM   1730 C  CB  . GLN A 1 288 ? 35.369 33.881  41.557 1.00 13.51 ? 288 GLN A CB  1 
ATOM   1731 C  CG  . GLN A 1 288 ? 34.659 34.725  42.609 1.00 16.09 ? 288 GLN A CG  1 
ATOM   1732 C  CD  . GLN A 1 288 ? 33.644 33.926  43.406 1.00 17.12 ? 288 GLN A CD  1 
ATOM   1733 O  OE1 . GLN A 1 288 ? 33.065 32.973  42.903 1.00 16.12 ? 288 GLN A OE1 1 
ATOM   1734 N  NE2 . GLN A 1 288 ? 33.420 34.321  44.661 1.00 18.89 ? 288 GLN A NE2 1 
ATOM   1735 N  N   . VAL A 1 289 ? 36.525 33.313  38.668 1.00 11.30 ? 289 VAL A N   1 
ATOM   1736 C  CA  . VAL A 1 289 ? 37.325 32.471  37.783 1.00 9.99  ? 289 VAL A CA  1 
ATOM   1737 C  C   . VAL A 1 289 ? 38.404 33.302  37.100 1.00 11.60 ? 289 VAL A C   1 
ATOM   1738 O  O   . VAL A 1 289 ? 39.576 32.920  37.052 1.00 12.81 ? 289 VAL A O   1 
ATOM   1739 C  CB  . VAL A 1 289 ? 36.429 31.765  36.755 1.00 12.89 ? 289 VAL A CB  1 
ATOM   1740 C  CG1 . VAL A 1 289 ? 37.278 31.000  35.728 1.00 12.78 ? 289 VAL A CG1 1 
ATOM   1741 C  CG2 . VAL A 1 289 ? 35.474 30.810  37.480 1.00 12.18 ? 289 VAL A CG2 1 
ATOM   1742 N  N   . TYR A 1 290 ? 38.018 34.443  36.547 1.00 12.13 ? 290 TYR A N   1 
ATOM   1743 C  CA  . TYR A 1 290 ? 38.999 35.292  35.883 1.00 13.90 ? 290 TYR A CA  1 
ATOM   1744 C  C   . TYR A 1 290 ? 40.106 35.721  36.844 1.00 13.53 ? 290 TYR A C   1 
ATOM   1745 O  O   . TYR A 1 290 ? 41.289 35.682  36.488 1.00 14.80 ? 290 TYR A O   1 
ATOM   1746 C  CB  . TYR A 1 290 ? 38.284 36.506  35.271 1.00 14.37 ? 290 TYR A CB  1 
ATOM   1747 C  CG  . TYR A 1 290 ? 39.189 37.361  34.427 1.00 22.09 ? 290 TYR A CG  1 
ATOM   1748 C  CD1 . TYR A 1 290 ? 39.324 37.132  33.066 1.00 28.85 ? 290 TYR A CD1 1 
ATOM   1749 C  CD2 . TYR A 1 290 ? 39.895 38.406  34.988 1.00 20.09 ? 290 TYR A CD2 1 
ATOM   1750 C  CE1 . TYR A 1 290 ? 40.160 37.919  32.295 1.00 23.74 ? 290 TYR A CE1 1 
ATOM   1751 C  CE2 . TYR A 1 290 ? 40.735 39.188  34.225 1.00 25.52 ? 290 TYR A CE2 1 
ATOM   1752 C  CZ  . TYR A 1 290 ? 40.858 38.933  32.891 1.00 22.76 ? 290 TYR A CZ  1 
ATOM   1753 O  OH  . TYR A 1 290 ? 41.682 39.729  32.127 1.00 33.46 ? 290 TYR A OH  1 
ATOM   1754 N  N   . ALA A 1 291 ? 39.743 36.136  38.068 1.00 14.40 ? 291 ALA A N   1 
ATOM   1755 C  CA  . ALA A 1 291 ? 40.742 36.545  39.058 1.00 15.55 ? 291 ALA A CA  1 
ATOM   1756 C  C   . ALA A 1 291 ? 41.669 35.390  39.416 1.00 13.57 ? 291 ALA A C   1 
ATOM   1757 O  O   . ALA A 1 291 ? 42.875 35.583  39.620 1.00 17.31 ? 291 ALA A O   1 
ATOM   1758 C  CB  . ALA A 1 291 ? 40.051 37.079  40.316 1.00 15.52 ? 291 ALA A CB  1 
ATOM   1759 N  N   . THR A 1 292 ? 41.126 34.173  39.472 1.00 12.34 ? 292 THR A N   1 
ATOM   1760 C  CA  . THR A 1 292 ? 41.968 33.008  39.741 1.00 12.50 ? 292 THR A CA  1 
ATOM   1761 C  C   . THR A 1 292 ? 42.952 32.765  38.605 1.00 13.90 ? 292 THR A C   1 
ATOM   1762 O  O   . THR A 1 292 ? 44.136 32.479  38.846 1.00 13.42 ? 292 THR A O   1 
ATOM   1763 C  CB  . THR A 1 292 ? 41.092 31.774  39.946 1.00 14.38 ? 292 THR A CB  1 
ATOM   1764 O  OG1 . THR A 1 292 ? 40.239 31.986  41.076 1.00 16.37 ? 292 THR A OG1 1 
ATOM   1765 C  CG2 . THR A 1 292 ? 41.947 30.513  40.169 1.00 14.20 ? 292 THR A CG2 1 
ATOM   1766 N  N   . MET A 1 293 ? 42.470 32.851  37.364 1.00 12.45 ? 293 MET A N   1 
ATOM   1767 C  CA  . MET A 1 293 ? 43.344 32.673  36.205 1.00 9.95  ? 293 MET A CA  1 
ATOM   1768 C  C   . MET A 1 293 ? 44.465 33.714  36.201 1.00 12.98 ? 293 MET A C   1 
ATOM   1769 O  O   . MET A 1 293 ? 45.620 33.386  35.909 1.00 14.02 ? 293 MET A O   1 
ATOM   1770 C  CB  . MET A 1 293 ? 42.495 32.717  34.927 1.00 12.74 ? 293 MET A CB  1 
ATOM   1771 C  CG  . MET A 1 293 ? 41.572 31.491  34.870 1.00 12.87 ? 293 MET A CG  1 
ATOM   1772 S  SD  . MET A 1 293 ? 40.440 31.452  33.444 1.00 18.64 ? 293 MET A SD  1 
ATOM   1773 C  CE  . MET A 1 293 ? 41.641 31.379  32.166 1.00 17.04 ? 293 MET A CE  1 
ATOM   1774 N  N   . LYS A 1 294 ? 44.144 34.968  36.560 1.00 14.07 ? 294 LYS A N   1 
ATOM   1775 C  CA  . LYS A 1 294 ? 45.177 36.003  36.630 1.00 16.80 ? 294 LYS A CA  1 
ATOM   1776 C  C   . LYS A 1 294 ? 46.199 35.700  37.713 1.00 16.14 ? 294 LYS A C   1 
ATOM   1777 O  O   . LYS A 1 294 ? 47.398 35.929  37.517 1.00 16.46 ? 294 LYS A O   1 
ATOM   1778 C  CB  . LYS A 1 294 ? 44.561 37.376  36.898 1.00 21.32 ? 294 LYS A CB  1 
ATOM   1779 C  CG  . LYS A 1 294 ? 43.890 38.019  35.702 1.00 28.78 ? 294 LYS A CG  1 
ATOM   1780 C  CD  . LYS A 1 294 ? 43.587 39.483  36.012 1.00 29.89 ? 294 LYS A CD  1 
ATOM   1781 C  CE  . LYS A 1 294 ? 44.848 40.326  35.976 1.00 40.50 ? 294 LYS A CE  1 
ATOM   1782 N  NZ  . LYS A 1 294 ? 45.460 40.298  34.614 1.00 40.78 ? 294 LYS A NZ  1 
ATOM   1783 N  N   . ALA A 1 295 ? 45.730 35.239  38.888 1.00 15.49 ? 295 ALA A N   1 
ATOM   1784 C  CA  . ALA A 1 295 ? 46.632 34.884  39.983 1.00 13.43 ? 295 ALA A CA  1 
ATOM   1785 C  C   . ALA A 1 295 ? 47.567 33.756  39.578 1.00 13.62 ? 295 ALA A C   1 
ATOM   1786 O  O   . ALA A 1 295 ? 48.742 33.745  39.957 1.00 16.24 ? 295 ALA A O   1 
ATOM   1787 C  CB  . ALA A 1 295 ? 45.842 34.474  41.223 1.00 19.23 ? 295 ALA A CB  1 
ATOM   1788 N  N   . LEU A 1 296 ? 47.049 32.789  38.811 1.00 12.40 ? 296 LEU A N   1 
ATOM   1789 C  CA  . LEU A 1 296 ? 47.876 31.684  38.345 1.00 12.24 ? 296 LEU A CA  1 
ATOM   1790 C  C   . LEU A 1 296 ? 48.953 32.178  37.383 1.00 11.52 ? 296 LEU A C   1 
ATOM   1791 O  O   . LEU A 1 296 ? 50.104 31.746  37.477 1.00 14.60 ? 296 LEU A O   1 
ATOM   1792 C  CB  . LEU A 1 296 ? 46.987 30.599  37.697 1.00 10.38 ? 296 LEU A CB  1 
ATOM   1793 C  CG  . LEU A 1 296 ? 46.130 29.869  38.723 1.00 12.28 ? 296 LEU A CG  1 
ATOM   1794 C  CD1 . LEU A 1 296 ? 45.029 29.046  38.034 1.00 13.66 ? 296 LEU A CD1 1 
ATOM   1795 C  CD2 . LEU A 1 296 ? 46.981 28.977  39.626 1.00 13.32 ? 296 LEU A CD2 1 
ATOM   1796 N  N   . ARG A 1 297 ? 48.602 33.087  36.455 1.00 14.81 ? 297 ARG A N   1 
ATOM   1797 C  CA  . ARG A 1 297 ? 49.629 33.651  35.571 1.00 16.65 ? 297 ARG A CA  1 
ATOM   1798 C  C   . ARG A 1 297 ? 50.701 34.377  36.371 1.00 20.77 ? 297 ARG A C   1 
ATOM   1799 O  O   . ARG A 1 297 ? 51.892 34.254  36.072 1.00 21.29 ? 297 ARG A O   1 
ATOM   1800 C  CB  . ARG A 1 297 ? 49.009 34.596  34.541 1.00 21.32 ? 297 ARG A CB  1 
ATOM   1801 C  CG  . ARG A 1 297 ? 48.227 33.878  33.500 1.00 22.94 ? 297 ARG A CG  1 
ATOM   1802 C  CD  . ARG A 1 297 ? 49.131 32.846  32.797 1.00 18.51 ? 297 ARG A CD  1 
ATOM   1803 N  NE  . ARG A 1 297 ? 50.205 33.455  32.017 1.00 17.14 ? 297 ARG A NE  1 
ATOM   1804 C  CZ  . ARG A 1 297 ? 51.405 32.919  31.827 1.00 23.37 ? 297 ARG A CZ  1 
ATOM   1805 N  NH1 . ARG A 1 297 ? 51.736 31.743  32.334 1.00 19.95 ? 297 ARG A NH1 1 
ATOM   1806 N  NH2 . ARG A 1 297 ? 52.312 33.589  31.126 1.00 21.21 ? 297 ARG A NH2 1 
ATOM   1807 N  N   . GLU A 1 298 ? 50.300 35.128  37.402 1.00 20.71 ? 298 GLU A N   1 
ATOM   1808 C  CA  A GLU A 1 298 ? 51.294 35.848  38.189 0.49 22.44 ? 298 GLU A CA  1 
ATOM   1809 C  CA  B GLU A 1 298 ? 51.253 35.845  38.256 0.51 22.50 ? 298 GLU A CA  1 
ATOM   1810 C  C   . GLU A 1 298 ? 52.221 34.886  38.936 1.00 27.43 ? 298 GLU A C   1 
ATOM   1811 O  O   . GLU A 1 298 ? 53.402 35.203  39.127 1.00 32.72 ? 298 GLU A O   1 
ATOM   1812 C  CB  A GLU A 1 298 ? 50.577 36.846  39.113 0.49 22.99 ? 298 GLU A CB  1 
ATOM   1813 C  CB  B GLU A 1 298 ? 50.491 36.666  39.303 0.51 23.09 ? 298 GLU A CB  1 
ATOM   1814 C  CG  A GLU A 1 298 ? 49.843 37.945  38.307 0.49 22.56 ? 298 GLU A CG  1 
ATOM   1815 C  CG  B GLU A 1 298 ? 51.338 37.210  40.451 0.51 26.72 ? 298 GLU A CG  1 
ATOM   1816 C  CD  A GLU A 1 298 ? 48.916 38.853  39.136 0.49 33.17 ? 298 GLU A CD  1 
ATOM   1817 C  CD  B GLU A 1 298 ? 51.827 38.626  40.200 0.51 31.41 ? 298 GLU A CD  1 
ATOM   1818 O  OE1 A GLU A 1 298 ? 48.892 38.724  40.378 0.49 37.71 ? 298 GLU A OE1 1 
ATOM   1819 O  OE1 B GLU A 1 298 ? 51.944 39.016  39.020 0.51 38.04 ? 298 GLU A OE1 1 
ATOM   1820 O  OE2 A GLU A 1 298 ? 48.197 39.699  38.542 0.49 31.13 ? 298 GLU A OE2 1 
ATOM   1821 O  OE2 B GLU A 1 298 ? 52.086 39.350  41.186 0.51 31.78 ? 298 GLU A OE2 1 
ATOM   1822 N  N   . ALA A 1 299 ? 51.738 33.699  39.314 1.00 20.92 ? 299 ALA A N   1 
ATOM   1823 C  CA  . ALA A 1 299 ? 52.582 32.643  39.866 1.00 22.17 ? 299 ALA A CA  1 
ATOM   1824 C  C   . ALA A 1 299 ? 53.385 31.894  38.787 1.00 24.78 ? 299 ALA A C   1 
ATOM   1825 O  O   . ALA A 1 299 ? 54.015 30.878  39.107 1.00 29.93 ? 299 ALA A O   1 
ATOM   1826 C  CB  . ALA A 1 299 ? 51.720 31.665  40.657 1.00 21.68 ? 299 ALA A CB  1 
ATOM   1827 N  N   . ASP A 1 300 ? 53.323 32.339  37.524 1.00 18.30 ? 300 ASP A N   1 
ATOM   1828 C  CA  . ASP A 1 300 ? 54.075 31.733  36.409 1.00 19.72 ? 300 ASP A CA  1 
ATOM   1829 C  C   . ASP A 1 300 ? 53.619 30.299  36.116 1.00 19.74 ? 300 ASP A C   1 
ATOM   1830 O  O   . ASP A 1 300 ? 54.408 29.450  35.688 1.00 16.74 ? 300 ASP A O   1 
ATOM   1831 C  CB  . ASP A 1 300 ? 55.590 31.773  36.673 1.00 24.97 ? 300 ASP A CB  1 
ATOM   1832 C  CG  . ASP A 1 300 ? 56.431 31.617  35.396 1.00 27.14 ? 300 ASP A CG  1 
ATOM   1833 O  OD1 . ASP A 1 300 ? 55.950 31.976  34.301 1.00 31.51 ? 300 ASP A OD1 1 
ATOM   1834 O  OD2 . ASP A 1 300 ? 57.591 31.138  35.506 1.00 37.82 ? 300 ASP A OD2 1 
ATOM   1835 N  N   . VAL A 1 301 ? 52.333 30.004  36.303 1.00 14.14 ? 301 VAL A N   1 
ATOM   1836 C  CA  . VAL A 1 301 ? 51.817 28.697  35.913 1.00 11.67 ? 301 VAL A CA  1 
ATOM   1837 C  C   . VAL A 1 301 ? 51.677 28.652  34.401 1.00 11.91 ? 301 VAL A C   1 
ATOM   1838 O  O   . VAL A 1 301 ? 51.018 29.505  33.802 1.00 13.84 ? 301 VAL A O   1 
ATOM   1839 C  CB  . VAL A 1 301 ? 50.466 28.430  36.590 1.00 10.55 ? 301 VAL A CB  1 
ATOM   1840 C  CG1 . VAL A 1 301 ? 49.865 27.118  36.086 1.00 11.64 ? 301 VAL A CG1 1 
ATOM   1841 C  CG2 . VAL A 1 301 ? 50.654 28.417  38.101 1.00 11.69 ? 301 VAL A CG2 1 
ATOM   1842 N  N   . ASP A 1 302 ? 52.277 27.638  33.782 1.00 8.92  ? 302 ASP A N   1 
ATOM   1843 C  CA  . ASP A 1 302 ? 52.383 27.588  32.332 1.00 10.92 ? 302 ASP A CA  1 
ATOM   1844 C  C   . ASP A 1 302 ? 51.076 27.152  31.673 1.00 10.09 ? 302 ASP A C   1 
ATOM   1845 O  O   . ASP A 1 302 ? 50.732 27.660  30.602 1.00 11.43 ? 302 ASP A O   1 
ATOM   1846 C  CB  . ASP A 1 302 ? 53.513 26.624  31.918 1.00 11.92 ? 302 ASP A CB  1 
ATOM   1847 C  CG  . ASP A 1 302 ? 54.881 27.136  32.318 1.00 17.46 ? 302 ASP A CG  1 
ATOM   1848 O  OD1 . ASP A 1 302 ? 55.189 28.315  32.032 1.00 16.30 ? 302 ASP A OD1 1 
ATOM   1849 O  OD2 . ASP A 1 302 ? 55.651 26.362  32.906 1.00 14.32 ? 302 ASP A OD2 1 
ATOM   1850 N  N   . CYS A 1 303 ? 50.393 26.147  32.245 1.00 9.06  ? 303 CYS A N   1 
ATOM   1851 C  CA  . CYS A 1 303 ? 49.280 25.472  31.584 1.00 8.43  ? 303 CYS A CA  1 
ATOM   1852 C  C   . CYS A 1 303 ? 48.122 25.325  32.546 1.00 9.14  ? 303 CYS A C   1 
ATOM   1853 O  O   . CYS A 1 303 ? 48.322 25.144  33.742 1.00 7.55  ? 303 CYS A O   1 
ATOM   1854 C  CB  . CYS A 1 303 ? 49.670 24.066  31.123 1.00 11.49 ? 303 CYS A CB  1 
ATOM   1855 S  SG  . CYS A 1 303 ? 51.119 24.086  30.002 1.00 18.17 ? 303 CYS A SG  1 
ATOM   1856 N  N   . LEU A 1 304 ? 46.903 25.361  32.008 1.00 8.76  ? 304 LEU A N   1 
ATOM   1857 C  CA  . LEU A 1 304 ? 45.699 25.304  32.827 1.00 9.08  ? 304 LEU A CA  1 
ATOM   1858 C  C   . LEU A 1 304 ? 44.684 24.360  32.197 1.00 8.87  ? 304 LEU A C   1 
ATOM   1859 O  O   . LEU A 1 304 ? 44.550 24.337  30.970 1.00 9.18  ? 304 LEU A O   1 
ATOM   1860 C  CB  . LEU A 1 304 ? 45.069 26.704  32.929 1.00 10.62 ? 304 LEU A CB  1 
ATOM   1861 C  CG  . LEU A 1 304 ? 43.731 26.836  33.641 1.00 11.39 ? 304 LEU A CG  1 
ATOM   1862 C  CD1 . LEU A 1 304 ? 43.880 26.478  35.086 1.00 13.15 ? 304 LEU A CD1 1 
ATOM   1863 C  CD2 . LEU A 1 304 ? 43.190 28.288  33.494 1.00 13.53 ? 304 LEU A CD2 1 
ATOM   1864 N  N   . THR A 1 305 ? 43.952 23.588  33.025 1.00 7.06  ? 305 THR A N   1 
ATOM   1865 C  CA  . THR A 1 305 ? 42.783 22.879  32.521 1.00 7.73  ? 305 THR A CA  1 
ATOM   1866 C  C   . THR A 1 305 ? 41.570 23.285  33.343 1.00 7.74  ? 305 THR A C   1 
ATOM   1867 O  O   . THR A 1 305 ? 41.687 23.585  34.535 1.00 8.80  ? 305 THR A O   1 
ATOM   1868 C  CB  . THR A 1 305 ? 42.932 21.354  32.524 1.00 10.44 ? 305 THR A CB  1 
ATOM   1869 O  OG1 . THR A 1 305 ? 42.674 20.828  33.826 1.00 14.36 ? 305 THR A OG1 1 
ATOM   1870 C  CG2 . THR A 1 305 ? 44.342 20.928  32.083 1.00 10.40 ? 305 THR A CG2 1 
ATOM   1871 N  N   . LEU A 1 306 ? 40.418 23.382  32.668 1.00 7.82  ? 306 LEU A N   1 
ATOM   1872 C  CA  . LEU A 1 306 ? 39.124 23.647  33.300 1.00 7.16  ? 306 LEU A CA  1 
ATOM   1873 C  C   . LEU A 1 306 ? 38.144 22.588  32.821 1.00 8.39  ? 306 LEU A C   1 
ATOM   1874 O  O   . LEU A 1 306 ? 38.050 22.334  31.611 1.00 7.56  ? 306 LEU A O   1 
ATOM   1875 C  CB  . LEU A 1 306 ? 38.545 25.035  32.930 1.00 9.07  ? 306 LEU A CB  1 
ATOM   1876 C  CG  . LEU A 1 306 ? 39.387 26.296  33.174 1.00 10.60 ? 306 LEU A CG  1 
ATOM   1877 C  CD1 . LEU A 1 306 ? 40.073 26.630  31.896 1.00 16.10 ? 306 LEU A CD1 1 
ATOM   1878 C  CD2 . LEU A 1 306 ? 38.507 27.454  33.596 1.00 18.90 ? 306 LEU A CD2 1 
ATOM   1879 N  N   . GLY A 1 307 ? 37.401 21.973  33.752 1.00 7.62  ? 307 GLY A N   1 
ATOM   1880 C  CA  . GLY A 1 307 ? 36.481 20.920  33.360 1.00 7.23  ? 307 GLY A CA  1 
ATOM   1881 C  C   . GLY A 1 307 ? 35.303 20.946  34.308 1.00 7.37  ? 307 GLY A C   1 
ATOM   1882 O  O   . GLY A 1 307 ? 35.280 21.726  35.251 1.00 9.27  ? 307 GLY A O   1 
ATOM   1883 N  N   . GLN A 1 308 ? 34.307 20.114  34.011 1.00 7.91  ? 308 GLN A N   1 
ATOM   1884 C  CA  . GLN A 1 308 ? 33.078 20.108  34.807 1.00 7.77  ? 308 GLN A CA  1 
ATOM   1885 C  C   . GLN A 1 308 ? 33.237 19.267  36.064 1.00 8.89  ? 308 GLN A C   1 
ATOM   1886 O  O   . GLN A 1 308 ? 33.641 18.101  35.975 1.00 10.67 ? 308 GLN A O   1 
ATOM   1887 C  CB  . GLN A 1 308 ? 31.930 19.539  33.970 1.00 8.08  ? 308 GLN A CB  1 
ATOM   1888 C  CG  . GLN A 1 308 ? 30.611 19.346  34.714 1.00 8.39  ? 308 GLN A CG  1 
ATOM   1889 C  CD  . GLN A 1 308 ? 29.986 20.668  35.116 1.00 8.59  ? 308 GLN A CD  1 
ATOM   1890 O  OE1 . GLN A 1 308 ? 29.898 21.593  34.305 1.00 9.81  ? 308 GLN A OE1 1 
ATOM   1891 N  NE2 . GLN A 1 308 ? 29.463 20.736  36.362 1.00 8.68  ? 308 GLN A NE2 1 
ATOM   1892 N  N   . TYR A 1 309 ? 32.830 19.826  37.210 1.00 7.93  ? 309 TYR A N   1 
ATOM   1893 C  CA  . TYR A 1 309 ? 32.686 19.019  38.416 1.00 9.69  ? 309 TYR A CA  1 
ATOM   1894 C  C   . TYR A 1 309 ? 31.524 18.052  38.244 1.00 9.91  ? 309 TYR A C   1 
ATOM   1895 O  O   . TYR A 1 309 ? 30.401 18.473  37.922 1.00 10.24 ? 309 TYR A O   1 
ATOM   1896 C  CB  . TYR A 1 309 ? 32.449 19.910  39.638 1.00 8.19  ? 309 TYR A CB  1 
ATOM   1897 C  CG  . TYR A 1 309 ? 31.980 19.085  40.832 1.00 8.47  ? 309 TYR A CG  1 
ATOM   1898 C  CD1 . TYR A 1 309 ? 32.797 18.115  41.375 1.00 9.86  ? 309 TYR A CD1 1 
ATOM   1899 C  CD2 . TYR A 1 309 ? 30.695 19.231  41.342 1.00 9.95  ? 309 TYR A CD2 1 
ATOM   1900 C  CE1 . TYR A 1 309 ? 32.364 17.321  42.446 1.00 9.99  ? 309 TYR A CE1 1 
ATOM   1901 C  CE2 . TYR A 1 309 ? 30.262 18.443  42.441 1.00 10.66 ? 309 TYR A CE2 1 
ATOM   1902 C  CZ  . TYR A 1 309 ? 31.122 17.496  42.957 1.00 9.96  ? 309 TYR A CZ  1 
ATOM   1903 O  OH  . TYR A 1 309 ? 30.736 16.668  44.004 1.00 11.84 ? 309 TYR A OH  1 
ATOM   1904 N  N   . MET A 1 310 ? 31.792 16.756  38.448 1.00 10.38 ? 310 MET A N   1 
ATOM   1905 C  CA  . MET A 1 310 ? 30.776 15.716  38.394 1.00 13.66 ? 310 MET A CA  1 
ATOM   1906 C  C   . MET A 1 310 ? 30.675 15.058  39.757 1.00 11.51 ? 310 MET A C   1 
ATOM   1907 O  O   . MET A 1 310 ? 31.675 14.523  40.248 1.00 15.21 ? 310 MET A O   1 
ATOM   1908 C  CB  . MET A 1 310 ? 31.124 14.653  37.359 1.00 16.10 ? 310 MET A CB  1 
ATOM   1909 C  CG  . MET A 1 310 ? 31.377 15.226  35.996 1.00 18.38 ? 310 MET A CG  1 
ATOM   1910 S  SD  . MET A 1 310 ? 29.801 15.608  35.293 1.00 25.22 ? 310 MET A SD  1 
ATOM   1911 C  CE  . MET A 1 310 ? 29.224 13.956  34.846 1.00 24.75 ? 310 MET A CE  1 
ATOM   1912 N  N   . GLN A 1 311 ? 29.474 15.050  40.322 1.00 13.00 ? 311 GLN A N   1 
ATOM   1913 C  CA  . GLN A 1 311 ? 29.280 14.553  41.690 1.00 10.48 ? 311 GLN A CA  1 
ATOM   1914 C  C   . GLN A 1 311 ? 29.473 13.040  41.704 1.00 13.96 ? 311 GLN A C   1 
ATOM   1915 O  O   . GLN A 1 311 ? 28.730 12.330  41.019 1.00 16.18 ? 311 GLN A O   1 
ATOM   1916 C  CB  . GLN A 1 311 ? 27.884 14.926  42.181 1.00 12.79 ? 311 GLN A CB  1 
ATOM   1917 C  CG  . GLN A 1 311 ? 27.539 14.381  43.574 1.00 13.45 ? 311 GLN A CG  1 
ATOM   1918 C  CD  . GLN A 1 311 ? 26.076 14.589  43.902 1.00 17.64 ? 311 GLN A CD  1 
ATOM   1919 O  OE1 . GLN A 1 311 ? 25.215 14.477  43.030 1.00 22.48 ? 311 GLN A OE1 1 
ATOM   1920 N  NE2 . GLN A 1 311 ? 25.788 14.901  45.149 1.00 16.67 ? 311 GLN A NE2 1 
ATOM   1921 N  N   . PRO A 1 312 ? 30.449 12.505  42.450 1.00 13.95 ? 312 PRO A N   1 
ATOM   1922 C  CA  . PRO A 1 312 ? 30.702 11.049  42.386 1.00 13.10 ? 312 PRO A CA  1 
ATOM   1923 C  C   . PRO A 1 312 ? 29.613 10.200  43.028 1.00 16.85 ? 312 PRO A C   1 
ATOM   1924 O  O   . PRO A 1 312 ? 29.222 9.184   42.446 1.00 23.35 ? 312 PRO A O   1 
ATOM   1925 C  CB  . PRO A 1 312 ? 32.032 10.887  43.136 1.00 16.17 ? 312 PRO A CB  1 
ATOM   1926 C  CG  . PRO A 1 312 ? 32.670 12.221  43.106 1.00 21.30 ? 312 PRO A CG  1 
ATOM   1927 C  CD  . PRO A 1 312 ? 31.535 13.229  43.124 1.00 15.03 ? 312 PRO A CD  1 
ATOM   1928 N  N   . THR A 1 313 ? 29.120 10.592  44.206 1.00 17.24 ? 313 THR A N   1 
ATOM   1929 C  CA  . THR A 1 313 ? 28.039 9.906   44.922 1.00 17.82 ? 313 THR A CA  1 
ATOM   1930 C  C   . THR A 1 313 ? 27.145 10.950  45.588 1.00 23.07 ? 313 THR A C   1 
ATOM   1931 O  O   . THR A 1 313 ? 27.473 12.136  45.639 1.00 15.44 ? 313 THR A O   1 
ATOM   1932 C  CB  . THR A 1 313 ? 28.562 8.966   46.004 1.00 19.20 ? 313 THR A CB  1 
ATOM   1933 O  OG1 . THR A 1 313 ? 28.922 9.737   47.162 1.00 22.95 ? 313 THR A OG1 1 
ATOM   1934 C  CG2 . THR A 1 313 ? 29.780 8.160   45.533 1.00 19.92 ? 313 THR A CG2 1 
ATOM   1935 N  N   . ARG A 1 314 ? 26.017 10.501  46.160 1.00 22.42 ? 314 ARG A N   1 
ATOM   1936 C  CA  A ARG A 1 314 ? 25.117 11.450  46.803 0.47 23.40 ? 314 ARG A CA  1 
ATOM   1937 C  CA  B ARG A 1 314 ? 25.103 11.420  46.835 0.53 23.45 ? 314 ARG A CA  1 
ATOM   1938 C  C   . ARG A 1 314 ? 25.726 12.099  48.048 1.00 18.68 ? 314 ARG A C   1 
ATOM   1939 O  O   . ARG A 1 314 ? 25.264 13.176  48.443 1.00 25.17 ? 314 ARG A O   1 
ATOM   1940 C  CB  A ARG A 1 314 ? 23.782 10.768  47.132 0.47 25.56 ? 314 ARG A CB  1 
ATOM   1941 C  CB  B ARG A 1 314 ? 23.838 10.689  47.282 0.53 25.64 ? 314 ARG A CB  1 
ATOM   1942 C  CG  A ARG A 1 314 ? 22.945 10.478  45.887 0.47 27.22 ? 314 ARG A CG  1 
ATOM   1943 C  CG  B ARG A 1 314 ? 22.910 10.333  46.164 0.53 26.92 ? 314 ARG A CG  1 
ATOM   1944 C  CD  A ARG A 1 314 ? 21.647 9.736   46.197 0.47 32.26 ? 314 ARG A CD  1 
ATOM   1945 C  CD  B ARG A 1 314 ? 21.860 9.355   46.652 0.53 34.14 ? 314 ARG A CD  1 
ATOM   1946 N  NE  A ARG A 1 314 ? 20.698 10.532  46.970 0.47 38.94 ? 314 ARG A NE  1 
ATOM   1947 N  NE  B ARG A 1 314 ? 20.943 9.941   47.623 0.53 37.82 ? 314 ARG A NE  1 
ATOM   1948 C  CZ  A ARG A 1 314 ? 19.551 10.065  47.450 0.47 36.04 ? 314 ARG A CZ  1 
ATOM   1949 C  CZ  B ARG A 1 314 ? 19.830 10.591  47.299 0.53 36.48 ? 314 ARG A CZ  1 
ATOM   1950 N  NH1 A ARG A 1 314 ? 19.174 8.811   47.246 0.47 35.61 ? 314 ARG A NH1 1 
ATOM   1951 N  NH1 B ARG A 1 314 ? 18.945 10.947  48.217 0.53 40.24 ? 314 ARG A NH1 1 
ATOM   1952 N  NH2 A ARG A 1 314 ? 18.765 10.872  48.157 0.47 39.91 ? 314 ARG A NH2 1 
ATOM   1953 N  NH2 B ARG A 1 314 ? 19.596 10.881  46.020 0.53 35.73 ? 314 ARG A NH2 1 
ATOM   1954 N  N   . ARG A 1 315 ? 26.764 11.506  48.648 1.00 19.70 ? 315 ARG A N   1 
ATOM   1955 C  CA  . ARG A 1 315 ? 27.408 12.146  49.797 1.00 22.48 ? 315 ARG A CA  1 
ATOM   1956 C  C   . ARG A 1 315 ? 28.258 13.335  49.370 1.00 15.79 ? 315 ARG A C   1 
ATOM   1957 O  O   . ARG A 1 315 ? 28.554 14.218  50.183 1.00 17.21 ? 315 ARG A O   1 
ATOM   1958 C  CB  . ARG A 1 315 ? 28.287 11.138  50.563 1.00 29.20 ? 315 ARG A CB  1 
ATOM   1959 C  CG  . ARG A 1 315 ? 29.783 11.510  50.622 1.00 32.90 ? 315 ARG A CG  1 
ATOM   1960 C  CD  . ARG A 1 315 ? 30.580 10.834  51.748 1.00 31.28 ? 315 ARG A CD  1 
ATOM   1961 N  NE  . ARG A 1 315 ? 31.750 10.155  51.202 1.00 25.36 ? 315 ARG A NE  1 
ATOM   1962 C  CZ  . ARG A 1 315 ? 32.892 10.739  50.852 1.00 28.87 ? 315 ARG A CZ  1 
ATOM   1963 N  NH1 . ARG A 1 315 ? 33.893 10.044  50.345 1.00 20.70 ? 315 ARG A NH1 1 
ATOM   1964 N  NH2 . ARG A 1 315 ? 33.033 12.053  51.011 1.00 27.05 ? 315 ARG A NH2 1 
ATOM   1965 N  N   . HIS A 1 316 ? 28.663 13.377  48.104 1.00 12.33 ? 316 HIS A N   1 
ATOM   1966 C  CA  . HIS A 1 316 ? 29.574 14.420  47.665 1.00 12.64 ? 316 HIS A CA  1 
ATOM   1967 C  C   . HIS A 1 316 ? 28.810 15.701  47.343 1.00 11.23 ? 316 HIS A C   1 
ATOM   1968 O  O   . HIS A 1 316 ? 27.577 15.728  47.316 1.00 13.42 ? 316 HIS A O   1 
ATOM   1969 C  CB  . HIS A 1 316 ? 30.380 13.932  46.454 1.00 11.76 ? 316 HIS A CB  1 
ATOM   1970 C  CG  . HIS A 1 316 ? 31.367 12.854  46.786 1.00 13.75 ? 316 HIS A CG  1 
ATOM   1971 N  ND1 . HIS A 1 316 ? 31.011 11.526  46.901 1.00 13.77 ? 316 HIS A ND1 1 
ATOM   1972 C  CD2 . HIS A 1 316 ? 32.690 12.916  47.077 1.00 13.61 ? 316 HIS A CD2 1 
ATOM   1973 C  CE1 . HIS A 1 316 ? 32.079 10.815  47.224 1.00 16.20 ? 316 HIS A CE1 1 
ATOM   1974 N  NE2 . HIS A 1 316 ? 33.108 11.635  47.340 1.00 13.21 ? 316 HIS A NE2 1 
ATOM   1975 N  N   . LEU A 1 317 ? 29.552 16.790  47.103 1.00 10.80 ? 317 LEU A N   1 
ATOM   1976 C  CA  . LEU A 1 317 ? 28.908 18.075  46.832 1.00 10.78 ? 317 LEU A CA  1 
ATOM   1977 C  C   . LEU A 1 317 ? 27.939 17.952  45.667 1.00 11.50 ? 317 LEU A C   1 
ATOM   1978 O  O   . LEU A 1 317 ? 28.232 17.304  44.666 1.00 12.95 ? 317 LEU A O   1 
ATOM   1979 C  CB  . LEU A 1 317 ? 29.917 19.170  46.488 1.00 13.40 ? 317 LEU A CB  1 
ATOM   1980 C  CG  . LEU A 1 317 ? 30.933 19.512  47.596 1.00 13.50 ? 317 LEU A CG  1 
ATOM   1981 C  CD1 . LEU A 1 317 ? 32.083 20.310  46.990 1.00 18.77 ? 317 LEU A CD1 1 
ATOM   1982 C  CD2 . LEU A 1 317 ? 30.244 20.308  48.691 1.00 22.98 ? 317 LEU A CD2 1 
ATOM   1983 N  N   . LYS A 1 318 ? 26.788 18.589  45.798 1.00 12.12 ? 318 LYS A N   1 
ATOM   1984 C  CA  . LYS A 1 318 ? 25.904 18.681  44.645 1.00 13.04 ? 318 LYS A CA  1 
ATOM   1985 C  C   . LYS A 1 318 ? 26.546 19.526  43.546 1.00 14.67 ? 318 LYS A C   1 
ATOM   1986 O  O   . LYS A 1 318 ? 27.258 20.499  43.812 1.00 13.28 ? 318 LYS A O   1 
ATOM   1987 C  CB  . LYS A 1 318 ? 24.561 19.293  45.049 1.00 15.25 ? 318 LYS A CB  1 
ATOM   1988 C  CG  . LYS A 1 318 ? 23.713 18.290  45.818 1.00 21.79 ? 318 LYS A CG  1 
ATOM   1989 C  CD  . LYS A 1 318 ? 22.290 18.771  46.069 1.00 32.04 ? 318 LYS A CD  1 
ATOM   1990 C  CE  . LYS A 1 318 ? 21.484 17.644  46.721 1.00 37.51 ? 318 LYS A CE  1 
ATOM   1991 N  NZ  . LYS A 1 318 ? 20.318 18.116  47.524 1.00 44.00 ? 318 LYS A NZ  1 
ATOM   1992 N  N   . VAL A 1 319 ? 26.212 19.196  42.295 1.00 12.23 ? 319 VAL A N   1 
ATOM   1993 C  CA  . VAL A 1 319 ? 26.592 20.081  41.187 1.00 11.38 ? 319 VAL A CA  1 
ATOM   1994 C  C   . VAL A 1 319 ? 25.731 21.332  41.215 1.00 10.70 ? 319 VAL A C   1 
ATOM   1995 O  O   . VAL A 1 319 ? 24.494 21.241  41.253 1.00 12.93 ? 319 VAL A O   1 
ATOM   1996 C  CB  . VAL A 1 319 ? 26.417 19.365  39.846 1.00 11.10 ? 319 VAL A CB  1 
ATOM   1997 C  CG1 . VAL A 1 319 ? 26.707 20.336  38.688 1.00 12.65 ? 319 VAL A CG1 1 
ATOM   1998 C  CG2 . VAL A 1 319 ? 27.325 18.137  39.787 1.00 12.46 ? 319 VAL A CG2 1 
ATOM   1999 N  N   . GLU A 1 320 ? 26.367 22.512  41.162 1.00 11.19 ? 320 GLU A N   1 
ATOM   2000 C  CA  . GLU A 1 320 ? 25.559 23.735  41.123 1.00 12.02 ? 320 GLU A CA  1 
ATOM   2001 C  C   . GLU A 1 320 ? 24.989 24.006  39.734 1.00 12.51 ? 320 GLU A C   1 
ATOM   2002 O  O   . GLU A 1 320 ? 23.879 24.551  39.607 1.00 14.03 ? 320 GLU A O   1 
ATOM   2003 C  CB  . GLU A 1 320 ? 26.366 24.943  41.600 1.00 13.19 ? 320 GLU A CB  1 
ATOM   2004 C  CG  . GLU A 1 320 ? 26.722 24.841  43.088 1.00 14.85 ? 320 GLU A CG  1 
ATOM   2005 C  CD  . GLU A 1 320 ? 25.494 24.912  43.987 1.00 22.65 ? 320 GLU A CD  1 
ATOM   2006 O  OE1 . GLU A 1 320 ? 24.592 25.730  43.722 1.00 31.09 ? 320 GLU A OE1 1 
ATOM   2007 O  OE2 . GLU A 1 320 ? 25.424 24.126  44.944 1.00 35.04 ? 320 GLU A OE2 1 
ATOM   2008 N  N   . GLU A 1 321 ? 25.734 23.651  38.686 1.00 11.66 ? 321 GLU A N   1 
ATOM   2009 C  CA  . GLU A 1 321 ? 25.239 23.793  37.326 1.00 11.66 ? 321 GLU A CA  1 
ATOM   2010 C  C   . GLU A 1 321 ? 26.208 23.083  36.406 1.00 10.47 ? 321 GLU A C   1 
ATOM   2011 O  O   . GLU A 1 321 ? 27.389 22.965  36.735 1.00 11.29 ? 321 GLU A O   1 
ATOM   2012 C  CB  . GLU A 1 321 ? 25.107 25.265  36.939 1.00 18.40 ? 321 GLU A CB  1 
ATOM   2013 C  CG  . GLU A 1 321 ? 26.374 26.040  36.917 1.00 22.87 ? 321 GLU A CG  1 
ATOM   2014 C  CD  . GLU A 1 321 ? 26.108 27.491  36.505 1.00 34.14 ? 321 GLU A CD  1 
ATOM   2015 O  OE1 . GLU A 1 321 ? 26.383 28.410  37.311 1.00 40.29 ? 321 GLU A OE1 1 
ATOM   2016 O  OE2 . GLU A 1 321 ? 25.596 27.702  35.382 1.00 23.92 ? 321 GLU A OE2 1 
ATOM   2017 N  N   . TYR A 1 322 ? 25.703 22.584  35.284 1.00 10.19 ? 322 TYR A N   1 
ATOM   2018 C  CA  . TYR A 1 322 ? 26.560 22.083  34.212 1.00 9.86  ? 322 TYR A CA  1 
ATOM   2019 C  C   . TYR A 1 322 ? 26.907 23.253  33.302 1.00 10.21 ? 322 TYR A C   1 
ATOM   2020 O  O   . TYR A 1 322 ? 26.003 23.892  32.734 1.00 10.73 ? 322 TYR A O   1 
ATOM   2021 C  CB  . TYR A 1 322 ? 25.874 20.949  33.438 1.00 9.94  ? 322 TYR A CB  1 
ATOM   2022 C  CG  . TYR A 1 322 ? 25.698 19.755  34.333 1.00 10.67 ? 322 TYR A CG  1 
ATOM   2023 C  CD1 . TYR A 1 322 ? 26.786 19.037  34.738 1.00 10.99 ? 322 TYR A CD1 1 
ATOM   2024 C  CD2 . TYR A 1 322 ? 24.434 19.371  34.803 1.00 16.58 ? 322 TYR A CD2 1 
ATOM   2025 C  CE1 . TYR A 1 322 ? 26.643 17.939  35.599 1.00 12.51 ? 322 TYR A CE1 1 
ATOM   2026 C  CE2 . TYR A 1 322 ? 24.292 18.274  35.654 1.00 17.77 ? 322 TYR A CE2 1 
ATOM   2027 C  CZ  . TYR A 1 322 ? 25.413 17.576  36.050 1.00 16.18 ? 322 TYR A CZ  1 
ATOM   2028 O  OH  . TYR A 1 322 ? 25.300 16.482  36.901 1.00 19.58 ? 322 TYR A OH  1 
ATOM   2029 N  N   . ILE A 1 323 ? 28.202 23.586  33.246 1.00 9.30  ? 323 ILE A N   1 
ATOM   2030 C  CA  . ILE A 1 323 ? 28.707 24.686  32.435 1.00 9.79  ? 323 ILE A CA  1 
ATOM   2031 C  C   . ILE A 1 323 ? 28.645 24.286  30.965 1.00 9.49  ? 323 ILE A C   1 
ATOM   2032 O  O   . ILE A 1 323 ? 28.883 23.132  30.605 1.00 9.68  ? 323 ILE A O   1 
ATOM   2033 C  CB  . ILE A 1 323 ? 30.140 25.018  32.885 1.00 9.60  ? 323 ILE A CB  1 
ATOM   2034 C  CG1 . ILE A 1 323 ? 30.161 25.359  34.391 1.00 13.21 ? 323 ILE A CG1 1 
ATOM   2035 C  CG2 . ILE A 1 323 ? 30.794 26.109  31.992 1.00 11.53 ? 323 ILE A CG2 1 
ATOM   2036 C  CD1 . ILE A 1 323 ? 29.465 26.657  34.763 1.00 16.27 ? 323 ILE A CD1 1 
ATOM   2037 N  N   . THR A 1 324 ? 28.250 25.216  30.114 1.00 9.87  ? 324 THR A N   1 
ATOM   2038 C  CA  . THR A 1 324 ? 27.966 24.825  28.751 1.00 10.18 ? 324 THR A CA  1 
ATOM   2039 C  C   . THR A 1 324 ? 29.248 24.660  27.933 1.00 9.95  ? 324 THR A C   1 
ATOM   2040 O  O   . THR A 1 324 ? 30.304 25.219  28.267 1.00 9.65  ? 324 THR A O   1 
ATOM   2041 C  CB  . THR A 1 324 ? 27.113 25.878  28.043 1.00 10.77 ? 324 THR A CB  1 
ATOM   2042 O  OG1 . THR A 1 324 ? 27.860 27.102  28.045 1.00 11.14 ? 324 THR A OG1 1 
ATOM   2043 C  CG2 . THR A 1 324 ? 25.729 26.085  28.702 1.00 11.13 ? 324 THR A CG2 1 
ATOM   2044 N  N   . PRO A 1 325 ? 29.163 23.934  26.825 1.00 10.18 ? 325 PRO A N   1 
ATOM   2045 C  CA  . PRO A 1 325 ? 30.328 23.803  25.943 1.00 10.09 ? 325 PRO A CA  1 
ATOM   2046 C  C   . PRO A 1 325 ? 30.872 25.137  25.478 1.00 10.25 ? 325 PRO A C   1 
ATOM   2047 O  O   . PRO A 1 325 ? 32.099 25.329  25.451 1.00 10.15 ? 325 PRO A O   1 
ATOM   2048 C  CB  . PRO A 1 325 ? 29.770 22.985  24.777 1.00 10.96 ? 325 PRO A CB  1 
ATOM   2049 C  CG  . PRO A 1 325 ? 28.706 22.109  25.420 1.00 11.03 ? 325 PRO A CG  1 
ATOM   2050 C  CD  . PRO A 1 325 ? 28.063 23.030  26.424 1.00 10.63 ? 325 PRO A CD  1 
ATOM   2051 N  N   . GLU A 1 326 ? 29.999 26.079  25.124 1.00 10.75 ? 326 GLU A N   1 
ATOM   2052 C  CA  . GLU A 1 326 ? 30.517 27.343  24.625 1.00 12.43 ? 326 GLU A CA  1 
ATOM   2053 C  C   . GLU A 1 326 ? 31.095 28.187  25.739 1.00 11.42 ? 326 GLU A C   1 
ATOM   2054 O  O   . GLU A 1 326 ? 32.006 28.987  25.482 1.00 11.10 ? 326 GLU A O   1 
ATOM   2055 C  CB  . GLU A 1 326 ? 29.424 28.100  23.874 1.00 12.76 ? 326 GLU A CB  1 
ATOM   2056 C  CG  . GLU A 1 326 ? 29.140 27.485  22.485 1.00 12.96 ? 326 GLU A CG  1 
ATOM   2057 C  CD  . GLU A 1 326 ? 30.382 27.417  21.555 1.00 20.79 ? 326 GLU A CD  1 
ATOM   2058 O  OE1 . GLU A 1 326 ? 31.204 28.349  21.558 1.00 24.56 ? 326 GLU A OE1 1 
ATOM   2059 O  OE2 . GLU A 1 326 ? 30.522 26.403  20.846 1.00 31.42 ? 326 GLU A OE2 1 
ATOM   2060 N  N   . LYS A 1 327 ? 30.600 28.039  26.977 1.00 10.45 ? 327 LYS A N   1 
ATOM   2061 C  CA  . LYS A 1 327 ? 31.215 28.797  28.059 1.00 10.23 ? 327 LYS A CA  1 
ATOM   2062 C  C   . LYS A 1 327 ? 32.612 28.254  28.348 1.00 11.07 ? 327 LYS A C   1 
ATOM   2063 O  O   . LYS A 1 327 ? 33.534 29.040  28.612 1.00 11.30 ? 327 LYS A O   1 
ATOM   2064 C  CB  . LYS A 1 327 ? 30.349 28.785  29.328 1.00 12.44 ? 327 LYS A CB  1 
ATOM   2065 C  CG  . LYS A 1 327 ? 30.829 29.810  30.379 1.00 12.93 ? 327 LYS A CG  1 
ATOM   2066 C  CD  . LYS A 1 327 ? 30.589 31.248  29.912 1.00 17.54 ? 327 LYS A CD  1 
ATOM   2067 C  CE  . LYS A 1 327 ? 30.985 32.241  30.998 1.00 22.76 ? 327 LYS A CE  1 
ATOM   2068 N  NZ  . LYS A 1 327 ? 30.032 32.178  32.140 1.00 24.40 ? 327 LYS A NZ  1 
ATOM   2069 N  N   . PHE A 1 328 ? 32.801 26.930  28.247 1.00 9.40  ? 328 PHE A N   1 
ATOM   2070 C  CA  . PHE A 1 328 ? 34.165 26.405  28.369 1.00 9.32  ? 328 PHE A CA  1 
ATOM   2071 C  C   . PHE A 1 328 ? 35.053 26.965  27.263 1.00 10.24 ? 328 PHE A C   1 
ATOM   2072 O  O   . PHE A 1 328 ? 36.239 27.247  27.497 1.00 11.27 ? 328 PHE A O   1 
ATOM   2073 C  CB  . PHE A 1 328 ? 34.189 24.870  28.344 1.00 9.08  ? 328 PHE A CB  1 
ATOM   2074 C  CG  . PHE A 1 328 ? 33.894 24.236  29.687 1.00 8.39  ? 328 PHE A CG  1 
ATOM   2075 C  CD1 . PHE A 1 328 ? 34.835 24.261  30.724 1.00 8.35  ? 328 PHE A CD1 1 
ATOM   2076 C  CD2 . PHE A 1 328 ? 32.668 23.619  29.923 1.00 8.53  ? 328 PHE A CD2 1 
ATOM   2077 C  CE1 . PHE A 1 328 ? 34.542 23.654  31.962 1.00 8.68  ? 328 PHE A CE1 1 
ATOM   2078 C  CE2 . PHE A 1 328 ? 32.368 23.048  31.139 1.00 8.59  ? 328 PHE A CE2 1 
ATOM   2079 C  CZ  . PHE A 1 328 ? 33.284 23.063  32.166 1.00 10.10 ? 328 PHE A CZ  1 
ATOM   2080 N  N   . LYS A 1 329 ? 34.498 27.135  26.053 1.00 9.64  ? 329 LYS A N   1 
ATOM   2081 C  CA  . LYS A 1 329 ? 35.305 27.693  24.973 1.00 10.58 ? 329 LYS A CA  1 
ATOM   2082 C  C   . LYS A 1 329 ? 35.654 29.148  25.236 1.00 11.33 ? 329 LYS A C   1 
ATOM   2083 O  O   . LYS A 1 329 ? 36.737 29.605  24.833 1.00 13.17 ? 329 LYS A O   1 
ATOM   2084 C  CB  . LYS A 1 329 ? 34.577 27.534  23.630 1.00 14.92 ? 329 LYS A CB  1 
ATOM   2085 C  CG  . LYS A 1 329 ? 34.531 26.080  23.205 1.00 13.36 ? 329 LYS A CG  1 
ATOM   2086 C  CD  . LYS A 1 329 ? 33.860 25.847  21.864 1.00 16.58 ? 329 LYS A CD  1 
ATOM   2087 C  CE  . LYS A 1 329 ? 33.561 24.365  21.663 1.00 23.97 ? 329 LYS A CE  1 
ATOM   2088 N  NZ  . LYS A 1 329 ? 32.676 24.210  20.464 1.00 26.14 ? 329 LYS A NZ  1 
ATOM   2089 N  N   . TYR A 1 330 ? 34.771 29.881  25.904 1.00 11.76 ? 330 TYR A N   1 
ATOM   2090 C  CA  . TYR A 1 330 ? 35.107 31.224  26.352 1.00 10.68 ? 330 TYR A CA  1 
ATOM   2091 C  C   . TYR A 1 330 ? 36.306 31.194  27.288 1.00 10.26 ? 330 TYR A C   1 
ATOM   2092 O  O   . TYR A 1 330 ? 37.249 31.975  27.139 1.00 10.61 ? 330 TYR A O   1 
ATOM   2093 C  CB  . TYR A 1 330 ? 33.901 31.870  27.025 1.00 11.33 ? 330 TYR A CB  1 
ATOM   2094 C  CG  . TYR A 1 330 ? 34.243 33.108  27.828 1.00 12.12 ? 330 TYR A CG  1 
ATOM   2095 C  CD1 . TYR A 1 330 ? 34.590 34.293  27.180 1.00 12.97 ? 330 TYR A CD1 1 
ATOM   2096 C  CD2 . TYR A 1 330 ? 34.257 33.084  29.226 1.00 12.16 ? 330 TYR A CD2 1 
ATOM   2097 C  CE1 . TYR A 1 330 ? 34.898 35.430  27.910 1.00 16.56 ? 330 TYR A CE1 1 
ATOM   2098 C  CE2 . TYR A 1 330 ? 34.545 34.231  29.962 1.00 14.24 ? 330 TYR A CE2 1 
ATOM   2099 C  CZ  . TYR A 1 330 ? 34.880 35.392  29.284 1.00 17.17 ? 330 TYR A CZ  1 
ATOM   2100 O  OH  . TYR A 1 330 ? 35.198 36.525  29.978 1.00 24.39 ? 330 TYR A OH  1 
ATOM   2101 N  N   . TRP A 1 331 ? 36.297 30.285  28.260 1.00 9.72  ? 331 TRP A N   1 
ATOM   2102 C  CA  . TRP A 1 331 ? 37.433 30.289  29.186 1.00 9.54  ? 331 TRP A CA  1 
ATOM   2103 C  C   . TRP A 1 331 ? 38.728 29.894  28.508 1.00 10.85 ? 331 TRP A C   1 
ATOM   2104 O  O   . TRP A 1 331 ? 39.800 30.352  28.947 1.00 11.01 ? 331 TRP A O   1 
ATOM   2105 C  CB  . TRP A 1 331 ? 37.161 29.376  30.388 1.00 10.73 ? 331 TRP A CB  1 
ATOM   2106 C  CG  . TRP A 1 331 ? 36.092 29.935  31.288 1.00 10.52 ? 331 TRP A CG  1 
ATOM   2107 C  CD1 . TRP A 1 331 ? 34.875 29.367  31.580 1.00 11.17 ? 331 TRP A CD1 1 
ATOM   2108 C  CD2 . TRP A 1 331 ? 36.125 31.198  31.980 1.00 12.36 ? 331 TRP A CD2 1 
ATOM   2109 N  NE1 . TRP A 1 331 ? 34.160 30.201  32.428 1.00 13.12 ? 331 TRP A NE1 1 
ATOM   2110 C  CE2 . TRP A 1 331 ? 34.904 31.332  32.672 1.00 13.30 ? 331 TRP A CE2 1 
ATOM   2111 C  CE3 . TRP A 1 331 ? 37.079 32.228  32.077 1.00 13.12 ? 331 TRP A CE3 1 
ATOM   2112 C  CZ2 . TRP A 1 331 ? 34.615 32.450  33.469 1.00 12.34 ? 331 TRP A CZ2 1 
ATOM   2113 C  CZ3 . TRP A 1 331 ? 36.782 33.344  32.865 1.00 15.18 ? 331 TRP A CZ3 1 
ATOM   2114 C  CH2 . TRP A 1 331 ? 35.559 33.439  33.548 1.00 14.44 ? 331 TRP A CH2 1 
ATOM   2115 N  N   . GLU A 1 332 ? 38.678 29.039  27.478 1.00 9.54  ? 332 GLU A N   1 
ATOM   2116 C  CA  . GLU A 1 332 ? 39.879 28.767  26.672 1.00 10.26 ? 332 GLU A CA  1 
ATOM   2117 C  C   . GLU A 1 332 ? 40.417 30.051  26.051 1.00 13.29 ? 332 GLU A C   1 
ATOM   2118 O  O   . GLU A 1 332 ? 41.628 30.317  26.074 1.00 12.94 ? 332 GLU A O   1 
ATOM   2119 C  CB  . GLU A 1 332 ? 39.566 27.751  25.577 1.00 11.96 ? 332 GLU A CB  1 
ATOM   2120 C  CG  . GLU A 1 332 ? 40.768 27.360  24.707 1.00 16.36 ? 332 GLU A CG  1 
ATOM   2121 C  CD  . GLU A 1 332 ? 40.367 26.508  23.502 1.00 27.89 ? 332 GLU A CD  1 
ATOM   2122 O  OE1 . GLU A 1 332 ? 39.152 26.319  23.260 1.00 39.32 ? 332 GLU A OE1 1 
ATOM   2123 O  OE2 . GLU A 1 332 ? 41.277 26.050  22.772 1.00 38.15 ? 332 GLU A OE2 1 
ATOM   2124 N  N   . LYS A 1 333 ? 39.523 30.855  25.468 1.00 12.05 ? 333 LYS A N   1 
ATOM   2125 C  CA  . LYS A 1 333 ? 39.918 32.140  24.878 1.00 12.25 ? 333 LYS A CA  1 
ATOM   2126 C  C   . LYS A 1 333 ? 40.548 33.060  25.919 1.00 14.28 ? 333 LYS A C   1 
ATOM   2127 O  O   . LYS A 1 333 ? 41.579 33.696  25.659 1.00 14.35 ? 333 LYS A O   1 
ATOM   2128 C  CB  . LYS A 1 333 ? 38.675 32.784  24.251 1.00 15.74 ? 333 LYS A CB  1 
ATOM   2129 C  CG  . LYS A 1 333 ? 38.824 34.172  23.665 1.00 26.55 ? 333 LYS A CG  1 
ATOM   2130 C  CD  . LYS A 1 333 ? 37.431 34.755  23.354 1.00 31.56 ? 333 LYS A CD  1 
ATOM   2131 C  CE  . LYS A 1 333 ? 37.361 36.246  23.715 1.00 41.44 ? 333 LYS A CE  1 
ATOM   2132 N  NZ  . LYS A 1 333 ? 35.983 36.703  24.122 1.00 37.60 ? 333 LYS A NZ  1 
ATOM   2133 N  N   . VAL A 1 334 ? 39.953 33.124  27.119 1.00 12.64 ? 334 VAL A N   1 
ATOM   2134 C  CA  . VAL A 1 334 ? 40.489 33.929  28.206 1.00 13.47 ? 334 VAL A CA  1 
ATOM   2135 C  C   . VAL A 1 334 ? 41.868 33.431  28.577 1.00 11.64 ? 334 VAL A C   1 
ATOM   2136 O  O   . VAL A 1 334 ? 42.788 34.228  28.770 1.00 15.27 ? 334 VAL A O   1 
ATOM   2137 C  CB  . VAL A 1 334 ? 39.554 33.913  29.432 1.00 12.96 ? 334 VAL A CB  1 
ATOM   2138 C  CG1 . VAL A 1 334 ? 40.223 34.544  30.644 1.00 16.78 ? 334 VAL A CG1 1 
ATOM   2139 C  CG2 . VAL A 1 334 ? 38.260 34.682  29.121 1.00 13.77 ? 334 VAL A CG2 1 
ATOM   2140 N  N   . GLY A 1 335 ? 42.034 32.108  28.677 1.00 10.87 ? 335 GLY A N   1 
ATOM   2141 C  CA  . GLY A 1 335 ? 43.341 31.570  29.015 1.00 12.10 ? 335 GLY A CA  1 
ATOM   2142 C  C   . GLY A 1 335 ? 44.381 31.942  27.972 1.00 12.37 ? 335 GLY A C   1 
ATOM   2143 O  O   . GLY A 1 335 ? 45.502 32.355  28.311 1.00 14.74 ? 335 GLY A O   1 
ATOM   2144 N  N   . ASN A 1 336 ? 44.002 31.864  26.694 1.00 12.29 ? 336 ASN A N   1 
ATOM   2145 C  CA  . ASN A 1 336 ? 44.917 32.246  25.618 1.00 15.50 ? 336 ASN A CA  1 
ATOM   2146 C  C   . ASN A 1 336 ? 45.331 33.703  25.766 1.00 14.79 ? 336 ASN A C   1 
ATOM   2147 O  O   . ASN A 1 336 ? 46.516 34.047  25.623 1.00 16.49 ? 336 ASN A O   1 
ATOM   2148 C  CB  . ASN A 1 336 ? 44.269 32.006  24.247 1.00 16.57 ? 336 ASN A CB  1 
ATOM   2149 C  CG  . ASN A 1 336 ? 44.121 30.534  23.913 1.00 20.19 ? 336 ASN A CG  1 
ATOM   2150 O  OD1 . ASN A 1 336 ? 44.738 29.683  24.538 1.00 21.85 ? 336 ASN A OD1 1 
ATOM   2151 N  ND2 . ASN A 1 336 ? 43.291 30.225  22.920 1.00 20.25 ? 336 ASN A ND2 1 
ATOM   2152 N  N   . GLU A 1 337 ? 44.365 34.575  26.057 1.00 14.40 ? 337 GLU A N   1 
ATOM   2153 C  CA  . GLU A 1 337 ? 44.660 35.997  26.161 1.00 18.03 ? 337 GLU A CA  1 
ATOM   2154 C  C   . GLU A 1 337 ? 45.515 36.319  27.376 1.00 17.78 ? 337 GLU A C   1 
ATOM   2155 O  O   . GLU A 1 337 ? 46.344 37.228  27.313 1.00 20.38 ? 337 GLU A O   1 
ATOM   2156 C  CB  . GLU A 1 337 ? 43.355 36.785  26.177 1.00 26.91 ? 337 GLU A CB  1 
ATOM   2157 C  CG  . GLU A 1 337 ? 42.620 36.637  24.857 1.00 23.15 ? 337 GLU A CG  1 
ATOM   2158 C  CD  . GLU A 1 337 ? 41.152 37.046  24.911 1.00 42.02 ? 337 GLU A CD  1 
ATOM   2159 O  OE1 . GLU A 1 337 ? 40.651 37.384  26.014 1.00 45.85 ? 337 GLU A OE1 1 
ATOM   2160 O  OE2 . GLU A 1 337 ? 40.493 37.017  23.838 1.00 41.97 ? 337 GLU A OE2 1 
ATOM   2161 N  N   . LEU A 1 338 ? 45.350 35.590  28.479 1.00 14.50 ? 338 LEU A N   1 
ATOM   2162 C  CA  . LEU A 1 338 ? 46.188 35.815  29.642 1.00 14.21 ? 338 LEU A CA  1 
ATOM   2163 C  C   . LEU A 1 338 ? 47.584 35.225  29.498 1.00 19.10 ? 338 LEU A C   1 
ATOM   2164 O  O   . LEU A 1 338 ? 48.417 35.460  30.382 1.00 18.69 ? 338 LEU A O   1 
ATOM   2165 C  CB  . LEU A 1 338 ? 45.531 35.221  30.882 1.00 14.93 ? 338 LEU A CB  1 
ATOM   2166 C  CG  . LEU A 1 338 ? 44.262 35.938  31.371 1.00 16.12 ? 338 LEU A CG  1 
ATOM   2167 C  CD1 . LEU A 1 338 ? 43.617 35.158  32.531 1.00 17.97 ? 338 LEU A CD1 1 
ATOM   2168 C  CD2 . LEU A 1 338 ? 44.590 37.356  31.808 1.00 23.05 ? 338 LEU A CD2 1 
ATOM   2169 N  N   . GLY A 1 339 ? 47.832 34.436  28.467 1.00 14.67 ? 339 GLY A N   1 
ATOM   2170 C  CA  . GLY A 1 339 ? 49.168 33.996  28.126 1.00 14.01 ? 339 GLY A CA  1 
ATOM   2171 C  C   . GLY A 1 339 ? 49.539 32.599  28.568 1.00 13.12 ? 339 GLY A C   1 
ATOM   2172 O  O   . GLY A 1 339 ? 50.712 32.237  28.465 1.00 14.12 ? 339 GLY A O   1 
ATOM   2173 N  N   . PHE A 1 340 ? 48.583 31.784  29.006 1.00 12.28 ? 340 PHE A N   1 
ATOM   2174 C  CA  . PHE A 1 340 ? 48.904 30.387  29.268 1.00 10.61 ? 340 PHE A CA  1 
ATOM   2175 C  C   . PHE A 1 340 ? 49.390 29.715  27.995 1.00 10.89 ? 340 PHE A C   1 
ATOM   2176 O  O   . PHE A 1 340 ? 48.877 29.968  26.897 1.00 13.17 ? 340 PHE A O   1 
ATOM   2177 C  CB  . PHE A 1 340 ? 47.678 29.626  29.804 1.00 11.56 ? 340 PHE A CB  1 
ATOM   2178 C  CG  . PHE A 1 340 ? 47.288 30.006  31.209 1.00 12.71 ? 340 PHE A CG  1 
ATOM   2179 C  CD1 . PHE A 1 340 ? 47.972 29.505  32.298 1.00 12.48 ? 340 PHE A CD1 1 
ATOM   2180 C  CD2 . PHE A 1 340 ? 46.215 30.846  31.442 1.00 13.53 ? 340 PHE A CD2 1 
ATOM   2181 C  CE1 . PHE A 1 340 ? 47.612 29.866  33.583 1.00 12.89 ? 340 PHE A CE1 1 
ATOM   2182 C  CE2 . PHE A 1 340 ? 45.847 31.201  32.700 1.00 15.12 ? 340 PHE A CE2 1 
ATOM   2183 C  CZ  . PHE A 1 340 ? 46.531 30.716  33.793 1.00 14.35 ? 340 PHE A CZ  1 
ATOM   2184 N  N   . HIS A 1 341 ? 50.370 28.821  28.138 1.00 10.63 ? 341 HIS A N   1 
ATOM   2185 C  CA  . HIS A 1 341 ? 50.861 28.124  26.957 1.00 13.89 ? 341 HIS A CA  1 
ATOM   2186 C  C   . HIS A 1 341 ? 49.821 27.183  26.378 1.00 13.52 ? 341 HIS A C   1 
ATOM   2187 O  O   . HIS A 1 341 ? 49.742 27.042  25.149 1.00 15.05 ? 341 HIS A O   1 
ATOM   2188 C  CB  . HIS A 1 341 ? 52.153 27.410  27.302 1.00 11.20 ? 341 HIS A CB  1 
ATOM   2189 C  CG  . HIS A 1 341 ? 53.263 28.375  27.532 1.00 12.36 ? 341 HIS A CG  1 
ATOM   2190 N  ND1 . HIS A 1 341 ? 54.042 28.843  26.497 1.00 12.96 ? 341 HIS A ND1 1 
ATOM   2191 C  CD2 . HIS A 1 341 ? 53.630 29.067  28.634 1.00 12.29 ? 341 HIS A CD2 1 
ATOM   2192 C  CE1 . HIS A 1 341 ? 54.883 29.747  26.971 1.00 16.30 ? 341 HIS A CE1 1 
ATOM   2193 N  NE2 . HIS A 1 341 ? 54.669 29.889  28.264 1.00 14.23 ? 341 HIS A NE2 1 
ATOM   2194 N  N   . TYR A 1 342 ? 48.977 26.581  27.223 1.00 10.51 ? 342 TYR A N   1 
ATOM   2195 C  CA  . TYR A 1 342 ? 47.715 26.084  26.711 1.00 11.15 ? 342 TYR A CA  1 
ATOM   2196 C  C   . TYR A 1 342 ? 46.683 26.138  27.826 1.00 10.07 ? 342 TYR A C   1 
ATOM   2197 O  O   . TYR A 1 342 ? 47.021 26.145  29.010 1.00 8.19  ? 342 TYR A O   1 
ATOM   2198 C  CB  . TYR A 1 342 ? 47.797 24.664  26.139 1.00 11.92 ? 342 TYR A CB  1 
ATOM   2199 C  CG  . TYR A 1 342 ? 48.078 23.517  27.090 1.00 11.40 ? 342 TYR A CG  1 
ATOM   2200 C  CD1 . TYR A 1 342 ? 47.079 22.996  27.931 1.00 14.01 ? 342 TYR A CD1 1 
ATOM   2201 C  CD2 . TYR A 1 342 ? 49.320 22.890  27.082 1.00 13.51 ? 342 TYR A CD2 1 
ATOM   2202 C  CE1 . TYR A 1 342 ? 47.345 21.906  28.773 1.00 14.24 ? 342 TYR A CE1 1 
ATOM   2203 C  CE2 . TYR A 1 342 ? 49.580 21.791  27.917 1.00 13.65 ? 342 TYR A CE2 1 
ATOM   2204 C  CZ  . TYR A 1 342 ? 48.583 21.312  28.744 1.00 18.26 ? 342 TYR A CZ  1 
ATOM   2205 O  OH  . TYR A 1 342 ? 48.853 20.237  29.550 1.00 17.34 ? 342 TYR A OH  1 
ATOM   2206 N  N   . THR A 1 343 ? 45.413 26.228  27.405 1.00 9.73  ? 343 THR A N   1 
ATOM   2207 C  CA  . THR A 1 343 ? 44.245 26.179  28.296 1.00 9.71  ? 343 THR A CA  1 
ATOM   2208 C  C   . THR A 1 343 ? 43.347 25.082  27.727 1.00 13.24 ? 343 THR A C   1 
ATOM   2209 O  O   . THR A 1 343 ? 42.715 25.273  26.680 1.00 13.77 ? 343 THR A O   1 
ATOM   2210 C  CB  . THR A 1 343 ? 43.517 27.524  28.331 1.00 10.83 ? 343 THR A CB  1 
ATOM   2211 O  OG1 . THR A 1 343 ? 44.452 28.543  28.698 1.00 12.81 ? 343 THR A OG1 1 
ATOM   2212 C  CG2 . THR A 1 343 ? 42.398 27.491  29.357 1.00 12.10 ? 343 THR A CG2 1 
ATOM   2213 N  N   . ALA A 1 344 ? 43.350 23.910  28.363 1.00 10.07 ? 344 ALA A N   1 
ATOM   2214 C  CA  . ALA A 1 344 ? 42.436 22.834  27.981 1.00 8.78  ? 344 ALA A CA  1 
ATOM   2215 C  C   . ALA A 1 344 ? 41.120 23.065  28.703 1.00 9.87  ? 344 ALA A C   1 
ATOM   2216 O  O   . ALA A 1 344 ? 41.100 23.115  29.928 1.00 9.95  ? 344 ALA A O   1 
ATOM   2217 C  CB  . ALA A 1 344 ? 43.013 21.469  28.347 1.00 12.55 ? 344 ALA A CB  1 
ATOM   2218 N  N   . SER A 1 345 ? 40.016 23.239  27.983 1.00 7.78  ? 345 SER A N   1 
ATOM   2219 C  CA  . SER A 1 345 ? 38.793 23.672  28.655 1.00 8.37  ? 345 SER A CA  1 
ATOM   2220 C  C   . SER A 1 345 ? 37.597 22.993  28.008 1.00 9.83  ? 345 SER A C   1 
ATOM   2221 O  O   . SER A 1 345 ? 37.413 23.082  26.789 1.00 11.11 ? 345 SER A O   1 
ATOM   2222 C  CB  . SER A 1 345 ? 38.674 25.206  28.603 1.00 8.78  ? 345 SER A CB  1 
ATOM   2223 O  OG  . SER A 1 345 ? 37.506 25.694  29.258 1.00 10.36 ? 345 SER A OG  1 
ATOM   2224 N  N   . GLY A 1 346 ? 36.787 22.300  28.804 1.00 8.08  ? 346 GLY A N   1 
ATOM   2225 C  CA  . GLY A 1 346 ? 35.622 21.660  28.226 1.00 8.38  ? 346 GLY A CA  1 
ATOM   2226 C  C   . GLY A 1 346 ? 34.959 20.789  29.271 1.00 9.14  ? 346 GLY A C   1 
ATOM   2227 O  O   . GLY A 1 346 ? 35.550 20.466  30.298 1.00 7.72  ? 346 GLY A O   1 
ATOM   2228 N  N   . PRO A 1 347 ? 33.707 20.408  29.042 1.00 9.32  ? 347 PRO A N   1 
ATOM   2229 C  CA  . PRO A 1 347 ? 32.977 19.689  30.106 1.00 9.52  ? 347 PRO A CA  1 
ATOM   2230 C  C   . PRO A 1 347 ? 33.676 18.427  30.562 1.00 10.57 ? 347 PRO A C   1 
ATOM   2231 O  O   . PRO A 1 347 ? 33.716 18.162  31.770 1.00 12.43 ? 347 PRO A O   1 
ATOM   2232 C  CB  . PRO A 1 347 ? 31.611 19.399  29.454 1.00 10.36 ? 347 PRO A CB  1 
ATOM   2233 C  CG  . PRO A 1 347 ? 31.410 20.590  28.510 1.00 12.07 ? 347 PRO A CG  1 
ATOM   2234 C  CD  . PRO A 1 347 ? 32.834 20.803  27.908 1.00 10.62 ? 347 PRO A CD  1 
ATOM   2235 N  N   . LEU A 1 348 ? 34.257 17.667  29.650 1.00 9.41  ? 348 LEU A N   1 
ATOM   2236 C  CA  . LEU A 1 348 ? 34.897 16.395  29.999 1.00 13.12 ? 348 LEU A CA  1 
ATOM   2237 C  C   . LEU A 1 348 ? 36.390 16.533  30.300 1.00 11.23 ? 348 LEU A C   1 
ATOM   2238 O  O   . LEU A 1 348 ? 37.055 15.530  30.586 1.00 13.29 ? 348 LEU A O   1 
ATOM   2239 C  CB  . LEU A 1 348 ? 34.718 15.392  28.858 1.00 12.86 ? 348 LEU A CB  1 
ATOM   2240 C  CG  . LEU A 1 348 ? 33.251 14.998  28.652 1.00 15.60 ? 348 LEU A CG  1 
ATOM   2241 C  CD1 . LEU A 1 348 ? 33.166 14.129  27.420 1.00 27.06 ? 348 LEU A CD1 1 
ATOM   2242 C  CD2 . LEU A 1 348 ? 32.718 14.289  29.860 1.00 22.14 ? 348 LEU A CD2 1 
ATOM   2243 N  N   . VAL A 1 349 ? 36.923 17.748  30.274 1.00 10.23 ? 349 VAL A N   1 
ATOM   2244 C  CA  . VAL A 1 349 ? 38.337 17.938  30.583 1.00 9.99  ? 349 VAL A CA  1 
ATOM   2245 C  C   . VAL A 1 349 ? 38.638 17.604  32.044 1.00 12.80 ? 349 VAL A C   1 
ATOM   2246 O  O   . VAL A 1 349 ? 37.825 17.832  32.961 1.00 16.15 ? 349 VAL A O   1 
ATOM   2247 C  CB  . VAL A 1 349 ? 38.736 19.378  30.237 1.00 10.00 ? 349 VAL A CB  1 
ATOM   2248 C  CG1 . VAL A 1 349 ? 40.179 19.723  30.742 1.00 15.15 ? 349 VAL A CG1 1 
ATOM   2249 C  CG2 . VAL A 1 349 ? 38.633 19.576  28.722 1.00 12.63 ? 349 VAL A CG2 1 
ATOM   2250 N  N   . ARG A 1 350 ? 39.785 16.971  32.241 1.00 18.35 ? 350 ARG A N   1 
ATOM   2251 C  CA  A ARG A 1 350 ? 40.421 16.823  33.536 0.56 17.66 ? 350 ARG A CA  1 
ATOM   2252 C  CA  C ARG A 1 350 ? 40.419 16.887  33.542 0.44 17.67 ? 350 ARG A CA  1 
ATOM   2253 C  C   . ARG A 1 350 ? 41.901 16.993  33.297 1.00 18.31 ? 350 ARG A C   1 
ATOM   2254 O  O   . ARG A 1 350 ? 42.334 17.194  32.167 1.00 14.10 ? 350 ARG A O   1 
ATOM   2255 C  CB  A ARG A 1 350 ? 40.091 15.475  34.174 0.56 19.44 ? 350 ARG A CB  1 
ATOM   2256 C  CB  C ARG A 1 350 ? 40.046 15.594  34.273 0.44 19.48 ? 350 ARG A CB  1 
ATOM   2257 C  CG  A ARG A 1 350 ? 40.324 14.316  33.251 0.56 19.10 ? 350 ARG A CG  1 
ATOM   2258 C  CG  C ARG A 1 350 ? 40.341 14.315  33.525 0.44 18.53 ? 350 ARG A CG  1 
ATOM   2259 C  CD  A ARG A 1 350 ? 39.856 13.025  33.885 0.56 19.71 ? 350 ARG A CD  1 
ATOM   2260 C  CD  C ARG A 1 350 ? 39.271 13.271  33.828 0.44 23.79 ? 350 ARG A CD  1 
ATOM   2261 N  NE  A ARG A 1 350 ? 40.634 12.700  35.070 0.56 17.86 ? 350 ARG A NE  1 
ATOM   2262 N  NE  C ARG A 1 350 ? 37.992 13.665  33.253 0.44 22.91 ? 350 ARG A NE  1 
ATOM   2263 C  CZ  A ARG A 1 350 ? 40.260 11.830  35.997 0.56 18.52 ? 350 ARG A CZ  1 
ATOM   2264 C  CZ  C ARG A 1 350 ? 36.887 12.931  33.273 0.44 19.72 ? 350 ARG A CZ  1 
ATOM   2265 N  NH1 A ARG A 1 350 ? 41.030 11.563  37.036 0.56 16.55 ? 350 ARG A NH1 1 
ATOM   2266 N  NH1 C ARG A 1 350 ? 36.843 11.750  33.882 0.44 15.20 ? 350 ARG A NH1 1 
ATOM   2267 N  NH2 A ARG A 1 350 ? 39.074 11.230  35.885 0.56 18.42 ? 350 ARG A NH2 1 
ATOM   2268 N  NH2 C ARG A 1 350 ? 35.802 13.382  32.652 0.44 17.10 ? 350 ARG A NH2 1 
ATOM   2269 N  N   . SER A 1 351 ? 42.706 16.905  34.352 1.00 18.23 ? 351 SER A N   1 
ATOM   2270 C  CA  A SER A 1 351 ? 44.093 17.331  34.204 0.54 19.42 ? 351 SER A CA  1 
ATOM   2271 C  CA  B SER A 1 351 ? 44.095 17.312  34.230 0.46 19.49 ? 351 SER A CA  1 
ATOM   2272 C  C   . SER A 1 351 ? 44.805 16.551  33.111 1.00 15.34 ? 351 SER A C   1 
ATOM   2273 O  O   . SER A 1 351 ? 45.600 17.121  32.360 1.00 22.01 ? 351 SER A O   1 
ATOM   2274 C  CB  A SER A 1 351 ? 44.879 17.211  35.522 0.54 21.40 ? 351 SER A CB  1 
ATOM   2275 C  CB  B SER A 1 351 ? 44.762 17.102  35.593 0.46 21.22 ? 351 SER A CB  1 
ATOM   2276 O  OG  A SER A 1 351 ? 46.254 17.525  35.265 0.54 23.72 ? 351 SER A OG  1 
ATOM   2277 O  OG  B SER A 1 351 ? 43.726 17.020  36.557 0.46 25.43 ? 351 SER A OG  1 
ATOM   2278 N  N   . SER A 1 352 ? 44.507 15.248  32.970 1.00 13.46 ? 352 SER A N   1 
ATOM   2279 C  CA  . SER A 1 352 ? 45.218 14.424  32.011 1.00 9.24  ? 352 SER A CA  1 
ATOM   2280 C  C   . SER A 1 352 ? 44.616 14.393  30.608 1.00 10.22 ? 352 SER A C   1 
ATOM   2281 O  O   . SER A 1 352 ? 45.233 13.814  29.724 1.00 11.35 ? 352 SER A O   1 
ATOM   2282 C  CB  . SER A 1 352 ? 45.280 12.987  32.512 1.00 11.73 ? 352 SER A CB  1 
ATOM   2283 O  OG  . SER A 1 352 ? 43.982 12.643  32.958 1.00 13.77 ? 352 SER A OG  1 
ATOM   2284 N  N   . TYR A 1 353 ? 43.449 15.003  30.390 1.00 10.28 ? 353 TYR A N   1 
ATOM   2285 C  CA  . TYR A 1 353 ? 42.734 14.869  29.120 1.00 8.24  ? 353 TYR A CA  1 
ATOM   2286 C  C   . TYR A 1 353 ? 43.602 15.274  27.930 1.00 8.95  ? 353 TYR A C   1 
ATOM   2287 O  O   . TYR A 1 353 ? 44.005 16.440  27.798 1.00 10.11 ? 353 TYR A O   1 
ATOM   2288 C  CB  . TYR A 1 353 ? 41.482 15.733  29.150 1.00 10.07 ? 353 TYR A CB  1 
ATOM   2289 C  CG  . TYR A 1 353 ? 40.716 15.715  27.856 1.00 10.92 ? 353 TYR A CG  1 
ATOM   2290 C  CD1 . TYR A 1 353 ? 40.105 14.549  27.419 1.00 14.06 ? 353 TYR A CD1 1 
ATOM   2291 C  CD2 . TYR A 1 353 ? 40.603 16.864  27.094 1.00 9.06  ? 353 TYR A CD2 1 
ATOM   2292 C  CE1 . TYR A 1 353 ? 39.348 14.526  26.226 1.00 15.95 ? 353 TYR A CE1 1 
ATOM   2293 C  CE2 . TYR A 1 353 ? 39.836 16.860  25.920 1.00 11.10 ? 353 TYR A CE2 1 
ATOM   2294 C  CZ  . TYR A 1 353 ? 39.231 15.692  25.506 1.00 15.91 ? 353 TYR A CZ  1 
ATOM   2295 O  OH  . TYR A 1 353 ? 38.493 15.689  24.342 1.00 18.44 ? 353 TYR A OH  1 
ATOM   2296 N  N   . LYS A 1 354 ? 43.873 14.291  27.072 1.00 10.44 ? 354 LYS A N   1 
ATOM   2297 C  CA  . LYS A 1 354 ? 44.680 14.476  25.866 1.00 8.60  ? 354 LYS A CA  1 
ATOM   2298 C  C   . LYS A 1 354 ? 45.965 15.237  26.166 1.00 8.77  ? 354 LYS A C   1 
ATOM   2299 O  O   . LYS A 1 354 ? 46.411 16.033  25.353 1.00 10.34 ? 354 LYS A O   1 
ATOM   2300 C  CB  . LYS A 1 354 ? 43.896 15.221  24.780 1.00 10.40 ? 354 LYS A CB  1 
ATOM   2301 C  CG  . LYS A 1 354 ? 42.620 14.518  24.321 1.00 16.68 ? 354 LYS A CG  1 
ATOM   2302 C  CD  . LYS A 1 354 ? 41.872 15.351  23.261 1.00 18.63 ? 354 LYS A CD  1 
ATOM   2303 C  CE  . LYS A 1 354 ? 42.556 15.289  21.926 1.00 23.44 ? 354 LYS A CE  1 
ATOM   2304 N  NZ  . LYS A 1 354 ? 41.711 15.930  20.856 1.00 26.73 ? 354 LYS A NZ  1 
ATOM   2305 N  N   . ALA A 1 355 ? 46.540 15.006  27.356 1.00 9.23  ? 355 ALA A N   1 
ATOM   2306 C  CA  . ALA A 1 355 ? 47.660 15.835  27.778 1.00 7.93  ? 355 ALA A CA  1 
ATOM   2307 C  C   . ALA A 1 355 ? 48.794 15.774  26.774 1.00 9.78  ? 355 ALA A C   1 
ATOM   2308 O  O   . ALA A 1 355 ? 49.453 16.786  26.527 1.00 12.09 ? 355 ALA A O   1 
ATOM   2309 C  CB  . ALA A 1 355 ? 48.142 15.424  29.153 1.00 8.76  ? 355 ALA A CB  1 
ATOM   2310 N  N   . GLY A 1 356 ? 49.018 14.615  26.171 1.00 9.56  ? 356 GLY A N   1 
ATOM   2311 C  CA  . GLY A 1 356 ? 50.098 14.520  25.194 1.00 9.96  ? 356 GLY A CA  1 
ATOM   2312 C  C   . GLY A 1 356 ? 49.811 15.321  23.944 1.00 13.51 ? 356 GLY A C   1 
ATOM   2313 O  O   . GLY A 1 356 ? 50.735 15.841  23.308 1.00 15.64 ? 356 GLY A O   1 
ATOM   2314 N  N   . GLU A 1 357 ? 48.532 15.433  23.572 1.00 10.17 ? 357 GLU A N   1 
ATOM   2315 C  CA  . GLU A 1 357 ? 48.174 16.215  22.387 1.00 10.92 ? 357 GLU A CA  1 
ATOM   2316 C  C   . GLU A 1 357 ? 48.312 17.701  22.660 1.00 11.43 ? 357 GLU A C   1 
ATOM   2317 O  O   . GLU A 1 357 ? 48.824 18.441  21.809 1.00 12.93 ? 357 GLU A O   1 
ATOM   2318 C  CB  . GLU A 1 357 ? 46.738 15.915  21.949 1.00 15.40 ? 357 GLU A CB  1 
ATOM   2319 C  CG  . GLU A 1 357 ? 46.488 14.488  21.570 1.00 18.20 ? 357 GLU A CG  1 
ATOM   2320 C  CD  . GLU A 1 357 ? 46.975 14.175  20.158 1.00 21.98 ? 357 GLU A CD  1 
ATOM   2321 O  OE1 . GLU A 1 357 ? 46.669 14.949  19.228 1.00 25.87 ? 357 GLU A OE1 1 
ATOM   2322 O  OE2 . GLU A 1 357 ? 47.682 13.171  20.002 1.00 27.61 ? 357 GLU A OE2 1 
ATOM   2323 N  N   . PHE A 1 358 ? 47.876 18.160  23.845 1.00 11.55 ? 358 PHE A N   1 
ATOM   2324 C  CA  . PHE A 1 358 ? 48.070 19.570  24.181 1.00 10.98 ? 358 PHE A CA  1 
ATOM   2325 C  C   . PHE A 1 358 ? 49.549 19.912  24.236 1.00 10.68 ? 358 PHE A C   1 
ATOM   2326 O  O   . PHE A 1 358 ? 49.962 20.998  23.800 1.00 11.72 ? 358 PHE A O   1 
ATOM   2327 C  CB  . PHE A 1 358 ? 47.394 19.932  25.508 1.00 9.99  ? 358 PHE A CB  1 
ATOM   2328 C  CG  . PHE A 1 358 ? 45.879 20.001  25.417 1.00 11.99 ? 358 PHE A CG  1 
ATOM   2329 C  CD1 . PHE A 1 358 ? 45.264 21.082  24.809 1.00 18.63 ? 358 PHE A CD1 1 
ATOM   2330 C  CD2 . PHE A 1 358 ? 45.077 18.988  25.951 1.00 10.85 ? 358 PHE A CD2 1 
ATOM   2331 C  CE1 . PHE A 1 358 ? 43.869 21.164  24.714 1.00 16.06 ? 358 PHE A CE1 1 
ATOM   2332 C  CE2 . PHE A 1 358 ? 43.672 19.059  25.843 1.00 15.11 ? 358 PHE A CE2 1 
ATOM   2333 C  CZ  . PHE A 1 358 ? 43.075 20.138  25.226 1.00 13.31 ? 358 PHE A CZ  1 
ATOM   2334 N  N   . PHE A 1 359 ? 50.353 19.000  24.770 1.00 10.42 ? 359 PHE A N   1 
ATOM   2335 C  CA  . PHE A 1 359 ? 51.792 19.251  24.872 1.00 9.77  ? 359 PHE A CA  1 
ATOM   2336 C  C   . PHE A 1 359 ? 52.417 19.345  23.485 1.00 11.07 ? 359 PHE A C   1 
ATOM   2337 O  O   . PHE A 1 359 ? 53.152 20.303  23.198 1.00 13.05 ? 359 PHE A O   1 
ATOM   2338 C  CB  . PHE A 1 359 ? 52.447 18.147  25.730 1.00 10.86 ? 359 PHE A CB  1 
ATOM   2339 C  CG  . PHE A 1 359 ? 53.854 18.482  26.196 1.00 10.18 ? 359 PHE A CG  1 
ATOM   2340 C  CD1 . PHE A 1 359 ? 54.069 19.035  27.450 1.00 11.21 ? 359 PHE A CD1 1 
ATOM   2341 C  CD2 . PHE A 1 359 ? 54.938 18.232  25.378 1.00 12.93 ? 359 PHE A CD2 1 
ATOM   2342 C  CE1 . PHE A 1 359 ? 55.365 19.352  27.886 1.00 12.12 ? 359 PHE A CE1 1 
ATOM   2343 C  CE2 . PHE A 1 359 ? 56.249 18.532  25.800 1.00 13.12 ? 359 PHE A CE2 1 
ATOM   2344 C  CZ  . PHE A 1 359 ? 56.460 19.093  27.039 1.00 12.46 ? 359 PHE A CZ  1 
ATOM   2345 N  N   . LEU A 1 360 ? 52.114 18.377  22.608 1.00 11.12 ? 360 LEU A N   1 
ATOM   2346 C  CA  . LEU A 1 360 ? 52.697 18.393  21.256 1.00 11.09 ? 360 LEU A CA  1 
ATOM   2347 C  C   . LEU A 1 360 ? 52.222 19.595  20.454 1.00 11.03 ? 360 LEU A C   1 
ATOM   2348 O  O   . LEU A 1 360 ? 53.008 20.220  19.740 1.00 13.58 ? 360 LEU A O   1 
ATOM   2349 C  CB  . LEU A 1 360 ? 52.387 17.106  20.496 1.00 15.03 ? 360 LEU A CB  1 
ATOM   2350 C  CG  . LEU A 1 360 ? 53.198 15.878  20.922 1.00 21.94 ? 360 LEU A CG  1 
ATOM   2351 C  CD1 . LEU A 1 360 ? 52.927 14.751  19.951 1.00 23.22 ? 360 LEU A CD1 1 
ATOM   2352 C  CD2 . LEU A 1 360 ? 54.693 16.164  20.947 1.00 25.73 ? 360 LEU A CD2 1 
ATOM   2353 N  N   . LYS A 1 361 ? 50.944 19.944  20.550 1.00 12.53 ? 361 LYS A N   1 
ATOM   2354 C  CA  . LYS A 1 361 ? 50.457 21.042  19.720 1.00 12.91 ? 361 LYS A CA  1 
ATOM   2355 C  C   . LYS A 1 361 ? 50.955 22.388  20.212 1.00 12.80 ? 361 LYS A C   1 
ATOM   2356 O  O   . LYS A 1 361 ? 51.339 23.255  19.410 1.00 15.39 ? 361 LYS A O   1 
ATOM   2357 C  CB  . LYS A 1 361 ? 48.929 21.024  19.706 1.00 13.50 ? 361 LYS A CB  1 
ATOM   2358 C  CG  . LYS A 1 361 ? 48.324 22.179  18.922 1.00 20.55 ? 361 LYS A CG  1 
ATOM   2359 C  CD  . LYS A 1 361 ? 46.806 22.102  18.981 1.00 28.18 ? 361 LYS A CD  1 
ATOM   2360 C  CE  . LYS A 1 361 ? 46.177 23.366  18.410 1.00 36.63 ? 361 LYS A CE  1 
ATOM   2361 N  NZ  . LYS A 1 361 ? 44.861 23.622  19.066 1.00 40.30 ? 361 LYS A NZ  1 
ATOM   2362 N  N   . ASN A 1 362 ? 50.915 22.609  21.521 1.00 12.60 ? 362 ASN A N   1 
ATOM   2363 C  CA  . ASN A 1 362 ? 51.019 23.957  22.062 1.00 13.44 ? 362 ASN A CA  1 
ATOM   2364 C  C   . ASN A 1 362 ? 52.373 24.297  22.662 1.00 15.76 ? 362 ASN A C   1 
ATOM   2365 O  O   . ASN A 1 362 ? 52.649 25.478  22.876 1.00 21.63 ? 362 ASN A O   1 
ATOM   2366 C  CB  . ASN A 1 362 ? 49.973 24.164  23.150 1.00 13.46 ? 362 ASN A CB  1 
ATOM   2367 C  CG  . ASN A 1 362 ? 48.574 24.229  22.594 1.00 19.26 ? 362 ASN A CG  1 
ATOM   2368 O  OD1 . ASN A 1 362 ? 48.178 25.243  22.011 1.00 24.81 ? 362 ASN A OD1 1 
ATOM   2369 N  ND2 . ASN A 1 362 ? 47.814 23.150  22.757 1.00 15.95 ? 362 ASN A ND2 1 
ATOM   2370 N  N   . LEU A 1 363 ? 53.151 23.302  23.071 1.00 11.82 ? 363 LEU A N   1 
ATOM   2371 C  CA  . LEU A 1 363 ? 54.490 23.548  23.599 1.00 12.54 ? 363 LEU A CA  1 
ATOM   2372 C  C   . LEU A 1 363 ? 55.561 23.151  22.590 1.00 17.03 ? 363 LEU A C   1 
ATOM   2373 O  O   . LEU A 1 363 ? 56.452 23.939  22.272 1.00 18.16 ? 363 LEU A O   1 
ATOM   2374 C  CB  . LEU A 1 363 ? 54.711 22.782  24.922 1.00 11.22 ? 363 LEU A CB  1 
ATOM   2375 C  CG  . LEU A 1 363 ? 53.956 23.409  26.116 1.00 17.82 ? 363 LEU A CG  1 
ATOM   2376 C  CD1 . LEU A 1 363 ? 53.894 22.416  27.266 1.00 22.62 ? 363 LEU A CD1 1 
ATOM   2377 C  CD2 . LEU A 1 363 ? 54.626 24.684  26.600 1.00 19.49 ? 363 LEU A CD2 1 
ATOM   2378 N  N   . VAL A 1 364 ? 55.495 21.922  22.096 1.00 11.97 ? 364 VAL A N   1 
ATOM   2379 C  CA  . VAL A 1 364 ? 56.443 21.424  21.112 1.00 11.10 ? 364 VAL A CA  1 
ATOM   2380 C  C   . VAL A 1 364 ? 56.178 22.042  19.738 1.00 13.27 ? 364 VAL A C   1 
ATOM   2381 O  O   . VAL A 1 364 ? 57.082 22.126  18.902 1.00 12.76 ? 364 VAL A O   1 
ATOM   2382 C  CB  . VAL A 1 364 ? 56.345 19.894  21.083 1.00 12.29 ? 364 VAL A CB  1 
ATOM   2383 C  CG1 . VAL A 1 364 ? 57.110 19.307  19.892 1.00 15.93 ? 364 VAL A CG1 1 
ATOM   2384 C  CG2 . VAL A 1 364 ? 56.895 19.331  22.406 1.00 14.56 ? 364 VAL A CG2 1 
ATOM   2385 N  N   . ALA A 1 365 ? 54.939 22.462  19.474 1.00 14.27 ? 365 ALA A N   1 
ATOM   2386 C  CA  . ALA A 1 365 ? 54.521 22.922  18.135 1.00 15.30 ? 365 ALA A CA  1 
ATOM   2387 C  C   . ALA A 1 365 ? 54.918 21.923  17.048 1.00 14.29 ? 365 ALA A C   1 
ATOM   2388 O  O   . ALA A 1 365 ? 55.483 22.282  16.012 1.00 17.52 ? 365 ALA A O   1 
ATOM   2389 C  CB  . ALA A 1 365 ? 55.078 24.323  17.834 1.00 17.70 ? 365 ALA A CB  1 
ATOM   2390 N  N   . LYS A 1 366 ? 54.663 20.645  17.301 1.00 14.11 ? 366 LYS A N   1 
ATOM   2391 C  CA  . LYS A 1 366 ? 55.097 19.598  16.384 1.00 14.45 ? 366 LYS A CA  1 
ATOM   2392 C  C   . LYS A 1 366 ? 54.378 19.708  15.041 1.00 15.86 ? 366 LYS A C   1 
ATOM   2393 O  O   . LYS A 1 366 ? 53.149 19.816  14.989 1.00 19.29 ? 366 LYS A O   1 
ATOM   2394 C  CB  . LYS A 1 366 ? 54.835 18.222  16.998 1.00 16.91 ? 366 LYS A CB  1 
ATOM   2395 C  CG  . LYS A 1 366 ? 55.411 17.106  16.143 1.00 24.26 ? 366 LYS A CG  1 
ATOM   2396 C  CD  . LYS A 1 366 ? 55.187 15.743  16.748 1.00 33.89 ? 366 LYS A CD  1 
ATOM   2397 C  CE  . LYS A 1 366 ? 55.955 14.692  15.976 1.00 36.31 ? 366 LYS A CE  1 
ATOM   2398 N  NZ  . LYS A 1 366 ? 57.411 14.782  16.232 1.00 39.15 ? 366 LYS A NZ  1 
ATOM   2399 N  N   . ARG A 1 367 ? 55.155 19.691  13.954 1.00 17.66 ? 367 ARG A N   1 
ATOM   2400 C  CA  . ARG A 1 367 ? 54.573 19.686  12.614 1.00 26.96 ? 367 ARG A CA  1 
ATOM   2401 C  C   . ARG A 1 367 ? 54.135 18.276  12.248 1.00 32.57 ? 367 ARG A C   1 
ATOM   2402 O  O   . ARG A 1 367 ? 54.927 17.333  12.317 1.00 35.26 ? 367 ARG A O   1 
ATOM   2403 C  CB  . ARG A 1 367 ? 55.578 20.216  11.589 1.00 24.03 ? 367 ARG A CB  1 
ATOM   2404 C  CG  . ARG A 1 367 ? 55.877 21.667  11.827 1.00 22.73 ? 367 ARG A CG  1 
ATOM   2405 C  CD  . ARG A 1 367 ? 56.649 22.299  10.677 1.00 25.69 ? 367 ARG A CD  1 
ATOM   2406 N  NE  . ARG A 1 367 ? 55.828 22.498  9.488  1.00 30.71 ? 367 ARG A NE  1 
ATOM   2407 C  CZ  . ARG A 1 367 ? 56.064 21.931  8.310  1.00 39.94 ? 367 ARG A CZ  1 
ATOM   2408 N  NH1 . ARG A 1 367 ? 57.071 21.094  8.133  1.00 38.46 ? 367 ARG A NH1 1 
ATOM   2409 N  NH2 . ARG A 1 367 ? 55.273 22.221  7.279  1.00 47.61 ? 367 ARG A NH2 1 
ATOM   2410 N  N   . LYS A 1 368 ? 52.875 18.137  11.855 1.00 45.13 ? 368 LYS A N   1 
ATOM   2411 C  CA  . LYS A 1 368 ? 52.294 16.819  11.607 1.00 43.96 ? 368 LYS A CA  1 
ATOM   2412 C  C   . LYS A 1 368 ? 52.998 16.094  10.461 1.00 45.34 ? 368 LYS A C   1 
ATOM   2413 O  O   . LYS A 1 368 ? 52.808 16.427  9.293  1.00 54.32 ? 368 LYS A O   1 
ATOM   2414 C  CB  . LYS A 1 368 ? 50.798 16.947  11.308 1.00 43.58 ? 368 LYS A CB  1 
ATOM   2415 C  CG  . LYS A 1 368 ? 50.103 15.618  11.068 1.00 48.84 ? 368 LYS A CG  1 
ATOM   2416 C  CD  . LYS A 1 368 ? 50.299 14.668  12.244 1.00 45.67 ? 368 LYS A CD  1 
ATOM   2417 C  CE  . LYS A 1 368 ? 49.413 13.441  12.100 1.00 44.31 ? 368 LYS A CE  1 
ATOM   2418 N  NZ  . LYS A 1 368 ? 49.739 12.389  13.100 1.00 44.61 ? 368 LYS A NZ  1 
HETATM 2419 C  C1  . GLC B 2 .   ? 69.237 25.759  31.503 1.00 21.92 ? 1   GLC E C1  1 
HETATM 2420 C  C2  . GLC B 2 .   ? 69.034 24.242  31.369 1.00 24.73 ? 1   GLC E C2  1 
HETATM 2421 C  C3  . GLC B 2 .   ? 70.130 23.635  30.576 1.00 24.09 ? 1   GLC E C3  1 
HETATM 2422 C  C4  . GLC B 2 .   ? 70.199 24.280  29.223 1.00 15.65 ? 1   GLC E C4  1 
HETATM 2423 C  C5  . GLC B 2 .   ? 70.293 25.809  29.305 1.00 18.67 ? 1   GLC E C5  1 
HETATM 2424 C  C6  . GLC B 2 .   ? 70.185 26.445  27.919 1.00 20.42 ? 1   GLC E C6  1 
HETATM 2425 O  O1  . GLC B 2 .   ? 70.481 26.015  32.050 1.00 21.10 ? 1   GLC E O1  1 
HETATM 2426 O  O2  . GLC B 2 .   ? 68.935 23.571  32.667 1.00 21.66 ? 1   GLC E O2  1 
HETATM 2427 O  O3  . GLC B 2 .   ? 69.913 22.186  30.381 1.00 21.17 ? 1   GLC E O3  1 
HETATM 2428 O  O4  . GLC B 2 .   ? 71.370 23.774  28.556 1.00 19.55 ? 1   GLC E O4  1 
HETATM 2429 O  O5  . GLC B 2 .   ? 69.251 26.401  30.163 1.00 20.55 ? 1   GLC E O5  1 
HETATM 2430 O  O6  . GLC B 2 .   ? 68.911 26.125  27.312 1.00 16.37 ? 1   GLC E O6  1 
HETATM 2431 C  C1  . GLC B 2 .   ? 70.587 27.326  32.511 1.00 25.09 ? 2   GLC E C1  1 
HETATM 2432 C  C2  . GLC B 2 .   ? 71.980 27.547  32.983 1.00 26.74 ? 2   GLC E C2  1 
HETATM 2433 C  C3  . GLC B 2 .   ? 72.303 26.681  34.109 1.00 27.82 ? 2   GLC E C3  1 
HETATM 2434 C  C4  . GLC B 2 .   ? 71.337 26.858  35.243 1.00 35.12 ? 2   GLC E C4  1 
HETATM 2435 C  C5  . GLC B 2 .   ? 69.904 26.523  34.766 1.00 30.63 ? 2   GLC E C5  1 
HETATM 2436 C  C6  . GLC B 2 .   ? 68.888 26.697  35.797 1.00 28.38 ? 2   GLC E C6  1 
HETATM 2437 O  O2  . GLC B 2 .   ? 72.928 27.239  31.862 1.00 22.51 ? 2   GLC E O2  1 
HETATM 2438 O  O3  . GLC B 2 .   ? 73.668 26.984  34.574 1.00 31.66 ? 2   GLC E O3  1 
HETATM 2439 O  O4  . GLC B 2 .   ? 71.690 26.006  36.330 1.00 36.35 ? 2   GLC E O4  1 
HETATM 2440 O  O5  . GLC B 2 .   ? 69.610 27.479  33.607 1.00 32.23 ? 2   GLC E O5  1 
HETATM 2441 O  O6  . GLC B 2 .   ? 67.623 26.286  35.244 1.00 36.12 ? 2   GLC E O6  1 
HETATM 2442 S  S1  A DTT C 3 .   ? 45.564 15.214  46.785 0.43 16.33 ? 401 DTT A S1  1 
HETATM 2443 S  S1  B DTT C 3 .   ? 45.586 14.955  46.874 0.57 12.71 ? 401 DTT A S1  1 
HETATM 2444 C  C1  A DTT C 3 .   ? 45.973 15.657  45.075 0.43 12.06 ? 401 DTT A C1  1 
HETATM 2445 C  C1  B DTT C 3 .   ? 45.860 14.542  45.126 0.57 21.86 ? 401 DTT A C1  1 
HETATM 2446 C  C2  A DTT C 3 .   ? 45.004 15.239  43.966 0.43 22.89 ? 401 DTT A C2  1 
HETATM 2447 C  C2  B DTT C 3 .   ? 44.790 15.091  44.220 0.57 22.12 ? 401 DTT A C2  1 
HETATM 2448 O  O2  A DTT C 3 .   ? 43.997 14.360  44.389 0.43 20.83 ? 401 DTT A O2  1 
HETATM 2449 O  O2  B DTT C 3 .   ? 43.477 14.883  44.635 0.57 17.80 ? 401 DTT A O2  1 
HETATM 2450 C  C3  A DTT C 3 .   ? 45.755 14.584  42.815 0.43 18.09 ? 401 DTT A C3  1 
HETATM 2451 C  C3  B DTT C 3 .   ? 44.836 14.543  42.824 0.57 28.68 ? 401 DTT A C3  1 
HETATM 2452 O  O3  A DTT C 3 .   ? 46.954 14.029  43.316 0.43 22.77 ? 401 DTT A O3  1 
HETATM 2453 O  O3  B DTT C 3 .   ? 45.242 15.745  42.230 0.57 12.58 ? 401 DTT A O3  1 
HETATM 2454 C  C4  A DTT C 3 .   ? 44.884 13.621  41.978 0.43 14.43 ? 401 DTT A C4  1 
HETATM 2455 C  C4  B DTT C 3 .   ? 45.746 13.321  42.647 0.57 17.04 ? 401 DTT A C4  1 
HETATM 2456 S  S4  A DTT C 3 .   ? 44.373 12.012  42.663 0.43 26.78 ? 401 DTT A S4  1 
HETATM 2457 S  S4  B DTT C 3 .   ? 44.933 11.656  42.570 0.57 18.00 ? 401 DTT A S4  1 
HETATM 2458 S  S   . SO4 D 4 .   ? 37.927 -0.375  53.813 0.44 38.56 ? 402 SO4 A S   1 
HETATM 2459 O  O1  . SO4 D 4 .   ? 39.356 -0.375  53.519 0.44 30.46 ? 402 SO4 A O1  1 
HETATM 2460 O  O2  . SO4 D 4 .   ? 37.225 0.267   52.706 0.44 25.65 ? 402 SO4 A O2  1 
HETATM 2461 O  O3  . SO4 D 4 .   ? 37.456 -1.746  53.957 0.44 27.57 ? 402 SO4 A O3  1 
HETATM 2462 O  O4  . SO4 D 4 .   ? 37.681 0.347   55.059 0.44 30.18 ? 402 SO4 A O4  1 
HETATM 2463 FE FE1 . SF4 E 5 .   ? 41.240 14.567  48.845 1.00 12.41 ? 403 SF4 A FE1 1 
HETATM 2464 FE FE2 . SF4 E 5 .   ? 42.488 12.182  48.680 1.00 11.72 ? 403 SF4 A FE2 1 
HETATM 2465 FE FE3 . SF4 E 5 .   ? 43.381 14.246  47.153 1.00 13.19 ? 403 SF4 A FE3 1 
HETATM 2466 FE FE4 . SF4 E 5 .   ? 41.002 13.086  46.680 1.00 11.71 ? 403 SF4 A FE4 1 
HETATM 2467 S  S1  . SF4 E 5 .   ? 43.009 12.095  46.487 1.00 11.83 ? 403 SF4 A S1  1 
HETATM 2468 S  S2  . SF4 E 5 .   ? 41.454 15.348  46.707 1.00 13.18 ? 403 SF4 A S2  1 
HETATM 2469 S  S3  . SF4 E 5 .   ? 40.247 12.495  48.753 1.00 11.99 ? 403 SF4 A S3  1 
HETATM 2470 S  S4  . SF4 E 5 .   ? 43.354 14.142  49.477 1.00 13.54 ? 403 SF4 A S4  1 
HETATM 2471 FE FE1 . SF4 F 5 .   ? 42.858 11.249  31.899 1.00 13.48 ? 404 SF4 A FE1 1 
HETATM 2472 FE FE2 . SF4 F 5 .   ? 42.839 8.634   31.186 1.00 11.34 ? 404 SF4 A FE2 1 
HETATM 2473 FE FE3 . SF4 F 5 .   ? 42.314 10.573  29.403 1.00 11.06 ? 404 SF4 A FE3 1 
HETATM 2474 FE FE4 . SF4 F 5 .   ? 40.523 10.015  31.306 1.00 11.41 ? 404 SF4 A FE4 1 
HETATM 2475 S  S1  . SF4 F 5 .   ? 41.184 8.611   29.580 1.00 11.42 ? 404 SF4 A S1  1 
HETATM 2476 S  S2  . SF4 F 5 .   ? 41.141 12.092  30.682 1.00 11.01 ? 404 SF4 A S2  1 
HETATM 2477 S  S3  . SF4 F 5 .   ? 41.892 9.511   33.064 1.00 14.64 ? 404 SF4 A S3  1 
HETATM 2478 S  S4  . SF4 F 5 .   ? 44.298 10.196  30.478 1.00 11.75 ? 404 SF4 A S4  1 
HETATM 2479 O  O   . HOH G 6 .   ? 47.118 8.565   54.321 1.00 33.73 ? 501 HOH A O   1 
HETATM 2480 O  O   . HOH G 6 .   ? 31.747 10.447  21.590 1.00 41.44 ? 502 HOH A O   1 
HETATM 2481 O  O   . HOH G 6 .   ? 26.883 28.611  39.501 1.00 36.57 ? 503 HOH A O   1 
HETATM 2482 O  O   . HOH G 6 .   ? 48.660 37.575  42.329 1.00 37.61 ? 504 HOH A O   1 
HETATM 2483 O  O   . HOH G 6 .   ? 65.792 11.508  38.462 1.00 23.85 ? 505 HOH A O   1 
HETATM 2484 O  O   . HOH G 6 .   ? 40.754 20.045  39.124 1.00 33.89 ? 506 HOH A O   1 
HETATM 2485 O  O   . HOH G 6 .   ? 47.790 17.476  50.794 1.00 39.79 ? 507 HOH A O   1 
HETATM 2486 O  O   . HOH G 6 .   ? 43.230 13.264  35.109 1.00 29.08 ? 508 HOH A O   1 
HETATM 2487 O  O   . HOH G 6 .   ? 36.019 -3.560  54.523 1.00 39.91 ? 509 HOH A O   1 
HETATM 2488 O  O   . HOH G 6 .   ? 47.113 15.357  34.705 1.00 36.40 ? 510 HOH A O   1 
HETATM 2489 O  O   . HOH G 6 .   ? 49.055 29.185  52.951 1.00 39.32 ? 511 HOH A O   1 
HETATM 2490 O  O   . HOH G 6 .   ? 57.267 17.506  12.922 1.00 37.73 ? 512 HOH A O   1 
HETATM 2491 O  O   . HOH G 6 .   ? 52.963 26.826  52.959 1.00 42.47 ? 513 HOH A O   1 
HETATM 2492 O  O   . HOH G 6 .   ? 37.830 24.666  24.514 1.00 26.24 ? 514 HOH A O   1 
HETATM 2493 O  O   . HOH G 6 .   ? 27.585 32.323  32.449 1.00 37.96 ? 515 HOH A O   1 
HETATM 2494 O  O   . HOH G 6 .   ? 48.340 33.383  46.760 1.00 43.14 ? 516 HOH A O   1 
HETATM 2495 O  O   . HOH G 6 .   ? 54.641 -4.366  23.834 1.00 33.17 ? 517 HOH A O   1 
HETATM 2496 O  O   . HOH G 6 .   ? 55.553 34.092  33.021 1.00 43.96 ? 518 HOH A O   1 
HETATM 2497 O  O   . HOH G 6 .   ? 22.827 26.111  45.477 1.00 39.34 ? 519 HOH A O   1 
HETATM 2498 O  O   . HOH G 6 .   ? 46.379 38.849  40.561 1.00 35.64 ? 520 HOH A O   1 
HETATM 2499 O  O   . HOH G 6 .   ? 27.999 29.796  35.948 1.00 29.66 ? 521 HOH A O   1 
HETATM 2500 O  O   . HOH G 6 .   ? 48.325 7.327   45.671 1.00 22.21 ? 522 HOH A O   1 
HETATM 2501 O  O   . HOH G 6 .   ? 42.923 24.478  23.883 1.00 32.90 ? 523 HOH A O   1 
HETATM 2502 O  O   . HOH G 6 .   ? 30.390 30.746  21.666 1.00 18.08 ? 524 HOH A O   1 
HETATM 2503 O  O   . HOH G 6 .   ? 46.040 -12.060 29.418 1.00 36.04 ? 525 HOH A O   1 
HETATM 2504 O  O   . HOH G 6 .   ? 56.745 -4.292  35.046 1.00 34.40 ? 526 HOH A O   1 
HETATM 2505 O  O   . HOH G 6 .   ? 35.997 38.656  42.340 1.00 44.54 ? 527 HOH A O   1 
HETATM 2506 O  O   . HOH G 6 .   ? 34.140 36.947  32.266 1.00 34.82 ? 528 HOH A O   1 
HETATM 2507 O  O   . HOH G 6 .   ? 58.735 8.674   53.141 1.00 37.66 ? 529 HOH A O   1 
HETATM 2508 O  O   . HOH G 6 .   ? 61.491 1.398   45.806 1.00 31.76 ? 530 HOH A O   1 
HETATM 2509 O  O   . HOH G 6 .   ? 42.979 16.472  41.269 1.00 36.44 ? 531 HOH A O   1 
HETATM 2510 O  O   . HOH G 6 .   ? 35.195 26.257  40.929 1.00 16.91 ? 532 HOH A O   1 
HETATM 2511 O  O   . HOH G 6 .   ? 32.990 12.201  39.436 1.00 38.80 ? 533 HOH A O   1 
HETATM 2512 O  O   . HOH G 6 .   ? 32.008 7.028   33.502 1.00 37.78 ? 534 HOH A O   1 
HETATM 2513 O  O   . HOH G 6 .   ? 46.583 19.812  36.429 1.00 17.25 ? 535 HOH A O   1 
HETATM 2514 O  O   . HOH G 6 .   ? 41.525 5.938   19.897 1.00 37.76 ? 536 HOH A O   1 
HETATM 2515 O  O   . HOH G 6 .   ? 43.146 27.520  21.748 1.00 36.48 ? 537 HOH A O   1 
HETATM 2516 O  O   . HOH G 6 .   ? 58.214 2.839   24.947 1.00 34.15 ? 538 HOH A O   1 
HETATM 2517 O  O   . HOH G 6 .   ? 33.286 13.550  33.263 1.00 36.04 ? 539 HOH A O   1 
HETATM 2518 O  O   . HOH G 6 .   ? 50.566 18.457  28.745 1.00 16.40 ? 540 HOH A O   1 
HETATM 2519 O  O   . HOH G 6 .   ? 38.368 0.545   28.073 1.00 39.78 ? 541 HOH A O   1 
HETATM 2520 O  O   . HOH G 6 .   ? 43.085 17.761  44.649 1.00 22.98 ? 542 HOH A O   1 
HETATM 2521 O  O   . HOH G 6 .   ? 31.237 29.400  36.626 1.00 30.73 ? 543 HOH A O   1 
HETATM 2522 O  O   . HOH G 6 .   ? 45.482 25.708  20.499 1.00 43.43 ? 544 HOH A O   1 
HETATM 2523 O  O   . HOH G 6 .   ? 71.662 4.689   32.714 1.00 41.88 ? 545 HOH A O   1 
HETATM 2524 O  O   . HOH G 6 .   ? 51.417 11.182  47.214 1.00 34.09 ? 546 HOH A O   1 
HETATM 2525 O  O   . HOH G 6 .   ? 67.244 22.981  44.753 1.00 36.57 ? 547 HOH A O   1 
HETATM 2526 O  O   . HOH G 6 .   ? 49.544 9.793   12.886 1.00 43.49 ? 548 HOH A O   1 
HETATM 2527 O  O   . HOH G 6 .   ? 56.524 10.876  23.794 1.00 19.30 ? 549 HOH A O   1 
HETATM 2528 O  O   . HOH G 6 .   ? 46.210 29.171  26.636 1.00 15.72 ? 550 HOH A O   1 
HETATM 2529 O  O   . HOH G 6 .   ? 57.221 -2.916  22.648 1.00 45.28 ? 551 HOH A O   1 
HETATM 2530 O  O   . HOH G 6 .   ? 44.379 12.378  22.436 1.00 39.65 ? 552 HOH A O   1 
HETATM 2531 O  O   . HOH G 6 .   ? 60.269 25.255  30.745 1.00 24.19 ? 553 HOH A O   1 
HETATM 2532 O  O   . HOH G 6 .   ? 28.423 25.757  19.398 1.00 25.27 ? 554 HOH A O   1 
HETATM 2533 O  O   . HOH G 6 .   ? 44.084 9.601   15.978 1.00 29.61 ? 555 HOH A O   1 
HETATM 2534 O  O   . HOH G 6 .   ? 50.538 15.519  50.743 1.00 32.20 ? 556 HOH A O   1 
HETATM 2535 O  O   . HOH G 6 .   ? 53.643 5.159   55.971 1.00 38.31 ? 557 HOH A O   1 
HETATM 2536 O  O   . HOH G 6 .   ? 46.447 18.599  29.689 1.00 30.50 ? 558 HOH A O   1 
HETATM 2537 O  O   . HOH G 6 .   ? 63.437 17.605  37.035 1.00 16.20 ? 559 HOH A O   1 
HETATM 2538 O  O   . HOH G 6 .   ? 59.630 12.649  23.176 1.00 31.21 ? 560 HOH A O   1 
HETATM 2539 O  O   . HOH G 6 .   ? 53.954 27.493  23.993 1.00 20.75 ? 561 HOH A O   1 
HETATM 2540 O  O   . HOH G 6 .   ? 65.339 29.633  40.236 1.00 33.57 ? 562 HOH A O   1 
HETATM 2541 O  O   . HOH G 6 .   ? 28.596 27.688  45.791 1.00 37.90 ? 563 HOH A O   1 
HETATM 2542 O  O   . HOH G 6 .   ? 56.752 -0.649  23.261 1.00 41.21 ? 564 HOH A O   1 
HETATM 2543 O  O   . HOH G 6 .   ? 35.479 14.602  41.120 1.00 25.74 ? 565 HOH A O   1 
HETATM 2544 O  O   . HOH G 6 .   ? 31.814 14.324  51.656 1.00 38.10 ? 566 HOH A O   1 
HETATM 2545 O  O   . HOH G 6 .   ? 29.280 20.731  31.683 1.00 9.61  ? 567 HOH A O   1 
HETATM 2546 O  O   . HOH G 6 .   ? 51.652 1.467   39.488 1.00 31.01 ? 568 HOH A O   1 
HETATM 2547 O  O   . HOH G 6 .   ? 36.030 -0.657  24.935 1.00 33.50 ? 569 HOH A O   1 
HETATM 2548 O  O   . HOH G 6 .   ? 46.770 5.161   48.543 1.00 30.36 ? 570 HOH A O   1 
HETATM 2549 O  O   . HOH G 6 .   ? 27.370 22.281  45.812 1.00 27.41 ? 571 HOH A O   1 
HETATM 2550 O  O   . HOH G 6 .   ? 50.918 1.397   47.797 1.00 32.57 ? 572 HOH A O   1 
HETATM 2551 O  O   . HOH G 6 .   ? 60.531 15.693  52.850 1.00 39.58 ? 573 HOH A O   1 
HETATM 2552 O  O   . HOH G 6 .   ? 49.611 2.085   42.903 1.00 24.67 ? 574 HOH A O   1 
HETATM 2553 O  O   . HOH G 6 .   ? 37.926 0.886   49.953 1.00 36.47 ? 575 HOH A O   1 
HETATM 2554 O  O   . HOH G 6 .   ? 56.772 24.201  14.637 1.00 25.91 ? 576 HOH A O   1 
HETATM 2555 O  O   . HOH G 6 .   ? 38.078 10.323  47.681 1.00 13.38 ? 577 HOH A O   1 
HETATM 2556 O  O   . HOH G 6 .   ? 34.424 28.392  50.877 1.00 21.98 ? 578 HOH A O   1 
HETATM 2557 O  O   . HOH G 6 .   ? 34.176 0.000   22.915 0.50 26.54 ? 579 HOH A O   1 
HETATM 2558 O  O   . HOH G 6 .   ? 63.073 13.134  28.166 1.00 12.24 ? 580 HOH A O   1 
HETATM 2559 O  O   . HOH G 6 .   ? 34.216 8.007   48.165 1.00 32.26 ? 581 HOH A O   1 
HETATM 2560 O  O   . HOH G 6 .   ? 66.806 8.686   35.079 1.00 29.02 ? 582 HOH A O   1 
HETATM 2561 O  O   . HOH G 6 .   ? 54.337 30.848  32.416 1.00 23.55 ? 583 HOH A O   1 
HETATM 2562 O  O   . HOH G 6 .   ? 67.762 8.742   30.136 1.00 27.44 ? 584 HOH A O   1 
HETATM 2563 O  O   . HOH G 6 .   ? 53.833 17.198  40.705 1.00 22.10 ? 585 HOH A O   1 
HETATM 2564 O  O   . HOH G 6 .   ? 48.626 38.424  28.139 1.00 30.03 ? 586 HOH A O   1 
HETATM 2565 O  O   . HOH G 6 .   ? 56.314 -5.289  32.613 1.00 43.26 ? 587 HOH A O   1 
HETATM 2566 O  O   . HOH G 6 .   ? 43.259 -4.260  28.358 1.00 39.11 ? 588 HOH A O   1 
HETATM 2567 O  O   . HOH G 6 .   ? 45.324 11.035  21.059 1.00 23.35 ? 589 HOH A O   1 
HETATM 2568 O  O   . HOH G 6 .   ? 68.400 6.285   28.520 1.00 38.54 ? 590 HOH A O   1 
HETATM 2569 O  O   . HOH G 6 .   ? 64.782 14.109  42.573 1.00 22.34 ? 591 HOH A O   1 
HETATM 2570 O  O   . HOH G 6 .   ? 30.421 32.436  43.753 1.00 27.34 ? 592 HOH A O   1 
HETATM 2571 O  O   . HOH G 6 .   ? 24.008 29.870  34.984 1.00 40.58 ? 593 HOH A O   1 
HETATM 2572 O  O   . HOH G 6 .   ? 59.889 28.771  32.806 1.00 37.44 ? 594 HOH A O   1 
HETATM 2573 O  O   . HOH G 6 .   ? 56.772 8.669   22.214 1.00 27.85 ? 595 HOH A O   1 
HETATM 2574 O  O   . HOH G 6 .   ? 26.866 30.648  42.812 1.00 38.71 ? 596 HOH A O   1 
HETATM 2575 O  O   . HOH G 6 .   ? 44.712 -2.490  33.065 1.00 37.62 ? 597 HOH A O   1 
HETATM 2576 O  O   . HOH G 6 .   ? 57.502 29.603  32.678 1.00 33.88 ? 598 HOH A O   1 
HETATM 2577 O  O   . HOH G 6 .   ? 23.570 14.858  47.128 1.00 38.30 ? 599 HOH A O   1 
HETATM 2578 O  O   . HOH G 6 .   ? 61.478 -0.233  42.479 1.00 23.23 ? 600 HOH A O   1 
HETATM 2579 O  O   . HOH G 6 .   ? 51.165 24.019  16.798 1.00 34.77 ? 601 HOH A O   1 
HETATM 2580 O  O   . HOH G 6 .   ? 43.539 4.579   51.220 1.00 19.56 ? 602 HOH A O   1 
HETATM 2581 O  O   . HOH G 6 .   ? 62.129 29.699  37.728 1.00 35.38 ? 603 HOH A O   1 
HETATM 2582 O  O   . HOH G 6 .   ? 36.651 18.387  50.908 1.00 14.53 ? 604 HOH A O   1 
HETATM 2583 O  O   . HOH G 6 .   ? 56.447 4.839   24.001 1.00 31.55 ? 605 HOH A O   1 
HETATM 2584 O  O   . HOH G 6 .   ? 46.643 11.724  24.000 1.00 17.85 ? 606 HOH A O   1 
HETATM 2585 O  O   . HOH G 6 .   ? 58.877 30.408  40.940 1.00 29.24 ? 607 HOH A O   1 
HETATM 2586 O  O   . HOH G 6 .   ? 62.211 12.542  50.175 1.00 39.39 ? 608 HOH A O   1 
HETATM 2587 O  O   . HOH G 6 .   ? 51.904 36.072  30.056 1.00 28.84 ? 609 HOH A O   1 
HETATM 2588 O  O   . HOH G 6 .   ? 37.988 28.924  22.496 1.00 25.50 ? 610 HOH A O   1 
HETATM 2589 O  O   . HOH G 6 .   ? 26.970 29.357  26.774 1.00 12.51 ? 611 HOH A O   1 
HETATM 2590 O  O   . HOH G 6 .   ? 27.756 30.977  39.568 1.00 35.44 ? 612 HOH A O   1 
HETATM 2591 O  O   . HOH G 6 .   ? 50.772 28.319  22.956 1.00 36.23 ? 613 HOH A O   1 
HETATM 2592 O  O   . HOH G 6 .   ? 64.684 17.326  48.574 1.00 29.76 ? 614 HOH A O   1 
HETATM 2593 O  O   . HOH G 6 .   ? 34.020 16.315  33.772 1.00 25.81 ? 615 HOH A O   1 
HETATM 2594 O  O   . HOH G 6 .   ? 31.994 36.684  31.832 1.00 34.63 ? 616 HOH A O   1 
HETATM 2595 O  O   . HOH G 6 .   ? 43.810 37.966  40.604 1.00 21.67 ? 617 HOH A O   1 
HETATM 2596 O  O   . HOH G 6 .   ? 47.375 38.405  34.086 1.00 40.71 ? 618 HOH A O   1 
HETATM 2597 O  O   . HOH G 6 .   ? 37.838 39.332  38.217 1.00 23.84 ? 619 HOH A O   1 
HETATM 2598 O  O   . HOH G 6 .   ? 25.535 16.315  49.054 1.00 23.38 ? 620 HOH A O   1 
HETATM 2599 O  O   . HOH G 6 .   ? 48.345 1.918   39.469 1.00 33.69 ? 621 HOH A O   1 
HETATM 2600 O  O   . HOH G 6 .   ? 63.749 23.132  48.331 1.00 25.79 ? 622 HOH A O   1 
HETATM 2601 O  O   . HOH G 6 .   ? 40.171 20.630  34.949 1.00 16.22 ? 623 HOH A O   1 
HETATM 2602 O  O   . HOH G 6 .   ? 44.093 18.396  29.733 1.00 18.54 ? 624 HOH A O   1 
HETATM 2603 O  O   . HOH G 6 .   ? 48.735 37.816  31.771 1.00 27.27 ? 625 HOH A O   1 
HETATM 2604 O  O   . HOH G 6 .   ? 35.742 11.453  48.654 1.00 12.68 ? 626 HOH A O   1 
HETATM 2605 O  O   . HOH G 6 .   ? 40.240 5.398   42.856 1.00 20.79 ? 627 HOH A O   1 
HETATM 2606 O  O   . HOH G 6 .   ? 43.985 -2.085  16.169 1.00 33.52 ? 628 HOH A O   1 
HETATM 2607 O  O   . HOH G 6 .   ? 27.116 14.938  38.297 1.00 20.51 ? 629 HOH A O   1 
HETATM 2608 O  O   . HOH G 6 .   ? 60.361 -4.437  28.696 1.00 38.02 ? 630 HOH A O   1 
HETATM 2609 O  O   . HOH G 6 .   ? 31.295 17.476  54.700 1.00 22.13 ? 631 HOH A O   1 
HETATM 2610 O  O   . HOH G 6 .   ? 49.479 35.013  42.303 1.00 23.28 ? 632 HOH A O   1 
HETATM 2611 O  O   . HOH G 6 .   ? 36.120 17.520  37.066 1.00 38.35 ? 633 HOH A O   1 
HETATM 2612 O  O   . HOH G 6 .   ? 46.910 17.898  42.759 1.00 12.21 ? 634 HOH A O   1 
HETATM 2613 O  O   . HOH G 6 .   ? 37.539 6.998   40.507 1.00 36.54 ? 635 HOH A O   1 
HETATM 2614 O  O   . HOH G 6 .   ? 43.547 10.269  56.924 1.00 32.77 ? 636 HOH A O   1 
HETATM 2615 O  O   . HOH G 6 .   ? 46.159 3.698   13.301 1.00 40.44 ? 637 HOH A O   1 
HETATM 2616 O  O   . HOH G 6 .   ? 38.879 9.319   50.001 1.00 14.14 ? 638 HOH A O   1 
HETATM 2617 O  O   . HOH G 6 .   ? 59.583 2.930   47.556 1.00 28.08 ? 639 HOH A O   1 
HETATM 2618 O  O   . HOH G 6 .   ? 46.169 7.679   56.754 1.00 43.96 ? 640 HOH A O   1 
HETATM 2619 O  O   . HOH G 6 .   ? 38.747 17.086  57.608 1.00 28.85 ? 641 HOH A O   1 
HETATM 2620 O  O   . HOH G 6 .   ? 51.297 12.935  50.048 1.00 29.10 ? 642 HOH A O   1 
HETATM 2621 O  O   . HOH G 6 .   ? 47.374 23.682  49.541 1.00 17.88 ? 643 HOH A O   1 
HETATM 2622 O  O   . HOH G 6 .   ? 62.179 0.176   35.126 1.00 23.29 ? 644 HOH A O   1 
HETATM 2623 O  O   . HOH G 6 .   ? 66.348 26.651  28.262 1.00 16.84 ? 645 HOH A O   1 
HETATM 2624 O  O   . HOH G 6 .   ? 59.673 28.798  46.673 1.00 34.25 ? 646 HOH A O   1 
HETATM 2625 O  O   . HOH G 6 .   ? 41.265 14.064  43.138 1.00 24.43 ? 647 HOH A O   1 
HETATM 2626 O  O   . HOH G 6 .   ? 61.281 18.692  29.431 1.00 10.04 ? 648 HOH A O   1 
HETATM 2627 O  O   . HOH G 6 .   ? 13.991 7.961   29.032 1.00 42.58 ? 649 HOH A O   1 
HETATM 2628 O  O   . HOH G 6 .   ? 35.051 7.969   22.338 1.00 37.91 ? 650 HOH A O   1 
HETATM 2629 O  O   . HOH G 6 .   ? 45.529 19.232  44.673 1.00 16.94 ? 651 HOH A O   1 
HETATM 2630 O  O   . HOH G 6 .   ? 29.097 27.037  39.237 1.00 20.40 ? 652 HOH A O   1 
HETATM 2631 O  O   . HOH G 6 .   ? 34.613 24.275  18.439 1.00 38.64 ? 653 HOH A O   1 
HETATM 2632 O  O   . HOH G 6 .   ? 36.283 12.841  25.019 1.00 31.40 ? 654 HOH A O   1 
HETATM 2633 O  O   . HOH G 6 .   ? 35.913 6.987   25.182 1.00 26.57 ? 655 HOH A O   1 
HETATM 2634 O  O   . HOH G 6 .   ? 60.044 20.533  30.973 1.00 15.37 ? 656 HOH A O   1 
HETATM 2635 O  O   . HOH G 6 .   ? 34.991 9.096   45.880 1.00 17.92 ? 657 HOH A O   1 
HETATM 2636 O  O   . HOH G 6 .   ? 25.681 26.689  32.738 1.00 13.26 ? 658 HOH A O   1 
HETATM 2637 O  O   . HOH G 6 .   ? 49.072 26.544  54.709 1.00 38.36 ? 659 HOH A O   1 
HETATM 2638 O  O   . HOH G 6 .   ? 53.212 1.206   46.419 1.00 26.84 ? 660 HOH A O   1 
HETATM 2639 O  O   . HOH G 6 .   ? 60.406 8.926   30.207 1.00 24.05 ? 661 HOH A O   1 
HETATM 2640 O  O   . HOH G 6 .   ? 36.435 10.700  37.984 1.00 42.39 ? 662 HOH A O   1 
HETATM 2641 O  O   . HOH G 6 .   ? 44.134 6.020   58.016 1.00 43.28 ? 663 HOH A O   1 
HETATM 2642 O  O   . HOH G 6 .   ? 24.297 17.176  41.809 1.00 23.05 ? 664 HOH A O   1 
HETATM 2643 O  O   . HOH G 6 .   ? 31.189 31.407  24.268 1.00 15.64 ? 665 HOH A O   1 
HETATM 2644 O  O   . HOH G 6 .   ? 51.359 5.639   20.550 1.00 34.84 ? 666 HOH A O   1 
HETATM 2645 O  O   . HOH G 6 .   ? 45.074 23.636  22.239 1.00 29.44 ? 667 HOH A O   1 
HETATM 2646 O  O   . HOH G 6 .   ? 45.493 8.543   51.986 1.00 20.19 ? 668 HOH A O   1 
HETATM 2647 O  O   . HOH G 6 .   ? 65.579 2.128   33.979 1.00 27.69 ? 669 HOH A O   1 
HETATM 2648 O  O   . HOH G 6 .   ? 51.411 -7.180  26.156 1.00 26.57 ? 670 HOH A O   1 
HETATM 2649 O  O   . HOH G 6 .   ? 46.381 3.491   38.186 1.00 17.79 ? 671 HOH A O   1 
HETATM 2650 O  O   . HOH G 6 .   ? 55.131 -3.795  41.392 1.00 32.83 ? 672 HOH A O   1 
HETATM 2651 O  O   . HOH G 6 .   ? 66.798 13.525  38.293 1.00 38.31 ? 673 HOH A O   1 
HETATM 2652 O  O   . HOH G 6 .   ? 32.720 27.641  19.263 1.00 30.96 ? 674 HOH A O   1 
HETATM 2653 O  O   . HOH G 6 .   ? 41.183 18.424  58.064 1.00 24.56 ? 675 HOH A O   1 
HETATM 2654 O  O   . HOH G 6 .   ? 38.719 7.236   55.520 1.00 37.92 ? 676 HOH A O   1 
HETATM 2655 O  O   . HOH G 6 .   ? 56.064 31.850  29.776 1.00 34.94 ? 677 HOH A O   1 
HETATM 2656 O  O   . HOH G 6 .   ? 30.717 12.759  32.100 1.00 36.19 ? 678 HOH A O   1 
HETATM 2657 O  O   . HOH G 6 .   ? 52.194 1.671   21.975 1.00 36.25 ? 679 HOH A O   1 
HETATM 2658 O  O   . HOH G 6 .   ? 52.111 -2.517  43.710 1.00 41.21 ? 680 HOH A O   1 
HETATM 2659 O  O   . HOH G 6 .   ? 37.819 29.432  51.063 1.00 24.02 ? 681 HOH A O   1 
HETATM 2660 O  O   . HOH G 6 .   ? 26.297 11.081  41.845 1.00 40.50 ? 682 HOH A O   1 
HETATM 2661 O  O   . HOH G 6 .   ? 38.581 5.306   20.055 1.00 31.82 ? 683 HOH A O   1 
HETATM 2662 O  O   . HOH G 6 .   ? 31.645 30.076  33.790 1.00 18.02 ? 684 HOH A O   1 
HETATM 2663 O  O   . HOH G 6 .   ? 60.216 -1.856  29.470 1.00 27.60 ? 685 HOH A O   1 
HETATM 2664 O  O   . HOH G 6 .   ? 43.952 16.197  19.070 1.00 35.13 ? 686 HOH A O   1 
HETATM 2665 O  O   . HOH G 6 .   ? 67.462 23.412  42.490 1.00 33.15 ? 687 HOH A O   1 
HETATM 2666 O  O   . HOH G 6 .   ? 56.865 28.965  47.045 1.00 25.73 ? 688 HOH A O   1 
HETATM 2667 O  O   . HOH G 6 .   ? 54.423 27.581  38.522 1.00 23.63 ? 689 HOH A O   1 
HETATM 2668 O  O   . HOH G 6 .   ? 37.286 3.909   30.493 1.00 36.64 ? 690 HOH A O   1 
HETATM 2669 O  O   . HOH G 6 .   ? 53.776 35.360  34.176 1.00 36.88 ? 691 HOH A O   1 
HETATM 2670 O  O   . HOH G 6 .   ? 40.380 24.380  52.086 1.00 21.42 ? 692 HOH A O   1 
HETATM 2671 O  O   . HOH G 6 .   ? 40.485 23.193  25.126 1.00 17.26 ? 693 HOH A O   1 
HETATM 2672 O  O   . HOH G 6 .   ? 40.583 3.687   13.539 1.00 45.67 ? 694 HOH A O   1 
HETATM 2673 O  O   . HOH G 6 .   ? 50.840 31.810  47.299 1.00 29.38 ? 695 HOH A O   1 
HETATM 2674 O  O   . HOH G 6 .   ? 66.343 27.152  32.815 1.00 35.75 ? 696 HOH A O   1 
HETATM 2675 O  O   . HOH G 6 .   ? 54.703 5.306   21.260 1.00 39.30 ? 697 HOH A O   1 
HETATM 2676 O  O   . HOH G 6 .   ? 20.798 18.139  33.478 1.00 27.01 ? 698 HOH A O   1 
HETATM 2677 O  O   . HOH G 6 .   ? 37.992 13.781  41.496 1.00 26.55 ? 699 HOH A O   1 
HETATM 2678 O  O   . HOH G 6 .   ? 55.200 15.976  53.051 1.00 36.29 ? 700 HOH A O   1 
HETATM 2679 O  O   . HOH G 6 .   ? 48.005 -4.762  20.366 1.00 39.46 ? 701 HOH A O   1 
HETATM 2680 O  O   . HOH G 6 .   ? 41.061 18.611  49.328 1.00 18.30 ? 702 HOH A O   1 
HETATM 2681 O  O   . HOH G 6 .   ? 37.601 37.350  43.088 1.00 32.35 ? 703 HOH A O   1 
HETATM 2682 O  O   . HOH G 6 .   ? 44.542 0.924   47.716 1.00 37.36 ? 704 HOH A O   1 
HETATM 2683 O  O   . HOH G 6 .   ? 38.987 34.643  42.736 1.00 29.11 ? 705 HOH A O   1 
HETATM 2684 O  O   . HOH G 6 .   ? 42.095 4.937   17.921 1.00 42.39 ? 706 HOH A O   1 
HETATM 2685 O  O   . HOH G 6 .   ? 29.746 9.746   29.984 1.00 36.46 ? 707 HOH A O   1 
HETATM 2686 O  O   . HOH G 6 .   ? 36.547 0.741   32.227 1.00 34.04 ? 708 HOH A O   1 
HETATM 2687 O  O   . HOH G 6 .   ? 67.836 23.140  38.683 1.00 39.17 ? 709 HOH A O   1 
HETATM 2688 O  O   . HOH G 6 .   ? 50.972 -6.332  21.920 1.00 35.63 ? 710 HOH A O   1 
HETATM 2689 O  O   . HOH G 6 .   ? 57.561 -3.682  49.381 1.00 36.21 ? 711 HOH A O   1 
HETATM 2690 O  O   . HOH G 6 .   ? 42.977 26.255  55.007 1.00 35.02 ? 712 HOH A O   1 
HETATM 2691 O  O   . HOH G 6 .   ? 51.833 7.336   18.902 1.00 39.55 ? 713 HOH A O   1 
HETATM 2692 O  O   . HOH G 6 .   ? 44.952 26.711  24.512 1.00 19.23 ? 714 HOH A O   1 
HETATM 2693 O  O   . HOH G 6 .   ? 33.899 7.573   43.469 1.00 37.01 ? 715 HOH A O   1 
HETATM 2694 O  O   . HOH G 6 .   ? 66.723 23.459  50.917 1.00 45.91 ? 716 HOH A O   1 
HETATM 2695 O  O   . HOH G 6 .   ? 43.661 12.684  37.847 1.00 29.71 ? 717 HOH A O   1 
HETATM 2696 O  O   . HOH G 6 .   ? 44.588 30.617  50.603 1.00 27.74 ? 718 HOH A O   1 
HETATM 2697 O  O   . HOH G 6 .   ? 49.450 -0.047  38.212 1.00 29.86 ? 719 HOH A O   1 
HETATM 2698 O  O   . HOH G 6 .   ? 43.961 33.430  48.561 1.00 41.01 ? 720 HOH A O   1 
HETATM 2699 O  O   . HOH G 6 .   ? 26.182 20.164  48.255 1.00 22.52 ? 721 HOH A O   1 
HETATM 2700 O  O   . HOH G 6 .   ? 26.329 8.670   49.460 1.00 40.08 ? 722 HOH A O   1 
HETATM 2701 O  O   . HOH G 6 .   ? 35.406 15.561  53.795 1.00 37.46 ? 723 HOH A O   1 
HETATM 2702 O  O   . HOH G 6 .   ? 48.073 2.364   19.490 1.00 33.25 ? 724 HOH A O   1 
HETATM 2703 O  O   . HOH G 6 .   ? 34.177 12.169  54.083 0.50 35.34 ? 725 HOH A O   1 
HETATM 2704 O  O   . HOH G 6 .   ? 54.147 -2.071  39.655 1.00 34.95 ? 726 HOH A O   1 
HETATM 2705 O  O   . HOH G 6 .   ? 28.732 29.716  33.250 1.00 17.50 ? 727 HOH A O   1 
HETATM 2706 O  O   . HOH G 6 .   ? 54.135 36.254  36.163 1.00 40.60 ? 728 HOH A O   1 
HETATM 2707 O  O   . HOH G 6 .   ? 68.353 18.701  54.083 0.50 44.51 ? 729 HOH A O   1 
HETATM 2708 O  O   . HOH G 6 .   ? 27.958 12.535  38.105 1.00 37.85 ? 730 HOH A O   1 
HETATM 2709 O  O   . HOH G 6 .   ? 34.601 5.186   47.538 1.00 27.56 ? 731 HOH A O   1 
HETATM 2710 O  O   . HOH G 6 .   ? 51.292 20.676  11.426 1.00 43.77 ? 732 HOH A O   1 
HETATM 2711 O  O   . HOH G 6 .   ? 35.230 9.481   35.062 1.00 36.71 ? 733 HOH A O   1 
HETATM 2712 O  O   . HOH G 6 .   ? 32.700 37.841  43.221 1.00 33.07 ? 734 HOH A O   1 
HETATM 2713 O  O   . HOH G 6 .   ? 30.053 7.891   49.281 1.00 40.10 ? 735 HOH A O   1 
HETATM 2714 O  O   . HOH G 6 .   ? 27.630 27.903  31.377 1.00 11.64 ? 736 HOH A O   1 
HETATM 2715 O  O   . HOH G 6 .   ? 51.800 -1.355  41.536 1.00 36.21 ? 737 HOH A O   1 
HETATM 2716 O  O   . HOH G 6 .   ? 42.265 29.329  50.301 1.00 22.32 ? 738 HOH A O   1 
HETATM 2717 O  O   . HOH G 6 .   ? 35.948 5.927   18.547 1.00 41.38 ? 739 HOH A O   1 
HETATM 2718 O  O   . HOH G 6 .   ? 34.696 15.941  38.861 1.00 19.09 ? 740 HOH A O   1 
HETATM 2719 O  O   . HOH G 6 .   ? 58.794 8.146   49.335 1.00 23.72 ? 741 HOH A O   1 
HETATM 2720 O  O   . HOH G 6 .   ? 53.644 -1.857  22.753 1.00 31.23 ? 742 HOH A O   1 
HETATM 2721 O  O   . HOH G 6 .   ? 61.013 -5.616  24.999 1.00 41.84 ? 743 HOH A O   1 
HETATM 2722 O  O   . HOH G 6 .   ? 37.396 38.292  28.807 1.00 36.41 ? 744 HOH A O   1 
HETATM 2723 O  O   . HOH G 6 .   ? 47.423 28.045  22.972 1.00 35.56 ? 745 HOH A O   1 
HETATM 2724 O  O   . HOH G 6 .   ? 59.293 23.291  54.110 1.00 27.95 ? 746 HOH A O   1 
HETATM 2725 O  O   . HOH G 6 .   ? 47.122 6.828   13.630 1.00 43.84 ? 747 HOH A O   1 
HETATM 2726 O  O   . HOH G 6 .   ? 29.123 35.326  37.024 1.00 32.63 ? 748 HOH A O   1 
HETATM 2727 O  O   . HOH G 6 .   ? 41.790 34.546  22.568 1.00 42.04 ? 749 HOH A O   1 
HETATM 2728 O  O   . HOH G 6 .   ? 28.649 34.299  43.473 1.00 37.81 ? 750 HOH A O   1 
HETATM 2729 O  O   . HOH G 6 .   ? 33.768 29.572  20.294 1.00 43.12 ? 751 HOH A O   1 
HETATM 2730 O  O   . HOH G 6 .   ? 55.126 20.310  56.215 1.00 42.49 ? 752 HOH A O   1 
HETATM 2731 O  O   . HOH G 6 .   ? 65.125 -0.259  35.140 1.00 31.04 ? 753 HOH A O   1 
HETATM 2732 O  O   . HOH G 6 .   ? 28.445 24.109  21.209 1.00 33.48 ? 754 HOH A O   1 
HETATM 2733 O  O   . HOH G 6 .   ? 65.340 5.172   39.865 1.00 24.75 ? 755 HOH A O   1 
HETATM 2734 O  O   . HOH G 6 .   ? 41.766 32.611  21.564 1.00 34.72 ? 756 HOH A O   1 
HETATM 2735 O  O   . HOH G 6 .   ? 55.353 26.218  51.669 1.00 37.76 ? 757 HOH A O   1 
HETATM 2736 O  O   . HOH G 6 .   ? 33.176 38.814  33.856 1.00 40.09 ? 758 HOH A O   1 
HETATM 2737 O  O   . HOH G 6 .   ? 42.969 24.516  58.718 1.00 36.44 ? 759 HOH A O   1 
HETATM 2738 O  O   . HOH G 6 .   ? 67.017 4.994   37.739 1.00 31.19 ? 760 HOH A O   1 
HETATM 2739 O  O   . HOH G 6 .   ? 65.938 10.982  35.989 1.00 33.76 ? 761 HOH A O   1 
HETATM 2740 O  O   . HOH G 6 .   ? 40.729 16.311  37.255 1.00 39.97 ? 762 HOH A O   1 
HETATM 2741 O  O   . HOH G 6 .   ? 42.680 19.041  47.112 1.00 29.35 ? 763 HOH A O   1 
HETATM 2742 O  O   . HOH G 6 .   ? 65.153 9.403   42.304 1.00 30.85 ? 764 HOH A O   1 
HETATM 2743 O  O   . HOH G 6 .   ? 31.558 33.136  46.948 1.00 36.26 ? 765 HOH A O   1 
HETATM 2744 O  O   . HOH G 6 .   ? 25.138 7.556   45.347 1.00 35.18 ? 766 HOH A O   1 
HETATM 2745 O  O   . HOH G 6 .   ? 37.932 9.319   19.397 1.00 41.33 ? 767 HOH A O   1 
HETATM 2746 O  O   . HOH G 6 .   ? 44.400 18.530  18.860 1.00 39.83 ? 768 HOH A O   1 
HETATM 2747 O  O   . HOH G 6 .   ? 65.496 11.942  40.958 1.00 34.22 ? 769 HOH A O   1 
HETATM 2748 O  O   . HOH G 6 .   ? 46.742 2.146   40.907 1.00 40.20 ? 770 HOH A O   1 
HETATM 2749 O  O   . HOH G 6 .   ? 46.673 18.991  47.490 1.00 35.11 ? 771 HOH A O   1 
HETATM 2750 O  O   . HOH G 6 .   ? 50.335 22.028  55.636 1.00 40.02 ? 772 HOH A O   1 
HETATM 2751 O  O   . HOH G 6 .   ? 22.560 14.652  45.267 1.00 37.67 ? 773 HOH A O   1 
HETATM 2752 O  O   . HOH G 6 .   ? 40.870 9.777   39.741 1.00 37.67 ? 774 HOH A O   1 
HETATM 2753 O  O   . HOH G 6 .   ? 52.809 13.286  23.488 1.00 26.68 ? 775 HOH A O   1 
HETATM 2754 O  O   . HOH G 6 .   ? 67.306 -1.470  39.314 1.00 38.97 ? 776 HOH A O   1 
HETATM 2755 O  O   . HOH G 6 .   ? 45.878 6.119   50.980 1.00 19.82 ? 777 HOH A O   1 
HETATM 2756 O  O   . HOH G 6 .   ? 53.913 35.789  42.385 1.00 42.38 ? 778 HOH A O   1 
HETATM 2757 O  O   . HOH G 6 .   ? 26.312 29.643  29.648 1.00 15.94 ? 779 HOH A O   1 
HETATM 2758 O  O   . HOH G 6 .   ? 52.910 14.800  52.820 1.00 34.21 ? 780 HOH A O   1 
HETATM 2759 O  O   . HOH G 6 .   ? 58.177 6.403   22.596 1.00 35.40 ? 781 HOH A O   1 
HETATM 2760 O  O   . HOH G 6 .   ? 68.009 10.606  38.825 1.00 38.26 ? 782 HOH A O   1 
HETATM 2761 O  O   . HOH G 6 .   ? 42.431 14.896  38.908 1.00 31.72 ? 783 HOH A O   1 
HETATM 2762 O  O   . HOH G 6 .   ? 25.865 8.551   42.680 1.00 42.69 ? 784 HOH A O   1 
HETATM 2763 O  O   . HOH G 6 .   ? 19.451 14.895  46.658 1.00 45.88 ? 785 HOH A O   1 
HETATM 2764 O  O   . HOH G 6 .   ? 62.129 15.066  50.876 1.00 38.34 ? 786 HOH A O   1 
HETATM 2765 O  O   . HOH G 6 .   ? 66.300 7.265   41.352 1.00 30.17 ? 787 HOH A O   1 
HETATM 2766 O  O   . HOH G 6 .   ? 39.062 14.458  37.878 1.00 35.38 ? 788 HOH A O   1 
HETATM 2767 O  O   . HOH G 6 .   ? 60.658 14.592  55.425 1.00 43.90 ? 789 HOH A O   1 
HETATM 2768 O  O   . HOH G 6 .   ? 56.142 3.340   21.581 1.00 43.95 ? 790 HOH A O   1 
HETATM 2769 O  O   . HOH G 6 .   ? 35.270 38.213  34.192 1.00 40.35 ? 791 HOH A O   1 
HETATM 2770 O  O   . HOH G 6 .   ? 54.188 25.476  55.022 1.00 47.26 ? 792 HOH A O   1 
HETATM 2771 O  O   . HOH G 6 .   ? 50.680 27.500  20.433 1.00 40.87 ? 793 HOH A O   1 
HETATM 2772 O  O   . HOH G 6 .   ? 40.516 26.449  53.420 1.00 35.53 ? 794 HOH A O   1 
HETATM 2773 O  O   . HOH G 6 .   ? 68.216 8.238   39.813 1.00 36.96 ? 795 HOH A O   1 
HETATM 2774 O  O   . HOH G 6 .   ? 61.367 5.079   47.817 1.00 37.69 ? 796 HOH A O   1 
HETATM 2775 O  O   . HOH G 6 .   ? 41.012 12.464  40.709 1.00 37.00 ? 797 HOH A O   1 
HETATM 2776 O  O   . HOH G 6 .   ? 43.908 3.197   39.242 1.00 27.97 ? 798 HOH A O   1 
HETATM 2777 O  O   . HOH G 6 .   ? 61.412 12.682  54.703 1.00 43.14 ? 799 HOH A O   1 
HETATM 2778 O  O   . HOH G 6 .   ? 40.263 18.516  37.207 1.00 37.39 ? 800 HOH A O   1 
HETATM 2779 O  O   . HOH G 6 .   ? 39.593 3.606   40.637 1.00 37.63 ? 801 HOH A O   1 
HETATM 2780 O  O   . HOH G 6 .   ? 34.177 9.112   54.083 0.50 45.71 ? 802 HOH A O   1 
HETATM 2781 O  O   . HOH G 6 .   ? 67.253 28.599  30.084 1.00 40.47 ? 803 HOH A O   1 
HETATM 2782 O  O   . HOH G 6 .   ? 61.130 31.311  41.027 1.00 40.14 ? 804 HOH A O   1 
HETATM 2783 O  O   . HOH G 6 .   ? 31.932 28.882  51.943 1.00 40.02 ? 805 HOH A O   1 
HETATM 2784 O  O   . HOH G 6 .   ? 43.767 10.687  39.702 1.00 35.72 ? 806 HOH A O   1 
HETATM 2785 O  O   . HOH G 6 .   ? 33.397 32.879  23.755 1.00 27.30 ? 807 HOH A O   1 
HETATM 2786 O  O   . HOH G 6 .   ? 36.503 7.401   20.487 1.00 39.91 ? 808 HOH A O   1 
HETATM 2787 O  O   . HOH G 6 .   ? 34.923 13.297  37.047 1.00 33.62 ? 809 HOH A O   1 
HETATM 2788 O  O   . HOH G 6 .   ? 66.324 16.918  46.405 1.00 35.01 ? 810 HOH A O   1 
HETATM 2789 O  O   . HOH G 6 .   ? 54.759 11.567  19.755 1.00 37.49 ? 811 HOH A O   1 
HETATM 2790 O  O   . HOH G 6 .   ? 61.017 9.265   54.003 1.00 42.40 ? 812 HOH A O   1 
HETATM 2791 O  O   . HOH G 6 .   ? 40.396 28.805  52.434 1.00 34.89 ? 813 HOH A O   1 
HETATM 2792 O  O   . HOH G 6 .   ? 32.254 31.927  19.976 1.00 28.83 ? 814 HOH A O   1 
HETATM 2793 O  O   . HOH G 6 .   ? 53.735 4.286   58.767 1.00 42.29 ? 815 HOH A O   1 
HETATM 2794 O  O   . HOH G 6 .   ? 66.799 0.945   32.052 1.00 42.08 ? 816 HOH A O   1 
HETATM 2795 O  O   . HOH G 6 .   ? 64.705 15.574  50.677 1.00 42.68 ? 817 HOH A O   1 
HETATM 2796 O  O   . HOH G 6 .   ? 40.582 40.140  38.257 1.00 31.89 ? 818 HOH A O   1 
HETATM 2797 O  O   . HOH G 6 .   ? 55.141 12.601  22.165 1.00 29.82 ? 819 HOH A O   1 
HETATM 2798 O  O   . HOH G 6 .   ? 50.136 0.488   20.559 1.00 37.63 ? 820 HOH A O   1 
HETATM 2799 O  O   . HOH G 6 .   ? 33.171 6.549   52.653 1.00 43.48 ? 821 HOH A O   1 
HETATM 2800 O  O   . HOH G 6 .   ? 43.307 29.116  54.891 1.00 41.62 ? 822 HOH A O   1 
HETATM 2801 O  O   . HOH G 6 .   ? 68.644 8.972   33.189 1.00 36.53 ? 823 HOH A O   1 
HETATM 2802 O  O   . HOH G 6 .   ? 68.029 12.689  40.527 1.00 38.33 ? 824 HOH A O   1 
HETATM 2803 O  O   . HOH G 6 .   ? 48.837 -5.624  16.321 1.00 42.18 ? 825 HOH A O   1 
HETATM 2804 O  O   . HOH G 6 .   ? 68.641 6.862   37.432 1.00 39.61 ? 826 HOH A O   1 
HETATM 2805 O  O   . HOH G 6 .   ? 30.946 10.807  37.699 1.00 38.67 ? 827 HOH A O   1 
HETATM 2806 O  O   . HOH G 6 .   ? 51.767 34.478  43.536 1.00 39.90 ? 828 HOH A O   1 
HETATM 2807 O  O   . HOH G 6 .   ? 36.165 -2.977  26.763 1.00 40.93 ? 829 HOH A O   1 
HETATM 2808 O  O   . HOH G 6 .   ? 59.939 6.250   50.322 1.00 36.34 ? 830 HOH A O   1 
HETATM 2809 O  O   . HOH G 6 .   ? 67.839 5.560   25.744 1.00 36.22 ? 831 HOH A O   1 
HETATM 2810 O  O   . HOH G 6 .   ? 37.129 1.735   29.780 1.00 38.82 ? 832 HOH A O   1 
HETATM 2811 O  O   . HOH G 6 .   ? 52.690 5.008   18.657 1.00 39.82 ? 833 HOH A O   1 
HETATM 2812 O  O   . HOH G 6 .   ? 63.162 23.692  53.425 1.00 44.13 ? 834 HOH A O   1 
HETATM 2813 O  O   . HOH G 6 .   ? 33.245 30.192  18.014 1.00 41.09 ? 835 HOH A O   1 
HETATM 2814 O  O   . HOH G 6 .   ? 42.150 4.550   39.793 1.00 35.68 ? 836 HOH A O   1 
HETATM 2815 O  O   . HOH G 6 .   ? 64.175 24.227  50.764 1.00 34.50 ? 837 HOH A O   1 
HETATM 2816 O  O   . HOH G 6 .   ? 67.582 -0.927  36.658 1.00 32.53 ? 838 HOH A O   1 
HETATM 2817 O  O   . HOH G 6 .   ? 52.688 32.606  45.940 1.00 42.81 ? 839 HOH A O   1 
HETATM 2818 O  O   . HOH G 6 .   ? 27.417 33.525  38.158 1.00 39.72 ? 840 HOH A O   1 
HETATM 2819 O  O   . HOH G 6 .   ? 67.702 21.565  28.860 1.00 15.55 ? 841 HOH A O   1 
HETATM 2820 O  O   . HOH G 6 .   ? 45.315 17.514  48.782 1.00 34.05 ? 842 HOH A O   1 
HETATM 2821 O  O   . HOH G 6 .   ? 58.062 9.818   20.121 1.00 39.51 ? 843 HOH A O   1 
HETATM 2822 O  O   . HOH G 6 .   ? 66.631 15.352  44.336 1.00 34.24 ? 844 HOH A O   1 
HETATM 2823 O  O   . HOH G 6 .   ? 36.304 40.112  35.818 1.00 39.05 ? 845 HOH A O   1 
HETATM 2824 O  O   . HOH G 6 .   ? 57.373 13.840  21.832 1.00 24.97 ? 846 HOH A O   1 
HETATM 2825 O  O   . HOH G 6 .   ? 38.986 25.940  55.651 1.00 37.49 ? 847 HOH A O   1 
HETATM 2826 O  O   . HOH G 6 .   ? 42.062 40.142  40.207 1.00 41.13 ? 848 HOH A O   1 
HETATM 2827 O  O   . HOH G 6 .   ? 25.921 6.163   43.832 1.00 46.01 ? 849 HOH A O   1 
HETATM 2828 O  O   . HOH G 6 .   ? 59.691 1.996   49.925 1.00 38.25 ? 850 HOH A O   1 
HETATM 2829 O  O   . HOH G 6 .   ? 70.974 22.245  33.818 1.00 38.55 ? 851 HOH A O   1 
HETATM 2830 O  O   . HOH G 6 .   ? 36.178 28.232  20.043 1.00 36.64 ? 852 HOH A O   1 
HETATM 2831 O  O   . HOH G 6 .   ? 68.803 16.038  42.745 1.00 38.24 ? 853 HOH A O   1 
HETATM 2832 O  O   . HOH G 6 .   ? 56.085 31.396  47.225 1.00 36.13 ? 854 HOH A O   1 
HETATM 2833 O  O   . HOH G 6 .   ? 30.297 38.632  30.662 1.00 38.49 ? 855 HOH A O   1 
HETATM 2834 O  O   . HOH G 6 .   ? 40.895 7.178   40.640 1.00 35.48 ? 856 HOH A O   1 
HETATM 2835 O  O   . HOH G 6 .   ? 57.093 26.745  15.013 1.00 33.25 ? 857 HOH A O   1 
HETATM 2836 O  O   . HOH G 6 .   ? 62.563 1.700   49.780 1.00 45.42 ? 858 HOH A O   1 
HETATM 2837 O  O   . HOH G 6 .   ? 39.501 -0.665  48.209 1.00 41.73 ? 859 HOH A O   1 
HETATM 2838 O  O   . HOH G 6 .   ? 34.467 32.536  21.409 1.00 36.05 ? 860 HOH A O   1 
HETATM 2839 O  O   . HOH G 6 .   ? 59.005 5.312   52.447 1.00 42.63 ? 861 HOH A O   1 
HETATM 2840 O  O   . HOH G 6 .   ? 58.235 16.087  23.047 1.00 16.12 ? 862 HOH A O   1 
HETATM 2841 O  O   . HOH G 6 .   ? 71.634 20.700  31.633 1.00 32.97 ? 863 HOH A O   1 
HETATM 2842 O  O   . HOH G 6 .   ? 71.024 19.338  34.138 1.00 40.53 ? 864 HOH A O   1 
HETATM 2843 O  O   . HOH G 6 .   ? 57.040 28.424  16.486 1.00 40.09 ? 865 HOH A O   1 
HETATM 2844 O  O   . HOH G 6 .   ? 35.980 30.551  17.879 1.00 41.50 ? 866 HOH A O   1 
HETATM 2845 O  O   . HOH G 6 .   ? 73.370 22.462  32.863 1.00 33.15 ? 867 HOH A O   1 
HETATM 2846 O  O   . HOH G 6 .   ? 73.916 24.789  31.504 1.00 31.51 ? 868 HOH A O   1 
HETATM 2847 O  O   . HOH G 6 .   ? 73.863 23.964  29.122 1.00 30.97 ? 869 HOH A O   1 
HETATM 2848 O  O   . HOH G 6 .   ? 76.078 25.487  32.609 1.00 40.05 ? 870 HOH A O   1 
HETATM 2849 O  O   . HOH G 6 .   ? 78.557 26.000  31.485 1.00 33.02 ? 871 HOH A 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   . ARG A 75  ? 0.3439 0.4774 0.4408 -0.0523 -0.0090 0.0359  75  ARG A N   
2    C  CA  . ARG A 75  ? 0.3400 0.4695 0.4331 -0.0553 -0.0144 0.0292  75  ARG A CA  
3    C  C   . ARG A 75  ? 0.2276 0.3475 0.3066 -0.0486 -0.0147 0.0277  75  ARG A C   
4    O  O   . ARG A 75  ? 0.2694 0.3953 0.3450 -0.0423 -0.0148 0.0299  75  ARG A O   
5    C  CB  . ARG A 75  ? 0.2544 0.4009 0.3551 -0.0577 -0.0194 0.0273  75  ARG A CB  
6    C  CG  . ARG A 75  ? 0.2381 0.3846 0.3345 -0.0603 -0.0254 0.0199  75  ARG A CG  
7    C  CD  . ARG A 75  ? 0.2556 0.4213 0.3624 -0.0644 -0.0306 0.0179  75  ARG A CD  
8    N  NE  . ARG A 75  ? 0.3166 0.4856 0.4376 -0.0729 -0.0300 0.0176  75  ARG A NE  
9    C  CZ  . ARG A 75  ? 0.3458 0.5291 0.4783 -0.0770 -0.0329 0.0166  75  ARG A CZ  
10   N  NH1 . ARG A 75  ? 0.4086 0.5894 0.5526 -0.0834 -0.0312 0.0158  75  ARG A NH1 
11   N  NH2 . ARG A 75  ? 0.2707 0.4684 0.4021 -0.0730 -0.0368 0.0163  75  ARG A NH2 
12   N  N   . LEU A 76  ? 0.2340 0.3393 0.3062 -0.0500 -0.0146 0.0243  76  LEU A N   
13   C  CA  . LEU A 76  ? 0.1974 0.2935 0.2574 -0.0445 -0.0146 0.0230  76  LEU A CA  
14   C  C   . LEU A 76  ? 0.1562 0.2600 0.2129 -0.0427 -0.0191 0.0204  76  LEU A C   
15   O  O   . LEU A 76  ? 0.1570 0.2693 0.2184 -0.0472 -0.0232 0.0168  76  LEU A O   
16   C  CB  . LEU A 76  ? 0.2831 0.3642 0.3382 -0.0469 -0.0140 0.0197  76  LEU A CB  
17   C  CG  . LEU A 76  ? 0.3009 0.3732 0.3574 -0.0477 -0.0096 0.0230  76  LEU A CG  
18   C  CD1 . LEU A 76  ? 0.3281 0.3864 0.3796 -0.0493 -0.0097 0.0195  76  LEU A CD1 
19   C  CD2 . LEU A 76  ? 0.3709 0.4430 0.4224 -0.0412 -0.0059 0.0278  76  LEU A CD2 
20   N  N   . PRO A 77  ? 0.1673 0.2684 0.2159 -0.0361 -0.0186 0.0223  77  PRO A N   
21   C  CA  . PRO A 77  ? 0.1630 0.2708 0.2073 -0.0339 -0.0224 0.0210  77  PRO A CA  
22   C  C   . PRO A 77  ? 0.1058 0.2079 0.1448 -0.0376 -0.0251 0.0149  77  PRO A C   
23   O  O   . PRO A 77  ? 0.1499 0.2394 0.1863 -0.0398 -0.0232 0.0124  77  PRO A O   
24   C  CB  . PRO A 77  ? 0.1178 0.2206 0.1558 -0.0263 -0.0199 0.0253  77  PRO A CB  
25   C  CG  . PRO A 77  ? 0.1155 0.2050 0.1510 -0.0258 -0.0156 0.0257  77  PRO A CG  
26   C  CD  . PRO A 77  ? 0.1532 0.2460 0.1968 -0.0305 -0.0143 0.0258  77  PRO A CD  
27   N  N   . PRO A 78  ? 0.1269 0.2388 0.1637 -0.0376 -0.0294 0.0125  78  PRO A N   
28   C  CA  . PRO A 78  ? 0.1658 0.2748 0.1983 -0.0416 -0.0322 0.0053  78  PRO A CA  
29   C  C   . PRO A 78  ? 0.1527 0.2489 0.1750 -0.0384 -0.0300 0.0047  78  PRO A C   
30   O  O   . PRO A 78  ? 0.2163 0.3058 0.2355 -0.0415 -0.0306 -0.0013 78  PRO A O   
31   C  CB  . PRO A 78  ? 0.2634 0.3894 0.2955 -0.0413 -0.0374 0.0037  78  PRO A CB  
32   C  CG  . PRO A 78  ? 0.1609 0.2947 0.1937 -0.0349 -0.0364 0.0117  78  PRO A CG  
33   C  CD  . PRO A 78  ? 0.1410 0.2687 0.1802 -0.0342 -0.0320 0.0161  78  PRO A CD  
34   N  N   . TRP A 79  ? 0.1392 0.2314 0.1574 -0.0324 -0.0272 0.0106  79  TRP A N   
35   C  CA  . TRP A 79  ? 0.1608 0.2417 0.1709 -0.0298 -0.0250 0.0105  79  TRP A CA  
36   C  C   . TRP A 79  ? 0.1822 0.2489 0.1929 -0.0318 -0.0217 0.0092  79  TRP A C   
37   O  O   . TRP A 79  ? 0.1812 0.2386 0.1862 -0.0299 -0.0199 0.0090  79  TRP A O   
38   C  CB  . TRP A 79  ? 0.1592 0.2408 0.1662 -0.0233 -0.0233 0.0172  79  TRP A CB  
39   C  CG  . TRP A 79  ? 0.1226 0.2016 0.1345 -0.0207 -0.0204 0.0218  79  TRP A CG  
40   C  CD1 . TRP A 79  ? 0.1170 0.1847 0.1289 -0.0207 -0.0170 0.0220  79  TRP A CD1 
41   C  CD2 . TRP A 79  ? 0.1012 0.1896 0.1180 -0.0171 -0.0205 0.0266  79  TRP A CD2 
42   N  NE1 . TRP A 79  ? 0.1022 0.1716 0.1180 -0.0174 -0.0150 0.0259  79  TRP A NE1 
43   C  CE2 . TRP A 79  ? 0.0983 0.1798 0.1175 -0.0150 -0.0168 0.0288  79  TRP A CE2 
44   C  CE3 . TRP A 79  ? 0.1032 0.2060 0.1225 -0.0149 -0.0234 0.0293  79  TRP A CE3 
45   C  CZ2 . TRP A 79  ? 0.1028 0.1902 0.1271 -0.0107 -0.0154 0.0330  79  TRP A CZ2 
46   C  CZ3 . TRP A 79  ? 0.1020 0.2107 0.1270 -0.0107 -0.0222 0.0343  79  TRP A CZ3 
47   C  CH2 . TRP A 79  ? 0.0993 0.2001 0.1269 -0.0085 -0.0180 0.0358  79  TRP A CH2 
48   N  N   . LEU A 80  ? 0.1340 0.1995 0.1517 -0.0355 -0.0209 0.0087  80  LEU A N   
49   C  CA  . LEU A 80  ? 0.1427 0.1960 0.1613 -0.0374 -0.0180 0.0081  80  LEU A CA  
50   C  C   . LEU A 80  ? 0.1922 0.2421 0.2142 -0.0431 -0.0194 0.0022  80  LEU A C   
51   O  O   . LEU A 80  ? 0.2615 0.3020 0.2861 -0.0451 -0.0170 0.0022  80  LEU A O   
52   C  CB  . LEU A 80  ? 0.1623 0.2158 0.1863 -0.0369 -0.0152 0.0129  80  LEU A CB  
53   C  CG  . LEU A 80  ? 0.2608 0.3141 0.2812 -0.0308 -0.0130 0.0175  80  LEU A CG  
54   C  CD1 . LEU A 80  ? 0.2872 0.3432 0.3127 -0.0301 -0.0102 0.0213  80  LEU A CD1 
55   C  CD2 . LEU A 80  ? 0.2226 0.2648 0.2359 -0.0281 -0.0113 0.0173  80  LEU A CD2 
56   N  N   . LYS A 81  ? 0.1906 0.2479 0.2126 -0.0456 -0.0231 -0.0029 81  LYS A N   
57   C  CA  A LYS A 81  ? 0.2949 0.3493 0.3205 -0.0511 -0.0249 -0.0103 81  LYS A CA  
58   C  CA  B LYS A 81  ? 0.2948 0.3496 0.3204 -0.0512 -0.0251 -0.0103 81  LYS A CA  
59   C  C   . LYS A 81  ? 0.3592 0.4110 0.3762 -0.0496 -0.0262 -0.0159 81  LYS A C   
60   O  O   . LYS A 81  ? 0.3959 0.4533 0.4053 -0.0452 -0.0269 -0.0141 81  LYS A O   
61   C  CB  A LYS A 81  ? 0.3422 0.4092 0.3755 -0.0559 -0.0288 -0.0133 81  LYS A CB  
62   C  CB  B LYS A 81  ? 0.3423 0.4103 0.3751 -0.0557 -0.0291 -0.0134 81  LYS A CB  
63   C  CG  A LYS A 81  ? 0.3446 0.4237 0.3725 -0.0550 -0.0333 -0.0177 81  LYS A CG  
64   C  CG  B LYS A 81  ? 0.3717 0.4490 0.3989 -0.0558 -0.0337 -0.0199 81  LYS A CG  
65   C  CD  A LYS A 81  ? 0.3755 0.4709 0.4105 -0.0577 -0.0372 -0.0177 81  LYS A CD  
66   C  CD  B LYS A 81  ? 0.4054 0.5008 0.4353 -0.0555 -0.0374 -0.0181 81  LYS A CD  
67   C  CE  A LYS A 81  ? 0.3568 0.4654 0.3849 -0.0559 -0.0419 -0.0215 81  LYS A CE  
68   C  CE  B LYS A 81  ? 0.3755 0.4800 0.3950 -0.0510 -0.0401 -0.0190 81  LYS A CE  
69   N  NZ  A LYS A 81  ? 0.3320 0.4589 0.3657 -0.0565 -0.0457 -0.0194 81  LYS A NZ  
70   N  NZ  B LYS A 81  ? 0.3341 0.4309 0.3450 -0.0443 -0.0363 -0.0128 81  LYS A NZ  
71   N  N   . THR A 82  ? 0.3619 0.4049 0.3805 -0.0529 -0.0260 -0.0223 82  THR A N   
72   C  CA  . THR A 82  ? 0.3771 0.4195 0.3883 -0.0519 -0.0274 -0.0293 82  THR A CA  
73   C  C   . THR A 82  ? 0.3802 0.4231 0.3968 -0.0578 -0.0304 -0.0392 82  THR A C   
74   O  O   . THR A 82  ? 0.3763 0.4156 0.4034 -0.0630 -0.0304 -0.0400 82  THR A O   
75   C  CB  . THR A 82  ? 0.3900 0.4196 0.3962 -0.0486 -0.0237 -0.0289 82  THR A CB  
76   O  OG1 . THR A 82  ? 0.4629 0.4803 0.4765 -0.0515 -0.0213 -0.0293 82  THR A OG1 
77   C  CG2 . THR A 82  ? 0.2737 0.3031 0.2743 -0.0430 -0.0212 -0.0206 82  THR A CG2 
78   N  N   . GLU A 83  ? 0.4721 0.5198 0.4816 -0.0570 -0.0327 -0.0467 83  GLU A N   
79   C  CA  . GLU A 83  ? 0.4874 0.5338 0.5005 -0.0620 -0.0354 -0.0583 83  GLU A CA  
80   C  C   . GLU A 83  ? 0.4261 0.4547 0.4428 -0.0629 -0.0318 -0.0613 83  GLU A C   
81   O  O   . GLU A 83  ? 0.4394 0.4593 0.4519 -0.0583 -0.0277 -0.0559 83  GLU A O   
82   C  CB  . GLU A 83  ? 0.5025 0.5598 0.5052 -0.0599 -0.0386 -0.0657 83  GLU A CB  
83   C  CG  . GLU A 83  ? 0.5441 0.6201 0.5469 -0.0615 -0.0438 -0.0665 83  GLU A CG  
84   C  CD  . GLU A 83  ? 0.5957 0.6730 0.6119 -0.0693 -0.0467 -0.0707 83  GLU A CD  
85   O  OE1 . GLU A 83  ? 0.5809 0.6514 0.6017 -0.0738 -0.0479 -0.0808 83  GLU A OE1 
86   O  OE2 . GLU A 83  ? 0.6027 0.6869 0.6254 -0.0704 -0.0473 -0.0633 83  GLU A OE2 
87   N  N   . ILE A 84  ? 0.4194 0.4427 0.4448 -0.0688 -0.0333 -0.0698 84  ILE A N   
88   C  CA  . ILE A 84  ? 0.4247 0.4308 0.4547 -0.0696 -0.0301 -0.0736 84  ILE A CA  
89   C  C   . ILE A 84  ? 0.3804 0.3838 0.3989 -0.0635 -0.0283 -0.0772 84  ILE A C   
90   O  O   . ILE A 84  ? 0.4285 0.4434 0.4373 -0.0613 -0.0308 -0.0822 84  ILE A O   
91   C  CB  . ILE A 84  ? 0.4247 0.4265 0.4656 -0.0769 -0.0326 -0.0844 84  ILE A CB  
92   C  CG1 . ILE A 84  ? 0.3979 0.4100 0.4311 -0.0763 -0.0372 -0.0945 84  ILE A CG1 
93   C  CG2 . ILE A 84  ? 0.4635 0.4682 0.5168 -0.0827 -0.0338 -0.0789 84  ILE A CG2 
94   C  CD1 . ILE A 84  ? 0.4681 0.4712 0.5075 -0.0796 -0.0385 -0.1029 84  ILE A CD1 
95   N  N   . PRO A 85  ? 0.4027 0.3926 0.4217 -0.0602 -0.0238 -0.0740 85  PRO A N   
96   C  CA  . PRO A 85  ? 0.3621 0.3497 0.3716 -0.0546 -0.0217 -0.0778 85  PRO A CA  
97   C  C   . PRO A 85  ? 0.3909 0.3753 0.4013 -0.0567 -0.0232 -0.0922 85  PRO A C   
98   O  O   . PRO A 85  ? 0.3778 0.3516 0.3991 -0.0614 -0.0232 -0.0973 85  PRO A O   
99   C  CB  . PRO A 85  ? 0.3313 0.3054 0.3441 -0.0514 -0.0168 -0.0701 85  PRO A CB  
100  C  CG  . PRO A 85  ? 0.3897 0.3552 0.4155 -0.0566 -0.0164 -0.0672 85  PRO A CG  
101  C  CD  . PRO A 85  ? 0.3830 0.3600 0.4118 -0.0615 -0.0203 -0.0668 85  PRO A CD  
102  N  N   . MET A 86  ? 0.3783 0.3723 0.3773 -0.0532 -0.0244 -0.0987 86  MET A N   
103  C  CA  . MET A 86  ? 0.4773 0.4707 0.4752 -0.0546 -0.0262 -0.1137 86  MET A CA  
104  C  C   . MET A 86  ? 0.4193 0.4150 0.4056 -0.0478 -0.0236 -0.1182 86  MET A C   
105  O  O   . MET A 86  ? 0.4762 0.4717 0.4597 -0.0466 -0.0242 -0.1276 86  MET A O   
106  C  CB  . MET A 86  ? 0.4608 0.4684 0.4565 -0.0576 -0.0318 -0.1174 86  MET A CB  
107  C  CG  . MET A 86  ? 0.4940 0.4995 0.5022 -0.0643 -0.0343 -0.1145 86  MET A CG  
108  S  SD  . MET A 86  ? 0.7702 0.7900 0.7776 -0.0678 -0.0408 -0.1215 86  MET A SD  
109  C  CE  . MET A 86  ? 0.5436 0.5855 0.5386 -0.0638 -0.0431 -0.1152 86  MET A CE  
110  N  N   . GLY A 87  ? 0.3534 0.3510 0.3333 -0.0420 -0.0201 -0.1079 87  GLY A N   
111  C  CA  . GLY A 87  ? 0.4364 0.4391 0.4054 -0.0357 -0.0175 -0.1109 87  GLY A CA  
112  C  C   . GLY A 87  ? 0.4612 0.4506 0.4337 -0.0335 -0.0140 -0.1194 87  GLY A C   
113  O  O   . GLY A 87  ? 0.4109 0.3846 0.3942 -0.0351 -0.0120 -0.1180 87  GLY A O   
114  N  N   . LYS A 88  ? 0.4426 0.4392 0.4054 -0.0292 -0.0131 -0.1282 88  LYS A N   
115  C  CA  . LYS A 88  ? 0.4383 0.4247 0.4022 -0.0250 -0.0089 -0.1355 88  LYS A CA  
116  C  C   . LYS A 88  ? 0.4487 0.4246 0.4174 -0.0209 -0.0038 -0.1249 88  LYS A C   
117  O  O   . LYS A 88  ? 0.3797 0.3403 0.3572 -0.0201 -0.0009 -0.1276 88  LYS A O   
118  C  CB  . LYS A 88  ? 0.4794 0.4799 0.4299 -0.0195 -0.0082 -0.1404 88  LYS A CB  
119  C  CG  . LYS A 88  ? 0.5765 0.5712 0.5253 -0.0138 -0.0038 -0.1472 88  LYS A CG  
120  C  CD  . LYS A 88  ? 0.6115 0.6246 0.5458 -0.0086 -0.0031 -0.1484 88  LYS A CD  
121  C  CE  . LYS A 88  ? 0.6392 0.6500 0.5702 -0.0034 0.0003  -0.1572 88  LYS A CE  
122  N  NZ  . LYS A 88  ? 0.6564 0.6672 0.5871 -0.0063 -0.0036 -0.1680 88  LYS A NZ  
123  N  N   . ASN A 89  ? 0.3559 0.3401 0.3194 -0.0182 -0.0025 -0.1123 89  ASN A N   
124  C  CA  . ASN A 89  ? 0.2638 0.2404 0.2315 -0.0145 0.0018  -0.1019 89  ASN A CA  
125  C  C   . ASN A 89  ? 0.3447 0.3081 0.3243 -0.0183 0.0014  -0.0953 89  ASN A C   
126  O  O   . ASN A 89  ? 0.2916 0.2435 0.2783 -0.0159 0.0047  -0.0925 89  ASN A O   
127  C  CB  . ASN A 89  ? 0.3231 0.3121 0.2834 -0.0117 0.0027  -0.0906 89  ASN A CB  
128  C  CG  . ASN A 89  ? 0.4211 0.4229 0.3704 -0.0066 0.0048  -0.0945 89  ASN A CG  
129  O  OD1 . ASN A 89  ? 0.4771 0.4769 0.4248 -0.0034 0.0071  -0.1043 89  ASN A OD1 
130  N  ND2 . ASN A 89  ? 0.3726 0.3877 0.3146 -0.0055 0.0043  -0.0865 89  ASN A ND2 
131  N  N   . TYR A 90  ? 0.3357 0.3020 0.3175 -0.0237 -0.0024 -0.0918 90  TYR A N   
132  C  CA  . TYR A 90  ? 0.3065 0.2617 0.2994 -0.0276 -0.0027 -0.0860 90  TYR A CA  
133  C  C   . TYR A 90  ? 0.3464 0.2869 0.3491 -0.0293 -0.0016 -0.0942 90  TYR A C   
134  O  O   . TYR A 90  ? 0.3061 0.2345 0.3175 -0.0285 0.0010  -0.0886 90  TYR A O   
135  C  CB  . TYR A 90  ? 0.3324 0.2948 0.3262 -0.0333 -0.0070 -0.0832 90  TYR A CB  
136  C  CG  . TYR A 90  ? 0.2622 0.2143 0.2682 -0.0383 -0.0074 -0.0798 90  TYR A CG  
137  C  CD1 . TYR A 90  ? 0.2964 0.2417 0.3073 -0.0370 -0.0049 -0.0688 90  TYR A CD1 
138  C  CD2 . TYR A 90  ? 0.3638 0.3136 0.3765 -0.0443 -0.0104 -0.0878 90  TYR A CD2 
139  C  CE1 . TYR A 90  ? 0.2958 0.2328 0.3176 -0.0411 -0.0048 -0.0646 90  TYR A CE1 
140  C  CE2 . TYR A 90  ? 0.4104 0.3513 0.4353 -0.0491 -0.0103 -0.0837 90  TYR A CE2 
141  C  CZ  . TYR A 90  ? 0.4528 0.3875 0.4818 -0.0473 -0.0073 -0.0718 90  TYR A CZ  
142  O  OH  . TYR A 90  ? 0.4113 0.3383 0.4519 -0.0517 -0.0068 -0.0669 90  TYR A OH  
143  N  N   . ASN A 91  ? 0.2912 0.2326 0.2930 -0.0315 -0.0037 -0.1076 91  ASN A N   
144  C  CA  . ASN A 91  ? 0.3574 0.2835 0.3701 -0.0338 -0.0028 -0.1162 91  ASN A CA  
145  C  C   . ASN A 91  ? 0.3716 0.2869 0.3868 -0.0272 0.0023  -0.1163 91  ASN A C   
146  O  O   . ASN A 91  ? 0.3128 0.2131 0.3396 -0.0276 0.0046  -0.1138 91  ASN A O   
147  C  CB  . ASN A 91  ? 0.3710 0.3023 0.3803 -0.0363 -0.0064 -0.1283 91  ASN A CB  
148  C  CG  . ASN A 91  ? 0.5450 0.4621 0.5654 -0.0392 -0.0065 -0.1317 91  ASN A CG  
149  O  OD1 . ASN A 91  ? 0.6094 0.5206 0.6399 -0.0444 -0.0077 -0.1259 91  ASN A OD1 
150  N  ND2 . ASN A 91  ? 0.6134 0.5253 0.6324 -0.0356 -0.0049 -0.1406 91  ASN A ND2 
151  N  N   . LYS A 92  ? 0.3470 0.2708 0.3520 -0.0209 0.0045  -0.1179 92  LYS A N   
152  C  CA  . LYS A 92  ? 0.3121 0.2278 0.3193 -0.0141 0.0096  -0.1180 92  LYS A CA  
153  C  C   . LYS A 92  ? 0.3410 0.2508 0.3547 -0.0120 0.0120  -0.1032 92  LYS A C   
154  O  O   . LYS A 92  ? 0.3195 0.2160 0.3426 -0.0094 0.0151  -0.1020 92  LYS A O   
155  C  CB  . LYS A 92  ? 0.3476 0.2764 0.3424 -0.0080 0.0115  -0.1218 92  LYS A CB  
156  C  CG  . LYS A 92  ? 0.5199 0.4414 0.5174 -0.0008 0.0167  -0.1259 92  LYS A CG  
157  C  CD  . LYS A 92  ? 0.5138 0.4486 0.4993 0.0048  0.0187  -0.1333 92  LYS A CD  
158  C  CE  . LYS A 92  ? 0.6380 0.5654 0.6276 0.0124  0.0243  -0.1370 92  LYS A CE  
159  N  NZ  . LYS A 92  ? 0.6401 0.5815 0.6185 0.0189  0.0274  -0.1424 92  LYS A NZ  
160  N  N   . LEU A 93  ? 0.2834 0.2028 0.2924 -0.0130 0.0106  -0.0918 93  LEU A N   
161  C  CA  . LEU A 93  ? 0.2461 0.1611 0.2607 -0.0116 0.0123  -0.0784 93  LEU A CA  
162  C  C   . LEU A 93  ? 0.2606 0.1626 0.2872 -0.0158 0.0118  -0.0754 93  LEU A C   
163  O  O   . LEU A 93  ? 0.2668 0.1597 0.3012 -0.0130 0.0146  -0.0688 93  LEU A O   
164  C  CB  . LEU A 93  ? 0.2397 0.1671 0.2474 -0.0127 0.0104  -0.0688 93  LEU A CB  
165  C  CG  . LEU A 93  ? 0.3331 0.2721 0.3313 -0.0079 0.0119  -0.0674 93  LEU A CG  
166  C  CD1 . LEU A 93  ? 0.3087 0.2600 0.2997 -0.0105 0.0091  -0.0621 93  LEU A CD1 
167  C  CD2 . LEU A 93  ? 0.2960 0.2322 0.2982 -0.0030 0.0152  -0.0593 93  LEU A CD2 
168  N  N   . LYS A 94  ? 0.2823 0.1844 0.3111 -0.0225 0.0085  -0.0795 94  LYS A N   
169  C  CA  . LYS A 94  ? 0.2959 0.1868 0.3368 -0.0272 0.0082  -0.0761 94  LYS A CA  
170  C  C   . LYS A 94  ? 0.3511 0.2257 0.4026 -0.0256 0.0112  -0.0820 94  LYS A C   
171  O  O   . LYS A 94  ? 0.3283 0.1927 0.3895 -0.0250 0.0134  -0.0736 94  LYS A O   
172  C  CB  . LYS A 94  ? 0.3171 0.2130 0.3587 -0.0348 0.0040  -0.0809 94  LYS A CB  
173  C  CG  . LYS A 94  ? 0.4335 0.3200 0.4883 -0.0406 0.0037  -0.0765 94  LYS A CG  
174  C  CD  . LYS A 94  ? 0.4418 0.3329 0.4966 -0.0409 0.0040  -0.0619 94  LYS A CD  
175  C  CE  . LYS A 94  ? 0.4768 0.3660 0.5415 -0.0481 0.0025  -0.0588 94  LYS A CE  
176  N  NZ  . LYS A 94  ? 0.5641 0.4551 0.6307 -0.0474 0.0041  -0.0442 94  LYS A NZ  
177  N  N   . ASN A 95  ? 0.3276 0.2012 0.3762 -0.0241 0.0111  -0.0948 95  ASN A N   
178  C  CA  . ASN A 95  ? 0.3889 0.2501 0.4447 -0.0214 0.0133  -0.0976 95  ASN A CA  
179  C  C   . ASN A 95  ? 0.4099 0.2646 0.4694 -0.0139 0.0180  -0.0905 95  ASN A C   
180  O  O   . ASN A 95  ? 0.4175 0.2617 0.4865 -0.0127 0.0199  -0.0834 95  ASN A O   
181  C  CB  . ASN A 95  ? 0.4187 0.2822 0.4685 -0.0205 0.0121  -0.1121 95  ASN A CB  
182  C  CG  . ASN A 95  ? 0.5818 0.4484 0.6319 -0.0281 0.0074  -0.1185 95  ASN A CG  
183  O  OD1 . ASN A 95  ? 0.5901 0.4515 0.6490 -0.0336 0.0060  -0.1129 95  ASN A OD1 
184  N  ND2 . ASN A 95  ? 0.6584 0.5346 0.6988 -0.0283 0.0050  -0.1299 95  ASN A ND2 
185  N  N   . THR A 96  ? 0.3580 0.2204 0.4102 -0.0086 0.0200  -0.0914 96  THR A N   
186  C  CA  . THR A 96  ? 0.3386 0.1982 0.3936 -0.0010 0.0241  -0.0837 96  THR A CA  
187  C  C   . THR A 96  ? 0.3684 0.2247 0.4301 -0.0016 0.0245  -0.0681 96  THR A C   
188  O  O   . THR A 96  ? 0.3549 0.2019 0.4256 0.0030  0.0276  -0.0623 96  THR A O   
189  C  CB  . THR A 96  ? 0.3762 0.2512 0.4189 0.0039  0.0248  -0.0828 96  THR A CB  
190  O  OG1 . THR A 96  ? 0.3842 0.2634 0.4200 0.0051  0.0249  -0.0969 96  THR A OG1 
191  C  CG2 . THR A 96  ? 0.3350 0.2090 0.3813 0.0117  0.0287  -0.0752 96  THR A CG2 
192  N  N   . LEU A 97  ? 0.3632 0.2279 0.4206 -0.0066 0.0213  -0.0611 97  LEU A N   
193  C  CA  . LEU A 97  ? 0.2549 0.1189 0.3171 -0.0070 0.0215  -0.0468 97  LEU A CA  
194  C  C   . LEU A 97  ? 0.3530 0.2018 0.4290 -0.0090 0.0231  -0.0438 97  LEU A C   
195  O  O   . LEU A 97  ? 0.3104 0.1570 0.3914 -0.0063 0.0246  -0.0319 97  LEU A O   
196  C  CB  . LEU A 97  ? 0.2507 0.1260 0.3060 -0.0123 0.0179  -0.0420 97  LEU A CB  
197  C  CG  . LEU A 97  ? 0.3510 0.2278 0.4093 -0.0131 0.0178  -0.0282 97  LEU A CG  
198  C  CD1 . LEU A 97  ? 0.2937 0.1753 0.3495 -0.0067 0.0194  -0.0195 97  LEU A CD1 
199  C  CD2 . LEU A 97  ? 0.2796 0.1668 0.3316 -0.0185 0.0144  -0.0262 97  LEU A CD2 
200  N  N   . ARG A 98  ? 0.3643 0.2084 0.4427 -0.0133 0.0215  -0.0521 98  ARG A N   
201  C  CA  . ARG A 98  ? 0.4843 0.3204 0.5721 -0.0160 0.0216  -0.0459 98  ARG A CA  
202  C  C   . ARG A 98  ? 0.4318 0.2585 0.5266 -0.0096 0.0251  -0.0415 98  ARG A C   
203  O  O   . ARG A 98  ? 0.4750 0.2971 0.5773 -0.0099 0.0262  -0.0314 98  ARG A O   
204  C  CB  . ARG A 98  ? 0.4952 0.3284 0.5850 -0.0225 0.0190  -0.0558 98  ARG A CB  
205  C  CG  . ARG A 98  ? 0.5747 0.3999 0.6750 -0.0260 0.0195  -0.0494 98  ARG A CG  
206  C  CD  . ARG A 98  ? 0.6777 0.4998 0.7806 -0.0321 0.0170  -0.0602 98  ARG A CD  
207  N  NE  . ARG A 98  ? 0.6904 0.5150 0.7857 -0.0308 0.0156  -0.0747 98  ARG A NE  
208  C  CZ  . ARG A 98  ? 0.6539 0.4884 0.7417 -0.0350 0.0120  -0.0829 98  ARG A CZ  
209  N  NH1 . ARG A 98  ? 0.6593 0.4978 0.7392 -0.0328 0.0110  -0.0953 98  ARG A NH1 
210  N  NH2 . ARG A 98  ? 0.5504 0.3921 0.6386 -0.0411 0.0093  -0.0781 98  ARG A NH2 
211  N  N   . ASN A 99  ? 0.3885 0.2136 0.4811 -0.0035 0.0271  -0.0483 99  ASN A N   
212  C  CA  . ASN A 99  ? 0.4777 0.2951 0.5771 0.0034  0.0305  -0.0438 99  ASN A CA  
213  C  C   . ASN A 99  ? 0.4247 0.2481 0.5231 0.0098  0.0324  -0.0328 99  ASN A C   
214  O  O   . ASN A 99  ? 0.4782 0.2975 0.5819 0.0163  0.0350  -0.0284 99  ASN A O   
215  C  CB  . ASN A 99  ? 0.4592 0.2713 0.5578 0.0071  0.0319  -0.0570 99  ASN A CB  
216  C  CG  . ASN A 99  ? 0.5566 0.3585 0.6608 0.0023  0.0308  -0.0646 99  ASN A CG  
217  O  OD1 . ASN A 99  ? 0.4647 0.2647 0.5731 -0.0044 0.0289  -0.0606 99  ASN A OD1 
218  N  ND2 . ASN A 99  ? 0.3810 0.1768 0.4853 0.0057  0.0322  -0.0756 99  ASN A ND2 
219  N  N   . LEU A 100 ? 0.4045 0.2378 0.4967 0.0083  0.0310  -0.0281 100 LEU A N   
220  C  CA  . LEU A 100 ? 0.3751 0.2151 0.4667 0.0136  0.0322  -0.0168 100 LEU A CA  
221  C  C   . LEU A 100 ? 0.4310 0.2730 0.5255 0.0111  0.0311  -0.0032 100 LEU A C   
222  O  O   . LEU A 100 ? 0.5288 0.3690 0.6244 0.0045  0.0294  -0.0028 100 LEU A O   
223  C  CB  . LEU A 100 ? 0.3667 0.2197 0.4474 0.0135  0.0307  -0.0190 100 LEU A CB  
224  C  CG  . LEU A 100 ? 0.4374 0.2949 0.5111 0.0159  0.0312  -0.0313 100 LEU A CG  
225  C  CD1 . LEU A 100 ? 0.4324 0.3064 0.4936 0.0137  0.0284  -0.0304 100 LEU A CD1 
226  C  CD2 . LEU A 100 ? 0.4922 0.3478 0.5702 0.0246  0.0350  -0.0313 100 LEU A CD2 
227  N  N   . ASN A 101 ? 0.4774 0.3248 0.5726 0.0165  0.0320  0.0079  101 ASN A N   
228  C  CA  . ASN A 101 ? 0.4974 0.3499 0.5933 0.0151  0.0310  0.0211  101 ASN A CA  
229  C  C   . ASN A 101 ? 0.5121 0.3759 0.5999 0.0139  0.0290  0.0247  101 ASN A C   
230  O  O   . ASN A 101 ? 0.5306 0.4035 0.6152 0.0189  0.0287  0.0305  101 ASN A O   
231  C  CB  . ASN A 101 ? 0.5747 0.4273 0.6763 0.0216  0.0328  0.0310  101 ASN A CB  
232  C  CG  . ASN A 101 ? 0.5675 0.4273 0.6686 0.0208  0.0319  0.0441  101 ASN A CG  
233  O  OD1 . ASN A 101 ? 0.6600 0.5215 0.7589 0.0148  0.0305  0.0456  101 ASN A OD1 
234  N  ND2 . ASN A 101 ? 0.6469 0.5125 0.7499 0.0271  0.0326  0.0535  101 ASN A ND2 
235  N  N   . LEU A 102 ? 0.4125 0.2786 0.4955 0.0070  0.0268  0.0208  102 LEU A N   
236  C  CA  . LEU A 102 ? 0.3955 0.2762 0.4667 0.0050  0.0237  0.0208  102 LEU A CA  
237  C  C   . LEU A 102 ? 0.3329 0.2148 0.4019 -0.0025 0.0217  0.0193  102 LEU A C   
238  O  O   . LEU A 102 ? 0.4319 0.3071 0.5036 -0.0067 0.0216  0.0108  102 LEU A O   
239  C  CB  . LEU A 102 ? 0.3381 0.2241 0.4022 0.0067  0.0230  0.0110  102 LEU A CB  
240  C  CG  . LEU A 102 ? 0.3360 0.2363 0.3892 0.0058  0.0203  0.0112  102 LEU A CG  
241  C  CD1 . LEU A 102 ? 0.3659 0.2740 0.4187 0.0100  0.0200  0.0211  102 LEU A CD1 
242  C  CD2 . LEU A 102 ? 0.3054 0.2095 0.3531 0.0070  0.0204  0.0017  102 LEU A CD2 
243  N  N   . HIS A 103 ? 0.2969 0.1879 0.3614 -0.0039 0.0202  0.0272  103 HIS A N   
244  C  CA  . HIS A 103 ? 0.3655 0.2605 0.4270 -0.0102 0.0183  0.0262  103 HIS A CA  
245  C  C   . HIS A 103 ? 0.2838 0.1906 0.3339 -0.0109 0.0155  0.0224  103 HIS A C   
246  O  O   . HIS A 103 ? 0.2990 0.2133 0.3439 -0.0071 0.0148  0.0252  103 HIS A O   
247  C  CB  . HIS A 103 ? 0.3540 0.2513 0.4186 -0.0110 0.0191  0.0376  103 HIS A CB  
248  C  CG  . HIS A 103 ? 0.4207 0.3083 0.4957 -0.0110 0.0217  0.0422  103 HIS A CG  
249  N  ND1 . HIS A 103 ? 0.5649 0.4533 0.6425 -0.0057 0.0232  0.0509  103 HIS A ND1 
250  C  CD2 . HIS A 103 ? 0.5665 0.4472 0.6478 -0.0155 0.0221  0.0381  103 HIS A CD2 
251  C  CE1 . HIS A 103 ? 0.5240 0.4053 0.6094 -0.0068 0.0249  0.0524  103 HIS A CE1 
252  N  NE2 . HIS A 103 ? 0.6226 0.4989 0.7105 -0.0129 0.0242  0.0447  103 HIS A NE2 
253  N  N   . THR A 104 ? 0.2505 0.1596 0.2978 -0.0161 0.0137  0.0166  104 THR A N   
254  C  CA  . THR A 104 ? 0.2275 0.1472 0.2651 -0.0168 0.0113  0.0138  104 THR A CA  
255  C  C   . THR A 104 ? 0.2234 0.1489 0.2593 -0.0206 0.0100  0.0177  104 THR A C   
256  O  O   . THR A 104 ? 0.2256 0.1474 0.2676 -0.0244 0.0105  0.0189  104 THR A O   
257  C  CB  . THR A 104 ? 0.1974 0.1174 0.2314 -0.0184 0.0101  0.0034  104 THR A CB  
258  O  OG1 . THR A 104 ? 0.2350 0.1510 0.2733 -0.0236 0.0094  -0.0011 104 THR A OG1 
259  C  CG2 . THR A 104 ? 0.2684 0.1832 0.3038 -0.0143 0.0119  -0.0013 104 THR A CG2 
260  N  N   . VAL A 105 ? 0.1803 0.1151 0.2086 -0.0194 0.0085  0.0196  105 VAL A N   
261  C  CA  . VAL A 105 ? 0.1770 0.1184 0.2026 -0.0224 0.0072  0.0216  105 VAL A CA  
262  C  C   . VAL A 105 ? 0.1850 0.1266 0.2110 -0.0267 0.0058  0.0148  105 VAL A C   
263  O  O   . VAL A 105 ? 0.2208 0.1648 0.2495 -0.0303 0.0055  0.0162  105 VAL A O   
264  C  CB  . VAL A 105 ? 0.1924 0.1425 0.2102 -0.0200 0.0058  0.0233  105 VAL A CB  
265  C  CG1 . VAL A 105 ? 0.2390 0.1956 0.2540 -0.0225 0.0047  0.0240  105 VAL A CG1 
266  C  CG2 . VAL A 105 ? 0.1628 0.1148 0.1803 -0.0162 0.0066  0.0299  105 VAL A CG2 
267  N  N   . CYS A 106 ? 0.1882 0.1287 0.2116 -0.0263 0.0050  0.0074  106 CYS A N   
268  C  CA  . CYS A 106 ? 0.1720 0.1146 0.1947 -0.0299 0.0032  0.0003  106 CYS A CA  
269  C  C   . CYS A 106 ? 0.2119 0.1494 0.2431 -0.0345 0.0034  -0.0008 106 CYS A C   
270  O  O   . CYS A 106 ? 0.2426 0.1850 0.2749 -0.0385 0.0017  -0.0022 106 CYS A O   
271  C  CB  . CYS A 106 ? 0.1471 0.0880 0.1666 -0.0281 0.0031  -0.0073 106 CYS A CB  
272  S  SG  . CYS A 106 ? 0.1618 0.1073 0.1742 -0.0226 0.0039  -0.0049 106 CYS A SG  
273  N  N   . GLU A 107 ? 0.1908 0.1185 0.2292 -0.0341 0.0055  0.0001  107 GLU A N   
274  C  CA  . GLU A 107 ? 0.2427 0.1639 0.2914 -0.0389 0.0061  -0.0006 107 GLU A CA  
275  C  C   . GLU A 107 ? 0.2965 0.2195 0.3500 -0.0404 0.0075  0.0094  107 GLU A C   
276  O  O   . GLU A 107 ? 0.2769 0.2018 0.3363 -0.0455 0.0070  0.0096  107 GLU A O   
277  C  CB  . GLU A 107 ? 0.2529 0.1616 0.3086 -0.0376 0.0081  -0.0037 107 GLU A CB  
278  C  CG  . GLU A 107 ? 0.3308 0.2378 0.3821 -0.0360 0.0072  -0.0143 107 GLU A CG  
279  C  CD  . GLU A 107 ? 0.4881 0.3831 0.5456 -0.0328 0.0100  -0.0163 107 GLU A CD  
280  O  OE1 . GLU A 107 ? 0.4946 0.3875 0.5527 -0.0279 0.0122  -0.0086 107 GLU A OE1 
281  O  OE2 . GLU A 107 ? 0.4457 0.3336 0.5078 -0.0351 0.0097  -0.0258 107 GLU A OE2 
282  N  N   . GLU A 108 ? 0.2882 0.2119 0.3395 -0.0360 0.0093  0.0177  108 GLU A N   
283  C  CA  . GLU A 108 ? 0.3523 0.2782 0.4078 -0.0367 0.0112  0.0277  108 GLU A CA  
284  C  C   . GLU A 108 ? 0.3697 0.3067 0.4214 -0.0390 0.0099  0.0290  108 GLU A C   
285  O  O   . GLU A 108 ? 0.3251 0.2642 0.3832 -0.0424 0.0111  0.0337  108 GLU A O   
286  C  CB  . GLU A 108 ? 0.3556 0.2820 0.4079 -0.0308 0.0129  0.0355  108 GLU A CB  
287  C  CG  . GLU A 108 ? 0.4101 0.3253 0.4695 -0.0284 0.0150  0.0367  108 GLU A CG  
288  C  CD  . GLU A 108 ? 0.5656 0.4723 0.6368 -0.0325 0.0168  0.0381  108 GLU A CD  
289  O  OE1 . GLU A 108 ? 0.5658 0.4776 0.6387 -0.0343 0.0177  0.0446  108 GLU A OE1 
290  O  OE2 . GLU A 108 ? 0.5987 0.4959 0.6748 -0.0332 0.0170  0.0312  108 GLU A OE2 
291  N  N   . ALA A 109 ? 0.2477 0.1919 0.2899 -0.0371 0.0076  0.0251  109 ALA A N   
292  C  CA  . ALA A 109 ? 0.2491 0.2034 0.2875 -0.0384 0.0064  0.0257  109 ALA A CA  
293  C  C   . ALA A 109 ? 0.2628 0.2195 0.3042 -0.0432 0.0042  0.0191  109 ALA A C   
294  O  O   . ALA A 109 ? 0.3562 0.3219 0.3950 -0.0440 0.0030  0.0192  109 ALA A O   
295  C  CB  . ALA A 109 ? 0.3586 0.3187 0.3866 -0.0341 0.0051  0.0249  109 ALA A CB  
296  N  N   . ARG A 110 ? 0.2473 0.1969 0.2940 -0.0461 0.0036  0.0129  110 ARG A N   
297  C  CA  . ARG A 110 ? 0.2441 0.1969 0.2933 -0.0507 0.0009  0.0055  110 ARG A CA  
298  C  C   . ARG A 110 ? 0.3084 0.2707 0.3480 -0.0486 -0.0017 0.0021  110 ARG A C   
299  O  O   . ARG A 110 ? 0.2593 0.2306 0.2990 -0.0506 -0.0034 0.0020  110 ARG A O   
300  C  CB  . ARG A 110 ? 0.2687 0.2255 0.3275 -0.0560 0.0012  0.0089  110 ARG A CB  
301  C  CG  . ARG A 110 ? 0.3394 0.2883 0.4083 -0.0577 0.0046  0.0158  110 ARG A CG  
302  C  CD  . ARG A 110 ? 0.3627 0.3192 0.4389 -0.0616 0.0057  0.0222  110 ARG A CD  
303  N  NE  . ARG A 110 ? 0.4204 0.3705 0.5064 -0.0631 0.0094  0.0301  110 ARG A NE  
304  C  CZ  . ARG A 110 ? 0.4130 0.3556 0.5065 -0.0666 0.0098  0.0270  110 ARG A CZ  
305  N  NH1 . ARG A 110 ? 0.4076 0.3458 0.5056 -0.0659 0.0131  0.0340  110 ARG A NH1 
306  N  NH2 . ARG A 110 ? 0.4491 0.3890 0.5454 -0.0707 0.0066  0.0164  110 ARG A NH2 
307  N  N   . CYS A 111 ? 0.2243 0.1850 0.2560 -0.0441 -0.0017 0.0002  111 CYS A N   
308  C  CA  . CYS A 111 ? 0.1931 0.1622 0.2163 -0.0416 -0.0034 -0.0006 111 CYS A CA  
309  C  C   . CYS A 111 ? 0.1855 0.1599 0.2074 -0.0441 -0.0064 -0.0080 111 CYS A C   
310  O  O   . CYS A 111 ? 0.2217 0.1918 0.2447 -0.0455 -0.0071 -0.0148 111 CYS A O   
311  C  CB  . CYS A 111 ? 0.1919 0.1585 0.2081 -0.0367 -0.0025 -0.0002 111 CYS A CB  
312  S  SG  . CYS A 111 ? 0.1714 0.1471 0.1787 -0.0338 -0.0040 0.0002  111 CYS A SG  
313  N  N   . PRO A 112 ? 0.1922 0.1766 0.2114 -0.0442 -0.0083 -0.0070 112 PRO A N   
314  C  CA  . PRO A 112 ? 0.2094 0.2011 0.2271 -0.0462 -0.0115 -0.0134 112 PRO A CA  
315  C  C   . PRO A 112 ? 0.1976 0.1902 0.2068 -0.0429 -0.0120 -0.0174 112 PRO A C   
316  O  O   . PRO A 112 ? 0.2076 0.2064 0.2144 -0.0441 -0.0146 -0.0233 112 PRO A O   
317  C  CB  . PRO A 112 ? 0.2260 0.2285 0.2436 -0.0461 -0.0128 -0.0092 112 PRO A CB  
318  C  CG  . PRO A 112 ? 0.3135 0.3138 0.3294 -0.0426 -0.0101 -0.0018 112 PRO A CG  
319  C  CD  . PRO A 112 ? 0.1788 0.1687 0.1972 -0.0425 -0.0075 -0.0002 112 PRO A CD  
320  N  N   . ASN A 113 ? 0.1633 0.1512 0.1680 -0.0387 -0.0097 -0.0144 113 ASN A N   
321  C  CA  . ASN A 113 ? 0.1763 0.1668 0.1734 -0.0354 -0.0098 -0.0168 113 ASN A CA  
322  C  C   . ASN A 113 ? 0.1690 0.1530 0.1656 -0.0348 -0.0087 -0.0229 113 ASN A C   
323  O  O   . ASN A 113 ? 0.1498 0.1367 0.1402 -0.0319 -0.0082 -0.0250 113 ASN A O   
324  C  CB  . ASN A 113 ? 0.1602 0.1507 0.1534 -0.0314 -0.0080 -0.0103 113 ASN A CB  
325  C  CG  . ASN A 113 ? 0.1682 0.1648 0.1615 -0.0311 -0.0088 -0.0051 113 ASN A CG  
326  O  OD1 . ASN A 113 ? 0.1817 0.1861 0.1745 -0.0321 -0.0110 -0.0061 113 ASN A OD1 
327  N  ND2 . ASN A 113 ? 0.1515 0.1451 0.1454 -0.0293 -0.0072 0.0002  113 ASN A ND2 
328  N  N   . ILE A 114 ? 0.1663 0.1421 0.1698 -0.0375 -0.0081 -0.0260 114 ILE A N   
329  C  CA  . ILE A 114 ? 0.1823 0.1498 0.1863 -0.0358 -0.0062 -0.0306 114 ILE A CA  
330  C  C   . ILE A 114 ? 0.2015 0.1737 0.1998 -0.0350 -0.0074 -0.0394 114 ILE A C   
331  O  O   . ILE A 114 ? 0.2087 0.1791 0.2030 -0.0312 -0.0054 -0.0415 114 ILE A O   
332  C  CB  . ILE A 114 ? 0.1795 0.1364 0.1934 -0.0388 -0.0051 -0.0315 114 ILE A CB  
333  C  CG1 . ILE A 114 ? 0.2310 0.1781 0.2466 -0.0358 -0.0024 -0.0344 114 ILE A CG1 
334  C  CG2 . ILE A 114 ? 0.2120 0.1705 0.2308 -0.0443 -0.0078 -0.0385 114 ILE A CG2 
335  C  CD1 . ILE A 114 ? 0.2868 0.2227 0.3126 -0.0373 -0.0005 -0.0312 114 ILE A CD1 
336  N  N   . GLY A 115 ? 0.1874 0.1673 0.1847 -0.0382 -0.0106 -0.0444 115 GLY A N   
337  C  CA  . GLY A 115 ? 0.2482 0.2346 0.2390 -0.0373 -0.0121 -0.0531 115 GLY A CA  
338  C  C   . GLY A 115 ? 0.2611 0.2560 0.2421 -0.0324 -0.0111 -0.0495 115 GLY A C   
339  O  O   . GLY A 115 ? 0.3134 0.3118 0.2882 -0.0297 -0.0104 -0.0552 115 GLY A O   
340  N  N   . GLU A 116 ? 0.1885 0.1869 0.1684 -0.0310 -0.0107 -0.0401 116 GLU A N   
341  C  CA  . GLU A 116 ? 0.2149 0.2203 0.1874 -0.0268 -0.0094 -0.0353 116 GLU A CA  
342  C  C   . GLU A 116 ? 0.1890 0.1873 0.1620 -0.0234 -0.0057 -0.0320 116 GLU A C   
343  O  O   . GLU A 116 ? 0.2009 0.2027 0.1687 -0.0201 -0.0038 -0.0330 116 GLU A O   
344  C  CB  . GLU A 116 ? 0.2522 0.2636 0.2247 -0.0269 -0.0107 -0.0272 116 GLU A CB  
345  C  CG  . GLU A 116 ? 0.3945 0.4143 0.3605 -0.0232 -0.0099 -0.0221 116 GLU A CG  
346  C  CD  . GLU A 116 ? 0.3757 0.4079 0.3352 -0.0226 -0.0122 -0.0260 116 GLU A CD  
347  O  OE1 . GLU A 116 ? 0.5374 0.5736 0.4982 -0.0258 -0.0155 -0.0313 116 GLU A OE1 
348  O  OE2 . GLU A 116 ? 0.4970 0.5357 0.4502 -0.0191 -0.0107 -0.0234 116 GLU A OE2 
349  N  N   . CYS A 117 ? 0.1563 0.1456 0.1355 -0.0241 -0.0045 -0.0280 117 CYS A N   
350  C  CA  . CYS A 117 ? 0.1609 0.1450 0.1410 -0.0209 -0.0014 -0.0245 117 CYS A CA  
351  C  C   . CYS A 117 ? 0.1750 0.1543 0.1555 -0.0189 0.0006  -0.0309 117 CYS A C   
352  O  O   . CYS A 117 ? 0.1636 0.1439 0.1424 -0.0153 0.0031  -0.0296 117 CYS A O   
353  C  CB  . CYS A 117 ? 0.1521 0.1293 0.1382 -0.0217 -0.0010 -0.0187 117 CYS A CB  
354  S  SG  . CYS A 117 ? 0.1535 0.1363 0.1386 -0.0227 -0.0025 -0.0114 117 CYS A SG  
355  N  N   . TRP A 118 ? 0.1690 0.1427 0.1533 -0.0213 -0.0002 -0.0378 118 TRP A N   
356  C  CA  . TRP A 118 ? 0.1730 0.1406 0.1589 -0.0192 0.0019  -0.0449 118 TRP A CA  
357  C  C   . TRP A 118 ? 0.1837 0.1595 0.1621 -0.0179 0.0014  -0.0533 118 TRP A C   
358  O  O   . TRP A 118 ? 0.2575 0.2319 0.2363 -0.0201 -0.0001 -0.0626 118 TRP A O   
359  C  CB  . TRP A 118 ? 0.1842 0.1406 0.1789 -0.0224 0.0015  -0.0484 118 TRP A CB  
360  C  CG  . TRP A 118 ? 0.1642 0.1132 0.1659 -0.0227 0.0026  -0.0400 118 TRP A CG  
361  C  CD1 . TRP A 118 ? 0.1612 0.1135 0.1617 -0.0216 0.0028  -0.0306 118 TRP A CD1 
362  C  CD2 . TRP A 118 ? 0.1907 0.1280 0.2016 -0.0241 0.0037  -0.0402 118 TRP A CD2 
363  N  NE1 . TRP A 118 ? 0.1912 0.1359 0.1987 -0.0220 0.0038  -0.0251 118 TRP A NE1 
364  C  CE2 . TRP A 118 ? 0.1942 0.1296 0.2084 -0.0234 0.0046  -0.0301 118 TRP A CE2 
365  C  CE3 . TRP A 118 ? 0.2386 0.1668 0.2558 -0.0258 0.0042  -0.0479 118 TRP A CE3 
366  C  CZ2 . TRP A 118 ? 0.2053 0.1309 0.2285 -0.0241 0.0061  -0.0263 118 TRP A CZ2 
367  C  CZ3 . TRP A 118 ? 0.2360 0.1530 0.2632 -0.0268 0.0057  -0.0443 118 TRP A CZ3 
368  C  CH2 . TRP A 118 ? 0.2170 0.1332 0.2470 -0.0258 0.0068  -0.0330 118 TRP A CH2 
369  N  N   . GLY A 119 ? 0.1799 0.1649 0.1513 -0.0145 0.0028  -0.0498 119 GLY A N   
370  C  CA  . GLY A 119 ? 0.2037 0.1977 0.1671 -0.0120 0.0033  -0.0564 119 GLY A CA  
371  C  C   . GLY A 119 ? 0.2269 0.2327 0.1836 -0.0140 -0.0001 -0.0581 119 GLY A C   
372  O  O   . GLY A 119 ? 0.2577 0.2724 0.2070 -0.0119 0.0000  -0.0643 119 GLY A O   
373  N  N   . GLY A 120 ? 0.2293 0.2368 0.1881 -0.0172 -0.0029 -0.0523 120 GLY A N   
374  C  CA  . GLY A 120 ? 0.2517 0.2709 0.2052 -0.0189 -0.0064 -0.0539 120 GLY A CA  
375  C  C   . GLY A 120 ? 0.2506 0.2818 0.1974 -0.0159 -0.0059 -0.0459 120 GLY A C   
376  O  O   . GLY A 120 ? 0.3349 0.3776 0.2767 -0.0164 -0.0088 -0.0464 120 GLY A O   
377  N  N   . GLY A 121 ? 0.2439 0.2732 0.1909 -0.0129 -0.0024 -0.0382 121 GLY A N   
378  C  CA  . GLY A 121 ? 0.3311 0.3697 0.2742 -0.0107 -0.0016 -0.0291 121 GLY A CA  
379  C  C   . GLY A 121 ? 0.3088 0.3582 0.2437 -0.0067 0.0008  -0.0299 121 GLY A C   
380  O  O   . GLY A 121 ? 0.2741 0.3249 0.2054 -0.0052 0.0018  -0.0385 121 GLY A O   
381  N  N   . GLU A 122 ? 0.2617 0.3186 0.1945 -0.0046 0.0023  -0.0202 122 GLU A N   
382  C  CA  . GLU A 122 ? 0.3086 0.3784 0.2336 -0.0007 0.0048  -0.0181 122 GLU A CA  
383  C  C   . GLU A 122 ? 0.3356 0.4035 0.2602 0.0021  0.0093  -0.0211 122 GLU A C   
384  O  O   . GLU A 122 ? 0.3325 0.4103 0.2496 0.0053  0.0111  -0.0253 122 GLU A O   
385  C  CB  . GLU A 122 ? 0.4245 0.4997 0.3502 0.0004  0.0059  -0.0054 122 GLU A CB  
386  C  CG  . GLU A 122 ? 0.4761 0.5620 0.3971 0.0044  0.0102  0.0008  122 GLU A CG  
387  C  CD  . GLU A 122 ? 0.5634 0.6516 0.4880 0.0048  0.0113  0.0140  122 GLU A CD  
388  O  OE1 . GLU A 122 ? 0.5393 0.6170 0.4717 0.0023  0.0101  0.0176  122 GLU A OE1 
389  O  OE2 . GLU A 122 ? 0.6083 0.7087 0.5280 0.0078  0.0136  0.0207  122 GLU A OE2 
390  N  N   . TYR A 123 ? 0.3025 0.3593 0.2351 0.0015  0.0112  -0.0187 123 TYR A N   
391  C  CA  . TYR A 123 ? 0.2871 0.3421 0.2210 0.0044  0.0154  -0.0213 123 TYR A CA  
392  C  C   . TYR A 123 ? 0.3136 0.3591 0.2498 0.0040  0.0148  -0.0321 123 TYR A C   
393  O  O   . TYR A 123 ? 0.3126 0.3553 0.2512 0.0068  0.0182  -0.0346 123 TYR A O   
394  C  CB  . TYR A 123 ? 0.2964 0.3461 0.2383 0.0042  0.0177  -0.0126 123 TYR A CB  
395  C  CG  . TYR A 123 ? 0.3031 0.3609 0.2448 0.0048  0.0195  -0.0019 123 TYR A CG  
396  C  CD1 . TYR A 123 ? 0.3172 0.3853 0.2562 0.0082  0.0239  0.0014  123 TYR A CD1 
397  C  CD2 . TYR A 123 ? 0.3013 0.3563 0.2464 0.0022  0.0172  0.0051  123 TYR A CD2 
398  C  CE1 . TYR A 123 ? 0.3011 0.3760 0.2414 0.0085  0.0259  0.0122  123 TYR A CE1 
399  C  CE2 . TYR A 123 ? 0.3544 0.4153 0.3008 0.0027  0.0191  0.0150  123 TYR A CE2 
400  C  CZ  . TYR A 123 ? 0.2495 0.3201 0.1938 0.0056  0.0234  0.0189  123 TYR A CZ  
401  O  OH  . TYR A 123 ? 0.3737 0.4495 0.3208 0.0057  0.0255  0.0298  123 TYR A OH  
402  N  N   . ALA A 124 ? 0.2700 0.3101 0.2070 0.0005  0.0107  -0.0378 124 ALA A N   
403  C  CA  . ALA A 124 ? 0.2973 0.3268 0.2382 -0.0005 0.0101  -0.0475 124 ALA A CA  
404  C  C   . ALA A 124 ? 0.2599 0.2773 0.2099 -0.0001 0.0122  -0.0443 124 ALA A C   
405  O  O   . ALA A 124 ? 0.2845 0.2943 0.2379 0.0012  0.0136  -0.0509 124 ALA A O   
406  C  CB  . ALA A 124 ? 0.2891 0.3238 0.2237 0.0027  0.0117  -0.0583 124 ALA A CB  
407  N  N   . THR A 125 ? 0.2298 0.2457 0.1840 -0.0011 0.0122  -0.0343 125 THR A N   
408  C  CA  . THR A 125 ? 0.2199 0.2261 0.1822 -0.0007 0.0136  -0.0310 125 THR A CA  
409  C  C   . THR A 125 ? 0.2137 0.2088 0.1815 -0.0039 0.0111  -0.0337 125 THR A C   
410  O  O   . THR A 125 ? 0.2197 0.2149 0.1864 -0.0074 0.0079  -0.0351 125 THR A O   
411  C  CB  . THR A 125 ? 0.2847 0.2929 0.2501 -0.0011 0.0141  -0.0206 125 THR A CB  
412  O  OG1 . THR A 125 ? 0.3056 0.3126 0.2713 -0.0047 0.0108  -0.0168 125 THR A OG1 
413  C  CG2 . THR A 125 ? 0.3466 0.3658 0.3080 0.0014  0.0167  -0.0166 125 THR A CG2 
414  N  N   . ALA A 126 ? 0.2077 0.1940 0.1820 -0.0025 0.0127  -0.0337 126 ALA A N   
415  C  CA  . ALA A 126 ? 0.1920 0.1676 0.1729 -0.0052 0.0111  -0.0338 126 ALA A CA  
416  C  C   . ALA A 126 ? 0.1945 0.1683 0.1797 -0.0054 0.0109  -0.0245 126 ALA A C   
417  O  O   . ALA A 126 ? 0.1700 0.1440 0.1580 -0.0023 0.0131  -0.0211 126 ALA A O   
418  C  CB  . ALA A 126 ? 0.2003 0.1669 0.1860 -0.0031 0.0131  -0.0402 126 ALA A CB  
419  N  N   . THR A 127 ? 0.1798 0.1529 0.1656 -0.0090 0.0083  -0.0208 127 THR A N   
420  C  CA  . THR A 127 ? 0.1529 0.1240 0.1423 -0.0097 0.0076  -0.0135 127 THR A CA  
421  C  C   . THR A 127 ? 0.1338 0.0968 0.1283 -0.0119 0.0066  -0.0133 127 THR A C   
422  O  O   . THR A 127 ? 0.1525 0.1140 0.1469 -0.0149 0.0051  -0.0169 127 THR A O   
423  C  CB  . THR A 127 ? 0.1486 0.1260 0.1346 -0.0115 0.0058  -0.0091 127 THR A CB  
424  O  OG1 . THR A 127 ? 0.1535 0.1384 0.1357 -0.0097 0.0071  -0.0082 127 THR A OG1 
425  C  CG2 . THR A 127 ? 0.1450 0.1207 0.1342 -0.0120 0.0051  -0.0028 127 THR A CG2 
426  N  N   . ALA A 128 ? 0.1480 0.1070 0.1471 -0.0105 0.0073  -0.0084 128 ALA A N   
427  C  CA  . ALA A 128 ? 0.1553 0.1079 0.1592 -0.0125 0.0067  -0.0061 128 ALA A CA  
428  C  C   . ALA A 128 ? 0.1610 0.1151 0.1664 -0.0112 0.0065  0.0014  128 ALA A C   
429  O  O   . ALA A 128 ? 0.1466 0.1050 0.1512 -0.0087 0.0069  0.0038  128 ALA A O   
430  C  CB  . ALA A 128 ? 0.1917 0.1353 0.2014 -0.0115 0.0084  -0.0097 128 ALA A CB  
431  N  N   . THR A 129 ? 0.1367 0.0884 0.1447 -0.0132 0.0058  0.0051  129 THR A N   
432  C  CA  . THR A 129 ? 0.1257 0.0798 0.1342 -0.0121 0.0054  0.0118  129 THR A CA  
433  C  C   . THR A 129 ? 0.1556 0.1038 0.1701 -0.0107 0.0068  0.0157  129 THR A C   
434  O  O   . THR A 129 ? 0.1767 0.1190 0.1952 -0.0130 0.0075  0.0149  129 THR A O   
435  C  CB  . THR A 129 ? 0.1535 0.1118 0.1591 -0.0148 0.0038  0.0136  129 THR A CB  
436  O  OG1 . THR A 129 ? 0.1602 0.1236 0.1612 -0.0154 0.0027  0.0109  129 THR A OG1 
437  C  CG2 . THR A 129 ? 0.1741 0.1356 0.1796 -0.0134 0.0034  0.0195  129 THR A CG2 
438  N  N   . ILE A 130 ? 0.1450 0.0951 0.1609 -0.0071 0.0072  0.0203  130 ILE A N   
439  C  CA  . ILE A 130 ? 0.1512 0.0967 0.1730 -0.0047 0.0087  0.0256  130 ILE A CA  
440  C  C   . ILE A 130 ? 0.1622 0.1146 0.1822 -0.0032 0.0076  0.0327  130 ILE A C   
441  O  O   . ILE A 130 ? 0.1575 0.1172 0.1741 -0.0017 0.0060  0.0329  130 ILE A O   
442  C  CB  . ILE A 130 ? 0.1597 0.1017 0.1855 -0.0005 0.0105  0.0242  130 ILE A CB  
443  C  CG1 . ILE A 130 ? 0.3137 0.2484 0.3411 -0.0019 0.0118  0.0162  130 ILE A CG1 
444  C  CG2 . ILE A 130 ? 0.1842 0.1226 0.2165 0.0031  0.0119  0.0315  130 ILE A CG2 
445  C  CD1 . ILE A 130 ? 0.3578 0.2911 0.3873 0.0023  0.0136  0.0128  130 ILE A CD1 
446  N  N   . MET A 131 ? 0.1748 0.1255 0.1973 -0.0036 0.0083  0.0385  131 MET A N   
447  C  CA  A MET A 131 ? 0.1467 0.1052 0.1665 -0.0019 0.0073  0.0451  131 MET A CA  
448  C  CA  B MET A 131 ? 0.1470 0.1056 0.1669 -0.0019 0.0073  0.0452  131 MET A CA  
449  C  C   . MET A 131 ? 0.2071 0.1663 0.2310 0.0030  0.0081  0.0514  131 MET A C   
450  O  O   . MET A 131 ? 0.2565 0.2078 0.2873 0.0044  0.0104  0.0543  131 MET A O   
451  C  CB  A MET A 131 ? 0.1951 0.1538 0.2152 -0.0044 0.0081  0.0493  131 MET A CB  
452  C  CB  B MET A 131 ? 0.1950 0.1537 0.2152 -0.0044 0.0082  0.0495  131 MET A CB  
453  C  CG  A MET A 131 ? 0.1561 0.1250 0.1709 -0.0029 0.0069  0.0542  131 MET A CG  
454  C  CG  B MET A 131 ? 0.1304 0.0933 0.1453 -0.0080 0.0068  0.0456  131 MET A CG  
455  S  SD  A MET A 131 ? 0.3462 0.3178 0.3601 -0.0058 0.0082  0.0580  131 MET A SD  
456  S  SD  B MET A 131 ? 0.4103 0.3743 0.4273 -0.0104 0.0086  0.0515  131 MET A SD  
457  C  CE  A MET A 131 ? 0.2308 0.2062 0.2382 -0.0088 0.0060  0.0496  131 MET A CE  
458  C  CE  B MET A 131 ? 0.3168 0.2914 0.3287 -0.0062 0.0081  0.0588  131 MET A CE  
459  N  N   . LEU A 132 ? 0.1605 0.1292 0.1810 0.0057  0.0060  0.0532  132 LEU A N   
460  C  CA  . LEU A 132 ? 0.1849 0.1573 0.2089 0.0108  0.0061  0.0598  132 LEU A CA  
461  C  C   . LEU A 132 ? 0.2054 0.1849 0.2269 0.0121  0.0056  0.0678  132 LEU A C   
462  O  O   . LEU A 132 ? 0.2236 0.2085 0.2389 0.0096  0.0043  0.0666  132 LEU A O   
463  C  CB  . LEU A 132 ? 0.1961 0.1768 0.2187 0.0128  0.0037  0.0571  132 LEU A CB  
464  C  CG  . LEU A 132 ? 0.1579 0.1340 0.1825 0.0122  0.0046  0.0500  132 LEU A CG  
465  C  CD1 . LEU A 132 ? 0.1909 0.1773 0.2147 0.0135  0.0022  0.0484  132 LEU A CD1 
466  C  CD2 . LEU A 132 ? 0.2441 0.2106 0.2760 0.0151  0.0078  0.0506  132 LEU A CD2 
467  N  N   . MET A 133 ? 0.1813 0.1612 0.2076 0.0165  0.0069  0.0764  133 MET A N   
468  C  CA  . MET A 133 ? 0.2167 0.2055 0.2402 0.0189  0.0065  0.0855  133 MET A CA  
469  C  C   . MET A 133 ? 0.3587 0.3445 0.3812 0.0155  0.0087  0.0883  133 MET A C   
470  O  O   . MET A 133 ? 0.2538 0.2495 0.2701 0.0156  0.0078  0.0916  133 MET A O   
471  C  CB  . MET A 133 ? 0.2595 0.2632 0.2751 0.0198  0.0025  0.0836  133 MET A CB  
472  C  CG  . MET A 133 ? 0.2572 0.2656 0.2748 0.0225  0.0002  0.0809  133 MET A CG  
473  S  SD  . MET A 133 ? 0.2668 0.2927 0.2772 0.0230  -0.0051 0.0779  133 MET A SD  
474  C  CE  . MET A 133 ? 0.2802 0.3022 0.2848 0.0164  -0.0060 0.0669  133 MET A CE  
475  N  N   . GLY A 134 ? 0.2383 0.2114 0.2671 0.0124  0.0114  0.0866  134 GLY A N   
476  C  CA  . GLY A 134 ? 0.2727 0.2426 0.3035 0.0093  0.0139  0.0909  134 GLY A CA  
477  C  C   . GLY A 134 ? 0.3432 0.3111 0.3707 0.0035  0.0133  0.0823  134 GLY A C   
478  O  O   . GLY A 134 ? 0.3838 0.3570 0.4044 0.0025  0.0106  0.0751  134 GLY A O   
479  N  N   . ASP A 135 ? 0.2748 0.2355 0.3082 -0.0003 0.0158  0.0837  135 ASP A N   
480  C  CA  . ASP A 135 ? 0.2459 0.2052 0.2777 -0.0057 0.0152  0.0762  135 ASP A CA  
481  C  C   . ASP A 135 ? 0.2026 0.1706 0.2310 -0.0073 0.0160  0.0806  135 ASP A C   
482  O  O   . ASP A 135 ? 0.2928 0.2597 0.3226 -0.0118 0.0163  0.0770  135 ASP A O   
483  C  CB  . ASP A 135 ? 0.3753 0.3218 0.4163 -0.0096 0.0168  0.0724  135 ASP A CB  
484  C  CG  . ASP A 135 ? 0.4199 0.3627 0.4686 -0.0109 0.0195  0.0782  135 ASP A CG  
485  O  OD1 . ASP A 135 ? 0.5053 0.4544 0.5532 -0.0075 0.0206  0.0861  135 ASP A OD1 
486  O  OD2 . ASP A 135 ? 0.5066 0.4412 0.5620 -0.0153 0.0203  0.0737  135 ASP A OD2 
487  N  N   . THR A 136 ? 0.1695 0.1472 0.1935 -0.0035 0.0163  0.0880  136 THR A N   
488  C  CA  . THR A 136 ? 0.1774 0.1655 0.1964 -0.0040 0.0170  0.0905  136 THR A CA  
489  C  C   . THR A 136 ? 0.1827 0.1827 0.1910 -0.0003 0.0146  0.0899  136 THR A C   
490  O  O   . THR A 136 ? 0.2046 0.2061 0.2104 0.0028  0.0122  0.0885  136 THR A O   
491  C  CB  . THR A 136 ? 0.1988 0.1896 0.2225 -0.0029 0.0199  0.0979  136 THR A CB  
492  O  OG1 . THR A 136 ? 0.2253 0.2192 0.2485 0.0022  0.0196  0.1031  136 THR A OG1 
493  C  CG2 . THR A 136 ? 0.2513 0.2307 0.2859 -0.0071 0.0220  0.0975  136 THR A CG2 
494  N  N   . CYS A 137 ? 0.1554 0.1648 0.1577 -0.0006 0.0149  0.0896  137 CYS A N   
495  C  CA  . CYS A 137 ? 0.1463 0.1678 0.1383 0.0029  0.0125  0.0873  137 CYS A CA  
496  C  C   . CYS A 137 ? 0.1658 0.1985 0.1540 0.0048  0.0149  0.0933  137 CYS A C   
497  O  O   . CYS A 137 ? 0.1609 0.1925 0.1534 0.0022  0.0177  0.0949  137 CYS A O   
498  C  CB  . CYS A 137 ? 0.1569 0.1784 0.1439 0.0009  0.0098  0.0759  137 CYS A CB  
499  S  SG  . CYS A 137 ? 0.1473 0.1813 0.1233 0.0048  0.0063  0.0712  137 CYS A SG  
500  N  N   . THR A 138 ? 0.1552 0.1995 0.1359 0.0092  0.0133  0.0944  138 THR A N   
501  C  CA  . THR A 138 ? 0.1612 0.2171 0.1382 0.0114  0.0153  0.0976  138 THR A CA  
502  C  C   . THR A 138 ? 0.1583 0.2223 0.1267 0.0115  0.0150  0.0917  138 THR A C   
503  O  O   . THR A 138 ? 0.1641 0.2373 0.1302 0.0132  0.0173  0.0940  138 THR A O   
504  C  CB  . THR A 138 ? 0.1882 0.2545 0.1612 0.0164  0.0139  0.1014  138 THR A CB  
505  O  OG1 . THR A 138 ? 0.2005 0.2730 0.1647 0.0183  0.0095  0.0947  138 THR A OG1 
506  C  CG2 . THR A 138 ? 0.2300 0.2892 0.2116 0.0172  0.0146  0.1078  138 THR A CG2 
507  N  N   . ARG A 139 ? 0.1511 0.2119 0.1156 0.0099  0.0123  0.0834  139 ARG A N   
508  C  CA  A ARG A 139 ? 0.1580 0.2265 0.1144 0.0111  0.0114  0.0755  139 ARG A CA  
509  C  CA  B ARG A 139 ? 0.1585 0.2275 0.1148 0.0112  0.0115  0.0757  139 ARG A CA  
510  C  C   . ARG A 139 ? 0.2003 0.2686 0.1591 0.0090  0.0148  0.0749  139 ARG A C   
511  O  O   . ARG A 139 ? 0.1715 0.2491 0.1238 0.0114  0.0157  0.0716  139 ARG A O   
512  C  CB  A ARG A 139 ? 0.1615 0.2248 0.1161 0.0100  0.0069  0.0639  139 ARG A CB  
513  C  CB  B ARG A 139 ? 0.1558 0.2204 0.1096 0.0104  0.0069  0.0641  139 ARG A CB  
514  C  CG  A ARG A 139 ? 0.2256 0.2925 0.1772 0.0123  0.0032  0.0632  139 ARG A CG  
515  C  CG  B ARG A 139 ? 0.2275 0.2935 0.1799 0.0121  0.0032  0.0638  139 ARG A CG  
516  C  CD  A ARG A 139 ? 0.2837 0.3653 0.2285 0.0168  0.0039  0.0701  139 ARG A CD  
517  C  CD  B ARG A 139 ? 0.3173 0.3982 0.2623 0.0169  0.0027  0.0691  139 ARG A CD  
518  N  NE  A ARG A 139 ? 0.4085 0.4992 0.3462 0.0194  -0.0006 0.0643  139 ARG A NE  
519  N  NE  B ARG A 139 ? 0.2973 0.3829 0.2389 0.0184  -0.0022 0.0641  139 ARG A NE  
520  C  CZ  A ARG A 139 ? 0.3282 0.4206 0.2673 0.0206  -0.0037 0.0663  139 ARG A CZ  
521  C  CZ  B ARG A 139 ? 0.3584 0.4587 0.2918 0.0223  -0.0045 0.0639  139 ARG A CZ  
522  N  NH1 A ARG A 139 ? 0.4389 0.5417 0.3718 0.0227  -0.0081 0.0609  139 ARG A NH1 
523  N  NH1 B ARG A 139 ? 0.4291 0.5337 0.3600 0.0226  -0.0096 0.0565  139 ARG A NH1 
524  N  NH2 A ARG A 139 ? 0.3514 0.4351 0.2988 0.0198  -0.0024 0.0735  139 ARG A NH2 
525  N  NH2 B ARG A 139 ? 0.3408 0.4493 0.2720 0.0249  -0.0015 0.0685  139 ARG A NH2 
526  N  N   . GLY A 140 ? 0.1621 0.2203 0.1303 0.0048  0.0165  0.0770  140 GLY A N   
527  C  CA  . GLY A 140 ? 0.1737 0.2333 0.1453 0.0027  0.0195  0.0770  140 GLY A CA  
528  C  C   . GLY A 140 ? 0.1489 0.2092 0.1167 0.0029  0.0181  0.0668  140 GLY A C   
529  O  O   . GLY A 140 ? 0.1554 0.2232 0.1220 0.0040  0.0207  0.0668  140 GLY A O   
530  N  N   . CYS A 141 ? 0.1340 0.1868 0.1007 0.0021  0.0143  0.0585  141 CYS A N   
531  C  CA  . CYS A 141 ? 0.1309 0.1832 0.0948 0.0026  0.0129  0.0493  141 CYS A CA  
532  C  C   . CYS A 141 ? 0.1518 0.2025 0.1218 0.0002  0.0151  0.0494  141 CYS A C   
533  O  O   . CYS A 141 ? 0.1469 0.1926 0.1245 -0.0034 0.0161  0.0537  141 CYS A O   
534  C  CB  . CYS A 141 ? 0.1263 0.1697 0.0904 0.0013  0.0089  0.0421  141 CYS A CB  
535  S  SG  . CYS A 141 ? 0.1662 0.2138 0.1237 0.0041  0.0055  0.0400  141 CYS A SG  
536  N  N   . ARG A 142 ? 0.1305 0.1855 0.0976 0.0024  0.0157  0.0441  142 ARG A N   
537  C  CA  . ARG A 142 ? 0.1369 0.1944 0.1090 0.0015  0.0182  0.0448  142 ARG A CA  
538  C  C   . ARG A 142 ? 0.1367 0.1852 0.1162 -0.0026 0.0165  0.0428  142 ARG A C   
539  O  O   . ARG A 142 ? 0.1441 0.1952 0.1295 -0.0043 0.0182  0.0449  142 ARG A O   
540  C  CB  . ARG A 142 ? 0.1540 0.2173 0.1213 0.0057  0.0189  0.0385  142 ARG A CB  
541  C  CG  . ARG A 142 ? 0.1363 0.2115 0.0954 0.0104  0.0212  0.0396  142 ARG A CG  
542  C  CD  . ARG A 142 ? 0.1728 0.2518 0.1273 0.0147  0.0216  0.0314  142 ARG A CD  
543  N  NE  . ARG A 142 ? 0.1586 0.2507 0.1050 0.0196  0.0243  0.0316  142 ARG A NE  
544  C  CZ  . ARG A 142 ? 0.1724 0.2686 0.1124 0.0241  0.0244  0.0231  142 ARG A CZ  
545  N  NH1 . ARG A 142 ? 0.1954 0.2828 0.1370 0.0245  0.0221  0.0141  142 ARG A NH1 
546  N  NH2 . ARG A 142 ? 0.1630 0.2726 0.0949 0.0287  0.0269  0.0236  142 ARG A NH2 
547  N  N   . PHE A 143 ? 0.1269 0.1661 0.1061 -0.0041 0.0131  0.0389  143 PHE A N   
548  C  CA  . PHE A 143 ? 0.1300 0.1618 0.1145 -0.0073 0.0114  0.0364  143 PHE A CA  
549  C  C   . PHE A 143 ? 0.1660 0.1908 0.1543 -0.0109 0.0103  0.0389  143 PHE A C   
550  O  O   . PHE A 143 ? 0.1584 0.1780 0.1509 -0.0137 0.0089  0.0370  143 PHE A O   
551  C  CB  . PHE A 143 ? 0.1349 0.1619 0.1164 -0.0057 0.0088  0.0294  143 PHE A CB  
552  C  CG  . PHE A 143 ? 0.1186 0.1412 0.0965 -0.0055 0.0065  0.0275  143 PHE A CG  
553  C  CD1 . PHE A 143 ? 0.1596 0.1748 0.1401 -0.0082 0.0047  0.0274  143 PHE A CD1 
554  C  CD2 . PHE A 143 ? 0.1332 0.1601 0.1051 -0.0025 0.0062  0.0256  143 PHE A CD2 
555  C  CE1 . PHE A 143 ? 0.1793 0.1918 0.1573 -0.0077 0.0028  0.0262  143 PHE A CE1 
556  C  CE2 . PHE A 143 ? 0.1768 0.2012 0.1463 -0.0024 0.0038  0.0241  143 PHE A CE2 
557  C  CZ  . PHE A 143 ? 0.1999 0.2172 0.1728 -0.0050 0.0023  0.0248  143 PHE A CZ  
558  N  N   . CYS A 144 ? 0.1360 0.1607 0.1229 -0.0104 0.0107  0.0429  144 CYS A N   
559  C  CA  . CYS A 144 ? 0.1214 0.1381 0.1107 -0.0123 0.0093  0.0436  144 CYS A CA  
560  C  C   . CYS A 144 ? 0.1412 0.1549 0.1384 -0.0159 0.0109  0.0484  144 CYS A C   
561  O  O   . CYS A 144 ? 0.1590 0.1776 0.1589 -0.0163 0.0137  0.0544  144 CYS A O   
562  C  CB  . CYS A 144 ? 0.1311 0.1495 0.1157 -0.0094 0.0087  0.0455  144 CYS A CB  
563  S  SG  . CYS A 144 ? 0.1530 0.1623 0.1412 -0.0108 0.0072  0.0464  144 CYS A SG  
564  N  N   A SER A 145 ? 0.1593 0.1647 0.1602 -0.0187 0.0093  0.0455  145 SER A N   
565  N  N   B SER A 145 ? 0.1591 0.1646 0.1601 -0.0187 0.0094  0.0456  145 SER A N   
566  C  CA  A SER A 145 ? 0.1742 0.1751 0.1833 -0.0226 0.0104  0.0480  145 SER A CA  
567  C  CA  B SER A 145 ? 0.1721 0.1733 0.1813 -0.0226 0.0105  0.0483  145 SER A CA  
568  C  C   A SER A 145 ? 0.1786 0.1738 0.1903 -0.0222 0.0113  0.0525  145 SER A C   
569  C  C   B SER A 145 ? 0.1779 0.1731 0.1897 -0.0222 0.0113  0.0524  145 SER A C   
570  O  O   A SER A 145 ? 0.2093 0.1996 0.2290 -0.0254 0.0126  0.0549  145 SER A O   
571  O  O   B SER A 145 ? 0.2099 0.1998 0.2296 -0.0254 0.0125  0.0546  145 SER A O   
572  C  CB  A SER A 145 ? 0.2004 0.1961 0.2121 -0.0256 0.0081  0.0417  145 SER A CB  
573  C  CB  B SER A 145 ? 0.2043 0.2008 0.2164 -0.0257 0.0084  0.0421  145 SER A CB  
574  O  OG  A SER A 145 ? 0.2022 0.2035 0.2129 -0.0259 0.0074  0.0388  145 SER A OG  
575  O  OG  B SER A 145 ? 0.2008 0.1920 0.2090 -0.0242 0.0064  0.0380  145 SER A OG  
576  N  N   . VAL A 146 ? 0.1631 0.1589 0.1693 -0.0184 0.0106  0.0534  146 VAL A N   
577  C  CA  . VAL A 146 ? 0.1638 0.1551 0.1731 -0.0172 0.0116  0.0584  146 VAL A CA  
578  C  C   . VAL A 146 ? 0.1696 0.1642 0.1833 -0.0176 0.0149  0.0675  146 VAL A C   
579  O  O   . VAL A 146 ? 0.1679 0.1719 0.1782 -0.0163 0.0163  0.0706  146 VAL A O   
580  C  CB  . VAL A 146 ? 0.1498 0.1439 0.1524 -0.0129 0.0099  0.0582  146 VAL A CB  
581  C  CG1 . VAL A 146 ? 0.1581 0.1489 0.1643 -0.0107 0.0110  0.0647  146 VAL A CG1 
582  C  CG2 . VAL A 146 ? 0.1713 0.1618 0.1712 -0.0130 0.0071  0.0501  146 VAL A CG2 
583  N  N   . LYS A 147 ? 0.1873 0.1744 0.2092 -0.0190 0.0166  0.0721  147 LYS A N   
584  C  CA  . LYS A 147 ? 0.1664 0.1560 0.1941 -0.0195 0.0202  0.0822  147 LYS A CA  
585  C  C   . LYS A 147 ? 0.1479 0.1474 0.1682 -0.0140 0.0209  0.0880  147 LYS A C   
586  O  O   . LYS A 147 ? 0.1909 0.1909 0.2062 -0.0103 0.0192  0.0881  147 LYS A O   
587  C  CB  . LYS A 147 ? 0.2096 0.1881 0.2464 -0.0207 0.0212  0.0833  147 LYS A CB  
588  C  CG  . LYS A 147 ? 0.4233 0.3922 0.4676 -0.0261 0.0204  0.0767  147 LYS A CG  
589  C  CD  . LYS A 147 ? 0.4187 0.3765 0.4715 -0.0266 0.0215  0.0772  147 LYS A CD  
590  C  CE  . LYS A 147 ? 0.5248 0.4813 0.5865 -0.0309 0.0234  0.0790  147 LYS A CE  
591  N  NZ  . LYS A 147 ? 0.6003 0.5603 0.6632 -0.0360 0.0222  0.0737  147 LYS A NZ  
592  N  N   . THR A 148 ? 0.1843 0.1926 0.2044 -0.0134 0.0232  0.0926  148 THR A N   
593  C  CA  . THR A 148 ? 0.1553 0.1749 0.1679 -0.0081 0.0238  0.0974  148 THR A CA  
594  C  C   . THR A 148 ? 0.1869 0.2049 0.2052 -0.0062 0.0256  0.1048  148 THR A C   
595  O  O   . THR A 148 ? 0.2496 0.2606 0.2778 -0.0093 0.0275  0.1072  148 THR A O   
596  C  CB  . THR A 148 ? 0.2077 0.2392 0.2165 -0.0076 0.0257  0.0983  148 THR A CB  
597  O  OG1 . THR A 148 ? 0.2495 0.2824 0.2537 -0.0091 0.0242  0.0917  148 THR A OG1 
598  C  CG2 . THR A 148 ? 0.3035 0.3475 0.3036 -0.0020 0.0260  0.1019  148 THR A CG2 
599  N  N   . ALA A 149 ? 0.1682 0.1933 0.1805 -0.0010 0.0248  0.1081  149 ALA A N   
600  C  CA  . ALA A 149 ? 0.2047 0.2312 0.2215 0.0017  0.0266  0.1163  149 ALA A CA  
601  C  C   . ALA A 149 ? 0.2193 0.2610 0.2269 0.0071  0.0261  0.1196  149 ALA A C   
602  O  O   . ALA A 149 ? 0.2805 0.3288 0.2783 0.0091  0.0235  0.1145  149 ALA A O   
603  C  CB  . ALA A 149 ? 0.2277 0.2433 0.2501 0.0025  0.0255  0.1167  149 ALA A CB  
604  N  N   . ARG A 150 ? 0.2184 0.2661 0.2293 0.0096  0.0286  0.1281  150 ARG A N   
605  C  CA  . ARG A 150 ? 0.2578 0.3213 0.2595 0.0148  0.0280  0.1306  150 ARG A CA  
606  C  C   . ARG A 150 ? 0.2910 0.3573 0.2885 0.0190  0.0250  0.1306  150 ARG A C   
607  O  O   . ARG A 150 ? 0.3554 0.4343 0.3431 0.0226  0.0229  0.1287  150 ARG A O   
608  C  CB  . ARG A 150 ? 0.3531 0.4250 0.3587 0.0166  0.0318  0.1400  150 ARG A CB  
609  C  CG  . ARG A 150 ? 0.3931 0.4717 0.3970 0.0148  0.0340  0.1389  150 ARG A CG  
610  C  CD  . ARG A 150 ? 0.3902 0.4786 0.3977 0.0168  0.0379  0.1485  150 ARG A CD  
611  N  NE  . ARG A 150 ? 0.4768 0.5705 0.4847 0.0147  0.0403  0.1477  150 ARG A NE  
612  C  CZ  . ARG A 150 ? 0.4695 0.5543 0.4867 0.0093  0.0421  0.1475  150 ARG A CZ  
613  N  NH1 . ARG A 150 ? 0.4819 0.5516 0.5085 0.0053  0.0416  0.1473  150 ARG A NH1 
614  N  NH2 . ARG A 150 ? 0.4952 0.5872 0.5125 0.0081  0.0443  0.1473  150 ARG A NH2 
615  N  N   . ASN A 151 ? 0.2322 0.2878 0.2366 0.0187  0.0244  0.1320  151 ASN A N   
616  C  CA  . ASN A 151 ? 0.2780 0.3380 0.2779 0.0227  0.0211  0.1312  151 ASN A CA  
617  C  C   . ASN A 151 ? 0.2995 0.3464 0.3031 0.0209  0.0190  0.1261  151 ASN A C   
618  O  O   . ASN A 151 ? 0.2175 0.2508 0.2289 0.0170  0.0206  0.1247  151 ASN A O   
619  C  CB  . ASN A 151 ? 0.3508 0.4179 0.3539 0.0273  0.0225  0.1408  151 ASN A CB  
620  C  CG  . ASN A 151 ? 0.4455 0.5016 0.4613 0.0261  0.0261  0.1478  151 ASN A CG  
621  O  OD1 . ASN A 151 ? 0.4327 0.4754 0.4554 0.0246  0.0258  0.1460  151 ASN A OD1 
622  N  ND2 . ASN A 151 ? 0.3626 0.4250 0.3818 0.0270  0.0295  0.1559  151 ASN A ND2 
623  N  N   . PRO A 152 ? 0.2510 0.3024 0.2492 0.0235  0.0153  0.1227  152 PRO A N   
624  C  CA  . PRO A 152 ? 0.2434 0.2837 0.2456 0.0225  0.0136  0.1187  152 PRO A CA  
625  C  C   . PRO A 152 ? 0.2678 0.2997 0.2804 0.0242  0.0157  0.1248  152 PRO A C   
626  O  O   . PRO A 152 ? 0.2711 0.3096 0.2860 0.0277  0.0172  0.1326  152 PRO A O   
627  C  CB  . PRO A 152 ? 0.2730 0.3237 0.2670 0.0255  0.0090  0.1149  152 PRO A CB  
628  C  CG  . PRO A 152 ? 0.3139 0.3808 0.2994 0.0280  0.0082  0.1161  152 PRO A CG  
629  C  CD  . PRO A 152 ? 0.3256 0.3933 0.3146 0.0278  0.0126  0.1229  152 PRO A CD  
630  N  N   . PRO A 153 ? 0.2985 0.3163 0.3179 0.0222  0.0160  0.1214  153 PRO A N   
631  C  CA  . PRO A 153 ? 0.3191 0.3283 0.3484 0.0243  0.0179  0.1258  153 PRO A CA  
632  C  C   . PRO A 153 ? 0.2590 0.2748 0.2871 0.0294  0.0154  0.1271  153 PRO A C   
633  O  O   . PRO A 153 ? 0.3247 0.3491 0.3449 0.0303  0.0117  0.1229  153 PRO A O   
634  C  CB  . PRO A 153 ? 0.2841 0.2769 0.3196 0.0200  0.0188  0.1192  153 PRO A CB  
635  C  CG  . PRO A 153 ? 0.2904 0.2860 0.3177 0.0179  0.0157  0.1115  153 PRO A CG  
636  C  CD  . PRO A 153 ? 0.2686 0.2782 0.2865 0.0181  0.0147  0.1128  153 PRO A CD  
637  N  N   . PRO A 154 ? 0.2453 0.2575 0.2814 0.0329  0.0171  0.1328  154 PRO A N   
638  C  CA  . PRO A 154 ? 0.2728 0.2920 0.3086 0.0380  0.0147  0.1343  154 PRO A CA  
639  C  C   . PRO A 154 ? 0.2726 0.2844 0.3096 0.0374  0.0128  0.1268  154 PRO A C   
640  O  O   . PRO A 154 ? 0.2897 0.2873 0.3314 0.0341  0.0144  0.1219  154 PRO A O   
641  C  CB  . PRO A 154 ? 0.3471 0.3625 0.3926 0.0416  0.0179  0.1427  154 PRO A CB  
642  C  CG  . PRO A 154 ? 0.4201 0.4283 0.4703 0.0383  0.0218  0.1460  154 PRO A CG  
643  C  CD  . PRO A 154 ? 0.3232 0.3248 0.3697 0.0323  0.0213  0.1379  154 PRO A CD  
644  N  N   . LEU A 155 ? 0.3733 0.3958 0.4067 0.0407  0.0092  0.1259  155 LEU A N   
645  C  CA  . LEU A 155 ? 0.3789 0.3969 0.4146 0.0412  0.0075  0.1201  155 LEU A CA  
646  C  C   . LEU A 155 ? 0.3540 0.3617 0.4006 0.0444  0.0104  0.1225  155 LEU A C   
647  O  O   . LEU A 155 ? 0.3217 0.3346 0.3721 0.0489  0.0112  0.1294  155 LEU A O   
648  C  CB  . LEU A 155 ? 0.4268 0.4611 0.4566 0.0437  0.0026  0.1187  155 LEU A CB  
649  C  CG  . LEU A 155 ? 0.4103 0.4440 0.4385 0.0418  -0.0003 0.1111  155 LEU A CG  
650  C  CD1 . LEU A 155 ? 0.4145 0.4421 0.4372 0.0362  -0.0001 0.1058  155 LEU A CD1 
651  C  CD2 . LEU A 155 ? 0.4723 0.5237 0.4960 0.0438  -0.0056 0.1097  155 LEU A CD2 
652  N  N   . ASP A 156 ? 0.3070 0.3000 0.3585 0.0423  0.0122  0.1167  156 ASP A N   
653  C  CA  . ASP A 156 ? 0.2867 0.2691 0.3482 0.0455  0.0150  0.1169  156 ASP A CA  
654  C  C   . ASP A 156 ? 0.3135 0.3014 0.3761 0.0493  0.0128  0.1138  156 ASP A C   
655  O  O   . ASP A 156 ? 0.2519 0.2374 0.3124 0.0471  0.0116  0.1069  156 ASP A O   
656  C  CB  . ASP A 156 ? 0.3097 0.2742 0.3762 0.0414  0.0181  0.1110  156 ASP A CB  
657  C  CG  . ASP A 156 ? 0.3809 0.3337 0.4571 0.0447  0.0209  0.1089  156 ASP A CG  
658  O  OD1 . ASP A 156 ? 0.3712 0.3296 0.4512 0.0505  0.0209  0.1129  156 ASP A OD1 
659  O  OD2 . ASP A 156 ? 0.4514 0.3900 0.5316 0.0414  0.0231  0.1025  156 ASP A OD2 
660  N  N   . ALA A 157 ? 0.2712 0.2671 0.3379 0.0550  0.0125  0.1193  157 ALA A N   
661  C  CA  . ALA A 157 ? 0.2543 0.2583 0.3227 0.0586  0.0102  0.1169  157 ALA A CA  
662  C  C   . ALA A 157 ? 0.2299 0.2209 0.3054 0.0597  0.0131  0.1107  157 ALA A C   
663  O  O   . ALA A 157 ? 0.2579 0.2549 0.3345 0.0616  0.0115  0.1070  157 ALA A O   
664  C  CB  . ALA A 157 ? 0.2876 0.3043 0.3589 0.0643  0.0091  0.1242  157 ALA A CB  
665  N  N   . SER A 158 ? 0.2381 0.2124 0.3187 0.0585  0.0172  0.1088  158 SER A N   
666  C  CA  . SER A 158 ? 0.3060 0.2677 0.3925 0.0594  0.0200  0.1014  158 SER A CA  
667  C  C   . SER A 158 ? 0.2862 0.2404 0.3685 0.0539  0.0200  0.0928  158 SER A C   
668  O  O   . SER A 158 ? 0.2578 0.2027 0.3438 0.0546  0.0223  0.0853  158 SER A O   
669  C  CB  . SER A 158 ? 0.4167 0.3639 0.5113 0.0608  0.0242  0.1023  158 SER A CB  
670  O  OG  . SER A 158 ? 0.5071 0.4464 0.6001 0.0553  0.0251  0.1030  158 SER A OG  
671  N  N   . GLU A 159 ? 0.2288 0.1870 0.3032 0.0487  0.0176  0.0934  159 GLU A N   
672  C  CA  . GLU A 159 ? 0.1802 0.1328 0.2490 0.0419  0.0173  0.0835  159 GLU A CA  
673  C  C   . GLU A 159 ? 0.2159 0.1752 0.2807 0.0408  0.0156  0.0743  159 GLU A C   
674  O  O   . GLU A 159 ? 0.2220 0.1731 0.2862 0.0380  0.0172  0.0652  159 GLU A O   
675  C  CB  . GLU A 159 ? 0.2300 0.1877 0.2906 0.0366  0.0150  0.0855  159 GLU A CB  
676  C  CG  . GLU A 159 ? 0.2811 0.2351 0.3353 0.0295  0.0142  0.0748  159 GLU A CG  
677  C  CD  . GLU A 159 ? 0.2845 0.2429 0.3316 0.0248  0.0126  0.0765  159 GLU A CD  
678  O  OE1 . GLU A 159 ? 0.2453 0.2163 0.2871 0.0258  0.0099  0.0808  159 GLU A OE1 
679  O  OE2 . GLU A 159 ? 0.2819 0.2316 0.3294 0.0202  0.0140  0.0731  159 GLU A OE2 
680  N  N   . PRO A 160 ? 0.2006 0.1748 0.2628 0.0427  0.0125  0.0760  160 PRO A N   
681  C  CA  . PRO A 160 ? 0.1925 0.1724 0.2526 0.0412  0.0115  0.0679  160 PRO A CA  
682  C  C   . PRO A 160 ? 0.1883 0.1608 0.2549 0.0448  0.0153  0.0632  160 PRO A C   
683  O  O   . PRO A 160 ? 0.2046 0.1731 0.2682 0.0416  0.0164  0.0545  160 PRO A O   
684  C  CB  . PRO A 160 ? 0.1820 0.1790 0.2417 0.0436  0.0078  0.0724  160 PRO A CB  
685  C  CG  . PRO A 160 ? 0.2411 0.2425 0.2970 0.0432  0.0056  0.0797  160 PRO A CG  
686  C  CD  . PRO A 160 ? 0.1905 0.1782 0.2511 0.0453  0.0094  0.0848  160 PRO A CD  
687  N  N   . TYR A 161 ? 0.1965 0.1670 0.2718 0.0518  0.0175  0.0690  161 TYR A N   
688  C  CA  . TYR A 161 ? 0.2295 0.1924 0.3115 0.0561  0.0216  0.0642  161 TYR A CA  
689  C  C   . TYR A 161 ? 0.2430 0.1886 0.3248 0.0530  0.0246  0.0572  161 TYR A C   
690  O  O   . TYR A 161 ? 0.2544 0.1960 0.3351 0.0522  0.0266  0.0478  161 TYR A O   
691  C  CB  . TYR A 161 ? 0.2006 0.1643 0.2930 0.0648  0.0234  0.0728  161 TYR A CB  
692  C  CG  . TYR A 161 ? 0.3164 0.2705 0.4166 0.0702  0.0282  0.0679  161 TYR A CG  
693  C  CD1 . TYR A 161 ? 0.3428 0.3066 0.4458 0.0743  0.0292  0.0647  161 TYR A CD1 
694  C  CD2 . TYR A 161 ? 0.3078 0.2437 0.4132 0.0712  0.0319  0.0661  161 TYR A CD2 
695  C  CE1 . TYR A 161 ? 0.3112 0.2667 0.4211 0.0799  0.0341  0.0594  161 TYR A CE1 
696  C  CE2 . TYR A 161 ? 0.3858 0.3128 0.4975 0.0758  0.0362  0.0596  161 TYR A CE2 
697  C  CZ  . TYR A 161 ? 0.3565 0.2930 0.4707 0.0811  0.0376  0.0567  161 TYR A CZ  
698  O  OH  . TYR A 161 ? 0.4172 0.3456 0.5368 0.0858  0.0420  0.0497  161 TYR A OH  
699  N  N   . ASN A 162 ? 0.2210 0.1569 0.3045 0.0513  0.0251  0.0617  162 ASN A N   
700  C  CA  . ASN A 162 ? 0.2675 0.1869 0.3532 0.0483  0.0278  0.0551  162 ASN A CA  
701  C  C   . ASN A 162 ? 0.2102 0.1299 0.2866 0.0408  0.0261  0.0455  162 ASN A C   
702  O  O   . ASN A 162 ? 0.2465 0.1576 0.3229 0.0392  0.0280  0.0360  162 ASN A O   
703  C  CB  . ASN A 162 ? 0.2448 0.1547 0.3358 0.0477  0.0288  0.0634  162 ASN A CB  
704  C  CG  . ASN A 162 ? 0.3330 0.2409 0.4320 0.0537  0.0308  0.0692  162 ASN A CG  
705  O  OD1 . ASN A 162 ? 0.3272 0.2323 0.4314 0.0588  0.0331  0.0653  162 ASN A OD1 
706  N  ND2 . ASN A 162 ? 0.3607 0.2711 0.4606 0.0532  0.0300  0.0784  162 ASN A ND2 
707  N  N   . THR A 163 ? 0.2020 0.1316 0.2705 0.0363  0.0226  0.0478  163 THR A N   
708  C  CA  . THR A 163 ? 0.1898 0.1200 0.2501 0.0296  0.0210  0.0401  163 THR A CA  
709  C  C   . THR A 163 ? 0.1995 0.1360 0.2559 0.0299  0.0210  0.0324  163 THR A C   
710  O  O   . THR A 163 ? 0.2087 0.1410 0.2615 0.0267  0.0217  0.0239  163 THR A O   
711  C  CB  . THR A 163 ? 0.2221 0.1608 0.2759 0.0256  0.0175  0.0449  163 THR A CB  
712  O  OG1 . THR A 163 ? 0.3048 0.2372 0.3617 0.0244  0.0182  0.0512  163 THR A OG1 
713  C  CG2 . THR A 163 ? 0.2125 0.1538 0.2581 0.0196  0.0158  0.0375  163 THR A CG2 
714  N  N   . ALA A 164 ? 0.2118 0.1589 0.2695 0.0339  0.0206  0.0355  164 ALA A N   
715  C  CA  . ALA A 164 ? 0.1904 0.1438 0.2461 0.0347  0.0215  0.0293  164 ALA A CA  
716  C  C   . ALA A 164 ? 0.1982 0.1424 0.2577 0.0381  0.0256  0.0224  164 ALA A C   
717  O  O   . ALA A 164 ? 0.2017 0.1463 0.2566 0.0363  0.0266  0.0145  164 ALA A O   
718  C  CB  . ALA A 164 ? 0.1901 0.1569 0.2489 0.0385  0.0204  0.0345  164 ALA A CB  
719  N  N   . LYS A 165 ? 0.2070 0.1427 0.2749 0.0432  0.0280  0.0255  165 LYS A N   
720  C  CA  . LYS A 165 ? 0.2279 0.1537 0.3003 0.0469  0.0320  0.0180  165 LYS A CA  
721  C  C   . LYS A 165 ? 0.2488 0.1642 0.3168 0.0413  0.0321  0.0091  165 LYS A C   
722  O  O   . LYS A 165 ? 0.2656 0.1799 0.3306 0.0415  0.0339  -0.0007 165 LYS A O   
723  C  CB  . LYS A 165 ? 0.2965 0.2140 0.3800 0.0534  0.0345  0.0241  165 LYS A CB  
724  C  CG  . LYS A 165 ? 0.3202 0.2268 0.4105 0.0589  0.0391  0.0171  165 LYS A CG  
725  C  CD  . LYS A 165 ? 0.3269 0.2249 0.4292 0.0652  0.0413  0.0256  165 LYS A CD  
726  C  CE  . LYS A 165 ? 0.4979 0.3965 0.6081 0.0745  0.0453  0.0243  165 LYS A CE  
727  N  NZ  . LYS A 165 ? 0.5826 0.4758 0.6907 0.0752  0.0485  0.0103  165 LYS A NZ  
728  N  N   . ALA A 166 ? 0.2250 0.1345 0.2924 0.0362  0.0301  0.0122  166 ALA A N   
729  C  CA  . ALA A 166 ? 0.2834 0.1837 0.3484 0.0306  0.0298  0.0043  166 ALA A CA  
730  C  C   . ALA A 166 ? 0.2570 0.1661 0.3114 0.0260  0.0277  -0.0024 166 ALA A C   
731  O  O   . ALA A 166 ? 0.2747 0.1799 0.3262 0.0241  0.0284  -0.0123 166 ALA A O   
732  C  CB  . ALA A 166 ? 0.2869 0.1811 0.3546 0.0262  0.0282  0.0107  166 ALA A CB  
733  N  N   . ILE A 167 ? 0.2042 0.1254 0.2529 0.0243  0.0252  0.0029  167 ILE A N   
734  C  CA  . ILE A 167 ? 0.1869 0.1163 0.2265 0.0204  0.0235  -0.0020 167 ILE A CA  
735  C  C   . ILE A 167 ? 0.1955 0.1289 0.2331 0.0239  0.0261  -0.0090 167 ILE A C   
736  O  O   . ILE A 167 ? 0.2571 0.1916 0.2886 0.0215  0.0261  -0.0167 167 ILE A O   
737  C  CB  . ILE A 167 ? 0.1895 0.1302 0.2253 0.0187  0.0208  0.0051  167 ILE A CB  
738  C  CG1 . ILE A 167 ? 0.2023 0.1401 0.2381 0.0150  0.0184  0.0105  167 ILE A CG1 
739  C  CG2 . ILE A 167 ? 0.1794 0.1285 0.2071 0.0157  0.0198  0.0009  167 ILE A CG2 
740  C  CD1 . ILE A 167 ? 0.1889 0.1367 0.2222 0.0144  0.0157  0.0176  167 ILE A CD1 
741  N  N   . ALA A 168 ? 0.2200 0.1573 0.2625 0.0299  0.0284  -0.0061 168 ALA A N   
742  C  CA  . ALA A 168 ? 0.2300 0.1727 0.2712 0.0340  0.0316  -0.0120 168 ALA A CA  
743  C  C   . ALA A 168 ? 0.2888 0.2211 0.3307 0.0356  0.0342  -0.0223 168 ALA A C   
744  O  O   . ALA A 168 ? 0.3261 0.2628 0.3619 0.0357  0.0355  -0.0302 168 ALA A O   
745  C  CB  . ALA A 168 ? 0.2857 0.2347 0.3338 0.0404  0.0335  -0.0062 168 ALA A CB  
746  N  N   . GLU A 169 ? 0.2578 0.1767 0.3073 0.0368  0.0349  -0.0224 169 GLU A N   
747  C  CA  A GLU A 169 ? 0.3728 0.2807 0.4239 0.0376  0.0371  -0.0333 169 GLU A CA  
748  C  CA  B GLU A 169 ? 0.3731 0.2801 0.4246 0.0375  0.0370  -0.0331 169 GLU A CA  
749  C  C   . GLU A 169 ? 0.3522 0.2592 0.3956 0.0306  0.0344  -0.0408 169 GLU A C   
750  O  O   . GLU A 169 ? 0.4050 0.3127 0.4436 0.0310  0.0356  -0.0515 169 GLU A O   
751  C  CB  A GLU A 169 ? 0.3779 0.2705 0.4404 0.0401  0.0387  -0.0310 169 GLU A CB  
752  C  CB  B GLU A 169 ? 0.3826 0.2742 0.4452 0.0387  0.0380  -0.0299 169 GLU A CB  
753  C  CG  A GLU A 169 ? 0.3881 0.2679 0.4544 0.0416  0.0414  -0.0433 169 GLU A CG  
754  C  CG  B GLU A 169 ? 0.3352 0.2261 0.4072 0.0463  0.0406  -0.0216 169 GLU A CG  
755  C  CD  A GLU A 169 ? 0.3732 0.2584 0.4370 0.0481  0.0451  -0.0517 169 GLU A CD  
756  C  CD  B GLU A 169 ? 0.3483 0.2235 0.4321 0.0480  0.0419  -0.0169 169 GLU A CD  
757  O  OE1 A GLU A 169 ? 0.3100 0.2024 0.3768 0.0545  0.0474  -0.0458 169 GLU A OE1 
758  O  OE1 B GLU A 169 ? 0.4776 0.3423 0.5633 0.0425  0.0407  -0.0188 169 GLU A OE1 
759  O  OE2 A GLU A 169 ? 0.3178 0.2012 0.3764 0.0468  0.0456  -0.0644 169 GLU A OE2 
760  O  OE2 B GLU A 169 ? 0.3296 0.2037 0.4217 0.0551  0.0443  -0.0103 169 GLU A OE2 
761  N  N   . TRP A 170 ? 0.3059 0.2130 0.3474 0.0244  0.0308  -0.0352 170 TRP A N   
762  C  CA  . TRP A 170 ? 0.3065 0.2141 0.3417 0.0178  0.0279  -0.0411 170 TRP A CA  
763  C  C   . TRP A 170 ? 0.3377 0.2580 0.3623 0.0176  0.0275  -0.0462 170 TRP A C   
764  O  O   . TRP A 170 ? 0.4280 0.3487 0.4475 0.0151  0.0267  -0.0556 170 TRP A O   
765  C  CB  . TRP A 170 ? 0.2974 0.2061 0.3324 0.0124  0.0245  -0.0324 170 TRP A CB  
766  C  CG  . TRP A 170 ? 0.2875 0.1952 0.3190 0.0057  0.0216  -0.0370 170 TRP A CG  
767  C  CD1 . TRP A 170 ? 0.3210 0.2248 0.3514 0.0033  0.0212  -0.0482 170 TRP A CD1 
768  C  CD2 . TRP A 170 ? 0.2240 0.1355 0.2534 0.0006  0.0185  -0.0308 170 TRP A CD2 
769  N  NE1 . TRP A 170 ? 0.2910 0.1967 0.3191 -0.0032 0.0178  -0.0488 170 TRP A NE1 
770  C  CE2 . TRP A 170 ? 0.2959 0.2060 0.3236 -0.0048 0.0164  -0.0380 170 TRP A CE2 
771  C  CE3 . TRP A 170 ? 0.2166 0.1331 0.2456 0.0001  0.0173  -0.0203 170 TRP A CE3 
772  C  CZ2 . TRP A 170 ? 0.2517 0.1654 0.2776 -0.0101 0.0134  -0.0343 170 TRP A CZ2 
773  C  CZ3 . TRP A 170 ? 0.2337 0.1531 0.2603 -0.0050 0.0146  -0.0174 170 TRP A CZ3 
774  C  CH2 . TRP A 170 ? 0.2525 0.1706 0.2779 -0.0100 0.0128  -0.0240 170 TRP A CH2 
775  N  N   . GLY A 171 ? 0.3092 0.2406 0.3309 0.0202  0.0282  -0.0399 171 GLY A N   
776  C  CA  . GLY A 171 ? 0.3941 0.3379 0.4069 0.0205  0.0286  -0.0430 171 GLY A CA  
777  C  C   . GLY A 171 ? 0.3143 0.2656 0.3204 0.0150  0.0251  -0.0391 171 GLY A C   
778  O  O   . GLY A 171 ? 0.3775 0.3365 0.3757 0.0139  0.0247  -0.0435 171 GLY A O   
779  N  N   . LEU A 172 ? 0.2929 0.2429 0.3016 0.0122  0.0227  -0.0307 172 LEU A N   
780  C  CA  . LEU A 172 ? 0.2203 0.1780 0.2235 0.0080  0.0199  -0.0264 172 LEU A CA  
781  C  C   . LEU A 172 ? 0.2581 0.2276 0.2575 0.0101  0.0214  -0.0235 172 LEU A C   
782  O  O   . LEU A 172 ? 0.2542 0.2268 0.2571 0.0143  0.0240  -0.0216 172 LEU A O   
783  C  CB  . LEU A 172 ? 0.2072 0.1621 0.2143 0.0056  0.0177  -0.0182 172 LEU A CB  
784  C  CG  . LEU A 172 ? 0.2484 0.1933 0.2597 0.0028  0.0163  -0.0184 172 LEU A CG  
785  C  CD1 . LEU A 172 ? 0.2049 0.1506 0.2183 0.0013  0.0145  -0.0096 172 LEU A CD1 
786  C  CD2 . LEU A 172 ? 0.2262 0.1705 0.2332 -0.0017 0.0144  -0.0245 172 LEU A CD2 
787  N  N   . ASP A 173 ? 0.1821 0.1585 0.1753 0.0070  0.0197  -0.0223 173 ASP A N   
788  C  CA  . ASP A 173 ? 0.1900 0.1770 0.1810 0.0080  0.0209  -0.0176 173 ASP A CA  
789  C  C   . ASP A 173 ? 0.1648 0.1532 0.1589 0.0056  0.0188  -0.0095 173 ASP A C   
790  O  O   . ASP A 173 ? 0.1638 0.1591 0.1600 0.0066  0.0200  -0.0049 173 ASP A O   
791  C  CB  . ASP A 173 ? 0.1923 0.1867 0.1752 0.0067  0.0207  -0.0202 173 ASP A CB  
792  C  CG  . ASP A 173 ? 0.3179 0.3127 0.2966 0.0092  0.0225  -0.0294 173 ASP A CG  
793  O  OD1 . ASP A 173 ? 0.3078 0.3057 0.2878 0.0138  0.0262  -0.0312 173 ASP A OD1 
794  O  OD2 . ASP A 173 ? 0.2610 0.2534 0.2360 0.0068  0.0203  -0.0352 173 ASP A OD2 
795  N  N   . TYR A 174 ? 0.1361 0.1185 0.1308 0.0023  0.0159  -0.0081 174 TYR A N   
796  C  CA  . TYR A 174 ? 0.1238 0.1074 0.1205 0.0000  0.0136  -0.0017 174 TYR A CA  
797  C  C   . TYR A 174 ? 0.1456 0.1213 0.1452 -0.0012 0.0118  -0.0009 174 TYR A C   
798  O  O   . TYR A 174 ? 0.1449 0.1157 0.1429 -0.0031 0.0110  -0.0043 174 TYR A O   
799  C  CB  . TYR A 174 ? 0.1290 0.1168 0.1209 -0.0030 0.0121  -0.0003 174 TYR A CB  
800  C  CG  . TYR A 174 ? 0.1193 0.1088 0.1130 -0.0051 0.0102  0.0051  174 TYR A CG  
801  C  CD1 . TYR A 174 ? 0.1173 0.1133 0.1113 -0.0054 0.0110  0.0086  174 TYR A CD1 
802  C  CD2 . TYR A 174 ? 0.1287 0.1136 0.1237 -0.0070 0.0079  0.0067  174 TYR A CD2 
803  C  CE1 . TYR A 174 ? 0.1219 0.1184 0.1182 -0.0076 0.0092  0.0124  174 TYR A CE1 
804  C  CE2 . TYR A 174 ? 0.1184 0.1050 0.1144 -0.0086 0.0062  0.0104  174 TYR A CE2 
805  C  CZ  . TYR A 174 ? 0.1188 0.1107 0.1157 -0.0090 0.0067  0.0127  174 TYR A CZ  
806  O  OH  . TYR A 174 ? 0.1438 0.1361 0.1423 -0.0109 0.0050  0.0153  174 TYR A OH  
807  N  N   . VAL A 175 ? 0.1207 0.0961 0.1247 -0.0002 0.0112  0.0038  175 VAL A N   
808  C  CA  . VAL A 175 ? 0.1421 0.1115 0.1486 -0.0010 0.0099  0.0060  175 VAL A CA  
809  C  C   . VAL A 175 ? 0.1392 0.1123 0.1451 -0.0029 0.0075  0.0108  175 VAL A C   
810  O  O   . VAL A 175 ? 0.1301 0.1091 0.1371 -0.0023 0.0070  0.0131  175 VAL A O   
811  C  CB  . VAL A 175 ? 0.1506 0.1159 0.1630 0.0029  0.0115  0.0072  175 VAL A CB  
812  C  CG1 . VAL A 175 ? 0.1331 0.1054 0.1489 0.0058  0.0117  0.0114  175 VAL A CG1 
813  C  CG2 . VAL A 175 ? 0.1680 0.1264 0.1831 0.0019  0.0107  0.0101  175 VAL A CG2 
814  N  N   . VAL A 176 ? 0.1478 0.1178 0.1524 -0.0053 0.0060  0.0117  176 VAL A N   
815  C  CA  . VAL A 176 ? 0.1229 0.0958 0.1268 -0.0064 0.0039  0.0155  176 VAL A CA  
816  C  C   . VAL A 176 ? 0.1484 0.1189 0.1555 -0.0047 0.0040  0.0194  176 VAL A C   
817  O  O   . VAL A 176 ? 0.1659 0.1309 0.1743 -0.0054 0.0047  0.0196  176 VAL A O   
818  C  CB  . VAL A 176 ? 0.1346 0.1073 0.1348 -0.0096 0.0027  0.0147  176 VAL A CB  
819  C  CG1 . VAL A 176 ? 0.1790 0.1548 0.1783 -0.0101 0.0009  0.0178  176 VAL A CG1 
820  C  CG2 . VAL A 176 ? 0.1297 0.1052 0.1269 -0.0109 0.0027  0.0120  176 VAL A CG2 
821  N  N   . LEU A 177 ? 0.1162 0.0914 0.1253 -0.0024 0.0032  0.0227  177 LEU A N   
822  C  CA  . LEU A 177 ? 0.1231 0.0985 0.1347 -0.0001 0.0029  0.0277  177 LEU A CA  
823  C  C   . LEU A 177 ? 0.1517 0.1314 0.1595 -0.0018 0.0007  0.0298  177 LEU A C   
824  O  O   . LEU A 177 ? 0.1729 0.1584 0.1786 -0.0028 -0.0012 0.0285  177 LEU A O   
825  C  CB  . LEU A 177 ? 0.1466 0.1273 0.1621 0.0036  0.0027  0.0302  177 LEU A CB  
826  C  CG  . LEU A 177 ? 0.1517 0.1290 0.1714 0.0063  0.0054  0.0281  177 LEU A CG  
827  C  CD1 . LEU A 177 ? 0.1731 0.1579 0.1974 0.0100  0.0051  0.0307  177 LEU A CD1 
828  C  CD2 . LEU A 177 ? 0.1932 0.1612 0.2162 0.0078  0.0076  0.0289  177 LEU A CD2 
829  N  N   . THR A 178 ? 0.1451 0.1221 0.1525 -0.0023 0.0012  0.0328  178 THR A N   
830  C  CA  . THR A 178 ? 0.1537 0.1356 0.1570 -0.0035 -0.0004 0.0341  178 THR A CA  
831  C  C   . THR A 178 ? 0.1852 0.1699 0.1891 -0.0011 -0.0002 0.0406  178 THR A C   
832  O  O   . THR A 178 ? 0.1889 0.1696 0.1973 0.0009  0.0015  0.0446  178 THR A O   
833  C  CB  . THR A 178 ? 0.2575 0.2361 0.2585 -0.0068 0.0002  0.0315  178 THR A CB  
834  O  OG1 . THR A 178 ? 0.3386 0.3227 0.3355 -0.0075 -0.0012 0.0318  178 THR A OG1 
835  C  CG2 . THR A 178 ? 0.1873 0.1599 0.1916 -0.0076 0.0022  0.0338  178 THR A CG2 
836  N  N   . SER A 179 ? 0.1704 0.1626 0.1699 -0.0008 -0.0020 0.0418  179 SER A N   
837  C  CA  . SER A 179 ? 0.1796 0.1766 0.1785 0.0018  -0.0018 0.0485  179 SER A CA  
838  C  C   . SER A 179 ? 0.1827 0.1859 0.1756 0.0009  -0.0026 0.0481  179 SER A C   
839  O  O   . SER A 179 ? 0.1749 0.1797 0.1645 -0.0010 -0.0041 0.0423  179 SER A O   
840  C  CB  . SER A 179 ? 0.2968 0.3008 0.2969 0.0055  -0.0035 0.0516  179 SER A CB  
841  O  OG  . SER A 179 ? 0.2705 0.2816 0.2675 0.0047  -0.0067 0.0466  179 SER A OG  
842  N  N   . VAL A 180 ? 0.1654 0.1719 0.1574 0.0026  -0.0013 0.0547  180 VAL A N   
843  C  CA  . VAL A 180 ? 0.1718 0.1851 0.1579 0.0024  -0.0013 0.0549  180 VAL A CA  
844  C  C   . VAL A 180 ? 0.2290 0.2541 0.2097 0.0054  -0.0041 0.0553  180 VAL A C   
845  O  O   . VAL A 180 ? 0.2480 0.2761 0.2304 0.0075  -0.0061 0.0563  180 VAL A O   
846  C  CB  . VAL A 180 ? 0.1537 0.1660 0.1417 0.0024  0.0020  0.0623  180 VAL A CB  
847  C  CG1 . VAL A 180 ? 0.2179 0.2187 0.2126 -0.0010 0.0043  0.0614  180 VAL A CG1 
848  C  CG2 . VAL A 180 ? 0.1773 0.1941 0.1667 0.0064  0.0028  0.0715  180 VAL A CG2 
849  N  N   . ASP A 181 ? 0.1805 0.2132 0.1548 0.0060  -0.0044 0.0542  181 ASP A N   
850  C  CA  . ASP A 181 ? 0.1854 0.2306 0.1537 0.0089  -0.0073 0.0537  181 ASP A CA  
851  C  C   . ASP A 181 ? 0.2598 0.3116 0.2284 0.0129  -0.0064 0.0640  181 ASP A C   
852  O  O   . ASP A 181 ? 0.2453 0.2985 0.2133 0.0140  -0.0032 0.0712  181 ASP A O   
853  C  CB  . ASP A 181 ? 0.2007 0.2523 0.1619 0.0089  -0.0074 0.0494  181 ASP A CB  
854  C  CG  . ASP A 181 ? 0.4052 0.4698 0.3595 0.0116  -0.0109 0.0464  181 ASP A CG  
855  O  OD1 . ASP A 181 ? 0.4828 0.5476 0.4367 0.0100  -0.0143 0.0378  181 ASP A OD1 
856  O  OD2 . ASP A 181 ? 0.4465 0.5216 0.3965 0.0151  -0.0105 0.0528  181 ASP A OD2 
857  N  N   . ARG A 182 ? 0.2393 0.2951 0.2099 0.0151  -0.0090 0.0656  182 ARG A N   
858  C  CA  . ARG A 182 ? 0.2784 0.3412 0.2499 0.0196  -0.0085 0.0760  182 ARG A CA  
859  C  C   . ARG A 182 ? 0.2864 0.3663 0.2500 0.0227  -0.0125 0.0749  182 ARG A C   
860  O  O   . ARG A 182 ? 0.3823 0.4688 0.3466 0.0240  -0.0164 0.0728  182 ARG A O   
861  C  CB  . ARG A 182 ? 0.2577 0.3140 0.2379 0.0208  -0.0085 0.0790  182 ARG A CB  
862  C  CG  . ARG A 182 ? 0.2688 0.3087 0.2567 0.0183  -0.0045 0.0801  182 ARG A CG  
863  C  CD  . ARG A 182 ? 0.2688 0.3059 0.2588 0.0195  -0.0003 0.0901  182 ARG A CD  
864  N  NE  . ARG A 182 ? 0.2783 0.3236 0.2695 0.0246  -0.0003 0.0995  182 ARG A NE  
865  C  CZ  . ARG A 182 ? 0.2593 0.2975 0.2591 0.0264  0.0025  0.1052  182 ARG A CZ  
866  N  NH1 . ARG A 182 ? 0.3114 0.3346 0.3190 0.0241  0.0052  0.1046  182 ARG A NH1 
867  N  NH2 . ARG A 182 ? 0.2619 0.3086 0.2628 0.0306  0.0026  0.1115  182 ARG A NH2 
868  N  N   . ASP A 183 ? 0.3914 0.4794 0.3472 0.0239  -0.0114 0.0763  183 ASP A N   
869  C  CA  . ASP A 183 ? 0.4940 0.5983 0.4417 0.0267  -0.0147 0.0735  183 ASP A CA  
870  C  C   . ASP A 183 ? 0.4267 0.5387 0.3773 0.0306  -0.0150 0.0805  183 ASP A C   
871  O  O   . ASP A 183 ? 0.5176 0.6424 0.4641 0.0325  -0.0189 0.0770  183 ASP A O   
872  C  CB  . ASP A 183 ? 0.4722 0.5814 0.4129 0.0270  -0.0121 0.0718  183 ASP A CB  
873  C  CG  . ASP A 183 ? 0.5265 0.6348 0.4708 0.0287  -0.0067 0.0821  183 ASP A CG  
874  O  OD1 . ASP A 183 ? 0.5450 0.6628 0.4841 0.0306  -0.0051 0.0826  183 ASP A OD1 
875  O  OD2 . ASP A 183 ? 0.5861 0.6843 0.5390 0.0281  -0.0040 0.0893  183 ASP A OD2 
876  N  N   . ASP A 184 ? 0.4105 0.5151 0.3687 0.0318  -0.0110 0.0901  184 ASP A N   
877  C  CA  . ASP A 184 ? 0.4287 0.5403 0.3903 0.0360  -0.0107 0.0977  184 ASP A CA  
878  C  C   . ASP A 184 ? 0.3668 0.4824 0.3316 0.0373  -0.0151 0.0959  184 ASP A C   
879  O  O   . ASP A 184 ? 0.4459 0.5712 0.4118 0.0410  -0.0161 0.1005  184 ASP A O   
880  C  CB  . ASP A 184 ? 0.4200 0.5208 0.3904 0.0365  -0.0054 0.1074  184 ASP A CB  
881  C  CG  . ASP A 184 ? 0.2907 0.3745 0.2686 0.0335  -0.0040 0.1064  184 ASP A CG  
882  O  OD1 . ASP A 184 ? 0.3833 0.4606 0.3587 0.0297  -0.0041 0.1003  184 ASP A OD1 
883  O  OD2 . ASP A 184 ? 0.4631 0.5403 0.4495 0.0352  -0.0026 0.1115  184 ASP A OD2 
884  N  N   . MET A 185 ? 0.2793 0.3885 0.2461 0.0345  -0.0177 0.0896  185 MET A N   
885  C  CA  . MET A 185 ? 0.3344 0.4486 0.3060 0.0360  -0.0215 0.0888  185 MET A CA  
886  C  C   . MET A 185 ? 0.2515 0.3763 0.2181 0.0339  -0.0276 0.0783  185 MET A C   
887  O  O   . MET A 185 ? 0.3090 0.4308 0.2713 0.0303  -0.0288 0.0707  185 MET A O   
888  C  CB  . MET A 185 ? 0.3182 0.4185 0.2989 0.0351  -0.0199 0.0906  185 MET A CB  
889  C  CG  . MET A 185 ? 0.4614 0.5518 0.4491 0.0375  -0.0145 0.0999  185 MET A CG  
890  S  SD  . MET A 185 ? 0.6628 0.7366 0.6610 0.0367  -0.0124 0.1002  185 MET A SD  
891  C  CE  . MET A 185 ? 0.2319 0.2938 0.2264 0.0301  -0.0106 0.0916  185 MET A CE  
892  N  N   . PRO A 186 ? 0.3549 0.4923 0.3227 0.0360  -0.0315 0.0775  186 PRO A N   
893  C  CA  . PRO A 186 ? 0.3638 0.5116 0.3279 0.0333  -0.0375 0.0664  186 PRO A CA  
894  C  C   . PRO A 186 ? 0.3158 0.4570 0.2841 0.0287  -0.0399 0.0590  186 PRO A C   
895  O  O   . PRO A 186 ? 0.4698 0.6117 0.4342 0.0246  -0.0424 0.0482  186 PRO A O   
896  C  CB  . PRO A 186 ? 0.2949 0.4556 0.2627 0.0362  -0.0407 0.0688  186 PRO A CB  
897  C  CG  . PRO A 186 ? 0.4558 0.6107 0.4309 0.0404  -0.0364 0.0808  186 PRO A CG  
898  C  CD  . PRO A 186 ? 0.3689 0.5117 0.3417 0.0406  -0.0306 0.0863  186 PRO A CD  
899  N  N   . ASP A 187 ? 0.3020 0.4320 0.2798 0.0282  -0.0373 0.0622  187 ASP A N   
900  C  CA  . ASP A 187 ? 0.2866 0.4050 0.2703 0.0227  -0.0369 0.0535  187 ASP A CA  
901  C  C   . ASP A 187 ? 0.2164 0.3168 0.1999 0.0202  -0.0314 0.0529  187 ASP A C   
902  O  O   . ASP A 187 ? 0.2470 0.3368 0.2359 0.0165  -0.0301 0.0481  187 ASP A O   
903  C  CB  . ASP A 187 ? 0.2809 0.4000 0.2751 0.0236  -0.0375 0.0558  187 ASP A CB  
904  C  CG  . ASP A 187 ? 0.3226 0.4317 0.3223 0.0273  -0.0324 0.0651  187 ASP A CG  
905  O  OD1 . ASP A 187 ? 0.3069 0.4101 0.3028 0.0295  -0.0289 0.0713  187 ASP A OD1 
906  O  OD2 . ASP A 187 ? 0.2664 0.3732 0.2748 0.0281  -0.0317 0.0660  187 ASP A OD2 
907  N  N   . GLY A 188 ? 0.2317 0.3294 0.2096 0.0220  -0.0283 0.0581  188 GLY A N   
908  C  CA  . GLY A 188 ? 0.2513 0.3335 0.2293 0.0193  -0.0237 0.0573  188 GLY A CA  
909  C  C   . GLY A 188 ? 0.2452 0.3145 0.2316 0.0192  -0.0200 0.0610  188 GLY A C   
910  O  O   . GLY A 188 ? 0.2288 0.2856 0.2163 0.0161  -0.0169 0.0583  188 GLY A O   
911  N  N   . GLY A 189 ? 0.1956 0.2680 0.1880 0.0227  -0.0204 0.0666  189 GLY A N   
912  C  CA  . GLY A 189 ? 0.2295 0.2898 0.2299 0.0231  -0.0169 0.0688  189 GLY A CA  
913  C  C   . GLY A 189 ? 0.2032 0.2615 0.2091 0.0207  -0.0180 0.0620  189 GLY A C   
914  O  O   . GLY A 189 ? 0.1963 0.2449 0.2081 0.0210  -0.0149 0.0625  189 GLY A O   
915  N  N   . ALA A 190 ? 0.1766 0.2444 0.1811 0.0185  -0.0222 0.0560  190 ALA A N   
916  C  CA  . ALA A 190 ? 0.1870 0.2528 0.1972 0.0154  -0.0228 0.0499  190 ALA A CA  
917  C  C   . ALA A 190 ? 0.2124 0.2797 0.2312 0.0190  -0.0217 0.0542  190 ALA A C   
918  O  O   . ALA A 190 ? 0.1865 0.2466 0.2102 0.0176  -0.0192 0.0515  190 ALA A O   
919  C  CB  . ALA A 190 ? 0.1791 0.2555 0.1879 0.0123  -0.0278 0.0432  190 ALA A CB  
920  N  N   . GLU A 191 ? 0.1833 0.2609 0.2041 0.0241  -0.0234 0.0610  191 GLU A N   
921  C  CA  . GLU A 191 ? 0.1686 0.2481 0.1985 0.0281  -0.0221 0.0650  191 GLU A CA  
922  C  C   . GLU A 191 ? 0.1649 0.2292 0.1979 0.0304  -0.0164 0.0682  191 GLU A C   
923  O  O   . GLU A 191 ? 0.1887 0.2486 0.2283 0.0313  -0.0140 0.0669  191 GLU A O   
924  C  CB  . GLU A 191 ? 0.2442 0.3390 0.2761 0.0337  -0.0253 0.0724  191 GLU A CB  
925  C  CG  . GLU A 191 ? 0.2941 0.3916 0.3367 0.0386  -0.0238 0.0768  191 GLU A CG  
926  C  CD  . GLU A 191 ? 0.4740 0.5729 0.5228 0.0350  -0.0240 0.0698  191 GLU A CD  
927  O  OE1 . GLU A 191 ? 0.5495 0.6618 0.5996 0.0323  -0.0287 0.0661  191 GLU A OE1 
928  O  OE2 . GLU A 191 ? 0.4642 0.5513 0.5168 0.0348  -0.0194 0.0678  191 GLU A OE2 
929  N  N   . HIS A 192 ? 0.1509 0.2073 0.1795 0.0309  -0.0142 0.0720  192 HIS A N   
930  C  CA  . HIS A 192 ? 0.1754 0.2166 0.2073 0.0322  -0.0091 0.0743  192 HIS A CA  
931  C  C   . HIS A 192 ? 0.1933 0.2238 0.2250 0.0275  -0.0070 0.0658  192 HIS A C   
932  O  O   . HIS A 192 ? 0.1956 0.2178 0.2326 0.0290  -0.0037 0.0646  192 HIS A O   
933  C  CB  . HIS A 192 ? 0.1772 0.2141 0.2047 0.0326  -0.0077 0.0799  192 HIS A CB  
934  C  CG  . HIS A 192 ? 0.1926 0.2141 0.2246 0.0335  -0.0029 0.0828  192 HIS A CG  
935  N  ND1 . HIS A 192 ? 0.2721 0.2909 0.3105 0.0390  -0.0005 0.0919  192 HIS A ND1 
936  C  CD2 . HIS A 192 ? 0.2237 0.2320 0.2552 0.0294  -0.0001 0.0778  192 HIS A CD2 
937  C  CE1 . HIS A 192 ? 0.2856 0.2890 0.3277 0.0378  0.0036  0.0917  192 HIS A CE1 
938  N  NE2 . HIS A 192 ? 0.2439 0.2413 0.2816 0.0319  0.0037  0.0829  192 HIS A NE2 
939  N  N   . ILE A 193 ? 0.1495 0.1808 0.1750 0.0223  -0.0089 0.0598  193 ILE A N   
940  C  CA  . ILE A 193 ? 0.1534 0.1765 0.1783 0.0180  -0.0072 0.0525  193 ILE A CA  
941  C  C   . ILE A 193 ? 0.1511 0.1784 0.1819 0.0187  -0.0071 0.0499  193 ILE A C   
942  O  O   . ILE A 193 ? 0.1570 0.1771 0.1907 0.0190  -0.0038 0.0475  193 ILE A O   
943  C  CB  . ILE A 193 ? 0.1483 0.1727 0.1665 0.0130  -0.0094 0.0475  193 ILE A CB  
944  C  CG1 . ILE A 193 ? 0.1871 0.2074 0.2000 0.0125  -0.0086 0.0501  193 ILE A CG1 
945  C  CG2 . ILE A 193 ? 0.1518 0.1699 0.1701 0.0091  -0.0079 0.0411  193 ILE A CG2 
946  C  CD1 . ILE A 193 ? 0.2205 0.2454 0.2267 0.0093  -0.0111 0.0465  193 ILE A CD1 
947  N  N   . ALA A 194 ? 0.1545 0.1946 0.1874 0.0189  -0.0107 0.0501  194 ALA A N   
948  C  CA  . ALA A 194 ? 0.1425 0.1883 0.1820 0.0190  -0.0106 0.0480  194 ALA A CA  
949  C  C   . ALA A 194 ? 0.1416 0.1855 0.1880 0.0247  -0.0072 0.0518  194 ALA A C   
950  O  O   . ALA A 194 ? 0.1518 0.1944 0.2024 0.0249  -0.0046 0.0491  194 ALA A O   
951  C  CB  . ALA A 194 ? 0.1747 0.2357 0.2165 0.0181  -0.0155 0.0480  194 ALA A CB  
952  N  N   . LYS A 195 ? 0.1590 0.2030 0.2069 0.0297  -0.0070 0.0583  195 LYS A N   
953  C  CA  . LYS A 195 ? 0.1677 0.2080 0.2228 0.0357  -0.0034 0.0619  195 LYS A CA  
954  C  C   . LYS A 195 ? 0.1450 0.1699 0.1994 0.0350  0.0014  0.0575  195 LYS A C   
955  O  O   . LYS A 195 ? 0.1597 0.1822 0.2198 0.0383  0.0047  0.0561  195 LYS A O   
956  C  CB  . LYS A 195 ? 0.1933 0.2351 0.2499 0.0410  -0.0038 0.0706  195 LYS A CB  
957  C  CG  . LYS A 195 ? 0.3161 0.3572 0.3819 0.0485  -0.0010 0.0760  195 LYS A CG  
958  C  CD  . LYS A 195 ? 0.2991 0.3457 0.3662 0.0537  -0.0025 0.0863  195 LYS A CD  
959  C  CE  . LYS A 195 ? 0.4489 0.4988 0.5263 0.0619  -0.0006 0.0928  195 LYS A CE  
960  N  NZ  . LYS A 195 ? 0.4362 0.4883 0.5152 0.0674  -0.0010 0.1040  195 LYS A NZ  
961  N  N   . THR A 196 ? 0.1375 0.1527 0.1854 0.0310  0.0018  0.0553  196 THR A N   
962  C  CA  . THR A 196 ? 0.1366 0.1383 0.1837 0.0297  0.0056  0.0505  196 THR A CA  
963  C  C   . THR A 196 ? 0.1555 0.1588 0.2015 0.0270  0.0065  0.0437  196 THR A C   
964  O  O   . THR A 196 ? 0.1514 0.1494 0.1999 0.0290  0.0100  0.0403  196 THR A O   
965  C  CB  . THR A 196 ? 0.1772 0.1708 0.2181 0.0255  0.0053  0.0498  196 THR A CB  
966  O  OG1 . THR A 196 ? 0.1544 0.1484 0.1962 0.0279  0.0046  0.0573  196 THR A OG1 
967  C  CG2 . THR A 196 ? 0.1844 0.1648 0.2254 0.0242  0.0087  0.0448  196 THR A CG2 
968  N  N   . VAL A 197 ? 0.1390 0.1497 0.1813 0.0226  0.0036  0.0417  197 VAL A N   
969  C  CA  . VAL A 197 ? 0.1420 0.1554 0.1841 0.0200  0.0047  0.0368  197 VAL A CA  
970  C  C   . VAL A 197 ? 0.1299 0.1501 0.1796 0.0244  0.0067  0.0377  197 VAL A C   
971  O  O   . VAL A 197 ? 0.1500 0.1682 0.2005 0.0252  0.0102  0.0342  197 VAL A O   
972  C  CB  . VAL A 197 ? 0.1351 0.1556 0.1744 0.0149  0.0010  0.0356  197 VAL A CB  
973  C  CG1 . VAL A 197 ? 0.1503 0.1742 0.1911 0.0124  0.0025  0.0322  197 VAL A CG1 
974  C  CG2 . VAL A 197 ? 0.1312 0.1454 0.1633 0.0112  -0.0004 0.0343  197 VAL A CG2 
975  N  N   . SER A 198 ? 0.1248 0.1543 0.1800 0.0276  0.0047  0.0426  198 SER A N   
976  C  CA  . SER A 198 ? 0.1630 0.2016 0.2266 0.0318  0.0063  0.0441  198 SER A CA  
977  C  C   . SER A 198 ? 0.1796 0.2102 0.2465 0.0376  0.0112  0.0435  198 SER A C   
978  O  O   . SER A 198 ? 0.1548 0.1881 0.2251 0.0396  0.0145  0.0409  198 SER A O   
979  C  CB  . SER A 198 ? 0.2014 0.2523 0.2701 0.0343  0.0025  0.0498  198 SER A CB  
980  O  OG  . SER A 198 ? 0.2575 0.3167 0.3240 0.0287  -0.0021 0.0487  198 SER A OG  
981  N  N   . TYR A 199 ? 0.1612 0.1818 0.2276 0.0405  0.0119  0.0459  199 TYR A N   
982  C  CA  . TYR A 199 ? 0.1908 0.2013 0.2607 0.0456  0.0167  0.0440  199 TYR A CA  
983  C  C   . TYR A 199 ? 0.1717 0.1747 0.2364 0.0427  0.0196  0.0359  199 TYR A C   
984  O  O   . TYR A 199 ? 0.1969 0.1982 0.2647 0.0467  0.0237  0.0322  199 TYR A O   
985  C  CB  . TYR A 199 ? 0.1669 0.1660 0.2374 0.0477  0.0170  0.0478  199 TYR A CB  
986  C  CG  . TYR A 199 ? 0.1986 0.2029 0.2763 0.0538  0.0161  0.0567  199 TYR A CG  
987  C  CD1 . TYR A 199 ? 0.2002 0.2107 0.2867 0.0608  0.0182  0.0590  199 TYR A CD1 
988  C  CD2 . TYR A 199 ? 0.2125 0.2159 0.2882 0.0532  0.0135  0.0632  199 TYR A CD2 
989  C  CE1 . TYR A 199 ? 0.2284 0.2444 0.3218 0.0670  0.0173  0.0680  199 TYR A CE1 
990  C  CE2 . TYR A 199 ? 0.1955 0.2045 0.2773 0.0593  0.0127  0.0723  199 TYR A CE2 
991  C  CZ  . TYR A 199 ? 0.2419 0.2571 0.3326 0.0661  0.0145  0.0748  199 TYR A CZ  
992  O  OH  . TYR A 199 ? 0.3261 0.3481 0.4232 0.0727  0.0135  0.0847  199 TYR A OH  
993  N  N   . LEU A 200 ? 0.1492 0.1480 0.2060 0.0363  0.0178  0.0329  200 LEU A N   
994  C  CA  . LEU A 200 ? 0.1562 0.1487 0.2075 0.0337  0.0201  0.0256  200 LEU A CA  
995  C  C   . LEU A 200 ? 0.1803 0.1828 0.2319 0.0337  0.0218  0.0231  200 LEU A C   
996  O  O   . LEU A 200 ? 0.1964 0.1969 0.2472 0.0359  0.0255  0.0180  200 LEU A O   
997  C  CB  . LEU A 200 ? 0.1702 0.1578 0.2137 0.0272  0.0174  0.0241  200 LEU A CB  
998  C  CG  . LEU A 200 ? 0.2207 0.2026 0.2582 0.0242  0.0190  0.0170  200 LEU A CG  
999  C  CD1 . LEU A 200 ? 0.2788 0.2516 0.3183 0.0279  0.0226  0.0119  200 LEU A CD1 
1000 C  CD2 . LEU A 200 ? 0.2559 0.2327 0.2874 0.0186  0.0162  0.0167  200 LEU A CD2 
1001 N  N   . LYS A 201 ? 0.1500 0.1639 0.2031 0.0311  0.0192  0.0266  201 LYS A N   
1002 C  CA  . LYS A 201 ? 0.1770 0.2010 0.2316 0.0303  0.0210  0.0254  201 LYS A CA  
1003 C  C   . LYS A 201 ? 0.1543 0.1848 0.2167 0.0369  0.0246  0.0263  201 LYS A C   
1004 O  O   . LYS A 201 ? 0.1971 0.2334 0.2599 0.0379  0.0281  0.0240  201 LYS A O   
1005 C  CB  . LYS A 201 ? 0.1508 0.1843 0.2068 0.0255  0.0172  0.0288  201 LYS A CB  
1006 C  CG  . LYS A 201 ? 0.1653 0.1939 0.2138 0.0191  0.0148  0.0269  201 LYS A CG  
1007 C  CD  . LYS A 201 ? 0.1409 0.1693 0.1852 0.0173  0.0178  0.0236  201 LYS A CD  
1008 C  CE  . LYS A 201 ? 0.1255 0.1498 0.1634 0.0115  0.0154  0.0226  201 LYS A CE  
1009 N  NZ  . LYS A 201 ? 0.1123 0.1362 0.1454 0.0106  0.0184  0.0200  201 LYS A NZ  
1010 N  N   . GLU A 202 ? 0.1494 0.1799 0.2181 0.0418  0.0241  0.0301  202 GLU A N   
1011 C  CA  . GLU A 202 ? 0.1552 0.1911 0.2320 0.0491  0.0279  0.0309  202 GLU A CA  
1012 C  C   . GLU A 202 ? 0.1942 0.2189 0.2687 0.0532  0.0327  0.0247  202 GLU A C   
1013 O  O   . GLU A 202 ? 0.2381 0.2675 0.3154 0.0576  0.0372  0.0219  202 GLU A O   
1014 C  CB  . GLU A 202 ? 0.2031 0.2423 0.2875 0.0535  0.0256  0.0376  202 GLU A CB  
1015 C  CG  . GLU A 202 ? 0.3221 0.3634 0.4156 0.0624  0.0296  0.0391  202 GLU A CG  
1016 C  CD  . GLU A 202 ? 0.4546 0.5018 0.5559 0.0668  0.0267  0.0473  202 GLU A CD  
1017 O  OE1 . GLU A 202 ? 0.4516 0.5133 0.5615 0.0705  0.0269  0.0509  202 GLU A OE1 
1018 O  OE2 . GLU A 202 ? 0.3997 0.4384 0.4985 0.0664  0.0243  0.0504  202 GLU A OE2 
1019 N  N   . ARG A 203 ? 0.2071 0.2176 0.2764 0.0514  0.0320  0.0219  203 ARG A N   
1020 C  CA  . ARG A 203 ? 0.1888 0.1874 0.2564 0.0546  0.0359  0.0149  203 ARG A CA  
1021 C  C   . ARG A 203 ? 0.1718 0.1714 0.2313 0.0518  0.0380  0.0074  203 ARG A C   
1022 O  O   . ARG A 203 ? 0.2565 0.2551 0.3160 0.0562  0.0424  0.0014  203 ARG A O   
1023 C  CB  . ARG A 203 ? 0.2891 0.2729 0.3551 0.0527  0.0340  0.0151  203 ARG A CB  
1024 C  CG  . ARG A 203 ? 0.4442 0.4148 0.5144 0.0578  0.0375  0.0109  203 ARG A CG  
1025 C  CD  . ARG A 203 ? 0.3073 0.2650 0.3781 0.0552  0.0353  0.0137  203 ARG A CD  
1026 N  NE  . ARG A 203 ? 0.3189 0.2747 0.3990 0.0608  0.0356  0.0217  203 ARG A NE  
1027 C  CZ  . ARG A 203 ? 0.3639 0.3122 0.4523 0.0679  0.0395  0.0208  203 ARG A CZ  
1028 N  NH1 . ARG A 203 ? 0.3682 0.3102 0.4565 0.0704  0.0435  0.0112  203 ARG A NH1 
1029 N  NH2 . ARG A 203 ? 0.3698 0.3173 0.4669 0.0731  0.0395  0.0298  203 ARG A NH2 
1030 N  N   . ASN A 204 ? 0.1787 0.1803 0.2309 0.0448  0.0350  0.0075  204 ASN A N   
1031 C  CA  . ASN A 204 ? 0.2301 0.2345 0.2745 0.0422  0.0367  0.0019  204 ASN A CA  
1032 C  C   . ASN A 204 ? 0.1746 0.1875 0.2159 0.0362  0.0338  0.0062  204 ASN A C   
1033 O  O   . ASN A 204 ? 0.1671 0.1750 0.2034 0.0308  0.0303  0.0067  204 ASN A O   
1034 C  CB  . ASN A 204 ? 0.3315 0.3237 0.3689 0.0401  0.0365  -0.0054 204 ASN A CB  
1035 C  CG  . ASN A 204 ? 0.3106 0.3077 0.3398 0.0391  0.0387  -0.0116 204 ASN A CG  
1036 O  OD1 . ASN A 204 ? 0.3161 0.3255 0.3446 0.0393  0.0404  -0.0091 204 ASN A OD1 
1037 N  ND2 . ASN A 204 ? 0.3302 0.3187 0.3537 0.0381  0.0388  -0.0194 204 ASN A ND2 
1038 N  N   . PRO A 205 ? 0.1979 0.2238 0.2428 0.0369  0.0354  0.0094  205 PRO A N   
1039 C  CA  . PRO A 205 ? 0.1598 0.1933 0.2034 0.0310  0.0332  0.0134  205 PRO A CA  
1040 C  C   . PRO A 205 ? 0.1484 0.1801 0.1827 0.0273  0.0336  0.0102  205 PRO A C   
1041 O  O   . PRO A 205 ? 0.1937 0.2291 0.2268 0.0222  0.0315  0.0136  205 PRO A O   
1042 C  CB  . PRO A 205 ? 0.1824 0.2302 0.2336 0.0334  0.0361  0.0170  205 PRO A CB  
1043 C  CG  . PRO A 205 ? 0.1921 0.2398 0.2435 0.0405  0.0413  0.0123  205 PRO A CG  
1044 C  CD  . PRO A 205 ? 0.2429 0.2774 0.2943 0.0432  0.0399  0.0095  205 PRO A CD  
1045 N  N   . LYS A 206 ? 0.1732 0.1997 0.2013 0.0296  0.0360  0.0037  206 LYS A N   
1046 C  CA  . LYS A 206 ? 0.1733 0.1994 0.1921 0.0262  0.0357  0.0009  206 LYS A CA  
1047 C  C   . LYS A 206 ? 0.1536 0.1702 0.1684 0.0212  0.0311  0.0006  206 LYS A C   
1048 O  O   . LYS A 206 ? 0.1888 0.2064 0.1974 0.0177  0.0300  0.0004  206 LYS A O   
1049 C  CB  . LYS A 206 ? 0.1900 0.2148 0.2028 0.0300  0.0392  -0.0070 206 LYS A CB  
1050 C  CG  . LYS A 206 ? 0.2206 0.2555 0.2364 0.0358  0.0446  -0.0078 206 LYS A CG  
1051 C  CD  . LYS A 206 ? 0.2761 0.3095 0.2845 0.0396  0.0477  -0.0173 206 LYS A CD  
1052 C  CE  . LYS A 206 ? 0.3761 0.4188 0.3876 0.0465  0.0536  -0.0191 206 LYS A CE  
1053 N  NZ  . LYS A 206 ? 0.5341 0.5803 0.5358 0.0495  0.0569  -0.0278 206 LYS A NZ  
1054 N  N   . ILE A 207 ? 0.1361 0.1441 0.1545 0.0213  0.0288  0.0010  207 ILE A N   
1055 C  CA  . ILE A 207 ? 0.1640 0.1635 0.1786 0.0170  0.0250  0.0005  207 ILE A CA  
1056 C  C   . ILE A 207 ? 0.1357 0.1390 0.1513 0.0128  0.0219  0.0064  207 ILE A C   
1057 O  O   . ILE A 207 ? 0.1579 0.1654 0.1796 0.0133  0.0209  0.0109  207 ILE A O   
1058 C  CB  . ILE A 207 ? 0.1478 0.1370 0.1660 0.0186  0.0242  -0.0005 207 ILE A CB  
1059 C  CG1 . ILE A 207 ? 0.2560 0.2396 0.2737 0.0225  0.0273  -0.0078 207 ILE A CG1 
1060 C  CG2 . ILE A 207 ? 0.1957 0.1777 0.2105 0.0139  0.0207  -0.0003 207 ILE A CG2 
1061 C  CD1 . ILE A 207 ? 0.2665 0.2383 0.2892 0.0242  0.0271  -0.0087 207 ILE A CD1 
1062 N  N   . LEU A 208 ? 0.1299 0.1322 0.1399 0.0087  0.0200  0.0061  208 LEU A N   
1063 C  CA  . LEU A 208 ? 0.1147 0.1190 0.1256 0.0048  0.0171  0.0106  208 LEU A CA  
1064 C  C   . LEU A 208 ? 0.1274 0.1250 0.1392 0.0035  0.0140  0.0115  208 LEU A C   
1065 O  O   . LEU A 208 ? 0.1162 0.1064 0.1256 0.0037  0.0137  0.0087  208 LEU A O   
1066 C  CB  . LEU A 208 ? 0.1133 0.1189 0.1185 0.0016  0.0166  0.0105  208 LEU A CB  
1067 C  CG  . LEU A 208 ? 0.1227 0.1367 0.1267 0.0026  0.0198  0.0114  208 LEU A CG  
1068 C  CD1 . LEU A 208 ? 0.1528 0.1679 0.1500 0.0008  0.0196  0.0109  208 LEU A CD1 
1069 C  CD2 . LEU A 208 ? 0.1305 0.1512 0.1415 0.0013  0.0200  0.0170  208 LEU A CD2 
1070 N  N   . VAL A 209 ? 0.1081 0.1087 0.1236 0.0022  0.0117  0.0154  209 VAL A N   
1071 C  CA  . VAL A 209 ? 0.1071 0.1036 0.1232 0.0017  0.0090  0.0170  209 VAL A CA  
1072 C  C   . VAL A 209 ? 0.1094 0.1073 0.1239 -0.0021 0.0060  0.0184  209 VAL A C   
1073 O  O   . VAL A 209 ? 0.1208 0.1246 0.1383 -0.0035 0.0051  0.0200  209 VAL A O   
1074 C  CB  . VAL A 209 ? 0.1081 0.1082 0.1304 0.0051  0.0087  0.0199  209 VAL A CB  
1075 C  CG1 . VAL A 209 ? 0.1657 0.1629 0.1877 0.0050  0.0061  0.0224  209 VAL A CG1 
1076 C  CG2 . VAL A 209 ? 0.1410 0.1387 0.1657 0.0096  0.0121  0.0182  209 VAL A CG2 
1077 N  N   . GLU A 210 ? 0.1129 0.1053 0.1234 -0.0037 0.0046  0.0178  210 GLU A N   
1078 C  CA  . GLU A 210 ? 0.1197 0.1128 0.1285 -0.0064 0.0019  0.0186  210 GLU A CA  
1079 C  C   . GLU A 210 ? 0.1447 0.1368 0.1537 -0.0052 0.0003  0.0206  210 GLU A C   
1080 O  O   . GLU A 210 ? 0.1381 0.1255 0.1468 -0.0037 0.0014  0.0210  210 GLU A O   
1081 C  CB  . GLU A 210 ? 0.1353 0.1245 0.1393 -0.0087 0.0020  0.0169  210 GLU A CB  
1082 C  CG  . GLU A 210 ? 0.1423 0.1311 0.1445 -0.0107 -0.0003 0.0173  210 GLU A CG  
1083 C  CD  . GLU A 210 ? 0.2171 0.2032 0.2154 -0.0124 -0.0001 0.0161  210 GLU A CD  
1084 O  OE1 . GLU A 210 ? 0.1926 0.1792 0.1898 -0.0127 0.0013  0.0153  210 GLU A OE1 
1085 O  OE2 . GLU A 210 ? 0.2361 0.2207 0.2325 -0.0132 -0.0013 0.0162  210 GLU A OE2 
1086 N  N   . CYS A 211 ? 0.1212 0.1179 0.1309 -0.0060 -0.0023 0.0217  211 CYS A N   
1087 C  CA  . CYS A 211 ? 0.1021 0.0995 0.1103 -0.0050 -0.0039 0.0238  211 CYS A CA  
1088 C  C   . CYS A 211 ? 0.1320 0.1285 0.1359 -0.0074 -0.0054 0.0223  211 CYS A C   
1089 O  O   . CYS A 211 ? 0.1563 0.1553 0.1605 -0.0094 -0.0068 0.0202  211 CYS A O   
1090 C  CB  . CYS A 211 ? 0.1306 0.1359 0.1421 -0.0032 -0.0061 0.0259  211 CYS A CB  
1091 S  SG  . CYS A 211 ? 0.1835 0.1907 0.2010 0.0009  -0.0042 0.0286  211 CYS A SG  
1092 N  N   . LEU A 212 ? 0.1327 0.1257 0.1335 -0.0072 -0.0048 0.0234  212 LEU A N   
1093 C  CA  . LEU A 212 ? 0.1088 0.1018 0.1057 -0.0088 -0.0057 0.0224  212 LEU A CA  
1094 C  C   . LEU A 212 ? 0.1329 0.1305 0.1281 -0.0070 -0.0070 0.0252  212 LEU A C   
1095 O  O   . LEU A 212 ? 0.1549 0.1509 0.1504 -0.0054 -0.0057 0.0290  212 LEU A O   
1096 C  CB  . LEU A 212 ? 0.1369 0.1244 0.1322 -0.0101 -0.0040 0.0219  212 LEU A CB  
1097 C  CG  . LEU A 212 ? 0.1536 0.1416 0.1455 -0.0110 -0.0043 0.0216  212 LEU A CG  
1098 C  CD1 . LEU A 212 ? 0.1890 0.1789 0.1799 -0.0121 -0.0057 0.0185  212 LEU A CD1 
1099 C  CD2 . LEU A 212 ? 0.1761 0.1600 0.1679 -0.0124 -0.0028 0.0215  212 LEU A CD2 
1100 N  N   . THR A 213 ? 0.1480 0.1514 0.1415 -0.0071 -0.0094 0.0234  213 THR A N   
1101 C  CA  . THR A 213 ? 0.1514 0.1618 0.1428 -0.0048 -0.0110 0.0260  213 THR A CA  
1102 C  C   . THR A 213 ? 0.1451 0.1591 0.1314 -0.0051 -0.0122 0.0236  213 THR A C   
1103 O  O   . THR A 213 ? 0.1304 0.1417 0.1158 -0.0072 -0.0123 0.0191  213 THR A O   
1104 C  CB  . THR A 213 ? 0.2476 0.2651 0.2422 -0.0039 -0.0136 0.0256  213 THR A CB  
1105 O  OG1 . THR A 213 ? 0.2378 0.2565 0.2336 -0.0067 -0.0155 0.0201  213 THR A OG1 
1106 C  CG2 . THR A 213 ? 0.3158 0.3313 0.3158 -0.0024 -0.0121 0.0285  213 THR A CG2 
1107 N  N   . PRO A 214 ? 0.1692 0.1895 0.1520 -0.0027 -0.0127 0.0268  214 PRO A N   
1108 C  CA  . PRO A 214 ? 0.1409 0.1671 0.1180 -0.0023 -0.0141 0.0237  214 PRO A CA  
1109 C  C   . PRO A 214 ? 0.1642 0.1962 0.1414 -0.0031 -0.0178 0.0177  214 PRO A C   
1110 O  O   . PRO A 214 ? 0.1475 0.1790 0.1299 -0.0044 -0.0192 0.0166  214 PRO A O   
1111 C  CB  . PRO A 214 ? 0.1828 0.2158 0.1564 0.0010  -0.0134 0.0302  214 PRO A CB  
1112 C  CG  . PRO A 214 ? 0.2460 0.2797 0.2243 0.0026  -0.0137 0.0352  214 PRO A CG  
1113 C  CD  . PRO A 214 ? 0.1638 0.1871 0.1479 0.0002  -0.0121 0.0336  214 PRO A CD  
1114 N  N   . ASP A 215 ? 0.1644 0.2024 0.1363 -0.0024 -0.0195 0.0136  215 ASP A N   
1115 C  CA  . ASP A 215 ? 0.1667 0.2089 0.1397 -0.0040 -0.0233 0.0063  215 ASP A CA  
1116 C  C   . ASP A 215 ? 0.1727 0.2269 0.1449 -0.0023 -0.0269 0.0072  215 ASP A C   
1117 O  O   . ASP A 215 ? 0.2048 0.2639 0.1788 -0.0040 -0.0307 0.0007  215 ASP A O   
1118 C  CB  . ASP A 215 ? 0.1911 0.2333 0.1598 -0.0043 -0.0237 -0.0010 215 ASP A CB  
1119 C  CG  . ASP A 215 ? 0.2595 0.3120 0.2195 -0.0008 -0.0241 -0.0008 215 ASP A CG  
1120 O  OD1 . ASP A 215 ? 0.2361 0.2956 0.1931 0.0020  -0.0238 0.0060  215 ASP A OD1 
1121 O  OD2 . ASP A 215 ? 0.2695 0.3230 0.2257 -0.0004 -0.0244 -0.0075 215 ASP A OD2 
1122 N  N   . PHE A 216 ? 0.1677 0.2270 0.1382 0.0011  -0.0260 0.0152  216 PHE A N   
1123 C  CA  . PHE A 216 ? 0.1680 0.2398 0.1379 0.0035  -0.0294 0.0177  216 PHE A CA  
1124 C  C   . PHE A 216 ? 0.2251 0.3088 0.1885 0.0042  -0.0333 0.0113  216 PHE A C   
1125 O  O   . PHE A 216 ? 0.2203 0.3151 0.1845 0.0047  -0.0377 0.0095  216 PHE A O   
1126 C  CB  . PHE A 216 ? 0.1475 0.2195 0.1261 0.0018  -0.0313 0.0173  216 PHE A CB  
1127 C  CG  . PHE A 216 ? 0.1983 0.2604 0.1827 0.0021  -0.0275 0.0233  216 PHE A CG  
1128 C  CD1 . PHE A 216 ? 0.1849 0.2476 0.1693 0.0059  -0.0253 0.0321  216 PHE A CD1 
1129 C  CD2 . PHE A 216 ? 0.2257 0.2786 0.2159 -0.0013 -0.0261 0.0201  216 PHE A CD2 
1130 C  CE1 . PHE A 216 ? 0.2044 0.2576 0.1944 0.0062  -0.0219 0.0362  216 PHE A CE1 
1131 C  CE2 . PHE A 216 ? 0.2423 0.2873 0.2370 -0.0008 -0.0227 0.0245  216 PHE A CE2 
1132 C  CZ  . PHE A 216 ? 0.1780 0.2227 0.1726 0.0029  -0.0207 0.0319  216 PHE A CZ  
1133 N  N   . ARG A 217 ? 0.1978 0.2797 0.1548 0.0045  -0.0317 0.0076  217 ARG A N   
1134 C  CA  A ARG A 217 ? 0.2273 0.3194 0.1773 0.0053  -0.0349 -0.0003 217 ARG A CA  
1135 C  CA  B ARG A 217 ? 0.2280 0.3195 0.1780 0.0052  -0.0348 -0.0005 217 ARG A CA  
1136 C  C   . ARG A 217 ? 0.2538 0.3466 0.2087 0.0014  -0.0395 -0.0107 217 ARG A C   
1137 O  O   . ARG A 217 ? 0.3269 0.4310 0.2776 0.0019  -0.0438 -0.0175 217 ARG A O   
1138 C  CB  A ARG A 217 ? 0.2921 0.4006 0.2351 0.0100  -0.0368 0.0050  217 ARG A CB  
1139 C  CB  B ARG A 217 ? 0.2915 0.3990 0.2336 0.0100  -0.0362 0.0046  217 ARG A CB  
1140 C  CG  A ARG A 217 ? 0.3265 0.4348 0.2654 0.0135  -0.0320 0.0155  217 ARG A CG  
1141 C  CG  B ARG A 217 ? 0.3333 0.4411 0.2693 0.0134  -0.0314 0.0123  217 ARG A CG  
1142 C  CD  A ARG A 217 ? 0.3678 0.4714 0.3017 0.0135  -0.0286 0.0118  217 ARG A CD  
1143 C  CD  B ARG A 217 ? 0.3758 0.4911 0.3113 0.0173  -0.0305 0.0247  217 ARG A CD  
1144 N  NE  A ARG A 217 ? 0.4498 0.5552 0.3803 0.0167  -0.0241 0.0223  217 ARG A NE  
1145 N  NE  B ARG A 217 ? 0.3548 0.4831 0.2903 0.0186  -0.0359 0.0239  217 ARG A NE  
1146 C  CZ  A ARG A 217 ? 0.2749 0.3685 0.2099 0.0153  -0.0195 0.0276  217 ARG A CZ  
1147 C  CZ  B ARG A 217 ? 0.3877 0.5236 0.3248 0.0221  -0.0363 0.0340  217 ARG A CZ  
1148 N  NH1 A ARG A 217 ? 0.4930 0.5884 0.4273 0.0176  -0.0157 0.0382  217 ARG A NH1 
1149 N  NH1 B ARG A 217 ? 0.3884 0.5348 0.3277 0.0229  -0.0410 0.0325  217 ARG A NH1 
1150 N  NH2 A ARG A 217 ? 0.3855 0.4659 0.3264 0.0114  -0.0188 0.0223  217 ARG A NH2 
1151 N  NH2 B ARG A 217 ? 0.4290 0.5601 0.3672 0.0247  -0.0315 0.0456  217 ARG A NH2 
1152 N  N   . GLY A 218 ? 0.2060 0.2873 0.1699 -0.0025 -0.0387 -0.0121 218 GLY A N   
1153 C  CA  . GLY A 218 ? 0.2551 0.3362 0.2257 -0.0068 -0.0425 -0.0207 218 GLY A CA  
1154 C  C   . GLY A 218 ? 0.2993 0.3923 0.2744 -0.0073 -0.0471 -0.0198 218 GLY A C   
1155 O  O   . GLY A 218 ? 0.3538 0.4495 0.3347 -0.0111 -0.0510 -0.0277 218 GLY A O   
1156 N  N   . ASP A 219 ? 0.2225 0.3228 0.1960 -0.0035 -0.0466 -0.0104 219 ASP A N   
1157 C  CA  . ASP A 219 ? 0.2463 0.3591 0.2245 -0.0028 -0.0506 -0.0077 219 ASP A CA  
1158 C  C   . ASP A 219 ? 0.1996 0.3052 0.1898 -0.0069 -0.0502 -0.0080 219 ASP A C   
1159 O  O   . ASP A 219 ? 0.2026 0.2996 0.1968 -0.0062 -0.0460 -0.0010 219 ASP A O   
1160 C  CB  . ASP A 219 ? 0.2086 0.3272 0.1832 0.0029  -0.0487 0.0041  219 ASP A CB  
1161 C  CG  . ASP A 219 ? 0.3021 0.4341 0.2820 0.0048  -0.0524 0.0086  219 ASP A CG  
1162 O  OD1 . ASP A 219 ? 0.3468 0.4830 0.3346 0.0013  -0.0560 0.0035  219 ASP A OD1 
1163 O  OD2 . ASP A 219 ? 0.4383 0.5768 0.4150 0.0101  -0.0514 0.0182  219 ASP A OD2 
1164 N  N   . LEU A 220 ? 0.2250 0.3350 0.2216 -0.0114 -0.0545 -0.0163 220 LEU A N   
1165 C  CA  . LEU A 220 ? 0.2277 0.3312 0.2364 -0.0159 -0.0537 -0.0168 220 LEU A CA  
1166 C  C   . LEU A 220 ? 0.2051 0.3143 0.2200 -0.0136 -0.0529 -0.0080 220 LEU A C   
1167 O  O   . LEU A 220 ? 0.2092 0.3103 0.2316 -0.0154 -0.0496 -0.0050 220 LEU A O   
1168 C  CB  . LEU A 220 ? 0.2804 0.3889 0.2961 -0.0215 -0.0588 -0.0271 220 LEU A CB  
1169 C  CG  . LEU A 220 ? 0.3210 0.4226 0.3332 -0.0243 -0.0596 -0.0376 220 LEU A CG  
1170 C  CD1 . LEU A 220 ? 0.3870 0.4922 0.4094 -0.0306 -0.0644 -0.0473 220 LEU A CD1 
1171 C  CD2 . LEU A 220 ? 0.3239 0.4074 0.3351 -0.0248 -0.0537 -0.0361 220 LEU A CD2 
1172 N  N   . LYS A 221 ? 0.2020 0.3252 0.2138 -0.0092 -0.0557 -0.0036 221 LYS A N   
1173 C  CA  A LYS A 221 ? 0.2170 0.3460 0.2356 -0.0062 -0.0550 0.0048  221 LYS A CA  
1174 C  CA  B LYS A 221 ? 0.2171 0.3460 0.2357 -0.0063 -0.0550 0.0048  221 LYS A CA  
1175 C  C   . LYS A 221 ? 0.2331 0.3501 0.2495 -0.0024 -0.0486 0.0135  221 LYS A C   
1176 O  O   . LYS A 221 ? 0.2222 0.3361 0.2460 -0.0016 -0.0459 0.0182  221 LYS A O   
1177 C  CB  A LYS A 221 ? 0.2547 0.4028 0.2709 -0.0021 -0.0599 0.0078  221 LYS A CB  
1178 C  CB  B LYS A 221 ? 0.2548 0.4029 0.2713 -0.0022 -0.0600 0.0077  221 LYS A CB  
1179 C  CG  A LYS A 221 ? 0.3045 0.4670 0.3242 -0.0061 -0.0671 -0.0013 221 LYS A CG  
1180 C  CG  B LYS A 221 ? 0.3037 0.4666 0.3240 -0.0062 -0.0672 -0.0013 221 LYS A CG  
1181 C  CD  A LYS A 221 ? 0.3153 0.4754 0.3488 -0.0121 -0.0676 -0.0052 221 LYS A CD  
1182 C  CD  B LYS A 221 ? 0.3154 0.4771 0.3498 -0.0121 -0.0680 -0.0051 221 LYS A CD  
1183 C  CE  A LYS A 221 ? 0.3826 0.5604 0.4255 -0.0111 -0.0718 -0.0021 221 LYS A CE  
1184 C  CE  B LYS A 221 ? 0.3564 0.5285 0.4003 -0.0093 -0.0683 0.0028  221 LYS A CE  
1185 N  NZ  A LYS A 221 ? 0.3324 0.5269 0.3715 -0.0112 -0.0789 -0.0079 221 LYS A NZ  
1186 N  NZ  B LYS A 221 ? 0.3366 0.5108 0.3950 -0.0154 -0.0695 -0.0011 221 LYS A NZ  
1187 N  N   . ALA A 222 ? 0.1819 0.2926 0.1885 -0.0001 -0.0462 0.0152  222 ALA A N   
1188 C  CA  . ALA A 222 ? 0.1728 0.2712 0.1779 0.0026  -0.0403 0.0222  222 ALA A CA  
1189 C  C   . ALA A 222 ? 0.1831 0.2672 0.1926 -0.0014 -0.0367 0.0192  222 ALA A C   
1190 O  O   . ALA A 222 ? 0.1639 0.2414 0.1779 -0.0002 -0.0331 0.0237  222 ALA A O   
1191 C  CB  . ALA A 222 ? 0.2214 0.3176 0.2161 0.0051  -0.0387 0.0244  222 ALA A CB  
1192 N  N   . ILE A 223 ? 0.1614 0.2411 0.1697 -0.0058 -0.0376 0.0116  223 ILE A N   
1193 C  CA  . ILE A 223 ? 0.1638 0.2313 0.1764 -0.0095 -0.0345 0.0093  223 ILE A CA  
1194 C  C   . ILE A 223 ? 0.1495 0.2197 0.1724 -0.0110 -0.0343 0.0107  223 ILE A C   
1195 O  O   . ILE A 223 ? 0.1591 0.2216 0.1851 -0.0109 -0.0302 0.0138  223 ILE A O   
1196 C  CB  . ILE A 223 ? 0.1428 0.2067 0.1540 -0.0136 -0.0361 0.0010  223 ILE A CB  
1197 C  CG1 . ILE A 223 ? 0.1917 0.2526 0.1927 -0.0115 -0.0352 0.0001  223 ILE A CG1 
1198 C  CG2 . ILE A 223 ? 0.2016 0.2546 0.2191 -0.0175 -0.0332 -0.0006 223 ILE A CG2 
1199 C  CD1 . ILE A 223 ? 0.1921 0.2535 0.1904 -0.0139 -0.0378 -0.0090 223 ILE A CD1 
1200 N  N   . GLU A 224 ? 0.1418 0.2243 0.1702 -0.0123 -0.0388 0.0084  224 GLU A N   
1201 C  CA  . GLU A 224 ? 0.1414 0.2289 0.1809 -0.0137 -0.0387 0.0101  224 GLU A CA  
1202 C  C   . GLU A 224 ? 0.1506 0.2385 0.1916 -0.0085 -0.0354 0.0180  224 GLU A C   
1203 O  O   . GLU A 224 ? 0.1795 0.2642 0.2269 -0.0089 -0.0320 0.0200  224 GLU A O   
1204 C  CB  . GLU A 224 ? 0.1872 0.2900 0.2323 -0.0158 -0.0448 0.0062  224 GLU A CB  
1205 C  CG  . GLU A 224 ? 0.2464 0.3576 0.3040 -0.0170 -0.0451 0.0085  224 GLU A CG  
1206 C  CD  . GLU A 224 ? 0.3595 0.4880 0.4230 -0.0190 -0.0519 0.0048  224 GLU A CD  
1207 O  OE1 . GLU A 224 ? 0.3519 0.4867 0.4082 -0.0182 -0.0562 0.0011  224 GLU A OE1 
1208 O  OE2 . GLU A 224 ? 0.4012 0.5381 0.4766 -0.0213 -0.0528 0.0055  224 GLU A OE2 
1209 N  N   . LYS A 225 ? 0.1554 0.2470 0.1908 -0.0033 -0.0358 0.0226  225 LYS A N   
1210 C  CA  . LYS A 225 ? 0.1280 0.2187 0.1658 0.0020  -0.0325 0.0300  225 LYS A CA  
1211 C  C   . LYS A 225 ? 0.1551 0.2306 0.1917 0.0019  -0.0267 0.0309  225 LYS A C   
1212 O  O   . LYS A 225 ? 0.1718 0.2455 0.2141 0.0038  -0.0235 0.0336  225 LYS A O   
1213 C  CB  . LYS A 225 ? 0.1898 0.2853 0.2217 0.0073  -0.0336 0.0354  225 LYS A CB  
1214 C  CG  . LYS A 225 ? 0.2975 0.3915 0.3328 0.0133  -0.0303 0.0434  225 LYS A CG  
1215 C  CD  . LYS A 225 ? 0.3991 0.5057 0.4442 0.0158  -0.0320 0.0462  225 LYS A CD  
1216 C  CE  . LYS A 225 ? 0.4147 0.5388 0.4592 0.0178  -0.0379 0.0480  225 LYS A CE  
1217 N  NZ  . LYS A 225 ? 0.4899 0.6159 0.5293 0.0242  -0.0374 0.0561  225 LYS A NZ  
1218 N  N   . VAL A 226 ? 0.1378 0.2033 0.1670 0.0000  -0.0254 0.0285  226 VAL A N   
1219 C  CA  . VAL A 226 ? 0.1304 0.1829 0.1582 -0.0005 -0.0206 0.0287  226 VAL A CA  
1220 C  C   . VAL A 226 ? 0.1208 0.1713 0.1539 -0.0043 -0.0192 0.0255  226 VAL A C   
1221 O  O   . VAL A 226 ? 0.1453 0.1912 0.1810 -0.0032 -0.0154 0.0269  226 VAL A O   
1222 C  CB  . VAL A 226 ? 0.1274 0.1717 0.1467 -0.0015 -0.0198 0.0272  226 VAL A CB  
1223 C  CG1 . VAL A 226 ? 0.1518 0.1841 0.1699 -0.0022 -0.0154 0.0271  226 VAL A CG1 
1224 C  CG2 . VAL A 226 ? 0.1673 0.2145 0.1821 0.0025  -0.0204 0.0318  226 VAL A CG2 
1225 N  N   . ALA A 227 ? 0.1132 0.1670 0.1482 -0.0087 -0.0221 0.0210  227 ALA A N   
1226 C  CA  . ALA A 227 ? 0.1444 0.1956 0.1851 -0.0126 -0.0204 0.0191  227 ALA A CA  
1227 C  C   . ALA A 227 ? 0.1448 0.2039 0.1949 -0.0119 -0.0194 0.0217  227 ALA A C   
1228 O  O   . ALA A 227 ? 0.1663 0.2227 0.2203 -0.0137 -0.0162 0.0221  227 ALA A O   
1229 C  CB  . ALA A 227 ? 0.1373 0.1891 0.1796 -0.0177 -0.0235 0.0137  227 ALA A CB  
1230 N  N   . LEU A 228 ? 0.1292 0.1988 0.1829 -0.0091 -0.0218 0.0239  228 LEU A N   
1231 C  CA  . LEU A 228 ? 0.1240 0.2027 0.1875 -0.0077 -0.0207 0.0267  228 LEU A CA  
1232 C  C   . LEU A 228 ? 0.1252 0.2011 0.1879 -0.0016 -0.0166 0.0312  228 LEU A C   
1233 O  O   . LEU A 228 ? 0.1606 0.2444 0.2312 0.0010  -0.0152 0.0340  228 LEU A O   
1234 C  CB  . LEU A 228 ? 0.1961 0.2898 0.2656 -0.0079 -0.0261 0.0265  228 LEU A CB  
1235 C  CG  . LEU A 228 ? 0.2533 0.3517 0.3277 -0.0147 -0.0301 0.0211  228 LEU A CG  
1236 C  CD1 . LEU A 228 ? 0.2213 0.3363 0.3015 -0.0147 -0.0360 0.0203  228 LEU A CD1 
1237 C  CD2 . LEU A 228 ? 0.2522 0.3486 0.3350 -0.0190 -0.0270 0.0209  228 LEU A CD2 
1238 N  N   . SER A 229 ? 0.1264 0.1913 0.1808 0.0007  -0.0143 0.0318  229 SER A N   
1239 C  CA  . SER A 229 ? 0.1267 0.1878 0.1807 0.0066  -0.0109 0.0354  229 SER A CA  
1240 C  C   . SER A 229 ? 0.1406 0.1977 0.1973 0.0077  -0.0059 0.0350  229 SER A C   
1241 O  O   . SER A 229 ? 0.1630 0.2180 0.2211 0.0128  -0.0029 0.0371  229 SER A O   
1242 C  CB  . SER A 229 ? 0.1347 0.1852 0.1800 0.0078  -0.0103 0.0358  229 SER A CB  
1243 O  OG  . SER A 229 ? 0.1483 0.1890 0.1884 0.0042  -0.0084 0.0322  229 SER A OG  
1244 N  N   . GLY A 230 ? 0.0979 0.1540 0.1552 0.0033  -0.0045 0.0324  230 GLY A N   
1245 C  CA  . GLY A 230 ? 0.1015 0.1546 0.1594 0.0045  0.0005  0.0320  230 GLY A CA  
1246 C  C   . GLY A 230 ? 0.1221 0.1636 0.1714 0.0030  0.0026  0.0295  230 GLY A C   
1247 O  O   . GLY A 230 ? 0.1172 0.1561 0.1653 0.0045  0.0067  0.0286  230 GLY A O   
1248 N  N   . LEU A 231 ? 0.1042 0.1395 0.1475 0.0006  -0.0001 0.0281  231 LEU A N   
1249 C  CA  . LEU A 231 ? 0.0975 0.1231 0.1333 -0.0010 0.0015  0.0259  231 LEU A CA  
1250 C  C   . LEU A 231 ? 0.1095 0.1360 0.1458 -0.0046 0.0029  0.0251  231 LEU A C   
1251 O  O   . LEU A 231 ? 0.1247 0.1578 0.1671 -0.0071 0.0020  0.0261  231 LEU A O   
1252 C  CB  . LEU A 231 ? 0.1133 0.1340 0.1436 -0.0026 -0.0016 0.0251  231 LEU A CB  
1253 C  CG  . LEU A 231 ? 0.1071 0.1305 0.1377 -0.0068 -0.0050 0.0238  231 LEU A CG  
1254 C  CD1 . LEU A 231 ? 0.1315 0.1511 0.1561 -0.0071 -0.0073 0.0230  231 LEU A CD1 
1255 C  CD2 . LEU A 231 ? 0.1194 0.1532 0.1577 -0.0080 -0.0075 0.0243  231 LEU A CD2 
1256 N  N   . ASP A 232 ? 0.1024 0.1224 0.1328 -0.0048 0.0051  0.0236  232 ASP A N   
1257 C  CA  . ASP A 232 ? 0.0960 0.1165 0.1258 -0.0078 0.0064  0.0239  232 ASP A CA  
1258 C  C   . ASP A 232 ? 0.1065 0.1224 0.1337 -0.0114 0.0038  0.0232  232 ASP A C   
1259 O  O   . ASP A 232 ? 0.1115 0.1290 0.1420 -0.0145 0.0037  0.0243  232 ASP A O   
1260 C  CB  . ASP A 232 ? 0.1065 0.1243 0.1309 -0.0058 0.0099  0.0227  232 ASP A CB  
1261 C  CG  . ASP A 232 ? 0.1267 0.1489 0.1537 -0.0018 0.0131  0.0226  232 ASP A CG  
1262 O  OD1 . ASP A 232 ? 0.1227 0.1528 0.1548 -0.0016 0.0153  0.0248  232 ASP A OD1 
1263 O  OD2 . ASP A 232 ? 0.1113 0.1291 0.1361 0.0014  0.0135  0.0204  232 ASP A OD2 
1264 N  N   . VAL A 233 ? 0.0941 0.1042 0.1159 -0.0110 0.0020  0.0215  233 VAL A N   
1265 C  CA  . VAL A 233 ? 0.0932 0.0988 0.1115 -0.0135 0.0001  0.0204  233 VAL A CA  
1266 C  C   . VAL A 233 ? 0.0930 0.0981 0.1101 -0.0132 -0.0029 0.0194  233 VAL A C   
1267 O  O   . VAL A 233 ? 0.0988 0.1027 0.1137 -0.0107 -0.0029 0.0198  233 VAL A O   
1268 C  CB  . VAL A 233 ? 0.0939 0.0942 0.1059 -0.0130 0.0017  0.0195  233 VAL A CB  
1269 C  CG1 . VAL A 233 ? 0.0997 0.0960 0.1088 -0.0150 -0.0001 0.0188  233 VAL A CG1 
1270 C  CG2 . VAL A 233 ? 0.1070 0.1097 0.1191 -0.0127 0.0047  0.0207  233 VAL A CG2 
1271 N  N   . TYR A 234 ? 0.0931 0.0991 0.1117 -0.0156 -0.0055 0.0181  234 TYR A N   
1272 C  CA  . TYR A 234 ? 0.0937 0.1006 0.1099 -0.0154 -0.0084 0.0166  234 TYR A CA  
1273 C  C   . TYR A 234 ? 0.1083 0.1094 0.1194 -0.0163 -0.0085 0.0150  234 TYR A C   
1274 O  O   . TYR A 234 ? 0.0957 0.0949 0.1085 -0.0185 -0.0089 0.0134  234 TYR A O   
1275 C  CB  . TYR A 234 ? 0.0960 0.1092 0.1175 -0.0173 -0.0115 0.0149  234 TYR A CB  
1276 C  CG  . TYR A 234 ? 0.1029 0.1198 0.1211 -0.0161 -0.0147 0.0134  234 TYR A CG  
1277 C  CD1 . TYR A 234 ? 0.1257 0.1508 0.1466 -0.0144 -0.0168 0.0147  234 TYR A CD1 
1278 C  CD2 . TYR A 234 ? 0.1401 0.1537 0.1527 -0.0163 -0.0156 0.0110  234 TYR A CD2 
1279 C  CE1 . TYR A 234 ? 0.1325 0.1627 0.1496 -0.0129 -0.0197 0.0141  234 TYR A CE1 
1280 C  CE2 . TYR A 234 ? 0.1685 0.1869 0.1771 -0.0148 -0.0182 0.0101  234 TYR A CE2 
1281 C  CZ  . TYR A 234 ? 0.1751 0.2019 0.1857 -0.0131 -0.0203 0.0117  234 TYR A CZ  
1282 O  OH  . TYR A 234 ? 0.1960 0.2291 0.2019 -0.0112 -0.0228 0.0114  234 TYR A OH  
1283 N  N   . ALA A 235 ? 0.0994 0.0979 0.1054 -0.0145 -0.0080 0.0156  235 ALA A N   
1284 C  CA  . ALA A 235 ? 0.1091 0.1036 0.1109 -0.0150 -0.0079 0.0144  235 ALA A CA  
1285 C  C   . ALA A 235 ? 0.1112 0.1080 0.1097 -0.0141 -0.0097 0.0136  235 ALA A C   
1286 O  O   . ALA A 235 ? 0.1189 0.1189 0.1165 -0.0122 -0.0102 0.0155  235 ALA A O   
1287 C  CB  . ALA A 235 ? 0.1283 0.1188 0.1273 -0.0143 -0.0056 0.0158  235 ALA A CB  
1288 N  N   . HIS A 236 ? 0.0988 0.0944 0.0955 -0.0149 -0.0105 0.0109  236 HIS A N   
1289 C  CA  . HIS A 236 ? 0.0999 0.0986 0.0925 -0.0136 -0.0118 0.0096  236 HIS A CA  
1290 C  C   . HIS A 236 ? 0.1181 0.1132 0.1087 -0.0138 -0.0109 0.0076  236 HIS A C   
1291 O  O   . HIS A 236 ? 0.1259 0.1180 0.1193 -0.0152 -0.0111 0.0051  236 HIS A O   
1292 C  CB  . HIS A 236 ? 0.1101 0.1147 0.1038 -0.0139 -0.0149 0.0065  236 HIS A CB  
1293 C  CG  . HIS A 236 ? 0.1372 0.1458 0.1256 -0.0124 -0.0161 0.0041  236 HIS A CG  
1294 N  ND1 . HIS A 236 ? 0.1708 0.1835 0.1545 -0.0098 -0.0156 0.0076  236 HIS A ND1 
1295 C  CD2 . HIS A 236 ? 0.1643 0.1729 0.1512 -0.0127 -0.0172 -0.0013 236 HIS A CD2 
1296 C  CE1 . HIS A 236 ? 0.2014 0.2181 0.1804 -0.0086 -0.0163 0.0047  236 HIS A CE1 
1297 N  NE2 . HIS A 236 ? 0.1751 0.1891 0.1557 -0.0101 -0.0174 -0.0013 236 HIS A NE2 
1298 N  N   . ASN A 237 ? 0.1211 0.1166 0.1077 -0.0124 -0.0096 0.0092  237 ASN A N   
1299 C  CA  . ASN A 237 ? 0.1246 0.1173 0.1102 -0.0122 -0.0083 0.0084  237 ASN A CA  
1300 C  C   . ASN A 237 ? 0.1512 0.1462 0.1344 -0.0109 -0.0090 0.0044  237 ASN A C   
1301 O  O   . ASN A 237 ? 0.1767 0.1770 0.1560 -0.0094 -0.0095 0.0042  237 ASN A O   
1302 C  CB  . ASN A 237 ? 0.1315 0.1242 0.1154 -0.0117 -0.0064 0.0121  237 ASN A CB  
1303 C  CG  . ASN A 237 ? 0.1605 0.1499 0.1469 -0.0131 -0.0055 0.0141  237 ASN A CG  
1304 O  OD1 . ASN A 237 ? 0.1767 0.1641 0.1654 -0.0139 -0.0058 0.0133  237 ASN A OD1 
1305 N  ND2 . ASN A 237 ? 0.2183 0.2071 0.2044 -0.0133 -0.0043 0.0166  237 ASN A ND2 
1306 N  N   . VAL A 238 ? 0.1349 0.1259 0.1202 -0.0111 -0.0087 0.0016  238 VAL A N   
1307 C  CA  . VAL A 238 ? 0.1249 0.1170 0.1081 -0.0093 -0.0088 -0.0029 238 VAL A CA  
1308 C  C   . VAL A 238 ? 0.1324 0.1264 0.1129 -0.0072 -0.0065 -0.0008 238 VAL A C   
1309 O  O   . VAL A 238 ? 0.1473 0.1449 0.1247 -0.0049 -0.0060 -0.0037 238 VAL A O   
1310 C  CB  . VAL A 238 ? 0.1590 0.1451 0.1471 -0.0101 -0.0091 -0.0068 238 VAL A CB  
1311 C  CG1 . VAL A 238 ? 0.1950 0.1804 0.1870 -0.0126 -0.0114 -0.0093 238 VAL A CG1 
1312 C  CG2 . VAL A 238 ? 0.1901 0.1713 0.1819 -0.0104 -0.0072 -0.0028 238 VAL A CG2 
1313 N  N   . GLU A 239 ? 0.1289 0.1215 0.1109 -0.0080 -0.0050 0.0038  239 GLU A N   
1314 C  CA  . GLU A 239 ? 0.1411 0.1366 0.1219 -0.0069 -0.0031 0.0068  239 GLU A CA  
1315 C  C   . GLU A 239 ? 0.1456 0.1407 0.1277 -0.0048 -0.0018 0.0050  239 GLU A C   
1316 O  O   . GLU A 239 ? 0.1480 0.1440 0.1320 -0.0048 -0.0006 0.0080  239 GLU A O   
1317 C  CB  . GLU A 239 ? 0.1853 0.1873 0.1622 -0.0057 -0.0024 0.0084  239 GLU A CB  
1318 C  CG  . GLU A 239 ? 0.1975 0.2004 0.1737 -0.0070 -0.0032 0.0115  239 GLU A CG  
1319 C  CD  . GLU A 239 ? 0.3027 0.3024 0.2820 -0.0092 -0.0025 0.0156  239 GLU A CD  
1320 O  OE1 . GLU A 239 ? 0.3476 0.3450 0.3293 -0.0102 -0.0018 0.0158  239 GLU A OE1 
1321 O  OE2 . GLU A 239 ? 0.3189 0.3185 0.2985 -0.0097 -0.0027 0.0182  239 GLU A OE2 
1322 N  N   . THR A 240 ? 0.1235 0.1180 0.1050 -0.0028 -0.0020 0.0000  240 THR A N   
1323 C  CA  . THR A 240 ? 0.1383 0.1319 0.1218 0.0000  -0.0004 -0.0017 240 THR A CA  
1324 C  C   . THR A 240 ? 0.1223 0.1104 0.1077 0.0009  -0.0013 -0.0079 240 THR A C   
1325 O  O   . THR A 240 ? 0.1663 0.1525 0.1515 -0.0009 -0.0033 -0.0111 240 THR A O   
1326 C  CB  . THR A 240 ? 0.1585 0.1596 0.1388 0.0028  0.0017  -0.0011 240 THR A CB  
1327 O  OG1 . THR A 240 ? 0.1633 0.1640 0.1468 0.0057  0.0035  -0.0018 240 THR A OG1 
1328 C  CG2 . THR A 240 ? 0.1690 0.1746 0.1440 0.0046  0.0014  -0.0058 240 THR A CG2 
1329 N  N   . VAL A 241 ? 0.1680 0.1537 0.1563 0.0039  0.0003  -0.0097 241 VAL A N   
1330 C  CA  . VAL A 241 ? 0.1627 0.1415 0.1546 0.0050  -0.0001 -0.0158 241 VAL A CA  
1331 C  C   . VAL A 241 ? 0.1796 0.1619 0.1666 0.0066  -0.0008 -0.0235 241 VAL A C   
1332 O  O   . VAL A 241 ? 0.1799 0.1709 0.1607 0.0082  0.0000  -0.0230 241 VAL A O   
1333 C  CB  . VAL A 241 ? 0.1636 0.1382 0.1608 0.0084  0.0021  -0.0148 241 VAL A CB  
1334 C  CG1 . VAL A 241 ? 0.1743 0.1478 0.1753 0.0069  0.0024  -0.0067 241 VAL A CG1 
1335 C  CG2 . VAL A 241 ? 0.1822 0.1637 0.1765 0.0129  0.0045  -0.0160 241 VAL A CG2 
1336 N  N   . PRO A 242 ? 0.2068 0.1833 0.1965 0.0060  -0.0023 -0.0307 242 PRO A N   
1337 C  CA  . PRO A 242 ? 0.2458 0.2273 0.2299 0.0073  -0.0037 -0.0390 242 PRO A CA  
1338 C  C   . PRO A 242 ? 0.2065 0.1944 0.1855 0.0126  -0.0010 -0.0418 242 PRO A C   
1339 O  O   . PRO A 242 ? 0.2443 0.2419 0.2156 0.0139  -0.0012 -0.0436 242 PRO A O   
1340 C  CB  . PRO A 242 ? 0.2311 0.2033 0.2216 0.0057  -0.0055 -0.0468 242 PRO A CB  
1341 C  CG  . PRO A 242 ? 0.2259 0.1911 0.2239 0.0017  -0.0060 -0.0404 242 PRO A CG  
1342 C  CD  . PRO A 242 ? 0.2064 0.1728 0.2043 0.0032  -0.0034 -0.0312 242 PRO A CD  
1343 N  N   . GLU A 243 ? 0.2096 0.1935 0.1930 0.0160  0.0019  -0.0410 243 GLU A N   
1344 C  CA  . GLU A 243 ? 0.2409 0.2311 0.2206 0.0215  0.0050  -0.0439 243 GLU A CA  
1345 C  C   . GLU A 243 ? 0.2421 0.2445 0.2160 0.0223  0.0067  -0.0369 243 GLU A C   
1346 O  O   . GLU A 243 ? 0.2669 0.2777 0.2359 0.0266  0.0092  -0.0393 243 GLU A O   
1347 C  CB  . GLU A 243 ? 0.2794 0.2624 0.2669 0.0251  0.0077  -0.0434 243 GLU A CB  
1348 C  CG  . GLU A 243 ? 0.4224 0.3926 0.4169 0.0252  0.0067  -0.0509 243 GLU A CG  
1349 C  CD  . GLU A 243 ? 0.4233 0.3836 0.4255 0.0202  0.0048  -0.0459 243 GLU A CD  
1350 O  OE1 . GLU A 243 ? 0.3060 0.2693 0.3069 0.0163  0.0035  -0.0381 243 GLU A OE1 
1351 O  OE2 . GLU A 243 ? 0.4962 0.4453 0.5063 0.0204  0.0048  -0.0499 243 GLU A OE2 
1352 N  N   . LEU A 244 ? 0.1838 0.1874 0.1582 0.0183  0.0057  -0.0285 244 LEU A N   
1353 C  CA  . LEU A 244 ? 0.1829 0.1966 0.1537 0.0183  0.0074  -0.0215 244 LEU A CA  
1354 C  C   . LEU A 244 ? 0.1828 0.2018 0.1479 0.0156  0.0055  -0.0194 244 LEU A C   
1355 O  O   . LEU A 244 ? 0.1784 0.2045 0.1414 0.0150  0.0069  -0.0128 244 LEU A O   
1356 C  CB  . LEU A 244 ? 0.2055 0.2172 0.1820 0.0163  0.0081  -0.0134 244 LEU A CB  
1357 C  CG  . LEU A 244 ? 0.2204 0.2310 0.2025 0.0198  0.0105  -0.0128 244 LEU A CG  
1358 C  CD1 . LEU A 244 ? 0.2513 0.2623 0.2383 0.0174  0.0104  -0.0050 244 LEU A CD1 
1359 C  CD2 . LEU A 244 ? 0.3233 0.3432 0.3027 0.0247  0.0138  -0.0146 244 LEU A CD2 
1360 N  N   . GLN A 245 ? 0.1839 0.1998 0.1471 0.0139  0.0024  -0.0247 245 GLN A N   
1361 C  CA  . GLN A 245 ? 0.1751 0.1963 0.1337 0.0116  0.0002  -0.0221 245 GLN A CA  
1362 C  C   . GLN A 245 ? 0.1562 0.1901 0.1072 0.0147  0.0021  -0.0203 245 GLN A C   
1363 O  O   . GLN A 245 ? 0.2192 0.2582 0.1685 0.0135  0.0027  -0.0127 245 GLN A O   
1364 C  CB  . GLN A 245 ? 0.2082 0.2260 0.1669 0.0097  -0.0036 -0.0291 245 GLN A CB  
1365 C  CG  . GLN A 245 ? 0.2139 0.2204 0.1806 0.0059  -0.0054 -0.0289 245 GLN A CG  
1366 C  CD  . GLN A 245 ? 0.1923 0.1990 0.1602 0.0024  -0.0067 -0.0219 245 GLN A CD  
1367 O  OE1 . GLN A 245 ? 0.2187 0.2321 0.1823 0.0020  -0.0083 -0.0208 245 GLN A OE1 
1368 N  NE2 . GLN A 245 ? 0.1798 0.1797 0.1534 0.0002  -0.0060 -0.0172 245 GLN A NE2 
1369 N  N   . SER A 246 ? 0.1911 0.2301 0.1378 0.0190  0.0037  -0.0268 246 SER A N   
1370 C  CA  . SER A 246 ? 0.1954 0.2482 0.1340 0.0223  0.0057  -0.0246 246 SER A CA  
1371 C  C   . SER A 246 ? 0.2632 0.3212 0.2038 0.0230  0.0099  -0.0152 246 SER A C   
1372 O  O   . SER A 246 ? 0.2627 0.3302 0.1993 0.0234  0.0114  -0.0084 246 SER A O   
1373 C  CB  . SER A 246 ? 0.3105 0.3684 0.2433 0.0271  0.0063  -0.0351 246 SER A CB  
1374 O  OG  . SER A 246 ? 0.4128 0.4682 0.3493 0.0304  0.0099  -0.0372 246 SER A OG  
1375 N  N   . LYS A 247 ? 0.1908 0.2431 0.1383 0.0230  0.0118  -0.0141 247 LYS A N   
1376 C  CA  . LYS A 247 ? 0.2273 0.2846 0.1784 0.0228  0.0153  -0.0054 247 LYS A CA  
1377 C  C   . LYS A 247 ? 0.2148 0.2692 0.1693 0.0177  0.0139  0.0029  247 LYS A C   
1378 O  O   . LYS A 247 ? 0.2088 0.2700 0.1638 0.0169  0.0162  0.0106  247 LYS A O   
1379 C  CB  . LYS A 247 ? 0.2936 0.3464 0.2518 0.0242  0.0169  -0.0066 247 LYS A CB  
1380 C  CG  . LYS A 247 ? 0.3191 0.3767 0.2832 0.0229  0.0196  0.0020  247 LYS A CG  
1381 C  CD  . LYS A 247 ? 0.4148 0.4685 0.3864 0.0242  0.0204  0.0012  247 LYS A CD  
1382 C  CE  . LYS A 247 ? 0.4743 0.5292 0.4529 0.0203  0.0205  0.0093  247 LYS A CE  
1383 N  NZ  . LYS A 247 ? 0.4597 0.5129 0.4457 0.0217  0.0208  0.0096  247 LYS A NZ  
1384 N  N   . VAL A 248 ? 0.1396 0.1840 0.0970 0.0142  0.0105  0.0016  248 VAL A N   
1385 C  CA  . VAL A 248 ? 0.1548 0.1949 0.1166 0.0097  0.0095  0.0083  248 VAL A CA  
1386 C  C   . VAL A 248 ? 0.1447 0.1862 0.1029 0.0082  0.0077  0.0109  248 VAL A C   
1387 O  O   . VAL A 248 ? 0.1584 0.2020 0.1182 0.0064  0.0087  0.0182  248 VAL A O   
1388 C  CB  . VAL A 248 ? 0.1836 0.2130 0.1511 0.0073  0.0075  0.0063  248 VAL A CB  
1389 C  CG1 . VAL A 248 ? 0.1909 0.2160 0.1620 0.0029  0.0062  0.0117  248 VAL A CG1 
1390 C  CG2 . VAL A 248 ? 0.1558 0.1853 0.1277 0.0091  0.0095  0.0059  248 VAL A CG2 
1391 N  N   . ARG A 249 ? 0.1587 0.1984 0.1133 0.0087  0.0048  0.0052  249 ARG A N   
1392 C  CA  . ARG A 249 ? 0.1809 0.2215 0.1334 0.0073  0.0023  0.0073  249 ARG A CA  
1393 C  C   . ARG A 249 ? 0.1791 0.2313 0.1238 0.0107  0.0026  0.0075  249 ARG A C   
1394 O  O   . ARG A 249 ? 0.2035 0.2619 0.1435 0.0140  0.0039  0.0028  249 ARG A O   
1395 C  CB  . ARG A 249 ? 0.1679 0.2013 0.1223 0.0054  -0.0014 0.0013  249 ARG A CB  
1396 C  CG  . ARG A 249 ? 0.1750 0.1981 0.1364 0.0024  -0.0016 0.0019  249 ARG A CG  
1397 C  CD  . ARG A 249 ? 0.2019 0.2191 0.1655 0.0006  -0.0049 -0.0032 249 ARG A CD  
1398 N  NE  . ARG A 249 ? 0.1931 0.2112 0.1571 -0.0012 -0.0068 -0.0001 249 ARG A NE  
1399 C  CZ  . ARG A 249 ? 0.1689 0.1853 0.1345 -0.0027 -0.0098 -0.0037 249 ARG A CZ  
1400 N  NH1 . ARG A 249 ? 0.1911 0.2047 0.1582 -0.0031 -0.0113 -0.0109 249 ARG A NH1 
1401 N  NH2 . ARG A 249 ? 0.2617 0.2797 0.2284 -0.0038 -0.0112 0.0000  249 ARG A NH2 
1402 N  N   . ASP A 250 ? 0.1722 0.2279 0.1154 0.0101  0.0016  0.0130  250 ASP A N   
1403 C  CA  . ASP A 250 ? 0.1966 0.2650 0.1318 0.0137  0.0016  0.0141  250 ASP A CA  
1404 C  C   . ASP A 250 ? 0.1888 0.2603 0.1187 0.0153  -0.0019 0.0035  250 ASP A C   
1405 O  O   . ASP A 250 ? 0.1875 0.2512 0.1211 0.0127  -0.0052 -0.0019 250 ASP A O   
1406 C  CB  . ASP A 250 ? 0.2746 0.3463 0.2097 0.0133  0.0009  0.0226  250 ASP A CB  
1407 C  CG  . ASP A 250 ? 0.3096 0.3963 0.2363 0.0176  0.0018  0.0260  250 ASP A CG  
1408 O  OD1 . ASP A 250 ? 0.3272 0.4201 0.2529 0.0192  0.0060  0.0327  250 ASP A OD1 
1409 O  OD2 . ASP A 250 ? 0.2659 0.3591 0.1871 0.0192  -0.0019 0.0215  250 ASP A OD2 
1410 N  N   . PRO A 251 ? 0.1917 0.2748 0.1133 0.0194  -0.0012 0.0000  251 PRO A N   
1411 C  CA  . PRO A 251 ? 0.2076 0.2934 0.1246 0.0206  -0.0048 -0.0118 251 PRO A CA  
1412 C  C   . PRO A 251 ? 0.2022 0.2903 0.1187 0.0189  -0.0100 -0.0132 251 PRO A C   
1413 O  O   . PRO A 251 ? 0.2551 0.3432 0.1703 0.0184  -0.0137 -0.0238 251 PRO A O   
1414 C  CB  . PRO A 251 ? 0.3163 0.4166 0.2234 0.0259  -0.0025 -0.0138 251 PRO A CB  
1415 C  CG  . PRO A 251 ? 0.3662 0.4669 0.2758 0.0269  0.0033  -0.0051 251 PRO A CG  
1416 C  CD  . PRO A 251 ? 0.2668 0.3606 0.1837 0.0230  0.0034  0.0056  251 PRO A CD  
1417 N  N   . ARG A 252 ? 0.2049 0.2945 0.1233 0.0179  -0.0103 -0.0033 252 ARG A N   
1418 C  CA  A ARG A 252 ? 0.1734 0.2650 0.0928 0.0164  -0.0152 -0.0043 252 ARG A CA  
1419 C  CA  B ARG A 252 ? 0.1739 0.2652 0.0937 0.0163  -0.0150 -0.0037 252 ARG A CA  
1420 C  C   . ARG A 252 ? 0.1883 0.2666 0.1167 0.0118  -0.0176 -0.0093 252 ARG A C   
1421 O  O   . ARG A 252 ? 0.2223 0.3027 0.1527 0.0102  -0.0218 -0.0123 252 ARG A O   
1422 C  CB  A ARG A 252 ? 0.2081 0.3045 0.1281 0.0173  -0.0143 0.0082  252 ARG A CB  
1423 C  CB  B ARG A 252 ? 0.2167 0.3102 0.1385 0.0166  -0.0140 0.0089  252 ARG A CB  
1424 C  CG  A ARG A 252 ? 0.3137 0.3975 0.2424 0.0145  -0.0113 0.0161  252 ARG A CG  
1425 C  CG  B ARG A 252 ? 0.2601 0.3682 0.1745 0.0210  -0.0124 0.0169  252 ARG A CG  
1426 C  CD  A ARG A 252 ? 0.3447 0.4319 0.2749 0.0157  -0.0099 0.0283  252 ARG A CD  
1427 C  CD  B ARG A 252 ? 0.3673 0.4720 0.2874 0.0205  -0.0105 0.0299  252 ARG A CD  
1428 N  NE  A ARG A 252 ? 0.3096 0.4077 0.2339 0.0194  -0.0066 0.0357  252 ARG A NE  
1429 N  NE  B ARG A 252 ? 0.3725 0.4808 0.2912 0.0224  -0.0052 0.0396  252 ARG A NE  
1430 C  CZ  A ARG A 252 ? 0.3510 0.4460 0.2780 0.0190  -0.0018 0.0425  252 ARG A CZ  
1431 C  CZ  B ARG A 252 ? 0.3389 0.4372 0.2643 0.0200  -0.0012 0.0440  252 ARG A CZ  
1432 N  NH1 A ARG A 252 ? 0.2499 0.3560 0.1721 0.0223  0.0015  0.0500  252 ARG A NH1 
1433 N  NH1 B ARG A 252 ? 0.3808 0.4650 0.3138 0.0159  -0.0018 0.0401  252 ARG A NH1 
1434 N  NH2 A ARG A 252 ? 0.3998 0.4813 0.3348 0.0152  -0.0002 0.0420  252 ARG A NH2 
1435 N  NH2 B ARG A 252 ? 0.2861 0.3898 0.2107 0.0216  0.0035  0.0528  252 ARG A NH2 
1436 N  N   . VAL A 253 ? 0.1675 0.2338 0.1017 0.0097  -0.0149 -0.0098 253 VAL A N   
1437 C  CA  . VAL A 253 ? 0.1770 0.2313 0.1195 0.0057  -0.0165 -0.0132 253 VAL A CA  
1438 C  C   . VAL A 253 ? 0.2212 0.2687 0.1653 0.0055  -0.0156 -0.0216 253 VAL A C   
1439 O  O   . VAL A 253 ? 0.2238 0.2745 0.1634 0.0086  -0.0131 -0.0234 253 VAL A O   
1440 C  CB  . VAL A 253 ? 0.1966 0.2424 0.1455 0.0035  -0.0142 -0.0047 253 VAL A CB  
1441 C  CG1 . VAL A 253 ? 0.2466 0.2976 0.1951 0.0041  -0.0149 0.0033  253 VAL A CG1 
1442 C  CG2 . VAL A 253 ? 0.1951 0.2373 0.1442 0.0043  -0.0099 -0.0011 253 VAL A CG2 
1443 N  N   . ASN A 254 ? 0.1750 0.2132 0.1260 0.0022  -0.0175 -0.0265 254 ASN A N   
1444 C  CA  . ASN A 254 ? 0.1624 0.1925 0.1165 0.0022  -0.0165 -0.0335 254 ASN A CA  
1445 C  C   . ASN A 254 ? 0.1883 0.2071 0.1520 -0.0019 -0.0174 -0.0338 254 ASN A C   
1446 O  O   . ASN A 254 ? 0.2072 0.2256 0.1744 -0.0045 -0.0190 -0.0297 254 ASN A O   
1447 C  CB  . ASN A 254 ? 0.1992 0.2347 0.1488 0.0041  -0.0186 -0.0445 254 ASN A CB  
1448 C  CG  . ASN A 254 ? 0.2782 0.3181 0.2289 0.0014  -0.0238 -0.0496 254 ASN A CG  
1449 O  OD1 . ASN A 254 ? 0.2507 0.2827 0.2095 -0.0024 -0.0258 -0.0530 254 ASN A OD1 
1450 N  ND2 . ASN A 254 ? 0.3407 0.3943 0.2835 0.0035  -0.0260 -0.0499 254 ASN A ND2 
1451 N  N   . PHE A 255 ? 0.2058 0.2158 0.1740 -0.0019 -0.0160 -0.0380 255 PHE A N   
1452 C  CA  . PHE A 255 ? 0.1741 0.1735 0.1515 -0.0053 -0.0159 -0.0365 255 PHE A CA  
1453 C  C   . PHE A 255 ? 0.1815 0.1803 0.1640 -0.0090 -0.0198 -0.0414 255 PHE A C   
1454 O  O   . PHE A 255 ? 0.1905 0.1869 0.1784 -0.0122 -0.0204 -0.0368 255 PHE A O   
1455 C  CB  . PHE A 255 ? 0.2338 0.2245 0.2153 -0.0038 -0.0135 -0.0392 255 PHE A CB  
1456 C  CG  . PHE A 255 ? 0.2012 0.1819 0.1916 -0.0065 -0.0127 -0.0355 255 PHE A CG  
1457 C  CD1 . PHE A 255 ? 0.2222 0.2015 0.2134 -0.0067 -0.0105 -0.0268 255 PHE A CD1 
1458 C  CD2 . PHE A 255 ? 0.2513 0.2245 0.2494 -0.0090 -0.0141 -0.0408 255 PHE A CD2 
1459 C  CE1 . PHE A 255 ? 0.2448 0.2168 0.2432 -0.0087 -0.0097 -0.0230 255 PHE A CE1 
1460 C  CE2 . PHE A 255 ? 0.3169 0.2819 0.3234 -0.0113 -0.0128 -0.0361 255 PHE A CE2 
1461 C  CZ  . PHE A 255 ? 0.2482 0.2131 0.2542 -0.0108 -0.0106 -0.0269 255 PHE A CZ  
1462 N  N   . ASP A 256 ? 0.2037 0.2058 0.1845 -0.0088 -0.0224 -0.0510 256 ASP A N   
1463 C  CA  . ASP A 256 ? 0.2459 0.2480 0.2328 -0.0130 -0.0265 -0.0565 256 ASP A CA  
1464 C  C   . ASP A 256 ? 0.2230 0.2344 0.2086 -0.0145 -0.0290 -0.0515 256 ASP A C   
1465 O  O   . ASP A 256 ? 0.2113 0.2209 0.2048 -0.0185 -0.0307 -0.0504 256 ASP A O   
1466 C  CB  . ASP A 256 ? 0.2540 0.2592 0.2386 -0.0123 -0.0293 -0.0690 256 ASP A CB  
1467 C  CG  . ASP A 256 ? 0.4135 0.4068 0.4032 -0.0117 -0.0271 -0.0753 256 ASP A CG  
1468 O  OD1 . ASP A 256 ? 0.4490 0.4320 0.4453 -0.0122 -0.0240 -0.0693 256 ASP A OD1 
1469 O  OD2 . ASP A 256 ? 0.5658 0.5607 0.5528 -0.0100 -0.0285 -0.0862 256 ASP A OD2 
1470 N  N   . GLN A 257 ? 0.1899 0.2116 0.1662 -0.0112 -0.0290 -0.0481 257 GLN A N   
1471 C  CA  A GLN A 257 ? 0.1819 0.2123 0.1574 -0.0118 -0.0311 -0.0425 257 GLN A CA  
1472 C  CA  B GLN A 257 ? 0.1828 0.2133 0.1580 -0.0116 -0.0310 -0.0423 257 GLN A CA  
1473 C  C   . GLN A 257 ? 0.1769 0.2011 0.1577 -0.0132 -0.0286 -0.0331 257 GLN A C   
1474 O  O   . GLN A 257 ? 0.1951 0.2216 0.1810 -0.0155 -0.0304 -0.0306 257 GLN A O   
1475 C  CB  A GLN A 257 ? 0.2482 0.2905 0.2133 -0.0075 -0.0311 -0.0395 257 GLN A CB  
1476 C  CB  B GLN A 257 ? 0.2464 0.2883 0.2110 -0.0072 -0.0306 -0.0390 257 GLN A CB  
1477 C  CG  A GLN A 257 ? 0.2301 0.2817 0.1951 -0.0075 -0.0336 -0.0338 257 GLN A CG  
1478 C  CG  B GLN A 257 ? 0.2656 0.3160 0.2291 -0.0065 -0.0320 -0.0313 257 GLN A CG  
1479 C  CD  A GLN A 257 ? 0.3293 0.3952 0.2844 -0.0034 -0.0350 -0.0330 257 GLN A CD  
1480 C  CD  B GLN A 257 ? 0.3195 0.3804 0.2837 -0.0078 -0.0374 -0.0364 257 GLN A CD  
1481 O  OE1 A GLN A 257 ? 0.4100 0.4854 0.3621 -0.0033 -0.0392 -0.0405 257 GLN A OE1 
1482 O  OE1 B GLN A 257 ? 0.3080 0.3665 0.2808 -0.0116 -0.0397 -0.0384 257 GLN A OE1 
1483 N  NE2 A GLN A 257 ? 0.2998 0.3679 0.2500 -0.0002 -0.0316 -0.0238 257 GLN A NE2 
1484 N  NE2 B GLN A 257 ? 0.3463 0.4203 0.3017 -0.0044 -0.0395 -0.0383 257 GLN A NE2 
1485 N  N   . SER A 258 ? 0.1671 0.1844 0.1470 -0.0118 -0.0245 -0.0282 258 SER A N   
1486 C  CA  . SER A 258 ? 0.1644 0.1762 0.1486 -0.0131 -0.0222 -0.0205 258 SER A CA  
1487 C  C   . SER A 258 ? 0.1832 0.1883 0.1768 -0.0169 -0.0227 -0.0220 258 SER A C   
1488 O  O   . SER A 258 ? 0.1804 0.1854 0.1782 -0.0185 -0.0224 -0.0173 258 SER A O   
1489 C  CB  . SER A 258 ? 0.1813 0.1884 0.1627 -0.0111 -0.0183 -0.0161 258 SER A CB  
1490 O  OG  . SER A 258 ? 0.1725 0.1864 0.1472 -0.0083 -0.0174 -0.0119 258 SER A OG  
1491 N  N   . LEU A 259 ? 0.1627 0.1620 0.1600 -0.0182 -0.0230 -0.0282 259 LEU A N   
1492 C  CA  . LEU A 259 ? 0.1770 0.1702 0.1843 -0.0222 -0.0234 -0.0289 259 LEU A CA  
1493 C  C   . LEU A 259 ? 0.2089 0.2092 0.2208 -0.0252 -0.0272 -0.0314 259 LEU A C   
1494 O  O   . LEU A 259 ? 0.2272 0.2260 0.2468 -0.0281 -0.0269 -0.0281 259 LEU A O   
1495 C  CB  . LEU A 259 ? 0.2434 0.2280 0.2553 -0.0229 -0.0228 -0.0348 259 LEU A CB  
1496 C  CG  . LEU A 259 ? 0.3129 0.2884 0.3282 -0.0224 -0.0189 -0.0290 259 LEU A CG  
1497 C  CD1 . LEU A 259 ? 0.3649 0.3424 0.3719 -0.0184 -0.0164 -0.0240 259 LEU A CD1 
1498 C  CD2 . LEU A 259 ? 0.4103 0.3766 0.4314 -0.0225 -0.0182 -0.0341 259 LEU A CD2 
1499 N  N   . ARG A 260 ? 0.1949 0.2042 0.2019 -0.0242 -0.0306 -0.0367 260 ARG A N   
1500 C  CA  . ARG A 260 ? 0.1856 0.2037 0.1970 -0.0269 -0.0348 -0.0391 260 ARG A CA  
1501 C  C   . ARG A 260 ? 0.1933 0.2173 0.2047 -0.0259 -0.0342 -0.0304 260 ARG A C   
1502 O  O   . ARG A 260 ? 0.2274 0.2558 0.2464 -0.0287 -0.0360 -0.0296 260 ARG A O   
1503 C  CB  . ARG A 260 ? 0.2496 0.2775 0.2545 -0.0255 -0.0389 -0.0471 260 ARG A CB  
1504 C  CG  . ARG A 260 ? 0.3275 0.3497 0.3352 -0.0274 -0.0404 -0.0582 260 ARG A CG  
1505 C  CD  . ARG A 260 ? 0.3647 0.3983 0.3686 -0.0276 -0.0458 -0.0684 260 ARG A CD  
1506 N  NE  . ARG A 260 ? 0.3985 0.4420 0.3890 -0.0221 -0.0458 -0.0673 260 ARG A NE  
1507 C  CZ  . ARG A 260 ? 0.4646 0.5066 0.4471 -0.0186 -0.0441 -0.0719 260 ARG A CZ  
1508 N  NH1 . ARG A 260 ? 0.4433 0.4737 0.4299 -0.0194 -0.0424 -0.0786 260 ARG A NH1 
1509 N  NH2 . ARG A 260 ? 0.4525 0.5052 0.4234 -0.0137 -0.0437 -0.0693 260 ARG A NH2 
1510 N  N   . VAL A 261 ? 0.1780 0.2021 0.1819 -0.0220 -0.0314 -0.0240 261 VAL A N   
1511 C  CA  . VAL A 261 ? 0.1584 0.1854 0.1631 -0.0207 -0.0300 -0.0160 261 VAL A CA  
1512 C  C   . VAL A 261 ? 0.1503 0.1707 0.1633 -0.0235 -0.0277 -0.0128 261 VAL A C   
1513 O  O   . VAL A 261 ? 0.1668 0.1918 0.1857 -0.0246 -0.0283 -0.0101 261 VAL A O   
1514 C  CB  . VAL A 261 ? 0.1707 0.1963 0.1675 -0.0168 -0.0269 -0.0103 261 VAL A CB  
1515 C  CG1 . VAL A 261 ? 0.2085 0.2340 0.2075 -0.0157 -0.0249 -0.0027 261 VAL A CG1 
1516 C  CG2 . VAL A 261 ? 0.2584 0.2928 0.2470 -0.0136 -0.0288 -0.0115 261 VAL A CG2 
1517 N  N   . LEU A 262 ? 0.1767 0.1874 0.1901 -0.0240 -0.0246 -0.0123 262 LEU A N   
1518 C  CA  . LEU A 262 ? 0.1948 0.2000 0.2148 -0.0260 -0.0219 -0.0083 262 LEU A CA  
1519 C  C   . LEU A 262 ? 0.2013 0.2079 0.2315 -0.0303 -0.0237 -0.0109 262 LEU A C   
1520 O  O   . LEU A 262 ? 0.1901 0.1987 0.2265 -0.0317 -0.0224 -0.0068 262 LEU A O   
1521 C  CB  . LEU A 262 ? 0.1675 0.1634 0.1859 -0.0255 -0.0189 -0.0074 262 LEU A CB  
1522 C  CG  . LEU A 262 ? 0.2068 0.2018 0.2169 -0.0220 -0.0167 -0.0039 262 LEU A CG  
1523 C  CD1 . LEU A 262 ? 0.2292 0.2177 0.2368 -0.0209 -0.0150 -0.0050 262 LEU A CD1 
1524 C  CD2 . LEU A 262 ? 0.2564 0.2511 0.2670 -0.0214 -0.0143 0.0021  262 LEU A CD2 
1525 N  N   . LYS A 263 ? 0.1644 0.1703 0.1973 -0.0325 -0.0265 -0.0180 263 LYS A N   
1526 C  CA  . LYS A 263 ? 0.1753 0.1826 0.2196 -0.0374 -0.0286 -0.0211 263 LYS A CA  
1527 C  C   . LYS A 263 ? 0.1844 0.2039 0.2318 -0.0382 -0.0316 -0.0205 263 LYS A C   
1528 O  O   . LYS A 263 ? 0.1854 0.2076 0.2429 -0.0415 -0.0315 -0.0183 263 LYS A O   
1529 C  CB  . LYS A 263 ? 0.1661 0.1698 0.2124 -0.0395 -0.0313 -0.0304 263 LYS A CB  
1530 C  CG  . LYS A 263 ? 0.2822 0.2731 0.3299 -0.0393 -0.0279 -0.0302 263 LYS A CG  
1531 C  CD  . LYS A 263 ? 0.3786 0.3641 0.4278 -0.0404 -0.0299 -0.0399 263 LYS A CD  
1532 C  CE  . LYS A 263 ? 0.4416 0.4266 0.5039 -0.0464 -0.0327 -0.0455 263 LYS A CE  
1533 N  NZ  . LYS A 263 ? 0.5531 0.5344 0.6269 -0.0500 -0.0299 -0.0379 263 LYS A NZ  
1534 N  N   . HIS A 264 ? 0.1515 0.1793 0.1910 -0.0350 -0.0342 -0.0218 264 HIS A N   
1535 C  CA  . HIS A 264 ? 0.1466 0.1870 0.1895 -0.0352 -0.0374 -0.0208 264 HIS A CA  
1536 C  C   . HIS A 264 ? 0.1428 0.1850 0.1881 -0.0334 -0.0341 -0.0122 264 HIS A C   
1537 O  O   . HIS A 264 ? 0.1713 0.2213 0.2250 -0.0351 -0.0353 -0.0105 264 HIS A O   
1538 C  CB  . HIS A 264 ? 0.1744 0.2241 0.2080 -0.0316 -0.0407 -0.0230 264 HIS A CB  
1539 C  CG  . HIS A 264 ? 0.2077 0.2719 0.2454 -0.0318 -0.0450 -0.0230 264 HIS A CG  
1540 N  ND1 . HIS A 264 ? 0.2408 0.3111 0.2882 -0.0369 -0.0492 -0.0290 264 HIS A ND1 
1541 C  CD2 . HIS A 264 ? 0.2086 0.2828 0.2432 -0.0277 -0.0459 -0.0175 264 HIS A CD2 
1542 C  CE1 . HIS A 264 ? 0.1808 0.2656 0.2305 -0.0357 -0.0527 -0.0273 264 HIS A CE1 
1543 N  NE2 . HIS A 264 ? 0.2480 0.3353 0.2898 -0.0299 -0.0507 -0.0201 264 HIS A NE2 
1544 N  N   . ALA A 265 ? 0.1835 0.2189 0.2222 -0.0300 -0.0300 -0.0072 265 ALA A N   
1545 C  CA  . ALA A 265 ? 0.1775 0.2136 0.2183 -0.0281 -0.0266 -0.0003 265 ALA A CA  
1546 C  C   . ALA A 265 ? 0.1350 0.1697 0.1861 -0.0318 -0.0247 0.0013  265 ALA A C   
1547 O  O   . ALA A 265 ? 0.1686 0.2100 0.2256 -0.0316 -0.0238 0.0049  265 ALA A O   
1548 C  CB  . ALA A 265 ? 0.1714 0.1993 0.2038 -0.0246 -0.0228 0.0033  265 ALA A CB  
1549 N  N   . LYS A 266 ? 0.1612 0.1877 0.2151 -0.0350 -0.0236 -0.0008 266 LYS A N   
1550 C  CA  . LYS A 266 ? 0.1810 0.2063 0.2453 -0.0388 -0.0213 0.0018  266 LYS A CA  
1551 C  C   . LYS A 266 ? 0.1915 0.2248 0.2673 -0.0434 -0.0248 -0.0014 266 LYS A C   
1552 O  O   . LYS A 266 ? 0.2194 0.2568 0.3050 -0.0458 -0.0231 0.0023  266 LYS A O   
1553 C  CB  . LYS A 266 ? 0.2352 0.2492 0.3001 -0.0405 -0.0190 0.0015  266 LYS A CB  
1554 C  CG  . LYS A 266 ? 0.3562 0.3632 0.4121 -0.0368 -0.0151 0.0056  266 LYS A CG  
1555 C  CD  . LYS A 266 ? 0.2940 0.3026 0.3519 -0.0359 -0.0108 0.0124  266 LYS A CD  
1556 C  CE  . LYS A 266 ? 0.3278 0.3305 0.3911 -0.0380 -0.0077 0.0160  266 LYS A CE  
1557 N  NZ  . LYS A 266 ? 0.4026 0.4096 0.4668 -0.0367 -0.0034 0.0227  266 LYS A NZ  
1558 N  N   . LYS A 267 ? 0.1539 0.1904 0.2290 -0.0448 -0.0298 -0.0085 267 LYS A N   
1559 C  CA  . LYS A 267 ? 0.1661 0.2120 0.2525 -0.0495 -0.0340 -0.0124 267 LYS A CA  
1560 C  C   . LYS A 267 ? 0.2077 0.2670 0.2973 -0.0476 -0.0347 -0.0080 267 LYS A C   
1561 O  O   . LYS A 267 ? 0.2164 0.2827 0.3184 -0.0513 -0.0349 -0.0064 267 LYS A O   
1562 C  CB  . LYS A 267 ? 0.2623 0.3104 0.3454 -0.0507 -0.0396 -0.0219 267 LYS A CB  
1563 C  CG  . LYS A 267 ? 0.2923 0.3523 0.3863 -0.0555 -0.0450 -0.0270 267 LYS A CG  
1564 C  CD  . LYS A 267 ? 0.3469 0.4102 0.4362 -0.0563 -0.0508 -0.0375 267 LYS A CD  
1565 C  CE  . LYS A 267 ? 0.3968 0.4718 0.4983 -0.0621 -0.0567 -0.0439 267 LYS A CE  
1566 N  NZ  . LYS A 267 ? 0.5478 0.6284 0.6430 -0.0622 -0.0628 -0.0548 267 LYS A NZ  
1567 N  N   . VAL A 268 ? 0.1872 0.2505 0.2668 -0.0418 -0.0349 -0.0056 268 VAL A N   
1568 C  CA  . VAL A 268 ? 0.2276 0.3038 0.3109 -0.0393 -0.0359 -0.0016 268 VAL A CA  
1569 C  C   . VAL A 268 ? 0.1891 0.2639 0.2751 -0.0369 -0.0301 0.0060  268 VAL A C   
1570 O  O   . VAL A 268 ? 0.2124 0.2980 0.3060 -0.0361 -0.0301 0.0093  268 VAL A O   
1571 C  CB  . VAL A 268 ? 0.2947 0.3772 0.3682 -0.0338 -0.0386 -0.0014 268 VAL A CB  
1572 C  CG1 . VAL A 268 ? 0.3593 0.4425 0.4271 -0.0353 -0.0435 -0.0091 268 VAL A CG1 
1573 C  CG2 . VAL A 268 ? 0.2624 0.3371 0.3262 -0.0283 -0.0342 0.0039  268 VAL A CG2 
1574 N  N   . GLN A 269 ? 0.1615 0.2246 0.2415 -0.0355 -0.0254 0.0085  269 GLN A N   
1575 C  CA  . GLN A 269 ? 0.1622 0.2241 0.2436 -0.0332 -0.0199 0.0146  269 GLN A CA  
1576 C  C   . GLN A 269 ? 0.1582 0.2102 0.2404 -0.0361 -0.0162 0.0157  269 GLN A C   
1577 O  O   . GLN A 269 ? 0.1459 0.1887 0.2192 -0.0338 -0.0137 0.0165  269 GLN A O   
1578 C  CB  . GLN A 269 ? 0.1647 0.2242 0.2362 -0.0267 -0.0178 0.0174  269 GLN A CB  
1579 C  CG  . GLN A 269 ? 0.1954 0.2542 0.2677 -0.0240 -0.0122 0.0222  269 GLN A CG  
1580 C  CD  . GLN A 269 ? 0.2549 0.3251 0.3387 -0.0247 -0.0114 0.0249  269 GLN A CD  
1581 O  OE1 . GLN A 269 ? 0.2418 0.3142 0.3342 -0.0294 -0.0105 0.0256  269 GLN A OE1 
1582 N  NE2 . GLN A 269 ? 0.3086 0.3866 0.3938 -0.0202 -0.0115 0.0270  269 GLN A NE2 
1583 N  N   . PRO A 270 ? 0.1420 0.1964 0.2357 -0.0411 -0.0157 0.0164  270 PRO A N   
1584 C  CA  . PRO A 270 ? 0.1379 0.1828 0.2333 -0.0439 -0.0125 0.0181  270 PRO A CA  
1585 C  C   . PRO A 270 ? 0.1680 0.2097 0.2579 -0.0403 -0.0067 0.0240  270 PRO A C   
1586 O  O   . PRO A 270 ? 0.2186 0.2519 0.3060 -0.0410 -0.0043 0.0257  270 PRO A O   
1587 C  CB  . PRO A 270 ? 0.2306 0.2806 0.3417 -0.0501 -0.0131 0.0186  270 PRO A CB  
1588 C  CG  . PRO A 270 ? 0.2232 0.2824 0.3384 -0.0517 -0.0191 0.0131  270 PRO A CG  
1589 C  CD  . PRO A 270 ? 0.2050 0.2703 0.3112 -0.0453 -0.0194 0.0145  270 PRO A CD  
1590 N  N   . ASP A 271 ? 0.1898 0.2382 0.2776 -0.0361 -0.0045 0.0270  271 ASP A N   
1591 C  CA  A ASP A 271 ? 0.1893 0.2338 0.2711 -0.0333 0.0007  0.0312  271 ASP A CA  
1592 C  CA  B ASP A 271 ? 0.2016 0.2490 0.2836 -0.0321 0.0007  0.0313  271 ASP A CA  
1593 C  C   . ASP A 271 ? 0.1824 0.2208 0.2509 -0.0284 0.0008  0.0293  271 ASP A C   
1594 O  O   . ASP A 271 ? 0.1547 0.1906 0.2174 -0.0258 0.0046  0.0317  271 ASP A O   
1595 C  CB  A ASP A 271 ? 0.1907 0.2448 0.2788 -0.0320 0.0051  0.0363  271 ASP A CB  
1596 C  CB  B ASP A 271 ? 0.0954 0.1531 0.1801 -0.0284 0.0023  0.0333  271 ASP A CB  
1597 C  CG  A ASP A 271 ? 0.2079 0.2642 0.3067 -0.0368 0.0079  0.0410  271 ASP A CG  
1598 C  CG  B ASP A 271 ? 0.1858 0.2546 0.2845 -0.0315 0.0033  0.0364  271 ASP A CG  
1599 O  OD1 A ASP A 271 ? 0.2222 0.2706 0.3226 -0.0404 0.0071  0.0409  271 ASP A OD1 
1600 O  OD1 B ASP A 271 ? 0.1581 0.2263 0.2631 -0.0355 0.0057  0.0395  271 ASP A OD1 
1601 O  OD2 A ASP A 271 ? 0.1881 0.2543 0.2945 -0.0367 0.0111  0.0453  271 ASP A OD2 
1602 O  OD2 B ASP A 271 ? 0.1543 0.2331 0.2585 -0.0299 0.0019  0.0364  271 ASP A OD2 
1603 N  N   . VAL A 272 ? 0.1451 0.1806 0.2088 -0.0277 -0.0032 0.0251  272 VAL A N   
1604 C  CA  . VAL A 272 ? 0.1168 0.1454 0.1692 -0.0242 -0.0030 0.0238  272 VAL A CA  
1605 C  C   . VAL A 272 ? 0.1329 0.1529 0.1811 -0.0257 -0.0021 0.0236  272 VAL A C   
1606 O  O   . VAL A 272 ? 0.1382 0.1558 0.1914 -0.0294 -0.0031 0.0230  272 VAL A O   
1607 C  CB  . VAL A 272 ? 0.1532 0.1823 0.2019 -0.0228 -0.0071 0.0205  272 VAL A CB  
1608 C  CG1 . VAL A 272 ? 0.1882 0.2137 0.2365 -0.0260 -0.0106 0.0166  272 VAL A CG1 
1609 C  CG2 . VAL A 272 ? 0.1654 0.1899 0.2049 -0.0185 -0.0059 0.0208  272 VAL A CG2 
1610 N  N   . ILE A 273 ? 0.1082 0.1236 0.1479 -0.0229 0.0000  0.0242  273 ILE A N   
1611 C  CA  . ILE A 273 ? 0.1026 0.1109 0.1375 -0.0235 0.0005  0.0241  273 ILE A CA  
1612 C  C   . ILE A 273 ? 0.1367 0.1405 0.1666 -0.0231 -0.0026 0.0203  273 ILE A C   
1613 O  O   . ILE A 273 ? 0.1313 0.1357 0.1566 -0.0207 -0.0034 0.0192  273 ILE A O   
1614 C  CB  . ILE A 273 ? 0.1079 0.1154 0.1364 -0.0208 0.0037  0.0261  273 ILE A CB  
1615 C  CG1 . ILE A 273 ? 0.1468 0.1601 0.1793 -0.0206 0.0074  0.0301  273 ILE A CG1 
1616 C  CG2 . ILE A 273 ? 0.1394 0.1409 0.1626 -0.0209 0.0036  0.0260  273 ILE A CG2 
1617 C  CD1 . ILE A 273 ? 0.2024 0.2151 0.2407 -0.0236 0.0086  0.0339  273 ILE A CD1 
1618 N  N   . SER A 274 ? 0.0993 0.0988 0.1304 -0.0252 -0.0041 0.0185  274 SER A N   
1619 C  CA  . SER A 274 ? 0.0979 0.0941 0.1237 -0.0244 -0.0066 0.0148  274 SER A CA  
1620 C  C   . SER A 274 ? 0.1083 0.0991 0.1281 -0.0229 -0.0051 0.0156  274 SER A C   
1621 O  O   . SER A 274 ? 0.1074 0.0960 0.1285 -0.0234 -0.0031 0.0183  274 SER A O   
1622 C  CB  . SER A 274 ? 0.1337 0.1290 0.1642 -0.0271 -0.0094 0.0109  274 SER A CB  
1623 O  OG  . SER A 274 ? 0.1554 0.1465 0.1918 -0.0295 -0.0080 0.0121  274 SER A OG  
1624 N  N   . LYS A 275 ? 0.1017 0.0915 0.1153 -0.0211 -0.0061 0.0139  275 LYS A N   
1625 C  CA  . LYS A 275 ? 0.0954 0.0818 0.1038 -0.0197 -0.0049 0.0147  275 LYS A CA  
1626 C  C   . LYS A 275 ? 0.1045 0.0898 0.1089 -0.0188 -0.0065 0.0121  275 LYS A C   
1627 O  O   . LYS A 275 ? 0.1072 0.0952 0.1102 -0.0182 -0.0080 0.0107  275 LYS A O   
1628 C  CB  . LYS A 275 ? 0.0984 0.0863 0.1036 -0.0182 -0.0033 0.0165  275 LYS A CB  
1629 C  CG  . LYS A 275 ? 0.1546 0.1404 0.1547 -0.0172 -0.0025 0.0168  275 LYS A CG  
1630 C  CD  . LYS A 275 ? 0.1635 0.1506 0.1618 -0.0162 -0.0010 0.0173  275 LYS A CD  
1631 C  CE  . LYS A 275 ? 0.3625 0.3484 0.3567 -0.0159 -0.0007 0.0167  275 LYS A CE  
1632 N  NZ  . LYS A 275 ? 0.3410 0.3276 0.3336 -0.0150 0.0006  0.0157  275 LYS A NZ  
1633 N  N   . THR A 276 ? 0.1057 0.0879 0.1082 -0.0182 -0.0058 0.0120  276 THR A N   
1634 C  CA  . THR A 276 ? 0.1035 0.0857 0.1020 -0.0169 -0.0065 0.0101  276 THR A CA  
1635 C  C   . THR A 276 ? 0.1097 0.0907 0.1057 -0.0159 -0.0051 0.0119  276 THR A C   
1636 O  O   . THR A 276 ? 0.1168 0.0969 0.1141 -0.0161 -0.0040 0.0142  276 THR A O   
1637 C  CB  . THR A 276 ? 0.1276 0.1088 0.1277 -0.0170 -0.0080 0.0062  276 THR A CB  
1638 O  OG1 . THR A 276 ? 0.1335 0.1171 0.1288 -0.0153 -0.0086 0.0042  276 THR A OG1 
1639 C  CG2 . THR A 276 ? 0.1765 0.1528 0.1797 -0.0170 -0.0069 0.0062  276 THR A CG2 
1640 N  N   . SER A 277 ? 0.0974 0.0798 0.0900 -0.0147 -0.0052 0.0113  277 SER A N   
1641 C  CA  . SER A 277 ? 0.1272 0.1100 0.1183 -0.0140 -0.0042 0.0128  277 SER A CA  
1642 C  C   . SER A 277 ? 0.1427 0.1265 0.1327 -0.0125 -0.0041 0.0112  277 SER A C   
1643 O  O   . SER A 277 ? 0.1442 0.1296 0.1325 -0.0118 -0.0047 0.0091  277 SER A O   
1644 C  CB  . SER A 277 ? 0.1487 0.1331 0.1379 -0.0145 -0.0039 0.0142  277 SER A CB  
1645 O  OG  . SER A 277 ? 0.2052 0.1888 0.1952 -0.0154 -0.0036 0.0150  277 SER A OG  
1646 N  N   . ILE A 278 ? 0.1349 0.1187 0.1258 -0.0115 -0.0033 0.0123  278 ILE A N   
1647 C  CA  . ILE A 278 ? 0.1138 0.0993 0.1041 -0.0094 -0.0026 0.0111  278 ILE A CA  
1648 C  C   . ILE A 278 ? 0.1224 0.1117 0.1126 -0.0092 -0.0019 0.0138  278 ILE A C   
1649 O  O   . ILE A 278 ? 0.1238 0.1136 0.1149 -0.0104 -0.0021 0.0159  278 ILE A O   
1650 C  CB  . ILE A 278 ? 0.2246 0.2063 0.2181 -0.0078 -0.0024 0.0095  278 ILE A CB  
1651 C  CG1 . ILE A 278 ? 0.3192 0.3026 0.3122 -0.0048 -0.0014 0.0072  278 ILE A CG1 
1652 C  CG2 . ILE A 278 ? 0.3190 0.2994 0.3154 -0.0077 -0.0019 0.0131  278 ILE A CG2 
1653 C  CD1 . ILE A 278 ? 0.3404 0.3185 0.3363 -0.0034 -0.0014 0.0032  278 ILE A CD1 
1654 N  N   . MET A 279 ? 0.1070 0.1003 0.0963 -0.0080 -0.0010 0.0137  279 MET A N   
1655 C  CA  . MET A 279 ? 0.1319 0.1300 0.1226 -0.0081 -0.0003 0.0160  279 MET A CA  
1656 C  C   . MET A 279 ? 0.1584 0.1583 0.1513 -0.0049 0.0006  0.0158  279 MET A C   
1657 O  O   . MET A 279 ? 0.1703 0.1690 0.1626 -0.0024 0.0014  0.0132  279 MET A O   
1658 C  CB  . MET A 279 ? 0.1698 0.1724 0.1595 -0.0087 0.0007  0.0172  279 MET A CB  
1659 C  CG  . MET A 279 ? 0.2504 0.2512 0.2391 -0.0113 0.0002  0.0183  279 MET A CG  
1660 S  SD  . MET A 279 ? 0.2889 0.2949 0.2766 -0.0110 0.0020  0.0208  279 MET A SD  
1661 C  CE  . MET A 279 ? 0.3530 0.3605 0.3360 -0.0075 0.0022  0.0179  279 MET A CE  
1662 N  N   . LEU A 280 ? 0.1085 0.1116 0.1041 -0.0048 0.0004  0.0183  280 LEU A N   
1663 C  CA  . LEU A 280 ? 0.1092 0.1156 0.1078 -0.0014 0.0015  0.0191  280 LEU A CA  
1664 C  C   . LEU A 280 ? 0.1094 0.1243 0.1098 -0.0016 0.0023  0.0208  280 LEU A C   
1665 O  O   . LEU A 280 ? 0.1364 0.1538 0.1365 -0.0051 0.0017  0.0218  280 LEU A O   
1666 C  CB  . LEU A 280 ? 0.1127 0.1186 0.1139 -0.0004 0.0006  0.0218  280 LEU A CB  
1667 C  CG  . LEU A 280 ? 0.1420 0.1399 0.1428 -0.0005 0.0002  0.0212  280 LEU A CG  
1668 C  CD1 . LEU A 280 ? 0.1732 0.1720 0.1769 0.0011  0.0000  0.0254  280 LEU A CD1 
1669 C  CD2 . LEU A 280 ? 0.1467 0.1387 0.1481 0.0015  0.0013  0.0175  280 LEU A CD2 
1670 N  N   . GLY A 281 ? 0.1064 0.1255 0.1095 0.0021  0.0038  0.0212  281 GLY A N   
1671 C  CA  . GLY A 281 ? 0.1465 0.1750 0.1524 0.0023  0.0050  0.0231  281 GLY A CA  
1672 C  C   . GLY A 281 ? 0.1540 0.1854 0.1579 0.0039  0.0076  0.0218  281 GLY A C   
1673 O  O   . GLY A 281 ? 0.1853 0.2251 0.1918 0.0031  0.0090  0.0242  281 GLY A O   
1674 N  N   . LEU A 282 ? 0.1347 0.1604 0.1344 0.0058  0.0082  0.0181  282 LEU A N   
1675 C  CA  . LEU A 282 ? 0.1616 0.1911 0.1579 0.0079  0.0104  0.0163  282 LEU A CA  
1676 C  C   . LEU A 282 ? 0.1781 0.2084 0.1748 0.0137  0.0125  0.0127  282 LEU A C   
1677 O  O   . LEU A 282 ? 0.2305 0.2636 0.2231 0.0162  0.0143  0.0096  282 LEU A O   
1678 C  CB  . LEU A 282 ? 0.1845 0.2086 0.1751 0.0061  0.0092  0.0138  282 LEU A CB  
1679 C  CG  . LEU A 282 ? 0.2579 0.2812 0.2478 0.0013  0.0079  0.0171  282 LEU A CG  
1680 C  CD1 . LEU A 282 ? 0.3166 0.3327 0.3029 -0.0001 0.0058  0.0146  282 LEU A CD1 
1681 C  CD2 . LEU A 282 ? 0.3194 0.3504 0.3085 0.0008  0.0100  0.0204  282 LEU A CD2 
1682 N  N   . GLY A 283 ? 0.2020 0.2304 0.2034 0.0162  0.0124  0.0130  283 GLY A N   
1683 C  CA  . GLY A 283 ? 0.2792 0.3074 0.2824 0.0222  0.0147  0.0096  283 GLY A CA  
1684 C  C   . GLY A 283 ? 0.2311 0.2475 0.2348 0.0238  0.0137  0.0052  283 GLY A C   
1685 O  O   . GLY A 283 ? 0.2594 0.2736 0.2656 0.0290  0.0156  0.0018  283 GLY A O   
1686 N  N   . GLU A 284 ? 0.1854 0.1942 0.1877 0.0197  0.0110  0.0053  284 GLU A N   
1687 C  CA  . GLU A 284 ? 0.1679 0.1658 0.1724 0.0204  0.0102  0.0021  284 GLU A CA  
1688 C  C   . GLU A 284 ? 0.2000 0.1956 0.2114 0.0237  0.0109  0.0058  284 GLU A C   
1689 O  O   . GLU A 284 ? 0.2314 0.2340 0.2453 0.0238  0.0108  0.0115  284 GLU A O   
1690 C  CB  . GLU A 284 ? 0.1663 0.1588 0.1687 0.0150  0.0074  0.0029  284 GLU A CB  
1691 C  CG  . GLU A 284 ? 0.1782 0.1723 0.1825 0.0122  0.0061  0.0095  284 GLU A CG  
1692 C  CD  . GLU A 284 ? 0.1865 0.1904 0.1892 0.0105  0.0061  0.0131  284 GLU A CD  
1693 O  OE1 . GLU A 284 ? 0.1782 0.1859 0.1772 0.0093  0.0066  0.0116  284 GLU A OE1 
1694 O  OE2 . GLU A 284 ? 0.1781 0.1860 0.1839 0.0101  0.0055  0.0175  284 GLU A OE2 
1695 N  N   . ASN A 285 ? 0.1695 0.1556 0.1849 0.0265  0.0116  0.0025  285 ASN A N   
1696 C  CA  . ASN A 285 ? 0.1856 0.1682 0.2084 0.0297  0.0123  0.0072  285 ASN A CA  
1697 C  C   . ASN A 285 ? 0.1772 0.1505 0.2024 0.0264  0.0107  0.0096  285 ASN A C   
1698 O  O   . ASN A 285 ? 0.1844 0.1534 0.2064 0.0220  0.0091  0.0063  285 ASN A O   
1699 C  CB  . ASN A 285 ? 0.2800 0.2590 0.3077 0.0364  0.0152  0.0032  285 ASN A CB  
1700 C  CG  . ASN A 285 ? 0.2463 0.2136 0.2746 0.0365  0.0154  -0.0051 285 ASN A CG  
1701 O  OD1 . ASN A 285 ? 0.2409 0.1997 0.2707 0.0326  0.0137  -0.0053 285 ASN A OD1 
1702 N  ND2 . ASN A 285 ? 0.2818 0.2493 0.3093 0.0410  0.0175  -0.0126 285 ASN A ND2 
1703 N  N   . ASP A 286 ? 0.2004 0.1718 0.2318 0.0288  0.0112  0.0160  286 ASP A N   
1704 C  CA  . ASP A 286 ? 0.1708 0.1358 0.2047 0.0258  0.0101  0.0204  286 ASP A CA  
1705 C  C   . ASP A 286 ? 0.2173 0.1694 0.2546 0.0245  0.0104  0.0151  286 ASP A C   
1706 O  O   . ASP A 286 ? 0.2413 0.1894 0.2783 0.0198  0.0091  0.0159  286 ASP A O   
1707 C  CB  . ASP A 286 ? 0.2075 0.1740 0.2474 0.0297  0.0109  0.0291  286 ASP A CB  
1708 C  CG  . ASP A 286 ? 0.2712 0.2513 0.3078 0.0295  0.0095  0.0347  286 ASP A CG  
1709 O  OD1 . ASP A 286 ? 0.2752 0.2625 0.3059 0.0264  0.0083  0.0316  286 ASP A OD1 
1710 O  OD2 . ASP A 286 ? 0.3198 0.3037 0.3602 0.0322  0.0095  0.0423  286 ASP A OD2 
1711 N  N   . GLU A 287 ? 0.2147 0.1606 0.2562 0.0286  0.0123  0.0095  287 GLU A N   
1712 C  CA  A GLU A 287 ? 0.2232 0.1568 0.2690 0.0271  0.0123  0.0029  287 GLU A CA  
1713 C  CA  B GLU A 287 ? 0.2235 0.1571 0.2693 0.0270  0.0123  0.0028  287 GLU A CA  
1714 C  C   . GLU A 287 ? 0.1929 0.1281 0.2317 0.0216  0.0099  -0.0040 287 GLU A C   
1715 O  O   . GLU A 287 ? 0.2225 0.1509 0.2639 0.0173  0.0086  -0.0059 287 GLU A O   
1716 C  CB  A GLU A 287 ? 0.2658 0.1937 0.3165 0.0331  0.0148  -0.0033 287 GLU A CB  
1717 C  CB  B GLU A 287 ? 0.2657 0.1934 0.3162 0.0329  0.0147  -0.0037 287 GLU A CB  
1718 C  CG  A GLU A 287 ? 0.3346 0.2606 0.3938 0.0396  0.0174  0.0042  287 GLU A CG  
1719 C  CG  B GLU A 287 ? 0.3554 0.2690 0.4124 0.0317  0.0148  -0.0113 287 GLU A CG  
1720 C  CD  A GLU A 287 ? 0.3677 0.3079 0.4238 0.0425  0.0176  0.0122  287 GLU A CD  
1721 C  CD  B GLU A 287 ? 0.3555 0.2651 0.4145 0.0375  0.0169  -0.0208 287 GLU A CD  
1722 O  OE1 A GLU A 287 ? 0.2799 0.2306 0.3296 0.0433  0.0175  0.0092  287 GLU A OE1 
1723 O  OE1 B GLU A 287 ? 0.3694 0.2846 0.4287 0.0436  0.0193  -0.0181 287 GLU A OE1 
1724 O  OE2 A GLU A 287 ? 0.4862 0.4279 0.5469 0.0441  0.0178  0.0220  287 GLU A OE2 
1725 O  OE2 B GLU A 287 ? 0.4078 0.3098 0.4679 0.0359  0.0162  -0.0314 287 GLU A OE2 
1726 N  N   . GLN A 288 ? 0.2143 0.1593 0.2447 0.0218  0.0094  -0.0069 288 GLN A N   
1727 C  CA  . GLN A 288 ? 0.1938 0.1420 0.2173 0.0175  0.0072  -0.0121 288 GLN A CA  
1728 C  C   . GLN A 288 ? 0.1723 0.1226 0.1939 0.0121  0.0052  -0.0064 288 GLN A C   
1729 O  O   . GLN A 288 ? 0.1875 0.1357 0.2078 0.0081  0.0033  -0.0098 288 GLN A O   
1730 C  CB  . GLN A 288 ? 0.1795 0.1383 0.1953 0.0195  0.0078  -0.0145 288 GLN A CB  
1731 C  CG  . GLN A 288 ? 0.2124 0.1700 0.2289 0.0249  0.0099  -0.0219 288 GLN A CG  
1732 C  CD  . GLN A 288 ? 0.2235 0.1932 0.2336 0.0278  0.0114  -0.0222 288 GLN A CD  
1733 O  OE1 . GLN A 288 ? 0.2088 0.1865 0.2170 0.0269  0.0116  -0.0152 288 GLN A OE1 
1734 N  NE2 . GLN A 288 ? 0.2465 0.2179 0.2532 0.0312  0.0127  -0.0306 288 GLN A NE2 
1735 N  N   . VAL A 289 ? 0.1508 0.1064 0.1720 0.0123  0.0056  0.0017  289 VAL A N   
1736 C  CA  . VAL A 289 ? 0.1342 0.0921 0.1532 0.0079  0.0040  0.0065  289 VAL A CA  
1737 C  C   . VAL A 289 ? 0.1553 0.1049 0.1805 0.0056  0.0039  0.0083  289 VAL A C   
1738 O  O   . VAL A 289 ? 0.1712 0.1201 0.1955 0.0014  0.0025  0.0074  289 VAL A O   
1739 C  CB  . VAL A 289 ? 0.1688 0.1345 0.1863 0.0088  0.0042  0.0136  289 VAL A CB  
1740 C  CG1 . VAL A 289 ? 0.1675 0.1351 0.1829 0.0047  0.0029  0.0179  289 VAL A CG1 
1741 C  CG2 . VAL A 289 ? 0.1588 0.1331 0.1711 0.0098  0.0043  0.0119  289 VAL A CG2 
1742 N  N   . TYR A 290 ? 0.1615 0.1052 0.1940 0.0085  0.0056  0.0116  290 TYR A N   
1743 C  CA  . TYR A 290 ? 0.1842 0.1198 0.2241 0.0062  0.0060  0.0145  290 TYR A CA  
1744 C  C   . TYR A 290 ? 0.1809 0.1098 0.2235 0.0028  0.0048  0.0063  290 TYR A C   
1745 O  O   . TYR A 290 ? 0.1967 0.1239 0.2419 -0.0016 0.0040  0.0075  290 TYR A O   
1746 C  CB  . TYR A 290 ? 0.1894 0.1191 0.2376 0.0106  0.0084  0.0196  290 TYR A CB  
1747 C  CG  . TYR A 290 ? 0.2868 0.2089 0.3436 0.0085  0.0095  0.0251  290 TYR A CG  
1748 C  CD1 . TYR A 290 ? 0.3708 0.2978 0.4276 0.0081  0.0101  0.0353  290 TYR A CD1 
1749 C  CD2 . TYR A 290 ? 0.2624 0.1730 0.3278 0.0068  0.0100  0.0202  290 TYR A CD2 
1750 C  CE1 . TYR A 290 ? 0.3054 0.2264 0.3703 0.0062  0.0117  0.0414  290 TYR A CE1 
1751 C  CE2 . TYR A 290 ? 0.3305 0.2340 0.4052 0.0043  0.0113  0.0259  290 TYR A CE2 
1752 C  CZ  . TYR A 290 ? 0.2938 0.2029 0.3682 0.0042  0.0123  0.0370  290 TYR A CZ  
1753 O  OH  . TYR A 290 ? 0.4281 0.3311 0.5121 0.0019  0.0142  0.0439  290 TYR A OH  
1754 N  N   . ALA A 291 ? 0.1930 0.1191 0.2351 0.0049  0.0047  -0.0024 291 ALA A N   
1755 C  CA  . ALA A 291 ? 0.2086 0.1296 0.2527 0.0017  0.0030  -0.0115 291 ALA A CA  
1756 C  C   . ALA A 291 ? 0.1832 0.1119 0.2203 -0.0026 0.0003  -0.0133 291 ALA A C   
1757 O  O   . ALA A 291 ? 0.2303 0.1566 0.2709 -0.0070 -0.0015 -0.0165 291 ALA A O   
1758 C  CB  . ALA A 291 ? 0.2093 0.1283 0.2521 0.0055  0.0033  -0.0211 291 ALA A CB  
1759 N  N   . THR A 292 ? 0.1675 0.1058 0.1957 -0.0015 0.0000  -0.0108 292 THR A N   
1760 C  CA  . THR A 292 ? 0.1692 0.1144 0.1914 -0.0049 -0.0021 -0.0113 292 THR A CA  
1761 C  C   . THR A 292 ? 0.1858 0.1306 0.2115 -0.0086 -0.0024 -0.0051 292 THR A C   
1762 O  O   . THR A 292 ? 0.1792 0.1252 0.2054 -0.0123 -0.0042 -0.0071 292 THR A O   
1763 C  CB  . THR A 292 ? 0.1928 0.1470 0.2065 -0.0030 -0.0018 -0.0090 292 THR A CB  
1764 O  OG1 . THR A 292 ? 0.2185 0.1747 0.2289 0.0006  -0.0012 -0.0146 292 THR A OG1 
1765 C  CG2 . THR A 292 ? 0.1903 0.1507 0.1986 -0.0060 -0.0037 -0.0084 292 THR A CG2 
1766 N  N   . MET A 293 ? 0.1670 0.1112 0.1948 -0.0074 -0.0005 0.0027  293 MET A N   
1767 C  CA  . MET A 293 ? 0.1342 0.0790 0.1648 -0.0103 -0.0001 0.0090  293 MET A CA  
1768 C  C   . MET A 293 ? 0.1718 0.1096 0.2118 -0.0135 -0.0002 0.0077  293 MET A C   
1769 O  O   . MET A 293 ? 0.1836 0.1236 0.2253 -0.0171 -0.0009 0.0090  293 MET A O   
1770 C  CB  . MET A 293 ? 0.1689 0.1155 0.1996 -0.0077 0.0018  0.0172  293 MET A CB  
1771 C  CG  . MET A 293 ? 0.1706 0.1255 0.1928 -0.0060 0.0013  0.0181  293 MET A CG  
1772 S  SD  . MET A 293 ? 0.2424 0.2022 0.2639 -0.0029 0.0027  0.0265  293 MET A SD  
1773 C  CE  . MET A 293 ? 0.2212 0.1820 0.2443 -0.0057 0.0033  0.0323  293 MET A CE  
1774 N  N   . LYS A 294 ? 0.1862 0.1154 0.2331 -0.0122 0.0006  0.0048  294 LYS A N   
1775 C  CA  . LYS A 294 ? 0.2198 0.1413 0.2773 -0.0159 0.0005  0.0027  294 LYS A CA  
1776 C  C   . LYS A 294 ? 0.2108 0.1349 0.2674 -0.0197 -0.0027 -0.0059 294 LYS A C   
1777 O  O   . LYS A 294 ? 0.2129 0.1362 0.2762 -0.0243 -0.0035 -0.0055 294 LYS A O   
1778 C  CB  . LYS A 294 ? 0.2778 0.1886 0.3435 -0.0135 0.0019  0.0001  294 LYS A CB  
1779 C  CG  . LYS A 294 ? 0.3720 0.2786 0.4430 -0.0104 0.0052  0.0101  294 LYS A CG  
1780 C  CD  . LYS A 294 ? 0.3866 0.2805 0.4688 -0.0087 0.0068  0.0073  294 LYS A CD  
1781 C  CE  . LYS A 294 ? 0.5196 0.4052 0.6139 -0.0143 0.0067  0.0060  294 LYS A CE  
1782 N  NZ  . LYS A 294 ? 0.5208 0.4094 0.6191 -0.0164 0.0086  0.0182  294 LYS A NZ  
1783 N  N   . ALA A 295 ? 0.2040 0.1318 0.2526 -0.0178 -0.0046 -0.0134 295 ALA A N   
1784 C  CA  . ALA A 295 ? 0.1772 0.1096 0.2235 -0.0207 -0.0080 -0.0213 295 ALA A CA  
1785 C  C   . ALA A 295 ? 0.1778 0.1186 0.2211 -0.0234 -0.0091 -0.0168 295 ALA A C   
1786 O  O   . ALA A 295 ? 0.2090 0.1524 0.2558 -0.0273 -0.0115 -0.0201 295 ALA A O   
1787 C  CB  . ALA A 295 ? 0.2522 0.1892 0.2891 -0.0172 -0.0091 -0.0283 295 ALA A CB  
1788 N  N   . LEU A 296 ? 0.1629 0.1083 0.2000 -0.0213 -0.0074 -0.0096 296 LEU A N   
1789 C  CA  . LEU A 296 ? 0.1595 0.1120 0.1937 -0.0232 -0.0080 -0.0054 296 LEU A CA  
1790 C  C   . LEU A 296 ? 0.1478 0.0985 0.1913 -0.0267 -0.0070 -0.0008 296 LEU A C   
1791 O  O   . LEU A 296 ? 0.1847 0.1402 0.2300 -0.0296 -0.0084 -0.0012 296 LEU A O   
1792 C  CB  . LEU A 296 ? 0.1371 0.0938 0.1634 -0.0202 -0.0063 0.0002  296 LEU A CB  
1793 C  CG  . LEU A 296 ? 0.1627 0.1234 0.1806 -0.0175 -0.0073 -0.0035 296 LEU A CG  
1794 C  CD1 . LEU A 296 ? 0.1810 0.1445 0.1936 -0.0150 -0.0055 0.0016  296 LEU A CD1 
1795 C  CD2 . LEU A 296 ? 0.1750 0.1421 0.1891 -0.0188 -0.0097 -0.0066 296 LEU A CD2 
1796 N  N   . ARG A 297 ? 0.1896 0.1340 0.2392 -0.0263 -0.0044 0.0042  297 ARG A N   
1797 C  CA  . ARG A 297 ? 0.2102 0.1531 0.2694 -0.0298 -0.0029 0.0094  297 ARG A CA  
1798 C  C   . ARG A 297 ? 0.2601 0.2005 0.3286 -0.0344 -0.0052 0.0031  297 ARG A C   
1799 O  O   . ARG A 297 ? 0.2634 0.2080 0.3376 -0.0381 -0.0055 0.0052  297 ARG A O   
1800 C  CB  . ARG A 297 ? 0.2696 0.2061 0.3344 -0.0282 0.0004  0.0166  297 ARG A CB  
1801 C  CG  . ARG A 297 ? 0.2910 0.2326 0.3481 -0.0246 0.0024  0.0239  297 ARG A CG  
1802 C  CD  . ARG A 297 ? 0.2331 0.1834 0.2869 -0.0262 0.0028  0.0277  297 ARG A CD  
1803 N  NE  . ARG A 297 ? 0.2125 0.1629 0.2758 -0.0293 0.0049  0.0334  297 ARG A NE  
1804 C  CZ  . ARG A 297 ? 0.2888 0.2455 0.3539 -0.0320 0.0048  0.0342  297 ARG A CZ  
1805 N  NH1 . ARG A 297 ? 0.2457 0.2085 0.3038 -0.0318 0.0028  0.0298  297 ARG A NH1 
1806 N  NH2 . ARG A 297 ? 0.2580 0.2149 0.3329 -0.0349 0.0072  0.0399  297 ARG A NH2 
1807 N  N   . GLU A 298 ? 0.2608 0.1951 0.3311 -0.0342 -0.0069 -0.0051 298 GLU A N   
1808 C  CA  A GLU A 298 ? 0.2803 0.2126 0.3597 -0.0390 -0.0097 -0.0125 298 GLU A CA  
1809 C  CA  B GLU A 298 ? 0.2812 0.2134 0.3602 -0.0389 -0.0098 -0.0130 298 GLU A CA  
1810 C  C   . GLU A 298 ? 0.3415 0.2845 0.4163 -0.0410 -0.0133 -0.0168 298 GLU A C   
1811 O  O   . GLU A 298 ? 0.4047 0.3501 0.4883 -0.0459 -0.0153 -0.0193 298 GLU A O   
1812 C  CB  A GLU A 298 ? 0.2896 0.2129 0.3711 -0.0377 -0.0106 -0.0215 298 GLU A CB  
1813 C  CB  B GLU A 298 ? 0.2912 0.2160 0.3702 -0.0371 -0.0111 -0.0226 298 GLU A CB  
1814 C  CG  A GLU A 298 ? 0.2853 0.1970 0.3747 -0.0360 -0.0068 -0.0163 298 GLU A CG  
1815 C  CG  B GLU A 298 ? 0.3353 0.2601 0.4199 -0.0414 -0.0152 -0.0339 298 GLU A CG  
1816 C  CD  A GLU A 298 ? 0.4224 0.3249 0.5129 -0.0330 -0.0069 -0.0246 298 GLU A CD  
1817 C  CD  B GLU A 298 ? 0.3930 0.3069 0.4935 -0.0456 -0.0144 -0.0355 298 GLU A CD  
1818 O  OE1 A GLU A 298 ? 0.4807 0.3859 0.5660 -0.0327 -0.0100 -0.0355 298 GLU A OE1 
1819 O  OE1 B GLU A 298 ? 0.4763 0.3868 0.5823 -0.0459 -0.0107 -0.0252 298 GLU A OE1 
1820 O  OE2 A GLU A 298 ? 0.3978 0.2908 0.4943 -0.0304 -0.0037 -0.0202 298 GLU A OE2 
1821 O  OE2 B GLU A 298 ? 0.3977 0.3096 0.5000 -0.0471 -0.0170 -0.0456 298 GLU A OE2 
1822 N  N   . ALA A 299 ? 0.2608 0.2111 0.3231 -0.0374 -0.0141 -0.0170 299 ALA A N   
1823 C  CA  . ALA A 299 ? 0.2744 0.2355 0.3323 -0.0382 -0.0169 -0.0185 299 ALA A CA  
1824 C  C   . ALA A 299 ? 0.3050 0.2716 0.3649 -0.0393 -0.0150 -0.0101 299 ALA A C   
1825 O  O   . ALA A 299 ? 0.3686 0.3440 0.4246 -0.0390 -0.0167 -0.0100 299 ALA A O   
1826 C  CB  . ALA A 299 ? 0.2710 0.2369 0.3159 -0.0338 -0.0178 -0.0207 299 ALA A CB  
1827 N  N   . ASP A 300 ? 0.2226 0.1847 0.2879 -0.0398 -0.0114 -0.0028 300 ASP A N   
1828 C  CA  . ASP A 300 ? 0.2381 0.2058 0.3053 -0.0405 -0.0090 0.0050  300 ASP A CA  
1829 C  C   . ASP A 300 ? 0.2404 0.2137 0.2959 -0.0364 -0.0082 0.0080  300 ASP A C   
1830 O  O   . ASP A 300 ? 0.2002 0.1805 0.2554 -0.0364 -0.0076 0.0111  300 ASP A O   
1831 C  CB  . ASP A 300 ? 0.2994 0.2737 0.3755 -0.0449 -0.0110 0.0036  300 ASP A CB  
1832 C  CG  . ASP A 300 ? 0.3235 0.3023 0.4055 -0.0462 -0.0076 0.0121  300 ASP A CG  
1833 O  OD1 . ASP A 300 ? 0.3800 0.3548 0.4627 -0.0451 -0.0037 0.0188  300 ASP A OD1 
1834 O  OD2 . ASP A 300 ? 0.4545 0.4420 0.5406 -0.0481 -0.0087 0.0123  300 ASP A OD2 
1835 N  N   . VAL A 301 ? 0.1734 0.1437 0.2203 -0.0328 -0.0079 0.0071  301 VAL A N   
1836 C  CA  . VAL A 301 ? 0.1439 0.1183 0.1814 -0.0295 -0.0069 0.0100  301 VAL A CA  
1837 C  C   . VAL A 301 ? 0.1467 0.1211 0.1846 -0.0287 -0.0034 0.0172  301 VAL A C   
1838 O  O   . VAL A 301 ? 0.1721 0.1417 0.2122 -0.0282 -0.0016 0.0202  301 VAL A O   
1839 C  CB  . VAL A 301 ? 0.1331 0.1051 0.1625 -0.0264 -0.0075 0.0070  301 VAL A CB  
1840 C  CG1 . VAL A 301 ? 0.1485 0.1239 0.1699 -0.0238 -0.0063 0.0103  301 VAL A CG1 
1841 C  CG2 . VAL A 301 ? 0.1475 0.1215 0.1753 -0.0268 -0.0108 0.0001  301 VAL A CG2 
1842 N  N   . ASP A 302 ? 0.1077 0.0881 0.1432 -0.0280 -0.0023 0.0201  302 ASP A N   
1843 C  CA  . ASP A 302 ? 0.1322 0.1147 0.1679 -0.0273 0.0010  0.0264  302 ASP A CA  
1844 C  C   . ASP A 302 ? 0.1247 0.1063 0.1523 -0.0242 0.0022  0.0282  302 ASP A C   
1845 O  O   . ASP A 302 ? 0.1415 0.1232 0.1697 -0.0234 0.0044  0.0332  302 ASP A O   
1846 C  CB  . ASP A 302 ? 0.1423 0.1322 0.1783 -0.0273 0.0020  0.0277  302 ASP A CB  
1847 C  CG  . ASP A 302 ? 0.2082 0.2011 0.2540 -0.0306 0.0012  0.0274  302 ASP A CG  
1848 O  OD1 . ASP A 302 ? 0.1915 0.1821 0.2457 -0.0333 0.0023  0.0298  302 ASP A OD1 
1849 O  OD2 . ASP A 302 ? 0.1667 0.1646 0.2128 -0.0305 -0.0003 0.0249  302 ASP A OD2 
1850 N  N   . CYS A 303 ? 0.1140 0.0960 0.1344 -0.0224 0.0006  0.0247  303 CYS A N   
1851 C  CA  . CYS A 303 ? 0.1080 0.0910 0.1213 -0.0200 0.0014  0.0258  303 CYS A CA  
1852 C  C   . CYS A 303 ? 0.1192 0.0993 0.1288 -0.0190 -0.0004 0.0224  303 CYS A C   
1853 O  O   . CYS A 303 ? 0.0993 0.0786 0.1089 -0.0195 -0.0022 0.0186  303 CYS A O   
1854 C  CB  . CYS A 303 ? 0.1468 0.1342 0.1557 -0.0190 0.0020  0.0253  303 CYS A CB  
1855 S  SG  . CYS A 303 ? 0.2282 0.2210 0.2410 -0.0195 0.0047  0.0290  303 CYS A SG  
1856 N  N   . LEU A 304 ? 0.1156 0.0955 0.1218 -0.0174 0.0001  0.0239  304 LEU A N   
1857 C  CA  . LEU A 304 ? 0.1211 0.0994 0.1245 -0.0162 -0.0011 0.0214  304 LEU A CA  
1858 C  C   . LEU A 304 ? 0.1191 0.1007 0.1174 -0.0151 -0.0010 0.0222  304 LEU A C   
1859 O  O   . LEU A 304 ? 0.1223 0.1069 0.1195 -0.0146 0.0000  0.0251  304 LEU A O   
1860 C  CB  . LEU A 304 ? 0.1406 0.1150 0.1479 -0.0153 -0.0007 0.0224  304 LEU A CB  
1861 C  CG  . LEU A 304 ? 0.1513 0.1249 0.1565 -0.0133 -0.0013 0.0204  304 LEU A CG  
1862 C  CD1 . LEU A 304 ? 0.1743 0.1475 0.1779 -0.0137 -0.0026 0.0154  304 LEU A CD1 
1863 C  CD2 . LEU A 304 ? 0.1782 0.1475 0.1884 -0.0117 -0.0003 0.0222  304 LEU A CD2 
1864 N  N   . THR A 305 ? 0.0969 0.0789 0.0924 -0.0148 -0.0020 0.0196  305 THR A N   
1865 C  CA  . THR A 305 ? 0.1053 0.0905 0.0978 -0.0143 -0.0021 0.0200  305 THR A CA  
1866 C  C   . THR A 305 ? 0.1054 0.0906 0.0982 -0.0131 -0.0025 0.0194  305 THR A C   
1867 O  O   . THR A 305 ? 0.1193 0.1024 0.1127 -0.0128 -0.0027 0.0173  305 THR A O   
1868 C  CB  . THR A 305 ? 0.1402 0.1265 0.1301 -0.0153 -0.0024 0.0182  305 THR A CB  
1869 O  OG1 . THR A 305 ? 0.1902 0.1754 0.1799 -0.0155 -0.0029 0.0167  305 THR A OG1 
1870 C  CG2 . THR A 305 ? 0.1396 0.1256 0.1299 -0.0158 -0.0017 0.0181  305 THR A CG2 
1871 N  N   . LEU A 306 ? 0.1054 0.0939 0.0978 -0.0122 -0.0025 0.0211  306 LEU A N   
1872 C  CA  . LEU A 306 ? 0.0962 0.0865 0.0894 -0.0107 -0.0026 0.0209  306 LEU A CA  
1873 C  C   . LEU A 306 ? 0.1104 0.1061 0.1023 -0.0118 -0.0033 0.0211  306 LEU A C   
1874 O  O   . LEU A 306 ? 0.0991 0.0983 0.0900 -0.0123 -0.0039 0.0222  306 LEU A O   
1875 C  CB  . LEU A 306 ? 0.1195 0.1095 0.1157 -0.0081 -0.0020 0.0235  306 LEU A CB  
1876 C  CG  . LEU A 306 ? 0.1398 0.1236 0.1394 -0.0073 -0.0012 0.0236  306 LEU A CG  
1877 C  CD1 . LEU A 306 ? 0.2091 0.1931 0.2097 -0.0077 -0.0007 0.0275  306 LEU A CD1 
1878 C  CD2 . LEU A 306 ? 0.2443 0.2263 0.2474 -0.0042 -0.0003 0.0240  306 LEU A CD2 
1879 N  N   . GLY A 307 ? 0.1000 0.0974 0.0922 -0.0122 -0.0032 0.0199  307 GLY A N   
1880 C  CA  . GLY A 307 ? 0.0933 0.0956 0.0859 -0.0141 -0.0039 0.0198  307 GLY A CA  
1881 C  C   . GLY A 307 ? 0.0931 0.0991 0.0879 -0.0133 -0.0032 0.0204  307 GLY A C   
1882 O  O   . GLY A 307 ? 0.1176 0.1221 0.1125 -0.0110 -0.0021 0.0203  307 GLY A O   
1883 N  N   . GLN A 308 ? 0.0973 0.1088 0.0944 -0.0153 -0.0039 0.0207  308 GLN A N   
1884 C  CA  . GLN A 308 ? 0.0927 0.1097 0.0930 -0.0146 -0.0029 0.0220  308 GLN A CA  
1885 C  C   . GLN A 308 ? 0.1074 0.1226 0.1076 -0.0159 -0.0014 0.0221  308 GLN A C   
1886 O  O   . GLN A 308 ? 0.1307 0.1435 0.1312 -0.0190 -0.0017 0.0216  308 GLN A O   
1887 C  CB  . GLN A 308 ? 0.0928 0.1175 0.0968 -0.0168 -0.0045 0.0225  308 GLN A CB  
1888 C  CG  . GLN A 308 ? 0.0927 0.1247 0.1015 -0.0170 -0.0034 0.0242  308 GLN A CG  
1889 C  CD  . GLN A 308 ? 0.0937 0.1291 0.1034 -0.0121 -0.0021 0.0259  308 GLN A CD  
1890 O  OE1 . GLN A 308 ? 0.1088 0.1454 0.1184 -0.0096 -0.0031 0.0267  308 GLN A OE1 
1891 N  NE2 . GLN A 308 ? 0.0935 0.1315 0.1047 -0.0106 0.0004  0.0269  308 GLN A NE2 
1892 N  N   . TYR A 309 ? 0.0946 0.1120 0.0947 -0.0133 0.0004  0.0229  309 TYR A N   
1893 C  CA  . TYR A 309 ? 0.1163 0.1353 0.1166 -0.0140 0.0022  0.0243  309 TYR A CA  
1894 C  C   . TYR A 309 ? 0.1152 0.1404 0.1211 -0.0171 0.0025  0.0265  309 TYR A C   
1895 O  O   . TYR A 309 ? 0.1158 0.1479 0.1254 -0.0164 0.0025  0.0273  309 TYR A O   
1896 C  CB  . TYR A 309 ? 0.0972 0.1187 0.0954 -0.0100 0.0042  0.0240  309 TYR A CB  
1897 C  CG  . TYR A 309 ? 0.0988 0.1254 0.0975 -0.0104 0.0065  0.0268  309 TYR A CG  
1898 C  CD1 . TYR A 309 ? 0.1181 0.1417 0.1149 -0.0121 0.0067  0.0282  309 TYR A CD1 
1899 C  CD2 . TYR A 309 ? 0.1137 0.1488 0.1155 -0.0089 0.0087  0.0288  309 TYR A CD2 
1900 C  CE1 . TYR A 309 ? 0.1177 0.1465 0.1154 -0.0124 0.0092  0.0322  309 TYR A CE1 
1901 C  CE2 . TYR A 309 ? 0.1205 0.1614 0.1231 -0.0093 0.0113  0.0325  309 TYR A CE2 
1902 C  CZ  . TYR A 309 ? 0.1136 0.1509 0.1139 -0.0111 0.0115  0.0344  309 TYR A CZ  
1903 O  OH  . TYR A 309 ? 0.1351 0.1782 0.1365 -0.0115 0.0144  0.0394  309 TYR A OH  
1904 N  N   . MET A 310 ? 0.1213 0.1442 0.1289 -0.0205 0.0028  0.0278  310 MET A N   
1905 C  CA  . MET A 310 ? 0.1589 0.1866 0.1733 -0.0244 0.0034  0.0300  310 MET A CA  
1906 C  C   . MET A 310 ? 0.1309 0.1602 0.1464 -0.0244 0.0064  0.0342  310 MET A C   
1907 O  O   . MET A 310 ? 0.1807 0.2040 0.1933 -0.0243 0.0069  0.0350  310 MET A O   
1908 C  CB  . MET A 310 ? 0.1906 0.2134 0.2076 -0.0288 0.0013  0.0278  310 MET A CB  
1909 C  CG  . MET A 310 ? 0.2206 0.2427 0.2351 -0.0285 -0.0015 0.0239  310 MET A CG  
1910 S  SD  . MET A 310 ? 0.3016 0.3350 0.3215 -0.0295 -0.0030 0.0240  310 MET A SD  
1911 C  CE  . MET A 310 ? 0.2928 0.3270 0.3206 -0.0364 -0.0042 0.0226  310 MET A CE  
1912 N  N   . GLN A 311 ? 0.1453 0.1834 0.1653 -0.0244 0.0084  0.0374  311 GLN A N   
1913 C  CA  . GLN A 311 ? 0.1119 0.1538 0.1325 -0.0237 0.0119  0.0424  311 GLN A CA  
1914 C  C   . GLN A 311 ? 0.1557 0.1932 0.1817 -0.0285 0.0125  0.0457  311 GLN A C   
1915 O  O   . GLN A 311 ? 0.1806 0.2194 0.2149 -0.0332 0.0118  0.0458  311 GLN A O   
1916 C  CB  . GLN A 311 ? 0.1358 0.1894 0.1608 -0.0225 0.0144  0.0452  311 GLN A CB  
1917 C  CG  . GLN A 311 ? 0.1418 0.2017 0.1677 -0.0217 0.0186  0.0514  311 GLN A CG  
1918 C  CD  . GLN A 311 ? 0.1885 0.2611 0.2207 -0.0213 0.0213  0.0545  311 GLN A CD  
1919 O  OE1 . GLN A 311 ? 0.2459 0.3223 0.2858 -0.0245 0.0198  0.0538  311 GLN A OE1 
1920 N  NE2 . GLN A 311 ? 0.1746 0.2550 0.2036 -0.0172 0.0252  0.0577  311 GLN A NE2 
1921 N  N   . PRO A 312 ? 0.1584 0.1907 0.1809 -0.0274 0.0137  0.0483  312 PRO A N   
1922 C  CA  . PRO A 312 ? 0.1475 0.1739 0.1764 -0.0316 0.0143  0.0516  312 PRO A CA  
1923 C  C   . PRO A 312 ? 0.1899 0.2225 0.2277 -0.0346 0.0176  0.0584  312 PRO A C   
1924 O  O   . PRO A 312 ? 0.2703 0.2994 0.3174 -0.0400 0.0173  0.0590  312 PRO A O   
1925 C  CB  . PRO A 312 ? 0.1903 0.2115 0.2126 -0.0283 0.0149  0.0535  312 PRO A CB  
1926 C  CG  . PRO A 312 ? 0.2582 0.2799 0.2714 -0.0239 0.0130  0.0485  312 PRO A CG  
1927 C  CD  . PRO A 312 ? 0.1759 0.2062 0.1891 -0.0226 0.0135  0.0470  312 PRO A CD  
1928 N  N   . THR A 313 ? 0.1925 0.2346 0.2280 -0.0314 0.0209  0.0634  313 THR A N   
1929 C  CA  . THR A 313 ? 0.1943 0.2447 0.2382 -0.0338 0.0248  0.0711  313 THR A CA  
1930 C  C   . THR A 313 ? 0.2574 0.3210 0.2982 -0.0297 0.0270  0.0719  313 THR A C   
1931 O  O   . THR A 313 ? 0.1633 0.2281 0.1952 -0.0248 0.0257  0.0667  313 THR A O   
1932 C  CB  . THR A 313 ? 0.2121 0.2611 0.2563 -0.0331 0.0281  0.0795  313 THR A CB  
1933 O  OG1 . THR A 313 ? 0.2607 0.3170 0.2943 -0.0266 0.0300  0.0814  313 THR A OG1 
1934 C  CG2 . THR A 313 ? 0.2257 0.2611 0.2700 -0.0345 0.0261  0.0782  313 THR A CG2 
1935 N  N   . ARG A 314 ? 0.2431 0.3169 0.2920 -0.0316 0.0308  0.0785  314 ARG A N   
1936 C  CA  A ARG A 314 ? 0.2518 0.3390 0.2984 -0.0273 0.0335  0.0793  314 ARG A CA  
1937 C  CA  B ARG A 314 ? 0.2522 0.3396 0.2990 -0.0273 0.0337  0.0796  314 ARG A CA  
1938 C  C   . ARG A 314 ? 0.1947 0.2859 0.2290 -0.0202 0.0358  0.0803  314 ARG A C   
1939 O  O   . ARG A 314 ? 0.2758 0.3753 0.3052 -0.0152 0.0371  0.0774  314 ARG A O   
1940 C  CB  A ARG A 314 ? 0.2719 0.3692 0.3302 -0.0307 0.0369  0.0858  314 ARG A CB  
1941 C  CB  B ARG A 314 ? 0.2732 0.3703 0.3309 -0.0303 0.0372  0.0865  314 ARG A CB  
1942 C  CG  A ARG A 314 ? 0.2887 0.3864 0.3590 -0.0371 0.0342  0.0831  314 ARG A CG  
1943 C  CG  B ARG A 314 ? 0.2848 0.3830 0.3550 -0.0367 0.0350  0.0845  314 ARG A CG  
1944 C  CD  A ARG A 314 ? 0.3464 0.4515 0.4278 -0.0402 0.0363  0.0873  314 ARG A CD  
1945 C  CD  B ARG A 314 ? 0.3714 0.4742 0.4516 -0.0397 0.0375  0.0897  314 ARG A CD  
1946 N  NE  A ARG A 314 ? 0.4265 0.5463 0.5068 -0.0353 0.0397  0.0897  314 ARG A NE  
1947 N  NE  B ARG A 314 ? 0.4137 0.5307 0.4927 -0.0350 0.0413  0.0932  314 ARG A NE  
1948 C  CZ  A ARG A 314 ? 0.3842 0.5125 0.4726 -0.0366 0.0423  0.0941  314 ARG A CZ  
1949 C  CZ  B ARG A 314 ? 0.3912 0.5195 0.4755 -0.0347 0.0416  0.0919  314 ARG A CZ  
1950 N  NH1 A ARG A 314 ? 0.3768 0.5007 0.4756 -0.0430 0.0419  0.0968  314 ARG A NH1 
1951 N  NH1 B ARG A 314 ? 0.4346 0.5753 0.5190 -0.0305 0.0454  0.0955  314 ARG A NH1 
1952 N  NH2 A ARG A 314 ? 0.4295 0.5711 0.5159 -0.0312 0.0454  0.0957  314 ARG A NH2 
1953 N  NH2 B ARG A 314 ? 0.3800 0.5079 0.4698 -0.0383 0.0377  0.0869  314 ARG A NH2 
1954 N  N   . ARG A 315 ? 0.2111 0.2970 0.2405 -0.0193 0.0362  0.0837  315 ARG A N   
1955 C  CA  . ARG A 315 ? 0.2488 0.3396 0.2658 -0.0127 0.0376  0.0835  315 ARG A CA  
1956 C  C   . ARG A 315 ? 0.1694 0.2536 0.1770 -0.0092 0.0334  0.0733  315 ARG A C   
1957 O  O   . ARG A 315 ? 0.1888 0.2783 0.1868 -0.0037 0.0340  0.0702  315 ARG A O   
1958 C  CB  . ARG A 315 ? 0.3360 0.4227 0.3508 -0.0122 0.0379  0.0891  315 ARG A CB  
1959 C  CG  . ARG A 315 ? 0.3883 0.4689 0.3929 -0.0094 0.0352  0.0858  315 ARG A CG  
1960 C  CD  . ARG A 315 ? 0.3691 0.4506 0.3690 -0.0062 0.0355  0.0904  315 ARG A CD  
1961 N  NE  . ARG A 315 ? 0.2976 0.3672 0.2988 -0.0081 0.0328  0.0907  315 ARG A NE  
1962 C  CZ  . ARG A 315 ? 0.3461 0.4108 0.3402 -0.0067 0.0296  0.0859  315 ARG A CZ  
1963 N  NH1 . ARG A 315 ? 0.2452 0.2995 0.2417 -0.0083 0.0274  0.0864  315 ARG A NH1 
1964 N  NH2 . ARG A 315 ? 0.3246 0.3932 0.3101 -0.0032 0.0278  0.0777  315 ARG A NH2 
1965 N  N   . HIS A 316 ? 0.1283 0.2016 0.1388 -0.0125 0.0293  0.0679  316 HIS A N   
1966 C  CA  . HIS A 316 ? 0.1370 0.2034 0.1398 -0.0098 0.0256  0.0595  316 HIS A CA  
1967 C  C   . HIS A 316 ? 0.1180 0.1886 0.1202 -0.0070 0.0253  0.0540  316 HIS A C   
1968 O  O   . HIS A 316 ? 0.1409 0.2197 0.1491 -0.0075 0.0276  0.0563  316 HIS A O   
1969 C  CB  . HIS A 316 ? 0.1291 0.1829 0.1348 -0.0139 0.0218  0.0567  316 HIS A CB  
1970 C  CG  . HIS A 316 ? 0.1563 0.2045 0.1615 -0.0151 0.0218  0.0610  316 HIS A CG  
1971 N  ND1 . HIS A 316 ? 0.1541 0.2018 0.1674 -0.0188 0.0239  0.0682  316 HIS A ND1 
1972 C  CD2 . HIS A 316 ? 0.1584 0.2018 0.1570 -0.0128 0.0200  0.0596  316 HIS A CD2 
1973 C  CE1 . HIS A 316 ? 0.1874 0.2295 0.1988 -0.0183 0.0236  0.0712  316 HIS A CE1 
1974 N  NE2 . HIS A 316 ? 0.1532 0.1933 0.1556 -0.0146 0.0212  0.0661  316 HIS A NE2 
1975 N  N   . LEU A 317 ? 0.1166 0.1817 0.1122 -0.0040 0.0227  0.0468  317 LEU A N   
1976 C  CA  . LEU A 317 ? 0.1155 0.1832 0.1109 -0.0007 0.0226  0.0417  317 LEU A CA  
1977 C  C   . LEU A 317 ? 0.1213 0.1898 0.1257 -0.0039 0.0218  0.0426  317 LEU A C   
1978 O  O   . LEU A 317 ? 0.1405 0.2026 0.1488 -0.0085 0.0192  0.0429  317 LEU A O   
1979 C  CB  . LEU A 317 ? 0.1535 0.2126 0.1431 0.0016  0.0195  0.0343  317 LEU A CB  
1980 C  CG  . LEU A 317 ? 0.1578 0.2167 0.1384 0.0049  0.0194  0.0315  317 LEU A CG  
1981 C  CD1 . LEU A 317 ? 0.2289 0.2775 0.2068 0.0049  0.0157  0.0251  317 LEU A CD1 
1982 C  CD2 . LEU A 317 ? 0.2761 0.3445 0.2527 0.0103  0.0225  0.0292  317 LEU A CD2 
1983 N  N   . LYS A 318 ? 0.1252 0.2024 0.1328 -0.0011 0.0239  0.0427  318 LYS A N   
1984 C  CA  . LYS A 318 ? 0.1335 0.2127 0.1493 -0.0033 0.0224  0.0428  318 LYS A CA  
1985 C  C   . LYS A 318 ? 0.1580 0.2279 0.1716 -0.0026 0.0186  0.0375  318 LYS A C   
1986 O  O   . LYS A 318 ? 0.1443 0.2087 0.1516 0.0013  0.0181  0.0331  318 LYS A O   
1987 C  CB  . LYS A 318 ? 0.1560 0.2475 0.1760 0.0005  0.0257  0.0442  318 LYS A CB  
1988 C  CG  . LYS A 318 ? 0.2333 0.3358 0.2588 -0.0017 0.0295  0.0510  318 LYS A CG  
1989 C  CD  . LYS A 318 ? 0.3563 0.4728 0.3882 0.0014  0.0328  0.0530  318 LYS A CD  
1990 C  CE  . LYS A 318 ? 0.4195 0.5470 0.4586 -0.0021 0.0366  0.0609  318 LYS A CE  
1991 N  NZ  . LYS A 318 ? 0.4955 0.6385 0.5378 0.0027  0.0416  0.0636  318 LYS A NZ  
1992 N  N   . VAL A 319 ? 0.1254 0.1945 0.1448 -0.0065 0.0158  0.0379  319 VAL A N   
1993 C  CA  . VAL A 319 ? 0.1171 0.1802 0.1352 -0.0051 0.0127  0.0343  319 VAL A CA  
1994 C  C   . VAL A 319 ? 0.1059 0.1748 0.1260 0.0004  0.0140  0.0335  319 VAL A C   
1995 O  O   . VAL A 319 ? 0.1283 0.2080 0.1549 0.0009  0.0155  0.0363  319 VAL A O   
1996 C  CB  . VAL A 319 ? 0.1120 0.1748 0.1350 -0.0103 0.0094  0.0348  319 VAL A CB  
1997 C  CG1 . VAL A 319 ? 0.1335 0.1924 0.1549 -0.0083 0.0066  0.0323  319 VAL A CG1 
1998 C  CG2 . VAL A 319 ? 0.1322 0.1877 0.1536 -0.0153 0.0084  0.0348  319 VAL A CG2 
1999 N  N   . GLU A 320 ? 0.1159 0.1776 0.1315 0.0046  0.0135  0.0298  320 GLU A N   
2000 C  CA  . GLU A 320 ? 0.1241 0.1899 0.1428 0.0104  0.0149  0.0292  320 GLU A CA  
2001 C  C   . GLU A 320 ? 0.1274 0.1960 0.1517 0.0100  0.0123  0.0313  320 GLU A C   
2002 O  O   . GLU A 320 ? 0.1420 0.2191 0.1720 0.0136  0.0134  0.0331  320 GLU A O   
2003 C  CB  . GLU A 320 ? 0.1437 0.2004 0.1572 0.0151  0.0155  0.0243  320 GLU A CB  
2004 C  CG  . GLU A 320 ? 0.1664 0.2238 0.1740 0.0168  0.0181  0.0216  320 GLU A CG  
2005 C  CD  . GLU A 320 ? 0.2604 0.3298 0.2704 0.0208  0.0222  0.0229  320 GLU A CD  
2006 O  OE1 . GLU A 320 ? 0.3641 0.4377 0.3792 0.0252  0.0235  0.0230  320 GLU A OE1 
2007 O  OE2 . GLU A 320 ? 0.4162 0.4916 0.4235 0.0197  0.0243  0.0246  320 GLU A OE2 
2008 N  N   . GLU A 321 ? 0.1193 0.1817 0.1420 0.0061  0.0089  0.0311  321 GLU A N   
2009 C  CA  . GLU A 321 ? 0.1165 0.1832 0.1434 0.0055  0.0061  0.0332  321 GLU A CA  
2010 C  C   . GLU A 321 ? 0.1047 0.1651 0.1281 0.0004  0.0029  0.0322  321 GLU A C   
2011 O  O   . GLU A 321 ? 0.1201 0.1708 0.1381 -0.0007 0.0031  0.0299  321 GLU A O   
2012 C  CB  . GLU A 321 ? 0.2021 0.2667 0.2302 0.0117  0.0064  0.0337  321 GLU A CB  
2013 C  CG  . GLU A 321 ? 0.2648 0.3163 0.2878 0.0132  0.0063  0.0311  321 GLU A CG  
2014 C  CD  . GLU A 321 ? 0.4072 0.4565 0.4335 0.0193  0.0070  0.0325  321 GLU A CD  
2015 O  OE1 . GLU A 321 ? 0.4875 0.5301 0.5132 0.0234  0.0094  0.0296  321 GLU A OE1 
2016 O  OE2 . GLU A 321 ? 0.2747 0.3295 0.3047 0.0202  0.0052  0.0365  321 GLU A OE2 
2017 N  N   . TYR A 322 ? 0.0979 0.1648 0.1246 -0.0025 0.0000  0.0335  322 TYR A N   
2018 C  CA  . TYR A 322 ? 0.0964 0.1585 0.1196 -0.0062 -0.0030 0.0321  322 TYR A CA  
2019 C  C   . TYR A 322 ? 0.1024 0.1621 0.1236 -0.0021 -0.0040 0.0334  322 TYR A C   
2020 O  O   . TYR A 322 ? 0.1048 0.1729 0.1300 0.0010  -0.0048 0.0363  322 TYR A O   
2021 C  CB  . TYR A 322 ? 0.0933 0.1638 0.1205 -0.0114 -0.0057 0.0318  322 TYR A CB  
2022 C  CG  . TYR A 322 ? 0.1017 0.1722 0.1316 -0.0159 -0.0043 0.0311  322 TYR A CG  
2023 C  CD1 . TYR A 322 ? 0.1104 0.1709 0.1362 -0.0185 -0.0036 0.0292  322 TYR A CD1 
2024 C  CD2 . TYR A 322 ? 0.1704 0.2516 0.2080 -0.0172 -0.0033 0.0333  322 TYR A CD2 
2025 C  CE1 . TYR A 322 ? 0.1289 0.1889 0.1576 -0.0222 -0.0019 0.0298  322 TYR A CE1 
2026 C  CE2 . TYR A 322 ? 0.1844 0.2654 0.2253 -0.0213 -0.0014 0.0339  322 TYR A CE2 
2027 C  CZ  . TYR A 322 ? 0.1696 0.2395 0.2058 -0.0236 -0.0007 0.0324  322 TYR A CZ  
2028 O  OH  . TYR A 322 ? 0.2115 0.2809 0.2514 -0.0274 0.0015  0.0342  322 TYR A OH  
2029 N  N   . ILE A 323 ? 0.0961 0.1450 0.1120 -0.0018 -0.0037 0.0320  323 ILE A N   
2030 C  CA  . ILE A 323 ? 0.1041 0.1493 0.1186 0.0015  -0.0041 0.0340  323 ILE A CA  
2031 C  C   . ILE A 323 ? 0.0986 0.1501 0.1120 -0.0004 -0.0072 0.0354  323 ILE A C   
2032 O  O   . ILE A 323 ? 0.1012 0.1541 0.1126 -0.0052 -0.0089 0.0327  323 ILE A O   
2033 C  CB  . ILE A 323 ? 0.1072 0.1400 0.1175 0.0014  -0.0029 0.0318  323 ILE A CB  
2034 C  CG1 . ILE A 323 ? 0.1544 0.1827 0.1649 0.0033  -0.0003 0.0294  323 ILE A CG1 
2035 C  CG2 . ILE A 323 ? 0.1333 0.1616 0.1431 0.0040  -0.0030 0.0346  323 ILE A CG2 
2036 C  CD1 . ILE A 323 ? 0.1917 0.2204 0.2062 0.0090  0.0016  0.0306  323 ILE A CD1 
2037 N  N   . THR A 324 ? 0.1013 0.1576 0.1163 0.0035  -0.0079 0.0396  324 THR A N   
2038 C  CA  . THR A 324 ? 0.1023 0.1682 0.1161 0.0021  -0.0112 0.0410  324 THR A CA  
2039 C  C   . THR A 324 ? 0.1034 0.1637 0.1110 0.0004  -0.0117 0.0402  324 THR A C   
2040 O  O   . THR A 324 ? 0.1039 0.1534 0.1095 0.0014  -0.0096 0.0405  324 THR A O   
2041 C  CB  . THR A 324 ? 0.1057 0.1804 0.1231 0.0075  -0.0118 0.0470  324 THR A CB  
2042 O  OG1 . THR A 324 ? 0.1136 0.1789 0.1306 0.0117  -0.0094 0.0505  324 THR A OG1 
2043 C  CG2 . THR A 324 ? 0.1051 0.1881 0.1297 0.0100  -0.0113 0.0483  324 THR A CG2 
2044 N  N   . PRO A 325 ? 0.1047 0.1730 0.1092 -0.0021 -0.0147 0.0390  325 PRO A N   
2045 C  CA  . PRO A 325 ? 0.1067 0.1717 0.1050 -0.0030 -0.0149 0.0385  325 PRO A CA  
2046 C  C   . PRO A 325 ? 0.1098 0.1720 0.1075 0.0017  -0.0131 0.0449  325 PRO A C   
2047 O  O   . PRO A 325 ? 0.1124 0.1660 0.1073 0.0013  -0.0112 0.0449  325 PRO A O   
2048 C  CB  . PRO A 325 ? 0.1142 0.1920 0.1101 -0.0052 -0.0187 0.0363  325 PRO A CB  
2049 C  CG  . PRO A 325 ? 0.1118 0.1942 0.1130 -0.0087 -0.0202 0.0324  325 PRO A CG  
2050 C  CD  . PRO A 325 ? 0.1054 0.1861 0.1123 -0.0051 -0.0179 0.0366  325 PRO A CD  
2051 N  N   . GLU A 326 ? 0.1126 0.1819 0.1139 0.0063  -0.0134 0.0508  326 GLU A N   
2052 C  CA  . GLU A 326 ? 0.1349 0.2009 0.1368 0.0108  -0.0114 0.0579  326 GLU A CA  
2053 C  C   . GLU A 326 ? 0.1255 0.1770 0.1314 0.0122  -0.0080 0.0581  326 GLU A C   
2054 O  O   . GLU A 326 ? 0.1238 0.1682 0.1300 0.0136  -0.0059 0.0618  326 GLU A O   
2055 C  CB  . GLU A 326 ? 0.1338 0.2119 0.1390 0.0158  -0.0127 0.0650  326 GLU A CB  
2056 C  CG  . GLU A 326 ? 0.1331 0.2266 0.1328 0.0150  -0.0164 0.0658  326 GLU A CG  
2057 C  CD  . GLU A 326 ? 0.2352 0.3271 0.2277 0.0142  -0.0156 0.0670  326 GLU A CD  
2058 O  OE1 . GLU A 326 ? 0.2854 0.3687 0.2791 0.0166  -0.0124 0.0724  326 GLU A OE1 
2059 O  OE2 . GLU A 326 ? 0.3693 0.4689 0.3556 0.0110  -0.0181 0.0622  326 GLU A OE2 
2060 N  N   . LYS A 327 ? 0.1134 0.1610 0.1227 0.0117  -0.0072 0.0540  327 LYS A N   
2061 C  CA  . LYS A 327 ? 0.1141 0.1485 0.1262 0.0128  -0.0043 0.0527  327 LYS A CA  
2062 C  C   . LYS A 327 ? 0.1290 0.1546 0.1369 0.0085  -0.0037 0.0484  327 LYS A C   
2063 O  O   . LYS A 327 ? 0.1347 0.1506 0.1442 0.0091  -0.0018 0.0492  327 LYS A O   
2064 C  CB  . LYS A 327 ? 0.1411 0.1748 0.1568 0.0140  -0.0033 0.0492  327 LYS A CB  
2065 C  CG  . LYS A 327 ? 0.1502 0.1717 0.1692 0.0164  -0.0004 0.0476  327 LYS A CG  
2066 C  CD  . LYS A 327 ? 0.2076 0.2264 0.2324 0.0220  0.0011  0.0537  327 LYS A CD  
2067 C  CE  . LYS A 327 ? 0.2765 0.2826 0.3054 0.0242  0.0038  0.0505  327 LYS A CE  
2068 N  NZ  . LYS A 327 ? 0.2960 0.3045 0.3266 0.0265  0.0049  0.0461  327 LYS A NZ  
2069 N  N   . PHE A 328 ? 0.1083 0.1373 0.1116 0.0042  -0.0054 0.0441  328 PHE A N   
2070 C  CA  . PHE A 328 ? 0.1109 0.1327 0.1106 0.0008  -0.0048 0.0409  328 PHE A CA  
2071 C  C   . PHE A 328 ? 0.1232 0.1446 0.1214 0.0017  -0.0042 0.0453  328 PHE A C   
2072 O  O   . PHE A 328 ? 0.1387 0.1523 0.1371 0.0007  -0.0026 0.0449  328 PHE A O   
2073 C  CB  . PHE A 328 ? 0.1079 0.1331 0.1038 -0.0034 -0.0065 0.0359  328 PHE A CB  
2074 C  CG  . PHE A 328 ? 0.0999 0.1218 0.0972 -0.0052 -0.0061 0.0317  328 PHE A CG  
2075 C  CD1 . PHE A 328 ? 0.1025 0.1154 0.0993 -0.0060 -0.0046 0.0293  328 PHE A CD1 
2076 C  CD2 . PHE A 328 ? 0.0987 0.1276 0.0980 -0.0060 -0.0072 0.0307  328 PHE A CD2 
2077 C  CE1 . PHE A 328 ? 0.1070 0.1185 0.1044 -0.0072 -0.0042 0.0264  328 PHE A CE1 
2078 C  CE2 . PHE A 328 ? 0.0995 0.1265 0.1003 -0.0075 -0.0064 0.0282  328 PHE A CE2 
2079 C  CZ  . PHE A 328 ? 0.1220 0.1405 0.1214 -0.0078 -0.0048 0.0262  328 PHE A CZ  
2080 N  N   . LYS A 329 ? 0.1128 0.1439 0.1096 0.0037  -0.0053 0.0499  329 LYS A N   
2081 C  CA  . LYS A 329 ? 0.1248 0.1572 0.1201 0.0050  -0.0042 0.0553  329 LYS A CA  
2082 C  C   . LYS A 329 ? 0.1350 0.1591 0.1365 0.0080  -0.0015 0.0610  329 LYS A C   
2083 O  O   . LYS A 329 ? 0.1595 0.1795 0.1615 0.0075  0.0004  0.0642  329 LYS A O   
2084 C  CB  . LYS A 329 ? 0.1763 0.2227 0.1680 0.0069  -0.0062 0.0592  329 LYS A CB  
2085 C  CG  . LYS A 329 ? 0.1563 0.2096 0.1418 0.0033  -0.0087 0.0525  329 LYS A CG  
2086 C  CD  . LYS A 329 ? 0.1934 0.2620 0.1745 0.0048  -0.0114 0.0547  329 LYS A CD  
2087 C  CE  . LYS A 329 ? 0.2866 0.3608 0.2635 0.0006  -0.0144 0.0460  329 LYS A CE  
2088 N  NZ  . LYS A 329 ? 0.3096 0.4003 0.2831 0.0020  -0.0177 0.0472  329 LYS A NZ  
2089 N  N   . TYR A 330 ? 0.1394 0.1610 0.1463 0.0109  -0.0011 0.0621  330 TYR A N   
2090 C  CA  . TYR A 330 ? 0.1268 0.1381 0.1408 0.0134  0.0015  0.0655  330 TYR A CA  
2091 C  C   . TYR A 330 ? 0.1251 0.1249 0.1400 0.0098  0.0027  0.0600  330 TYR A C   
2092 O  O   . TYR A 330 ? 0.1305 0.1233 0.1494 0.0094  0.0046  0.0630  330 TYR A O   
2093 C  CB  . TYR A 330 ? 0.1335 0.1441 0.1529 0.0174  0.0018  0.0658  330 TYR A CB  
2094 C  CG  . TYR A 330 ? 0.1454 0.1429 0.1723 0.0194  0.0045  0.0658  330 TYR A CG  
2095 C  CD1 . TYR A 330 ? 0.1558 0.1485 0.1887 0.0221  0.0066  0.0736  330 TYR A CD1 
2096 C  CD2 . TYR A 330 ? 0.1480 0.1380 0.1762 0.0184  0.0049  0.0579  330 TYR A CD2 
2097 C  CE1 . TYR A 330 ? 0.2029 0.1824 0.2439 0.0236  0.0089  0.0727  330 TYR A CE1 
2098 C  CE2 . TYR A 330 ? 0.1760 0.1541 0.2110 0.0202  0.0070  0.0565  330 TYR A CE2 
2099 C  CZ  . TYR A 330 ? 0.2127 0.1850 0.2546 0.0225  0.0090  0.0636  330 TYR A CZ  
2100 O  OH  . TYR A 330 ? 0.3058 0.2652 0.3557 0.0238  0.0110  0.0615  330 TYR A OH  
2101 N  N   . TRP A 331 ? 0.1197 0.1182 0.1315 0.0070  0.0016  0.0523  331 TRP A N   
2102 C  CA  . TRP A 331 ? 0.1202 0.1094 0.1330 0.0040  0.0023  0.0474  331 TRP A CA  
2103 C  C   . TRP A 331 ? 0.1376 0.1268 0.1480 0.0010  0.0026  0.0485  331 TRP A C   
2104 O  O   . TRP A 331 ? 0.1409 0.1227 0.1547 -0.0008 0.0037  0.0473  331 TRP A O   
2105 C  CB  . TRP A 331 ? 0.1363 0.1253 0.1460 0.0022  0.0011  0.0400  331 TRP A CB  
2106 C  CG  . TRP A 331 ? 0.1331 0.1208 0.1460 0.0054  0.0016  0.0383  331 TRP A CG  
2107 C  CD1 . TRP A 331 ? 0.1394 0.1342 0.1509 0.0066  0.0009  0.0372  331 TRP A CD1 
2108 C  CD2 . TRP A 331 ? 0.1571 0.1365 0.1758 0.0079  0.0033  0.0374  331 TRP A CD2 
2109 N  NE1 . TRP A 331 ? 0.1636 0.1556 0.1792 0.0102  0.0023  0.0359  331 TRP A NE1 
2110 C  CE2 . TRP A 331 ? 0.1678 0.1499 0.1876 0.0112  0.0037  0.0356  331 TRP A CE2 
2111 C  CE3 . TRP A 331 ? 0.1683 0.1381 0.1920 0.0075  0.0045  0.0376  331 TRP A CE3 
2112 C  CZ2 . TRP A 331 ? 0.1562 0.1315 0.1812 0.0147  0.0054  0.0333  331 TRP A CZ2 
2113 C  CZ3 . TRP A 331 ? 0.1950 0.1571 0.2245 0.0104  0.0059  0.0351  331 TRP A CZ3 
2114 C  CH2 . TRP A 331 ? 0.1847 0.1495 0.2144 0.0142  0.0063  0.0326  331 TRP A CH2 
2115 N  N   . GLU A 332 ? 0.1199 0.1178 0.1247 0.0004  0.0017  0.0501  332 GLU A N   
2116 C  CA  . GLU A 332 ? 0.1292 0.1286 0.1319 -0.0015 0.0026  0.0519  332 GLU A CA  
2117 C  C   . GLU A 332 ? 0.1667 0.1633 0.1749 0.0000  0.0051  0.0595  332 GLU A C   
2118 O  O   . GLU A 332 ? 0.1627 0.1551 0.1739 -0.0021 0.0066  0.0603  332 GLU A O   
2119 C  CB  . GLU A 332 ? 0.1496 0.1597 0.1452 -0.0015 0.0013  0.0520  332 GLU A CB  
2120 C  CG  . GLU A 332 ? 0.2054 0.2185 0.1979 -0.0028 0.0027  0.0532  332 GLU A CG  
2121 C  CD  . GLU A 332 ? 0.3500 0.3746 0.3351 -0.0021 0.0014  0.0530  332 GLU A CD  
2122 O  OE1 . GLU A 332 ? 0.4933 0.5241 0.4765 -0.0008 -0.0008 0.0527  332 GLU A OE1 
2123 O  OE2 . GLU A 332 ? 0.4800 0.5081 0.4614 -0.0027 0.0026  0.0529  332 GLU A OE2 
2124 N  N   . LYS A 333 ? 0.1491 0.1489 0.1597 0.0038  0.0055  0.0659  333 LYS A N   
2125 C  CA  . LYS A 333 ? 0.1505 0.1471 0.1677 0.0057  0.0082  0.0746  333 LYS A CA  
2126 C  C   . LYS A 333 ? 0.1778 0.1610 0.2038 0.0042  0.0096  0.0725  333 LYS A C   
2127 O  O   . LYS A 333 ? 0.1784 0.1571 0.2099 0.0025  0.0118  0.0764  333 LYS A O   
2128 C  CB  . LYS A 333 ? 0.1924 0.1946 0.2110 0.0107  0.0081  0.0816  333 LYS A CB  
2129 C  CG  . LYS A 333 ? 0.3278 0.3266 0.3544 0.0137  0.0110  0.0921  333 LYS A CG  
2130 C  CD  . LYS A 333 ? 0.3890 0.3925 0.4178 0.0194  0.0104  0.0977  333 LYS A CD  
2131 C  CE  . LYS A 333 ? 0.5140 0.5063 0.5543 0.0219  0.0131  0.1009  333 LYS A CE  
2132 N  NZ  . LYS A 333 ? 0.4642 0.4565 0.5081 0.0270  0.0124  0.1018  333 LYS A NZ  
2133 N  N   . VAL A 334 ? 0.1584 0.1357 0.1861 0.0045  0.0084  0.0658  334 VAL A N   
2134 C  CA  . VAL A 334 ? 0.1705 0.1358 0.2056 0.0030  0.0092  0.0616  334 VAL A CA  
2135 C  C   . VAL A 334 ? 0.1482 0.1113 0.1827 -0.0019 0.0089  0.0572  334 VAL A C   
2136 O  O   . VAL A 334 ? 0.1941 0.1499 0.2361 -0.0041 0.0102  0.0578  334 VAL A O   
2137 C  CB  . VAL A 334 ? 0.1652 0.1272 0.1999 0.0047  0.0080  0.0544  334 VAL A CB  
2138 C  CG1 . VAL A 334 ? 0.2154 0.1665 0.2557 0.0027  0.0082  0.0477  334 VAL A CG1 
2139 C  CG2 . VAL A 334 ? 0.1739 0.1370 0.2122 0.0102  0.0089  0.0594  334 VAL A CG2 
2140 N  N   . GLY A 335 ? 0.1390 0.1084 0.1654 -0.0038 0.0071  0.0527  335 GLY A N   
2141 C  CA  . GLY A 335 ? 0.1551 0.1235 0.1810 -0.0078 0.0068  0.0489  335 GLY A CA  
2142 C  C   . GLY A 335 ? 0.1567 0.1270 0.1863 -0.0091 0.0090  0.0556  335 GLY A C   
2143 O  O   . GLY A 335 ? 0.1861 0.1519 0.2219 -0.0122 0.0097  0.0548  335 GLY A O   
2144 N  N   . ASN A 336 ? 0.1544 0.1321 0.1806 -0.0067 0.0102  0.0627  336 ASN A N   
2145 C  CA  . ASN A 336 ? 0.1929 0.1741 0.2220 -0.0074 0.0130  0.0703  336 ASN A CA  
2146 C  C   . ASN A 336 ? 0.1829 0.1552 0.2239 -0.0081 0.0152  0.0753  336 ASN A C   
2147 O  O   . ASN A 336 ? 0.2029 0.1736 0.2502 -0.0112 0.0170  0.0778  336 ASN A O   
2148 C  CB  . ASN A 336 ? 0.2049 0.1969 0.2276 -0.0039 0.0137  0.0772  336 ASN A CB  
2149 C  CG  . ASN A 336 ? 0.2514 0.2523 0.2633 -0.0040 0.0119  0.0719  336 ASN A CG  
2150 O  OD1 . ASN A 336 ? 0.2738 0.2729 0.2837 -0.0067 0.0109  0.0650  336 ASN A OD1 
2151 N  ND2 . ASN A 336 ? 0.2512 0.2618 0.2566 -0.0011 0.0113  0.0752  336 ASN A ND2 
2152 N  N   . GLU A 337 ? 0.1784 0.1448 0.2237 -0.0053 0.0152  0.0769  337 GLU A N   
2153 C  CA  . GLU A 337 ? 0.2236 0.1809 0.2804 -0.0056 0.0171  0.0801  337 GLU A CA  
2154 C  C   . GLU A 337 ? 0.2214 0.1687 0.2856 -0.0101 0.0163  0.0725  337 GLU A C   
2155 O  O   . GLU A 337 ? 0.2528 0.1960 0.3254 -0.0123 0.0176  0.0733  337 GLU A O   
2156 C  CB  . GLU A 337 ? 0.3364 0.2904 0.3956 -0.0007 0.0173  0.0826  337 GLU A CB  
2157 C  CG  . GLU A 337 ? 0.2869 0.2526 0.3401 0.0035  0.0179  0.0905  337 GLU A CG  
2158 C  CD  . GLU A 337 ? 0.5258 0.4916 0.5794 0.0088  0.0173  0.0926  337 GLU A CD  
2159 O  OE1 . GLU A 337 ? 0.5760 0.5323 0.6339 0.0095  0.0167  0.0877  337 GLU A OE1 
2160 O  OE2 . GLU A 337 ? 0.5229 0.4992 0.5725 0.0124  0.0174  0.0990  337 GLU A OE2 
2161 N  N   . LEU A 338 ? 0.1819 0.1278 0.2413 -0.0112 0.0135  0.0629  338 LEU A N   
2162 C  CA  . LEU A 338 ? 0.1787 0.1176 0.2435 -0.0153 0.0120  0.0547  338 LEU A CA  
2163 C  C   . LEU A 338 ? 0.2388 0.1827 0.3041 -0.0197 0.0119  0.0542  338 LEU A C   
2164 O  O   . LEU A 338 ? 0.2332 0.1729 0.3042 -0.0236 0.0105  0.0480  338 LEU A O   
2165 C  CB  . LEU A 338 ? 0.1902 0.1286 0.2484 -0.0143 0.0091  0.0445  338 LEU A CB  
2166 C  CG  . LEU A 338 ? 0.2068 0.1391 0.2664 -0.0102 0.0092  0.0427  338 LEU A CG  
2167 C  CD1 . LEU A 338 ? 0.2322 0.1669 0.2836 -0.0091 0.0067  0.0335  338 LEU A CD1 
2168 C  CD2 . LEU A 338 ? 0.2945 0.2147 0.3665 -0.0113 0.0103  0.0412  338 LEU A CD2 
2169 N  N   . GLY A 339 ? 0.1816 0.1351 0.2408 -0.0191 0.0131  0.0596  339 GLY A N   
2170 C  CA  . GLY A 339 ? 0.1708 0.1298 0.2318 -0.0224 0.0140  0.0609  339 GLY A CA  
2171 C  C   . GLY A 339 ? 0.1602 0.1256 0.2127 -0.0231 0.0117  0.0542  339 GLY A C   
2172 O  O   . GLY A 339 ? 0.1706 0.1403 0.2255 -0.0258 0.0122  0.0543  339 GLY A O   
2173 N  N   . PHE A 340 ? 0.1522 0.1189 0.1954 -0.0207 0.0095  0.0493  340 PHE A N   
2174 C  CA  . PHE A 340 ? 0.1318 0.1043 0.1673 -0.0209 0.0080  0.0445  340 PHE A CA  
2175 C  C   . PHE A 340 ? 0.1337 0.1147 0.1653 -0.0201 0.0102  0.0495  340 PHE A C   
2176 O  O   . PHE A 340 ? 0.1621 0.1466 0.1916 -0.0179 0.0121  0.0557  340 PHE A O   
2177 C  CB  . PHE A 340 ? 0.1465 0.1192 0.1735 -0.0185 0.0059  0.0399  340 PHE A CB  
2178 C  CG  . PHE A 340 ? 0.1626 0.1291 0.1914 -0.0189 0.0037  0.0336  340 PHE A CG  
2179 C  CD1 . PHE A 340 ? 0.1598 0.1263 0.1882 -0.0208 0.0017  0.0275  340 PHE A CD1 
2180 C  CD2 . PHE A 340 ? 0.1741 0.1356 0.2045 -0.0168 0.0038  0.0337  340 PHE A CD2 
2181 C  CE1 . PHE A 340 ? 0.1662 0.1286 0.1952 -0.0208 -0.0003 0.0214  340 PHE A CE1 
2182 C  CE2 . PHE A 340 ? 0.1955 0.1522 0.2269 -0.0166 0.0023  0.0274  340 PHE A CE2 
2183 C  CZ  . PHE A 340 ? 0.1858 0.1432 0.2161 -0.0187 0.0001  0.0210  340 PHE A CZ  
2184 N  N   . HIS A 341 ? 0.1294 0.1147 0.1598 -0.0214 0.0099  0.0467  341 HIS A N   
2185 C  CA  . HIS A 341 ? 0.1693 0.1630 0.1957 -0.0202 0.0123  0.0503  341 HIS A CA  
2186 C  C   . HIS A 341 ? 0.1667 0.1642 0.1826 -0.0171 0.0117  0.0489  341 HIS A C   
2187 O  O   . HIS A 341 ? 0.1852 0.1895 0.1971 -0.0152 0.0138  0.0532  341 HIS A O   
2188 C  CB  . HIS A 341 ? 0.1333 0.1304 0.1619 -0.0218 0.0123  0.0474  341 HIS A CB  
2189 C  CG  . HIS A 341 ? 0.1445 0.1408 0.1845 -0.0251 0.0133  0.0501  341 HIS A CG  
2190 N  ND1 . HIS A 341 ? 0.1485 0.1502 0.1936 -0.0257 0.0170  0.0573  341 HIS A ND1 
2191 C  CD2 . HIS A 341 ? 0.1428 0.1336 0.1907 -0.0283 0.0112  0.0469  341 HIS A CD2 
2192 C  CE1 . HIS A 341 ? 0.1878 0.1870 0.2445 -0.0296 0.0171  0.0584  341 HIS A CE1 
2193 N  NE2 . HIS A 341 ? 0.1633 0.1558 0.2217 -0.0313 0.0133  0.0516  341 HIS A NE2 
2194 N  N   . TYR A 342 ? 0.1312 0.1253 0.1429 -0.0167 0.0090  0.0432  342 TYR A N   
2195 C  CA  . TYR A 342 ? 0.1409 0.1376 0.1453 -0.0144 0.0081  0.0427  342 TYR A CA  
2196 C  C   . TYR A 342 ? 0.1291 0.1203 0.1331 -0.0144 0.0056  0.0387  342 TYR A C   
2197 O  O   . TYR A 342 ? 0.1060 0.0925 0.1128 -0.0159 0.0044  0.0349  342 TYR A O   
2198 C  CB  . TYR A 342 ? 0.1512 0.1534 0.1484 -0.0135 0.0081  0.0394  342 TYR A CB  
2199 C  CG  . TYR A 342 ? 0.1459 0.1453 0.1418 -0.0144 0.0065  0.0331  342 TYR A CG  
2200 C  CD1 . TYR A 342 ? 0.1809 0.1769 0.1745 -0.0145 0.0042  0.0291  342 TYR A CD1 
2201 C  CD2 . TYR A 342 ? 0.1716 0.1728 0.1690 -0.0147 0.0077  0.0318  342 TYR A CD2 
2202 C  CE1 . TYR A 342 ? 0.1848 0.1787 0.1777 -0.0151 0.0031  0.0247  342 TYR A CE1 
2203 C  CE2 . TYR A 342 ? 0.1744 0.1734 0.1710 -0.0149 0.0064  0.0270  342 TYR A CE2 
2204 C  CZ  . TYR A 342 ? 0.2349 0.2299 0.2291 -0.0151 0.0042  0.0239  342 TYR A CZ  
2205 O  OH  . TYR A 342 ? 0.2239 0.2169 0.2180 -0.0151 0.0033  0.0205  342 TYR A OH  
2206 N  N   . THR A 343 ? 0.1253 0.1185 0.1260 -0.0125 0.0050  0.0401  343 THR A N   
2207 C  CA  . THR A 343 ? 0.1264 0.1165 0.1261 -0.0119 0.0031  0.0369  343 THR A CA  
2208 C  C   . THR A 343 ? 0.1713 0.1674 0.1646 -0.0111 0.0019  0.0351  343 THR A C   
2209 O  O   . THR A 343 ? 0.1768 0.1786 0.1678 -0.0095 0.0020  0.0385  343 THR A O   
2210 C  CB  . THR A 343 ? 0.1401 0.1272 0.1442 -0.0102 0.0035  0.0407  343 THR A CB  
2211 O  OG1 . THR A 343 ? 0.1648 0.1460 0.1760 -0.0115 0.0047  0.0421  343 THR A OG1 
2212 C  CG2 . THR A 343 ? 0.1571 0.1418 0.1608 -0.0092 0.0020  0.0370  343 THR A CG2 
2213 N  N   . ALA A 344 ? 0.1322 0.1275 0.1230 -0.0124 0.0007  0.0300  344 ALA A N   
2214 C  CA  . ALA A 344 ? 0.1159 0.1154 0.1023 -0.0125 -0.0006 0.0274  344 ALA A CA  
2215 C  C   . ALA A 344 ? 0.1295 0.1285 0.1171 -0.0120 -0.0019 0.0269  344 ALA A C   
2216 O  O   . ALA A 344 ? 0.1313 0.1258 0.1209 -0.0125 -0.0020 0.0250  344 ALA A O   
2217 C  CB  . ALA A 344 ? 0.1648 0.1627 0.1495 -0.0140 -0.0008 0.0228  344 ALA A CB  
2218 N  N   . SER A 345 ? 0.1014 0.1062 0.0879 -0.0108 -0.0027 0.0287  345 SER A N   
2219 C  CA  . SER A 345 ? 0.1080 0.1132 0.0970 -0.0098 -0.0035 0.0292  345 SER A CA  
2220 C  C   . SER A 345 ? 0.1244 0.1376 0.1115 -0.0101 -0.0053 0.0285  345 SER A C   
2221 O  O   . SER A 345 ? 0.1391 0.1590 0.1239 -0.0091 -0.0060 0.0305  345 SER A O   
2222 C  CB  . SER A 345 ? 0.1125 0.1158 0.1052 -0.0070 -0.0023 0.0340  345 SER A CB  
2223 O  OG  . SER A 345 ? 0.1315 0.1352 0.1270 -0.0052 -0.0026 0.0343  345 SER A OG  
2224 N  N   . GLY A 346 ? 0.1016 0.1153 0.0901 -0.0114 -0.0062 0.0256  346 GLY A N   
2225 C  CA  . GLY A 346 ? 0.1027 0.1245 0.0910 -0.0124 -0.0082 0.0246  346 GLY A CA  
2226 C  C   . GLY A 346 ? 0.1118 0.1327 0.1028 -0.0147 -0.0084 0.0218  346 GLY A C   
2227 O  O   . GLY A 346 ? 0.0959 0.1102 0.0873 -0.0155 -0.0071 0.0204  346 GLY A O   
2228 N  N   . PRO A 347 ? 0.1108 0.1392 0.1040 -0.0157 -0.0100 0.0214  347 PRO A N   
2229 C  CA  . PRO A 347 ? 0.1120 0.1404 0.1091 -0.0178 -0.0097 0.0201  347 PRO A CA  
2230 C  C   . PRO A 347 ? 0.1276 0.1497 0.1243 -0.0212 -0.0092 0.0168  347 PRO A C   
2231 O  O   . PRO A 347 ? 0.1519 0.1701 0.1503 -0.0215 -0.0076 0.0174  347 PRO A O   
2232 C  CB  . PRO A 347 ? 0.1179 0.1572 0.1183 -0.0191 -0.0120 0.0200  347 PRO A CB  
2233 C  CG  . PRO A 347 ? 0.1382 0.1833 0.1370 -0.0152 -0.0129 0.0236  347 PRO A CG  
2234 C  CD  . PRO A 347 ? 0.1238 0.1626 0.1171 -0.0144 -0.0121 0.0233  347 PRO A CD  
2235 N  N   . LEU A 348 ? 0.1141 0.1352 0.1083 -0.0231 -0.0102 0.0136  348 LEU A N   
2236 C  CA  . LEU A 348 ? 0.1630 0.1777 0.1578 -0.0258 -0.0096 0.0105  348 LEU A CA  
2237 C  C   . LEU A 348 ? 0.1427 0.1496 0.1344 -0.0241 -0.0079 0.0107  348 LEU A C   
2238 O  O   . LEU A 348 ? 0.1704 0.1718 0.1627 -0.0255 -0.0071 0.0087  348 LEU A O   
2239 C  CB  . LEU A 348 ? 0.1588 0.1763 0.1535 -0.0287 -0.0116 0.0056  348 LEU A CB  
2240 C  CG  . LEU A 348 ? 0.1892 0.2146 0.1887 -0.0316 -0.0138 0.0044  348 LEU A CG  
2241 C  CD1 . LEU A 348 ? 0.3336 0.3623 0.3321 -0.0344 -0.0163 -0.0018 348 LEU A CD1 
2242 C  CD2 . LEU A 348 ? 0.2711 0.2934 0.2769 -0.0342 -0.0125 0.0057  348 LEU A CD2 
2243 N  N   . VAL A 349 ? 0.1309 0.1375 0.1202 -0.0211 -0.0072 0.0134  349 VAL A N   
2244 C  CA  . VAL A 349 ? 0.1305 0.1311 0.1181 -0.0199 -0.0058 0.0137  349 VAL A CA  
2245 C  C   . VAL A 349 ? 0.1671 0.1628 0.1564 -0.0201 -0.0047 0.0142  349 VAL A C   
2246 O  O   . VAL A 349 ? 0.2085 0.2056 0.1996 -0.0199 -0.0044 0.0156  349 VAL A O   
2247 C  CB  . VAL A 349 ? 0.1308 0.1322 0.1172 -0.0174 -0.0053 0.0166  349 VAL A CB  
2248 C  CG1 . VAL A 349 ? 0.1979 0.1937 0.1841 -0.0166 -0.0039 0.0171  349 VAL A CG1 
2249 C  CG2 . VAL A 349 ? 0.1630 0.1701 0.1469 -0.0168 -0.0060 0.0170  349 VAL A CG2 
2250 N  N   . ARG A 350 ? 0.2390 0.2303 0.2278 -0.0203 -0.0040 0.0132  350 ARG A N   
2251 C  CA  A ARG A 350 ? 0.2313 0.2190 0.2208 -0.0196 -0.0032 0.0144  350 ARG A CA  
2252 C  CA  C ARG A 350 ? 0.2314 0.2192 0.2209 -0.0196 -0.0032 0.0144  350 ARG A CA  
2253 C  C   . ARG A 350 ? 0.2406 0.2259 0.2291 -0.0186 -0.0027 0.0140  350 ARG A C   
2254 O  O   . ARG A 350 ? 0.1874 0.1737 0.1748 -0.0183 -0.0026 0.0132  350 ARG A O   
2255 C  CB  A ARG A 350 ? 0.2537 0.2395 0.2456 -0.0212 -0.0027 0.0145  350 ARG A CB  
2256 C  CB  C ARG A 350 ? 0.2541 0.2402 0.2458 -0.0210 -0.0027 0.0147  350 ARG A CB  
2257 C  CG  A ARG A 350 ? 0.2498 0.2332 0.2428 -0.0228 -0.0027 0.0118  350 ARG A CG  
2258 C  CG  C ARG A 350 ? 0.2426 0.2257 0.2358 -0.0226 -0.0026 0.0124  350 ARG A CG  
2259 C  CD  A ARG A 350 ? 0.2571 0.2376 0.2542 -0.0247 -0.0020 0.0124  350 ARG A CD  
2260 C  CD  C ARG A 350 ? 0.3080 0.2908 0.3053 -0.0252 -0.0024 0.0125  350 ARG A CD  
2261 N  NE  A ARG A 350 ? 0.2344 0.2120 0.2322 -0.0231 -0.0008 0.0156  350 ARG A NE  
2262 N  NE  C ARG A 350 ? 0.2947 0.2830 0.2927 -0.0268 -0.0037 0.0116  350 ARG A NE  
2263 C  CZ  A ARG A 350 ? 0.2422 0.2182 0.2434 -0.0238 0.0002  0.0186  350 ARG A CZ  
2264 C  CZ  C ARG A 350 ? 0.2522 0.2424 0.2547 -0.0298 -0.0040 0.0113  350 ARG A CZ  
2265 N  NH1 A ARG A 350 ? 0.2177 0.1924 0.2188 -0.0218 0.0012  0.0221  350 ARG A NH1 
2266 N  NH1 C ARG A 350 ? 0.1948 0.1807 0.2019 -0.0317 -0.0029 0.0122  350 ARG A NH1 
2267 N  NH2 A ARG A 350 ? 0.2393 0.2160 0.2445 -0.0268 0.0004  0.0186  350 ARG A NH2 
2268 N  NH2 C ARG A 350 ? 0.2166 0.2134 0.2198 -0.0309 -0.0055 0.0103  350 ARG A NH2 
2269 N  N   . SER A 351 ? 0.2401 0.2234 0.2292 -0.0177 -0.0024 0.0149  351 SER A N   
2270 C  CA  A SER A 351 ? 0.2553 0.2379 0.2445 -0.0168 -0.0023 0.0149  351 SER A CA  
2271 C  CA  B SER A 351 ? 0.2563 0.2388 0.2455 -0.0168 -0.0023 0.0149  351 SER A CA  
2272 C  C   . SER A 351 ? 0.2039 0.1858 0.1932 -0.0168 -0.0015 0.0136  351 SER A C   
2273 O  O   . SER A 351 ? 0.2880 0.2713 0.2771 -0.0162 -0.0010 0.0137  351 SER A O   
2274 C  CB  A SER A 351 ? 0.2803 0.2626 0.2703 -0.0159 -0.0026 0.0158  351 SER A CB  
2275 C  CB  B SER A 351 ? 0.2780 0.2603 0.2680 -0.0159 -0.0026 0.0158  351 SER A CB  
2276 O  OG  A SER A 351 ? 0.3090 0.2917 0.3004 -0.0154 -0.0026 0.0156  351 SER A OG  
2277 O  OG  B SER A 351 ? 0.3312 0.3145 0.3205 -0.0160 -0.0027 0.0167  351 SER A OG  
2278 N  N   . SER A 352 ? 0.1806 0.1604 0.1705 -0.0173 -0.0011 0.0122  352 SER A N   
2279 C  CA  . SER A 352 ? 0.1275 0.1061 0.1176 -0.0168 -0.0001 0.0099  352 SER A CA  
2280 C  C   . SER A 352 ? 0.1399 0.1209 0.1275 -0.0176 -0.0003 0.0069  352 SER A C   
2281 O  O   . SER A 352 ? 0.1545 0.1354 0.1413 -0.0168 0.0007  0.0042  352 SER A O   
2282 C  CB  . SER A 352 ? 0.1596 0.1335 0.1525 -0.0168 0.0005  0.0093  352 SER A CB  
2283 O  OG  . SER A 352 ? 0.1854 0.1585 0.1794 -0.0189 -0.0001 0.0097  352 SER A OG  
2284 N  N   . TYR A 353 ? 0.1401 0.1242 0.1264 -0.0188 -0.0015 0.0074  353 TYR A N   
2285 C  CA  . TYR A 353 ? 0.1137 0.1018 0.0976 -0.0196 -0.0023 0.0046  353 TYR A CA  
2286 C  C   . TYR A 353 ? 0.1226 0.1143 0.1031 -0.0179 -0.0013 0.0040  353 TYR A C   
2287 O  O   . TYR A 353 ? 0.1366 0.1310 0.1164 -0.0166 -0.0007 0.0077  353 TYR A O   
2288 C  CB  . TYR A 353 ? 0.1355 0.1279 0.1191 -0.0203 -0.0037 0.0066  353 TYR A CB  
2289 C  CG  . TYR A 353 ? 0.1451 0.1438 0.1261 -0.0209 -0.0050 0.0043  353 TYR A CG  
2290 C  CD1 . TYR A 353 ? 0.1844 0.1835 0.1662 -0.0231 -0.0062 -0.0005 353 TYR A CD1 
2291 C  CD2 . TYR A 353 ? 0.1205 0.1251 0.0988 -0.0192 -0.0053 0.0072  353 TYR A CD2 
2292 C  CE1 . TYR A 353 ? 0.2067 0.2134 0.1858 -0.0238 -0.0081 -0.0034 353 TYR A CE1 
2293 C  CE2 . TYR A 353 ? 0.1447 0.1571 0.1201 -0.0193 -0.0069 0.0057  353 TYR A CE2 
2294 C  CZ  . TYR A 353 ? 0.2050 0.2189 0.1805 -0.0217 -0.0085 0.0000  353 TYR A CZ  
2295 O  OH  . TYR A 353 ? 0.2351 0.2582 0.2074 -0.0219 -0.0106 -0.0022 353 TYR A OH  
2296 N  N   . LYS A 354 ? 0.1419 0.1339 0.1210 -0.0177 -0.0008 -0.0007 354 LYS A N   
2297 C  CA  . LYS A 354 ? 0.1183 0.1151 0.0935 -0.0157 0.0006  -0.0018 354 LYS A CA  
2298 C  C   . LYS A 354 ? 0.1199 0.1167 0.0965 -0.0138 0.0026  0.0026  354 LYS A C   
2299 O  O   . LYS A 354 ? 0.1388 0.1412 0.1131 -0.0124 0.0038  0.0051  354 LYS A O   
2300 C  CB  . LYS A 354 ? 0.1398 0.1450 0.1105 -0.0155 -0.0005 -0.0011 354 LYS A CB  
2301 C  CG  . LYS A 354 ? 0.2189 0.2267 0.1883 -0.0176 -0.0031 -0.0060 354 LYS A CG  
2302 C  CD  . LYS A 354 ? 0.2416 0.2598 0.2065 -0.0169 -0.0046 -0.0043 354 LYS A CD  
2303 C  CE  . LYS A 354 ? 0.3021 0.3274 0.2610 -0.0146 -0.0033 -0.0064 354 LYS A CE  
2304 N  NZ  . LYS A 354 ? 0.3416 0.3786 0.2955 -0.0137 -0.0052 -0.0048 354 LYS A NZ  
2305 N  N   . ALA A 355 ? 0.1262 0.1174 0.1071 -0.0138 0.0030  0.0040  355 ALA A N   
2306 C  CA  . ALA A 355 ? 0.1086 0.1007 0.0919 -0.0128 0.0041  0.0080  355 ALA A CA  
2307 C  C   . ALA A 355 ? 0.1310 0.1274 0.1134 -0.0108 0.0066  0.0077  355 ALA A C   
2308 O  O   . ALA A 355 ? 0.1585 0.1588 0.1421 -0.0104 0.0077  0.0116  355 ALA A O   
2309 C  CB  . ALA A 355 ? 0.1194 0.1067 0.1068 -0.0128 0.0037  0.0089  355 ALA A CB  
2310 N  N   . GLY A 356 ? 0.1288 0.1248 0.1097 -0.0094 0.0077  0.0030  356 GLY A N   
2311 C  CA  . GLY A 356 ? 0.1325 0.1337 0.1122 -0.0068 0.0105  0.0023  356 GLY A CA  
2312 C  C   . GLY A 356 ? 0.1764 0.1858 0.1510 -0.0064 0.0112  0.0038  356 GLY A C   
2313 O  O   . GLY A 356 ? 0.2014 0.2169 0.1759 -0.0047 0.0138  0.0068  356 GLY A O   
2314 N  N   . GLU A 357 ? 0.1351 0.1457 0.1057 -0.0078 0.0090  0.0024  357 GLU A N   
2315 C  CA  . GLU A 357 ? 0.1434 0.1629 0.1088 -0.0070 0.0094  0.0047  357 GLU A CA  
2316 C  C   . GLU A 357 ? 0.1483 0.1694 0.1166 -0.0075 0.0098  0.0129  357 GLU A C   
2317 O  O   . GLU A 357 ? 0.1653 0.1935 0.1323 -0.0060 0.0121  0.0174  357 GLU A O   
2318 C  CB  . GLU A 357 ? 0.2008 0.2224 0.1619 -0.0082 0.0065  0.0010  357 GLU A CB  
2319 C  CG  . GLU A 357 ? 0.2376 0.2574 0.1964 -0.0084 0.0058  -0.0079 357 GLU A CG  
2320 C  CD  . GLU A 357 ? 0.2847 0.3134 0.2370 -0.0056 0.0076  -0.0118 357 GLU A CD  
2321 O  OE1 . GLU A 357 ? 0.3324 0.3711 0.2794 -0.0045 0.0076  -0.0087 357 GLU A OE1 
2322 O  OE2 . GLU A 357 ? 0.3569 0.3827 0.3094 -0.0041 0.0094  -0.0176 357 GLU A OE2 
2323 N  N   . PHE A 358 ? 0.1505 0.1651 0.1234 -0.0095 0.0080  0.0149  358 PHE A N   
2324 C  CA  . PHE A 358 ? 0.1420 0.1565 0.1189 -0.0100 0.0084  0.0216  358 PHE A CA  
2325 C  C   . PHE A 358 ? 0.1363 0.1519 0.1177 -0.0096 0.0111  0.0245  358 PHE A C   
2326 O  O   . PHE A 358 ? 0.1474 0.1665 0.1313 -0.0096 0.0128  0.0304  358 PHE A O   
2327 C  CB  . PHE A 358 ? 0.1306 0.1380 0.1111 -0.0119 0.0061  0.0218  358 PHE A CB  
2328 C  CG  . PHE A 358 ? 0.1566 0.1647 0.1344 -0.0122 0.0038  0.0211  358 PHE A CG  
2329 C  CD1 . PHE A 358 ? 0.2395 0.2517 0.2166 -0.0114 0.0038  0.0258  358 PHE A CD1 
2330 C  CD2 . PHE A 358 ? 0.1435 0.1486 0.1203 -0.0134 0.0019  0.0164  358 PHE A CD2 
2331 C  CE1 . PHE A 358 ? 0.2068 0.2211 0.1822 -0.0113 0.0017  0.0256  358 PHE A CE1 
2332 C  CE2 . PHE A 358 ? 0.1971 0.2044 0.1725 -0.0139 -0.0001 0.0159  358 PHE A CE2 
2333 C  CZ  . PHE A 358 ? 0.1730 0.1853 0.1476 -0.0128 -0.0004 0.0203  358 PHE A CZ  
2334 N  N   . PHE A 359 ? 0.1332 0.1461 0.1166 -0.0094 0.0115  0.0210  359 PHE A N   
2335 C  CA  . PHE A 359 ? 0.1224 0.1377 0.1111 -0.0090 0.0138  0.0236  359 PHE A CA  
2336 C  C   . PHE A 359 ? 0.1368 0.1610 0.1230 -0.0068 0.0173  0.0258  359 PHE A C   
2337 O  O   . PHE A 359 ? 0.1590 0.1875 0.1495 -0.0073 0.0194  0.0316  359 PHE A O   
2338 C  CB  . PHE A 359 ? 0.1366 0.1481 0.1280 -0.0083 0.0133  0.0196  359 PHE A CB  
2339 C  CG  . PHE A 359 ? 0.1246 0.1387 0.1233 -0.0084 0.0146  0.0224  359 PHE A CG  
2340 C  CD1 . PHE A 359 ? 0.1371 0.1478 0.1412 -0.0106 0.0123  0.0237  359 PHE A CD1 
2341 C  CD2 . PHE A 359 ? 0.1568 0.1776 0.1568 -0.0063 0.0180  0.0233  359 PHE A CD2 
2342 C  CE1 . PHE A 359 ? 0.1449 0.1592 0.1564 -0.0112 0.0129  0.0259  359 PHE A CE1 
2343 C  CE2 . PHE A 359 ? 0.1553 0.1799 0.1633 -0.0066 0.0190  0.0261  359 PHE A CE2 
2344 C  CZ  . PHE A 359 ? 0.1460 0.1675 0.1600 -0.0093 0.0163  0.0273  359 PHE A CZ  
2345 N  N   . LEU A 360 ? 0.1385 0.1660 0.1180 -0.0046 0.0180  0.0210  360 LEU A N   
2346 C  CA  . LEU A 360 ? 0.1360 0.1735 0.1116 -0.0019 0.0216  0.0224  360 LEU A CA  
2347 C  C   . LEU A 360 ? 0.1339 0.1778 0.1072 -0.0020 0.0223  0.0292  360 LEU A C   
2348 O  O   . LEU A 360 ? 0.1632 0.2148 0.1378 -0.0009 0.0258  0.0350  360 LEU A O   
2349 C  CB  . LEU A 360 ? 0.1878 0.2273 0.1560 0.0006  0.0218  0.0144  360 LEU A CB  
2350 C  CG  . LEU A 360 ? 0.2757 0.3110 0.2468 0.0023  0.0229  0.0087  360 LEU A CG  
2351 C  CD1 . LEU A 360 ? 0.2935 0.3314 0.2574 0.0049  0.0237  0.0005  360 LEU A CD1 
2352 C  CD2 . LEU A 360 ? 0.3202 0.3603 0.2972 0.0039  0.0265  0.0129  360 LEU A CD2 
2353 N  N   . LYS A 361 ? 0.1548 0.1961 0.1253 -0.0032 0.0193  0.0295  361 LYS A N   
2354 C  CA  . LYS A 361 ? 0.1581 0.2060 0.1264 -0.0026 0.0201  0.0366  361 LYS A CA  
2355 C  C   . LYS A 361 ? 0.1548 0.1998 0.1319 -0.0043 0.0213  0.0449  361 LYS A C   
2356 O  O   . LYS A 361 ? 0.1849 0.2367 0.1632 -0.0034 0.0243  0.0527  361 LYS A O   
2357 C  CB  . LYS A 361 ? 0.1675 0.2142 0.1313 -0.0030 0.0163  0.0346  361 LYS A CB  
2358 C  CG  . LYS A 361 ? 0.2550 0.3086 0.2172 -0.0017 0.0168  0.0427  361 LYS A CG  
2359 C  CD  . LYS A 361 ? 0.3529 0.4063 0.3116 -0.0020 0.0128  0.0405  361 LYS A CD  
2360 C  CE  . LYS A 361 ? 0.4580 0.5168 0.4170 -0.0003 0.0131  0.0498  361 LYS A CE  
2361 N  NZ  . LYS A 361 ? 0.5054 0.5596 0.4663 -0.0012 0.0095  0.0490  361 LYS A NZ  
2362 N  N   . ASN A 362 ? 0.1533 0.1885 0.1369 -0.0070 0.0191  0.0436  362 ASN A N   
2363 C  CA  . ASN A 362 ? 0.1627 0.1935 0.1544 -0.0090 0.0193  0.0498  362 ASN A CA  
2364 C  C   . ASN A 362 ? 0.1897 0.2187 0.1905 -0.0111 0.0209  0.0515  362 ASN A C   
2365 O  O   . ASN A 362 ? 0.2623 0.2889 0.2709 -0.0131 0.0217  0.0571  362 ASN A O   
2366 C  CB  . ASN A 362 ? 0.1655 0.1873 0.1584 -0.0105 0.0156  0.0469  362 ASN A CB  
2367 C  CG  . ASN A 362 ? 0.2403 0.2645 0.2271 -0.0089 0.0140  0.0475  362 ASN A CG  
2368 O  OD1 . ASN A 362 ? 0.3093 0.3362 0.2972 -0.0079 0.0150  0.0543  362 ASN A OD1 
2369 N  ND2 . ASN A 362 ? 0.2004 0.2241 0.1815 -0.0086 0.0115  0.0408  362 ASN A ND2 
2370 N  N   . LEU A 363 ? 0.1396 0.1687 0.1407 -0.0110 0.0208  0.0464  363 LEU A N   
2371 C  CA  . LEU A 363 ? 0.1455 0.1753 0.1557 -0.0128 0.0221  0.0478  363 LEU A CA  
2372 C  C   . LEU A 363 ? 0.1990 0.2389 0.2090 -0.0107 0.0263  0.0501  363 LEU A C   
2373 O  O   . LEU A 363 ? 0.2093 0.2540 0.2266 -0.0119 0.0292  0.0563  363 LEU A O   
2374 C  CB  . LEU A 363 ? 0.1301 0.1541 0.1422 -0.0137 0.0190  0.0415  363 LEU A CB  
2375 C  CG  . LEU A 363 ? 0.2158 0.2311 0.2303 -0.0162 0.0153  0.0399  363 LEU A CG  
2376 C  CD1 . LEU A 363 ? 0.2784 0.2895 0.2915 -0.0161 0.0125  0.0339  363 LEU A CD1 
2377 C  CD2 . LEU A 363 ? 0.2341 0.2478 0.2588 -0.0195 0.0154  0.0436  363 LEU A CD2 
2378 N  N   . VAL A 364 ? 0.1364 0.1795 0.1388 -0.0075 0.0269  0.0449  364 VAL A N   
2379 C  CA  . VAL A 364 ? 0.1225 0.1757 0.1235 -0.0045 0.0312  0.0457  364 VAL A CA  
2380 C  C   . VAL A 364 ? 0.1487 0.2108 0.1446 -0.0028 0.0344  0.0517  364 VAL A C   
2381 O  O   . VAL A 364 ? 0.1385 0.2108 0.1355 -0.0009 0.0389  0.0557  364 VAL A O   
2382 C  CB  . VAL A 364 ? 0.1401 0.1921 0.1347 -0.0015 0.0306  0.0370  364 VAL A CB  
2383 C  CG1 . VAL A 364 ? 0.1839 0.2466 0.1746 0.0026  0.0353  0.0363  364 VAL A CG1 
2384 C  CG2 . VAL A 364 ? 0.1690 0.2142 0.1701 -0.0026 0.0284  0.0334  364 VAL A CG2 
2385 N  N   . ALA A 365 ? 0.1639 0.2239 0.1543 -0.0030 0.0323  0.0528  365 ALA A N   
2386 C  CA  . ALA A 365 ? 0.1759 0.2457 0.1597 -0.0005 0.0348  0.0583  365 ALA A CA  
2387 C  C   . ALA A 365 ? 0.1624 0.2429 0.1375 0.0037  0.0377  0.0542  365 ALA A C   
2388 O  O   . ALA A 365 ? 0.2000 0.2921 0.1734 0.0059  0.0421  0.0602  365 ALA A O   
2389 C  CB  . ALA A 365 ? 0.2023 0.2758 0.1944 -0.0020 0.0381  0.0699  365 ALA A CB  
2390 N  N   . LYS A 366 ? 0.1632 0.2398 0.1332 0.0048  0.0355  0.0439  366 LYS A N   
2391 C  CA  . LYS A 366 ? 0.1671 0.2521 0.1298 0.0089  0.0383  0.0380  366 LYS A CA  
2392 C  C   . LYS A 366 ? 0.1850 0.2812 0.1364 0.0117  0.0390  0.0388  366 LYS A C   
2393 O  O   . LYS A 366 ? 0.2308 0.3249 0.1773 0.0108  0.0351  0.0374  366 LYS A O   
2394 C  CB  . LYS A 366 ? 0.2018 0.2779 0.1626 0.0092  0.0354  0.0266  366 LYS A CB  
2395 C  CG  . LYS A 366 ? 0.2946 0.3776 0.2496 0.0137  0.0386  0.0194  366 LYS A CG  
2396 C  CD  . LYS A 366 ? 0.4200 0.4929 0.3748 0.0140  0.0362  0.0087  366 LYS A CD  
2397 C  CE  . LYS A 366 ? 0.4500 0.5286 0.4011 0.0188  0.0400  0.0016  366 LYS A CE  
2398 N  NZ  . LYS A 366 ? 0.4821 0.5641 0.4414 0.0207  0.0442  0.0059  366 LYS A NZ  
2399 N  N   . ARG A 367 ? 0.2047 0.3143 0.1522 0.0154  0.0440  0.0414  367 ARG A N   
2400 C  CA  . ARG A 367 ? 0.3221 0.4449 0.2575 0.0188  0.0448  0.0415  367 ARG A CA  
2401 C  C   . ARG A 367 ? 0.3962 0.5192 0.3221 0.0211  0.0428  0.0275  367 ARG A C   
2402 O  O   . ARG A 367 ? 0.4304 0.5521 0.3572 0.0231  0.0450  0.0203  367 ARG A O   
2403 C  CB  . ARG A 367 ? 0.2804 0.4165 0.2162 0.0218  0.0504  0.0492  367 ARG A CB  
2404 C  CG  . ARG A 367 ? 0.2610 0.3946 0.2079 0.0189  0.0511  0.0621  367 ARG A CG  
2405 C  CD  . ARG A 367 ? 0.2945 0.4388 0.2429 0.0214  0.0546  0.0693  367 ARG A CD  
2406 N  NE  . ARG A 367 ? 0.3582 0.5112 0.2975 0.0244  0.0529  0.0702  367 ARG A NE  
2407 C  CZ  . ARG A 367 ? 0.4740 0.6389 0.4046 0.0287  0.0546  0.0663  367 ARG A CZ  
2408 N  NH1 . ARG A 367 ? 0.4543 0.6233 0.3837 0.0310  0.0582  0.0608  367 ARG A NH1 
2409 N  NH2 . ARG A 367 ? 0.5707 0.7442 0.4941 0.0311  0.0526  0.0680  367 ARG A NH2 
2410 N  N   . LYS A 368 ? 0.5574 0.6822 0.4751 0.0209  0.0386  0.0235  368 LYS A N   
2411 C  CA  . LYS A 368 ? 0.5456 0.6687 0.4558 0.0218  0.0357  0.0093  368 LYS A CA  
2412 C  C   . LYS A 368 ? 0.5618 0.6975 0.4633 0.0270  0.0399  0.0029  368 LYS A C   
2413 O  O   . LYS A 368 ? 0.6739 0.8211 0.5690 0.0293  0.0400  0.0052  368 LYS A O   
2414 C  CB  . LYS A 368 ? 0.5422 0.6678 0.4459 0.0203  0.0303  0.0073  368 LYS A CB  
2415 C  CG  . LYS A 368 ? 0.6115 0.7352 0.5090 0.0201  0.0267  -0.0078 368 LYS A CG  
2416 C  CD  . LYS A 368 ? 0.5745 0.6805 0.4804 0.0175  0.0254  -0.0154 368 LYS A CD  
2417 C  CE  . LYS A 368 ? 0.5599 0.6619 0.4619 0.0161  0.0212  -0.0294 368 LYS A CE  
2418 N  NZ  . LYS A 368 ? 0.5664 0.6522 0.4765 0.0145  0.0211  -0.0366 368 LYS A NZ  
2419 C  C1  . GLC B .   ? 0.1945 0.2968 0.3417 -0.0450 0.0076  0.0482  1   GLC E C1  
2420 C  C2  . GLC B .   ? 0.2336 0.3371 0.3689 -0.0367 0.0091  0.0474  1   GLC E C2  
2421 C  C3  . GLC B .   ? 0.2190 0.3356 0.3606 -0.0332 0.0139  0.0522  1   GLC E C3  
2422 C  C4  . GLC B .   ? 0.1107 0.2288 0.2553 -0.0346 0.0203  0.0584  1   GLC E C4  
2423 C  C5  . GLC B .   ? 0.1459 0.2618 0.3019 -0.0431 0.0192  0.0606  1   GLC E C5  
2424 C  C6  . GLC B .   ? 0.1674 0.2835 0.3248 -0.0439 0.0261  0.0683  1   GLC E C6  
2425 O  O1  . GLC B .   ? 0.1750 0.2898 0.3369 -0.0487 0.0050  0.0481  1   GLC E O1  
2426 O  O2  . GLC B .   ? 0.1962 0.2996 0.3273 -0.0347 0.0032  0.0420  1   GLC E O2  
2427 O  O3  . GLC B .   ? 0.1858 0.3019 0.3168 -0.0250 0.0157  0.0509  1   GLC E O3  
2428 O  O4  . GLC B .   ? 0.1526 0.2854 0.3049 -0.0316 0.0249  0.0629  1   GLC E O4  
2429 O  O5  . GLC B .   ? 0.1760 0.2780 0.3267 -0.0464 0.0140  0.0552  1   GLC E O5  
2430 O  O6  . GLC B .   ? 0.1252 0.2306 0.2663 -0.0395 0.0281  0.0678  1   GLC E O6  
2431 C  C1  . GLC B .   ? 0.2229 0.3349 0.3955 -0.0568 0.0019  0.0462  2   GLC E C1  
2432 C  C2  . GLC B .   ? 0.2340 0.3603 0.4218 -0.0605 -0.0007 0.0458  2   GLC E C2  
2433 C  C3  . GLC B .   ? 0.2454 0.3801 0.4317 -0.0578 -0.0064 0.0412  2   GLC E C3  
2434 C  C4  . GLC B .   ? 0.3446 0.4687 0.5210 -0.0586 -0.0125 0.0333  2   GLC E C4  
2435 C  C5  . GLC B .   ? 0.2987 0.4070 0.4580 -0.0539 -0.0093 0.0336  2   GLC E C5  
2436 C  C6  . GLC B .   ? 0.2769 0.3750 0.4263 -0.0542 -0.0143 0.0266  2   GLC E C6  
2437 O  O2  . GLC B .   ? 0.1755 0.3118 0.3679 -0.0577 0.0058  0.0527  2   GLC E O2  
2438 O  O3  . GLC B .   ? 0.2846 0.4335 0.4850 -0.0615 -0.0093 0.0401  2   GLC E O3  
2439 O  O4  . GLC B .   ? 0.3583 0.4912 0.5315 -0.0551 -0.0178 0.0296  2   GLC E O4  
2440 O  O5  . GLC B .   ? 0.3200 0.4210 0.4835 -0.0574 -0.0039 0.0385  2   GLC E O5  
2441 O  O6  . GLC B .   ? 0.3840 0.4696 0.5189 -0.0496 -0.0108 0.0278  2   GLC E O6  
2442 S  S1  A DTT C .   ? 0.2090 0.2301 0.1815 -0.0016 -0.0058 0.0332  401 DTT A S1  
2443 S  S1  B DTT C .   ? 0.1630 0.1843 0.1356 -0.0013 -0.0055 0.0347  401 DTT A S1  
2444 C  C1  A DTT C .   ? 0.1564 0.1676 0.1341 -0.0048 -0.0063 0.0285  401 DTT A C1  
2445 C  C1  B DTT C .   ? 0.2803 0.2903 0.2598 -0.0041 -0.0048 0.0336  401 DTT A C1  
2446 C  C2  A DTT C .   ? 0.2950 0.2988 0.2759 -0.0069 -0.0040 0.0292  401 DTT A C2  
2447 C  C2  B DTT C .   ? 0.2851 0.2900 0.2654 -0.0066 -0.0036 0.0302  401 DTT A C2  
2448 O  O2  A DTT C .   ? 0.2686 0.2731 0.2498 -0.0068 -0.0017 0.0339  401 DTT A O2  
2449 O  O2  B DTT C .   ? 0.2301 0.2367 0.2094 -0.0068 -0.0016 0.0325  401 DTT A O2  
2450 C  C3  A DTT C .   ? 0.2348 0.2325 0.2202 -0.0080 -0.0038 0.0294  401 DTT A C3  
2451 C  C3  B DTT C .   ? 0.3692 0.3664 0.3542 -0.0087 -0.0027 0.0299  401 DTT A C3  
2452 O  O3  A DTT C .   ? 0.2927 0.2932 0.2791 -0.0059 -0.0047 0.0320  401 DTT A O3  
2453 O  O3  B DTT C .   ? 0.1658 0.1621 0.1501 -0.0095 -0.0043 0.0248  401 DTT A O3  
2454 C  C4  A DTT C .   ? 0.1893 0.1810 0.1780 -0.0097 -0.0016 0.0311  401 DTT A C4  
2455 C  C4  B DTT C .   ? 0.2214 0.2160 0.2099 -0.0077 -0.0022 0.0333  401 DTT A C4  
2456 S  S4  A DTT C .   ? 0.3450 0.3357 0.3368 -0.0091 0.0008  0.0382  401 DTT A S4  
2457 S  S4  B DTT C .   ? 0.2338 0.2232 0.2270 -0.0084 0.0007  0.0389  401 DTT A S4  
2458 S  S   . SO4 D .   ? 0.4654 0.4884 0.5112 0.0009  0.0369  0.1420  402 SO4 A S   
2459 O  O1  . SO4 D .   ? 0.3653 0.3838 0.4082 0.0040  0.0343  0.1398  402 SO4 A O1  
2460 O  O2  . SO4 D .   ? 0.3039 0.3209 0.3498 -0.0044 0.0357  0.1333  402 SO4 A O2  
2461 O  O3  . SO4 D .   ? 0.3241 0.3413 0.3822 -0.0008 0.0401  0.1491  402 SO4 A O3  
2462 O  O4  . SO4 D .   ? 0.3566 0.3965 0.3935 0.0048  0.0375  0.1455  402 SO4 A O4  
2463 FE FE1 . SF4 E .   ? 0.1570 0.1916 0.1230 0.0006  0.0035  0.0441  403 SF4 A FE1 
2464 FE FE2 . SF4 E .   ? 0.1475 0.1762 0.1215 0.0007  0.0044  0.0566  403 SF4 A FE2 
2465 FE FE3 . SF4 E .   ? 0.1691 0.1903 0.1418 -0.0019 -0.0006 0.0405  403 SF4 A FE3 
2466 FE FE4 . SF4 E .   ? 0.1495 0.1667 0.1288 -0.0052 0.0050  0.0472  403 SF4 A FE4 
2467 S  S1  . SF4 E .   ? 0.1516 0.1642 0.1335 -0.0037 0.0030  0.0500  403 SF4 A S1  
2468 S  S2  . SF4 E .   ? 0.1695 0.1898 0.1416 -0.0038 0.0014  0.0356  403 SF4 A S2  
2469 S  S3  . SF4 E .   ? 0.1497 0.1813 0.1244 -0.0014 0.0085  0.0571  403 SF4 A S3  
2470 S  S4  . SF4 E .   ? 0.1708 0.2093 0.1344 0.0034  -0.0003 0.0459  403 SF4 A S4  
2471 FE FE1 . SF4 F .   ? 0.1818 0.1520 0.1782 -0.0220 -0.0003 0.0046  404 SF4 A FE1 
2472 FE FE2 . SF4 F .   ? 0.1560 0.1150 0.1598 -0.0240 0.0011  -0.0024 404 SF4 A FE2 
2473 FE FE3 . SF4 F .   ? 0.1514 0.1241 0.1449 -0.0240 -0.0015 -0.0059 404 SF4 A FE3 
2474 FE FE4 . SF4 F .   ? 0.1538 0.1238 0.1557 -0.0283 -0.0021 -0.0002 404 SF4 A FE4 
2475 S  S1  . SF4 F .   ? 0.1556 0.1205 0.1578 -0.0287 -0.0019 -0.0105 404 SF4 A S1  
2476 S  S2  . SF4 F .   ? 0.1489 0.1272 0.1423 -0.0248 -0.0028 0.0016  404 SF4 A S2  
2477 S  S3  . SF4 F .   ? 0.1962 0.1592 0.2009 -0.0249 0.0006  0.0067  404 SF4 A S3  
2478 S  S4  . SF4 F .   ? 0.1614 0.1276 0.1573 -0.0197 0.0014  -0.0018 404 SF4 A S4  
2479 O  O   . HOH G .   ? 0.4136 0.4886 0.3793 0.0236  0.0011  0.0947  501 HOH A O   
2480 O  O   . HOH G .   ? 0.5080 0.5661 0.5004 -0.0476 -0.0322 -0.0413 502 HOH A O   
2481 O  O   . HOH G .   ? 0.4441 0.4812 0.4641 0.0257  0.0132  0.0216  503 HOH A O   
2482 O  O   . HOH G .   ? 0.4808 0.4000 0.5481 -0.0300 -0.0149 -0.0489 504 HOH A O   
2483 O  O   . HOH G .   ? 0.2535 0.3273 0.3254 0.0212  -0.0046 0.0444  505 HOH A O   
2484 O  O   . HOH G .   ? 0.4369 0.4279 0.4227 -0.0125 -0.0026 0.0152  506 HOH A O   
2485 O  O   . HOH G .   ? 0.5002 0.5571 0.4546 0.0054  -0.0164 0.0217  507 HOH A O   
2486 O  O   . HOH G .   ? 0.3784 0.3537 0.3728 -0.0188 -0.0006 0.0155  508 HOH A O   
2487 O  O   . HOH G .   ? 0.4751 0.4894 0.5519 -0.0046 0.0461  0.1616  509 HOH A O   
2488 O  O   . HOH G .   ? 0.4700 0.4499 0.4632 -0.0143 -0.0010 0.0154  510 HOH A O   
2489 O  O   . HOH G .   ? 0.4961 0.5403 0.4575 -0.0074 -0.0369 -0.0721 511 HOH A O   
2490 O  O   . HOH G .   ? 0.4562 0.5790 0.3986 0.0243  0.0525  0.0273  512 HOH A O   
2491 O  O   . HOH G .   ? 0.5241 0.5961 0.4934 -0.0130 -0.0476 -0.0573 513 HOH A O   
2492 O  O   . HOH G .   ? 0.3283 0.3584 0.3104 -0.0043 -0.0047 0.0413  514 HOH A O   
2493 O  O   . HOH G .   ? 0.4600 0.4850 0.4974 0.0337  0.0057  0.0490  515 HOH A O   
2494 O  O   . HOH G .   ? 0.5511 0.5209 0.5671 -0.0207 -0.0248 -0.0638 516 HOH A O   
2495 O  O   . HOH G .   ? 0.4443 0.3227 0.4934 0.0336  0.0398  -0.0779 517 HOH A O   
2496 O  O   . HOH G .   ? 0.5370 0.4987 0.6347 -0.0477 0.0015  0.0279  518 HOH A O   
2497 O  O   . HOH G .   ? 0.4613 0.5547 0.4788 0.0338  0.0314  0.0233  519 HOH A O   
2498 O  O   . HOH G .   ? 0.4597 0.3603 0.5341 -0.0214 -0.0060 -0.0351 520 HOH A O   
2499 O  O   . HOH G .   ? 0.3589 0.3842 0.3840 0.0243  0.0074  0.0309  521 HOH A O   
2500 O  O   . HOH G .   ? 0.2812 0.2766 0.2861 0.0064  0.0034  0.0682  522 HOH A O   
2501 O  O   . HOH G .   ? 0.4167 0.4358 0.3975 -0.0073 0.0032  0.0422  523 HOH A O   
2502 O  O   . HOH G .   ? 0.2002 0.2805 0.2061 0.0268  -0.0090 0.0878  524 HOH A O   
2503 O  O   . HOH G .   ? 0.4849 0.2755 0.6090 -0.0137 0.0282  -0.0474 525 HOH A O   
2504 O  O   . HOH G .   ? 0.4429 0.3278 0.5364 0.0455  0.0348  0.0316  526 HOH A O   
2505 O  O   . HOH G .   ? 0.5771 0.4964 0.6188 0.0268  0.0111  -0.0340 527 HOH A O   
2506 O  O   . HOH G .   ? 0.4395 0.3914 0.4920 0.0278  0.0119  0.0474  528 HOH A O   
2507 O  O   . HOH G .   ? 0.4388 0.5573 0.4350 0.0401  -0.0283 0.0897  529 HOH A O   
2508 O  O   . HOH G .   ? 0.3702 0.3987 0.4379 0.0608  0.0024  0.1067  530 HOH A O   
2509 O  O   . HOH G .   ? 0.4689 0.4624 0.4533 -0.0119 -0.0025 0.0225  531 HOH A O   
2510 O  O   . HOH G .   ? 0.2175 0.2156 0.2094 0.0040  0.0036  0.0066  532 HOH A O   
2511 O  O   . HOH G .   ? 0.4826 0.4915 0.5003 -0.0304 0.0057  0.0348  533 HOH A O   
2512 O  O   . HOH G .   ? 0.4668 0.4548 0.5141 -0.0551 -0.0042 0.0080  534 HOH A O   
2513 O  O   . HOH G .   ? 0.2262 0.2106 0.2188 -0.0155 -0.0044 0.0146  535 HOH A O   
2514 O  O   . HOH G .   ? 0.4900 0.4841 0.4607 -0.0268 -0.0083 -0.0733 536 HOH A O   
2515 O  O   . HOH G .   ? 0.4571 0.4855 0.4435 -0.0015 0.0084  0.0651  537 HOH A O   
2516 O  O   . HOH G .   ? 0.4376 0.3994 0.4606 0.0354  0.0366  -0.0308 538 HOH A O   
2517 O  O   . HOH G .   ? 0.4497 0.4586 0.4609 -0.0337 -0.0060 0.0137  539 HOH A O   
2518 O  O   . HOH G .   ? 0.2108 0.2076 0.2048 -0.0127 0.0061  0.0180  540 HOH A O   
2519 O  O   . HOH G .   ? 0.5138 0.4324 0.5651 -0.0511 -0.0023 -0.0449 541 HOH A O   
2520 O  O   . HOH G .   ? 0.2967 0.3054 0.2711 -0.0066 -0.0040 0.0209  542 HOH A O   
2521 O  O   . HOH G .   ? 0.3831 0.3869 0.3976 0.0159  0.0058  0.0227  543 HOH A O   
2522 O  O   . HOH G .   ? 0.5447 0.5835 0.5219 -0.0030 0.0119  0.0596  544 HOH A O   
2523 O  O   . HOH G .   ? 0.4628 0.5465 0.5821 0.0732  0.0331  0.0477  545 HOH A O   
2524 O  O   . HOH G .   ? 0.4252 0.4554 0.4147 0.0095  -0.0098 0.0540  546 HOH A O   
2525 O  O   . HOH G .   ? 0.3893 0.5174 0.4828 -0.0336 -0.0506 -0.0009 547 HOH A O   
2526 O  O   . HOH G .   ? 0.5565 0.6301 0.4659 0.0148  0.0195  -0.0620 548 HOH A O   
2527 O  O   . HOH G .   ? 0.2426 0.2538 0.2368 0.0126  0.0268  -0.0061 549 HOH A O   
2528 O  O   . HOH G .   ? 0.1980 0.1858 0.2136 -0.0123 0.0093  0.0534  550 HOH A O   
2529 O  O   . HOH G .   ? 0.5913 0.5006 0.6284 0.0464  0.0458  -0.0754 551 HOH A O   
2530 O  O   . HOH G .   ? 0.5116 0.5197 0.4751 -0.0144 0.0003  -0.0201 552 HOH A O   
2531 O  O   . HOH G .   ? 0.2742 0.3028 0.3421 -0.0314 0.0076  0.0369  553 HOH A O   
2532 O  O   . HOH G .   ? 0.2811 0.4132 0.2660 0.0119  -0.0262 0.0620  554 HOH A O   
2533 O  O   . HOH G .   ? 0.3830 0.4285 0.3135 -0.0084 -0.0019 -0.0617 555 HOH A O   
2534 O  O   . HOH G .   ? 0.3988 0.4630 0.3617 0.0084  -0.0200 0.0337  556 HOH A O   
2535 O  O   . HOH G .   ? 0.4564 0.5560 0.4433 0.0435  -0.0066 0.1183  557 HOH A O   
2536 O  O   . HOH G .   ? 0.3939 0.3841 0.3810 -0.0152 0.0011  0.0156  558 HOH A O   
2537 O  O   . HOH G .   ? 0.1643 0.2249 0.2262 -0.0083 -0.0086 0.0280  559 HOH A O   
2538 O  O   . HOH G .   ? 0.3811 0.4182 0.3866 0.0161  0.0340  0.0069  560 HOH A O   
2539 O  O   . HOH G .   ? 0.2465 0.2654 0.2764 -0.0193 0.0225  0.0636  561 HOH A O   
2540 O  O   . HOH G .   ? 0.3618 0.4238 0.4901 -0.0641 -0.0344 -0.0087 562 HOH A O   
2541 O  O   . HOH G .   ? 0.4687 0.5107 0.4608 0.0289  0.0207  0.0015  563 HOH A O   
2542 O  O   . HOH G .   ? 0.5369 0.4657 0.5632 0.0384  0.0402  -0.0608 564 HOH A O   
2543 O  O   . HOH G .   ? 0.3240 0.3314 0.3225 -0.0192 0.0054  0.0327  565 HOH A O   
2544 O  O   . HOH G .   ? 0.4630 0.5460 0.4388 0.0031  0.0292  0.0670  566 HOH A O   
2545 O  O   . HOH G .   ? 0.1021 0.1499 0.1132 -0.0140 -0.0087 0.0264  567 HOH A O   
2546 O  O   . HOH G .   ? 0.3988 0.3317 0.4478 0.0144  0.0158  0.0535  568 HOH A O   
2547 O  O   . HOH G .   ? 0.4293 0.3580 0.4853 -0.0653 -0.0126 -0.0780 569 HOH A O   
2548 O  O   . HOH G .   ? 0.3805 0.3845 0.3886 0.0111  0.0100  0.0952  570 HOH A O   
2549 O  O   . HOH G .   ? 0.3254 0.3937 0.3224 0.0121  0.0224  0.0264  571 HOH A O   
2550 O  O   . HOH G .   ? 0.4051 0.3915 0.4408 0.0256  0.0125  0.1066  572 HOH A O   
2551 O  O   . HOH G .   ? 0.4556 0.6000 0.4483 0.0146  -0.0511 0.0324  573 HOH A O   
2552 O  O   . HOH G .   ? 0.3156 0.2650 0.3569 0.0111  0.0140  0.0743  574 HOH A O   
2553 O  O   . HOH G .   ? 0.4480 0.4427 0.4949 -0.0106 0.0306  0.1154  575 HOH A O   
2554 O  O   . HOH G .   ? 0.2979 0.4059 0.2805 0.0066  0.0501  0.0803  576 HOH A O   
2555 O  O   . HOH G .   ? 0.1647 0.1865 0.1573 -0.0089 0.0147  0.0677  577 HOH A O   
2556 O  O   . HOH G .   ? 0.2816 0.3179 0.2356 0.0279  0.0115  -0.0319 578 HOH A O   
2557 O  O   . HOH G .   ? 0.3345 0.2899 0.3839 -0.0729 0.0000  0.0000  579 HOH A O   
2558 O  O   . HOH G .   ? 0.1256 0.1705 0.1688 0.0143  0.0256  0.0233  580 HOH A O   
2559 O  O   . HOH G .   ? 0.3934 0.4222 0.4100 -0.0182 0.0256  0.0869  581 HOH A O   
2560 O  O   . HOH G .   ? 0.3205 0.3813 0.4009 0.0368  0.0126  0.0427  582 HOH A O   
2561 O  O   . HOH G .   ? 0.2845 0.2602 0.3502 -0.0370 0.0019  0.0294  583 HOH A O   
2562 O  O   . HOH G .   ? 0.2998 0.3639 0.3789 0.0415  0.0308  0.0304  584 HOH A O   
2563 O  O   . HOH G .   ? 0.2740 0.2860 0.2797 -0.0091 -0.0124 0.0194  585 HOH A O   
2564 O  O   . HOH G .   ? 0.3725 0.3064 0.4623 -0.0211 0.0179  0.0672  586 HOH A O   
2565 O  O   . HOH G .   ? 0.5607 0.4272 0.6558 0.0442  0.0389  0.0076  587 HOH A O   
2566 O  O   . HOH G .   ? 0.5171 0.3770 0.5919 -0.0314 0.0131  -0.0515 588 HOH A O   
2567 O  O   . HOH G .   ? 0.3061 0.3160 0.2650 -0.0115 0.0026  -0.0310 589 HOH A O   
2568 O  O   . HOH G .   ? 0.4421 0.4987 0.5235 0.0569  0.0417  0.0227  590 HOH A O   
2569 O  O   . HOH G .   ? 0.2325 0.3243 0.2920 0.0095  -0.0233 0.0398  591 HOH A O   
2570 O  O   . HOH G .   ? 0.3447 0.3425 0.3517 0.0353  0.0169  -0.0123 592 HOH A O   
2571 O  O   . HOH G .   ? 0.4797 0.5410 0.5212 0.0331  0.0077  0.0424  593 HOH A O   
2572 O  O   . HOH G .   ? 0.4407 0.4536 0.5282 -0.0442 0.0000  0.0299  594 HOH A O   
2573 O  O   . HOH G .   ? 0.3534 0.3615 0.3432 0.0201  0.0318  -0.0211 595 HOH A O   
2574 O  O   . HOH G .   ? 0.4751 0.5058 0.4899 0.0384  0.0209  0.0058  596 HOH A O   
2575 O  O   . HOH G .   ? 0.4946 0.3663 0.5687 -0.0207 0.0182  -0.0025 597 HOH A O   
2576 O  O   . HOH G .   ? 0.4050 0.4006 0.4816 -0.0416 0.0006  0.0290  598 HOH A O   
2577 O  O   . HOH G .   ? 0.4368 0.5454 0.4731 -0.0133 0.0350  0.0688  599 HOH A O   
2578 O  O   . HOH G .   ? 0.2699 0.2601 0.3527 0.0625  0.0140  0.0919  600 HOH A O   
2579 O  O   . HOH G .   ? 0.4263 0.5011 0.3938 0.0022  0.0295  0.0645  601 HOH A O   
2580 O  O   . HOH G .   ? 0.2388 0.2604 0.2439 0.0094  0.0170  0.1071  602 HOH A O   
2581 O  O   . HOH G .   ? 0.4034 0.4308 0.5099 -0.0557 -0.0201 0.0035  603 HOH A O   
2582 O  O   . HOH G .   ? 0.1801 0.2395 0.1324 0.0088  0.0112  0.0295  604 HOH A O   
2583 O  O   . HOH G .   ? 0.4067 0.3795 0.4127 0.0248  0.0315  -0.0319 605 HOH A O   
2584 O  O   . HOH G .   ? 0.2371 0.2316 0.2093 -0.0113 0.0051  -0.0165 606 HOH A O   
2585 O  O   . HOH G .   ? 0.3410 0.3500 0.4200 -0.0506 -0.0288 -0.0190 607 HOH A O   
2586 O  O   . HOH G .   ? 0.4505 0.5772 0.4690 0.0236  -0.0401 0.0551  608 HOH A O   
2587 O  O   . HOH G .   ? 0.3535 0.2983 0.4439 -0.0347 0.0120  0.0502  609 HOH A O   
2588 O  O   . HOH G .   ? 0.3142 0.3486 0.3060 0.0068  0.0011  0.0698  610 HOH A O   
2589 O  O   . HOH G .   ? 0.1259 0.1993 0.1500 0.0233  -0.0088 0.0644  611 HOH A O   
2590 O  O   . HOH G .   ? 0.4352 0.4538 0.4577 0.0327  0.0146  0.0164  612 HOH A O   
2591 O  O   . HOH G .   ? 0.4480 0.4638 0.4649 -0.0139 0.0207  0.0691  613 HOH A O   
2592 O  O   . HOH G .   ? 0.3166 0.4554 0.3586 0.0002  -0.0510 0.0227  614 HOH A O   
2593 O  O   . HOH G .   ? 0.3227 0.3332 0.3248 -0.0251 -0.0049 0.0174  615 HOH A O   
2594 O  O   . HOH G .   ? 0.4320 0.3997 0.4841 0.0352  0.0118  0.0532  616 HOH A O   
2595 O  O   . HOH G .   ? 0.2860 0.1937 0.3438 -0.0098 -0.0024 -0.0304 617 HOH A O   
2596 O  O   . HOH G .   ? 0.5167 0.4232 0.6067 -0.0242 0.0061  0.0215  618 HOH A O   
2597 O  O   . HOH G .   ? 0.3130 0.2173 0.3755 0.0172  0.0108  -0.0045 619 HOH A O   
2598 O  O   . HOH G .   ? 0.2580 0.3626 0.2676 -0.0008 0.0362  0.0621  620 HOH A O   
2599 O  O   . HOH G .   ? 0.4358 0.3639 0.4803 0.0012  0.0151  0.0499  621 HOH A O   
2600 O  O   . HOH G .   ? 0.2700 0.3898 0.3200 -0.0271 -0.0586 -0.0157 622 HOH A O   
2601 O  O   . HOH G .   ? 0.2127 0.2017 0.2020 -0.0147 -0.0030 0.0168  623 HOH A O   
2602 O  O   . HOH G .   ? 0.2431 0.2339 0.2276 -0.0164 -0.0010 0.0143  624 HOH A O   
2603 O  O   . HOH G .   ? 0.3419 0.2615 0.4330 -0.0271 0.0099  0.0398  625 HOH A O   
2604 O  O   . HOH G .   ? 0.1513 0.1897 0.1408 -0.0081 0.0187  0.0683  626 HOH A O   
2605 O  O   . HOH G .   ? 0.2651 0.2316 0.2934 -0.0200 0.0140  0.0624  627 HOH A O   
2606 O  O   . HOH G .   ? 0.4483 0.3926 0.4326 -0.0196 -0.0006 -0.1488 628 HOH A O   
2607 O  O   . HOH G .   ? 0.2309 0.2831 0.2653 -0.0303 0.0047  0.0355  629 HOH A O   
2608 O  O   . HOH G .   ? 0.4878 0.3839 0.5729 0.0644  0.0483  -0.0191 630 HOH A O   
2609 O  O   . HOH G .   ? 0.2599 0.3736 0.2073 0.0207  0.0328  0.0512  631 HOH A O   
2610 O  O   . HOH G .   ? 0.2972 0.2388 0.3485 -0.0304 -0.0175 -0.0408 632 HOH A O   
2611 O  O   . HOH G .   ? 0.4870 0.4883 0.4818 -0.0184 -0.0009 0.0207  633 HOH A O   
2612 O  O   . HOH G .   ? 0.1597 0.1613 0.1428 -0.0093 -0.0086 0.0175  634 HOH A O   
2613 O  O   . HOH G .   ? 0.4628 0.4346 0.4910 -0.0300 0.0103  0.0456  635 HOH A O   
2614 O  O   . HOH G .   ? 0.3991 0.5004 0.3456 0.0249  0.0074  0.0897  636 HOH A O   
2615 O  O   . HOH G .   ? 0.5282 0.5531 0.4552 -0.0004 0.0048  -0.1244 637 HOH A O   
2616 O  O   . HOH G .   ? 0.1716 0.2065 0.1589 -0.0023 0.0174  0.0826  638 HOH A O   
2617 O  O   . HOH G .   ? 0.3264 0.3664 0.3739 0.0518  -0.0033 0.1072  639 HOH A O   
2618 O  O   . HOH G .   ? 0.5380 0.6320 0.5003 0.0288  0.0057  0.1056  640 HOH A O   
2619 O  O   . HOH G .   ? 0.3541 0.4763 0.2658 0.0276  0.0113  0.0419  641 HOH A O   
2620 O  O   . HOH G .   ? 0.3583 0.4160 0.3316 0.0120  -0.0161 0.0503  642 HOH A O   
2621 O  O   . HOH G .   ? 0.2276 0.2628 0.1891 -0.0036 -0.0217 -0.0184 643 HOH A O   
2622 O  O   . HOH G .   ? 0.2802 0.2433 0.3615 0.0577  0.0282  0.0400  644 HOH A O   
2623 O  O   . HOH G .   ? 0.1468 0.2240 0.2690 -0.0406 0.0212  0.0593  645 HOH A O   
2624 O  O   . HOH G .   ? 0.3988 0.4504 0.4521 -0.0444 -0.0498 -0.0442 646 HOH A O   
2625 O  O   . HOH G .   ? 0.3144 0.3135 0.3004 -0.0114 0.0019  0.0340  647 HOH A O   
2626 O  O   . HOH G .   ? 0.0981 0.1400 0.1434 -0.0088 0.0151  0.0315  648 HOH A O   
2627 O  O   . HOH G .   ? 0.4265 0.6028 0.5885 -0.0986 -0.0378 0.0005  649 HOH A O   
2628 O  O   . HOH G .   ? 0.4766 0.4943 0.4696 -0.0464 -0.0230 -0.0519 650 HOH A O   
2629 O  O   . HOH G .   ? 0.2197 0.2288 0.1951 -0.0071 -0.0092 0.0130  651 HOH A O   
2630 O  O   . HOH G .   ? 0.2460 0.2728 0.2564 0.0150  0.0091  0.0199  652 HOH A O   
2631 O  O   . HOH G .   ? 0.4701 0.5679 0.4303 0.0044  -0.0151 0.0508  653 HOH A O   
2632 O  O   . HOH G .   ? 0.3965 0.4161 0.3807 -0.0320 -0.0151 -0.0145 654 HOH A O   
2633 O  O   . HOH G .   ? 0.3371 0.3275 0.3448 -0.0472 -0.0159 -0.0410 655 HOH A O   
2634 O  O   . HOH G .   ? 0.1687 0.2009 0.2144 -0.0165 0.0083  0.0302  656 HOH A O   
2635 O  O   . HOH G .   ? 0.2172 0.2323 0.2313 -0.0207 0.0186  0.0690  657 HOH A O   
2636 O  O   . HOH G .   ? 0.1369 0.2012 0.1658 0.0138  -0.0017 0.0416  658 HOH A O   
2637 O  O   . HOH G .   ? 0.4805 0.5558 0.4212 0.0006  -0.0375 -0.0575 659 HOH A O   
2638 O  O   . HOH G .   ? 0.3315 0.3129 0.3752 0.0319  0.0112  0.1024  660 HOH A O   
2639 O  O   . HOH G .   ? 0.2912 0.2969 0.3258 0.0215  0.0214  0.0147  661 HOH A O   
2640 O  O   . HOH G .   ? 0.5371 0.5228 0.5507 -0.0301 0.0033  0.0282  662 HOH A O   
2641 O  O   . HOH G .   ? 0.5254 0.6234 0.4957 0.0296  0.0150  0.1210  663 HOH A O   
2642 O  O   . HOH G .   ? 0.2516 0.3355 0.2888 -0.0160 0.0166  0.0458  664 HOH A O   
2643 O  O   . HOH G .   ? 0.1765 0.2260 0.1917 0.0247  -0.0038 0.0794  665 HOH A O   
2644 O  O   . HOH G .   ? 0.4561 0.4377 0.4300 0.0087  0.0211  -0.0564 666 HOH A O   
2645 O  O   . HOH G .   ? 0.3717 0.3999 0.3468 -0.0068 0.0073  0.0425  667 HOH A O   
2646 O  O   . HOH G .   ? 0.2477 0.2971 0.2225 0.0149  0.0053  0.0907  668 HOH A O   
2647 O  O   . HOH G .   ? 0.3200 0.3246 0.4075 0.0636  0.0292  0.0391  669 HOH A O   
2648 O  O   . HOH G .   ? 0.3655 0.2004 0.4434 0.0164  0.0339  -0.0697 670 HOH A O   
2649 O  O   . HOH G .   ? 0.2361 0.1687 0.2711 -0.0086 0.0119  0.0373  671 HOH A O   
2650 O  O   . HOH G .   ? 0.4149 0.3304 0.5021 0.0408  0.0261  0.0821  672 HOH A O   
2651 O  O   . HOH G .   ? 0.4290 0.5178 0.5087 0.0129  -0.0080 0.0412  673 HOH A O   
2652 O  O   . HOH G .   ? 0.3672 0.4636 0.3457 0.0153  -0.0130 0.0742  674 HOH A O   
2653 O  O   . HOH G .   ? 0.3019 0.4275 0.2039 0.0286  0.0003  0.0250  675 HOH A O   
2654 O  O   . HOH G .   ? 0.4615 0.5376 0.4416 0.0129  0.0249  0.1103  676 HOH A O   
2655 O  O   . HOH G .   ? 0.4203 0.4043 0.5030 -0.0405 0.0107  0.0480  677 HOH A O   
2656 O  O   . HOH G .   ? 0.4426 0.4669 0.4654 -0.0409 -0.0099 0.0106  678 HOH A O   
2657 O  O   . HOH G .   ? 0.4787 0.4209 0.4779 0.0142  0.0258  -0.0687 679 HOH A O   
2658 O  O   . HOH G .   ? 0.5212 0.4518 0.5928 0.0280  0.0223  0.0929  680 HOH A O   
2659 O  O   . HOH G .   ? 0.3125 0.3346 0.2657 0.0206  0.0010  -0.0469 681 HOH A O   
2660 O  O   . HOH G .   ? 0.4766 0.5321 0.5301 -0.0398 0.0166  0.0559  682 HOH A O   
2661 O  O   . HOH G .   ? 0.4098 0.4081 0.3911 -0.0391 -0.0170 -0.0797 683 HOH A O   
2662 O  O   . HOH G .   ? 0.2210 0.2241 0.2395 0.0157  0.0035  0.0334  684 HOH A O   
2663 O  O   . HOH G .   ? 0.3517 0.2743 0.4227 0.0553  0.0412  -0.0077 685 HOH A O   
2664 O  O   . HOH G .   ? 0.4477 0.4948 0.3923 -0.0077 0.0007  -0.0034 686 HOH A O   
2665 O  O   . HOH G .   ? 0.3464 0.4622 0.4511 -0.0370 -0.0414 0.0051  687 HOH A O   
2666 O  O   . HOH G .   ? 0.3033 0.3376 0.3368 -0.0374 -0.0446 -0.0468 688 HOH A O   
2667 O  O   . HOH G .   ? 0.2886 0.2799 0.3293 -0.0329 -0.0151 -0.0002 689 HOH A O   
2668 O  O   . HOH G .   ? 0.4694 0.4144 0.5084 -0.0481 -0.0028 -0.0175 690 HOH A O   
2669 O  O   . HOH G .   ? 0.4535 0.3980 0.5499 -0.0453 -0.0007 0.0190  691 HOH A O   
2670 O  O   . HOH G .   ? 0.2752 0.3248 0.2138 0.0133  -0.0043 -0.0195 692 HOH A O   
2671 O  O   . HOH G .   ? 0.2194 0.2378 0.1988 -0.0090 -0.0021 0.0332  693 HOH A O   
2672 O  O   . HOH G .   ? 0.5874 0.6222 0.5257 -0.0249 -0.0180 -0.1297 694 HOH A O   
2673 O  O   . HOH G .   ? 0.3702 0.3610 0.3852 -0.0264 -0.0319 -0.0611 695 HOH A O   
2674 O  O   . HOH G .   ? 0.3866 0.4558 0.5160 -0.0494 0.0002  0.0374  696 HOH A O   
2675 O  O   . HOH G .   ? 0.5082 0.4911 0.4938 0.0206  0.0302  -0.0478 697 HOH A O   
2676 O  O   . HOH G .   ? 0.2808 0.4014 0.3442 -0.0258 -0.0089 0.0363  698 HOH A O   
2677 O  O   . HOH G .   ? 0.3385 0.3371 0.3332 -0.0176 0.0043  0.0333  699 HOH A O   
2678 O  O   . HOH G .   ? 0.4348 0.5441 0.4000 0.0134  -0.0371 0.0303  700 HOH A O   
2679 O  O   . HOH G .   ? 0.5302 0.4107 0.5583 -0.0027 0.0193  -0.1246 701 HOH A O   
2680 O  O   . HOH G .   ? 0.2337 0.2729 0.1889 0.0034  -0.0008 0.0206  702 HOH A O   
2681 O  O   . HOH G .   ? 0.4236 0.3509 0.4547 0.0182  0.0062  -0.0390 703 HOH A O   
2682 O  O   . HOH G .   ? 0.4695 0.4409 0.5092 0.0040  0.0209  0.1035  704 HOH A O   
2683 O  O   . HOH G .   ? 0.3814 0.3259 0.3986 0.0089  0.0015  -0.0302 705 HOH A O   
2684 O  O   . HOH G .   ? 0.5497 0.5500 0.5111 -0.0237 -0.0081 -0.0916 706 HOH A O   
2685 O  O   . HOH G .   ? 0.4414 0.4658 0.4780 -0.0550 -0.0159 -0.0045 707 HOH A O   
2686 O  O   . HOH G .   ? 0.4345 0.3549 0.5040 -0.0561 0.0026  -0.0103 708 HOH A O   
2687 O  O   . HOH G .   ? 0.4233 0.5267 0.5383 -0.0358 -0.0242 0.0195  709 HOH A O   
2688 O  O   . HOH G .   ? 0.4830 0.3401 0.5308 0.0147  0.0310  -0.1109 710 HOH A O   
2689 O  O   . HOH G .   ? 0.4347 0.4324 0.5086 0.0598  0.0171  0.1371  711 HOH A O   
2690 O  O   . HOH G .   ? 0.4462 0.5148 0.3698 0.0158  -0.0157 -0.0467 712 HOH A O   
2691 O  O   . HOH G .   ? 0.5124 0.5179 0.4725 0.0114  0.0230  -0.0527 713 HOH A O   
2692 O  O   . HOH G .   ? 0.2425 0.2506 0.2374 -0.0084 0.0079  0.0516  714 HOH A O   
2693 O  O   . HOH G .   ? 0.4575 0.4578 0.4908 -0.0319 0.0173  0.0635  715 HOH A O   
2694 O  O   . HOH G .   ? 0.5031 0.6755 0.5657 -0.0298 -0.0776 -0.0251 716 HOH A O   
2695 O  O   . HOH G .   ? 0.3855 0.3622 0.3812 -0.0162 0.0002  0.0230  717 HOH A O   
2696 O  O   . HOH G .   ? 0.3594 0.3668 0.3279 -0.0002 -0.0198 -0.0648 718 HOH A O   
2697 O  O   . HOH G .   ? 0.3889 0.2985 0.4469 0.0058  0.0192  0.0449  719 HOH A O   
2698 O  O   . HOH G .   ? 0.5307 0.5047 0.5229 -0.0025 -0.0160 -0.0700 720 HOH A O   
2699 O  O   . HOH G .   ? 0.2555 0.3484 0.2520 0.0115  0.0309  0.0392  721 HOH A O   
2700 O  O   . HOH G .   ? 0.4658 0.5461 0.5111 -0.0255 0.0394  0.0969  722 HOH A O   
2701 O  O   . HOH G .   ? 0.4622 0.5515 0.4094 0.0136  0.0211  0.0561  723 HOH A O   
2702 O  O   . HOH G .   ? 0.4421 0.4008 0.4205 -0.0021 0.0134  -0.0899 724 HOH A O   
2703 O  O   . HOH G .   ? 0.4285 0.5211 0.3931 0.0000  0.0301  0.0000  725 HOH A O   
2704 O  O   . HOH G .   ? 0.4461 0.3589 0.5229 0.0320  0.0241  0.0655  726 HOH A O   
2705 O  O   . HOH G .   ? 0.2047 0.2310 0.2293 0.0209  0.0030  0.0396  727 HOH A O   
2706 O  O   . HOH G .   ? 0.5002 0.4385 0.6039 -0.0497 -0.0065 0.0027  728 HOH A O   
2707 O  O   . HOH G .   ? 0.4762 0.6968 0.5183 0.0000  -0.0816 0.0000  729 HOH A O   
2708 O  O   . HOH G .   ? 0.4527 0.4925 0.4930 -0.0389 0.0043  0.0355  730 HOH A O   
2709 O  O   . HOH G .   ? 0.3344 0.3432 0.3696 -0.0231 0.0266  0.0917  731 HOH A O   
2710 O  O   . HOH G .   ? 0.5376 0.6686 0.4569 0.0187  0.0351  0.0450  732 HOH A O   
2711 O  O   . HOH G .   ? 0.4631 0.4462 0.4854 -0.0387 -0.0006 0.0165  733 HOH A O   
2712 O  O   . HOH G .   ? 0.4271 0.3696 0.4597 0.0407  0.0170  -0.0314 734 HOH A O   
2713 O  O   . HOH G .   ? 0.4794 0.5335 0.5106 -0.0222 0.0338  0.0947  735 HOH A O   
2714 O  O   . HOH G .   ? 0.1234 0.1721 0.1466 0.0154  -0.0025 0.0442  736 HOH A O   
2715 O  O   . HOH G .   ? 0.4623 0.3830 0.5304 0.0226  0.0214  0.0764  737 HOH A O   
2716 O  O   . HOH G .   ? 0.2917 0.3036 0.2527 0.0063  -0.0121 -0.0511 738 HOH A O   
2717 O  O   . HOH G .   ? 0.5225 0.5501 0.4998 -0.0461 -0.0276 -0.0869 739 HOH A O   
2718 O  O   . HOH G .   ? 0.2393 0.2469 0.2392 -0.0204 0.0022  0.0262  740 HOH A O   
2719 O  O   . HOH G .   ? 0.2692 0.3475 0.2843 0.0344  -0.0198 0.0818  741 HOH A O   
2720 O  O   . HOH G .   ? 0.4180 0.3255 0.4429 0.0250  0.0337  -0.0779 742 HOH A O   
2721 O  O   . HOH G .   ? 0.5401 0.4312 0.6184 0.0737  0.0582  -0.0554 743 HOH A O   
2722 O  O   . HOH G .   ? 0.4589 0.4013 0.5230 0.0204  0.0150  0.0729  744 HOH A O   
2723 O  O   . HOH G .   ? 0.4447 0.4585 0.4480 -0.0090 0.0150  0.0652  745 HOH A O   
2724 O  O   . HOH G .   ? 0.3128 0.4503 0.2989 -0.0121 -0.0666 -0.0348 746 HOH A O   
2725 O  O   . HOH G .   ? 0.5669 0.6130 0.4859 0.0045  0.0089  -0.0915 747 HOH A O   
2726 O  O   . HOH G .   ? 0.4050 0.3876 0.4474 0.0421  0.0152  0.0231  748 HOH A O   
2727 O  O   . HOH G .   ? 0.5234 0.5202 0.5538 0.0075  0.0160  0.0972  749 HOH A O   
2728 O  O   . HOH G .   ? 0.4740 0.4697 0.4931 0.0469  0.0218  -0.0125 750 HOH A O   
2729 O  O   . HOH G .   ? 0.5250 0.5990 0.5145 0.0186  -0.0062 0.0838  751 HOH A O   
2730 O  O   . HOH G .   ? 0.5098 0.6510 0.4538 0.0085  -0.0524 -0.0097 752 HOH A O   
2731 O  O   . HOH G .   ? 0.3661 0.3497 0.4636 0.0725  0.0315  0.0469  753 HOH A O   
2732 O  O   . HOH G .   ? 0.3888 0.5053 0.3782 0.0027  -0.0258 0.0475  754 HOH A O   
2733 O  O   . HOH G .   ? 0.2717 0.3180 0.3506 0.0505  0.0047  0.0646  755 HOH A O   
2734 O  O   . HOH G .   ? 0.4302 0.4450 0.4439 0.0071  0.0138  0.0949  756 HOH A O   
2735 O  O   . HOH G .   ? 0.4574 0.5325 0.4449 -0.0192 -0.0512 -0.0490 757 HOH A O   
2736 O  O   . HOH G .   ? 0.5074 0.4440 0.5720 0.0363  0.0158  0.0391  758 HOH A O   
2737 O  O   . HOH G .   ? 0.4580 0.5757 0.3508 0.0274  -0.0160 -0.0405 759 HOH A O   
2738 O  O   . HOH G .   ? 0.3479 0.3991 0.4381 0.0556  0.0117  0.0585  760 HOH A O   
2739 O  O   . HOH G .   ? 0.3815 0.4464 0.4548 0.0238  0.0049  0.0408  761 HOH A O   
2740 O  O   . HOH G .   ? 0.5139 0.5007 0.5040 -0.0176 -0.0017 0.0189  762 HOH A O   
2741 O  O   . HOH G .   ? 0.3761 0.3987 0.3404 -0.0019 -0.0048 0.0160  763 HOH A O   
2742 O  O   . HOH G .   ? 0.3423 0.4222 0.4076 0.0319  -0.0128 0.0587  764 HOH A O   
2743 O  O   . HOH G .   ? 0.4624 0.4600 0.4554 0.0388  0.0177  -0.0344 765 HOH A O   
2744 O  O   . HOH G .   ? 0.3998 0.4623 0.4746 -0.0455 0.0308  0.0839  766 HOH A O   
2745 O  O   . HOH G .   ? 0.5247 0.5581 0.4874 -0.0320 -0.0193 -0.0561 767 HOH A O   
2746 O  O   . HOH G .   ? 0.5046 0.5581 0.4506 -0.0048 0.0036  0.0132  768 HOH A O   
2747 O  O   . HOH G .   ? 0.3829 0.4671 0.4502 0.0196  -0.0140 0.0470  769 HOH A O   
2748 O  O   . HOH G .   ? 0.5168 0.4507 0.5598 -0.0028 0.0151  0.0589  770 HOH A O   
2749 O  O   . HOH G .   ? 0.4466 0.4743 0.4132 -0.0026 -0.0131 0.0128  771 HOH A O   
2750 O  O   . HOH G .   ? 0.4944 0.6011 0.4250 0.0085  -0.0373 -0.0209 772 HOH A O   
2751 O  O   . HOH G .   ? 0.4240 0.5328 0.4745 -0.0201 0.0305  0.0662  773 HOH A O   
2752 O  O   . HOH G .   ? 0.4833 0.4576 0.4903 -0.0203 0.0048  0.0347  774 HOH A O   
2753 O  O   . HOH G .   ? 0.3412 0.3518 0.3210 0.0010  0.0183  -0.0023 775 HOH A O   
2754 O  O   . HOH G .   ? 0.4497 0.4618 0.5693 0.0901  0.0243  0.0840  776 HOH A O   
2755 O  O   . HOH G .   ? 0.2433 0.2727 0.2371 0.0141  0.0095  0.0999  777 HOH A O   
2756 O  O   . HOH G .   ? 0.5260 0.4771 0.6070 -0.0488 -0.0258 -0.0467 778 HOH A O   
2757 O  O   . HOH G .   ? 0.1710 0.2322 0.2023 0.0252  -0.0035 0.0564  779 HOH A O   
2758 O  O   . HOH G .   ? 0.4152 0.5095 0.3751 0.0155  -0.0277 0.0405  780 HOH A O   
2759 O  O   . HOH G .   ? 0.4488 0.4468 0.4496 0.0292  0.0365  -0.0278 781 HOH A O   
2760 O  O   . HOH G .   ? 0.4237 0.5180 0.5118 0.0297  -0.0048 0.0512  782 HOH A O   
2761 O  O   . HOH G .   ? 0.4100 0.3950 0.4003 -0.0157 -0.0010 0.0226  783 HOH A O   
2762 O  O   . HOH G .   ? 0.4996 0.5518 0.5708 -0.0489 0.0214  0.0671  784 HOH A O   
2763 O  O   . HOH G .   ? 0.5097 0.6562 0.5773 -0.0169 0.0407  0.0777  785 HOH A O   
2764 O  O   . HOH G .   ? 0.4358 0.5723 0.4487 0.0138  -0.0480 0.0371  786 HOH A O   
2765 O  O   . HOH G .   ? 0.3309 0.4065 0.4091 0.0441  -0.0054 0.0656  787 HOH A O   
2766 O  O   . HOH G .   ? 0.4536 0.4418 0.4487 -0.0205 0.0001  0.0226  788 HOH A O   
2767 O  O   . HOH G .   ? 0.5059 0.6768 0.4852 0.0245  -0.0545 0.0425  789 HOH A O   
2768 O  O   . HOH G .   ? 0.5672 0.5379 0.5648 0.0294  0.0357  -0.0536 790 HOH A O   
2769 O  O   . HOH G .   ? 0.5144 0.4445 0.5743 0.0260  0.0134  0.0327  791 HOH A O   
2770 O  O   . HOH G .   ? 0.5777 0.6834 0.5346 -0.0078 -0.0550 -0.0545 792 HOH A O   
2771 O  O   . HOH G .   ? 0.5046 0.5413 0.5069 -0.0081 0.0249  0.0754  793 HOH A O   
2772 O  O   . HOH G .   ? 0.4549 0.5077 0.3875 0.0173  -0.0066 -0.0389 794 HOH A O   
2773 O  O   . HOH G .   ? 0.4072 0.4986 0.4984 0.0429  -0.0033 0.0607  795 HOH A O   
2774 O  O   . HOH G .   ? 0.4397 0.5088 0.4835 0.0493  -0.0126 0.0972  796 HOH A O   
2775 O  O   . HOH G .   ? 0.4747 0.4610 0.4702 -0.0166 0.0025  0.0324  797 HOH A O   
2776 O  O   . HOH G .   ? 0.3633 0.2968 0.4025 -0.0158 0.0129  0.0441  798 HOH A O   
2777 O  O   . HOH G .   ? 0.4943 0.6604 0.4846 0.0310  -0.0497 0.0591  799 HOH A O   
2778 O  O   . HOH G .   ? 0.4810 0.4704 0.4693 -0.0157 -0.0023 0.0173  800 HOH A O   
2779 O  O   . HOH G .   ? 0.4795 0.4262 0.5241 -0.0280 0.0145  0.0530  801 HOH A O   
2780 O  O   . HOH G .   ? 0.5563 0.6414 0.5393 0.0000  0.0354  0.0000  802 HOH A O   
2781 O  O   . HOH G .   ? 0.4383 0.5137 0.5857 -0.0540 0.0129  0.0546  803 HOH A O   
2782 O  O   . HOH G .   ? 0.4676 0.4878 0.5697 -0.0601 -0.0328 -0.0216 804 HOH A O   
2783 O  O   . HOH G .   ? 0.5055 0.5573 0.4577 0.0384  0.0200  -0.0330 805 HOH A O   
2784 O  O   . HOH G .   ? 0.4605 0.4354 0.4611 -0.0144 0.0025  0.0321  806 HOH A O   
2785 O  O   . HOH G .   ? 0.3290 0.3609 0.3475 0.0249  0.0016  0.0878  807 HOH A O   
2786 O  O   . HOH G .   ? 0.5055 0.5251 0.4860 -0.0420 -0.0224 -0.0648 808 HOH A O   
2787 O  O   . HOH G .   ? 0.4233 0.4225 0.4315 -0.0284 0.0006  0.0240  809 HOH A O   
2788 O  O   . HOH G .   ? 0.3769 0.5137 0.4395 -0.0003 -0.0452 0.0280  810 HOH A O   
2789 O  O   . HOH G .   ? 0.4753 0.5064 0.4428 0.0133  0.0293  -0.0163 811 HOH A O   
2790 O  O   . HOH G .   ? 0.4887 0.6333 0.4890 0.0423  -0.0365 0.0859  812 HOH A O   
2791 O  O   . HOH G .   ? 0.4498 0.4823 0.3938 0.0161  -0.0073 -0.0532 813 HOH A O   
2792 O  O   . HOH G .   ? 0.3384 0.4159 0.3410 0.0293  -0.0044 0.1007  814 HOH A O   
2793 O  O   . HOH G .   ? 0.4995 0.6264 0.4808 0.0511  -0.0051 0.1315  815 HOH A O   
2794 O  O   . HOH G .   ? 0.5004 0.5027 0.5957 0.0744  0.0388  0.0302  816 HOH A O   
2795 O  O   . HOH G .   ? 0.4772 0.6360 0.5083 0.0119  -0.0548 0.0346  817 HOH A O   
2796 O  O   . HOH G .   ? 0.4159 0.3058 0.4899 0.0054  0.0081  -0.0099 818 HOH A O   
2797 O  O   . HOH G .   ? 0.3766 0.3985 0.3579 0.0085  0.0259  -0.0042 819 HOH A O   
2798 O  O   . HOH G .   ? 0.4996 0.4352 0.4949 0.0069  0.0213  -0.0900 820 HOH A O   
2799 O  O   . HOH G .   ? 0.5265 0.5858 0.5400 -0.0072 0.0346  0.1093  821 HOH A O   
2800 O  O   . HOH G .   ? 0.5323 0.5850 0.4639 0.0139  -0.0192 -0.0716 822 HOH A O   
2801 O  O   . HOH G .   ? 0.4067 0.4832 0.4980 0.0405  0.0199  0.0413  823 HOH A O   
2802 O  O   . HOH G .   ? 0.4201 0.5296 0.5067 0.0192  -0.0157 0.0479  824 HOH A O   
2803 O  O   . HOH G .   ? 0.5672 0.4670 0.5684 0.0066  0.0201  -0.1588 825 HOH A O   
2804 O  O   . HOH G .   ? 0.4434 0.5211 0.5405 0.0507  0.0085  0.0570  826 HOH A O   
2805 O  O   . HOH G .   ? 0.4742 0.4873 0.5079 -0.0405 0.0034  0.0314  827 HOH A O   
2806 O  O   . HOH G .   ? 0.5017 0.4584 0.5557 -0.0375 -0.0251 -0.0494 828 HOH A O   
2807 O  O   . HOH G .   ? 0.5257 0.4268 0.6028 -0.0664 -0.0065 -0.0661 829 HOH A O   
2808 O  O   . HOH G .   ? 0.4229 0.5114 0.4463 0.0460  -0.0190 0.0998  830 HOH A O   
2809 O  O   . HOH G .   ? 0.4193 0.4695 0.4876 0.0617  0.0516  0.0079  831 HOH A O   
2810 O  O   . HOH G .   ? 0.4974 0.4272 0.5502 -0.0535 -0.0024 -0.0281 832 HOH A O   
2811 O  O   . HOH G .   ? 0.5183 0.5101 0.4846 0.0171  0.0271  -0.0680 833 HOH A O   
2812 O  O   . HOH G .   ? 0.4987 0.6605 0.5176 -0.0214 -0.0776 -0.0366 834 HOH A O   
2813 O  O   . HOH G .   ? 0.4933 0.5900 0.4780 0.0245  -0.0071 0.0948  835 HOH A O   
2814 O  O   . HOH G .   ? 0.4590 0.4047 0.4919 -0.0204 0.0114  0.0450  836 HOH A O   
2815 O  O   . HOH G .   ? 0.3745 0.5168 0.4194 -0.0299 -0.0711 -0.0315 837 HOH A O   
2816 O  O   . HOH G .   ? 0.3708 0.3775 0.4874 0.0872  0.0306  0.0642  838 HOH A O   
2817 O  O   . HOH G .   ? 0.5355 0.5201 0.5711 -0.0354 -0.0333 -0.0581 839 HOH A O   
2818 O  O   . HOH G .   ? 0.4890 0.4954 0.5249 0.0420  0.0159  0.0212  840 HOH A O   
2819 O  O   . HOH G .   ? 0.1300 0.2261 0.2348 -0.0190 0.0215  0.0498  841 HOH A O   
2820 O  O   . HOH G .   ? 0.4324 0.4685 0.3929 0.0013  -0.0092 0.0226  842 HOH A O   
2821 O  O   . HOH G .   ? 0.4954 0.5278 0.4780 0.0246  0.0386  -0.0188 843 HOH A O   
2822 O  O   . HOH G .   ? 0.3694 0.4927 0.4390 0.0061  -0.0345 0.0373  844 HOH A O   
2823 O  O   . HOH G .   ? 0.5019 0.4072 0.5745 0.0253  0.0151  0.0182  845 HOH A O   
2824 O  O   . HOH G .   ? 0.3072 0.3447 0.2967 0.0110  0.0315  0.0060  846 HOH A O   
2825 O  O   . HOH G .   ? 0.4769 0.5550 0.3927 0.0267  -0.0011 -0.0381 847 HOH A O   
2826 O  O   . HOH G .   ? 0.5341 0.4225 0.6060 -0.0012 0.0033  -0.0297 848 HOH A O   
2827 O  O   . HOH G .   ? 0.5408 0.5835 0.6238 -0.0532 0.0264  0.0775  849 HOH A O   
2828 O  O   . HOH G .   ? 0.4513 0.5070 0.4950 0.0562  -0.0038 0.1193  850 HOH A O   
2829 O  O   . HOH G .   ? 0.3975 0.5257 0.5417 -0.0301 -0.0010 0.0423  851 HOH A O   
2830 O  O   . HOH G .   ? 0.4485 0.5150 0.4285 0.0116  -0.0039 0.0750  852 HOH A O   
2831 O  O   . HOH G .   ? 0.4079 0.5446 0.5002 0.0025  -0.0321 0.0373  853 HOH A O   
2832 O  O   . HOH G .   ? 0.4381 0.4551 0.4797 -0.0422 -0.0449 -0.0616 854 HOH A O   
2833 O  O   . HOH G .   ? 0.4752 0.4443 0.5429 0.0486  0.0152  0.0687  855 HOH A O   
2834 O  O   . HOH G .   ? 0.4545 0.4200 0.4735 -0.0209 0.0087  0.0445  856 HOH A O   
2835 O  O   . HOH G .   ? 0.3871 0.4856 0.3905 0.0011  0.0496  0.0954  857 HOH A O   
2836 O  O   . HOH G .   ? 0.5320 0.6056 0.5881 0.0652  -0.0070 0.1217  858 HOH A O   
2837 O  O   . HOH G .   ? 0.5194 0.4881 0.5780 -0.0116 0.0291  0.1097  859 HOH A O   
2838 O  O   . HOH G .   ? 0.4379 0.4852 0.4465 0.0245  0.0015  0.0977  860 HOH A O   
2839 O  O   . HOH G .   ? 0.5032 0.5988 0.5179 0.0489  -0.0167 0.1096  861 HOH A O   
2840 O  O   . HOH G .   ? 0.1895 0.2313 0.1918 0.0050  0.0299  0.0199  862 HOH A O   
2841 O  O   . HOH G .   ? 0.3252 0.4607 0.4669 -0.0189 0.0117  0.0501  863 HOH A O   
2842 O  O   . HOH G .   ? 0.4261 0.5566 0.5572 -0.0137 0.0007  0.0432  864 HOH A O   
2843 O  O   . HOH G .   ? 0.4736 0.5541 0.4956 -0.0058 0.0466  0.1003  865 HOH A O   
2844 O  O   . HOH G .   ? 0.5042 0.5846 0.4880 0.0212  -0.0002 0.0970  866 HOH A O   
2845 O  O   . HOH G .   ? 0.3113 0.4669 0.4815 -0.0316 0.0041  0.0506  867 HOH A O   
2846 O  O   . HOH G .   ? 0.2828 0.4412 0.4732 -0.0447 0.0097  0.0575  868 HOH A O   
2847 O  O   . HOH G .   ? 0.2783 0.4391 0.4595 -0.0354 0.0238  0.0668  869 HOH A O   
2848 O  O   . HOH G .   ? 0.3772 0.5551 0.5893 -0.0513 0.0033  0.0543  870 HOH A O   
2849 O  O   . HOH G .   ? 0.2740 0.4736 0.5070 -0.0534 0.0099  0.0615  871 HOH A O   
# 
